data_9CJJ
# 
_entry.id   9CJJ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9CJJ         pdb_00009cjj 10.2210/pdb9cjj/pdb 
WWPDB D_1000285689 ?            ?                   
EMDB  EMD-45633    ?            ?                   
# 
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 1 
4  'Additional map'  1 0 2025-01-08 2 
5  FSC               1 0 2025-01-08 ? 
6  'Half map'        1 0 2025-01-08 1 
7  'Half map'        1 0 2025-01-08 2 
8  Image             1 0 2025-01-08 ? 
9  Mask              1 0 2025-01-08 ? 
10 'Primary map'     1 0 2025-01-08 ? 
11 'Structure model' 2 0 2025-03-26 ? 
12 'Additional map'  1 0 2025-01-08 1 
13 'Additional map'  1 0 2025-01-08 2 
14 FSC               1 0 2025-01-08 ? 
15 'Half map'        1 0 2025-01-08 1 
16 'Half map'        1 0 2025-01-08 2 
17 Image             1 0 2025-01-08 ? 
18 Mask              1 0 2025-01-08 ? 
19 'Primary map'     1 0 2025-01-08 ? 
20 'Structure model' 2 1 2025-05-21 ? 
21 'EM metadata'     1 1 2025-05-21 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1  1  'Structure model' repository 'Initial release'        ?                ? 
2  2  'EM metadata'     repository 'Initial release'        ?                ? 
3  3  'Additional map'  repository 'Initial release'        ?                ? 
4  4  'Additional map'  repository 'Initial release'        ?                ? 
5  5  FSC               repository 'Initial release'        ?                ? 
6  6  'Half map'        repository 'Initial release'        ?                ? 
7  7  'Half map'        repository 'Initial release'        ?                ? 
8  8  Image             repository 'Initial release'        ?                ? 
9  9  Mask              repository 'Initial release'        ?                ? 
10 10 'Primary map'     repository 'Initial release'        ?                ? 
11 11 'Structure model' author     'Coordinate replacement' 'Atomic clashes' ? 
12 12 'Additional map'  repository 'Initial release'        ?                ? 
13 13 'Additional map'  repository 'Initial release'        ?                ? 
14 14 FSC               repository 'Initial release'        ?                ? 
15 15 'Half map'        repository 'Initial release'        ?                ? 
16 16 'Half map'        repository 'Initial release'        ?                ? 
17 17 Image             repository 'Initial release'        ?                ? 
18 18 Mask              repository 'Initial release'        ?                ? 
19 19 'Primary map'     repository 'Initial release'        ?                ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1  11 'Structure model' Advisory                 
2  11 'Structure model' 'Atomic model'           
3  11 'Structure model' 'Data collection'        
4  11 'Structure model' 'Database references'    
5  11 'Structure model' 'Derived calculations'   
6  11 'Structure model' 'Refinement description' 
7  11 'Structure model' 'Structure summary'      
8  20 'Structure model' 'Data collection'        
9  21 'EM metadata'     'Data processing'        
10 21 '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  11 'Structure model' atom_site                   
2  11 'Structure model' citation                    
3  11 'Structure model' database_PDB_caveat         
4  11 'Structure model' em_admin                    
5  11 'Structure model' pdbx_contact_author         
6  11 'Structure model' pdbx_poly_seq_scheme        
7  11 'Structure model' pdbx_struct_assembly        
8  11 'Structure model' pdbx_struct_oper_list       
9  11 'Structure model' pdbx_validate_close_contact 
10 11 'Structure model' pdbx_validate_torsion       
11 11 'Structure model' refine                      
12 11 'Structure model' refine_ls_restr             
13 11 'Structure model' struct_conf                 
14 20 'Structure model' em_admin                    
15 20 'Structure model' em_software                 
16 21 'EM metadata'     em_admin                    
17 21 'EM metadata'     em_software                 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  11 'Structure model' '_atom_site.Cartn_x'                         
2  11 'Structure model' '_atom_site.Cartn_y'                         
3  11 'Structure model' '_atom_site.Cartn_z'                         
4  11 'Structure model' '_citation.journal_volume'                   
5  11 'Structure model' '_citation.year'                             
6  11 'Structure model' '_em_admin.last_update'                      
7  11 'Structure model' '_pdbx_poly_seq_scheme.auth_mon_id'          
8  11 'Structure model' '_pdbx_struct_assembly.details'              
9  11 'Structure model' '_pdbx_struct_oper_list.symmetry_operation'  
10 11 'Structure model' '_refine.ls_d_res_high'                      
11 11 'Structure model' '_refine.pdbx_stereochemistry_target_values' 
12 11 'Structure model' '_refine_ls_restr.dev_ideal'                 
13 11 'Structure model' '_refine_ls_restr.number'                    
14 11 'Structure model' '_struct_conf.beg_auth_comp_id'              
15 11 'Structure model' '_struct_conf.beg_auth_seq_id'               
16 11 'Structure model' '_struct_conf.beg_label_comp_id'             
17 11 'Structure model' '_struct_conf.beg_label_seq_id'              
18 11 'Structure model' '_struct_conf.end_auth_comp_id'              
19 11 'Structure model' '_struct_conf.end_auth_seq_id'               
20 11 'Structure model' '_struct_conf.end_label_comp_id'             
21 11 'Structure model' '_struct_conf.end_label_seq_id'              
22 11 'Structure model' '_struct_conf.pdbx_PDB_helix_class'          
23 11 'Structure model' '_struct_conf.pdbx_PDB_helix_length'         
24 20 'Structure model' '_em_admin.last_update'                      
25 20 'Structure model' '_em_software.name'                          
26 21 'EM metadata'     '_em_admin.last_update'                      
27 21 'EM metadata'     '_em_software.name'                          
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CJJ 
_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'      
EMDB .                                                                              EMD-45632 'other EM volume'      
PDB  .                                                                              9CJH      unspecified            
PDB  .                                                                              9CJI      unspecified            
EMDB 'Cas12a:gRNA:DNA (Acidaminococcus sp.) with 0 RNA:DNA base pairs, structure 3' EMD-45633 '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 0000-0003-3847-1652 
primary 'Doudna, J.A.' 5 0000-0001-9161-999X 
# 
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 'guide RNA (25-MER)'                    13418.956  1 ?                 ?     ? ? 
2 polymer man 'CRISPR-associated endonuclease Cas12a' 151680.250 1 3.1.21.1,4.6.1.22 N551C ? ? 
3 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
;
4 polymer syn 'Target DNA strand'                     9557.205   1 ?                 ?     ? ? 
# 
_entity_name_com.entity_id   2 
_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 polyribonucleotide      no no  UUUAAUUUCUACUCUUGUAGAUAGCAGAGUAGACAUACGCAG UUUAAUUUCUACUCUUGUAGAUAGCAGAGUAGACAUACGCAG B ? 
2 '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 ? 
3 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 ? 
4 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 ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    U   n 
1 2    U   n 
1 3    U   n 
1 4    A   n 
1 5    A   n 
1 6    U   n 
1 7    U   n 
1 8    U   n 
1 9    C   n 
1 10   U   n 
1 11   A   n 
1 12   C   n 
1 13   U   n 
1 14   C   n 
1 15   U   n 
1 16   U   n 
1 17   G   n 
1 18   U   n 
1 19   A   n 
1 20   G   n 
1 21   A   n 
1 22   U   n 
1 23   A   n 
1 24   G   n 
1 25   C   n 
1 26   A   n 
1 27   G   n 
1 28   A   n 
1 29   G   n 
1 30   U   n 
1 31   A   n 
1 32   G   n 
1 33   A   n 
1 34   C   n 
1 35   A   n 
1 36   U   n 
1 37   A   n 
1 38   C   n 
1 39   G   n 
1 40   C   n 
1 41   A   n 
1 42   G   n 
2 1    SER n 
2 2    ASN n 
2 3    ALA n 
2 4    MET n 
2 5    THR n 
2 6    GLN n 
2 7    PHE n 
2 8    GLU n 
2 9    GLY n 
2 10   PHE n 
2 11   THR n 
2 12   ASN n 
2 13   LEU n 
2 14   TYR n 
2 15   GLN n 
2 16   VAL n 
2 17   SER n 
2 18   LYS n 
2 19   THR n 
2 20   LEU n 
2 21   ARG n 
2 22   PHE n 
2 23   GLU n 
2 24   LEU n 
2 25   ILE n 
2 26   PRO n 
2 27   GLN n 
2 28   GLY n 
2 29   LYS n 
2 30   THR n 
2 31   LEU n 
2 32   LYS n 
2 33   HIS n 
2 34   ILE n 
2 35   GLN n 
2 36   GLU n 
2 37   GLN n 
2 38   GLY n 
2 39   PHE n 
2 40   ILE n 
2 41   GLU n 
2 42   GLU n 
2 43   ASP n 
2 44   LYS n 
2 45   ALA n 
2 46   ARG n 
2 47   ASN n 
2 48   ASP n 
2 49   HIS n 
2 50   TYR n 
2 51   LYS n 
2 52   GLU n 
2 53   LEU n 
2 54   LYS n 
2 55   PRO n 
2 56   ILE n 
2 57   ILE n 
2 58   ASP n 
2 59   ARG n 
2 60   ILE n 
2 61   TYR n 
2 62   LYS n 
2 63   THR n 
2 64   TYR n 
2 65   ALA n 
2 66   ASP n 
2 67   GLN n 
2 68   CYS n 
2 69   LEU n 
2 70   GLN n 
2 71   LEU n 
2 72   VAL n 
2 73   GLN n 
2 74   LEU n 
2 75   ASP n 
2 76   TRP n 
2 77   GLU n 
2 78   ASN n 
2 79   LEU n 
2 80   SER n 
2 81   ALA n 
2 82   ALA n 
2 83   ILE n 
2 84   ASP n 
2 85   SER n 
2 86   TYR n 
2 87   ARG n 
2 88   LYS n 
2 89   GLU n 
2 90   LYS n 
2 91   THR n 
2 92   GLU n 
2 93   GLU n 
2 94   THR n 
2 95   ARG n 
2 96   ASN n 
2 97   ALA n 
2 98   LEU n 
2 99   ILE n 
2 100  GLU n 
2 101  GLU n 
2 102  GLN n 
2 103  ALA n 
2 104  THR n 
2 105  TYR n 
2 106  ARG n 
2 107  ASN n 
2 108  ALA n 
2 109  ILE n 
2 110  HIS n 
2 111  ASP n 
2 112  TYR n 
2 113  PHE n 
2 114  ILE n 
2 115  GLY n 
2 116  ARG n 
2 117  THR n 
2 118  ASP n 
2 119  ASN n 
2 120  LEU n 
2 121  THR n 
2 122  ASP n 
2 123  ALA n 
2 124  ILE n 
2 125  ASN n 
2 126  LYS n 
2 127  ARG n 
2 128  HIS n 
2 129  ALA n 
2 130  GLU n 
2 131  ILE n 
2 132  TYR n 
2 133  LYS n 
2 134  GLY n 
2 135  LEU n 
2 136  PHE n 
2 137  LYS n 
2 138  ALA n 
2 139  GLU n 
2 140  LEU n 
2 141  PHE n 
2 142  ASN n 
2 143  GLY n 
2 144  LYS n 
2 145  VAL n 
2 146  LEU n 
2 147  LYS n 
2 148  GLN n 
2 149  LEU n 
2 150  GLY n 
2 151  THR n 
2 152  VAL n 
2 153  THR n 
2 154  THR n 
2 155  THR n 
2 156  GLU n 
2 157  HIS n 
2 158  GLU n 
2 159  ASN n 
2 160  ALA n 
2 161  LEU n 
2 162  LEU n 
2 163  ARG n 
2 164  SER n 
2 165  PHE n 
2 166  ASP n 
2 167  LYS n 
2 168  PHE n 
2 169  THR n 
2 170  THR n 
2 171  TYR n 
2 172  PHE n 
2 173  SER n 
2 174  GLY n 
2 175  PHE n 
2 176  TYR n 
2 177  GLU n 
2 178  ASN n 
2 179  ARG n 
2 180  LYS n 
2 181  ASN n 
2 182  VAL n 
2 183  PHE n 
2 184  SER n 
2 185  ALA n 
2 186  GLU n 
2 187  ASP n 
2 188  ILE n 
2 189  SER n 
2 190  THR n 
2 191  ALA n 
2 192  ILE n 
2 193  PRO n 
2 194  HIS n 
2 195  ARG n 
2 196  ILE n 
2 197  VAL n 
2 198  GLN n 
2 199  ASP n 
2 200  ASN n 
2 201  PHE n 
2 202  PRO n 
2 203  LYS n 
2 204  PHE n 
2 205  LYS n 
2 206  GLU n 
2 207  ASN n 
2 208  CYS n 
2 209  HIS n 
2 210  ILE n 
2 211  PHE n 
2 212  THR n 
2 213  ARG n 
2 214  LEU n 
2 215  ILE n 
2 216  THR n 
2 217  ALA n 
2 218  VAL n 
2 219  PRO n 
2 220  SER n 
2 221  LEU n 
2 222  ARG n 
2 223  GLU n 
2 224  HIS n 
2 225  PHE n 
2 226  GLU n 
2 227  ASN n 
2 228  VAL n 
2 229  LYS n 
2 230  LYS n 
2 231  ALA n 
2 232  ILE n 
2 233  GLY n 
2 234  ILE n 
2 235  PHE n 
2 236  VAL n 
2 237  SER n 
2 238  THR n 
2 239  SER n 
2 240  ILE n 
2 241  GLU n 
2 242  GLU n 
2 243  VAL n 
2 244  PHE n 
2 245  SER n 
2 246  PHE n 
2 247  PRO n 
2 248  PHE n 
2 249  TYR n 
2 250  ASN n 
2 251  GLN n 
2 252  LEU n 
2 253  LEU n 
2 254  THR n 
2 255  GLN n 
2 256  THR n 
2 257  GLN n 
2 258  ILE n 
2 259  ASP n 
2 260  LEU n 
2 261  TYR n 
2 262  ASN n 
2 263  GLN n 
2 264  LEU n 
2 265  LEU n 
2 266  GLY n 
2 267  GLY n 
2 268  ILE n 
2 269  SER n 
2 270  ARG n 
2 271  GLU n 
2 272  ALA n 
2 273  GLY n 
2 274  THR n 
2 275  GLU n 
2 276  LYS n 
2 277  ILE n 
2 278  LYS n 
2 279  GLY n 
2 280  LEU n 
2 281  ASN n 
2 282  GLU n 
2 283  VAL n 
2 284  LEU n 
2 285  ASN n 
2 286  LEU n 
2 287  ALA n 
2 288  ILE n 
2 289  GLN n 
2 290  LYS n 
2 291  ASN n 
2 292  ASP n 
2 293  GLU n 
2 294  THR n 
2 295  ALA n 
2 296  HIS n 
2 297  ILE n 
2 298  ILE n 
2 299  ALA n 
2 300  SER n 
2 301  LEU n 
2 302  PRO n 
2 303  HIS n 
2 304  ARG n 
2 305  PHE n 
2 306  ILE n 
2 307  PRO n 
2 308  LEU n 
2 309  PHE n 
2 310  LYS n 
2 311  GLN n 
2 312  ILE n 
2 313  LEU n 
2 314  SER n 
2 315  ASP n 
2 316  ARG n 
2 317  ASN n 
2 318  THR n 
2 319  LEU n 
2 320  SER n 
2 321  PHE n 
2 322  ILE n 
2 323  LEU n 
2 324  GLU n 
2 325  GLU n 
2 326  PHE n 
2 327  LYS n 
2 328  SER n 
2 329  ASP n 
2 330  GLU n 
2 331  GLU n 
2 332  VAL n 
2 333  ILE n 
2 334  GLN n 
2 335  SER n 
2 336  PHE n 
2 337  CYS n 
2 338  LYS n 
2 339  TYR n 
2 340  LYS n 
2 341  THR n 
2 342  LEU n 
2 343  LEU n 
2 344  ARG n 
2 345  ASN n 
2 346  GLU n 
2 347  ASN n 
2 348  VAL n 
2 349  LEU n 
2 350  GLU n 
2 351  THR n 
2 352  ALA n 
2 353  GLU n 
2 354  ALA n 
2 355  LEU n 
2 356  PHE n 
2 357  ASN n 
2 358  GLU n 
2 359  LEU n 
2 360  ASN n 
2 361  SER n 
2 362  ILE n 
2 363  ASP n 
2 364  LEU n 
2 365  THR n 
2 366  HIS n 
2 367  ILE n 
2 368  PHE n 
2 369  ILE n 
2 370  SER n 
2 371  HIS n 
2 372  LYS n 
2 373  LYS n 
2 374  LEU n 
2 375  GLU n 
2 376  THR n 
2 377  ILE n 
2 378  SER n 
2 379  SER n 
2 380  ALA n 
2 381  LEU n 
2 382  CYS n 
2 383  ASP n 
2 384  HIS n 
2 385  TRP n 
2 386  ASP n 
2 387  THR n 
2 388  LEU n 
2 389  ARG n 
2 390  ASN n 
2 391  ALA n 
2 392  LEU n 
2 393  TYR n 
2 394  GLU n 
2 395  ARG n 
2 396  ARG n 
2 397  ILE n 
2 398  SER n 
2 399  GLU n 
2 400  LEU n 
2 401  THR n 
2 402  GLY n 
2 403  LYS n 
2 404  ILE n 
2 405  THR n 
2 406  LYS n 
2 407  SER n 
2 408  ALA n 
2 409  LYS n 
2 410  GLU n 
2 411  LYS n 
2 412  VAL n 
2 413  GLN n 
2 414  ARG n 
2 415  SER n 
2 416  LEU n 
2 417  LYS n 
2 418  HIS n 
2 419  GLU n 
2 420  ASP n 
2 421  ILE n 
2 422  ASN n 
2 423  LEU n 
2 424  GLN n 
2 425  GLU n 
2 426  ILE n 
2 427  ILE n 
2 428  SER n 
2 429  ALA n 
2 430  ALA n 
2 431  GLY n 
2 432  LYS n 
2 433  GLU n 
2 434  LEU n 
2 435  SER n 
2 436  GLU n 
2 437  ALA n 
2 438  PHE n 
2 439  LYS n 
2 440  GLN n 
2 441  LYS n 
2 442  THR n 
2 443  SER n 
2 444  GLU n 
2 445  ILE n 
2 446  LEU n 
2 447  SER n 
2 448  HIS n 
2 449  ALA n 
2 450  HIS n 
2 451  ALA n 
2 452  ALA n 
2 453  LEU n 
2 454  ASP n 
2 455  GLN n 
2 456  PRO n 
2 457  LEU n 
2 458  PRO n 
2 459  THR n 
2 460  THR n 
2 461  LEU n 
2 462  LYS n 
2 463  LYS n 
2 464  GLN n 
2 465  GLU n 
2 466  GLU n 
2 467  LYS n 
2 468  GLU n 
2 469  ILE n 
2 470  LEU n 
2 471  LYS n 
2 472  SER n 
2 473  GLN n 
2 474  LEU n 
2 475  ASP n 
2 476  SER n 
2 477  LEU n 
2 478  LEU n 
2 479  GLY n 
2 480  LEU n 
2 481  TYR n 
2 482  HIS n 
2 483  LEU n 
2 484  LEU n 
2 485  ASP n 
2 486  TRP n 
2 487  PHE n 
2 488  ALA n 
2 489  VAL n 
2 490  ASP n 
2 491  GLU n 
2 492  SER n 
2 493  ASN n 
2 494  GLU n 
2 495  VAL n 
2 496  ASP n 
2 497  PRO n 
2 498  GLU n 
2 499  PHE n 
2 500  SER n 
2 501  ALA n 
2 502  ARG n 
2 503  LEU n 
2 504  THR n 
2 505  GLY n 
2 506  ILE n 
2 507  LYS n 
2 508  LEU n 
2 509  GLU n 
2 510  MET n 
2 511  GLU n 
2 512  PRO n 
2 513  SER n 
2 514  LEU n 
2 515  SER n 
2 516  PHE n 
2 517  TYR n 
2 518  ASN n 
2 519  LYS n 
2 520  ALA n 
2 521  ARG n 
2 522  ASN n 
2 523  TYR n 
2 524  ALA n 
2 525  THR n 
2 526  LYS n 
2 527  LYS n 
2 528  PRO n 
2 529  TYR n 
2 530  SER n 
2 531  VAL n 
2 532  GLU n 
2 533  LYS n 
2 534  PHE n 
2 535  LYS n 
2 536  LEU n 
2 537  ASN n 
2 538  PHE n 
2 539  GLN n 
2 540  MET n 
2 541  PRO n 
2 542  THR n 
2 543  LEU n 
2 544  ALA n 
2 545  SER n 
2 546  GLY n 
2 547  TRP n 
2 548  ASP n 
2 549  VAL n 
2 550  ASN n 
2 551  LYS n 
2 552  GLU n 
2 553  LYS n 
2 554  CYS n 
2 555  ASN n 
2 556  GLY n 
2 557  ALA n 
2 558  ILE n 
2 559  LEU n 
2 560  PHE n 
2 561  VAL n 
2 562  LYS n 
2 563  ASN n 
2 564  GLY n 
2 565  LEU n 
2 566  TYR n 
2 567  TYR n 
2 568  LEU n 
2 569  GLY n 
2 570  ILE n 
2 571  MET n 
2 572  PRO n 
2 573  LYS n 
2 574  GLN n 
2 575  LYS n 
2 576  GLY n 
2 577  ARG n 
2 578  TYR n 
2 579  LYS n 
2 580  ALA n 
2 581  LEU n 
2 582  SER n 
2 583  PHE n 
2 584  GLU n 
2 585  PRO n 
2 586  THR n 
2 587  GLU n 
2 588  LYS n 
2 589  THR n 
2 590  SER n 
2 591  GLU n 
2 592  GLY n 
2 593  PHE n 
2 594  ASP n 
2 595  LYS n 
2 596  MET n 
2 597  TYR n 
2 598  TYR n 
2 599  ASP n 
2 600  TYR n 
2 601  PHE n 
2 602  PRO n 
2 603  ASP n 
2 604  ALA n 
2 605  ALA n 
2 606  LYS n 
2 607  MET n 
2 608  ILE n 
2 609  PRO n 
2 610  LYS n 
2 611  CYS n 
2 612  SER n 
2 613  THR n 
2 614  GLN n 
2 615  LEU n 
2 616  LYS n 
2 617  ALA n 
2 618  VAL n 
2 619  THR n 
2 620  ALA n 
2 621  HIS n 
2 622  PHE n 
2 623  GLN n 
2 624  THR n 
2 625  HIS n 
2 626  THR n 
2 627  THR n 
2 628  PRO n 
2 629  ILE n 
2 630  LEU n 
2 631  LEU n 
2 632  SER n 
2 633  ASN n 
2 634  ASN n 
2 635  PHE n 
2 636  ILE n 
2 637  GLU n 
2 638  PRO n 
2 639  LEU n 
2 640  GLU n 
2 641  ILE n 
2 642  THR n 
2 643  LYS n 
2 644  GLU n 
2 645  ILE n 
2 646  TYR n 
2 647  ASP n 
2 648  LEU n 
2 649  ASN n 
2 650  ASN n 
2 651  PRO n 
2 652  GLU n 
2 653  LYS n 
2 654  GLU n 
2 655  PRO n 
2 656  LYS n 
2 657  LYS n 
2 658  PHE n 
2 659  GLN n 
2 660  THR n 
2 661  ALA n 
2 662  TYR n 
2 663  ALA n 
2 664  LYS n 
2 665  LYS n 
2 666  THR n 
2 667  GLY n 
2 668  ASP n 
2 669  GLN n 
2 670  LYS n 
2 671  GLY n 
2 672  TYR n 
2 673  ARG n 
2 674  GLU n 
2 675  ALA n 
2 676  LEU n 
2 677  CYS n 
2 678  LYS n 
2 679  TRP n 
2 680  ILE n 
2 681  ASP n 
2 682  PHE n 
2 683  THR n 
2 684  ARG n 
2 685  ASP n 
2 686  PHE n 
2 687  LEU n 
2 688  SER n 
2 689  LYS n 
2 690  TYR n 
2 691  THR n 
2 692  LYS n 
2 693  THR n 
2 694  THR n 
2 695  SER n 
2 696  ILE n 
2 697  ASP n 
2 698  LEU n 
2 699  SER n 
2 700  SER n 
2 701  LEU n 
2 702  ARG n 
2 703  PRO n 
2 704  SER n 
2 705  SER n 
2 706  GLN n 
2 707  TYR n 
2 708  LYS n 
2 709  ASP n 
2 710  LEU n 
2 711  GLY n 
2 712  GLU n 
2 713  TYR n 
2 714  TYR n 
2 715  ALA n 
2 716  GLU n 
2 717  LEU n 
2 718  ASN n 
2 719  PRO n 
2 720  LEU n 
2 721  LEU n 
2 722  TYR n 
2 723  HIS n 
2 724  ILE n 
2 725  SER n 
2 726  PHE n 
2 727  GLN n 
2 728  ARG n 
2 729  ILE n 
2 730  ALA n 
2 731  GLU n 
2 732  LYS n 
2 733  GLU n 
2 734  ILE n 
2 735  MET n 
2 736  ASP n 
2 737  ALA n 
2 738  VAL n 
2 739  GLU n 
2 740  THR n 
2 741  GLY n 
2 742  LYS n 
2 743  LEU n 
2 744  TYR n 
2 745  LEU n 
2 746  PHE n 
2 747  GLN n 
2 748  ILE n 
2 749  TYR n 
2 750  ASN n 
2 751  LYS n 
2 752  ASP n 
2 753  PHE n 
2 754  ALA n 
2 755  LYS n 
2 756  GLY n 
2 757  HIS n 
2 758  HIS n 
2 759  GLY n 
2 760  LYS n 
2 761  PRO n 
2 762  ASN n 
2 763  LEU n 
2 764  HIS n 
2 765  THR n 
2 766  LEU n 
2 767  TYR n 
2 768  TRP n 
2 769  THR n 
2 770  GLY n 
2 771  LEU n 
2 772  PHE n 
2 773  SER n 
2 774  PRO n 
2 775  GLU n 
2 776  ASN n 
2 777  LEU n 
2 778  ALA n 
2 779  LYS n 
2 780  THR n 
2 781  SER n 
2 782  ILE n 
2 783  LYS n 
2 784  LEU n 
2 785  ASN n 
2 786  GLY n 
2 787  GLN n 
2 788  ALA n 
2 789  GLU n 
2 790  LEU n 
2 791  PHE n 
2 792  TYR n 
2 793  ARG n 
2 794  PRO n 
2 795  LYS n 
2 796  SER n 
2 797  ARG n 
2 798  MET n 
2 799  LYS n 
2 800  ARG n 
2 801  MET n 
2 802  ALA n 
2 803  HIS n 
2 804  ARG n 
2 805  LEU n 
2 806  GLY n 
2 807  GLU n 
2 808  LYS n 
2 809  MET n 
2 810  LEU n 
2 811  ASN n 
2 812  LYS n 
2 813  LYS n 
2 814  LEU n 
2 815  LYS n 
2 816  ASP n 
2 817  GLN n 
2 818  LYS n 
2 819  THR n 
2 820  PRO n 
2 821  ILE n 
2 822  PRO n 
2 823  ASP n 
2 824  THR n 
2 825  LEU n 
2 826  TYR n 
2 827  GLN n 
2 828  GLU n 
2 829  LEU n 
2 830  TYR n 
2 831  ASP n 
2 832  TYR n 
2 833  VAL n 
2 834  ASN n 
2 835  HIS n 
2 836  ARG n 
2 837  LEU n 
2 838  SER n 
2 839  HIS n 
2 840  ASP n 
2 841  LEU n 
2 842  SER n 
2 843  ASP n 
2 844  GLU n 
2 845  ALA n 
2 846  ARG n 
2 847  ALA n 
2 848  LEU n 
2 849  LEU n 
2 850  PRO n 
2 851  ASN n 
2 852  VAL n 
2 853  ILE n 
2 854  THR n 
2 855  LYS n 
2 856  GLU n 
2 857  VAL n 
2 858  SER n 
2 859  HIS n 
2 860  GLU n 
2 861  ILE n 
2 862  ILE n 
2 863  LYS n 
2 864  ASP n 
2 865  ARG n 
2 866  ARG n 
2 867  PHE n 
2 868  THR n 
2 869  SER n 
2 870  ASP n 
2 871  LYS n 
2 872  PHE n 
2 873  PHE n 
2 874  PHE n 
2 875  HIS n 
2 876  VAL n 
2 877  PRO n 
2 878  ILE n 
2 879  THR n 
2 880  LEU n 
2 881  ASN n 
2 882  TYR n 
2 883  GLN n 
2 884  ALA n 
2 885  ALA n 
2 886  ASN n 
2 887  SER n 
2 888  PRO n 
2 889  SER n 
2 890  LYS n 
2 891  PHE n 
2 892  ASN n 
2 893  GLN n 
2 894  ARG n 
2 895  VAL n 
2 896  ASN n 
2 897  ALA n 
2 898  TYR n 
2 899  LEU n 
2 900  LYS n 
2 901  GLU n 
2 902  HIS n 
2 903  PRO n 
2 904  GLU n 
2 905  THR n 
2 906  PRO n 
2 907  ILE n 
2 908  ILE n 
2 909  GLY n 
2 910  ILE n 
2 911  ASP n 
2 912  ARG n 
2 913  GLY n 
2 914  GLU n 
2 915  ARG n 
2 916  ASN n 
2 917  LEU n 
2 918  ILE n 
2 919  TYR n 
2 920  ILE n 
2 921  THR n 
2 922  VAL n 
2 923  ILE n 
2 924  ASP n 
2 925  SER n 
2 926  THR n 
2 927  GLY n 
2 928  LYS n 
2 929  ILE n 
2 930  LEU n 
2 931  GLU n 
2 932  GLN n 
2 933  ARG n 
2 934  SER n 
2 935  LEU n 
2 936  ASN n 
2 937  THR n 
2 938  ILE n 
2 939  GLN n 
2 940  GLN n 
2 941  PHE n 
2 942  ASP n 
2 943  TYR n 
2 944  GLN n 
2 945  LYS n 
2 946  LYS n 
2 947  LEU n 
2 948  ASP n 
2 949  ASN n 
2 950  ARG n 
2 951  GLU n 
2 952  LYS n 
2 953  GLU n 
2 954  ARG n 
2 955  VAL n 
2 956  ALA n 
2 957  ALA n 
2 958  ARG n 
2 959  GLN n 
2 960  ALA n 
2 961  TRP n 
2 962  SER n 
2 963  VAL n 
2 964  VAL n 
2 965  GLY n 
2 966  THR n 
2 967  ILE n 
2 968  LYS n 
2 969  ASP n 
2 970  LEU n 
2 971  LYS n 
2 972  GLN n 
2 973  GLY n 
2 974  TYR n 
2 975  LEU n 
2 976  SER n 
2 977  GLN n 
2 978  VAL n 
2 979  ILE n 
2 980  HIS n 
2 981  GLU n 
2 982  ILE n 
2 983  VAL n 
2 984  ASP n 
2 985  LEU n 
2 986  MET n 
2 987  ILE n 
2 988  HIS n 
2 989  TYR n 
2 990  GLN n 
2 991  ALA n 
2 992  VAL n 
2 993  VAL n 
2 994  VAL n 
2 995  LEU n 
2 996  GLU n 
2 997  ASN n 
2 998  LEU n 
2 999  ASN n 
2 1000 PHE n 
2 1001 GLY n 
2 1002 PHE n 
2 1003 LYS n 
2 1004 SER n 
2 1005 LYS n 
2 1006 ARG n 
2 1007 THR n 
2 1008 GLY n 
2 1009 ILE n 
2 1010 ALA n 
2 1011 GLU n 
2 1012 LYS n 
2 1013 ALA n 
2 1014 VAL n 
2 1015 TYR n 
2 1016 GLN n 
2 1017 GLN n 
2 1018 PHE n 
2 1019 GLU n 
2 1020 LYS n 
2 1021 MET n 
2 1022 LEU n 
2 1023 ILE n 
2 1024 ASP n 
2 1025 LYS n 
2 1026 LEU n 
2 1027 ASN n 
2 1028 CYS n 
2 1029 LEU n 
2 1030 VAL n 
2 1031 LEU n 
2 1032 LYS n 
2 1033 ASP n 
2 1034 TYR n 
2 1035 PRO n 
2 1036 ALA n 
2 1037 GLU n 
2 1038 LYS n 
2 1039 VAL n 
2 1040 GLY n 
2 1041 GLY n 
2 1042 VAL n 
2 1043 LEU n 
2 1044 ASN n 
2 1045 PRO n 
2 1046 TYR n 
2 1047 GLN n 
2 1048 LEU n 
2 1049 THR n 
2 1050 ASP n 
2 1051 GLN n 
2 1052 PHE n 
2 1053 THR n 
2 1054 SER n 
2 1055 PHE n 
2 1056 ALA n 
2 1057 LYS n 
2 1058 MET n 
2 1059 GLY n 
2 1060 THR n 
2 1061 GLN n 
2 1062 SER n 
2 1063 GLY n 
2 1064 PHE n 
2 1065 LEU n 
2 1066 PHE n 
2 1067 TYR n 
2 1068 VAL n 
2 1069 PRO n 
2 1070 ALA n 
2 1071 PRO n 
2 1072 TYR n 
2 1073 THR n 
2 1074 SER n 
2 1075 LYS n 
2 1076 ILE n 
2 1077 ASP n 
2 1078 PRO n 
2 1079 LEU n 
2 1080 THR n 
2 1081 GLY n 
2 1082 PHE n 
2 1083 VAL n 
2 1084 ASP n 
2 1085 PRO n 
2 1086 PHE n 
2 1087 VAL n 
2 1088 TRP n 
2 1089 LYS n 
2 1090 THR n 
2 1091 ILE n 
2 1092 LYS n 
2 1093 ASN n 
2 1094 HIS n 
2 1095 GLU n 
2 1096 SER n 
2 1097 ARG n 
2 1098 LYS n 
2 1099 HIS n 
2 1100 PHE n 
2 1101 LEU n 
2 1102 GLU n 
2 1103 GLY n 
2 1104 PHE n 
2 1105 ASP n 
2 1106 PHE n 
2 1107 LEU n 
2 1108 HIS n 
2 1109 TYR n 
2 1110 ASP n 
2 1111 VAL n 
2 1112 LYS n 
2 1113 THR n 
2 1114 GLY n 
2 1115 ASP n 
2 1116 PHE n 
2 1117 ILE n 
2 1118 LEU n 
2 1119 HIS n 
2 1120 PHE n 
2 1121 LYS n 
2 1122 MET n 
2 1123 ASN n 
2 1124 ARG n 
2 1125 ASN n 
2 1126 LEU n 
2 1127 SER n 
2 1128 PHE n 
2 1129 GLN n 
2 1130 ARG n 
2 1131 GLY n 
2 1132 LEU n 
2 1133 PRO n 
2 1134 GLY n 
2 1135 PHE n 
2 1136 MET n 
2 1137 PRO n 
2 1138 ALA n 
2 1139 TRP n 
2 1140 ASP n 
2 1141 ILE n 
2 1142 VAL n 
2 1143 PHE n 
2 1144 GLU n 
2 1145 LYS n 
2 1146 ASN n 
2 1147 GLU n 
2 1148 THR n 
2 1149 GLN n 
2 1150 PHE n 
2 1151 ASP n 
2 1152 ALA n 
2 1153 LYS n 
2 1154 GLY n 
2 1155 THR n 
2 1156 PRO n 
2 1157 PHE n 
2 1158 ILE n 
2 1159 ALA n 
2 1160 GLY n 
2 1161 LYS n 
2 1162 ARG n 
2 1163 ILE n 
2 1164 VAL n 
2 1165 PRO n 
2 1166 VAL n 
2 1167 ILE n 
2 1168 GLU n 
2 1169 ASN n 
2 1170 HIS n 
2 1171 ARG n 
2 1172 PHE n 
2 1173 THR n 
2 1174 GLY n 
2 1175 ARG n 
2 1176 TYR n 
2 1177 ARG n 
2 1178 ASP n 
2 1179 LEU n 
2 1180 TYR n 
2 1181 PRO n 
2 1182 ALA n 
2 1183 ASN n 
2 1184 GLU n 
2 1185 LEU n 
2 1186 ILE n 
2 1187 ALA n 
2 1188 LEU n 
2 1189 LEU n 
2 1190 GLU n 
2 1191 GLU n 
2 1192 LYS n 
2 1193 GLY n 
2 1194 ILE n 
2 1195 VAL n 
2 1196 PHE n 
2 1197 ARG n 
2 1198 ASP n 
2 1199 GLY n 
2 1200 SER n 
2 1201 ASN n 
2 1202 ILE n 
2 1203 LEU n 
2 1204 PRO n 
2 1205 LYS n 
2 1206 LEU n 
2 1207 LEU n 
2 1208 GLU n 
2 1209 ASN n 
2 1210 ASP n 
2 1211 ASP n 
2 1212 SER n 
2 1213 HIS n 
2 1214 ALA n 
2 1215 ILE n 
2 1216 ASP n 
2 1217 THR n 
2 1218 MET n 
2 1219 VAL n 
2 1220 ALA n 
2 1221 LEU n 
2 1222 ILE n 
2 1223 ARG n 
2 1224 SER n 
2 1225 VAL n 
2 1226 LEU n 
2 1227 GLN n 
2 1228 MET n 
2 1229 ARG n 
2 1230 ASN n 
2 1231 SER n 
2 1232 ASN n 
2 1233 ALA n 
2 1234 ALA n 
2 1235 THR n 
2 1236 GLY n 
2 1237 GLU n 
2 1238 ASP n 
2 1239 TYR n 
2 1240 ILE n 
2 1241 ASN n 
2 1242 SER n 
2 1243 PRO n 
2 1244 VAL n 
2 1245 ARG n 
2 1246 ASP n 
2 1247 LEU n 
2 1248 ASN n 
2 1249 GLY n 
2 1250 VAL n 
2 1251 CYS n 
2 1252 PHE n 
2 1253 ASP n 
2 1254 SER n 
2 1255 ARG n 
2 1256 PHE n 
2 1257 GLN n 
2 1258 ASN n 
2 1259 PRO n 
2 1260 GLU n 
2 1261 TRP n 
2 1262 PRO n 
2 1263 MET n 
2 1264 ASP n 
2 1265 ALA n 
2 1266 ASP n 
2 1267 ALA n 
2 1268 ASN n 
2 1269 GLY n 
2 1270 ALA n 
2 1271 TYR n 
2 1272 HIS n 
2 1273 ILE n 
2 1274 ALA n 
2 1275 LEU n 
2 1276 LYS n 
2 1277 GLY n 
2 1278 GLN n 
2 1279 LEU n 
2 1280 LEU n 
2 1281 LEU n 
2 1282 ASN n 
2 1283 HIS n 
2 1284 LEU n 
2 1285 LYS n 
2 1286 GLU n 
2 1287 SER n 
2 1288 LYS n 
2 1289 ASP n 
2 1290 LEU n 
2 1291 LYS n 
2 1292 LEU n 
2 1293 GLN n 
2 1294 ASN n 
2 1295 GLY n 
2 1296 ILE n 
2 1297 SER n 
2 1298 ASN n 
2 1299 GLN n 
2 1300 ASP n 
2 1301 TRP n 
2 1302 LEU n 
2 1303 ALA n 
2 1304 TYR n 
2 1305 ILE n 
2 1306 GLN n 
2 1307 GLU n 
2 1308 LEU n 
2 1309 ARG n 
2 1310 ASN n 
3 1    DG  n 
3 2    DT  n 
3 3    DA  n 
3 4    DG  n 
3 5    DT  n 
3 6    DG  n 
3 7    2YR n 
3 8    DT  n 
3 9    DT  n 
3 10   DT  n 
3 11   DG  n 
3 12   DT  n 
3 13   DC  n 
3 14   DG  n 
3 15   DT  n 
3 16   DC  n 
3 17   DT  n 
3 18   DC  n 
3 19   DA  n 
3 20   DT  n 
3 21   DC  n 
3 22   DT  n 
3 23   DG  n 
3 24   DT  n 
3 25   DA  n 
3 26   DT  n 
3 27   DG  n 
3 28   DC  n 
3 29   DG  n 
3 30   DT  n 
3 31   DC  n 
4 1    DG  n 
4 2    DA  n 
4 3    DC  n 
4 4    DG  n 
4 5    DC  n 
4 6    DA  n 
4 7    DT  n 
4 8    DA  n 
4 9    DC  n 
4 10   DA  n 
4 11   DG  n 
4 12   DA  n 
4 13   DT  n 
4 14   DG  n 
4 15   DA  n 
4 16   DG  n 
4 17   DA  n 
4 18   DC  n 
4 19   DG  n 
4 20   DA  n 
4 21   DC  n 
4 22   DA  n 
4 23   DA  n 
4 24   DA  n 
4 25   DG  n 
4 26   DC  n 
4 27   DA  n 
4 28   DC  n 
4 29   DT  n 
4 30   DA  n 
4 31   DC  n 
# 
_entity_src_gen.entity_id                          2 
_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 42 'synthetic construct' ? 32630 ? 
3 1 sample 1 31 'synthetic construct' ? 32630 ? 
4 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    U   1    1    ?    ?   ?   B . n 
A 1 2    U   2    2    ?    ?   ?   B . n 
A 1 3    U   3    3    ?    ?   ?   B . n 
A 1 4    A   4    4    4    A   A   B . n 
A 1 5    A   5    5    5    A   A   B . n 
A 1 6    U   6    6    6    U   U   B . n 
A 1 7    U   7    7    7    U   U   B . n 
A 1 8    U   8    8    8    U   U   B . n 
A 1 9    C   9    9    9    C   C   B . n 
A 1 10   U   10   10   10   U   U   B . n 
A 1 11   A   11   11   11   A   A   B . n 
A 1 12   C   12   12   12   C   C   B . n 
A 1 13   U   13   13   13   U   U   B . n 
A 1 14   C   14   14   14   C   C   B . n 
A 1 15   U   15   15   15   U   U   B . n 
A 1 16   U   16   16   16   U   U   B . n 
A 1 17   G   17   17   17   G   G   B . n 
A 1 18   U   18   18   18   U   U   B . n 
A 1 19   A   19   19   19   A   A   B . n 
A 1 20   G   20   20   20   G   G   B . n 
A 1 21   A   21   21   21   A   A   B . n 
A 1 22   U   22   22   22   U   U   B . n 
A 1 23   A   23   23   23   A   A   B . n 
A 1 24   G   24   24   24   G   G   B . n 
A 1 25   C   25   25   25   C   C   B . n 
A 1 26   A   26   26   26   A   A   B . n 
A 1 27   G   27   27   27   G   G   B . n 
A 1 28   A   28   28   28   A   A   B . n 
A 1 29   G   29   29   ?    ?   ?   B . n 
A 1 30   U   30   30   ?    ?   ?   B . n 
A 1 31   A   31   31   ?    ?   ?   B . n 
A 1 32   G   32   32   ?    ?   ?   B . n 
A 1 33   A   33   33   ?    ?   ?   B . n 
A 1 34   C   34   34   ?    ?   ?   B . n 
A 1 35   A   35   35   ?    ?   ?   B . n 
A 1 36   U   36   36   ?    ?   ?   B . n 
A 1 37   A   37   37   ?    ?   ?   B . n 
A 1 38   C   38   38   ?    ?   ?   B . n 
A 1 39   G   39   39   ?    ?   ?   B . n 
A 1 40   C   40   40   ?    ?   ?   B . n 
A 1 41   A   41   41   ?    ?   ?   B . n 
A 1 42   G   42   42   ?    ?   ?   B . n 
B 2 1    SER 1    -2   ?    ?   ?   A . n 
B 2 2    ASN 2    -1   ?    ?   ?   A . n 
B 2 3    ALA 3    0    ?    ?   ?   A . n 
B 2 4    MET 4    1    ?    ?   ?   A . n 
B 2 5    THR 5    2    2    THR THR A . n 
B 2 6    GLN 6    3    3    GLN GLN A . n 
B 2 7    PHE 7    4    4    PHE PHE A . n 
B 2 8    GLU 8    5    5    GLU GLU A . n 
B 2 9    GLY 9    6    6    GLY GLY A . n 
B 2 10   PHE 10   7    7    PHE PHE A . n 
B 2 11   THR 11   8    8    THR THR A . n 
B 2 12   ASN 12   9    9    ASN ASN A . n 
B 2 13   LEU 13   10   10   LEU LEU A . n 
B 2 14   TYR 14   11   11   TYR TYR A . n 
B 2 15   GLN 15   12   12   GLN GLN A . n 
B 2 16   VAL 16   13   13   VAL VAL A . n 
B 2 17   SER 17   14   14   SER SER A . n 
B 2 18   LYS 18   15   15   LYS LYS A . n 
B 2 19   THR 19   16   16   THR THR A . n 
B 2 20   LEU 20   17   17   LEU LEU A . n 
B 2 21   ARG 21   18   18   ARG ARG A . n 
B 2 22   PHE 22   19   19   PHE PHE A . n 
B 2 23   GLU 23   20   20   GLU GLU A . n 
B 2 24   LEU 24   21   21   LEU LEU A . n 
B 2 25   ILE 25   22   22   ILE ILE A . n 
B 2 26   PRO 26   23   23   PRO PRO A . n 
B 2 27   GLN 27   24   24   GLN GLN A . n 
B 2 28   GLY 28   25   25   GLY GLY A . n 
B 2 29   LYS 29   26   26   LYS LYS A . n 
B 2 30   THR 30   27   27   THR THR A . n 
B 2 31   LEU 31   28   28   LEU LEU A . n 
B 2 32   LYS 32   29   29   LYS LYS A . n 
B 2 33   HIS 33   30   30   HIS HIS A . n 
B 2 34   ILE 34   31   31   ILE ILE A . n 
B 2 35   GLN 35   32   32   GLN GLN A . n 
B 2 36   GLU 36   33   33   GLU GLU A . n 
B 2 37   GLN 37   34   34   GLN GLN A . n 
B 2 38   GLY 38   35   35   GLY GLY A . n 
B 2 39   PHE 39   36   36   PHE PHE A . n 
B 2 40   ILE 40   37   37   ILE ILE A . n 
B 2 41   GLU 41   38   38   GLU GLU A . n 
B 2 42   GLU 42   39   39   GLU GLU A . n 
B 2 43   ASP 43   40   40   ASP ASP A . n 
B 2 44   LYS 44   41   41   LYS LYS A . n 
B 2 45   ALA 45   42   42   ALA ALA A . n 
B 2 46   ARG 46   43   43   ARG ARG A . n 
B 2 47   ASN 47   44   44   ASN ASN A . n 
B 2 48   ASP 48   45   45   ASP ASP A . n 
B 2 49   HIS 49   46   46   HIS HIS A . n 
B 2 50   TYR 50   47   47   TYR TYR A . n 
B 2 51   LYS 51   48   48   LYS LYS A . n 
B 2 52   GLU 52   49   49   GLU GLU A . n 
B 2 53   LEU 53   50   50   LEU LEU A . n 
B 2 54   LYS 54   51   51   LYS LYS A . n 
B 2 55   PRO 55   52   52   PRO PRO A . n 
B 2 56   ILE 56   53   53   ILE ILE A . n 
B 2 57   ILE 57   54   54   ILE ILE A . n 
B 2 58   ASP 58   55   55   ASP ASP A . n 
B 2 59   ARG 59   56   56   ARG ARG A . n 
B 2 60   ILE 60   57   57   ILE ILE A . n 
B 2 61   TYR 61   58   58   TYR TYR A . n 
B 2 62   LYS 62   59   59   LYS LYS A . n 
B 2 63   THR 63   60   60   THR THR A . n 
B 2 64   TYR 64   61   61   TYR TYR A . n 
B 2 65   ALA 65   62   62   ALA ALA A . n 
B 2 66   ASP 66   63   63   ASP ASP A . n 
B 2 67   GLN 67   64   64   GLN GLN A . n 
B 2 68   CYS 68   65   65   CYS CYS A . n 
B 2 69   LEU 69   66   66   LEU LEU A . n 
B 2 70   GLN 70   67   67   GLN GLN A . n 
B 2 71   LEU 71   68   68   LEU LEU A . n 
B 2 72   VAL 72   69   69   VAL VAL A . n 
B 2 73   GLN 73   70   70   GLN GLN A . n 
B 2 74   LEU 74   71   71   LEU LEU A . n 
B 2 75   ASP 75   72   72   ASP ASP A . n 
B 2 76   TRP 76   73   73   TRP TRP A . n 
B 2 77   GLU 77   74   74   GLU GLU A . n 
B 2 78   ASN 78   75   75   ASN ASN A . n 
B 2 79   LEU 79   76   76   LEU LEU A . n 
B 2 80   SER 80   77   77   SER SER A . n 
B 2 81   ALA 81   78   78   ALA ALA A . n 
B 2 82   ALA 82   79   79   ALA ALA A . n 
B 2 83   ILE 83   80   80   ILE ILE A . n 
B 2 84   ASP 84   81   81   ASP ASP A . n 
B 2 85   SER 85   82   82   SER SER A . n 
B 2 86   TYR 86   83   83   TYR TYR A . n 
B 2 87   ARG 87   84   84   ARG ARG A . n 
B 2 88   LYS 88   85   85   LYS LYS A . n 
B 2 89   GLU 89   86   86   GLU GLU A . n 
B 2 90   LYS 90   87   87   LYS LYS A . n 
B 2 91   THR 91   88   88   THR THR A . n 
B 2 92   GLU 92   89   89   GLU GLU A . n 
B 2 93   GLU 93   90   90   GLU GLU A . n 
B 2 94   THR 94   91   91   THR THR A . n 
B 2 95   ARG 95   92   92   ARG ARG A . n 
B 2 96   ASN 96   93   93   ASN ASN A . n 
B 2 97   ALA 97   94   94   ALA ALA A . n 
B 2 98   LEU 98   95   95   LEU LEU A . n 
B 2 99   ILE 99   96   96   ILE ILE A . n 
B 2 100  GLU 100  97   97   GLU GLU A . n 
B 2 101  GLU 101  98   98   GLU GLU A . n 
B 2 102  GLN 102  99   99   GLN GLN A . n 
B 2 103  ALA 103  100  100  ALA ALA A . n 
B 2 104  THR 104  101  101  THR THR A . n 
B 2 105  TYR 105  102  102  TYR TYR A . n 
B 2 106  ARG 106  103  103  ARG ARG A . n 
B 2 107  ASN 107  104  104  ASN ASN A . n 
B 2 108  ALA 108  105  105  ALA ALA A . n 
B 2 109  ILE 109  106  106  ILE ILE A . n 
B 2 110  HIS 110  107  107  HIS HIS A . n 
B 2 111  ASP 111  108  108  ASP ASP A . n 
B 2 112  TYR 112  109  109  TYR TYR A . n 
B 2 113  PHE 113  110  110  PHE PHE A . n 
B 2 114  ILE 114  111  111  ILE ILE A . n 
B 2 115  GLY 115  112  112  GLY GLY A . n 
B 2 116  ARG 116  113  113  ARG ARG A . n 
B 2 117  THR 117  114  114  THR THR A . n 
B 2 118  ASP 118  115  115  ASP ASP A . n 
B 2 119  ASN 119  116  116  ASN ASN A . n 
B 2 120  LEU 120  117  117  LEU LEU A . n 
B 2 121  THR 121  118  118  THR THR A . n 
B 2 122  ASP 122  119  119  ASP ASP A . n 
B 2 123  ALA 123  120  120  ALA ALA A . n 
B 2 124  ILE 124  121  121  ILE ILE A . n 
B 2 125  ASN 125  122  122  ASN ASN A . n 
B 2 126  LYS 126  123  123  LYS LYS A . n 
B 2 127  ARG 127  124  124  ARG ARG A . n 
B 2 128  HIS 128  125  125  HIS HIS A . n 
B 2 129  ALA 129  126  126  ALA ALA A . n 
B 2 130  GLU 130  127  127  GLU GLU A . n 
B 2 131  ILE 131  128  128  ILE ILE A . n 
B 2 132  TYR 132  129  129  TYR TYR A . n 
B 2 133  LYS 133  130  130  LYS LYS A . n 
B 2 134  GLY 134  131  131  GLY GLY A . n 
B 2 135  LEU 135  132  132  LEU LEU A . n 
B 2 136  PHE 136  133  133  PHE PHE A . n 
B 2 137  LYS 137  134  134  LYS LYS A . n 
B 2 138  ALA 138  135  135  ALA ALA A . n 
B 2 139  GLU 139  136  136  GLU GLU A . n 
B 2 140  LEU 140  137  137  LEU LEU A . n 
B 2 141  PHE 141  138  138  PHE PHE A . n 
B 2 142  ASN 142  139  139  ASN ASN A . n 
B 2 143  GLY 143  140  140  GLY GLY A . n 
B 2 144  LYS 144  141  141  LYS LYS A . n 
B 2 145  VAL 145  142  142  VAL VAL A . n 
B 2 146  LEU 146  143  143  LEU LEU A . n 
B 2 147  LYS 147  144  144  LYS LYS A . n 
B 2 148  GLN 148  145  145  GLN GLN A . n 
B 2 149  LEU 149  146  146  LEU LEU A . n 
B 2 150  GLY 150  147  ?    ?   ?   A . n 
B 2 151  THR 151  148  ?    ?   ?   A . n 
B 2 152  VAL 152  149  ?    ?   ?   A . n 
B 2 153  THR 153  150  150  THR THR A . n 
B 2 154  THR 154  151  151  THR THR A . n 
B 2 155  THR 155  152  152  THR THR A . n 
B 2 156  GLU 156  153  153  GLU GLU A . n 
B 2 157  HIS 157  154  154  HIS HIS A . n 
B 2 158  GLU 158  155  155  GLU GLU A . n 
B 2 159  ASN 159  156  156  ASN ASN A . n 
B 2 160  ALA 160  157  157  ALA ALA A . n 
B 2 161  LEU 161  158  158  LEU LEU A . n 
B 2 162  LEU 162  159  159  LEU LEU A . n 
B 2 163  ARG 163  160  160  ARG ARG A . n 
B 2 164  SER 164  161  161  SER SER A . n 
B 2 165  PHE 165  162  162  PHE PHE A . n 
B 2 166  ASP 166  163  163  ASP ASP A . n 
B 2 167  LYS 167  164  164  LYS LYS A . n 
B 2 168  PHE 168  165  165  PHE PHE A . n 
B 2 169  THR 169  166  166  THR THR A . n 
B 2 170  THR 170  167  167  THR THR A . n 
B 2 171  TYR 171  168  168  TYR TYR A . n 
B 2 172  PHE 172  169  169  PHE PHE A . n 
B 2 173  SER 173  170  170  SER SER A . n 
B 2 174  GLY 174  171  171  GLY GLY A . n 
B 2 175  PHE 175  172  172  PHE PHE A . n 
B 2 176  TYR 176  173  173  TYR TYR A . n 
B 2 177  GLU 177  174  174  GLU GLU A . n 
B 2 178  ASN 178  175  175  ASN ASN A . n 
B 2 179  ARG 179  176  176  ARG ARG A . n 
B 2 180  LYS 180  177  177  LYS LYS A . n 
B 2 181  ASN 181  178  178  ASN ASN A . n 
B 2 182  VAL 182  179  179  VAL VAL A . n 
B 2 183  PHE 183  180  180  PHE PHE A . n 
B 2 184  SER 184  181  181  SER SER A . n 
B 2 185  ALA 185  182  182  ALA ALA A . n 
B 2 186  GLU 186  183  183  GLU GLU A . n 
B 2 187  ASP 187  184  184  ASP ASP A . n 
B 2 188  ILE 188  185  185  ILE ILE A . n 
B 2 189  SER 189  186  186  SER SER A . n 
B 2 190  THR 190  187  187  THR THR A . n 
B 2 191  ALA 191  188  188  ALA ALA A . n 
B 2 192  ILE 192  189  189  ILE ILE A . n 
B 2 193  PRO 193  190  190  PRO PRO A . n 
B 2 194  HIS 194  191  191  HIS HIS A . n 
B 2 195  ARG 195  192  192  ARG ARG A . n 
B 2 196  ILE 196  193  193  ILE ILE A . n 
B 2 197  VAL 197  194  194  VAL VAL A . n 
B 2 198  GLN 198  195  195  GLN GLN A . n 
B 2 199  ASP 199  196  196  ASP ASP A . n 
B 2 200  ASN 200  197  197  ASN ASN A . n 
B 2 201  PHE 201  198  198  PHE PHE A . n 
B 2 202  PRO 202  199  199  PRO PRO A . n 
B 2 203  LYS 203  200  200  LYS LYS A . n 
B 2 204  PHE 204  201  201  PHE PHE A . n 
B 2 205  LYS 205  202  202  LYS LYS A . n 
B 2 206  GLU 206  203  203  GLU GLU A . n 
B 2 207  ASN 207  204  204  ASN ASN A . n 
B 2 208  CYS 208  205  205  CYS CYS A . n 
B 2 209  HIS 209  206  206  HIS HIS A . n 
B 2 210  ILE 210  207  207  ILE ILE A . n 
B 2 211  PHE 211  208  208  PHE PHE A . n 
B 2 212  THR 212  209  209  THR THR A . n 
B 2 213  ARG 213  210  210  ARG ARG A . n 
B 2 214  LEU 214  211  211  LEU LEU A . n 
B 2 215  ILE 215  212  212  ILE ILE A . n 
B 2 216  THR 216  213  213  THR THR A . n 
B 2 217  ALA 217  214  214  ALA ALA A . n 
B 2 218  VAL 218  215  215  VAL VAL A . n 
B 2 219  PRO 219  216  216  PRO PRO A . n 
B 2 220  SER 220  217  217  SER SER A . n 
B 2 221  LEU 221  218  218  LEU LEU A . n 
B 2 222  ARG 222  219  219  ARG ARG A . n 
B 2 223  GLU 223  220  220  GLU GLU A . n 
B 2 224  HIS 224  221  221  HIS HIS A . n 
B 2 225  PHE 225  222  222  PHE PHE A . n 
B 2 226  GLU 226  223  223  GLU GLU A . n 
B 2 227  ASN 227  224  224  ASN ASN A . n 
B 2 228  VAL 228  225  225  VAL VAL A . n 
B 2 229  LYS 229  226  226  LYS LYS A . n 
B 2 230  LYS 230  227  227  LYS LYS A . n 
B 2 231  ALA 231  228  228  ALA ALA A . n 
B 2 232  ILE 232  229  229  ILE ILE A . n 
B 2 233  GLY 233  230  230  GLY GLY A . n 
B 2 234  ILE 234  231  231  ILE ILE A . n 
B 2 235  PHE 235  232  232  PHE PHE A . n 
B 2 236  VAL 236  233  233  VAL VAL A . n 
B 2 237  SER 237  234  234  SER SER A . n 
B 2 238  THR 238  235  235  THR THR A . n 
B 2 239  SER 239  236  236  SER SER A . n 
B 2 240  ILE 240  237  237  ILE ILE A . n 
B 2 241  GLU 241  238  238  GLU GLU A . n 
B 2 242  GLU 242  239  239  GLU GLU A . n 
B 2 243  VAL 243  240  240  VAL VAL A . n 
B 2 244  PHE 244  241  241  PHE PHE A . n 
B 2 245  SER 245  242  242  SER SER A . n 
B 2 246  PHE 246  243  243  PHE PHE A . n 
B 2 247  PRO 247  244  244  PRO PRO A . n 
B 2 248  PHE 248  245  245  PHE PHE A . n 
B 2 249  TYR 249  246  246  TYR TYR A . n 
B 2 250  ASN 250  247  247  ASN ASN A . n 
B 2 251  GLN 251  248  248  GLN GLN A . n 
B 2 252  LEU 252  249  249  LEU LEU A . n 
B 2 253  LEU 253  250  250  LEU LEU A . n 
B 2 254  THR 254  251  251  THR THR A . n 
B 2 255  GLN 255  252  252  GLN GLN A . n 
B 2 256  THR 256  253  253  THR THR A . n 
B 2 257  GLN 257  254  254  GLN GLN A . n 
B 2 258  ILE 258  255  255  ILE ILE A . n 
B 2 259  ASP 259  256  256  ASP ASP A . n 
B 2 260  LEU 260  257  257  LEU LEU A . n 
B 2 261  TYR 261  258  258  TYR TYR A . n 
B 2 262  ASN 262  259  259  ASN ASN A . n 
B 2 263  GLN 263  260  260  GLN GLN A . n 
B 2 264  LEU 264  261  261  LEU LEU A . n 
B 2 265  LEU 265  262  262  LEU LEU A . n 
B 2 266  GLY 266  263  263  GLY GLY A . n 
B 2 267  GLY 267  264  264  GLY GLY A . n 
B 2 268  ILE 268  265  ?    ?   ?   A . n 
B 2 269  SER 269  266  ?    ?   ?   A . n 
B 2 270  ARG 270  267  ?    ?   ?   A . n 
B 2 271  GLU 271  268  ?    ?   ?   A . n 
B 2 272  ALA 272  269  ?    ?   ?   A . n 
B 2 273  GLY 273  270  ?    ?   ?   A . n 
B 2 274  THR 274  271  ?    ?   ?   A . n 
B 2 275  GLU 275  272  ?    ?   ?   A . n 
B 2 276  LYS 276  273  ?    ?   ?   A . n 
B 2 277  ILE 277  274  ?    ?   ?   A . n 
B 2 278  LYS 278  275  ?    ?   ?   A . n 
B 2 279  GLY 279  276  ?    ?   ?   A . n 
B 2 280  LEU 280  277  ?    ?   ?   A . n 
B 2 281  ASN 281  278  ?    ?   ?   A . n 
B 2 282  GLU 282  279  ?    ?   ?   A . n 
B 2 283  VAL 283  280  ?    ?   ?   A . n 
B 2 284  LEU 284  281  ?    ?   ?   A . n 
B 2 285  ASN 285  282  ?    ?   ?   A . n 
B 2 286  LEU 286  283  ?    ?   ?   A . n 
B 2 287  ALA 287  284  ?    ?   ?   A . n 
B 2 288  ILE 288  285  ?    ?   ?   A . n 
B 2 289  GLN 289  286  ?    ?   ?   A . n 
B 2 290  LYS 290  287  ?    ?   ?   A . n 
B 2 291  ASN 291  288  ?    ?   ?   A . n 
B 2 292  ASP 292  289  ?    ?   ?   A . n 
B 2 293  GLU 293  290  ?    ?   ?   A . n 
B 2 294  THR 294  291  ?    ?   ?   A . n 
B 2 295  ALA 295  292  ?    ?   ?   A . n 
B 2 296  HIS 296  293  ?    ?   ?   A . n 
B 2 297  ILE 297  294  ?    ?   ?   A . n 
B 2 298  ILE 298  295  ?    ?   ?   A . n 
B 2 299  ALA 299  296  ?    ?   ?   A . n 
B 2 300  SER 300  297  ?    ?   ?   A . n 
B 2 301  LEU 301  298  ?    ?   ?   A . n 
B 2 302  PRO 302  299  ?    ?   ?   A . n 
B 2 303  HIS 303  300  ?    ?   ?   A . n 
B 2 304  ARG 304  301  ?    ?   ?   A . n 
B 2 305  PHE 305  302  ?    ?   ?   A . n 
B 2 306  ILE 306  303  ?    ?   ?   A . n 
B 2 307  PRO 307  304  ?    ?   ?   A . n 
B 2 308  LEU 308  305  ?    ?   ?   A . n 
B 2 309  PHE 309  306  ?    ?   ?   A . n 
B 2 310  LYS 310  307  ?    ?   ?   A . n 
B 2 311  GLN 311  308  ?    ?   ?   A . n 
B 2 312  ILE 312  309  ?    ?   ?   A . n 
B 2 313  LEU 313  310  ?    ?   ?   A . n 
B 2 314  SER 314  311  ?    ?   ?   A . n 
B 2 315  ASP 315  312  ?    ?   ?   A . n 
B 2 316  ARG 316  313  ?    ?   ?   A . n 
B 2 317  ASN 317  314  ?    ?   ?   A . n 
B 2 318  THR 318  315  ?    ?   ?   A . n 
B 2 319  LEU 319  316  ?    ?   ?   A . n 
B 2 320  SER 320  317  ?    ?   ?   A . n 
B 2 321  PHE 321  318  ?    ?   ?   A . n 
B 2 322  ILE 322  319  ?    ?   ?   A . n 
B 2 323  LEU 323  320  ?    ?   ?   A . n 
B 2 324  GLU 324  321  ?    ?   ?   A . n 
B 2 325  GLU 325  322  ?    ?   ?   A . n 
B 2 326  PHE 326  323  ?    ?   ?   A . n 
B 2 327  LYS 327  324  324  LYS LYS A . n 
B 2 328  SER 328  325  325  SER SER A . n 
B 2 329  ASP 329  326  326  ASP ASP A . n 
B 2 330  GLU 330  327  327  GLU GLU A . n 
B 2 331  GLU 331  328  328  GLU GLU A . n 
B 2 332  VAL 332  329  329  VAL VAL A . n 
B 2 333  ILE 333  330  330  ILE ILE A . n 
B 2 334  GLN 334  331  331  GLN GLN A . n 
B 2 335  SER 335  332  332  SER SER A . n 
B 2 336  PHE 336  333  333  PHE PHE A . n 
B 2 337  CYS 337  334  334  CYS CYS A . n 
B 2 338  LYS 338  335  335  LYS LYS A . n 
B 2 339  TYR 339  336  336  TYR TYR A . n 
B 2 340  LYS 340  337  337  LYS LYS A . n 
B 2 341  THR 341  338  338  THR THR A . n 
B 2 342  LEU 342  339  339  LEU LEU A . n 
B 2 343  LEU 343  340  340  LEU LEU A . n 
B 2 344  ARG 344  341  341  ARG ARG A . n 
B 2 345  ASN 345  342  342  ASN ASN A . n 
B 2 346  GLU 346  343  343  GLU GLU A . n 
B 2 347  ASN 347  344  344  ASN ASN A . n 
B 2 348  VAL 348  345  345  VAL VAL A . n 
B 2 349  LEU 349  346  346  LEU LEU A . n 
B 2 350  GLU 350  347  347  GLU GLU A . n 
B 2 351  THR 351  348  348  THR THR A . n 
B 2 352  ALA 352  349  349  ALA ALA A . n 
B 2 353  GLU 353  350  350  GLU GLU A . n 
B 2 354  ALA 354  351  351  ALA ALA A . n 
B 2 355  LEU 355  352  352  LEU LEU A . n 
B 2 356  PHE 356  353  353  PHE PHE A . n 
B 2 357  ASN 357  354  354  ASN ASN A . n 
B 2 358  GLU 358  355  355  GLU GLU A . n 
B 2 359  LEU 359  356  356  LEU LEU A . n 
B 2 360  ASN 360  357  357  ASN ASN A . n 
B 2 361  SER 361  358  358  SER SER A . n 
B 2 362  ILE 362  359  359  ILE ILE A . n 
B 2 363  ASP 363  360  360  ASP ASP A . n 
B 2 364  LEU 364  361  361  LEU LEU A . n 
B 2 365  THR 365  362  362  THR THR A . n 
B 2 366  HIS 366  363  363  HIS HIS A . n 
B 2 367  ILE 367  364  364  ILE ILE A . n 
B 2 368  PHE 368  365  365  PHE PHE A . n 
B 2 369  ILE 369  366  366  ILE ILE A . n 
B 2 370  SER 370  367  367  SER SER A . n 
B 2 371  HIS 371  368  368  HIS HIS A . n 
B 2 372  LYS 372  369  369  LYS LYS A . n 
B 2 373  LYS 373  370  370  LYS LYS A . n 
B 2 374  LEU 374  371  371  LEU LEU A . n 
B 2 375  GLU 375  372  372  GLU GLU A . n 
B 2 376  THR 376  373  373  THR THR A . n 
B 2 377  ILE 377  374  374  ILE ILE A . n 
B 2 378  SER 378  375  375  SER SER A . n 
B 2 379  SER 379  376  376  SER SER A . n 
B 2 380  ALA 380  377  377  ALA ALA A . n 
B 2 381  LEU 381  378  378  LEU LEU A . n 
B 2 382  CYS 382  379  379  CYS CYS A . n 
B 2 383  ASP 383  380  380  ASP ASP A . n 
B 2 384  HIS 384  381  381  HIS HIS A . n 
B 2 385  TRP 385  382  382  TRP TRP A . n 
B 2 386  ASP 386  383  383  ASP ASP A . n 
B 2 387  THR 387  384  384  THR THR A . n 
B 2 388  LEU 388  385  385  LEU LEU A . n 
B 2 389  ARG 389  386  386  ARG ARG A . n 
B 2 390  ASN 390  387  387  ASN ASN A . n 
B 2 391  ALA 391  388  388  ALA ALA A . n 
B 2 392  LEU 392  389  389  LEU LEU A . n 
B 2 393  TYR 393  390  390  TYR TYR A . n 
B 2 394  GLU 394  391  391  GLU GLU A . n 
B 2 395  ARG 395  392  392  ARG ARG A . n 
B 2 396  ARG 396  393  393  ARG ARG A . n 
B 2 397  ILE 397  394  394  ILE ILE A . n 
B 2 398  SER 398  395  395  SER SER A . n 
B 2 399  GLU 399  396  396  GLU GLU A . n 
B 2 400  LEU 400  397  397  LEU LEU A . n 
B 2 401  THR 401  398  398  THR THR A . n 
B 2 402  GLY 402  399  399  GLY GLY A . n 
B 2 403  LYS 403  400  400  LYS LYS A . n 
B 2 404  ILE 404  401  401  ILE ILE A . n 
B 2 405  THR 405  402  402  THR THR A . n 
B 2 406  LYS 406  403  403  LYS LYS A . n 
B 2 407  SER 407  404  404  SER SER A . n 
B 2 408  ALA 408  405  405  ALA ALA A . n 
B 2 409  LYS 409  406  406  LYS LYS A . n 
B 2 410  GLU 410  407  407  GLU GLU A . n 
B 2 411  LYS 411  408  408  LYS LYS A . n 
B 2 412  VAL 412  409  409  VAL VAL A . n 
B 2 413  GLN 413  410  410  GLN GLN A . n 
B 2 414  ARG 414  411  411  ARG ARG A . n 
B 2 415  SER 415  412  412  SER SER A . n 
B 2 416  LEU 416  413  413  LEU LEU A . n 
B 2 417  LYS 417  414  414  LYS LYS A . n 
B 2 418  HIS 418  415  415  HIS HIS A . n 
B 2 419  GLU 419  416  416  GLU GLU A . n 
B 2 420  ASP 420  417  417  ASP ASP A . n 
B 2 421  ILE 421  418  418  ILE ILE A . n 
B 2 422  ASN 422  419  419  ASN ASN A . n 
B 2 423  LEU 423  420  420  LEU LEU A . n 
B 2 424  GLN 424  421  421  GLN GLN A . n 
B 2 425  GLU 425  422  422  GLU GLU A . n 
B 2 426  ILE 426  423  423  ILE ILE A . n 
B 2 427  ILE 427  424  424  ILE ILE A . n 
B 2 428  SER 428  425  425  SER SER A . n 
B 2 429  ALA 429  426  426  ALA ALA A . n 
B 2 430  ALA 430  427  427  ALA ALA A . n 
B 2 431  GLY 431  428  428  GLY GLY A . n 
B 2 432  LYS 432  429  429  LYS LYS A . n 
B 2 433  GLU 433  430  430  GLU GLU A . n 
B 2 434  LEU 434  431  431  LEU LEU A . n 
B 2 435  SER 435  432  432  SER SER A . n 
B 2 436  GLU 436  433  433  GLU GLU A . n 
B 2 437  ALA 437  434  434  ALA ALA A . n 
B 2 438  PHE 438  435  435  PHE PHE A . n 
B 2 439  LYS 439  436  436  LYS LYS A . n 
B 2 440  GLN 440  437  437  GLN GLN A . n 
B 2 441  LYS 441  438  438  LYS LYS A . n 
B 2 442  THR 442  439  439  THR THR A . n 
B 2 443  SER 443  440  440  SER SER A . n 
B 2 444  GLU 444  441  441  GLU GLU A . n 
B 2 445  ILE 445  442  442  ILE ILE A . n 
B 2 446  LEU 446  443  443  LEU LEU A . n 
B 2 447  SER 447  444  444  SER SER A . n 
B 2 448  HIS 448  445  445  HIS HIS A . n 
B 2 449  ALA 449  446  446  ALA ALA A . n 
B 2 450  HIS 450  447  447  HIS HIS A . n 
B 2 451  ALA 451  448  448  ALA ALA A . n 
B 2 452  ALA 452  449  449  ALA ALA A . n 
B 2 453  LEU 453  450  450  LEU LEU A . n 
B 2 454  ASP 454  451  451  ASP ASP A . n 
B 2 455  GLN 455  452  452  GLN GLN A . n 
B 2 456  PRO 456  453  453  PRO PRO A . n 
B 2 457  LEU 457  454  454  LEU LEU A . n 
B 2 458  PRO 458  455  455  PRO PRO A . n 
B 2 459  THR 459  456  456  THR THR A . n 
B 2 460  THR 460  457  457  THR THR A . n 
B 2 461  LEU 461  458  458  LEU LEU A . n 
B 2 462  LYS 462  459  459  LYS LYS A . n 
B 2 463  LYS 463  460  460  LYS LYS A . n 
B 2 464  GLN 464  461  461  GLN GLN A . n 
B 2 465  GLU 465  462  462  GLU GLU A . n 
B 2 466  GLU 466  463  463  GLU GLU A . n 
B 2 467  LYS 467  464  464  LYS LYS A . n 
B 2 468  GLU 468  465  465  GLU GLU A . n 
B 2 469  ILE 469  466  466  ILE ILE A . n 
B 2 470  LEU 470  467  467  LEU LEU A . n 
B 2 471  LYS 471  468  468  LYS LYS A . n 
B 2 472  SER 472  469  469  SER SER A . n 
B 2 473  GLN 473  470  470  GLN GLN A . n 
B 2 474  LEU 474  471  471  LEU LEU A . n 
B 2 475  ASP 475  472  472  ASP ASP A . n 
B 2 476  SER 476  473  473  SER SER A . n 
B 2 477  LEU 477  474  474  LEU LEU A . n 
B 2 478  LEU 478  475  475  LEU LEU A . n 
B 2 479  GLY 479  476  476  GLY GLY A . n 
B 2 480  LEU 480  477  477  LEU LEU A . n 
B 2 481  TYR 481  478  478  TYR TYR A . n 
B 2 482  HIS 482  479  479  HIS HIS A . n 
B 2 483  LEU 483  480  480  LEU LEU A . n 
B 2 484  LEU 484  481  481  LEU LEU A . n 
B 2 485  ASP 485  482  482  ASP ASP A . n 
B 2 486  TRP 486  483  483  TRP TRP A . n 
B 2 487  PHE 487  484  484  PHE PHE A . n 
B 2 488  ALA 488  485  485  ALA ALA A . n 
B 2 489  VAL 489  486  486  VAL VAL A . n 
B 2 490  ASP 490  487  487  ASP ASP A . n 
B 2 491  GLU 491  488  488  GLU GLU A . n 
B 2 492  SER 492  489  489  SER SER A . n 
B 2 493  ASN 493  490  490  ASN ASN A . n 
B 2 494  GLU 494  491  491  GLU GLU A . n 
B 2 495  VAL 495  492  492  VAL VAL A . n 
B 2 496  ASP 496  493  493  ASP ASP A . n 
B 2 497  PRO 497  494  494  PRO PRO A . n 
B 2 498  GLU 498  495  495  GLU GLU A . n 
B 2 499  PHE 499  496  496  PHE PHE A . n 
B 2 500  SER 500  497  497  SER SER A . n 
B 2 501  ALA 501  498  498  ALA ALA A . n 
B 2 502  ARG 502  499  499  ARG ARG A . n 
B 2 503  LEU 503  500  500  LEU LEU A . n 
B 2 504  THR 504  501  501  THR THR A . n 
B 2 505  GLY 505  502  502  GLY GLY A . n 
B 2 506  ILE 506  503  503  ILE ILE A . n 
B 2 507  LYS 507  504  504  LYS LYS A . n 
B 2 508  LEU 508  505  505  LEU LEU A . n 
B 2 509  GLU 509  506  506  GLU GLU A . n 
B 2 510  MET 510  507  507  MET MET A . n 
B 2 511  GLU 511  508  508  GLU GLU A . n 
B 2 512  PRO 512  509  509  PRO PRO A . n 
B 2 513  SER 513  510  510  SER SER A . n 
B 2 514  LEU 514  511  511  LEU LEU A . n 
B 2 515  SER 515  512  512  SER SER A . n 
B 2 516  PHE 516  513  513  PHE PHE A . n 
B 2 517  TYR 517  514  514  TYR TYR A . n 
B 2 518  ASN 518  515  515  ASN ASN A . n 
B 2 519  LYS 519  516  516  LYS LYS A . n 
B 2 520  ALA 520  517  517  ALA ALA A . n 
B 2 521  ARG 521  518  518  ARG ARG A . n 
B 2 522  ASN 522  519  519  ASN ASN A . n 
B 2 523  TYR 523  520  520  TYR TYR A . n 
B 2 524  ALA 524  521  521  ALA ALA A . n 
B 2 525  THR 525  522  522  THR THR A . n 
B 2 526  LYS 526  523  523  LYS LYS A . n 
B 2 527  LYS 527  524  524  LYS LYS A . n 
B 2 528  PRO 528  525  525  PRO PRO A . n 
B 2 529  TYR 529  526  526  TYR TYR A . n 
B 2 530  SER 530  527  527  SER SER A . n 
B 2 531  VAL 531  528  528  VAL VAL A . n 
B 2 532  GLU 532  529  529  GLU GLU A . n 
B 2 533  LYS 533  530  530  LYS LYS A . n 
B 2 534  PHE 534  531  531  PHE PHE A . n 
B 2 535  LYS 535  532  532  LYS LYS A . n 
B 2 536  LEU 536  533  533  LEU LEU A . n 
B 2 537  ASN 537  534  534  ASN ASN A . n 
B 2 538  PHE 538  535  535  PHE PHE A . n 
B 2 539  GLN 539  536  536  GLN GLN A . n 
B 2 540  MET 540  537  537  MET MET A . n 
B 2 541  PRO 541  538  538  PRO PRO A . n 
B 2 542  THR 542  539  539  THR THR A . n 
B 2 543  LEU 543  540  540  LEU LEU A . n 
B 2 544  ALA 544  541  541  ALA ALA A . n 
B 2 545  SER 545  542  542  SER SER A . n 
B 2 546  GLY 546  543  543  GLY GLY A . n 
B 2 547  TRP 547  544  544  TRP TRP A . n 
B 2 548  ASP 548  545  545  ASP ASP A . n 
B 2 549  VAL 549  546  546  VAL VAL A . n 
B 2 550  ASN 550  547  547  ASN ASN A . n 
B 2 551  LYS 551  548  548  LYS LYS A . n 
B 2 552  GLU 552  549  549  GLU GLU A . n 
B 2 553  LYS 553  550  550  LYS LYS A . n 
B 2 554  CYS 554  551  551  CYS CYS A . n 
B 2 555  ASN 555  552  552  ASN ASN A . n 
B 2 556  GLY 556  553  553  GLY GLY A . n 
B 2 557  ALA 557  554  554  ALA ALA A . n 
B 2 558  ILE 558  555  555  ILE ILE A . n 
B 2 559  LEU 559  556  556  LEU LEU A . n 
B 2 560  PHE 560  557  557  PHE PHE A . n 
B 2 561  VAL 561  558  558  VAL VAL A . n 
B 2 562  LYS 562  559  559  LYS LYS A . n 
B 2 563  ASN 563  560  560  ASN ASN A . n 
B 2 564  GLY 564  561  561  GLY GLY A . n 
B 2 565  LEU 565  562  562  LEU LEU A . n 
B 2 566  TYR 566  563  563  TYR TYR A . n 
B 2 567  TYR 567  564  564  TYR TYR A . n 
B 2 568  LEU 568  565  565  LEU LEU A . n 
B 2 569  GLY 569  566  566  GLY GLY A . n 
B 2 570  ILE 570  567  567  ILE ILE A . n 
B 2 571  MET 571  568  568  MET MET A . n 
B 2 572  PRO 572  569  569  PRO PRO A . n 
B 2 573  LYS 573  570  570  LYS LYS A . n 
B 2 574  GLN 574  571  571  GLN GLN A . n 
B 2 575  LYS 575  572  572  LYS LYS A . n 
B 2 576  GLY 576  573  573  GLY GLY A . n 
B 2 577  ARG 577  574  574  ARG ARG A . n 
B 2 578  TYR 578  575  575  TYR TYR A . n 
B 2 579  LYS 579  576  576  LYS LYS A . n 
B 2 580  ALA 580  577  577  ALA ALA A . n 
B 2 581  LEU 581  578  578  LEU LEU A . n 
B 2 582  SER 582  579  579  SER SER A . n 
B 2 583  PHE 583  580  580  PHE PHE A . n 
B 2 584  GLU 584  581  581  GLU GLU A . n 
B 2 585  PRO 585  582  582  PRO PRO A . n 
B 2 586  THR 586  583  583  THR THR A . n 
B 2 587  GLU 587  584  584  GLU GLU A . n 
B 2 588  LYS 588  585  585  LYS LYS A . n 
B 2 589  THR 589  586  586  THR THR A . n 
B 2 590  SER 590  587  587  SER SER A . n 
B 2 591  GLU 591  588  588  GLU GLU A . n 
B 2 592  GLY 592  589  589  GLY GLY A . n 
B 2 593  PHE 593  590  590  PHE PHE A . n 
B 2 594  ASP 594  591  591  ASP ASP A . n 
B 2 595  LYS 595  592  592  LYS LYS A . n 
B 2 596  MET 596  593  593  MET MET A . n 
B 2 597  TYR 597  594  594  TYR TYR A . n 
B 2 598  TYR 598  595  595  TYR TYR A . n 
B 2 599  ASP 599  596  596  ASP ASP A . n 
B 2 600  TYR 600  597  597  TYR TYR A . n 
B 2 601  PHE 601  598  598  PHE PHE A . n 
B 2 602  PRO 602  599  599  PRO PRO A . n 
B 2 603  ASP 603  600  600  ASP ASP A . n 
B 2 604  ALA 604  601  601  ALA ALA A . n 
B 2 605  ALA 605  602  602  ALA ALA A . n 
B 2 606  LYS 606  603  603  LYS LYS A . n 
B 2 607  MET 607  604  604  MET MET A . n 
B 2 608  ILE 608  605  605  ILE ILE A . n 
B 2 609  PRO 609  606  606  PRO PRO A . n 
B 2 610  LYS 610  607  607  LYS LYS A . n 
B 2 611  CYS 611  608  608  CYS CYS A . n 
B 2 612  SER 612  609  609  SER SER A . n 
B 2 613  THR 613  610  610  THR THR A . n 
B 2 614  GLN 614  611  611  GLN GLN A . n 
B 2 615  LEU 615  612  612  LEU LEU A . n 
B 2 616  LYS 616  613  613  LYS LYS A . n 
B 2 617  ALA 617  614  614  ALA ALA A . n 
B 2 618  VAL 618  615  615  VAL VAL A . n 
B 2 619  THR 619  616  616  THR THR A . n 
B 2 620  ALA 620  617  617  ALA ALA A . n 
B 2 621  HIS 621  618  618  HIS HIS A . n 
B 2 622  PHE 622  619  619  PHE PHE A . n 
B 2 623  GLN 623  620  620  GLN GLN A . n 
B 2 624  THR 624  621  621  THR THR A . n 
B 2 625  HIS 625  622  622  HIS HIS A . n 
B 2 626  THR 626  623  623  THR THR A . n 
B 2 627  THR 627  624  624  THR THR A . n 
B 2 628  PRO 628  625  625  PRO PRO A . n 
B 2 629  ILE 629  626  626  ILE ILE A . n 
B 2 630  LEU 630  627  627  LEU LEU A . n 
B 2 631  LEU 631  628  628  LEU LEU A . n 
B 2 632  SER 632  629  629  SER SER A . n 
B 2 633  ASN 633  630  630  ASN ASN A . n 
B 2 634  ASN 634  631  631  ASN ASN A . n 
B 2 635  PHE 635  632  632  PHE PHE A . n 
B 2 636  ILE 636  633  633  ILE ILE A . n 
B 2 637  GLU 637  634  634  GLU GLU A . n 
B 2 638  PRO 638  635  635  PRO PRO A . n 
B 2 639  LEU 639  636  636  LEU LEU A . n 
B 2 640  GLU 640  637  637  GLU GLU A . n 
B 2 641  ILE 641  638  638  ILE ILE A . n 
B 2 642  THR 642  639  639  THR THR A . n 
B 2 643  LYS 643  640  640  LYS LYS A . n 
B 2 644  GLU 644  641  641  GLU GLU A . n 
B 2 645  ILE 645  642  642  ILE ILE A . n 
B 2 646  TYR 646  643  643  TYR TYR A . n 
B 2 647  ASP 647  644  644  ASP ASP A . n 
B 2 648  LEU 648  645  645  LEU LEU A . n 
B 2 649  ASN 649  646  646  ASN ASN A . n 
B 2 650  ASN 650  647  647  ASN ASN A . n 
B 2 651  PRO 651  648  ?    ?   ?   A . n 
B 2 652  GLU 652  649  ?    ?   ?   A . n 
B 2 653  LYS 653  650  ?    ?   ?   A . n 
B 2 654  GLU 654  651  ?    ?   ?   A . n 
B 2 655  PRO 655  652  652  PRO PRO A . n 
B 2 656  LYS 656  653  653  LYS LYS A . n 
B 2 657  LYS 657  654  654  LYS LYS A . n 
B 2 658  PHE 658  655  655  PHE PHE A . n 
B 2 659  GLN 659  656  656  GLN GLN A . n 
B 2 660  THR 660  657  657  THR THR A . n 
B 2 661  ALA 661  658  658  ALA ALA A . n 
B 2 662  TYR 662  659  659  TYR TYR A . n 
B 2 663  ALA 663  660  660  ALA ALA A . n 
B 2 664  LYS 664  661  661  LYS LYS A . n 
B 2 665  LYS 665  662  662  LYS LYS A . n 
B 2 666  THR 666  663  663  THR THR A . n 
B 2 667  GLY 667  664  664  GLY GLY A . n 
B 2 668  ASP 668  665  665  ASP ASP A . n 
B 2 669  GLN 669  666  666  GLN GLN A . n 
B 2 670  LYS 670  667  667  LYS LYS A . n 
B 2 671  GLY 671  668  668  GLY GLY A . n 
B 2 672  TYR 672  669  669  TYR TYR A . n 
B 2 673  ARG 673  670  670  ARG ARG A . n 
B 2 674  GLU 674  671  671  GLU GLU A . n 
B 2 675  ALA 675  672  672  ALA ALA A . n 
B 2 676  LEU 676  673  673  LEU LEU A . n 
B 2 677  CYS 677  674  674  CYS CYS A . n 
B 2 678  LYS 678  675  675  LYS LYS A . n 
B 2 679  TRP 679  676  676  TRP TRP A . n 
B 2 680  ILE 680  677  677  ILE ILE A . n 
B 2 681  ASP 681  678  678  ASP ASP A . n 
B 2 682  PHE 682  679  679  PHE PHE A . n 
B 2 683  THR 683  680  680  THR THR A . n 
B 2 684  ARG 684  681  681  ARG ARG A . n 
B 2 685  ASP 685  682  682  ASP ASP A . n 
B 2 686  PHE 686  683  683  PHE PHE A . n 
B 2 687  LEU 687  684  684  LEU LEU A . n 
B 2 688  SER 688  685  685  SER SER A . n 
B 2 689  LYS 689  686  686  LYS LYS A . n 
B 2 690  TYR 690  687  687  TYR TYR A . n 
B 2 691  THR 691  688  688  THR THR A . n 
B 2 692  LYS 692  689  689  LYS LYS A . n 
B 2 693  THR 693  690  690  THR THR A . n 
B 2 694  THR 694  691  691  THR THR A . n 
B 2 695  SER 695  692  692  SER SER A . n 
B 2 696  ILE 696  693  693  ILE ILE A . n 
B 2 697  ASP 697  694  694  ASP ASP A . n 
B 2 698  LEU 698  695  695  LEU LEU A . n 
B 2 699  SER 699  696  696  SER SER A . n 
B 2 700  SER 700  697  697  SER SER A . n 
B 2 701  LEU 701  698  698  LEU LEU A . n 
B 2 702  ARG 702  699  699  ARG ARG A . n 
B 2 703  PRO 703  700  700  PRO PRO A . n 
B 2 704  SER 704  701  701  SER SER A . n 
B 2 705  SER 705  702  702  SER SER A . n 
B 2 706  GLN 706  703  703  GLN GLN A . n 
B 2 707  TYR 707  704  704  TYR TYR A . n 
B 2 708  LYS 708  705  705  LYS LYS A . n 
B 2 709  ASP 709  706  706  ASP ASP A . n 
B 2 710  LEU 710  707  707  LEU LEU A . n 
B 2 711  GLY 711  708  708  GLY GLY A . n 
B 2 712  GLU 712  709  709  GLU GLU A . n 
B 2 713  TYR 713  710  710  TYR TYR A . n 
B 2 714  TYR 714  711  711  TYR TYR A . n 
B 2 715  ALA 715  712  712  ALA ALA A . n 
B 2 716  GLU 716  713  713  GLU GLU A . n 
B 2 717  LEU 717  714  714  LEU LEU A . n 
B 2 718  ASN 718  715  715  ASN ASN A . n 
B 2 719  PRO 719  716  716  PRO PRO A . n 
B 2 720  LEU 720  717  717  LEU LEU A . n 
B 2 721  LEU 721  718  718  LEU LEU A . n 
B 2 722  TYR 722  719  719  TYR TYR A . n 
B 2 723  HIS 723  720  720  HIS HIS A . n 
B 2 724  ILE 724  721  721  ILE ILE A . n 
B 2 725  SER 725  722  722  SER SER A . n 
B 2 726  PHE 726  723  723  PHE PHE A . n 
B 2 727  GLN 727  724  724  GLN GLN A . n 
B 2 728  ARG 728  725  725  ARG ARG A . n 
B 2 729  ILE 729  726  726  ILE ILE A . n 
B 2 730  ALA 730  727  727  ALA ALA A . n 
B 2 731  GLU 731  728  728  GLU GLU A . n 
B 2 732  LYS 732  729  729  LYS LYS A . n 
B 2 733  GLU 733  730  730  GLU GLU A . n 
B 2 734  ILE 734  731  731  ILE ILE A . n 
B 2 735  MET 735  732  732  MET MET A . n 
B 2 736  ASP 736  733  733  ASP ASP A . n 
B 2 737  ALA 737  734  734  ALA ALA A . n 
B 2 738  VAL 738  735  735  VAL VAL A . n 
B 2 739  GLU 739  736  736  GLU GLU A . n 
B 2 740  THR 740  737  737  THR THR A . n 
B 2 741  GLY 741  738  738  GLY GLY A . n 
B 2 742  LYS 742  739  739  LYS LYS A . n 
B 2 743  LEU 743  740  740  LEU LEU A . n 
B 2 744  TYR 744  741  741  TYR TYR A . n 
B 2 745  LEU 745  742  742  LEU LEU A . n 
B 2 746  PHE 746  743  743  PHE PHE A . n 
B 2 747  GLN 747  744  744  GLN GLN A . n 
B 2 748  ILE 748  745  745  ILE ILE A . n 
B 2 749  TYR 749  746  746  TYR TYR A . n 
B 2 750  ASN 750  747  747  ASN ASN A . n 
B 2 751  LYS 751  748  748  LYS LYS A . n 
B 2 752  ASP 752  749  749  ASP ASP A . n 
B 2 753  PHE 753  750  750  PHE PHE A . n 
B 2 754  ALA 754  751  751  ALA ALA A . n 
B 2 755  LYS 755  752  752  LYS LYS A . n 
B 2 756  GLY 756  753  753  GLY GLY A . n 
B 2 757  HIS 757  754  754  HIS HIS A . n 
B 2 758  HIS 758  755  755  HIS HIS A . n 
B 2 759  GLY 759  756  756  GLY GLY A . n 
B 2 760  LYS 760  757  757  LYS LYS A . n 
B 2 761  PRO 761  758  758  PRO PRO A . n 
B 2 762  ASN 762  759  759  ASN ASN A . n 
B 2 763  LEU 763  760  760  LEU LEU A . n 
B 2 764  HIS 764  761  761  HIS HIS A . n 
B 2 765  THR 765  762  762  THR THR A . n 
B 2 766  LEU 766  763  763  LEU LEU A . n 
B 2 767  TYR 767  764  764  TYR TYR A . n 
B 2 768  TRP 768  765  765  TRP TRP A . n 
B 2 769  THR 769  766  766  THR THR A . n 
B 2 770  GLY 770  767  767  GLY GLY A . n 
B 2 771  LEU 771  768  768  LEU LEU A . n 
B 2 772  PHE 772  769  769  PHE PHE A . n 
B 2 773  SER 773  770  770  SER SER A . n 
B 2 774  PRO 774  771  771  PRO PRO A . n 
B 2 775  GLU 775  772  772  GLU GLU A . n 
B 2 776  ASN 776  773  773  ASN ASN A . n 
B 2 777  LEU 777  774  774  LEU LEU A . n 
B 2 778  ALA 778  775  775  ALA ALA A . n 
B 2 779  LYS 779  776  776  LYS LYS A . n 
B 2 780  THR 780  777  777  THR THR A . n 
B 2 781  SER 781  778  778  SER SER A . n 
B 2 782  ILE 782  779  779  ILE ILE A . n 
B 2 783  LYS 783  780  780  LYS LYS A . n 
B 2 784  LEU 784  781  781  LEU LEU A . n 
B 2 785  ASN 785  782  782  ASN ASN A . n 
B 2 786  GLY 786  783  783  GLY GLY A . n 
B 2 787  GLN 787  784  784  GLN GLN A . n 
B 2 788  ALA 788  785  785  ALA ALA A . n 
B 2 789  GLU 789  786  786  GLU GLU A . n 
B 2 790  LEU 790  787  787  LEU LEU A . n 
B 2 791  PHE 791  788  788  PHE PHE A . n 
B 2 792  TYR 792  789  789  TYR TYR A . n 
B 2 793  ARG 793  790  790  ARG ARG A . n 
B 2 794  PRO 794  791  791  PRO PRO A . n 
B 2 795  LYS 795  792  792  LYS LYS A . n 
B 2 796  SER 796  793  793  SER SER A . n 
B 2 797  ARG 797  794  794  ARG ARG A . n 
B 2 798  MET 798  795  795  MET MET A . n 
B 2 799  LYS 799  796  796  LYS LYS A . n 
B 2 800  ARG 800  797  797  ARG ARG A . n 
B 2 801  MET 801  798  798  MET MET A . n 
B 2 802  ALA 802  799  799  ALA ALA A . n 
B 2 803  HIS 803  800  800  HIS HIS A . n 
B 2 804  ARG 804  801  801  ARG ARG A . n 
B 2 805  LEU 805  802  802  LEU LEU A . n 
B 2 806  GLY 806  803  803  GLY GLY A . n 
B 2 807  GLU 807  804  804  GLU GLU A . n 
B 2 808  LYS 808  805  805  LYS LYS A . n 
B 2 809  MET 809  806  806  MET MET A . n 
B 2 810  LEU 810  807  807  LEU LEU A . n 
B 2 811  ASN 811  808  808  ASN ASN A . n 
B 2 812  LYS 812  809  809  LYS LYS A . n 
B 2 813  LYS 813  810  810  LYS LYS A . n 
B 2 814  LEU 814  811  811  LEU LEU A . n 
B 2 815  LYS 815  812  812  LYS LYS A . n 
B 2 816  ASP 816  813  813  ASP ASP A . n 
B 2 817  GLN 817  814  814  GLN GLN A . n 
B 2 818  LYS 818  815  815  LYS LYS A . n 
B 2 819  THR 819  816  816  THR THR A . n 
B 2 820  PRO 820  817  817  PRO PRO A . n 
B 2 821  ILE 821  818  818  ILE ILE A . n 
B 2 822  PRO 822  819  819  PRO PRO A . n 
B 2 823  ASP 823  820  820  ASP ASP A . n 
B 2 824  THR 824  821  821  THR THR A . n 
B 2 825  LEU 825  822  822  LEU LEU A . n 
B 2 826  TYR 826  823  823  TYR TYR A . n 
B 2 827  GLN 827  824  824  GLN GLN A . n 
B 2 828  GLU 828  825  825  GLU GLU A . n 
B 2 829  LEU 829  826  826  LEU LEU A . n 
B 2 830  TYR 830  827  827  TYR TYR A . n 
B 2 831  ASP 831  828  828  ASP ASP A . n 
B 2 832  TYR 832  829  829  TYR TYR A . n 
B 2 833  VAL 833  830  830  VAL VAL A . n 
B 2 834  ASN 834  831  831  ASN ASN A . n 
B 2 835  HIS 835  832  832  HIS HIS A . n 
B 2 836  ARG 836  833  833  ARG ARG A . n 
B 2 837  LEU 837  834  834  LEU LEU A . n 
B 2 838  SER 838  835  835  SER SER A . n 
B 2 839  HIS 839  836  836  HIS HIS A . n 
B 2 840  ASP 840  837  837  ASP ASP A . n 
B 2 841  LEU 841  838  838  LEU LEU A . n 
B 2 842  SER 842  839  839  SER SER A . n 
B 2 843  ASP 843  840  840  ASP ASP A . n 
B 2 844  GLU 844  841  841  GLU GLU A . n 
B 2 845  ALA 845  842  842  ALA ALA A . n 
B 2 846  ARG 846  843  843  ARG ARG A . n 
B 2 847  ALA 847  844  844  ALA ALA A . n 
B 2 848  LEU 848  845  845  LEU LEU A . n 
B 2 849  LEU 849  846  846  LEU LEU A . n 
B 2 850  PRO 850  847  847  PRO PRO A . n 
B 2 851  ASN 851  848  848  ASN ASN A . n 
B 2 852  VAL 852  849  849  VAL VAL A . n 
B 2 853  ILE 853  850  850  ILE ILE A . n 
B 2 854  THR 854  851  851  THR THR A . n 
B 2 855  LYS 855  852  852  LYS LYS A . n 
B 2 856  GLU 856  853  853  GLU GLU A . n 
B 2 857  VAL 857  854  854  VAL VAL A . n 
B 2 858  SER 858  855  855  SER SER A . n 
B 2 859  HIS 859  856  856  HIS HIS A . n 
B 2 860  GLU 860  857  857  GLU GLU A . n 
B 2 861  ILE 861  858  858  ILE ILE A . n 
B 2 862  ILE 862  859  859  ILE ILE A . n 
B 2 863  LYS 863  860  860  LYS LYS A . n 
B 2 864  ASP 864  861  861  ASP ASP A . n 
B 2 865  ARG 865  862  862  ARG ARG A . n 
B 2 866  ARG 866  863  863  ARG ARG A . n 
B 2 867  PHE 867  864  864  PHE PHE A . n 
B 2 868  THR 868  865  865  THR THR A . n 
B 2 869  SER 869  866  866  SER SER A . n 
B 2 870  ASP 870  867  867  ASP ASP A . n 
B 2 871  LYS 871  868  868  LYS LYS A . n 
B 2 872  PHE 872  869  869  PHE PHE A . n 
B 2 873  PHE 873  870  870  PHE PHE A . n 
B 2 874  PHE 874  871  871  PHE PHE A . n 
B 2 875  HIS 875  872  872  HIS HIS A . n 
B 2 876  VAL 876  873  873  VAL VAL A . n 
B 2 877  PRO 877  874  874  PRO PRO A . n 
B 2 878  ILE 878  875  875  ILE ILE A . n 
B 2 879  THR 879  876  876  THR THR A . n 
B 2 880  LEU 880  877  877  LEU LEU A . n 
B 2 881  ASN 881  878  878  ASN ASN A . n 
B 2 882  TYR 882  879  879  TYR TYR A . n 
B 2 883  GLN 883  880  880  GLN GLN A . n 
B 2 884  ALA 884  881  881  ALA ALA A . n 
B 2 885  ALA 885  882  882  ALA ALA A . n 
B 2 886  ASN 886  883  883  ASN ASN A . n 
B 2 887  SER 887  884  884  SER SER A . n 
B 2 888  PRO 888  885  885  PRO PRO A . n 
B 2 889  SER 889  886  886  SER SER A . n 
B 2 890  LYS 890  887  887  LYS LYS A . n 
B 2 891  PHE 891  888  888  PHE PHE A . n 
B 2 892  ASN 892  889  889  ASN ASN A . n 
B 2 893  GLN 893  890  890  GLN GLN A . n 
B 2 894  ARG 894  891  891  ARG ARG A . n 
B 2 895  VAL 895  892  892  VAL VAL A . n 
B 2 896  ASN 896  893  893  ASN ASN A . n 
B 2 897  ALA 897  894  894  ALA ALA A . n 
B 2 898  TYR 898  895  895  TYR TYR A . n 
B 2 899  LEU 899  896  896  LEU LEU A . n 
B 2 900  LYS 900  897  897  LYS LYS A . n 
B 2 901  GLU 901  898  898  GLU GLU A . n 
B 2 902  HIS 902  899  899  HIS HIS A . n 
B 2 903  PRO 903  900  900  PRO PRO A . n 
B 2 904  GLU 904  901  901  GLU GLU A . n 
B 2 905  THR 905  902  902  THR THR A . n 
B 2 906  PRO 906  903  903  PRO PRO A . n 
B 2 907  ILE 907  904  904  ILE ILE A . n 
B 2 908  ILE 908  905  905  ILE ILE A . n 
B 2 909  GLY 909  906  906  GLY GLY A . n 
B 2 910  ILE 910  907  907  ILE ILE A . n 
B 2 911  ASP 911  908  908  ASP ASP A . n 
B 2 912  ARG 912  909  909  ARG ARG A . n 
B 2 913  GLY 913  910  910  GLY GLY A . n 
B 2 914  GLU 914  911  911  GLU GLU A . n 
B 2 915  ARG 915  912  912  ARG ARG A . n 
B 2 916  ASN 916  913  913  ASN ASN A . n 
B 2 917  LEU 917  914  914  LEU LEU A . n 
B 2 918  ILE 918  915  915  ILE ILE A . n 
B 2 919  TYR 919  916  916  TYR TYR A . n 
B 2 920  ILE 920  917  917  ILE ILE A . n 
B 2 921  THR 921  918  918  THR THR A . n 
B 2 922  VAL 922  919  919  VAL VAL A . n 
B 2 923  ILE 923  920  920  ILE ILE A . n 
B 2 924  ASP 924  921  921  ASP ASP A . n 
B 2 925  SER 925  922  922  SER SER A . n 
B 2 926  THR 926  923  923  THR THR A . n 
B 2 927  GLY 927  924  924  GLY GLY A . n 
B 2 928  LYS 928  925  925  LYS LYS A . n 
B 2 929  ILE 929  926  926  ILE ILE A . n 
B 2 930  LEU 930  927  927  LEU LEU A . n 
B 2 931  GLU 931  928  928  GLU GLU A . n 
B 2 932  GLN 932  929  929  GLN GLN A . n 
B 2 933  ARG 933  930  930  ARG ARG A . n 
B 2 934  SER 934  931  931  SER SER A . n 
B 2 935  LEU 935  932  932  LEU LEU A . n 
B 2 936  ASN 936  933  933  ASN ASN A . n 
B 2 937  THR 937  934  934  THR THR A . n 
B 2 938  ILE 938  935  935  ILE ILE A . n 
B 2 939  GLN 939  936  936  GLN GLN A . n 
B 2 940  GLN 940  937  937  GLN GLN A . n 
B 2 941  PHE 941  938  938  PHE PHE A . n 
B 2 942  ASP 942  939  939  ASP ASP A . n 
B 2 943  TYR 943  940  940  TYR TYR A . n 
B 2 944  GLN 944  941  941  GLN GLN A . n 
B 2 945  LYS 945  942  942  LYS LYS A . n 
B 2 946  LYS 946  943  943  LYS LYS A . n 
B 2 947  LEU 947  944  944  LEU LEU A . n 
B 2 948  ASP 948  945  945  ASP ASP A . n 
B 2 949  ASN 949  946  946  ASN ASN A . n 
B 2 950  ARG 950  947  947  ARG ARG A . n 
B 2 951  GLU 951  948  948  GLU GLU A . n 
B 2 952  LYS 952  949  949  LYS LYS A . n 
B 2 953  GLU 953  950  950  GLU GLU A . n 
B 2 954  ARG 954  951  951  ARG ARG A . n 
B 2 955  VAL 955  952  952  VAL VAL A . n 
B 2 956  ALA 956  953  953  ALA ALA A . n 
B 2 957  ALA 957  954  954  ALA ALA A . n 
B 2 958  ARG 958  955  955  ARG ARG A . n 
B 2 959  GLN 959  956  956  GLN GLN A . n 
B 2 960  ALA 960  957  957  ALA ALA A . n 
B 2 961  TRP 961  958  958  TRP TRP A . n 
B 2 962  SER 962  959  959  SER SER A . n 
B 2 963  VAL 963  960  960  VAL VAL A . n 
B 2 964  VAL 964  961  961  VAL VAL A . n 
B 2 965  GLY 965  962  962  GLY GLY A . n 
B 2 966  THR 966  963  963  THR THR A . n 
B 2 967  ILE 967  964  964  ILE ILE A . n 
B 2 968  LYS 968  965  965  LYS LYS A . n 
B 2 969  ASP 969  966  966  ASP ASP A . n 
B 2 970  LEU 970  967  967  LEU LEU A . n 
B 2 971  LYS 971  968  968  LYS LYS A . n 
B 2 972  GLN 972  969  969  GLN GLN A . n 
B 2 973  GLY 973  970  970  GLY GLY A . n 
B 2 974  TYR 974  971  971  TYR TYR A . n 
B 2 975  LEU 975  972  972  LEU LEU A . n 
B 2 976  SER 976  973  973  SER SER A . n 
B 2 977  GLN 977  974  974  GLN GLN A . n 
B 2 978  VAL 978  975  975  VAL VAL A . n 
B 2 979  ILE 979  976  976  ILE ILE A . n 
B 2 980  HIS 980  977  977  HIS HIS A . n 
B 2 981  GLU 981  978  978  GLU GLU A . n 
B 2 982  ILE 982  979  979  ILE ILE A . n 
B 2 983  VAL 983  980  980  VAL VAL A . n 
B 2 984  ASP 984  981  981  ASP ASP A . n 
B 2 985  LEU 985  982  982  LEU LEU A . n 
B 2 986  MET 986  983  983  MET MET A . n 
B 2 987  ILE 987  984  984  ILE ILE A . n 
B 2 988  HIS 988  985  985  HIS HIS A . n 
B 2 989  TYR 989  986  986  TYR TYR A . n 
B 2 990  GLN 990  987  987  GLN GLN A . n 
B 2 991  ALA 991  988  988  ALA ALA A . n 
B 2 992  VAL 992  989  989  VAL VAL A . n 
B 2 993  VAL 993  990  990  VAL VAL A . n 
B 2 994  VAL 994  991  991  VAL VAL A . n 
B 2 995  LEU 995  992  992  LEU LEU A . n 
B 2 996  GLU 996  993  993  GLU GLU A . n 
B 2 997  ASN 997  994  994  ASN ASN A . n 
B 2 998  LEU 998  995  995  LEU LEU A . n 
B 2 999  ASN 999  996  996  ASN ASN A . n 
B 2 1000 PHE 1000 997  997  PHE PHE A . n 
B 2 1001 GLY 1001 998  998  GLY GLY A . n 
B 2 1002 PHE 1002 999  999  PHE PHE A . n 
B 2 1003 LYS 1003 1000 1000 LYS LYS A . n 
B 2 1004 SER 1004 1001 1001 SER SER A . n 
B 2 1005 LYS 1005 1002 1002 LYS LYS A . n 
B 2 1006 ARG 1006 1003 1003 ARG ARG A . n 
B 2 1007 THR 1007 1004 1004 THR THR A . n 
B 2 1008 GLY 1008 1005 1005 GLY GLY A . n 
B 2 1009 ILE 1009 1006 1006 ILE ILE A . n 
B 2 1010 ALA 1010 1007 1007 ALA ALA A . n 
B 2 1011 GLU 1011 1008 1008 GLU GLU A . n 
B 2 1012 LYS 1012 1009 1009 LYS LYS A . n 
B 2 1013 ALA 1013 1010 1010 ALA ALA A . n 
B 2 1014 VAL 1014 1011 1011 VAL VAL A . n 
B 2 1015 TYR 1015 1012 1012 TYR TYR A . n 
B 2 1016 GLN 1016 1013 1013 GLN GLN A . n 
B 2 1017 GLN 1017 1014 1014 GLN GLN A . n 
B 2 1018 PHE 1018 1015 1015 PHE PHE A . n 
B 2 1019 GLU 1019 1016 1016 GLU GLU A . n 
B 2 1020 LYS 1020 1017 1017 LYS LYS A . n 
B 2 1021 MET 1021 1018 1018 MET MET A . n 
B 2 1022 LEU 1022 1019 1019 LEU LEU A . n 
B 2 1023 ILE 1023 1020 1020 ILE ILE A . n 
B 2 1024 ASP 1024 1021 1021 ASP ASP A . n 
B 2 1025 LYS 1025 1022 1022 LYS LYS A . n 
B 2 1026 LEU 1026 1023 1023 LEU LEU A . n 
B 2 1027 ASN 1027 1024 1024 ASN ASN A . n 
B 2 1028 CYS 1028 1025 1025 CYS CYS A . n 
B 2 1029 LEU 1029 1026 1026 LEU LEU A . n 
B 2 1030 VAL 1030 1027 1027 VAL VAL A . n 
B 2 1031 LEU 1031 1028 1028 LEU LEU A . n 
B 2 1032 LYS 1032 1029 1029 LYS LYS A . n 
B 2 1033 ASP 1033 1030 1030 ASP ASP A . n 
B 2 1034 TYR 1034 1031 1031 TYR TYR A . n 
B 2 1035 PRO 1035 1032 1032 PRO PRO A . n 
B 2 1036 ALA 1036 1033 1033 ALA ALA A . n 
B 2 1037 GLU 1037 1034 1034 GLU GLU A . n 
B 2 1038 LYS 1038 1035 1035 LYS LYS A . n 
B 2 1039 VAL 1039 1036 1036 VAL VAL A . n 
B 2 1040 GLY 1040 1037 1037 GLY GLY A . n 
B 2 1041 GLY 1041 1038 1038 GLY GLY A . n 
B 2 1042 VAL 1042 1039 1039 VAL VAL A . n 
B 2 1043 LEU 1043 1040 1040 LEU LEU A . n 
B 2 1044 ASN 1044 1041 1041 ASN ASN A . n 
B 2 1045 PRO 1045 1042 1042 PRO PRO A . n 
B 2 1046 TYR 1046 1043 1043 TYR TYR A . n 
B 2 1047 GLN 1047 1044 1044 GLN GLN A . n 
B 2 1048 LEU 1048 1045 1045 LEU LEU A . n 
B 2 1049 THR 1049 1046 1046 THR THR A . n 
B 2 1050 ASP 1050 1047 1047 ASP ASP A . n 
B 2 1051 GLN 1051 1048 1048 GLN GLN A . n 
B 2 1052 PHE 1052 1049 1049 PHE PHE A . n 
B 2 1053 THR 1053 1050 1050 THR THR A . n 
B 2 1054 SER 1054 1051 1051 SER SER A . n 
B 2 1055 PHE 1055 1052 1052 PHE PHE A . n 
B 2 1056 ALA 1056 1053 1053 ALA ALA A . n 
B 2 1057 LYS 1057 1054 1054 LYS LYS A . n 
B 2 1058 MET 1058 1055 1055 MET MET A . n 
B 2 1059 GLY 1059 1056 1056 GLY GLY A . n 
B 2 1060 THR 1060 1057 1057 THR THR A . n 
B 2 1061 GLN 1061 1058 1058 GLN GLN A . n 
B 2 1062 SER 1062 1059 1059 SER SER A . n 
B 2 1063 GLY 1063 1060 1060 GLY GLY A . n 
B 2 1064 PHE 1064 1061 1061 PHE PHE A . n 
B 2 1065 LEU 1065 1062 1062 LEU LEU A . n 
B 2 1066 PHE 1066 1063 1063 PHE PHE A . n 
B 2 1067 TYR 1067 1064 1064 TYR TYR A . n 
B 2 1068 VAL 1068 1065 1065 VAL VAL A . n 
B 2 1069 PRO 1069 1066 1066 PRO PRO A . n 
B 2 1070 ALA 1070 1067 1067 ALA ALA A . n 
B 2 1071 PRO 1071 1068 1068 PRO PRO A . n 
B 2 1072 TYR 1072 1069 1069 TYR TYR A . n 
B 2 1073 THR 1073 1070 1070 THR THR A . n 
B 2 1074 SER 1074 1071 1071 SER SER A . n 
B 2 1075 LYS 1075 1072 1072 LYS LYS A . n 
B 2 1076 ILE 1076 1073 1073 ILE ILE A . n 
B 2 1077 ASP 1077 1074 1074 ASP ASP A . n 
B 2 1078 PRO 1078 1075 1075 PRO PRO A . n 
B 2 1079 LEU 1079 1076 1076 LEU LEU A . n 
B 2 1080 THR 1080 1077 1077 THR THR A . n 
B 2 1081 GLY 1081 1078 1078 GLY GLY A . n 
B 2 1082 PHE 1082 1079 1079 PHE PHE A . n 
B 2 1083 VAL 1083 1080 1080 VAL VAL A . n 
B 2 1084 ASP 1084 1081 1081 ASP ASP A . n 
B 2 1085 PRO 1085 1082 1082 PRO PRO A . n 
B 2 1086 PHE 1086 1083 1083 PHE PHE A . n 
B 2 1087 VAL 1087 1084 1084 VAL VAL A . n 
B 2 1088 TRP 1088 1085 1085 TRP TRP A . n 
B 2 1089 LYS 1089 1086 1086 LYS LYS A . n 
B 2 1090 THR 1090 1087 1087 THR THR A . n 
B 2 1091 ILE 1091 1088 1088 ILE ILE A . n 
B 2 1092 LYS 1092 1089 1089 LYS LYS A . n 
B 2 1093 ASN 1093 1090 1090 ASN ASN A . n 
B 2 1094 HIS 1094 1091 1091 HIS HIS A . n 
B 2 1095 GLU 1095 1092 1092 GLU GLU A . n 
B 2 1096 SER 1096 1093 1093 SER SER A . n 
B 2 1097 ARG 1097 1094 1094 ARG ARG A . n 
B 2 1098 LYS 1098 1095 1095 LYS LYS A . n 
B 2 1099 HIS 1099 1096 1096 HIS HIS A . n 
B 2 1100 PHE 1100 1097 1097 PHE PHE A . n 
B 2 1101 LEU 1101 1098 1098 LEU LEU A . n 
B 2 1102 GLU 1102 1099 1099 GLU GLU A . n 
B 2 1103 GLY 1103 1100 1100 GLY GLY A . n 
B 2 1104 PHE 1104 1101 1101 PHE PHE A . n 
B 2 1105 ASP 1105 1102 1102 ASP ASP A . n 
B 2 1106 PHE 1106 1103 1103 PHE PHE A . n 
B 2 1107 LEU 1107 1104 1104 LEU LEU A . n 
B 2 1108 HIS 1108 1105 1105 HIS HIS A . n 
B 2 1109 TYR 1109 1106 1106 TYR TYR A . n 
B 2 1110 ASP 1110 1107 1107 ASP ASP A . n 
B 2 1111 VAL 1111 1108 1108 VAL VAL A . n 
B 2 1112 LYS 1112 1109 1109 LYS LYS A . n 
B 2 1113 THR 1113 1110 1110 THR THR A . n 
B 2 1114 GLY 1114 1111 1111 GLY GLY A . n 
B 2 1115 ASP 1115 1112 1112 ASP ASP A . n 
B 2 1116 PHE 1116 1113 1113 PHE PHE A . n 
B 2 1117 ILE 1117 1114 1114 ILE ILE A . n 
B 2 1118 LEU 1118 1115 1115 LEU LEU A . n 
B 2 1119 HIS 1119 1116 1116 HIS HIS A . n 
B 2 1120 PHE 1120 1117 1117 PHE PHE A . n 
B 2 1121 LYS 1121 1118 1118 LYS LYS A . n 
B 2 1122 MET 1122 1119 1119 MET MET A . n 
B 2 1123 ASN 1123 1120 1120 ASN ASN A . n 
B 2 1124 ARG 1124 1121 1121 ARG ARG A . n 
B 2 1125 ASN 1125 1122 1122 ASN ASN A . n 
B 2 1126 LEU 1126 1123 1123 LEU LEU A . n 
B 2 1127 SER 1127 1124 1124 SER SER A . n 
B 2 1128 PHE 1128 1125 1125 PHE PHE A . n 
B 2 1129 GLN 1129 1126 1126 GLN GLN A . n 
B 2 1130 ARG 1130 1127 1127 ARG ARG A . n 
B 2 1131 GLY 1131 1128 1128 GLY GLY A . n 
B 2 1132 LEU 1132 1129 1129 LEU LEU A . n 
B 2 1133 PRO 1133 1130 1130 PRO PRO A . n 
B 2 1134 GLY 1134 1131 1131 GLY GLY A . n 
B 2 1135 PHE 1135 1132 1132 PHE PHE A . n 
B 2 1136 MET 1136 1133 1133 MET MET A . n 
B 2 1137 PRO 1137 1134 1134 PRO PRO A . n 
B 2 1138 ALA 1138 1135 1135 ALA ALA A . n 
B 2 1139 TRP 1139 1136 1136 TRP TRP A . n 
B 2 1140 ASP 1140 1137 1137 ASP ASP A . n 
B 2 1141 ILE 1141 1138 1138 ILE ILE A . n 
B 2 1142 VAL 1142 1139 1139 VAL VAL A . n 
B 2 1143 PHE 1143 1140 1140 PHE PHE A . n 
B 2 1144 GLU 1144 1141 1141 GLU GLU A . n 
B 2 1145 LYS 1145 1142 1142 LYS LYS A . n 
B 2 1146 ASN 1146 1143 1143 ASN ASN A . n 
B 2 1147 GLU 1147 1144 1144 GLU GLU A . n 
B 2 1148 THR 1148 1145 1145 THR THR A . n 
B 2 1149 GLN 1149 1146 1146 GLN GLN A . n 
B 2 1150 PHE 1150 1147 1147 PHE PHE A . n 
B 2 1151 ASP 1151 1148 1148 ASP ASP A . n 
B 2 1152 ALA 1152 1149 1149 ALA ALA A . n 
B 2 1153 LYS 1153 1150 1150 LYS LYS A . n 
B 2 1154 GLY 1154 1151 1151 GLY GLY A . n 
B 2 1155 THR 1155 1152 1152 THR THR A . n 
B 2 1156 PRO 1156 1153 1153 PRO PRO A . n 
B 2 1157 PHE 1157 1154 1154 PHE PHE A . n 
B 2 1158 ILE 1158 1155 1155 ILE ILE A . n 
B 2 1159 ALA 1159 1156 1156 ALA ALA A . n 
B 2 1160 GLY 1160 1157 1157 GLY GLY A . n 
B 2 1161 LYS 1161 1158 1158 LYS LYS A . n 
B 2 1162 ARG 1162 1159 1159 ARG ARG A . n 
B 2 1163 ILE 1163 1160 1160 ILE ILE A . n 
B 2 1164 VAL 1164 1161 1161 VAL VAL A . n 
B 2 1165 PRO 1165 1162 1162 PRO PRO A . n 
B 2 1166 VAL 1166 1163 1163 VAL VAL A . n 
B 2 1167 ILE 1167 1164 1164 ILE ILE A . n 
B 2 1168 GLU 1168 1165 1165 GLU GLU A . n 
B 2 1169 ASN 1169 1166 1166 ASN ASN A . n 
B 2 1170 HIS 1170 1167 1167 HIS HIS A . n 
B 2 1171 ARG 1171 1168 1168 ARG ARG A . n 
B 2 1172 PHE 1172 1169 1169 PHE PHE A . n 
B 2 1173 THR 1173 1170 1170 THR THR A . n 
B 2 1174 GLY 1174 1171 1171 GLY GLY A . n 
B 2 1175 ARG 1175 1172 1172 ARG ARG A . n 
B 2 1176 TYR 1176 1173 1173 TYR TYR A . n 
B 2 1177 ARG 1177 1174 1174 ARG ARG A . n 
B 2 1178 ASP 1178 1175 1175 ASP ASP A . n 
B 2 1179 LEU 1179 1176 1176 LEU LEU A . n 
B 2 1180 TYR 1180 1177 1177 TYR TYR A . n 
B 2 1181 PRO 1181 1178 1178 PRO PRO A . n 
B 2 1182 ALA 1182 1179 1179 ALA ALA A . n 
B 2 1183 ASN 1183 1180 1180 ASN ASN A . n 
B 2 1184 GLU 1184 1181 1181 GLU GLU A . n 
B 2 1185 LEU 1185 1182 1182 LEU LEU A . n 
B 2 1186 ILE 1186 1183 1183 ILE ILE A . n 
B 2 1187 ALA 1187 1184 1184 ALA ALA A . n 
B 2 1188 LEU 1188 1185 1185 LEU LEU A . n 
B 2 1189 LEU 1189 1186 1186 LEU LEU A . n 
B 2 1190 GLU 1190 1187 1187 GLU GLU A . n 
B 2 1191 GLU 1191 1188 1188 GLU GLU A . n 
B 2 1192 LYS 1192 1189 1189 LYS LYS A . n 
B 2 1193 GLY 1193 1190 1190 GLY GLY A . n 
B 2 1194 ILE 1194 1191 1191 ILE ILE A . n 
B 2 1195 VAL 1195 1192 1192 VAL VAL A . n 
B 2 1196 PHE 1196 1193 1193 PHE PHE A . n 
B 2 1197 ARG 1197 1194 1194 ARG ARG A . n 
B 2 1198 ASP 1198 1195 1195 ASP ASP A . n 
B 2 1199 GLY 1199 1196 1196 GLY GLY A . n 
B 2 1200 SER 1200 1197 1197 SER SER A . n 
B 2 1201 ASN 1201 1198 1198 ASN ASN A . n 
B 2 1202 ILE 1202 1199 1199 ILE ILE A . n 
B 2 1203 LEU 1203 1200 1200 LEU LEU A . n 
B 2 1204 PRO 1204 1201 1201 PRO PRO A . n 
B 2 1205 LYS 1205 1202 1202 LYS LYS A . n 
B 2 1206 LEU 1206 1203 1203 LEU LEU A . n 
B 2 1207 LEU 1207 1204 1204 LEU LEU A . n 
B 2 1208 GLU 1208 1205 1205 GLU GLU A . n 
B 2 1209 ASN 1209 1206 1206 ASN ASN A . n 
B 2 1210 ASP 1210 1207 1207 ASP ASP A . n 
B 2 1211 ASP 1211 1208 1208 ASP ASP A . n 
B 2 1212 SER 1212 1209 1209 SER SER A . n 
B 2 1213 HIS 1213 1210 1210 HIS HIS A . n 
B 2 1214 ALA 1214 1211 1211 ALA ALA A . n 
B 2 1215 ILE 1215 1212 1212 ILE ILE A . n 
B 2 1216 ASP 1216 1213 1213 ASP ASP A . n 
B 2 1217 THR 1217 1214 1214 THR THR A . n 
B 2 1218 MET 1218 1215 1215 MET MET A . n 
B 2 1219 VAL 1219 1216 1216 VAL VAL A . n 
B 2 1220 ALA 1220 1217 1217 ALA ALA A . n 
B 2 1221 LEU 1221 1218 1218 LEU LEU A . n 
B 2 1222 ILE 1222 1219 1219 ILE ILE A . n 
B 2 1223 ARG 1223 1220 1220 ARG ARG A . n 
B 2 1224 SER 1224 1221 1221 SER SER A . n 
B 2 1225 VAL 1225 1222 1222 VAL VAL A . n 
B 2 1226 LEU 1226 1223 1223 LEU LEU A . n 
B 2 1227 GLN 1227 1224 1224 GLN GLN A . n 
B 2 1228 MET 1228 1225 1225 MET MET A . n 
B 2 1229 ARG 1229 1226 1226 ARG ARG A . n 
B 2 1230 ASN 1230 1227 1227 ASN ASN A . n 
B 2 1231 SER 1231 1228 1228 SER SER A . n 
B 2 1232 ASN 1232 1229 1229 ASN ASN A . n 
B 2 1233 ALA 1233 1230 1230 ALA ALA A . n 
B 2 1234 ALA 1234 1231 1231 ALA ALA A . n 
B 2 1235 THR 1235 1232 1232 THR THR A . n 
B 2 1236 GLY 1236 1233 1233 GLY GLY A . n 
B 2 1237 GLU 1237 1234 1234 GLU GLU A . n 
B 2 1238 ASP 1238 1235 1235 ASP ASP A . n 
B 2 1239 TYR 1239 1236 1236 TYR TYR A . n 
B 2 1240 ILE 1240 1237 1237 ILE ILE A . n 
B 2 1241 ASN 1241 1238 1238 ASN ASN A . n 
B 2 1242 SER 1242 1239 1239 SER SER A . n 
B 2 1243 PRO 1243 1240 1240 PRO PRO A . n 
B 2 1244 VAL 1244 1241 1241 VAL VAL A . n 
B 2 1245 ARG 1245 1242 1242 ARG ARG A . n 
B 2 1246 ASP 1246 1243 1243 ASP ASP A . n 
B 2 1247 LEU 1247 1244 1244 LEU LEU A . n 
B 2 1248 ASN 1248 1245 1245 ASN ASN A . n 
B 2 1249 GLY 1249 1246 1246 GLY GLY A . n 
B 2 1250 VAL 1250 1247 1247 VAL VAL A . n 
B 2 1251 CYS 1251 1248 1248 CYS CYS A . n 
B 2 1252 PHE 1252 1249 1249 PHE PHE A . n 
B 2 1253 ASP 1253 1250 1250 ASP ASP A . n 
B 2 1254 SER 1254 1251 1251 SER SER A . n 
B 2 1255 ARG 1255 1252 1252 ARG ARG A . n 
B 2 1256 PHE 1256 1253 1253 PHE PHE A . n 
B 2 1257 GLN 1257 1254 1254 GLN GLN A . n 
B 2 1258 ASN 1258 1255 1255 ASN ASN A . n 
B 2 1259 PRO 1259 1256 1256 PRO PRO A . n 
B 2 1260 GLU 1260 1257 1257 GLU GLU A . n 
B 2 1261 TRP 1261 1258 1258 TRP TRP A . n 
B 2 1262 PRO 1262 1259 1259 PRO PRO A . n 
B 2 1263 MET 1263 1260 1260 MET MET A . n 
B 2 1264 ASP 1264 1261 1261 ASP ASP A . n 
B 2 1265 ALA 1265 1262 1262 ALA ALA A . n 
B 2 1266 ASP 1266 1263 1263 ASP ASP A . n 
B 2 1267 ALA 1267 1264 1264 ALA ALA A . n 
B 2 1268 ASN 1268 1265 1265 ASN ASN A . n 
B 2 1269 GLY 1269 1266 1266 GLY GLY A . n 
B 2 1270 ALA 1270 1267 1267 ALA ALA A . n 
B 2 1271 TYR 1271 1268 1268 TYR TYR A . n 
B 2 1272 HIS 1272 1269 1269 HIS HIS A . n 
B 2 1273 ILE 1273 1270 1270 ILE ILE A . n 
B 2 1274 ALA 1274 1271 1271 ALA ALA A . n 
B 2 1275 LEU 1275 1272 1272 LEU LEU A . n 
B 2 1276 LYS 1276 1273 1273 LYS LYS A . n 
B 2 1277 GLY 1277 1274 1274 GLY GLY A . n 
B 2 1278 GLN 1278 1275 1275 GLN GLN A . n 
B 2 1279 LEU 1279 1276 1276 LEU LEU A . n 
B 2 1280 LEU 1280 1277 1277 LEU LEU A . n 
B 2 1281 LEU 1281 1278 1278 LEU LEU A . n 
B 2 1282 ASN 1282 1279 1279 ASN ASN A . n 
B 2 1283 HIS 1283 1280 1280 HIS HIS A . n 
B 2 1284 LEU 1284 1281 1281 LEU LEU A . n 
B 2 1285 LYS 1285 1282 1282 LYS LYS A . n 
B 2 1286 GLU 1286 1283 1283 GLU GLU A . n 
B 2 1287 SER 1287 1284 1284 SER SER A . n 
B 2 1288 LYS 1288 1285 1285 LYS LYS A . n 
B 2 1289 ASP 1289 1286 1286 ASP ASP A . n 
B 2 1290 LEU 1290 1287 1287 LEU LEU A . n 
B 2 1291 LYS 1291 1288 1288 LYS LYS A . n 
B 2 1292 LEU 1292 1289 1289 LEU LEU A . n 
B 2 1293 GLN 1293 1290 1290 GLN GLN A . n 
B 2 1294 ASN 1294 1291 1291 ASN ASN A . n 
B 2 1295 GLY 1295 1292 1292 GLY GLY A . n 
B 2 1296 ILE 1296 1293 1293 ILE ILE A . n 
B 2 1297 SER 1297 1294 1294 SER SER A . n 
B 2 1298 ASN 1298 1295 1295 ASN ASN A . n 
B 2 1299 GLN 1299 1296 1296 GLN GLN A . n 
B 2 1300 ASP 1300 1297 1297 ASP ASP A . n 
B 2 1301 TRP 1301 1298 1298 TRP TRP A . n 
B 2 1302 LEU 1302 1299 1299 LEU LEU A . n 
B 2 1303 ALA 1303 1300 1300 ALA ALA A . n 
B 2 1304 TYR 1304 1301 1301 TYR TYR A . n 
B 2 1305 ILE 1305 1302 1302 ILE ILE A . n 
B 2 1306 GLN 1306 1303 1303 GLN GLN A . n 
B 2 1307 GLU 1307 1304 1304 GLU GLU A . n 
B 2 1308 LEU 1308 1305 1305 LEU LEU A . n 
B 2 1309 ARG 1309 1306 1306 ARG ARG A . n 
B 2 1310 ASN 1310 1307 1307 ASN ASN A . n 
C 3 1    DG  1    1    ?    ?   ?   C . n 
C 3 2    DT  2    2    2    DT  DT  C . n 
C 3 3    DA  3    3    3    DA  DA  C . n 
C 3 4    DG  4    4    4    DG  DG  C . n 
C 3 5    DT  5    5    5    DT  DT  C . n 
C 3 6    DG  6    6    6    DG  DG  C . n 
C 3 7    2YR 7    7    7    2YR 2YR C . n 
C 3 8    DT  8    8    8    DT  DT  C . n 
C 3 9    DT  9    9    9    DT  DT  C . n 
C 3 10   DT  10   10   10   DT  DT  C . n 
C 3 11   DG  11   11   11   DG  DG  C . n 
C 3 12   DT  12   12   12   DT  DT  C . n 
C 3 13   DC  13   13   13   DC  DC  C . n 
C 3 14   DG  14   14   14   DG  DG  C . n 
C 3 15   DT  15   15   15   DT  DT  C . n 
C 3 16   DC  16   16   16   DC  DC  C . n 
C 3 17   DT  17   17   ?    ?   ?   C . n 
C 3 18   DC  18   18   ?    ?   ?   C . n 
C 3 19   DA  19   19   ?    ?   ?   C . n 
C 3 20   DT  20   20   ?    ?   ?   C . n 
C 3 21   DC  21   21   ?    ?   ?   C . n 
C 3 22   DT  22   22   ?    ?   ?   C . n 
C 3 23   DG  23   23   ?    ?   ?   C . n 
C 3 24   DT  24   24   ?    ?   ?   C . n 
C 3 25   DA  25   25   ?    ?   ?   C . n 
C 3 26   DT  26   26   ?    ?   ?   C . n 
C 3 27   DG  27   27   ?    ?   ?   C . n 
C 3 28   DC  28   28   ?    ?   ?   C . n 
C 3 29   DG  29   29   ?    ?   ?   C . n 
C 3 30   DT  30   30   ?    ?   ?   C . n 
C 3 31   DC  31   31   ?    ?   ?   C . n 
D 4 1    DG  1    1    ?    ?   ?   D . n 
D 4 2    DA  2    2    ?    ?   ?   D . n 
D 4 3    DC  3    3    ?    ?   ?   D . n 
D 4 4    DG  4    4    ?    ?   ?   D . n 
D 4 5    DC  5    5    ?    ?   ?   D . n 
D 4 6    DA  6    6    ?    ?   ?   D . n 
D 4 7    DT  7    7    ?    ?   ?   D . n 
D 4 8    DA  8    8    ?    ?   ?   D . n 
D 4 9    DC  9    9    ?    ?   ?   D . n 
D 4 10   DA  10   10   ?    ?   ?   D . n 
D 4 11   DG  11   11   ?    ?   ?   D . n 
D 4 12   DA  12   12   ?    ?   ?   D . n 
D 4 13   DT  13   13   ?    ?   ?   D . n 
D 4 14   DG  14   14   ?    ?   ?   D . n 
D 4 15   DA  15   15   ?    ?   ?   D . n 
D 4 16   DG  16   16   16   DG  DG  D . n 
D 4 17   DA  17   17   17   DA  DA  D . n 
D 4 18   DC  18   18   18   DC  DC  D . n 
D 4 19   DG  19   19   19   DG  DG  D . n 
D 4 20   DA  20   20   20   DA  DA  D . n 
D 4 21   DC  21   21   21   DC  DC  D . n 
D 4 22   DA  22   22   22   DA  DA  D . n 
D 4 23   DA  23   23   23   DA  DA  D . n 
D 4 24   DA  24   24   24   DA  DA  D . n 
D 4 25   DG  25   25   25   DG  DG  D . n 
D 4 26   DC  26   26   26   DC  DC  D . n 
D 4 27   DA  27   27   27   DA  DA  D . n 
D 4 28   DC  28   28   28   DC  DC  D . n 
D 4 29   DT  29   29   29   DT  DT  D . n 
D 4 30   DA  30   30   30   DA  DA  D . n 
D 4 31   DC  31   31   ?    ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        2YR 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   2YR 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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  ? B GLU 92  CG  
2  1 Y 1 A GLU 89  ? CD  ? B GLU 92  CD  
3  1 Y 1 A GLU 89  ? OE1 ? B GLU 92  OE1 
4  1 Y 1 A GLU 89  ? OE2 ? B GLU 92  OE2 
5  1 Y 1 A LYS 123 ? CG  ? B LYS 126 CG  
6  1 Y 1 A LYS 123 ? CD  ? B LYS 126 CD  
7  1 Y 1 A LYS 123 ? CE  ? B LYS 126 CE  
8  1 Y 1 A LYS 123 ? NZ  ? B LYS 126 NZ  
9  1 Y 1 A ARG 124 ? CG  ? B ARG 127 CG  
10 1 Y 1 A ARG 124 ? CD  ? B ARG 127 CD  
11 1 Y 1 A ARG 124 ? NE  ? B ARG 127 NE  
12 1 Y 1 A ARG 124 ? CZ  ? B ARG 127 CZ  
13 1 Y 1 A ARG 124 ? NH1 ? B ARG 127 NH1 
14 1 Y 1 A ARG 124 ? NH2 ? B ARG 127 NH2 
15 1 Y 1 A GLU 127 ? CG  ? B GLU 130 CG  
16 1 Y 1 A GLU 127 ? CD  ? B GLU 130 CD  
17 1 Y 1 A GLU 127 ? OE1 ? B GLU 130 OE1 
18 1 Y 1 A GLU 127 ? OE2 ? B GLU 130 OE2 
19 1 Y 1 A LYS 130 ? CG  ? B LYS 133 CG  
20 1 Y 1 A LYS 130 ? CD  ? B LYS 133 CD  
21 1 Y 1 A LYS 130 ? CE  ? B LYS 133 CE  
22 1 Y 1 A LYS 130 ? NZ  ? B LYS 133 NZ  
23 1 Y 1 A LYS 141 ? CG  ? B LYS 144 CG  
24 1 Y 1 A LYS 141 ? CD  ? B LYS 144 CD  
25 1 Y 1 A LYS 141 ? CE  ? B LYS 144 CE  
26 1 Y 1 A LYS 141 ? NZ  ? B LYS 144 NZ  
27 1 Y 1 A LYS 144 ? CG  ? B LYS 147 CG  
28 1 Y 1 A LYS 144 ? CD  ? B LYS 147 CD  
29 1 Y 1 A LYS 144 ? CE  ? B LYS 147 CE  
30 1 Y 1 A LYS 144 ? NZ  ? B LYS 147 NZ  
31 1 Y 1 A GLU 153 ? CG  ? B GLU 156 CG  
32 1 Y 1 A GLU 153 ? CD  ? B GLU 156 CD  
33 1 Y 1 A GLU 153 ? OE1 ? B GLU 156 OE1 
34 1 Y 1 A GLU 153 ? OE2 ? B GLU 156 OE2 
35 1 Y 1 A ASP 163 ? CG  ? B ASP 166 CG  
36 1 Y 1 A ASP 163 ? OD1 ? B ASP 166 OD1 
37 1 Y 1 A ASP 163 ? OD2 ? B ASP 166 OD2 
38 1 Y 1 A LYS 164 ? CG  ? B LYS 167 CG  
39 1 Y 1 A LYS 164 ? CD  ? B LYS 167 CD  
40 1 Y 1 A LYS 164 ? CE  ? B LYS 167 CE  
41 1 Y 1 A LYS 164 ? NZ  ? B LYS 167 NZ  
42 1 Y 1 A GLU 220 ? CG  ? B GLU 223 CG  
43 1 Y 1 A GLU 220 ? CD  ? B GLU 223 CD  
44 1 Y 1 A GLU 220 ? OE1 ? B GLU 223 OE1 
45 1 Y 1 A GLU 220 ? OE2 ? B GLU 223 OE2 
46 1 Y 1 A GLU 327 ? CG  ? B GLU 330 CG  
47 1 Y 1 A GLU 327 ? CD  ? B GLU 330 CD  
48 1 Y 1 A GLU 327 ? OE1 ? B GLU 330 OE1 
49 1 Y 1 A GLU 327 ? OE2 ? B GLU 330 OE2 
50 1 Y 1 A GLN 331 ? CG  ? B GLN 334 CG  
51 1 Y 1 A GLN 331 ? CD  ? B GLN 334 CD  
52 1 Y 1 A GLN 331 ? OE1 ? B GLN 334 OE1 
53 1 Y 1 A GLN 331 ? NE2 ? B GLN 334 NE2 
54 1 Y 1 A LYS 335 ? CG  ? B LYS 338 CG  
55 1 Y 1 A LYS 335 ? CD  ? B LYS 338 CD  
56 1 Y 1 A LYS 335 ? CE  ? B LYS 338 CE  
57 1 Y 1 A LYS 335 ? NZ  ? B LYS 338 NZ  
58 1 Y 1 A ASN 344 ? CG  ? B ASN 347 CG  
59 1 Y 1 A ASN 344 ? OD1 ? B ASN 347 OD1 
60 1 Y 1 A ASN 344 ? ND2 ? B ASN 347 ND2 
61 1 Y 1 A GLU 347 ? CG  ? B GLU 350 CG  
62 1 Y 1 A GLU 347 ? CD  ? B GLU 350 CD  
63 1 Y 1 A GLU 347 ? OE1 ? B GLU 350 OE1 
64 1 Y 1 A GLU 347 ? OE2 ? B GLU 350 OE2 
65 1 Y 1 A LYS 400 ? CG  ? B LYS 403 CG  
66 1 Y 1 A LYS 400 ? CD  ? B LYS 403 CD  
67 1 Y 1 A LYS 400 ? CE  ? B LYS 403 CE  
68 1 Y 1 A LYS 400 ? NZ  ? B LYS 403 NZ  
69 1 Y 1 A GLN 437 ? CG  ? B GLN 440 CG  
70 1 Y 1 A GLN 437 ? CD  ? B GLN 440 CD  
71 1 Y 1 A GLN 437 ? OE1 ? B GLN 440 OE1 
72 1 Y 1 A GLN 437 ? NE2 ? B GLN 440 NE2 
73 1 Y 1 A LYS 459 ? CG  ? B LYS 462 CG  
74 1 Y 1 A LYS 459 ? CD  ? B LYS 462 CD  
75 1 Y 1 A LYS 459 ? CE  ? B LYS 462 CE  
76 1 Y 1 A LYS 459 ? NZ  ? B LYS 462 NZ  
77 1 Y 1 A LYS 460 ? CG  ? B LYS 463 CG  
78 1 Y 1 A LYS 460 ? CD  ? B LYS 463 CD  
79 1 Y 1 A LYS 460 ? CE  ? B LYS 463 CE  
80 1 Y 1 A LYS 460 ? NZ  ? B LYS 463 NZ  
81 1 Y 1 A GLU 462 ? CG  ? B GLU 465 CG  
82 1 Y 1 A GLU 462 ? CD  ? B GLU 465 CD  
83 1 Y 1 A GLU 462 ? OE1 ? B GLU 465 OE1 
84 1 Y 1 A GLU 462 ? OE2 ? B GLU 465 OE2 
85 1 Y 1 A ASP 487 ? CG  ? B ASP 490 CG  
86 1 Y 1 A ASP 487 ? OD1 ? B ASP 490 OD1 
87 1 Y 1 A ASP 487 ? OD2 ? B ASP 490 OD2 
88 1 Y 1 A GLU 488 ? CG  ? B GLU 491 CG  
89 1 Y 1 A GLU 488 ? CD  ? B GLU 491 CD  
90 1 Y 1 A GLU 488 ? OE1 ? B GLU 491 OE1 
91 1 Y 1 A GLU 488 ? OE2 ? B GLU 491 OE2 
92 1 Y 1 A GLU 495 ? CG  ? B GLU 498 CG  
93 1 Y 1 A GLU 495 ? CD  ? B GLU 498 CD  
94 1 Y 1 A GLU 495 ? OE1 ? B GLU 498 OE1 
95 1 Y 1 A GLU 495 ? OE2 ? B GLU 498 OE2 
96 1 Y 1 A LYS 796 ? CG  ? B LYS 799 CG  
97 1 Y 1 A LYS 796 ? CD  ? B LYS 799 CD  
98 1 Y 1 A LYS 796 ? CE  ? B LYS 799 CE  
99 1 Y 1 A LYS 796 ? NZ  ? B LYS 799 NZ  
# 
_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                     9CJJ 
_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                         9CJJ 
_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                   9CJJ 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9CJJ 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.50 
_refine.ls_d_res_low                             ? 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.005  ? 11610 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.594  ? 15949 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 17.208 ? 4433  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.041  ? 1775  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.005  ? 1842  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9CJJ 
_struct.title                        'Cas12a:gRNA:DNA (Acidaminococcus sp.) with 0 RNA:DNA base pairs, structure 3' 
_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        9CJJ 
_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 9CJJ        9CJJ   ? 1 ? 1 
2 UNP CS12A_ACISB U2UMQ6 ? 2 
;MTQFEGFTNLYQVSKTLRFELIPQGKTLKHIQEQGFIEEDKARNDHYKELKPIIDRIYKTYADQCLQLVQLDWENLSAAI
DSYRKEKTEETRNALIEEQATYRNAIHDYFIGRTDNLTDAINKRHAEIYKGLFKAELFNGKVLKQLGTVTTTEHENALLR
SFDKFTTYFSGFYENRKNVFSAEDISTAIPHRIVQDNFPKFKENCHIFTRLITAVPSLREHFENVKKAIGIFVSTSIEEV
FSFPFYNQLLTQTQIDLYNQLLGGISREAGTEKIKGLNEVLNLAIQKNDETAHIIASLPHRFIPLFKQILSDRNTLSFIL
EEFKSDEEVIQSFCKYKTLLRNENVLETAEALFNELNSIDLTHIFISHKKLETISSALCDHWDTLRNALYERRISELTGK
ITKSAKEKVQRSLKHEDINLQEIISAAGKELSEAFKQKTSEILSHAHAALDQPLPTTLKKQEEKEILKSQLDSLLGLYHL
LDWFAVDESNEVDPEFSARLTGIKLEMEPSLSFYNKARNYATKKPYSVEKFKLNFQMPTLASGWDVNKEKNNGAILFVKN
GLYYLGIMPKQKGRYKALSFEPTEKTSEGFDKMYYDYFPDAAKMIPKCSTQLKAVTAHFQTHTTPILLSNNFIEPLEITK
EIYDLNNPEKEPKKFQTAYAKKTGDQKGYREALCKWIDFTRDFLSKYTKTTSIDLSSLRPSSQYKDLGEYYAELNPLLYH
ISFQRIAEKEIMDAVETGKLYLFQIYNKDFAKGHHGKPNLHTLYWTGLFSPENLAKTSIKLNGQAELFYRPKSRMKRMAH
RLGEKMLNKKLKDQKTPIPDTLYQELYDYVNHRLSHDLSDEARALLPNVITKEVSHEIIKDRRFTSDKFFFHVPITLNYQ
AANSPSKFNQRVNAYLKEHPETPIIGIDRGERNLIYITVIDSTGKILEQRSLNTIQQFDYQKKLDNREKERVAARQAWSV
VGTIKDLKQGYLSQVIHEIVDLMIHYQAVVVLENLNFGFKSKRTGIAEKAVYQQFEKMLIDKLNCLVLKDYPAEKVGGVL
NPYQLTDQFTSFAKMGTQSGFLFYVPAPYTSKIDPLTGFVDPFVWKTIKNHESRKHFLEGFDFLHYDVKTGDFILHFKMN
RNLSFQRGLPGFMPAWDIVFEKNETQFDAKGTPFIAGKRIVPVIENHRFTGRYRDLYPANELIALLEEKGIVFRDGSNIL
PKLLENDDSHAIDTMVALIRSVLQMRNSNAATGEDYINSPVRDLNGVCFDSRFQNPEWPMDADANGAYHIALKGQLLLNH
LKESKDLKLQNGISNQDWLAYIQELRN
;
1 
3 PDB 9CJJ        9CJJ   ? 3 ? 1 
4 PDB 9CJJ        9CJJ   ? 4 ? 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 9CJJ B 1 ? 42   ? 9CJJ   1 ? 42   ? 1 42   
2 2 9CJJ A 4 ? 1310 ? U2UMQ6 1 ? 1307 ? 1 1307 
3 3 9CJJ C 1 ? 31   ? 9CJJ   1 ? 31   ? 1 31   
4 4 9CJJ D 1 ? 31   ? 9CJJ   1 ? 31   ? 1 31   
# 
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 
2 9CJJ SER A 1   ? UNP U2UMQ6 ?   ?   'expression tag'      -2  1 
2 9CJJ ASN A 2   ? UNP U2UMQ6 ?   ?   'expression tag'      -1  2 
2 9CJJ ALA A 3   ? UNP U2UMQ6 ?   ?   'expression tag'      0   3 
2 9CJJ 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 B 6    ? PHE B 10   ? GLN A 3    PHE A 7    5 ? 5  
HELX_P HELX_P2  AA2 LYS B 29   ? GLY B 38   ? LYS A 26   GLY A 35   1 ? 10 
HELX_P HELX_P3  AA3 GLY B 38   ? LEU B 53   ? GLY A 35   LEU A 50   1 ? 16 
HELX_P HELX_P4  AA4 LEU B 53   ? LEU B 71   ? LEU A 50   LEU A 68   1 ? 19 
HELX_P HELX_P5  AA5 TRP B 76   ? GLU B 89   ? TRP A 73   GLU A 86   1 ? 14 
HELX_P HELX_P6  AA6 THR B 91   ? GLY B 115  ? THR A 88   GLY A 112  1 ? 25 
HELX_P HELX_P7  AA7 THR B 121  ? GLY B 134  ? THR A 118  GLY A 131  1 ? 14 
HELX_P HELX_P8  AA8 LEU B 135  ? LYS B 137  ? LEU A 132  LYS A 134  5 ? 3  
HELX_P HELX_P9  AA9 ALA B 138  ? GLY B 143  ? ALA A 135  GLY A 140  1 ? 6  
HELX_P HELX_P10 AB1 GLY B 143  ? LEU B 149  ? GLY A 140  LEU A 146  1 ? 7  
HELX_P HELX_P11 AB2 THR B 155  ? ARG B 163  ? THR A 152  ARG A 160  1 ? 9  
HELX_P HELX_P12 AB3 SER B 164  ? ASP B 166  ? SER A 161  ASP A 163  5 ? 3  
HELX_P HELX_P13 AB4 PHE B 168  ? TYR B 171  ? PHE A 165  TYR A 168  5 ? 4  
HELX_P HELX_P14 AB5 PHE B 172  ? ASN B 181  ? PHE A 169  ASN A 178  1 ? 10 
HELX_P HELX_P15 AB6 ALA B 191  ? ASP B 199  ? ALA A 188  ASP A 196  1 ? 9  
HELX_P HELX_P16 AB7 ASP B 199  ? VAL B 218  ? ASP A 196  VAL A 215  1 ? 20 
HELX_P HELX_P17 AB8 PRO B 219  ? GLY B 233  ? PRO A 216  GLY A 230  1 ? 15 
HELX_P HELX_P18 AB9 SER B 245  ? LEU B 252  ? SER A 242  LEU A 249  5 ? 8  
HELX_P HELX_P19 AC1 THR B 254  ? GLY B 267  ? THR A 251  GLY A 264  1 ? 14 
HELX_P HELX_P20 AC2 SER B 328  ? ASN B 347  ? SER A 325  ASN A 344  1 ? 20 
HELX_P HELX_P21 AC3 ASN B 347  ? LEU B 359  ? ASN A 344  LEU A 356  1 ? 13 
HELX_P HELX_P22 AC4 ASP B 363  ? HIS B 366  ? ASP A 360  HIS A 363  5 ? 4  
HELX_P HELX_P23 AC5 SER B 370  ? CYS B 382  ? SER A 367  CYS A 379  1 ? 13 
HELX_P HELX_P24 AC6 TRP B 385  ? SER B 398  ? TRP A 382  SER A 395  1 ? 14 
HELX_P HELX_P25 AC7 THR B 405  ? HIS B 418  ? THR A 402  HIS A 415  1 ? 14 
HELX_P HELX_P26 AC8 LEU B 423  ? GLY B 431  ? LEU A 420  GLY A 428  1 ? 9  
HELX_P HELX_P27 AC9 GLY B 431  ? ASP B 454  ? GLY A 428  ASP A 451  1 ? 24 
HELX_P HELX_P28 AD1 LYS B 463  ? ASP B 485  ? LYS A 460  ASP A 482  1 ? 23 
HELX_P HELX_P29 AD2 ASP B 496  ? LYS B 526  ? ASP A 493  LYS A 523  1 ? 31 
HELX_P HELX_P30 AD3 ASP B 548  ? ASN B 550  ? ASP A 545  ASN A 547  5 ? 3  
HELX_P HELX_P31 AD4 LYS B 551  ? GLY B 556  ? LYS A 548  GLY A 553  1 ? 6  
HELX_P HELX_P32 AD5 LYS B 573  ? ARG B 577  ? LYS A 570  ARG A 574  5 ? 5  
HELX_P HELX_P33 AD6 ASP B 603  ? THR B 613  ? ASP A 600  THR A 610  1 ? 11 
HELX_P HELX_P34 AD7 LEU B 615  ? HIS B 625  ? LEU A 612  HIS A 622  1 ? 11 
HELX_P HELX_P35 AD8 THR B 642  ? ASN B 650  ? THR A 639  ASN A 647  1 ? 9  
HELX_P HELX_P36 AD9 GLN B 659  ? THR B 666  ? GLN A 656  THR A 663  1 ? 8  
HELX_P HELX_P37 AE1 ASP B 668  ? TYR B 690  ? ASP A 665  TYR A 687  1 ? 23 
HELX_P HELX_P38 AE2 PRO B 703  ? TYR B 707  ? PRO A 700  TYR A 704  5 ? 5  
HELX_P HELX_P39 AE3 ASP B 709  ? TYR B 722  ? ASP A 706  TYR A 719  1 ? 14 
HELX_P HELX_P40 AE4 GLU B 731  ? GLY B 741  ? GLU A 728  GLY A 738  1 ? 11 
HELX_P HELX_P41 AE5 ASN B 762  ? PHE B 772  ? ASN A 759  PHE A 769  1 ? 11 
HELX_P HELX_P42 AE6 SER B 773  ? LYS B 779  ? SER A 770  LYS A 776  1 ? 7  
HELX_P HELX_P43 AE7 PRO B 822  ? ASN B 834  ? PRO A 819  ASN A 831  1 ? 13 
HELX_P HELX_P44 AE8 SER B 842  ? LEU B 849  ? SER A 839  LEU A 846  1 ? 8  
HELX_P HELX_P45 AE9 ASP B 864  ? THR B 868  ? ASP A 861  THR A 865  5 ? 5  
HELX_P HELX_P46 AF1 LYS B 890  ? HIS B 902  ? LYS A 887  HIS A 899  1 ? 13 
HELX_P HELX_P47 AF2 LYS B 946  ? ARG B 958  ? LYS A 943  ARG A 955  1 ? 13 
HELX_P HELX_P48 AF3 ALA B 960  ? GLN B 990  ? ALA A 957  GLN A 987  1 ? 31 
HELX_P HELX_P49 AF4 VAL B 1014 ? CYS B 1028 ? VAL A 1011 CYS A 1025 1 ? 15 
HELX_P HELX_P50 AF5 VAL B 1087 ? ILE B 1091 ? VAL A 1084 ILE A 1088 5 ? 5  
HELX_P HELX_P51 AF6 ASN B 1093 ? GLY B 1103 ? ASN A 1090 GLY A 1100 1 ? 11 
HELX_P HELX_P52 AF7 TYR B 1180 ? GLY B 1193 ? TYR A 1177 GLY A 1190 1 ? 14 
HELX_P HELX_P53 AF8 ILE B 1202 ? ASP B 1210 ? ILE A 1199 ASP A 1207 1 ? 9  
HELX_P HELX_P54 AF9 ASP B 1211 ? LEU B 1226 ? ASP A 1208 LEU A 1223 1 ? 16 
HELX_P HELX_P55 AG1 ASP B 1253 ? GLN B 1257 ? ASP A 1250 GLN A 1254 5 ? 5  
HELX_P HELX_P56 AG2 ASP B 1264 ? SER B 1287 ? ASP A 1261 SER A 1284 1 ? 24 
HELX_P HELX_P57 AG3 SER B 1297 ? ARG B 1309 ? SER A 1294 ARG A 1306 1 ? 13 
# 
_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 one  ? B CYS 554 SG    ? ? ? 1_555 C 2YR 7  S  ? ? A CYS 551 C 2YR 7  1_555 ? ? ? ? ? ? ?                    2.028 
? ? 
covale2  covale both ? C DG  6   "O3'" ? ? ? 1_555 C 2YR 7  P  ? ? C DG  6   C 2YR 7  1_555 ? ? ? ? ? ? ?                    1.607 
? ? 
covale3  covale both ? C 2YR 7   "O3'" ? ? ? 1_555 C DT  8  P  ? ? C 2YR 7   C DT  8  1_555 ? ? ? ? ? ? ?                    1.607 
? ? 
hydrog1  hydrog ?    ? A A   5   N6    ? ? ? 1_555 A U   13 O2 ? ? B A   5   B U   13 1_555 ? ? ? ? ? ? 'REVERSED HOOGSTEEN' ?     
? ? 
hydrog2  hydrog ?    ? A A   5   N7    ? ? ? 1_555 A U   13 N3 ? ? B A   5   B U   13 1_555 ? ? ? ? ? ? 'REVERSED HOOGSTEEN' ?     
? ? 
hydrog3  hydrog ?    ? A U   7   N3    ? ? ? 1_555 A U   22 O2 ? ? B U   7   B U   22 1_555 ? ? ? ? ? ? TYPE_16_PAIR         ?     
? ? 
hydrog4  hydrog ?    ? A U   7   O4    ? ? ? 1_555 A U   22 N3 ? ? B U   7   B U   22 1_555 ? ? ? ? ? ? TYPE_16_PAIR         ?     
? ? 
hydrog5  hydrog ?    ? A U   8   N3    ? ? ? 1_555 A A   21 N1 ? ? B U   8   B A   21 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog6  hydrog ?    ? A U   8   O4    ? ? ? 1_555 A A   21 N6 ? ? B U   8   B A   21 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog7  hydrog ?    ? A C   9   N3    ? ? ? 1_555 A G   20 N1 ? ? B C   9   B G   20 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog8  hydrog ?    ? A C   9   N4    ? ? ? 1_555 A G   20 O6 ? ? B C   9   B G   20 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog9  hydrog ?    ? A C   9   O2    ? ? ? 1_555 A G   20 N2 ? ? B C   9   B G   20 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog10 hydrog ?    ? A U   10  N3    ? ? ? 1_555 A A   19 N1 ? ? B U   10  B A   19 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog11 hydrog ?    ? A U   10  O4    ? ? ? 1_555 A A   19 N6 ? ? B U   10  B A   19 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog12 hydrog ?    ? A A   11  N1    ? ? ? 1_555 A U   18 N3 ? ? B A   11  B U   18 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog13 hydrog ?    ? A A   11  N6    ? ? ? 1_555 A U   18 O4 ? ? B A   11  B U   18 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog14 hydrog ?    ? A C   12  N3    ? ? ? 1_555 A G   17 N1 ? ? B C   12  B G   17 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog15 hydrog ?    ? A C   12  N4    ? ? ? 1_555 A G   17 O6 ? ? B C   12  B G   17 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog16 hydrog ?    ? A C   12  O2    ? ? ? 1_555 A G   17 N2 ? ? B C   12  B G   17 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog17 hydrog ?    ? C DT  2   N3    ? ? ? 1_555 D DA  30 N1 ? ? C DT  2   D DA  30 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog18 hydrog ?    ? C DT  2   O4    ? ? ? 1_555 D DA  30 N6 ? ? C DT  2   D DA  30 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog19 hydrog ?    ? C DA  3   N1    ? ? ? 1_555 D DT  29 N3 ? ? C DA  3   D DT  29 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog20 hydrog ?    ? C DA  3   N6    ? ? ? 1_555 D DT  29 O4 ? ? C DA  3   D DT  29 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog21 hydrog ?    ? C DG  4   N1    ? ? ? 1_555 D DC  28 N3 ? ? C DG  4   D DC  28 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog22 hydrog ?    ? C DG  4   N2    ? ? ? 1_555 D DC  28 O2 ? ? C DG  4   D DC  28 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog23 hydrog ?    ? C DG  4   O6    ? ? ? 1_555 D DC  28 N4 ? ? C DG  4   D DC  28 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog24 hydrog ?    ? C DT  5   N3    ? ? ? 1_555 D DA  27 N1 ? ? C DT  5   D DA  27 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog25 hydrog ?    ? C DT  5   O4    ? ? ? 1_555 D DA  27 N6 ? ? C DT  5   D DA  27 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog26 hydrog ?    ? C DG  6   N1    ? ? ? 1_555 D DC  26 N3 ? ? C DG  6   D DC  26 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog27 hydrog ?    ? C DG  6   N2    ? ? ? 1_555 D DC  26 O2 ? ? C DG  6   D DC  26 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog28 hydrog ?    ? C DG  6   O6    ? ? ? 1_555 D DC  26 N4 ? ? C DG  6   D DC  26 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog29 hydrog ?    ? C DT  8   N3    ? ? ? 1_555 D DA  24 N1 ? ? C DT  8   D DA  24 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog30 hydrog ?    ? C DT  8   O4    ? ? ? 1_555 D DA  24 N6 ? ? C DT  8   D DA  24 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog31 hydrog ?    ? C DT  9   N3    ? ? ? 1_555 D DA  23 N1 ? ? C DT  9   D DA  23 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog32 hydrog ?    ? C DT  9   O4    ? ? ? 1_555 D DA  23 N6 ? ? C DT  9   D DA  23 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog33 hydrog ?    ? C DT  10  N3    ? ? ? 1_555 D DA  22 N1 ? ? C DT  10  D DA  22 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog34 hydrog ?    ? C DT  10  O4    ? ? ? 1_555 D DA  22 N6 ? ? C DT  10  D DA  22 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog35 hydrog ?    ? C DG  11  N1    ? ? ? 1_555 D DC  21 N3 ? ? C DG  11  D DC  21 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog36 hydrog ?    ? C DG  11  N2    ? ? ? 1_555 D DC  21 O2 ? ? C DG  11  D DC  21 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog37 hydrog ?    ? C DG  11  O6    ? ? ? 1_555 D DC  21 N4 ? ? C DG  11  D DC  21 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog38 hydrog ?    ? C DT  12  N3    ? ? ? 1_555 D DA  20 N1 A ? C DT  12  D DA  20 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog39 hydrog ?    ? C DT  12  N3    ? ? ? 1_555 D DA  20 N1 B ? C DT  12  D DA  20 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog40 hydrog ?    ? C DT  12  O4    ? ? ? 1_555 D DA  20 N6 A ? C DT  12  D DA  20 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog41 hydrog ?    ? C DC  13  N3    ? ? ? 1_555 D DG  19 N2 A ? C DC  13  D DG  19 1_555 ? ? ? ? ? ? 'DC-DG PAIR'         ?     
? ? 
hydrog42 hydrog ?    ? C DG  14  N1    ? ? ? 1_555 D DC  18 N3 ? ? C DG  14  D DC  18 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog43 hydrog ?    ? C DG  14  N2    ? ? ? 1_555 D DC  18 O2 ? ? C DG  14  D DC  18 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog44 hydrog ?    ? C DG  14  O6    ? ? ? 1_555 D DC  18 N4 ? ? C DG  14  D DC  18 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog45 hydrog ?    ? C DT  15  N3    ? ? ? 1_555 D DA  17 N1 ? ? C DT  15  D DA  17 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog46 hydrog ?    ? C DT  15  O4    ? ? ? 1_555 D DA  17 N6 ? ? C DT  15  D DA  17 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog47 hydrog ?    ? C DC  16  N3    ? ? ? 1_555 D DG  16 N1 ? ? C DC  16  D DG  16 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog48 hydrog ?    ? C DC  16  N4    ? ? ? 1_555 D DG  16 O6 ? ? C DC  16  D DG  16 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog49 hydrog ?    ? C DC  16  O2    ? ? ? 1_555 D DG  16 N2 ? ? C DC  16  D DG  16 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                      C 
_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     B 
_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 ? 9 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 5 ? 
AA7 ? 3 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
# 
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 
AA1 7 8 ? anti-parallel 
AA1 8 9 ? 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 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? 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 B 534  ? LYS B 535  ? PHE A 531  LYS A 532  
AA1 2 GLU B 789  ? ARG B 793  ? GLU A 786  ARG A 790  
AA1 3 LYS B 871  ? LEU B 880  ? LYS A 868  LEU A 877  
AA1 4 VAL B 16   ? PRO B 26   ? VAL A 13   PRO A 23   
AA1 5 TYR B 744  ? TYR B 749  ? TYR A 741  TYR A 746  
AA1 6 LEU B 565  ? ILE B 570  ? LEU A 562  ILE A 567  
AA1 7 ALA B 557  ? LYS B 562  ? ALA A 554  LYS A 559  
AA1 8 GLY B 592  ? ASP B 599  ? GLY A 589  ASP A 596  
AA1 9 HIS B 723  ? ALA B 730  ? HIS A 720  ALA A 727  
AA2 1 PHE B 534  ? LYS B 535  ? PHE A 531  LYS A 532  
AA2 2 GLU B 789  ? ARG B 793  ? GLU A 786  ARG A 790  
AA2 3 LYS B 871  ? LEU B 880  ? LYS A 868  LEU A 877  
AA2 4 ILE B 782  ? LEU B 784  ? ILE A 779  LEU A 781  
AA3 1 PHE B 368  ? ILE B 369  ? PHE A 365  ILE A 366  
AA3 2 ILE B 421  ? ASN B 422  ? ILE A 418  ASN A 419  
AA4 1 ILE B 629  ? LEU B 631  ? ILE A 626  LEU A 628  
AA4 2 LEU B 639  ? ILE B 641  ? LEU A 636  ILE A 638  
AA5 1 LYS B 808  ? LEU B 814  ? LYS A 805  LEU A 811  
AA5 2 VAL B 852  ? GLU B 856  ? VAL A 849  GLU A 853  
AA6 1 ILE B 929  ? SER B 934  ? ILE A 926  SER A 931  
AA6 2 TYR B 919  ? ILE B 923  ? TYR A 916  ILE A 920  
AA6 3 ILE B 907  ? ASP B 911  ? ILE A 904  ASP A 908  
AA6 4 VAL B 992  ? ASN B 997  ? VAL A 989  ASN A 994  
AA6 5 LEU B 1065 ? PRO B 1069 ? LEU A 1062 PRO A 1066 
AA7 1 PHE B 1106 ? TYR B 1109 ? PHE A 1103 TYR A 1106 
AA7 2 PHE B 1116 ? LYS B 1121 ? PHE A 1113 LYS A 1118 
AA7 3 ALA B 1138 ? PHE B 1143 ? ALA A 1135 PHE A 1140 
AA8 1 THR B 1148 ? PHE B 1150 ? THR A 1145 PHE A 1147 
AA8 2 PRO B 1156 ? ILE B 1158 ? PRO A 1153 ILE A 1155 
AA9 1 ARG B 1162 ? VAL B 1164 ? ARG A 1159 VAL A 1161 
AA9 2 ARG B 1177 ? LEU B 1179 ? ARG A 1174 LEU A 1176 
# 
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 B 534  ? N PHE A 531  O TYR B 792  ? O TYR A 789  
AA1 2 3 N ARG B 793  ? N ARG A 790  O LYS B 871  ? O LYS A 868  
AA1 3 4 O ILE B 878  ? O ILE A 875  N LYS B 18   ? N LYS A 15   
AA1 4 5 N ILE B 25   ? N ILE A 22   O GLN B 747  ? O GLN A 744  
AA1 5 6 O PHE B 746  ? O PHE A 743  N LEU B 568  ? N LEU A 565  
AA1 6 7 O GLY B 569  ? O GLY A 566  N ILE B 558  ? N ILE A 555  
AA1 7 8 N VAL B 561  ? N VAL A 558  O ASP B 594  ? O ASP A 591  
AA1 8 9 N PHE B 593  ? N PHE A 590  O ILE B 729  ? O ILE A 726  
AA2 1 2 N PHE B 534  ? N PHE A 531  O TYR B 792  ? O TYR A 789  
AA2 2 3 N ARG B 793  ? N ARG A 790  O LYS B 871  ? O LYS A 868  
AA2 3 4 O THR B 879  ? O THR A 876  N LYS B 783  ? N LYS A 780  
AA3 1 2 N ILE B 369  ? N ILE A 366  O ILE B 421  ? O ILE A 418  
AA4 1 2 N LEU B 631  ? N LEU A 628  O LEU B 639  ? O LEU A 636  
AA5 1 2 N MET B 809  ? N MET A 806  O LYS B 855  ? O LYS A 852  
AA6 1 2 O ARG B 933  ? O ARG A 930  N ILE B 920  ? N ILE A 917  
AA6 2 3 O ILE B 923  ? O ILE A 920  N ILE B 907  ? N ILE A 904  
AA6 3 4 N ILE B 908  ? N ILE A 905  O VAL B 994  ? O VAL A 991  
AA6 4 5 N LEU B 995  ? N LEU A 992  O PHE B 1066 ? O PHE A 1063 
AA7 1 2 N PHE B 1106 ? N PHE A 1103 O HIS B 1119 ? O HIS A 1116 
AA7 2 3 N LEU B 1118 ? N LEU A 1115 O ILE B 1141 ? O ILE A 1138 
AA8 1 2 N GLN B 1149 ? N GLN A 1146 O PHE B 1157 ? O PHE A 1154 
AA9 1 2 N ARG B 1162 ? N ARG A 1159 O LEU B 1179 ? O LEU A 1176 
# 
_pdbx_entry_details.entry_id                   9CJJ 
_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 
# 
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   ? ? -91.75  49.52   
2 1 THR A 114  ? ? -122.87 -168.23 
3 1 ALA A 120  ? ? -39.73  -35.88  
4 1 PHE A 165  ? ? -155.32 23.71   
5 1 PHE A 180  ? ? -98.09  -126.03 
6 1 SER A 181  ? ? 82.04   -16.63  
7 1 LYS A 748  ? ? 70.87   -8.16   
8 1 MET A 1133 ? ? 53.57   76.76   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9CJJ 
_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                    9CJJ 
_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                  3.5 
_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               27031 
_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 3' ? ? ? '1, 2, 3, 4' 
2 1 RECOMBINANT        COMPLEX Cas12a                                                                         ? ? ? 2            
3 1 SYNTHETIC          COMPLEX gRNA:DNA                                                                       ? ? ? 1,3,4        
# 
_em_imaging.entry_id                        9CJJ 
_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              9CJJ 
_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                9CJJ 
_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              9CJJ 
_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 B U   1   ? A U   1   
2   1 Y 1 B U   2   ? A U   2   
3   1 Y 1 B U   3   ? A U   3   
4   1 Y 1 B G   29  ? A G   29  
5   1 Y 1 B U   30  ? A U   30  
6   1 Y 1 B A   31  ? A A   31  
7   1 Y 1 B G   32  ? A G   32  
8   1 Y 1 B A   33  ? A A   33  
9   1 Y 1 B C   34  ? A C   34  
10  1 Y 1 B A   35  ? A A   35  
11  1 Y 1 B U   36  ? A U   36  
12  1 Y 1 B A   37  ? A A   37  
13  1 Y 1 B C   38  ? A C   38  
14  1 Y 1 B G   39  ? A G   39  
15  1 Y 1 B C   40  ? A C   40  
16  1 Y 1 B A   41  ? A A   41  
17  1 Y 1 B G   42  ? A G   42  
18  1 Y 1 A SER -2  ? B SER 1   
19  1 Y 1 A ASN -1  ? B ASN 2   
20  1 Y 1 A ALA 0   ? B ALA 3   
21  1 Y 1 A MET 1   ? B MET 4   
22  1 Y 1 A GLY 147 ? B GLY 150 
23  1 Y 1 A THR 148 ? B THR 151 
24  1 Y 1 A VAL 149 ? B VAL 152 
25  1 Y 1 A ILE 265 ? B ILE 268 
26  1 Y 1 A SER 266 ? B SER 269 
27  1 Y 1 A ARG 267 ? B ARG 270 
28  1 Y 1 A GLU 268 ? B GLU 271 
29  1 Y 1 A ALA 269 ? B ALA 272 
30  1 Y 1 A GLY 270 ? B GLY 273 
31  1 Y 1 A THR 271 ? B THR 274 
32  1 Y 1 A GLU 272 ? B GLU 275 
33  1 Y 1 A LYS 273 ? B LYS 276 
34  1 Y 1 A ILE 274 ? B ILE 277 
35  1 Y 1 A LYS 275 ? B LYS 278 
36  1 Y 1 A GLY 276 ? B GLY 279 
37  1 Y 1 A LEU 277 ? B LEU 280 
38  1 Y 1 A ASN 278 ? B ASN 281 
39  1 Y 1 A GLU 279 ? B GLU 282 
40  1 Y 1 A VAL 280 ? B VAL 283 
41  1 Y 1 A LEU 281 ? B LEU 284 
42  1 Y 1 A ASN 282 ? B ASN 285 
43  1 Y 1 A LEU 283 ? B LEU 286 
44  1 Y 1 A ALA 284 ? B ALA 287 
45  1 Y 1 A ILE 285 ? B ILE 288 
46  1 Y 1 A GLN 286 ? B GLN 289 
47  1 Y 1 A LYS 287 ? B LYS 290 
48  1 Y 1 A ASN 288 ? B ASN 291 
49  1 Y 1 A ASP 289 ? B ASP 292 
50  1 Y 1 A GLU 290 ? B GLU 293 
51  1 Y 1 A THR 291 ? B THR 294 
52  1 Y 1 A ALA 292 ? B ALA 295 
53  1 Y 1 A HIS 293 ? B HIS 296 
54  1 Y 1 A ILE 294 ? B ILE 297 
55  1 Y 1 A ILE 295 ? B ILE 298 
56  1 Y 1 A ALA 296 ? B ALA 299 
57  1 Y 1 A SER 297 ? B SER 300 
58  1 Y 1 A LEU 298 ? B LEU 301 
59  1 Y 1 A PRO 299 ? B PRO 302 
60  1 Y 1 A HIS 300 ? B HIS 303 
61  1 Y 1 A ARG 301 ? B ARG 304 
62  1 Y 1 A PHE 302 ? B PHE 305 
63  1 Y 1 A ILE 303 ? B ILE 306 
64  1 Y 1 A PRO 304 ? B PRO 307 
65  1 Y 1 A LEU 305 ? B LEU 308 
66  1 Y 1 A PHE 306 ? B PHE 309 
67  1 Y 1 A LYS 307 ? B LYS 310 
68  1 Y 1 A GLN 308 ? B GLN 311 
69  1 Y 1 A ILE 309 ? B ILE 312 
70  1 Y 1 A LEU 310 ? B LEU 313 
71  1 Y 1 A SER 311 ? B SER 314 
72  1 Y 1 A ASP 312 ? B ASP 315 
73  1 Y 1 A ARG 313 ? B ARG 316 
74  1 Y 1 A ASN 314 ? B ASN 317 
75  1 Y 1 A THR 315 ? B THR 318 
76  1 Y 1 A LEU 316 ? B LEU 319 
77  1 Y 1 A SER 317 ? B SER 320 
78  1 Y 1 A PHE 318 ? B PHE 321 
79  1 Y 1 A ILE 319 ? B ILE 322 
80  1 Y 1 A LEU 320 ? B LEU 323 
81  1 Y 1 A GLU 321 ? B GLU 324 
82  1 Y 1 A GLU 322 ? B GLU 325 
83  1 Y 1 A PHE 323 ? B PHE 326 
84  1 Y 1 A PRO 648 ? B PRO 651 
85  1 Y 1 A GLU 649 ? B GLU 652 
86  1 Y 1 A LYS 650 ? B LYS 653 
87  1 Y 1 A GLU 651 ? B GLU 654 
88  1 Y 1 C DG  1   ? C DG  1   
89  1 Y 1 C DT  17  ? C DT  17  
90  1 Y 1 C DC  18  ? C DC  18  
91  1 Y 1 C DA  19  ? C DA  19  
92  1 Y 1 C DT  20  ? C DT  20  
93  1 Y 1 C DC  21  ? C DC  21  
94  1 Y 1 C DT  22  ? C DT  22  
95  1 Y 1 C DG  23  ? C DG  23  
96  1 Y 1 C DT  24  ? C DT  24  
97  1 Y 1 C DA  25  ? C DA  25  
98  1 Y 1 C DT  26  ? C DT  26  
99  1 Y 1 C DG  27  ? C DG  27  
100 1 Y 1 C DC  28  ? C DC  28  
101 1 Y 1 C DG  29  ? C DG  29  
102 1 Y 1 C DT  30  ? C DT  30  
103 1 Y 1 C DC  31  ? C DC  31  
104 1 Y 1 D DG  1   ? D DG  1   
105 1 Y 1 D DA  2   ? D DA  2   
106 1 Y 1 D DC  3   ? D DC  3   
107 1 Y 1 D DG  4   ? D DG  4   
108 1 Y 1 D DC  5   ? D DC  5   
109 1 Y 1 D DA  6   ? D DA  6   
110 1 Y 1 D DT  7   ? D DT  7   
111 1 Y 1 D DA  8   ? D DA  8   
112 1 Y 1 D DC  9   ? D DC  9   
113 1 Y 1 D DA  10  ? D DA  10  
114 1 Y 1 D DG  11  ? D DG  11  
115 1 Y 1 D DA  12  ? D DA  12  
116 1 Y 1 D DT  13  ? D DT  13  
117 1 Y 1 D DG  14  ? D DG  14  
118 1 Y 1 D DA  15  ? D DA  15  
119 1 Y 1 D DC  31  ? D DC  31  
# 
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           9CJJ 
_em_admin.last_update        2025-05-21 
_em_admin.map_release_date   2025-01-08 
_em_admin.title              'Cas12a:gRNA:DNA (Acidaminococcus sp.) with 0 RNA:DNA base pairs, structure 3' 
# 
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  ? ? ? PHENIX    ?      
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 
9CJJ 'double helix'         
9CJJ 'a-form double helix'  
9CJJ 'b-form double helix'  
9CJJ 'hairpin loop'         
9CJJ 'mismatched base pair' 
# 
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 A  5  1_555 A U  13 1_555 -4.201 -1.552 -0.707 -20.281 -20.650 -107.351 1  B_A5:U13_B    B 5  ? B 13 ? 24 4 
1 A G  17 1_555 A C  12 1_555 -0.715 0.269  -0.502 -17.449 -16.381 14.299   2  B_G17:C12_B   B 17 ? B 12 ? 19 1 
1 A U  18 1_555 A A  11 1_555 -0.701 -0.203 -0.261 -4.146  -16.473 0.108    3  B_U18:A11_B   B 18 ? B 11 ? 20 1 
1 A A  19 1_555 A U  10 1_555 0.376  0.067  -0.201 -11.443 0.018   1.417    4  B_A19:U10_B   B 19 ? B 10 ? 20 1 
1 A G  20 1_555 A C  9  1_555 0.267  -0.433 -0.195 9.397   -1.855  1.044    5  B_G20:C9_B    B 20 ? B 9  ? 19 1 
1 A A  21 1_555 A U  8  1_555 0.346  -0.405 -1.896 -34.217 -14.545 -8.217   6  B_A21:U8_B    B 21 ? B 8  ? 20 1 
1 A U  22 1_555 A U  7  1_555 2.882  -1.836 -0.552 -6.927  -19.528 4.936    7  B_U22:U7_B    B 22 ? B 7  ? 16 1 
1 C DT 2  1_555 D DA 30 1_555 -0.039 -0.984 -1.958 -4.064  -15.152 12.500   8  C_DT2:DA30_D  C 2  ? D 30 ? 20 1 
1 C DA 3  1_555 D DT 29 1_555 0.091  -0.232 -1.124 -14.569 -10.186 -0.853   9  C_DA3:DT29_D  C 3  ? D 29 ? 20 1 
1 C DG 4  1_555 D DC 28 1_555 -0.155 -0.434 -1.540 -12.445 -2.218  0.587    10 C_DG4:DC28_D  C 4  ? D 28 ? 19 1 
1 C DT 5  1_555 D DA 27 1_555 -0.123 -0.241 -0.877 -0.853  -0.457  1.764    11 C_DT5:DA27_D  C 5  ? D 27 ? 20 1 
1 C DG 6  1_555 D DC 26 1_555 -0.181 -0.161 -0.432 -0.980  -2.054  -0.287   12 C_DG6:DC26_D  C 6  ? D 26 ? 19 1 
1 C DT 8  1_555 D DA 24 1_555 -0.126 -0.177 0.388  0.097   -13.809 0.396    13 C_DT8:DA24_D  C 8  ? D 24 ? 20 1 
1 C DT 9  1_555 D DA 23 1_555 -0.236 -0.152 0.223  -8.121  -11.094 0.728    14 C_DT9:DA23_D  C 9  ? D 23 ? 20 1 
1 C DT 10 1_555 D DA 22 1_555 -0.082 -0.150 -0.292 -6.172  -5.390  0.420    15 C_DT10:DA22_D C 10 ? D 22 ? 20 1 
1 C DG 11 1_555 D DC 21 1_555 -0.216 -0.216 -0.680 -4.882  -4.678  0.325    16 C_DG11:DC21_D C 11 ? D 21 ? 19 1 
1 C DT 12 1_555 D DA 20 1_555 -0.058 -0.203 -0.675 -9.104  -13.661 2.536    17 C_DT12:DA20_D C 12 ? D 20 ? 20 1 
1 C DC 13 1_555 D DG 19 1_555 -2.243 0.310  0.080  -9.711  -44.759 25.518   18 C_DC13:DG19_D C 13 ? D 19 ? ?  ? 
1 C DG 14 1_555 D DC 18 1_555 -0.188 -0.129 0.117  -0.979  0.152   -1.120   19 C_DG14:DC18_D C 14 ? D 18 ? 19 1 
1 C DT 15 1_555 D DA 17 1_555 -0.091 -0.131 -0.002 2.791   1.151   0.402    20 C_DT15:DA17_D C 15 ? D 17 ? 20 1 
1 C DC 16 1_555 D DG 16 1_555 0.186  -0.127 -0.008 0.264   -0.226  1.191    21 C_DC16:DG16_D C 16 ? D 16 ? 19 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 A  5  1_555 A U  13 1_555 A G  17 1_555 A C  12 1_555 3.421  -2.238 3.517 -0.157  16.363 86.143 -1.984 -2.480 3.135 11.889  
0.114   87.383 1  BB_A5G17:C12U13_BB      B 5  ? B 13 ? B 17 ? B 12 ? 
1 A G  17 1_555 A C  12 1_555 A U  18 1_555 A A  11 1_555 -1.673 -2.047 3.286 -4.724  -6.415 26.933 -2.526 2.203  3.892 -13.406 
9.872   28.065 2  BB_G17U18:A11C12_BB     B 17 ? B 12 ? B 18 ? B 11 ? 
1 A U  18 1_555 A A  11 1_555 A A  19 1_555 A U  10 1_555 -0.130 -1.053 3.377 -0.792  22.913 36.965 -3.566 0.102  2.367 32.586  
1.127   43.285 3  BB_U18A19:U10A11_BB     B 18 ? B 11 ? B 19 ? B 10 ? 
1 A A  19 1_555 A U  10 1_555 A G  20 1_555 A C  9  1_555 0.066  -1.163 2.831 0.713   6.426  26.080 -3.867 0.010  2.479 13.968  
-1.551  26.856 4  BB_A19G20:C9U10_BB      B 19 ? B 10 ? B 20 ? B 9  ? 
1 A G  20 1_555 A C  9  1_555 A A  21 1_555 A U  8  1_555 0.272  -1.450 4.517 16.192  19.833 35.897 -4.416 1.655  3.191 28.199  
-23.021 43.846 5  BB_G20A21:U8C9_BB       B 20 ? B 9  ? B 21 ? B 8  ? 
1 A A  21 1_555 A U  8  1_555 A U  22 1_555 A U  7  1_555 0.732  -0.135 2.783 -12.138 15.351 41.540 -1.273 -1.811 2.311 20.344  
16.086  45.734 6  BB_A21U22:U7U8_BB       B 21 ? B 8  ? B 22 ? B 7  ? 
1 C DT 2  1_555 D DA 30 1_555 C DA 3  1_555 D DT 29 1_555 -2.062 0.181  5.704 0.047   -1.551 42.660 0.520  2.842  5.693 -2.131  
-0.065  42.686 7  CC_DT2DA3:DT29DA30_DD   C 2  ? D 30 ? C 3  ? D 29 ? 
1 C DA 3  1_555 D DT 29 1_555 C DG 4  1_555 D DC 28 1_555 -1.600 1.493  3.448 -5.722  1.934  33.393 2.215  1.725  3.741 3.332   
9.858   33.919 8  CC_DA3DG4:DC28DT29_DD   C 3  ? D 29 ? C 4  ? D 28 ? 
1 C DG 4  1_555 D DC 28 1_555 C DT 5  1_555 D DA 27 1_555 0.602  -0.324 3.015 -4.580  4.796  30.175 -1.448 -1.931 2.811 9.076   
8.665   30.878 9  CC_DG4DT5:DA27DC28_DD   C 4  ? D 28 ? C 5  ? D 27 ? 
1 C DT 5  1_555 D DA 27 1_555 C DG 6  1_555 D DC 26 1_555 -0.357 1.305  3.341 -1.160  2.069  38.295 1.719  0.393  3.413 3.151   
1.766   38.366 10 CC_DT5DG6:DC26DA27_DD   C 5  ? D 27 ? C 6  ? D 26 ? 
1 C DG 6  1_555 D DC 26 1_555 C DT 8  1_555 D DA 24 1_555 0.237  -1.260 6.534 -0.126  0.454  68.835 -1.148 -0.219 6.526 0.402   
0.111   68.836 11 CC_DG6DT8:DA24DC26_DD   C 6  ? D 26 ? C 8  ? D 24 ? 
1 C DT 8  1_555 D DA 24 1_555 C DT 9  1_555 D DA 23 1_555 -0.109 -0.377 3.200 3.348   -0.042 42.663 -0.513 0.476  3.184 -0.057  
-4.594  42.788 12 CC_DT8DT9:DA23DA24_DD   C 8  ? D 24 ? C 9  ? D 23 ? 
1 C DT 9  1_555 D DA 23 1_555 C DT 10 1_555 D DA 22 1_555 -0.168 0.308  3.568 -3.450  4.135  31.850 -0.254 -0.371 3.577 7.469   
6.231   32.290 13 CC_DT9DT10:DA22DA23_DD  C 9  ? D 23 ? C 10 ? D 22 ? 
1 C DT 10 1_555 D DA 22 1_555 C DG 11 1_555 D DC 21 1_555 -0.337 0.886  3.186 -3.974  13.614 34.721 -0.468 -0.014 3.310 21.725  
6.342   37.423 14 CC_DT10DG11:DC21DA22_DD C 10 ? D 22 ? C 11 ? D 21 ? 
1 C DG 11 1_555 D DC 21 1_555 C DT 12 1_555 D DA 20 1_555 -0.319 2.284  3.920 2.577   15.292 12.288 -4.525 2.813  4.164 51.110  
-8.614  19.763 15 CC_DG11DT12:DA20DC21_DD C 11 ? D 21 ? C 12 ? D 20 ? 
1 C DT 12 1_555 D DA 20 1_555 C DC 13 1_555 D DG 19 1_555 0.004  3.577  3.536 -1.663  6.960  27.805 5.314  -0.463 4.279 14.188  
3.390   28.694 16 CC_DT12DC13:DG19DA20_DD C 12 ? D 20 ? C 13 ? D 19 ? 
1 C DC 13 1_555 D DG 19 1_555 C DG 14 1_555 D DC 18 1_555 -0.312 1.926  3.445 -12.797 15.119 31.679 0.593  -1.564 3.812 24.888  
21.066  37.227 17 CC_DC13DG14:DC18DG19_DD C 13 ? D 19 ? C 14 ? D 18 ? 
1 C DG 14 1_555 D DC 18 1_555 C DT 15 1_555 D DA 17 1_555 1.034  -0.406 3.689 1.381   3.308  33.846 -1.289 -1.519 3.672 5.662   
-2.363  34.030 18 CC_DG14DT15:DA17DC18_DD C 14 ? D 18 ? C 15 ? D 17 ? 
1 C DT 15 1_555 D DA 17 1_555 C DC 16 1_555 D DG 16 1_555 0.562  -1.042 3.332 2.641   -0.623 41.364 -1.405 -0.505 3.375 -0.881  
-3.734  41.449 19 CC_DT15DC16:DG16DA17_DD C 15 ? D 17 ? C 16 ? D 16 ? 
# 
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 Neurological Disorders and Stroke (NIH/NINDS)' 'United States' U19NS132303 4 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)'   'United States' 
'U19AI171110, U54AI170792, U19AI135990, UH3AI150552, U01AI142817' 5 
'Department of Energy (DOE, United States)'                                                         'United States' 
'DE-AC02-05CH11231, 2553571, B656358'                             6 
# 
_atom_sites.entry_id                    9CJJ 
_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     . A   A 1 4    ? 167.739 160.356 136.228 1.00 48.45  ? 4    A   B P     1 
ATOM   2     O OP1   . A   A 1 4    ? 166.602 159.846 135.421 1.00 48.45  ? 4    A   B OP1   1 
ATOM   3     O OP2   . A   A 1 4    ? 168.767 161.215 135.586 1.00 48.45  ? 4    A   B OP2   1 
ATOM   4     O "O5'" . A   A 1 4    ? 167.141 161.152 137.472 1.00 48.45  ? 4    A   B "O5'" 1 
ATOM   5     C "C5'" . A   A 1 4    ? 165.743 161.172 137.722 1.00 48.45  ? 4    A   B "C5'" 1 
ATOM   6     C "C4'" . A   A 1 4    ? 165.404 162.091 138.869 1.00 48.45  ? 4    A   B "C4'" 1 
ATOM   7     O "O4'" . A   A 1 4    ? 165.920 163.419 138.596 1.00 48.45  ? 4    A   B "O4'" 1 
ATOM   8     C "C3'" . A   A 1 4    ? 163.921 162.310 139.134 1.00 48.45  ? 4    A   B "C3'" 1 
ATOM   9     O "O3'" . A   A 1 4    ? 163.350 161.251 139.893 1.00 48.45  ? 4    A   B "O3'" 1 
ATOM   10    C "C2'" . A   A 1 4    ? 163.902 163.673 139.817 1.00 48.45  ? 4    A   B "C2'" 1 
ATOM   11    O "O2'" . A   A 1 4    ? 164.269 163.554 141.183 1.00 48.45  ? 4    A   B "O2'" 1 
ATOM   12    C "C1'" . A   A 1 4    ? 165.029 164.397 139.082 1.00 48.45  ? 4    A   B "C1'" 1 
ATOM   13    N N9    . A   A 1 4    ? 164.547 165.184 137.931 1.00 48.45  ? 4    A   B N9    1 
ATOM   14    C C8    . A   A 1 4    ? 164.220 164.718 136.682 1.00 48.45  ? 4    A   B C8    1 
ATOM   15    N N7    . A   A 1 4    ? 163.833 165.651 135.850 1.00 48.45  ? 4    A   B N7    1 
ATOM   16    C C5    . A   A 1 4    ? 163.917 166.815 136.597 1.00 48.45  ? 4    A   B C5    1 
ATOM   17    C C6    . A   A 1 4    ? 163.642 168.157 136.284 1.00 48.45  ? 4    A   B C6    1 
ATOM   18    N N6    . A   A 1 4    ? 163.209 168.564 135.089 1.00 48.45  ? 4    A   B N6    1 
ATOM   19    N N1    . A   A 1 4    ? 163.827 169.079 137.250 1.00 48.45  ? 4    A   B N1    1 
ATOM   20    C C2    . A   A 1 4    ? 164.259 168.667 138.447 1.00 48.45  ? 4    A   B C2    1 
ATOM   21    N N3    . A   A 1 4    ? 164.554 167.437 138.863 1.00 48.45  ? 4    A   B N3    1 
ATOM   22    C C4    . A   A 1 4    ? 164.357 166.544 137.879 1.00 48.45  ? 4    A   B C4    1 
ATOM   23    P P     . A   A 1 5    ? 162.038 161.459 140.803 1.00 42.64  ? 5    A   B P     1 
ATOM   24    O OP1   . A   A 1 5    ? 161.512 160.111 141.127 1.00 42.64  ? 5    A   B OP1   1 
ATOM   25    O OP2   . A   A 1 5    ? 161.130 162.447 140.169 1.00 42.64  ? 5    A   B OP2   1 
ATOM   26    O "O5'" . A   A 1 5    ? 162.615 162.062 142.157 1.00 42.64  ? 5    A   B "O5'" 1 
ATOM   27    C "C5'" . A   A 1 5    ? 161.768 162.387 143.248 1.00 42.64  ? 5    A   B "C5'" 1 
ATOM   28    C "C4'" . A   A 1 5    ? 162.525 163.171 144.289 1.00 42.64  ? 5    A   B "C4'" 1 
ATOM   29    O "O4'" . A   A 1 5    ? 163.098 164.352 143.681 1.00 42.64  ? 5    A   B "O4'" 1 
ATOM   30    C "C3'" . A   A 1 5    ? 161.723 163.701 145.468 1.00 42.64  ? 5    A   B "C3'" 1 
ATOM   31    O "O3'" . A   A 1 5    ? 161.555 162.708 146.470 1.00 42.64  ? 5    A   B "O3'" 1 
ATOM   32    C "C2'" . A   A 1 5    ? 162.551 164.896 145.931 1.00 42.64  ? 5    A   B "C2'" 1 
ATOM   33    O "O2'" . A   A 1 5    ? 163.612 164.473 146.776 1.00 42.64  ? 5    A   B "O2'" 1 
ATOM   34    C "C1'" . A   A 1 5    ? 163.153 165.400 144.619 1.00 42.64  ? 5    A   B "C1'" 1 
ATOM   35    N N9    . A   A 1 5    ? 162.451 166.573 144.064 1.00 42.64  ? 5    A   B N9    1 
ATOM   36    C C8    . A   A 1 5    ? 161.712 166.636 142.911 1.00 42.64  ? 5    A   B C8    1 
ATOM   37    N N7    . A   A 1 5    ? 161.228 167.827 142.660 1.00 42.64  ? 5    A   B N7    1 
ATOM   38    C C5    . A   A 1 5    ? 161.682 168.599 143.717 1.00 42.64  ? 5    A   B C5    1 
ATOM   39    C C6    . A   A 1 5    ? 161.511 169.955 144.036 1.00 42.64  ? 5    A   B C6    1 
ATOM   40    N N6    . A   A 1 5    ? 160.802 170.805 143.292 1.00 42.64  ? 5    A   B N6    1 
ATOM   41    N N1    . A   A 1 5    ? 162.099 170.414 145.160 1.00 42.64  ? 5    A   B N1    1 
ATOM   42    C C2    . A   A 1 5    ? 162.810 169.561 145.906 1.00 42.64  ? 5    A   B C2    1 
ATOM   43    N N3    . A   A 1 5    ? 163.044 168.266 145.710 1.00 42.64  ? 5    A   B N3    1 
ATOM   44    C C4    . A   A 1 5    ? 162.445 167.843 144.585 1.00 42.64  ? 5    A   B C4    1 
ATOM   45    P P     . U   A 1 6    ? 160.706 162.977 147.812 1.00 41.93  ? 6    U   B P     1 
ATOM   46    O OP1   . U   A 1 6    ? 161.020 164.299 148.411 1.00 41.93  ? 6    U   B OP1   1 
ATOM   47    O OP2   . U   A 1 6    ? 160.873 161.772 148.655 1.00 41.93  ? 6    U   B OP2   1 
ATOM   48    O "O5'" . U   A 1 6    ? 159.194 163.016 147.323 1.00 41.93  ? 6    U   B "O5'" 1 
ATOM   49    C "C5'" . U   A 1 6    ? 158.201 163.663 148.110 1.00 41.93  ? 6    U   B "C5'" 1 
ATOM   50    C "C4'" . U   A 1 6    ? 156.886 162.925 148.086 1.00 41.93  ? 6    U   B "C4'" 1 
ATOM   51    O "O4'" . U   A 1 6    ? 156.378 162.885 146.725 1.00 41.93  ? 6    U   B "O4'" 1 
ATOM   52    C "C3'" . U   A 1 6    ? 156.932 161.478 148.569 1.00 41.93  ? 6    U   B "C3'" 1 
ATOM   53    O "O3'" . U   A 1 6    ? 155.714 161.170 149.242 1.00 41.93  ? 6    U   B "O3'" 1 
ATOM   54    C "C2'" . U   A 1 6    ? 157.001 160.690 147.265 1.00 41.93  ? 6    U   B "C2'" 1 
ATOM   55    O "O2'" . U   A 1 6    ? 156.521 159.366 147.354 1.00 41.93  ? 6    U   B "O2'" 1 
ATOM   56    C "C1'" . U   A 1 6    ? 156.137 161.544 146.345 1.00 41.93  ? 6    U   B "C1'" 1 
ATOM   57    N N1    . U   A 1 6    ? 156.468 161.407 144.921 1.00 41.93  ? 6    U   B N1    1 
ATOM   58    C C2    . U   A 1 6    ? 155.555 160.772 144.108 1.00 41.93  ? 6    U   B C2    1 
ATOM   59    O O2    . U   A 1 6    ? 154.499 160.328 144.523 1.00 41.93  ? 6    U   B O2    1 
ATOM   60    N N3    . U   A 1 6    ? 155.925 160.675 142.791 1.00 41.93  ? 6    U   B N3    1 
ATOM   61    C C4    . U   A 1 6    ? 157.090 161.139 142.220 1.00 41.93  ? 6    U   B C4    1 
ATOM   62    O O4    . U   A 1 6    ? 157.279 160.976 141.015 1.00 41.93  ? 6    U   B O4    1 
ATOM   63    C C5    . U   A 1 6    ? 157.981 161.785 143.129 1.00 41.93  ? 6    U   B C5    1 
ATOM   64    C C6    . U   A 1 6    ? 157.647 161.893 144.416 1.00 41.93  ? 6    U   B C6    1 
ATOM   65    P P     . U   A 1 7    ? 155.532 161.532 150.796 1.00 39.16  ? 7    U   B P     1 
ATOM   66    O OP1   . U   A 1 7    ? 154.612 162.684 150.880 1.00 39.16  ? 7    U   B OP1   1 
ATOM   67    O OP2   . U   A 1 7    ? 156.869 161.601 151.435 1.00 39.16  ? 7    U   B OP2   1 
ATOM   68    O "O5'" . U   A 1 7    ? 154.752 160.281 151.392 1.00 39.16  ? 7    U   B "O5'" 1 
ATOM   69    C "C5'" . U   A 1 7    ? 155.069 159.755 152.670 1.00 39.16  ? 7    U   B "C5'" 1 
ATOM   70    C "C4'" . U   A 1 7    ? 154.421 158.410 152.864 1.00 39.16  ? 7    U   B "C4'" 1 
ATOM   71    O "O4'" . U   A 1 7    ? 153.009 158.589 153.130 1.00 39.16  ? 7    U   B "O4'" 1 
ATOM   72    C "C3'" . U   A 1 7    ? 154.468 157.493 151.651 1.00 39.16  ? 7    U   B "C3'" 1 
ATOM   73    O "O3'" . U   A 1 7    ? 155.680 156.765 151.580 1.00 39.16  ? 7    U   B "O3'" 1 
ATOM   74    C "C2'" . U   A 1 7    ? 153.243 156.607 151.837 1.00 39.16  ? 7    U   B "C2'" 1 
ATOM   75    O "O2'" . U   A 1 7    ? 153.526 155.543 152.734 1.00 39.16  ? 7    U   B "O2'" 1 
ATOM   76    C "C1'" . U   A 1 7    ? 152.263 157.563 152.518 1.00 39.16  ? 7    U   B "C1'" 1 
ATOM   77    N N1    . U   A 1 7    ? 151.299 158.185 151.583 1.00 39.16  ? 7    U   B N1    1 
ATOM   78    C C2    . U   A 1 7    ? 150.311 157.407 151.012 1.00 39.16  ? 7    U   B C2    1 
ATOM   79    O O2    . U   A 1 7    ? 150.195 156.211 151.207 1.00 39.16  ? 7    U   B O2    1 
ATOM   80    N N3    . U   A 1 7    ? 149.456 158.080 150.179 1.00 39.16  ? 7    U   B N3    1 
ATOM   81    C C4    . U   A 1 7    ? 149.475 159.422 149.874 1.00 39.16  ? 7    U   B C4    1 
ATOM   82    O O4    . U   A 1 7    ? 148.633 159.878 149.101 1.00 39.16  ? 7    U   B O4    1 
ATOM   83    C C5    . U   A 1 7    ? 150.518 160.161 150.511 1.00 39.16  ? 7    U   B C5    1 
ATOM   84    C C6    . U   A 1 7    ? 151.367 159.533 151.328 1.00 39.16  ? 7    U   B C6    1 
ATOM   85    P P     . U   A 1 8    ? 156.790 157.132 150.481 1.00 40.45  ? 8    U   B P     1 
ATOM   86    O OP1   . U   A 1 8    ? 158.108 156.676 150.986 1.00 40.45  ? 8    U   B OP1   1 
ATOM   87    O OP2   . U   A 1 8    ? 156.609 158.548 150.081 1.00 40.45  ? 8    U   B OP2   1 
ATOM   88    O "O5'" . U   A 1 8    ? 156.399 156.223 149.237 1.00 40.45  ? 8    U   B "O5'" 1 
ATOM   89    C "C5'" . U   A 1 8    ? 156.100 154.842 149.405 1.00 40.45  ? 8    U   B "C5'" 1 
ATOM   90    C "C4'" . U   A 1 8    ? 155.373 154.283 148.209 1.00 40.45  ? 8    U   B "C4'" 1 
ATOM   91    O "O4'" . U   A 1 8    ? 154.050 154.886 148.129 1.00 40.45  ? 8    U   B "O4'" 1 
ATOM   92    C "C3'" . U   A 1 8    ? 156.042 154.547 146.860 1.00 40.45  ? 8    U   B "C3'" 1 
ATOM   93    O "O3'" . U   A 1 8    ? 155.802 153.446 145.986 1.00 40.45  ? 8    U   B "O3'" 1 
ATOM   94    C "C2'" . U   A 1 8    ? 155.291 155.772 146.354 1.00 40.45  ? 8    U   B "C2'" 1 
ATOM   95    O "O2'" . U   A 1 8    ? 155.327 155.963 144.956 1.00 40.45  ? 8    U   B "O2'" 1 
ATOM   96    C "C1'" . U   A 1 8    ? 153.881 155.489 146.861 1.00 40.45  ? 8    U   B "C1'" 1 
ATOM   97    N N1    . U   A 1 8    ? 153.063 156.698 147.013 1.00 40.45  ? 8    U   B N1    1 
ATOM   98    C C2    . U   A 1 8    ? 151.693 156.580 146.911 1.00 40.45  ? 8    U   B C2    1 
ATOM   99    O O2    . U   A 1 8    ? 151.134 155.513 146.734 1.00 40.45  ? 8    U   B O2    1 
ATOM   100   N N3    . U   A 1 8    ? 151.005 157.759 147.043 1.00 40.45  ? 8    U   B N3    1 
ATOM   101   C C4    . U   A 1 8    ? 151.541 159.014 147.246 1.00 40.45  ? 8    U   B C4    1 
ATOM   102   O O4    . U   A 1 8    ? 150.795 159.988 147.340 1.00 40.45  ? 8    U   B O4    1 
ATOM   103   C C5    . U   A 1 8    ? 152.965 159.052 147.324 1.00 40.45  ? 8    U   B C5    1 
ATOM   104   C C6    . U   A 1 8    ? 153.659 157.921 147.202 1.00 40.45  ? 8    U   B C6    1 
ATOM   105   P P     . C   A 1 9    ? 156.628 153.308 144.616 1.00 44.73  ? 9    C   B P     1 
ATOM   106   O OP1   . C   A 1 9    ? 157.067 151.897 144.474 1.00 44.73  ? 9    C   B OP1   1 
ATOM   107   O OP2   . C   A 1 9    ? 157.632 154.399 144.576 1.00 44.73  ? 9    C   B OP2   1 
ATOM   108   O "O5'" . C   A 1 9    ? 155.542 153.606 143.490 1.00 44.73  ? 9    C   B "O5'" 1 
ATOM   109   C "C5'" . C   A 1 9    ? 154.533 152.653 143.192 1.00 44.73  ? 9    C   B "C5'" 1 
ATOM   110   C "C4'" . C   A 1 9    ? 153.641 153.107 142.063 1.00 44.73  ? 9    C   B "C4'" 1 
ATOM   111   O "O4'" . C   A 1 9    ? 152.500 153.835 142.580 1.00 44.73  ? 9    C   B "O4'" 1 
ATOM   112   C "C3'" . C   A 1 9    ? 154.252 154.062 141.054 1.00 44.73  ? 9    C   B "C3'" 1 
ATOM   113   O "O3'" . C   A 1 9    ? 155.092 153.416 140.116 1.00 44.73  ? 9    C   B "O3'" 1 
ATOM   114   C "C2'" . C   A 1 9    ? 153.021 154.707 140.429 1.00 44.73  ? 9    C   B "C2'" 1 
ATOM   115   O "O2'" . C   A 1 9    ? 152.438 153.844 139.463 1.00 44.73  ? 9    C   B "O2'" 1 
ATOM   116   C "C1'" . C   A 1 9    ? 152.076 154.792 141.631 1.00 44.73  ? 9    C   B "C1'" 1 
ATOM   117   N N1    . C   A 1 9    ? 152.080 156.134 142.254 1.00 44.73  ? 9    C   B N1    1 
ATOM   118   C C2    . C   A 1 9    ? 151.231 157.110 141.732 1.00 44.73  ? 9    C   B C2    1 
ATOM   119   O O2    . C   A 1 9    ? 150.505 156.819 140.771 1.00 44.73  ? 9    C   B O2    1 
ATOM   120   N N3    . C   A 1 9    ? 151.218 158.344 142.284 1.00 44.73  ? 9    C   B N3    1 
ATOM   121   C C4    . C   A 1 9    ? 152.012 158.620 143.316 1.00 44.73  ? 9    C   B C4    1 
ATOM   122   N N4    . C   A 1 9    ? 151.968 159.850 143.831 1.00 44.73  ? 9    C   B N4    1 
ATOM   123   C C5    . C   A 1 9    ? 152.888 157.644 143.866 1.00 44.73  ? 9    C   B C5    1 
ATOM   124   C C6    . C   A 1 9    ? 152.888 156.429 143.309 1.00 44.73  ? 9    C   B C6    1 
ATOM   125   P P     . U   A 1 10   ? 156.256 154.239 139.375 1.00 39.97  ? 10   U   B P     1 
ATOM   126   O OP1   . U   A 1 10   ? 157.122 153.271 138.658 1.00 39.97  ? 10   U   B OP1   1 
ATOM   127   O OP2   . U   A 1 10   ? 156.859 155.175 140.354 1.00 39.97  ? 10   U   B OP2   1 
ATOM   128   O "O5'" . U   A 1 10   ? 155.481 155.100 138.284 1.00 39.97  ? 10   U   B "O5'" 1 
ATOM   129   C "C5'" . U   A 1 10   ? 154.746 154.467 137.249 1.00 39.97  ? 10   U   B "C5'" 1 
ATOM   130   C "C4'" . U   A 1 10   ? 153.885 155.451 136.500 1.00 39.97  ? 10   U   B "C4'" 1 
ATOM   131   O "O4'" . U   A 1 10   ? 152.874 155.998 137.385 1.00 39.97  ? 10   U   B "O4'" 1 
ATOM   132   C "C3'" . U   A 1 10   ? 154.595 156.678 135.957 1.00 39.97  ? 10   U   B "C3'" 1 
ATOM   133   O "O3'" . U   A 1 10   ? 155.293 156.426 134.752 1.00 39.97  ? 10   U   B "O3'" 1 
ATOM   134   C "C2'" . U   A 1 10   ? 153.458 157.679 135.811 1.00 39.97  ? 10   U   B "C2'" 1 
ATOM   135   O "O2'" . U   A 1 10   ? 152.703 157.413 134.639 1.00 39.97  ? 10   U   B "O2'" 1 
ATOM   136   C "C1'" . U   A 1 10   ? 152.596 157.335 137.028 1.00 39.97  ? 10   U   B "C1'" 1 
ATOM   137   N N1    . U   A 1 10   ? 152.885 158.212 138.186 1.00 39.97  ? 10   U   B N1    1 
ATOM   138   C C2    . U   A 1 10   ? 152.162 159.381 138.291 1.00 39.97  ? 10   U   B C2    1 
ATOM   139   O O2    . U   A 1 10   ? 151.312 159.705 137.481 1.00 39.97  ? 10   U   B O2    1 
ATOM   140   N N3    . U   A 1 10   ? 152.467 160.156 139.381 1.00 39.97  ? 10   U   B N3    1 
ATOM   141   C C4    . U   A 1 10   ? 153.403 159.889 140.356 1.00 39.97  ? 10   U   B C4    1 
ATOM   142   O O4    . U   A 1 10   ? 153.563 160.688 141.278 1.00 39.97  ? 10   U   B O4    1 
ATOM   143   C C5    . U   A 1 10   ? 154.111 158.662 140.178 1.00 39.97  ? 10   U   B C5    1 
ATOM   144   C C6    . U   A 1 10   ? 153.834 157.887 139.126 1.00 39.97  ? 10   U   B C6    1 
ATOM   145   P P     . A   A 1 11   ? 156.691 157.161 134.465 1.00 44.73  ? 11   A   B P     1 
ATOM   146   O OP1   . A   A 1 11   ? 157.323 156.507 133.294 1.00 44.73  ? 11   A   B OP1   1 
ATOM   147   O OP2   . A   A 1 11   ? 157.439 157.249 135.744 1.00 44.73  ? 11   A   B OP2   1 
ATOM   148   O "O5'" . A   A 1 11   ? 156.265 158.633 134.038 1.00 44.73  ? 11   A   B "O5'" 1 
ATOM   149   C "C5'" . A   A 1 11   ? 155.465 158.848 132.887 1.00 44.73  ? 11   A   B "C5'" 1 
ATOM   150   C "C4'" . A   A 1 11   ? 154.849 160.223 132.886 1.00 44.73  ? 11   A   B "C4'" 1 
ATOM   151   O "O4'" . A   A 1 11   ? 153.910 160.348 133.986 1.00 44.73  ? 11   A   B "O4'" 1 
ATOM   152   C "C3'" . A   A 1 11   ? 155.801 161.387 133.092 1.00 44.73  ? 11   A   B "C3'" 1 
ATOM   153   O "O3'" . A   A 1 11   ? 156.529 161.736 131.930 1.00 44.73  ? 11   A   B "O3'" 1 
ATOM   154   C "C2'" . A   A 1 11   ? 154.867 162.480 133.586 1.00 44.73  ? 11   A   B "C2'" 1 
ATOM   155   O "O2'" . A   A 1 11   ? 154.117 163.023 132.509 1.00 44.73  ? 11   A   B "O2'" 1 
ATOM   156   C "C1'" . A   A 1 11   ? 153.921 161.675 134.473 1.00 44.73  ? 11   A   B "C1'" 1 
ATOM   157   N N9    . A   A 1 11   ? 154.384 161.663 135.872 1.00 44.73  ? 11   A   B N9    1 
ATOM   158   C C8    . A   A 1 11   ? 155.082 160.679 136.523 1.00 44.73  ? 11   A   B C8    1 
ATOM   159   N N7    . A   A 1 11   ? 155.362 160.968 137.770 1.00 44.73  ? 11   A   B N7    1 
ATOM   160   C C5    . A   A 1 11   ? 154.818 162.231 137.948 1.00 44.73  ? 11   A   B C5    1 
ATOM   161   C C6    . A   A 1 11   ? 154.774 163.095 139.053 1.00 44.73  ? 11   A   B C6    1 
ATOM   162   N N6    . A   A 1 11   ? 155.309 162.808 140.241 1.00 44.73  ? 11   A   B N6    1 
ATOM   163   N N1    . A   A 1 11   ? 154.153 164.283 138.898 1.00 44.73  ? 11   A   B N1    1 
ATOM   164   C C2    . A   A 1 11   ? 153.614 164.573 137.708 1.00 44.73  ? 11   A   B C2    1 
ATOM   165   N N3    . A   A 1 11   ? 153.590 163.844 136.597 1.00 44.73  ? 11   A   B N3    1 
ATOM   166   C C4    . A   A 1 11   ? 154.216 162.672 136.786 1.00 44.73  ? 11   A   B C4    1 
ATOM   167   P P     . C   A 1 12   ? 158.046 162.244 132.065 1.00 39.58  ? 12   C   B P     1 
ATOM   168   O OP1   . C   A 1 12   ? 158.555 162.534 130.703 1.00 39.58  ? 12   C   B OP1   1 
ATOM   169   O OP2   . C   A 1 12   ? 158.776 161.285 132.931 1.00 39.58  ? 12   C   B OP2   1 
ATOM   170   O "O5'" . C   A 1 12   ? 157.922 163.625 132.849 1.00 39.58  ? 12   C   B "O5'" 1 
ATOM   171   C "C5'" . C   A 1 12   ? 157.285 164.740 132.245 1.00 39.58  ? 12   C   B "C5'" 1 
ATOM   172   C "C4'" . C   A 1 12   ? 156.865 165.779 133.256 1.00 39.58  ? 12   C   B "C4'" 1 
ATOM   173   O "O4'" . C   A 1 12   ? 156.355 165.150 134.455 1.00 39.58  ? 12   C   B "O4'" 1 
ATOM   174   C "C3'" . C   A 1 12   ? 157.949 166.707 133.770 1.00 39.58  ? 12   C   B "C3'" 1 
ATOM   175   O "O3'" . C   A 1 12   ? 158.251 167.739 132.850 1.00 39.58  ? 12   C   B "O3'" 1 
ATOM   176   C "C2'" . C   A 1 12   ? 157.353 167.220 135.076 1.00 39.58  ? 12   C   B "C2'" 1 
ATOM   177   O "O2'" . C   A 1 12   ? 156.430 168.270 134.828 1.00 39.58  ? 12   C   B "O2'" 1 
ATOM   178   C "C1'" . C   A 1 12   ? 156.573 165.996 135.564 1.00 39.58  ? 12   C   B "C1'" 1 
ATOM   179   N N1    . C   A 1 12   ? 157.287 165.252 136.624 1.00 39.58  ? 12   C   B N1    1 
ATOM   180   C C2    . C   A 1 12   ? 157.133 165.698 137.936 1.00 39.58  ? 12   C   B C2    1 
ATOM   181   O O2    . C   A 1 12   ? 156.414 166.684 138.151 1.00 39.58  ? 12   C   B O2    1 
ATOM   182   N N3    . C   A 1 12   ? 157.765 165.050 138.937 1.00 39.58  ? 12   C   B N3    1 
ATOM   183   C C4    . C   A 1 12   ? 158.526 163.995 138.665 1.00 39.58  ? 12   C   B C4    1 
ATOM   184   N N4    . C   A 1 12   ? 159.128 163.391 139.689 1.00 39.58  ? 12   C   B N4    1 
ATOM   185   C C5    . C   A 1 12   ? 158.704 163.516 137.336 1.00 39.58  ? 12   C   B C5    1 
ATOM   186   C C6    . C   A 1 12   ? 158.072 164.168 136.352 1.00 39.58  ? 12   C   B C6    1 
ATOM   187   P P     . U   A 1 13   ? 159.726 168.365 132.789 1.00 42.48  ? 13   U   B P     1 
ATOM   188   O OP1   . U   A 1 13   ? 159.826 169.149 131.532 1.00 42.48  ? 13   U   B OP1   1 
ATOM   189   O OP2   . U   A 1 13   ? 160.703 167.283 133.065 1.00 42.48  ? 13   U   B OP2   1 
ATOM   190   O "O5'" . U   A 1 13   ? 159.758 169.385 134.010 1.00 42.48  ? 13   U   B "O5'" 1 
ATOM   191   C "C5'" . U   A 1 13   ? 158.812 170.446 134.100 1.00 42.48  ? 13   U   B "C5'" 1 
ATOM   192   C "C4'" . U   A 1 13   ? 159.083 171.342 135.284 1.00 42.48  ? 13   U   B "C4'" 1 
ATOM   193   O "O4'" . U   A 1 13   ? 158.919 170.579 136.510 1.00 42.48  ? 13   U   B "O4'" 1 
ATOM   194   C "C3'" . U   A 1 13   ? 160.485 171.943 135.340 1.00 42.48  ? 13   U   B "C3'" 1 
ATOM   195   O "O3'" . U   A 1 13   ? 160.415 173.253 135.899 1.00 42.48  ? 13   U   B "O3'" 1 
ATOM   196   C "C2'" . U   A 1 13   ? 161.213 171.013 136.305 1.00 42.48  ? 13   U   B "C2'" 1 
ATOM   197   O "O2'" . U   A 1 13   ? 162.321 171.591 136.962 1.00 42.48  ? 13   U   B "O2'" 1 
ATOM   198   C "C1'" . U   A 1 13   ? 160.100 170.655 137.283 1.00 42.48  ? 13   U   B "C1'" 1 
ATOM   199   N N1    . U   A 1 13   ? 160.292 169.365 137.959 1.00 42.48  ? 13   U   B N1    1 
ATOM   200   C C2    . U   A 1 13   ? 160.383 169.372 139.334 1.00 42.48  ? 13   U   B C2    1 
ATOM   201   O O2    . U   A 1 13   ? 160.310 170.392 139.997 1.00 42.48  ? 13   U   B O2    1 
ATOM   202   N N3    . U   A 1 13   ? 160.561 168.139 139.908 1.00 42.48  ? 13   U   B N3    1 
ATOM   203   C C4    . U   A 1 13   ? 160.656 166.927 139.259 1.00 42.48  ? 13   U   B C4    1 
ATOM   204   O O4    . U   A 1 13   ? 160.818 165.898 139.916 1.00 42.48  ? 13   U   B O4    1 
ATOM   205   C C5    . U   A 1 13   ? 160.554 167.006 137.836 1.00 42.48  ? 13   U   B C5    1 
ATOM   206   C C6    . U   A 1 13   ? 160.379 168.194 137.251 1.00 42.48  ? 13   U   B C6    1 
ATOM   207   P P     . C   A 1 14   ? 160.202 174.526 134.943 1.00 45.75  ? 14   C   B P     1 
ATOM   208   O OP1   . C   A 1 14   ? 158.743 174.740 134.783 1.00 45.75  ? 14   C   B OP1   1 
ATOM   209   O OP2   . C   A 1 14   ? 161.048 174.348 133.738 1.00 45.75  ? 14   C   B OP2   1 
ATOM   210   O "O5'" . C   A 1 14   ? 160.795 175.743 135.783 1.00 45.75  ? 14   C   B "O5'" 1 
ATOM   211   C "C5'" . C   A 1 14   ? 160.192 176.156 137.002 1.00 45.75  ? 14   C   B "C5'" 1 
ATOM   212   C "C4'" . C   A 1 14   ? 159.432 177.446 136.825 1.00 45.75  ? 14   C   B "C4'" 1 
ATOM   213   O "O4'" . C   A 1 14   ? 158.211 177.194 136.083 1.00 45.75  ? 14   C   B "O4'" 1 
ATOM   214   C "C3'" . C   A 1 14   ? 158.955 178.133 138.097 1.00 45.75  ? 14   C   B "C3'" 1 
ATOM   215   O "O3'" . C   A 1 14   ? 159.984 178.880 138.730 1.00 45.75  ? 14   C   B "O3'" 1 
ATOM   216   C "C2'" . C   A 1 14   ? 157.792 178.976 137.592 1.00 45.75  ? 14   C   B "C2'" 1 
ATOM   217   O "O2'" . C   A 1 14   ? 158.266 180.147 136.944 1.00 45.75  ? 14   C   B "O2'" 1 
ATOM   218   C "C1'" . C   A 1 14   ? 157.187 178.052 136.536 1.00 45.75  ? 14   C   B "C1'" 1 
ATOM   219   N N1    . C   A 1 14   ? 156.084 177.227 137.080 1.00 45.75  ? 14   C   B N1    1 
ATOM   220   C C2    . C   A 1 14   ? 154.818 177.800 137.229 1.00 45.75  ? 14   C   B C2    1 
ATOM   221   O O2    . C   A 1 14   ? 154.650 178.985 136.905 1.00 45.75  ? 14   C   B O2    1 
ATOM   222   N N3    . C   A 1 14   ? 153.807 177.051 137.724 1.00 45.75  ? 14   C   B N3    1 
ATOM   223   C C4    . C   A 1 14   ? 154.020 175.780 138.062 1.00 45.75  ? 14   C   B C4    1 
ATOM   224   N N4    . C   A 1 14   ? 152.992 175.079 138.546 1.00 45.75  ? 14   C   B N4    1 
ATOM   225   C C5    . C   A 1 14   ? 155.297 175.168 137.919 1.00 45.75  ? 14   C   B C5    1 
ATOM   226   C C6    . C   A 1 14   ? 156.288 175.921 137.428 1.00 45.75  ? 14   C   B C6    1 
ATOM   227   P P     . U   A 1 15   ? 159.698 179.780 140.036 1.00 49.76  ? 15   U   B P     1 
ATOM   228   O OP1   . U   A 1 15   ? 158.265 179.756 140.424 1.00 49.76  ? 15   U   B OP1   1 
ATOM   229   O OP2   . U   A 1 15   ? 160.340 181.093 139.783 1.00 49.76  ? 15   U   B OP2   1 
ATOM   230   O "O5'" . U   A 1 15   ? 160.534 179.068 141.192 1.00 49.76  ? 15   U   B "O5'" 1 
ATOM   231   C "C5'" . U   A 1 15   ? 160.376 177.685 141.479 1.00 49.76  ? 15   U   B "C5'" 1 
ATOM   232   C "C4'" . U   A 1 15   ? 159.111 177.418 142.254 1.00 49.76  ? 15   U   B "C4'" 1 
ATOM   233   O "O4'" . U   A 1 15   ? 158.035 177.117 141.330 1.00 49.76  ? 15   U   B "O4'" 1 
ATOM   234   C "C3'" . U   A 1 15   ? 159.141 176.223 143.192 1.00 49.76  ? 15   U   B "C3'" 1 
ATOM   235   O "O3'" . U   A 1 15   ? 159.731 176.528 144.442 1.00 49.76  ? 15   U   B "O3'" 1 
ATOM   236   C "C2'" . U   A 1 15   ? 157.670 175.844 143.301 1.00 49.76  ? 15   U   B "C2'" 1 
ATOM   237   O "O2'" . U   A 1 15   ? 156.999 176.701 144.213 1.00 49.76  ? 15   U   B "O2'" 1 
ATOM   238   C "C1'" . U   A 1 15   ? 157.169 176.156 141.891 1.00 49.76  ? 15   U   B "C1'" 1 
ATOM   239   N N1    . U   A 1 15   ? 157.159 174.960 141.019 1.00 49.76  ? 15   U   B N1    1 
ATOM   240   C C2    . U   A 1 15   ? 156.086 174.100 141.124 1.00 49.76  ? 15   U   B C2    1 
ATOM   241   O O2    . U   A 1 15   ? 155.166 174.285 141.901 1.00 49.76  ? 15   U   B O2    1 
ATOM   242   N N3    . U   A 1 15   ? 156.130 173.013 140.290 1.00 49.76  ? 15   U   B N3    1 
ATOM   243   C C4    . U   A 1 15   ? 157.115 172.705 139.377 1.00 49.76  ? 15   U   B C4    1 
ATOM   244   O O4    . U   A 1 15   ? 157.012 171.685 138.695 1.00 49.76  ? 15   U   B O4    1 
ATOM   245   C C5    . U   A 1 15   ? 158.191 173.645 139.325 1.00 49.76  ? 15   U   B C5    1 
ATOM   246   C C6    . U   A 1 15   ? 158.175 174.714 140.126 1.00 49.76  ? 15   U   B C6    1 
ATOM   247   P P     . U   A 1 16   ? 161.226 176.048 144.777 1.00 45.66  ? 16   U   B P     1 
ATOM   248   O OP1   . U   A 1 16   ? 162.035 177.252 145.087 1.00 45.66  ? 16   U   B OP1   1 
ATOM   249   O OP2   . U   A 1 16   ? 161.664 175.131 143.696 1.00 45.66  ? 16   U   B OP2   1 
ATOM   250   O "O5'" . U   A 1 16   ? 161.066 175.196 146.114 1.00 45.66  ? 16   U   B "O5'" 1 
ATOM   251   C "C5'" . U   A 1 16   ? 160.579 173.860 146.071 1.00 45.66  ? 16   U   B "C5'" 1 
ATOM   252   C "C4'" . U   A 1 16   ? 161.169 173.002 147.164 1.00 45.66  ? 16   U   B "C4'" 1 
ATOM   253   O "O4'" . U   A 1 16   ? 162.616 173.169 147.197 1.00 45.66  ? 16   U   B "O4'" 1 
ATOM   254   C "C3'" . U   A 1 16   ? 160.673 173.294 148.582 1.00 45.66  ? 16   U   B "C3'" 1 
ATOM   255   O "O3'" . U   A 1 16   ? 160.567 172.068 149.303 1.00 45.66  ? 16   U   B "O3'" 1 
ATOM   256   C "C2'" . U   A 1 16   ? 161.810 174.122 149.173 1.00 45.66  ? 16   U   B "C2'" 1 
ATOM   257   O "O2'" . U   A 1 16   ? 161.894 174.086 150.582 1.00 45.66  ? 16   U   B "O2'" 1 
ATOM   258   C "C1'" . U   A 1 16   ? 163.020 173.468 148.517 1.00 45.66  ? 16   U   B "C1'" 1 
ATOM   259   N N1    . U   A 1 16   ? 164.244 174.289 148.490 1.00 45.66  ? 16   U   B N1    1 
ATOM   260   C C2    . U   A 1 16   ? 164.278 175.516 147.849 1.00 45.66  ? 16   U   B C2    1 
ATOM   261   O O2    . U   A 1 16   ? 163.335 176.008 147.262 1.00 45.66  ? 16   U   B O2    1 
ATOM   262   N N3    . U   A 1 16   ? 165.483 176.169 147.908 1.00 45.66  ? 16   U   B N3    1 
ATOM   263   C C4    . U   A 1 16   ? 166.636 175.744 148.529 1.00 45.66  ? 16   U   B C4    1 
ATOM   264   O O4    . U   A 1 16   ? 167.643 176.453 148.492 1.00 45.66  ? 16   U   B O4    1 
ATOM   265   C C5    . U   A 1 16   ? 166.524 174.475 149.173 1.00 45.66  ? 16   U   B C5    1 
ATOM   266   C C6    . U   A 1 16   ? 165.364 173.814 149.130 1.00 45.66  ? 16   U   B C6    1 
ATOM   267   P P     . G   A 1 17   ? 159.124 171.448 149.635 1.00 42.27  ? 17   G   B P     1 
ATOM   268   O OP1   . G   A 1 17   ? 158.738 171.908 150.992 1.00 42.27  ? 17   G   B OP1   1 
ATOM   269   O OP2   . G   A 1 17   ? 159.155 169.995 149.337 1.00 42.27  ? 17   G   B OP2   1 
ATOM   270   O "O5'" . G   A 1 17   ? 158.160 172.151 148.581 1.00 42.27  ? 17   G   B "O5'" 1 
ATOM   271   C "C5'" . G   A 1 17   ? 157.079 171.445 147.990 1.00 42.27  ? 17   G   B "C5'" 1 
ATOM   272   C "C4'" . G   A 1 17   ? 156.883 171.859 146.555 1.00 42.27  ? 17   G   B "C4'" 1 
ATOM   273   O "O4'" . G   A 1 17   ? 158.076 171.541 145.789 1.00 42.27  ? 17   G   B "O4'" 1 
ATOM   274   C "C3'" . G   A 1 17   ? 155.769 171.156 145.798 1.00 42.27  ? 17   G   B "C3'" 1 
ATOM   275   O "O3'" . G   A 1 17   ? 154.481 171.677 146.065 1.00 42.27  ? 17   G   B "O3'" 1 
ATOM   276   C "C2'" . G   A 1 17   ? 156.209 171.319 144.354 1.00 42.27  ? 17   G   B "C2'" 1 
ATOM   277   O "O2'" . G   A 1 17   ? 155.975 172.646 143.909 1.00 42.27  ? 17   G   B "O2'" 1 
ATOM   278   C "C1'" . G   A 1 17   ? 157.714 171.120 144.491 1.00 42.27  ? 17   G   B "C1'" 1 
ATOM   279   N N9    . G   A 1 17   ? 158.073 169.697 144.351 1.00 42.27  ? 17   G   B N9    1 
ATOM   280   C C8    . G   A 1 17   ? 158.599 168.879 145.318 1.00 42.27  ? 17   G   B C8    1 
ATOM   281   N N7    . G   A 1 17   ? 158.801 167.660 144.901 1.00 42.27  ? 17   G   B N7    1 
ATOM   282   C C5    . G   A 1 17   ? 158.375 167.674 143.581 1.00 42.27  ? 17   G   B C5    1 
ATOM   283   C C6    . G   A 1 17   ? 158.354 166.638 142.614 1.00 42.27  ? 17   G   B C6    1 
ATOM   284   O O6    . G   A 1 17   ? 158.717 165.462 142.736 1.00 42.27  ? 17   G   B O6    1 
ATOM   285   N N1    . G   A 1 17   ? 157.846 167.084 141.400 1.00 42.27  ? 17   G   B N1    1 
ATOM   286   C C2    . G   A 1 17   ? 157.414 168.360 141.147 1.00 42.27  ? 17   G   B C2    1 
ATOM   287   N N2    . G   A 1 17   ? 156.957 168.595 139.909 1.00 42.27  ? 17   G   B N2    1 
ATOM   288   N N3    . G   A 1 17   ? 157.431 169.334 142.038 1.00 42.27  ? 17   G   B N3    1 
ATOM   289   C C4    . G   A 1 17   ? 157.924 168.924 143.225 1.00 42.27  ? 17   G   B C4    1 
ATOM   290   P P     . U   A 1 18   ? 153.188 170.747 145.858 1.00 37.53  ? 18   U   B P     1 
ATOM   291   O OP1   . U   A 1 18   ? 152.036 171.383 146.540 1.00 37.53  ? 18   U   B OP1   1 
ATOM   292   O OP2   . U   A 1 18   ? 153.567 169.358 146.217 1.00 37.53  ? 18   U   B OP2   1 
ATOM   293   O "O5'" . U   A 1 18   ? 152.932 170.789 144.286 1.00 37.53  ? 18   U   B "O5'" 1 
ATOM   294   C "C5'" . U   A 1 18   ? 152.805 172.026 143.601 1.00 37.53  ? 18   U   B "C5'" 1 
ATOM   295   C "C4'" . U   A 1 18   ? 152.688 171.829 142.111 1.00 37.53  ? 18   U   B "C4'" 1 
ATOM   296   O "O4'" . U   A 1 18   ? 153.861 171.138 141.609 1.00 37.53  ? 18   U   B "O4'" 1 
ATOM   297   C "C3'" . U   A 1 18   ? 151.528 170.967 141.644 1.00 37.53  ? 18   U   B "C3'" 1 
ATOM   298   O "O3'" . U   A 1 18   ? 150.299 171.667 141.605 1.00 37.53  ? 18   U   B "O3'" 1 
ATOM   299   C "C2'" . U   A 1 18   ? 152.004 170.484 140.282 1.00 37.53  ? 18   U   B "C2'" 1 
ATOM   300   O "O2'" . U   A 1 18   ? 151.846 171.502 139.305 1.00 37.53  ? 18   U   B "O2'" 1 
ATOM   301   C "C1'" . U   A 1 18   ? 153.499 170.291 140.539 1.00 37.53  ? 18   U   B "C1'" 1 
ATOM   302   N N1    . U   A 1 18   ? 153.824 168.896 140.910 1.00 37.53  ? 18   U   B N1    1 
ATOM   303   C C2    . U   A 1 18   ? 153.880 167.955 139.903 1.00 37.53  ? 18   U   B C2    1 
ATOM   304   O O2    . U   A 1 18   ? 153.675 168.221 138.732 1.00 37.53  ? 18   U   B O2    1 
ATOM   305   N N3    . U   A 1 18   ? 154.187 166.685 140.316 1.00 37.53  ? 18   U   B N3    1 
ATOM   306   C C4    . U   A 1 18   ? 154.438 166.268 141.604 1.00 37.53  ? 18   U   B C4    1 
ATOM   307   O O4    . U   A 1 18   ? 154.702 165.084 141.819 1.00 37.53  ? 18   U   B O4    1 
ATOM   308   C C5    . U   A 1 18   ? 154.361 167.299 142.589 1.00 37.53  ? 18   U   B C5    1 
ATOM   309   C C6    . U   A 1 18   ? 154.065 168.546 142.215 1.00 37.53  ? 18   U   B C6    1 
ATOM   310   P P     . A   A 1 19   ? 148.990 171.015 142.266 1.00 39.59  ? 19   A   B P     1 
ATOM   311   O OP1   . A   A 1 19   ? 147.946 172.066 142.358 1.00 39.59  ? 19   A   B OP1   1 
ATOM   312   O OP2   . A   A 1 19   ? 149.409 170.285 143.487 1.00 39.59  ? 19   A   B OP2   1 
ATOM   313   O "O5'" . A   A 1 19   ? 148.516 169.940 141.194 1.00 39.59  ? 19   A   B "O5'" 1 
ATOM   314   C "C5'" . A   A 1 19   ? 147.981 170.347 139.945 1.00 39.59  ? 19   A   B "C5'" 1 
ATOM   315   C "C4'" . A   A 1 19   ? 147.677 169.163 139.063 1.00 39.59  ? 19   A   B "C4'" 1 
ATOM   316   O "O4'" . A   A 1 19   ? 148.914 168.567 138.594 1.00 39.59  ? 19   A   B "O4'" 1 
ATOM   317   C "C3'" . A   A 1 19   ? 146.943 168.009 139.723 1.00 39.59  ? 19   A   B "C3'" 1 
ATOM   318   O "O3'" . A   A 1 19   ? 145.548 168.223 139.834 1.00 39.59  ? 19   A   B "O3'" 1 
ATOM   319   C "C2'" . A   A 1 19   ? 147.313 166.834 138.831 1.00 39.59  ? 19   A   B "C2'" 1 
ATOM   320   O "O2'" . A   A 1 19   ? 146.558 166.859 137.629 1.00 39.59  ? 19   A   B "O2'" 1 
ATOM   321   C "C1'" . A   A 1 19   ? 148.765 167.167 138.494 1.00 39.59  ? 19   A   B "C1'" 1 
ATOM   322   N N9    . A   A 1 19   ? 149.699 166.531 139.439 1.00 39.59  ? 19   A   B N9    1 
ATOM   323   C C8    . A   A 1 19   ? 150.281 167.092 140.546 1.00 39.59  ? 19   A   B C8    1 
ATOM   324   N N7    . A   A 1 19   ? 151.068 166.276 141.201 1.00 39.59  ? 19   A   B N7    1 
ATOM   325   C C5    . A   A 1 19   ? 150.996 165.096 140.476 1.00 39.59  ? 19   A   B C5    1 
ATOM   326   C C6    . A   A 1 19   ? 151.605 163.843 140.650 1.00 39.59  ? 19   A   B C6    1 
ATOM   327   N N6    . A   A 1 19   ? 152.440 163.557 141.651 1.00 39.59  ? 19   A   B N6    1 
ATOM   328   N N1    . A   A 1 19   ? 151.324 162.879 139.748 1.00 39.59  ? 19   A   B N1    1 
ATOM   329   C C2    . A   A 1 19   ? 150.487 163.164 138.745 1.00 39.59  ? 19   A   B C2    1 
ATOM   330   N N3    . A   A 1 19   ? 149.854 164.302 138.476 1.00 39.59  ? 19   A   B N3    1 
ATOM   331   C C4    . A   A 1 19   ? 150.156 165.239 139.389 1.00 39.59  ? 19   A   B C4    1 
ATOM   332   P P     . G   A 1 20   ? 144.721 167.535 141.027 1.00 36.97  ? 20   G   B P     1 
ATOM   333   O OP1   . G   A 1 20   ? 143.334 168.059 140.981 1.00 36.97  ? 20   G   B OP1   1 
ATOM   334   O OP2   . G   A 1 20   ? 145.518 167.641 142.274 1.00 36.97  ? 20   G   B OP2   1 
ATOM   335   O "O5'" . G   A 1 20   ? 144.651 166.002 140.613 1.00 36.97  ? 20   G   B "O5'" 1 
ATOM   336   C "C5'" . G   A 1 20   ? 143.858 165.592 139.513 1.00 36.97  ? 20   G   B "C5'" 1 
ATOM   337   C "C4'" . G   A 1 20   ? 144.147 164.166 139.124 1.00 36.97  ? 20   G   B "C4'" 1 
ATOM   338   O "O4'" . G   A 1 20   ? 145.563 164.006 138.850 1.00 36.97  ? 20   G   B "O4'" 1 
ATOM   339   C "C3'" . G   A 1 20   ? 143.867 163.111 140.178 1.00 36.97  ? 20   G   B "C3'" 1 
ATOM   340   O "O3'" . G   A 1 20   ? 142.496 162.782 140.296 1.00 36.97  ? 20   G   B "O3'" 1 
ATOM   341   C "C2'" . G   A 1 20   ? 144.738 161.957 139.711 1.00 36.97  ? 20   G   B "C2'" 1 
ATOM   342   O "O2'" . G   A 1 20   ? 144.140 161.294 138.607 1.00 36.97  ? 20   G   B "O2'" 1 
ATOM   343   C "C1'" . G   A 1 20   ? 145.972 162.703 139.212 1.00 36.97  ? 20   G   B "C1'" 1 
ATOM   344   N N9    . G   A 1 20   ? 147.003 162.795 140.261 1.00 36.97  ? 20   G   B N9    1 
ATOM   345   C C8    . G   A 1 20   ? 147.210 163.818 141.153 1.00 36.97  ? 20   G   B C8    1 
ATOM   346   N N7    . G   A 1 20   ? 148.205 163.588 141.967 1.00 36.97  ? 20   G   B N7    1 
ATOM   347   C C5    . G   A 1 20   ? 148.675 162.337 141.594 1.00 36.97  ? 20   G   B C5    1 
ATOM   348   C C6    . G   A 1 20   ? 149.740 161.558 142.114 1.00 36.97  ? 20   G   B C6    1 
ATOM   349   O O6    . G   A 1 20   ? 150.512 161.827 143.043 1.00 36.97  ? 20   G   B O6    1 
ATOM   350   N N1    . G   A 1 20   ? 149.869 160.350 141.435 1.00 36.97  ? 20   G   B N1    1 
ATOM   351   C C2    . G   A 1 20   ? 149.075 159.943 140.392 1.00 36.97  ? 20   G   B C2    1 
ATOM   352   N N2    . G   A 1 20   ? 149.352 158.743 139.864 1.00 36.97  ? 20   G   B N2    1 
ATOM   353   N N3    . G   A 1 20   ? 148.080 160.660 139.900 1.00 36.97  ? 20   G   B N3    1 
ATOM   354   C C4    . G   A 1 20   ? 147.940 161.834 140.545 1.00 36.97  ? 20   G   B C4    1 
ATOM   355   P P     . A   A 1 21   ? 141.913 162.265 141.701 1.00 40.07  ? 21   A   B P     1 
ATOM   356   O OP1   . A   A 1 21   ? 140.438 162.170 141.583 1.00 40.07  ? 21   A   B OP1   1 
ATOM   357   O OP2   . A   A 1 21   ? 142.507 163.095 142.777 1.00 40.07  ? 21   A   B OP2   1 
ATOM   358   O "O5'" . A   A 1 21   ? 142.496 160.789 141.839 1.00 40.07  ? 21   A   B "O5'" 1 
ATOM   359   C "C5'" . A   A 1 21   ? 142.169 159.789 140.887 1.00 40.07  ? 21   A   B "C5'" 1 
ATOM   360   C "C4'" . A   A 1 21   ? 143.107 158.611 140.964 1.00 40.07  ? 21   A   B "C4'" 1 
ATOM   361   O "O4'" . A   A 1 21   ? 144.478 159.049 140.799 1.00 40.07  ? 21   A   B "O4'" 1 
ATOM   362   C "C3'" . A   A 1 21   ? 143.122 157.846 142.276 1.00 40.07  ? 21   A   B "C3'" 1 
ATOM   363   O "O3'" . A   A 1 21   ? 142.039 156.942 142.390 1.00 40.07  ? 21   A   B "O3'" 1 
ATOM   364   C "C2'" . A   A 1 21   ? 144.483 157.163 142.244 1.00 40.07  ? 21   A   B "C2'" 1 
ATOM   365   O "O2'" . A   A 1 21   ? 144.444 156.007 141.421 1.00 40.07  ? 21   A   B "O2'" 1 
ATOM   366   C "C1'" . A   A 1 21   ? 145.340 158.221 141.548 1.00 40.07  ? 21   A   B "C1'" 1 
ATOM   367   N N9    . A   A 1 21   ? 146.089 159.056 142.505 1.00 40.07  ? 21   A   B N9    1 
ATOM   368   C C8    . A   A 1 21   ? 145.879 160.374 142.821 1.00 40.07  ? 21   A   B C8    1 
ATOM   369   N N7    . A   A 1 21   ? 146.720 160.844 143.710 1.00 40.07  ? 21   A   B N7    1 
ATOM   370   C C5    . A   A 1 21   ? 147.541 159.763 143.993 1.00 40.07  ? 21   A   B C5    1 
ATOM   371   C C6    . A   A 1 21   ? 148.635 159.609 144.860 1.00 40.07  ? 21   A   B C6    1 
ATOM   372   N N6    . A   A 1 21   ? 149.111 160.588 145.633 1.00 40.07  ? 21   A   B N6    1 
ATOM   373   N N1    . A   A 1 21   ? 149.234 158.399 144.909 1.00 40.07  ? 21   A   B N1    1 
ATOM   374   C C2    . A   A 1 21   ? 148.756 157.417 144.134 1.00 40.07  ? 21   A   B C2    1 
ATOM   375   N N3    . A   A 1 21   ? 147.736 157.441 143.280 1.00 40.07  ? 21   A   B N3    1 
ATOM   376   C C4    . A   A 1 21   ? 147.165 158.657 143.256 1.00 40.07  ? 21   A   B C4    1 
ATOM   377   P P     . U   A 1 22   ? 141.247 156.797 143.778 1.00 34.67  ? 22   U   B P     1 
ATOM   378   O OP1   . U   A 1 22   ? 140.123 155.851 143.570 1.00 34.67  ? 22   U   B OP1   1 
ATOM   379   O OP2   . U   A 1 22   ? 140.973 158.157 144.303 1.00 34.67  ? 22   U   B OP2   1 
ATOM   380   O "O5'" . U   A 1 22   ? 142.300 156.095 144.742 1.00 34.67  ? 22   U   B "O5'" 1 
ATOM   381   C "C5'" . U   A 1 22   ? 142.840 154.822 144.425 1.00 34.67  ? 22   U   B "C5'" 1 
ATOM   382   C "C4'" . U   A 1 22   ? 144.050 154.518 145.267 1.00 34.67  ? 22   U   B "C4'" 1 
ATOM   383   O "O4'" . U   A 1 22   ? 145.134 155.416 144.914 1.00 34.67  ? 22   U   B "O4'" 1 
ATOM   384   C "C3'" . U   A 1 22   ? 143.880 154.722 146.761 1.00 34.67  ? 22   U   B "C3'" 1 
ATOM   385   O "O3'" . U   A 1 22   ? 143.214 153.647 147.396 1.00 34.67  ? 22   U   B "O3'" 1 
ATOM   386   C "C2'" . U   A 1 22   ? 145.313 154.928 147.229 1.00 34.67  ? 22   U   B "C2'" 1 
ATOM   387   O "O2'" . U   A 1 22   ? 146.002 153.687 147.297 1.00 34.67  ? 22   U   B "O2'" 1 
ATOM   388   C "C1'" . U   A 1 22   ? 145.891 155.732 146.065 1.00 34.67  ? 22   U   B "C1'" 1 
ATOM   389   N N1    . U   A 1 22   ? 145.801 157.190 146.303 1.00 34.67  ? 22   U   B N1    1 
ATOM   390   C C2    . U   A 1 22   ? 146.776 157.773 147.085 1.00 34.67  ? 22   U   B C2    1 
ATOM   391   O O2    . U   A 1 22   ? 147.696 157.142 147.576 1.00 34.67  ? 22   U   B O2    1 
ATOM   392   N N3    . U   A 1 22   ? 146.639 159.125 147.271 1.00 34.67  ? 22   U   B N3    1 
ATOM   393   C C4    . U   A 1 22   ? 145.647 159.938 146.768 1.00 34.67  ? 22   U   B C4    1 
ATOM   394   O O4    . U   A 1 22   ? 145.660 161.142 147.025 1.00 34.67  ? 22   U   B O4    1 
ATOM   395   C C5    . U   A 1 22   ? 144.673 159.261 145.969 1.00 34.67  ? 22   U   B C5    1 
ATOM   396   C C6    . U   A 1 22   ? 144.783 157.945 145.771 1.00 34.67  ? 22   U   B C6    1 
ATOM   397   P P     . A   A 1 23   ? 141.726 153.851 147.965 1.00 33.77  ? 23   A   B P     1 
ATOM   398   O OP1   . A   A 1 23   ? 140.776 153.257 146.992 1.00 33.77  ? 23   A   B OP1   1 
ATOM   399   O OP2   . A   A 1 23   ? 141.575 155.272 148.364 1.00 33.77  ? 23   A   B OP2   1 
ATOM   400   O "O5'" . A   A 1 23   ? 141.701 152.965 149.286 1.00 33.77  ? 23   A   B "O5'" 1 
ATOM   401   C "C5'" . A   A 1 23   ? 142.716 153.109 150.271 1.00 33.77  ? 23   A   B "C5'" 1 
ATOM   402   C "C4'" . A   A 1 23   ? 143.341 151.784 150.632 1.00 33.77  ? 23   A   B "C4'" 1 
ATOM   403   O "O4'" . A   A 1 23   ? 142.452 151.054 151.519 1.00 33.77  ? 23   A   B "O4'" 1 
ATOM   404   C "C3'" . A   A 1 23   ? 143.638 150.849 149.459 1.00 33.77  ? 23   A   B "C3'" 1 
ATOM   405   O "O3'" . A   A 1 23   ? 144.843 150.134 149.723 1.00 33.77  ? 23   A   B "O3'" 1 
ATOM   406   C "C2'" . A   A 1 23   ? 142.461 149.879 149.497 1.00 33.77  ? 23   A   B "C2'" 1 
ATOM   407   O "O2'" . A   A 1 23   ? 142.717 148.621 148.910 1.00 33.77  ? 23   A   B "O2'" 1 
ATOM   408   C "C1'" . A   A 1 23   ? 142.218 149.764 150.997 1.00 33.77  ? 23   A   B "C1'" 1 
ATOM   409   N N9    . A   A 1 23   ? 140.861 149.356 151.364 1.00 33.77  ? 23   A   B N9    1 
ATOM   410   C C8    . A   A 1 23   ? 139.738 149.334 150.577 1.00 33.77  ? 23   A   B C8    1 
ATOM   411   N N7    . A   A 1 23   ? 138.667 148.910 151.202 1.00 33.77  ? 23   A   B N7    1 
ATOM   412   C C5    . A   A 1 23   ? 139.118 148.635 152.485 1.00 33.77  ? 23   A   B C5    1 
ATOM   413   C C6    . A   A 1 23   ? 138.470 148.154 153.634 1.00 33.77  ? 23   A   B C6    1 
ATOM   414   N N6    . A   A 1 23   ? 137.171 147.849 153.677 1.00 33.77  ? 23   A   B N6    1 
ATOM   415   N N1    . A   A 1 23   ? 139.208 147.992 154.752 1.00 33.77  ? 23   A   B N1    1 
ATOM   416   C C2    . A   A 1 23   ? 140.510 148.295 154.709 1.00 33.77  ? 23   A   B C2    1 
ATOM   417   N N3    . A   A 1 23   ? 141.231 148.755 153.691 1.00 33.77  ? 23   A   B N3    1 
ATOM   418   C C4    . A   A 1 23   ? 140.467 148.905 152.597 1.00 33.77  ? 23   A   B C4    1 
ATOM   419   P P     . G   A 1 24   ? 146.263 150.764 149.318 1.00 45.83  ? 24   G   B P     1 
ATOM   420   O OP1   . G   A 1 24   ? 146.064 152.191 148.965 1.00 45.83  ? 24   G   B OP1   1 
ATOM   421   O OP2   . G   A 1 24   ? 146.904 149.849 148.341 1.00 45.83  ? 24   G   B OP2   1 
ATOM   422   O "O5'" . G   A 1 24   ? 147.107 150.706 150.665 1.00 45.83  ? 24   G   B "O5'" 1 
ATOM   423   C "C5'" . G   A 1 24   ? 147.714 149.496 151.090 1.00 45.83  ? 24   G   B "C5'" 1 
ATOM   424   C "C4'" . G   A 1 24   ? 147.511 149.264 152.564 1.00 45.83  ? 24   G   B "C4'" 1 
ATOM   425   O "O4'" . G   A 1 24   ? 146.094 149.179 152.851 1.00 45.83  ? 24   G   B "O4'" 1 
ATOM   426   C "C3'" . G   A 1 24   ? 148.078 147.965 153.112 1.00 45.83  ? 24   G   B "C3'" 1 
ATOM   427   O "O3'" . G   A 1 24   ? 149.464 148.048 153.391 1.00 45.83  ? 24   G   B "O3'" 1 
ATOM   428   C "C2'" . G   A 1 24   ? 147.221 147.718 154.347 1.00 45.83  ? 24   G   B "C2'" 1 
ATOM   429   O "O2'" . G   A 1 24   ? 147.667 148.515 155.434 1.00 45.83  ? 24   G   B "O2'" 1 
ATOM   430   C "C1'" . G   A 1 24   ? 145.864 148.249 153.886 1.00 45.83  ? 24   G   B "C1'" 1 
ATOM   431   N N9    . G   A 1 24   ? 144.982 147.186 153.371 1.00 45.83  ? 24   G   B N9    1 
ATOM   432   C C8    . G   A 1 24   ? 144.832 146.806 152.061 1.00 45.83  ? 24   G   B C8    1 
ATOM   433   N N7    . G   A 1 24   ? 143.973 145.837 151.904 1.00 45.83  ? 24   G   B N7    1 
ATOM   434   C C5    . G   A 1 24   ? 143.525 145.564 153.189 1.00 45.83  ? 24   G   B C5    1 
ATOM   435   C C6    . G   A 1 24   ? 142.583 144.609 153.647 1.00 45.83  ? 24   G   B C6    1 
ATOM   436   O O6    . G   A 1 24   ? 141.935 143.787 152.989 1.00 45.83  ? 24   G   B O6    1 
ATOM   437   N N1    . G   A 1 24   ? 142.426 144.671 155.027 1.00 45.83  ? 24   G   B N1    1 
ATOM   438   C C2    . G   A 1 24   ? 143.089 145.538 155.859 1.00 45.83  ? 24   G   B C2    1 
ATOM   439   N N2    . G   A 1 24   ? 142.799 145.441 157.165 1.00 45.83  ? 24   G   B N2    1 
ATOM   440   N N3    . G   A 1 24   ? 143.969 146.432 155.444 1.00 45.83  ? 24   G   B N3    1 
ATOM   441   C C4    . G   A 1 24   ? 144.137 146.389 154.106 1.00 45.83  ? 24   G   B C4    1 
ATOM   442   P P     . C   A 1 25   ? 150.469 146.927 152.834 1.00 56.29  ? 25   C   B P     1 
ATOM   443   O OP1   . C   A 1 25   ? 151.853 147.445 152.966 1.00 56.29  ? 25   C   B OP1   1 
ATOM   444   O OP2   . C   A 1 25   ? 149.975 146.487 151.505 1.00 56.29  ? 25   C   B OP2   1 
ATOM   445   O "O5'" . C   A 1 25   ? 150.294 145.717 153.854 1.00 56.29  ? 25   C   B "O5'" 1 
ATOM   446   C "C5'" . C   A 1 25   ? 150.664 145.858 155.217 1.00 56.29  ? 25   C   B "C5'" 1 
ATOM   447   C "C4'" . C   A 1 25   ? 149.932 144.877 156.097 1.00 56.29  ? 25   C   B "C4'" 1 
ATOM   448   O "O4'" . C   A 1 25   ? 148.502 145.068 155.958 1.00 56.29  ? 25   C   B "O4'" 1 
ATOM   449   C "C3'" . C   A 1 25   ? 150.140 143.405 155.778 1.00 56.29  ? 25   C   B "C3'" 1 
ATOM   450   O "O3'" . C   A 1 25   ? 151.344 142.891 156.319 1.00 56.29  ? 25   C   B "O3'" 1 
ATOM   451   C "C2'" . C   A 1 25   ? 148.890 142.757 156.361 1.00 56.29  ? 25   C   B "C2'" 1 
ATOM   452   O "O2'" . C   A 1 25   ? 149.019 142.595 157.766 1.00 56.29  ? 25   C   B "O2'" 1 
ATOM   453   C "C1'" . C   A 1 25   ? 147.835 143.832 156.095 1.00 56.29  ? 25   C   B "C1'" 1 
ATOM   454   N N1    . C   A 1 25   ? 147.059 143.570 154.862 1.00 56.29  ? 25   C   B N1    1 
ATOM   455   C C2    . C   A 1 25   ? 145.953 142.720 154.938 1.00 56.29  ? 25   C   B C2    1 
ATOM   456   O O2    . C   A 1 25   ? 145.660 142.213 156.029 1.00 56.29  ? 25   C   B O2    1 
ATOM   457   N N3    . C   A 1 25   ? 145.231 142.473 153.823 1.00 56.29  ? 25   C   B N3    1 
ATOM   458   C C4    . C   A 1 25   ? 145.576 143.036 152.665 1.00 56.29  ? 25   C   B C4    1 
ATOM   459   N N4    . C   A 1 25   ? 144.834 142.763 151.590 1.00 56.29  ? 25   C   B N4    1 
ATOM   460   C C5    . C   A 1 25   ? 146.698 143.908 152.559 1.00 56.29  ? 25   C   B C5    1 
ATOM   461   C C6    . C   A 1 25   ? 147.403 144.145 153.671 1.00 56.29  ? 25   C   B C6    1 
ATOM   462   P P     . A   A 1 26   ? 152.368 142.079 155.387 1.00 78.07  ? 26   A   B P     1 
ATOM   463   O OP1   . A   A 1 26   ? 153.621 141.875 156.156 1.00 78.07  ? 26   A   B OP1   1 
ATOM   464   O OP2   . A   A 1 26   ? 152.418 142.745 154.062 1.00 78.07  ? 26   A   B OP2   1 
ATOM   465   O "O5'" . A   A 1 26   ? 151.674 140.660 155.195 1.00 78.07  ? 26   A   B "O5'" 1 
ATOM   466   C "C5'" . A   A 1 26   ? 151.533 139.760 156.284 1.00 78.07  ? 26   A   B "C5'" 1 
ATOM   467   C "C4'" . A   A 1 26   ? 150.625 138.611 155.928 1.00 78.07  ? 26   A   B "C4'" 1 
ATOM   468   O "O4'" . A   A 1 26   ? 149.302 139.122 155.619 1.00 78.07  ? 26   A   B "O4'" 1 
ATOM   469   C "C3'" . A   A 1 26   ? 151.019 137.818 154.690 1.00 78.07  ? 26   A   B "C3'" 1 
ATOM   470   O "O3'" . A   A 1 26   ? 152.000 136.831 154.958 1.00 78.07  ? 26   A   B "O3'" 1 
ATOM   471   C "C2'" . A   A 1 26   ? 149.690 137.245 154.219 1.00 78.07  ? 26   A   B "C2'" 1 
ATOM   472   O "O2'" . A   A 1 26   ? 149.337 136.107 154.990 1.00 78.07  ? 26   A   B "O2'" 1 
ATOM   473   C "C1'" . A   A 1 26   ? 148.730 138.383 154.563 1.00 78.07  ? 26   A   B "C1'" 1 
ATOM   474   N N9    . A   A 1 26   ? 148.520 139.296 153.422 1.00 78.07  ? 26   A   B N9    1 
ATOM   475   C C8    . A   A 1 26   ? 149.302 140.361 153.049 1.00 78.07  ? 26   A   B C8    1 
ATOM   476   N N7    . A   A 1 26   ? 148.866 140.994 151.987 1.00 78.07  ? 26   A   B N7    1 
ATOM   477   C C5    . A   A 1 26   ? 147.719 140.298 151.635 1.00 78.07  ? 26   A   B C5    1 
ATOM   478   C C6    . A   A 1 26   ? 146.794 140.470 150.592 1.00 78.07  ? 26   A   B C6    1 
ATOM   479   N N6    . A   A 1 26   ? 146.883 141.436 149.676 1.00 78.07  ? 26   A   B N6    1 
ATOM   480   N N1    . A   A 1 26   ? 145.760 139.605 150.522 1.00 78.07  ? 26   A   B N1    1 
ATOM   481   C C2    . A   A 1 26   ? 145.671 138.636 151.442 1.00 78.07  ? 26   A   B C2    1 
ATOM   482   N N3    . A   A 1 26   ? 146.477 138.373 152.468 1.00 78.07  ? 26   A   B N3    1 
ATOM   483   C C4    . A   A 1 26   ? 147.494 139.249 152.509 1.00 78.07  ? 26   A   B C4    1 
ATOM   484   P P     . G   A 1 27   ? 153.147 136.508 153.879 1.00 104.14 ? 27   G   B P     1 
ATOM   485   O OP1   . G   A 1 27   ? 154.185 135.683 154.546 1.00 104.14 ? 27   G   B OP1   1 
ATOM   486   O OP2   . G   A 1 27   ? 153.533 137.782 153.223 1.00 104.14 ? 27   G   B OP2   1 
ATOM   487   O "O5'" . G   A 1 27   ? 152.416 135.596 152.795 1.00 104.14 ? 27   G   B "O5'" 1 
ATOM   488   C "C5'" . G   A 1 27   ? 151.886 134.325 153.144 1.00 104.14 ? 27   G   B "C5'" 1 
ATOM   489   C "C4'" . G   A 1 27   ? 150.839 133.875 152.156 1.00 104.14 ? 27   G   B "C4'" 1 
ATOM   490   O "O4'" . G   A 1 27   ? 149.799 134.884 152.063 1.00 104.14 ? 27   G   B "O4'" 1 
ATOM   491   C "C3'" . G   A 1 27   ? 151.312 133.696 150.721 1.00 104.14 ? 27   G   B "C3'" 1 
ATOM   492   O "O3'" . G   A 1 27   ? 151.939 132.445 150.493 1.00 104.14 ? 27   G   B "O3'" 1 
ATOM   493   C "C2'" . G   A 1 27   ? 150.032 133.895 149.922 1.00 104.14 ? 27   G   B "C2'" 1 
ATOM   494   O "O2'" . G   A 1 27   ? 149.223 132.729 149.974 1.00 104.14 ? 27   G   B "O2'" 1 
ATOM   495   C "C1'" . G   A 1 27   ? 149.346 134.993 150.730 1.00 104.14 ? 27   G   B "C1'" 1 
ATOM   496   N N9    . G   A 1 27   ? 149.697 136.337 150.234 1.00 104.14 ? 27   G   B N9    1 
ATOM   497   C C8    . G   A 1 27   ? 150.665 137.173 150.737 1.00 104.14 ? 27   G   B C8    1 
ATOM   498   N N7    . G   A 1 27   ? 150.754 138.303 150.091 1.00 104.14 ? 27   G   B N7    1 
ATOM   499   C C5    . G   A 1 27   ? 149.787 138.208 149.100 1.00 104.14 ? 27   G   B C5    1 
ATOM   500   C C6    . G   A 1 27   ? 149.417 139.131 148.090 1.00 104.14 ? 27   G   B C6    1 
ATOM   501   O O6    . G   A 1 27   ? 149.884 140.254 147.861 1.00 104.14 ? 27   G   B O6    1 
ATOM   502   N N1    . G   A 1 27   ? 148.388 138.634 147.296 1.00 104.14 ? 27   G   B N1    1 
ATOM   503   C C2    . G   A 1 27   ? 147.793 137.407 147.453 1.00 104.14 ? 27   G   B C2    1 
ATOM   504   N N2    . G   A 1 27   ? 146.816 137.108 146.584 1.00 104.14 ? 27   G   B N2    1 
ATOM   505   N N3    . G   A 1 27   ? 148.129 136.536 148.391 1.00 104.14 ? 27   G   B N3    1 
ATOM   506   C C4    . G   A 1 27   ? 149.126 136.999 149.173 1.00 104.14 ? 27   G   B C4    1 
ATOM   507   P P     . A   A 1 28   ? 152.930 132.255 149.241 1.00 125.59 ? 28   A   B P     1 
ATOM   508   O OP1   . A   A 1 28   ? 153.560 130.915 149.353 1.00 125.59 ? 28   A   B OP1   1 
ATOM   509   O OP2   . A   A 1 28   ? 153.787 133.463 149.144 1.00 125.59 ? 28   A   B OP2   1 
ATOM   510   O "O5'" . A   A 1 28   ? 151.957 132.238 147.980 1.00 125.59 ? 28   A   B "O5'" 1 
ATOM   511   C "C5'" . A   A 1 28   ? 152.463 132.385 146.661 1.00 125.59 ? 28   A   B "C5'" 1 
ATOM   512   C "C4'" . A   A 1 28   ? 151.351 132.392 145.643 1.00 125.59 ? 28   A   B "C4'" 1 
ATOM   513   O "O4'" . A   A 1 28   ? 150.367 133.398 145.998 1.00 125.59 ? 28   A   B "O4'" 1 
ATOM   514   C "C3'" . A   A 1 28   ? 151.750 132.750 144.220 1.00 125.59 ? 28   A   B "C3'" 1 
ATOM   515   O "O3'" . A   A 1 28   ? 152.307 131.657 143.510 1.00 125.59 ? 28   A   B "O3'" 1 
ATOM   516   C "C2'" . A   A 1 28   ? 150.443 133.260 143.627 1.00 125.59 ? 28   A   B "C2'" 1 
ATOM   517   O "O2'" . A   A 1 28   ? 149.596 132.176 143.272 1.00 125.59 ? 28   A   B "O2'" 1 
ATOM   518   C "C1'" . A   A 1 28   ? 149.828 133.979 144.828 1.00 125.59 ? 28   A   B "C1'" 1 
ATOM   519   N N9    . A   A 1 28   ? 150.145 135.420 144.832 1.00 125.59 ? 28   A   B N9    1 
ATOM   520   C C8    . A   A 1 28   ? 151.069 136.076 145.605 1.00 125.59 ? 28   A   B C8    1 
ATOM   521   N N7    . A   A 1 28   ? 151.124 137.367 145.381 1.00 125.59 ? 28   A   B N7    1 
ATOM   522   C C5    . A   A 1 28   ? 150.172 137.574 144.393 1.00 125.59 ? 28   A   B C5    1 
ATOM   523   C C6    . A   A 1 28   ? 149.742 138.730 143.719 1.00 125.59 ? 28   A   B C6    1 
ATOM   524   N N6    . A   A 1 28   ? 150.239 139.948 143.948 1.00 125.59 ? 28   A   B N6    1 
ATOM   525   N N1    . A   A 1 28   ? 148.773 138.592 142.788 1.00 125.59 ? 28   A   B N1    1 
ATOM   526   C C2    . A   A 1 28   ? 148.274 137.371 142.558 1.00 125.59 ? 28   A   B C2    1 
ATOM   527   N N3    . A   A 1 28   ? 148.595 136.211 143.126 1.00 125.59 ? 28   A   B N3    1 
ATOM   528   C C4    . A   A 1 28   ? 149.561 136.383 144.045 1.00 125.59 ? 28   A   B C4    1 
ATOM   529   N N     . THR B 2 5    ? 113.508 162.454 143.107 1.00 33.57  ? 2    THR A N     1 
ATOM   530   C CA    . THR B 2 5    ? 114.870 161.938 143.062 1.00 33.57  ? 2    THR A CA    1 
ATOM   531   C C     . THR B 2 5    ? 115.803 162.944 142.395 1.00 33.57  ? 2    THR A C     1 
ATOM   532   O O     . THR B 2 5    ? 115.484 163.496 141.343 1.00 33.57  ? 2    THR A O     1 
ATOM   533   C CB    . THR B 2 5    ? 114.941 160.597 142.308 1.00 33.57  ? 2    THR A CB    1 
ATOM   534   O OG1   . THR B 2 5    ? 113.990 159.682 142.867 1.00 33.57  ? 2    THR A OG1   1 
ATOM   535   C CG2   . THR B 2 5    ? 116.333 159.996 142.417 1.00 33.57  ? 2    THR A CG2   1 
ATOM   536   N N     . GLN B 2 6    ? 116.956 163.177 143.014 1.00 31.46  ? 3    GLN A N     1 
ATOM   537   C CA    . GLN B 2 6    ? 117.932 164.136 142.524 1.00 31.46  ? 3    GLN A CA    1 
ATOM   538   C C     . GLN B 2 6    ? 119.295 163.472 142.391 1.00 31.46  ? 3    GLN A C     1 
ATOM   539   O O     . GLN B 2 6    ? 119.636 162.558 143.148 1.00 31.46  ? 3    GLN A O     1 
ATOM   540   C CB    . GLN B 2 6    ? 118.035 165.347 143.458 1.00 31.46  ? 3    GLN A CB    1 
ATOM   541   C CG    . GLN B 2 6    ? 118.224 166.672 142.743 1.00 31.46  ? 3    GLN A CG    1 
ATOM   542   C CD    . GLN B 2 6    ? 118.268 167.845 143.700 1.00 31.46  ? 3    GLN A CD    1 
ATOM   543   O OE1   . GLN B 2 6    ? 117.803 167.751 144.836 1.00 31.46  ? 3    GLN A OE1   1 
ATOM   544   N NE2   . GLN B 2 6    ? 118.831 168.959 143.247 1.00 31.46  ? 3    GLN A NE2   1 
ATOM   545   N N     . PHE B 2 7    ? 120.072 163.937 141.409 1.00 26.59  ? 4    PHE A N     1 
ATOM   546   C CA    . PHE B 2 7    ? 121.416 163.403 141.214 1.00 26.59  ? 4    PHE A CA    1 
ATOM   547   C C     . PHE B 2 7    ? 122.311 163.721 142.404 1.00 26.59  ? 4    PHE A C     1 
ATOM   548   O O     . PHE B 2 7    ? 123.181 162.922 142.768 1.00 26.59  ? 4    PHE A O     1 
ATOM   549   C CB    . PHE B 2 7    ? 122.020 163.956 139.924 1.00 26.59  ? 4    PHE A CB    1 
ATOM   550   C CG    . PHE B 2 7    ? 123.344 163.346 139.565 1.00 26.59  ? 4    PHE A CG    1 
ATOM   551   C CD1   . PHE B 2 7    ? 123.412 162.067 139.041 1.00 26.59  ? 4    PHE A CD1   1 
ATOM   552   C CD2   . PHE B 2 7    ? 124.519 164.051 139.745 1.00 26.59  ? 4    PHE A CD2   1 
ATOM   553   C CE1   . PHE B 2 7    ? 124.627 161.503 138.706 1.00 26.59  ? 4    PHE A CE1   1 
ATOM   554   C CE2   . PHE B 2 7    ? 125.737 163.492 139.412 1.00 26.59  ? 4    PHE A CE2   1 
ATOM   555   C CZ    . PHE B 2 7    ? 125.790 162.217 138.893 1.00 26.59  ? 4    PHE A CZ    1 
ATOM   556   N N     . GLU B 2 8    ? 122.113 164.886 143.023 1.00 25.14  ? 5    GLU A N     1 
ATOM   557   C CA    . GLU B 2 8    ? 122.846 165.231 144.233 1.00 25.14  ? 5    GLU A CA    1 
ATOM   558   C C     . GLU B 2 8    ? 122.427 164.390 145.429 1.00 25.14  ? 5    GLU A C     1 
ATOM   559   O O     . GLU B 2 8    ? 123.095 164.445 146.466 1.00 25.14  ? 5    GLU A O     1 
ATOM   560   C CB    . GLU B 2 8    ? 122.664 166.715 144.554 1.00 25.14  ? 5    GLU A CB    1 
ATOM   561   C CG    . GLU B 2 8    ? 123.691 167.622 143.896 1.00 25.14  ? 5    GLU A CG    1 
ATOM   562   C CD    . GLU B 2 8    ? 123.196 168.217 142.593 1.00 25.14  ? 5    GLU A CD    1 
ATOM   563   O OE1   . GLU B 2 8    ? 122.135 167.776 142.101 1.00 25.14  ? 5    GLU A OE1   1 
ATOM   564   O OE2   . GLU B 2 8    ? 123.866 169.126 142.060 1.00 25.14  ? 5    GLU A OE2   1 
ATOM   565   N N     . GLY B 2 9    ? 121.345 163.626 145.314 1.00 21.67  ? 6    GLY A N     1 
ATOM   566   C CA    . GLY B 2 9    ? 120.888 162.759 146.377 1.00 21.67  ? 6    GLY A CA    1 
ATOM   567   C C     . GLY B 2 9    ? 121.574 161.418 146.458 1.00 21.67  ? 6    GLY A C     1 
ATOM   568   O O     . GLY B 2 9    ? 121.212 160.599 147.307 1.00 21.67  ? 6    GLY A O     1 
ATOM   569   N N     . PHE B 2 10   ? 122.559 161.164 145.599 1.00 21.68  ? 7    PHE A N     1 
ATOM   570   C CA    . PHE B 2 10   ? 123.288 159.896 145.604 1.00 21.68  ? 7    PHE A CA    1 
ATOM   571   C C     . PHE B 2 10   ? 124.504 159.981 146.527 1.00 21.68  ? 7    PHE A C     1 
ATOM   572   O O     . PHE B 2 10   ? 125.657 159.893 146.107 1.00 21.68  ? 7    PHE A O     1 
ATOM   573   C CB    . PHE B 2 10   ? 123.692 159.515 144.186 1.00 21.68  ? 7    PHE A CB    1 
ATOM   574   C CG    . PHE B 2 10   ? 122.647 158.733 143.449 1.00 21.68  ? 7    PHE A CG    1 
ATOM   575   C CD1   . PHE B 2 10   ? 122.609 157.354 143.532 1.00 21.68  ? 7    PHE A CD1   1 
ATOM   576   C CD2   . PHE B 2 10   ? 121.698 159.376 142.678 1.00 21.68  ? 7    PHE A CD2   1 
ATOM   577   C CE1   . PHE B 2 10   ? 121.647 156.633 142.856 1.00 21.68  ? 7    PHE A CE1   1 
ATOM   578   C CE2   . PHE B 2 10   ? 120.735 158.660 142.001 1.00 21.68  ? 7    PHE A CE2   1 
ATOM   579   C CZ    . PHE B 2 10   ? 120.709 157.288 142.091 1.00 21.68  ? 7    PHE A CZ    1 
ATOM   580   N N     . THR B 2 11   ? 124.220 160.153 147.815 1.00 21.90  ? 8    THR A N     1 
ATOM   581   C CA    . THR B 2 11   ? 125.264 160.228 148.825 1.00 21.90  ? 8    THR A CA    1 
ATOM   582   C C     . THR B 2 11   ? 124.745 159.622 150.119 1.00 21.90  ? 8    THR A C     1 
ATOM   583   O O     . THR B 2 11   ? 123.535 159.527 150.342 1.00 21.90  ? 8    THR A O     1 
ATOM   584   C CB    . THR B 2 11   ? 125.722 161.671 149.060 1.00 21.90  ? 8    THR A CB    1 
ATOM   585   O OG1   . THR B 2 11   ? 126.670 161.704 150.134 1.00 21.90  ? 8    THR A OG1   1 
ATOM   586   C CG2   . THR B 2 11   ? 124.538 162.555 149.410 1.00 21.90  ? 8    THR A CG2   1 
ATOM   587   N N     . ASN B 2 12   ? 125.684 159.209 150.972 1.00 21.91  ? 9    ASN A N     1 
ATOM   588   C CA    . ASN B 2 12   ? 125.368 158.640 152.284 1.00 21.91  ? 9    ASN A CA    1 
ATOM   589   C C     . ASN B 2 12   ? 124.448 157.427 152.162 1.00 21.91  ? 9    ASN A C     1 
ATOM   590   O O     . ASN B 2 12   ? 123.427 157.329 152.845 1.00 21.91  ? 9    ASN A O     1 
ATOM   591   C CB    . ASN B 2 12   ? 124.755 159.695 153.207 1.00 21.91  ? 9    ASN A CB    1 
ATOM   592   C CG    . ASN B 2 12   ? 124.880 159.333 154.671 1.00 21.91  ? 9    ASN A CG    1 
ATOM   593   O OD1   . ASN B 2 12   ? 125.593 158.398 155.033 1.00 21.91  ? 9    ASN A OD1   1 
ATOM   594   N ND2   . ASN B 2 12   ? 124.181 160.071 155.524 1.00 21.91  ? 9    ASN A ND2   1 
ATOM   595   N N     . LEU B 2 13   ? 124.811 156.493 151.284 1.00 23.13  ? 10   LEU A N     1 
ATOM   596   C CA    . LEU B 2 13   ? 123.992 155.311 151.049 1.00 23.13  ? 10   LEU A CA    1 
ATOM   597   C C     . LEU B 2 13   ? 124.579 154.038 151.640 1.00 23.13  ? 10   LEU A C     1 
ATOM   598   O O     . LEU B 2 13   ? 123.820 153.185 152.111 1.00 23.13  ? 10   LEU A O     1 
ATOM   599   C CB    . LEU B 2 13   ? 123.765 155.115 149.548 1.00 23.13  ? 10   LEU A CB    1 
ATOM   600   C CG    . LEU B 2 13   ? 123.023 156.272 148.880 1.00 23.13  ? 10   LEU A CG    1 
ATOM   601   C CD1   . LEU B 2 13   ? 122.696 155.952 147.437 1.00 23.13  ? 10   LEU A CD1   1 
ATOM   602   C CD2   . LEU B 2 13   ? 121.760 156.614 149.654 1.00 23.13  ? 10   LEU A CD2   1 
ATOM   603   N N     . TYR B 2 14   ? 125.900 153.883 151.629 1.00 23.63  ? 11   TYR A N     1 
ATOM   604   C CA    . TYR B 2 14   ? 126.523 152.746 152.289 1.00 23.63  ? 11   TYR A CA    1 
ATOM   605   C C     . TYR B 2 14   ? 127.902 153.155 152.780 1.00 23.63  ? 11   TYR A C     1 
ATOM   606   O O     . TYR B 2 14   ? 128.549 154.037 152.211 1.00 23.63  ? 11   TYR A O     1 
ATOM   607   C CB    . TYR B 2 14   ? 126.610 151.526 151.365 1.00 23.63  ? 11   TYR A CB    1 
ATOM   608   C CG    . TYR B 2 14   ? 127.382 151.756 150.088 1.00 23.63  ? 11   TYR A CG    1 
ATOM   609   C CD1   . TYR B 2 14   ? 128.747 151.515 150.024 1.00 23.63  ? 11   TYR A CD1   1 
ATOM   610   C CD2   . TYR B 2 14   ? 126.742 152.202 148.941 1.00 23.63  ? 11   TYR A CD2   1 
ATOM   611   C CE1   . TYR B 2 14   ? 129.453 151.720 148.859 1.00 23.63  ? 11   TYR A CE1   1 
ATOM   612   C CE2   . TYR B 2 14   ? 127.441 152.410 147.771 1.00 23.63  ? 11   TYR A CE2   1 
ATOM   613   C CZ    . TYR B 2 14   ? 128.795 152.168 147.736 1.00 23.63  ? 11   TYR A CZ    1 
ATOM   614   O OH    . TYR B 2 14   ? 129.492 152.374 146.570 1.00 23.63  ? 11   TYR A OH    1 
ATOM   615   N N     . GLN B 2 15   ? 128.339 152.501 153.852 1.00 23.40  ? 12   GLN A N     1 
ATOM   616   C CA    . GLN B 2 15   ? 129.649 152.781 154.418 1.00 23.40  ? 12   GLN A CA    1 
ATOM   617   C C     . GLN B 2 15   ? 130.752 152.296 153.487 1.00 23.40  ? 12   GLN A C     1 
ATOM   618   O O     . GLN B 2 15   ? 130.660 151.219 152.893 1.00 23.40  ? 12   GLN A O     1 
ATOM   619   C CB    . GLN B 2 15   ? 129.796 152.113 155.784 1.00 23.40  ? 12   GLN A CB    1 
ATOM   620   C CG    . GLN B 2 15   ? 128.981 152.755 156.887 1.00 23.40  ? 12   GLN A CG    1 
ATOM   621   C CD    . GLN B 2 15   ? 129.328 152.208 158.255 1.00 23.40  ? 12   GLN A CD    1 
ATOM   622   O OE1   . GLN B 2 15   ? 129.273 152.923 159.255 1.00 23.40  ? 12   GLN A OE1   1 
ATOM   623   N NE2   . GLN B 2 15   ? 129.692 150.933 158.307 1.00 23.40  ? 12   GLN A NE2   1 
ATOM   624   N N     . VAL B 2 16   ? 131.801 153.102 153.363 1.00 22.27  ? 13   VAL A N     1 
ATOM   625   C CA    . VAL B 2 16   ? 132.993 152.738 152.612 1.00 22.27  ? 13   VAL A CA    1 
ATOM   626   C C     . VAL B 2 16   ? 134.205 152.934 153.512 1.00 22.27  ? 13   VAL A C     1 
ATOM   627   O O     . VAL B 2 16   ? 134.324 153.954 154.202 1.00 22.27  ? 13   VAL A O     1 
ATOM   628   C CB    . VAL B 2 16   ? 133.118 153.543 151.299 1.00 22.27  ? 13   VAL A CB    1 
ATOM   629   C CG1   . VAL B 2 16   ? 133.312 155.023 151.571 1.00 22.27  ? 13   VAL A CG1   1 
ATOM   630   C CG2   . VAL B 2 16   ? 134.259 153.002 150.452 1.00 22.27  ? 13   VAL A CG2   1 
ATOM   631   N N     . SER B 2 17   ? 135.082 151.938 153.539 1.00 23.82  ? 14   SER A N     1 
ATOM   632   C CA    . SER B 2 17   ? 136.252 151.950 154.402 1.00 23.82  ? 14   SER A CA    1 
ATOM   633   C C     . SER B 2 17   ? 137.510 152.166 153.574 1.00 23.82  ? 14   SER A C     1 
ATOM   634   O O     . SER B 2 17   ? 137.772 151.430 152.618 1.00 23.82  ? 14   SER A O     1 
ATOM   635   C CB    . SER B 2 17   ? 136.366 150.646 155.194 1.00 23.82  ? 14   SER A CB    1 
ATOM   636   O OG    . SER B 2 17   ? 137.523 150.645 156.011 1.00 23.82  ? 14   SER A OG    1 
ATOM   637   N N     . LYS B 2 18   ? 138.279 153.183 153.947 1.00 24.38  ? 15   LYS A N     1 
ATOM   638   C CA    . LYS B 2 18   ? 139.561 153.476 153.330 1.00 24.38  ? 15   LYS A CA    1 
ATOM   639   C C     . LYS B 2 18   ? 140.604 153.626 154.426 1.00 24.38  ? 15   LYS A C     1 
ATOM   640   O O     . LYS B 2 18   ? 140.331 154.190 155.487 1.00 24.38  ? 15   LYS A O     1 
ATOM   641   C CB    . LYS B 2 18   ? 139.507 154.758 152.487 1.00 24.38  ? 15   LYS A CB    1 
ATOM   642   C CG    . LYS B 2 18   ? 138.495 154.728 151.357 1.00 24.38  ? 15   LYS A CG    1 
ATOM   643   C CD    . LYS B 2 18   ? 138.871 155.711 150.262 1.00 24.38  ? 15   LYS A CD    1 
ATOM   644   C CE    . LYS B 2 18   ? 137.981 155.548 149.043 1.00 24.38  ? 15   LYS A CE    1 
ATOM   645   N NZ    . LYS B 2 18   ? 138.421 154.420 148.179 1.00 24.38  ? 15   LYS A NZ    1 
ATOM   646   N N     . THR B 2 19   ? 141.801 153.117 154.169 1.00 24.16  ? 16   THR A N     1 
ATOM   647   C CA    . THR B 2 19   ? 142.900 153.222 155.123 1.00 24.16  ? 16   THR A CA    1 
ATOM   648   C C     . THR B 2 19   ? 143.944 154.182 154.560 1.00 24.16  ? 16   THR A C     1 
ATOM   649   O O     . THR B 2 19   ? 144.520 153.949 153.494 1.00 24.16  ? 16   THR A O     1 
ATOM   650   C CB    . THR B 2 19   ? 143.478 151.846 155.455 1.00 24.16  ? 16   THR A CB    1 
ATOM   651   O OG1   . THR B 2 19   ? 144.529 151.980 156.420 1.00 24.16  ? 16   THR A OG1   1 
ATOM   652   C CG2   . THR B 2 19   ? 143.988 151.142 154.224 1.00 24.16  ? 16   THR A CG2   1 
ATOM   653   N N     . LEU B 2 20   ? 144.147 155.291 155.263 1.00 26.40  ? 17   LEU A N     1 
ATOM   654   C CA    . LEU B 2 20   ? 145.152 156.259 154.859 1.00 26.40  ? 17   LEU A CA    1 
ATOM   655   C C     . LEU B 2 20   ? 146.525 155.836 155.366 1.00 26.40  ? 17   LEU A C     1 
ATOM   656   O O     . LEU B 2 20   ? 146.656 155.183 156.405 1.00 26.40  ? 17   LEU A O     1 
ATOM   657   C CB    . LEU B 2 20   ? 144.800 157.646 155.394 1.00 26.40  ? 17   LEU A CB    1 
ATOM   658   C CG    . LEU B 2 20   ? 143.327 158.061 155.379 1.00 26.40  ? 17   LEU A CG    1 
ATOM   659   C CD1   . LEU B 2 20   ? 143.169 159.465 155.938 1.00 26.40  ? 17   LEU A CD1   1 
ATOM   660   C CD2   . LEU B 2 20   ? 142.744 157.976 153.979 1.00 26.40  ? 17   LEU A CD2   1 
ATOM   661   N N     . ARG B 2 21   ? 147.557 156.214 154.620 1.00 32.85  ? 18   ARG A N     1 
ATOM   662   C CA    . ARG B 2 21   ? 148.932 155.916 154.985 1.00 32.85  ? 18   ARG A CA    1 
ATOM   663   C C     . ARG B 2 21   ? 149.726 157.211 155.049 1.00 32.85  ? 18   ARG A C     1 
ATOM   664   O O     . ARG B 2 21   ? 149.561 158.093 154.201 1.00 32.85  ? 18   ARG A O     1 
ATOM   665   C CB    . ARG B 2 21   ? 149.575 154.947 153.989 1.00 32.85  ? 18   ARG A CB    1 
ATOM   666   C CG    . ARG B 2 21   ? 148.733 153.718 153.694 1.00 32.85  ? 18   ARG A CG    1 
ATOM   667   C CD    . ARG B 2 21   ? 148.933 153.233 152.270 1.00 32.85  ? 18   ARG A CD    1 
ATOM   668   N NE    . ARG B 2 21   ? 150.336 152.976 151.968 1.00 32.85  ? 18   ARG A NE    1 
ATOM   669   C CZ    . ARG B 2 21   ? 150.808 152.755 150.750 1.00 32.85  ? 18   ARG A CZ    1 
ATOM   670   N NH1   . ARG B 2 21   ? 150.015 152.755 149.691 1.00 32.85  ? 18   ARG A NH1   1 
ATOM   671   N NH2   . ARG B 2 21   ? 152.109 152.529 150.590 1.00 32.85  ? 18   ARG A NH2   1 
ATOM   672   N N     . PHE B 2 22   ? 150.579 157.325 156.064 1.00 30.73  ? 19   PHE A N     1 
ATOM   673   C CA    . PHE B 2 22   ? 151.383 158.518 156.274 1.00 30.73  ? 19   PHE A CA    1 
ATOM   674   C C     . PHE B 2 22   ? 152.784 158.108 156.700 1.00 30.73  ? 19   PHE A C     1 
ATOM   675   O O     . PHE B 2 22   ? 153.040 156.951 157.045 1.00 30.73  ? 19   PHE A O     1 
ATOM   676   C CB    . PHE B 2 22   ? 150.766 159.443 157.329 1.00 30.73  ? 19   PHE A CB    1 
ATOM   677   C CG    . PHE B 2 22   ? 149.351 159.843 157.036 1.00 30.73  ? 19   PHE A CG    1 
ATOM   678   C CD1   . PHE B 2 22   ? 149.077 160.895 156.181 1.00 30.73  ? 19   PHE A CD1   1 
ATOM   679   C CD2   . PHE B 2 22   ? 148.295 159.178 157.630 1.00 30.73  ? 19   PHE A CD2   1 
ATOM   680   C CE1   . PHE B 2 22   ? 147.778 161.268 155.916 1.00 30.73  ? 19   PHE A CE1   1 
ATOM   681   C CE2   . PHE B 2 22   ? 146.993 159.547 157.369 1.00 30.73  ? 19   PHE A CE2   1 
ATOM   682   C CZ    . PHE B 2 22   ? 146.734 160.593 156.509 1.00 30.73  ? 19   PHE A CZ    1 
ATOM   683   N N     . GLU B 2 23   ? 153.694 159.074 156.675 1.00 35.76  ? 20   GLU A N     1 
ATOM   684   C CA    . GLU B 2 23   ? 155.061 158.874 157.131 1.00 35.76  ? 20   GLU A CA    1 
ATOM   685   C C     . GLU B 2 23   ? 155.248 159.537 158.487 1.00 35.76  ? 20   GLU A C     1 
ATOM   686   O O     . GLU B 2 23   ? 154.827 160.679 158.696 1.00 35.76  ? 20   GLU A O     1 
ATOM   687   C CB    . GLU B 2 23   ? 156.068 159.444 156.132 1.00 35.76  ? 20   GLU A CB    1 
ATOM   688   C CG    . GLU B 2 23   ? 157.490 159.489 156.657 1.00 35.76  ? 20   GLU A CG    1 
ATOM   689   C CD    . GLU B 2 23   ? 158.426 160.252 155.746 1.00 35.76  ? 20   GLU A CD    1 
ATOM   690   O OE1   . GLU B 2 23   ? 158.791 159.714 154.680 1.00 35.76  ? 20   GLU A OE1   1 
ATOM   691   O OE2   . GLU B 2 23   ? 158.800 161.390 156.097 1.00 35.76  ? 20   GLU A OE2   1 
ATOM   692   N N     . LEU B 2 24   ? 155.880 158.816 159.405 1.00 32.23  ? 21   LEU A N     1 
ATOM   693   C CA    . LEU B 2 24   ? 156.125 159.307 160.752 1.00 32.23  ? 21   LEU A CA    1 
ATOM   694   C C     . LEU B 2 24   ? 157.557 159.810 160.857 1.00 32.23  ? 21   LEU A C     1 
ATOM   695   O O     . LEU B 2 24   ? 158.504 159.067 160.581 1.00 32.23  ? 21   LEU A O     1 
ATOM   696   C CB    . LEU B 2 24   ? 155.872 158.209 161.783 1.00 32.23  ? 21   LEU A CB    1 
ATOM   697   C CG    . LEU B 2 24   ? 154.470 157.604 161.783 1.00 32.23  ? 21   LEU A CG    1 
ATOM   698   C CD1   . LEU B 2 24   ? 154.405 156.435 162.744 1.00 32.23  ? 21   LEU A CD1   1 
ATOM   699   C CD2   . LEU B 2 24   ? 153.438 158.656 162.145 1.00 32.23  ? 21   LEU A CD2   1 
ATOM   700   N N     . ILE B 2 25   ? 157.708 161.068 161.253 1.00 28.35  ? 22   ILE A N     1 
ATOM   701   C CA    . ILE B 2 25   ? 159.006 161.702 161.445 1.00 28.35  ? 22   ILE A CA    1 
ATOM   702   C C     . ILE B 2 25   ? 159.252 161.804 162.948 1.00 28.35  ? 22   ILE A C     1 
ATOM   703   O O     . ILE B 2 25   ? 158.459 162.436 163.661 1.00 28.35  ? 22   ILE A O     1 
ATOM   704   C CB    . ILE B 2 25   ? 159.071 163.080 160.777 1.00 28.35  ? 22   ILE A CB    1 
ATOM   705   C CG1   . ILE B 2 25   ? 158.822 162.957 159.275 1.00 28.35  ? 22   ILE A CG1   1 
ATOM   706   C CG2   . ILE B 2 25   ? 160.414 163.739 161.048 1.00 28.35  ? 22   ILE A CG2   1 
ATOM   707   C CD1   . ILE B 2 25   ? 158.948 164.263 158.533 1.00 28.35  ? 22   ILE A CD1   1 
ATOM   708   N N     . PRO B 2 26   ? 160.310 161.190 163.475 1.00 25.49  ? 23   PRO A N     1 
ATOM   709   C CA    . PRO B 2 26   ? 160.587 161.310 164.910 1.00 25.49  ? 23   PRO A CA    1 
ATOM   710   C C     . PRO B 2 26   ? 160.793 162.763 165.312 1.00 25.49  ? 23   PRO A C     1 
ATOM   711   O O     . PRO B 2 26   ? 161.426 163.542 164.597 1.00 25.49  ? 23   PRO A O     1 
ATOM   712   C CB    . PRO B 2 26   ? 161.867 160.486 165.096 1.00 25.49  ? 23   PRO A CB    1 
ATOM   713   C CG    . PRO B 2 26   ? 162.458 160.363 163.731 1.00 25.49  ? 23   PRO A CG    1 
ATOM   714   C CD    . PRO B 2 26   ? 161.308 160.364 162.780 1.00 25.49  ? 23   PRO A CD    1 
ATOM   715   N N     . GLN B 2 27   ? 160.250 163.121 166.471 1.00 28.66  ? 24   GLN A N     1 
ATOM   716   C CA    . GLN B 2 27   ? 160.299 164.483 166.979 1.00 28.66  ? 24   GLN A CA    1 
ATOM   717   C C     . GLN B 2 27   ? 161.151 164.539 168.237 1.00 28.66  ? 24   GLN A C     1 
ATOM   718   O O     . GLN B 2 27   ? 161.065 163.658 169.097 1.00 28.66  ? 24   GLN A O     1 
ATOM   719   C CB    . GLN B 2 27   ? 158.894 165.011 167.274 1.00 28.66  ? 24   GLN A CB    1 
ATOM   720   C CG    . GLN B 2 27   ? 158.158 165.511 166.049 1.00 28.66  ? 24   GLN A CG    1 
ATOM   721   C CD    . GLN B 2 27   ? 158.959 166.532 165.269 1.00 28.66  ? 24   GLN A CD    1 
ATOM   722   O OE1   . GLN B 2 27   ? 159.445 166.251 164.174 1.00 28.66  ? 24   GLN A OE1   1 
ATOM   723   N NE2   . GLN B 2 27   ? 159.102 167.727 165.830 1.00 28.66  ? 24   GLN A NE2   1 
ATOM   724   N N     . GLY B 2 28   ? 161.967 165.583 168.343 1.00 36.00  ? 25   GLY A N     1 
ATOM   725   C CA    . GLY B 2 28   ? 162.859 165.721 169.474 1.00 36.00  ? 25   GLY A CA    1 
ATOM   726   C C     . GLY B 2 28   ? 163.928 164.651 169.481 1.00 36.00  ? 25   GLY A C     1 
ATOM   727   O O     . GLY B 2 28   ? 164.757 164.588 168.570 1.00 36.00  ? 25   GLY A O     1 
ATOM   728   N N     . LYS B 2 29   ? 163.918 163.801 170.507 1.00 44.73  ? 26   LYS A N     1 
ATOM   729   C CA    . LYS B 2 29   ? 164.863 162.696 170.605 1.00 44.73  ? 26   LYS A CA    1 
ATOM   730   C C     . LYS B 2 29   ? 164.162 161.356 170.783 1.00 44.73  ? 26   LYS A C     1 
ATOM   731   O O     . LYS B 2 29   ? 164.725 160.442 171.394 1.00 44.73  ? 26   LYS A O     1 
ATOM   732   C CB    . LYS B 2 29   ? 165.851 162.933 171.747 1.00 32.45  ? 26   LYS A CB    1 
ATOM   733   C CG    . LYS B 2 29   ? 165.199 163.200 173.084 1.00 32.45  ? 26   LYS A CG    1 
ATOM   734   C CD    . LYS B 2 29   ? 166.149 163.941 174.000 1.00 32.45  ? 26   LYS A CD    1 
ATOM   735   C CE    . LYS B 2 29   ? 167.168 162.996 174.616 1.00 32.45  ? 26   LYS A CE    1 
ATOM   736   N NZ    . LYS B 2 29   ? 167.734 163.541 175.881 1.00 32.45  ? 26   LYS A NZ    1 
ATOM   737   N N     . THR B 2 30   ? 162.940 161.217 170.264 1.00 44.73  ? 27   THR A N     1 
ATOM   738   C CA    . THR B 2 30   ? 162.258 159.932 170.344 1.00 44.73  ? 27   THR A CA    1 
ATOM   739   C C     . THR B 2 30   ? 162.960 158.873 169.505 1.00 44.73  ? 27   THR A C     1 
ATOM   740   O O     . THR B 2 30   ? 162.854 157.678 169.806 1.00 44.73  ? 27   THR A O     1 
ATOM   741   C CB    . THR B 2 30   ? 160.800 160.072 169.912 1.00 44.73  ? 27   THR A CB    1 
ATOM   742   O OG1   . THR B 2 30   ? 160.147 158.803 170.028 1.00 44.73  ? 27   THR A OG1   1 
ATOM   743   C CG2   . THR B 2 30   ? 160.710 160.544 168.482 1.00 44.73  ? 27   THR A CG2   1 
ATOM   744   N N     . LEU B 2 31   ? 163.672 159.282 168.453 1.00 44.73  ? 28   LEU A N     1 
ATOM   745   C CA    . LEU B 2 31   ? 164.465 158.326 167.690 1.00 44.73  ? 28   LEU A CA    1 
ATOM   746   C C     . LEU B 2 31   ? 165.624 157.795 168.523 1.00 44.73  ? 28   LEU A C     1 
ATOM   747   O O     . LEU B 2 31   ? 165.968 156.610 168.439 1.00 44.73  ? 28   LEU A O     1 
ATOM   748   C CB    . LEU B 2 31   ? 164.975 158.974 166.403 1.00 44.73  ? 28   LEU A CB    1 
ATOM   749   C CG    . LEU B 2 31   ? 165.775 158.078 165.458 1.00 44.73  ? 28   LEU A CG    1 
ATOM   750   C CD1   . LEU B 2 31   ? 164.974 156.842 165.090 1.00 44.73  ? 28   LEU A CD1   1 
ATOM   751   C CD2   . LEU B 2 31   ? 166.183 158.844 164.213 1.00 44.73  ? 28   LEU A CD2   1 
ATOM   752   N N     . LYS B 2 32   ? 166.241 158.661 169.329 1.00 44.73  ? 29   LYS A N     1 
ATOM   753   C CA    . LYS B 2 32   ? 167.340 158.228 170.185 1.00 44.73  ? 29   LYS A CA    1 
ATOM   754   C C     . LYS B 2 32   ? 166.862 157.235 171.237 1.00 44.73  ? 29   LYS A C     1 
ATOM   755   O O     . LYS B 2 32   ? 167.551 156.251 171.530 1.00 44.73  ? 29   LYS A O     1 
ATOM   756   C CB    . LYS B 2 32   ? 167.994 159.443 170.843 1.00 44.73  ? 29   LYS A CB    1 
ATOM   757   C CG    . LYS B 2 32   ? 169.439 159.230 171.255 1.00 44.73  ? 29   LYS A CG    1 
ATOM   758   C CD    . LYS B 2 32   ? 169.548 158.902 172.734 1.00 44.73  ? 29   LYS A CD    1 
ATOM   759   C CE    . LYS B 2 32   ? 170.882 158.252 173.059 1.00 44.73  ? 29   LYS A CE    1 
ATOM   760   N NZ    . LYS B 2 32   ? 171.073 158.085 174.526 1.00 44.73  ? 29   LYS A NZ    1 
ATOM   761   N N     . HIS B 2 33   ? 165.688 157.481 171.823 1.00 44.73  ? 30   HIS A N     1 
ATOM   762   C CA    . HIS B 2 33   ? 165.152 156.564 172.823 1.00 44.73  ? 30   HIS A CA    1 
ATOM   763   C C     . HIS B 2 33   ? 164.819 155.209 172.210 1.00 44.73  ? 30   HIS A C     1 
ATOM   764   O O     . HIS B 2 33   ? 165.049 154.165 172.832 1.00 44.73  ? 30   HIS A O     1 
ATOM   765   C CB    . HIS B 2 33   ? 163.916 157.171 173.484 1.00 44.73  ? 30   HIS A CB    1 
ATOM   766   C CG    . HIS B 2 33   ? 164.231 158.205 174.519 1.00 44.73  ? 30   HIS A CG    1 
ATOM   767   N ND1   . HIS B 2 33   ? 164.873 157.905 175.701 1.00 44.73  ? 30   HIS A ND1   1 
ATOM   768   C CD2   . HIS B 2 33   ? 163.984 159.536 174.553 1.00 44.73  ? 30   HIS A CD2   1 
ATOM   769   C CE1   . HIS B 2 33   ? 165.013 159.007 176.416 1.00 44.73  ? 30   HIS A CE1   1 
ATOM   770   N NE2   . HIS B 2 33   ? 164.481 160.010 175.742 1.00 44.73  ? 30   HIS A NE2   1 
ATOM   771   N N     . ILE B 2 34   ? 164.266 155.206 170.995 1.00 44.73  ? 31   ILE A N     1 
ATOM   772   C CA    . ILE B 2 34   ? 163.933 153.949 170.329 1.00 44.73  ? 31   ILE A CA    1 
ATOM   773   C C     . ILE B 2 34   ? 165.194 153.138 170.060 1.00 44.73  ? 31   ILE A C     1 
ATOM   774   O O     . ILE B 2 34   ? 165.234 151.926 170.305 1.00 44.73  ? 31   ILE A O     1 
ATOM   775   C CB    . ILE B 2 34   ? 163.148 154.224 169.033 1.00 44.73  ? 31   ILE A CB    1 
ATOM   776   C CG1   . ILE B 2 34   ? 161.689 154.543 169.352 1.00 44.73  ? 31   ILE A CG1   1 
ATOM   777   C CG2   . ILE B 2 34   ? 163.235 153.039 168.087 1.00 44.73  ? 31   ILE A CG2   1 
ATOM   778   C CD1   . ILE B 2 34   ? 160.888 154.972 168.151 1.00 44.73  ? 31   ILE A CD1   1 
ATOM   779   N N     . GLN B 2 35   ? 166.243 153.792 169.558 1.00 44.73  ? 32   GLN A N     1 
ATOM   780   C CA    . GLN B 2 35   ? 167.492 153.088 169.286 1.00 44.73  ? 32   GLN A CA    1 
ATOM   781   C C     . GLN B 2 35   ? 168.110 152.541 170.566 1.00 44.73  ? 32   GLN A C     1 
ATOM   782   O O     . GLN B 2 35   ? 168.638 151.423 170.581 1.00 44.73  ? 32   GLN A O     1 
ATOM   783   C CB    . GLN B 2 35   ? 168.474 154.015 168.572 1.00 44.73  ? 32   GLN A CB    1 
ATOM   784   C CG    . GLN B 2 35   ? 168.313 154.048 167.063 1.00 44.73  ? 32   GLN A CG    1 
ATOM   785   C CD    . GLN B 2 35   ? 169.271 155.017 166.399 1.00 44.73  ? 32   GLN A CD    1 
ATOM   786   O OE1   . GLN B 2 35   ? 169.954 155.790 167.069 1.00 44.73  ? 32   GLN A OE1   1 
ATOM   787   N NE2   . GLN B 2 35   ? 169.326 154.978 165.073 1.00 44.73  ? 32   GLN A NE2   1 
ATOM   788   N N     . GLU B 2 36   ? 168.064 153.320 171.650 1.00 44.73  ? 33   GLU A N     1 
ATOM   789   C CA    . GLU B 2 36   ? 168.634 152.863 172.914 1.00 44.73  ? 33   GLU A CA    1 
ATOM   790   C C     . GLU B 2 36   ? 167.910 151.627 173.431 1.00 44.73  ? 33   GLU A C     1 
ATOM   791   O O     . GLU B 2 36   ? 168.546 150.675 173.898 1.00 44.73  ? 33   GLU A O     1 
ATOM   792   C CB    . GLU B 2 36   ? 168.585 153.990 173.947 1.00 44.73  ? 33   GLU A CB    1 
ATOM   793   C CG    . GLU B 2 36   ? 168.482 153.518 175.388 1.00 44.73  ? 33   GLU A CG    1 
ATOM   794   C CD    . GLU B 2 36   ? 168.374 154.668 176.371 1.00 44.73  ? 33   GLU A CD    1 
ATOM   795   O OE1   . GLU B 2 36   ? 168.575 155.828 175.955 1.00 44.73  ? 33   GLU A OE1   1 
ATOM   796   O OE2   . GLU B 2 36   ? 168.089 154.411 177.560 1.00 44.73  ? 33   GLU A OE2   1 
ATOM   797   N N     . GLN B 2 37   ? 166.579 151.617 173.348 1.00 44.73  ? 34   GLN A N     1 
ATOM   798   C CA    . GLN B 2 37   ? 165.810 150.451 173.764 1.00 44.73  ? 34   GLN A CA    1 
ATOM   799   C C     . GLN B 2 37   ? 165.832 149.332 172.732 1.00 44.73  ? 34   GLN A C     1 
ATOM   800   O O     . GLN B 2 37   ? 165.458 148.203 173.064 1.00 44.73  ? 34   GLN A O     1 
ATOM   801   C CB    . GLN B 2 37   ? 164.365 150.852 174.055 1.00 44.73  ? 34   GLN A CB    1 
ATOM   802   C CG    . GLN B 2 37   ? 164.216 151.938 175.104 1.00 44.73  ? 34   GLN A CG    1 
ATOM   803   C CD    . GLN B 2 37   ? 163.934 151.377 176.482 1.00 44.73  ? 34   GLN A CD    1 
ATOM   804   O OE1   . GLN B 2 37   ? 163.842 150.163 176.663 1.00 44.73  ? 34   GLN A OE1   1 
ATOM   805   N NE2   . GLN B 2 37   ? 163.793 152.261 177.463 1.00 44.73  ? 34   GLN A NE2   1 
ATOM   806   N N     . GLY B 2 38   ? 166.257 149.613 171.504 1.00 44.73  ? 35   GLY A N     1 
ATOM   807   C CA    . GLY B 2 38   ? 166.331 148.580 170.482 1.00 44.73  ? 35   GLY A CA    1 
ATOM   808   C C     . GLY B 2 38   ? 164.989 148.028 170.054 1.00 44.73  ? 35   GLY A C     1 
ATOM   809   O O     . GLY B 2 38   ? 164.842 146.809 169.905 1.00 44.73  ? 35   GLY A O     1 
ATOM   810   N N     . PHE B 2 39   ? 164.000 148.901 169.853 1.00 44.73  ? 36   PHE A N     1 
ATOM   811   C CA    . PHE B 2 39   ? 162.687 148.437 169.417 1.00 44.73  ? 36   PHE A CA    1 
ATOM   812   C C     . PHE B 2 39   ? 162.709 147.980 167.964 1.00 44.73  ? 36   PHE A C     1 
ATOM   813   O O     . PHE B 2 39   ? 162.139 146.935 167.629 1.00 44.73  ? 36   PHE A O     1 
ATOM   814   C CB    . PHE B 2 39   ? 161.650 149.542 169.606 1.00 44.73  ? 36   PHE A CB    1 
ATOM   815   C CG    . PHE B 2 39   ? 161.197 149.714 171.024 1.00 44.73  ? 36   PHE A CG    1 
ATOM   816   C CD1   . PHE B 2 39   ? 160.460 148.727 171.653 1.00 44.73  ? 36   PHE A CD1   1 
ATOM   817   C CD2   . PHE B 2 39   ? 161.500 150.866 171.725 1.00 44.73  ? 36   PHE A CD2   1 
ATOM   818   C CE1   . PHE B 2 39   ? 160.038 148.886 172.956 1.00 44.73  ? 36   PHE A CE1   1 
ATOM   819   C CE2   . PHE B 2 39   ? 161.077 151.031 173.028 1.00 44.73  ? 36   PHE A CE2   1 
ATOM   820   C CZ    . PHE B 2 39   ? 160.348 150.039 173.645 1.00 44.73  ? 36   PHE A CZ    1 
ATOM   821   N N     . ILE B 2 40   ? 163.351 148.753 167.086 1.00 44.73  ? 37   ILE A N     1 
ATOM   822   C CA    . ILE B 2 40   ? 163.363 148.413 165.665 1.00 44.73  ? 37   ILE A CA    1 
ATOM   823   C C     . ILE B 2 40   ? 164.135 147.122 165.426 1.00 44.73  ? 37   ILE A C     1 
ATOM   824   O O     . ILE B 2 40   ? 163.711 146.266 164.639 1.00 44.73  ? 37   ILE A O     1 
ATOM   825   C CB    . ILE B 2 40   ? 163.934 149.580 164.839 1.00 44.73  ? 37   ILE A CB    1 
ATOM   826   C CG1   . ILE B 2 40   ? 165.226 150.107 165.466 1.00 44.73  ? 37   ILE A CG1   1 
ATOM   827   C CG2   . ILE B 2 40   ? 162.909 150.694 164.715 1.00 44.73  ? 37   ILE A CG2   1 
ATOM   828   C CD1   . ILE B 2 40   ? 165.994 151.055 164.573 1.00 44.73  ? 37   ILE A CD1   1 
ATOM   829   N N     . GLU B 2 41   ? 165.283 146.963 166.089 1.00 44.73  ? 38   GLU A N     1 
ATOM   830   C CA    . GLU B 2 41   ? 166.065 145.740 165.929 1.00 44.73  ? 38   GLU A CA    1 
ATOM   831   C C     . GLU B 2 41   ? 165.299 144.528 166.439 1.00 44.73  ? 38   GLU A C     1 
ATOM   832   O O     . GLU B 2 41   ? 165.330 143.458 165.819 1.00 44.73  ? 38   GLU A O     1 
ATOM   833   C CB    . GLU B 2 41   ? 167.403 145.873 166.654 1.00 44.73  ? 38   GLU A CB    1 
ATOM   834   C CG    . GLU B 2 41   ? 168.212 147.090 166.247 1.00 44.73  ? 38   GLU A CG    1 
ATOM   835   C CD    . GLU B 2 41   ? 169.331 147.396 167.220 1.00 44.73  ? 38   GLU A CD    1 
ATOM   836   O OE1   . GLU B 2 41   ? 169.613 146.545 168.090 1.00 44.73  ? 38   GLU A OE1   1 
ATOM   837   O OE2   . GLU B 2 41   ? 169.930 148.487 167.117 1.00 44.73  ? 38   GLU A OE2   1 
ATOM   838   N N     . GLU B 2 42   ? 164.610 144.672 167.574 1.00 44.73  ? 39   GLU A N     1 
ATOM   839   C CA    . GLU B 2 42   ? 163.830 143.563 168.111 1.00 44.73  ? 39   GLU A CA    1 
ATOM   840   C C     . GLU B 2 42   ? 162.687 143.190 167.177 1.00 44.73  ? 39   GLU A C     1 
ATOM   841   O O     . GLU B 2 42   ? 162.405 142.004 166.972 1.00 44.73  ? 39   GLU A O     1 
ATOM   842   C CB    . GLU B 2 42   ? 163.296 143.919 169.498 1.00 44.73  ? 39   GLU A CB    1 
ATOM   843   C CG    . GLU B 2 42   ? 162.705 142.743 170.251 1.00 44.73  ? 39   GLU A CG    1 
ATOM   844   C CD    . GLU B 2 42   ? 161.510 143.136 171.096 1.00 44.73  ? 39   GLU A CD    1 
ATOM   845   O OE1   . GLU B 2 42   ? 161.263 144.350 171.248 1.00 44.73  ? 39   GLU A OE1   1 
ATOM   846   O OE2   . GLU B 2 42   ? 160.819 142.230 171.608 1.00 44.73  ? 39   GLU A OE2   1 
ATOM   847   N N     . ASP B 2 43   ? 162.015 144.190 166.602 1.00 44.73  ? 40   ASP A N     1 
ATOM   848   C CA    . ASP B 2 43   ? 160.940 143.904 165.660 1.00 44.73  ? 40   ASP A CA    1 
ATOM   849   C C     . ASP B 2 43   ? 161.479 143.372 164.341 1.00 44.73  ? 40   ASP A C     1 
ATOM   850   O O     . ASP B 2 43   ? 160.804 142.581 163.672 1.00 44.73  ? 40   ASP A O     1 
ATOM   851   C CB    . ASP B 2 43   ? 160.098 145.157 165.428 1.00 44.73  ? 40   ASP A CB    1 
ATOM   852   C CG    . ASP B 2 43   ? 159.289 145.547 166.649 1.00 44.73  ? 40   ASP A CG    1 
ATOM   853   O OD1   . ASP B 2 43   ? 158.926 144.647 167.434 1.00 44.73  ? 40   ASP A OD1   1 
ATOM   854   O OD2   . ASP B 2 43   ? 159.018 146.754 166.825 1.00 44.73  ? 40   ASP A OD2   1 
ATOM   855   N N     . LYS B 2 44   ? 162.683 143.794 163.947 1.00 44.73  ? 41   LYS A N     1 
ATOM   856   C CA    . LYS B 2 44   ? 163.313 143.217 162.764 1.00 44.73  ? 41   LYS A CA    1 
ATOM   857   C C     . LYS B 2 44   ? 163.616 141.741 162.976 1.00 44.73  ? 41   LYS A C     1 
ATOM   858   O O     . LYS B 2 44   ? 163.436 140.924 162.066 1.00 44.73  ? 41   LYS A O     1 
ATOM   859   C CB    . LYS B 2 44   ? 164.588 143.984 162.416 1.00 44.73  ? 41   LYS A CB    1 
ATOM   860   C CG    . LYS B 2 44   ? 165.291 143.474 161.171 1.00 44.73  ? 41   LYS A CG    1 
ATOM   861   C CD    . LYS B 2 44   ? 166.464 144.362 160.796 1.00 44.73  ? 41   LYS A CD    1 
ATOM   862   C CE    . LYS B 2 44   ? 167.614 144.198 161.776 1.00 44.73  ? 41   LYS A CE    1 
ATOM   863   N NZ    . LYS B 2 44   ? 168.241 142.851 161.674 1.00 44.73  ? 41   LYS A NZ    1 
ATOM   864   N N     . ALA B 2 45   ? 164.084 141.382 164.174 1.00 45.83  ? 42   ALA A N     1 
ATOM   865   C CA    . ALA B 2 45   ? 164.302 139.975 164.492 1.00 45.83  ? 42   ALA A CA    1 
ATOM   866   C C     . ALA B 2 45   ? 162.990 139.204 164.492 1.00 45.83  ? 42   ALA A C     1 
ATOM   867   O O     . ALA B 2 45   ? 162.940 138.049 164.052 1.00 45.83  ? 42   ALA A O     1 
ATOM   868   C CB    . ALA B 2 45   ? 165.005 139.844 165.843 1.00 45.83  ? 42   ALA A CB    1 
ATOM   869   N N     . ARG B 2 46   ? 161.917 139.823 164.989 1.00 45.96  ? 43   ARG A N     1 
ATOM   870   C CA    . ARG B 2 46   ? 160.614 139.167 164.974 1.00 45.96  ? 43   ARG A CA    1 
ATOM   871   C C     . ARG B 2 46   ? 160.149 138.903 163.547 1.00 45.96  ? 43   ARG A C     1 
ATOM   872   O O     . ARG B 2 46   ? 159.476 137.901 163.281 1.00 45.96  ? 43   ARG A O     1 
ATOM   873   C CB    . ARG B 2 46   ? 159.590 140.013 165.732 1.00 45.96  ? 43   ARG A CB    1 
ATOM   874   C CG    . ARG B 2 46   ? 158.215 139.374 165.842 1.00 45.96  ? 43   ARG A CG    1 
ATOM   875   C CD    . ARG B 2 46   ? 157.505 139.788 167.121 1.00 45.96  ? 43   ARG A CD    1 
ATOM   876   N NE    . ARG B 2 46   ? 158.329 139.559 168.302 1.00 45.96  ? 43   ARG A NE    1 
ATOM   877   C CZ    . ARG B 2 46   ? 158.267 140.282 169.412 1.00 45.96  ? 43   ARG A CZ    1 
ATOM   878   N NH1   . ARG B 2 46   ? 157.422 141.292 169.532 1.00 45.96  ? 43   ARG A NH1   1 
ATOM   879   N NH2   . ARG B 2 46   ? 159.072 139.983 170.427 1.00 45.96  ? 43   ARG A NH2   1 
ATOM   880   N N     . ASN B 2 47   ? 160.498 139.793 162.616 1.00 45.00  ? 44   ASN A N     1 
ATOM   881   C CA    . ASN B 2 47   ? 160.192 139.552 161.209 1.00 45.00  ? 44   ASN A CA    1 
ATOM   882   C C     . ASN B 2 47   ? 160.944 138.331 160.691 1.00 45.00  ? 44   ASN A C     1 
ATOM   883   O O     . ASN B 2 47   ? 160.372 137.482 159.997 1.00 45.00  ? 44   ASN A O     1 
ATOM   884   C CB    . ASN B 2 47   ? 160.539 140.788 160.380 1.00 45.00  ? 44   ASN A CB    1 
ATOM   885   C CG    . ASN B 2 47   ? 160.125 140.652 158.930 1.00 45.00  ? 44   ASN A CG    1 
ATOM   886   O OD1   . ASN B 2 47   ? 159.361 139.756 158.571 1.00 45.00  ? 44   ASN A OD1   1 
ATOM   887   N ND2   . ASN B 2 47   ? 160.632 141.541 158.085 1.00 45.00  ? 44   ASN A ND2   1 
ATOM   888   N N     . ASP B 2 48   ? 162.233 138.229 161.020 1.00 47.99  ? 45   ASP A N     1 
ATOM   889   C CA    . ASP B 2 48   ? 163.013 137.068 160.607 1.00 47.99  ? 45   ASP A CA    1 
ATOM   890   C C     . ASP B 2 48   ? 162.529 135.804 161.305 1.00 47.99  ? 45   ASP A C     1 
ATOM   891   O O     . ASP B 2 48   ? 162.493 134.726 160.701 1.00 47.99  ? 45   ASP A O     1 
ATOM   892   C CB    . ASP B 2 48   ? 164.495 137.307 160.890 1.00 47.99  ? 45   ASP A CB    1 
ATOM   893   C CG    . ASP B 2 48   ? 165.092 138.374 159.997 1.00 47.99  ? 45   ASP A CG    1 
ATOM   894   O OD1   . ASP B 2 48   ? 164.606 138.537 158.858 1.00 47.99  ? 45   ASP A OD1   1 
ATOM   895   O OD2   . ASP B 2 48   ? 166.046 139.051 160.433 1.00 47.99  ? 45   ASP A OD2   1 
ATOM   896   N N     . HIS B 2 49   ? 162.162 135.916 162.584 1.00 52.31  ? 46   HIS A N     1 
ATOM   897   C CA    . HIS B 2 49   ? 161.628 134.766 163.307 1.00 52.31  ? 46   HIS A CA    1 
ATOM   898   C C     . HIS B 2 49   ? 160.317 134.289 162.696 1.00 52.31  ? 46   HIS A C     1 
ATOM   899   O O     . HIS B 2 49   ? 160.075 133.081 162.592 1.00 52.31  ? 46   HIS A O     1 
ATOM   900   C CB    . HIS B 2 49   ? 161.432 135.119 164.781 1.00 52.31  ? 46   HIS A CB    1 
ATOM   901   C CG    . HIS B 2 49   ? 162.712 135.295 165.537 1.00 52.31  ? 46   HIS A CG    1 
ATOM   902   N ND1   . HIS B 2 49   ? 162.791 136.016 166.709 1.00 52.31  ? 46   HIS A ND1   1 
ATOM   903   C CD2   . HIS B 2 49   ? 163.964 134.845 165.288 1.00 52.31  ? 46   HIS A CD2   1 
ATOM   904   C CE1   . HIS B 2 49   ? 164.036 136.001 167.150 1.00 52.31  ? 46   HIS A CE1   1 
ATOM   905   N NE2   . HIS B 2 49   ? 164.768 135.297 166.306 1.00 52.31  ? 46   HIS A NE2   1 
ATOM   906   N N     . TYR B 2 50   ? 159.455 135.225 162.296 1.00 54.95  ? 47   TYR A N     1 
ATOM   907   C CA    . TYR B 2 50   ? 158.186 134.858 161.676 1.00 54.95  ? 47   TYR A CA    1 
ATOM   908   C C     . TYR B 2 50   ? 158.410 134.123 160.360 1.00 54.95  ? 47   TYR A C     1 
ATOM   909   O O     . TYR B 2 50   ? 157.723 133.141 160.058 1.00 54.95  ? 47   TYR A O     1 
ATOM   910   C CB    . TYR B 2 50   ? 157.335 136.111 161.466 1.00 54.95  ? 47   TYR A CB    1 
ATOM   911   C CG    . TYR B 2 50   ? 156.187 135.944 160.498 1.00 54.95  ? 47   TYR A CG    1 
ATOM   912   C CD1   . TYR B 2 50   ? 155.092 135.154 160.817 1.00 54.95  ? 47   TYR A CD1   1 
ATOM   913   C CD2   . TYR B 2 50   ? 156.193 136.588 159.269 1.00 54.95  ? 47   TYR A CD2   1 
ATOM   914   C CE1   . TYR B 2 50   ? 154.040 135.005 159.936 1.00 54.95  ? 47   TYR A CE1   1 
ATOM   915   C CE2   . TYR B 2 50   ? 155.145 136.443 158.383 1.00 54.95  ? 47   TYR A CE2   1 
ATOM   916   C CZ    . TYR B 2 50   ? 154.072 135.651 158.722 1.00 54.95  ? 47   TYR A CZ    1 
ATOM   917   O OH    . TYR B 2 50   ? 153.025 135.503 157.842 1.00 54.95  ? 47   TYR A OH    1 
ATOM   918   N N     . LYS B 2 51   ? 159.374 134.587 159.560 1.00 52.37  ? 48   LYS A N     1 
ATOM   919   C CA    . LYS B 2 51   ? 159.654 133.935 158.284 1.00 52.37  ? 48   LYS A CA    1 
ATOM   920   C C     . LYS B 2 51   ? 160.333 132.585 158.484 1.00 52.37  ? 48   LYS A C     1 
ATOM   921   O O     . LYS B 2 51   ? 160.048 131.626 157.758 1.00 52.37  ? 48   LYS A O     1 
ATOM   922   C CB    . LYS B 2 51   ? 160.516 134.843 157.409 1.00 52.37  ? 48   LYS A CB    1 
ATOM   923   C CG    . LYS B 2 51   ? 159.815 136.110 156.950 1.00 52.37  ? 48   LYS A CG    1 
ATOM   924   C CD    . LYS B 2 51   ? 160.668 136.881 155.956 1.00 52.37  ? 48   LYS A CD    1 
ATOM   925   C CE    . LYS B 2 51   ? 161.833 137.569 156.650 1.00 52.37  ? 48   LYS A CE    1 
ATOM   926   N NZ    . LYS B 2 51   ? 162.618 138.418 155.713 1.00 52.37  ? 48   LYS A NZ    1 
ATOM   927   N N     . GLU B 2 52   ? 161.242 132.491 159.457 1.00 54.46  ? 49   GLU A N     1 
ATOM   928   C CA    . GLU B 2 52   ? 161.922 131.225 159.706 1.00 54.46  ? 49   GLU A CA    1 
ATOM   929   C C     . GLU B 2 52   ? 160.976 130.196 160.312 1.00 54.46  ? 49   GLU A C     1 
ATOM   930   O O     . GLU B 2 52   ? 161.215 128.989 160.197 1.00 54.46  ? 49   GLU A O     1 
ATOM   931   C CB    . GLU B 2 52   ? 163.126 131.448 160.622 1.00 54.46  ? 49   GLU A CB    1 
ATOM   932   C CG    . GLU B 2 52   ? 164.076 130.263 160.739 1.00 54.46  ? 49   GLU A CG    1 
ATOM   933   C CD    . GLU B 2 52   ? 164.220 129.491 159.440 1.00 54.46  ? 49   GLU A CD    1 
ATOM   934   O OE1   . GLU B 2 52   ? 164.819 130.035 158.489 1.00 54.46  ? 49   GLU A OE1   1 
ATOM   935   O OE2   . GLU B 2 52   ? 163.735 128.342 159.368 1.00 54.46  ? 49   GLU A OE2   1 
ATOM   936   N N     . LEU B 2 53   ? 159.901 130.649 160.954 1.00 59.41  ? 50   LEU A N     1 
ATOM   937   C CA    . LEU B 2 53   ? 158.914 129.747 161.530 1.00 59.41  ? 50   LEU A CA    1 
ATOM   938   C C     . LEU B 2 53   ? 157.850 129.332 160.520 1.00 59.41  ? 50   LEU A C     1 
ATOM   939   O O     . LEU B 2 53   ? 157.027 128.461 160.824 1.00 59.41  ? 50   LEU A O     1 
ATOM   940   C CB    . LEU B 2 53   ? 158.270 130.408 162.756 1.00 59.41  ? 50   LEU A CB    1 
ATOM   941   C CG    . LEU B 2 53   ? 157.238 129.665 163.608 1.00 59.41  ? 50   LEU A CG    1 
ATOM   942   C CD1   . LEU B 2 53   ? 157.860 128.432 164.243 1.00 59.41  ? 50   LEU A CD1   1 
ATOM   943   C CD2   . LEU B 2 53   ? 156.665 130.582 164.674 1.00 59.41  ? 50   LEU A CD2   1 
ATOM   944   N N     . LYS B 2 54   ? 157.865 129.920 159.324 1.00 66.17  ? 51   LYS A N     1 
ATOM   945   C CA    . LYS B 2 54   ? 156.931 129.543 158.262 1.00 66.17  ? 51   LYS A CA    1 
ATOM   946   C C     . LYS B 2 54   ? 156.955 128.057 157.918 1.00 66.17  ? 51   LYS A C     1 
ATOM   947   O O     . LYS B 2 54   ? 155.873 127.454 157.836 1.00 66.17  ? 51   LYS A O     1 
ATOM   948   C CB    . LYS B 2 54   ? 157.218 130.398 157.020 1.00 66.17  ? 51   LYS A CB    1 
ATOM   949   C CG    . LYS B 2 54   ? 156.443 129.999 155.774 1.00 66.17  ? 51   LYS A CG    1 
ATOM   950   C CD    . LYS B 2 54   ? 154.990 130.438 155.833 1.00 66.17  ? 51   LYS A CD    1 
ATOM   951   C CE    . LYS B 2 54   ? 154.252 130.016 154.571 1.00 66.17  ? 51   LYS A CE    1 
ATOM   952   N NZ    . LYS B 2 54   ? 152.802 130.347 154.620 1.00 66.17  ? 51   LYS A NZ    1 
ATOM   953   N N     . PRO B 2 55   ? 158.106 127.408 157.702 1.00 60.15  ? 52   PRO A N     1 
ATOM   954   C CA    . PRO B 2 55   ? 158.060 125.971 157.399 1.00 60.15  ? 52   PRO A CA    1 
ATOM   955   C C     . PRO B 2 55   ? 158.022 125.095 158.637 1.00 60.15  ? 52   PRO A C     1 
ATOM   956   O O     . PRO B 2 55   ? 157.594 123.938 158.547 1.00 60.15  ? 52   PRO A O     1 
ATOM   957   C CB    . PRO B 2 55   ? 159.336 125.743 156.578 1.00 60.15  ? 52   PRO A CB    1 
ATOM   958   C CG    . PRO B 2 55   ? 160.234 126.917 156.878 1.00 60.15  ? 52   PRO A CG    1 
ATOM   959   C CD    . PRO B 2 55   ? 159.497 127.894 157.748 1.00 60.15  ? 52   PRO A CD    1 
ATOM   960   N N     . ILE B 2 56   ? 158.459 125.606 159.791 1.00 61.63  ? 53   ILE A N     1 
ATOM   961   C CA    . ILE B 2 56   ? 158.384 124.823 161.021 1.00 61.63  ? 53   ILE A CA    1 
ATOM   962   C C     . ILE B 2 56   ? 156.933 124.531 161.377 1.00 61.63  ? 53   ILE A C     1 
ATOM   963   O O     . ILE B 2 56   ? 156.580 123.396 161.719 1.00 61.63  ? 53   ILE A O     1 
ATOM   964   C CB    . ILE B 2 56   ? 159.114 125.548 162.166 1.00 61.63  ? 53   ILE A CB    1 
ATOM   965   C CG1   . ILE B 2 56   ? 160.616 125.613 161.887 1.00 61.63  ? 53   ILE A CG1   1 
ATOM   966   C CG2   . ILE B 2 56   ? 158.855 124.851 163.489 1.00 61.63  ? 53   ILE A CG2   1 
ATOM   967   C CD1   . ILE B 2 56   ? 161.311 126.771 162.566 1.00 61.63  ? 53   ILE A CD1   1 
ATOM   968   N N     . ILE B 2 57   ? 156.068 125.543 161.296 1.00 65.42  ? 54   ILE A N     1 
ATOM   969   C CA    . ILE B 2 57   ? 154.647 125.317 161.533 1.00 65.42  ? 54   ILE A CA    1 
ATOM   970   C C     . ILE B 2 57   ? 154.054 124.470 160.416 1.00 65.42  ? 54   ILE A C     1 
ATOM   971   O O     . ILE B 2 57   ? 153.226 123.585 160.662 1.00 65.42  ? 54   ILE A O     1 
ATOM   972   C CB    . ILE B 2 57   ? 153.907 126.658 161.685 1.00 65.42  ? 54   ILE A CB    1 
ATOM   973   C CG1   . ILE B 2 57   ? 154.480 127.449 162.860 1.00 65.42  ? 54   ILE A CG1   1 
ATOM   974   C CG2   . ILE B 2 57   ? 152.426 126.423 161.903 1.00 65.42  ? 54   ILE A CG2   1 
ATOM   975   C CD1   . ILE B 2 57   ? 154.342 126.746 164.192 1.00 65.42  ? 54   ILE A CD1   1 
ATOM   976   N N     . ASP B 2 58   ? 154.472 124.720 159.173 1.00 65.79  ? 55   ASP A N     1 
ATOM   977   C CA    . ASP B 2 58   ? 154.029 123.884 158.062 1.00 65.79  ? 55   ASP A CA    1 
ATOM   978   C C     . ASP B 2 58   ? 154.471 122.440 158.256 1.00 65.79  ? 55   ASP A C     1 
ATOM   979   O O     . ASP B 2 58   ? 153.750 121.506 157.887 1.00 65.79  ? 55   ASP A O     1 
ATOM   980   C CB    . ASP B 2 58   ? 154.562 124.438 156.741 1.00 65.79  ? 55   ASP A CB    1 
ATOM   981   C CG    . ASP B 2 58   ? 153.978 123.730 155.535 1.00 65.79  ? 55   ASP A CG    1 
ATOM   982   O OD1   . ASP B 2 58   ? 152.851 123.204 155.641 1.00 65.79  ? 55   ASP A OD1   1 
ATOM   983   O OD2   . ASP B 2 58   ? 154.647 123.699 154.481 1.00 65.79  ? 55   ASP A OD2   1 
ATOM   984   N N     . ARG B 2 59   ? 155.662 122.239 158.823 1.00 70.12  ? 56   ARG A N     1 
ATOM   985   C CA    . ARG B 2 59   ? 156.100 120.891 159.168 1.00 70.12  ? 56   ARG A CA    1 
ATOM   986   C C     . ARG B 2 59   ? 155.205 120.285 160.241 1.00 70.12  ? 56   ARG A C     1 
ATOM   987   O O     . ARG B 2 59   ? 154.874 119.096 160.181 1.00 70.12  ? 56   ARG A O     1 
ATOM   988   C CB    . ARG B 2 59   ? 157.558 120.918 159.623 1.00 70.12  ? 56   ARG A CB    1 
ATOM   989   C CG    . ARG B 2 59   ? 158.047 119.634 160.258 1.00 70.12  ? 56   ARG A CG    1 
ATOM   990   C CD    . ARG B 2 59   ? 159.485 119.778 160.727 1.00 70.12  ? 56   ARG A CD    1 
ATOM   991   N NE    . ARG B 2 59   ? 159.569 120.024 162.161 1.00 70.12  ? 56   ARG A NE    1 
ATOM   992   C CZ    . ARG B 2 59   ? 160.698 120.026 162.854 1.00 70.12  ? 56   ARG A CZ    1 
ATOM   993   N NH1   . ARG B 2 59   ? 161.867 119.812 162.272 1.00 70.12  ? 56   ARG A NH1   1 
ATOM   994   N NH2   . ARG B 2 59   ? 160.655 120.247 164.164 1.00 70.12  ? 56   ARG A NH2   1 
ATOM   995   N N     . ILE B 2 60   ? 154.847 121.038 161.284 1.00 68.71  ? 57   ILE A N     1 
ATOM   996   C CA    . ILE B 2 60   ? 154.006 120.465 162.384 1.00 68.71  ? 57   ILE A CA    1 
ATOM   997   C C     . ILE B 2 60   ? 152.567 120.465 161.870 1.00 68.71  ? 57   ILE A C     1 
ATOM   998   O O     . ILE B 2 60   ? 151.635 120.261 162.662 1.00 68.71  ? 57   ILE A O     1 
ATOM   999   C CB    . ILE B 2 60   ? 154.146 121.252 163.708 1.00 68.71  ? 57   ILE A CB    1 
ATOM   1000  C CG1   . ILE B 2 60   ? 155.588 121.685 163.971 1.00 68.71  ? 57   ILE A CG1   1 
ATOM   1001  C CG2   . ILE B 2 60   ? 153.591 120.458 164.880 1.00 68.71  ? 57   ILE A CG2   1 
ATOM   1002  C CD1   . ILE B 2 60   ? 155.743 122.570 165.183 1.00 68.71  ? 57   ILE A CD1   1 
ATOM   1003  N N     . TYR B 2 61   ? 152.407 120.725 160.578 1.00 76.23  ? 58   TYR A N     1 
ATOM   1004  C CA    . TYR B 2 61   ? 151.048 120.827 160.006 1.00 76.23  ? 58   TYR A CA    1 
ATOM   1005  C C     . TYR B 2 61   ? 150.841 119.538 159.253 1.00 76.23  ? 58   TYR A C     1 
ATOM   1006  O O     . TYR B 2 61   ? 149.703 119.108 159.028 1.00 76.23  ? 58   TYR A O     1 
ATOM   1007  C CB    . TYR B 2 61   ? 150.972 121.997 159.026 1.00 76.23  ? 58   TYR A CB    1 
ATOM   1008  C CG    . TYR B 2 61   ? 149.890 123.015 159.279 1.00 76.23  ? 58   TYR A CG    1 
ATOM   1009  C CD1   . TYR B 2 61   ? 148.577 122.771 158.917 1.00 76.23  ? 58   TYR A CD1   1 
ATOM   1010  C CD2   . TYR B 2 61   ? 150.187 124.240 159.852 1.00 76.23  ? 58   TYR A CD2   1 
ATOM   1011  C CE1   . TYR B 2 61   ? 147.582 123.709 159.134 1.00 76.23  ? 58   TYR A CE1   1 
ATOM   1012  C CE2   . TYR B 2 61   ? 149.206 125.189 160.075 1.00 76.23  ? 58   TYR A CE2   1 
ATOM   1013  C CZ    . TYR B 2 61   ? 147.898 124.923 159.715 1.00 76.23  ? 58   TYR A CZ    1 
ATOM   1014  O OH    . TYR B 2 61   ? 146.927 125.856 159.930 1.00 76.23  ? 58   TYR A OH    1 
ATOM   1015  N N     . LYS B 2 62   ? 151.960 118.961 158.855 1.00 66.76  ? 59   LYS A N     1 
ATOM   1016  C CA    . LYS B 2 62   ? 151.856 117.649 158.190 1.00 64.88  ? 59   LYS A CA    1 
ATOM   1017  C C     . LYS B 2 62   ? 151.699 116.615 159.292 1.00 69.08  ? 59   LYS A C     1 
ATOM   1018  O O     . LYS B 2 62   ? 150.865 115.713 159.150 1.00 70.16  ? 59   LYS A O     1 
ATOM   1019  C CB    . LYS B 2 62   ? 153.112 117.380 157.359 1.00 64.02  ? 59   LYS A CB    1 
ATOM   1020  C CG    . LYS B 2 62   ? 153.482 118.482 156.376 1.00 62.74  ? 59   LYS A CG    1 
ATOM   1021  C CD    . LYS B 2 62   ? 154.839 118.276 155.743 1.00 63.27  ? 59   LYS A CD    1 
ATOM   1022  C CE    . LYS B 2 62   ? 155.946 118.134 156.766 1.00 66.52  ? 59   LYS A CE    1 
ATOM   1023  N NZ    . LYS B 2 62   ? 157.268 117.949 156.124 1.00 66.37  ? 59   LYS A NZ    1 
ATOM   1024  N N     . THR B 2 63   ? 152.419 116.805 160.397 1.00 73.25  ? 60   THR A N     1 
ATOM   1025  C CA    . THR B 2 63   ? 152.267 115.707 161.347 1.00 76.55  ? 60   THR A CA    1 
ATOM   1026  C C     . THR B 2 63   ? 150.798 115.381 161.578 1.00 78.91  ? 60   THR A C     1 
ATOM   1027  O O     . THR B 2 63   ? 150.393 114.214 161.503 1.00 79.19  ? 60   THR A O     1 
ATOM   1028  C CB    . THR B 2 63   ? 152.956 116.053 162.666 1.00 80.26  ? 60   THR A CB    1 
ATOM   1029  O OG1   . THR B 2 63   ? 154.285 116.521 162.403 1.00 82.54  ? 60   THR A OG1   1 
ATOM   1030  C CG2   . THR B 2 63   ? 153.029 114.828 163.567 1.00 81.68  ? 60   THR A CG2   1 
ATOM   1031  N N     . TYR B 2 64   ? 149.980 116.400 161.856 1.00 81.09  ? 61   TYR A N     1 
ATOM   1032  C CA    . TYR B 2 64   ? 148.569 116.157 162.139 1.00 83.09  ? 61   TYR A CA    1 
ATOM   1033  C C     . TYR B 2 64   ? 147.852 115.572 160.930 1.00 83.80  ? 61   TYR A C     1 
ATOM   1034  O O     . TYR B 2 64   ? 147.043 114.646 161.067 1.00 84.04  ? 61   TYR A O     1 
ATOM   1035  C CB    . TYR B 2 64   ? 147.892 117.448 162.593 1.00 81.79  ? 61   TYR A CB    1 
ATOM   1036  C CG    . TYR B 2 64   ? 146.399 117.310 162.783 1.00 79.80  ? 61   TYR A CG    1 
ATOM   1037  C CD1   . TYR B 2 64   ? 145.877 116.706 163.920 1.00 80.90  ? 61   TYR A CD1   1 
ATOM   1038  C CD2   . TYR B 2 64   ? 145.512 117.782 161.825 1.00 77.87  ? 61   TYR A CD2   1 
ATOM   1039  C CE1   . TYR B 2 64   ? 144.513 116.574 164.095 1.00 81.09  ? 61   TYR A CE1   1 
ATOM   1040  C CE2   . TYR B 2 64   ? 144.149 117.657 161.991 1.00 77.99  ? 61   TYR A CE2   1 
ATOM   1041  C CZ    . TYR B 2 64   ? 143.654 117.053 163.128 1.00 79.63  ? 61   TYR A CZ    1 
ATOM   1042  O OH    . TYR B 2 64   ? 142.294 116.928 163.294 1.00 79.57  ? 61   TYR A OH    1 
ATOM   1043  N N     . ALA B 2 65   ? 148.131 116.098 159.734 1.00 84.26  ? 62   ALA A N     1 
ATOM   1044  C CA    . ALA B 2 65   ? 147.506 115.554 158.532 1.00 84.02  ? 62   ALA A CA    1 
ATOM   1045  C C     . ALA B 2 65   ? 147.962 114.124 158.279 1.00 85.43  ? 62   ALA A C     1 
ATOM   1046  O O     . ALA B 2 65   ? 147.149 113.257 157.936 1.00 86.51  ? 62   ALA A O     1 
ATOM   1047  C CB    . ALA B 2 65   ? 147.815 116.438 157.323 1.00 82.50  ? 62   ALA A CB    1 
ATOM   1048  N N     . ASP B 2 66   ? 149.259 113.855 158.450 1.00 86.48  ? 63   ASP A N     1 
ATOM   1049  C CA    . ASP B 2 66   ? 149.760 112.500 158.252 1.00 88.87  ? 63   ASP A CA    1 
ATOM   1050  C C     . ASP B 2 66   ? 149.153 111.538 159.266 1.00 90.28  ? 63   ASP A C     1 
ATOM   1051  O O     . ASP B 2 66   ? 148.804 110.404 158.922 1.00 91.39  ? 63   ASP A O     1 
ATOM   1052  C CB    . ASP B 2 66   ? 151.288 112.492 158.341 1.00 93.16  ? 63   ASP A CB    1 
ATOM   1053  C CG    . ASP B 2 66   ? 151.907 111.269 157.692 1.00 97.49  ? 63   ASP A CG    1 
ATOM   1054  O OD1   . ASP B 2 66   ? 151.474 110.139 157.999 1.00 100.21 ? 63   ASP A OD1   1 
ATOM   1055  O OD2   . ASP B 2 66   ? 152.829 111.441 156.866 1.00 98.07  ? 63   ASP A OD2   1 
ATOM   1056  N N     . GLN B 2 67   ? 149.007 111.979 160.518 1.00 89.86  ? 64   GLN A N     1 
ATOM   1057  C CA    . GLN B 2 67   ? 148.423 111.116 161.541 1.00 88.06  ? 64   GLN A CA    1 
ATOM   1058  C C     . GLN B 2 67   ? 146.959 110.813 161.244 1.00 83.49  ? 64   GLN A C     1 
ATOM   1059  O O     . GLN B 2 67   ? 146.502 109.682 161.447 1.00 83.81  ? 64   GLN A O     1 
ATOM   1060  C CB    . GLN B 2 67   ? 148.568 111.762 162.919 1.00 88.84  ? 64   GLN A CB    1 
ATOM   1061  C CG    . GLN B 2 67   ? 149.986 111.749 163.463 1.00 90.92  ? 64   GLN A CG    1 
ATOM   1062  C CD    . GLN B 2 67   ? 150.121 112.530 164.755 1.00 94.52  ? 64   GLN A CD    1 
ATOM   1063  O OE1   . GLN B 2 67   ? 150.039 113.757 164.764 1.00 97.42  ? 64   GLN A OE1   1 
ATOM   1064  N NE2   . GLN B 2 67   ? 150.328 111.818 165.857 1.00 94.55  ? 64   GLN A NE2   1 
ATOM   1065  N N     . CYS B 2 68   ? 146.210 111.807 160.758 1.00 79.56  ? 65   CYS A N     1 
ATOM   1066  C CA    . CYS B 2 68   ? 144.802 111.581 160.443 1.00 77.17  ? 65   CYS A CA    1 
ATOM   1067  C C     . CYS B 2 68   ? 144.630 110.661 159.242 1.00 74.34  ? 65   CYS A C     1 
ATOM   1068  O O     . CYS B 2 68   ? 143.659 109.898 159.184 1.00 71.82  ? 65   CYS A O     1 
ATOM   1069  C CB    . CYS B 2 68   ? 144.096 112.913 160.195 1.00 77.04  ? 65   CYS A CB    1 
ATOM   1070  S SG    . CYS B 2 68   ? 143.890 113.934 161.671 1.00 81.69  ? 65   CYS A SG    1 
ATOM   1071  N N     . LEU B 2 69   ? 145.548 110.716 158.278 1.00 73.22  ? 66   LEU A N     1 
ATOM   1072  C CA    . LEU B 2 69   ? 145.452 109.870 157.096 1.00 71.15  ? 66   LEU A CA    1 
ATOM   1073  C C     . LEU B 2 69   ? 145.866 108.429 157.358 1.00 75.33  ? 66   LEU A C     1 
ATOM   1074  O O     . LEU B 2 69   ? 145.629 107.570 156.503 1.00 77.12  ? 66   LEU A O     1 
ATOM   1075  C CB    . LEU B 2 69   ? 146.303 110.452 155.962 1.00 65.00  ? 66   LEU A CB    1 
ATOM   1076  C CG    . LEU B 2 69   ? 145.839 111.804 155.413 1.00 58.74  ? 66   LEU A CG    1 
ATOM   1077  C CD1   . LEU B 2 69   ? 146.764 112.303 154.313 1.00 54.64  ? 66   LEU A CD1   1 
ATOM   1078  C CD2   . LEU B 2 69   ? 144.404 111.724 154.917 1.00 56.42  ? 66   LEU A CD2   1 
ATOM   1079  N N     . GLN B 2 70   ? 146.472 108.136 158.512 1.00 78.16  ? 67   GLN A N     1 
ATOM   1080  C CA    . GLN B 2 70   ? 146.880 106.766 158.803 1.00 82.42  ? 67   GLN A CA    1 
ATOM   1081  C C     . GLN B 2 70   ? 145.703 105.893 159.220 1.00 85.59  ? 67   GLN A C     1 
ATOM   1082  O O     . GLN B 2 70   ? 145.760 104.668 159.057 1.00 87.67  ? 67   GLN A O     1 
ATOM   1083  C CB    . GLN B 2 70   ? 147.952 106.750 159.894 1.00 85.82  ? 67   GLN A CB    1 
ATOM   1084  C CG    . GLN B 2 70   ? 149.284 107.352 159.473 1.00 85.53  ? 67   GLN A CG    1 
ATOM   1085  C CD    . GLN B 2 70   ? 150.313 107.323 160.587 1.00 87.69  ? 67   GLN A CD    1 
ATOM   1086  O OE1   . GLN B 2 70   ? 150.628 106.263 161.126 1.00 89.72  ? 67   GLN A OE1   1 
ATOM   1087  N NE2   . GLN B 2 70   ? 150.837 108.493 160.943 1.00 87.30  ? 67   GLN A NE2   1 
ATOM   1088  N N     . LEU B 2 71   ? 144.640 106.490 159.755 1.00 86.89  ? 68   LEU A N     1 
ATOM   1089  C CA    . LEU B 2 71   ? 143.476 105.741 160.206 1.00 90.18  ? 68   LEU A CA    1 
ATOM   1090  C C     . LEU B 2 71   ? 142.385 105.634 159.149 1.00 90.06  ? 68   LEU A C     1 
ATOM   1091  O O     . LEU B 2 71   ? 141.323 105.070 159.432 1.00 91.05  ? 68   LEU A O     1 
ATOM   1092  C CB    . LEU B 2 71   ? 142.890 106.379 161.469 1.00 92.47  ? 68   LEU A CB    1 
ATOM   1093  C CG    . LEU B 2 71   ? 143.795 106.512 162.694 1.00 94.87  ? 68   LEU A CG    1 
ATOM   1094  C CD1   . LEU B 2 71   ? 144.265 107.945 162.855 1.00 93.49  ? 68   LEU A CD1   1 
ATOM   1095  C CD2   . LEU B 2 71   ? 143.071 106.039 163.944 1.00 98.14  ? 68   LEU A CD2   1 
ATOM   1096  N N     . VAL B 2 72   ? 142.612 106.161 157.947 1.00 88.71  ? 69   VAL A N     1 
ATOM   1097  C CA    . VAL B 2 72   ? 141.563 106.189 156.932 1.00 86.66  ? 69   VAL A CA    1 
ATOM   1098  C C     . VAL B 2 72   ? 141.381 104.791 156.355 1.00 86.87  ? 69   VAL A C     1 
ATOM   1099  O O     . VAL B 2 72   ? 142.316 104.205 155.797 1.00 87.21  ? 69   VAL A O     1 
ATOM   1100  C CB    . VAL B 2 72   ? 141.890 107.204 155.831 1.00 81.61  ? 69   VAL A CB    1 
ATOM   1101  C CG1   . VAL B 2 72   ? 140.782 107.224 154.791 1.00 79.70  ? 69   VAL A CG1   1 
ATOM   1102  C CG2   . VAL B 2 72   ? 142.089 108.588 156.427 1.00 80.65  ? 69   VAL A CG2   1 
ATOM   1103  N N     . GLN B 2 73   ? 140.170 104.254 156.486 1.00 88.38  ? 70   GLN A N     1 
ATOM   1104  C CA    . GLN B 2 73   ? 139.790 102.974 155.894 1.00 88.49  ? 70   GLN A CA    1 
ATOM   1105  C C     . GLN B 2 73   ? 138.436 103.158 155.222 1.00 85.74  ? 70   GLN A C     1 
ATOM   1106  O O     . GLN B 2 73   ? 137.427 103.360 155.905 1.00 87.42  ? 70   GLN A O     1 
ATOM   1107  C CB    . GLN B 2 73   ? 139.732 101.864 156.944 1.00 94.00  ? 70   GLN A CB    1 
ATOM   1108  C CG    . GLN B 2 73   ? 140.966 100.971 156.996 1.00 99.61  ? 70   GLN A CG    1 
ATOM   1109  C CD    . GLN B 2 73   ? 142.173 101.663 157.599 1.00 102.76 ? 70   GLN A CD    1 
ATOM   1110  O OE1   . GLN B 2 73   ? 143.139 101.973 156.900 1.00 104.11 ? 70   GLN A OE1   1 
ATOM   1111  N NE2   . GLN B 2 73   ? 142.124 101.911 158.903 1.00 102.05 ? 70   GLN A NE2   1 
ATOM   1112  N N     . LEU B 2 74   ? 138.413 103.093 153.894 1.00 83.59  ? 71   LEU A N     1 
ATOM   1113  C CA    . LEU B 2 74   ? 137.191 103.294 153.131 1.00 80.35  ? 71   LEU A CA    1 
ATOM   1114  C C     . LEU B 2 74   ? 137.034 102.195 152.090 1.00 78.91  ? 71   LEU A C     1 
ATOM   1115  O O     . LEU B 2 74   ? 137.995 101.524 151.708 1.00 79.78  ? 71   LEU A O     1 
ATOM   1116  C CB    . LEU B 2 74   ? 137.177 104.662 152.436 1.00 74.28  ? 71   LEU A CB    1 
ATOM   1117  C CG    . LEU B 2 74   ? 137.178 105.896 153.335 1.00 71.19  ? 71   LEU A CG    1 
ATOM   1118  C CD1   . LEU B 2 74   ? 137.123 107.153 152.487 1.00 67.32  ? 71   LEU A CD1   1 
ATOM   1119  C CD2   . LEU B 2 74   ? 136.013 105.848 154.310 1.00 71.98  ? 71   LEU A CD2   1 
ATOM   1120  N N     . ASP B 2 75   ? 135.794 102.023 151.636 1.00 78.75  ? 72   ASP A N     1 
ATOM   1121  C CA    . ASP B 2 75   ? 135.462 101.094 150.563 1.00 80.11  ? 72   ASP A CA    1 
ATOM   1122  C C     . ASP B 2 75   ? 135.303 101.904 149.282 1.00 78.86  ? 72   ASP A C     1 
ATOM   1123  O O     . ASP B 2 75   ? 134.311 102.618 149.110 1.00 79.00  ? 72   ASP A O     1 
ATOM   1124  C CB    . ASP B 2 75   ? 134.190 100.314 150.890 1.00 83.64  ? 72   ASP A CB    1 
ATOM   1125  C CG    . ASP B 2 75   ? 133.993 99.108  149.989 1.00 87.93  ? 72   ASP A CG    1 
ATOM   1126  O OD1   . ASP B 2 75   ? 134.554 99.090  148.873 1.00 89.44  ? 72   ASP A OD1   1 
ATOM   1127  O OD2   . ASP B 2 75   ? 133.275 98.173  150.401 1.00 91.11  ? 72   ASP A OD2   1 
ATOM   1128  N N     . TRP B 2 76   ? 136.281 101.792 148.387 1.00 77.19  ? 73   TRP A N     1 
ATOM   1129  C CA    . TRP B 2 76   ? 136.327 102.589 147.169 1.00 74.62  ? 73   TRP A CA    1 
ATOM   1130  C C     . TRP B 2 76   ? 135.550 101.962 146.018 1.00 76.79  ? 73   TRP A C     1 
ATOM   1131  O O     . TRP B 2 76   ? 135.688 102.414 144.877 1.00 76.14  ? 73   TRP A O     1 
ATOM   1132  C CB    . TRP B 2 76   ? 137.780 102.813 146.749 1.00 70.57  ? 73   TRP A CB    1 
ATOM   1133  C CG    . TRP B 2 76   ? 138.636 103.389 147.834 1.00 67.54  ? 73   TRP A CG    1 
ATOM   1134  C CD1   . TRP B 2 76   ? 139.299 102.701 148.809 1.00 67.81  ? 73   TRP A CD1   1 
ATOM   1135  C CD2   . TRP B 2 76   ? 138.922 104.776 148.057 1.00 65.75  ? 73   TRP A CD2   1 
ATOM   1136  N NE1   . TRP B 2 76   ? 139.981 103.571 149.624 1.00 67.17  ? 73   TRP A NE1   1 
ATOM   1137  C CE2   . TRP B 2 76   ? 139.765 104.851 149.184 1.00 66.42  ? 73   TRP A CE2   1 
ATOM   1138  C CE3   . TRP B 2 76   ? 138.549 105.959 147.414 1.00 63.59  ? 73   TRP A CE3   1 
ATOM   1139  C CZ2   . TRP B 2 76   ? 140.241 106.064 149.681 1.00 65.46  ? 73   TRP A CZ2   1 
ATOM   1140  C CZ3   . TRP B 2 76   ? 139.020 107.162 147.909 1.00 61.89  ? 73   TRP A CZ3   1 
ATOM   1141  C CH2   . TRP B 2 76   ? 139.857 107.204 149.031 1.00 63.01  ? 73   TRP A CH2   1 
ATOM   1142  N N     . GLU B 2 77   ? 134.735 100.938 146.288 1.00 83.38  ? 74   GLU A N     1 
ATOM   1143  C CA    . GLU B 2 77   ? 134.016 100.266 145.210 1.00 87.04  ? 74   GLU A CA    1 
ATOM   1144  C C     . GLU B 2 77   ? 132.964 101.178 144.588 1.00 85.01  ? 74   GLU A C     1 
ATOM   1145  O O     . GLU B 2 77   ? 132.753 101.149 143.369 1.00 83.95  ? 74   GLU A O     1 
ATOM   1146  C CB    . GLU B 2 77   ? 133.373 98.980  145.732 1.00 93.55  ? 74   GLU A CB    1 
ATOM   1147  C CG    . GLU B 2 77   ? 132.689 98.150  144.659 1.00 99.07  ? 74   GLU A CG    1 
ATOM   1148  C CD    . GLU B 2 77   ? 133.662 97.620  143.621 1.00 103.74 ? 74   GLU A CD    1 
ATOM   1149  O OE1   . GLU B 2 77   ? 134.832 97.362  143.976 1.00 105.48 ? 74   GLU A OE1   1 
ATOM   1150  O OE2   . GLU B 2 77   ? 133.257 97.465  142.449 1.00 105.20 ? 74   GLU A OE2   1 
ATOM   1151  N N     . ASN B 2 78   ? 132.296 101.994 145.405 1.00 83.74  ? 75   ASN A N     1 
ATOM   1152  C CA    . ASN B 2 78   ? 131.273 102.891 144.876 1.00 81.18  ? 75   ASN A CA    1 
ATOM   1153  C C     . ASN B 2 78   ? 131.887 103.964 143.985 1.00 76.47  ? 75   ASN A C     1 
ATOM   1154  O O     . ASN B 2 78   ? 131.316 104.318 142.948 1.00 75.05  ? 75   ASN A O     1 
ATOM   1155  C CB    . ASN B 2 78   ? 130.488 103.527 146.022 1.00 83.59  ? 75   ASN A CB    1 
ATOM   1156  C CG    . ASN B 2 78   ? 129.670 102.516 146.796 1.00 87.54  ? 75   ASN A CG    1 
ATOM   1157  O OD1   . ASN B 2 78   ? 128.471 102.359 146.562 1.00 88.15  ? 75   ASN A OD1   1 
ATOM   1158  N ND2   . ASN B 2 78   ? 130.315 101.818 147.724 1.00 89.66  ? 75   ASN A ND2   1 
ATOM   1159  N N     . LEU B 2 79   ? 133.048 104.493 144.375 1.00 73.26  ? 76   LEU A N     1 
ATOM   1160  C CA    . LEU B 2 79   ? 133.705 105.512 143.564 1.00 66.85  ? 76   LEU A CA    1 
ATOM   1161  C C     . LEU B 2 79   ? 134.156 104.943 142.224 1.00 62.54  ? 76   LEU A C     1 
ATOM   1162  O O     . LEU B 2 79   ? 134.074 105.623 141.195 1.00 61.31  ? 76   LEU A O     1 
ATOM   1163  C CB    . LEU B 2 79   ? 134.890 106.105 144.327 1.00 62.16  ? 76   LEU A CB    1 
ATOM   1164  C CG    . LEU B 2 79   ? 135.638 107.258 143.656 1.00 54.99  ? 76   LEU A CG    1 
ATOM   1165  C CD1   . LEU B 2 79   ? 134.684 108.392 143.317 1.00 50.61  ? 76   LEU A CD1   1 
ATOM   1166  C CD2   . LEU B 2 79   ? 136.760 107.752 144.554 1.00 53.62  ? 76   LEU A CD2   1 
ATOM   1167  N N     . SER B 2 80   ? 134.628 103.693 142.215 1.00 62.07  ? 77   SER A N     1 
ATOM   1168  C CA    . SER B 2 80   ? 135.047 103.072 140.963 1.00 61.99  ? 77   SER A CA    1 
ATOM   1169  C C     . SER B 2 80   ? 133.869 102.891 140.016 1.00 63.06  ? 77   SER A C     1 
ATOM   1170  O O     . SER B 2 80   ? 134.005 103.080 138.800 1.00 62.63  ? 77   SER A O     1 
ATOM   1171  C CB    . SER B 2 80   ? 135.715 101.726 141.243 1.00 64.84  ? 77   SER A CB    1 
ATOM   1172  O OG    . SER B 2 80   ? 136.027 101.049 140.038 1.00 66.14  ? 77   SER A OG    1 
ATOM   1173  N N     . ALA B 2 81   ? 132.702 102.525 140.552 1.00 63.69  ? 78   ALA A N     1 
ATOM   1174  C CA    . ALA B 2 81   ? 131.536 102.312 139.701 1.00 63.04  ? 78   ALA A CA    1 
ATOM   1175  C C     . ALA B 2 81   ? 131.056 103.621 139.085 1.00 59.75  ? 78   ALA A C     1 
ATOM   1176  O O     . ALA B 2 81   ? 130.578 103.637 137.945 1.00 61.45  ? 78   ALA A O     1 
ATOM   1177  C CB    . ALA B 2 81   ? 130.414 101.651 140.499 1.00 64.74  ? 78   ALA A CB    1 
ATOM   1178  N N     . ALA B 2 82   ? 131.165 104.726 139.827 1.00 56.33  ? 79   ALA A N     1 
ATOM   1179  C CA    . ALA B 2 82   ? 130.787 106.024 139.278 1.00 56.08  ? 79   ALA A CA    1 
ATOM   1180  C C     . ALA B 2 82   ? 131.763 106.481 138.200 1.00 58.12  ? 79   ALA A C     1 
ATOM   1181  O O     . ALA B 2 82   ? 131.359 107.152 137.243 1.00 57.56  ? 79   ALA A O     1 
ATOM   1182  C CB    . ALA B 2 82   ? 130.699 107.062 140.396 1.00 55.90  ? 79   ALA A CB    1 
ATOM   1183  N N     . ILE B 2 83   ? 133.043 106.133 138.339 1.00 60.17  ? 80   ILE A N     1 
ATOM   1184  C CA    . ILE B 2 83   ? 134.014 106.444 137.295 1.00 60.66  ? 80   ILE A CA    1 
ATOM   1185  C C     . ILE B 2 83   ? 133.745 105.604 136.053 1.00 57.88  ? 80   ILE A C     1 
ATOM   1186  O O     . ILE B 2 83   ? 133.806 106.104 134.922 1.00 56.54  ? 80   ILE A O     1 
ATOM   1187  C CB    . ILE B 2 83   ? 135.446 106.240 137.821 1.00 64.17  ? 80   ILE A CB    1 
ATOM   1188  C CG1   . ILE B 2 83   ? 135.729 107.191 138.986 1.00 41.39  ? 80   ILE A CG1   1 
ATOM   1189  C CG2   . ILE B 2 83   ? 136.465 106.447 136.711 1.00 40.42  ? 80   ILE A CG2   1 
ATOM   1190  C CD1   . ILE B 2 83   ? 137.111 107.033 139.579 1.00 41.07  ? 80   ILE A CD1   1 
ATOM   1191  N N     . ASP B 2 84   ? 133.434 104.318 136.241 1.00 57.17  ? 81   ASP A N     1 
ATOM   1192  C CA    . ASP B 2 84   ? 133.160 103.443 135.106 1.00 57.86  ? 81   ASP A CA    1 
ATOM   1193  C C     . ASP B 2 84   ? 131.915 103.887 134.349 1.00 57.68  ? 81   ASP A C     1 
ATOM   1194  O O     . ASP B 2 84   ? 131.902 103.896 133.112 1.00 55.78  ? 81   ASP A O     1 
ATOM   1195  C CB    . ASP B 2 84   ? 133.006 101.998 135.579 1.00 62.59  ? 81   ASP A CB    1 
ATOM   1196  C CG    . ASP B 2 84   ? 134.332 101.356 135.929 1.00 67.37  ? 81   ASP A CG    1 
ATOM   1197  O OD1   . ASP B 2 84   ? 135.329 102.092 136.067 1.00 66.53  ? 81   ASP A OD1   1 
ATOM   1198  O OD2   . ASP B 2 84   ? 134.375 100.116 136.071 1.00 71.57  ? 81   ASP A OD2   1 
ATOM   1199  N N     . SER B 2 85   ? 130.857 104.260 135.075 1.00 60.14  ? 82   SER A N     1 
ATOM   1200  C CA    . SER B 2 85   ? 129.612 104.645 134.419 1.00 61.49  ? 82   SER A CA    1 
ATOM   1201  C C     . SER B 2 85   ? 129.764 105.931 133.617 1.00 60.13  ? 82   SER A C     1 
ATOM   1202  O O     . SER B 2 85   ? 129.124 106.084 132.571 1.00 60.87  ? 82   SER A O     1 
ATOM   1203  C CB    . SER B 2 85   ? 128.496 104.796 135.453 1.00 61.30  ? 82   SER A CB    1 
ATOM   1204  O OG    . SER B 2 85   ? 128.098 103.534 135.965 1.00 61.66  ? 82   SER A OG    1 
ATOM   1205  N N     . TYR B 2 86   ? 130.602 106.862 134.080 1.00 58.96  ? 83   TYR A N     1 
ATOM   1206  C CA    . TYR B 2 86   ? 130.799 108.099 133.331 1.00 59.49  ? 83   TYR A CA    1 
ATOM   1207  C C     . TYR B 2 86   ? 131.625 107.853 132.072 1.00 60.01  ? 83   TYR A C     1 
ATOM   1208  O O     . TYR B 2 86   ? 131.360 108.454 131.025 1.00 60.47  ? 83   TYR A O     1 
ATOM   1209  C CB    . TYR B 2 86   ? 131.457 109.158 134.215 1.00 59.79  ? 83   TYR A CB    1 
ATOM   1210  C CG    . TYR B 2 86   ? 131.646 110.486 133.516 1.00 59.83  ? 83   TYR A CG    1 
ATOM   1211  C CD1   . TYR B 2 86   ? 130.599 111.081 132.825 1.00 61.96  ? 83   TYR A CD1   1 
ATOM   1212  C CD2   . TYR B 2 86   ? 132.866 111.147 133.552 1.00 56.76  ? 83   TYR A CD2   1 
ATOM   1213  C CE1   . TYR B 2 86   ? 130.763 112.293 132.180 1.00 61.29  ? 83   TYR A CE1   1 
ATOM   1214  C CE2   . TYR B 2 86   ? 133.040 112.362 132.914 1.00 56.87  ? 83   TYR A CE2   1 
ATOM   1215  C CZ    . TYR B 2 86   ? 131.984 112.929 132.230 1.00 60.40  ? 83   TYR A CZ    1 
ATOM   1216  O OH    . TYR B 2 86   ? 132.148 114.138 131.592 1.00 61.83  ? 83   TYR A OH    1 
ATOM   1217  N N     . ARG B 2 87   ? 132.630 106.978 132.157 1.00 60.14  ? 84   ARG A N     1 
ATOM   1218  C CA    . ARG B 2 87   ? 133.377 106.603 130.962 1.00 60.01  ? 84   ARG A CA    1 
ATOM   1219  C C     . ARG B 2 87   ? 132.536 105.742 130.026 1.00 61.04  ? 84   ARG A C     1 
ATOM   1220  O O     . ARG B 2 87   ? 132.747 105.763 128.808 1.00 55.45  ? 84   ARG A O     1 
ATOM   1221  C CB    . ARG B 2 87   ? 134.660 105.868 131.349 1.00 59.11  ? 84   ARG A CB    1 
ATOM   1222  C CG    . ARG B 2 87   ? 135.629 106.692 132.181 1.00 59.11  ? 84   ARG A CG    1 
ATOM   1223  C CD    . ARG B 2 87   ? 136.818 105.856 132.621 1.00 59.60  ? 84   ARG A CD    1 
ATOM   1224  N NE    . ARG B 2 87   ? 137.733 106.603 133.476 1.00 59.81  ? 84   ARG A NE    1 
ATOM   1225  C CZ    . ARG B 2 87   ? 138.766 106.065 134.117 1.00 60.93  ? 84   ARG A CZ    1 
ATOM   1226  N NH1   . ARG B 2 87   ? 139.013 104.767 134.002 1.00 61.84  ? 84   ARG A NH1   1 
ATOM   1227  N NH2   . ARG B 2 87   ? 139.548 106.820 134.876 1.00 59.37  ? 84   ARG A NH2   1 
ATOM   1228  N N     . LYS B 2 88   ? 131.588 104.983 130.575 1.00 66.49  ? 85   LYS A N     1 
ATOM   1229  C CA    . LYS B 2 88   ? 130.703 104.142 129.778 1.00 73.50  ? 85   LYS A CA    1 
ATOM   1230  C C     . LYS B 2 88   ? 129.726 105.011 128.993 1.00 78.32  ? 85   LYS A C     1 
ATOM   1231  O O     . LYS B 2 88   ? 129.802 105.083 127.762 1.00 77.46  ? 85   LYS A O     1 
ATOM   1232  C CB    . LYS B 2 88   ? 129.955 103.158 130.683 1.00 74.93  ? 85   LYS A CB    1 
ATOM   1233  C CG    . LYS B 2 88   ? 129.778 101.755 130.116 1.00 73.49  ? 85   LYS A CG    1 
ATOM   1234  C CD    . LYS B 2 88   ? 128.663 101.696 129.086 1.00 74.66  ? 85   LYS A CD    1 
ATOM   1235  C CE    . LYS B 2 88   ? 128.176 100.268 128.883 1.00 77.90  ? 85   LYS A CE    1 
ATOM   1236  N NZ    . LYS B 2 88   ? 129.288 99.335  128.544 1.00 78.09  ? 85   LYS A NZ    1 
ATOM   1237  N N     . GLU B 2 89   ? 128.811 105.672 129.694 1.00 85.09  ? 86   GLU A N     1 
ATOM   1238  C CA    . GLU B 2 89   ? 127.888 106.624 129.089 1.00 87.26  ? 86   GLU A CA    1 
ATOM   1239  C C     . GLU B 2 89   ? 128.368 108.042 129.370 1.00 86.95  ? 86   GLU A C     1 
ATOM   1240  O O     . GLU B 2 89   ? 128.592 108.408 130.528 1.00 87.92  ? 86   GLU A O     1 
ATOM   1241  C CB    . GLU B 2 89   ? 126.466 106.436 129.624 1.00 89.93  ? 86   GLU A CB    1 
ATOM   1242  C CG    . GLU B 2 89   ? 125.605 105.463 128.824 1.00 94.70  ? 86   GLU A CG    1 
ATOM   1243  C CD    . GLU B 2 89   ? 125.602 104.059 129.400 1.00 98.50  ? 86   GLU A CD    1 
ATOM   1244  O OE1   . GLU B 2 89   ? 126.367 103.802 130.354 1.00 99.08  ? 86   GLU A OE1   1 
ATOM   1245  O OE2   . GLU B 2 89   ? 124.827 103.214 128.902 1.00 100.51 ? 86   GLU A OE2   1 
ATOM   1246  N N     . LYS B 2 90   ? 128.523 108.834 128.313 1.00 85.57  ? 87   LYS A N     1 
ATOM   1247  C CA    . LYS B 2 90   ? 128.978 110.219 128.437 1.00 82.07  ? 87   LYS A CA    1 
ATOM   1248  C C     . LYS B 2 90   ? 127.802 111.184 128.567 1.00 81.28  ? 87   LYS A C     1 
ATOM   1249  O O     . LYS B 2 90   ? 127.718 112.192 127.869 1.00 82.27  ? 87   LYS A O     1 
ATOM   1250  C CB    . LYS B 2 90   ? 129.858 110.590 127.247 1.00 79.64  ? 87   LYS A CB    1 
ATOM   1251  C CG    . LYS B 2 90   ? 131.143 109.780 127.119 1.00 77.99  ? 87   LYS A CG    1 
ATOM   1252  C CD    . LYS B 2 90   ? 130.954 108.556 126.233 1.00 80.07  ? 87   LYS A CD    1 
ATOM   1253  C CE    . LYS B 2 90   ? 132.286 107.891 125.915 1.00 81.40  ? 87   LYS A CE    1 
ATOM   1254  N NZ    . LYS B 2 90   ? 133.011 107.476 127.147 1.00 82.33  ? 87   LYS A NZ    1 
ATOM   1255  N N     . THR B 2 91   ? 126.881 110.876 129.472 1.00 82.09  ? 88   THR A N     1 
ATOM   1256  C CA    . THR B 2 91   ? 125.701 111.698 129.695 1.00 83.14  ? 88   THR A CA    1 
ATOM   1257  C C     . THR B 2 91   ? 125.890 112.581 130.922 1.00 82.62  ? 88   THR A C     1 
ATOM   1258  O O     . THR B 2 91   ? 126.670 112.272 131.828 1.00 83.80  ? 88   THR A O     1 
ATOM   1259  C CB    . THR B 2 91   ? 124.449 110.829 129.858 1.00 87.46  ? 88   THR A CB    1 
ATOM   1260  O OG1   . THR B 2 91   ? 123.336 111.653 130.229 1.00 91.55  ? 88   THR A OG1   1 
ATOM   1261  C CG2   . THR B 2 91   ? 124.667 109.765 130.923 1.00 87.64  ? 88   THR A CG2   1 
ATOM   1262  N N     . GLU B 2 92   ? 125.160 113.700 130.936 1.00 81.31  ? 89   GLU A N     1 
ATOM   1263  C CA    . GLU B 2 92   ? 125.250 114.648 132.041 1.00 79.08  ? 89   GLU A CA    1 
ATOM   1264  C C     . GLU B 2 92   ? 124.735 114.066 133.351 1.00 78.11  ? 89   GLU A C     1 
ATOM   1265  O O     . GLU B 2 92   ? 125.068 114.588 134.420 1.00 77.47  ? 89   GLU A O     1 
ATOM   1266  C CB    . GLU B 2 92   ? 124.482 115.926 131.700 1.00 78.95  ? 89   GLU A CB    1 
ATOM   1267  N N     . GLU B 2 93   ? 123.928 113.005 133.294 1.00 76.90  ? 90   GLU A N     1 
ATOM   1268  C CA    . GLU B 2 93   ? 123.457 112.375 134.522 1.00 75.54  ? 90   GLU A CA    1 
ATOM   1269  C C     . GLU B 2 93   ? 124.581 111.609 135.210 1.00 73.52  ? 90   GLU A C     1 
ATOM   1270  O O     . GLU B 2 93   ? 124.703 111.648 136.440 1.00 71.81  ? 90   GLU A O     1 
ATOM   1271  C CB    . GLU B 2 93   ? 122.274 111.453 134.221 1.00 75.97  ? 90   GLU A CB    1 
ATOM   1272  C CG    . GLU B 2 93   ? 121.654 110.794 135.448 1.00 77.60  ? 90   GLU A CG    1 
ATOM   1273  C CD    . GLU B 2 93   ? 122.351 109.504 135.840 1.00 80.21  ? 90   GLU A CD    1 
ATOM   1274  O OE1   . GLU B 2 93   ? 122.827 108.786 134.935 1.00 79.93  ? 90   GLU A OE1   1 
ATOM   1275  O OE2   . GLU B 2 93   ? 122.430 109.216 137.051 1.00 82.82  ? 90   GLU A OE2   1 
ATOM   1276  N N     . THR B 2 94   ? 125.412 110.909 134.434 1.00 73.51  ? 91   THR A N     1 
ATOM   1277  C CA    . THR B 2 94   ? 126.528 110.179 135.024 1.00 73.44  ? 91   THR A CA    1 
ATOM   1278  C C     . THR B 2 94   ? 127.637 111.120 135.478 1.00 71.42  ? 91   THR A C     1 
ATOM   1279  O O     . THR B 2 94   ? 128.410 110.772 136.378 1.00 71.30  ? 91   THR A O     1 
ATOM   1280  C CB    . THR B 2 94   ? 127.076 109.153 134.032 1.00 75.50  ? 91   THR A CB    1 
ATOM   1281  O OG1   . THR B 2 94   ? 127.353 109.796 132.781 1.00 76.80  ? 91   THR A OG1   1 
ATOM   1282  C CG2   . THR B 2 94   ? 126.068 108.035 133.814 1.00 77.65  ? 91   THR A CG2   1 
ATOM   1283  N N     . ARG B 2 95   ? 127.733 112.305 134.874 1.00 72.07  ? 92   ARG A N     1 
ATOM   1284  C CA    . ARG B 2 95   ? 128.715 113.283 135.329 1.00 71.33  ? 92   ARG A CA    1 
ATOM   1285  C C     . ARG B 2 95   ? 128.337 113.832 136.698 1.00 69.67  ? 92   ARG A C     1 
ATOM   1286  O O     . ARG B 2 95   ? 129.168 113.869 137.614 1.00 70.46  ? 92   ARG A O     1 
ATOM   1287  C CB    . ARG B 2 95   ? 128.844 114.418 134.313 1.00 77.35  ? 92   ARG A CB    1 
ATOM   1288  C CG    . ARG B 2 95   ? 130.179 115.151 134.377 1.00 83.35  ? 92   ARG A CG    1 
ATOM   1289  C CD    . ARG B 2 95   ? 130.020 116.662 134.258 1.00 89.54  ? 92   ARG A CD    1 
ATOM   1290  N NE    . ARG B 2 95   ? 129.129 117.053 133.169 1.00 95.56  ? 92   ARG A NE    1 
ATOM   1291  C CZ    . ARG B 2 95   ? 127.921 117.577 133.347 1.00 100.09 ? 92   ARG A CZ    1 
ATOM   1292  N NH1   . ARG B 2 95   ? 127.459 117.785 134.573 1.00 102.26 ? 92   ARG A NH1   1 
ATOM   1293  N NH2   . ARG B 2 95   ? 127.174 117.901 132.298 1.00 100.52 ? 92   ARG A NH2   1 
ATOM   1294  N N     . ASN B 2 96   ? 127.081 114.259 136.857 1.00 67.36  ? 93   ASN A N     1 
ATOM   1295  C CA    . ASN B 2 96   ? 126.626 114.769 138.146 1.00 65.01  ? 93   ASN A CA    1 
ATOM   1296  C C     . ASN B 2 96   ? 126.653 113.686 139.214 1.00 60.28  ? 93   ASN A C     1 
ATOM   1297  O O     . ASN B 2 96   ? 126.858 113.984 140.397 1.00 58.84  ? 93   ASN A O     1 
ATOM   1298  C CB    . ASN B 2 96   ? 125.219 115.352 138.016 1.00 68.48  ? 93   ASN A CB    1 
ATOM   1299  C CG    . ASN B 2 96   ? 125.176 116.575 137.124 1.00 72.30  ? 93   ASN A CG    1 
ATOM   1300  O OD1   . ASN B 2 96   ? 126.149 116.895 136.440 1.00 72.69  ? 93   ASN A OD1   1 
ATOM   1301  N ND2   . ASN B 2 96   ? 124.043 117.267 137.123 1.00 75.13  ? 93   ASN A ND2   1 
ATOM   1302  N N     . ALA B 2 97   ? 126.439 112.428 138.825 1.00 58.13  ? 94   ALA A N     1 
ATOM   1303  C CA    . ALA B 2 97   ? 126.543 111.335 139.784 1.00 56.83  ? 94   ALA A CA    1 
ATOM   1304  C C     . ALA B 2 97   ? 127.977 111.165 140.266 1.00 56.60  ? 94   ALA A C     1 
ATOM   1305  O O     . ALA B 2 97   ? 128.213 110.894 141.449 1.00 57.66  ? 94   ALA A O     1 
ATOM   1306  C CB    . ALA B 2 97   ? 126.023 110.039 139.162 1.00 55.85  ? 94   ALA A CB    1 
ATOM   1307  N N     . LEU B 2 98   ? 128.949 111.328 139.366 1.00 55.31  ? 95   LEU A N     1 
ATOM   1308  C CA    . LEU B 2 98   ? 130.349 111.231 139.766 1.00 55.64  ? 95   LEU A CA    1 
ATOM   1309  C C     . LEU B 2 98   ? 130.769 112.431 140.605 1.00 56.49  ? 95   LEU A C     1 
ATOM   1310  O O     . LEU B 2 98   ? 131.534 112.285 141.565 1.00 57.90  ? 95   LEU A O     1 
ATOM   1311  C CB    . LEU B 2 98   ? 131.238 111.099 138.530 1.00 55.45  ? 95   LEU A CB    1 
ATOM   1312  C CG    . LEU B 2 98   ? 132.746 111.042 138.778 1.00 40.33  ? 95   LEU A CG    1 
ATOM   1313  C CD1   . LEU B 2 98   ? 133.093 109.919 139.741 1.00 43.74  ? 95   LEU A CD1   1 
ATOM   1314  C CD2   . LEU B 2 98   ? 133.497 110.878 137.469 1.00 39.45  ? 95   LEU A CD2   1 
ATOM   1315  N N     . ILE B 2 99   ? 130.276 113.624 140.262 1.00 55.24  ? 96   ILE A N     1 
ATOM   1316  C CA    . ILE B 2 99   ? 130.624 114.824 141.021 1.00 54.80  ? 96   ILE A CA    1 
ATOM   1317  C C     . ILE B 2 99   ? 130.116 114.715 142.453 1.00 57.37  ? 96   ILE A C     1 
ATOM   1318  O O     . ILE B 2 99   ? 130.812 115.092 143.404 1.00 57.51  ? 96   ILE A O     1 
ATOM   1319  C CB    . ILE B 2 99   ? 130.074 116.078 140.314 1.00 52.47  ? 96   ILE A CB    1 
ATOM   1320  C CG1   . ILE B 2 99   ? 130.780 116.285 138.973 1.00 48.58  ? 96   ILE A CG1   1 
ATOM   1321  C CG2   . ILE B 2 99   ? 130.232 117.306 141.198 1.00 52.51  ? 96   ILE A CG2   1 
ATOM   1322  C CD1   . ILE B 2 99   ? 130.273 117.477 138.193 1.00 46.40  ? 96   ILE A CD1   1 
ATOM   1323  N N     . GLU B 2 100  ? 128.900 114.195 142.633 1.00 61.07  ? 97   GLU A N     1 
ATOM   1324  C CA    . GLU B 2 100  ? 128.384 113.993 143.982 1.00 63.16  ? 97   GLU A CA    1 
ATOM   1325  C C     . GLU B 2 100  ? 129.135 112.878 144.700 1.00 61.32  ? 97   GLU A C     1 
ATOM   1326  O O     . GLU B 2 100  ? 129.407 112.981 145.902 1.00 61.31  ? 97   GLU A O     1 
ATOM   1327  C CB    . GLU B 2 100  ? 126.888 113.687 143.939 1.00 70.39  ? 97   GLU A CB    1 
ATOM   1328  C CG    . GLU B 2 100  ? 126.023 114.854 143.496 1.00 76.09  ? 97   GLU A CG    1 
ATOM   1329  C CD    . GLU B 2 100  ? 124.548 114.593 143.719 1.00 82.26  ? 97   GLU A CD    1 
ATOM   1330  O OE1   . GLU B 2 100  ? 124.213 113.550 144.318 1.00 84.96  ? 97   GLU A OE1   1 
ATOM   1331  O OE2   . GLU B 2 100  ? 123.723 115.431 143.295 1.00 83.79  ? 97   GLU A OE2   1 
ATOM   1332  N N     . GLU B 2 101  ? 129.474 111.806 143.980 1.00 60.35  ? 98   GLU A N     1 
ATOM   1333  C CA    . GLU B 2 101  ? 130.202 110.703 144.601 1.00 62.79  ? 98   GLU A CA    1 
ATOM   1334  C C     . GLU B 2 101  ? 131.582 111.149 145.063 1.00 60.33  ? 98   GLU A C     1 
ATOM   1335  O O     . GLU B 2 101  ? 132.056 110.730 146.126 1.00 59.75  ? 98   GLU A O     1 
ATOM   1336  C CB    . GLU B 2 101  ? 130.314 109.531 143.627 1.00 66.23  ? 98   GLU A CB    1 
ATOM   1337  C CG    . GLU B 2 101  ? 130.726 108.225 144.286 1.00 69.85  ? 98   GLU A CG    1 
ATOM   1338  C CD    . GLU B 2 101  ? 129.642 107.670 145.190 1.00 75.65  ? 98   GLU A CD    1 
ATOM   1339  O OE1   . GLU B 2 101  ? 128.453 107.783 144.826 1.00 78.48  ? 98   GLU A OE1   1 
ATOM   1340  O OE2   . GLU B 2 101  ? 129.976 107.127 146.264 1.00 78.09  ? 98   GLU A OE2   1 
ATOM   1341  N N     . GLN B 2 102  ? 132.244 112.002 144.275 1.00 57.89  ? 99   GLN A N     1 
ATOM   1342  C CA    . GLN B 2 102  ? 133.538 112.534 144.688 1.00 53.92  ? 99   GLN A CA    1 
ATOM   1343  C C     . GLN B 2 102  ? 133.398 113.435 145.910 1.00 53.36  ? 99   GLN A C     1 
ATOM   1344  O O     . GLN B 2 102  ? 134.218 113.369 146.833 1.00 53.06  ? 99   GLN A O     1 
ATOM   1345  C CB    . GLN B 2 102  ? 134.186 113.295 143.532 1.00 50.83  ? 99   GLN A CB    1 
ATOM   1346  C CG    . GLN B 2 102  ? 134.581 112.418 142.356 1.00 48.83  ? 99   GLN A CG    1 
ATOM   1347  C CD    . GLN B 2 102  ? 134.907 113.226 141.117 1.00 44.98  ? 99   GLN A CD    1 
ATOM   1348  O OE1   . GLN B 2 102  ? 134.674 114.434 141.070 1.00 46.87  ? 99   GLN A OE1   1 
ATOM   1349  N NE2   . GLN B 2 102  ? 135.448 112.562 140.101 1.00 42.28  ? 99   GLN A NE2   1 
ATOM   1350  N N     . ALA B 2 103  ? 132.363 114.278 145.933 1.00 53.05  ? 100  ALA A N     1 
ATOM   1351  C CA    . ALA B 2 103  ? 132.144 115.149 147.085 1.00 54.63  ? 100  ALA A CA    1 
ATOM   1352  C C     . ALA B 2 103  ? 131.859 114.347 148.348 1.00 57.18  ? 100  ALA A C     1 
ATOM   1353  O O     . ALA B 2 103  ? 132.241 114.766 149.446 1.00 58.73  ? 100  ALA A O     1 
ATOM   1354  C CB    . ALA B 2 103  ? 130.996 116.118 146.802 1.00 53.32  ? 100  ALA A CB    1 
ATOM   1355  N N     . THR B 2 104  ? 131.195 113.198 148.215 1.00 57.84  ? 101  THR A N     1 
ATOM   1356  C CA    . THR B 2 104  ? 130.947 112.349 149.374 1.00 60.57  ? 101  THR A CA    1 
ATOM   1357  C C     . THR B 2 104  ? 132.247 111.771 149.918 1.00 62.07  ? 101  THR A C     1 
ATOM   1358  O O     . THR B 2 104  ? 132.463 111.745 151.136 1.00 63.41  ? 101  THR A O     1 
ATOM   1359  C CB    . THR B 2 104  ? 129.971 111.228 149.008 1.00 61.73  ? 101  THR A CB    1 
ATOM   1360  O OG1   . THR B 2 104  ? 128.721 111.796 148.597 1.00 62.40  ? 101  THR A OG1   1 
ATOM   1361  C CG2   . THR B 2 104  ? 129.735 110.310 150.199 1.00 62.46  ? 101  THR A CG2   1 
ATOM   1362  N N     . TYR B 2 105  ? 133.131 111.309 149.030 1.00 61.96  ? 102  TYR A N     1 
ATOM   1363  C CA    . TYR B 2 105  ? 134.404 110.750 149.479 1.00 63.27  ? 102  TYR A CA    1 
ATOM   1364  C C     . TYR B 2 105  ? 135.316 111.826 150.053 1.00 62.70  ? 102  TYR A C     1 
ATOM   1365  O O     . TYR B 2 105  ? 136.047 111.574 151.017 1.00 63.79  ? 102  TYR A O     1 
ATOM   1366  C CB    . TYR B 2 105  ? 135.091 110.016 148.326 1.00 63.32  ? 102  TYR A CB    1 
ATOM   1367  C CG    . TYR B 2 105  ? 134.671 108.571 148.185 1.00 64.22  ? 102  TYR A CG    1 
ATOM   1368  C CD1   . TYR B 2 105  ? 133.570 108.218 147.416 1.00 64.37  ? 102  TYR A CD1   1 
ATOM   1369  C CD2   . TYR B 2 105  ? 135.377 107.559 148.822 1.00 64.75  ? 102  TYR A CD2   1 
ATOM   1370  C CE1   . TYR B 2 105  ? 133.184 106.897 147.286 1.00 65.84  ? 102  TYR A CE1   1 
ATOM   1371  C CE2   . TYR B 2 105  ? 134.999 106.235 148.696 1.00 66.56  ? 102  TYR A CE2   1 
ATOM   1372  C CZ    . TYR B 2 105  ? 133.903 105.910 147.926 1.00 66.41  ? 102  TYR A CZ    1 
ATOM   1373  O OH    . TYR B 2 105  ? 133.522 104.593 147.799 1.00 66.14  ? 102  TYR A OH    1 
ATOM   1374  N N     . ARG B 2 106  ? 135.292 113.031 149.473 1.00 60.46  ? 103  ARG A N     1 
ATOM   1375  C CA    . ARG B 2 106  ? 136.107 114.117 150.011 1.00 59.30  ? 103  ARG A CA    1 
ATOM   1376  C C     . ARG B 2 106  ? 135.682 114.470 151.431 1.00 61.36  ? 103  ARG A C     1 
ATOM   1377  O O     . ARG B 2 106  ? 136.528 114.754 152.288 1.00 62.56  ? 103  ARG A O     1 
ATOM   1378  C CB    . ARG B 2 106  ? 136.026 115.347 149.105 1.00 56.63  ? 103  ARG A CB    1 
ATOM   1379  C CG    . ARG B 2 106  ? 136.663 115.168 147.736 1.00 51.75  ? 103  ARG A CG    1 
ATOM   1380  C CD    . ARG B 2 106  ? 136.857 116.504 147.035 1.00 47.67  ? 103  ARG A CD    1 
ATOM   1381  N NE    . ARG B 2 106  ? 135.627 117.291 146.985 1.00 49.19  ? 103  ARG A NE    1 
ATOM   1382  C CZ    . ARG B 2 106  ? 134.775 117.286 145.966 1.00 50.08  ? 103  ARG A CZ    1 
ATOM   1383  N NH1   . ARG B 2 106  ? 135.016 116.536 144.898 1.00 50.40  ? 103  ARG A NH1   1 
ATOM   1384  N NH2   . ARG B 2 106  ? 133.682 118.035 146.009 1.00 49.39  ? 103  ARG A NH2   1 
ATOM   1385  N N     . ASN B 2 107  ? 134.374 114.451 151.700 1.00 61.62  ? 104  ASN A N     1 
ATOM   1386  C CA    . ASN B 2 107  ? 133.898 114.709 153.056 1.00 63.17  ? 104  ASN A CA    1 
ATOM   1387  C C     . ASN B 2 107  ? 134.257 113.569 154.000 1.00 65.54  ? 104  ASN A C     1 
ATOM   1388  O O     . ASN B 2 107  ? 134.502 113.808 155.189 1.00 68.30  ? 104  ASN A O     1 
ATOM   1389  C CB    . ASN B 2 107  ? 132.386 114.939 153.051 1.00 65.58  ? 104  ASN A CB    1 
ATOM   1390  C CG    . ASN B 2 107  ? 131.996 116.240 152.377 1.00 68.26  ? 104  ASN A CG    1 
ATOM   1391  O OD1   . ASN B 2 107  ? 132.683 117.253 152.509 1.00 70.18  ? 104  ASN A OD1   1 
ATOM   1392  N ND2   . ASN B 2 107  ? 130.885 116.219 151.647 1.00 68.13  ? 104  ASN A ND2   1 
ATOM   1393  N N     . ALA B 2 108  ? 134.291 112.332 153.498 1.00 67.05  ? 105  ALA A N     1 
ATOM   1394  C CA    . ALA B 2 108  ? 134.688 111.204 154.333 1.00 70.46  ? 105  ALA A CA    1 
ATOM   1395  C C     . ALA B 2 108  ? 136.125 111.355 154.813 1.00 71.65  ? 105  ALA A C     1 
ATOM   1396  O O     . ALA B 2 108  ? 136.444 111.016 155.960 1.00 74.61  ? 105  ALA A O     1 
ATOM   1397  C CB    . ALA B 2 108  ? 134.511 109.893 153.568 1.00 70.09  ? 105  ALA A CB    1 
ATOM   1398  N N     . ILE B 2 109  ? 137.008 111.861 153.949 1.00 68.34  ? 106  ILE A N     1 
ATOM   1399  C CA    . ILE B 2 109  ? 138.370 112.168 154.373 1.00 66.72  ? 106  ILE A CA    1 
ATOM   1400  C C     . ILE B 2 109  ? 138.377 113.386 155.288 1.00 70.90  ? 106  ILE A C     1 
ATOM   1401  O O     . ILE B 2 109  ? 139.127 113.440 156.271 1.00 72.92  ? 106  ILE A O     1 
ATOM   1402  C CB    . ILE B 2 109  ? 139.274 112.382 153.145 1.00 60.73  ? 106  ILE A CB    1 
ATOM   1403  C CG1   . ILE B 2 109  ? 139.098 111.242 152.139 1.00 59.82  ? 106  ILE A CG1   1 
ATOM   1404  C CG2   . ILE B 2 109  ? 140.731 112.503 153.571 1.00 58.67  ? 106  ILE A CG2   1 
ATOM   1405  C CD1   . ILE B 2 109  ? 139.545 109.895 152.651 1.00 61.82  ? 106  ILE A CD1   1 
ATOM   1406  N N     . HIS B 2 110  ? 137.537 114.381 154.982 1.00 71.32  ? 107  HIS A N     1 
ATOM   1407  C CA    . HIS B 2 110  ? 137.491 115.600 155.781 1.00 72.60  ? 107  HIS A CA    1 
ATOM   1408  C C     . HIS B 2 110  ? 137.020 115.326 157.202 1.00 76.50  ? 107  HIS A C     1 
ATOM   1409  O O     . HIS B 2 110  ? 137.457 116.001 158.141 1.00 78.56  ? 107  HIS A O     1 
ATOM   1410  C CB    . HIS B 2 110  ? 136.575 116.623 155.106 1.00 70.77  ? 107  HIS A CB    1 
ATOM   1411  C CG    . HIS B 2 110  ? 136.608 117.981 155.735 1.00 71.02  ? 107  HIS A CG    1 
ATOM   1412  N ND1   . HIS B 2 110  ? 137.688 118.828 155.621 1.00 71.06  ? 107  HIS A ND1   1 
ATOM   1413  C CD2   . HIS B 2 110  ? 135.687 118.643 156.475 1.00 71.82  ? 107  HIS A CD2   1 
ATOM   1414  C CE1   . HIS B 2 110  ? 137.434 119.953 156.268 1.00 71.62  ? 107  HIS A CE1   1 
ATOM   1415  N NE2   . HIS B 2 110  ? 136.226 119.865 156.794 1.00 72.27  ? 107  HIS A NE2   1 
ATOM   1416  N N     . ASP B 2 111  ? 136.133 114.344 157.382 1.00 78.28  ? 108  ASP A N     1 
ATOM   1417  C CA    . ASP B 2 111  ? 135.643 114.021 158.717 1.00 80.94  ? 108  ASP A CA    1 
ATOM   1418  C C     . ASP B 2 111  ? 136.731 113.429 159.605 1.00 84.57  ? 108  ASP A C     1 
ATOM   1419  O O     . ASP B 2 111  ? 136.602 113.477 160.831 1.00 86.53  ? 108  ASP A O     1 
ATOM   1420  C CB    . ASP B 2 111  ? 134.455 113.060 158.623 1.00 81.41  ? 108  ASP A CB    1 
ATOM   1421  C CG    . ASP B 2 111  ? 133.236 113.701 157.983 1.00 80.91  ? 108  ASP A CG    1 
ATOM   1422  O OD1   . ASP B 2 111  ? 133.134 114.947 158.003 1.00 80.12  ? 108  ASP A OD1   1 
ATOM   1423  O OD2   . ASP B 2 111  ? 132.375 112.959 157.463 1.00 81.63  ? 108  ASP A OD2   1 
ATOM   1424  N N     . TYR B 2 112  ? 137.794 112.872 159.018 1.00 84.67  ? 109  TYR A N     1 
ATOM   1425  C CA    . TYR B 2 112  ? 138.942 112.463 159.821 1.00 84.08  ? 109  TYR A CA    1 
ATOM   1426  C C     . TYR B 2 112  ? 139.696 113.668 160.369 1.00 81.45  ? 109  TYR A C     1 
ATOM   1427  O O     . TYR B 2 112  ? 140.239 113.608 161.478 1.00 82.19  ? 109  TYR A O     1 
ATOM   1428  C CB    . TYR B 2 112  ? 139.879 111.581 158.993 1.00 82.25  ? 109  TYR A CB    1 
ATOM   1429  C CG    . TYR B 2 112  ? 139.497 110.117 158.973 1.00 83.64  ? 109  TYR A CG    1 
ATOM   1430  C CD1   . TYR B 2 112  ? 138.488 109.652 158.141 1.00 83.07  ? 109  TYR A CD1   1 
ATOM   1431  C CD2   . TYR B 2 112  ? 140.151 109.199 159.784 1.00 86.48  ? 109  TYR A CD2   1 
ATOM   1432  C CE1   . TYR B 2 112  ? 138.137 108.313 158.120 1.00 84.08  ? 109  TYR A CE1   1 
ATOM   1433  C CE2   . TYR B 2 112  ? 139.808 107.860 159.770 1.00 87.75  ? 109  TYR A CE2   1 
ATOM   1434  C CZ    . TYR B 2 112  ? 138.801 107.422 158.936 1.00 86.17  ? 109  TYR A CZ    1 
ATOM   1435  O OH    . TYR B 2 112  ? 138.458 106.089 158.919 1.00 86.77  ? 109  TYR A OH    1 
ATOM   1436  N N     . PHE B 2 113  ? 139.780 114.737 159.569 1.00 78.56  ? 110  PHE A N     1 
ATOM   1437  C CA    . PHE B 2 113  ? 140.482 115.973 160.007 1.00 74.76  ? 110  PHE A CA    1 
ATOM   1438  C C     . PHE B 2 113  ? 139.563 116.752 160.947 1.00 74.35  ? 110  PHE A C     1 
ATOM   1439  O O     . PHE B 2 113  ? 139.975 117.038 162.084 1.00 73.98  ? 110  PHE A O     1 
ATOM   1440  C CB    . PHE B 2 113  ? 140.867 116.839 158.806 1.00 72.17  ? 110  PHE A CB    1 
ATOM   1441  C CG    . PHE B 2 113  ? 141.788 116.179 157.811 1.00 70.91  ? 110  PHE A CG    1 
ATOM   1442  C CD1   . PHE B 2 113  ? 143.108 115.912 158.135 1.00 72.33  ? 110  PHE A CD1   1 
ATOM   1443  C CD2   . PHE B 2 113  ? 141.340 115.843 156.544 1.00 69.41  ? 110  PHE A CD2   1 
ATOM   1444  C CE1   . PHE B 2 113  ? 143.956 115.311 157.219 1.00 70.99  ? 110  PHE A CE1   1 
ATOM   1445  C CE2   . PHE B 2 113  ? 142.189 115.244 155.627 1.00 68.24  ? 110  PHE A CE2   1 
ATOM   1446  C CZ    . PHE B 2 113  ? 143.496 114.979 155.966 1.00 69.17  ? 110  PHE A CZ    1 
ATOM   1447  N N     . ILE B 2 114  ? 138.371 117.117 160.469 1.00 74.31  ? 111  ILE A N     1 
ATOM   1448  C CA    . ILE B 2 114  ? 137.365 117.798 161.338 1.00 74.06  ? 111  ILE A CA    1 
ATOM   1449  C C     . ILE B 2 114  ? 135.989 117.286 160.901 1.00 75.11  ? 111  ILE A C     1 
ATOM   1450  O O     . ILE B 2 114  ? 135.321 117.959 160.091 1.00 75.36  ? 111  ILE A O     1 
ATOM   1451  C CB    . ILE B 2 114  ? 137.506 119.336 161.280 1.00 69.34  ? 111  ILE A CB    1 
ATOM   1452  C CG1   . ILE B 2 114  ? 136.357 120.041 162.009 1.00 67.28  ? 111  ILE A CG1   1 
ATOM   1453  C CG2   . ILE B 2 114  ? 137.666 119.828 159.849 1.00 65.32  ? 111  ILE A CG2   1 
ATOM   1454  C CD1   . ILE B 2 114  ? 136.307 121.533 161.787 1.00 64.89  ? 111  ILE A CD1   1 
ATOM   1455  N N     . GLY B 2 115  ? 135.601 116.106 161.390 1.00 76.02  ? 112  GLY A N     1 
ATOM   1456  C CA    . GLY B 2 115  ? 134.330 115.500 160.949 1.00 78.49  ? 112  GLY A CA    1 
ATOM   1457  C C     . GLY B 2 115  ? 133.122 116.180 161.554 1.00 81.82  ? 112  GLY A C     1 
ATOM   1458  O O     . GLY B 2 115  ? 132.161 116.437 160.802 1.00 84.29  ? 112  GLY A O     1 
ATOM   1459  N N     . ARG B 2 116  ? 133.162 116.462 162.859 1.00 84.28  ? 113  ARG A N     1 
ATOM   1460  C CA    . ARG B 2 116  ? 131.964 117.035 163.527 1.00 87.18  ? 113  ARG A CA    1 
ATOM   1461  C C     . ARG B 2 116  ? 130.762 116.218 163.050 1.00 88.25  ? 113  ARG A C     1 
ATOM   1462  O O     . ARG B 2 116  ? 129.674 116.806 162.898 1.00 87.26  ? 113  ARG A O     1 
ATOM   1463  C CB    . ARG B 2 116  ? 131.804 118.518 163.179 1.00 86.81  ? 113  ARG A CB    1 
ATOM   1464  C CG    . ARG B 2 116  ? 132.927 119.411 163.687 1.00 89.08  ? 113  ARG A CG    1 
ATOM   1465  C CD    . ARG B 2 116  ? 132.775 119.730 165.161 1.00 90.55  ? 113  ARG A CD    1 
ATOM   1466  N NE    . ARG B 2 116  ? 133.598 120.862 165.562 1.00 94.37  ? 113  ARG A NE    1 
ATOM   1467  C CZ    . ARG B 2 116  ? 133.598 121.398 166.777 1.00 99.89  ? 113  ARG A CZ    1 
ATOM   1468  N NH1   . ARG B 2 116  ? 132.815 120.902 167.719 1.00 102.79 ? 113  ARG A NH1   1 
ATOM   1469  N NH2   . ARG B 2 116  ? 134.382 122.426 167.046 1.00 100.99 ? 113  ARG A NH2   1 
ATOM   1470  N N     . THR B 2 117  ? 130.959 114.915 162.821 1.00 90.66  ? 114  THR A N     1 
ATOM   1471  C CA    . THR B 2 117  ? 129.876 114.063 162.261 1.00 93.05  ? 114  THR A CA    1 
ATOM   1472  C C     . THR B 2 117  ? 129.592 112.892 163.202 1.00 97.06  ? 114  THR A C     1 
ATOM   1473  O O     . THR B 2 117  ? 130.096 112.916 164.343 1.00 97.34  ? 114  THR A O     1 
ATOM   1474  C CB    . THR B 2 117  ? 130.260 113.546 160.870 1.00 93.92  ? 114  THR A CB    1 
ATOM   1475  O OG1   . THR B 2 117  ? 129.157 112.812 160.338 1.00 95.05  ? 114  THR A OG1   1 
ATOM   1476  C CG2   . THR B 2 117  ? 131.493 112.669 160.893 1.00 95.80  ? 114  THR A CG2   1 
ATOM   1477  N N     . ASP B 2 118  ? 128.821 111.907 162.733 1.00 100.12 ? 115  ASP A N     1 
ATOM   1478  C CA    . ASP B 2 118  ? 128.442 110.746 163.582 1.00 104.58 ? 115  ASP A CA    1 
ATOM   1479  C C     . ASP B 2 118  ? 129.100 109.486 163.013 1.00 105.97 ? 115  ASP A C     1 
ATOM   1480  O O     . ASP B 2 118  ? 129.105 108.456 163.714 1.00 107.71 ? 115  ASP A O     1 
ATOM   1481  C CB    . ASP B 2 118  ? 126.922 110.604 163.682 1.00 104.27 ? 115  ASP A CB    1 
ATOM   1482  C CG    . ASP B 2 118  ? 126.240 111.835 164.253 1.00 103.27 ? 115  ASP A CG    1 
ATOM   1483  O OD1   . ASP B 2 118  ? 126.958 112.791 164.608 1.00 103.23 ? 115  ASP A OD1   1 
ATOM   1484  O OD2   . ASP B 2 118  ? 124.996 111.829 164.337 1.00 102.66 ? 115  ASP A OD2   1 
ATOM   1485  N N     . ASN B 2 119  ? 129.638 109.575 161.792 1.00 106.41 ? 116  ASN A N     1 
ATOM   1486  C CA    . ASN B 2 119  ? 130.285 108.404 161.141 1.00 110.52 ? 116  ASN A CA    1 
ATOM   1487  C C     . ASN B 2 119  ? 131.466 107.943 161.999 1.00 114.11 ? 116  ASN A C     1 
ATOM   1488  O O     . ASN B 2 119  ? 131.586 106.724 162.230 1.00 116.13 ? 116  ASN A O     1 
ATOM   1489  C CB    . ASN B 2 119  ? 130.734 108.730 159.716 1.00 110.84 ? 116  ASN A CB    1 
ATOM   1490  C CG    . ASN B 2 119  ? 129.646 109.387 158.892 1.00 111.20 ? 116  ASN A CG    1 
ATOM   1491  O OD1   . ASN B 2 119  ? 128.522 109.554 159.360 1.00 113.05 ? 116  ASN A OD1   1 
ATOM   1492  N ND2   . ASN B 2 119  ? 129.972 109.764 157.667 1.00 108.73 ? 116  ASN A ND2   1 
ATOM   1493  N N     . LEU B 2 120  ? 132.297 108.885 162.453 1.00 114.46 ? 117  LEU A N     1 
ATOM   1494  C CA    . LEU B 2 120  ? 133.450 108.536 163.325 1.00 115.36 ? 117  LEU A CA    1 
ATOM   1495  C C     . LEU B 2 120  ? 133.022 108.656 164.790 1.00 117.05 ? 117  LEU A C     1 
ATOM   1496  O O     . LEU B 2 120  ? 132.303 109.621 165.117 1.00 114.30 ? 117  LEU A O     1 
ATOM   1497  C CB    . LEU B 2 120  ? 134.619 109.478 163.017 1.00 113.00 ? 117  LEU A CB    1 
ATOM   1498  C CG    . LEU B 2 120  ? 135.228 109.334 161.624 1.00 110.16 ? 117  LEU A CG    1 
ATOM   1499  C CD1   . LEU B 2 120  ? 136.461 110.213 161.485 1.00 108.32 ? 117  LEU A CD1   1 
ATOM   1500  C CD2   . LEU B 2 120  ? 135.579 107.883 161.336 1.00 111.92 ? 117  LEU A CD2   1 
ATOM   1501  N N     . THR B 2 121  ? 133.449 107.710 165.632 1.00 120.81 ? 118  THR A N     1 
ATOM   1502  C CA    . THR B 2 121  ? 133.124 107.773 167.081 1.00 122.13 ? 118  THR A CA    1 
ATOM   1503  C C     . THR B 2 121  ? 133.645 109.096 167.644 1.00 120.17 ? 118  THR A C     1 
ATOM   1504  O O     . THR B 2 121  ? 134.806 109.438 167.353 1.00 119.17 ? 118  THR A O     1 
ATOM   1505  C CB    . THR B 2 121  ? 133.730 106.585 167.835 1.00 123.23 ? 118  THR A CB    1 
ATOM   1506  O OG1   . THR B 2 121  ? 135.150 106.743 167.835 1.00 121.30 ? 118  THR A OG1   1 
ATOM   1507  C CG2   . THR B 2 121  ? 133.360 105.250 167.226 1.00 123.88 ? 118  THR A CG2   1 
ATOM   1508  N N     . ASP B 2 122  ? 132.823 109.798 168.429 1.00 120.85 ? 119  ASP A N     1 
ATOM   1509  C CA    . ASP B 2 122  ? 133.217 111.126 168.970 1.00 120.25 ? 119  ASP A CA    1 
ATOM   1510  C C     . ASP B 2 122  ? 134.528 110.974 169.745 1.00 120.86 ? 119  ASP A C     1 
ATOM   1511  O O     . ASP B 2 122  ? 135.382 111.873 169.633 1.00 116.86 ? 119  ASP A O     1 
ATOM   1512  C CB    . ASP B 2 122  ? 132.099 111.735 169.820 1.00 123.00 ? 119  ASP A CB    1 
ATOM   1513  C CG    . ASP B 2 122  ? 130.831 112.001 169.029 1.00 123.51 ? 119  ASP A CG    1 
ATOM   1514  O OD1   . ASP B 2 122  ? 130.832 111.727 167.812 1.00 123.76 ? 119  ASP A OD1   1 
ATOM   1515  O OD2   . ASP B 2 122  ? 129.853 112.481 169.636 1.00 123.23 ? 119  ASP A OD2   1 
ATOM   1516  N N     . ALA B 2 123  ? 134.679 109.881 170.499 1.00 124.96 ? 120  ALA A N     1 
ATOM   1517  C CA    . ALA B 2 123  ? 135.954 109.628 171.209 1.00 125.52 ? 120  ALA A CA    1 
ATOM   1518  C C     . ALA B 2 123  ? 137.114 110.026 170.293 1.00 122.28 ? 120  ALA A C     1 
ATOM   1519  O O     . ALA B 2 123  ? 138.125 110.540 170.808 1.00 123.01 ? 120  ALA A O     1 
ATOM   1520  C CB    . ALA B 2 123  ? 136.040 108.177 171.609 1.00 127.62 ? 120  ALA A CB    1 
ATOM   1521  N N     . ILE B 2 124  ? 136.965 109.797 168.984 1.00 118.43 ? 121  ILE A N     1 
ATOM   1522  C CA    . ILE B 2 124  ? 138.006 110.166 168.031 1.00 113.10 ? 121  ILE A CA    1 
ATOM   1523  C C     . ILE B 2 124  ? 137.577 111.379 167.215 1.00 108.01 ? 121  ILE A C     1 
ATOM   1524  O O     . ILE B 2 124  ? 138.394 112.248 166.887 1.00 106.68 ? 121  ILE A O     1 
ATOM   1525  C CB    . ILE B 2 124  ? 138.346 108.967 167.127 1.00 114.71 ? 121  ILE A CB    1 
ATOM   1526  C CG1   . ILE B 2 124  ? 138.701 107.745 167.974 1.00 118.87 ? 121  ILE A CG1   1 
ATOM   1527  C CG2   . ILE B 2 124  ? 139.487 109.313 166.181 1.00 113.27 ? 121  ILE A CG2   1 
ATOM   1528  C CD1   . ILE B 2 124  ? 138.967 106.496 167.160 1.00 119.43 ? 121  ILE A CD1   1 
ATOM   1529  N N     . ASN B 2 125  ? 136.286 111.464 166.885 1.00 102.76 ? 122  ASN A N     1 
ATOM   1530  C CA    . ASN B 2 125  ? 135.801 112.545 166.037 1.00 97.74  ? 122  ASN A CA    1 
ATOM   1531  C C     . ASN B 2 125  ? 135.889 113.895 166.742 1.00 96.00  ? 122  ASN A C     1 
ATOM   1532  O O     . ASN B 2 125  ? 136.223 114.908 166.114 1.00 96.25  ? 122  ASN A O     1 
ATOM   1533  C CB    . ASN B 2 125  ? 134.363 112.256 165.604 1.00 98.17  ? 122  ASN A CB    1 
ATOM   1534  C CG    . ASN B 2 125  ? 133.863 113.215 164.551 1.00 97.33  ? 122  ASN A CG    1 
ATOM   1535  O OD1   . ASN B 2 125  ? 134.079 113.008 163.355 1.00 95.67  ? 122  ASN A OD1   1 
ATOM   1536  N ND2   . ASN B 2 125  ? 133.180 114.266 164.985 1.00 98.25  ? 122  ASN A ND2   1 
ATOM   1537  N N     . LYS B 2 126  ? 135.599 113.931 168.042 1.00 95.44  ? 123  LYS A N     1 
ATOM   1538  C CA    . LYS B 2 126  ? 135.651 115.191 168.779 1.00 92.61  ? 123  LYS A CA    1 
ATOM   1539  C C     . LYS B 2 126  ? 137.080 115.606 169.106 1.00 91.88  ? 123  LYS A C     1 
ATOM   1540  O O     . LYS B 2 126  ? 137.351 116.802 169.259 1.00 86.71  ? 123  LYS A O     1 
ATOM   1541  C CB    . LYS B 2 126  ? 134.828 115.085 170.065 1.00 94.32  ? 123  LYS A CB    1 
ATOM   1542  N N     . ARG B 2 127  ? 137.999 114.644 169.217 1.00 95.36  ? 124  ARG A N     1 
ATOM   1543  C CA    . ARG B 2 127  ? 139.387 114.978 169.520 1.00 94.83  ? 124  ARG A CA    1 
ATOM   1544  C C     . ARG B 2 127  ? 140.036 115.769 168.391 1.00 92.57  ? 124  ARG A C     1 
ATOM   1545  O O     . ARG B 2 127  ? 140.897 116.618 168.648 1.00 93.81  ? 124  ARG A O     1 
ATOM   1546  C CB    . ARG B 2 127  ? 140.186 113.706 169.802 1.00 94.10  ? 124  ARG A CB    1 
ATOM   1547  N N     . HIS B 2 128  ? 139.639 115.507 167.143 1.00 90.07  ? 125  HIS A N     1 
ATOM   1548  C CA    . HIS B 2 128  ? 140.184 116.262 166.021 1.00 87.44  ? 125  HIS A CA    1 
ATOM   1549  C C     . HIS B 2 128  ? 139.673 117.698 166.008 1.00 88.43  ? 125  HIS A C     1 
ATOM   1550  O O     . HIS B 2 128  ? 140.403 118.608 165.598 1.00 86.28  ? 125  HIS A O     1 
ATOM   1551  C CB    . HIS B 2 128  ? 139.839 115.569 164.704 1.00 88.75  ? 125  HIS A CB    1 
ATOM   1552  C CG    . HIS B 2 128  ? 140.520 114.247 164.520 1.00 93.75  ? 125  HIS A CG    1 
ATOM   1553  N ND1   . HIS B 2 128  ? 140.022 113.264 163.692 1.00 94.52  ? 125  HIS A ND1   1 
ATOM   1554  C CD2   . HIS B 2 128  ? 141.661 113.750 165.051 1.00 96.27  ? 125  HIS A CD2   1 
ATOM   1555  C CE1   . HIS B 2 128  ? 140.825 112.215 163.725 1.00 94.82  ? 125  HIS A CE1   1 
ATOM   1556  N NE2   . HIS B 2 128  ? 141.827 112.485 164.543 1.00 95.91  ? 125  HIS A NE2   1 
ATOM   1557  N N     . ALA B 2 129  ? 138.432 117.919 166.448 1.00 91.97  ? 126  ALA A N     1 
ATOM   1558  C CA    . ALA B 2 129  ? 137.882 119.271 166.456 1.00 92.28  ? 126  ALA A CA    1 
ATOM   1559  C C     . ALA B 2 129  ? 138.604 120.158 167.461 1.00 94.29  ? 126  ALA A C     1 
ATOM   1560  O O     . ALA B 2 129  ? 138.795 121.355 167.216 1.00 91.61  ? 126  ALA A O     1 
ATOM   1561  C CB    . ALA B 2 129  ? 136.384 119.225 166.757 1.00 92.60  ? 126  ALA A CB    1 
ATOM   1562  N N     . GLU B 2 130  ? 139.010 119.593 168.602 1.00 99.36  ? 127  GLU A N     1 
ATOM   1563  C CA    . GLU B 2 130  ? 139.758 120.362 169.588 1.00 103.55 ? 127  GLU A CA    1 
ATOM   1564  C C     . GLU B 2 130  ? 141.130 120.773 169.072 1.00 104.67 ? 127  GLU A C     1 
ATOM   1565  O O     . GLU B 2 130  ? 141.708 121.741 169.580 1.00 104.69 ? 127  GLU A O     1 
ATOM   1566  C CB    . GLU B 2 130  ? 139.904 119.560 170.883 1.00 107.12 ? 127  GLU A CB    1 
ATOM   1567  N N     . ILE B 2 131  ? 141.655 120.063 168.079 1.00 107.27 ? 128  ILE A N     1 
ATOM   1568  C CA    . ILE B 2 131  ? 142.936 120.411 167.473 1.00 105.30 ? 128  ILE A CA    1 
ATOM   1569  C C     . ILE B 2 131  ? 142.752 121.380 166.314 1.00 100.49 ? 128  ILE A C     1 
ATOM   1570  O O     . ILE B 2 131  ? 143.471 122.374 166.200 1.00 100.10 ? 128  ILE A O     1 
ATOM   1571  C CB    . ILE B 2 131  ? 143.666 119.130 167.020 1.00 106.95 ? 128  ILE A CB    1 
ATOM   1572  C CG1   . ILE B 2 131  ? 143.856 118.184 168.206 1.00 110.84 ? 128  ILE A CG1   1 
ATOM   1573  C CG2   . ILE B 2 131  ? 144.999 119.476 166.376 1.00 106.26 ? 128  ILE A CG2   1 
ATOM   1574  C CD1   . ILE B 2 131  ? 144.494 116.867 167.832 1.00 111.75 ? 128  ILE A CD1   1 
ATOM   1575  N N     . TYR B 2 132  ? 141.782 121.104 165.434 1.00 94.08  ? 129  TYR A N     1 
ATOM   1576  C CA    . TYR B 2 132  ? 141.557 121.961 164.277 1.00 86.96  ? 129  TYR A CA    1 
ATOM   1577  C C     . TYR B 2 132  ? 141.077 123.349 164.677 1.00 82.73  ? 129  TYR A C     1 
ATOM   1578  O O     . TYR B 2 132  ? 141.278 124.304 163.919 1.00 81.42  ? 129  TYR A O     1 
ATOM   1579  C CB    . TYR B 2 132  ? 140.548 121.305 163.331 1.00 84.76  ? 129  TYR A CB    1 
ATOM   1580  C CG    . TYR B 2 132  ? 140.439 121.971 161.975 1.00 81.18  ? 129  TYR A CG    1 
ATOM   1581  C CD1   . TYR B 2 132  ? 141.287 121.615 160.935 1.00 78.83  ? 129  TYR A CD1   1 
ATOM   1582  C CD2   . TYR B 2 132  ? 139.481 122.947 161.735 1.00 79.94  ? 129  TYR A CD2   1 
ATOM   1583  C CE1   . TYR B 2 132  ? 141.188 122.216 159.694 1.00 77.71  ? 129  TYR A CE1   1 
ATOM   1584  C CE2   . TYR B 2 132  ? 139.375 123.556 160.496 1.00 77.78  ? 129  TYR A CE2   1 
ATOM   1585  C CZ    . TYR B 2 132  ? 140.230 123.185 159.479 1.00 77.28  ? 129  TYR A CZ    1 
ATOM   1586  O OH    . TYR B 2 132  ? 140.126 123.787 158.244 1.00 75.16  ? 129  TYR A OH    1 
ATOM   1587  N N     . LYS B 2 133  ? 140.456 123.485 165.850 1.00 83.28  ? 130  LYS A N     1 
ATOM   1588  C CA    . LYS B 2 133  ? 140.008 124.797 166.307 1.00 82.82  ? 130  LYS A CA    1 
ATOM   1589  C C     . LYS B 2 133  ? 141.195 125.712 166.584 1.00 83.85  ? 130  LYS A C     1 
ATOM   1590  O O     . LYS B 2 133  ? 141.271 126.825 166.051 1.00 83.27  ? 130  LYS A O     1 
ATOM   1591  C CB    . LYS B 2 133  ? 139.136 124.648 167.553 1.00 84.76  ? 130  LYS A CB    1 
ATOM   1592  N N     . GLY B 2 134  ? 142.133 125.258 167.412 1.00 84.65  ? 131  GLY A N     1 
ATOM   1593  C CA    . GLY B 2 134  ? 143.313 126.041 167.718 1.00 84.56  ? 131  GLY A CA    1 
ATOM   1594  C C     . GLY B 2 134  ? 144.481 125.731 166.804 1.00 81.10  ? 131  GLY A C     1 
ATOM   1595  O O     . GLY B 2 134  ? 145.641 125.808 167.217 1.00 81.11  ? 131  GLY A O     1 
ATOM   1596  N N     . LEU B 2 135  ? 144.162 125.184 165.627 1.00 78.28  ? 132  LEU A N     1 
ATOM   1597  C CA    . LEU B 2 135  ? 145.212 124.995 164.599 1.00 75.48  ? 132  LEU A CA    1 
ATOM   1598  C C     . LEU B 2 135  ? 145.259 126.366 163.944 1.00 73.01  ? 132  LEU A C     1 
ATOM   1599  O O     . LEU B 2 135  ? 146.252 126.680 163.258 1.00 69.06  ? 132  LEU A O     1 
ATOM   1600  C CB    . LEU B 2 135  ? 144.757 123.913 163.619 1.00 72.22  ? 132  LEU A CB    1 
ATOM   1601  C CG    . LEU B 2 135  ? 145.735 123.571 162.496 1.00 70.29  ? 132  LEU A CG    1 
ATOM   1602  C CD1   . LEU B 2 135  ? 147.053 123.066 163.060 1.00 71.12  ? 132  LEU A CD1   1 
ATOM   1603  C CD2   . LEU B 2 135  ? 145.130 122.542 161.553 1.00 69.68  ? 132  LEU A CD2   1 
ATOM   1604  N N     . PHE B 2 136  ? 144.199 127.146 164.172 1.00 77.39  ? 133  PHE A N     1 
ATOM   1605  C CA    . PHE B 2 136  ? 144.138 128.536 163.661 1.00 78.23  ? 133  PHE A CA    1 
ATOM   1606  C C     . PHE B 2 136  ? 143.978 129.445 164.883 1.00 80.21  ? 133  PHE A C     1 
ATOM   1607  O O     . PHE B 2 136  ? 143.260 130.460 164.787 1.00 78.46  ? 133  PHE A O     1 
ATOM   1608  C CB    . PHE B 2 136  ? 143.013 128.671 162.633 1.00 77.98  ? 133  PHE A CB    1 
ATOM   1609  C CG    . PHE B 2 136  ? 143.066 127.636 161.538 1.00 79.56  ? 133  PHE A CG    1 
ATOM   1610  C CD1   . PHE B 2 136  ? 143.901 127.801 160.445 1.00 80.67  ? 133  PHE A CD1   1 
ATOM   1611  C CD2   . PHE B 2 136  ? 142.298 126.486 161.610 1.00 80.49  ? 133  PHE A CD2   1 
ATOM   1612  C CE1   . PHE B 2 136  ? 143.956 126.845 159.442 1.00 80.62  ? 133  PHE A CE1   1 
ATOM   1613  C CE2   . PHE B 2 136  ? 142.356 125.530 160.608 1.00 80.79  ? 133  PHE A CE2   1 
ATOM   1614  C CZ    . PHE B 2 136  ? 143.184 125.711 159.526 1.00 80.86  ? 133  PHE A CZ    1 
ATOM   1615  N N     . LYS B 2 137  ? 144.616 129.073 166.001 1.00 80.68  ? 134  LYS A N     1 
ATOM   1616  C CA    . LYS B 2 137  ? 144.557 129.887 167.247 1.00 82.22  ? 134  LYS A CA    1 
ATOM   1617  C C     . LYS B 2 137  ? 145.910 129.817 167.964 1.00 84.97  ? 134  LYS A C     1 
ATOM   1618  O O     . LYS B 2 137  ? 146.871 129.310 167.354 1.00 86.22  ? 134  LYS A O     1 
ATOM   1619  C CB    . LYS B 2 137  ? 143.443 129.396 168.177 1.00 82.22  ? 134  LYS A CB    1 
ATOM   1620  C CG    . LYS B 2 137  ? 142.021 129.621 167.683 1.00 80.69  ? 134  LYS A CG    1 
ATOM   1621  C CD    . LYS B 2 137  ? 140.975 129.001 168.583 1.00 77.48  ? 134  LYS A CD    1 
ATOM   1622  C CE    . LYS B 2 137  ? 139.573 129.109 168.023 1.00 76.40  ? 134  LYS A CE    1 
ATOM   1623  N NZ    . LYS B 2 137  ? 138.584 128.416 168.883 1.00 75.88  ? 134  LYS A NZ    1 
ATOM   1624  N N     . ALA B 2 138  ? 145.974 130.282 169.215 1.00 86.78  ? 135  ALA A N     1 
ATOM   1625  C CA    . ALA B 2 138  ? 147.255 130.330 169.963 1.00 93.94  ? 135  ALA A CA    1 
ATOM   1626  C C     . ALA B 2 138  ? 147.775 128.925 170.287 1.00 112.24 ? 135  ALA A C     1 
ATOM   1627  O O     . ALA B 2 138  ? 148.993 128.799 170.523 1.00 129.30 ? 135  ALA A O     1 
ATOM   1628  C CB    . ALA B 2 138  ? 147.071 131.139 171.225 1.00 116.29 ? 135  ALA A CB    1 
ATOM   1629  N N     . GLU B 2 139  ? 146.907 127.909 170.279 1.00 109.33 ? 136  GLU A N     1 
ATOM   1630  C CA    . GLU B 2 139  ? 147.330 126.540 170.689 1.00 113.99 ? 136  GLU A CA    1 
ATOM   1631  C C     . GLU B 2 139  ? 148.659 126.167 170.018 1.00 114.10 ? 136  GLU A C     1 
ATOM   1632  O O     . GLU B 2 139  ? 149.486 125.513 170.683 1.00 116.37 ? 136  GLU A O     1 
ATOM   1633  C CB    . GLU B 2 139  ? 146.239 125.521 170.357 1.00 116.25 ? 136  GLU A CB    1 
ATOM   1634  C CG    . GLU B 2 139  ? 144.943 125.761 171.109 1.00 119.26 ? 136  GLU A CG    1 
ATOM   1635  C CD    . GLU B 2 139  ? 143.859 124.731 170.840 1.00 121.80 ? 136  GLU A CD    1 
ATOM   1636  O OE1   . GLU B 2 139  ? 144.138 123.755 170.117 1.00 123.52 ? 136  GLU A OE1   1 
ATOM   1637  O OE2   . GLU B 2 139  ? 142.736 124.911 171.351 1.00 121.83 ? 136  GLU A OE2   1 
ATOM   1638  N N     . LEU B 2 140  ? 148.850 126.560 168.755 1.00 107.02 ? 137  LEU A N     1 
ATOM   1639  C CA    . LEU B 2 140  ? 150.098 126.226 168.016 1.00 101.61 ? 137  LEU A CA    1 
ATOM   1640  C C     . LEU B 2 140  ? 151.316 126.433 168.922 1.00 103.71 ? 137  LEU A C     1 
ATOM   1641  O O     . LEU B 2 140  ? 152.176 125.531 168.958 1.00 107.16 ? 137  LEU A O     1 
ATOM   1642  C CB    . LEU B 2 140  ? 150.190 127.112 166.769 1.00 94.93  ? 137  LEU A CB    1 
ATOM   1643  C CG    . LEU B 2 140  ? 149.105 126.881 165.720 1.00 89.43  ? 137  LEU A CG    1 
ATOM   1644  C CD1   . LEU B 2 140  ? 149.462 127.584 164.420 1.00 86.10  ? 137  LEU A CD1   1 
ATOM   1645  C CD2   . LEU B 2 140  ? 148.903 125.394 165.474 1.00 87.84  ? 137  LEU A CD2   1 
ATOM   1646  N N     . PHE B 2 141  ? 151.390 127.568 169.622 1.00 103.02 ? 138  PHE A N     1 
ATOM   1647  C CA    . PHE B 2 141  ? 152.551 127.864 170.450 1.00 105.69 ? 138  PHE A CA    1 
ATOM   1648  C C     . PHE B 2 141  ? 152.390 127.400 171.890 1.00 110.93 ? 138  PHE A C     1 
ATOM   1649  O O     . PHE B 2 141  ? 153.385 127.344 172.620 1.00 112.12 ? 138  PHE A O     1 
ATOM   1650  C CB    . PHE B 2 141  ? 152.834 129.368 170.421 1.00 105.68 ? 138  PHE A CB    1 
ATOM   1651  C CG    . PHE B 2 141  ? 152.968 129.935 169.031 1.00 103.39 ? 138  PHE A CG    1 
ATOM   1652  C CD1   . PHE B 2 141  ? 151.843 130.251 168.284 1.00 100.97 ? 138  PHE A CD1   1 
ATOM   1653  C CD2   . PHE B 2 141  ? 154.216 130.155 168.476 1.00 103.07 ? 138  PHE A CD2   1 
ATOM   1654  C CE1   . PHE B 2 141  ? 151.961 130.768 167.010 1.00 97.47  ? 138  PHE A CE1   1 
ATOM   1655  C CE2   . PHE B 2 141  ? 154.341 130.675 167.201 1.00 100.07 ? 138  PHE A CE2   1 
ATOM   1656  C CZ    . PHE B 2 141  ? 153.212 130.980 166.467 1.00 96.94  ? 138  PHE A CZ    1 
ATOM   1657  N N     . ASN B 2 142  ? 151.166 127.068 172.314 1.00 114.51 ? 139  ASN A N     1 
ATOM   1658  C CA    . ASN B 2 142  ? 150.950 126.559 173.662 1.00 118.97 ? 139  ASN A CA    1 
ATOM   1659  C C     . ASN B 2 142  ? 151.663 125.237 173.900 1.00 121.33 ? 139  ASN A C     1 
ATOM   1660  O O     . ASN B 2 142  ? 151.866 124.856 175.059 1.00 123.03 ? 139  ASN A O     1 
ATOM   1661  C CB    . ASN B 2 142  ? 149.457 126.364 173.923 1.00 118.90 ? 139  ASN A CB    1 
ATOM   1662  C CG    . ASN B 2 142  ? 148.656 127.629 173.711 1.00 117.27 ? 139  ASN A CG    1 
ATOM   1663  O OD1   . ASN B 2 142  ? 149.207 128.677 173.383 1.00 115.83 ? 139  ASN A OD1   1 
ATOM   1664  N ND2   . ASN B 2 142  ? 147.345 127.533 173.891 1.00 117.24 ? 139  ASN A ND2   1 
ATOM   1665  N N     . GLY B 2 143  ? 152.046 124.535 172.838 1.00 121.35 ? 140  GLY A N     1 
ATOM   1666  C CA    . GLY B 2 143  ? 152.378 123.135 172.956 1.00 124.23 ? 140  GLY A CA    1 
ATOM   1667  C C     . GLY B 2 143  ? 151.186 122.242 173.195 1.00 125.94 ? 140  GLY A C     1 
ATOM   1668  O O     . GLY B 2 143  ? 151.353 121.020 173.268 1.00 127.20 ? 140  GLY A O     1 
ATOM   1669  N N     . LYS B 2 144  ? 149.984 122.816 173.316 1.00 126.32 ? 141  LYS A N     1 
ATOM   1670  C CA    . LYS B 2 144  ? 148.786 122.019 173.545 1.00 127.37 ? 141  LYS A CA    1 
ATOM   1671  C C     . LYS B 2 144  ? 148.511 121.098 172.364 1.00 126.44 ? 141  LYS A C     1 
ATOM   1672  O O     . LYS B 2 144  ? 148.316 119.892 172.542 1.00 128.10 ? 141  LYS A O     1 
ATOM   1673  C CB    . LYS B 2 144  ? 147.589 122.935 173.808 1.00 126.48 ? 141  LYS A CB    1 
ATOM   1674  N N     . VAL B 2 145  ? 148.503 121.650 171.148 1.00 123.65 ? 142  VAL A N     1 
ATOM   1675  C CA    . VAL B 2 145  ? 148.290 120.827 169.959 1.00 121.53 ? 142  VAL A CA    1 
ATOM   1676  C C     . VAL B 2 145  ? 149.381 119.767 169.846 1.00 123.73 ? 142  VAL A C     1 
ATOM   1677  O O     . VAL B 2 145  ? 149.106 118.604 169.527 1.00 122.20 ? 142  VAL A O     1 
ATOM   1678  C CB    . VAL B 2 145  ? 148.207 121.714 168.703 1.00 118.95 ? 142  VAL A CB    1 
ATOM   1679  C CG1   . VAL B 2 145  ? 146.894 122.482 168.687 1.00 118.40 ? 142  VAL A CG1   1 
ATOM   1680  C CG2   . VAL B 2 145  ? 149.375 122.687 168.656 1.00 119.55 ? 142  VAL A CG2   1 
ATOM   1681  N N     . LEU B 2 146  ? 150.626 120.145 170.134 1.00 126.87 ? 143  LEU A N     1 
ATOM   1682  C CA    . LEU B 2 146  ? 151.703 119.167 170.205 1.00 128.66 ? 143  LEU A CA    1 
ATOM   1683  C C     . LEU B 2 146  ? 151.551 118.238 171.402 1.00 134.39 ? 143  LEU A C     1 
ATOM   1684  O O     . LEU B 2 146  ? 152.044 117.105 171.359 1.00 133.38 ? 143  LEU A O     1 
ATOM   1685  C CB    . LEU B 2 146  ? 153.053 119.892 170.232 1.00 125.15 ? 143  LEU A CB    1 
ATOM   1686  C CG    . LEU B 2 146  ? 154.270 119.259 170.904 1.00 124.33 ? 143  LEU A CG    1 
ATOM   1687  C CD1   . LEU B 2 146  ? 155.442 119.197 169.939 1.00 121.41 ? 143  LEU A CD1   1 
ATOM   1688  C CD2   . LEU B 2 146  ? 154.642 120.058 172.141 1.00 126.05 ? 143  LEU A CD2   1 
ATOM   1689  N N     . LYS B 2 147  ? 150.864 118.678 172.459 1.00 142.81 ? 144  LYS A N     1 
ATOM   1690  C CA    . LYS B 2 147  ? 150.574 117.771 173.564 1.00 146.04 ? 144  LYS A CA    1 
ATOM   1691  C C     . LYS B 2 147  ? 149.540 116.722 173.172 1.00 145.97 ? 144  LYS A C     1 
ATOM   1692  O O     . LYS B 2 147  ? 149.582 115.599 173.687 1.00 149.19 ? 144  LYS A O     1 
ATOM   1693  C CB    . LYS B 2 147  ? 150.103 118.550 174.793 1.00 147.77 ? 144  LYS A CB    1 
ATOM   1694  N N     . GLN B 2 148  ? 148.608 117.061 172.272 1.00 137.88 ? 145  GLN A N     1 
ATOM   1695  C CA    . GLN B 2 148  ? 147.696 116.041 171.760 1.00 130.71 ? 145  GLN A CA    1 
ATOM   1696  C C     . GLN B 2 148  ? 148.432 115.034 170.888 1.00 127.34 ? 145  GLN A C     1 
ATOM   1697  O O     . GLN B 2 148  ? 148.000 113.884 170.769 1.00 129.20 ? 145  GLN A O     1 
ATOM   1698  C CB    . GLN B 2 148  ? 146.546 116.669 170.962 1.00 123.13 ? 145  GLN A CB    1 
ATOM   1699  C CG    . GLN B 2 148  ? 146.274 118.136 171.250 1.00 119.79 ? 145  GLN A CG    1 
ATOM   1700  C CD    . GLN B 2 148  ? 144.843 118.416 171.672 1.00 119.01 ? 145  GLN A CD    1 
ATOM   1701  O OE1   . GLN B 2 148  ? 144.043 117.493 171.842 1.00 117.50 ? 145  GLN A OE1   1 
ATOM   1702  N NE2   . GLN B 2 148  ? 144.509 119.690 171.835 1.00 120.01 ? 145  GLN A NE2   1 
ATOM   1703  N N     . LEU B 2 149  ? 149.541 115.446 170.283 1.00 122.10 ? 146  LEU A N     1 
ATOM   1704  C CA    . LEU B 2 149  ? 150.310 114.581 169.399 1.00 117.84 ? 146  LEU A CA    1 
ATOM   1705  C C     . LEU B 2 149  ? 151.458 113.914 170.149 1.00 118.91 ? 146  LEU A C     1 
ATOM   1706  O O     . LEU B 2 149  ? 151.599 112.690 170.133 1.00 119.01 ? 146  LEU A O     1 
ATOM   1707  C CB    . LEU B 2 149  ? 150.849 115.379 168.209 1.00 113.63 ? 146  LEU A CB    1 
ATOM   1708  C CG    . LEU B 2 149  ? 149.959 115.621 166.981 1.00 110.55 ? 146  LEU A CG    1 
ATOM   1709  C CD1   . LEU B 2 149  ? 148.473 115.529 167.300 1.00 111.34 ? 146  LEU A CD1   1 
ATOM   1710  C CD2   . LEU B 2 149  ? 150.283 116.973 166.352 1.00 107.90 ? 146  LEU A CD2   1 
ATOM   1711  N N     . THR B 2 153  ? 157.509 115.402 169.158 1.00 113.34 ? 150  THR A N     1 
ATOM   1712  C CA    . THR B 2 153  ? 158.095 116.014 170.343 1.00 118.25 ? 150  THR A CA    1 
ATOM   1713  C C     . THR B 2 153  ? 158.912 117.245 169.968 1.00 117.75 ? 150  THR A C     1 
ATOM   1714  O O     . THR B 2 153  ? 159.745 117.204 169.063 1.00 116.11 ? 150  THR A O     1 
ATOM   1715  C CB    . THR B 2 153  ? 158.983 115.018 171.121 1.00 122.60 ? 150  THR A CB    1 
ATOM   1716  O OG1   . THR B 2 153  ? 159.941 114.428 170.232 1.00 122.26 ? 150  THR A OG1   1 
ATOM   1717  C CG2   . THR B 2 153  ? 158.136 113.922 171.757 1.00 124.04 ? 150  THR A CG2   1 
ATOM   1718  N N     . THR B 2 154  ? 158.661 118.342 170.674 1.00 119.02 ? 151  THR A N     1 
ATOM   1719  C CA    . THR B 2 154  ? 159.330 119.607 170.414 1.00 118.47 ? 151  THR A CA    1 
ATOM   1720  C C     . THR B 2 154  ? 160.741 119.604 170.998 1.00 121.21 ? 151  THR A C     1 
ATOM   1721  O O     . THR B 2 154  ? 161.002 119.002 172.043 1.00 122.91 ? 151  THR A O     1 
ATOM   1722  C CB    . THR B 2 154  ? 158.512 120.758 171.012 1.00 118.38 ? 151  THR A CB    1 
ATOM   1723  O OG1   . THR B 2 154  ? 157.154 120.666 170.562 1.00 116.23 ? 151  THR A OG1   1 
ATOM   1724  C CG2   . THR B 2 154  ? 159.078 122.106 170.604 1.00 116.75 ? 151  THR A CG2   1 
ATOM   1725  N N     . THR B 2 155  ? 161.660 120.269 170.298 1.00 121.09 ? 152  THR A N     1 
ATOM   1726  C CA    . THR B 2 155  ? 163.019 120.479 170.774 1.00 121.57 ? 152  THR A CA    1 
ATOM   1727  C C     . THR B 2 155  ? 163.127 121.859 171.416 1.00 121.81 ? 152  THR A C     1 
ATOM   1728  O O     . THR B 2 155  ? 162.282 122.734 171.199 1.00 120.92 ? 152  THR A O     1 
ATOM   1729  C CB    . THR B 2 155  ? 164.034 120.349 169.632 1.00 116.03 ? 152  THR A CB    1 
ATOM   1730  O OG1   . THR B 2 155  ? 164.104 121.582 168.904 1.00 112.08 ? 152  THR A OG1   1 
ATOM   1731  C CG2   . THR B 2 155  ? 163.627 119.237 168.677 1.00 112.06 ? 152  THR A CG2   1 
ATOM   1732  N N     . GLU B 2 156  ? 164.186 122.049 172.210 1.00 123.10 ? 153  GLU A N     1 
ATOM   1733  C CA    . GLU B 2 156  ? 164.303 123.260 173.024 1.00 121.92 ? 153  GLU A CA    1 
ATOM   1734  C C     . GLU B 2 156  ? 164.310 124.522 172.167 1.00 118.78 ? 153  GLU A C     1 
ATOM   1735  O O     . GLU B 2 156  ? 163.651 125.512 172.508 1.00 118.51 ? 153  GLU A O     1 
ATOM   1736  C CB    . GLU B 2 156  ? 165.563 123.191 173.888 1.00 124.48 ? 153  GLU A CB    1 
ATOM   1737  N N     . HIS B 2 157  ? 165.052 124.510 171.056 1.00 116.04 ? 154  HIS A N     1 
ATOM   1738  C CA    . HIS B 2 157  ? 165.075 125.686 170.189 1.00 111.24 ? 154  HIS A CA    1 
ATOM   1739  C C     . HIS B 2 157  ? 163.714 125.922 169.542 1.00 109.05 ? 154  HIS A C     1 
ATOM   1740  O O     . HIS B 2 157  ? 163.290 127.072 169.379 1.00 108.24 ? 154  HIS A O     1 
ATOM   1741  C CB    . HIS B 2 157  ? 166.168 125.547 169.128 1.00 106.23 ? 154  HIS A CB    1 
ATOM   1742  C CG    . HIS B 2 157  ? 166.260 126.719 168.200 1.00 101.74 ? 154  HIS A CG    1 
ATOM   1743  N ND1   . HIS B 2 157  ? 165.887 126.649 166.875 1.00 98.32  ? 154  HIS A ND1   1 
ATOM   1744  C CD2   . HIS B 2 157  ? 166.664 127.994 168.412 1.00 101.44 ? 154  HIS A CD2   1 
ATOM   1745  C CE1   . HIS B 2 157  ? 166.063 127.829 166.308 1.00 97.09  ? 154  HIS A CE1   1 
ATOM   1746  N NE2   . HIS B 2 157  ? 166.535 128.663 167.217 1.00 99.06  ? 154  HIS A NE2   1 
ATOM   1747  N N     . GLU B 2 158  ? 163.013 124.845 169.177 1.00 108.15 ? 155  GLU A N     1 
ATOM   1748  C CA    . GLU B 2 158  ? 161.650 124.990 168.672 1.00 106.08 ? 155  GLU A CA    1 
ATOM   1749  C C     . GLU B 2 158  ? 160.720 125.521 169.756 1.00 108.19 ? 155  GLU A C     1 
ATOM   1750  O O     . GLU B 2 158  ? 159.885 126.396 169.495 1.00 108.29 ? 155  GLU A O     1 
ATOM   1751  C CB    . GLU B 2 158  ? 161.143 123.650 168.130 1.00 105.31 ? 155  GLU A CB    1 
ATOM   1752  C CG    . GLU B 2 158  ? 161.894 123.128 166.907 1.00 103.75 ? 155  GLU A CG    1 
ATOM   1753  C CD    . GLU B 2 158  ? 161.861 124.102 165.742 1.00 102.52 ? 155  GLU A CD    1 
ATOM   1754  O OE1   . GLU B 2 158  ? 160.801 124.719 165.509 1.00 102.99 ? 155  GLU A OE1   1 
ATOM   1755  O OE2   . GLU B 2 158  ? 162.895 124.245 165.052 1.00 100.59 ? 155  GLU A OE2   1 
ATOM   1756  N N     . ASN B 2 159  ? 160.856 125.008 170.983 1.00 114.27 ? 156  ASN A N     1 
ATOM   1757  C CA    . ASN B 2 159  ? 160.076 125.543 172.095 1.00 115.87 ? 156  ASN A CA    1 
ATOM   1758  C C     . ASN B 2 159  ? 160.390 127.018 172.325 1.00 114.15 ? 156  ASN A C     1 
ATOM   1759  O O     . ASN B 2 159  ? 159.489 127.816 172.610 1.00 113.05 ? 156  ASN A O     1 
ATOM   1760  C CB    . ASN B 2 159  ? 160.334 124.734 173.370 1.00 123.27 ? 156  ASN A CB    1 
ATOM   1761  C CG    . ASN B 2 159  ? 159.256 123.684 173.640 1.00 125.57 ? 156  ASN A CG    1 
ATOM   1762  O OD1   . ASN B 2 159  ? 158.060 123.943 173.484 1.00 124.81 ? 156  ASN A OD1   1 
ATOM   1763  N ND2   . ASN B 2 159  ? 159.681 122.499 174.060 1.00 127.74 ? 156  ASN A ND2   1 
ATOM   1764  N N     . ALA B 2 160  ? 161.665 127.401 172.200 1.00 114.07 ? 157  ALA A N     1 
ATOM   1765  C CA    . ALA B 2 160  ? 162.022 128.812 172.320 1.00 111.66 ? 157  ALA A CA    1 
ATOM   1766  C C     . ALA B 2 160  ? 161.453 129.632 171.169 1.00 104.25 ? 157  ALA A C     1 
ATOM   1767  O O     . ALA B 2 160  ? 161.191 130.830 171.334 1.00 103.00 ? 157  ALA A O     1 
ATOM   1768  C CB    . ALA B 2 160  ? 163.540 128.974 172.384 1.00 113.69 ? 157  ALA A CB    1 
ATOM   1769  N N     . LEU B 2 161  ? 161.259 129.015 170.002 1.00 98.50  ? 158  LEU A N     1 
ATOM   1770  C CA    . LEU B 2 161  ? 160.646 129.717 168.881 1.00 94.06  ? 158  LEU A CA    1 
ATOM   1771  C C     . LEU B 2 161  ? 159.141 129.869 169.054 1.00 93.31  ? 158  LEU A C     1 
ATOM   1772  O O     . LEU B 2 161  ? 158.570 130.875 168.615 1.00 93.33  ? 158  LEU A O     1 
ATOM   1773  C CB    . LEU B 2 161  ? 160.948 128.990 167.570 1.00 90.41  ? 158  LEU A CB    1 
ATOM   1774  C CG    . LEU B 2 161  ? 162.183 129.467 166.804 1.00 89.99  ? 158  LEU A CG    1 
ATOM   1775  C CD1   . LEU B 2 161  ? 162.308 128.722 165.486 1.00 88.47  ? 158  LEU A CD1   1 
ATOM   1776  C CD2   . LEU B 2 161  ? 162.114 130.968 166.572 1.00 88.47  ? 158  LEU A CD2   1 
ATOM   1777  N N     . LEU B 2 162  ? 158.481 128.888 169.679 1.00 91.16  ? 159  LEU A N     1 
ATOM   1778  C CA    . LEU B 2 162  ? 157.048 129.005 169.925 1.00 86.84  ? 159  LEU A CA    1 
ATOM   1779  C C     . LEU B 2 162  ? 156.746 130.130 170.906 1.00 88.43  ? 159  LEU A C     1 
ATOM   1780  O O     . LEU B 2 162  ? 155.813 130.913 170.694 1.00 84.71  ? 159  LEU A O     1 
ATOM   1781  C CB    . LEU B 2 162  ? 156.490 127.682 170.446 1.00 86.53  ? 159  LEU A CB    1 
ATOM   1782  C CG    . LEU B 2 162  ? 156.455 126.497 169.480 1.00 85.36  ? 159  LEU A CG    1 
ATOM   1783  C CD1   . LEU B 2 162  ? 155.979 125.242 170.194 1.00 86.84  ? 159  LEU A CD1   1 
ATOM   1784  C CD2   . LEU B 2 162  ? 155.567 126.805 168.286 1.00 81.82  ? 159  LEU A CD2   1 
ATOM   1785  N N     . ARG B 2 163  ? 157.526 130.228 171.986 1.00 93.93  ? 160  ARG A N     1 
ATOM   1786  C CA    . ARG B 2 163  ? 157.295 131.256 172.993 1.00 84.24  ? 160  ARG A CA    1 
ATOM   1787  C C     . ARG B 2 163  ? 157.627 132.656 172.500 1.00 83.30  ? 160  ARG A C     1 
ATOM   1788  O O     . ARG B 2 163  ? 157.235 133.630 173.152 1.00 84.04  ? 160  ARG A O     1 
ATOM   1789  C CB    . ARG B 2 163  ? 158.106 130.950 174.254 1.00 96.86  ? 160  ARG A CB    1 
ATOM   1790  C CG    . ARG B 2 163  ? 157.899 129.551 174.803 1.00 98.39  ? 160  ARG A CG    1 
ATOM   1791  C CD    . ARG B 2 163  ? 158.442 129.433 176.216 1.00 93.33  ? 160  ARG A CD    1 
ATOM   1792  N NE    . ARG B 2 163  ? 159.695 130.162 176.383 1.00 101.10 ? 160  ARG A NE    1 
ATOM   1793  C CZ    . ARG B 2 163  ? 160.901 129.635 176.200 1.00 101.24 ? 160  ARG A CZ    1 
ATOM   1794  N NH1   . ARG B 2 163  ? 161.027 128.365 175.841 1.00 96.15  ? 160  ARG A NH1   1 
ATOM   1795  N NH2   . ARG B 2 163  ? 161.985 130.379 176.375 1.00 101.73 ? 160  ARG A NH2   1 
ATOM   1796  N N     . SER B 2 164  ? 158.337 132.786 171.376 1.00 84.68  ? 161  SER A N     1 
ATOM   1797  C CA    . SER B 2 164  ? 158.597 134.107 170.814 1.00 80.84  ? 161  SER A CA    1 
ATOM   1798  C C     . SER B 2 164  ? 157.318 134.788 170.350 1.00 81.53  ? 161  SER A C     1 
ATOM   1799  O O     . SER B 2 164  ? 157.319 136.006 170.133 1.00 77.86  ? 161  SER A O     1 
ATOM   1800  C CB    . SER B 2 164  ? 159.590 134.001 169.653 1.00 79.73  ? 161  SER A CB    1 
ATOM   1801  O OG    . SER B 2 164  ? 160.860 133.560 170.102 1.00 79.34  ? 161  SER A OG    1 
ATOM   1802  N N     . PHE B 2 165  ? 156.233 134.035 170.198 1.00 79.65  ? 162  PHE A N     1 
ATOM   1803  C CA    . PHE B 2 165  ? 154.926 134.562 169.832 1.00 77.85  ? 162  PHE A CA    1 
ATOM   1804  C C     . PHE B 2 165  ? 153.919 134.346 170.956 1.00 78.98  ? 162  PHE A C     1 
ATOM   1805  O O     . PHE B 2 165  ? 152.738 134.087 170.718 1.00 77.33  ? 162  PHE A O     1 
ATOM   1806  C CB    . PHE B 2 165  ? 154.430 133.934 168.533 1.00 76.31  ? 162  PHE A CB    1 
ATOM   1807  C CG    . PHE B 2 165  ? 155.159 134.418 167.313 1.00 76.35  ? 162  PHE A CG    1 
ATOM   1808  C CD1   . PHE B 2 165  ? 154.917 135.684 166.808 1.00 76.27  ? 162  PHE A CD1   1 
ATOM   1809  C CD2   . PHE B 2 165  ? 156.085 133.612 166.673 1.00 76.20  ? 162  PHE A CD2   1 
ATOM   1810  C CE1   . PHE B 2 165  ? 155.583 136.139 165.688 1.00 74.11  ? 162  PHE A CE1   1 
ATOM   1811  C CE2   . PHE B 2 165  ? 156.755 134.061 165.550 1.00 75.44  ? 162  PHE A CE2   1 
ATOM   1812  C CZ    . PHE B 2 165  ? 156.504 135.328 165.057 1.00 74.23  ? 162  PHE A CZ    1 
ATOM   1813  N N     . ASP B 2 166  ? 154.382 134.440 172.201 1.00 82.48  ? 163  ASP A N     1 
ATOM   1814  C CA    . ASP B 2 166  ? 153.468 134.426 173.333 1.00 84.23  ? 163  ASP A CA    1 
ATOM   1815  C C     . ASP B 2 166  ? 152.697 135.739 173.374 1.00 85.21  ? 163  ASP A C     1 
ATOM   1816  O O     . ASP B 2 166  ? 153.282 136.819 173.232 1.00 86.32  ? 163  ASP A O     1 
ATOM   1817  C CB    . ASP B 2 166  ? 154.234 134.211 174.637 1.00 88.02  ? 163  ASP A CB    1 
ATOM   1818  N N     . LYS B 2 167  ? 151.376 135.644 173.555 1.00 84.41  ? 164  LYS A N     1 
ATOM   1819  C CA    . LYS B 2 167  ? 150.475 136.796 173.480 1.00 81.83  ? 164  LYS A CA    1 
ATOM   1820  C C     . LYS B 2 167  ? 150.631 137.543 172.156 1.00 80.33  ? 164  LYS A C     1 
ATOM   1821  O O     . LYS B 2 167  ? 150.511 138.770 172.100 1.00 78.15  ? 164  LYS A O     1 
ATOM   1822  C CB    . LYS B 2 167  ? 150.679 137.746 174.663 1.00 83.32  ? 164  LYS A CB    1 
ATOM   1823  N N     . PHE B 2 168  ? 150.901 136.796 171.077 1.00 83.02  ? 165  PHE A N     1 
ATOM   1824  C CA    . PHE B 2 168  ? 151.086 137.433 169.767 1.00 84.45  ? 165  PHE A CA    1 
ATOM   1825  C C     . PHE B 2 168  ? 150.787 136.481 168.615 1.00 82.33  ? 165  PHE A C     1 
ATOM   1826  O O     . PHE B 2 168  ? 151.307 136.702 167.516 1.00 85.33  ? 165  PHE A O     1 
ATOM   1827  C CB    . PHE B 2 168  ? 152.517 137.974 169.640 1.00 86.22  ? 165  PHE A CB    1 
ATOM   1828  C CG    . PHE B 2 168  ? 152.604 139.335 169.003 1.00 84.41  ? 165  PHE A CG    1 
ATOM   1829  C CD1   . PHE B 2 168  ? 152.424 139.494 167.636 1.00 67.98  ? 165  PHE A CD1   1 
ATOM   1830  C CD2   . PHE B 2 168  ? 152.884 140.455 169.769 1.00 72.30  ? 165  PHE A CD2   1 
ATOM   1831  C CE1   . PHE B 2 168  ? 152.509 140.742 167.051 1.00 67.25  ? 165  PHE A CE1   1 
ATOM   1832  C CE2   . PHE B 2 168  ? 152.973 141.706 169.188 1.00 71.57  ? 165  PHE A CE2   1 
ATOM   1833  C CZ    . PHE B 2 168  ? 152.785 141.849 167.828 1.00 69.05  ? 165  PHE A CZ    1 
ATOM   1834  N N     . THR B 2 169  ? 149.981 135.436 168.817 1.00 77.76  ? 166  THR A N     1 
ATOM   1835  C CA    . THR B 2 169  ? 149.700 134.482 167.752 1.00 76.86  ? 166  THR A CA    1 
ATOM   1836  C C     . THR B 2 169  ? 148.828 135.064 166.647 1.00 75.42  ? 166  THR A C     1 
ATOM   1837  O O     . THR B 2 169  ? 148.636 134.399 165.624 1.00 75.41  ? 166  THR A O     1 
ATOM   1838  C CB    . THR B 2 169  ? 149.030 133.231 168.324 1.00 80.29  ? 166  THR A CB    1 
ATOM   1839  O OG1   . THR B 2 169  ? 147.775 133.585 168.920 1.00 82.78  ? 166  THR A OG1   1 
ATOM   1840  C CG2   . THR B 2 169  ? 149.922 132.585 169.374 1.00 83.41  ? 166  THR A CG2   1 
ATOM   1841  N N     . THR B 2 170  ? 148.299 136.278 166.823 1.00 73.83  ? 167  THR A N     1 
ATOM   1842  C CA    . THR B 2 170  ? 147.586 136.949 165.743 1.00 70.13  ? 167  THR A CA    1 
ATOM   1843  C C     . THR B 2 170  ? 148.512 137.329 164.592 1.00 66.91  ? 167  THR A C     1 
ATOM   1844  O O     . THR B 2 170  ? 148.025 137.705 163.522 1.00 63.17  ? 167  THR A O     1 
ATOM   1845  C CB    . THR B 2 170  ? 146.870 138.196 166.273 1.00 67.72  ? 167  THR A CB    1 
ATOM   1846  O OG1   . THR B 2 170  ? 146.326 137.917 167.568 1.00 67.15  ? 167  THR A OG1   1 
ATOM   1847  C CG2   . THR B 2 170  ? 145.731 138.603 165.346 1.00 63.29  ? 167  THR A CG2   1 
ATOM   1848  N N     . TYR B 2 171  ? 149.830 137.234 164.785 1.00 68.68  ? 168  TYR A N     1 
ATOM   1849  C CA    . TYR B 2 171  ? 150.766 137.441 163.689 1.00 69.23  ? 168  TYR A CA    1 
ATOM   1850  C C     . TYR B 2 171  ? 150.590 136.403 162.588 1.00 64.81  ? 168  TYR A C     1 
ATOM   1851  O O     . TYR B 2 171  ? 150.957 136.665 161.436 1.00 65.00  ? 168  TYR A O     1 
ATOM   1852  C CB    . TYR B 2 171  ? 152.201 137.407 164.218 1.00 73.94  ? 168  TYR A CB    1 
ATOM   1853  C CG    . TYR B 2 171  ? 153.219 138.073 163.322 1.00 61.61  ? 168  TYR A CG    1 
ATOM   1854  C CD1   . TYR B 2 171  ? 153.277 139.456 163.215 1.00 61.69  ? 168  TYR A CD1   1 
ATOM   1855  C CD2   . TYR B 2 171  ? 154.137 137.323 162.600 1.00 61.30  ? 168  TYR A CD2   1 
ATOM   1856  C CE1   . TYR B 2 171  ? 154.212 140.073 162.406 1.00 61.52  ? 168  TYR A CE1   1 
ATOM   1857  C CE2   . TYR B 2 171  ? 155.077 137.930 161.789 1.00 61.05  ? 168  TYR A CE2   1 
ATOM   1858  C CZ    . TYR B 2 171  ? 155.110 139.305 161.697 1.00 61.19  ? 168  TYR A CZ    1 
ATOM   1859  O OH    . TYR B 2 171  ? 156.042 139.917 160.891 1.00 61.09  ? 168  TYR A OH    1 
ATOM   1860  N N     . PHE B 2 172  ? 150.036 135.234 162.919 1.00 62.69  ? 169  PHE A N     1 
ATOM   1861  C CA    . PHE B 2 172  ? 149.715 134.199 161.943 1.00 63.52  ? 169  PHE A CA    1 
ATOM   1862  C C     . PHE B 2 172  ? 148.281 134.296 161.437 1.00 63.33  ? 169  PHE A C     1 
ATOM   1863  O O     . PHE B 2 172  ? 147.707 133.282 161.020 1.00 61.82  ? 169  PHE A O     1 
ATOM   1864  C CB    . PHE B 2 172  ? 149.966 132.816 162.546 1.00 64.12  ? 169  PHE A CB    1 
ATOM   1865  C CG    . PHE B 2 172  ? 151.405 132.551 162.896 1.00 65.56  ? 169  PHE A CG    1 
ATOM   1866  C CD1   . PHE B 2 172  ? 151.916 132.932 164.127 1.00 66.96  ? 169  PHE A CD1   1 
ATOM   1867  C CD2   . PHE B 2 172  ? 152.241 131.906 162.000 1.00 64.94  ? 169  PHE A CD2   1 
ATOM   1868  C CE1   . PHE B 2 172  ? 153.237 132.686 164.451 1.00 67.82  ? 169  PHE A CE1   1 
ATOM   1869  C CE2   . PHE B 2 172  ? 153.563 131.655 162.320 1.00 65.91  ? 169  PHE A CE2   1 
ATOM   1870  C CZ    . PHE B 2 172  ? 154.062 132.047 163.549 1.00 67.72  ? 169  PHE A CZ    1 
ATOM   1871  N N     . SER B 2 173  ? 147.685 135.492 161.463 1.00 63.36  ? 170  SER A N     1 
ATOM   1872  C CA    . SER B 2 173  ? 146.288 135.641 161.065 1.00 61.26  ? 170  SER A CA    1 
ATOM   1873  C C     . SER B 2 173  ? 146.102 135.307 159.588 1.00 59.08  ? 170  SER A C     1 
ATOM   1874  O O     . SER B 2 173  ? 145.289 134.445 159.230 1.00 58.26  ? 170  SER A O     1 
ATOM   1875  C CB    . SER B 2 173  ? 145.807 137.062 161.364 1.00 61.06  ? 170  SER A CB    1 
ATOM   1876  O OG    . SER B 2 173  ? 144.419 137.194 161.119 1.00 61.66  ? 170  SER A OG    1 
ATOM   1877  N N     . GLY B 2 174  ? 146.846 135.986 158.715 1.00 58.91  ? 171  GLY A N     1 
ATOM   1878  C CA    . GLY B 2 174  ? 146.764 135.683 157.297 1.00 59.54  ? 171  GLY A CA    1 
ATOM   1879  C C     . GLY B 2 174  ? 147.293 134.309 156.951 1.00 62.71  ? 171  GLY A C     1 
ATOM   1880  O O     . GLY B 2 174  ? 146.815 133.675 156.002 1.00 63.50  ? 171  GLY A O     1 
ATOM   1881  N N     . PHE B 2 175  ? 148.284 133.826 157.706 1.00 65.06  ? 172  PHE A N     1 
ATOM   1882  C CA    . PHE B 2 175  ? 148.792 132.475 157.503 1.00 64.17  ? 172  PHE A CA    1 
ATOM   1883  C C     . PHE B 2 175  ? 147.728 131.423 157.792 1.00 62.49  ? 172  PHE A C     1 
ATOM   1884  O O     . PHE B 2 175  ? 147.699 130.377 157.133 1.00 60.51  ? 172  PHE A O     1 
ATOM   1885  C CB    . PHE B 2 175  ? 150.027 132.247 158.378 1.00 67.89  ? 172  PHE A CB    1 
ATOM   1886  C CG    . PHE B 2 175  ? 150.492 130.816 158.417 1.00 69.08  ? 172  PHE A CG    1 
ATOM   1887  C CD1   . PHE B 2 175  ? 151.201 130.273 157.357 1.00 68.91  ? 172  PHE A CD1   1 
ATOM   1888  C CD2   . PHE B 2 175  ? 150.233 130.018 159.519 1.00 69.15  ? 172  PHE A CD2   1 
ATOM   1889  C CE1   . PHE B 2 175  ? 151.631 128.960 157.393 1.00 68.25  ? 172  PHE A CE1   1 
ATOM   1890  C CE2   . PHE B 2 175  ? 150.660 128.704 159.561 1.00 68.95  ? 172  PHE A CE2   1 
ATOM   1891  C CZ    . PHE B 2 175  ? 151.361 128.175 158.495 1.00 69.03  ? 172  PHE A CZ    1 
ATOM   1892  N N     . TYR B 2 176  ? 146.855 131.677 158.772 1.00 60.81  ? 173  TYR A N     1 
ATOM   1893  C CA    . TYR B 2 176  ? 145.761 130.749 159.043 1.00 58.36  ? 173  TYR A CA    1 
ATOM   1894  C C     . TYR B 2 176  ? 144.849 130.609 157.833 1.00 53.40  ? 173  TYR A C     1 
ATOM   1895  O O     . TYR B 2 176  ? 144.356 129.514 157.540 1.00 50.06  ? 173  TYR A O     1 
ATOM   1896  C CB    . TYR B 2 176  ? 144.958 131.210 160.260 1.00 60.04  ? 173  TYR A CB    1 
ATOM   1897  C CG    . TYR B 2 176  ? 145.646 130.990 161.589 1.00 63.74  ? 173  TYR A CG    1 
ATOM   1898  C CD1   . TYR B 2 176  ? 146.569 129.966 161.754 1.00 65.55  ? 173  TYR A CD1   1 
ATOM   1899  C CD2   . TYR B 2 176  ? 145.368 131.803 162.680 1.00 64.67  ? 173  TYR A CD2   1 
ATOM   1900  C CE1   . TYR B 2 176  ? 147.199 129.760 162.968 1.00 67.78  ? 173  TYR A CE1   1 
ATOM   1901  C CE2   . TYR B 2 176  ? 145.994 131.605 163.898 1.00 66.57  ? 173  TYR A CE2   1 
ATOM   1902  C CZ    . TYR B 2 176  ? 146.907 130.582 164.036 1.00 69.82  ? 173  TYR A CZ    1 
ATOM   1903  O OH    . TYR B 2 176  ? 147.532 130.383 165.244 1.00 75.30  ? 173  TYR A OH    1 
ATOM   1904  N N     . GLU B 2 177  ? 144.608 131.711 157.116 1.00 54.59  ? 174  GLU A N     1 
ATOM   1905  C CA    . GLU B 2 177  ? 143.775 131.648 155.921 1.00 55.64  ? 174  GLU A CA    1 
ATOM   1906  C C     . GLU B 2 177  ? 144.463 130.874 154.804 1.00 53.07  ? 174  GLU A C     1 
ATOM   1907  O O     . GLU B 2 177  ? 143.811 130.127 154.064 1.00 49.50  ? 174  GLU A O     1 
ATOM   1908  C CB    . GLU B 2 177  ? 143.419 133.060 155.457 1.00 59.70  ? 174  GLU A CB    1 
ATOM   1909  C CG    . GLU B 2 177  ? 142.397 133.756 156.338 1.00 64.70  ? 174  GLU A CG    1 
ATOM   1910  C CD    . GLU B 2 177  ? 141.027 133.112 156.252 1.00 67.31  ? 174  GLU A CD    1 
ATOM   1911  O OE1   . GLU B 2 177  ? 140.693 132.561 155.181 1.00 67.21  ? 174  GLU A OE1   1 
ATOM   1912  O OE2   . GLU B 2 177  ? 140.286 133.152 157.256 1.00 68.49  ? 174  GLU A OE2   1 
ATOM   1913  N N     . ASN B 2 178  ? 145.782 131.036 154.671 1.00 53.77  ? 175  ASN A N     1 
ATOM   1914  C CA    . ASN B 2 178  ? 146.514 130.308 153.640 1.00 52.60  ? 175  ASN A CA    1 
ATOM   1915  C C     . ASN B 2 178  ? 146.480 128.804 153.886 1.00 54.41  ? 175  ASN A C     1 
ATOM   1916  O O     . ASN B 2 178  ? 146.530 128.019 152.932 1.00 54.14  ? 175  ASN A O     1 
ATOM   1917  C CB    . ASN B 2 178  ? 147.957 130.804 153.577 1.00 54.12  ? 175  ASN A CB    1 
ATOM   1918  C CG    . ASN B 2 178  ? 148.047 132.290 153.294 1.00 55.02  ? 175  ASN A CG    1 
ATOM   1919  O OD1   . ASN B 2 178  ? 148.733 133.025 154.001 1.00 58.84  ? 175  ASN A OD1   1 
ATOM   1920  N ND2   . ASN B 2 178  ? 147.366 132.734 152.244 1.00 52.67  ? 175  ASN A ND2   1 
ATOM   1921  N N     . ARG B 2 179  ? 146.390 128.387 155.151 1.00 57.14  ? 176  ARG A N     1 
ATOM   1922  C CA    . ARG B 2 179  ? 146.314 126.965 155.454 1.00 60.11  ? 176  ARG A CA    1 
ATOM   1923  C C     . ARG B 2 179  ? 144.891 126.430 155.343 1.00 62.20  ? 176  ARG A C     1 
ATOM   1924  O O     . ARG B 2 179  ? 144.705 125.236 155.081 1.00 64.76  ? 176  ARG A O     1 
ATOM   1925  C CB    . ARG B 2 179  ? 146.884 126.694 156.846 1.00 61.46  ? 176  ARG A CB    1 
ATOM   1926  C CG    . ARG B 2 179  ? 148.400 126.783 156.898 1.00 61.19  ? 176  ARG A CG    1 
ATOM   1927  C CD    . ARG B 2 179  ? 149.028 125.818 155.902 1.00 58.79  ? 176  ARG A CD    1 
ATOM   1928  N NE    . ARG B 2 179  ? 150.465 126.029 155.748 1.00 57.40  ? 176  ARG A NE    1 
ATOM   1929  C CZ    . ARG B 2 179  ? 151.013 126.797 154.811 1.00 56.21  ? 176  ARG A CZ    1 
ATOM   1930  N NH1   . ARG B 2 179  ? 150.245 127.434 153.937 1.00 57.40  ? 176  ARG A NH1   1 
ATOM   1931  N NH2   . ARG B 2 179  ? 152.331 126.928 154.748 1.00 53.53  ? 176  ARG A NH2   1 
ATOM   1932  N N     . LYS B 2 180  ? 143.881 127.283 155.537 1.00 61.87  ? 177  LYS A N     1 
ATOM   1933  C CA    . LYS B 2 180  ? 142.521 126.871 155.213 1.00 60.62  ? 177  LYS A CA    1 
ATOM   1934  C C     . LYS B 2 180  ? 142.357 126.657 153.717 1.00 58.13  ? 177  LYS A C     1 
ATOM   1935  O O     . LYS B 2 180  ? 141.584 125.788 153.295 1.00 57.87  ? 177  LYS A O     1 
ATOM   1936  C CB    . LYS B 2 180  ? 141.508 127.904 155.708 1.00 62.74  ? 177  LYS A CB    1 
ATOM   1937  C CG    . LYS B 2 180  ? 141.468 128.091 157.213 1.00 67.60  ? 177  LYS A CG    1 
ATOM   1938  C CD    . LYS B 2 180  ? 140.066 128.454 157.671 1.00 69.76  ? 177  LYS A CD    1 
ATOM   1939  C CE    . LYS B 2 180  ? 140.088 129.422 158.842 1.00 70.84  ? 177  LYS A CE    1 
ATOM   1940  N NZ    . LYS B 2 180  ? 140.536 130.776 158.416 1.00 70.07  ? 177  LYS A NZ    1 
ATOM   1941  N N     . ASN B 2 181  ? 143.077 127.431 152.902 1.00 53.03  ? 178  ASN A N     1 
ATOM   1942  C CA    . ASN B 2 181  ? 143.050 127.235 151.456 1.00 51.79  ? 178  ASN A CA    1 
ATOM   1943  C C     . ASN B 2 181  ? 143.657 125.904 151.042 1.00 51.12  ? 178  ASN A C     1 
ATOM   1944  O O     . ASN B 2 181  ? 143.418 125.453 149.918 1.00 49.58  ? 178  ASN A O     1 
ATOM   1945  C CB    . ASN B 2 181  ? 143.789 128.376 150.755 1.00 49.23  ? 178  ASN A CB    1 
ATOM   1946  C CG    . ASN B 2 181  ? 143.148 129.724 151.003 1.00 41.02  ? 178  ASN A CG    1 
ATOM   1947  O OD1   . ASN B 2 181  ? 141.952 129.813 151.282 1.00 47.20  ? 178  ASN A OD1   1 
ATOM   1948  N ND2   . ASN B 2 181  ? 143.941 130.784 150.900 1.00 40.88  ? 178  ASN A ND2   1 
ATOM   1949  N N     . VAL B 2 182  ? 144.437 125.268 151.917 1.00 52.49  ? 179  VAL A N     1 
ATOM   1950  C CA    . VAL B 2 182  ? 145.049 123.987 151.584 1.00 49.03  ? 179  VAL A CA    1 
ATOM   1951  C C     . VAL B 2 182  ? 144.064 122.844 151.799 1.00 51.77  ? 179  VAL A C     1 
ATOM   1952  O O     . VAL B 2 182  ? 143.995 121.910 150.992 1.00 52.43  ? 179  VAL A O     1 
ATOM   1953  C CB    . VAL B 2 182  ? 146.335 123.789 152.405 1.00 47.28  ? 179  VAL A CB    1 
ATOM   1954  C CG1   . VAL B 2 182  ? 146.930 122.412 152.147 1.00 46.11  ? 179  VAL A CG1   1 
ATOM   1955  C CG2   . VAL B 2 182  ? 147.346 124.879 152.083 1.00 44.97  ? 179  VAL A CG2   1 
ATOM   1956  N N     . PHE B 2 183  ? 143.210 122.955 152.824 1.00 52.46  ? 180  PHE A N     1 
ATOM   1957  C CA    . PHE B 2 183  ? 142.167 121.916 153.059 1.00 52.58  ? 180  PHE A CA    1 
ATOM   1958  C C     . PHE B 2 183  ? 140.826 122.372 152.471 1.00 52.59  ? 180  PHE A C     1 
ATOM   1959  O O     . PHE B 2 183  ? 140.843 122.732 151.277 1.00 54.53  ? 180  PHE A O     1 
ATOM   1960  C CB    . PHE B 2 183  ? 142.024 121.629 154.556 1.00 53.74  ? 180  PHE A CB    1 
ATOM   1961  C CG    . PHE B 2 183  ? 143.307 121.262 155.255 1.00 53.51  ? 180  PHE A CG    1 
ATOM   1962  C CD1   . PHE B 2 183  ? 143.782 119.960 155.231 1.00 53.04  ? 180  PHE A CD1   1 
ATOM   1963  C CD2   . PHE B 2 183  ? 144.041 122.217 155.939 1.00 55.35  ? 180  PHE A CD2   1 
ATOM   1964  C CE1   . PHE B 2 183  ? 144.962 119.624 155.875 1.00 54.23  ? 180  PHE A CE1   1 
ATOM   1965  C CE2   . PHE B 2 183  ? 145.222 121.881 156.582 1.00 57.39  ? 180  PHE A CE2   1 
ATOM   1966  C CZ    . PHE B 2 183  ? 145.680 120.585 156.549 1.00 52.39  ? 180  PHE A CZ    1 
ATOM   1967  N N     . SER B 2 184  ? 139.756 122.380 153.279 1.00 52.07  ? 181  SER A N     1 
ATOM   1968  C CA    . SER B 2 184  ? 138.389 122.766 152.823 1.00 50.03  ? 181  SER A CA    1 
ATOM   1969  C C     . SER B 2 184  ? 137.717 121.570 152.137 1.00 51.68  ? 181  SER A C     1 
ATOM   1970  O O     . SER B 2 184  ? 136.481 121.606 151.983 1.00 52.15  ? 181  SER A O     1 
ATOM   1971  C CB    . SER B 2 184  ? 138.390 123.999 151.948 1.00 47.24  ? 181  SER A CB    1 
ATOM   1972  O OG    . SER B 2 184  ? 137.064 124.409 151.651 1.00 46.86  ? 181  SER A OG    1 
ATOM   1973  N N     . ALA B 2 185  ? 138.498 120.557 151.748 1.00 53.19  ? 182  ALA A N     1 
ATOM   1974  C CA    . ALA B 2 185  ? 137.928 119.327 151.143 1.00 53.44  ? 182  ALA A CA    1 
ATOM   1975  C C     . ALA B 2 185  ? 136.963 119.685 150.008 1.00 53.95  ? 182  ALA A C     1 
ATOM   1976  O O     . ALA B 2 185  ? 135.836 119.151 150.003 1.00 55.53  ? 182  ALA A O     1 
ATOM   1977  C CB    . ALA B 2 185  ? 137.240 118.504 152.202 1.00 52.24  ? 182  ALA A CB    1 
ATOM   1978  N N     . GLU B 2 186  ? 137.391 120.546 149.082 1.00 54.32  ? 183  GLU A N     1 
ATOM   1979  C CA    . GLU B 2 186  ? 136.537 120.900 147.917 1.00 55.61  ? 183  GLU A CA    1 
ATOM   1980  C C     . GLU B 2 186  ? 137.208 120.399 146.636 1.00 52.94  ? 183  GLU A C     1 
ATOM   1981  O O     . GLU B 2 186  ? 138.248 119.718 146.742 1.00 50.73  ? 183  GLU A O     1 
ATOM   1982  C CB    . GLU B 2 186  ? 136.311 122.411 147.853 1.00 59.72  ? 183  GLU A CB    1 
ATOM   1983  C CG    . GLU B 2 186  ? 135.656 122.978 149.099 1.00 65.56  ? 183  GLU A CG    1 
ATOM   1984  C CD    . GLU B 2 186  ? 134.272 122.434 149.410 1.00 72.08  ? 183  GLU A CD    1 
ATOM   1985  O OE1   . GLU B 2 186  ? 133.593 121.969 148.473 1.00 75.13  ? 183  GLU A OE1   1 
ATOM   1986  O OE2   . GLU B 2 186  ? 133.878 122.475 150.592 1.00 74.22  ? 183  GLU A OE2   1 
ATOM   1987  N N     . ASP B 2 187  ? 136.639 120.732 145.475 1.00 52.32  ? 184  ASP A N     1 
ATOM   1988  C CA    . ASP B 2 187  ? 137.255 120.341 144.179 1.00 50.47  ? 184  ASP A CA    1 
ATOM   1989  C C     . ASP B 2 187  ? 138.573 121.107 144.016 1.00 47.17  ? 184  ASP A C     1 
ATOM   1990  O O     . ASP B 2 187  ? 139.355 120.754 143.113 1.00 45.93  ? 184  ASP A O     1 
ATOM   1991  C CB    . ASP B 2 187  ? 136.293 120.582 143.013 1.00 51.81  ? 184  ASP A CB    1 
ATOM   1992  C CG    . ASP B 2 187  ? 136.657 119.815 141.754 1.00 53.38  ? 184  ASP A CG    1 
ATOM   1993  O OD1   . ASP B 2 187  ? 137.494 118.896 141.848 1.00 53.32  ? 184  ASP A OD1   1 
ATOM   1994  O OD2   . ASP B 2 187  ? 136.101 120.144 140.688 1.00 55.72  ? 184  ASP A OD2   1 
ATOM   1995  N N     . ILE B 2 188  ? 138.806 122.116 144.863 1.00 46.62  ? 185  ILE A N     1 
ATOM   1996  C CA    . ILE B 2 188  ? 140.086 122.882 144.812 1.00 44.22  ? 185  ILE A CA    1 
ATOM   1997  C C     . ILE B 2 188  ? 141.245 121.880 144.819 1.00 46.68  ? 185  ILE A C     1 
ATOM   1998  O O     . ILE B 2 188  ? 141.255 120.986 145.689 1.00 49.42  ? 185  ILE A O     1 
ATOM   1999  C CB    . ILE B 2 188  ? 140.177 123.890 145.976 1.00 42.86  ? 185  ILE A CB    1 
ATOM   2000  C CG1   . ILE B 2 188  ? 140.010 123.214 147.339 1.00 46.57  ? 185  ILE A CG1   1 
ATOM   2001  C CG2   . ILE B 2 188  ? 139.174 125.017 145.787 1.00 39.40  ? 185  ILE A CG2   1 
ATOM   2002  C CD1   . ILE B 2 188  ? 140.062 124.173 148.504 1.00 39.19  ? 185  ILE A CD1   1 
ATOM   2003  N N     . SER B 2 189  ? 142.177 122.020 143.874 1.00 45.17  ? 186  SER A N     1 
ATOM   2004  C CA    . SER B 2 189  ? 143.300 121.053 143.766 1.00 42.99  ? 186  SER A CA    1 
ATOM   2005  C C     . SER B 2 189  ? 144.261 121.226 144.944 1.00 42.86  ? 186  SER A C     1 
ATOM   2006  O O     . SER B 2 189  ? 145.091 120.321 145.157 1.00 44.80  ? 186  SER A O     1 
ATOM   2007  C CB    . SER B 2 189  ? 144.017 121.211 142.452 1.00 35.22  ? 186  SER A CB    1 
ATOM   2008  O OG    . SER B 2 189  ? 144.577 122.512 142.339 1.00 34.87  ? 186  SER A OG    1 
ATOM   2009  N N     . THR B 2 190  ? 144.154 122.335 145.683 1.00 42.71  ? 187  THR A N     1 
ATOM   2010  C CA    . THR B 2 190  ? 145.114 122.573 146.752 1.00 43.97  ? 187  THR A CA    1 
ATOM   2011  C C     . THR B 2 190  ? 144.912 121.656 147.951 1.00 45.91  ? 187  THR A C     1 
ATOM   2012  O O     . THR B 2 190  ? 145.752 121.658 148.857 1.00 52.52  ? 187  THR A O     1 
ATOM   2013  C CB    . THR B 2 190  ? 145.033 124.030 147.219 1.00 38.89  ? 187  THR A CB    1 
ATOM   2014  O OG1   . THR B 2 190  ? 143.682 124.339 147.588 1.00 38.93  ? 187  THR A OG1   1 
ATOM   2015  C CG2   . THR B 2 190  ? 145.478 124.974 146.115 1.00 41.00  ? 187  THR A CG2   1 
ATOM   2016  N N     . ALA B 2 191  ? 143.839 120.873 147.977 1.00 42.48  ? 188  ALA A N     1 
ATOM   2017  C CA    . ALA B 2 191  ? 143.417 120.167 149.176 1.00 43.86  ? 188  ALA A CA    1 
ATOM   2018  C C     . ALA B 2 191  ? 143.888 118.717 149.180 1.00 47.01  ? 188  ALA A C     1 
ATOM   2019  O O     . ALA B 2 191  ? 144.169 118.120 148.138 1.00 48.54  ? 188  ALA A O     1 
ATOM   2020  C CB    . ALA B 2 191  ? 141.895 120.219 149.322 1.00 44.48  ? 188  ALA A CB    1 
ATOM   2021  N N     . ILE B 2 192  ? 143.960 118.159 150.385 1.00 47.89  ? 189  ILE A N     1 
ATOM   2022  C CA    . ILE B 2 192  ? 144.341 116.767 150.606 1.00 47.84  ? 189  ILE A CA    1 
ATOM   2023  C C     . ILE B 2 192  ? 143.206 115.827 150.200 1.00 50.65  ? 189  ILE A C     1 
ATOM   2024  O O     . ILE B 2 192  ? 143.471 114.830 149.512 1.00 51.63  ? 189  ILE A O     1 
ATOM   2025  C CB    . ILE B 2 192  ? 144.767 116.537 152.067 1.00 46.17  ? 189  ILE A CB    1 
ATOM   2026  C CG1   . ILE B 2 192  ? 146.077 117.271 152.361 1.00 46.62  ? 189  ILE A CG1   1 
ATOM   2027  C CG2   . ILE B 2 192  ? 144.903 115.052 152.365 1.00 46.31  ? 189  ILE A CG2   1 
ATOM   2028  C CD1   . ILE B 2 192  ? 146.582 117.078 153.773 1.00 50.06  ? 189  ILE A CD1   1 
ATOM   2029  N N     . PRO B 2 193  ? 141.944 116.072 150.591 1.00 51.02  ? 190  PRO A N     1 
ATOM   2030  C CA    . PRO B 2 193  ? 140.873 115.171 150.124 1.00 51.20  ? 190  PRO A CA    1 
ATOM   2031  C C     . PRO B 2 193  ? 140.750 115.110 148.612 1.00 51.02  ? 190  PRO A C     1 
ATOM   2032  O O     . PRO B 2 193  ? 140.499 114.032 148.060 1.00 51.30  ? 190  PRO A O     1 
ATOM   2033  C CB    . PRO B 2 193  ? 139.614 115.760 150.774 1.00 52.45  ? 190  PRO A CB    1 
ATOM   2034  C CG    . PRO B 2 193  ? 140.112 116.458 151.978 1.00 53.13  ? 190  PRO A CG    1 
ATOM   2035  C CD    . PRO B 2 193  ? 141.424 117.049 151.567 1.00 52.18  ? 190  PRO A CD    1 
ATOM   2036  N N     . HIS B 2 194  ? 140.924 116.242 147.922 1.00 50.66  ? 191  HIS A N     1 
ATOM   2037  C CA    . HIS B 2 194  ? 140.854 116.234 146.463 1.00 47.97  ? 191  HIS A CA    1 
ATOM   2038  C C     . HIS B 2 194  ? 141.999 115.427 145.858 1.00 46.90  ? 191  HIS A C     1 
ATOM   2039  O O     . HIS B 2 194  ? 141.796 114.684 144.890 1.00 47.43  ? 191  HIS A O     1 
ATOM   2040  C CB    . HIS B 2 194  ? 140.870 117.663 145.927 1.00 47.26  ? 191  HIS A CB    1 
ATOM   2041  C CG    . HIS B 2 194  ? 141.061 117.749 144.446 1.00 48.28  ? 191  HIS A CG    1 
ATOM   2042  N ND1   . HIS B 2 194  ? 142.305 117.811 143.858 1.00 50.95  ? 191  HIS A ND1   1 
ATOM   2043  C CD2   . HIS B 2 194  ? 140.163 117.799 143.432 1.00 46.40  ? 191  HIS A CD2   1 
ATOM   2044  C CE1   . HIS B 2 194  ? 142.168 117.886 142.546 1.00 48.86  ? 191  HIS A CE1   1 
ATOM   2045  N NE2   . HIS B 2 194  ? 140.878 117.880 142.261 1.00 46.58  ? 191  HIS A NE2   1 
ATOM   2046  N N     . ARG B 2 195  ? 143.206 115.569 146.408 1.00 44.20  ? 192  ARG A N     1 
ATOM   2047  C CA    . ARG B 2 195  ? 144.345 114.800 145.916 1.00 42.29  ? 192  ARG A CA    1 
ATOM   2048  C C     . ARG B 2 195  ? 144.117 113.303 146.074 1.00 42.52  ? 192  ARG A C     1 
ATOM   2049  O O     . ARG B 2 195  ? 144.546 112.514 145.224 1.00 44.01  ? 192  ARG A O     1 
ATOM   2050  C CB    . ARG B 2 195  ? 145.617 115.234 146.648 1.00 42.33  ? 192  ARG A CB    1 
ATOM   2051  C CG    . ARG B 2 195  ? 146.864 114.422 146.324 1.00 43.26  ? 192  ARG A CG    1 
ATOM   2052  C CD    . ARG B 2 195  ? 147.171 114.413 144.834 1.00 43.42  ? 192  ARG A CD    1 
ATOM   2053  N NE    . ARG B 2 195  ? 147.268 115.758 144.271 1.00 43.74  ? 192  ARG A NE    1 
ATOM   2054  C CZ    . ARG B 2 195  ? 148.400 116.448 144.172 1.00 37.72  ? 192  ARG A CZ    1 
ATOM   2055  N NH1   . ARG B 2 195  ? 149.540 115.922 144.600 1.00 57.88  ? 192  ARG A NH1   1 
ATOM   2056  N NH2   . ARG B 2 195  ? 148.394 117.663 143.644 1.00 37.06  ? 192  ARG A NH2   1 
ATOM   2057  N N     . ILE B 2 196  ? 143.430 112.891 147.137 1.00 42.60  ? 193  ILE A N     1 
ATOM   2058  C CA    . ILE B 2 196  ? 143.203 111.469 147.378 1.00 44.76  ? 193  ILE A CA    1 
ATOM   2059  C C     . ILE B 2 196  ? 142.099 110.935 146.475 1.00 46.28  ? 193  ILE A C     1 
ATOM   2060  O O     . ILE B 2 196  ? 142.234 109.867 145.867 1.00 48.93  ? 193  ILE A O     1 
ATOM   2061  C CB    . ILE B 2 196  ? 142.881 111.227 148.863 1.00 47.51  ? 193  ILE A CB    1 
ATOM   2062  C CG1   . ILE B 2 196  ? 144.099 111.543 149.729 1.00 47.66  ? 193  ILE A CG1   1 
ATOM   2063  C CG2   . ILE B 2 196  ? 142.408 109.796 149.085 1.00 50.84  ? 193  ILE A CG2   1 
ATOM   2064  C CD1   . ILE B 2 196  ? 143.859 111.360 151.214 1.00 49.08  ? 193  ILE A CD1   1 
ATOM   2065  N N     . VAL B 2 197  ? 140.993 111.673 146.367 1.00 45.11  ? 194  VAL A N     1 
ATOM   2066  C CA    . VAL B 2 197  ? 139.812 111.149 145.694 1.00 45.99  ? 194  VAL A CA    1 
ATOM   2067  C C     . VAL B 2 197  ? 139.914 111.312 144.181 1.00 46.95  ? 194  VAL A C     1 
ATOM   2068  O O     . VAL B 2 197  ? 139.613 110.382 143.425 1.00 51.34  ? 194  VAL A O     1 
ATOM   2069  C CB    . VAL B 2 197  ? 138.549 111.827 146.256 1.00 47.44  ? 194  VAL A CB    1 
ATOM   2070  C CG1   . VAL B 2 197  ? 137.314 111.358 145.504 1.00 46.92  ? 194  VAL A CG1   1 
ATOM   2071  C CG2   . VAL B 2 197  ? 138.415 111.543 147.746 1.00 49.10  ? 194  VAL A CG2   1 
ATOM   2072  N N     . GLN B 2 198  ? 140.339 112.484 143.708 1.00 45.02  ? 195  GLN A N     1 
ATOM   2073  C CA    . GLN B 2 198  ? 140.230 112.817 142.294 1.00 45.99  ? 195  GLN A CA    1 
ATOM   2074  C C     . GLN B 2 198  ? 141.554 112.813 141.543 1.00 51.42  ? 195  GLN A C     1 
ATOM   2075  O O     . GLN B 2 198  ? 141.544 112.956 140.316 1.00 54.12  ? 195  GLN A O     1 
ATOM   2076  C CB    . GLN B 2 198  ? 139.560 114.188 142.131 1.00 42.70  ? 195  GLN A CB    1 
ATOM   2077  C CG    . GLN B 2 198  ? 138.223 114.295 142.848 1.00 42.95  ? 195  GLN A CG    1 
ATOM   2078  C CD    . GLN B 2 198  ? 137.627 115.684 142.778 1.00 43.57  ? 195  GLN A CD    1 
ATOM   2079  O OE1   . GLN B 2 198  ? 137.154 116.219 143.779 1.00 42.98  ? 195  GLN A OE1   1 
ATOM   2080  N NE2   . GLN B 2 198  ? 137.637 116.274 141.588 1.00 44.95  ? 195  GLN A NE2   1 
ATOM   2081  N N     . ASP B 2 199  ? 142.685 112.650 142.229 1.00 52.81  ? 196  ASP A N     1 
ATOM   2082  C CA    . ASP B 2 199  ? 143.987 112.623 141.576 1.00 53.13  ? 196  ASP A CA    1 
ATOM   2083  C C     . ASP B 2 199  ? 144.638 111.247 141.643 1.00 52.75  ? 196  ASP A C     1 
ATOM   2084  O O     . ASP B 2 199  ? 144.948 110.659 140.604 1.00 53.41  ? 196  ASP A O     1 
ATOM   2085  C CB    . ASP B 2 199  ? 144.915 113.678 142.195 1.00 57.35  ? 196  ASP A CB    1 
ATOM   2086  C CG    . ASP B 2 199  ? 144.754 115.045 141.557 1.00 61.57  ? 196  ASP A CG    1 
ATOM   2087  O OD1   . ASP B 2 199  ? 144.355 115.110 140.375 1.00 61.13  ? 196  ASP A OD1   1 
ATOM   2088  O OD2   . ASP B 2 199  ? 145.039 116.056 142.234 1.00 63.77  ? 196  ASP A OD2   1 
ATOM   2089  N N     . ASN B 2 200  ? 144.850 110.710 142.846 1.00 52.35  ? 197  ASN A N     1 
ATOM   2090  C CA    . ASN B 2 200  ? 145.633 109.485 142.974 1.00 50.77  ? 197  ASN A CA    1 
ATOM   2091  C C     . ASN B 2 200  ? 144.790 108.232 142.752 1.00 50.48  ? 197  ASN A C     1 
ATOM   2092  O O     . ASN B 2 200  ? 145.273 107.264 142.153 1.00 50.23  ? 197  ASN A O     1 
ATOM   2093  C CB    . ASN B 2 200  ? 146.311 109.437 144.344 1.00 49.95  ? 197  ASN A CB    1 
ATOM   2094  C CG    . ASN B 2 200  ? 147.533 110.331 144.417 1.00 46.83  ? 197  ASN A CG    1 
ATOM   2095  O OD1   . ASN B 2 200  ? 148.073 110.748 143.392 1.00 40.29  ? 197  ASN A OD1   1 
ATOM   2096  N ND2   . ASN B 2 200  ? 147.984 110.621 145.634 1.00 46.84  ? 197  ASN A ND2   1 
ATOM   2097  N N     . PHE B 2 201  ? 143.543 108.220 143.225 1.00 49.23  ? 198  PHE A N     1 
ATOM   2098  C CA    . PHE B 2 201  ? 142.735 107.010 143.084 1.00 50.96  ? 198  PHE A CA    1 
ATOM   2099  C C     . PHE B 2 201  ? 142.440 106.658 141.631 1.00 48.80  ? 198  PHE A C     1 
ATOM   2100  O O     . PHE B 2 201  ? 142.571 105.474 141.272 1.00 48.44  ? 198  PHE A O     1 
ATOM   2101  C CB    . PHE B 2 201  ? 141.440 107.130 143.895 1.00 51.80  ? 198  PHE A CB    1 
ATOM   2102  C CG    . PHE B 2 201  ? 140.510 105.965 143.708 1.00 53.76  ? 198  PHE A CG    1 
ATOM   2103  C CD1   . PHE B 2 201  ? 140.775 104.748 144.313 1.00 55.29  ? 198  PHE A CD1   1 
ATOM   2104  C CD2   . PHE B 2 201  ? 139.383 106.079 142.911 1.00 55.12  ? 198  PHE A CD2   1 
ATOM   2105  C CE1   . PHE B 2 201  ? 139.929 103.669 144.136 1.00 57.04  ? 198  PHE A CE1   1 
ATOM   2106  C CE2   . PHE B 2 201  ? 138.530 105.004 142.732 1.00 56.41  ? 198  PHE A CE2   1 
ATOM   2107  C CZ    . PHE B 2 201  ? 138.803 103.797 143.346 1.00 57.31  ? 198  PHE A CZ    1 
ATOM   2108  N N     . PRO B 2 202  ? 142.031 107.587 140.757 1.00 45.03  ? 199  PRO A N     1 
ATOM   2109  C CA    . PRO B 2 202  ? 141.914 107.221 139.334 1.00 43.90  ? 199  PRO A CA    1 
ATOM   2110  C C     . PRO B 2 202  ? 143.214 106.702 138.746 1.00 44.03  ? 199  PRO A C     1 
ATOM   2111  O O     . PRO B 2 202  ? 143.181 105.860 137.839 1.00 44.03  ? 199  PRO A O     1 
ATOM   2112  C CB    . PRO B 2 202  ? 141.472 108.534 138.671 1.00 40.33  ? 199  PRO A CB    1 
ATOM   2113  C CG    . PRO B 2 202  ? 140.766 109.267 139.748 1.00 39.75  ? 199  PRO A CG    1 
ATOM   2114  C CD    . PRO B 2 202  ? 141.522 108.950 141.005 1.00 42.11  ? 199  PRO A CD    1 
ATOM   2115  N N     . LYS B 2 203  ? 144.359 107.176 139.240 1.00 41.78  ? 200  LYS A N     1 
ATOM   2116  C CA    . LYS B 2 203  ? 145.635 106.601 138.831 1.00 41.65  ? 200  LYS A CA    1 
ATOM   2117  C C     . LYS B 2 203  ? 145.808 105.200 139.403 1.00 46.11  ? 200  LYS A C     1 
ATOM   2118  O O     . LYS B 2 203  ? 146.198 104.270 138.686 1.00 47.39  ? 200  LYS A O     1 
ATOM   2119  C CB    . LYS B 2 203  ? 146.786 107.510 139.271 1.00 40.83  ? 200  LYS A CB    1 
ATOM   2120  C CG    . LYS B 2 203  ? 146.759 108.894 138.644 1.00 41.28  ? 200  LYS A CG    1 
ATOM   2121  C CD    . LYS B 2 203  ? 147.883 109.768 139.176 1.00 40.85  ? 200  LYS A CD    1 
ATOM   2122  C CE    . LYS B 2 203  ? 147.797 111.179 138.615 1.00 41.63  ? 200  LYS A CE    1 
ATOM   2123  N NZ    . LYS B 2 203  ? 147.823 111.189 137.124 1.00 44.33  ? 200  LYS A NZ    1 
ATOM   2124  N N     . PHE B 2 204  ? 145.516 105.029 140.694 1.00 47.99  ? 201  PHE A N     1 
ATOM   2125  C CA    . PHE B 2 204  ? 145.631 103.711 141.310 1.00 46.10  ? 201  PHE A CA    1 
ATOM   2126  C C     . PHE B 2 204  ? 144.612 102.738 140.728 1.00 46.55  ? 201  PHE A C     1 
ATOM   2127  O O     . PHE B 2 204  ? 144.928 101.566 140.496 1.00 46.01  ? 201  PHE A O     1 
ATOM   2128  C CB    . PHE B 2 204  ? 145.464 103.822 142.825 1.00 43.93  ? 201  PHE A CB    1 
ATOM   2129  C CG    . PHE B 2 204  ? 145.485 102.498 143.532 1.00 46.69  ? 201  PHE A CG    1 
ATOM   2130  C CD1   . PHE B 2 204  ? 146.685 101.877 143.829 1.00 48.40  ? 201  PHE A CD1   1 
ATOM   2131  C CD2   . PHE B 2 204  ? 144.304 101.875 143.901 1.00 48.37  ? 201  PHE A CD2   1 
ATOM   2132  C CE1   . PHE B 2 204  ? 146.708 100.658 144.478 1.00 49.32  ? 201  PHE A CE1   1 
ATOM   2133  C CE2   . PHE B 2 204  ? 144.321 100.655 144.549 1.00 48.68  ? 201  PHE A CE2   1 
ATOM   2134  C CZ    . PHE B 2 204  ? 145.524 100.048 144.839 1.00 48.93  ? 201  PHE A CZ    1 
ATOM   2135  N N     . LYS B 2 205  ? 143.385 103.207 140.493 1.00 47.92  ? 202  LYS A N     1 
ATOM   2136  C CA    . LYS B 2 205  ? 142.363 102.358 139.888 1.00 50.01  ? 202  LYS A CA    1 
ATOM   2137  C C     . LYS B 2 205  ? 142.777 101.907 138.491 1.00 50.96  ? 202  LYS A C     1 
ATOM   2138  O O     . LYS B 2 205  ? 142.547 100.753 138.109 1.00 51.99  ? 202  LYS A O     1 
ATOM   2139  C CB    . LYS B 2 205  ? 141.030 103.106 139.847 1.00 49.07  ? 202  LYS A CB    1 
ATOM   2140  C CG    . LYS B 2 205  ? 139.964 102.470 138.977 1.00 47.14  ? 202  LYS A CG    1 
ATOM   2141  C CD    . LYS B 2 205  ? 138.714 103.332 138.954 1.00 44.43  ? 202  LYS A CD    1 
ATOM   2142  C CE    . LYS B 2 205  ? 137.777 102.920 137.837 1.00 45.83  ? 202  LYS A CE    1 
ATOM   2143  N NZ    . LYS B 2 205  ? 137.309 101.514 137.979 1.00 49.36  ? 202  LYS A NZ    1 
ATOM   2144  N N     . GLU B 2 206  ? 143.395 102.802 137.717 1.00 50.24  ? 203  GLU A N     1 
ATOM   2145  C CA    . GLU B 2 206  ? 143.904 102.417 136.405 1.00 48.73  ? 203  GLU A CA    1 
ATOM   2146  C C     . GLU B 2 206  ? 145.063 101.435 136.520 1.00 48.01  ? 203  GLU A C     1 
ATOM   2147  O O     . GLU B 2 206  ? 145.197 100.539 135.682 1.00 47.75  ? 203  GLU A O     1 
ATOM   2148  C CB    . GLU B 2 206  ? 144.331 103.660 135.625 1.00 48.35  ? 203  GLU A CB    1 
ATOM   2149  C CG    . GLU B 2 206  ? 144.988 103.376 134.281 1.00 51.03  ? 203  GLU A CG    1 
ATOM   2150  C CD    . GLU B 2 206  ? 144.039 102.746 133.275 1.00 55.86  ? 203  GLU A CD    1 
ATOM   2151  O OE1   . GLU B 2 206  ? 142.808 102.838 133.467 1.00 59.20  ? 203  GLU A OE1   1 
ATOM   2152  O OE2   . GLU B 2 206  ? 144.527 102.159 132.286 1.00 56.88  ? 203  GLU A OE2   1 
ATOM   2153  N N     . ASN B 2 207  ? 145.898 101.577 137.553 1.00 49.86  ? 204  ASN A N     1 
ATOM   2154  C CA    . ASN B 2 207  ? 147.015 100.654 137.734 1.00 49.74  ? 204  ASN A CA    1 
ATOM   2155  C C     . ASN B 2 207  ? 146.523 99.230  137.959 1.00 50.71  ? 204  ASN A C     1 
ATOM   2156  O O     . ASN B 2 207  ? 147.119 98.273  137.452 1.00 51.39  ? 204  ASN A O     1 
ATOM   2157  C CB    . ASN B 2 207  ? 147.894 101.109 138.900 1.00 50.18  ? 204  ASN A CB    1 
ATOM   2158  C CG    . ASN B 2 207  ? 148.797 102.274 138.532 1.00 49.25  ? 204  ASN A CG    1 
ATOM   2159  O OD1   . ASN B 2 207  ? 148.725 102.808 137.424 1.00 51.01  ? 204  ASN A OD1   1 
ATOM   2160  N ND2   . ASN B 2 207  ? 149.653 102.676 139.466 1.00 45.34  ? 204  ASN A ND2   1 
ATOM   2161  N N     . CYS B 2 208  ? 145.437 99.070  138.718 1.00 51.88  ? 205  CYS A N     1 
ATOM   2162  C CA    . CYS B 2 208  ? 144.886 97.740  138.948 1.00 54.00  ? 205  CYS A CA    1 
ATOM   2163  C C     . CYS B 2 208  ? 144.360 97.120  137.661 1.00 56.69  ? 205  CYS A C     1 
ATOM   2164  O O     . CYS B 2 208  ? 144.452 95.901  137.477 1.00 60.05  ? 205  CYS A O     1 
ATOM   2165  C CB    . CYS B 2 208  ? 143.775 97.804  139.996 1.00 56.49  ? 205  CYS A CB    1 
ATOM   2166  S SG    . CYS B 2 208  ? 144.264 98.581  141.552 1.00 58.59  ? 205  CYS A SG    1 
ATOM   2167  N N     . HIS B 2 209  ? 143.808 97.938  136.762 1.00 54.86  ? 206  HIS A N     1 
ATOM   2168  C CA    . HIS B 2 209  ? 143.293 97.410  135.504 1.00 53.39  ? 206  HIS A CA    1 
ATOM   2169  C C     . HIS B 2 209  ? 144.428 97.044  134.555 1.00 53.76  ? 206  HIS A C     1 
ATOM   2170  O O     . HIS B 2 209  ? 144.349 96.032  133.848 1.00 55.26  ? 206  HIS A O     1 
ATOM   2171  C CB    . HIS B 2 209  ? 142.352 98.427  134.859 1.00 53.68  ? 206  HIS A CB    1 
ATOM   2172  C CG    . HIS B 2 209  ? 141.665 97.918  133.630 1.00 59.22  ? 206  HIS A CG    1 
ATOM   2173  N ND1   . HIS B 2 209  ? 141.947 98.393  132.367 1.00 62.09  ? 206  HIS A ND1   1 
ATOM   2174  C CD2   . HIS B 2 209  ? 140.707 96.974  133.472 1.00 64.63  ? 206  HIS A CD2   1 
ATOM   2175  C CE1   . HIS B 2 209  ? 141.192 97.764  131.485 1.00 65.48  ? 206  HIS A CE1   1 
ATOM   2176  N NE2   . HIS B 2 209  ? 140.432 96.896  132.129 1.00 66.67  ? 206  HIS A NE2   1 
ATOM   2177  N N     . ILE B 2 210  ? 145.487 97.856  134.521 1.00 50.80  ? 207  ILE A N     1 
ATOM   2178  C CA    . ILE B 2 210  ? 146.654 97.523  133.708 1.00 52.06  ? 207  ILE A CA    1 
ATOM   2179  C C     . ILE B 2 210  ? 147.300 96.240  134.212 1.00 54.26  ? 207  ILE A C     1 
ATOM   2180  O O     . ILE B 2 210  ? 147.791 95.419  133.425 1.00 52.97  ? 207  ILE A O     1 
ATOM   2181  C CB    . ILE B 2 210  ? 147.653 98.696  133.703 1.00 50.86  ? 207  ILE A CB    1 
ATOM   2182  C CG1   . ILE B 2 210  ? 147.009 99.947  133.105 1.00 51.17  ? 207  ILE A CG1   1 
ATOM   2183  C CG2   . ILE B 2 210  ? 148.915 98.331  132.937 1.00 48.81  ? 207  ILE A CG2   1 
ATOM   2184  C CD1   . ILE B 2 210  ? 147.910 101.160 133.128 1.00 50.14  ? 207  ILE A CD1   1 
ATOM   2185  N N     . PHE B 2 211  ? 147.296 96.039  135.531 1.00 56.95  ? 208  PHE A N     1 
ATOM   2186  C CA    . PHE B 2 211  ? 147.930 94.862  136.114 1.00 58.13  ? 208  PHE A CA    1 
ATOM   2187  C C     . PHE B 2 211  ? 147.218 93.582  135.688 1.00 63.71  ? 208  PHE A C     1 
ATOM   2188  O O     . PHE B 2 211  ? 147.844 92.662  135.150 1.00 66.74  ? 208  PHE A O     1 
ATOM   2189  C CB    . PHE B 2 211  ? 147.952 94.992  137.637 1.00 56.09  ? 208  PHE A CB    1 
ATOM   2190  C CG    . PHE B 2 211  ? 148.451 93.766  138.349 1.00 56.86  ? 208  PHE A CG    1 
ATOM   2191  C CD1   . PHE B 2 211  ? 149.808 93.527  138.477 1.00 56.92  ? 208  PHE A CD1   1 
ATOM   2192  C CD2   . PHE B 2 211  ? 147.561 92.860  138.902 1.00 58.33  ? 208  PHE A CD2   1 
ATOM   2193  C CE1   . PHE B 2 211  ? 150.269 92.401  139.137 1.00 58.89  ? 208  PHE A CE1   1 
ATOM   2194  C CE2   . PHE B 2 211  ? 148.014 91.733  139.561 1.00 59.39  ? 208  PHE A CE2   1 
ATOM   2195  C CZ    . PHE B 2 211  ? 149.370 91.503  139.680 1.00 59.60  ? 208  PHE A CZ    1 
ATOM   2196  N N     . THR B 2 212  ? 145.902 93.512  135.909 1.00 65.50  ? 209  THR A N     1 
ATOM   2197  C CA    . THR B 2 212  ? 145.178 92.272  135.645 1.00 66.58  ? 209  THR A CA    1 
ATOM   2198  C C     . THR B 2 212  ? 145.136 91.939  134.158 1.00 64.64  ? 209  THR A C     1 
ATOM   2199  O O     . THR B 2 212  ? 145.080 90.760  133.793 1.00 67.48  ? 209  THR A O     1 
ATOM   2200  C CB    . THR B 2 212  ? 143.760 92.353  136.209 1.00 68.88  ? 209  THR A CB    1 
ATOM   2201  O OG1   . THR B 2 212  ? 143.033 93.389  135.537 1.00 70.87  ? 209  THR A OG1   1 
ATOM   2202  C CG2   . THR B 2 212  ? 143.797 92.652  137.699 1.00 69.33  ? 209  THR A CG2   1 
ATOM   2203  N N     . ARG B 2 213  ? 145.163 92.950  133.285 1.00 61.32  ? 210  ARG A N     1 
ATOM   2204  C CA    . ARG B 2 213  ? 145.179 92.674  131.852 1.00 62.46  ? 210  ARG A CA    1 
ATOM   2205  C C     . ARG B 2 213  ? 146.495 92.035  131.426 1.00 64.13  ? 210  ARG A C     1 
ATOM   2206  O O     . ARG B 2 213  ? 146.507 91.126  130.588 1.00 66.76  ? 210  ARG A O     1 
ATOM   2207  C CB    . ARG B 2 213  ? 144.925 93.952  131.055 1.00 61.76  ? 210  ARG A CB    1 
ATOM   2208  C CG    . ARG B 2 213  ? 143.486 94.429  131.085 1.00 66.62  ? 210  ARG A CG    1 
ATOM   2209  C CD    . ARG B 2 213  ? 143.212 95.388  129.939 1.00 69.61  ? 210  ARG A CD    1 
ATOM   2210  N NE    . ARG B 2 213  ? 143.311 94.724  128.643 1.00 73.49  ? 210  ARG A NE    1 
ATOM   2211  C CZ    . ARG B 2 213  ? 143.201 95.345  127.473 1.00 75.30  ? 210  ARG A CZ    1 
ATOM   2212  N NH1   . ARG B 2 213  ? 142.991 96.653  127.432 1.00 74.58  ? 210  ARG A NH1   1 
ATOM   2213  N NH2   . ARG B 2 213  ? 143.304 94.658  126.343 1.00 75.78  ? 210  ARG A NH2   1 
ATOM   2214  N N     . LEU B 2 214  ? 147.614 92.496  131.991 1.00 60.40  ? 211  LEU A N     1 
ATOM   2215  C CA    . LEU B 2 214  ? 148.906 91.903  131.661 1.00 56.19  ? 211  LEU A CA    1 
ATOM   2216  C C     . LEU B 2 214  ? 149.032 90.496  132.233 1.00 58.63  ? 211  LEU A C     1 
ATOM   2217  O O     . LEU B 2 214  ? 149.527 89.587  131.554 1.00 58.47  ? 211  LEU A O     1 
ATOM   2218  C CB    . LEU B 2 214  ? 150.040 92.792  132.171 1.00 51.00  ? 211  LEU A CB    1 
ATOM   2219  C CG    . LEU B 2 214  ? 150.220 94.158  131.504 1.00 46.48  ? 211  LEU A CG    1 
ATOM   2220  C CD1   . LEU B 2 214  ? 151.316 94.955  132.200 1.00 43.47  ? 211  LEU A CD1   1 
ATOM   2221  C CD2   . LEU B 2 214  ? 150.530 94.003  130.025 1.00 43.76  ? 211  LEU A CD2   1 
ATOM   2222  N N     . ILE B 2 215  ? 148.585 90.295  133.474 1.00 61.06  ? 212  ILE A N     1 
ATOM   2223  C CA    . ILE B 2 215  ? 148.726 88.989  134.114 1.00 64.53  ? 212  ILE A CA    1 
ATOM   2224  C C     . ILE B 2 215  ? 147.850 87.950  133.428 1.00 67.37  ? 212  ILE A C     1 
ATOM   2225  O O     . ILE B 2 215  ? 148.219 86.772  133.346 1.00 71.35  ? 212  ILE A O     1 
ATOM   2226  C CB    . ILE B 2 215  ? 148.409 89.097  135.617 1.00 67.42  ? 212  ILE A CB    1 
ATOM   2227  C CG1   . ILE B 2 215  ? 149.311 90.141  136.280 1.00 67.04  ? 212  ILE A CG1   1 
ATOM   2228  C CG2   . ILE B 2 215  ? 148.568 87.752  136.306 1.00 70.25  ? 212  ILE A CG2   1 
ATOM   2229  C CD1   . ILE B 2 215  ? 150.777 89.996  135.936 1.00 64.77  ? 212  ILE A CD1   1 
ATOM   2230  N N     . THR B 2 216  ? 146.685 88.355  132.921 1.00 67.19  ? 213  THR A N     1 
ATOM   2231  C CA    . THR B 2 216  ? 145.818 87.402  132.237 1.00 69.20  ? 213  THR A CA    1 
ATOM   2232  C C     . THR B 2 216  ? 146.405 86.989  130.893 1.00 68.66  ? 213  THR A C     1 
ATOM   2233  O O     . THR B 2 216  ? 146.380 85.806  130.535 1.00 71.03  ? 213  THR A O     1 
ATOM   2234  C CB    . THR B 2 216  ? 144.420 87.994  132.058 1.00 69.13  ? 213  THR A CB    1 
ATOM   2235  O OG1   . THR B 2 216  ? 143.886 88.352  133.339 1.00 69.23  ? 213  THR A OG1   1 
ATOM   2236  C CG2   . THR B 2 216  ? 143.493 86.984  131.397 1.00 70.97  ? 213  THR A CG2   1 
ATOM   2237  N N     . ALA B 2 217  ? 146.950 87.946  130.140 1.00 66.99  ? 214  ALA A N     1 
ATOM   2238  C CA    . ALA B 2 217  ? 147.541 87.623  128.845 1.00 67.93  ? 214  ALA A CA    1 
ATOM   2239  C C     . ALA B 2 217  ? 148.889 86.930  129.007 1.00 68.20  ? 214  ALA A C     1 
ATOM   2240  O O     . ALA B 2 217  ? 149.154 85.915  128.354 1.00 70.74  ? 214  ALA A O     1 
ATOM   2241  C CB    . ALA B 2 217  ? 147.685 88.891  128.003 1.00 65.45  ? 214  ALA A CB    1 
ATOM   2242  N N     . VAL B 2 218  ? 149.750 87.460  129.871 1.00 64.72  ? 215  VAL A N     1 
ATOM   2243  C CA    . VAL B 2 218  ? 151.066 86.871  130.113 1.00 61.88  ? 215  VAL A CA    1 
ATOM   2244  C C     . VAL B 2 218  ? 151.160 86.478  131.583 1.00 63.91  ? 215  VAL A C     1 
ATOM   2245  O O     . VAL B 2 218  ? 151.621 87.280  132.409 1.00 62.67  ? 215  VAL A O     1 
ATOM   2246  C CB    . VAL B 2 218  ? 152.192 87.839  129.715 1.00 57.65  ? 215  VAL A CB    1 
ATOM   2247  C CG1   . VAL B 2 218  ? 153.546 87.153  129.826 1.00 57.44  ? 215  VAL A CG1   1 
ATOM   2248  C CG2   . VAL B 2 218  ? 151.969 88.365  128.305 1.00 54.60  ? 215  VAL A CG2   1 
ATOM   2249  N N     . PRO B 2 219  ? 150.735 85.268  131.956 1.00 67.37  ? 216  PRO A N     1 
ATOM   2250  C CA    . PRO B 2 219  ? 150.760 84.888  133.379 1.00 70.11  ? 216  PRO A CA    1 
ATOM   2251  C C     . PRO B 2 219  ? 152.156 84.829  133.974 1.00 70.60  ? 216  PRO A C     1 
ATOM   2252  O O     . PRO B 2 219  ? 152.304 84.988  135.193 1.00 72.10  ? 216  PRO A O     1 
ATOM   2253  C CB    . PRO B 2 219  ? 150.084 83.510  133.386 1.00 71.86  ? 216  PRO A CB    1 
ATOM   2254  C CG    . PRO B 2 219  ? 149.269 83.477  132.132 1.00 71.81  ? 216  PRO A CG    1 
ATOM   2255  C CD    . PRO B 2 219  ? 150.056 84.259  131.126 1.00 69.31  ? 216  PRO A CD    1 
ATOM   2256  N N     . SER B 2 220  ? 153.186 84.597  133.157 1.00 70.69  ? 217  SER A N     1 
ATOM   2257  C CA    . SER B 2 220  ? 154.550 84.580  133.671 1.00 70.11  ? 217  SER A CA    1 
ATOM   2258  C C     . SER B 2 220  ? 154.963 85.930  134.241 1.00 72.13  ? 217  SER A C     1 
ATOM   2259  O O     . SER B 2 220  ? 155.887 85.992  135.058 1.00 73.31  ? 217  SER A O     1 
ATOM   2260  C CB    . SER B 2 220  ? 155.524 84.160  132.570 1.00 66.62  ? 217  SER A CB    1 
ATOM   2261  O OG    . SER B 2 220  ? 155.502 85.079  131.491 1.00 64.23  ? 217  SER A OG    1 
ATOM   2262  N N     . LEU B 2 221  ? 154.293 87.008  133.828 1.00 72.36  ? 218  LEU A N     1 
ATOM   2263  C CA    . LEU B 2 221  ? 154.594 88.337  134.343 1.00 70.08  ? 218  LEU A CA    1 
ATOM   2264  C C     . LEU B 2 221  ? 154.182 88.502  135.800 1.00 69.70  ? 218  LEU A C     1 
ATOM   2265  O O     . LEU B 2 221  ? 154.650 89.435  136.461 1.00 66.73  ? 218  LEU A O     1 
ATOM   2266  C CB    . LEU B 2 221  ? 153.902 89.391  133.481 1.00 67.60  ? 218  LEU A CB    1 
ATOM   2267  C CG    . LEU B 2 221  ? 154.766 90.508  132.896 1.00 66.01  ? 218  LEU A CG    1 
ATOM   2268  C CD1   . LEU B 2 221  ? 156.044 89.944  132.300 1.00 65.68  ? 218  LEU A CD1   1 
ATOM   2269  C CD2   . LEU B 2 221  ? 153.974 91.260  131.844 1.00 65.72  ? 218  LEU A CD2   1 
ATOM   2270  N N     . ARG B 2 222  ? 153.318 87.622  136.313 1.00 72.45  ? 219  ARG A N     1 
ATOM   2271  C CA    . ARG B 2 222  ? 152.891 87.717  137.705 1.00 73.88  ? 219  ARG A CA    1 
ATOM   2272  C C     . ARG B 2 222  ? 154.042 87.404  138.650 1.00 74.85  ? 219  ARG A C     1 
ATOM   2273  O O     . ARG B 2 222  ? 154.375 88.204  139.532 1.00 74.50  ? 219  ARG A O     1 
ATOM   2274  C CB    . ARG B 2 222  ? 151.705 86.779  137.955 1.00 75.00  ? 219  ARG A CB    1 
ATOM   2275  C CG    . ARG B 2 222  ? 151.091 86.883  139.349 1.00 77.38  ? 219  ARG A CG    1 
ATOM   2276  C CD    . ARG B 2 222  ? 151.703 85.875  140.314 1.00 81.80  ? 219  ARG A CD    1 
ATOM   2277  N NE    . ARG B 2 222  ? 151.373 86.167  141.704 1.00 85.67  ? 219  ARG A NE    1 
ATOM   2278  C CZ    . ARG B 2 222  ? 151.927 85.556  142.747 1.00 89.55  ? 219  ARG A CZ    1 
ATOM   2279  N NH1   . ARG B 2 222  ? 152.843 84.616  142.555 1.00 90.84  ? 219  ARG A NH1   1 
ATOM   2280  N NH2   . ARG B 2 222  ? 151.567 85.885  143.980 1.00 91.28  ? 219  ARG A NH2   1 
ATOM   2281  N N     . GLU B 2 223  ? 154.660 86.232  138.485 1.00 76.59  ? 220  GLU A N     1 
ATOM   2282  C CA    . GLU B 2 223  ? 155.805 85.882  139.319 1.00 78.48  ? 220  GLU A CA    1 
ATOM   2283  C C     . GLU B 2 223  ? 156.962 86.847  139.103 1.00 78.70  ? 220  GLU A C     1 
ATOM   2284  O O     . GLU B 2 223  ? 157.760 87.074  140.020 1.00 80.10  ? 220  GLU A O     1 
ATOM   2285  C CB    . GLU B 2 223  ? 156.247 84.448  139.032 1.00 80.03  ? 220  GLU A CB    1 
ATOM   2286  N N     . HIS B 2 224  ? 157.063 87.434  137.908 1.00 78.14  ? 221  HIS A N     1 
ATOM   2287  C CA    . HIS B 2 224  ? 158.139 88.381  137.637 1.00 78.04  ? 221  HIS A CA    1 
ATOM   2288  C C     . HIS B 2 224  ? 157.925 89.690  138.390 1.00 76.03  ? 221  HIS A C     1 
ATOM   2289  O O     . HIS B 2 224  ? 158.878 90.262  138.932 1.00 74.48  ? 221  HIS A O     1 
ATOM   2290  C CB    . HIS B 2 224  ? 158.246 88.631  136.132 1.00 79.31  ? 221  HIS A CB    1 
ATOM   2291  C CG    . HIS B 2 224  ? 159.594 89.109  135.694 1.00 81.77  ? 221  HIS A CG    1 
ATOM   2292  N ND1   . HIS B 2 224  ? 160.122 88.813  134.455 1.00 81.94  ? 221  HIS A ND1   1 
ATOM   2293  C CD2   . HIS B 2 224  ? 160.522 89.867  136.327 1.00 82.42  ? 221  HIS A CD2   1 
ATOM   2294  C CE1   . HIS B 2 224  ? 161.318 89.364  134.345 1.00 81.01  ? 221  HIS A CE1   1 
ATOM   2295  N NE2   . HIS B 2 224  ? 161.583 90.010  135.466 1.00 81.38  ? 221  HIS A NE2   1 
ATOM   2296  N N     . PHE B 2 225  ? 156.683 90.179  138.433 1.00 74.16  ? 222  PHE A N     1 
ATOM   2297  C CA    . PHE B 2 225  ? 156.385 91.363  139.234 1.00 70.75  ? 222  PHE A CA    1 
ATOM   2298  C C     . PHE B 2 225  ? 156.600 91.087  140.718 1.00 71.71  ? 222  PHE A C     1 
ATOM   2299  O O     . PHE B 2 225  ? 157.084 91.953  141.456 1.00 69.46  ? 222  PHE A O     1 
ATOM   2300  C CB    . PHE B 2 225  ? 154.949 91.829  138.984 1.00 67.25  ? 222  PHE A CB    1 
ATOM   2301  C CG    . PHE B 2 225  ? 154.726 92.426  137.622 1.00 63.41  ? 222  PHE A CG    1 
ATOM   2302  C CD1   . PHE B 2 225  ? 155.776 92.976  136.905 1.00 62.19  ? 222  PHE A CD1   1 
ATOM   2303  C CD2   . PHE B 2 225  ? 153.458 92.442  137.062 1.00 61.50  ? 222  PHE A CD2   1 
ATOM   2304  C CE1   . PHE B 2 225  ? 155.567 93.528  135.651 1.00 58.48  ? 222  PHE A CE1   1 
ATOM   2305  C CE2   . PHE B 2 225  ? 153.244 92.991  135.808 1.00 58.65  ? 222  PHE A CE2   1 
ATOM   2306  C CZ    . PHE B 2 225  ? 154.299 93.534  135.104 1.00 56.90  ? 222  PHE A CZ    1 
ATOM   2307  N N     . GLU B 2 226  ? 156.240 89.882  141.172 1.00 76.18  ? 223  GLU A N     1 
ATOM   2308  C CA    . GLU B 2 226  ? 156.416 89.530  142.579 1.00 80.68  ? 223  GLU A CA    1 
ATOM   2309  C C     . GLU B 2 226  ? 157.889 89.517  142.967 1.00 81.80  ? 223  GLU A C     1 
ATOM   2310  O O     . GLU B 2 226  ? 158.249 89.908  144.084 1.00 82.47  ? 223  GLU A O     1 
ATOM   2311  C CB    . GLU B 2 226  ? 155.776 88.169  142.860 1.00 85.00  ? 223  GLU A CB    1 
ATOM   2312  C CG    . GLU B 2 226  ? 155.947 87.673  144.290 1.00 90.35  ? 223  GLU A CG    1 
ATOM   2313  C CD    . GLU B 2 226  ? 154.950 88.290  145.251 1.00 94.27  ? 223  GLU A CD    1 
ATOM   2314  O OE1   . GLU B 2 226  ? 153.762 88.407  144.885 1.00 94.85  ? 223  GLU A OE1   1 
ATOM   2315  O OE2   . GLU B 2 226  ? 155.353 88.661  146.375 1.00 96.61  ? 223  GLU A OE2   1 
ATOM   2316  N N     . ASN B 2 227  ? 158.759 89.074  142.055 1.00 84.12  ? 224  ASN A N     1 
ATOM   2317  C CA    . ASN B 2 227  ? 160.188 89.051  142.352 1.00 84.83  ? 224  ASN A CA    1 
ATOM   2318  C C     . ASN B 2 227  ? 160.748 90.461  142.486 1.00 81.88  ? 224  ASN A C     1 
ATOM   2319  O O     . ASN B 2 227  ? 161.629 90.706  143.319 1.00 83.93  ? 224  ASN A O     1 
ATOM   2320  C CB    . ASN B 2 227  ? 160.941 88.276  141.270 1.00 86.11  ? 224  ASN A CB    1 
ATOM   2321  C CG    . ASN B 2 227  ? 160.545 86.814  141.216 1.00 89.01  ? 224  ASN A CG    1 
ATOM   2322  O OD1   . ASN B 2 227  ? 160.295 86.189  142.246 1.00 88.84  ? 224  ASN A OD1   1 
ATOM   2323  N ND2   . ASN B 2 227  ? 160.493 86.259  140.010 1.00 91.13  ? 224  ASN A ND2   1 
ATOM   2324  N N     . VAL B 2 228  ? 160.253 91.399  141.676 1.00 77.14  ? 225  VAL A N     1 
ATOM   2325  C CA    . VAL B 2 228  ? 160.718 92.781  141.770 1.00 73.62  ? 225  VAL A CA    1 
ATOM   2326  C C     . VAL B 2 228  ? 160.332 93.380  143.116 1.00 72.48  ? 225  VAL A C     1 
ATOM   2327  O O     . VAL B 2 228  ? 161.110 94.121  143.730 1.00 72.08  ? 225  VAL A O     1 
ATOM   2328  C CB    . VAL B 2 228  ? 160.166 93.612  140.597 1.00 70.02  ? 225  VAL A CB    1 
ATOM   2329  C CG1   . VAL B 2 228  ? 160.608 95.063  140.715 1.00 67.54  ? 225  VAL A CG1   1 
ATOM   2330  C CG2   . VAL B 2 228  ? 160.620 93.024  139.271 1.00 68.30  ? 225  VAL A CG2   1 
ATOM   2331  N N     . LYS B 2 229  ? 159.130 93.063  143.602 1.00 71.50  ? 226  LYS A N     1 
ATOM   2332  C CA    . LYS B 2 229  ? 158.697 93.587  144.893 1.00 70.90  ? 226  LYS A CA    1 
ATOM   2333  C C     . LYS B 2 229  ? 159.511 92.989  146.033 1.00 74.76  ? 226  LYS A C     1 
ATOM   2334  O O     . LYS B 2 229  ? 159.872 93.695  146.982 1.00 75.26  ? 226  LYS A O     1 
ATOM   2335  C CB    . LYS B 2 229  ? 157.207 93.315  145.098 1.00 68.59  ? 226  LYS A CB    1 
ATOM   2336  C CG    . LYS B 2 229  ? 156.563 94.183  146.167 1.00 67.33  ? 226  LYS A CG    1 
ATOM   2337  C CD    . LYS B 2 229  ? 155.556 93.402  146.989 1.00 68.21  ? 226  LYS A CD    1 
ATOM   2338  C CE    . LYS B 2 229  ? 156.250 92.342  147.829 1.00 72.35  ? 226  LYS A CE    1 
ATOM   2339  N NZ    . LYS B 2 229  ? 155.301 91.633  148.730 1.00 76.36  ? 226  LYS A NZ    1 
ATOM   2340  N N     . LYS B 2 230  ? 159.811 91.689  145.957 1.00 78.69  ? 227  LYS A N     1 
ATOM   2341  C CA    . LYS B 2 230  ? 160.594 91.046  147.007 1.00 82.93  ? 227  LYS A CA    1 
ATOM   2342  C C     . LYS B 2 230  ? 162.058 91.463  146.960 1.00 84.30  ? 227  LYS A C     1 
ATOM   2343  O O     . LYS B 2 230  ? 162.710 91.546  148.007 1.00 82.57  ? 227  LYS A O     1 
ATOM   2344  C CB    . LYS B 2 230  ? 160.475 89.525  146.898 1.00 85.07  ? 227  LYS A CB    1 
ATOM   2345  C CG    . LYS B 2 230  ? 159.095 88.972  147.225 1.00 87.04  ? 227  LYS A CG    1 
ATOM   2346  C CD    . LYS B 2 230  ? 159.081 87.450  147.150 1.00 89.07  ? 227  LYS A CD    1 
ATOM   2347  C CE    . LYS B 2 230  ? 157.745 86.882  147.606 1.00 90.62  ? 227  LYS A CE    1 
ATOM   2348  N NZ    . LYS B 2 230  ? 157.723 85.393  147.557 1.00 91.59  ? 227  LYS A NZ    1 
ATOM   2349  N N     . ALA B 2 231  ? 162.591 91.726  145.764 1.00 89.28  ? 228  ALA A N     1 
ATOM   2350  C CA    . ALA B 2 231  ? 163.998 92.089  145.641 1.00 88.26  ? 228  ALA A CA    1 
ATOM   2351  C C     . ALA B 2 231  ? 164.292 93.486  146.172 1.00 88.39  ? 228  ALA A C     1 
ATOM   2352  O O     . ALA B 2 231  ? 165.450 93.786  146.478 1.00 89.54  ? 228  ALA A O     1 
ATOM   2353  C CB    . ALA B 2 231  ? 164.445 91.988  144.182 1.00 85.51  ? 228  ALA A CB    1 
ATOM   2354  N N     . ILE B 2 232  ? 163.281 94.343  146.284 1.00 87.16  ? 229  ILE A N     1 
ATOM   2355  C CA    . ILE B 2 232  ? 163.490 95.692  146.801 1.00 86.15  ? 229  ILE A CA    1 
ATOM   2356  C C     . ILE B 2 232  ? 163.265 95.753  148.306 1.00 89.54  ? 229  ILE A C     1 
ATOM   2357  O O     . ILE B 2 232  ? 164.040 96.381  149.031 1.00 92.63  ? 229  ILE A O     1 
ATOM   2358  C CB    . ILE B 2 232  ? 162.580 96.687  146.055 1.00 81.39  ? 229  ILE A CB    1 
ATOM   2359  C CG1   . ILE B 2 232  ? 162.922 96.711  144.565 1.00 79.22  ? 229  ILE A CG1   1 
ATOM   2360  C CG2   . ILE B 2 232  ? 162.716 98.077  146.647 1.00 80.39  ? 229  ILE A CG2   1 
ATOM   2361  C CD1   . ILE B 2 232  ? 162.135 97.737  143.780 1.00 75.42  ? 229  ILE A CD1   1 
ATOM   2362  N N     . GLY B 2 233  ? 162.213 95.104  148.798 1.00 88.21  ? 230  GLY A N     1 
ATOM   2363  C CA    . GLY B 2 233  ? 161.890 95.110  150.208 1.00 89.36  ? 230  GLY A CA    1 
ATOM   2364  C C     . GLY B 2 233  ? 160.674 95.927  150.587 1.00 88.96  ? 230  GLY A C     1 
ATOM   2365  O O     . GLY B 2 233  ? 160.408 96.086  151.784 1.00 92.02  ? 230  GLY A O     1 
ATOM   2366  N N     . ILE B 2 234  ? 159.932 96.444  149.619 1.00 85.71  ? 231  ILE A N     1 
ATOM   2367  C CA    . ILE B 2 234  ? 158.754 97.262  149.875 1.00 84.82  ? 231  ILE A CA    1 
ATOM   2368  C C     . ILE B 2 234  ? 157.540 96.357  150.010 1.00 86.47  ? 231  ILE A C     1 
ATOM   2369  O O     . ILE B 2 234  ? 157.388 95.383  149.262 1.00 86.60  ? 231  ILE A O     1 
ATOM   2370  C CB    . ILE B 2 234  ? 158.555 98.294  148.749 1.00 80.76  ? 231  ILE A CB    1 
ATOM   2371  C CG1   . ILE B 2 234  ? 159.818 99.139  148.572 1.00 79.01  ? 231  ILE A CG1   1 
ATOM   2372  C CG2   . ILE B 2 234  ? 157.361 99.186  149.040 1.00 80.92  ? 231  ILE A CG2   1 
ATOM   2373  C CD1   . ILE B 2 234  ? 159.737 100.113 147.421 1.00 76.03  ? 231  ILE A CD1   1 
ATOM   2374  N N     . PHE B 2 235  ? 156.673 96.677  150.972 1.00 87.34  ? 232  PHE A N     1 
ATOM   2375  C CA    . PHE B 2 235  ? 155.404 95.978  151.176 1.00 88.25  ? 232  PHE A CA    1 
ATOM   2376  C C     . PHE B 2 235  ? 155.633 94.481  151.392 1.00 92.75  ? 232  PHE A C     1 
ATOM   2377  O O     . PHE B 2 235  ? 155.150 93.631  150.642 1.00 91.88  ? 232  PHE A O     1 
ATOM   2378  C CB    . PHE B 2 235  ? 154.449 96.226  150.002 1.00 83.62  ? 232  PHE A CB    1 
ATOM   2379  C CG    . PHE B 2 235  ? 154.218 97.682  149.698 1.00 79.27  ? 232  PHE A CG    1 
ATOM   2380  C CD1   . PHE B 2 235  ? 154.199 98.628  150.711 1.00 79.06  ? 232  PHE A CD1   1 
ATOM   2381  C CD2   . PHE B 2 235  ? 154.017 98.104  148.393 1.00 75.89  ? 232  PHE A CD2   1 
ATOM   2382  C CE1   . PHE B 2 235  ? 153.986 99.965  150.428 1.00 76.80  ? 232  PHE A CE1   1 
ATOM   2383  C CE2   . PHE B 2 235  ? 153.804 99.440  148.105 1.00 73.89  ? 232  PHE A CE2   1 
ATOM   2384  C CZ    . PHE B 2 235  ? 153.789 100.370 149.123 1.00 74.14  ? 232  PHE A CZ    1 
ATOM   2385  N N     . VAL B 2 236  ? 156.392 94.170  152.447 1.00 100.14 ? 233  VAL A N     1 
ATOM   2386  C CA    . VAL B 2 236  ? 156.738 92.778  152.716 1.00 101.71 ? 233  VAL A CA    1 
ATOM   2387  C C     . VAL B 2 236  ? 155.516 91.986  153.164 1.00 102.99 ? 233  VAL A C     1 
ATOM   2388  O O     . VAL B 2 236  ? 155.434 90.774  152.929 1.00 104.72 ? 233  VAL A O     1 
ATOM   2389  C CB    . VAL B 2 236  ? 157.874 92.704  153.752 1.00 102.91 ? 233  VAL A CB    1 
ATOM   2390  C CG1   . VAL B 2 236  ? 159.152 93.295  153.178 1.00 100.26 ? 233  VAL A CG1   1 
ATOM   2391  C CG2   . VAL B 2 236  ? 157.480 93.427  155.032 1.00 105.70 ? 233  VAL A CG2   1 
ATOM   2392  N N     . SER B 2 237  ? 154.550 92.643  153.802 1.00 101.44 ? 234  SER A N     1 
ATOM   2393  C CA    . SER B 2 237  ? 153.352 91.980  154.298 1.00 100.90 ? 234  SER A CA    1 
ATOM   2394  C C     . SER B 2 237  ? 152.219 91.966  153.280 1.00 95.14  ? 234  SER A C     1 
ATOM   2395  O O     . SER B 2 237  ? 151.096 91.585  153.626 1.00 92.91  ? 234  SER A O     1 
ATOM   2396  C CB    . SER B 2 237  ? 152.877 92.652  155.588 1.00 104.06 ? 234  SER A CB    1 
ATOM   2397  O OG    . SER B 2 237  ? 151.653 92.093  156.034 1.00 106.64 ? 234  SER A OG    1 
ATOM   2398  N N     . THR B 2 238  ? 152.485 92.364  152.037 1.00 91.81  ? 235  THR A N     1 
ATOM   2399  C CA    . THR B 2 238  ? 151.453 92.489  151.017 1.00 87.05  ? 235  THR A CA    1 
ATOM   2400  C C     . THR B 2 238  ? 151.943 91.858  149.723 1.00 83.66  ? 235  THR A C     1 
ATOM   2401  O O     . THR B 2 238  ? 153.037 92.180  149.248 1.00 86.08  ? 235  THR A O     1 
ATOM   2402  C CB    . THR B 2 238  ? 151.091 93.959  150.783 1.00 82.71  ? 235  THR A CB    1 
ATOM   2403  O OG1   . THR B 2 238  ? 151.057 94.650  152.039 1.00 82.34  ? 235  THR A OG1   1 
ATOM   2404  C CG2   . THR B 2 238  ? 149.731 94.070  150.124 1.00 81.03  ? 235  THR A CG2   1 
ATOM   2405  N N     . SER B 2 239  ? 151.135 90.965  149.156 1.00 80.10  ? 236  SER A N     1 
ATOM   2406  C CA    . SER B 2 239  ? 151.486 90.332  147.895 1.00 78.19  ? 236  SER A CA    1 
ATOM   2407  C C     . SER B 2 239  ? 151.307 91.316  146.740 1.00 77.76  ? 236  SER A C     1 
ATOM   2408  O O     . SER B 2 239  ? 150.812 92.436  146.906 1.00 79.26  ? 236  SER A O     1 
ATOM   2409  C CB    . SER B 2 239  ? 150.639 89.082  147.664 1.00 79.97  ? 236  SER A CB    1 
ATOM   2410  O OG    . SER B 2 239  ? 149.280 89.422  147.456 1.00 81.28  ? 236  SER A OG    1 
ATOM   2411  N N     . ILE B 2 240  ? 151.713 90.882  145.543 1.00 77.51  ? 237  ILE A N     1 
ATOM   2412  C CA    . ILE B 2 240  ? 151.666 91.775  144.391 1.00 75.15  ? 237  ILE A CA    1 
ATOM   2413  C C     . ILE B 2 240  ? 150.236 91.938  143.884 1.00 76.51  ? 237  ILE A C     1 
ATOM   2414  O O     . ILE B 2 240  ? 149.890 92.974  143.305 1.00 75.56  ? 237  ILE A O     1 
ATOM   2415  C CB    . ILE B 2 240  ? 152.612 91.276  143.281 1.00 71.86  ? 237  ILE A CB    1 
ATOM   2416  C CG1   . ILE B 2 240  ? 152.796 92.353  142.208 1.00 67.73  ? 237  ILE A CG1   1 
ATOM   2417  C CG2   . ILE B 2 240  ? 152.087 89.996  142.652 1.00 72.83  ? 237  ILE A CG2   1 
ATOM   2418  C CD1   . ILE B 2 240  ? 153.358 93.653  142.736 1.00 65.15  ? 237  ILE A CD1   1 
ATOM   2419  N N     . GLU B 2 241  ? 149.382 90.934  144.091 1.00 79.70  ? 238  GLU A N     1 
ATOM   2420  C CA    . GLU B 2 241  ? 147.991 91.072  143.676 1.00 79.90  ? 238  GLU A CA    1 
ATOM   2421  C C     . GLU B 2 241  ? 147.224 92.015  144.594 1.00 78.03  ? 238  GLU A C     1 
ATOM   2422  O O     . GLU B 2 241  ? 146.296 92.697  144.144 1.00 76.17  ? 238  GLU A O     1 
ATOM   2423  C CB    . GLU B 2 241  ? 147.308 89.704  143.634 1.00 84.76  ? 238  GLU A CB    1 
ATOM   2424  C CG    . GLU B 2 241  ? 147.707 88.841  142.448 1.00 86.48  ? 238  GLU A CG    1 
ATOM   2425  C CD    . GLU B 2 241  ? 148.875 87.925  142.754 1.00 87.95  ? 238  GLU A CD    1 
ATOM   2426  O OE1   . GLU B 2 241  ? 149.605 88.192  143.729 1.00 86.69  ? 238  GLU A OE1   1 
ATOM   2427  O OE2   . GLU B 2 241  ? 149.057 86.931  142.020 1.00 89.96  ? 238  GLU A OE2   1 
ATOM   2428  N N     . GLU B 2 242  ? 147.599 92.072  145.874 1.00 80.65  ? 239  GLU A N     1 
ATOM   2429  C CA    . GLU B 2 242  ? 146.873 92.912  146.822 1.00 79.11  ? 239  GLU A CA    1 
ATOM   2430  C C     . GLU B 2 242  ? 147.216 94.386  146.649 1.00 76.49  ? 239  GLU A C     1 
ATOM   2431  O O     . GLU B 2 242  ? 146.344 95.246  146.811 1.00 75.59  ? 239  GLU A O     1 
ATOM   2432  C CB    . GLU B 2 242  ? 147.162 92.458  148.253 1.00 82.69  ? 239  GLU A CB    1 
ATOM   2433  C CG    . GLU B 2 242  ? 146.699 91.043  148.560 1.00 87.57  ? 239  GLU A CG    1 
ATOM   2434  C CD    . GLU B 2 242  ? 147.020 90.619  149.979 1.00 91.24  ? 239  GLU A CD    1 
ATOM   2435  O OE1   . GLU B 2 242  ? 147.402 91.490  150.788 1.00 92.19  ? 239  GLU A OE1   1 
ATOM   2436  O OE2   . GLU B 2 242  ? 146.895 89.413  150.283 1.00 93.10  ? 239  GLU A OE2   1 
ATOM   2437  N N     . VAL B 2 243  ? 148.472 94.704  146.319 1.00 75.42  ? 240  VAL A N     1 
ATOM   2438  C CA    . VAL B 2 243  ? 148.827 96.098  146.075 1.00 71.59  ? 240  VAL A CA    1 
ATOM   2439  C C     . VAL B 2 243  ? 148.140 96.630  144.825 1.00 70.55  ? 240  VAL A C     1 
ATOM   2440  O O     . VAL B 2 243  ? 148.082 97.848  144.623 1.00 70.93  ? 240  VAL A O     1 
ATOM   2441  C CB    . VAL B 2 243  ? 150.354 96.282  145.967 1.00 65.07  ? 240  VAL A CB    1 
ATOM   2442  C CG1   . VAL B 2 243  ? 151.054 95.680  147.175 1.00 66.03  ? 240  VAL A CG1   1 
ATOM   2443  C CG2   . VAL B 2 243  ? 150.881 95.679  144.680 1.00 61.88  ? 240  VAL A CG2   1 
ATOM   2444  N N     . PHE B 2 244  ? 147.618 95.744  143.977 1.00 69.97  ? 241  PHE A N     1 
ATOM   2445  C CA    . PHE B 2 244  ? 146.781 96.127  142.848 1.00 68.63  ? 241  PHE A CA    1 
ATOM   2446  C C     . PHE B 2 244  ? 145.319 95.770  143.094 1.00 71.87  ? 241  PHE A C     1 
ATOM   2447  O O     . PHE B 2 244  ? 144.579 95.459  142.156 1.00 74.43  ? 241  PHE A O     1 
ATOM   2448  C CB    . PHE B 2 244  ? 147.289 95.487  141.559 1.00 64.96  ? 241  PHE A CB    1 
ATOM   2449  C CG    . PHE B 2 244  ? 148.580 96.075  141.064 1.00 62.76  ? 241  PHE A CG    1 
ATOM   2450  C CD1   . PHE B 2 244  ? 148.583 97.243  140.318 1.00 60.66  ? 241  PHE A CD1   1 
ATOM   2451  C CD2   . PHE B 2 244  ? 149.790 95.464  141.347 1.00 63.65  ? 241  PHE A CD2   1 
ATOM   2452  C CE1   . PHE B 2 244  ? 149.769 97.790  139.862 1.00 58.22  ? 241  PHE A CE1   1 
ATOM   2453  C CE2   . PHE B 2 244  ? 150.979 96.005  140.894 1.00 61.98  ? 241  PHE A CE2   1 
ATOM   2454  C CZ    . PHE B 2 244  ? 150.968 97.169  140.149 1.00 58.93  ? 241  PHE A CZ    1 
ATOM   2455  N N     . SER B 2 245  ? 144.896 95.803  144.354 1.00 73.77  ? 242  SER A N     1 
ATOM   2456  C CA    . SER B 2 245  ? 143.498 95.669  144.732 1.00 75.29  ? 242  SER A CA    1 
ATOM   2457  C C     . SER B 2 245  ? 143.074 96.913  145.500 1.00 73.80  ? 242  SER A C     1 
ATOM   2458  O O     . SER B 2 245  ? 143.900 97.595  146.113 1.00 72.07  ? 242  SER A O     1 
ATOM   2459  C CB    . SER B 2 245  ? 143.260 94.415  145.584 1.00 82.38  ? 242  SER A CB    1 
ATOM   2460  O OG    . SER B 2 245  ? 143.906 94.520  146.843 1.00 87.41  ? 242  SER A OG    1 
ATOM   2461  N N     . PHE B 2 246  ? 141.774 97.200  145.459 1.00 70.61  ? 243  PHE A N     1 
ATOM   2462  C CA    . PHE B 2 246  ? 141.269 98.437  146.052 1.00 66.42  ? 243  PHE A CA    1 
ATOM   2463  C C     . PHE B 2 246  ? 141.578 98.602  147.539 1.00 66.23  ? 243  PHE A C     1 
ATOM   2464  O O     . PHE B 2 246  ? 141.947 99.722  147.934 1.00 63.91  ? 243  PHE A O     1 
ATOM   2465  C CB    . PHE B 2 246  ? 139.757 98.547  145.806 1.00 64.18  ? 243  PHE A CB    1 
ATOM   2466  C CG    . PHE B 2 246  ? 139.401 98.932  144.400 1.00 60.48  ? 243  PHE A CG    1 
ATOM   2467  C CD1   . PHE B 2 246  ? 140.375 99.373  143.518 1.00 57.82  ? 243  PHE A CD1   1 
ATOM   2468  C CD2   . PHE B 2 246  ? 138.090 98.861  143.961 1.00 60.79  ? 243  PHE A CD2   1 
ATOM   2469  C CE1   . PHE B 2 246  ? 140.049 99.731  142.225 1.00 56.81  ? 243  PHE A CE1   1 
ATOM   2470  C CE2   . PHE B 2 246  ? 137.757 99.217  142.669 1.00 60.39  ? 243  PHE A CE2   1 
ATOM   2471  C CZ    . PHE B 2 246  ? 138.739 99.653  141.800 1.00 58.12  ? 243  PHE A CZ    1 
ATOM   2472  N N     . PRO B 2 247  ? 141.447 97.587  148.403 1.00 68.96  ? 244  PRO A N     1 
ATOM   2473  C CA    . PRO B 2 247  ? 141.693 97.822  149.838 1.00 69.74  ? 244  PRO A CA    1 
ATOM   2474  C C     . PRO B 2 247  ? 143.084 98.345  150.159 1.00 67.62  ? 244  PRO A C     1 
ATOM   2475  O O     . PRO B 2 247  ? 143.257 98.980  151.207 1.00 69.29  ? 244  PRO A O     1 
ATOM   2476  C CB    . PRO B 2 247  ? 141.458 96.441  150.465 1.00 71.56  ? 244  PRO A CB    1 
ATOM   2477  C CG    . PRO B 2 247  ? 140.517 95.774  149.542 1.00 71.35  ? 244  PRO A CG    1 
ATOM   2478  C CD    . PRO B 2 247  ? 140.921 96.227  148.171 1.00 69.97  ? 244  PRO A CD    1 
ATOM   2479  N N     . PHE B 2 248  ? 144.078 98.110  149.301 1.00 64.63  ? 245  PHE A N     1 
ATOM   2480  C CA    . PHE B 2 248  ? 145.428 98.573  149.603 1.00 64.24  ? 245  PHE A CA    1 
ATOM   2481  C C     . PHE B 2 248  ? 145.580 100.078 149.426 1.00 61.40  ? 245  PHE A C     1 
ATOM   2482  O O     . PHE B 2 248  ? 146.522 100.660 149.975 1.00 61.08  ? 245  PHE A O     1 
ATOM   2483  C CB    . PHE B 2 248  ? 146.448 97.838  148.735 1.00 65.73  ? 245  PHE A CB    1 
ATOM   2484  C CG    . PHE B 2 248  ? 147.876 98.118  149.111 1.00 67.57  ? 245  PHE A CG    1 
ATOM   2485  C CD1   . PHE B 2 248  ? 148.410 97.608  150.285 1.00 69.47  ? 245  PHE A CD1   1 
ATOM   2486  C CD2   . PHE B 2 248  ? 148.686 98.887  148.293 1.00 65.14  ? 245  PHE A CD2   1 
ATOM   2487  C CE1   . PHE B 2 248  ? 149.723 97.863  150.636 1.00 68.94  ? 245  PHE A CE1   1 
ATOM   2488  C CE2   . PHE B 2 248  ? 150.001 99.145  148.636 1.00 64.62  ? 245  PHE A CE2   1 
ATOM   2489  C CZ    . PHE B 2 248  ? 150.519 98.631  149.810 1.00 66.68  ? 245  PHE A CZ    1 
ATOM   2490  N N     . TYR B 2 249  ? 144.677 100.724 148.684 1.00 60.14  ? 246  TYR A N     1 
ATOM   2491  C CA    . TYR B 2 249  ? 144.784 102.164 148.477 1.00 58.45  ? 246  TYR A CA    1 
ATOM   2492  C C     . TYR B 2 249  ? 144.606 102.948 149.769 1.00 59.05  ? 246  TYR A C     1 
ATOM   2493  O O     . TYR B 2 249  ? 145.067 104.093 149.855 1.00 58.91  ? 246  TYR A O     1 
ATOM   2494  C CB    . TYR B 2 249  ? 143.762 102.624 147.434 1.00 55.97  ? 246  TYR A CB    1 
ATOM   2495  C CG    . TYR B 2 249  ? 143.840 104.098 147.106 1.00 46.90  ? 246  TYR A CG    1 
ATOM   2496  C CD1   . TYR B 2 249  ? 144.983 104.643 146.535 1.00 45.62  ? 246  TYR A CD1   1 
ATOM   2497  C CD2   . TYR B 2 249  ? 142.769 104.943 147.362 1.00 46.79  ? 246  TYR A CD2   1 
ATOM   2498  C CE1   . TYR B 2 249  ? 145.060 105.989 146.234 1.00 44.34  ? 246  TYR A CE1   1 
ATOM   2499  C CE2   . TYR B 2 249  ? 142.835 106.291 147.064 1.00 45.45  ? 246  TYR A CE2   1 
ATOM   2500  C CZ    . TYR B 2 249  ? 143.983 106.809 146.500 1.00 50.46  ? 246  TYR A CZ    1 
ATOM   2501  O OH    . TYR B 2 249  ? 144.051 108.150 146.203 1.00 49.71  ? 246  TYR A OH    1 
ATOM   2502  N N     . ASN B 2 250  ? 143.956 102.360 150.777 1.00 60.91  ? 247  ASN A N     1 
ATOM   2503  C CA    . ASN B 2 250  ? 143.862 103.017 152.076 1.00 64.66  ? 247  ASN A CA    1 
ATOM   2504  C C     . ASN B 2 250  ? 145.234 103.196 152.712 1.00 69.90  ? 247  ASN A C     1 
ATOM   2505  O O     . ASN B 2 250  ? 145.435 104.124 153.504 1.00 72.91  ? 247  ASN A O     1 
ATOM   2506  C CB    . ASN B 2 250  ? 142.943 102.222 153.004 1.00 67.39  ? 247  ASN A CB    1 
ATOM   2507  C CG    . ASN B 2 250  ? 141.487 102.305 152.591 1.00 69.64  ? 247  ASN A CG    1 
ATOM   2508  O OD1   . ASN B 2 250  ? 141.022 103.343 152.121 1.00 69.29  ? 247  ASN A OD1   1 
ATOM   2509  N ND2   . ASN B 2 250  ? 140.757 101.209 152.765 1.00 72.35  ? 247  ASN A ND2   1 
ATOM   2510  N N     . GLN B 2 251  ? 146.188 102.326 152.378 1.00 73.18  ? 248  GLN A N     1 
ATOM   2511  C CA    . GLN B 2 251  ? 147.563 102.445 152.840 1.00 74.55  ? 248  GLN A CA    1 
ATOM   2512  C C     . GLN B 2 251  ? 148.456 103.154 151.829 1.00 69.59  ? 248  GLN A C     1 
ATOM   2513  O O     . GLN B 2 251  ? 149.677 102.971 151.853 1.00 69.26  ? 248  GLN A O     1 
ATOM   2514  C CB    . GLN B 2 251  ? 148.131 101.066 153.175 1.00 80.28  ? 248  GLN A CB    1 
ATOM   2515  C CG    . GLN B 2 251  ? 147.884 100.635 154.609 1.00 88.93  ? 248  GLN A CG    1 
ATOM   2516  C CD    . GLN B 2 251  ? 148.554 101.558 155.610 1.00 95.38  ? 248  GLN A CD    1 
ATOM   2517  O OE1   . GLN B 2 251  ? 149.781 101.643 155.670 1.00 96.87  ? 248  GLN A OE1   1 
ATOM   2518  N NE2   . GLN B 2 251  ? 147.748 102.262 156.399 1.00 97.77  ? 248  GLN A NE2   1 
ATOM   2519  N N     . LEU B 2 252  ? 147.871 103.951 150.940 1.00 67.16  ? 249  LEU A N     1 
ATOM   2520  C CA    . LEU B 2 252  ? 148.607 104.759 149.975 1.00 63.82  ? 249  LEU A CA    1 
ATOM   2521  C C     . LEU B 2 252  ? 148.180 106.214 150.071 1.00 61.36  ? 249  LEU A C     1 
ATOM   2522  O O     . LEU B 2 252  ? 148.095 106.929 149.069 1.00 58.60  ? 249  LEU A O     1 
ATOM   2523  C CB    . LEU B 2 252  ? 148.412 104.232 148.555 1.00 60.70  ? 249  LEU A CB    1 
ATOM   2524  C CG    . LEU B 2 252  ? 148.955 102.833 148.262 1.00 59.57  ? 249  LEU A CG    1 
ATOM   2525  C CD1   . LEU B 2 252  ? 148.721 102.472 146.805 1.00 58.03  ? 249  LEU A CD1   1 
ATOM   2526  C CD2   . LEU B 2 252  ? 150.432 102.746 148.612 1.00 57.69  ? 249  LEU A CD2   1 
ATOM   2527  N N     . LEU B 2 253  ? 147.903 106.673 151.291 1.00 60.30  ? 250  LEU A N     1 
ATOM   2528  C CA    . LEU B 2 253  ? 147.416 108.024 151.522 1.00 56.71  ? 250  LEU A CA    1 
ATOM   2529  C C     . LEU B 2 253  ? 148.448 108.927 152.184 1.00 58.98  ? 250  LEU A C     1 
ATOM   2530  O O     . LEU B 2 253  ? 148.179 110.118 152.368 1.00 60.11  ? 250  LEU A O     1 
ATOM   2531  C CB    . LEU B 2 253  ? 146.142 107.981 152.374 1.00 54.27  ? 250  LEU A CB    1 
ATOM   2532  C CG    . LEU B 2 253  ? 145.066 107.024 151.859 1.00 54.37  ? 250  LEU A CG    1 
ATOM   2533  C CD1   . LEU B 2 253  ? 143.829 107.087 152.731 1.00 55.48  ? 250  LEU A CD1   1 
ATOM   2534  C CD2   . LEU B 2 253  ? 144.720 107.327 150.409 1.00 54.61  ? 250  LEU A CD2   1 
ATOM   2535  N N     . THR B 2 254  ? 149.611 108.398 152.547 1.00 60.37  ? 251  THR A N     1 
ATOM   2536  C CA    . THR B 2 254  ? 150.680 109.187 153.137 1.00 64.42  ? 251  THR A CA    1 
ATOM   2537  C C     . THR B 2 254  ? 151.879 109.200 152.197 1.00 67.03  ? 251  THR A C     1 
ATOM   2538  O O     . THR B 2 254  ? 152.050 108.307 151.363 1.00 70.78  ? 251  THR A O     1 
ATOM   2539  C CB    . THR B 2 254  ? 151.087 108.644 154.513 1.00 65.68  ? 251  THR A CB    1 
ATOM   2540  O OG1   . THR B 2 254  ? 151.523 107.286 154.388 1.00 65.55  ? 251  THR A OG1   1 
ATOM   2541  C CG2   . THR B 2 254  ? 149.910 108.705 155.475 1.00 65.39  ? 251  THR A CG2   1 
ATOM   2542  N N     . GLN B 2 255  ? 152.717 110.229 152.349 1.00 66.58  ? 252  GLN A N     1 
ATOM   2543  C CA    . GLN B 2 255  ? 153.816 110.436 151.411 1.00 67.12  ? 252  GLN A CA    1 
ATOM   2544  C C     . GLN B 2 255  ? 154.818 109.288 151.458 1.00 71.85  ? 252  GLN A C     1 
ATOM   2545  O O     . GLN B 2 255  ? 155.314 108.849 150.414 1.00 70.80  ? 252  GLN A O     1 
ATOM   2546  C CB    . GLN B 2 255  ? 154.512 111.764 151.701 1.00 65.99  ? 252  GLN A CB    1 
ATOM   2547  C CG    . GLN B 2 255  ? 155.633 112.107 150.731 1.00 65.94  ? 252  GLN A CG    1 
ATOM   2548  C CD    . GLN B 2 255  ? 155.147 112.280 149.305 1.00 67.74  ? 252  GLN A CD    1 
ATOM   2549  O OE1   . GLN B 2 255  ? 153.981 112.596 149.068 1.00 68.38  ? 252  GLN A OE1   1 
ATOM   2550  N NE2   . GLN B 2 255  ? 156.040 112.072 148.345 1.00 68.41  ? 252  GLN A NE2   1 
ATOM   2551  N N     . THR B 2 256  ? 155.137 108.797 152.658 1.00 73.58  ? 253  THR A N     1 
ATOM   2552  C CA    . THR B 2 256  ? 156.083 107.691 152.769 1.00 73.69  ? 253  THR A CA    1 
ATOM   2553  C C     . THR B 2 256  ? 155.572 106.454 152.045 1.00 71.78  ? 253  THR A C     1 
ATOM   2554  O O     . THR B 2 256  ? 156.348 105.728 151.413 1.00 73.59  ? 253  THR A O     1 
ATOM   2555  C CB    . THR B 2 256  ? 156.362 107.376 154.239 1.00 75.01  ? 253  THR A CB    1 
ATOM   2556  O OG1   . THR B 2 256  ? 155.127 107.109 154.917 1.00 75.45  ? 253  THR A OG1   1 
ATOM   2557  C CG2   . THR B 2 256  ? 157.063 108.548 154.912 1.00 75.47  ? 253  THR A CG2   1 
ATOM   2558  N N     . GLN B 2 257  ? 154.263 106.204 152.112 1.00 69.16  ? 254  GLN A N     1 
ATOM   2559  C CA    . GLN B 2 257  ? 153.681 105.086 151.380 1.00 68.31  ? 254  GLN A CA    1 
ATOM   2560  C C     . GLN B 2 257  ? 153.575 105.389 149.889 1.00 67.81  ? 254  GLN A C     1 
ATOM   2561  O O     . GLN B 2 257  ? 153.771 104.497 149.057 1.00 66.41  ? 254  GLN A O     1 
ATOM   2562  C CB    . GLN B 2 257  ? 152.309 104.741 151.957 1.00 69.43  ? 254  GLN A CB    1 
ATOM   2563  C CG    . GLN B 2 257  ? 152.345 104.278 153.407 1.00 75.54  ? 254  GLN A CG    1 
ATOM   2564  C CD    . GLN B 2 257  ? 153.189 103.032 153.601 1.00 79.16  ? 254  GLN A CD    1 
ATOM   2565  O OE1   . GLN B 2 257  ? 154.226 103.070 154.264 1.00 80.83  ? 254  GLN A OE1   1 
ATOM   2566  N NE2   . GLN B 2 257  ? 152.745 101.921 153.028 1.00 79.30  ? 254  GLN A NE2   1 
ATOM   2567  N N     . ILE B 2 258  ? 153.266 106.639 149.535 1.00 65.99  ? 255  ILE A N     1 
ATOM   2568  C CA    . ILE B 2 258  ? 153.225 107.019 148.126 1.00 61.25  ? 255  ILE A CA    1 
ATOM   2569  C C     . ILE B 2 258  ? 154.620 106.950 147.514 1.00 63.78  ? 255  ILE A C     1 
ATOM   2570  O O     . ILE B 2 258  ? 154.786 106.527 146.363 1.00 63.80  ? 255  ILE A O     1 
ATOM   2571  C CB    . ILE B 2 258  ? 152.599 108.417 147.967 1.00 53.09  ? 255  ILE A CB    1 
ATOM   2572  C CG1   . ILE B 2 258  ? 151.109 108.378 148.316 1.00 50.59  ? 255  ILE A CG1   1 
ATOM   2573  C CG2   . ILE B 2 258  ? 152.794 108.944 146.552 1.00 49.91  ? 255  ILE A CG2   1 
ATOM   2574  C CD1   . ILE B 2 258  ? 150.428 109.726 148.239 1.00 44.29  ? 255  ILE A CD1   1 
ATOM   2575  N N     . ASP B 2 259  ? 155.643 107.352 148.272 1.00 67.25  ? 256  ASP A N     1 
ATOM   2576  C CA    . ASP B 2 259  ? 157.012 107.259 147.775 1.00 68.61  ? 256  ASP A CA    1 
ATOM   2577  C C     . ASP B 2 259  ? 157.426 105.808 147.565 1.00 67.87  ? 256  ASP A C     1 
ATOM   2578  O O     . ASP B 2 259  ? 158.034 105.474 146.540 1.00 67.13  ? 256  ASP A O     1 
ATOM   2579  C CB    . ASP B 2 259  ? 157.972 107.957 148.737 1.00 73.38  ? 256  ASP A CB    1 
ATOM   2580  C CG    . ASP B 2 259  ? 157.867 109.466 148.672 1.00 79.68  ? 256  ASP A CG    1 
ATOM   2581  O OD1   . ASP B 2 259  ? 157.568 109.998 147.582 1.00 80.20  ? 256  ASP A OD1   1 
ATOM   2582  O OD2   . ASP B 2 259  ? 158.090 110.124 149.711 1.00 84.04  ? 256  ASP A OD2   1 
ATOM   2583  N N     . LEU B 2 260  ? 157.110 104.932 148.521 1.00 67.44  ? 257  LEU A N     1 
ATOM   2584  C CA    . LEU B 2 260  ? 157.435 103.519 148.362 1.00 64.71  ? 257  LEU A CA    1 
ATOM   2585  C C     . LEU B 2 260  ? 156.681 102.909 147.187 1.00 59.16  ? 257  LEU A C     1 
ATOM   2586  O O     . LEU B 2 260  ? 157.225 102.070 146.460 1.00 57.24  ? 257  LEU A O     1 
ATOM   2587  C CB    . LEU B 2 260  ? 157.124 102.761 149.653 1.00 65.29  ? 257  LEU A CB    1 
ATOM   2588  C CG    . LEU B 2 260  ? 158.066 103.022 150.828 1.00 67.07  ? 257  LEU A CG    1 
ATOM   2589  C CD1   . LEU B 2 260  ? 157.574 102.304 152.073 1.00 69.56  ? 257  LEU A CD1   1 
ATOM   2590  C CD2   . LEU B 2 260  ? 159.482 102.591 150.478 1.00 66.65  ? 257  LEU A CD2   1 
ATOM   2591  N N     . TYR B 2 261  ? 155.427 103.320 146.987 1.00 56.17  ? 258  TYR A N     1 
ATOM   2592  C CA    . TYR B 2 261  ? 154.662 102.836 145.844 1.00 54.41  ? 258  TYR A CA    1 
ATOM   2593  C C     . TYR B 2 261  ? 155.273 103.309 144.531 1.00 56.04  ? 258  TYR A C     1 
ATOM   2594  O O     . TYR B 2 261  ? 155.380 102.533 143.574 1.00 57.15  ? 258  TYR A O     1 
ATOM   2595  C CB    . TYR B 2 261  ? 153.208 103.294 145.961 1.00 51.85  ? 258  TYR A CB    1 
ATOM   2596  C CG    . TYR B 2 261  ? 152.286 102.748 144.894 1.00 51.15  ? 258  TYR A CG    1 
ATOM   2597  C CD1   . TYR B 2 261  ? 151.710 101.492 145.025 1.00 53.44  ? 258  TYR A CD1   1 
ATOM   2598  C CD2   . TYR B 2 261  ? 151.977 103.496 143.765 1.00 49.86  ? 258  TYR A CD2   1 
ATOM   2599  C CE1   . TYR B 2 261  ? 150.860 100.990 144.057 1.00 53.30  ? 258  TYR A CE1   1 
ATOM   2600  C CE2   . TYR B 2 261  ? 151.127 103.001 142.790 1.00 47.62  ? 258  TYR A CE2   1 
ATOM   2601  C CZ    . TYR B 2 261  ? 150.572 101.749 142.942 1.00 49.77  ? 258  TYR A CZ    1 
ATOM   2602  O OH    . TYR B 2 261  ? 149.726 101.251 141.979 1.00 50.05  ? 258  TYR A OH    1 
ATOM   2603  N N     . ASN B 2 262  ? 155.686 104.578 144.468 1.00 54.59  ? 259  ASN A N     1 
ATOM   2604  C CA    . ASN B 2 262  ? 156.307 105.089 143.250 1.00 52.61  ? 259  ASN A CA    1 
ATOM   2605  C C     . ASN B 2 262  ? 157.669 104.456 143.000 1.00 53.01  ? 259  ASN A C     1 
ATOM   2606  O O     . ASN B 2 262  ? 158.071 104.293 141.841 1.00 51.79  ? 259  ASN A O     1 
ATOM   2607  C CB    . ASN B 2 262  ? 156.434 106.611 143.316 1.00 51.60  ? 259  ASN A CB    1 
ATOM   2608  C CG    . ASN B 2 262  ? 155.108 107.319 143.112 1.00 51.57  ? 259  ASN A CG    1 
ATOM   2609  O OD1   . ASN B 2 262  ? 154.154 106.735 142.599 1.00 53.47  ? 259  ASN A OD1   1 
ATOM   2610  N ND2   . ASN B 2 262  ? 155.046 108.586 143.503 1.00 50.65  ? 259  ASN A ND2   1 
ATOM   2611  N N     . GLN B 2 263  ? 158.395 104.094 144.060 1.00 54.76  ? 260  GLN A N     1 
ATOM   2612  C CA    . GLN B 2 263  ? 159.702 103.473 143.878 1.00 54.41  ? 260  GLN A CA    1 
ATOM   2613  C C     . GLN B 2 263  ? 159.586 102.005 143.487 1.00 54.43  ? 260  GLN A C     1 
ATOM   2614  O O     . GLN B 2 263  ? 160.504 101.462 142.862 1.00 53.01  ? 260  GLN A O     1 
ATOM   2615  C CB    . GLN B 2 263  ? 160.545 103.630 145.144 1.00 53.89  ? 260  GLN A CB    1 
ATOM   2616  C CG    . GLN B 2 263  ? 160.978 105.064 145.404 1.00 54.92  ? 260  GLN A CG    1 
ATOM   2617  C CD    . GLN B 2 263  ? 162.039 105.172 146.477 1.00 61.21  ? 260  GLN A CD    1 
ATOM   2618  O OE1   . GLN B 2 263  ? 161.736 105.414 147.645 1.00 64.38  ? 260  GLN A OE1   1 
ATOM   2619  N NE2   . GLN B 2 263  ? 163.295 104.999 146.085 1.00 63.27  ? 260  GLN A NE2   1 
ATOM   2620  N N     . LEU B 2 264  ? 158.481 101.347 143.847 1.00 54.91  ? 261  LEU A N     1 
ATOM   2621  C CA    . LEU B 2 264  ? 158.202 100.030 143.286 1.00 55.07  ? 261  LEU A CA    1 
ATOM   2622  C C     . LEU B 2 264  ? 158.007 100.109 141.779 1.00 53.74  ? 261  LEU A C     1 
ATOM   2623  O O     . LEU B 2 264  ? 158.374 99.178  141.052 1.00 52.88  ? 261  LEU A O     1 
ATOM   2624  C CB    . LEU B 2 264  ? 156.964 99.425  143.952 1.00 56.87  ? 261  LEU A CB    1 
ATOM   2625  C CG    . LEU B 2 264  ? 156.463 98.085  143.410 1.00 56.59  ? 261  LEU A CG    1 
ATOM   2626  C CD1   . LEU B 2 264  ? 157.455 96.971  143.710 1.00 57.02  ? 261  LEU A CD1   1 
ATOM   2627  C CD2   . LEU B 2 264  ? 155.087 97.753  143.969 1.00 56.90  ? 261  LEU A CD2   1 
ATOM   2628  N N     . LEU B 2 265  ? 157.442 101.216 141.293 1.00 55.18  ? 262  LEU A N     1 
ATOM   2629  C CA    . LEU B 2 265  ? 157.240 101.402 139.860 1.00 52.92  ? 262  LEU A CA    1 
ATOM   2630  C C     . LEU B 2 265  ? 158.502 101.913 139.177 1.00 51.37  ? 262  LEU A C     1 
ATOM   2631  O O     . LEU B 2 265  ? 158.774 101.556 138.025 1.00 50.02  ? 262  LEU A O     1 
ATOM   2632  C CB    . LEU B 2 265  ? 156.086 102.377 139.614 1.00 53.02  ? 262  LEU A CB    1 
ATOM   2633  C CG    . LEU B 2 265  ? 154.637 101.880 139.601 1.00 53.63  ? 262  LEU A CG    1 
ATOM   2634  C CD1   . LEU B 2 265  ? 154.273 101.154 140.884 1.00 56.55  ? 262  LEU A CD1   1 
ATOM   2635  C CD2   . LEU B 2 265  ? 153.697 103.053 139.369 1.00 53.02  ? 262  LEU A CD2   1 
ATOM   2636  N N     . GLY B 2 266  ? 159.282 102.745 139.866 1.00 48.62  ? 263  GLY A N     1 
ATOM   2637  C CA    . GLY B 2 266  ? 160.400 103.424 139.242 1.00 49.22  ? 263  GLY A CA    1 
ATOM   2638  C C     . GLY B 2 266  ? 161.766 102.857 139.569 1.00 51.70  ? 263  GLY A C     1 
ATOM   2639  O O     . GLY B 2 266  ? 162.738 103.129 138.857 1.00 50.97  ? 263  GLY A O     1 
ATOM   2640  N N     . GLY B 2 267  ? 161.863 102.076 140.641 1.00 53.73  ? 264  GLY A N     1 
ATOM   2641  C CA    . GLY B 2 267  ? 163.133 101.496 141.026 1.00 56.95  ? 264  GLY A CA    1 
ATOM   2642  C C     . GLY B 2 267  ? 163.968 102.436 141.872 1.00 59.64  ? 264  GLY A C     1 
ATOM   2643  O O     . GLY B 2 267  ? 163.581 103.559 142.197 1.00 62.18  ? 264  GLY A O     1 
ATOM   2644  N N     . LYS B 2 327  ? 168.039 137.076 144.220 1.00 105.25 ? 324  LYS A N     1 
ATOM   2645  C CA    . LYS B 2 327  ? 168.522 138.093 145.143 1.00 105.46 ? 324  LYS A CA    1 
ATOM   2646  C C     . LYS B 2 327  ? 169.756 138.845 144.662 1.00 106.48 ? 324  LYS A C     1 
ATOM   2647  O O     . LYS B 2 327  ? 170.068 139.900 145.224 1.00 106.46 ? 324  LYS A O     1 
ATOM   2648  C CB    . LYS B 2 327  ? 168.821 137.460 146.510 1.00 106.73 ? 324  LYS A CB    1 
ATOM   2649  C CG    . LYS B 2 327  ? 167.586 136.942 147.235 1.00 105.20 ? 324  LYS A CG    1 
ATOM   2650  C CD    . LYS B 2 327  ? 166.595 138.066 147.504 1.00 103.53 ? 324  LYS A CD    1 
ATOM   2651  C CE    . LYS B 2 327  ? 165.356 137.562 148.227 1.00 102.73 ? 324  LYS A CE    1 
ATOM   2652  N NZ    . LYS B 2 327  ? 164.382 138.662 148.486 1.00 99.75  ? 324  LYS A NZ    1 
ATOM   2653  N N     . SER B 2 328  ? 170.466 138.350 143.650 1.00 108.92 ? 325  SER A N     1 
ATOM   2654  C CA    . SER B 2 328  ? 171.680 139.017 143.204 1.00 112.73 ? 325  SER A CA    1 
ATOM   2655  C C     . SER B 2 328  ? 171.819 138.870 141.693 1.00 112.17 ? 325  SER A C     1 
ATOM   2656  O O     . SER B 2 328  ? 171.017 138.202 141.034 1.00 110.18 ? 325  SER A O     1 
ATOM   2657  C CB    . SER B 2 328  ? 172.914 138.469 143.932 1.00 117.56 ? 325  SER A CB    1 
ATOM   2658  O OG    . SER B 2 328  ? 173.227 137.156 143.502 1.00 118.93 ? 325  SER A OG    1 
ATOM   2659  N N     . ASP B 2 329  ? 172.856 139.508 141.151 1.00 114.71 ? 326  ASP A N     1 
ATOM   2660  C CA    . ASP B 2 329  ? 173.087 139.508 139.710 1.00 115.09 ? 326  ASP A CA    1 
ATOM   2661  C C     . ASP B 2 329  ? 173.657 138.175 139.239 1.00 117.19 ? 326  ASP A C     1 
ATOM   2662  O O     . ASP B 2 329  ? 173.191 137.608 138.246 1.00 116.07 ? 326  ASP A O     1 
ATOM   2663  C CB    . ASP B 2 329  ? 174.023 140.659 139.337 1.00 117.35 ? 326  ASP A CB    1 
ATOM   2664  C CG    . ASP B 2 329  ? 173.959 141.011 137.867 1.00 116.26 ? 326  ASP A CG    1 
ATOM   2665  O OD1   . ASP B 2 329  ? 174.720 140.412 137.076 1.00 118.06 ? 326  ASP A OD1   1 
ATOM   2666  O OD2   . ASP B 2 329  ? 173.149 141.889 137.503 1.00 113.92 ? 326  ASP A OD2   1 
ATOM   2667  N N     . GLU B 2 330  ? 174.666 137.661 139.943 1.00 120.49 ? 327  GLU A N     1 
ATOM   2668  C CA    . GLU B 2 330  ? 175.279 136.390 139.580 1.00 122.30 ? 327  GLU A CA    1 
ATOM   2669  C C     . GLU B 2 330  ? 174.436 135.188 139.981 1.00 122.50 ? 327  GLU A C     1 
ATOM   2670  O O     . GLU B 2 330  ? 174.708 134.079 139.506 1.00 122.41 ? 327  GLU A O     1 
ATOM   2671  C CB    . GLU B 2 330  ? 176.668 136.277 140.212 1.00 124.73 ? 327  GLU A CB    1 
ATOM   2672  N N     . GLU B 2 331  ? 173.427 135.373 140.838 1.00 121.40 ? 328  GLU A N     1 
ATOM   2673  C CA    . GLU B 2 331  ? 172.587 134.248 141.236 1.00 119.35 ? 328  GLU A CA    1 
ATOM   2674  C C     . GLU B 2 331  ? 171.783 133.717 140.056 1.00 116.34 ? 328  GLU A C     1 
ATOM   2675  O O     . GLU B 2 331  ? 171.562 132.507 139.944 1.00 115.25 ? 328  GLU A O     1 
ATOM   2676  C CB    . GLU B 2 331  ? 171.654 134.659 142.375 1.00 116.65 ? 328  GLU A CB    1 
ATOM   2677  C CG    . GLU B 2 331  ? 170.830 133.514 142.947 1.00 115.81 ? 328  GLU A CG    1 
ATOM   2678  C CD    . GLU B 2 331  ? 169.838 133.974 144.000 1.00 115.55 ? 328  GLU A CD    1 
ATOM   2679  O OE1   . GLU B 2 331  ? 169.714 135.200 144.207 1.00 114.69 ? 328  GLU A OE1   1 
ATOM   2680  O OE2   . GLU B 2 331  ? 169.182 133.111 144.621 1.00 116.52 ? 328  GLU A OE2   1 
ATOM   2681  N N     . VAL B 2 332  ? 171.343 134.605 139.163 1.00 118.09 ? 329  VAL A N     1 
ATOM   2682  C CA    . VAL B 2 332  ? 170.596 134.150 137.996 1.00 114.87 ? 329  VAL A CA    1 
ATOM   2683  C C     . VAL B 2 332  ? 171.525 133.488 136.989 1.00 116.01 ? 329  VAL A C     1 
ATOM   2684  O O     . VAL B 2 332  ? 171.094 132.635 136.207 1.00 116.94 ? 329  VAL A O     1 
ATOM   2685  C CB    . VAL B 2 332  ? 169.812 135.317 137.363 1.00 113.17 ? 329  VAL A CB    1 
ATOM   2686  C CG1   . VAL B 2 332  ? 169.083 136.108 138.434 1.00 112.44 ? 329  VAL A CG1   1 
ATOM   2687  C CG2   . VAL B 2 332  ? 170.734 136.223 136.559 1.00 114.05 ? 329  VAL A CG2   1 
ATOM   2688  N N     . ILE B 2 333  ? 172.808 133.854 136.991 1.00 116.48 ? 330  ILE A N     1 
ATOM   2689  C CA    . ILE B 2 333  ? 173.744 133.249 136.052 1.00 110.83 ? 330  ILE A CA    1 
ATOM   2690  C C     . ILE B 2 333  ? 174.231 131.903 136.571 1.00 108.13 ? 330  ILE A C     1 
ATOM   2691  O O     . ILE B 2 333  ? 174.325 130.934 135.813 1.00 107.26 ? 330  ILE A O     1 
ATOM   2692  C CB    . ILE B 2 333  ? 174.915 134.206 135.774 1.00 104.58 ? 330  ILE A CB    1 
ATOM   2693  C CG1   . ILE B 2 333  ? 174.396 135.581 135.354 1.00 96.96  ? 330  ILE A CG1   1 
ATOM   2694  C CG2   . ILE B 2 333  ? 175.823 133.636 134.695 1.00 103.21 ? 330  ILE A CG2   1 
ATOM   2695  C CD1   . ILE B 2 333  ? 175.493 136.587 135.092 1.00 95.34  ? 330  ILE A CD1   1 
ATOM   2696  N N     . GLN B 2 334  ? 174.543 131.822 137.866 1.00 108.13 ? 331  GLN A N     1 
ATOM   2697  C CA    . GLN B 2 334  ? 175.032 130.568 138.429 1.00 111.56 ? 331  GLN A CA    1 
ATOM   2698  C C     . GLN B 2 334  ? 173.933 129.514 138.475 1.00 112.21 ? 331  GLN A C     1 
ATOM   2699  O O     . GLN B 2 334  ? 174.191 128.329 138.234 1.00 113.89 ? 331  GLN A O     1 
ATOM   2700  C CB    . GLN B 2 334  ? 175.606 130.809 139.825 1.00 113.13 ? 331  GLN A CB    1 
ATOM   2701  N N     . SER B 2 335  ? 172.699 129.924 138.778 1.00 110.88 ? 332  SER A N     1 
ATOM   2702  C CA    . SER B 2 335  ? 171.604 128.961 138.871 1.00 109.08 ? 332  SER A CA    1 
ATOM   2703  C C     . SER B 2 335  ? 171.154 128.497 137.493 1.00 106.57 ? 332  SER A C     1 
ATOM   2704  O O     . SER B 2 335  ? 170.906 127.304 137.284 1.00 105.31 ? 332  SER A O     1 
ATOM   2705  C CB    . SER B 2 335  ? 170.432 129.569 139.641 1.00 107.27 ? 332  SER A CB    1 
ATOM   2706  O OG    . SER B 2 335  ? 169.369 128.641 139.766 1.00 107.23 ? 332  SER A OG    1 
ATOM   2707  N N     . PHE B 2 336  ? 171.034 129.426 136.539 1.00 104.19 ? 333  PHE A N     1 
ATOM   2708  C CA    . PHE B 2 336  ? 170.618 129.045 135.192 1.00 100.04 ? 333  PHE A CA    1 
ATOM   2709  C C     . PHE B 2 336  ? 171.676 128.182 134.521 1.00 102.92 ? 333  PHE A C     1 
ATOM   2710  O O     . PHE B 2 336  ? 171.359 127.134 133.948 1.00 103.05 ? 333  PHE A O     1 
ATOM   2711  C CB    . PHE B 2 336  ? 170.324 130.293 134.358 1.00 94.00  ? 333  PHE A CB    1 
ATOM   2712  C CG    . PHE B 2 336  ? 169.816 129.995 132.975 1.00 90.46  ? 333  PHE A CG    1 
ATOM   2713  C CD1   . PHE B 2 336  ? 168.714 129.181 132.791 1.00 87.98  ? 333  PHE A CD1   1 
ATOM   2714  C CD2   . PHE B 2 336  ? 170.432 130.544 131.862 1.00 90.37  ? 333  PHE A CD2   1 
ATOM   2715  C CE1   . PHE B 2 336  ? 168.241 128.907 131.521 1.00 86.69  ? 333  PHE A CE1   1 
ATOM   2716  C CE2   . PHE B 2 336  ? 169.963 130.276 130.590 1.00 88.66  ? 333  PHE A CE2   1 
ATOM   2717  C CZ    . PHE B 2 336  ? 168.865 129.456 130.419 1.00 86.79  ? 333  PHE A CZ    1 
ATOM   2718  N N     . CYS B 2 337  ? 172.943 128.598 134.595 1.00 107.47 ? 334  CYS A N     1 
ATOM   2719  C CA    . CYS B 2 337  ? 174.019 127.802 134.012 1.00 110.44 ? 334  CYS A CA    1 
ATOM   2720  C C     . CYS B 2 337  ? 174.122 126.433 134.671 1.00 113.43 ? 334  CYS A C     1 
ATOM   2721  O O     . CYS B 2 337  ? 174.540 125.465 134.024 1.00 114.52 ? 334  CYS A O     1 
ATOM   2722  C CB    . CYS B 2 337  ? 175.349 128.548 134.123 1.00 113.73 ? 334  CYS A CB    1 
ATOM   2723  S SG    . CYS B 2 337  ? 176.750 127.721 133.337 1.00 118.68 ? 334  CYS A SG    1 
ATOM   2724  N N     . LYS B 2 338  ? 173.751 126.328 135.949 1.00 115.22 ? 335  LYS A N     1 
ATOM   2725  C CA    . LYS B 2 338  ? 173.703 125.019 136.595 1.00 117.67 ? 335  LYS A CA    1 
ATOM   2726  C C     . LYS B 2 338  ? 172.554 124.181 136.048 1.00 115.38 ? 335  LYS A C     1 
ATOM   2727  O O     . LYS B 2 338  ? 172.718 122.985 135.791 1.00 116.32 ? 335  LYS A O     1 
ATOM   2728  C CB    . LYS B 2 338  ? 173.579 125.183 138.110 1.00 118.16 ? 335  LYS A CB    1 
ATOM   2729  N N     . TYR B 2 339  ? 171.381 124.794 135.868 1.00 111.45 ? 336  TYR A N     1 
ATOM   2730  C CA    . TYR B 2 339  ? 170.279 124.097 135.214 1.00 107.89 ? 336  TYR A CA    1 
ATOM   2731  C C     . TYR B 2 339  ? 170.540 123.923 133.725 1.00 102.25 ? 336  TYR A C     1 
ATOM   2732  O O     . TYR B 2 339  ? 170.099 122.932 133.130 1.00 101.75 ? 336  TYR A O     1 
ATOM   2733  C CB    . TYR B 2 339  ? 168.971 124.854 135.445 1.00 108.02 ? 336  TYR A CB    1 
ATOM   2734  C CG    . TYR B 2 339  ? 167.833 124.427 134.543 1.00 107.66 ? 336  TYR A CG    1 
ATOM   2735  C CD1   . TYR B 2 339  ? 167.107 123.273 134.806 1.00 108.62 ? 336  TYR A CD1   1 
ATOM   2736  C CD2   . TYR B 2 339  ? 167.479 125.184 133.432 1.00 105.60 ? 336  TYR A CD2   1 
ATOM   2737  C CE1   . TYR B 2 339  ? 166.065 122.883 133.986 1.00 106.67 ? 336  TYR A CE1   1 
ATOM   2738  C CE2   . TYR B 2 339  ? 166.441 124.801 132.606 1.00 103.47 ? 336  TYR A CE2   1 
ATOM   2739  C CZ    . TYR B 2 339  ? 165.735 123.650 132.889 1.00 104.20 ? 336  TYR A CZ    1 
ATOM   2740  O OH    . TYR B 2 339  ? 164.700 123.263 132.069 1.00 102.33 ? 336  TYR A OH    1 
ATOM   2741  N N     . LYS B 2 340  ? 171.252 124.869 133.112 1.00 97.81  ? 337  LYS A N     1 
ATOM   2742  C CA    . LYS B 2 340  ? 171.566 124.761 131.693 1.00 94.74  ? 337  LYS A CA    1 
ATOM   2743  C C     . LYS B 2 340  ? 172.536 123.613 131.433 1.00 98.35  ? 337  LYS A C     1 
ATOM   2744  O O     . LYS B 2 340  ? 172.332 122.815 130.513 1.00 98.39  ? 337  LYS A O     1 
ATOM   2745  C CB    . LYS B 2 340  ? 172.137 126.088 131.191 1.00 92.46  ? 337  LYS A CB    1 
ATOM   2746  C CG    . LYS B 2 340  ? 172.477 126.131 129.721 1.00 90.58  ? 337  LYS A CG    1 
ATOM   2747  C CD    . LYS B 2 340  ? 172.684 127.565 129.280 1.00 88.48  ? 337  LYS A CD    1 
ATOM   2748  C CE    . LYS B 2 340  ? 173.545 127.637 128.038 1.00 89.72  ? 337  LYS A CE    1 
ATOM   2749  N NZ    . LYS B 2 340  ? 173.678 129.027 127.528 1.00 88.85  ? 337  LYS A NZ    1 
ATOM   2750  N N     . THR B 2 341  ? 173.591 123.506 132.248 1.00 100.96 ? 338  THR A N     1 
ATOM   2751  C CA    . THR B 2 341  ? 174.537 122.407 132.090 1.00 101.82 ? 338  THR A CA    1 
ATOM   2752  C C     . THR B 2 341  ? 173.925 121.064 132.464 1.00 101.52 ? 338  THR A C     1 
ATOM   2753  O O     . THR B 2 341  ? 174.462 120.020 132.071 1.00 102.56 ? 338  THR A O     1 
ATOM   2754  C CB    . THR B 2 341  ? 175.799 122.660 132.924 1.00 103.05 ? 338  THR A CB    1 
ATOM   2755  O OG1   . THR B 2 341  ? 176.846 121.785 132.487 1.00 106.87 ? 338  THR A OG1   1 
ATOM   2756  C CG2   . THR B 2 341  ? 175.533 122.405 134.402 1.00 102.09 ? 338  THR A CG2   1 
ATOM   2757  N N     . LEU B 2 342  ? 172.816 121.066 133.208 1.00 102.17 ? 339  LEU A N     1 
ATOM   2758  C CA    . LEU B 2 342  ? 172.111 119.827 133.515 1.00 103.53 ? 339  LEU A CA    1 
ATOM   2759  C C     . LEU B 2 342  ? 171.349 119.298 132.308 1.00 102.63 ? 339  LEU A C     1 
ATOM   2760  O O     . LEU B 2 342  ? 171.144 118.083 132.192 1.00 101.63 ? 339  LEU A O     1 
ATOM   2761  C CB    . LEU B 2 342  ? 171.161 120.052 134.695 1.00 104.21 ? 339  LEU A CB    1 
ATOM   2762  C CG    . LEU B 2 342  ? 170.392 118.859 135.268 1.00 106.12 ? 339  LEU A CG    1 
ATOM   2763  C CD1   . LEU B 2 342  ? 170.331 118.957 136.780 1.00 108.19 ? 339  LEU A CD1   1 
ATOM   2764  C CD2   . LEU B 2 342  ? 168.990 118.791 134.690 1.00 104.03 ? 339  LEU A CD2   1 
ATOM   2765  N N     . LEU B 2 343  ? 170.931 120.183 131.399 1.00 102.68 ? 340  LEU A N     1 
ATOM   2766  C CA    . LEU B 2 343  ? 170.224 119.751 130.202 1.00 102.74 ? 340  LEU A CA    1 
ATOM   2767  C C     . LEU B 2 343  ? 171.137 119.039 129.215 1.00 104.95 ? 340  LEU A C     1 
ATOM   2768  O O     . LEU B 2 343  ? 170.652 118.234 128.415 1.00 104.96 ? 340  LEU A O     1 
ATOM   2769  C CB    . LEU B 2 343  ? 169.557 120.952 129.527 1.00 101.14 ? 340  LEU A CB    1 
ATOM   2770  C CG    . LEU B 2 343  ? 168.533 121.714 130.372 1.00 98.30  ? 340  LEU A CG    1 
ATOM   2771  C CD1   . LEU B 2 343  ? 168.100 122.989 129.672 1.00 94.25  ? 340  LEU A CD1   1 
ATOM   2772  C CD2   . LEU B 2 343  ? 167.328 120.839 130.685 1.00 96.62  ? 340  LEU A CD2   1 
ATOM   2773  N N     . ARG B 2 344  ? 172.443 119.316 129.250 1.00 107.33 ? 341  ARG A N     1 
ATOM   2774  C CA    . ARG B 2 344  ? 173.369 118.595 128.385 1.00 110.50 ? 341  ARG A CA    1 
ATOM   2775  C C     . ARG B 2 344  ? 173.585 117.169 128.878 1.00 113.25 ? 341  ARG A C     1 
ATOM   2776  O O     . ARG B 2 344  ? 173.587 116.224 128.080 1.00 113.74 ? 341  ARG A O     1 
ATOM   2777  C CB    . ARG B 2 344  ? 174.710 119.329 128.298 1.00 113.99 ? 341  ARG A CB    1 
ATOM   2778  C CG    . ARG B 2 344  ? 174.710 120.607 127.473 1.00 113.53 ? 341  ARG A CG    1 
ATOM   2779  C CD    . ARG B 2 344  ? 174.271 121.801 128.301 1.00 113.95 ? 341  ARG A CD    1 
ATOM   2780  N NE    . ARG B 2 344  ? 174.981 123.022 127.934 1.00 115.55 ? 341  ARG A NE    1 
ATOM   2781  C CZ    . ARG B 2 344  ? 176.106 123.432 128.510 1.00 118.46 ? 341  ARG A CZ    1 
ATOM   2782  N NH1   . ARG B 2 344  ? 176.655 122.716 129.481 1.00 121.22 ? 341  ARG A NH1   1 
ATOM   2783  N NH2   . ARG B 2 344  ? 176.685 124.558 128.115 1.00 118.53 ? 341  ARG A NH2   1 
ATOM   2784  N N     . ASN B 2 345  ? 173.769 116.998 130.190 1.00 114.62 ? 342  ASN A N     1 
ATOM   2785  C CA    . ASN B 2 345  ? 174.045 115.673 130.736 1.00 116.13 ? 342  ASN A CA    1 
ATOM   2786  C C     . ASN B 2 345  ? 172.853 114.741 130.566 1.00 115.20 ? 342  ASN A C     1 
ATOM   2787  O O     . ASN B 2 345  ? 173.021 113.556 130.255 1.00 116.25 ? 342  ASN A O     1 
ATOM   2788  C CB    . ASN B 2 345  ? 174.439 115.785 132.208 1.00 116.22 ? 342  ASN A CB    1 
ATOM   2789  C CG    . ASN B 2 345  ? 175.625 116.710 132.427 1.00 116.84 ? 342  ASN A CG    1 
ATOM   2790  O OD1   . ASN B 2 345  ? 176.474 116.866 131.552 1.00 117.55 ? 342  ASN A OD1   1 
ATOM   2791  N ND2   . ASN B 2 345  ? 175.684 117.327 133.601 1.00 116.72 ? 342  ASN A ND2   1 
ATOM   2792  N N     . GLU B 2 346  ? 171.636 115.256 130.766 1.00 111.92 ? 343  GLU A N     1 
ATOM   2793  C CA    . GLU B 2 346  ? 170.442 114.452 130.525 1.00 109.11 ? 343  GLU A CA    1 
ATOM   2794  C C     . GLU B 2 346  ? 170.178 114.248 129.040 1.00 107.79 ? 343  GLU A C     1 
ATOM   2795  O O     . GLU B 2 346  ? 169.395 113.361 128.681 1.00 105.60 ? 343  GLU A O     1 
ATOM   2796  C CB    . GLU B 2 346  ? 169.224 115.101 131.184 1.00 104.32 ? 343  GLU A CB    1 
ATOM   2797  C CG    . GLU B 2 346  ? 169.240 115.064 132.703 1.00 103.95 ? 343  GLU A CG    1 
ATOM   2798  C CD    . GLU B 2 346  ? 168.048 115.775 133.317 1.00 101.05 ? 343  GLU A CD    1 
ATOM   2799  O OE1   . GLU B 2 346  ? 167.476 116.665 132.651 1.00 98.91  ? 343  GLU A OE1   1 
ATOM   2800  O OE2   . GLU B 2 346  ? 167.683 115.445 134.465 1.00 101.42 ? 343  GLU A OE2   1 
ATOM   2801  N N     . ASN B 2 347  ? 170.810 115.046 128.177 1.00 109.45 ? 344  ASN A N     1 
ATOM   2802  C CA    . ASN B 2 347  ? 170.633 114.959 126.727 1.00 109.06 ? 344  ASN A CA    1 
ATOM   2803  C C     . ASN B 2 347  ? 169.158 115.086 126.347 1.00 105.87 ? 344  ASN A C     1 
ATOM   2804  O O     . ASN B 2 347  ? 168.627 114.316 125.545 1.00 104.52 ? 344  ASN A O     1 
ATOM   2805  C CB    . ASN B 2 347  ? 171.237 113.663 126.176 1.00 111.26 ? 344  ASN A CB    1 
ATOM   2806  N N     . VAL B 2 348  ? 168.492 116.079 126.941 1.00 105.13 ? 345  VAL A N     1 
ATOM   2807  C CA    . VAL B 2 348  ? 167.070 116.271 126.678 1.00 103.11 ? 345  VAL A CA    1 
ATOM   2808  C C     . VAL B 2 348  ? 166.842 116.784 125.264 1.00 101.24 ? 345  VAL A C     1 
ATOM   2809  O O     . VAL B 2 348  ? 165.789 116.527 124.667 1.00 97.55  ? 345  VAL A O     1 
ATOM   2810  C CB    . VAL B 2 348  ? 166.447 117.211 127.729 1.00 102.40 ? 345  VAL A CB    1 
ATOM   2811  C CG1   . VAL B 2 348  ? 166.537 116.588 129.112 1.00 104.27 ? 345  VAL A CG1   1 
ATOM   2812  C CG2   . VAL B 2 348  ? 167.131 118.568 127.706 1.00 103.47 ? 345  VAL A CG2   1 
ATOM   2813  N N     . LEU B 2 349  ? 167.808 117.513 124.698 1.00 103.31 ? 346  LEU A N     1 
ATOM   2814  C CA    . LEU B 2 349  ? 167.685 117.930 123.305 1.00 101.76 ? 346  LEU A CA    1 
ATOM   2815  C C     . LEU B 2 349  ? 167.747 116.731 122.368 1.00 100.10 ? 346  LEU A C     1 
ATOM   2816  O O     . LEU B 2 349  ? 166.924 116.602 121.457 1.00 97.78  ? 346  LEU A O     1 
ATOM   2817  C CB    . LEU B 2 349  ? 168.767 118.957 122.948 1.00 105.30 ? 346  LEU A CB    1 
ATOM   2818  C CG    . LEU B 2 349  ? 170.111 119.084 123.678 1.00 110.95 ? 346  LEU A CG    1 
ATOM   2819  C CD1   . LEU B 2 349  ? 170.887 117.776 123.763 1.00 113.43 ? 346  LEU A CD1   1 
ATOM   2820  C CD2   . LEU B 2 349  ? 170.952 120.138 122.976 1.00 112.56 ? 346  LEU A CD2   1 
ATOM   2821  N N     . GLU B 2 350  ? 168.712 115.834 122.588 1.00 102.06 ? 347  GLU A N     1 
ATOM   2822  C CA    . GLU B 2 350  ? 168.826 114.652 121.741 1.00 100.49 ? 347  GLU A CA    1 
ATOM   2823  C C     . GLU B 2 350  ? 167.609 113.750 121.892 1.00 96.96  ? 347  GLU A C     1 
ATOM   2824  O O     . GLU B 2 350  ? 167.159 113.133 120.920 1.00 93.08  ? 347  GLU A O     1 
ATOM   2825  C CB    . GLU B 2 350  ? 170.108 113.889 122.078 1.00 102.99 ? 347  GLU A CB    1 
ATOM   2826  N N     . THR B 2 351  ? 167.059 113.664 123.104 1.00 98.00  ? 348  THR A N     1 
ATOM   2827  C CA    . THR B 2 351  ? 165.847 112.880 123.309 1.00 96.48  ? 348  THR A CA    1 
ATOM   2828  C C     . THR B 2 351  ? 164.649 113.537 122.634 1.00 93.15  ? 348  THR A C     1 
ATOM   2829  O O     . THR B 2 351  ? 163.800 112.850 122.057 1.00 92.60  ? 348  THR A O     1 
ATOM   2830  C CB    . THR B 2 351  ? 165.583 112.694 124.803 1.00 95.65  ? 348  THR A CB    1 
ATOM   2831  O OG1   . THR B 2 351  ? 166.780 112.241 125.448 1.00 98.29  ? 348  THR A OG1   1 
ATOM   2832  C CG2   . THR B 2 351  ? 164.479 111.673 125.027 1.00 93.45  ? 348  THR A CG2   1 
ATOM   2833  N N     . ALA B 2 352  ? 164.568 114.869 122.694 1.00 91.33  ? 349  ALA A N     1 
ATOM   2834  C CA    . ALA B 2 352  ? 163.470 115.574 122.041 1.00 88.04  ? 349  ALA A CA    1 
ATOM   2835  C C     . ALA B 2 352  ? 163.599 115.519 120.525 1.00 88.99  ? 349  ALA A C     1 
ATOM   2836  O O     . ALA B 2 352  ? 162.608 115.303 119.818 1.00 86.44  ? 349  ALA A O     1 
ATOM   2837  C CB    . ALA B 2 352  ? 163.412 117.023 122.523 1.00 87.74  ? 349  ALA A CB    1 
ATOM   2838  N N     . GLU B 2 353  ? 164.816 115.712 120.004 1.00 92.33  ? 350  GLU A N     1 
ATOM   2839  C CA    . GLU B 2 353  ? 165.023 115.623 118.562 1.00 92.52  ? 350  GLU A CA    1 
ATOM   2840  C C     . GLU B 2 353  ? 164.727 114.223 118.041 1.00 91.73  ? 350  GLU A C     1 
ATOM   2841  O O     . GLU B 2 353  ? 164.321 114.064 116.884 1.00 90.57  ? 350  GLU A O     1 
ATOM   2842  C CB    . GLU B 2 353  ? 166.454 116.036 118.208 1.00 94.61  ? 350  GLU A CB    1 
ATOM   2843  C CG    . GLU B 2 353  ? 166.770 117.500 118.490 1.00 95.40  ? 350  GLU A CG    1 
ATOM   2844  C CD    . GLU B 2 353  ? 168.256 117.803 118.425 1.00 99.29  ? 350  GLU A CD    1 
ATOM   2845  O OE1   . GLU B 2 353  ? 168.951 117.207 117.573 1.00 100.83 ? 350  GLU A OE1   1 
ATOM   2846  O OE2   . GLU B 2 353  ? 168.733 118.633 119.229 1.00 100.16 ? 350  GLU A OE2   1 
ATOM   2847  N N     . ALA B 2 354  ? 164.915 113.199 118.878 1.00 92.39  ? 351  ALA A N     1 
ATOM   2848  C CA    . ALA B 2 354  ? 164.610 111.834 118.468 1.00 91.05  ? 351  ALA A CA    1 
ATOM   2849  C C     . ALA B 2 354  ? 163.115 111.545 118.501 1.00 87.24  ? 351  ALA A C     1 
ATOM   2850  O O     . ALA B 2 354  ? 162.625 110.754 117.686 1.00 87.35  ? 351  ALA A O     1 
ATOM   2851  C CB    . ALA B 2 354  ? 165.356 110.838 119.358 1.00 94.16  ? 351  ALA A CB    1 
ATOM   2852  N N     . LEU B 2 355  ? 162.379 112.166 119.426 1.00 84.23  ? 352  LEU A N     1 
ATOM   2853  C CA    . LEU B 2 355  ? 160.939 111.944 119.496 1.00 77.51  ? 352  LEU A CA    1 
ATOM   2854  C C     . LEU B 2 355  ? 160.231 112.533 118.284 1.00 73.06  ? 352  LEU A C     1 
ATOM   2855  O O     . LEU B 2 355  ? 159.388 111.874 117.665 1.00 72.80  ? 352  LEU A O     1 
ATOM   2856  C CB    . LEU B 2 355  ? 160.373 112.539 120.785 1.00 73.00  ? 352  LEU A CB    1 
ATOM   2857  C CG    . LEU B 2 355  ? 160.451 111.657 122.028 1.00 73.05  ? 352  LEU A CG    1 
ATOM   2858  C CD1   . LEU B 2 355  ? 159.733 112.322 123.187 1.00 72.47  ? 352  LEU A CD1   1 
ATOM   2859  C CD2   . LEU B 2 355  ? 159.865 110.283 121.743 1.00 72.02  ? 352  LEU A CD2   1 
ATOM   2860  N N     . PHE B 2 356  ? 160.552 113.780 117.936 1.00 71.29  ? 353  PHE A N     1 
ATOM   2861  C CA    . PHE B 2 356  ? 159.922 114.401 116.779 1.00 71.33  ? 353  PHE A CA    1 
ATOM   2862  C C     . PHE B 2 356  ? 160.352 113.750 115.472 1.00 74.85  ? 353  PHE A C     1 
ATOM   2863  O O     . PHE B 2 356  ? 159.620 113.837 114.480 1.00 74.54  ? 353  PHE A O     1 
ATOM   2864  C CB    . PHE B 2 356  ? 160.222 115.898 116.755 1.00 70.58  ? 353  PHE A CB    1 
ATOM   2865  C CG    . PHE B 2 356  ? 159.520 116.670 117.836 1.00 71.19  ? 353  PHE A CG    1 
ATOM   2866  C CD1   . PHE B 2 356  ? 158.203 117.070 117.675 1.00 70.15  ? 353  PHE A CD1   1 
ATOM   2867  C CD2   . PHE B 2 356  ? 160.174 116.991 119.013 1.00 72.74  ? 353  PHE A CD2   1 
ATOM   2868  C CE1   . PHE B 2 356  ? 157.553 117.775 118.670 1.00 69.49  ? 353  PHE A CE1   1 
ATOM   2869  C CE2   . PHE B 2 356  ? 159.530 117.698 120.010 1.00 71.46  ? 353  PHE A CE2   1 
ATOM   2870  C CZ    . PHE B 2 356  ? 158.218 118.090 119.838 1.00 70.08  ? 353  PHE A CZ    1 
ATOM   2871  N N     . ASN B 2 357  ? 161.516 113.099 115.449 1.00 78.80  ? 354  ASN A N     1 
ATOM   2872  C CA    . ASN B 2 357  ? 161.907 112.318 114.283 1.00 80.91  ? 354  ASN A CA    1 
ATOM   2873  C C     . ASN B 2 357  ? 161.162 110.993 114.201 1.00 81.70  ? 354  ASN A C     1 
ATOM   2874  O O     . ASN B 2 357  ? 161.019 110.445 113.102 1.00 80.63  ? 354  ASN A O     1 
ATOM   2875  C CB    . ASN B 2 357  ? 163.416 112.071 114.293 1.00 85.48  ? 354  ASN A CB    1 
ATOM   2876  C CG    . ASN B 2 357  ? 163.910 111.433 113.011 1.00 88.53  ? 354  ASN A CG    1 
ATOM   2877  O OD1   . ASN B 2 357  ? 164.144 110.226 112.954 1.00 90.33  ? 354  ASN A OD1   1 
ATOM   2878  N ND2   . ASN B 2 357  ? 164.063 112.241 111.968 1.00 88.81  ? 354  ASN A ND2   1 
ATOM   2879  N N     . GLU B 2 358  ? 160.678 110.473 115.333 1.00 82.95  ? 355  GLU A N     1 
ATOM   2880  C CA    . GLU B 2 358  ? 159.857 109.267 115.306 1.00 82.30  ? 355  GLU A CA    1 
ATOM   2881  C C     . GLU B 2 358  ? 158.541 109.500 114.577 1.00 75.99  ? 355  GLU A C     1 
ATOM   2882  O O     . GLU B 2 358  ? 157.979 108.563 113.997 1.00 72.20  ? 355  GLU A O     1 
ATOM   2883  C CB    . GLU B 2 358  ? 159.578 108.780 116.730 1.00 85.13  ? 355  GLU A CB    1 
ATOM   2884  C CG    . GLU B 2 358  ? 160.636 107.861 117.312 1.00 89.31  ? 355  GLU A CG    1 
ATOM   2885  C CD    . GLU B 2 358  ? 160.254 107.345 118.686 1.00 91.80  ? 355  GLU A CD    1 
ATOM   2886  O OE1   . GLU B 2 358  ? 159.279 106.570 118.780 1.00 94.59  ? 355  GLU A OE1   1 
ATOM   2887  O OE2   . GLU B 2 358  ? 160.919 107.723 119.675 1.00 90.93  ? 355  GLU A OE2   1 
ATOM   2888  N N     . LEU B 2 359  ? 158.039 110.735 114.587 1.00 75.35  ? 356  LEU A N     1 
ATOM   2889  C CA    . LEU B 2 359  ? 156.734 111.031 114.004 1.00 72.72  ? 356  LEU A CA    1 
ATOM   2890  C C     . LEU B 2 359  ? 156.694 110.827 112.496 1.00 75.05  ? 356  LEU A C     1 
ATOM   2891  O O     . LEU B 2 359  ? 155.606 110.873 111.913 1.00 75.40  ? 356  LEU A O     1 
ATOM   2892  C CB    . LEU B 2 359  ? 156.331 112.469 114.344 1.00 66.63  ? 356  LEU A CB    1 
ATOM   2893  C CG    . LEU B 2 359  ? 156.300 112.820 115.832 1.00 61.22  ? 356  LEU A CG    1 
ATOM   2894  C CD1   . LEU B 2 359  ? 156.037 114.302 116.023 1.00 58.93  ? 356  LEU A CD1   1 
ATOM   2895  C CD2   . LEU B 2 359  ? 155.253 111.990 116.562 1.00 58.90  ? 356  LEU A CD2   1 
ATOM   2896  N N     . ASN B 2 360  ? 157.840 110.600 111.851 1.00 79.90  ? 357  ASN A N     1 
ATOM   2897  C CA    . ASN B 2 360  ? 157.863 110.378 110.412 1.00 80.98  ? 357  ASN A CA    1 
ATOM   2898  C C     . ASN B 2 360  ? 157.530 108.944 110.029 1.00 81.94  ? 357  ASN A C     1 
ATOM   2899  O O     . ASN B 2 360  ? 157.211 108.688 108.862 1.00 83.54  ? 357  ASN A O     1 
ATOM   2900  C CB    . ASN B 2 360  ? 159.235 110.745 109.844 1.00 85.08  ? 357  ASN A CB    1 
ATOM   2901  C CG    . ASN B 2 360  ? 159.687 112.126 110.259 1.00 89.55  ? 357  ASN A CG    1 
ATOM   2902  O OD1   . ASN B 2 360  ? 159.275 113.128 109.679 1.00 90.12  ? 357  ASN A OD1   1 
ATOM   2903  N ND2   . ASN B 2 360  ? 160.542 112.187 111.272 1.00 92.49  ? 357  ASN A ND2   1 
ATOM   2904  N N     . SER B 2 361  ? 157.593 108.007 110.974 1.00 81.07  ? 358  SER A N     1 
ATOM   2905  C CA    . SER B 2 361  ? 157.378 106.598 110.671 1.00 79.32  ? 358  SER A CA    1 
ATOM   2906  C C     . SER B 2 361  ? 156.404 105.889 111.602 1.00 78.85  ? 358  SER A C     1 
ATOM   2907  O O     . SER B 2 361  ? 155.828 104.875 111.191 1.00 76.86  ? 358  SER A O     1 
ATOM   2908  C CB    . SER B 2 361  ? 158.713 105.838 110.691 1.00 80.39  ? 358  SER A CB    1 
ATOM   2909  O OG    . SER B 2 361  ? 159.367 105.990 111.939 1.00 81.35  ? 358  SER A OG    1 
ATOM   2910  N N     . ILE B 2 362  ? 156.193 106.374 112.823 1.00 79.87  ? 359  ILE A N     1 
ATOM   2911  C CA    . ILE B 2 362  ? 155.323 105.685 113.770 1.00 79.86  ? 359  ILE A CA    1 
ATOM   2912  C C     . ILE B 2 362  ? 153.865 105.967 113.434 1.00 80.13  ? 359  ILE A C     1 
ATOM   2913  O O     . ILE B 2 362  ? 153.561 106.827 112.599 1.00 81.13  ? 359  ILE A O     1 
ATOM   2914  C CB    . ILE B 2 362  ? 155.639 106.088 115.222 1.00 74.89  ? 359  ILE A CB    1 
ATOM   2915  C CG1   . ILE B 2 362  ? 155.278 107.555 115.462 1.00 68.22  ? 359  ILE A CG1   1 
ATOM   2916  C CG2   . ILE B 2 362  ? 157.104 105.825 115.541 1.00 76.10  ? 359  ILE A CG2   1 
ATOM   2917  C CD1   . ILE B 2 362  ? 155.486 108.009 116.889 1.00 64.70  ? 359  ILE A CD1   1 
ATOM   2918  N N     . ASP B 2 363  ? 152.959 105.242 114.086 1.00 78.63  ? 360  ASP A N     1 
ATOM   2919  C CA    . ASP B 2 363  ? 151.526 105.394 113.853 1.00 75.85  ? 360  ASP A CA    1 
ATOM   2920  C C     . ASP B 2 363  ? 151.045 106.701 114.474 1.00 73.17  ? 360  ASP A C     1 
ATOM   2921  O O     . ASP B 2 363  ? 151.063 106.859 115.698 1.00 72.35  ? 360  ASP A O     1 
ATOM   2922  C CB    . ASP B 2 363  ? 150.777 104.199 114.437 1.00 78.71  ? 360  ASP A CB    1 
ATOM   2923  C CG    . ASP B 2 363  ? 149.281 104.276 114.205 1.00 80.24  ? 360  ASP A CG    1 
ATOM   2924  O OD1   . ASP B 2 363  ? 148.855 104.961 113.252 1.00 81.36  ? 360  ASP A OD1   1 
ATOM   2925  O OD2   . ASP B 2 363  ? 148.531 103.643 114.977 1.00 80.57  ? 360  ASP A OD2   1 
ATOM   2926  N N     . LEU B 2 364  ? 150.609 107.634 113.630 1.00 71.76  ? 361  LEU A N     1 
ATOM   2927  C CA    . LEU B 2 364  ? 150.204 108.960 114.079 1.00 69.00  ? 361  LEU A CA    1 
ATOM   2928  C C     . LEU B 2 364  ? 148.749 109.027 114.525 1.00 67.77  ? 361  LEU A C     1 
ATOM   2929  O O     . LEU B 2 364  ? 148.304 110.092 114.969 1.00 65.72  ? 361  LEU A O     1 
ATOM   2930  C CB    . LEU B 2 364  ? 150.449 109.989 112.971 1.00 65.30  ? 361  LEU A CB    1 
ATOM   2931  C CG    . LEU B 2 364  ? 151.916 110.237 112.617 1.00 64.67  ? 361  LEU A CG    1 
ATOM   2932  C CD1   . LEU B 2 364  ? 152.041 111.352 111.592 1.00 62.82  ? 361  LEU A CD1   1 
ATOM   2933  C CD2   . LEU B 2 364  ? 152.725 110.558 113.866 1.00 65.38  ? 361  LEU A CD2   1 
ATOM   2934  N N     . THR B 2 365  ? 147.996 107.931 114.422 1.00 67.42  ? 362  THR A N     1 
ATOM   2935  C CA    . THR B 2 365  ? 146.630 107.919 114.926 1.00 64.12  ? 362  THR A CA    1 
ATOM   2936  C C     . THR B 2 365  ? 146.565 107.830 116.444 1.00 64.41  ? 362  THR A C     1 
ATOM   2937  O O     . THR B 2 365  ? 145.470 107.921 117.007 1.00 65.92  ? 362  THR A O     1 
ATOM   2938  C CB    . THR B 2 365  ? 145.842 106.755 114.317 1.00 61.78  ? 362  THR A CB    1 
ATOM   2939  O OG1   . THR B 2 365  ? 146.328 105.515 114.848 1.00 63.34  ? 362  THR A OG1   1 
ATOM   2940  C CG2   . THR B 2 365  ? 145.991 106.743 112.806 1.00 60.52  ? 362  THR A CG2   1 
ATOM   2941  N N     . HIS B 2 366  ? 147.705 107.651 117.114 1.00 65.75  ? 363  HIS A N     1 
ATOM   2942  C CA    . HIS B 2 366  ? 147.759 107.600 118.569 1.00 67.74  ? 363  HIS A CA    1 
ATOM   2943  C C     . HIS B 2 366  ? 148.612 108.715 119.162 1.00 67.04  ? 363  HIS A C     1 
ATOM   2944  O O     . HIS B 2 366  ? 148.878 108.704 120.370 1.00 69.17  ? 363  HIS A O     1 
ATOM   2945  C CB    . HIS B 2 366  ? 148.275 106.234 119.032 1.00 71.85  ? 363  HIS A CB    1 
ATOM   2946  C CG    . HIS B 2 366  ? 147.326 105.106 118.756 1.00 75.11  ? 363  HIS A CG    1 
ATOM   2947  N ND1   . HIS B 2 366  ? 146.288 104.783 119.604 1.00 77.47  ? 363  HIS A ND1   1 
ATOM   2948  C CD2   . HIS B 2 366  ? 147.258 104.230 117.726 1.00 76.03  ? 363  HIS A CD2   1 
ATOM   2949  C CE1   . HIS B 2 366  ? 145.623 103.755 119.109 1.00 77.53  ? 363  HIS A CE1   1 
ATOM   2950  N NE2   . HIS B 2 366  ? 146.189 103.401 117.971 1.00 76.67  ? 363  HIS A NE2   1 
ATOM   2951  N N     . ILE B 2 367  ? 149.050 109.670 118.347 1.00 64.34  ? 364  ILE A N     1 
ATOM   2952  C CA    . ILE B 2 367  ? 149.718 110.877 118.821 1.00 62.36  ? 364  ILE A CA    1 
ATOM   2953  C C     . ILE B 2 367  ? 148.680 111.990 118.802 1.00 57.80  ? 364  ILE A C     1 
ATOM   2954  O O     . ILE B 2 367  ? 148.233 112.417 117.732 1.00 58.18  ? 364  ILE A O     1 
ATOM   2955  C CB    . ILE B 2 367  ? 150.937 111.229 117.959 1.00 61.75  ? 364  ILE A CB    1 
ATOM   2956  C CG1   . ILE B 2 367  ? 151.923 110.062 117.927 1.00 63.65  ? 364  ILE A CG1   1 
ATOM   2957  C CG2   . ILE B 2 367  ? 151.619 112.478 118.489 1.00 58.79  ? 364  ILE A CG2   1 
ATOM   2958  C CD1   . ILE B 2 367  ? 152.469 109.692 119.287 1.00 64.31  ? 364  ILE A CD1   1 
ATOM   2959  N N     . PHE B 2 368  ? 148.289 112.465 119.980 1.00 54.96  ? 365  PHE A N     1 
ATOM   2960  C CA    . PHE B 2 368  ? 147.159 113.369 120.120 1.00 52.26  ? 365  PHE A CA    1 
ATOM   2961  C C     . PHE B 2 368  ? 147.621 114.791 120.405 1.00 52.41  ? 365  PHE A C     1 
ATOM   2962  O O     . PHE B 2 368  ? 148.575 115.010 121.160 1.00 51.82  ? 365  PHE A O     1 
ATOM   2963  C CB    . PHE B 2 368  ? 146.221 112.897 121.233 1.00 52.55  ? 365  PHE A CB    1 
ATOM   2964  C CG    . PHE B 2 368  ? 145.529 111.603 120.924 1.00 56.23  ? 365  PHE A CG    1 
ATOM   2965  C CD1   . PHE B 2 368  ? 146.111 110.392 121.264 1.00 57.64  ? 365  PHE A CD1   1 
ATOM   2966  C CD2   . PHE B 2 368  ? 144.301 111.594 120.284 1.00 56.80  ? 365  PHE A CD2   1 
ATOM   2967  C CE1   . PHE B 2 368  ? 145.479 109.200 120.976 1.00 59.25  ? 365  PHE A CE1   1 
ATOM   2968  C CE2   . PHE B 2 368  ? 143.663 110.405 119.994 1.00 58.05  ? 365  PHE A CE2   1 
ATOM   2969  C CZ    . PHE B 2 368  ? 144.252 109.205 120.341 1.00 60.16  ? 365  PHE A CZ    1 
ATOM   2970  N N     . ILE B 2 369  ? 146.932 115.751 119.794 1.00 52.31  ? 366  ILE A N     1 
ATOM   2971  C CA    . ILE B 2 369  ? 147.157 117.175 120.021 1.00 52.49  ? 366  ILE A CA    1 
ATOM   2972  C C     . ILE B 2 369  ? 146.075 117.691 120.959 1.00 53.71  ? 366  ILE A C     1 
ATOM   2973  O O     . ILE B 2 369  ? 144.893 117.362 120.801 1.00 54.44  ? 366  ILE A O     1 
ATOM   2974  C CB    . ILE B 2 369  ? 147.157 117.953 118.690 1.00 51.28  ? 366  ILE A CB    1 
ATOM   2975  C CG1   . ILE B 2 369  ? 148.299 117.476 117.793 1.00 50.67  ? 366  ILE A CG1   1 
ATOM   2976  C CG2   . ILE B 2 369  ? 147.263 119.445 118.943 1.00 50.77  ? 366  ILE A CG2   1 
ATOM   2977  C CD1   . ILE B 2 369  ? 149.670 117.650 118.406 1.00 49.77  ? 366  ILE A CD1   1 
ATOM   2978  N N     . SER B 2 370  ? 146.476 118.497 121.935 1.00 54.71  ? 367  SER A N     1 
ATOM   2979  C CA    . SER B 2 370  ? 145.526 119.032 122.900 1.00 54.34  ? 367  SER A CA    1 
ATOM   2980  C C     . SER B 2 370  ? 144.617 120.067 122.247 1.00 55.91  ? 367  SER A C     1 
ATOM   2981  O O     . SER B 2 370  ? 145.065 120.891 121.445 1.00 55.68  ? 367  SER A O     1 
ATOM   2982  C CB    . SER B 2 370  ? 146.265 119.655 124.082 1.00 54.51  ? 367  SER A CB    1 
ATOM   2983  O OG    . SER B 2 370  ? 145.353 120.227 125.004 1.00 55.35  ? 367  SER A OG    1 
ATOM   2984  N N     . HIS B 2 371  ? 143.329 120.022 122.601 1.00 57.17  ? 368  HIS A N     1 
ATOM   2985  C CA    . HIS B 2 371  ? 142.381 120.988 122.058 1.00 56.25  ? 368  HIS A CA    1 
ATOM   2986  C C     . HIS B 2 371  ? 142.662 122.396 122.562 1.00 55.12  ? 368  HIS A C     1 
ATOM   2987  O O     . HIS B 2 371  ? 142.346 123.375 121.878 1.00 54.89  ? 368  HIS A O     1 
ATOM   2988  C CB    . HIS B 2 371  ? 140.947 120.578 122.401 1.00 59.84  ? 368  HIS A CB    1 
ATOM   2989  C CG    . HIS B 2 371  ? 140.668 120.518 123.872 1.00 65.77  ? 368  HIS A CG    1 
ATOM   2990  N ND1   . HIS B 2 371  ? 140.656 119.338 124.581 1.00 69.98  ? 368  HIS A ND1   1 
ATOM   2991  C CD2   . HIS B 2 371  ? 140.383 121.496 124.765 1.00 66.18  ? 368  HIS A CD2   1 
ATOM   2992  C CE1   . HIS B 2 371  ? 140.379 119.589 125.846 1.00 68.93  ? 368  HIS A CE1   1 
ATOM   2993  N NE2   . HIS B 2 371  ? 140.208 120.891 125.986 1.00 67.13  ? 368  HIS A NE2   1 
ATOM   2994  N N     . LYS B 2 372  ? 143.258 122.517 123.752 1.00 56.01  ? 369  LYS A N     1 
ATOM   2995  C CA    . LYS B 2 372  ? 143.627 123.822 124.288 1.00 57.47  ? 369  LYS A CA    1 
ATOM   2996  C C     . LYS B 2 372  ? 144.754 124.481 123.504 1.00 58.23  ? 369  LYS A C     1 
ATOM   2997  O O     . LYS B 2 372  ? 144.994 125.679 123.689 1.00 59.14  ? 369  LYS A O     1 
ATOM   2998  C CB    . LYS B 2 372  ? 144.037 123.686 125.756 1.00 58.16  ? 369  LYS A CB    1 
ATOM   2999  C CG    . LYS B 2 372  ? 142.956 123.103 126.652 1.00 58.45  ? 369  LYS A CG    1 
ATOM   3000  C CD    . LYS B 2 372  ? 143.472 122.888 128.067 1.00 59.54  ? 369  LYS A CD    1 
ATOM   3001  C CE    . LYS B 2 372  ? 142.392 122.317 128.970 1.00 58.62  ? 369  LYS A CE    1 
ATOM   3002  N NZ    . LYS B 2 372  ? 142.909 122.034 130.337 1.00 60.64  ? 369  LYS A NZ    1 
ATOM   3003  N N     . LYS B 2 373  ? 145.445 123.737 122.639 1.00 57.16  ? 370  LYS A N     1 
ATOM   3004  C CA    . LYS B 2 373  ? 146.551 124.263 121.856 1.00 53.66  ? 370  LYS A CA    1 
ATOM   3005  C C     . LYS B 2 373  ? 146.298 124.223 120.356 1.00 50.19  ? 370  LYS A C     1 
ATOM   3006  O O     . LYS B 2 373  ? 147.135 124.716 119.592 1.00 51.70  ? 370  LYS A O     1 
ATOM   3007  C CB    . LYS B 2 373  ? 147.841 123.488 122.167 1.00 53.51  ? 370  LYS A CB    1 
ATOM   3008  C CG    . LYS B 2 373  ? 148.139 123.325 123.649 1.00 55.98  ? 370  LYS A CG    1 
ATOM   3009  C CD    . LYS B 2 373  ? 148.444 124.657 124.314 1.00 59.11  ? 370  LYS A CD    1 
ATOM   3010  C CE    . LYS B 2 373  ? 148.784 124.470 125.786 1.00 62.87  ? 370  LYS A CE    1 
ATOM   3011  N NZ    . LYS B 2 373  ? 149.094 125.763 126.460 1.00 65.60  ? 370  LYS A NZ    1 
ATOM   3012  N N     . LEU B 2 374  ? 145.173 123.655 119.910 1.00 46.07  ? 371  LEU A N     1 
ATOM   3013  C CA    . LEU B 2 374  ? 144.952 123.475 118.477 1.00 46.14  ? 371  LEU A CA    1 
ATOM   3014  C C     . LEU B 2 374  ? 144.881 124.812 117.749 1.00 42.45  ? 371  LEU A C     1 
ATOM   3015  O O     . LEU B 2 374  ? 145.424 124.956 116.646 1.00 41.17  ? 371  LEU A O     1 
ATOM   3016  C CB    . LEU B 2 374  ? 143.676 122.669 118.235 1.00 46.66  ? 371  LEU A CB    1 
ATOM   3017  C CG    . LEU B 2 374  ? 143.322 122.419 116.769 1.00 43.67  ? 371  LEU A CG    1 
ATOM   3018  C CD1   . LEU B 2 374  ? 144.425 121.634 116.075 1.00 43.80  ? 371  LEU A CD1   1 
ATOM   3019  C CD2   . LEU B 2 374  ? 141.991 121.696 116.647 1.00 42.51  ? 371  LEU A CD2   1 
ATOM   3020  N N     . GLU B 2 375  ? 144.216 125.804 118.344 1.00 41.71  ? 372  GLU A N     1 
ATOM   3021  C CA    . GLU B 2 375  ? 144.115 127.107 117.696 1.00 45.20  ? 372  GLU A CA    1 
ATOM   3022  C C     . GLU B 2 375  ? 145.461 127.819 117.677 1.00 47.19  ? 372  GLU A C     1 
ATOM   3023  O O     . GLU B 2 375  ? 145.784 128.524 116.712 1.00 48.35  ? 372  GLU A O     1 
ATOM   3024  C CB    . GLU B 2 375  ? 143.056 127.963 118.391 1.00 47.18  ? 372  GLU A CB    1 
ATOM   3025  C CG    . GLU B 2 375  ? 141.643 127.726 117.879 1.00 50.70  ? 372  GLU A CG    1 
ATOM   3026  C CD    . GLU B 2 375  ? 141.178 126.297 118.075 1.00 55.36  ? 372  GLU A CD    1 
ATOM   3027  O OE1   . GLU B 2 375  ? 141.308 125.777 119.204 1.00 59.66  ? 372  GLU A OE1   1 
ATOM   3028  O OE2   . GLU B 2 375  ? 140.691 125.688 117.099 1.00 54.43  ? 372  GLU A OE2   1 
ATOM   3029  N N     . THR B 2 376  ? 146.262 127.649 118.731 1.00 48.75  ? 373  THR A N     1 
ATOM   3030  C CA    . THR B 2 376  ? 147.596 128.242 118.744 1.00 51.15  ? 373  THR A CA    1 
ATOM   3031  C C     . THR B 2 376  ? 148.483 127.613 117.675 1.00 52.59  ? 373  THR A C     1 
ATOM   3032  O O     . THR B 2 376  ? 149.239 128.316 116.995 1.00 53.75  ? 373  THR A O     1 
ATOM   3033  C CB    . THR B 2 376  ? 148.225 128.089 120.128 1.00 53.69  ? 373  THR A CB    1 
ATOM   3034  O OG1   . THR B 2 376  ? 147.369 128.679 121.113 1.00 55.64  ? 373  THR A OG1   1 
ATOM   3035  C CG2   . THR B 2 376  ? 149.585 128.770 120.177 1.00 53.21  ? 373  THR A CG2   1 
ATOM   3036  N N     . ILE B 2 377  ? 148.396 126.293 117.507 1.00 53.59  ? 374  ILE A N     1 
ATOM   3037  C CA    . ILE B 2 377  ? 149.181 125.614 116.481 1.00 53.18  ? 374  ILE A CA    1 
ATOM   3038  C C     . ILE B 2 377  ? 148.736 126.046 115.091 1.00 54.37  ? 374  ILE A C     1 
ATOM   3039  O O     . ILE B 2 377  ? 149.561 126.224 114.186 1.00 55.41  ? 374  ILE A O     1 
ATOM   3040  C CB    . ILE B 2 377  ? 149.080 124.088 116.658 1.00 49.88  ? 374  ILE A CB    1 
ATOM   3041  C CG1   . ILE B 2 377  ? 149.661 123.673 118.009 1.00 49.44  ? 374  ILE A CG1   1 
ATOM   3042  C CG2   . ILE B 2 377  ? 149.791 123.362 115.527 1.00 49.72  ? 374  ILE A CG2   1 
ATOM   3043  C CD1   . ILE B 2 377  ? 149.451 122.216 118.328 1.00 50.33  ? 374  ILE A CD1   1 
ATOM   3044  N N     . SER B 2 378  ? 147.427 126.224 114.897 1.00 54.70  ? 375  SER A N     1 
ATOM   3045  C CA    . SER B 2 378  ? 146.921 126.656 113.599 1.00 53.71  ? 375  SER A CA    1 
ATOM   3046  C C     . SER B 2 378  ? 147.479 128.022 113.220 1.00 53.81  ? 375  SER A C     1 
ATOM   3047  O O     . SER B 2 378  ? 147.839 128.253 112.059 1.00 55.04  ? 375  SER A O     1 
ATOM   3048  C CB    . SER B 2 378  ? 145.394 126.689 113.616 1.00 52.66  ? 375  SER A CB    1 
ATOM   3049  O OG    . SER B 2 378  ? 144.875 126.893 112.314 1.00 52.00  ? 375  SER A OG    1 
ATOM   3050  N N     . SER B 2 379  ? 147.564 128.938 114.186 1.00 55.60  ? 376  SER A N     1 
ATOM   3051  C CA    . SER B 2 379  ? 148.080 130.270 113.902 1.00 56.79  ? 376  SER A CA    1 
ATOM   3052  C C     . SER B 2 379  ? 149.588 130.276 113.692 1.00 56.92  ? 376  SER A C     1 
ATOM   3053  O O     . SER B 2 379  ? 150.101 131.174 113.017 1.00 58.36  ? 376  SER A O     1 
ATOM   3054  C CB    . SER B 2 379  ? 147.706 131.228 115.036 1.00 58.68  ? 376  SER A CB    1 
ATOM   3055  O OG    . SER B 2 379  ? 148.066 132.561 114.720 1.00 62.48  ? 376  SER A OG    1 
ATOM   3056  N N     . ALA B 2 380  ? 150.305 129.297 114.242 1.00 57.39  ? 377  ALA A N     1 
ATOM   3057  C CA    . ALA B 2 380  ? 151.754 129.245 114.111 1.00 61.15  ? 377  ALA A CA    1 
ATOM   3058  C C     . ALA B 2 380  ? 152.219 128.497 112.870 1.00 62.37  ? 377  ALA A C     1 
ATOM   3059  O O     . ALA B 2 380  ? 153.345 128.724 112.414 1.00 65.68  ? 377  ALA A O     1 
ATOM   3060  C CB    . ALA B 2 380  ? 152.375 128.593 115.352 1.00 61.93  ? 377  ALA A CB    1 
ATOM   3061  N N     . LEU B 2 381  ? 151.385 127.618 112.314 1.00 60.26  ? 378  LEU A N     1 
ATOM   3062  C CA    . LEU B 2 381  ? 151.765 126.819 111.161 1.00 59.72  ? 378  LEU A CA    1 
ATOM   3063  C C     . LEU B 2 381  ? 150.952 127.115 109.911 1.00 63.33  ? 378  LEU A C     1 
ATOM   3064  O O     . LEU B 2 381  ? 151.357 126.696 108.822 1.00 64.33  ? 378  LEU A O     1 
ATOM   3065  C CB    . LEU B 2 381  ? 151.641 125.322 111.481 1.00 59.49  ? 378  LEU A CB    1 
ATOM   3066  C CG    . LEU B 2 381  ? 152.388 124.828 112.719 1.00 62.36  ? 378  LEU A CG    1 
ATOM   3067  C CD1   . LEU B 2 381  ? 152.315 123.313 112.819 1.00 62.95  ? 378  LEU A CD1   1 
ATOM   3068  C CD2   . LEU B 2 381  ? 153.829 125.296 112.690 1.00 65.54  ? 378  LEU A CD2   1 
ATOM   3069  N N     . CYS B 2 382  ? 149.823 127.813 110.028 1.00 67.35  ? 379  CYS A N     1 
ATOM   3070  C CA    . CYS B 2 382  ? 148.963 128.038 108.874 1.00 71.16  ? 379  CYS A CA    1 
ATOM   3071  C C     . CYS B 2 382  ? 148.626 129.513 108.703 1.00 73.73  ? 379  CYS A C     1 
ATOM   3072  O O     . CYS B 2 382  ? 149.205 130.374 109.374 1.00 72.71  ? 379  CYS A O     1 
ATOM   3073  C CB    . CYS B 2 382  ? 147.680 127.217 109.005 1.00 69.33  ? 379  CYS A CB    1 
ATOM   3074  S SG    . CYS B 2 382  ? 147.942 125.468 109.370 1.00 67.69  ? 379  CYS A SG    1 
ATOM   3075  N N     . ASP B 2 383  ? 147.687 129.809 107.802 1.00 80.10  ? 380  ASP A N     1 
ATOM   3076  C CA    . ASP B 2 383  ? 147.318 131.193 107.532 1.00 85.60  ? 380  ASP A CA    1 
ATOM   3077  C C     . ASP B 2 383  ? 146.700 131.848 108.761 1.00 85.11  ? 380  ASP A C     1 
ATOM   3078  O O     . ASP B 2 383  ? 147.127 132.928 109.186 1.00 85.73  ? 380  ASP A O     1 
ATOM   3079  C CB    . ASP B 2 383  ? 146.357 131.258 106.343 1.00 89.96  ? 380  ASP A CB    1 
ATOM   3080  C CG    . ASP B 2 383  ? 146.929 130.617 105.092 1.00 94.25  ? 380  ASP A CG    1 
ATOM   3081  O OD1   . ASP B 2 383  ? 146.761 129.391 104.920 1.00 96.19  ? 380  ASP A OD1   1 
ATOM   3082  O OD2   . ASP B 2 383  ? 147.540 131.340 104.277 1.00 95.77  ? 380  ASP A OD2   1 
ATOM   3083  N N     . HIS B 2 384  ? 145.690 131.208 109.347 1.00 80.78  ? 381  HIS A N     1 
ATOM   3084  C CA    . HIS B 2 384  ? 144.980 131.765 110.486 1.00 78.81  ? 381  HIS A CA    1 
ATOM   3085  C C     . HIS B 2 384  ? 144.766 130.682 111.533 1.00 74.26  ? 381  HIS A C     1 
ATOM   3086  O O     . HIS B 2 384  ? 145.063 129.504 111.320 1.00 73.43  ? 381  HIS A O     1 
ATOM   3087  C CB    . HIS B 2 384  ? 143.628 132.364 110.074 1.00 79.52  ? 381  HIS A CB    1 
ATOM   3088  C CG    . HIS B 2 384  ? 143.624 132.962 108.701 1.00 82.73  ? 381  HIS A CG    1 
ATOM   3089  N ND1   . HIS B 2 384  ? 143.013 132.352 107.628 1.00 83.94  ? 381  HIS A ND1   1 
ATOM   3090  C CD2   . HIS B 2 384  ? 144.163 134.109 108.226 1.00 84.55  ? 381  HIS A CD2   1 
ATOM   3091  C CE1   . HIS B 2 384  ? 143.171 133.100 106.551 1.00 84.94  ? 381  HIS A CE1   1 
ATOM   3092  N NE2   . HIS B 2 384  ? 143.866 134.172 106.886 1.00 85.18  ? 381  HIS A NE2   1 
ATOM   3093  N N     . TRP B 2 385  ? 144.235 131.107 112.681 1.00 69.68  ? 382  TRP A N     1 
ATOM   3094  C CA    . TRP B 2 385  ? 143.810 130.169 113.713 1.00 66.96  ? 382  TRP A CA    1 
ATOM   3095  C C     . TRP B 2 385  ? 142.633 129.317 113.257 1.00 69.37  ? 382  TRP A C     1 
ATOM   3096  O O     . TRP B 2 385  ? 142.378 128.261 113.846 1.00 71.19  ? 382  TRP A O     1 
ATOM   3097  C CB    . TRP B 2 385  ? 143.424 130.936 114.973 1.00 61.32  ? 382  TRP A CB    1 
ATOM   3098  C CG    . TRP B 2 385  ? 142.224 131.796 114.748 1.00 55.72  ? 382  TRP A CG    1 
ATOM   3099  C CD1   . TRP B 2 385  ? 142.198 133.039 114.185 1.00 53.57  ? 382  TRP A CD1   1 
ATOM   3100  C CD2   . TRP B 2 385  ? 140.865 131.467 115.054 1.00 54.55  ? 382  TRP A CD2   1 
ATOM   3101  N NE1   . TRP B 2 385  ? 140.909 133.508 114.132 1.00 53.29  ? 382  TRP A NE1   1 
ATOM   3102  C CE2   . TRP B 2 385  ? 140.071 132.560 114.661 1.00 53.40  ? 382  TRP A CE2   1 
ATOM   3103  C CE3   . TRP B 2 385  ? 140.244 130.354 115.631 1.00 54.39  ? 382  TRP A CE3   1 
ATOM   3104  C CZ2   . TRP B 2 385  ? 138.688 132.574 114.824 1.00 53.68  ? 382  TRP A CZ2   1 
ATOM   3105  C CZ3   . TRP B 2 385  ? 138.871 130.370 115.792 1.00 52.80  ? 382  TRP A CZ3   1 
ATOM   3106  C CH2   . TRP B 2 385  ? 138.108 131.473 115.390 1.00 53.54  ? 382  TRP A CH2   1 
ATOM   3107  N N     . ASP B 2 386  ? 141.913 129.758 112.224 1.00 71.11  ? 383  ASP A N     1 
ATOM   3108  C CA    . ASP B 2 386  ? 140.702 129.079 111.779 1.00 67.80  ? 383  ASP A CA    1 
ATOM   3109  C C     . ASP B 2 386  ? 140.991 127.810 110.992 1.00 65.87  ? 383  ASP A C     1 
ATOM   3110  O O     . ASP B 2 386  ? 140.216 126.849 111.076 1.00 65.70  ? 383  ASP A O     1 
ATOM   3111  C CB    . ASP B 2 386  ? 139.869 130.023 110.911 1.00 70.79  ? 383  ASP A CB    1 
ATOM   3112  C CG    . ASP B 2 386  ? 138.681 130.592 111.644 1.00 77.68  ? 383  ASP A CG    1 
ATOM   3113  O OD1   . ASP B 2 386  ? 138.164 129.908 112.554 1.00 81.17  ? 383  ASP A OD1   1 
ATOM   3114  O OD2   . ASP B 2 386  ? 138.260 131.719 111.310 1.00 81.25  ? 383  ASP A OD2   1 
ATOM   3115  N N     . THR B 2 387  ? 142.092 127.784 110.238 1.00 62.87  ? 384  THR A N     1 
ATOM   3116  C CA    . THR B 2 387  ? 142.246 126.806 109.165 1.00 61.57  ? 384  THR A CA    1 
ATOM   3117  C C     . THR B 2 387  ? 142.195 125.372 109.679 1.00 59.61  ? 384  THR A C     1 
ATOM   3118  O O     . THR B 2 387  ? 141.575 124.507 109.050 1.00 59.56  ? 384  THR A O     1 
ATOM   3119  C CB    . THR B 2 387  ? 143.550 127.058 108.412 1.00 63.09  ? 384  THR A CB    1 
ATOM   3120  O OG1   . THR B 2 387  ? 144.620 127.193 109.354 1.00 66.51  ? 384  THR A OG1   1 
ATOM   3121  C CG2   . THR B 2 387  ? 143.447 128.329 107.580 1.00 61.17  ? 384  THR A CG2   1 
ATOM   3122  N N     . LEU B 2 388  ? 142.834 125.098 110.818 1.00 56.51  ? 385  LEU A N     1 
ATOM   3123  C CA    . LEU B 2 388  ? 142.868 123.725 111.318 1.00 53.86  ? 385  LEU A CA    1 
ATOM   3124  C C     . LEU B 2 388  ? 141.494 123.271 111.792 1.00 52.80  ? 385  LEU A C     1 
ATOM   3125  O O     . LEU B 2 388  ? 141.008 122.212 111.380 1.00 53.82  ? 385  LEU A O     1 
ATOM   3126  C CB    . LEU B 2 388  ? 143.895 123.592 112.442 1.00 53.86  ? 385  LEU A CB    1 
ATOM   3127  C CG    . LEU B 2 388  ? 145.346 123.535 111.968 1.00 55.35  ? 385  LEU A CG    1 
ATOM   3128  C CD1   . LEU B 2 388  ? 146.220 122.839 112.999 1.00 53.69  ? 385  LEU A CD1   1 
ATOM   3129  C CD2   . LEU B 2 388  ? 145.430 122.847 110.617 1.00 57.18  ? 385  LEU A CD2   1 
ATOM   3130  N N     . ARG B 2 389  ? 140.857 124.055 112.665 1.00 51.99  ? 386  ARG A N     1 
ATOM   3131  C CA    . ARG B 2 389  ? 139.530 123.691 113.148 1.00 52.98  ? 386  ARG A CA    1 
ATOM   3132  C C     . ARG B 2 389  ? 138.540 123.569 111.997 1.00 55.75  ? 386  ARG A C     1 
ATOM   3133  O O     . ARG B 2 389  ? 137.655 122.707 112.015 1.00 58.06  ? 386  ARG A O     1 
ATOM   3134  C CB    . ARG B 2 389  ? 139.045 124.721 114.166 1.00 55.21  ? 386  ARG A CB    1 
ATOM   3135  C CG    . ARG B 2 389  ? 137.699 124.394 114.790 1.00 57.31  ? 386  ARG A CG    1 
ATOM   3136  C CD    . ARG B 2 389  ? 137.037 125.644 115.338 1.00 59.90  ? 386  ARG A CD    1 
ATOM   3137  N NE    . ARG B 2 389  ? 136.753 126.609 114.280 1.00 62.20  ? 386  ARG A NE    1 
ATOM   3138  C CZ    . ARG B 2 389  ? 136.129 127.765 114.472 1.00 63.82  ? 386  ARG A CZ    1 
ATOM   3139  N NH1   . ARG B 2 389  ? 135.718 128.108 115.687 1.00 64.52  ? 386  ARG A NH1   1 
ATOM   3140  N NH2   . ARG B 2 389  ? 135.912 128.582 113.450 1.00 63.16  ? 386  ARG A NH2   1 
ATOM   3141  N N     . ASN B 2 390  ? 138.683 124.420 110.977 1.00 56.16  ? 387  ASN A N     1 
ATOM   3142  C CA    . ASN B 2 390  ? 137.786 124.360 109.829 1.00 56.50  ? 387  ASN A CA    1 
ATOM   3143  C C     . ASN B 2 390  ? 138.072 123.139 108.963 1.00 57.90  ? 387  ASN A C     1 
ATOM   3144  O O     . ASN B 2 390  ? 137.142 122.483 108.479 1.00 58.95  ? 387  ASN A O     1 
ATOM   3145  C CB    . ASN B 2 390  ? 137.901 125.645 109.008 1.00 58.12  ? 387  ASN A CB    1 
ATOM   3146  C CG    . ASN B 2 390  ? 137.299 126.846 109.716 1.00 59.62  ? 387  ASN A CG    1 
ATOM   3147  O OD1   . ASN B 2 390  ? 136.286 127.391 109.281 1.00 60.93  ? 387  ASN A OD1   1 
ATOM   3148  N ND2   . ASN B 2 390  ? 137.919 127.256 110.816 1.00 60.40  ? 387  ASN A ND2   1 
ATOM   3149  N N     . ALA B 2 391  ? 139.353 122.819 108.755 1.00 57.69  ? 388  ALA A N     1 
ATOM   3150  C CA    . ALA B 2 391  ? 139.701 121.656 107.941 1.00 54.96  ? 388  ALA A CA    1 
ATOM   3151  C C     . ALA B 2 391  ? 139.220 120.365 108.588 1.00 56.87  ? 388  ALA A C     1 
ATOM   3152  O O     . ALA B 2 391  ? 138.720 119.467 107.900 1.00 58.11  ? 388  ALA A O     1 
ATOM   3153  C CB    . ALA B 2 391  ? 141.212 121.609 107.707 1.00 51.53  ? 388  ALA A CB    1 
ATOM   3154  N N     . LEU B 2 392  ? 139.364 120.252 109.910 1.00 55.66  ? 389  LEU A N     1 
ATOM   3155  C CA    . LEU B 2 392  ? 138.830 119.090 110.612 1.00 53.61  ? 389  LEU A CA    1 
ATOM   3156  C C     . LEU B 2 392  ? 137.312 119.050 110.528 1.00 53.06  ? 389  LEU A C     1 
ATOM   3157  O O     . LEU B 2 392  ? 136.712 117.972 110.446 1.00 52.01  ? 389  LEU A O     1 
ATOM   3158  C CB    . LEU B 2 392  ? 139.284 119.100 112.073 1.00 51.97  ? 389  LEU A CB    1 
ATOM   3159  C CG    . LEU B 2 392  ? 140.786 118.984 112.335 1.00 52.74  ? 389  LEU A CG    1 
ATOM   3160  C CD1   . LEU B 2 392  ? 141.070 119.101 113.822 1.00 55.03  ? 389  LEU A CD1   1 
ATOM   3161  C CD2   . LEU B 2 392  ? 141.325 117.674 111.784 1.00 52.55  ? 389  LEU A CD2   1 
ATOM   3162  N N     . TYR B 2 393  ? 136.672 120.222 110.547 1.00 53.69  ? 390  TYR A N     1 
ATOM   3163  C CA    . TYR B 2 393  ? 135.217 120.279 110.449 1.00 51.99  ? 390  TYR A CA    1 
ATOM   3164  C C     . TYR B 2 393  ? 134.736 119.740 109.108 1.00 52.12  ? 390  TYR A C     1 
ATOM   3165  O O     . TYR B 2 393  ? 133.792 118.946 109.047 1.00 53.37  ? 390  TYR A O     1 
ATOM   3166  C CB    . TYR B 2 393  ? 134.733 121.714 110.655 1.00 48.18  ? 390  TYR A CB    1 
ATOM   3167  C CG    . TYR B 2 393  ? 133.264 121.910 110.352 1.00 48.90  ? 390  TYR A CG    1 
ATOM   3168  C CD1   . TYR B 2 393  ? 132.293 121.573 111.284 1.00 49.62  ? 390  TYR A CD1   1 
ATOM   3169  C CD2   . TYR B 2 393  ? 132.849 122.434 109.133 1.00 48.46  ? 390  TYR A CD2   1 
ATOM   3170  C CE1   . TYR B 2 393  ? 130.950 121.748 111.011 1.00 49.58  ? 390  TYR A CE1   1 
ATOM   3171  C CE2   . TYR B 2 393  ? 131.508 122.612 108.851 1.00 47.26  ? 390  TYR A CE2   1 
ATOM   3172  C CZ    . TYR B 2 393  ? 130.562 122.268 109.795 1.00 47.49  ? 390  TYR A CZ    1 
ATOM   3173  O OH    . TYR B 2 393  ? 129.225 122.444 109.525 1.00 46.61  ? 390  TYR A OH    1 
ATOM   3174  N N     . GLU B 2 394  ? 135.384 120.158 108.019 1.00 52.24  ? 391  GLU A N     1 
ATOM   3175  C CA    . GLU B 2 394  ? 134.943 119.733 106.695 1.00 53.91  ? 391  GLU A CA    1 
ATOM   3176  C C     . GLU B 2 394  ? 135.152 118.239 106.490 1.00 54.96  ? 391  GLU A C     1 
ATOM   3177  O O     . GLU B 2 394  ? 134.309 117.569 105.882 1.00 57.69  ? 391  GLU A O     1 
ATOM   3178  C CB    . GLU B 2 394  ? 135.671 120.536 105.617 1.00 55.46  ? 391  GLU A CB    1 
ATOM   3179  C CG    . GLU B 2 394  ? 135.368 122.029 105.650 1.00 57.86  ? 391  GLU A CG    1 
ATOM   3180  C CD    . GLU B 2 394  ? 133.909 122.338 105.364 1.00 60.24  ? 391  GLU A CD    1 
ATOM   3181  O OE1   . GLU B 2 394  ? 133.259 121.555 104.639 1.00 59.38  ? 391  GLU A OE1   1 
ATOM   3182  O OE2   . GLU B 2 394  ? 133.410 123.368 105.867 1.00 62.65  ? 391  GLU A OE2   1 
ATOM   3183  N N     . ARG B 2 395  ? 136.260 117.692 106.995 1.00 54.30  ? 392  ARG A N     1 
ATOM   3184  C CA    . ARG B 2 395  ? 136.516 116.268 106.801 1.00 53.47  ? 392  ARG A CA    1 
ATOM   3185  C C     . ARG B 2 395  ? 135.586 115.410 107.647 1.00 53.15  ? 392  ARG A C     1 
ATOM   3186  O O     . ARG B 2 395  ? 135.241 114.293 107.244 1.00 54.84  ? 392  ARG A O     1 
ATOM   3187  C CB    . ARG B 2 395  ? 137.972 115.935 107.120 1.00 55.02  ? 392  ARG A CB    1 
ATOM   3188  C CG    . ARG B 2 395  ? 138.431 114.614 106.525 1.00 57.39  ? 392  ARG A CG    1 
ATOM   3189  C CD    . ARG B 2 395  ? 139.861 114.291 106.915 1.00 61.93  ? 392  ARG A CD    1 
ATOM   3190  N NE    . ARG B 2 395  ? 139.926 113.331 108.012 1.00 66.40  ? 392  ARG A NE    1 
ATOM   3191  C CZ    . ARG B 2 395  ? 140.100 112.025 107.846 1.00 69.75  ? 392  ARG A CZ    1 
ATOM   3192  N NH1   . ARG B 2 395  ? 140.231 111.521 106.626 1.00 69.57  ? 392  ARG A NH1   1 
ATOM   3193  N NH2   . ARG B 2 395  ? 140.147 111.220 108.900 1.00 70.91  ? 392  ARG A NH2   1 
ATOM   3194  N N     . ARG B 2 396  ? 135.169 115.906 108.814 1.00 52.22  ? 393  ARG A N     1 
ATOM   3195  C CA    . ARG B 2 396  ? 134.245 115.145 109.645 1.00 54.26  ? 393  ARG A CA    1 
ATOM   3196  C C     . ARG B 2 396  ? 132.824 115.201 109.093 1.00 55.70  ? 393  ARG A C     1 
ATOM   3197  O O     . ARG B 2 396  ? 132.099 114.202 109.139 1.00 57.36  ? 393  ARG A O     1 
ATOM   3198  C CB    . ARG B 2 396  ? 134.289 115.651 111.088 1.00 54.41  ? 393  ARG A CB    1 
ATOM   3199  C CG    . ARG B 2 396  ? 135.573 115.277 111.816 1.00 56.79  ? 393  ARG A CG    1 
ATOM   3200  C CD    . ARG B 2 396  ? 135.481 115.545 113.309 1.00 60.52  ? 393  ARG A CD    1 
ATOM   3201  N NE    . ARG B 2 396  ? 136.641 115.012 114.021 1.00 64.57  ? 393  ARG A NE    1 
ATOM   3202  C CZ    . ARG B 2 396  ? 136.779 115.024 115.344 1.00 65.42  ? 393  ARG A CZ    1 
ATOM   3203  N NH1   . ARG B 2 396  ? 135.827 115.540 116.109 1.00 65.57  ? 393  ARG A NH1   1 
ATOM   3204  N NH2   . ARG B 2 396  ? 137.869 114.514 115.902 1.00 64.56  ? 393  ARG A NH2   1 
ATOM   3205  N N     . ILE B 2 397  ? 132.412 116.358 108.568 1.00 54.07  ? 394  ILE A N     1 
ATOM   3206  C CA    . ILE B 2 397  ? 131.146 116.427 107.843 1.00 53.38  ? 394  ILE A CA    1 
ATOM   3207  C C     . ILE B 2 397  ? 131.197 115.531 106.614 1.00 53.15  ? 394  ILE A C     1 
ATOM   3208  O O     . ILE B 2 397  ? 130.176 114.968 106.197 1.00 52.69  ? 394  ILE A O     1 
ATOM   3209  C CB    . ILE B 2 397  ? 130.823 117.890 107.472 1.00 53.94  ? 394  ILE A CB    1 
ATOM   3210  C CG1   . ILE B 2 397  ? 130.683 118.739 108.734 1.00 54.47  ? 394  ILE A CG1   1 
ATOM   3211  C CG2   . ILE B 2 397  ? 129.544 117.976 106.655 1.00 55.30  ? 394  ILE A CG2   1 
ATOM   3212  C CD1   . ILE B 2 397  ? 129.581 118.283 109.652 1.00 56.02  ? 394  ILE A CD1   1 
ATOM   3213  N N     . SER B 2 398  ? 132.386 115.360 106.032 1.00 52.75  ? 395  SER A N     1 
ATOM   3214  C CA    . SER B 2 398  ? 132.557 114.503 104.866 1.00 52.50  ? 395  SER A CA    1 
ATOM   3215  C C     . SER B 2 398  ? 132.294 113.034 105.167 1.00 54.01  ? 395  SER A C     1 
ATOM   3216  O O     . SER B 2 398  ? 132.107 112.251 104.230 1.00 55.81  ? 395  SER A O     1 
ATOM   3217  C CB    . SER B 2 398  ? 133.971 114.669 104.305 1.00 50.75  ? 395  SER A CB    1 
ATOM   3218  O OG    . SER B 2 398  ? 134.308 113.601 103.435 1.00 53.05  ? 395  SER A OG    1 
ATOM   3219  N N     . GLU B 2 399  ? 132.278 112.636 106.439 1.00 55.21  ? 396  GLU A N     1 
ATOM   3220  C CA    . GLU B 2 399  ? 132.119 111.237 106.812 1.00 57.39  ? 396  GLU A CA    1 
ATOM   3221  C C     . GLU B 2 399  ? 130.922 111.022 107.738 1.00 59.41  ? 396  GLU A C     1 
ATOM   3222  O O     . GLU B 2 399  ? 130.910 110.086 108.541 1.00 61.15  ? 396  GLU A O     1 
ATOM   3223  C CB    . GLU B 2 399  ? 133.402 110.703 107.448 1.00 60.42  ? 396  GLU A CB    1 
ATOM   3224  C CG    . GLU B 2 399  ? 134.022 111.616 108.490 1.00 64.28  ? 396  GLU A CG    1 
ATOM   3225  C CD    . GLU B 2 399  ? 135.502 111.342 108.699 1.00 67.07  ? 396  GLU A CD    1 
ATOM   3226  O OE1   . GLU B 2 399  ? 136.107 110.657 107.847 1.00 65.64  ? 396  GLU A OE1   1 
ATOM   3227  O OE2   . GLU B 2 399  ? 136.062 111.810 109.713 1.00 69.02  ? 396  GLU A OE2   1 
ATOM   3228  N N     . LEU B 2 400  ? 129.907 111.875 107.632 1.00 60.34  ? 397  LEU A N     1 
ATOM   3229  C CA    . LEU B 2 400  ? 128.654 111.642 108.332 1.00 61.52  ? 397  LEU A CA    1 
ATOM   3230  C C     . LEU B 2 400  ? 127.763 110.703 107.523 1.00 66.17  ? 397  LEU A C     1 
ATOM   3231  O O     . LEU B 2 400  ? 127.968 110.485 106.327 1.00 67.89  ? 397  LEU A O     1 
ATOM   3232  C CB    . LEU B 2 400  ? 127.927 112.957 108.605 1.00 58.33  ? 397  LEU A CB    1 
ATOM   3233  C CG    . LEU B 2 400  ? 128.470 113.869 109.706 1.00 56.07  ? 397  LEU A CG    1 
ATOM   3234  C CD1   . LEU B 2 400  ? 127.647 115.143 109.791 1.00 52.93  ? 397  LEU A CD1   1 
ATOM   3235  C CD2   . LEU B 2 400  ? 128.477 113.153 111.045 1.00 56.87  ? 397  LEU A CD2   1 
ATOM   3236  N N     . THR B 2 401  ? 126.754 110.153 108.193 1.00 67.17  ? 398  THR A N     1 
ATOM   3237  C CA    . THR B 2 401  ? 125.875 109.148 107.610 1.00 68.26  ? 398  THR A CA    1 
ATOM   3238  C C     . THR B 2 401  ? 124.501 109.742 107.336 1.00 70.42  ? 398  THR A C     1 
ATOM   3239  O O     . THR B 2 401  ? 123.928 110.417 108.199 1.00 69.99  ? 398  THR A O     1 
ATOM   3240  C CB    . THR B 2 401  ? 125.739 107.937 108.535 1.00 69.51  ? 398  THR A CB    1 
ATOM   3241  O OG1   . THR B 2 401  ? 127.037 107.420 108.842 1.00 71.09  ? 398  THR A OG1   1 
ATOM   3242  C CG2   . THR B 2 401  ? 124.912 106.849 107.870 1.00 69.04  ? 398  THR A CG2   1 
ATOM   3243  N N     . GLY B 2 402  ? 123.977 109.486 106.138 1.00 72.94  ? 399  GLY A N     1 
ATOM   3244  C CA    . GLY B 2 402  ? 122.617 109.854 105.805 1.00 73.38  ? 399  GLY A CA    1 
ATOM   3245  C C     . GLY B 2 402  ? 122.425 111.348 105.600 1.00 71.54  ? 399  GLY A C     1 
ATOM   3246  O O     . GLY B 2 402  ? 123.356 112.103 105.302 1.00 68.17  ? 399  GLY A O     1 
ATOM   3247  N N     . LYS B 2 403  ? 121.170 111.770 105.764 1.00 73.98  ? 400  LYS A N     1 
ATOM   3248  C CA    . LYS B 2 403  ? 120.792 113.166 105.598 1.00 75.40  ? 400  LYS A CA    1 
ATOM   3249  C C     . LYS B 2 403  ? 121.491 114.040 106.633 1.00 76.42  ? 400  LYS A C     1 
ATOM   3250  O O     . LYS B 2 403  ? 121.094 114.068 107.801 1.00 78.29  ? 400  LYS A O     1 
ATOM   3251  C CB    . LYS B 2 403  ? 119.274 113.326 105.701 1.00 75.22  ? 400  LYS A CB    1 
ATOM   3252  N N     . ILE B 2 404  ? 122.535 114.750 106.209 1.00 77.32  ? 401  ILE A N     1 
ATOM   3253  C CA    . ILE B 2 404  ? 123.310 115.594 107.110 1.00 79.60  ? 401  ILE A CA    1 
ATOM   3254  C C     . ILE B 2 404  ? 122.502 116.834 107.474 1.00 80.05  ? 401  ILE A C     1 
ATOM   3255  O O     . ILE B 2 404  ? 122.498 117.830 106.744 1.00 81.20  ? 401  ILE A O     1 
ATOM   3256  C CB    . ILE B 2 404  ? 124.671 115.968 106.488 1.00 81.75  ? 401  ILE A CB    1 
ATOM   3257  C CG1   . ILE B 2 404  ? 124.517 116.356 105.015 1.00 84.74  ? 401  ILE A CG1   1 
ATOM   3258  C CG2   . ILE B 2 404  ? 125.642 114.809 106.609 1.00 81.77  ? 401  ILE A CG2   1 
ATOM   3259  C CD1   . ILE B 2 404  ? 125.810 116.814 104.369 1.00 85.76  ? 401  ILE A CD1   1 
ATOM   3260  N N     . THR B 2 405  ? 121.805 116.776 108.607 1.00 82.99  ? 402  THR A N     1 
ATOM   3261  C CA    . THR B 2 405  ? 121.026 117.916 109.061 1.00 83.36  ? 402  THR A CA    1 
ATOM   3262  C C     . THR B 2 405  ? 121.952 119.006 109.600 1.00 80.94  ? 402  THR A C     1 
ATOM   3263  O O     . THR B 2 405  ? 123.160 118.817 109.760 1.00 81.11  ? 402  THR A O     1 
ATOM   3264  C CB    . THR B 2 405  ? 120.036 117.494 110.145 1.00 81.38  ? 402  THR A CB    1 
ATOM   3265  O OG1   . THR B 2 405  ? 120.739 117.269 111.374 1.00 80.24  ? 402  THR A OG1   1 
ATOM   3266  C CG2   . THR B 2 405  ? 119.317 116.214 109.740 1.00 79.79  ? 402  THR A CG2   1 
ATOM   3267  N N     . LYS B 2 406  ? 121.363 120.170 109.886 1.00 78.98  ? 403  LYS A N     1 
ATOM   3268  C CA    . LYS B 2 406  ? 122.128 121.219 110.545 1.00 77.98  ? 403  LYS A CA    1 
ATOM   3269  C C     . LYS B 2 406  ? 122.385 120.890 112.010 1.00 78.45  ? 403  LYS A C     1 
ATOM   3270  O O     . LYS B 2 406  ? 123.283 121.485 112.618 1.00 78.31  ? 403  LYS A O     1 
ATOM   3271  C CB    . LYS B 2 406  ? 121.410 122.567 110.425 1.00 79.48  ? 403  LYS A CB    1 
ATOM   3272  C CG    . LYS B 2 406  ? 120.525 122.920 111.610 1.00 83.78  ? 403  LYS A CG    1 
ATOM   3273  C CD    . LYS B 2 406  ? 120.740 124.366 112.032 1.00 85.62  ? 403  LYS A CD    1 
ATOM   3274  C CE    . LYS B 2 406  ? 119.976 124.698 113.303 1.00 86.78  ? 403  LYS A CE    1 
ATOM   3275  N NZ    . LYS B 2 406  ? 120.298 126.067 113.796 1.00 86.12  ? 403  LYS A NZ    1 
ATOM   3276  N N     . SER B 2 407  ? 121.619 119.961 112.585 1.00 74.71  ? 404  SER A N     1 
ATOM   3277  C CA    . SER B 2 407  ? 121.901 119.498 113.937 1.00 71.62  ? 404  SER A CA    1 
ATOM   3278  C C     . SER B 2 407  ? 123.163 118.648 113.973 1.00 65.44  ? 404  SER A C     1 
ATOM   3279  O O     . SER B 2 407  ? 123.960 118.744 114.914 1.00 60.62  ? 404  SER A O     1 
ATOM   3280  C CB    . SER B 2 407  ? 120.709 118.711 114.481 1.00 74.39  ? 404  SER A CB    1 
ATOM   3281  O OG    . SER B 2 407  ? 121.020 118.115 115.730 1.00 75.44  ? 404  SER A OG    1 
ATOM   3282  N N     . ALA B 2 408  ? 123.364 117.809 112.951 1.00 63.23  ? 405  ALA A N     1 
ATOM   3283  C CA    . ALA B 2 408  ? 124.573 116.997 112.888 1.00 61.48  ? 405  ALA A CA    1 
ATOM   3284  C C     . ALA B 2 408  ? 125.817 117.854 112.692 1.00 58.53  ? 405  ALA A C     1 
ATOM   3285  O O     . ALA B 2 408  ? 126.900 117.487 113.160 1.00 58.67  ? 405  ALA A O     1 
ATOM   3286  C CB    . ALA B 2 408  ? 124.457 115.967 111.762 1.00 62.47  ? 405  ALA A CB    1 
ATOM   3287  N N     . LYS B 2 409  ? 125.685 118.993 112.010 1.00 57.00  ? 406  LYS A N     1 
ATOM   3288  C CA    . LYS B 2 409  ? 126.830 119.880 111.839 1.00 56.36  ? 406  LYS A CA    1 
ATOM   3289  C C     . LYS B 2 409  ? 127.196 120.562 113.150 1.00 54.87  ? 406  LYS A C     1 
ATOM   3290  O O     . LYS B 2 409  ? 128.382 120.710 113.470 1.00 53.77  ? 406  LYS A O     1 
ATOM   3291  C CB    . LYS B 2 409  ? 126.539 120.915 110.752 1.00 61.01  ? 406  LYS A CB    1 
ATOM   3292  C CG    . LYS B 2 409  ? 126.293 120.312 109.378 1.00 65.36  ? 406  LYS A CG    1 
ATOM   3293  C CD    . LYS B 2 409  ? 126.295 121.379 108.296 1.00 67.88  ? 406  LYS A CD    1 
ATOM   3294  C CE    . LYS B 2 409  ? 126.169 120.759 106.915 1.00 71.70  ? 406  LYS A CE    1 
ATOM   3295  N NZ    . LYS B 2 409  ? 126.335 121.772 105.833 1.00 73.84  ? 406  LYS A NZ    1 
ATOM   3296  N N     . GLU B 2 410  ? 126.194 120.981 113.926 1.00 55.94  ? 407  GLU A N     1 
ATOM   3297  C CA    . GLU B 2 410  ? 126.472 121.606 115.213 1.00 57.70  ? 407  GLU A CA    1 
ATOM   3298  C C     . GLU B 2 410  ? 127.087 120.618 116.195 1.00 55.32  ? 407  GLU A C     1 
ATOM   3299  O O     . GLU B 2 410  ? 127.872 121.017 117.063 1.00 52.80  ? 407  GLU A O     1 
ATOM   3300  C CB    . GLU B 2 410  ? 125.192 122.211 115.789 1.00 63.55  ? 407  GLU A CB    1 
ATOM   3301  C CG    . GLU B 2 410  ? 124.619 123.337 114.944 1.00 70.51  ? 407  GLU A CG    1 
ATOM   3302  C CD    . GLU B 2 410  ? 123.331 123.895 115.513 1.00 77.80  ? 407  GLU A CD    1 
ATOM   3303  O OE1   . GLU B 2 410  ? 122.830 123.336 116.511 1.00 80.15  ? 407  GLU A OE1   1 
ATOM   3304  O OE2   . GLU B 2 410  ? 122.822 124.894 114.962 1.00 80.58  ? 407  GLU A OE2   1 
ATOM   3305  N N     . LYS B 2 411  ? 126.746 119.331 116.075 1.00 54.41  ? 408  LYS A N     1 
ATOM   3306  C CA    . LYS B 2 411  ? 127.382 118.320 116.915 1.00 49.77  ? 408  LYS A CA    1 
ATOM   3307  C C     . LYS B 2 411  ? 128.857 118.165 116.564 1.00 48.18  ? 408  LYS A C     1 
ATOM   3308  O O     . LYS B 2 411  ? 129.693 117.966 117.455 1.00 49.97  ? 408  LYS A O     1 
ATOM   3309  C CB    . LYS B 2 411  ? 126.652 116.983 116.773 1.00 48.74  ? 408  LYS A CB    1 
ATOM   3310  C CG    . LYS B 2 411  ? 125.236 116.984 117.322 1.00 47.76  ? 408  LYS A CG    1 
ATOM   3311  C CD    . LYS B 2 411  ? 124.610 115.602 117.227 1.00 45.74  ? 408  LYS A CD    1 
ATOM   3312  C CE    . LYS B 2 411  ? 123.218 115.583 117.839 1.00 44.65  ? 408  LYS A CE    1 
ATOM   3313  N NZ    . LYS B 2 411  ? 122.622 114.218 117.816 1.00 44.18  ? 408  LYS A NZ    1 
ATOM   3314  N N     . VAL B 2 412  ? 129.194 118.256 115.278 1.00 46.81  ? 409  VAL A N     1 
ATOM   3315  C CA    . VAL B 2 412  ? 130.594 118.192 114.871 1.00 44.92  ? 409  VAL A CA    1 
ATOM   3316  C C     . VAL B 2 412  ? 131.346 119.428 115.357 1.00 46.96  ? 409  VAL A C     1 
ATOM   3317  O O     . VAL B 2 412  ? 132.512 119.345 115.757 1.00 48.55  ? 409  VAL A O     1 
ATOM   3318  C CB    . VAL B 2 412  ? 130.697 118.019 113.345 1.00 41.72  ? 409  VAL A CB    1 
ATOM   3319  C CG1   . VAL B 2 412  ? 132.147 118.091 112.889 1.00 39.72  ? 409  VAL A CG1   1 
ATOM   3320  C CG2   . VAL B 2 412  ? 130.071 116.698 112.918 1.00 40.35  ? 409  VAL A CG2   1 
ATOM   3321  N N     . GLN B 2 413  ? 130.685 120.589 115.349 1.00 50.27  ? 410  GLN A N     1 
ATOM   3322  C CA    . GLN B 2 413  ? 131.317 121.808 115.844 1.00 54.59  ? 410  GLN A CA    1 
ATOM   3323  C C     . GLN B 2 413  ? 131.632 121.698 117.330 1.00 56.91  ? 410  GLN A C     1 
ATOM   3324  O O     . GLN B 2 413  ? 132.761 121.966 117.760 1.00 58.31  ? 410  GLN A O     1 
ATOM   3325  C CB    . GLN B 2 413  ? 130.415 123.016 115.582 1.00 60.84  ? 410  GLN A CB    1 
ATOM   3326  C CG    . GLN B 2 413  ? 130.218 123.362 114.119 1.00 66.82  ? 410  GLN A CG    1 
ATOM   3327  C CD    . GLN B 2 413  ? 129.457 124.661 113.929 1.00 70.48  ? 410  GLN A CD    1 
ATOM   3328  O OE1   . GLN B 2 413  ? 129.407 125.503 114.825 1.00 73.35  ? 410  GLN A OE1   1 
ATOM   3329  N NE2   . GLN B 2 413  ? 128.855 124.828 112.756 1.00 69.47  ? 410  GLN A NE2   1 
ATOM   3330  N N     . ARG B 2 414  ? 130.640 121.307 118.135 1.00 58.45  ? 411  ARG A N     1 
ATOM   3331  C CA    . ARG B 2 414  ? 130.850 121.216 119.576 1.00 62.08  ? 411  ARG A CA    1 
ATOM   3332  C C     . ARG B 2 414  ? 131.876 120.148 119.932 1.00 60.96  ? 411  ARG A C     1 
ATOM   3333  O O     . ARG B 2 414  ? 132.584 120.281 120.937 1.00 62.33  ? 411  ARG A O     1 
ATOM   3334  C CB    . ARG B 2 414  ? 129.522 120.939 120.283 1.00 68.98  ? 411  ARG A CB    1 
ATOM   3335  C CG    . ARG B 2 414  ? 128.683 122.185 120.543 1.00 74.07  ? 411  ARG A CG    1 
ATOM   3336  C CD    . ARG B 2 414  ? 127.236 121.987 120.123 1.00 77.19  ? 411  ARG A CD    1 
ATOM   3337  N NE    . ARG B 2 414  ? 126.639 120.801 120.727 1.00 80.01  ? 411  ARG A NE    1 
ATOM   3338  C CZ    . ARG B 2 414  ? 125.412 120.363 120.460 1.00 82.13  ? 411  ARG A CZ    1 
ATOM   3339  N NH1   . ARG B 2 414  ? 124.649 121.017 119.594 1.00 82.60  ? 411  ARG A NH1   1 
ATOM   3340  N NH2   . ARG B 2 414  ? 124.950 119.272 121.055 1.00 82.76  ? 411  ARG A NH2   1 
ATOM   3341  N N     . SER B 2 415  ? 131.978 119.090 119.124 1.00 59.70  ? 412  SER A N     1 
ATOM   3342  C CA    . SER B 2 415  ? 132.953 118.042 119.405 1.00 60.25  ? 412  SER A CA    1 
ATOM   3343  C C     . SER B 2 415  ? 134.379 118.557 119.246 1.00 59.40  ? 412  SER A C     1 
ATOM   3344  O O     . SER B 2 415  ? 135.275 118.164 120.003 1.00 59.22  ? 412  SER A O     1 
ATOM   3345  C CB    . SER B 2 415  ? 132.709 116.839 118.496 1.00 59.64  ? 412  SER A CB    1 
ATOM   3346  O OG    . SER B 2 415  ? 132.855 117.189 117.131 1.00 57.95  ? 412  SER A OG    1 
ATOM   3347  N N     . LEU B 2 416  ? 134.607 119.444 118.277 1.00 57.65  ? 413  LEU A N     1 
ATOM   3348  C CA    . LEU B 2 416  ? 135.946 119.967 118.027 1.00 56.59  ? 413  LEU A CA    1 
ATOM   3349  C C     . LEU B 2 416  ? 136.413 120.951 119.092 1.00 56.85  ? 413  LEU A C     1 
ATOM   3350  O O     . LEU B 2 416  ? 137.604 121.277 119.126 1.00 57.64  ? 413  LEU A O     1 
ATOM   3351  C CB    . LEU B 2 416  ? 135.997 120.639 116.653 1.00 55.53  ? 413  LEU A CB    1 
ATOM   3352  C CG    . LEU B 2 416  ? 135.800 119.720 115.447 1.00 56.32  ? 413  LEU A CG    1 
ATOM   3353  C CD1   . LEU B 2 416  ? 135.790 120.520 114.154 1.00 56.37  ? 413  LEU A CD1   1 
ATOM   3354  C CD2   . LEU B 2 416  ? 136.884 118.652 115.409 1.00 57.40  ? 413  LEU A CD2   1 
ATOM   3355  N N     . LYS B 2 417  ? 135.518 121.431 119.957 1.00 58.81  ? 414  LYS A N     1 
ATOM   3356  C CA    . LYS B 2 417  ? 135.924 122.393 120.974 1.00 62.96  ? 414  LYS A CA    1 
ATOM   3357  C C     . LYS B 2 417  ? 136.592 121.727 122.170 1.00 70.32  ? 414  LYS A C     1 
ATOM   3358  O O     . LYS B 2 417  ? 137.511 122.306 122.760 1.00 74.45  ? 414  LYS A O     1 
ATOM   3359  C CB    . LYS B 2 417  ? 134.724 123.212 121.450 1.00 64.17  ? 414  LYS A CB    1 
ATOM   3360  C CG    . LYS B 2 417  ? 134.223 124.240 120.452 1.00 65.36  ? 414  LYS A CG    1 
ATOM   3361  C CD    . LYS B 2 417  ? 133.171 125.133 121.086 1.00 68.65  ? 414  LYS A CD    1 
ATOM   3362  C CE    . LYS B 2 417  ? 132.592 126.116 120.084 1.00 71.61  ? 414  LYS A CE    1 
ATOM   3363  N NZ    . LYS B 2 417  ? 131.625 127.048 120.729 1.00 73.27  ? 414  LYS A NZ    1 
ATOM   3364  N N     . HIS B 2 418  ? 136.154 120.523 122.545 1.00 73.22  ? 415  HIS A N     1 
ATOM   3365  C CA    . HIS B 2 418  ? 136.630 119.873 123.763 1.00 78.11  ? 415  HIS A CA    1 
ATOM   3366  C C     . HIS B 2 418  ? 136.927 118.391 123.520 1.00 80.86  ? 415  HIS A C     1 
ATOM   3367  O O     . HIS B 2 418  ? 136.364 117.500 124.148 1.00 82.13  ? 415  HIS A O     1 
ATOM   3368  C CB    . HIS B 2 418  ? 135.618 120.056 124.895 1.00 82.40  ? 415  HIS A CB    1 
ATOM   3369  C CG    . HIS B 2 418  ? 134.241 119.566 124.569 1.00 85.61  ? 415  HIS A CG    1 
ATOM   3370  N ND1   . HIS B 2 418  ? 133.967 118.248 124.276 1.00 86.50  ? 415  HIS A ND1   1 
ATOM   3371  C CD2   . HIS B 2 418  ? 133.056 120.219 124.500 1.00 87.03  ? 415  HIS A CD2   1 
ATOM   3372  C CE1   . HIS B 2 418  ? 132.675 118.109 124.034 1.00 87.72  ? 415  HIS A CE1   1 
ATOM   3373  N NE2   . HIS B 2 418  ? 132.099 119.292 124.163 1.00 88.00  ? 415  HIS A NE2   1 
ATOM   3374  N N     . GLU B 2 419  ? 137.844 118.114 122.596 1.00 83.95  ? 416  GLU A N     1 
ATOM   3375  C CA    . GLU B 2 419  ? 138.364 116.762 122.441 1.00 83.79  ? 416  GLU A CA    1 
ATOM   3376  C C     . GLU B 2 419  ? 139.740 116.844 121.798 1.00 78.53  ? 416  GLU A C     1 
ATOM   3377  O O     . GLU B 2 419  ? 140.034 117.775 121.045 1.00 77.95  ? 416  GLU A O     1 
ATOM   3378  C CB    . GLU B 2 419  ? 137.436 115.869 121.606 1.00 87.67  ? 416  GLU A CB    1 
ATOM   3379  C CG    . GLU B 2 419  ? 137.584 116.019 120.100 1.00 90.17  ? 416  GLU A CG    1 
ATOM   3380  C CD    . GLU B 2 419  ? 137.184 114.761 119.353 1.00 93.38  ? 416  GLU A CD    1 
ATOM   3381  O OE1   . GLU B 2 419  ? 138.048 113.876 119.172 1.00 94.41  ? 416  GLU A OE1   1 
ATOM   3382  O OE2   . GLU B 2 419  ? 136.005 114.649 118.958 1.00 94.47  ? 416  GLU A OE2   1 
ATOM   3383  N N     . ASP B 2 420  ? 140.582 115.862 122.111 1.00 71.23  ? 417  ASP A N     1 
ATOM   3384  C CA    . ASP B 2 420  ? 141.930 115.824 121.568 1.00 65.54  ? 417  ASP A CA    1 
ATOM   3385  C C     . ASP B 2 420  ? 141.918 115.150 120.204 1.00 63.16  ? 417  ASP A C     1 
ATOM   3386  O O     . ASP B 2 420  ? 141.352 114.066 120.043 1.00 65.36  ? 417  ASP A O     1 
ATOM   3387  C CB    . ASP B 2 420  ? 142.871 115.087 122.519 1.00 65.54  ? 417  ASP A CB    1 
ATOM   3388  C CG    . ASP B 2 420  ? 142.948 115.742 123.881 1.00 66.13  ? 417  ASP A CG    1 
ATOM   3389  O OD1   . ASP B 2 420  ? 142.913 116.990 123.947 1.00 63.56  ? 417  ASP A OD1   1 
ATOM   3390  O OD2   . ASP B 2 420  ? 143.036 115.010 124.888 1.00 69.64  ? 417  ASP A OD2   1 
ATOM   3391  N N     . ILE B 2 421  ? 142.535 115.801 119.220 1.00 60.55  ? 418  ILE A N     1 
ATOM   3392  C CA    . ILE B 2 421  ? 142.601 115.295 117.857 1.00 60.91  ? 418  ILE A CA    1 
ATOM   3393  C C     . ILE B 2 421  ? 143.928 114.574 117.676 1.00 63.56  ? 418  ILE A C     1 
ATOM   3394  O O     . ILE B 2 421  ? 144.979 115.083 118.081 1.00 67.57  ? 418  ILE A O     1 
ATOM   3395  C CB    . ILE B 2 421  ? 142.454 116.430 116.830 1.00 62.30  ? 418  ILE A CB    1 
ATOM   3396  C CG1   . ILE B 2 421  ? 141.348 117.403 117.251 1.00 60.60  ? 418  ILE A CG1   1 
ATOM   3397  C CG2   . ILE B 2 421  ? 142.168 115.859 115.447 1.00 64.15  ? 418  ILE A CG2   1 
ATOM   3398  C CD1   . ILE B 2 421  ? 139.961 116.801 117.249 1.00 59.92  ? 418  ILE A CD1   1 
ATOM   3399  N N     . ASN B 2 422  ? 143.886 113.388 117.071 1.00 63.00  ? 419  ASN A N     1 
ATOM   3400  C CA    . ASN B 2 422  ? 145.121 112.687 116.763 1.00 62.27  ? 419  ASN A CA    1 
ATOM   3401  C C     . ASN B 2 422  ? 145.814 113.350 115.577 1.00 59.36  ? 419  ASN A C     1 
ATOM   3402  O O     . ASN B 2 422  ? 145.177 113.976 114.725 1.00 57.11  ? 419  ASN A O     1 
ATOM   3403  C CB    . ASN B 2 422  ? 144.855 111.209 116.472 1.00 65.14  ? 419  ASN A CB    1 
ATOM   3404  C CG    . ASN B 2 422  ? 143.982 110.997 115.252 1.00 67.96  ? 419  ASN A CG    1 
ATOM   3405  O OD1   . ASN B 2 422  ? 144.445 111.102 114.116 1.00 67.95  ? 419  ASN A OD1   1 
ATOM   3406  N ND2   . ASN B 2 422  ? 142.713 110.679 115.481 1.00 70.51  ? 419  ASN A ND2   1 
ATOM   3407  N N     . LEU B 2 423  ? 147.142 113.206 115.531 1.00 59.65  ? 420  LEU A N     1 
ATOM   3408  C CA    . LEU B 2 423  ? 147.930 113.904 114.522 1.00 57.46  ? 420  LEU A CA    1 
ATOM   3409  C C     . LEU B 2 423  ? 147.599 113.432 113.109 1.00 55.20  ? 420  LEU A C     1 
ATOM   3410  O O     . LEU B 2 423  ? 147.740 114.205 112.155 1.00 55.83  ? 420  LEU A O     1 
ATOM   3411  C CB    . LEU B 2 423  ? 149.422 113.725 114.809 1.00 55.94  ? 420  LEU A CB    1 
ATOM   3412  C CG    . LEU B 2 423  ? 150.394 114.553 113.966 1.00 52.83  ? 420  LEU A CG    1 
ATOM   3413  C CD1   . LEU B 2 423  ? 150.055 116.033 114.053 1.00 50.48  ? 420  LEU A CD1   1 
ATOM   3414  C CD2   . LEU B 2 423  ? 151.831 114.304 114.401 1.00 53.36  ? 420  LEU A CD2   1 
ATOM   3415  N N     . GLN B 2 424  ? 147.150 112.185 112.954 1.00 54.17  ? 421  GLN A N     1 
ATOM   3416  C CA    . GLN B 2 424  ? 146.851 111.682 111.616 1.00 57.88  ? 421  GLN A CA    1 
ATOM   3417  C C     . GLN B 2 424  ? 145.617 112.359 111.029 1.00 57.24  ? 421  GLN A C     1 
ATOM   3418  O O     . GLN B 2 424  ? 145.604 112.711 109.845 1.00 58.01  ? 421  GLN A O     1 
ATOM   3419  C CB    . GLN B 2 424  ? 146.663 110.165 111.651 1.00 62.21  ? 421  GLN A CB    1 
ATOM   3420  C CG    . GLN B 2 424  ? 146.483 109.544 110.274 1.00 66.03  ? 421  GLN A CG    1 
ATOM   3421  C CD    . GLN B 2 424  ? 147.631 109.867 109.337 1.00 70.27  ? 421  GLN A CD    1 
ATOM   3422  O OE1   . GLN B 2 424  ? 148.802 109.736 109.703 1.00 74.17  ? 421  GLN A OE1   1 
ATOM   3423  N NE2   . GLN B 2 424  ? 147.305 110.303 108.126 1.00 67.95  ? 421  GLN A NE2   1 
ATOM   3424  N N     . GLU B 2 425  ? 144.573 112.550 111.841 1.00 54.96  ? 422  GLU A N     1 
ATOM   3425  C CA    . GLU B 2 425  ? 143.375 113.219 111.348 1.00 53.95  ? 422  GLU A CA    1 
ATOM   3426  C C     . GLU B 2 425  ? 143.655 114.671 110.981 1.00 52.50  ? 422  GLU A C     1 
ATOM   3427  O O     . GLU B 2 425  ? 142.986 115.228 110.103 1.00 50.75  ? 422  GLU A O     1 
ATOM   3428  C CB    . GLU B 2 425  ? 142.258 113.142 112.390 1.00 56.69  ? 422  GLU A CB    1 
ATOM   3429  C CG    . GLU B 2 425  ? 140.897 113.584 111.868 1.00 60.25  ? 422  GLU A CG    1 
ATOM   3430  C CD    . GLU B 2 425  ? 139.812 113.526 112.929 1.00 65.93  ? 422  GLU A CD    1 
ATOM   3431  O OE1   . GLU B 2 425  ? 140.154 113.457 114.128 1.00 70.77  ? 422  GLU A OE1   1 
ATOM   3432  O OE2   . GLU B 2 425  ? 138.618 113.548 112.560 1.00 65.23  ? 422  GLU A OE2   1 
ATOM   3433  N N     . ILE B 2 426  ? 144.641 115.295 111.629 1.00 52.90  ? 423  ILE A N     1 
ATOM   3434  C CA    . ILE B 2 426  ? 145.009 116.660 111.270 1.00 54.91  ? 423  ILE A CA    1 
ATOM   3435  C C     . ILE B 2 426  ? 145.695 116.687 109.910 1.00 58.00  ? 423  ILE A C     1 
ATOM   3436  O O     . ILE B 2 426  ? 145.393 117.535 109.063 1.00 59.25  ? 423  ILE A O     1 
ATOM   3437  C CB    . ILE B 2 426  ? 145.896 117.281 112.365 1.00 51.61  ? 423  ILE A CB    1 
ATOM   3438  C CG1   . ILE B 2 426  ? 145.179 117.250 113.716 1.00 51.48  ? 423  ILE A CG1   1 
ATOM   3439  C CG2   . ILE B 2 426  ? 146.277 118.708 112.002 1.00 47.13  ? 423  ILE A CG2   1 
ATOM   3440  C CD1   . ILE B 2 426  ? 145.976 117.876 114.841 1.00 51.56  ? 423  ILE A CD1   1 
ATOM   3441  N N     . ILE B 2 427  ? 146.621 115.754 109.676 1.00 59.00  ? 424  ILE A N     1 
ATOM   3442  C CA    . ILE B 2 427  ? 147.342 115.717 108.407 1.00 60.20  ? 424  ILE A CA    1 
ATOM   3443  C C     . ILE B 2 427  ? 146.401 115.346 107.268 1.00 60.59  ? 424  ILE A C     1 
ATOM   3444  O O     . ILE B 2 427  ? 146.465 115.927 106.177 1.00 61.13  ? 424  ILE A O     1 
ATOM   3445  C CB    . ILE B 2 427  ? 148.532 114.746 108.499 1.00 61.48  ? 424  ILE A CB    1 
ATOM   3446  C CG1   . ILE B 2 427  ? 149.527 115.224 109.559 1.00 60.61  ? 424  ILE A CG1   1 
ATOM   3447  C CG2   . ILE B 2 427  ? 149.215 114.598 107.148 1.00 63.62  ? 424  ILE A CG2   1 
ATOM   3448  C CD1   . ILE B 2 427  ? 150.723 114.314 109.726 1.00 60.75  ? 424  ILE A CD1   1 
ATOM   3449  N N     . SER B 2 428  ? 145.506 114.383 107.500 1.00 59.87  ? 425  SER A N     1 
ATOM   3450  C CA    . SER B 2 428  ? 144.572 113.960 106.462 1.00 60.24  ? 425  SER A CA    1 
ATOM   3451  C C     . SER B 2 428  ? 143.560 115.043 106.112 1.00 60.39  ? 425  SER A C     1 
ATOM   3452  O O     . SER B 2 428  ? 142.949 114.976 105.040 1.00 61.34  ? 425  SER A O     1 
ATOM   3453  C CB    . SER B 2 428  ? 143.839 112.693 106.900 1.00 61.33  ? 425  SER A CB    1 
ATOM   3454  O OG    . SER B 2 428  ? 144.747 111.635 107.146 1.00 64.10  ? 425  SER A OG    1 
ATOM   3455  N N     . ALA B 2 429  ? 143.372 116.035 106.981 1.00 58.46  ? 426  ALA A N     1 
ATOM   3456  C CA    . ALA B 2 429  ? 142.396 117.090 106.748 1.00 56.73  ? 426  ALA A CA    1 
ATOM   3457  C C     . ALA B 2 429  ? 143.014 118.398 106.280 1.00 56.81  ? 426  ALA A C     1 
ATOM   3458  O O     . ALA B 2 429  ? 142.335 119.187 105.614 1.00 54.87  ? 426  ALA A O     1 
ATOM   3459  C CB    . ALA B 2 429  ? 141.585 117.352 108.022 1.00 55.01  ? 426  ALA A CB    1 
ATOM   3460  N N     . ALA B 2 430  ? 144.281 118.651 106.607 1.00 58.19  ? 427  ALA A N     1 
ATOM   3461  C CA    . ALA B 2 430  ? 144.920 119.918 106.277 1.00 60.00  ? 427  ALA A CA    1 
ATOM   3462  C C     . ALA B 2 430  ? 145.782 119.857 105.026 1.00 63.25  ? 427  ALA A C     1 
ATOM   3463  O O     . ALA B 2 430  ? 145.973 120.888 104.375 1.00 64.89  ? 427  ALA A O     1 
ATOM   3464  C CB    . ALA B 2 430  ? 145.779 120.399 107.452 1.00 60.15  ? 427  ALA A CB    1 
ATOM   3465  N N     . GLY B 2 431  ? 146.302 118.691 104.678 1.00 64.73  ? 428  GLY A N     1 
ATOM   3466  C CA    . GLY B 2 431  ? 147.144 118.532 103.511 1.00 66.84  ? 428  GLY A CA    1 
ATOM   3467  C C     . GLY B 2 431  ? 148.607 118.354 103.882 1.00 70.62  ? 428  GLY A C     1 
ATOM   3468  O O     . GLY B 2 431  ? 149.015 118.473 105.037 1.00 71.44  ? 428  GLY A O     1 
ATOM   3469  N N     . LYS B 2 432  ? 149.405 118.065 102.851 1.00 75.03  ? 429  LYS A N     1 
ATOM   3470  C CA    . LYS B 2 432  ? 150.826 117.814 103.058 1.00 78.06  ? 429  LYS A CA    1 
ATOM   3471  C C     . LYS B 2 432  ? 151.589 119.071 103.451 1.00 81.83  ? 429  LYS A C     1 
ATOM   3472  O O     . LYS B 2 432  ? 152.701 118.964 103.979 1.00 84.59  ? 429  LYS A O     1 
ATOM   3473  C CB    . LYS B 2 432  ? 151.445 117.206 101.798 1.00 77.14  ? 429  LYS A CB    1 
ATOM   3474  C CG    . LYS B 2 432  ? 151.500 118.152 100.608 1.00 75.93  ? 429  LYS A CG    1 
ATOM   3475  C CD    . LYS B 2 432  ? 152.160 117.485 99.410  1.00 76.10  ? 429  LYS A CD    1 
ATOM   3476  C CE    . LYS B 2 432  ? 152.313 118.456 98.251  1.00 75.72  ? 429  LYS A CE    1 
ATOM   3477  N NZ    . LYS B 2 432  ? 152.932 117.808 97.060  1.00 75.64  ? 429  LYS A NZ    1 
ATOM   3478  N N     . GLU B 2 433  ? 151.025 120.256 103.212 1.00 83.67  ? 430  GLU A N     1 
ATOM   3479  C CA    . GLU B 2 433  ? 151.715 121.491 103.560 1.00 84.17  ? 430  GLU A CA    1 
ATOM   3480  C C     . GLU B 2 433  ? 151.740 121.755 105.059 1.00 80.64  ? 430  GLU A C     1 
ATOM   3481  O O     . GLU B 2 433  ? 152.512 122.611 105.504 1.00 80.72  ? 430  GLU A O     1 
ATOM   3482  C CB    . GLU B 2 433  ? 151.078 122.676 102.831 1.00 88.06  ? 430  GLU A CB    1 
ATOM   3483  C CG    . GLU B 2 433  ? 151.414 122.744 101.347 1.00 93.19  ? 430  GLU A CG    1 
ATOM   3484  C CD    . GLU B 2 433  ? 152.912 122.705 101.083 1.00 97.69  ? 430  GLU A CD    1 
ATOM   3485  O OE1   . GLU B 2 433  ? 153.570 123.757 101.235 1.00 98.64  ? 430  GLU A OE1   1 
ATOM   3486  O OE2   . GLU B 2 433  ? 153.431 121.625 100.734 1.00 99.47  ? 430  GLU A OE2   1 
ATOM   3487  N N     . LEU B 2 434  ? 150.922 121.053 105.845 1.00 76.25  ? 431  LEU A N     1 
ATOM   3488  C CA    . LEU B 2 434  ? 151.045 121.156 107.294 1.00 73.45  ? 431  LEU A CA    1 
ATOM   3489  C C     . LEU B 2 434  ? 152.245 120.369 107.799 1.00 75.00  ? 431  LEU A C     1 
ATOM   3490  O O     . LEU B 2 434  ? 152.947 120.820 108.713 1.00 73.35  ? 431  LEU A O     1 
ATOM   3491  C CB    . LEU B 2 434  ? 149.766 120.669 107.978 1.00 69.31  ? 431  LEU A CB    1 
ATOM   3492  C CG    . LEU B 2 434  ? 149.747 120.717 109.508 1.00 66.05  ? 431  LEU A CG    1 
ATOM   3493  C CD1   . LEU B 2 434  ? 148.375 121.106 109.991 1.00 63.30  ? 431  LEU A CD1   1 
ATOM   3494  C CD2   . LEU B 2 434  ? 150.149 119.382 110.126 1.00 66.91  ? 431  LEU A CD2   1 
ATOM   3495  N N     . SER B 2 435  ? 152.489 119.191 107.223 1.00 77.08  ? 432  SER A N     1 
ATOM   3496  C CA    . SER B 2 435  ? 153.653 118.403 107.611 1.00 78.73  ? 432  SER A CA    1 
ATOM   3497  C C     . SER B 2 435  ? 154.941 119.181 107.379 1.00 80.79  ? 432  SER A C     1 
ATOM   3498  O O     . SER B 2 435  ? 155.846 119.161 108.222 1.00 83.35  ? 432  SER A O     1 
ATOM   3499  C CB    . SER B 2 435  ? 153.673 117.083 106.840 1.00 77.43  ? 432  SER A CB    1 
ATOM   3500  O OG    . SER B 2 435  ? 152.447 116.388 106.993 1.00 74.11  ? 432  SER A OG    1 
ATOM   3501  N N     . GLU B 2 436  ? 155.036 119.884 106.248 1.00 81.23  ? 433  GLU A N     1 
ATOM   3502  C CA    . GLU B 2 436  ? 156.209 120.715 105.993 1.00 83.87  ? 433  GLU A CA    1 
ATOM   3503  C C     . GLU B 2 436  ? 156.298 121.861 106.993 1.00 81.75  ? 433  GLU A C     1 
ATOM   3504  O O     . GLU B 2 436  ? 157.394 122.232 107.425 1.00 84.25  ? 433  GLU A O     1 
ATOM   3505  C CB    . GLU B 2 436  ? 156.175 121.250 104.562 1.00 87.14  ? 433  GLU A CB    1 
ATOM   3506  C CG    . GLU B 2 436  ? 156.307 120.178 103.492 1.00 92.14  ? 433  GLU A CG    1 
ATOM   3507  C CD    . GLU B 2 436  ? 157.535 119.308 103.689 1.00 98.50  ? 433  GLU A CD    1 
ATOM   3508  O OE1   . GLU B 2 436  ? 158.654 119.785 103.406 1.00 99.42  ? 433  GLU A OE1   1 
ATOM   3509  O OE2   . GLU B 2 436  ? 157.382 118.151 104.134 1.00 101.10 ? 433  GLU A OE2   1 
ATOM   3510  N N     . ALA B 2 437  ? 155.154 122.434 107.372 1.00 78.11  ? 434  ALA A N     1 
ATOM   3511  C CA    . ALA B 2 437  ? 155.153 123.466 108.405 1.00 73.42  ? 434  ALA A CA    1 
ATOM   3512  C C     . ALA B 2 437  ? 155.499 122.877 109.766 1.00 70.08  ? 434  ALA A C     1 
ATOM   3513  O O     . ALA B 2 437  ? 156.203 123.511 110.562 1.00 72.44  ? 434  ALA A O     1 
ATOM   3514  C CB    . ALA B 2 437  ? 153.796 124.167 108.449 1.00 68.60  ? 434  ALA A CB    1 
ATOM   3515  N N     . PHE B 2 438  ? 155.015 121.666 110.047 1.00 65.40  ? 435  PHE A N     1 
ATOM   3516  C CA    . PHE B 2 438  ? 155.334 121.015 111.315 1.00 64.44  ? 435  PHE A CA    1 
ATOM   3517  C C     . PHE B 2 438  ? 156.810 120.647 111.383 1.00 67.81  ? 435  PHE A C     1 
ATOM   3518  O O     . PHE B 2 438  ? 157.447 120.814 112.429 1.00 72.12  ? 435  PHE A O     1 
ATOM   3519  C CB    . PHE B 2 438  ? 154.458 119.775 111.500 1.00 66.88  ? 435  PHE A CB    1 
ATOM   3520  C CG    . PHE B 2 438  ? 154.367 119.301 112.925 1.00 70.76  ? 435  PHE A CG    1 
ATOM   3521  C CD1   . PHE B 2 438  ? 155.349 118.489 113.468 1.00 73.90  ? 435  PHE A CD1   1 
ATOM   3522  C CD2   . PHE B 2 438  ? 153.288 119.661 113.718 1.00 70.82  ? 435  PHE A CD2   1 
ATOM   3523  C CE1   . PHE B 2 438  ? 155.263 118.051 114.777 1.00 74.01  ? 435  PHE A CE1   1 
ATOM   3524  C CE2   . PHE B 2 438  ? 153.196 119.226 115.028 1.00 71.95  ? 435  PHE A CE2   1 
ATOM   3525  C CZ    . PHE B 2 438  ? 154.185 118.420 115.557 1.00 73.00  ? 435  PHE A CZ    1 
ATOM   3526  N N     . LYS B 2 439  ? 157.370 120.140 110.282 1.00 68.66  ? 436  LYS A N     1 
ATOM   3527  C CA    . LYS B 2 439  ? 158.790 119.801 110.257 1.00 71.97  ? 436  LYS A CA    1 
ATOM   3528  C C     . LYS B 2 439  ? 159.654 121.048 110.401 1.00 75.23  ? 436  LYS A C     1 
ATOM   3529  O O     . LYS B 2 439  ? 160.616 121.065 111.180 1.00 78.49  ? 436  LYS A O     1 
ATOM   3530  C CB    . LYS B 2 439  ? 159.136 119.063 108.965 1.00 74.40  ? 436  LYS A CB    1 
ATOM   3531  C CG    . LYS B 2 439  ? 158.541 117.671 108.834 1.00 75.85  ? 436  LYS A CG    1 
ATOM   3532  C CD    . LYS B 2 439  ? 158.867 117.078 107.471 1.00 77.22  ? 436  LYS A CD    1 
ATOM   3533  C CE    . LYS B 2 439  ? 158.137 115.767 107.241 1.00 77.04  ? 436  LYS A CE    1 
ATOM   3534  N NZ    . LYS B 2 439  ? 158.497 114.755 108.270 1.00 78.26  ? 436  LYS A NZ    1 
ATOM   3535  N N     . GLN B 2 440  ? 159.326 122.104 109.653 1.00 74.16  ? 437  GLN A N     1 
ATOM   3536  C CA    . GLN B 2 440  ? 160.146 123.311 109.673 1.00 73.05  ? 437  GLN A CA    1 
ATOM   3537  C C     . GLN B 2 440  ? 160.090 124.000 111.030 1.00 71.98  ? 437  GLN A C     1 
ATOM   3538  O O     . GLN B 2 440  ? 161.118 124.464 111.539 1.00 71.92  ? 437  GLN A O     1 
ATOM   3539  C CB    . GLN B 2 440  ? 159.701 124.267 108.566 1.00 70.87  ? 437  GLN A CB    1 
ATOM   3540  N N     . LYS B 2 441  ? 158.902 124.076 111.636 1.00 71.57  ? 438  LYS A N     1 
ATOM   3541  C CA    . LYS B 2 441  ? 158.782 124.730 112.936 1.00 73.43  ? 438  LYS A CA    1 
ATOM   3542  C C     . LYS B 2 441  ? 159.469 123.921 114.027 1.00 76.29  ? 438  LYS A C     1 
ATOM   3543  O O     . LYS B 2 441  ? 160.048 124.491 114.959 1.00 78.76  ? 438  LYS A O     1 
ATOM   3544  C CB    . LYS B 2 441  ? 157.309 124.944 113.284 1.00 72.83  ? 438  LYS A CB    1 
ATOM   3545  C CG    . LYS B 2 441  ? 157.068 125.915 114.432 1.00 72.88  ? 438  LYS A CG    1 
ATOM   3546  C CD    . LYS B 2 441  ? 157.050 127.356 113.940 1.00 73.60  ? 438  LYS A CD    1 
ATOM   3547  C CE    . LYS B 2 441  ? 156.888 128.342 115.087 1.00 75.06  ? 438  LYS A CE    1 
ATOM   3548  N NZ    . LYS B 2 441  ? 158.096 128.388 115.958 1.00 78.59  ? 438  LYS A NZ    1 
ATOM   3549  N N     . THR B 2 442  ? 159.416 122.590 113.930 1.00 78.54  ? 439  THR A N     1 
ATOM   3550  C CA    . THR B 2 442  ? 160.038 121.748 114.945 1.00 81.90  ? 439  THR A CA    1 
ATOM   3551  C C     . THR B 2 442  ? 161.557 121.876 114.912 1.00 85.48  ? 439  THR A C     1 
ATOM   3552  O O     . THR B 2 442  ? 162.196 122.061 115.952 1.00 86.85  ? 439  THR A O     1 
ATOM   3553  C CB    . THR B 2 442  ? 159.613 120.291 114.753 1.00 83.01  ? 439  THR A CB    1 
ATOM   3554  O OG1   . THR B 2 442  ? 158.190 120.187 114.882 1.00 82.75  ? 439  THR A OG1   1 
ATOM   3555  C CG2   . THR B 2 442  ? 160.277 119.405 115.790 1.00 84.91  ? 439  THR A CG2   1 
ATOM   3556  N N     . SER B 2 443  ? 162.153 121.779 113.721 1.00 86.01  ? 440  SER A N     1 
ATOM   3557  C CA    . SER B 2 443  ? 163.599 121.928 113.612 1.00 87.83  ? 440  SER A CA    1 
ATOM   3558  C C     . SER B 2 443  ? 164.039 123.349 113.941 1.00 85.40  ? 440  SER A C     1 
ATOM   3559  O O     . SER B 2 443  ? 165.136 123.546 114.475 1.00 87.95  ? 440  SER A O     1 
ATOM   3560  C CB    . SER B 2 443  ? 164.070 121.542 112.209 1.00 89.67  ? 440  SER A CB    1 
ATOM   3561  O OG    . SER B 2 443  ? 163.630 122.483 111.246 1.00 89.22  ? 440  SER A OG    1 
ATOM   3562  N N     . GLU B 2 444  ? 163.206 124.344 113.631 1.00 81.24  ? 441  GLU A N     1 
ATOM   3563  C CA    . GLU B 2 444  ? 163.541 125.727 113.951 1.00 80.45  ? 441  GLU A CA    1 
ATOM   3564  C C     . GLU B 2 444  ? 163.638 125.927 115.460 1.00 77.42  ? 441  GLU A C     1 
ATOM   3565  O O     . GLU B 2 444  ? 164.573 126.564 115.957 1.00 74.97  ? 441  GLU A O     1 
ATOM   3566  C CB    . GLU B 2 444  ? 162.498 126.670 113.349 1.00 83.37  ? 441  GLU A CB    1 
ATOM   3567  C CG    . GLU B 2 444  ? 162.859 128.144 113.412 1.00 89.14  ? 441  GLU A CG    1 
ATOM   3568  C CD    . GLU B 2 444  ? 161.709 129.038 112.986 1.00 91.57  ? 441  GLU A CD    1 
ATOM   3569  O OE1   . GLU B 2 444  ? 160.720 129.140 113.743 1.00 90.05  ? 441  GLU A OE1   1 
ATOM   3570  O OE2   . GLU B 2 444  ? 161.789 129.631 111.889 1.00 93.69  ? 441  GLU A OE2   1 
ATOM   3571  N N     . ILE B 2 445  ? 162.672 125.384 116.205 1.00 77.37  ? 442  ILE A N     1 
ATOM   3572  C CA    . ILE B 2 445  ? 162.702 125.496 117.659 1.00 77.48  ? 442  ILE A CA    1 
ATOM   3573  C C     . ILE B 2 445  ? 163.829 124.653 118.241 1.00 81.29  ? 442  ILE A C     1 
ATOM   3574  O O     . ILE B 2 445  ? 164.548 125.091 119.147 1.00 83.89  ? 442  ILE A O     1 
ATOM   3575  C CB    . ILE B 2 445  ? 161.335 125.103 118.249 1.00 71.65  ? 442  ILE A CB    1 
ATOM   3576  C CG1   . ILE B 2 445  ? 160.257 126.091 117.802 1.00 68.15  ? 442  ILE A CG1   1 
ATOM   3577  C CG2   . ILE B 2 445  ? 161.403 125.037 119.767 1.00 70.36  ? 442  ILE A CG2   1 
ATOM   3578  C CD1   . ILE B 2 445  ? 158.869 125.744 118.295 1.00 65.90  ? 442  ILE A CD1   1 
ATOM   3579  N N     . LEU B 2 446  ? 164.007 123.431 117.726 1.00 83.47  ? 443  LEU A N     1 
ATOM   3580  C CA    . LEU B 2 446  ? 165.046 122.548 118.248 1.00 85.31  ? 443  LEU A CA    1 
ATOM   3581  C C     . LEU B 2 446  ? 166.439 123.102 117.973 1.00 86.32  ? 443  LEU A C     1 
ATOM   3582  O O     . LEU B 2 446  ? 167.341 122.962 118.807 1.00 86.56  ? 443  LEU A O     1 
ATOM   3583  C CB    . LEU B 2 446  ? 164.896 121.150 117.648 1.00 86.70  ? 443  LEU A CB    1 
ATOM   3584  C CG    . LEU B 2 446  ? 163.742 120.301 118.189 1.00 87.22  ? 443  LEU A CG    1 
ATOM   3585  C CD1   . LEU B 2 446  ? 163.614 119.002 117.409 1.00 88.01  ? 443  LEU A CD1   1 
ATOM   3586  C CD2   . LEU B 2 446  ? 163.936 120.024 119.671 1.00 88.52  ? 443  LEU A CD2   1 
ATOM   3587  N N     . SER B 2 447  ? 166.637 123.733 116.813 1.00 88.14  ? 444  SER A N     1 
ATOM   3588  C CA    . SER B 2 447  ? 167.943 124.308 116.507 1.00 91.13  ? 444  SER A CA    1 
ATOM   3589  C C     . SER B 2 447  ? 168.249 125.496 117.409 1.00 90.72  ? 444  SER A C     1 
ATOM   3590  O O     . SER B 2 447  ? 169.390 125.664 117.857 1.00 92.77  ? 444  SER A O     1 
ATOM   3591  C CB    . SER B 2 447  ? 168.010 124.720 115.036 1.00 93.47  ? 444  SER A CB    1 
ATOM   3592  O OG    . SER B 2 447  ? 167.039 125.709 114.738 1.00 94.40  ? 444  SER A OG    1 
ATOM   3593  N N     . HIS B 2 448  ? 167.245 126.330 117.692 1.00 87.50  ? 445  HIS A N     1 
ATOM   3594  C CA    . HIS B 2 448  ? 167.462 127.472 118.575 1.00 87.46  ? 445  HIS A CA    1 
ATOM   3595  C C     . HIS B 2 448  ? 167.774 127.022 119.998 1.00 89.75  ? 445  HIS A C     1 
ATOM   3596  O O     . HIS B 2 448  ? 168.634 127.607 120.664 1.00 85.95  ? 445  HIS A O     1 
ATOM   3597  C CB    . HIS B 2 448  ? 166.241 128.391 118.558 1.00 85.74  ? 445  HIS A CB    1 
ATOM   3598  C CG    . HIS B 2 448  ? 166.172 129.277 117.353 1.00 85.36  ? 445  HIS A CG    1 
ATOM   3599  N ND1   . HIS B 2 448  ? 164.994 129.534 116.684 1.00 83.08  ? 445  HIS A ND1   1 
ATOM   3600  C CD2   . HIS B 2 448  ? 167.134 129.974 116.702 1.00 86.80  ? 445  HIS A CD2   1 
ATOM   3601  C CE1   . HIS B 2 448  ? 165.236 130.346 115.670 1.00 82.91  ? 445  HIS A CE1   1 
ATOM   3602  N NE2   . HIS B 2 448  ? 166.526 130.627 115.660 1.00 85.21  ? 445  HIS A NE2   1 
ATOM   3603  N N     . ALA B 2 449  ? 167.085 125.985 120.481 1.00 100.67 ? 446  ALA A N     1 
ATOM   3604  C CA    . ALA B 2 449  ? 167.400 125.447 121.800 1.00 107.66 ? 446  ALA A CA    1 
ATOM   3605  C C     . ALA B 2 449  ? 168.751 124.745 121.793 1.00 112.85 ? 446  ALA A C     1 
ATOM   3606  O O     . ALA B 2 449  ? 169.494 124.805 122.782 1.00 115.14 ? 446  ALA A O     1 
ATOM   3607  C CB    . ALA B 2 449  ? 166.297 124.496 122.259 1.00 102.88 ? 446  ALA A CB    1 
ATOM   3608  N N     . HIS B 2 450  ? 169.088 124.072 120.691 1.00 115.10 ? 447  HIS A N     1 
ATOM   3609  C CA    . HIS B 2 450  ? 170.401 123.447 120.577 1.00 118.19 ? 447  HIS A CA    1 
ATOM   3610  C C     . HIS B 2 450  ? 171.499 124.496 120.458 1.00 118.55 ? 447  HIS A C     1 
ATOM   3611  O O     . HIS B 2 450  ? 172.588 124.328 121.019 1.00 121.24 ? 447  HIS A O     1 
ATOM   3612  C CB    . HIS B 2 450  ? 170.425 122.497 119.380 1.00 121.14 ? 447  HIS A CB    1 
ATOM   3613  C CG    . HIS B 2 450  ? 171.796 122.227 118.846 1.00 128.20 ? 447  HIS A CG    1 
ATOM   3614  N ND1   . HIS B 2 450  ? 172.815 121.724 119.626 1.00 133.27 ? 447  HIS A ND1   1 
ATOM   3615  C CD2   . HIS B 2 450  ? 172.316 122.389 117.606 1.00 130.97 ? 447  HIS A CD2   1 
ATOM   3616  C CE1   . HIS B 2 450  ? 173.904 121.590 118.891 1.00 136.11 ? 447  HIS A CE1   1 
ATOM   3617  N NE2   . HIS B 2 450  ? 173.628 121.986 117.661 1.00 135.00 ? 447  HIS A NE2   1 
ATOM   3618  N N     . ALA B 2 451  ? 171.233 125.586 119.736 1.00 114.33 ? 448  ALA A N     1 
ATOM   3619  C CA    . ALA B 2 451  ? 172.207 126.663 119.599 1.00 111.04 ? 448  ALA A CA    1 
ATOM   3620  C C     . ALA B 2 451  ? 172.312 127.532 120.844 1.00 106.42 ? 448  ALA A C     1 
ATOM   3621  O O     . ALA B 2 451  ? 173.236 128.347 120.935 1.00 109.27 ? 448  ALA A O     1 
ATOM   3622  C CB    . ALA B 2 451  ? 171.862 127.542 118.394 1.00 106.97 ? 448  ALA A CB    1 
ATOM   3623  N N     . ALA B 2 452  ? 171.395 127.381 121.799 1.00 100.07 ? 449  ALA A N     1 
ATOM   3624  C CA    . ALA B 2 452  ? 171.434 128.152 123.033 1.00 97.80  ? 449  ALA A CA    1 
ATOM   3625  C C     . ALA B 2 452  ? 172.068 127.400 124.194 1.00 99.67  ? 449  ALA A C     1 
ATOM   3626  O O     . ALA B 2 452  ? 172.629 128.036 125.090 1.00 99.07  ? 449  ALA A O     1 
ATOM   3627  C CB    . ALA B 2 452  ? 170.020 128.590 123.435 1.00 95.05  ? 449  ALA A CB    1 
ATOM   3628  N N     . LEU B 2 453  ? 171.996 126.066 124.200 1.00 102.48 ? 450  LEU A N     1 
ATOM   3629  C CA    . LEU B 2 453  ? 172.585 125.303 125.295 1.00 105.44 ? 450  LEU A CA    1 
ATOM   3630  C C     . LEU B 2 453  ? 174.106 125.339 125.263 1.00 113.03 ? 450  LEU A C     1 
ATOM   3631  O O     . LEU B 2 453  ? 174.747 125.275 126.317 1.00 115.75 ? 450  LEU A O     1 
ATOM   3632  C CB    . LEU B 2 453  ? 172.092 123.856 125.262 1.00 102.11 ? 450  LEU A CB    1 
ATOM   3633  C CG    . LEU B 2 453  ? 170.717 123.592 125.874 1.00 96.49  ? 450  LEU A CG    1 
ATOM   3634  C CD1   . LEU B 2 453  ? 170.431 122.102 125.916 1.00 95.71  ? 450  LEU A CD1   1 
ATOM   3635  C CD2   . LEU B 2 453  ? 170.632 124.191 127.266 1.00 95.06  ? 450  LEU A CD2   1 
ATOM   3636  N N     . ASP B 2 454  ? 174.701 125.430 124.075 1.00 121.03 ? 451  ASP A N     1 
ATOM   3637  C CA    . ASP B 2 454  ? 176.151 125.510 123.965 1.00 126.47 ? 451  ASP A CA    1 
ATOM   3638  C C     . ASP B 2 454  ? 176.670 126.942 123.994 1.00 127.80 ? 451  ASP A C     1 
ATOM   3639  O O     . ASP B 2 454  ? 177.866 127.146 124.227 1.00 131.43 ? 451  ASP A O     1 
ATOM   3640  C CB    . ASP B 2 454  ? 176.623 124.814 122.683 1.00 128.65 ? 451  ASP A CB    1 
ATOM   3641  C CG    . ASP B 2 454  ? 175.916 125.324 121.446 1.00 129.79 ? 451  ASP A CG    1 
ATOM   3642  O OD1   . ASP B 2 454  ? 174.861 125.978 121.589 1.00 130.11 ? 451  ASP A OD1   1 
ATOM   3643  O OD2   . ASP B 2 454  ? 176.409 125.066 120.326 1.00 131.16 ? 451  ASP A OD2   1 
ATOM   3644  N N     . GLN B 2 455  ? 175.807 127.924 123.770 1.00 119.27 ? 452  GLN A N     1 
ATOM   3645  C CA    . GLN B 2 455  ? 176.214 129.323 123.857 1.00 117.23 ? 452  GLN A CA    1 
ATOM   3646  C C     . GLN B 2 455  ? 176.400 129.707 125.319 1.00 117.40 ? 452  GLN A C     1 
ATOM   3647  O O     . GLN B 2 455  ? 175.448 129.599 126.104 1.00 115.47 ? 452  GLN A O     1 
ATOM   3648  C CB    . GLN B 2 455  ? 175.172 130.221 123.198 1.00 113.66 ? 452  GLN A CB    1 
ATOM   3649  C CG    . GLN B 2 455  ? 175.560 131.691 123.141 1.00 114.16 ? 452  GLN A CG    1 
ATOM   3650  C CD    . GLN B 2 455  ? 174.406 132.583 122.724 1.00 111.69 ? 452  GLN A CD    1 
ATOM   3651  O OE1   . GLN B 2 455  ? 173.265 132.380 123.144 1.00 109.11 ? 452  GLN A OE1   1 
ATOM   3652  N NE2   . GLN B 2 455  ? 174.694 133.576 121.891 1.00 112.62 ? 452  GLN A NE2   1 
ATOM   3653  N N     . PRO B 2 456  ? 177.583 130.154 125.732 1.00 119.43 ? 453  PRO A N     1 
ATOM   3654  C CA    . PRO B 2 456  ? 177.807 130.458 127.146 1.00 120.27 ? 453  PRO A CA    1 
ATOM   3655  C C     . PRO B 2 456  ? 177.177 131.776 127.565 1.00 117.33 ? 453  PRO A C     1 
ATOM   3656  O O     . PRO B 2 456  ? 177.079 132.729 126.789 1.00 117.36 ? 453  PRO A O     1 
ATOM   3657  C CB    . PRO B 2 456  ? 179.335 130.521 127.250 1.00 123.73 ? 453  PRO A CB    1 
ATOM   3658  C CG    . PRO B 2 456  ? 179.767 130.969 125.895 1.00 123.50 ? 453  PRO A CG    1 
ATOM   3659  C CD    . PRO B 2 456  ? 178.800 130.344 124.922 1.00 120.99 ? 453  PRO A CD    1 
ATOM   3660  N N     . LEU B 2 457  ? 176.748 131.818 128.826 1.00 114.91 ? 454  LEU A N     1 
ATOM   3661  C CA    . LEU B 2 457  ? 176.199 133.034 129.397 1.00 113.11 ? 454  LEU A CA    1 
ATOM   3662  C C     . LEU B 2 457  ? 177.307 134.059 129.626 1.00 115.46 ? 454  LEU A C     1 
ATOM   3663  O O     . LEU B 2 457  ? 178.483 133.704 129.735 1.00 118.75 ? 454  LEU A O     1 
ATOM   3664  C CB    . LEU B 2 457  ? 175.483 132.731 130.713 1.00 114.30 ? 454  LEU A CB    1 
ATOM   3665  C CG    . LEU B 2 457  ? 174.030 132.261 130.643 1.00 113.38 ? 454  LEU A CG    1 
ATOM   3666  C CD1   . LEU B 2 457  ? 173.232 133.107 129.658 1.00 110.47 ? 454  LEU A CD1   1 
ATOM   3667  C CD2   . LEU B 2 457  ? 173.944 130.788 130.295 1.00 115.64 ? 454  LEU A CD2   1 
ATOM   3668  N N     . PRO B 2 458  ? 176.956 135.352 129.702 1.00 114.32 ? 455  PRO A N     1 
ATOM   3669  C CA    . PRO B 2 458  ? 177.977 136.371 129.975 1.00 116.61 ? 455  PRO A CA    1 
ATOM   3670  C C     . PRO B 2 458  ? 178.455 136.335 131.418 1.00 118.12 ? 455  PRO A C     1 
ATOM   3671  O O     . PRO B 2 458  ? 177.982 135.522 132.217 1.00 119.72 ? 455  PRO A O     1 
ATOM   3672  C CB    . PRO B 2 458  ? 177.254 137.683 129.654 1.00 112.98 ? 455  PRO A CB    1 
ATOM   3673  C CG    . PRO B 2 458  ? 175.822 137.381 129.917 1.00 108.76 ? 455  PRO A CG    1 
ATOM   3674  C CD    . PRO B 2 458  ? 175.627 135.952 129.487 1.00 109.94 ? 455  PRO A CD    1 
ATOM   3675  N N     . THR B 2 459  ? 179.391 137.219 131.762 1.00 118.19 ? 456  THR A N     1 
ATOM   3676  C CA    . THR B 2 459  ? 179.925 137.239 133.120 1.00 119.56 ? 456  THR A CA    1 
ATOM   3677  C C     . THR B 2 459  ? 179.018 138.012 134.070 1.00 117.71 ? 456  THR A C     1 
ATOM   3678  O O     . THR B 2 459  ? 178.840 137.608 135.226 1.00 117.84 ? 456  THR A O     1 
ATOM   3679  C CB    . THR B 2 459  ? 181.332 137.836 133.122 1.00 123.08 ? 456  THR A CB    1 
ATOM   3680  O OG1   . THR B 2 459  ? 181.301 139.146 132.542 1.00 122.90 ? 456  THR A OG1   1 
ATOM   3681  C CG2   . THR B 2 459  ? 182.285 136.955 132.325 1.00 125.17 ? 456  THR A CG2   1 
ATOM   3682  N N     . THR B 2 460  ? 178.437 139.120 133.611 1.00 116.18 ? 457  THR A N     1 
ATOM   3683  C CA    . THR B 2 460  ? 177.563 139.941 134.434 1.00 114.36 ? 457  THR A CA    1 
ATOM   3684  C C     . THR B 2 460  ? 176.368 140.398 133.606 1.00 111.03 ? 457  THR A C     1 
ATOM   3685  O O     . THR B 2 460  ? 176.321 140.224 132.386 1.00 108.59 ? 457  THR A O     1 
ATOM   3686  C CB    . THR B 2 460  ? 178.298 141.161 135.008 1.00 115.73 ? 457  THR A CB    1 
ATOM   3687  O OG1   . THR B 2 460  ? 179.016 141.828 133.961 1.00 117.12 ? 457  THR A OG1   1 
ATOM   3688  C CG2   . THR B 2 460  ? 179.267 140.745 136.106 1.00 119.14 ? 457  THR A CG2   1 
ATOM   3689  N N     . LEU B 2 461  ? 175.390 140.988 134.296 1.00 109.57 ? 458  LEU A N     1 
ATOM   3690  C CA    . LEU B 2 461  ? 174.224 141.595 133.669 1.00 104.67 ? 458  LEU A CA    1 
ATOM   3691  C C     . LEU B 2 461  ? 174.314 143.118 133.649 1.00 104.08 ? 458  LEU A C     1 
ATOM   3692  O O     . LEU B 2 461  ? 173.286 143.803 133.646 1.00 102.62 ? 458  LEU A O     1 
ATOM   3693  C CB    . LEU B 2 461  ? 172.946 141.151 134.381 1.00 100.50 ? 458  LEU A CB    1 
ATOM   3694  C CG    . LEU B 2 461  ? 172.143 139.990 133.791 1.00 97.36  ? 458  LEU A CG    1 
ATOM   3695  C CD1   . LEU B 2 461  ? 173.022 138.772 133.558 1.00 99.18  ? 458  LEU A CD1   1 
ATOM   3696  C CD2   . LEU B 2 461  ? 170.979 139.644 134.704 1.00 94.91  ? 458  LEU A CD2   1 
ATOM   3697  N N     . LYS B 2 462  ? 175.534 143.662 133.639 1.00 107.06 ? 459  LYS A N     1 
ATOM   3698  C CA    . LYS B 2 462  ? 175.706 145.108 133.706 1.00 106.37 ? 459  LYS A CA    1 
ATOM   3699  C C     . LYS B 2 462  ? 175.251 145.779 132.414 1.00 104.15 ? 459  LYS A C     1 
ATOM   3700  O O     . LYS B 2 462  ? 174.528 146.782 132.444 1.00 100.03 ? 459  LYS A O     1 
ATOM   3701  C CB    . LYS B 2 462  ? 177.165 145.448 134.008 1.00 110.59 ? 459  LYS A CB    1 
ATOM   3702  N N     . LYS B 2 463  ? 175.665 145.242 131.271 1.00 106.81 ? 460  LYS A N     1 
ATOM   3703  C CA    . LYS B 2 463  ? 175.314 145.818 129.982 1.00 106.37 ? 460  LYS A CA    1 
ATOM   3704  C C     . LYS B 2 463  ? 174.007 145.227 129.466 1.00 103.79 ? 460  LYS A C     1 
ATOM   3705  O O     . LYS B 2 463  ? 173.646 144.090 129.785 1.00 105.94 ? 460  LYS A O     1 
ATOM   3706  C CB    . LYS B 2 463  ? 176.429 145.582 128.963 1.00 107.92 ? 460  LYS A CB    1 
ATOM   3707  N N     . GLN B 2 464  ? 173.293 146.020 128.662 1.00 99.44  ? 461  GLN A N     1 
ATOM   3708  C CA    . GLN B 2 464  ? 172.053 145.540 128.062 1.00 94.74  ? 461  GLN A CA    1 
ATOM   3709  C C     . GLN B 2 464  ? 172.318 144.455 127.026 1.00 94.89  ? 461  GLN A C     1 
ATOM   3710  O O     . GLN B 2 464  ? 171.484 143.562 126.840 1.00 91.32  ? 461  GLN A O     1 
ATOM   3711  C CB    . GLN B 2 464  ? 171.288 146.703 127.428 1.00 94.02  ? 461  GLN A CB    1 
ATOM   3712  C CG    . GLN B 2 464  ? 169.921 146.328 126.874 1.00 93.35  ? 461  GLN A CG    1 
ATOM   3713  C CD    . GLN B 2 464  ? 168.927 145.963 127.961 1.00 93.30  ? 461  GLN A CD    1 
ATOM   3714  O OE1   . GLN B 2 464  ? 168.885 146.594 129.018 1.00 93.98  ? 461  GLN A OE1   1 
ATOM   3715  N NE2   . GLN B 2 464  ? 168.119 144.939 127.706 1.00 91.14  ? 461  GLN A NE2   1 
ATOM   3716  N N     . GLU B 2 465  ? 173.469 144.513 126.349 1.00 100.41 ? 462  GLU A N     1 
ATOM   3717  C CA    . GLU B 2 465  ? 173.822 143.462 125.401 1.00 99.85  ? 462  GLU A CA    1 
ATOM   3718  C C     . GLU B 2 465  ? 173.996 142.119 126.098 1.00 98.56  ? 462  GLU A C     1 
ATOM   3719  O O     . GLU B 2 465  ? 173.791 141.068 125.481 1.00 99.86  ? 462  GLU A O     1 
ATOM   3720  C CB    . GLU B 2 465  ? 175.099 143.840 124.649 1.00 99.10  ? 462  GLU A CB    1 
ATOM   3721  N N     . GLU B 2 466  ? 174.368 142.135 127.379 1.00 95.50  ? 463  GLU A N     1 
ATOM   3722  C CA    . GLU B 2 466  ? 174.463 140.902 128.151 1.00 98.40  ? 463  GLU A CA    1 
ATOM   3723  C C     . GLU B 2 466  ? 173.108 140.467 128.694 1.00 97.71  ? 463  GLU A C     1 
ATOM   3724  O O     . GLU B 2 466  ? 172.892 139.270 128.923 1.00 94.71  ? 463  GLU A O     1 
ATOM   3725  C CB    . GLU B 2 466  ? 175.469 141.074 129.291 1.00 103.30 ? 463  GLU A CB    1 
ATOM   3726  C CG    . GLU B 2 466  ? 176.907 141.248 128.819 1.00 108.98 ? 463  GLU A CG    1 
ATOM   3727  C CD    . GLU B 2 466  ? 177.858 141.608 129.946 1.00 112.74 ? 463  GLU A CD    1 
ATOM   3728  O OE1   . GLU B 2 466  ? 177.449 142.361 130.853 1.00 111.64 ? 463  GLU A OE1   1 
ATOM   3729  O OE2   . GLU B 2 466  ? 179.015 141.136 129.921 1.00 115.84 ? 463  GLU A OE2   1 
ATOM   3730  N N     . LYS B 2 467  ? 172.190 141.411 128.912 1.00 100.66 ? 464  LYS A N     1 
ATOM   3731  C CA    . LYS B 2 467  ? 170.826 141.041 129.275 1.00 99.79  ? 464  LYS A CA    1 
ATOM   3732  C C     . LYS B 2 467  ? 170.090 140.415 128.099 1.00 99.19  ? 464  LYS A C     1 
ATOM   3733  O O     . LYS B 2 467  ? 169.236 139.543 128.297 1.00 96.31  ? 464  LYS A O     1 
ATOM   3734  C CB    . LYS B 2 467  ? 170.055 142.264 129.776 1.00 96.47  ? 464  LYS A CB    1 
ATOM   3735  C CG    . LYS B 2 467  ? 170.563 142.856 131.080 1.00 96.26  ? 464  LYS A CG    1 
ATOM   3736  C CD    . LYS B 2 467  ? 169.657 143.988 131.547 1.00 92.50  ? 464  LYS A CD    1 
ATOM   3737  C CE    . LYS B 2 467  ? 170.147 144.600 132.849 1.00 93.21  ? 464  LYS A CE    1 
ATOM   3738  N NZ    . LYS B 2 467  ? 169.237 145.677 133.330 1.00 91.33  ? 464  LYS A NZ    1 
ATOM   3739  N N     . GLU B 2 468  ? 170.409 140.841 126.875 1.00 104.32 ? 465  GLU A N     1 
ATOM   3740  C CA    . GLU B 2 468  ? 169.686 140.355 125.705 1.00 104.58 ? 465  GLU A CA    1 
ATOM   3741  C C     . GLU B 2 468  ? 169.969 138.881 125.445 1.00 102.27 ? 465  GLU A C     1 
ATOM   3742  O O     . GLU B 2 468  ? 169.051 138.117 125.120 1.00 100.21 ? 465  GLU A O     1 
ATOM   3743  C CB    . GLU B 2 468  ? 170.055 141.194 124.482 1.00 109.72 ? 465  GLU A CB    1 
ATOM   3744  C CG    . GLU B 2 468  ? 169.290 140.827 123.224 1.00 112.31 ? 465  GLU A CG    1 
ATOM   3745  C CD    . GLU B 2 468  ? 169.751 141.620 122.018 1.00 116.62 ? 465  GLU A CD    1 
ATOM   3746  O OE1   . GLU B 2 468  ? 170.849 142.210 122.079 1.00 119.43 ? 465  GLU A OE1   1 
ATOM   3747  O OE2   . GLU B 2 468  ? 169.012 141.655 121.012 1.00 116.64 ? 465  GLU A OE2   1 
ATOM   3748  N N     . ILE B 2 469  ? 171.229 138.460 125.582 1.00 100.52 ? 466  ILE A N     1 
ATOM   3749  C CA    . ILE B 2 469  ? 171.566 137.068 125.305 1.00 98.57  ? 466  ILE A CA    1 
ATOM   3750  C C     . ILE B 2 469  ? 170.992 136.145 126.373 1.00 93.64  ? 466  ILE A C     1 
ATOM   3751  O O     . ILE B 2 469  ? 170.690 134.978 126.094 1.00 92.53  ? 466  ILE A O     1 
ATOM   3752  C CB    . ILE B 2 469  ? 173.090 136.897 125.167 1.00 103.21 ? 466  ILE A CB    1 
ATOM   3753  C CG1   . ILE B 2 469  ? 173.817 137.503 126.369 1.00 105.63 ? 466  ILE A CG1   1 
ATOM   3754  C CG2   . ILE B 2 469  ? 173.580 137.529 123.871 1.00 104.37 ? 466  ILE A CG2   1 
ATOM   3755  C CD1   . ILE B 2 469  ? 175.324 137.488 126.235 1.00 109.15 ? 466  ILE A CD1   1 
ATOM   3756  N N     . LEU B 2 470  ? 170.825 136.640 127.602 1.00 89.71  ? 467  LEU A N     1 
ATOM   3757  C CA    . LEU B 2 470  ? 170.148 135.841 128.620 1.00 86.53  ? 467  LEU A CA    1 
ATOM   3758  C C     . LEU B 2 470  ? 168.679 135.643 128.270 1.00 79.99  ? 467  LEU A C     1 
ATOM   3759  O O     . LEU B 2 470  ? 168.140 134.541 128.424 1.00 78.87  ? 467  LEU A O     1 
ATOM   3760  C CB    . LEU B 2 470  ? 170.291 136.498 129.993 1.00 87.22  ? 467  LEU A CB    1 
ATOM   3761  C CG    . LEU B 2 470  ? 169.517 135.825 131.133 1.00 86.75  ? 467  LEU A CG    1 
ATOM   3762  C CD1   . LEU B 2 470  ? 169.974 134.386 131.322 1.00 65.94  ? 467  LEU A CD1   1 
ATOM   3763  C CD2   . LEU B 2 470  ? 169.653 136.610 132.429 1.00 64.76  ? 467  LEU A CD2   1 
ATOM   3764  N N     . LYS B 2 471  ? 168.017 136.700 127.791 1.00 74.89  ? 468  LYS A N     1 
ATOM   3765  C CA    . LYS B 2 471  ? 166.629 136.566 127.359 1.00 70.96  ? 468  LYS A CA    1 
ATOM   3766  C C     . LYS B 2 471  ? 166.526 135.699 126.110 1.00 67.59  ? 468  LYS A C     1 
ATOM   3767  O O     . LYS B 2 471  ? 165.583 134.909 125.971 1.00 65.01  ? 468  LYS A O     1 
ATOM   3768  C CB    . LYS B 2 471  ? 166.020 137.943 127.102 1.00 73.91  ? 468  LYS A CB    1 
ATOM   3769  C CG    . LYS B 2 471  ? 164.571 137.897 126.640 1.00 75.39  ? 468  LYS A CG    1 
ATOM   3770  C CD    . LYS B 2 471  ? 164.196 139.137 125.844 1.00 75.19  ? 468  LYS A CD    1 
ATOM   3771  C CE    . LYS B 2 471  ? 162.852 138.956 125.155 1.00 72.68  ? 468  LYS A CE    1 
ATOM   3772  N NZ    . LYS B 2 471  ? 162.584 140.027 124.156 1.00 71.46  ? 468  LYS A NZ    1 
ATOM   3773  N N     . SER B 2 472  ? 167.489 135.826 125.193 1.00 68.41  ? 469  SER A N     1 
ATOM   3774  C CA    . SER B 2 472  ? 167.444 135.058 123.952 1.00 67.77  ? 469  SER A CA    1 
ATOM   3775  C C     . SER B 2 472  ? 167.521 133.563 124.222 1.00 66.87  ? 469  SER A C     1 
ATOM   3776  O O     . SER B 2 472  ? 166.803 132.773 123.596 1.00 66.10  ? 469  SER A O     1 
ATOM   3777  C CB    . SER B 2 472  ? 168.577 135.496 123.026 1.00 69.74  ? 469  SER A CB    1 
ATOM   3778  O OG    . SER B 2 472  ? 168.576 134.746 121.824 1.00 69.95  ? 469  SER A OG    1 
ATOM   3779  N N     . GLN B 2 473  ? 168.387 133.151 125.151 1.00 68.20  ? 470  GLN A N     1 
ATOM   3780  C CA    . GLN B 2 473  ? 168.488 131.733 125.481 1.00 70.57  ? 470  GLN A CA    1 
ATOM   3781  C C     . GLN B 2 473  ? 167.260 131.246 126.241 1.00 72.83  ? 470  GLN A C     1 
ATOM   3782  O O     . GLN B 2 473  ? 166.851 130.091 126.076 1.00 72.14  ? 470  GLN A O     1 
ATOM   3783  C CB    . GLN B 2 473  ? 169.755 131.473 126.294 1.00 74.11  ? 470  GLN A CB    1 
ATOM   3784  C CG    . GLN B 2 473  ? 171.038 131.815 125.555 1.00 76.56  ? 470  GLN A CG    1 
ATOM   3785  C CD    . GLN B 2 473  ? 172.274 131.616 126.410 1.00 77.40  ? 470  GLN A CD    1 
ATOM   3786  O OE1   . GLN B 2 473  ? 172.240 130.903 127.410 1.00 75.67  ? 470  GLN A OE1   1 
ATOM   3787  N NE2   . GLN B 2 473  ? 173.371 132.253 126.019 1.00 79.94  ? 470  GLN A NE2   1 
ATOM   3788  N N     . LEU B 2 474  ? 166.663 132.104 127.071 1.00 75.55  ? 471  LEU A N     1 
ATOM   3789  C CA    . LEU B 2 474  ? 165.434 131.727 127.760 1.00 77.12  ? 471  LEU A CA    1 
ATOM   3790  C C     . LEU B 2 474  ? 164.261 131.614 126.796 1.00 71.75  ? 471  LEU A C     1 
ATOM   3791  O O     . LEU B 2 474  ? 163.377 130.774 126.995 1.00 71.07  ? 471  LEU A O     1 
ATOM   3792  C CB    . LEU B 2 474  ? 165.120 132.734 128.868 1.00 80.44  ? 471  LEU A CB    1 
ATOM   3793  C CG    . LEU B 2 474  ? 165.993 132.654 130.120 1.00 58.88  ? 471  LEU A CG    1 
ATOM   3794  C CD1   . LEU B 2 474  ? 165.706 133.823 131.043 1.00 60.52  ? 471  LEU A CD1   1 
ATOM   3795  C CD2   . LEU B 2 474  ? 165.760 131.338 130.840 1.00 59.54  ? 471  LEU A CD2   1 
ATOM   3796  N N     . ASP B 2 475  ? 164.232 132.449 125.754 1.00 68.64  ? 472  ASP A N     1 
ATOM   3797  C CA    . ASP B 2 475  ? 163.183 132.331 124.744 1.00 66.28  ? 472  ASP A CA    1 
ATOM   3798  C C     . ASP B 2 475  ? 163.284 131.004 124.004 1.00 66.04  ? 472  ASP A C     1 
ATOM   3799  O O     . ASP B 2 475  ? 162.265 130.380 123.687 1.00 64.97  ? 472  ASP A O     1 
ATOM   3800  C CB    . ASP B 2 475  ? 163.260 133.501 123.761 1.00 68.60  ? 472  ASP A CB    1 
ATOM   3801  C CG    . ASP B 2 475  ? 162.980 134.838 124.420 1.00 73.49  ? 472  ASP A CG    1 
ATOM   3802  O OD1   . ASP B 2 475  ? 162.244 134.870 125.429 1.00 74.30  ? 472  ASP A OD1   1 
ATOM   3803  O OD2   . ASP B 2 475  ? 163.499 135.863 123.926 1.00 76.76  ? 472  ASP A OD2   1 
ATOM   3804  N N     . SER B 2 476  ? 164.510 130.557 123.720 1.00 67.57  ? 473  SER A N     1 
ATOM   3805  C CA    . SER B 2 476  ? 164.693 129.264 123.068 1.00 67.93  ? 473  SER A CA    1 
ATOM   3806  C C     . SER B 2 476  ? 164.284 128.122 123.988 1.00 66.79  ? 473  SER A C     1 
ATOM   3807  O O     . SER B 2 476  ? 163.705 127.128 123.536 1.00 65.37  ? 473  SER A O     1 
ATOM   3808  C CB    . SER B 2 476  ? 166.144 129.106 122.620 1.00 68.89  ? 473  SER A CB    1 
ATOM   3809  O OG    . SER B 2 476  ? 166.546 130.194 121.806 1.00 68.08  ? 473  SER A OG    1 
ATOM   3810  N N     . LEU B 2 477  ? 164.577 128.246 125.285 1.00 67.29  ? 474  LEU A N     1 
ATOM   3811  C CA    . LEU B 2 477  ? 164.165 127.222 126.238 1.00 68.69  ? 474  LEU A CA    1 
ATOM   3812  C C     . LEU B 2 477  ? 162.652 127.213 126.419 1.00 65.97  ? 474  LEU A C     1 
ATOM   3813  O O     . LEU B 2 477  ? 162.037 126.143 126.503 1.00 66.56  ? 474  LEU A O     1 
ATOM   3814  C CB    . LEU B 2 477  ? 164.862 127.437 127.581 1.00 73.32  ? 474  LEU A CB    1 
ATOM   3815  C CG    . LEU B 2 477  ? 166.138 126.630 127.828 1.00 77.31  ? 474  LEU A CG    1 
ATOM   3816  C CD1   . LEU B 2 477  ? 165.818 125.146 127.859 1.00 79.38  ? 474  LEU A CD1   1 
ATOM   3817  C CD2   . LEU B 2 477  ? 167.189 126.927 126.771 1.00 77.75  ? 474  LEU A CD2   1 
ATOM   3818  N N     . LEU B 2 478  ? 162.032 128.396 126.486 1.00 64.71  ? 475  LEU A N     1 
ATOM   3819  C CA    . LEU B 2 478  ? 160.580 128.456 126.593 1.00 62.41  ? 475  LEU A CA    1 
ATOM   3820  C C     . LEU B 2 478  ? 159.910 128.036 125.292 1.00 62.51  ? 475  LEU A C     1 
ATOM   3821  O O     . LEU B 2 478  ? 158.784 127.524 125.312 1.00 62.11  ? 475  LEU A O     1 
ATOM   3822  C CB    . LEU B 2 478  ? 160.137 129.865 126.994 1.00 59.61  ? 475  LEU A CB    1 
ATOM   3823  C CG    . LEU B 2 478  ? 158.681 130.012 127.443 1.00 56.12  ? 475  LEU A CG    1 
ATOM   3824  C CD1   . LEU B 2 478  ? 158.428 129.199 128.702 1.00 57.41  ? 475  LEU A CD1   1 
ATOM   3825  C CD2   . LEU B 2 478  ? 158.319 131.473 127.661 1.00 53.35  ? 475  LEU A CD2   1 
ATOM   3826  N N     . GLY B 2 479  ? 160.579 128.245 124.155 1.00 62.12  ? 476  GLY A N     1 
ATOM   3827  C CA    . GLY B 2 479  ? 160.022 127.799 122.890 1.00 61.59  ? 476  GLY A CA    1 
ATOM   3828  C C     . GLY B 2 479  ? 159.916 126.290 122.803 1.00 64.11  ? 476  GLY A C     1 
ATOM   3829  O O     . GLY B 2 479  ? 158.914 125.752 122.328 1.00 64.88  ? 476  GLY A O     1 
ATOM   3830  N N     . LEU B 2 480  ? 160.952 125.584 123.264 1.00 66.05  ? 477  LEU A N     1 
ATOM   3831  C CA    . LEU B 2 480  ? 160.882 124.127 123.319 1.00 65.05  ? 477  LEU A CA    1 
ATOM   3832  C C     . LEU B 2 480  ? 159.870 123.665 124.357 1.00 64.78  ? 477  LEU A C     1 
ATOM   3833  O O     . LEU B 2 480  ? 159.156 122.678 124.143 1.00 64.93  ? 477  LEU A O     1 
ATOM   3834  C CB    . LEU B 2 480  ? 162.265 123.548 123.615 1.00 64.07  ? 477  LEU A CB    1 
ATOM   3835  C CG    . LEU B 2 480  ? 162.341 122.029 123.767 1.00 63.64  ? 477  LEU A CG    1 
ATOM   3836  C CD1   . LEU B 2 480  ? 161.835 121.337 122.511 1.00 63.27  ? 477  LEU A CD1   1 
ATOM   3837  C CD2   . LEU B 2 480  ? 163.763 121.604 124.083 1.00 66.18  ? 477  LEU A CD2   1 
ATOM   3838  N N     . TYR B 2 481  ? 159.792 124.370 125.492 1.00 65.27  ? 478  TYR A N     1 
ATOM   3839  C CA    . TYR B 2 481  ? 158.788 124.043 126.500 1.00 66.19  ? 478  TYR A CA    1 
ATOM   3840  C C     . TYR B 2 481  ? 157.380 124.270 125.965 1.00 62.10  ? 478  TYR A C     1 
ATOM   3841  O O     . TYR B 2 481  ? 156.458 123.510 126.282 1.00 60.52  ? 478  TYR A O     1 
ATOM   3842  C CB    . TYR B 2 481  ? 159.028 124.872 127.763 1.00 72.60  ? 478  TYR A CB    1 
ATOM   3843  C CG    . TYR B 2 481  ? 157.934 124.750 128.803 1.00 79.32  ? 478  TYR A CG    1 
ATOM   3844  C CD1   . TYR B 2 481  ? 157.887 123.662 129.663 1.00 83.61  ? 478  TYR A CD1   1 
ATOM   3845  C CD2   . TYR B 2 481  ? 156.955 125.729 128.928 1.00 81.64  ? 478  TYR A CD2   1 
ATOM   3846  C CE1   . TYR B 2 481  ? 156.891 123.548 130.616 1.00 85.19  ? 478  TYR A CE1   1 
ATOM   3847  C CE2   . TYR B 2 481  ? 155.956 125.623 129.877 1.00 82.85  ? 478  TYR A CE2   1 
ATOM   3848  C CZ    . TYR B 2 481  ? 155.928 124.532 130.718 1.00 84.32  ? 478  TYR A CZ    1 
ATOM   3849  O OH    . TYR B 2 481  ? 154.935 124.424 131.665 1.00 84.24  ? 478  TYR A OH    1 
ATOM   3850  N N     . HIS B 2 482  ? 157.198 125.313 125.151 1.00 59.93  ? 479  HIS A N     1 
ATOM   3851  C CA    . HIS B 2 482  ? 155.902 125.541 124.519 1.00 57.10  ? 479  HIS A CA    1 
ATOM   3852  C C     . HIS B 2 482  ? 155.570 124.438 123.525 1.00 57.22  ? 479  HIS A C     1 
ATOM   3853  O O     . HIS B 2 482  ? 154.413 124.018 123.417 1.00 57.45  ? 479  HIS A O     1 
ATOM   3854  C CB    . HIS B 2 482  ? 155.889 126.902 123.825 1.00 54.21  ? 479  HIS A CB    1 
ATOM   3855  C CG    . HIS B 2 482  ? 155.677 128.053 124.755 1.00 54.70  ? 479  HIS A CG    1 
ATOM   3856  N ND1   . HIS B 2 482  ? 155.016 127.929 125.957 1.00 55.09  ? 479  HIS A ND1   1 
ATOM   3857  C CD2   . HIS B 2 482  ? 156.045 129.353 124.660 1.00 54.58  ? 479  HIS A CD2   1 
ATOM   3858  C CE1   . HIS B 2 482  ? 154.983 129.101 126.563 1.00 55.29  ? 479  HIS A CE1   1 
ATOM   3859  N NE2   . HIS B 2 482  ? 155.601 129.983 125.797 1.00 54.99  ? 479  HIS A NE2   1 
ATOM   3860  N N     . LEU B 2 483  ? 156.575 123.960 122.790 1.00 58.11  ? 480  LEU A N     1 
ATOM   3861  C CA    . LEU B 2 483  ? 156.331 122.946 121.770 1.00 57.89  ? 480  LEU A CA    1 
ATOM   3862  C C     . LEU B 2 483  ? 155.862 121.635 122.387 1.00 59.17  ? 480  LEU A C     1 
ATOM   3863  O O     . LEU B 2 483  ? 154.978 120.965 121.842 1.00 59.88  ? 480  LEU A O     1 
ATOM   3864  C CB    . LEU B 2 483  ? 157.596 122.731 120.939 1.00 57.68  ? 480  LEU A CB    1 
ATOM   3865  C CG    . LEU B 2 483  ? 157.546 121.649 119.859 1.00 55.56  ? 480  LEU A CG    1 
ATOM   3866  C CD1   . LEU B 2 483  ? 156.439 121.937 118.861 1.00 54.20  ? 480  LEU A CD1   1 
ATOM   3867  C CD2   . LEU B 2 483  ? 158.886 121.533 119.156 1.00 55.50  ? 480  LEU A CD2   1 
ATOM   3868  N N     . LEU B 2 484  ? 156.435 121.256 123.531 1.00 60.00  ? 481  LEU A N     1 
ATOM   3869  C CA    . LEU B 2 484  ? 156.092 119.972 124.138 1.00 60.84  ? 481  LEU A CA    1 
ATOM   3870  C C     . LEU B 2 484  ? 154.667 119.961 124.676 1.00 61.91  ? 481  LEU A C     1 
ATOM   3871  O O     . LEU B 2 484  ? 154.039 118.897 124.733 1.00 65.30  ? 481  LEU A O     1 
ATOM   3872  C CB    . LEU B 2 484  ? 157.085 119.633 125.249 1.00 61.05  ? 481  LEU A CB    1 
ATOM   3873  C CG    . LEU B 2 484  ? 158.538 119.439 124.810 1.00 62.36  ? 481  LEU A CG    1 
ATOM   3874  C CD1   . LEU B 2 484  ? 159.408 119.034 125.991 1.00 65.84  ? 481  LEU A CD1   1 
ATOM   3875  C CD2   . LEU B 2 484  ? 158.635 118.414 123.689 1.00 59.89  ? 481  LEU A CD2   1 
ATOM   3876  N N     . ASP B 2 485  ? 154.139 121.118 125.068 1.00 59.93  ? 482  ASP A N     1 
ATOM   3877  C CA    . ASP B 2 485  ? 152.773 121.209 125.572 1.00 59.54  ? 482  ASP A CA    1 
ATOM   3878  C C     . ASP B 2 485  ? 151.725 121.127 124.468 1.00 59.21  ? 482  ASP A C     1 
ATOM   3879  O O     . ASP B 2 485  ? 150.533 121.291 124.753 1.00 56.86  ? 482  ASP A O     1 
ATOM   3880  C CB    . ASP B 2 485  ? 152.591 122.501 126.370 1.00 60.17  ? 482  ASP A CB    1 
ATOM   3881  C CG    . ASP B 2 485  ? 152.988 122.346 127.826 1.00 64.91  ? 482  ASP A CG    1 
ATOM   3882  O OD1   . ASP B 2 485  ? 153.891 121.534 128.114 1.00 68.43  ? 482  ASP A OD1   1 
ATOM   3883  O OD2   . ASP B 2 485  ? 152.393 123.031 128.684 1.00 66.76  ? 482  ASP A OD2   1 
ATOM   3884  N N     . TRP B 2 486  ? 152.138 120.881 123.223 1.00 59.22  ? 483  TRP A N     1 
ATOM   3885  C CA    . TRP B 2 486  ? 151.172 120.689 122.145 1.00 56.64  ? 483  TRP A CA    1 
ATOM   3886  C C     . TRP B 2 486  ? 150.435 119.363 122.277 1.00 58.54  ? 483  TRP A C     1 
ATOM   3887  O O     . TRP B 2 486  ? 149.293 119.242 121.822 1.00 58.97  ? 483  TRP A O     1 
ATOM   3888  C CB    . TRP B 2 486  ? 151.873 120.760 120.790 1.00 55.98  ? 483  TRP A CB    1 
ATOM   3889  C CG    . TRP B 2 486  ? 152.280 122.138 120.369 1.00 56.90  ? 483  TRP A CG    1 
ATOM   3890  C CD1   . TRP B 2 486  ? 152.242 123.273 121.125 1.00 56.59  ? 483  TRP A CD1   1 
ATOM   3891  C CD2   . TRP B 2 486  ? 152.776 122.527 119.084 1.00 55.97  ? 483  TRP A CD2   1 
ATOM   3892  N NE1   . TRP B 2 486  ? 152.689 124.346 120.392 1.00 54.32  ? 483  TRP A NE1   1 
ATOM   3893  C CE2   . TRP B 2 486  ? 153.023 123.914 119.133 1.00 54.76  ? 483  TRP A CE2   1 
ATOM   3894  C CE3   . TRP B 2 486  ? 153.035 121.837 117.895 1.00 55.78  ? 483  TRP A CE3   1 
ATOM   3895  C CZ2   . TRP B 2 486  ? 153.517 124.624 118.041 1.00 55.30  ? 483  TRP A CZ2   1 
ATOM   3896  C CZ3   . TRP B 2 486  ? 153.527 122.544 116.812 1.00 56.83  ? 483  TRP A CZ3   1 
ATOM   3897  C CH2   . TRP B 2 486  ? 153.763 123.921 116.892 1.00 56.14  ? 483  TRP A CH2   1 
ATOM   3898  N N     . PHE B 2 487  ? 151.066 118.365 122.890 1.00 61.90  ? 484  PHE A N     1 
ATOM   3899  C CA    . PHE B 2 487  ? 150.516 117.019 122.937 1.00 66.86  ? 484  PHE A CA    1 
ATOM   3900  C C     . PHE B 2 487  ? 149.638 116.830 124.166 1.00 74.18  ? 484  PHE A C     1 
ATOM   3901  O O     . PHE B 2 487  ? 149.935 117.355 125.244 1.00 71.55  ? 484  PHE A O     1 
ATOM   3902  C CB    . PHE B 2 487  ? 151.643 115.985 122.931 1.00 67.09  ? 484  PHE A CB    1 
ATOM   3903  C CG    . PHE B 2 487  ? 152.577 116.119 121.762 1.00 65.91  ? 484  PHE A CG    1 
ATOM   3904  C CD1   . PHE B 2 487  ? 152.222 115.632 120.515 1.00 62.18  ? 484  PHE A CD1   1 
ATOM   3905  C CD2   . PHE B 2 487  ? 153.810 116.735 121.910 1.00 67.70  ? 484  PHE A CD2   1 
ATOM   3906  C CE1   . PHE B 2 487  ? 153.080 115.755 119.438 1.00 61.39  ? 484  PHE A CE1   1 
ATOM   3907  C CE2   . PHE B 2 487  ? 154.671 116.860 120.835 1.00 67.20  ? 484  PHE A CE2   1 
ATOM   3908  C CZ    . PHE B 2 487  ? 154.305 116.369 119.597 1.00 63.97  ? 484  PHE A CZ    1 
ATOM   3909  N N     . ALA B 2 488  ? 148.558 116.072 123.995 1.00 83.31  ? 485  ALA A N     1 
ATOM   3910  C CA    . ALA B 2 488  ? 147.633 115.817 125.089 1.00 90.72  ? 485  ALA A CA    1 
ATOM   3911  C C     . ALA B 2 488  ? 148.296 114.974 126.171 1.00 96.80  ? 485  ALA A C     1 
ATOM   3912  O O     . ALA B 2 488  ? 149.019 114.016 125.882 1.00 95.35  ? 485  ALA A O     1 
ATOM   3913  C CB    . ALA B 2 488  ? 146.378 115.114 124.570 1.00 89.57  ? 485  ALA A CB    1 
ATOM   3914  N N     . VAL B 2 489  ? 148.034 115.332 127.426 1.00 105.19 ? 486  VAL A N     1 
ATOM   3915  C CA    . VAL B 2 489  ? 148.675 114.684 128.566 1.00 109.76 ? 486  VAL A CA    1 
ATOM   3916  C C     . VAL B 2 489  ? 147.695 113.726 129.232 1.00 109.59 ? 486  VAL A C     1 
ATOM   3917  O O     . VAL B 2 489  ? 148.104 112.730 129.842 1.00 111.37 ? 486  VAL A O     1 
ATOM   3918  C CB    . VAL B 2 489  ? 149.193 115.731 129.571 1.00 112.13 ? 486  VAL A CB    1 
ATOM   3919  C CG1   . VAL B 2 489  ? 150.110 115.084 130.600 1.00 115.35 ? 486  VAL A CG1   1 
ATOM   3920  C CG2   . VAL B 2 489  ? 149.908 116.856 128.839 1.00 111.13 ? 486  VAL A CG2   1 
ATOM   3921  N N     . ASP B 2 490  ? 146.401 114.015 129.116 1.00 105.19 ? 487  ASP A N     1 
ATOM   3922  C CA    . ASP B 2 490  ? 145.390 113.200 129.776 1.00 105.27 ? 487  ASP A CA    1 
ATOM   3923  C C     . ASP B 2 490  ? 145.407 111.774 129.240 1.00 105.98 ? 487  ASP A C     1 
ATOM   3924  O O     . ASP B 2 490  ? 145.604 111.543 128.045 1.00 106.07 ? 487  ASP A O     1 
ATOM   3925  C CB    . ASP B 2 490  ? 144.003 113.818 129.583 1.00 103.54 ? 487  ASP A CB    1 
ATOM   3926  N N     . GLU B 2 491  ? 145.203 110.815 130.141 1.00 105.09 ? 488  GLU A N     1 
ATOM   3927  C CA    . GLU B 2 491  ? 145.174 109.402 129.786 1.00 101.99 ? 488  GLU A CA    1 
ATOM   3928  C C     . GLU B 2 491  ? 143.847 108.972 129.172 1.00 97.73  ? 488  GLU A C     1 
ATOM   3929  O O     . GLU B 2 491  ? 143.628 107.770 128.983 1.00 97.66  ? 488  GLU A O     1 
ATOM   3930  C CB    . GLU B 2 491  ? 145.478 108.544 131.017 1.00 102.24 ? 488  GLU A CB    1 
ATOM   3931  N N     . SER B 2 492  ? 142.962 109.921 128.865 1.00 93.83  ? 489  SER A N     1 
ATOM   3932  C CA    . SER B 2 492  ? 141.692 109.576 128.234 1.00 90.65  ? 489  SER A CA    1 
ATOM   3933  C C     . SER B 2 492  ? 141.889 109.086 126.804 1.00 89.67  ? 489  SER A C     1 
ATOM   3934  O O     . SER B 2 492  ? 141.055 108.330 126.291 1.00 90.05  ? 489  SER A O     1 
ATOM   3935  C CB    . SER B 2 492  ? 140.751 110.779 128.263 1.00 87.23  ? 489  SER A CB    1 
ATOM   3936  O OG    . SER B 2 492  ? 141.376 111.931 127.724 1.00 83.94  ? 489  SER A OG    1 
ATOM   3937  N N     . ASN B 2 493  ? 142.974 109.493 126.153 1.00 88.83  ? 490  ASN A N     1 
ATOM   3938  C CA    . ASN B 2 493  ? 143.269 109.074 124.792 1.00 87.07  ? 490  ASN A CA    1 
ATOM   3939  C C     . ASN B 2 493  ? 144.189 107.855 124.795 1.00 89.27  ? 490  ASN A C     1 
ATOM   3940  O O     . ASN B 2 493  ? 144.890 107.575 125.772 1.00 88.67  ? 490  ASN A O     1 
ATOM   3941  C CB    . ASN B 2 493  ? 143.919 110.212 124.005 1.00 84.17  ? 490  ASN A CB    1 
ATOM   3942  C CG    . ASN B 2 493  ? 143.260 111.554 124.263 1.00 81.82  ? 490  ASN A CG    1 
ATOM   3943  O OD1   . ASN B 2 493  ? 142.233 111.880 123.667 1.00 80.56  ? 490  ASN A OD1   1 
ATOM   3944  N ND2   . ASN B 2 493  ? 143.854 112.346 125.150 1.00 81.05  ? 490  ASN A ND2   1 
ATOM   3945  N N     . GLU B 2 494  ? 144.178 107.127 123.678 1.00 91.56  ? 491  GLU A N     1 
ATOM   3946  C CA    . GLU B 2 494  ? 145.041 105.960 123.501 1.00 92.54  ? 491  GLU A CA    1 
ATOM   3947  C C     . GLU B 2 494  ? 146.433 106.446 123.112 1.00 94.62  ? 491  GLU A C     1 
ATOM   3948  O O     . GLU B 2 494  ? 146.805 106.517 121.938 1.00 92.87  ? 491  GLU A O     1 
ATOM   3949  C CB    . GLU B 2 494  ? 144.468 105.012 122.457 1.00 88.15  ? 491  GLU A CB    1 
ATOM   3950  C CG    . GLU B 2 494  ? 143.275 104.207 122.940 1.00 85.16  ? 491  GLU A CG    1 
ATOM   3951  C CD    . GLU B 2 494  ? 142.840 103.157 121.937 1.00 83.10  ? 491  GLU A CD    1 
ATOM   3952  O OE1   . GLU B 2 494  ? 142.743 103.487 120.737 1.00 81.29  ? 491  GLU A OE1   1 
ATOM   3953  O OE2   . GLU B 2 494  ? 142.600 102.001 122.347 1.00 84.13  ? 491  GLU A OE2   1 
ATOM   3954  N N     . VAL B 2 495  ? 147.221 106.787 124.132 1.00 100.90 ? 492  VAL A N     1 
ATOM   3955  C CA    . VAL B 2 495  ? 148.565 107.310 123.923 1.00 99.65  ? 492  VAL A CA    1 
ATOM   3956  C C     . VAL B 2 495  ? 149.526 106.165 123.641 1.00 98.55  ? 492  VAL A C     1 
ATOM   3957  O O     . VAL B 2 495  ? 149.330 105.027 124.086 1.00 98.98  ? 492  VAL A O     1 
ATOM   3958  C CB    . VAL B 2 495  ? 149.020 108.139 125.143 1.00 101.24 ? 492  VAL A CB    1 
ATOM   3959  C CG1   . VAL B 2 495  ? 148.174 109.398 125.267 1.00 99.94  ? 492  VAL A CG1   1 
ATOM   3960  C CG2   . VAL B 2 495  ? 148.932 107.303 126.413 1.00 104.30 ? 492  VAL A CG2   1 
ATOM   3961  N N     . ASP B 2 496  ? 150.576 106.469 122.886 1.00 97.18  ? 493  ASP A N     1 
ATOM   3962  C CA    . ASP B 2 496  ? 151.584 105.474 122.564 1.00 96.99  ? 493  ASP A CA    1 
ATOM   3963  C C     . ASP B 2 496  ? 152.334 105.064 123.829 1.00 98.87  ? 493  ASP A C     1 
ATOM   3964  O O     . ASP B 2 496  ? 152.587 105.903 124.699 1.00 100.36 ? 493  ASP A O     1 
ATOM   3965  C CB    . ASP B 2 496  ? 152.560 106.030 121.527 1.00 94.48  ? 493  ASP A CB    1 
ATOM   3966  C CG    . ASP B 2 496  ? 153.515 104.982 120.996 1.00 95.54  ? 493  ASP A CG    1 
ATOM   3967  O OD1   . ASP B 2 496  ? 153.174 104.322 119.992 1.00 94.90  ? 493  ASP A OD1   1 
ATOM   3968  O OD2   . ASP B 2 496  ? 154.608 104.821 121.577 1.00 97.72  ? 493  ASP A OD2   1 
ATOM   3969  N N     . PRO B 2 497  ? 152.683 103.780 123.974 1.00 99.80  ? 494  PRO A N     1 
ATOM   3970  C CA    . PRO B 2 497  ? 153.422 103.346 125.169 1.00 100.18 ? 494  PRO A CA    1 
ATOM   3971  C C     . PRO B 2 497  ? 154.753 104.062 125.336 1.00 97.70  ? 494  PRO A C     1 
ATOM   3972  O O     . PRO B 2 497  ? 154.973 104.754 126.334 1.00 96.91  ? 494  PRO A O     1 
ATOM   3973  C CB    . PRO B 2 497  ? 153.622 101.844 124.927 1.00 103.34 ? 494  PRO A CB    1 
ATOM   3974  C CG    . PRO B 2 497  ? 152.517 101.458 124.005 1.00 101.94 ? 494  PRO A CG    1 
ATOM   3975  C CD    . PRO B 2 497  ? 152.301 102.646 123.116 1.00 99.88  ? 494  PRO A CD    1 
ATOM   3976  N N     . GLU B 2 498  ? 155.644 103.909 124.354 1.00 96.41  ? 495  GLU A N     1 
ATOM   3977  C CA    . GLU B 2 498  ? 156.983 104.475 124.477 1.00 95.14  ? 495  GLU A CA    1 
ATOM   3978  C C     . GLU B 2 498  ? 156.967 105.992 124.332 1.00 92.29  ? 495  GLU A C     1 
ATOM   3979  O O     . GLU B 2 498  ? 157.666 106.697 125.069 1.00 93.51  ? 495  GLU A O     1 
ATOM   3980  C CB    . GLU B 2 498  ? 157.915 103.846 123.440 1.00 95.44  ? 495  GLU A CB    1 
ATOM   3981  N N     . PHE B 2 499  ? 156.174 106.517 123.393 1.00 86.17  ? 496  PHE A N     1 
ATOM   3982  C CA    . PHE B 2 499  ? 156.206 107.949 123.113 1.00 79.92  ? 496  PHE A CA    1 
ATOM   3983  C C     . PHE B 2 499  ? 155.708 108.763 124.301 1.00 76.77  ? 496  PHE A C     1 
ATOM   3984  O O     . PHE B 2 499  ? 156.324 109.772 124.666 1.00 77.69  ? 496  PHE A O     1 
ATOM   3985  C CB    . PHE B 2 499  ? 155.380 108.264 121.867 1.00 75.12  ? 496  PHE A CB    1 
ATOM   3986  C CG    . PHE B 2 499  ? 155.548 109.674 121.367 1.00 72.57  ? 496  PHE A CG    1 
ATOM   3987  C CD1   . PHE B 2 499  ? 154.745 110.698 121.845 1.00 70.92  ? 496  PHE A CD1   1 
ATOM   3988  C CD2   . PHE B 2 499  ? 156.514 109.975 120.419 1.00 73.09  ? 496  PHE A CD2   1 
ATOM   3989  C CE1   . PHE B 2 499  ? 154.901 111.993 121.387 1.00 69.17  ? 496  PHE A CE1   1 
ATOM   3990  C CE2   . PHE B 2 499  ? 156.673 111.269 119.957 1.00 71.51  ? 496  PHE A CE2   1 
ATOM   3991  C CZ    . PHE B 2 499  ? 155.865 112.279 120.443 1.00 69.31  ? 496  PHE A CZ    1 
ATOM   3992  N N     . SER B 2 500  ? 154.596 108.349 124.911 1.00 74.04  ? 497  SER A N     1 
ATOM   3993  C CA    . SER B 2 500  ? 154.057 109.099 126.040 1.00 73.44  ? 497  SER A CA    1 
ATOM   3994  C C     . SER B 2 500  ? 154.994 109.064 127.240 1.00 78.22  ? 497  SER A C     1 
ATOM   3995  O O     . SER B 2 500  ? 155.025 110.016 128.027 1.00 75.81  ? 497  SER A O     1 
ATOM   3996  C CB    . SER B 2 500  ? 152.681 108.559 126.428 1.00 72.94  ? 497  SER A CB    1 
ATOM   3997  O OG    . SER B 2 500  ? 152.132 109.288 127.510 1.00 74.00  ? 497  SER A OG    1 
ATOM   3998  N N     . ALA B 2 501  ? 155.763 107.984 127.397 1.00 83.05  ? 498  ALA A N     1 
ATOM   3999  C CA    . ALA B 2 501  ? 156.693 107.906 128.519 1.00 85.02  ? 498  ALA A CA    1 
ATOM   4000  C C     . ALA B 2 501  ? 157.914 108.787 128.285 1.00 84.98  ? 498  ALA A C     1 
ATOM   4001  O O     . ALA B 2 501  ? 158.357 109.494 129.197 1.00 85.84  ? 498  ALA A O     1 
ATOM   4002  C CB    . ALA B 2 501  ? 157.111 106.455 128.757 1.00 86.72  ? 498  ALA A CB    1 
ATOM   4003  N N     . ARG B 2 502  ? 158.472 108.756 127.071 1.00 85.52  ? 499  ARG A N     1 
ATOM   4004  C CA    . ARG B 2 502  ? 159.636 109.583 126.772 1.00 88.02  ? 499  ARG A CA    1 
ATOM   4005  C C     . ARG B 2 502  ? 159.276 111.062 126.707 1.00 87.53  ? 499  ARG A C     1 
ATOM   4006  O O     . ARG B 2 502  ? 160.096 111.913 127.074 1.00 89.00  ? 499  ARG A O     1 
ATOM   4007  C CB    . ARG B 2 502  ? 160.277 109.137 125.458 1.00 91.14  ? 499  ARG A CB    1 
ATOM   4008  C CG    . ARG B 2 502  ? 160.678 107.672 125.419 1.00 98.39  ? 499  ARG A CG    1 
ATOM   4009  C CD    . ARG B 2 502  ? 161.502 107.369 124.180 1.00 103.76 ? 499  ARG A CD    1 
ATOM   4010  N NE    . ARG B 2 502  ? 162.821 107.988 124.249 1.00 109.77 ? 499  ARG A NE    1 
ATOM   4011  C CZ    . ARG B 2 502  ? 163.676 108.046 123.232 1.00 113.65 ? 499  ARG A CZ    1 
ATOM   4012  N NH1   . ARG B 2 502  ? 163.348 107.529 122.056 1.00 113.83 ? 499  ARG A NH1   1 
ATOM   4013  N NH2   . ARG B 2 502  ? 164.858 108.629 123.390 1.00 115.95 ? 499  ARG A NH2   1 
ATOM   4014  N N     . LEU B 2 503  ? 158.069 111.387 126.242 1.00 86.59  ? 500  LEU A N     1 
ATOM   4015  C CA    . LEU B 2 503  ? 157.651 112.784 126.182 1.00 83.48  ? 500  LEU A CA    1 
ATOM   4016  C C     . LEU B 2 503  ? 157.410 113.343 127.578 1.00 82.48  ? 500  LEU A C     1 
ATOM   4017  O O     . LEU B 2 503  ? 157.865 114.446 127.902 1.00 82.34  ? 500  LEU A O     1 
ATOM   4018  C CB    . LEU B 2 503  ? 156.393 112.919 125.324 1.00 78.20  ? 500  LEU A CB    1 
ATOM   4019  C CG    . LEU B 2 503  ? 155.775 114.315 125.255 1.00 74.84  ? 500  LEU A CG    1 
ATOM   4020  C CD1   . LEU B 2 503  ? 156.760 115.311 124.660 1.00 75.31  ? 500  LEU A CD1   1 
ATOM   4021  C CD2   . LEU B 2 503  ? 154.484 114.291 124.456 1.00 72.65  ? 500  LEU A CD2   1 
ATOM   4022  N N     . THR B 2 504  ? 156.698 112.590 128.422 1.00 82.46  ? 501  THR A N     1 
ATOM   4023  C CA    . THR B 2 504  ? 156.426 113.052 129.779 1.00 83.03  ? 501  THR A CA    1 
ATOM   4024  C C     . THR B 2 504  ? 157.711 113.203 130.585 1.00 83.95  ? 501  THR A C     1 
ATOM   4025  O O     . THR B 2 504  ? 157.772 114.024 131.506 1.00 84.42  ? 501  THR A O     1 
ATOM   4026  C CB    . THR B 2 504  ? 155.470 112.087 130.482 1.00 85.10  ? 501  THR A CB    1 
ATOM   4027  O OG1   . THR B 2 504  ? 154.439 111.687 129.571 1.00 84.13  ? 501  THR A OG1   1 
ATOM   4028  C CG2   . THR B 2 504  ? 154.831 112.754 131.692 1.00 87.44  ? 501  THR A CG2   1 
ATOM   4029  N N     . GLY B 2 505  ? 158.742 112.426 130.251 1.00 85.49  ? 502  GLY A N     1 
ATOM   4030  C CA    . GLY B 2 505  ? 160.006 112.556 130.959 1.00 87.05  ? 502  GLY A CA    1 
ATOM   4031  C C     . GLY B 2 505  ? 160.705 113.869 130.659 1.00 83.65  ? 502  GLY A C     1 
ATOM   4032  O O     . GLY B 2 505  ? 161.095 114.603 131.571 1.00 84.50  ? 502  GLY A O     1 
ATOM   4033  N N     . ILE B 2 506  ? 161.037 114.130 129.390 1.00 80.70  ? 503  ILE A N     1 
ATOM   4034  C CA    . ILE B 2 506  ? 161.847 115.366 129.139 1.00 80.89  ? 503  ILE A CA    1 
ATOM   4035  C C     . ILE B 2 506  ? 160.979 116.554 129.556 1.00 83.11  ? 503  ILE A C     1 
ATOM   4036  O O     . ILE B 2 506  ? 161.552 117.607 129.910 1.00 83.07  ? 503  ILE A O     1 
ATOM   4037  C CB    . ILE B 2 506  ? 162.354 115.477 127.683 1.00 78.19  ? 503  ILE A CB    1 
ATOM   4038  C CG1   . ILE B 2 506  ? 161.336 114.915 126.688 1.00 75.43  ? 503  ILE A CG1   1 
ATOM   4039  C CG2   . ILE B 2 506  ? 163.705 114.802 127.531 1.00 80.82  ? 503  ILE A CG2   1 
ATOM   4040  C CD1   . ILE B 2 506  ? 161.958 114.191 125.519 1.00 74.34  ? 503  ILE A CD1   1 
ATOM   4041  N N     . LYS B 2 507  ? 159.654 116.361 129.555 1.00 85.24  ? 504  LYS A N     1 
ATOM   4042  C CA    . LYS B 2 507  ? 158.716 117.450 129.942 1.00 85.52  ? 504  LYS A CA    1 
ATOM   4043  C C     . LYS B 2 507  ? 158.851 117.749 131.434 1.00 90.70  ? 504  LYS A C     1 
ATOM   4044  O O     . LYS B 2 507  ? 159.094 118.918 131.784 1.00 87.62  ? 504  LYS A O     1 
ATOM   4045  C CB    . LYS B 2 507  ? 157.267 117.047 129.660 1.00 82.62  ? 504  LYS A CB    1 
ATOM   4046  C CG    . LYS B 2 507  ? 156.219 118.078 130.056 1.00 81.76  ? 504  LYS A CG    1 
ATOM   4047  C CD    . LYS B 2 507  ? 154.881 117.858 129.385 1.00 81.05  ? 504  LYS A CD    1 
ATOM   4048  C CE    . LYS B 2 507  ? 154.962 117.931 127.875 1.00 80.65  ? 504  LYS A CE    1 
ATOM   4049  N NZ    . LYS B 2 507  ? 153.623 117.839 127.247 1.00 78.56  ? 504  LYS A NZ    1 
ATOM   4050  N N     . LEU B 2 508  ? 158.696 116.729 132.276 1.00 96.65  ? 505  LEU A N     1 
ATOM   4051  C CA    . LEU B 2 508  ? 158.724 116.980 133.734 1.00 96.65  ? 505  LEU A CA    1 
ATOM   4052  C C     . LEU B 2 508  ? 159.980 117.781 134.015 1.00 96.65  ? 505  LEU A C     1 
ATOM   4053  O O     . LEU B 2 508  ? 160.039 118.462 135.049 1.00 96.65  ? 505  LEU A O     1 
ATOM   4054  C CB    . LEU B 2 508  ? 158.762 115.631 134.455 1.00 96.65  ? 505  LEU A CB    1 
ATOM   4055  C CG    . LEU B 2 508  ? 158.631 115.694 135.976 1.00 96.65  ? 505  LEU A CG    1 
ATOM   4056  C CD1   . LEU B 2 508  ? 157.357 116.421 136.378 1.00 96.65  ? 505  LEU A CD1   1 
ATOM   4057  C CD2   . LEU B 2 508  ? 158.663 114.299 136.580 1.00 96.65  ? 505  LEU A CD2   1 
ATOM   4058  N N     . GLU B 2 509  ? 160.930 117.707 133.103 1.00 95.21  ? 506  GLU A N     1 
ATOM   4059  C CA    . GLU B 2 509  ? 162.214 118.346 133.364 1.00 95.21  ? 506  GLU A CA    1 
ATOM   4060  C C     . GLU B 2 509  ? 162.217 119.811 132.947 1.00 95.21  ? 506  GLU A C     1 
ATOM   4061  O O     . GLU B 2 509  ? 162.972 120.610 133.513 1.00 95.21  ? 506  GLU A O     1 
ATOM   4062  C CB    . GLU B 2 509  ? 163.329 117.587 132.643 1.00 95.21  ? 506  GLU A CB    1 
ATOM   4063  C CG    . GLU B 2 509  ? 164.730 117.947 133.107 1.00 95.21  ? 506  GLU A CG    1 
ATOM   4064  C CD    . GLU B 2 509  ? 165.363 119.026 132.253 1.00 95.21  ? 506  GLU A CD    1 
ATOM   4065  O OE1   . GLU B 2 509  ? 164.981 119.146 131.070 1.00 95.21  ? 506  GLU A OE1   1 
ATOM   4066  O OE2   . GLU B 2 509  ? 166.239 119.754 132.764 1.00 95.21  ? 506  GLU A OE2   1 
ATOM   4067  N N     . MET B 2 510  ? 161.390 120.183 131.973 1.00 89.61  ? 507  MET A N     1 
ATOM   4068  C CA    . MET B 2 510  ? 161.348 121.547 131.463 1.00 89.61  ? 507  MET A CA    1 
ATOM   4069  C C     . MET B 2 510  ? 160.313 122.423 132.158 1.00 89.61  ? 507  MET A C     1 
ATOM   4070  O O     . MET B 2 510  ? 160.223 123.613 131.839 1.00 89.61  ? 507  MET A O     1 
ATOM   4071  C CB    . MET B 2 510  ? 161.073 121.539 129.955 1.00 89.61  ? 507  MET A CB    1 
ATOM   4072  C CG    . MET B 2 510  ? 162.097 120.777 129.135 1.00 89.61  ? 507  MET A CG    1 
ATOM   4073  S SD    . MET B 2 510  ? 163.728 121.537 129.205 1.00 89.61  ? 507  MET A SD    1 
ATOM   4074  C CE    . MET B 2 510  ? 164.291 121.284 127.525 1.00 89.61  ? 507  MET A CE    1 
ATOM   4075  N N     . GLU B 2 511  ? 159.528 121.874 133.085 1.00 89.19  ? 508  GLU A N     1 
ATOM   4076  C CA    . GLU B 2 511  ? 158.539 122.696 133.779 1.00 89.19  ? 508  GLU A CA    1 
ATOM   4077  C C     . GLU B 2 511  ? 159.142 123.835 134.605 1.00 89.19  ? 508  GLU A C     1 
ATOM   4078  O O     . GLU B 2 511  ? 158.565 124.937 134.575 1.00 89.19  ? 508  GLU A O     1 
ATOM   4079  C CB    . GLU B 2 511  ? 157.609 121.810 134.627 1.00 89.19  ? 508  GLU A CB    1 
ATOM   4080  C CG    . GLU B 2 511  ? 158.211 121.133 135.847 1.00 89.19  ? 508  GLU A CG    1 
ATOM   4081  C CD    . GLU B 2 511  ? 158.114 121.987 137.096 1.00 89.19  ? 508  GLU A CD    1 
ATOM   4082  O OE1   . GLU B 2 511  ? 157.295 122.930 137.111 1.00 89.19  ? 508  GLU A OE1   1 
ATOM   4083  O OE2   . GLU B 2 511  ? 158.856 121.716 138.063 1.00 89.19  ? 508  GLU A OE2   1 
ATOM   4084  N N     . PRO B 2 512  ? 160.249 123.675 135.350 1.00 88.15  ? 509  PRO A N     1 
ATOM   4085  C CA    . PRO B 2 512  ? 160.756 124.827 136.113 1.00 88.15  ? 509  PRO A CA    1 
ATOM   4086  C C     . PRO B 2 512  ? 161.325 125.927 135.235 1.00 88.15  ? 509  PRO A C     1 
ATOM   4087  O O     . PRO B 2 512  ? 161.426 127.070 135.696 1.00 88.15  ? 509  PRO A O     1 
ATOM   4088  C CB    . PRO B 2 512  ? 161.834 124.213 137.012 1.00 88.15  ? 509  PRO A CB    1 
ATOM   4089  C CG    . PRO B 2 512  ? 162.341 123.073 136.246 1.00 88.15  ? 509  PRO A CG    1 
ATOM   4090  C CD    . PRO B 2 512  ? 161.203 122.547 135.414 1.00 88.15  ? 509  PRO A CD    1 
ATOM   4091  N N     . SER B 2 513  ? 161.621 125.619 133.969 1.00 83.28  ? 510  SER A N     1 
ATOM   4092  C CA    . SER B 2 513  ? 162.085 126.682 133.039 1.00 83.28  ? 510  SER A CA    1 
ATOM   4093  C C     . SER B 2 513  ? 161.066 127.828 133.028 1.00 83.28  ? 510  SER A C     1 
ATOM   4094  O O     . SER B 2 513  ? 161.491 128.994 133.126 1.00 83.28  ? 510  SER A O     1 
ATOM   4095  C CB    . SER B 2 513  ? 162.310 126.137 131.653 1.00 83.28  ? 510  SER A CB    1 
ATOM   4096  O OG    . SER B 2 513  ? 161.075 125.809 131.034 1.00 83.28  ? 510  SER A OG    1 
ATOM   4097  N N     . LEU B 2 514  ? 159.780 127.494 132.884 1.00 82.75  ? 511  LEU A N     1 
ATOM   4098  C CA    . LEU B 2 514  ? 158.711 128.526 132.829 1.00 82.75  ? 511  LEU A CA    1 
ATOM   4099  C C     . LEU B 2 514  ? 158.751 129.364 134.110 1.00 82.75  ? 511  LEU A C     1 
ATOM   4100  O O     . LEU B 2 514  ? 158.803 130.602 134.003 1.00 82.75  ? 511  LEU A O     1 
ATOM   4101  C CB    . LEU B 2 514  ? 157.358 127.825 132.676 1.00 82.75  ? 511  LEU A CB    1 
ATOM   4102  C CG    . LEU B 2 514  ? 156.135 128.739 132.724 1.00 82.75  ? 511  LEU A CG    1 
ATOM   4103  C CD1   . LEU B 2 514  ? 156.211 129.805 131.642 1.00 82.75  ? 511  LEU A CD1   1 
ATOM   4104  C CD2   . LEU B 2 514  ? 154.852 127.934 132.591 1.00 82.75  ? 511  LEU A CD2   1 
ATOM   4105  N N     . SER B 2 515  ? 158.723 128.705 135.272 1.00 80.91  ? 512  SER A N     1 
ATOM   4106  C CA    . SER B 2 515  ? 158.789 129.434 136.564 1.00 80.91  ? 512  SER A CA    1 
ATOM   4107  C C     . SER B 2 515  ? 160.102 130.219 136.630 1.00 80.91  ? 512  SER A C     1 
ATOM   4108  O O     . SER B 2 515  ? 160.062 131.410 136.999 1.00 80.91  ? 512  SER A O     1 
ATOM   4109  C CB    . SER B 2 515  ? 158.659 128.488 137.727 1.00 80.91  ? 512  SER A CB    1 
ATOM   4110  O OG    . SER B 2 515  ? 159.766 127.601 137.780 1.00 80.91  ? 512  SER A OG    1 
ATOM   4111  N N     . PHE B 2 516  ? 161.213 129.575 136.260 1.00 76.13  ? 513  PHE A N     1 
ATOM   4112  C CA    . PHE B 2 516  ? 162.534 130.256 136.278 1.00 76.13  ? 513  PHE A CA    1 
ATOM   4113  C C     . PHE B 2 516  ? 162.490 131.454 135.326 1.00 76.13  ? 513  PHE A C     1 
ATOM   4114  O O     . PHE B 2 516  ? 162.987 132.516 135.706 1.00 76.13  ? 513  PHE A O     1 
ATOM   4115  C CB    . PHE B 2 516  ? 163.658 129.292 135.892 1.00 76.13  ? 513  PHE A CB    1 
ATOM   4116  C CG    . PHE B 2 516  ? 165.046 129.854 136.065 1.00 76.13  ? 513  PHE A CG    1 
ATOM   4117  C CD1   . PHE B 2 516  ? 165.652 130.580 135.052 1.00 76.13  ? 513  PHE A CD1   1 
ATOM   4118  C CD2   . PHE B 2 516  ? 165.746 129.665 137.246 1.00 76.13  ? 513  PHE A CD2   1 
ATOM   4119  C CE1   . PHE B 2 516  ? 166.925 131.103 135.216 1.00 76.13  ? 513  PHE A CE1   1 
ATOM   4120  C CE2   . PHE B 2 516  ? 167.021 130.184 137.408 1.00 76.13  ? 513  PHE A CE2   1 
ATOM   4121  C CZ    . PHE B 2 516  ? 167.607 130.903 136.393 1.00 76.13  ? 513  PHE A CZ    1 
ATOM   4122  N N     . TYR B 2 517  ? 161.907 131.278 134.137 1.00 76.24  ? 514  TYR A N     1 
ATOM   4123  C CA    . TYR B 2 517  ? 161.811 132.382 133.145 1.00 76.24  ? 514  TYR A CA    1 
ATOM   4124  C C     . TYR B 2 517  ? 161.045 133.554 133.764 1.00 76.24  ? 514  TYR A C     1 
ATOM   4125  O O     . TYR B 2 517  ? 161.501 134.704 133.632 1.00 76.24  ? 514  TYR A O     1 
ATOM   4126  C CB    . TYR B 2 517  ? 161.117 131.895 131.870 1.00 76.24  ? 514  TYR A CB    1 
ATOM   4127  C CG    . TYR B 2 517  ? 160.941 132.942 130.800 1.00 76.24  ? 514  TYR A CG    1 
ATOM   4128  C CD1   . TYR B 2 517  ? 159.815 133.748 130.762 1.00 76.24  ? 514  TYR A CD1   1 
ATOM   4129  C CD2   . TYR B 2 517  ? 161.898 133.124 129.817 1.00 76.24  ? 514  TYR A CD2   1 
ATOM   4130  C CE1   . TYR B 2 517  ? 159.649 134.712 129.782 1.00 76.24  ? 514  TYR A CE1   1 
ATOM   4131  C CE2   . TYR B 2 517  ? 161.747 134.081 128.828 1.00 76.24  ? 514  TYR A CE2   1 
ATOM   4132  C CZ    . TYR B 2 517  ? 160.618 134.879 128.810 1.00 76.24  ? 514  TYR A CZ    1 
ATOM   4133  O OH    . TYR B 2 517  ? 160.463 135.824 127.838 1.00 76.24  ? 514  TYR A OH    1 
ATOM   4134  N N     . ASN B 2 518  ? 159.917 133.265 134.419 1.00 69.93  ? 515  ASN A N     1 
ATOM   4135  C CA    . ASN B 2 518  ? 159.084 134.336 135.028 1.00 69.93  ? 515  ASN A CA    1 
ATOM   4136  C C     . ASN B 2 518  ? 159.893 135.040 136.122 1.00 69.93  ? 515  ASN A C     1 
ATOM   4137  O O     . ASN B 2 518  ? 159.828 136.281 136.194 1.00 69.93  ? 515  ASN A O     1 
ATOM   4138  C CB    . ASN B 2 518  ? 157.764 133.781 135.567 1.00 69.93  ? 515  ASN A CB    1 
ATOM   4139  C CG    . ASN B 2 518  ? 156.953 133.068 134.506 1.00 69.93  ? 515  ASN A CG    1 
ATOM   4140  O OD1   . ASN B 2 518  ? 157.252 133.169 133.318 1.00 69.93  ? 515  ASN A OD1   1 
ATOM   4141  N ND2   . ASN B 2 518  ? 155.927 132.345 134.923 1.00 69.93  ? 515  ASN A ND2   1 
ATOM   4142  N N     . LYS B 2 519  ? 160.627 134.271 136.931 1.00 65.31  ? 516  LYS A N     1 
ATOM   4143  C CA    . LYS B 2 519  ? 161.450 134.860 138.021 1.00 65.31  ? 516  LYS A CA    1 
ATOM   4144  C C     . LYS B 2 519  ? 162.496 135.788 137.398 1.00 65.31  ? 516  LYS A C     1 
ATOM   4145  O O     . LYS B 2 519  ? 162.704 136.893 137.938 1.00 65.31  ? 516  LYS A O     1 
ATOM   4146  C CB    . LYS B 2 519  ? 162.091 133.739 138.846 1.00 65.31  ? 516  LYS A CB    1 
ATOM   4147  C CG    . LYS B 2 519  ? 163.415 134.080 139.517 1.00 65.31  ? 516  LYS A CG    1 
ATOM   4148  C CD    . LYS B 2 519  ? 164.616 133.504 138.796 1.00 65.31  ? 516  LYS A CD    1 
ATOM   4149  C CE    . LYS B 2 519  ? 165.932 133.890 139.438 1.00 65.31  ? 516  LYS A CE    1 
ATOM   4150  N NZ    . LYS B 2 519  ? 167.085 133.281 138.735 1.00 65.31  ? 516  LYS A NZ    1 
ATOM   4151  N N     . ALA B 2 520  ? 163.112 135.357 136.296 1.00 63.32  ? 517  ALA A N     1 
ATOM   4152  C CA    . ALA B 2 520  ? 164.156 136.163 135.626 1.00 63.32  ? 517  ALA A CA    1 
ATOM   4153  C C     . ALA B 2 520  ? 163.525 137.436 135.061 1.00 63.32  ? 517  ALA A C     1 
ATOM   4154  O O     . ALA B 2 520  ? 164.147 138.512 135.203 1.00 63.32  ? 517  ALA A O     1 
ATOM   4155  C CB    . ALA B 2 520  ? 164.817 135.346 134.543 1.00 63.32  ? 517  ALA A CB    1 
ATOM   4156  N N     . ARG B 2 521  ? 162.341 137.331 134.447 1.00 60.42  ? 518  ARG A N     1 
ATOM   4157  C CA    . ARG B 2 521  ? 161.803 138.550 133.849 1.00 60.42  ? 518  ARG A CA    1 
ATOM   4158  C C     . ARG B 2 521  ? 161.460 139.582 134.917 1.00 60.42  ? 518  ARG A C     1 
ATOM   4159  O O     . ARG B 2 521  ? 161.635 140.787 134.702 1.00 60.42  ? 518  ARG A O     1 
ATOM   4160  C CB    . ARG B 2 521  ? 160.581 138.210 132.991 1.00 60.42  ? 518  ARG A CB    1 
ATOM   4161  C CG    . ARG B 2 521  ? 160.012 139.354 132.154 1.00 60.42  ? 518  ARG A CG    1 
ATOM   4162  C CD    . ARG B 2 521  ? 158.952 140.147 132.902 1.00 60.42  ? 518  ARG A CD    1 
ATOM   4163  N NE    . ARG B 2 521  ? 157.880 139.287 133.388 1.00 60.42  ? 518  ARG A NE    1 
ATOM   4164  C CZ    . ARG B 2 521  ? 156.860 138.871 132.652 1.00 60.42  ? 518  ARG A CZ    1 
ATOM   4165  N NH1   . ARG B 2 521  ? 156.741 139.212 131.379 1.00 60.42  ? 518  ARG A NH1   1 
ATOM   4166  N NH2   . ARG B 2 521  ? 155.935 138.092 133.205 1.00 60.42  ? 518  ARG A NH2   1 
ATOM   4167  N N     . ASN B 2 522  ? 160.969 139.130 136.074 1.00 57.06  ? 519  ASN A N     1 
ATOM   4168  C CA    . ASN B 2 522  ? 160.630 140.061 137.146 1.00 57.06  ? 519  ASN A CA    1 
ATOM   4169  C C     . ASN B 2 522  ? 161.866 140.752 137.705 1.00 57.06  ? 519  ASN A C     1 
ATOM   4170  O O     . ASN B 2 522  ? 161.779 141.898 138.160 1.00 57.06  ? 519  ASN A O     1 
ATOM   4171  C CB    . ASN B 2 522  ? 159.880 139.335 138.260 1.00 57.06  ? 519  ASN A CB    1 
ATOM   4172  C CG    . ASN B 2 522  ? 158.379 139.364 138.063 1.00 57.06  ? 519  ASN A CG    1 
ATOM   4173  O OD1   . ASN B 2 522  ? 157.890 139.361 136.935 1.00 57.06  ? 519  ASN A OD1   1 
ATOM   4174  N ND2   . ASN B 2 522  ? 157.639 139.392 139.165 1.00 57.06  ? 519  ASN A ND2   1 
ATOM   4175  N N     . TYR B 2 523  ? 163.017 140.076 137.692 1.00 58.96  ? 520  TYR A N     1 
ATOM   4176  C CA    . TYR B 2 523  ? 164.250 140.717 138.135 1.00 58.96  ? 520  TYR A CA    1 
ATOM   4177  C C     . TYR B 2 523  ? 164.605 141.900 137.244 1.00 58.96  ? 520  TYR A C     1 
ATOM   4178  O O     . TYR B 2 523  ? 165.011 142.958 137.737 1.00 58.96  ? 520  TYR A O     1 
ATOM   4179  C CB    . TYR B 2 523  ? 165.394 139.705 138.156 1.00 58.96  ? 520  TYR A CB    1 
ATOM   4180  C CG    . TYR B 2 523  ? 166.754 140.330 138.363 1.00 58.96  ? 520  TYR A CG    1 
ATOM   4181  C CD1   . TYR B 2 523  ? 167.153 140.768 139.617 1.00 58.96  ? 520  TYR A CD1   1 
ATOM   4182  C CD2   . TYR B 2 523  ? 167.636 140.488 137.304 1.00 58.96  ? 520  TYR A CD2   1 
ATOM   4183  C CE1   . TYR B 2 523  ? 168.393 141.341 139.812 1.00 58.96  ? 520  TYR A CE1   1 
ATOM   4184  C CE2   . TYR B 2 523  ? 168.878 141.063 137.489 1.00 58.96  ? 520  TYR A CE2   1 
ATOM   4185  C CZ    . TYR B 2 523  ? 169.251 141.487 138.745 1.00 58.96  ? 520  TYR A CZ    1 
ATOM   4186  O OH    . TYR B 2 523  ? 170.487 142.058 138.935 1.00 58.96  ? 520  TYR A OH    1 
ATOM   4187  N N     . ALA B 2 524  ? 164.469 141.735 135.927 1.00 55.71  ? 521  ALA A N     1 
ATOM   4188  C CA    . ALA B 2 524  ? 164.720 142.848 135.016 1.00 55.71  ? 521  ALA A CA    1 
ATOM   4189  C C     . ALA B 2 524  ? 163.699 143.960 135.213 1.00 55.71  ? 521  ALA A C     1 
ATOM   4190  O O     . ALA B 2 524  ? 164.051 145.145 135.200 1.00 55.71  ? 521  ALA A O     1 
ATOM   4191  C CB    . ALA B 2 524  ? 164.710 142.356 133.570 1.00 55.71  ? 521  ALA A CB    1 
ATOM   4192  N N     . THR B 2 525  ? 162.429 143.596 135.397 1.00 51.87  ? 522  THR A N     1 
ATOM   4193  C CA    . THR B 2 525  ? 161.382 144.581 135.632 1.00 51.87  ? 522  THR A CA    1 
ATOM   4194  C C     . THR B 2 525  ? 161.531 145.259 136.991 1.00 51.87  ? 522  THR A C     1 
ATOM   4195  O O     . THR B 2 525  ? 161.111 146.411 137.146 1.00 51.87  ? 522  THR A O     1 
ATOM   4196  C CB    . THR B 2 525  ? 160.011 143.902 135.503 1.00 51.87  ? 522  THR A CB    1 
ATOM   4197  O OG1   . THR B 2 525  ? 159.760 143.598 134.125 1.00 51.87  ? 522  THR A OG1   1 
ATOM   4198  C CG2   . THR B 2 525  ? 158.885 144.790 136.019 1.00 51.87  ? 522  THR A CG2   1 
ATOM   4199  N N     . LYS B 2 526  ? 162.165 144.590 137.954 1.00 51.76  ? 523  LYS A N     1 
ATOM   4200  C CA    . LYS B 2 526  ? 162.235 145.100 139.317 1.00 51.76  ? 523  LYS A CA    1 
ATOM   4201  C C     . LYS B 2 526  ? 162.919 146.461 139.362 1.00 51.76  ? 523  LYS A C     1 
ATOM   4202  O O     . LYS B 2 526  ? 163.759 146.794 138.520 1.00 51.76  ? 523  LYS A O     1 
ATOM   4203  C CB    . LYS B 2 526  ? 162.978 144.111 140.219 1.00 51.76  ? 523  LYS A CB    1 
ATOM   4204  C CG    . LYS B 2 526  ? 164.435 144.468 140.481 1.00 51.76  ? 523  LYS A CG    1 
ATOM   4205  C CD    . LYS B 2 526  ? 165.006 143.671 141.641 1.00 51.76  ? 523  LYS A CD    1 
ATOM   4206  C CE    . LYS B 2 526  ? 166.471 144.004 141.866 1.00 51.76  ? 523  LYS A CE    1 
ATOM   4207  N NZ    . LYS B 2 526  ? 166.679 145.460 142.102 1.00 51.76  ? 523  LYS A NZ    1 
ATOM   4208  N N     . LYS B 2 527  ? 162.533 147.257 140.353 1.00 44.73  ? 524  LYS A N     1 
ATOM   4209  C CA    . LYS B 2 527  ? 163.042 148.595 140.581 1.00 44.73  ? 524  LYS A CA    1 
ATOM   4210  C C     . LYS B 2 527  ? 164.145 148.569 141.637 1.00 44.73  ? 524  LYS A C     1 
ATOM   4211  O O     . LYS B 2 527  ? 164.162 147.686 142.500 1.00 44.73  ? 524  LYS A O     1 
ATOM   4212  C CB    . LYS B 2 527  ? 161.909 149.529 141.024 1.00 43.07  ? 524  LYS A CB    1 
ATOM   4213  C CG    . LYS B 2 527  ? 160.835 149.703 139.958 1.00 43.07  ? 524  LYS A CG    1 
ATOM   4214  C CD    . LYS B 2 527  ? 159.444 149.822 140.557 1.00 43.07  ? 524  LYS A CD    1 
ATOM   4215  C CE    . LYS B 2 527  ? 159.161 151.233 141.031 1.00 43.07  ? 524  LYS A CE    1 
ATOM   4216  N NZ    . LYS B 2 527  ? 159.126 152.199 139.899 1.00 43.07  ? 524  LYS A NZ    1 
ATOM   4217  N N     . PRO B 2 528  ? 165.083 149.522 141.599 1.00 44.73  ? 525  PRO A N     1 
ATOM   4218  C CA    . PRO B 2 528  ? 166.261 149.431 142.475 1.00 44.73  ? 525  PRO A CA    1 
ATOM   4219  C C     . PRO B 2 528  ? 165.966 149.715 143.940 1.00 44.73  ? 525  PRO A C     1 
ATOM   4220  O O     . PRO B 2 528  ? 166.894 149.851 144.744 1.00 44.73  ? 525  PRO A O     1 
ATOM   4221  C CB    . PRO B 2 528  ? 167.210 150.483 141.887 1.00 44.73  ? 525  PRO A CB    1 
ATOM   4222  C CG    . PRO B 2 528  ? 166.316 151.460 141.225 1.00 44.73  ? 525  PRO A CG    1 
ATOM   4223  C CD    . PRO B 2 528  ? 165.171 150.666 140.676 1.00 44.73  ? 525  PRO A CD    1 
ATOM   4224  N N     . TYR B 2 529  ? 164.691 149.807 144.303 1.00 44.73  ? 526  TYR A N     1 
ATOM   4225  C CA    . TYR B 2 529  ? 164.316 150.142 145.668 1.00 44.73  ? 526  TYR A CA    1 
ATOM   4226  C C     . TYR B 2 529  ? 164.293 148.873 146.515 1.00 44.73  ? 526  TYR A C     1 
ATOM   4227  O O     . TYR B 2 529  ? 164.712 147.795 146.085 1.00 44.73  ? 526  TYR A O     1 
ATOM   4228  C CB    . TYR B 2 529  ? 162.954 150.825 145.698 1.00 44.73  ? 526  TYR A CB    1 
ATOM   4229  C CG    . TYR B 2 529  ? 162.777 151.893 144.655 1.00 44.73  ? 526  TYR A CG    1 
ATOM   4230  C CD1   . TYR B 2 529  ? 163.751 152.851 144.444 1.00 44.73  ? 526  TYR A CD1   1 
ATOM   4231  C CD2   . TYR B 2 529  ? 161.614 151.960 143.902 1.00 44.73  ? 526  TYR A CD2   1 
ATOM   4232  C CE1   . TYR B 2 529  ? 163.586 153.827 143.496 1.00 44.73  ? 526  TYR A CE1   1 
ATOM   4233  C CE2   . TYR B 2 529  ? 161.437 152.940 142.953 1.00 44.73  ? 526  TYR A CE2   1 
ATOM   4234  C CZ    . TYR B 2 529  ? 162.427 153.873 142.752 1.00 44.73  ? 526  TYR A CZ    1 
ATOM   4235  O OH    . TYR B 2 529  ? 162.259 154.855 141.804 1.00 44.73  ? 526  TYR A OH    1 
ATOM   4236  N N     . SER B 2 530  ? 163.796 148.998 147.744 1.00 44.73  ? 527  SER A N     1 
ATOM   4237  C CA    . SER B 2 530  ? 163.371 147.841 148.532 1.00 44.73  ? 527  SER A CA    1 
ATOM   4238  C C     . SER B 2 530  ? 162.216 148.327 149.409 1.00 44.73  ? 527  SER A C     1 
ATOM   4239  O O     . SER B 2 530  ? 162.429 148.844 150.507 1.00 44.73  ? 527  SER A O     1 
ATOM   4240  C CB    . SER B 2 530  ? 164.502 147.259 149.365 1.00 44.73  ? 527  SER A CB    1 
ATOM   4241  O OG    . SER B 2 530  ? 164.919 148.168 150.367 1.00 44.73  ? 527  SER A OG    1 
ATOM   4242  N N     . VAL B 2 531  ? 160.992 148.157 148.904 1.00 44.73  ? 528  VAL A N     1 
ATOM   4243  C CA    . VAL B 2 531  ? 159.806 148.559 149.649 1.00 44.73  ? 528  VAL A CA    1 
ATOM   4244  C C     . VAL B 2 531  ? 159.515 147.609 150.801 1.00 44.73  ? 528  VAL A C     1 
ATOM   4245  O O     . VAL B 2 531  ? 158.636 147.888 151.625 1.00 44.73  ? 528  VAL A O     1 
ATOM   4246  C CB    . VAL B 2 531  ? 158.613 148.667 148.673 1.00 44.73  ? 528  VAL A CB    1 
ATOM   4247  C CG1   . VAL B 2 531  ? 157.409 149.331 149.329 1.00 44.73  ? 528  VAL A CG1   1 
ATOM   4248  C CG2   . VAL B 2 531  ? 159.024 149.429 147.426 1.00 44.73  ? 528  VAL A CG2   1 
ATOM   4249  N N     . GLU B 2 532  ? 160.251 146.502 150.889 1.00 44.73  ? 529  GLU A N     1 
ATOM   4250  C CA    . GLU B 2 532  ? 160.054 145.538 151.962 1.00 44.73  ? 529  GLU A CA    1 
ATOM   4251  C C     . GLU B 2 532  ? 160.228 146.203 153.320 1.00 44.73  ? 529  GLU A C     1 
ATOM   4252  O O     . GLU B 2 532  ? 161.165 146.977 153.534 1.00 44.73  ? 529  GLU A O     1 
ATOM   4253  C CB    . GLU B 2 532  ? 161.037 144.377 151.809 1.00 44.73  ? 529  GLU A CB    1 
ATOM   4254  C CG    . GLU B 2 532  ? 160.603 143.330 150.796 1.00 44.73  ? 529  GLU A CG    1 
ATOM   4255  C CD    . GLU B 2 532  ? 161.128 141.946 151.126 1.00 44.73  ? 529  GLU A CD    1 
ATOM   4256  O OE1   . GLU B 2 532  ? 162.080 141.845 151.928 1.00 44.73  ? 529  GLU A OE1   1 
ATOM   4257  O OE2   . GLU B 2 532  ? 160.588 140.960 150.582 1.00 44.73  ? 529  GLU A OE2   1 
ATOM   4258  N N     . LYS B 2 533  ? 159.317 145.894 154.238 1.00 44.73  ? 530  LYS A N     1 
ATOM   4259  C CA    . LYS B 2 533  ? 159.279 146.533 155.544 1.00 44.73  ? 530  LYS A CA    1 
ATOM   4260  C C     . LYS B 2 533  ? 158.690 145.556 156.549 1.00 44.73  ? 530  LYS A C     1 
ATOM   4261  O O     . LYS B 2 533  ? 158.114 144.529 156.180 1.00 44.73  ? 530  LYS A O     1 
ATOM   4262  C CB    . LYS B 2 533  ? 158.456 147.824 155.507 1.00 44.73  ? 530  LYS A CB    1 
ATOM   4263  C CG    . LYS B 2 533  ? 156.983 147.590 155.229 1.00 44.73  ? 530  LYS A CG    1 
ATOM   4264  C CD    . LYS B 2 533  ? 156.295 148.851 154.753 1.00 44.73  ? 530  LYS A CD    1 
ATOM   4265  C CE    . LYS B 2 533  ? 154.792 148.659 154.694 1.00 44.73  ? 530  LYS A CE    1 
ATOM   4266  N NZ    . LYS B 2 533  ? 154.418 147.526 153.806 1.00 44.73  ? 530  LYS A NZ    1 
ATOM   4267  N N     . PHE B 2 534  ? 158.838 145.885 157.829 1.00 44.73  ? 531  PHE A N     1 
ATOM   4268  C CA    . PHE B 2 534  ? 158.311 145.055 158.900 1.00 44.73  ? 531  PHE A CA    1 
ATOM   4269  C C     . PHE B 2 534  ? 157.539 145.909 159.894 1.00 44.73  ? 531  PHE A C     1 
ATOM   4270  O O     . PHE B 2 534  ? 157.820 147.098 160.070 1.00 44.73  ? 531  PHE A O     1 
ATOM   4271  C CB    . PHE B 2 534  ? 159.422 144.281 159.621 1.00 44.73  ? 531  PHE A CB    1 
ATOM   4272  C CG    . PHE B 2 534  ? 160.628 145.106 159.948 1.00 44.73  ? 531  PHE A CG    1 
ATOM   4273  C CD1   . PHE B 2 534  ? 160.697 145.817 161.131 1.00 44.73  ? 531  PHE A CD1   1 
ATOM   4274  C CD2   . PHE B 2 534  ? 161.702 145.159 159.078 1.00 44.73  ? 531  PHE A CD2   1 
ATOM   4275  C CE1   . PHE B 2 534  ? 161.810 146.569 161.437 1.00 44.73  ? 531  PHE A CE1   1 
ATOM   4276  C CE2   . PHE B 2 534  ? 162.817 145.911 159.378 1.00 44.73  ? 531  PHE A CE2   1 
ATOM   4277  C CZ    . PHE B 2 534  ? 162.871 146.616 160.560 1.00 44.73  ? 531  PHE A CZ    1 
ATOM   4278  N N     . LYS B 2 535  ? 156.564 145.281 160.544 1.00 44.73  ? 532  LYS A N     1 
ATOM   4279  C CA    . LYS B 2 535  ? 155.649 145.985 161.432 1.00 44.73  ? 532  LYS A CA    1 
ATOM   4280  C C     . LYS B 2 535  ? 156.276 146.170 162.806 1.00 44.73  ? 532  LYS A C     1 
ATOM   4281  O O     . LYS B 2 535  ? 156.828 145.226 163.379 1.00 44.73  ? 532  LYS A O     1 
ATOM   4282  C CB    . LYS B 2 535  ? 154.335 145.213 161.546 1.00 44.73  ? 532  LYS A CB    1 
ATOM   4283  C CG    . LYS B 2 535  ? 153.542 145.493 162.810 1.00 44.73  ? 532  LYS A CG    1 
ATOM   4284  C CD    . LYS B 2 535  ? 152.105 145.021 162.666 1.00 44.73  ? 532  LYS A CD    1 
ATOM   4285  C CE    . LYS B 2 535  ? 151.406 144.956 164.013 1.00 44.73  ? 532  LYS A CE    1 
ATOM   4286  N NZ    . LYS B 2 535  ? 151.280 146.301 164.638 1.00 44.73  ? 532  LYS A NZ    1 
ATOM   4287  N N     . LEU B 2 536  ? 156.189 147.389 163.331 1.00 44.73  ? 533  LEU A N     1 
ATOM   4288  C CA    . LEU B 2 536  ? 156.709 147.708 164.652 1.00 44.73  ? 533  LEU A CA    1 
ATOM   4289  C C     . LEU B 2 536  ? 155.620 147.493 165.695 1.00 44.73  ? 533  LEU A C     1 
ATOM   4290  O O     . LEU B 2 536  ? 154.523 148.046 165.580 1.00 44.73  ? 533  LEU A O     1 
ATOM   4291  C CB    . LEU B 2 536  ? 157.209 149.150 164.706 1.00 44.73  ? 533  LEU A CB    1 
ATOM   4292  C CG    . LEU B 2 536  ? 158.368 149.528 163.785 1.00 44.73  ? 533  LEU A CG    1 
ATOM   4293  C CD1   . LEU B 2 536  ? 158.716 150.994 163.956 1.00 44.73  ? 533  LEU A CD1   1 
ATOM   4294  C CD2   . LEU B 2 536  ? 159.580 148.657 164.055 1.00 44.73  ? 533  LEU A CD2   1 
ATOM   4295  N N     . ASN B 2 537  ? 155.929 146.691 166.711 1.00 44.73  ? 534  ASN A N     1 
ATOM   4296  C CA    . ASN B 2 537  ? 154.985 146.383 167.775 1.00 44.73  ? 534  ASN A CA    1 
ATOM   4297  C C     . ASN B 2 537  ? 155.252 147.135 169.066 1.00 44.73  ? 534  ASN A C     1 
ATOM   4298  O O     . ASN B 2 537  ? 154.310 147.394 169.816 1.00 44.73  ? 534  ASN A O     1 
ATOM   4299  C CB    . ASN B 2 537  ? 154.996 144.880 168.077 1.00 44.73  ? 534  ASN A CB    1 
ATOM   4300  C CG    . ASN B 2 537  ? 154.230 144.077 167.054 1.00 44.73  ? 534  ASN A CG    1 
ATOM   4301  O OD1   . ASN B 2 537  ? 153.089 144.397 166.727 1.00 44.73  ? 534  ASN A OD1   1 
ATOM   4302  N ND2   . ASN B 2 537  ? 154.854 143.024 166.541 1.00 44.73  ? 534  ASN A ND2   1 
ATOM   4303  N N     . PHE B 2 538  ? 156.509 147.490 169.336 1.00 44.73  ? 535  PHE A N     1 
ATOM   4304  C CA    . PHE B 2 538  ? 156.905 148.098 170.605 1.00 44.73  ? 535  PHE A CA    1 
ATOM   4305  C C     . PHE B 2 538  ? 156.480 147.224 171.782 1.00 44.73  ? 535  PHE A C     1 
ATOM   4306  O O     . PHE B 2 538  ? 156.023 147.713 172.818 1.00 44.73  ? 535  PHE A O     1 
ATOM   4307  C CB    . PHE B 2 538  ? 156.349 149.515 170.738 1.00 44.73  ? 535  PHE A CB    1 
ATOM   4308  C CG    . PHE B 2 538  ? 157.049 150.519 169.874 1.00 44.73  ? 535  PHE A CG    1 
ATOM   4309  C CD1   . PHE B 2 538  ? 156.685 150.685 168.552 1.00 44.73  ? 535  PHE A CD1   1 
ATOM   4310  C CD2   . PHE B 2 538  ? 158.076 151.290 170.383 1.00 44.73  ? 535  PHE A CD2   1 
ATOM   4311  C CE1   . PHE B 2 538  ? 157.328 151.606 167.754 1.00 44.73  ? 535  PHE A CE1   1 
ATOM   4312  C CE2   . PHE B 2 538  ? 158.724 152.212 169.588 1.00 44.73  ? 535  PHE A CE2   1 
ATOM   4313  C CZ    . PHE B 2 538  ? 158.349 152.370 168.272 1.00 44.73  ? 535  PHE A CZ    1 
ATOM   4314  N N     . GLN B 2 539  ? 156.633 145.910 171.610 1.00 44.73  ? 536  GLN A N     1 
ATOM   4315  C CA    . GLN B 2 539  ? 156.362 144.918 172.651 1.00 44.73  ? 536  GLN A CA    1 
ATOM   4316  C C     . GLN B 2 539  ? 154.928 145.000 173.167 1.00 44.73  ? 536  GLN A C     1 
ATOM   4317  O O     . GLN B 2 539  ? 154.660 144.707 174.334 1.00 44.73  ? 536  GLN A O     1 
ATOM   4318  C CB    . GLN B 2 539  ? 157.358 145.043 173.808 1.00 44.73  ? 536  GLN A CB    1 
ATOM   4319  C CG    . GLN B 2 539  ? 158.800 144.796 173.398 1.00 44.73  ? 536  GLN A CG    1 
ATOM   4320  C CD    . GLN B 2 539  ? 159.781 145.681 174.137 1.00 44.73  ? 536  GLN A CD    1 
ATOM   4321  O OE1   . GLN B 2 539  ? 159.386 146.568 174.894 1.00 44.73  ? 536  GLN A OE1   1 
ATOM   4322  N NE2   . GLN B 2 539  ? 161.069 145.447 173.919 1.00 44.73  ? 536  GLN A NE2   1 
ATOM   4323  N N     . MET B 2 540  ? 153.994 145.392 172.304 1.00 44.73  ? 537  MET A N     1 
ATOM   4324  C CA    . MET B 2 540  ? 152.577 145.428 172.648 1.00 44.73  ? 537  MET A CA    1 
ATOM   4325  C C     . MET B 2 540  ? 151.787 144.690 171.578 1.00 44.73  ? 537  MET A C     1 
ATOM   4326  O O     . MET B 2 540  ? 151.843 145.077 170.392 1.00 44.73  ? 537  MET A O     1 
ATOM   4327  C CB    . MET B 2 540  ? 152.076 146.864 172.801 1.00 44.73  ? 537  MET A CB    1 
ATOM   4328  C CG    . MET B 2 540  ? 152.665 147.589 173.990 1.00 44.73  ? 537  MET A CG    1 
ATOM   4329  S SD    . MET B 2 540  ? 152.066 149.277 174.143 1.00 44.73  ? 537  MET A SD    1 
ATOM   4330  C CE    . MET B 2 540  ? 153.025 149.809 175.550 1.00 44.73  ? 537  MET A CE    1 
ATOM   4331  N N     . PRO B 2 541  ? 151.044 143.638 171.931 1.00 44.73  ? 538  PRO A N     1 
ATOM   4332  C CA    . PRO B 2 541  ? 150.234 142.938 170.924 1.00 44.73  ? 538  PRO A CA    1 
ATOM   4333  C C     . PRO B 2 541  ? 149.001 143.710 170.491 1.00 44.73  ? 538  PRO A C     1 
ATOM   4334  O O     . PRO B 2 541  ? 148.390 143.343 169.479 1.00 44.73  ? 538  PRO A O     1 
ATOM   4335  C CB    . PRO B 2 541  ? 149.849 141.625 171.622 1.00 44.73  ? 538  PRO A CB    1 
ATOM   4336  C CG    . PRO B 2 541  ? 150.277 141.761 173.063 1.00 44.73  ? 538  PRO A CG    1 
ATOM   4337  C CD    . PRO B 2 541  ? 150.805 143.138 173.292 1.00 44.73  ? 538  PRO A CD    1 
ATOM   4338  N N     . THR B 2 542  ? 148.616 144.762 171.214 1.00 44.73  ? 539  THR A N     1 
ATOM   4339  C CA    . THR B 2 542  ? 147.435 145.551 170.888 1.00 44.73  ? 539  THR A CA    1 
ATOM   4340  C C     . THR B 2 542  ? 147.786 147.017 170.657 1.00 44.73  ? 539  THR A C     1 
ATOM   4341  O O     . THR B 2 542  ? 147.000 147.907 170.982 1.00 44.73  ? 539  THR A O     1 
ATOM   4342  C CB    . THR B 2 542  ? 146.379 145.430 171.986 1.00 44.73  ? 539  THR A CB    1 
ATOM   4343  O OG1   . THR B 2 542  ? 146.909 145.931 173.219 1.00 44.73  ? 539  THR A OG1   1 
ATOM   4344  C CG2   . THR B 2 542  ? 145.959 143.980 172.170 1.00 44.73  ? 539  THR A CG2   1 
ATOM   4345  N N     . LEU B 2 543  ? 148.963 147.281 170.096 1.00 44.73  ? 540  LEU A N     1 
ATOM   4346  C CA    . LEU B 2 543  ? 149.364 148.654 169.821 1.00 44.73  ? 540  LEU A CA    1 
ATOM   4347  C C     . LEU B 2 543  ? 148.491 149.245 168.721 1.00 44.73  ? 540  LEU A C     1 
ATOM   4348  O O     . LEU B 2 543  ? 148.337 148.651 167.649 1.00 44.73  ? 540  LEU A O     1 
ATOM   4349  C CB    . LEU B 2 543  ? 150.836 148.708 169.419 1.00 44.73  ? 540  LEU A CB    1 
ATOM   4350  C CG    . LEU B 2 543  ? 151.373 150.077 168.999 1.00 44.73  ? 540  LEU A CG    1 
ATOM   4351  C CD1   . LEU B 2 543  ? 151.436 151.016 170.188 1.00 44.73  ? 540  LEU A CD1   1 
ATOM   4352  C CD2   . LEU B 2 543  ? 152.739 149.941 168.350 1.00 44.73  ? 540  LEU A CD2   1 
ATOM   4353  N N     . ALA B 2 544  ? 147.917 150.417 168.996 1.00 44.73  ? 541  ALA A N     1 
ATOM   4354  C CA    . ALA B 2 544  ? 147.048 151.126 168.058 1.00 44.73  ? 541  ALA A CA    1 
ATOM   4355  C C     . ALA B 2 544  ? 145.847 150.282 167.643 1.00 44.73  ? 541  ALA A C     1 
ATOM   4356  O O     . ALA B 2 544  ? 145.324 150.428 166.536 1.00 44.73  ? 541  ALA A O     1 
ATOM   4357  C CB    . ALA B 2 544  ? 147.824 151.596 166.825 1.00 44.73  ? 541  ALA A CB    1 
ATOM   4358  N N     . SER B 2 545  ? 145.398 149.393 168.529 1.00 44.73  ? 542  SER A N     1 
ATOM   4359  C CA    . SER B 2 545  ? 144.239 148.555 168.255 1.00 44.73  ? 542  SER A CA    1 
ATOM   4360  C C     . SER B 2 545  ? 142.923 149.221 168.632 1.00 44.73  ? 542  SER A C     1 
ATOM   4361  O O     . SER B 2 545  ? 141.860 148.679 168.312 1.00 44.73  ? 542  SER A O     1 
ATOM   4362  C CB    . SER B 2 545  ? 144.367 147.224 168.999 1.00 44.73  ? 542  SER A CB    1 
ATOM   4363  O OG    . SER B 2 545  ? 143.212 146.424 168.815 1.00 44.73  ? 542  SER A OG    1 
ATOM   4364  N N     . GLY B 2 546  ? 142.970 150.368 169.301 1.00 44.73  ? 543  GLY A N     1 
ATOM   4365  C CA    . GLY B 2 546  ? 141.775 151.087 169.696 1.00 44.73  ? 543  GLY A CA    1 
ATOM   4366  C C     . GLY B 2 546  ? 142.121 152.424 170.315 1.00 44.73  ? 543  GLY A C     1 
ATOM   4367  O O     . GLY B 2 546  ? 143.041 152.513 171.133 1.00 44.73  ? 543  GLY A O     1 
ATOM   4368  N N     . TRP B 2 547  ? 141.396 153.471 169.936 1.00 44.73  ? 544  TRP A N     1 
ATOM   4369  C CA    . TRP B 2 547  ? 141.722 154.826 170.356 1.00 44.73  ? 544  TRP A CA    1 
ATOM   4370  C C     . TRP B 2 547  ? 140.989 155.259 171.619 1.00 44.73  ? 544  TRP A C     1 
ATOM   4371  O O     . TRP B 2 547  ? 141.212 156.379 172.087 1.00 44.73  ? 544  TRP A O     1 
ATOM   4372  C CB    . TRP B 2 547  ? 141.414 155.809 169.222 1.00 44.73  ? 544  TRP A CB    1 
ATOM   4373  C CG    . TRP B 2 547  ? 142.029 155.415 167.921 1.00 44.73  ? 544  TRP A CG    1 
ATOM   4374  C CD1   . TRP B 2 547  ? 141.401 154.829 166.864 1.00 44.73  ? 544  TRP A CD1   1 
ATOM   4375  C CD2   . TRP B 2 547  ? 143.398 155.574 167.536 1.00 44.73  ? 544  TRP A CD2   1 
ATOM   4376  N NE1   . TRP B 2 547  ? 142.293 154.613 165.843 1.00 44.73  ? 544  TRP A NE1   1 
ATOM   4377  C CE2   . TRP B 2 547  ? 143.527 155.061 166.232 1.00 44.73  ? 544  TRP A CE2   1 
ATOM   4378  C CE3   . TRP B 2 547  ? 144.526 156.101 168.168 1.00 44.73  ? 544  TRP A CE3   1 
ATOM   4379  C CZ2   . TRP B 2 547  ? 144.739 155.061 165.549 1.00 44.73  ? 544  TRP A CZ2   1 
ATOM   4380  C CZ3   . TRP B 2 547  ? 145.727 156.098 167.489 1.00 44.73  ? 544  TRP A CZ3   1 
ATOM   4381  C CH2   . TRP B 2 547  ? 145.825 155.582 166.194 1.00 44.73  ? 544  TRP A CH2   1 
ATOM   4382  N N     . ASP B 2 548  ? 140.143 154.401 172.185 1.00 44.73  ? 545  ASP A N     1 
ATOM   4383  C CA    . ASP B 2 548  ? 139.307 154.797 173.311 1.00 44.73  ? 545  ASP A CA    1 
ATOM   4384  C C     . ASP B 2 548  ? 140.160 155.216 174.502 1.00 44.73  ? 545  ASP A C     1 
ATOM   4385  O O     . ASP B 2 548  ? 141.220 154.641 174.764 1.00 44.73  ? 545  ASP A O     1 
ATOM   4386  C CB    . ASP B 2 548  ? 138.381 153.647 173.704 1.00 44.73  ? 545  ASP A CB    1 
ATOM   4387  C CG    . ASP B 2 548  ? 137.243 154.089 174.604 1.00 44.73  ? 545  ASP A CG    1 
ATOM   4388  O OD1   . ASP B 2 548  ? 137.232 155.261 175.033 1.00 44.73  ? 545  ASP A OD1   1 
ATOM   4389  O OD2   . ASP B 2 548  ? 136.353 153.259 174.883 1.00 44.73  ? 545  ASP A OD2   1 
ATOM   4390  N N     . VAL B 2 549  ? 139.687 156.235 175.223 1.00 44.73  ? 546  VAL A N     1 
ATOM   4391  C CA    . VAL B 2 549  ? 140.454 156.779 176.338 1.00 44.73  ? 546  VAL A CA    1 
ATOM   4392  C C     . VAL B 2 549  ? 140.568 155.766 177.470 1.00 44.73  ? 546  VAL A C     1 
ATOM   4393  O O     . VAL B 2 549  ? 141.598 155.706 178.153 1.00 44.73  ? 546  VAL A O     1 
ATOM   4394  C CB    . VAL B 2 549  ? 139.834 158.107 176.814 1.00 44.73  ? 546  VAL A CB    1 
ATOM   4395  C CG1   . VAL B 2 549  ? 138.415 157.897 177.322 1.00 44.73  ? 546  VAL A CG1   1 
ATOM   4396  C CG2   . VAL B 2 549  ? 140.703 158.752 177.883 1.00 44.73  ? 546  VAL A CG2   1 
ATOM   4397  N N     . ASN B 2 550  ? 139.532 154.953 177.692 1.00 44.73  ? 547  ASN A N     1 
ATOM   4398  C CA    . ASN B 2 550  ? 139.607 153.937 178.734 1.00 44.73  ? 547  ASN A CA    1 
ATOM   4399  C C     . ASN B 2 550  ? 140.622 152.852 178.408 1.00 44.73  ? 547  ASN A C     1 
ATOM   4400  O O     . ASN B 2 550  ? 141.033 152.113 179.308 1.00 44.73  ? 547  ASN A O     1 
ATOM   4401  C CB    . ASN B 2 550  ? 138.232 153.313 178.967 1.00 44.73  ? 547  ASN A CB    1 
ATOM   4402  C CG    . ASN B 2 550  ? 137.329 154.196 179.800 1.00 44.73  ? 547  ASN A CG    1 
ATOM   4403  O OD1   . ASN B 2 550  ? 137.230 155.399 179.567 1.00 44.73  ? 547  ASN A OD1   1 
ATOM   4404  N ND2   . ASN B 2 550  ? 136.664 153.600 180.782 1.00 44.73  ? 547  ASN A ND2   1 
ATOM   4405  N N     . LYS B 2 551  ? 141.033 152.741 177.146 1.00 44.73  ? 548  LYS A N     1 
ATOM   4406  C CA    . LYS B 2 551  ? 142.104 151.841 176.743 1.00 44.73  ? 548  LYS A CA    1 
ATOM   4407  C C     . LYS B 2 551  ? 143.397 152.597 176.462 1.00 44.73  ? 548  LYS A C     1 
ATOM   4408  O O     . LYS B 2 551  ? 144.180 152.188 175.599 1.00 44.73  ? 548  LYS A O     1 
ATOM   4409  C CB    . LYS B 2 551  ? 141.675 151.024 175.526 1.00 44.73  ? 548  LYS A CB    1 
ATOM   4410  C CG    . LYS B 2 551  ? 140.378 150.261 175.737 1.00 44.73  ? 548  LYS A CG    1 
ATOM   4411  C CD    . LYS B 2 551  ? 140.636 148.811 176.094 1.00 44.73  ? 548  LYS A CD    1 
ATOM   4412  C CE    . LYS B 2 551  ? 141.419 148.108 175.000 1.00 44.73  ? 548  LYS A CE    1 
ATOM   4413  N NZ    . LYS B 2 551  ? 141.851 146.746 175.413 1.00 44.73  ? 548  LYS A NZ    1 
ATOM   4414  N N     . GLU B 2 552  ? 143.619 153.709 177.170 1.00 44.73  ? 549  GLU A N     1 
ATOM   4415  C CA    . GLU B 2 552  ? 144.855 154.471 177.027 1.00 44.73  ? 549  GLU A CA    1 
ATOM   4416  C C     . GLU B 2 552  ? 146.078 153.602 177.286 1.00 44.73  ? 549  GLU A C     1 
ATOM   4417  O O     . GLU B 2 552  ? 146.993 153.539 176.458 1.00 44.73  ? 549  GLU A O     1 
ATOM   4418  C CB    . GLU B 2 552  ? 144.830 155.659 177.993 1.00 44.73  ? 549  GLU A CB    1 
ATOM   4419  C CG    . GLU B 2 552  ? 145.795 156.801 177.700 1.00 44.73  ? 549  GLU A CG    1 
ATOM   4420  C CD    . GLU B 2 552  ? 145.762 157.298 176.268 1.00 44.73  ? 549  GLU A CD    1 
ATOM   4421  O OE1   . GLU B 2 552  ? 144.738 157.123 175.573 1.00 44.73  ? 549  GLU A OE1   1 
ATOM   4422  O OE2   . GLU B 2 552  ? 146.768 157.903 175.849 1.00 44.73  ? 549  GLU A OE2   1 
ATOM   4423  N N     . LYS B 2 553  ? 146.107 152.923 178.433 1.00 44.73  ? 550  LYS A N     1 
ATOM   4424  C CA    . LYS B 2 553  ? 147.227 152.048 178.753 1.00 44.73  ? 550  LYS A CA    1 
ATOM   4425  C C     . LYS B 2 553  ? 147.239 150.818 177.859 1.00 44.73  ? 550  LYS A C     1 
ATOM   4426  O O     . LYS B 2 553  ? 148.307 150.328 177.476 1.00 44.73  ? 550  LYS A O     1 
ATOM   4427  C CB    . LYS B 2 553  ? 147.154 151.629 180.219 1.00 44.73  ? 550  LYS A CB    1 
ATOM   4428  C CG    . LYS B 2 553  ? 146.864 152.766 181.182 1.00 44.73  ? 550  LYS A CG    1 
ATOM   4429  C CD    . LYS B 2 553  ? 147.103 152.327 182.617 1.00 44.73  ? 550  LYS A CD    1 
ATOM   4430  C CE    . LYS B 2 553  ? 148.470 151.687 182.781 1.00 44.73  ? 550  LYS A CE    1 
ATOM   4431  N NZ    . LYS B 2 553  ? 148.520 150.786 183.965 1.00 44.73  ? 550  LYS A NZ    1 
ATOM   4432  N N     . CYS B 2 554  ? 146.054 150.303 177.527 1.00 44.73  ? 551  CYS A N     1 
ATOM   4433  C CA    . CYS B 2 554  ? 145.947 148.992 176.899 1.00 44.73  ? 551  CYS A CA    1 
ATOM   4434  C C     . CYS B 2 554  ? 146.575 148.998 175.512 1.00 44.73  ? 551  CYS A C     1 
ATOM   4435  O O     . CYS B 2 554  ? 147.257 148.044 175.126 1.00 44.73  ? 551  CYS A O     1 
ATOM   4436  C CB    . CYS B 2 554  ? 144.476 148.594 176.807 1.00 41.02  ? 551  CYS A CB    1 
ATOM   4437  S SG    . CYS B 2 554  ? 143.647 148.358 178.406 1.00 41.02  ? 551  CYS A SG    1 
ATOM   4438  N N     . ASN B 2 555  ? 146.349 150.064 174.748 1.00 44.73  ? 552  ASN A N     1 
ATOM   4439  C CA    . ASN B 2 555  ? 146.830 150.162 173.375 1.00 44.73  ? 552  ASN A CA    1 
ATOM   4440  C C     . ASN B 2 555  ? 148.036 151.084 173.243 1.00 44.73  ? 552  ASN A C     1 
ATOM   4441  O O     . ASN B 2 555  ? 148.980 150.770 172.510 1.00 44.73  ? 552  ASN A O     1 
ATOM   4442  C CB    . ASN B 2 555  ? 145.704 150.650 172.466 1.00 44.73  ? 552  ASN A CB    1 
ATOM   4443  C CG    . ASN B 2 555  ? 144.444 149.833 172.626 1.00 44.73  ? 552  ASN A CG    1 
ATOM   4444  O OD1   . ASN B 2 555  ? 144.497 148.626 172.858 1.00 44.73  ? 552  ASN A OD1   1 
ATOM   4445  N ND2   . ASN B 2 555  ? 143.297 150.487 172.512 1.00 44.73  ? 552  ASN A ND2   1 
ATOM   4446  N N     . GLY B 2 556  ? 148.017 152.223 173.930 1.00 44.73  ? 553  GLY A N     1 
ATOM   4447  C CA    . GLY B 2 556  ? 149.130 153.151 173.905 1.00 44.73  ? 553  GLY A CA    1 
ATOM   4448  C C     . GLY B 2 556  ? 149.381 153.812 172.567 1.00 44.73  ? 553  GLY A C     1 
ATOM   4449  O O     . GLY B 2 556  ? 150.507 153.778 172.064 1.00 44.73  ? 553  GLY A O     1 
ATOM   4450  N N     . ALA B 2 557  ? 148.347 154.402 171.971 1.00 44.73  ? 554  ALA A N     1 
ATOM   4451  C CA    . ALA B 2 557  ? 148.507 155.135 170.718 1.00 44.73  ? 554  ALA A CA    1 
ATOM   4452  C C     . ALA B 2 557  ? 147.482 156.256 170.668 1.00 44.73  ? 554  ALA A C     1 
ATOM   4453  O O     . ALA B 2 557  ? 146.276 155.992 170.686 1.00 44.73  ? 554  ALA A O     1 
ATOM   4454  C CB    . ALA B 2 557  ? 148.353 154.211 169.510 1.00 44.73  ? 554  ALA A CB    1 
ATOM   4455  N N     . ILE B 2 558  ? 147.962 157.501 170.612 1.00 44.73  ? 555  ILE A N     1 
ATOM   4456  C CA    . ILE B 2 558  ? 147.109 158.682 170.555 1.00 44.73  ? 555  ILE A CA    1 
ATOM   4457  C C     . ILE B 2 558  ? 147.695 159.687 169.573 1.00 44.73  ? 555  ILE A C     1 
ATOM   4458  O O     . ILE B 2 558  ? 148.855 159.595 169.169 1.00 44.73  ? 555  ILE A O     1 
ATOM   4459  C CB    . ILE B 2 558  ? 146.921 159.339 171.941 1.00 44.73  ? 555  ILE A CB    1 
ATOM   4460  C CG1   . ILE B 2 558  ? 148.267 159.813 172.493 1.00 44.73  ? 555  ILE A CG1   1 
ATOM   4461  C CG2   . ILE B 2 558  ? 146.199 158.402 172.890 1.00 44.73  ? 555  ILE A CG2   1 
ATOM   4462  C CD1   . ILE B 2 558  ? 148.151 160.664 173.728 1.00 44.73  ? 555  ILE A CD1   1 
ATOM   4463  N N     . LEU B 2 559  ? 146.870 160.659 169.193 1.00 44.73  ? 556  LEU A N     1 
ATOM   4464  C CA    . LEU B 2 559  ? 147.230 161.659 168.198 1.00 44.73  ? 556  LEU A CA    1 
ATOM   4465  C C     . LEU B 2 559  ? 147.182 163.053 168.806 1.00 44.73  ? 556  LEU A C     1 
ATOM   4466  O O     . LEU B 2 559  ? 146.395 163.317 169.719 1.00 44.73  ? 556  LEU A O     1 
ATOM   4467  C CB    . LEU B 2 559  ? 146.301 161.592 166.980 1.00 44.73  ? 556  LEU A CB    1 
ATOM   4468  C CG    . LEU B 2 559  ? 146.403 160.327 166.128 1.00 44.73  ? 556  LEU A CG    1 
ATOM   4469  C CD1   . LEU B 2 559  ? 145.341 160.303 165.048 1.00 44.73  ? 556  LEU A CD1   1 
ATOM   4470  C CD2   . LEU B 2 559  ? 147.778 160.242 165.507 1.00 44.73  ? 556  LEU A CD2   1 
ATOM   4471  N N     . PHE B 2 560  ? 148.032 163.937 168.291 1.00 44.73  ? 557  PHE A N     1 
ATOM   4472  C CA    . PHE B 2 560  ? 148.090 165.330 168.704 1.00 44.73  ? 557  PHE A CA    1 
ATOM   4473  C C     . PHE B 2 560  ? 147.973 166.224 167.479 1.00 44.73  ? 557  PHE A C     1 
ATOM   4474  O O     . PHE B 2 560  ? 148.488 165.892 166.406 1.00 44.73  ? 557  PHE A O     1 
ATOM   4475  C CB    . PHE B 2 560  ? 149.398 165.644 169.437 1.00 44.73  ? 557  PHE A CB    1 
ATOM   4476  C CG    . PHE B 2 560  ? 149.537 164.954 170.760 1.00 44.73  ? 557  PHE A CG    1 
ATOM   4477  C CD1   . PHE B 2 560  ? 148.923 165.462 171.889 1.00 44.73  ? 557  PHE A CD1   1 
ATOM   4478  C CD2   . PHE B 2 560  ? 150.296 163.804 170.878 1.00 44.73  ? 557  PHE A CD2   1 
ATOM   4479  C CE1   . PHE B 2 560  ? 149.057 164.832 173.106 1.00 44.73  ? 557  PHE A CE1   1 
ATOM   4480  C CE2   . PHE B 2 560  ? 150.432 163.171 172.092 1.00 44.73  ? 557  PHE A CE2   1 
ATOM   4481  C CZ    . PHE B 2 560  ? 149.812 163.686 173.208 1.00 44.73  ? 557  PHE A CZ    1 
ATOM   4482  N N     . VAL B 2 561  ? 147.294 167.356 167.639 1.00 44.73  ? 558  VAL A N     1 
ATOM   4483  C CA    . VAL B 2 561  ? 147.211 168.374 166.600 1.00 44.73  ? 558  VAL A CA    1 
ATOM   4484  C C     . VAL B 2 561  ? 147.697 169.697 167.180 1.00 44.73  ? 558  VAL A C     1 
ATOM   4485  O O     . VAL B 2 561  ? 147.297 170.092 168.282 1.00 44.73  ? 558  VAL A O     1 
ATOM   4486  C CB    . VAL B 2 561  ? 145.784 168.491 166.017 1.00 44.73  ? 558  VAL A CB    1 
ATOM   4487  C CG1   . VAL B 2 561  ? 144.787 168.973 167.058 1.00 44.73  ? 558  VAL A CG1   1 
ATOM   4488  C CG2   . VAL B 2 561  ? 145.780 169.413 164.808 1.00 44.73  ? 558  VAL A CG2   1 
ATOM   4489  N N     . LYS B 2 562  ? 148.594 170.361 166.455 1.00 44.73  ? 559  LYS A N     1 
ATOM   4490  C CA    . LYS B 2 562  ? 149.188 171.608 166.931 1.00 44.73  ? 559  LYS A CA    1 
ATOM   4491  C C     . LYS B 2 562  ? 149.670 172.405 165.731 1.00 44.73  ? 559  LYS A C     1 
ATOM   4492  O O     . LYS B 2 562  ? 150.524 171.927 164.977 1.00 44.73  ? 559  LYS A O     1 
ATOM   4493  C CB    . LYS B 2 562  ? 150.340 171.330 167.896 1.00 44.73  ? 559  LYS A CB    1 
ATOM   4494  C CG    . LYS B 2 562  ? 151.319 172.483 168.051 1.00 44.73  ? 559  LYS A CG    1 
ATOM   4495  C CD    . LYS B 2 562  ? 152.568 172.047 168.796 1.00 44.73  ? 559  LYS A CD    1 
ATOM   4496  C CE    . LYS B 2 562  ? 153.477 173.227 169.087 1.00 44.73  ? 559  LYS A CE    1 
ATOM   4497  N NZ    . LYS B 2 562  ? 154.599 172.854 169.990 1.00 44.73  ? 559  LYS A NZ    1 
ATOM   4498  N N     . ASN B 2 563  ? 149.125 173.609 165.556 1.00 44.73  ? 560  ASN A N     1 
ATOM   4499  C CA    . ASN B 2 563  ? 149.501 174.508 164.464 1.00 44.73  ? 560  ASN A CA    1 
ATOM   4500  C C     . ASN B 2 563  ? 149.316 173.856 163.097 1.00 44.73  ? 560  ASN A C     1 
ATOM   4501  O O     . ASN B 2 563  ? 150.108 174.080 162.179 1.00 44.73  ? 560  ASN A O     1 
ATOM   4502  C CB    . ASN B 2 563  ? 150.940 175.007 164.626 1.00 44.73  ? 560  ASN A CB    1 
ATOM   4503  C CG    . ASN B 2 563  ? 151.095 175.970 165.785 1.00 44.73  ? 560  ASN A CG    1 
ATOM   4504  O OD1   . ASN B 2 563  ? 150.162 176.184 166.558 1.00 44.73  ? 560  ASN A OD1   1 
ATOM   4505  N ND2   . ASN B 2 563  ? 152.278 176.559 165.910 1.00 44.73  ? 560  ASN A ND2   1 
ATOM   4506  N N     . GLY B 2 564  ? 148.271 173.046 162.950 1.00 44.73  ? 561  GLY A N     1 
ATOM   4507  C CA    . GLY B 2 564  ? 147.984 172.393 161.692 1.00 44.73  ? 561  GLY A CA    1 
ATOM   4508  C C     . GLY B 2 564  ? 148.824 171.173 161.394 1.00 44.73  ? 561  GLY A C     1 
ATOM   4509  O O     . GLY B 2 564  ? 148.675 170.589 160.313 1.00 44.73  ? 561  GLY A O     1 
ATOM   4510  N N     . LEU B 2 565  ? 149.698 170.767 162.308 1.00 44.73  ? 562  LEU A N     1 
ATOM   4511  C CA    . LEU B 2 565  ? 150.557 169.607 162.127 1.00 44.73  ? 562  LEU A CA    1 
ATOM   4512  C C     . LEU B 2 565  ? 150.087 168.494 163.051 1.00 44.73  ? 562  LEU A C     1 
ATOM   4513  O O     . LEU B 2 565  ? 149.899 168.717 164.252 1.00 44.73  ? 562  LEU A O     1 
ATOM   4514  C CB    . LEU B 2 565  ? 152.018 169.958 162.412 1.00 44.73  ? 562  LEU A CB    1 
ATOM   4515  C CG    . LEU B 2 565  ? 152.878 170.418 161.231 1.00 44.73  ? 562  LEU A CG    1 
ATOM   4516  C CD1   . LEU B 2 565  ? 152.275 171.629 160.539 1.00 44.73  ? 562  LEU A CD1   1 
ATOM   4517  C CD2   . LEU B 2 565  ? 154.297 170.716 161.691 1.00 44.73  ? 562  LEU A CD2   1 
ATOM   4518  N N     . TYR B 2 566  ? 149.901 167.302 162.494 1.00 44.73  ? 563  TYR A N     1 
ATOM   4519  C CA    . TYR B 2 566  ? 149.374 166.164 163.234 1.00 44.73  ? 563  TYR A CA    1 
ATOM   4520  C C     . TYR B 2 566  ? 150.519 165.293 163.728 1.00 44.73  ? 563  TYR A C     1 
ATOM   4521  O O     . TYR B 2 566  ? 151.404 164.921 162.951 1.00 44.73  ? 563  TYR A O     1 
ATOM   4522  C CB    . TYR B 2 566  ? 148.419 165.347 162.364 1.00 44.73  ? 563  TYR A CB    1 
ATOM   4523  C CG    . TYR B 2 566  ? 147.212 166.128 161.906 1.00 44.73  ? 563  TYR A CG    1 
ATOM   4524  C CD1   . TYR B 2 566  ? 146.082 166.225 162.704 1.00 44.73  ? 563  TYR A CD1   1 
ATOM   4525  C CD2   . TYR B 2 566  ? 147.204 166.774 160.679 1.00 44.73  ? 563  TYR A CD2   1 
ATOM   4526  C CE1   . TYR B 2 566  ? 144.978 166.943 162.291 1.00 44.73  ? 563  TYR A CE1   1 
ATOM   4527  C CE2   . TYR B 2 566  ? 146.105 167.491 160.258 1.00 44.73  ? 563  TYR A CE2   1 
ATOM   4528  C CZ    . TYR B 2 566  ? 144.995 167.573 161.068 1.00 44.73  ? 563  TYR A CZ    1 
ATOM   4529  O OH    . TYR B 2 566  ? 143.897 168.288 160.650 1.00 44.73  ? 563  TYR A OH    1 
ATOM   4530  N N     . TYR B 2 567  ? 150.495 164.971 165.018 1.00 44.73  ? 564  TYR A N     1 
ATOM   4531  C CA    . TYR B 2 567  ? 151.532 164.175 165.655 1.00 44.73  ? 564  TYR A CA    1 
ATOM   4532  C C     . TYR B 2 567  ? 150.928 162.895 166.211 1.00 44.73  ? 564  TYR A C     1 
ATOM   4533  O O     . TYR B 2 567  ? 149.792 162.894 166.694 1.00 44.73  ? 564  TYR A O     1 
ATOM   4534  C CB    . TYR B 2 567  ? 152.216 164.957 166.780 1.00 44.73  ? 564  TYR A CB    1 
ATOM   4535  C CG    . TYR B 2 567  ? 152.954 166.190 166.316 1.00 44.73  ? 564  TYR A CG    1 
ATOM   4536  C CD1   . TYR B 2 567  ? 152.284 167.384 166.101 1.00 44.73  ? 564  TYR A CD1   1 
ATOM   4537  C CD2   . TYR B 2 567  ? 154.323 166.161 166.099 1.00 44.73  ? 564  TYR A CD2   1 
ATOM   4538  C CE1   . TYR B 2 567  ? 152.954 168.513 165.677 1.00 44.73  ? 564  TYR A CE1   1 
ATOM   4539  C CE2   . TYR B 2 567  ? 155.002 167.283 165.676 1.00 44.73  ? 564  TYR A CE2   1 
ATOM   4540  C CZ    . TYR B 2 567  ? 154.313 168.457 165.466 1.00 44.73  ? 564  TYR A CZ    1 
ATOM   4541  O OH    . TYR B 2 567  ? 154.986 169.579 165.044 1.00 44.73  ? 564  TYR A OH    1 
ATOM   4542  N N     . LEU B 2 568  ? 151.690 161.808 166.139 1.00 44.73  ? 565  LEU A N     1 
ATOM   4543  C CA    . LEU B 2 568  ? 151.293 160.526 166.707 1.00 44.73  ? 565  LEU A CA    1 
ATOM   4544  C C     . LEU B 2 568  ? 152.107 160.268 167.967 1.00 44.73  ? 565  LEU A C     1 
ATOM   4545  O O     . LEU B 2 568  ? 153.336 160.403 167.955 1.00 44.73  ? 565  LEU A O     1 
ATOM   4546  C CB    . LEU B 2 568  ? 151.489 159.392 165.703 1.00 44.73  ? 565  LEU A CB    1 
ATOM   4547  C CG    . LEU B 2 568  ? 151.383 157.972 166.266 1.00 44.73  ? 565  LEU A CG    1 
ATOM   4548  C CD1   . LEU B 2 568  ? 149.952 157.625 166.632 1.00 44.73  ? 565  LEU A CD1   1 
ATOM   4549  C CD2   . LEU B 2 568  ? 151.934 156.961 165.284 1.00 44.73  ? 565  LEU A CD2   1 
ATOM   4550  N N     . GLY B 2 569  ? 151.425 159.900 169.046 1.00 44.73  ? 566  GLY A N     1 
ATOM   4551  C CA    . GLY B 2 569  ? 152.098 159.603 170.292 1.00 44.73  ? 566  GLY A CA    1 
ATOM   4552  C C     . GLY B 2 569  ? 151.807 158.207 170.800 1.00 44.73  ? 566  GLY A C     1 
ATOM   4553  O O     . GLY B 2 569  ? 150.650 157.859 171.051 1.00 44.73  ? 566  GLY A O     1 
ATOM   4554  N N     . ILE B 2 570  ? 152.851 157.398 170.955 1.00 44.73  ? 567  ILE A N     1 
ATOM   4555  C CA    . ILE B 2 570  ? 152.733 156.037 171.463 1.00 44.73  ? 567  ILE A CA    1 
ATOM   4556  C C     . ILE B 2 570  ? 153.525 155.940 172.758 1.00 44.73  ? 567  ILE A C     1 
ATOM   4557  O O     . ILE B 2 570  ? 154.645 156.457 172.850 1.00 44.73  ? 567  ILE A O     1 
ATOM   4558  C CB    . ILE B 2 570  ? 153.209 154.994 170.432 1.00 44.73  ? 567  ILE A CB    1 
ATOM   4559  C CG1   . ILE B 2 570  ? 154.687 155.185 170.096 1.00 44.73  ? 567  ILE A CG1   1 
ATOM   4560  C CG2   . ILE B 2 570  ? 152.368 155.070 169.168 1.00 44.73  ? 567  ILE A CG2   1 
ATOM   4561  C CD1   . ILE B 2 570  ? 155.272 154.063 169.275 1.00 44.73  ? 567  ILE A CD1   1 
ATOM   4562  N N     . MET B 2 571  ? 152.929 155.308 173.768 1.00 44.73  ? 568  MET A N     1 
ATOM   4563  C CA    . MET B 2 571  ? 153.572 155.179 175.066 1.00 44.73  ? 568  MET A CA    1 
ATOM   4564  C C     . MET B 2 571  ? 154.232 153.817 175.167 1.00 44.73  ? 568  MET A C     1 
ATOM   4565  O O     . MET B 2 571  ? 153.528 152.799 175.140 1.00 44.73  ? 568  MET A O     1 
ATOM   4566  C CB    . MET B 2 571  ? 152.559 155.359 176.192 1.00 44.73  ? 568  MET A CB    1 
ATOM   4567  C CG    . MET B 2 571  ? 152.198 156.801 176.479 1.00 44.73  ? 568  MET A CG    1 
ATOM   4568  S SD    . MET B 2 571  ? 150.701 157.312 175.626 1.00 44.73  ? 568  MET A SD    1 
ATOM   4569  C CE    . MET B 2 571  ? 149.471 156.552 176.677 1.00 44.73  ? 568  MET A CE    1 
ATOM   4570  N N     . PRO B 2 572  ? 155.553 153.737 175.273 1.00 44.73  ? 569  PRO A N     1 
ATOM   4571  C CA    . PRO B 2 572  ? 156.213 152.439 175.440 1.00 44.73  ? 569  PRO A CA    1 
ATOM   4572  C C     . PRO B 2 572  ? 155.989 151.886 176.841 1.00 44.73  ? 569  PRO A C     1 
ATOM   4573  O O     . PRO B 2 572  ? 155.651 152.605 177.781 1.00 44.73  ? 569  PRO A O     1 
ATOM   4574  C CB    . PRO B 2 572  ? 157.700 152.737 175.215 1.00 44.73  ? 569  PRO A CB    1 
ATOM   4575  C CG    . PRO B 2 572  ? 157.830 154.203 175.112 1.00 44.73  ? 569  PRO A CG    1 
ATOM   4576  C CD    . PRO B 2 572  ? 156.495 154.853 175.094 1.00 44.73  ? 569  PRO A CD    1 
ATOM   4577  N N     . LYS B 2 573  ? 156.186 150.576 176.965 1.00 51.16  ? 570  LYS A N     1 
ATOM   4578  C CA    . LYS B 2 573  ? 156.215 149.939 178.277 1.00 51.16  ? 570  LYS A CA    1 
ATOM   4579  C C     . LYS B 2 573  ? 157.429 150.449 179.040 1.00 51.16  ? 570  LYS A C     1 
ATOM   4580  O O     . LYS B 2 573  ? 158.566 150.080 178.728 1.00 51.16  ? 570  LYS A O     1 
ATOM   4581  C CB    . LYS B 2 573  ? 156.262 148.421 178.138 1.00 51.16  ? 570  LYS A CB    1 
ATOM   4582  C CG    . LYS B 2 573  ? 154.963 147.785 177.691 1.00 51.16  ? 570  LYS A CG    1 
ATOM   4583  C CD    . LYS B 2 573  ? 155.090 146.275 177.623 1.00 51.16  ? 570  LYS A CD    1 
ATOM   4584  C CE    . LYS B 2 573  ? 153.763 145.626 177.281 1.00 51.16  ? 570  LYS A CE    1 
ATOM   4585  N NZ    . LYS B 2 573  ? 153.869 144.142 177.239 1.00 51.16  ? 570  LYS A NZ    1 
ATOM   4586  N N     . GLN B 2 574  ? 157.195 151.296 180.038 1.00 60.76  ? 571  GLN A N     1 
ATOM   4587  C CA    . GLN B 2 574  ? 158.288 151.898 180.794 1.00 60.76  ? 571  GLN A CA    1 
ATOM   4588  C C     . GLN B 2 574  ? 159.004 150.822 181.599 1.00 60.76  ? 571  GLN A C     1 
ATOM   4589  O O     . GLN B 2 574  ? 158.444 150.273 182.554 1.00 60.76  ? 571  GLN A O     1 
ATOM   4590  C CB    . GLN B 2 574  ? 157.756 153.003 181.700 1.00 60.76  ? 571  GLN A CB    1 
ATOM   4591  C CG    . GLN B 2 574  ? 157.809 154.388 181.075 1.00 60.76  ? 571  GLN A CG    1 
ATOM   4592  C CD    . GLN B 2 574  ? 159.188 155.017 181.159 1.00 60.76  ? 571  GLN A CD    1 
ATOM   4593  O OE1   . GLN B 2 574  ? 160.157 154.370 181.554 1.00 60.76  ? 571  GLN A OE1   1 
ATOM   4594  N NE2   . GLN B 2 574  ? 159.281 156.286 180.782 1.00 60.76  ? 571  GLN A NE2   1 
ATOM   4595  N N     . LYS B 2 575  ? 160.247 150.526 181.212 1.00 64.23  ? 572  LYS A N     1 
ATOM   4596  C CA    . LYS B 2 575  ? 161.071 149.512 181.874 1.00 64.23  ? 572  LYS A CA    1 
ATOM   4597  C C     . LYS B 2 575  ? 160.366 148.158 181.914 1.00 64.23  ? 572  LYS A C     1 
ATOM   4598  O O     . LYS B 2 575  ? 160.420 147.437 182.912 1.00 64.23  ? 572  LYS A O     1 
ATOM   4599  C CB    . LYS B 2 575  ? 161.478 149.957 183.281 1.00 64.23  ? 572  LYS A CB    1 
ATOM   4600  C CG    . LYS B 2 575  ? 161.890 151.418 183.383 1.00 64.23  ? 572  LYS A CG    1 
ATOM   4601  C CD    . LYS B 2 575  ? 163.055 151.736 182.458 1.00 64.23  ? 572  LYS A CD    1 
ATOM   4602  C CE    . LYS B 2 575  ? 164.328 151.039 182.908 1.00 64.23  ? 572  LYS A CE    1 
ATOM   4603  N NZ    . LYS B 2 575  ? 165.480 151.377 182.028 1.00 64.23  ? 572  LYS A NZ    1 
ATOM   4604  N N     . GLY B 2 576  ? 159.698 147.810 180.817 1.00 64.66  ? 573  GLY A N     1 
ATOM   4605  C CA    . GLY B 2 576  ? 159.055 146.518 180.697 1.00 64.66  ? 573  GLY A CA    1 
ATOM   4606  C C     . GLY B 2 576  ? 157.685 146.405 181.325 1.00 64.66  ? 573  GLY A C     1 
ATOM   4607  O O     . GLY B 2 576  ? 157.122 145.305 181.342 1.00 64.66  ? 573  GLY A O     1 
ATOM   4608  N N     . ARG B 2 577  ? 157.128 147.497 181.844 1.00 63.05  ? 574  ARG A N     1 
ATOM   4609  C CA    . ARG B 2 577  ? 155.808 147.479 182.455 1.00 63.05  ? 574  ARG A CA    1 
ATOM   4610  C C     . ARG B 2 577  ? 154.977 148.640 181.930 1.00 63.05  ? 574  ARG A C     1 
ATOM   4611  O O     . ARG B 2 577  ? 155.509 149.691 181.564 1.00 63.05  ? 574  ARG A O     1 
ATOM   4612  C CB    . ARG B 2 577  ? 155.890 147.555 183.987 1.00 63.05  ? 574  ARG A CB    1 
ATOM   4613  C CG    . ARG B 2 577  ? 156.714 146.450 184.629 1.00 63.05  ? 574  ARG A CG    1 
ATOM   4614  C CD    . ARG B 2 577  ? 157.186 146.854 186.017 1.00 63.05  ? 574  ARG A CD    1 
ATOM   4615  N NE    . ARG B 2 577  ? 157.640 148.239 186.059 1.00 63.05  ? 574  ARG A NE    1 
ATOM   4616  C CZ    . ARG B 2 577  ? 158.829 148.652 185.640 1.00 63.05  ? 574  ARG A CZ    1 
ATOM   4617  N NH1   . ARG B 2 577  ? 159.720 147.806 185.149 1.00 63.05  ? 574  ARG A NH1   1 
ATOM   4618  N NH2   . ARG B 2 577  ? 159.131 149.944 185.718 1.00 63.05  ? 574  ARG A NH2   1 
ATOM   4619  N N     . TYR B 2 578  ? 153.661 148.435 181.895 1.00 53.66  ? 575  TYR A N     1 
ATOM   4620  C CA    . TYR B 2 578  ? 152.745 149.501 181.512 1.00 53.66  ? 575  TYR A CA    1 
ATOM   4621  C C     . TYR B 2 578  ? 152.785 150.624 182.542 1.00 53.66  ? 575  TYR A C     1 
ATOM   4622  O O     . TYR B 2 578  ? 152.791 150.372 183.751 1.00 53.66  ? 575  TYR A O     1 
ATOM   4623  C CB    . TYR B 2 578  ? 151.322 148.962 181.383 1.00 53.66  ? 575  TYR A CB    1 
ATOM   4624  C CG    . TYR B 2 578  ? 151.048 148.210 180.102 1.00 53.66  ? 575  TYR A CG    1 
ATOM   4625  C CD1   . TYR B 2 578  ? 150.968 148.876 178.887 1.00 53.66  ? 575  TYR A CD1   1 
ATOM   4626  C CD2   . TYR B 2 578  ? 150.852 146.836 180.109 1.00 53.66  ? 575  TYR A CD2   1 
ATOM   4627  C CE1   . TYR B 2 578  ? 150.711 148.194 177.715 1.00 53.66  ? 575  TYR A CE1   1 
ATOM   4628  C CE2   . TYR B 2 578  ? 150.595 146.146 178.941 1.00 53.66  ? 575  TYR A CE2   1 
ATOM   4629  C CZ    . TYR B 2 578  ? 150.525 146.830 177.747 1.00 53.66  ? 575  TYR A CZ    1 
ATOM   4630  O OH    . TYR B 2 578  ? 150.270 146.146 176.581 1.00 53.66  ? 575  TYR A OH    1 
ATOM   4631  N N     . LYS B 2 579  ? 152.807 151.865 182.061 1.00 52.92  ? 576  LYS A N     1 
ATOM   4632  C CA    . LYS B 2 579  ? 152.826 153.042 182.927 1.00 52.92  ? 576  LYS A CA    1 
ATOM   4633  C C     . LYS B 2 579  ? 152.001 154.133 182.261 1.00 52.92  ? 576  LYS A C     1 
ATOM   4634  O O     . LYS B 2 579  ? 152.351 154.599 181.172 1.00 52.92  ? 576  LYS A O     1 
ATOM   4635  C CB    . LYS B 2 579  ? 154.255 153.521 183.188 1.00 52.92  ? 576  LYS A CB    1 
ATOM   4636  C CG    . LYS B 2 579  ? 155.041 152.655 184.160 1.00 52.92  ? 576  LYS A CG    1 
ATOM   4637  C CD    . LYS B 2 579  ? 154.434 152.697 185.553 1.00 52.92  ? 576  LYS A CD    1 
ATOM   4638  C CE    . LYS B 2 579  ? 154.526 154.091 186.152 1.00 52.92  ? 576  LYS A CE    1 
ATOM   4639  N NZ    . LYS B 2 579  ? 155.938 154.517 186.351 1.00 52.92  ? 576  LYS A NZ    1 
ATOM   4640  N N     . ALA B 2 580  ? 150.914 154.538 182.909 1.00 44.73  ? 577  ALA A N     1 
ATOM   4641  C CA    . ALA B 2 580  ? 150.065 155.584 182.361 1.00 44.73  ? 577  ALA A CA    1 
ATOM   4642  C C     . ALA B 2 580  ? 150.723 156.949 182.517 1.00 44.73  ? 577  ALA A C     1 
ATOM   4643  O O     . ALA B 2 580  ? 151.527 157.178 183.424 1.00 44.73  ? 577  ALA A O     1 
ATOM   4644  C CB    . ALA B 2 580  ? 148.700 155.581 183.047 1.00 44.73  ? 577  ALA A CB    1 
ATOM   4645  N N     . LEU B 2 581  ? 150.373 157.862 181.615 1.00 44.73  ? 578  LEU A N     1 
ATOM   4646  C CA    . LEU B 2 581  ? 150.871 159.231 181.637 1.00 44.73  ? 578  LEU A CA    1 
ATOM   4647  C C     . LEU B 2 581  ? 149.748 160.156 182.078 1.00 44.73  ? 578  LEU A C     1 
ATOM   4648  O O     . LEU B 2 581  ? 148.679 160.181 181.459 1.00 44.73  ? 578  LEU A O     1 
ATOM   4649  C CB    . LEU B 2 581  ? 151.403 159.646 180.266 1.00 36.08  ? 578  LEU A CB    1 
ATOM   4650  C CG    . LEU B 2 581  ? 152.701 158.980 179.815 1.00 36.08  ? 578  LEU A CG    1 
ATOM   4651  C CD1   . LEU B 2 581  ? 153.229 159.644 178.556 1.00 36.08  ? 578  LEU A CD1   1 
ATOM   4652  C CD2   . LEU B 2 581  ? 153.734 159.030 180.927 1.00 36.08  ? 578  LEU A CD2   1 
ATOM   4653  N N     . SER B 2 582  ? 149.993 160.918 183.144 1.00 44.73  ? 579  SER A N     1 
ATOM   4654  C CA    . SER B 2 582  ? 148.993 161.828 183.699 1.00 44.73  ? 579  SER A CA    1 
ATOM   4655  C C     . SER B 2 582  ? 149.053 163.146 182.933 1.00 44.73  ? 579  SER A C     1 
ATOM   4656  O O     . SER B 2 582  ? 149.619 164.147 183.383 1.00 44.73  ? 579  SER A O     1 
ATOM   4657  C CB    . SER B 2 582  ? 149.220 162.030 185.191 1.00 44.73  ? 579  SER A CB    1 
ATOM   4658  O OG    . SER B 2 582  ? 150.343 162.861 185.429 1.00 44.73  ? 579  SER A OG    1 
ATOM   4659  N N     . PHE B 2 583  ? 148.453 163.140 181.746 1.00 44.73  ? 580  PHE A N     1 
ATOM   4660  C CA    . PHE B 2 583  ? 148.369 164.348 180.931 1.00 44.73  ? 580  PHE A CA    1 
ATOM   4661  C C     . PHE B 2 583  ? 147.273 165.249 181.487 1.00 44.73  ? 580  PHE A C     1 
ATOM   4662  O O     . PHE B 2 583  ? 146.084 164.939 181.365 1.00 44.73  ? 580  PHE A O     1 
ATOM   4663  C CB    . PHE B 2 583  ? 148.095 163.985 179.475 1.00 44.73  ? 580  PHE A CB    1 
ATOM   4664  C CG    . PHE B 2 583  ? 149.325 163.613 178.703 1.00 44.73  ? 580  PHE A CG    1 
ATOM   4665  C CD1   . PHE B 2 583  ? 150.484 164.359 178.818 1.00 44.73  ? 580  PHE A CD1   1 
ATOM   4666  C CD2   . PHE B 2 583  ? 149.323 162.517 177.859 1.00 44.73  ? 580  PHE A CD2   1 
ATOM   4667  C CE1   . PHE B 2 583  ? 151.617 164.018 178.108 1.00 44.73  ? 580  PHE A CE1   1 
ATOM   4668  C CE2   . PHE B 2 583  ? 150.452 162.172 177.147 1.00 44.73  ? 580  PHE A CE2   1 
ATOM   4669  C CZ    . PHE B 2 583  ? 151.600 162.922 177.271 1.00 44.73  ? 580  PHE A CZ    1 
ATOM   4670  N N     . GLU B 2 584  ? 147.669 166.359 182.096 1.00 44.73  ? 581  GLU A N     1 
ATOM   4671  C CA    . GLU B 2 584  ? 146.712 167.254 182.735 1.00 44.73  ? 581  GLU A CA    1 
ATOM   4672  C C     . GLU B 2 584  ? 146.086 168.181 181.701 1.00 44.73  ? 581  GLU A C     1 
ATOM   4673  O O     . GLU B 2 584  ? 146.817 168.896 181.006 1.00 44.73  ? 581  GLU A O     1 
ATOM   4674  C CB    . GLU B 2 584  ? 147.395 168.070 183.824 1.00 32.25  ? 581  GLU A CB    1 
ATOM   4675  C CG    . GLU B 2 584  ? 146.475 169.038 184.550 1.00 32.25  ? 581  GLU A CG    1 
ATOM   4676  C CD    . GLU B 2 584  ? 145.426 168.333 185.388 1.00 32.25  ? 581  GLU A CD    1 
ATOM   4677  O OE1   . GLU B 2 584  ? 145.688 167.200 185.844 1.00 32.25  ? 581  GLU A OE1   1 
ATOM   4678  O OE2   . GLU B 2 584  ? 144.339 168.914 185.593 1.00 32.25  ? 581  GLU A OE2   1 
ATOM   4679  N N     . PRO B 2 585  ? 144.758 168.191 181.553 1.00 44.73  ? 582  PRO A N     1 
ATOM   4680  C CA    . PRO B 2 585  ? 144.123 169.147 180.634 1.00 44.73  ? 582  PRO A CA    1 
ATOM   4681  C C     . PRO B 2 585  ? 144.429 170.589 181.007 1.00 44.73  ? 582  PRO A C     1 
ATOM   4682  O O     . PRO B 2 585  ? 144.021 171.063 182.071 1.00 44.73  ? 582  PRO A O     1 
ATOM   4683  C CB    . PRO B 2 585  ? 142.626 168.847 180.777 1.00 44.73  ? 582  PRO A CB    1 
ATOM   4684  C CG    . PRO B 2 585  ? 142.534 167.486 181.359 1.00 44.73  ? 582  PRO A CG    1 
ATOM   4685  C CD    . PRO B 2 585  ? 143.839 167.134 182.006 1.00 44.73  ? 582  PRO A CD    1 
ATOM   4686  N N     . THR B 2 586  ? 145.145 171.292 180.138 1.00 44.73  ? 583  THR A N     1 
ATOM   4687  C CA    . THR B 2 586  ? 145.547 172.665 180.392 1.00 44.73  ? 583  THR A CA    1 
ATOM   4688  C C     . THR B 2 586  ? 144.672 173.614 179.572 1.00 44.73  ? 583  THR A C     1 
ATOM   4689  O O     . THR B 2 586  ? 144.098 173.236 178.548 1.00 44.73  ? 583  THR A O     1 
ATOM   4690  C CB    . THR B 2 586  ? 147.033 172.842 180.056 1.00 44.73  ? 583  THR A CB    1 
ATOM   4691  O OG1   . THR B 2 586  ? 147.806 171.953 180.871 1.00 44.73  ? 583  THR A OG1   1 
ATOM   4692  C CG2   . THR B 2 586  ? 147.508 174.256 180.351 1.00 44.73  ? 583  THR A CG2   1 
ATOM   4693  N N     . GLU B 2 587  ? 144.557 174.853 180.050 1.00 44.73  ? 584  GLU A N     1 
ATOM   4694  C CA    . GLU B 2 587  ? 143.701 175.837 179.401 1.00 44.73  ? 584  GLU A CA    1 
ATOM   4695  C C     . GLU B 2 587  ? 144.135 176.068 177.959 1.00 44.73  ? 584  GLU A C     1 
ATOM   4696  O O     . GLU B 2 587  ? 145.327 176.061 177.641 1.00 44.73  ? 584  GLU A O     1 
ATOM   4697  C CB    . GLU B 2 587  ? 143.730 177.156 180.175 1.00 44.73  ? 584  GLU A CB    1 
ATOM   4698  C CG    . GLU B 2 587  ? 142.872 177.160 181.429 1.00 44.73  ? 584  GLU A CG    1 
ATOM   4699  C CD    . GLU B 2 587  ? 141.390 177.274 181.128 1.00 44.73  ? 584  GLU A CD    1 
ATOM   4700  O OE1   . GLU B 2 587  ? 141.038 177.723 180.017 1.00 44.73  ? 584  GLU A OE1   1 
ATOM   4701  O OE2   . GLU B 2 587  ? 140.576 176.915 182.005 1.00 44.73  ? 584  GLU A OE2   1 
ATOM   4702  N N     . LYS B 2 588  ? 143.147 176.269 177.083 1.00 44.73  ? 585  LYS A N     1 
ATOM   4703  C CA    . LYS B 2 588  ? 143.409 176.395 175.654 1.00 44.73  ? 585  LYS A CA    1 
ATOM   4704  C C     . LYS B 2 588  ? 144.270 177.606 175.318 1.00 44.73  ? 585  LYS A C     1 
ATOM   4705  O O     . LYS B 2 588  ? 144.906 177.624 174.259 1.00 44.73  ? 585  LYS A O     1 
ATOM   4706  C CB    . LYS B 2 588  ? 142.086 176.470 174.889 1.00 33.74  ? 585  LYS A CB    1 
ATOM   4707  C CG    . LYS B 2 588  ? 142.206 176.191 173.401 1.00 33.74  ? 585  LYS A CG    1 
ATOM   4708  C CD    . LYS B 2 588  ? 140.845 176.175 172.725 1.00 33.74  ? 585  LYS A CD    1 
ATOM   4709  C CE    . LYS B 2 588  ? 139.964 177.317 173.211 1.00 33.74  ? 585  LYS A CE    1 
ATOM   4710  N NZ    . LYS B 2 588  ? 139.095 177.843 172.123 1.00 33.74  ? 585  LYS A NZ    1 
ATOM   4711  N N     . THR B 2 589  ? 144.302 178.616 176.189 1.00 44.73  ? 586  THR A N     1 
ATOM   4712  C CA    . THR B 2 589  ? 145.094 179.809 175.908 1.00 44.73  ? 586  THR A CA    1 
ATOM   4713  C C     . THR B 2 589  ? 146.580 179.483 175.825 1.00 44.73  ? 586  THR A C     1 
ATOM   4714  O O     . THR B 2 589  ? 147.291 180.012 174.963 1.00 44.73  ? 586  THR A O     1 
ATOM   4715  C CB    . THR B 2 589  ? 144.841 180.871 176.977 1.00 44.73  ? 586  THR A CB    1 
ATOM   4716  O OG1   . THR B 2 589  ? 145.240 180.366 178.257 1.00 44.73  ? 586  THR A OG1   1 
ATOM   4717  C CG2   . THR B 2 589  ? 143.365 181.237 177.021 1.00 44.73  ? 586  THR A CG2   1 
ATOM   4718  N N     . SER B 2 590  ? 147.067 178.622 176.714 1.00 44.73  ? 587  SER A N     1 
ATOM   4719  C CA    . SER B 2 590  ? 148.482 178.281 176.731 1.00 44.73  ? 587  SER A CA    1 
ATOM   4720  C C     . SER B 2 590  ? 148.862 177.496 175.483 1.00 44.73  ? 587  SER A C     1 
ATOM   4721  O O     . SER B 2 590  ? 148.097 176.659 174.997 1.00 44.73  ? 587  SER A O     1 
ATOM   4722  C CB    . SER B 2 590  ? 148.818 177.467 177.978 1.00 44.73  ? 587  SER A CB    1 
ATOM   4723  O OG    . SER B 2 590  ? 148.213 176.189 177.920 1.00 44.73  ? 587  SER A OG    1 
ATOM   4724  N N     . GLU B 2 591  ? 150.054 177.774 174.963 1.00 44.73  ? 588  GLU A N     1 
ATOM   4725  C CA    . GLU B 2 591  ? 150.526 177.091 173.766 1.00 44.73  ? 588  GLU A CA    1 
ATOM   4726  C C     . GLU B 2 591  ? 150.886 175.648 174.090 1.00 44.73  ? 588  GLU A C     1 
ATOM   4727  O O     . GLU B 2 591  ? 151.603 175.376 175.058 1.00 44.73  ? 588  GLU A O     1 
ATOM   4728  C CB    . GLU B 2 591  ? 151.735 177.821 173.180 1.00 44.73  ? 588  GLU A CB    1 
ATOM   4729  C CG    . GLU B 2 591  ? 151.484 179.279 172.798 1.00 44.73  ? 588  GLU A CG    1 
ATOM   4730  C CD    . GLU B 2 591  ? 150.310 179.471 171.847 1.00 44.73  ? 588  GLU A CD    1 
ATOM   4731  O OE1   . GLU B 2 591  ? 149.936 178.514 171.135 1.00 44.73  ? 588  GLU A OE1   1 
ATOM   4732  O OE2   . GLU B 2 591  ? 149.784 180.602 171.783 1.00 44.73  ? 588  GLU A OE2   1 
ATOM   4733  N N     . GLY B 2 592  ? 150.387 174.723 173.280 1.00 44.73  ? 589  GLY A N     1 
ATOM   4734  C CA    . GLY B 2 592  ? 150.674 173.318 173.493 1.00 44.73  ? 589  GLY A CA    1 
ATOM   4735  C C     . GLY B 2 592  ? 149.898 172.467 172.515 1.00 44.73  ? 589  GLY A C     1 
ATOM   4736  O O     . GLY B 2 592  ? 149.104 172.964 171.709 1.00 44.73  ? 589  GLY A O     1 
ATOM   4737  N N     . PHE B 2 593  ? 150.142 171.163 172.598 1.00 44.73  ? 590  PHE A N     1 
ATOM   4738  C CA    . PHE B 2 593  ? 149.471 170.215 171.723 1.00 44.73  ? 590  PHE A CA    1 
ATOM   4739  C C     . PHE B 2 593  ? 148.026 170.012 172.162 1.00 44.73  ? 590  PHE A C     1 
ATOM   4740  O O     . PHE B 2 593  ? 147.666 170.236 173.321 1.00 44.73  ? 590  PHE A O     1 
ATOM   4741  C CB    . PHE B 2 593  ? 150.203 168.874 171.723 1.00 44.73  ? 590  PHE A CB    1 
ATOM   4742  C CG    . PHE B 2 593  ? 151.621 168.949 171.230 1.00 44.73  ? 590  PHE A CG    1 
ATOM   4743  C CD1   . PHE B 2 593  ? 152.627 169.446 172.038 1.00 44.73  ? 590  PHE A CD1   1 
ATOM   4744  C CD2   . PHE B 2 593  ? 151.947 168.507 169.961 1.00 44.73  ? 590  PHE A CD2   1 
ATOM   4745  C CE1   . PHE B 2 593  ? 153.929 169.510 171.588 1.00 44.73  ? 590  PHE A CE1   1 
ATOM   4746  C CE2   . PHE B 2 593  ? 153.249 168.568 169.506 1.00 44.73  ? 590  PHE A CE2   1 
ATOM   4747  C CZ    . PHE B 2 593  ? 154.240 169.071 170.321 1.00 44.73  ? 590  PHE A CZ    1 
ATOM   4748  N N     . ASP B 2 594  ? 147.194 169.580 171.221 1.00 44.73  ? 591  ASP A N     1 
ATOM   4749  C CA    . ASP B 2 594  ? 145.806 169.233 171.498 1.00 44.73  ? 591  ASP A CA    1 
ATOM   4750  C C     . ASP B 2 594  ? 145.658 167.721 171.393 1.00 44.73  ? 591  ASP A C     1 
ATOM   4751  O O     . ASP B 2 594  ? 145.961 167.136 170.349 1.00 44.73  ? 591  ASP A O     1 
ATOM   4752  C CB    . ASP B 2 594  ? 144.860 169.937 170.528 1.00 44.73  ? 591  ASP A CB    1 
ATOM   4753  C CG    . ASP B 2 594  ? 144.857 171.441 170.705 1.00 44.73  ? 591  ASP A CG    1 
ATOM   4754  O OD1   . ASP B 2 594  ? 144.871 171.905 171.865 1.00 44.73  ? 591  ASP A OD1   1 
ATOM   4755  O OD2   . ASP B 2 594  ? 144.842 172.161 169.685 1.00 44.73  ? 591  ASP A OD2   1 
ATOM   4756  N N     . LYS B 2 595  ? 145.186 167.094 172.466 1.00 44.73  ? 592  LYS A N     1 
ATOM   4757  C CA    . LYS B 2 595  ? 145.143 165.642 172.550 1.00 44.73  ? 592  LYS A CA    1 
ATOM   4758  C C     . LYS B 2 595  ? 143.747 165.125 172.232 1.00 44.73  ? 592  LYS A C     1 
ATOM   4759  O O     . LYS B 2 595  ? 142.743 165.713 172.642 1.00 44.73  ? 592  LYS A O     1 
ATOM   4760  C CB    . LYS B 2 595  ? 145.571 165.176 173.942 1.00 44.73  ? 592  LYS A CB    1 
ATOM   4761  C CG    . LYS B 2 595  ? 145.456 163.683 174.163 1.00 44.73  ? 592  LYS A CG    1 
ATOM   4762  C CD    . LYS B 2 595  ? 146.216 163.253 175.400 1.00 44.73  ? 592  LYS A CD    1 
ATOM   4763  C CE    . LYS B 2 595  ? 145.441 162.206 176.172 1.00 44.73  ? 592  LYS A CE    1 
ATOM   4764  N NZ    . LYS B 2 595  ? 144.896 161.156 175.270 1.00 44.73  ? 592  LYS A NZ    1 
ATOM   4765  N N     . MET B 2 596  ? 143.691 164.018 171.496 1.00 44.73  ? 593  MET A N     1 
ATOM   4766  C CA    . MET B 2 596  ? 142.421 163.395 171.158 1.00 44.73  ? 593  MET A CA    1 
ATOM   4767  C C     . MET B 2 596  ? 141.833 162.686 172.369 1.00 44.73  ? 593  MET A C     1 
ATOM   4768  O O     . MET B 2 596  ? 142.508 161.879 173.016 1.00 44.73  ? 593  MET A O     1 
ATOM   4769  C CB    . MET B 2 596  ? 142.597 162.389 170.025 1.00 44.73  ? 593  MET A CB    1 
ATOM   4770  C CG    . MET B 2 596  ? 141.383 162.258 169.131 1.00 44.73  ? 593  MET A CG    1 
ATOM   4771  S SD    . MET B 2 596  ? 141.312 160.649 168.334 1.00 44.73  ? 593  MET A SD    1 
ATOM   4772  C CE    . MET B 2 596  ? 142.942 160.566 167.616 1.00 44.73  ? 593  MET A CE    1 
ATOM   4773  N N     . TYR B 2 597  ? 140.572 162.975 172.665 1.00 44.73  ? 594  TYR A N     1 
ATOM   4774  C CA    . TYR B 2 597  ? 139.799 162.218 173.642 1.00 44.73  ? 594  TYR A CA    1 
ATOM   4775  C C     . TYR B 2 597  ? 138.741 161.438 172.872 1.00 44.73  ? 594  TYR A C     1 
ATOM   4776  O O     . TYR B 2 597  ? 137.763 162.016 172.386 1.00 44.73  ? 594  TYR A O     1 
ATOM   4777  C CB    . TYR B 2 597  ? 139.172 163.129 174.696 1.00 44.73  ? 594  TYR A CB    1 
ATOM   4778  C CG    . TYR B 2 597  ? 140.130 163.568 175.782 1.00 44.73  ? 594  TYR A CG    1 
ATOM   4779  C CD1   . TYR B 2 597  ? 141.502 163.531 175.586 1.00 44.73  ? 594  TYR A CD1   1 
ATOM   4780  C CD2   . TYR B 2 597  ? 139.659 163.999 177.014 1.00 44.73  ? 594  TYR A CD2   1 
ATOM   4781  C CE1   . TYR B 2 597  ? 142.377 163.924 176.576 1.00 44.73  ? 594  TYR A CE1   1 
ATOM   4782  C CE2   . TYR B 2 597  ? 140.528 164.393 178.012 1.00 44.73  ? 594  TYR A CE2   1 
ATOM   4783  C CZ    . TYR B 2 597  ? 141.886 164.354 177.786 1.00 44.73  ? 594  TYR A CZ    1 
ATOM   4784  O OH    . TYR B 2 597  ? 142.758 164.746 178.776 1.00 44.73  ? 594  TYR A OH    1 
ATOM   4785  N N     . TYR B 2 598  ? 138.943 160.130 172.765 1.00 44.73  ? 595  TYR A N     1 
ATOM   4786  C CA    . TYR B 2 598  ? 138.135 159.255 171.927 1.00 44.73  ? 595  TYR A CA    1 
ATOM   4787  C C     . TYR B 2 598  ? 137.215 158.433 172.818 1.00 44.73  ? 595  TYR A C     1 
ATOM   4788  O O     . TYR B 2 598  ? 137.688 157.654 173.652 1.00 44.73  ? 595  TYR A O     1 
ATOM   4789  C CB    . TYR B 2 598  ? 139.044 158.352 171.094 1.00 44.73  ? 595  TYR A CB    1 
ATOM   4790  C CG    . TYR B 2 598  ? 138.385 157.567 169.984 1.00 44.73  ? 595  TYR A CG    1 
ATOM   4791  C CD1   . TYR B 2 598  ? 137.811 156.329 170.231 1.00 44.73  ? 595  TYR A CD1   1 
ATOM   4792  C CD2   . TYR B 2 598  ? 138.380 158.040 168.681 1.00 44.73  ? 595  TYR A CD2   1 
ATOM   4793  C CE1   . TYR B 2 598  ? 137.227 155.599 169.218 1.00 44.73  ? 595  TYR A CE1   1 
ATOM   4794  C CE2   . TYR B 2 598  ? 137.797 157.316 167.661 1.00 44.73  ? 595  TYR A CE2   1 
ATOM   4795  C CZ    . TYR B 2 598  ? 137.222 156.097 167.936 1.00 44.73  ? 595  TYR A CZ    1 
ATOM   4796  O OH    . TYR B 2 598  ? 136.639 155.367 166.926 1.00 44.73  ? 595  TYR A OH    1 
ATOM   4797  N N     . ASP B 2 599  ? 135.909 158.611 172.644 1.00 44.73  ? 596  ASP A N     1 
ATOM   4798  C CA    . ASP B 2 599  ? 134.900 157.858 173.375 1.00 44.73  ? 596  ASP A CA    1 
ATOM   4799  C C     . ASP B 2 599  ? 134.096 157.036 172.382 1.00 44.73  ? 596  ASP A C     1 
ATOM   4800  O O     . ASP B 2 599  ? 133.593 157.575 171.391 1.00 44.73  ? 596  ASP A O     1 
ATOM   4801  C CB    . ASP B 2 599  ? 133.978 158.789 174.166 1.00 44.73  ? 596  ASP A CB    1 
ATOM   4802  C CG    . ASP B 2 599  ? 134.670 159.422 175.355 1.00 44.73  ? 596  ASP A CG    1 
ATOM   4803  O OD1   . ASP B 2 599  ? 135.822 159.040 175.647 1.00 44.73  ? 596  ASP A OD1   1 
ATOM   4804  O OD2   . ASP B 2 599  ? 134.062 160.303 175.999 1.00 44.73  ? 596  ASP A OD2   1 
ATOM   4805  N N     . TYR B 2 600  ? 133.972 155.738 172.645 1.00 44.73  ? 597  TYR A N     1 
ATOM   4806  C CA    . TYR B 2 600  ? 133.336 154.845 171.689 1.00 44.73  ? 597  TYR A CA    1 
ATOM   4807  C C     . TYR B 2 600  ? 132.722 153.654 172.408 1.00 44.73  ? 597  TYR A C     1 
ATOM   4808  O O     . TYR B 2 600  ? 133.387 152.984 173.202 1.00 44.73  ? 597  TYR A O     1 
ATOM   4809  C CB    . TYR B 2 600  ? 134.342 154.365 170.638 1.00 44.73  ? 597  TYR A CB    1 
ATOM   4810  C CG    . TYR B 2 600  ? 133.736 153.555 169.517 1.00 44.73  ? 597  TYR A CG    1 
ATOM   4811  C CD1   . TYR B 2 600  ? 132.476 153.851 169.022 1.00 44.73  ? 597  TYR A CD1   1 
ATOM   4812  C CD2   . TYR B 2 600  ? 134.431 152.499 168.947 1.00 44.73  ? 597  TYR A CD2   1 
ATOM   4813  C CE1   . TYR B 2 600  ? 131.923 153.113 167.998 1.00 44.73  ? 597  TYR A CE1   1 
ATOM   4814  C CE2   . TYR B 2 600  ? 133.886 151.758 167.922 1.00 44.73  ? 597  TYR A CE2   1 
ATOM   4815  C CZ    . TYR B 2 600  ? 132.633 152.068 167.451 1.00 44.73  ? 597  TYR A CZ    1 
ATOM   4816  O OH    . TYR B 2 600  ? 132.086 151.330 166.428 1.00 44.73  ? 597  TYR A OH    1 
ATOM   4817  N N     . PHE B 2 601  ? 131.448 153.406 172.121 1.00 46.64  ? 598  PHE A N     1 
ATOM   4818  C CA    . PHE B 2 601  ? 130.749 152.193 172.544 1.00 46.64  ? 598  PHE A CA    1 
ATOM   4819  C C     . PHE B 2 601  ? 130.454 151.394 171.283 1.00 46.64  ? 598  PHE A C     1 
ATOM   4820  O O     . PHE B 2 601  ? 129.658 151.843 170.439 1.00 46.64  ? 598  PHE A O     1 
ATOM   4821  C CB    . PHE B 2 601  ? 129.463 152.537 173.290 1.00 46.64  ? 598  PHE A CB    1 
ATOM   4822  C CG    . PHE B 2 601  ? 129.101 151.557 174.365 1.00 46.64  ? 598  PHE A CG    1 
ATOM   4823  C CD1   . PHE B 2 601  ? 129.931 151.368 175.454 1.00 46.64  ? 598  PHE A CD1   1 
ATOM   4824  C CD2   . PHE B 2 601  ? 127.923 150.836 174.293 1.00 46.64  ? 598  PHE A CD2   1 
ATOM   4825  C CE1   . PHE B 2 601  ? 129.596 150.471 176.447 1.00 46.64  ? 598  PHE A CE1   1 
ATOM   4826  C CE2   . PHE B 2 601  ? 127.584 149.941 175.282 1.00 46.64  ? 598  PHE A CE2   1 
ATOM   4827  C CZ    . PHE B 2 601  ? 128.421 149.757 176.360 1.00 46.64  ? 598  PHE A CZ    1 
ATOM   4828  N N     . PRO B 2 602  ? 131.080 150.220 171.099 1.00 48.35  ? 599  PRO A N     1 
ATOM   4829  C CA    . PRO B 2 602  ? 131.043 149.535 169.795 1.00 48.35  ? 599  PRO A CA    1 
ATOM   4830  C C     . PRO B 2 602  ? 129.669 149.410 169.153 1.00 48.35  ? 599  PRO A C     1 
ATOM   4831  O O     . PRO B 2 602  ? 129.466 149.898 168.037 1.00 48.35  ? 599  PRO A O     1 
ATOM   4832  C CB    . PRO B 2 602  ? 131.617 148.150 170.113 1.00 48.35  ? 599  PRO A CB    1 
ATOM   4833  C CG    . PRO B 2 602  ? 132.435 148.328 171.340 1.00 48.35  ? 599  PRO A CG    1 
ATOM   4834  C CD    . PRO B 2 602  ? 132.055 149.614 172.020 1.00 48.35  ? 599  PRO A CD    1 
ATOM   4835  N N     . ASP B 2 603  ? 128.718 148.772 169.832 1.00 53.80  ? 600  ASP A N     1 
ATOM   4836  C CA    . ASP B 2 603  ? 127.394 148.575 169.247 1.00 53.80  ? 600  ASP A CA    1 
ATOM   4837  C C     . ASP B 2 603  ? 126.417 148.299 170.375 1.00 53.80  ? 600  ASP A C     1 
ATOM   4838  O O     . ASP B 2 603  ? 126.749 147.575 171.319 1.00 53.80  ? 600  ASP A O     1 
ATOM   4839  C CB    . ASP B 2 603  ? 127.413 147.422 168.235 1.00 53.80  ? 600  ASP A CB    1 
ATOM   4840  C CG    . ASP B 2 603  ? 126.076 147.218 167.531 1.00 53.80  ? 600  ASP A CG    1 
ATOM   4841  O OD1   . ASP B 2 603  ? 125.012 147.283 168.181 1.00 53.80  ? 600  ASP A OD1   1 
ATOM   4842  O OD2   . ASP B 2 603  ? 126.095 146.987 166.304 1.00 53.80  ? 600  ASP A OD2   1 
ATOM   4843  N N     . ALA B 2 604  ? 125.219 148.874 170.278 1.00 57.62  ? 601  ALA A N     1 
ATOM   4844  C CA    . ALA B 2 604  ? 124.210 148.663 171.308 1.00 57.62  ? 601  ALA A CA    1 
ATOM   4845  C C     . ALA B 2 604  ? 123.698 147.229 171.295 1.00 57.62  ? 601  ALA A C     1 
ATOM   4846  O O     . ALA B 2 604  ? 123.335 146.682 172.342 1.00 57.62  ? 601  ALA A O     1 
ATOM   4847  C CB    . ALA B 2 604  ? 123.058 149.648 171.118 1.00 57.62  ? 601  ALA A CB    1 
ATOM   4848  N N     . ALA B 2 605  ? 123.654 146.605 170.116 1.00 58.49  ? 602  ALA A N     1 
ATOM   4849  C CA    . ALA B 2 605  ? 123.087 145.265 170.011 1.00 58.49  ? 602  ALA A CA    1 
ATOM   4850  C C     . ALA B 2 605  ? 123.957 144.234 170.716 1.00 58.49  ? 602  ALA A C     1 
ATOM   4851  O O     . ALA B 2 605  ? 123.445 143.257 171.275 1.00 58.49  ? 602  ALA A O     1 
ATOM   4852  C CB    . ALA B 2 605  ? 122.900 144.887 168.542 1.00 58.49  ? 602  ALA A CB    1 
ATOM   4853  N N     . LYS B 2 606  ? 125.273 144.432 170.702 1.00 57.62  ? 603  LYS A N     1 
ATOM   4854  C CA    . LYS B 2 606  ? 126.202 143.434 171.212 1.00 57.62  ? 603  LYS A CA    1 
ATOM   4855  C C     . LYS B 2 606  ? 126.845 143.808 172.541 1.00 57.62  ? 603  LYS A C     1 
ATOM   4856  O O     . LYS B 2 606  ? 127.133 142.912 173.341 1.00 57.62  ? 603  LYS A O     1 
ATOM   4857  C CB    . LYS B 2 606  ? 127.288 143.157 170.165 1.00 57.62  ? 603  LYS A CB    1 
ATOM   4858  C CG    . LYS B 2 606  ? 128.335 144.245 170.003 1.00 57.62  ? 603  LYS A CG    1 
ATOM   4859  C CD    . LYS B 2 606  ? 129.319 143.890 168.896 1.00 57.62  ? 603  LYS A CD    1 
ATOM   4860  C CE    . LYS B 2 606  ? 130.070 145.118 168.404 1.00 57.62  ? 603  LYS A CE    1 
ATOM   4861  N NZ    . LYS B 2 606  ? 130.398 145.045 166.955 1.00 57.62  ? 603  LYS A NZ    1 
ATOM   4862  N N     . MET B 2 607  ? 127.062 145.092 172.810 1.00 53.19  ? 604  MET A N     1 
ATOM   4863  C CA    . MET B 2 607  ? 127.708 145.479 174.057 1.00 53.19  ? 604  MET A CA    1 
ATOM   4864  C C     . MET B 2 607  ? 126.725 145.593 175.215 1.00 53.19  ? 604  MET A C     1 
ATOM   4865  O O     . MET B 2 607  ? 127.070 145.255 176.352 1.00 53.19  ? 604  MET A O     1 
ATOM   4866  C CB    . MET B 2 607  ? 128.454 146.801 173.877 1.00 53.19  ? 604  MET A CB    1 
ATOM   4867  C CG    . MET B 2 607  ? 129.694 146.689 173.018 1.00 53.19  ? 604  MET A CG    1 
ATOM   4868  S SD    . MET B 2 607  ? 131.106 146.065 173.942 1.00 53.19  ? 604  MET A SD    1 
ATOM   4869  C CE    . MET B 2 607  ? 131.126 147.196 175.330 1.00 53.19  ? 604  MET A CE    1 
ATOM   4870  N N     . ILE B 2 608  ? 125.508 146.072 174.952 1.00 56.52  ? 605  ILE A N     1 
ATOM   4871  C CA    . ILE B 2 608  ? 124.539 146.260 176.032 1.00 56.52  ? 605  ILE A CA    1 
ATOM   4872  C C     . ILE B 2 608  ? 124.165 144.940 176.697 1.00 56.52  ? 605  ILE A C     1 
ATOM   4873  O O     . ILE B 2 608  ? 124.265 144.848 177.932 1.00 56.52  ? 605  ILE A O     1 
ATOM   4874  C CB    . ILE B 2 608  ? 123.312 147.030 175.513 1.00 56.52  ? 605  ILE A CB    1 
ATOM   4875  C CG1   . ILE B 2 608  ? 123.587 148.530 175.493 1.00 56.52  ? 605  ILE A CG1   1 
ATOM   4876  C CG2   . ILE B 2 608  ? 122.090 146.739 176.373 1.00 56.52  ? 605  ILE A CG2   1 
ATOM   4877  C CD1   . ILE B 2 608  ? 122.596 149.288 174.659 1.00 56.52  ? 605  ILE A CD1   1 
ATOM   4878  N N     . PRO B 2 609  ? 123.733 143.898 175.974 1.00 56.98  ? 606  PRO A N     1 
ATOM   4879  C CA    . PRO B 2 609  ? 123.436 142.632 176.660 1.00 56.98  ? 606  PRO A CA    1 
ATOM   4880  C C     . PRO B 2 609  ? 124.652 142.011 177.316 1.00 56.98  ? 606  PRO A C     1 
ATOM   4881  O O     . PRO B 2 609  ? 124.518 141.351 178.353 1.00 56.98  ? 606  PRO A O     1 
ATOM   4882  C CB    . PRO B 2 609  ? 122.882 141.742 175.537 1.00 56.98  ? 606  PRO A CB    1 
ATOM   4883  C CG    . PRO B 2 609  ? 122.476 142.684 174.458 1.00 56.98  ? 606  PRO A CG    1 
ATOM   4884  C CD    . PRO B 2 609  ? 123.470 143.791 174.528 1.00 56.98  ? 606  PRO A CD    1 
ATOM   4885  N N     . LYS B 2 610  ? 125.839 142.209 176.739 1.00 57.08  ? 607  LYS A N     1 
ATOM   4886  C CA    . LYS B 2 610  ? 127.053 141.630 177.305 1.00 57.08  ? 607  LYS A CA    1 
ATOM   4887  C C     . LYS B 2 610  ? 127.322 142.172 178.703 1.00 57.08  ? 607  LYS A C     1 
ATOM   4888  O O     . LYS B 2 610  ? 127.679 141.420 179.617 1.00 57.08  ? 607  LYS A O     1 
ATOM   4889  C CB    . LYS B 2 610  ? 128.237 141.905 176.378 1.00 57.08  ? 607  LYS A CB    1 
ATOM   4890  C CG    . LYS B 2 610  ? 129.576 142.034 177.083 1.00 57.08  ? 607  LYS A CG    1 
ATOM   4891  C CD    . LYS B 2 610  ? 130.605 142.693 176.180 1.00 57.08  ? 607  LYS A CD    1 
ATOM   4892  C CE    . LYS B 2 610  ? 131.868 143.034 176.942 1.00 57.08  ? 607  LYS A CE    1 
ATOM   4893  N NZ    . LYS B 2 610  ? 132.446 141.838 177.612 1.00 57.08  ? 607  LYS A NZ    1 
ATOM   4894  N N     . CYS B 2 611  ? 127.149 143.478 178.890 1.00 58.49  ? 608  CYS A N     1 
ATOM   4895  C CA    . CYS B 2 611  ? 127.470 144.103 180.164 1.00 58.49  ? 608  CYS A CA    1 
ATOM   4896  C C     . CYS B 2 611  ? 126.278 144.216 181.104 1.00 58.49  ? 608  CYS A C     1 
ATOM   4897  O O     . CYS B 2 611  ? 126.463 144.618 182.258 1.00 58.49  ? 608  CYS A O     1 
ATOM   4898  C CB    . CYS B 2 611  ? 128.063 145.493 179.927 1.00 58.49  ? 608  CYS A CB    1 
ATOM   4899  S SG    . CYS B 2 611  ? 129.627 145.495 179.019 1.00 58.49  ? 608  CYS A SG    1 
ATOM   4900  N N     . SER B 2 612  ? 125.067 143.885 180.655 1.00 62.86  ? 609  SER A N     1 
ATOM   4901  C CA    . SER B 2 612  ? 123.877 144.090 181.475 1.00 62.86  ? 609  SER A CA    1 
ATOM   4902  C C     . SER B 2 612  ? 123.138 142.796 181.788 1.00 62.86  ? 609  SER A C     1 
ATOM   4903  O O     . SER B 2 612  ? 122.867 142.520 182.961 1.00 62.86  ? 609  SER A O     1 
ATOM   4904  C CB    . SER B 2 612  ? 122.938 145.089 180.788 1.00 62.86  ? 609  SER A CB    1 
ATOM   4905  O OG    . SER B 2 612  ? 121.893 145.480 181.658 1.00 62.86  ? 609  SER A OG    1 
ATOM   4906  N N     . THR B 2 613  ? 122.792 141.993 180.781 1.00 66.30  ? 610  THR A N     1 
ATOM   4907  C CA    . THR B 2 613  ? 121.932 140.838 180.991 1.00 66.30  ? 610  THR A CA    1 
ATOM   4908  C C     . THR B 2 613  ? 122.568 139.506 180.629 1.00 66.30  ? 610  THR A C     1 
ATOM   4909  O O     . THR B 2 613  ? 122.029 138.463 181.018 1.00 66.30  ? 610  THR A O     1 
ATOM   4910  C CB    . THR B 2 613  ? 120.626 140.988 180.193 1.00 66.30  ? 610  THR A CB    1 
ATOM   4911  O OG1   . THR B 2 613  ? 119.726 139.931 180.544 1.00 66.30  ? 610  THR A OG1   1 
ATOM   4912  C CG2   . THR B 2 613  ? 120.903 140.934 178.700 1.00 66.30  ? 610  THR A CG2   1 
ATOM   4913  N N     . GLN B 2 614  ? 123.680 139.499 179.899 1.00 61.53  ? 611  GLN A N     1 
ATOM   4914  C CA    . GLN B 2 614  ? 124.339 138.260 179.512 1.00 61.53  ? 611  GLN A CA    1 
ATOM   4915  C C     . GLN B 2 614  ? 125.695 138.085 180.178 1.00 61.53  ? 611  GLN A C     1 
ATOM   4916  O O     . GLN B 2 614  ? 126.505 137.280 179.706 1.00 61.53  ? 611  GLN A O     1 
ATOM   4917  C CB    . GLN B 2 614  ? 124.486 138.192 177.992 1.00 61.53  ? 611  GLN A CB    1 
ATOM   4918  C CG    . GLN B 2 614  ? 123.166 138.255 177.246 1.00 61.53  ? 611  GLN A CG    1 
ATOM   4919  C CD    . GLN B 2 614  ? 122.555 136.886 177.021 1.00 61.53  ? 611  GLN A CD    1 
ATOM   4920  O OE1   . GLN B 2 614  ? 122.469 136.071 177.940 1.00 61.53  ? 611  GLN A OE1   1 
ATOM   4921  N NE2   . GLN B 2 614  ? 122.126 136.625 175.791 1.00 61.53  ? 611  GLN A NE2   1 
ATOM   4922  N N     . LEU B 2 615  ? 125.968 138.817 181.253 1.00 60.56  ? 612  LEU A N     1 
ATOM   4923  C CA    . LEU B 2 615  ? 127.201 138.597 181.986 1.00 60.56  ? 612  LEU A CA    1 
ATOM   4924  C C     . LEU B 2 615  ? 127.038 137.434 182.961 1.00 60.56  ? 612  LEU A C     1 
ATOM   4925  O O     . LEU B 2 615  ? 125.927 136.978 183.249 1.00 60.56  ? 612  LEU A O     1 
ATOM   4926  C CB    . LEU B 2 615  ? 127.643 139.862 182.729 1.00 60.56  ? 612  LEU A CB    1 
ATOM   4927  C CG    . LEU B 2 615  ? 126.911 140.358 183.975 1.00 60.56  ? 612  LEU A CG    1 
ATOM   4928  C CD1   . LEU B 2 615  ? 127.778 141.357 184.715 1.00 60.56  ? 612  LEU A CD1   1 
ATOM   4929  C CD2   . LEU B 2 615  ? 125.609 141.014 183.591 1.00 60.56  ? 612  LEU A CD2   1 
ATOM   4930  N N     . LYS B 2 616  ? 128.176 136.948 183.463 1.00 55.77  ? 613  LYS A N     1 
ATOM   4931  C CA    . LYS B 2 616  ? 128.178 135.738 184.279 1.00 55.77  ? 613  LYS A CA    1 
ATOM   4932  C C     . LYS B 2 616  ? 127.395 135.929 185.573 1.00 55.77  ? 613  LYS A C     1 
ATOM   4933  O O     . LYS B 2 616  ? 126.774 134.986 186.075 1.00 55.77  ? 613  LYS A O     1 
ATOM   4934  C CB    . LYS B 2 616  ? 129.617 135.320 184.581 1.00 55.77  ? 613  LYS A CB    1 
ATOM   4935  C CG    . LYS B 2 616  ? 129.814 133.823 184.726 1.00 55.77  ? 613  LYS A CG    1 
ATOM   4936  C CD    . LYS B 2 616  ? 131.279 133.448 184.589 1.00 55.77  ? 613  LYS A CD    1 
ATOM   4937  C CE    . LYS B 2 616  ? 131.853 133.949 183.275 1.00 55.77  ? 613  LYS A CE    1 
ATOM   4938  N NZ    . LYS B 2 616  ? 131.047 133.494 182.109 1.00 55.77  ? 613  LYS A NZ    1 
ATOM   4939  N N     . ALA B 2 617  ? 127.419 137.140 186.131 1.00 62.89  ? 614  ALA A N     1 
ATOM   4940  C CA    . ALA B 2 617  ? 126.790 137.371 187.427 1.00 62.89  ? 614  ALA A CA    1 
ATOM   4941  C C     . ALA B 2 617  ? 125.276 137.207 187.355 1.00 62.89  ? 614  ALA A C     1 
ATOM   4942  O O     . ALA B 2 617  ? 124.681 136.483 188.161 1.00 62.89  ? 614  ALA A O     1 
ATOM   4943  C CB    . ALA B 2 617  ? 127.158 138.760 187.946 1.00 62.89  ? 614  ALA A CB    1 
ATOM   4944  N N     . VAL B 2 618  ? 124.631 137.870 186.391 1.00 72.06  ? 615  VAL A N     1 
ATOM   4945  C CA    . VAL B 2 618  ? 123.170 137.876 186.374 1.00 72.06  ? 615  VAL A CA    1 
ATOM   4946  C C     . VAL B 2 618  ? 122.624 136.589 185.768 1.00 72.06  ? 615  VAL A C     1 
ATOM   4947  O O     . VAL B 2 618  ? 121.522 136.151 186.123 1.00 72.06  ? 615  VAL A O     1 
ATOM   4948  C CB    . VAL B 2 618  ? 122.636 139.120 185.637 1.00 72.06  ? 615  VAL A CB    1 
ATOM   4949  C CG1   . VAL B 2 618  ? 122.795 138.974 184.134 1.00 72.06  ? 615  VAL A CG1   1 
ATOM   4950  C CG2   . VAL B 2 618  ? 121.181 139.371 186.004 1.00 72.06  ? 615  VAL A CG2   1 
ATOM   4951  N N     . THR B 2 619  ? 123.365 135.965 184.849 1.00 67.20  ? 616  THR A N     1 
ATOM   4952  C CA    . THR B 2 619  ? 122.912 134.705 184.270 1.00 67.20  ? 616  THR A CA    1 
ATOM   4953  C C     . THR B 2 619  ? 122.821 133.621 185.337 1.00 67.20  ? 616  THR A C     1 
ATOM   4954  O O     . THR B 2 619  ? 121.840 132.871 185.399 1.00 67.20  ? 616  THR A O     1 
ATOM   4955  C CB    . THR B 2 619  ? 123.852 134.279 183.141 1.00 67.20  ? 616  THR A CB    1 
ATOM   4956  O OG1   . THR B 2 619  ? 123.638 135.117 181.999 1.00 67.20  ? 616  THR A OG1   1 
ATOM   4957  C CG2   . THR B 2 619  ? 123.601 132.831 182.751 1.00 67.20  ? 616  THR A CG2   1 
ATOM   4958  N N     . ALA B 2 620  ? 123.837 133.535 186.198 1.00 69.54  ? 617  ALA A N     1 
ATOM   4959  C CA    . ALA B 2 620  ? 123.796 132.574 187.294 1.00 69.54  ? 617  ALA A CA    1 
ATOM   4960  C C     . ALA B 2 620  ? 122.787 132.989 188.356 1.00 69.54  ? 617  ALA A C     1 
ATOM   4961  O O     . ALA B 2 620  ? 122.075 132.143 188.909 1.00 69.54  ? 617  ALA A O     1 
ATOM   4962  C CB    . ALA B 2 620  ? 125.188 132.416 187.905 1.00 69.54  ? 617  ALA A CB    1 
ATOM   4963  N N     . HIS B 2 621  ? 122.717 134.287 188.660 1.00 74.57  ? 618  HIS A N     1 
ATOM   4964  C CA    . HIS B 2 621  ? 121.810 134.755 189.704 1.00 74.57  ? 618  HIS A CA    1 
ATOM   4965  C C     . HIS B 2 621  ? 120.356 134.496 189.335 1.00 74.57  ? 618  HIS A C     1 
ATOM   4966  O O     . HIS B 2 621  ? 119.562 134.063 190.177 1.00 74.57  ? 618  HIS A O     1 
ATOM   4967  C CB    . HIS B 2 621  ? 122.033 136.243 189.972 1.00 74.57  ? 618  HIS A CB    1 
ATOM   4968  C CG    . HIS B 2 621  ? 121.189 136.788 191.081 1.00 74.57  ? 618  HIS A CG    1 
ATOM   4969  N ND1   . HIS B 2 621  ? 119.896 137.224 190.888 1.00 74.57  ? 618  HIS A ND1   1 
ATOM   4970  C CD2   . HIS B 2 621  ? 121.452 136.965 192.398 1.00 74.57  ? 618  HIS A CD2   1 
ATOM   4971  C CE1   . HIS B 2 621  ? 119.399 137.646 192.037 1.00 74.57  ? 618  HIS A CE1   1 
ATOM   4972  N NE2   . HIS B 2 621  ? 120.323 137.501 192.969 1.00 74.57  ? 618  HIS A NE2   1 
ATOM   4973  N N     . PHE B 2 622  ? 119.985 134.756 188.082 1.00 77.77  ? 619  PHE A N     1 
ATOM   4974  C CA    . PHE B 2 622  ? 118.617 134.510 187.647 1.00 77.77  ? 619  PHE A CA    1 
ATOM   4975  C C     . PHE B 2 622  ? 118.305 133.026 187.522 1.00 77.77  ? 619  PHE A C     1 
ATOM   4976  O O     . PHE B 2 622  ? 117.128 132.650 187.549 1.00 77.77  ? 619  PHE A O     1 
ATOM   4977  C CB    . PHE B 2 622  ? 118.355 135.212 186.313 1.00 77.77  ? 619  PHE A CB    1 
ATOM   4978  C CG    . PHE B 2 622  ? 118.024 136.670 186.451 1.00 77.77  ? 619  PHE A CG    1 
ATOM   4979  C CD1   . PHE B 2 622  ? 117.961 137.266 187.700 1.00 77.77  ? 619  PHE A CD1   1 
ATOM   4980  C CD2   . PHE B 2 622  ? 117.782 137.447 185.332 1.00 77.77  ? 619  PHE A CD2   1 
ATOM   4981  C CE1   . PHE B 2 622  ? 117.658 138.608 187.831 1.00 77.77  ? 619  PHE A CE1   1 
ATOM   4982  C CE2   . PHE B 2 622  ? 117.480 138.790 185.455 1.00 77.77  ? 619  PHE A CE2   1 
ATOM   4983  C CZ    . PHE B 2 622  ? 117.418 139.371 186.706 1.00 77.77  ? 619  PHE A CZ    1 
ATOM   4984  N N     . GLN B 2 623  ? 119.327 132.181 187.387 1.00 72.89  ? 620  GLN A N     1 
ATOM   4985  C CA    . GLN B 2 623  ? 119.101 130.743 187.324 1.00 72.89  ? 620  GLN A CA    1 
ATOM   4986  C C     . GLN B 2 623  ? 118.751 130.175 188.695 1.00 72.89  ? 620  GLN A C     1 
ATOM   4987  O O     . GLN B 2 623  ? 117.857 129.330 188.810 1.00 72.89  ? 620  GLN A O     1 
ATOM   4988  C CB    . GLN B 2 623  ? 120.342 130.047 186.757 1.00 72.89  ? 620  GLN A CB    1 
ATOM   4989  C CG    . GLN B 2 623  ? 120.351 128.506 186.766 1.00 72.89  ? 620  GLN A CG    1 
ATOM   4990  C CD    . GLN B 2 623  ? 119.149 127.845 186.087 1.00 72.89  ? 620  GLN A CD    1 
ATOM   4991  O OE1   . GLN B 2 623  ? 117.992 128.165 186.353 1.00 72.89  ? 620  GLN A OE1   1 
ATOM   4992  N NE2   . GLN B 2 623  ? 119.438 126.906 185.193 1.00 72.89  ? 620  GLN A NE2   1 
ATOM   4993  N N     . THR B 2 624  ? 119.433 130.636 189.745 1.00 75.22  ? 621  THR A N     1 
ATOM   4994  C CA    . THR B 2 624  ? 119.278 130.085 191.086 1.00 75.22  ? 621  THR A CA    1 
ATOM   4995  C C     . THR B 2 624  ? 118.581 131.047 192.044 1.00 75.22  ? 621  THR A C     1 
ATOM   4996  O O     . THR B 2 624  ? 118.611 130.830 193.259 1.00 75.22  ? 621  THR A O     1 
ATOM   4997  C CB    . THR B 2 624  ? 120.640 129.681 191.652 1.00 75.22  ? 621  THR A CB    1 
ATOM   4998  O OG1   . THR B 2 624  ? 121.440 130.852 191.858 1.00 75.22  ? 621  THR A OG1   1 
ATOM   4999  C CG2   . THR B 2 624  ? 121.360 128.748 190.690 1.00 75.22  ? 621  THR A CG2   1 
ATOM   5000  N N     . HIS B 2 625  ? 117.953 132.100 191.527 1.00 75.88  ? 622  HIS A N     1 
ATOM   5001  C CA    . HIS B 2 625  ? 117.261 133.055 192.380 1.00 75.88  ? 622  HIS A CA    1 
ATOM   5002  C C     . HIS B 2 625  ? 116.306 133.861 191.512 1.00 75.88  ? 622  HIS A C     1 
ATOM   5003  O O     . HIS B 2 625  ? 116.696 134.350 190.449 1.00 75.88  ? 622  HIS A O     1 
ATOM   5004  C CB    . HIS B 2 625  ? 118.260 133.972 193.100 1.00 75.88  ? 622  HIS A CB    1 
ATOM   5005  C CG    . HIS B 2 625  ? 117.638 134.871 194.122 1.00 75.88  ? 622  HIS A CG    1 
ATOM   5006  N ND1   . HIS B 2 625  ? 118.314 135.933 194.684 1.00 75.88  ? 622  HIS A ND1   1 
ATOM   5007  C CD2   . HIS B 2 625  ? 116.411 134.861 194.693 1.00 75.88  ? 622  HIS A CD2   1 
ATOM   5008  C CE1   . HIS B 2 625  ? 117.530 136.538 195.557 1.00 75.88  ? 622  HIS A CE1   1 
ATOM   5009  N NE2   . HIS B 2 625  ? 116.367 135.911 195.578 1.00 75.88  ? 622  HIS A NE2   1 
ATOM   5010  N N     . THR B 2 626  ? 115.061 133.994 191.970 1.00 82.92  ? 623  THR A N     1 
ATOM   5011  C CA    . THR B 2 626  ? 113.972 134.520 191.153 1.00 82.92  ? 623  THR A CA    1 
ATOM   5012  C C     . THR B 2 626  ? 113.586 135.950 191.525 1.00 82.92  ? 623  THR A C     1 
ATOM   5013  O O     . THR B 2 626  ? 112.409 136.314 191.464 1.00 82.92  ? 623  THR A O     1 
ATOM   5014  C CB    . THR B 2 626  ? 112.752 133.603 191.246 1.00 82.92  ? 623  THR A CB    1 
ATOM   5015  O OG1   . THR B 2 626  ? 111.659 134.183 190.523 1.00 82.92  ? 623  THR A OG1   1 
ATOM   5016  C CG2   . THR B 2 626  ? 112.348 133.388 192.700 1.00 82.92  ? 623  THR A CG2   1 
ATOM   5017  N N     . THR B 2 627  ? 114.558 136.775 191.902 1.00 81.76  ? 624  THR A N     1 
ATOM   5018  C CA    . THR B 2 627  ? 114.296 138.177 192.182 1.00 81.76  ? 624  THR A CA    1 
ATOM   5019  C C     . THR B 2 627  ? 115.276 139.048 191.412 1.00 81.76  ? 624  THR A C     1 
ATOM   5020  O O     . THR B 2 627  ? 116.386 138.608 191.093 1.00 81.76  ? 624  THR A O     1 
ATOM   5021  C CB    . THR B 2 627  ? 114.411 138.491 193.682 1.00 81.76  ? 624  THR A CB    1 
ATOM   5022  O OG1   . THR B 2 627  ? 115.768 138.326 194.103 1.00 81.76  ? 624  THR A OG1   1 
ATOM   5023  C CG2   . THR B 2 627  ? 113.511 137.574 194.499 1.00 81.76  ? 624  THR A CG2   1 
ATOM   5024  N N     . PRO B 2 628  ? 114.889 140.282 191.089 1.00 80.95  ? 625  PRO A N     1 
ATOM   5025  C CA    . PRO B 2 628  ? 115.818 141.189 190.403 1.00 80.95  ? 625  PRO A CA    1 
ATOM   5026  C C     . PRO B 2 628  ? 117.056 141.470 191.244 1.00 80.95  ? 625  PRO A C     1 
ATOM   5027  O O     . PRO B 2 628  ? 116.992 141.548 192.473 1.00 80.95  ? 625  PRO A O     1 
ATOM   5028  C CB    . PRO B 2 628  ? 114.984 142.458 190.187 1.00 80.95  ? 625  PRO A CB    1 
ATOM   5029  C CG    . PRO B 2 628  ? 113.818 142.331 191.122 1.00 80.95  ? 625  PRO A CG    1 
ATOM   5030  C CD    . PRO B 2 628  ? 113.546 140.869 191.218 1.00 80.95  ? 625  PRO A CD    1 
ATOM   5031  N N     . ILE B 2 629  ? 118.189 141.626 190.565 1.00 78.51  ? 626  ILE A N     1 
ATOM   5032  C CA    . ILE B 2 629  ? 119.470 141.870 191.216 1.00 78.51  ? 626  ILE A CA    1 
ATOM   5033  C C     . ILE B 2 629  ? 119.978 143.245 190.802 1.00 78.51  ? 626  ILE A C     1 
ATOM   5034  O O     . ILE B 2 629  ? 119.699 143.732 189.701 1.00 78.51  ? 626  ILE A O     1 
ATOM   5035  C CB    . ILE B 2 629  ? 120.499 140.768 190.880 1.00 78.51  ? 626  ILE A CB    1 
ATOM   5036  C CG1   . ILE B 2 629  ? 121.722 140.864 191.796 1.00 78.51  ? 626  ILE A CG1   1 
ATOM   5037  C CG2   . ILE B 2 629  ? 120.915 140.841 189.419 1.00 78.51  ? 626  ILE A CG2   1 
ATOM   5038  C CD1   . ILE B 2 629  ? 121.401 140.696 193.266 1.00 78.51  ? 626  ILE A CD1   1 
ATOM   5039  N N     . LEU B 2 630  ? 120.719 143.879 191.706 1.00 75.62  ? 627  LEU A N     1 
ATOM   5040  C CA    . LEU B 2 630  ? 121.245 145.219 191.496 1.00 75.62  ? 627  LEU A CA    1 
ATOM   5041  C C     . LEU B 2 630  ? 122.705 145.145 191.067 1.00 75.62  ? 627  LEU A C     1 
ATOM   5042  O O     . LEU B 2 630  ? 123.504 144.423 191.670 1.00 75.62  ? 627  LEU A O     1 
ATOM   5043  C CB    . LEU B 2 630  ? 121.118 146.060 192.769 1.00 75.62  ? 627  LEU A CB    1 
ATOM   5044  C CG    . LEU B 2 630  ? 119.803 146.809 193.012 1.00 75.62  ? 627  LEU A CG    1 
ATOM   5045  C CD1   . LEU B 2 630  ? 119.531 147.803 191.895 1.00 75.62  ? 627  LEU A CD1   1 
ATOM   5046  C CD2   . LEU B 2 630  ? 118.630 145.851 193.183 1.00 75.62  ? 627  LEU A CD2   1 
ATOM   5047  N N     . LEU B 2 631  ? 123.047 145.897 190.025 1.00 67.10  ? 628  LEU A N     1 
ATOM   5048  C CA    . LEU B 2 631  ? 124.406 145.959 189.506 1.00 67.10  ? 628  LEU A CA    1 
ATOM   5049  C C     . LEU B 2 631  ? 125.063 147.250 189.971 1.00 67.10  ? 628  LEU A C     1 
ATOM   5050  O O     . LEU B 2 631  ? 124.532 148.340 189.737 1.00 67.10  ? 628  LEU A O     1 
ATOM   5051  C CB    . LEU B 2 631  ? 124.413 145.880 187.978 1.00 67.10  ? 628  LEU A CB    1 
ATOM   5052  C CG    . LEU B 2 631  ? 123.579 144.760 187.354 1.00 67.10  ? 628  LEU A CG    1 
ATOM   5053  C CD1   . LEU B 2 631  ? 123.330 145.030 185.880 1.00 67.10  ? 628  LEU A CD1   1 
ATOM   5054  C CD2   . LEU B 2 631  ? 124.262 143.416 187.546 1.00 67.10  ? 628  LEU A CD2   1 
ATOM   5055  N N     . SER B 2 632  ? 126.216 147.126 190.620 1.00 67.03  ? 629  SER A N     1 
ATOM   5056  C CA    . SER B 2 632  ? 126.922 148.271 191.181 1.00 67.03  ? 629  SER A CA    1 
ATOM   5057  C C     . SER B 2 632  ? 128.223 148.591 190.464 1.00 67.03  ? 629  SER A C     1 
ATOM   5058  O O     . SER B 2 632  ? 128.514 149.767 190.228 1.00 67.03  ? 629  SER A O     1 
ATOM   5059  C CB    . SER B 2 632  ? 127.209 148.036 192.671 1.00 67.03  ? 629  SER A CB    1 
ATOM   5060  O OG    . SER B 2 632  ? 128.193 147.033 192.850 1.00 67.03  ? 629  SER A OG    1 
ATOM   5061  N N     . ASN B 2 633  ? 129.018 147.581 190.119 1.00 62.20  ? 630  ASN A N     1 
ATOM   5062  C CA    . ASN B 2 633  ? 130.281 147.824 189.435 1.00 62.20  ? 630  ASN A CA    1 
ATOM   5063  C C     . ASN B 2 633  ? 130.033 148.418 188.054 1.00 62.20  ? 630  ASN A C     1 
ATOM   5064  O O     . ASN B 2 633  ? 129.153 147.961 187.318 1.00 62.20  ? 630  ASN A O     1 
ATOM   5065  C CB    . ASN B 2 633  ? 131.076 146.523 189.319 1.00 62.20  ? 630  ASN A CB    1 
ATOM   5066  C CG    . ASN B 2 633  ? 132.544 146.762 189.024 1.00 62.20  ? 630  ASN A CG    1 
ATOM   5067  O OD1   . ASN B 2 633  ? 132.982 147.901 188.872 1.00 62.20  ? 630  ASN A OD1   1 
ATOM   5068  N ND2   . ASN B 2 633  ? 133.313 145.682 188.943 1.00 62.20  ? 630  ASN A ND2   1 
ATOM   5069  N N     . ASN B 2 634  ? 130.820 149.439 187.706 1.00 61.51  ? 631  ASN A N     1 
ATOM   5070  C CA    . ASN B 2 634  ? 130.698 150.145 186.429 1.00 61.51  ? 631  ASN A CA    1 
ATOM   5071  C C     . ASN B 2 634  ? 129.290 150.711 186.240 1.00 61.51  ? 631  ASN A C     1 
ATOM   5072  O O     . ASN B 2 634  ? 128.701 150.631 185.161 1.00 61.51  ? 631  ASN A O     1 
ATOM   5073  C CB    . ASN B 2 634  ? 131.087 149.238 185.259 1.00 61.51  ? 631  ASN A CB    1 
ATOM   5074  C CG    . ASN B 2 634  ? 132.539 148.815 185.310 1.00 61.51  ? 631  ASN A CG    1 
ATOM   5075  O OD1   . ASN B 2 634  ? 132.848 147.635 185.479 1.00 61.51  ? 631  ASN A OD1   1 
ATOM   5076  N ND2   . ASN B 2 634  ? 133.442 149.777 185.164 1.00 61.51  ? 631  ASN A ND2   1 
ATOM   5077  N N     . PHE B 2 635  ? 128.754 151.297 187.308 1.00 60.13  ? 632  PHE A N     1 
ATOM   5078  C CA    . PHE B 2 635  ? 127.423 151.888 187.278 1.00 60.13  ? 632  PHE A CA    1 
ATOM   5079  C C     . PHE B 2 635  ? 127.385 153.075 188.227 1.00 60.13  ? 632  PHE A C     1 
ATOM   5080  O O     . PHE B 2 635  ? 127.803 152.959 189.383 1.00 60.13  ? 632  PHE A O     1 
ATOM   5081  C CB    . PHE B 2 635  ? 126.354 150.864 187.669 1.00 60.13  ? 632  PHE A CB    1 
ATOM   5082  C CG    . PHE B 2 635  ? 125.842 150.049 186.519 1.00 60.13  ? 632  PHE A CG    1 
ATOM   5083  C CD1   . PHE B 2 635  ? 124.777 150.497 185.760 1.00 60.13  ? 632  PHE A CD1   1 
ATOM   5084  C CD2   . PHE B 2 635  ? 126.416 148.832 186.205 1.00 60.13  ? 632  PHE A CD2   1 
ATOM   5085  C CE1   . PHE B 2 635  ? 124.299 149.750 184.703 1.00 60.13  ? 632  PHE A CE1   1 
ATOM   5086  C CE2   . PHE B 2 635  ? 125.942 148.079 185.150 1.00 60.13  ? 632  PHE A CE2   1 
ATOM   5087  C CZ    . PHE B 2 635  ? 124.883 148.538 184.399 1.00 60.13  ? 632  PHE A CZ    1 
ATOM   5088  N N     . ILE B 2 636  ? 126.885 154.212 187.738 1.00 68.23  ? 633  ILE A N     1 
ATOM   5089  C CA    . ILE B 2 636  ? 126.759 155.392 188.590 1.00 68.23  ? 633  ILE A CA    1 
ATOM   5090  C C     . ILE B 2 636  ? 125.702 155.165 189.663 1.00 68.23  ? 633  ILE A C     1 
ATOM   5091  O O     . ILE B 2 636  ? 125.929 155.440 190.848 1.00 68.23  ? 633  ILE A O     1 
ATOM   5092  C CB    . ILE B 2 636  ? 126.446 156.635 187.738 1.00 68.23  ? 633  ILE A CB    1 
ATOM   5093  C CG1   . ILE B 2 636  ? 127.608 156.936 186.788 1.00 68.23  ? 633  ILE A CG1   1 
ATOM   5094  C CG2   . ILE B 2 636  ? 126.151 157.834 188.627 1.00 68.23  ? 633  ILE A CG2   1 
ATOM   5095  C CD1   . ILE B 2 636  ? 128.939 157.101 187.490 1.00 68.23  ? 633  ILE A CD1   1 
ATOM   5096  N N     . GLU B 2 637  ? 124.540 154.656 189.272 1.00 67.95  ? 634  GLU A N     1 
ATOM   5097  C CA    . GLU B 2 637  ? 123.451 154.314 190.170 1.00 67.95  ? 634  GLU A CA    1 
ATOM   5098  C C     . GLU B 2 637  ? 123.038 152.881 189.875 1.00 67.95  ? 634  GLU A C     1 
ATOM   5099  O O     . GLU B 2 637  ? 122.917 152.500 188.707 1.00 67.95  ? 634  GLU A O     1 
ATOM   5100  C CB    . GLU B 2 637  ? 122.252 155.257 189.972 1.00 67.95  ? 634  GLU A CB    1 
ATOM   5101  C CG    . GLU B 2 637  ? 121.115 155.222 191.021 1.00 67.95  ? 634  GLU A CG    1 
ATOM   5102  C CD    . GLU B 2 637  ? 121.558 155.239 192.489 1.00 67.95  ? 634  GLU A CD    1 
ATOM   5103  O OE1   . GLU B 2 637  ? 122.750 155.465 192.790 1.00 67.95  ? 634  GLU A OE1   1 
ATOM   5104  O OE2   . GLU B 2 637  ? 120.689 155.021 193.359 1.00 67.95  ? 634  GLU A OE2   1 
ATOM   5105  N N     . PRO B 2 638  ? 122.835 152.059 190.906 1.00 70.55  ? 635  PRO A N     1 
ATOM   5106  C CA    . PRO B 2 638  ? 122.573 150.635 190.667 1.00 70.55  ? 635  PRO A CA    1 
ATOM   5107  C C     . PRO B 2 638  ? 121.353 150.405 189.786 1.00 70.55  ? 635  PRO A C     1 
ATOM   5108  O O     . PRO B 2 638  ? 120.340 151.098 189.894 1.00 70.55  ? 635  PRO A O     1 
ATOM   5109  C CB    . PRO B 2 638  ? 122.363 150.076 192.078 1.00 70.55  ? 635  PRO A CB    1 
ATOM   5110  C CG    . PRO B 2 638  ? 123.168 150.974 192.944 1.00 70.55  ? 635  PRO A CG    1 
ATOM   5111  C CD    . PRO B 2 638  ? 123.044 152.343 192.336 1.00 70.55  ? 635  PRO A CD    1 
ATOM   5112  N N     . LEU B 2 639  ? 121.468 149.413 188.907 1.00 70.90  ? 636  LEU A N     1 
ATOM   5113  C CA    . LEU B 2 639  ? 120.426 149.058 187.953 1.00 70.90  ? 636  LEU A CA    1 
ATOM   5114  C C     . LEU B 2 639  ? 119.735 147.786 188.418 1.00 70.90  ? 636  LEU A C     1 
ATOM   5115  O O     . LEU B 2 639  ? 120.398 146.796 188.740 1.00 70.90  ? 636  LEU A O     1 
ATOM   5116  C CB    . LEU B 2 639  ? 121.010 148.858 186.553 1.00 70.90  ? 636  LEU A CB    1 
ATOM   5117  C CG    . LEU B 2 639  ? 120.125 148.138 185.531 1.00 70.90  ? 636  LEU A CG    1 
ATOM   5118  C CD1   . LEU B 2 639  ? 118.865 148.937 185.239 1.00 70.90  ? 636  LEU A CD1   1 
ATOM   5119  C CD2   . LEU B 2 639  ? 120.896 147.858 184.250 1.00 70.90  ? 636  LEU A CD2   1 
ATOM   5120  N N     . GLU B 2 640  ? 118.404 147.815 188.446 1.00 80.19  ? 637  GLU A N     1 
ATOM   5121  C CA    . GLU B 2 640  ? 117.612 146.680 188.912 1.00 80.19  ? 637  GLU A CA    1 
ATOM   5122  C C     . GLU B 2 640  ? 117.141 145.891 187.694 1.00 80.19  ? 637  GLU A C     1 
ATOM   5123  O O     . GLU B 2 640  ? 116.028 146.060 187.194 1.00 80.19  ? 637  GLU A O     1 
ATOM   5124  C CB    . GLU B 2 640  ? 116.447 147.158 189.773 1.00 80.19  ? 637  GLU A CB    1 
ATOM   5125  C CG    . GLU B 2 640  ? 115.683 146.043 190.464 1.00 80.19  ? 637  GLU A CG    1 
ATOM   5126  C CD    . GLU B 2 640  ? 114.798 146.554 191.583 1.00 80.19  ? 637  GLU A CD    1 
ATOM   5127  O OE1   . GLU B 2 640  ? 114.110 147.575 191.378 1.00 80.19  ? 637  GLU A OE1   1 
ATOM   5128  O OE2   . GLU B 2 640  ? 114.791 145.934 192.668 1.00 80.19  ? 637  GLU A OE2   1 
ATOM   5129  N N     . ILE B 2 641  ? 118.020 145.015 187.206 1.00 76.72  ? 638  ILE A N     1 
ATOM   5130  C CA    . ILE B 2 641  ? 117.650 144.118 186.119 1.00 76.72  ? 638  ILE A CA    1 
ATOM   5131  C C     . ILE B 2 641  ? 116.689 143.062 186.647 1.00 76.72  ? 638  ILE A C     1 
ATOM   5132  O O     . ILE B 2 641  ? 116.942 142.427 187.679 1.00 76.72  ? 638  ILE A O     1 
ATOM   5133  C CB    . ILE B 2 641  ? 118.899 143.487 185.485 1.00 76.72  ? 638  ILE A CB    1 
ATOM   5134  C CG1   . ILE B 2 641  ? 118.491 142.472 184.416 1.00 76.72  ? 638  ILE A CG1   1 
ATOM   5135  C CG2   . ILE B 2 641  ? 119.797 142.859 186.541 1.00 76.72  ? 638  ILE A CG2   1 
ATOM   5136  C CD1   . ILE B 2 641  ? 119.637 141.985 183.574 1.00 76.72  ? 638  ILE A CD1   1 
ATOM   5137  N N     . THR B 2 642  ? 115.578 142.872 185.942 1.00 77.92  ? 639  THR A N     1 
ATOM   5138  C CA    . THR B 2 642  ? 114.496 142.017 186.400 1.00 77.92  ? 639  THR A CA    1 
ATOM   5139  C C     . THR B 2 642  ? 114.472 140.750 185.548 1.00 77.92  ? 639  THR A C     1 
ATOM   5140  O O     . THR B 2 642  ? 115.066 140.694 184.470 1.00 77.92  ? 639  THR A O     1 
ATOM   5141  C CB    . THR B 2 642  ? 113.159 142.774 186.338 1.00 77.92  ? 639  THR A CB    1 
ATOM   5142  O OG1   . THR B 2 642  ? 113.305 144.026 187.018 1.00 77.92  ? 639  THR A OG1   1 
ATOM   5143  C CG2   . THR B 2 642  ? 112.064 142.010 187.059 1.00 77.92  ? 639  THR A CG2   1 
ATOM   5144  N N     . LYS B 2 643  ? 113.795 139.715 186.055 1.00 82.27  ? 640  LYS A N     1 
ATOM   5145  C CA    . LYS B 2 643  ? 113.911 138.382 185.469 1.00 82.27  ? 640  LYS A CA    1 
ATOM   5146  C C     . LYS B 2 643  ? 113.322 138.293 184.064 1.00 82.27  ? 640  LYS A C     1 
ATOM   5147  O O     . LYS B 2 643  ? 113.894 137.610 183.206 1.00 82.27  ? 640  LYS A O     1 
ATOM   5148  C CB    . LYS B 2 643  ? 113.245 137.350 186.378 1.00 82.27  ? 640  LYS A CB    1 
ATOM   5149  C CG    . LYS B 2 643  ? 113.683 135.921 186.101 1.00 82.27  ? 640  LYS A CG    1 
ATOM   5150  C CD    . LYS B 2 643  ? 113.635 135.064 187.353 1.00 82.27  ? 640  LYS A CD    1 
ATOM   5151  C CE    . LYS B 2 643  ? 113.987 133.621 187.035 1.00 82.27  ? 640  LYS A CE    1 
ATOM   5152  N NZ    . LYS B 2 643  ? 113.901 132.744 188.233 1.00 82.27  ? 640  LYS A NZ    1 
ATOM   5153  N N     . GLU B 2 644  ? 112.186 138.947 183.807 1.00 82.22  ? 641  GLU A N     1 
ATOM   5154  C CA    . GLU B 2 644  ? 111.484 138.725 182.544 1.00 82.22  ? 641  GLU A CA    1 
ATOM   5155  C C     . GLU B 2 644  ? 112.316 139.174 181.348 1.00 82.22  ? 641  GLU A C     1 
ATOM   5156  O O     . GLU B 2 644  ? 112.373 138.480 180.327 1.00 82.22  ? 641  GLU A O     1 
ATOM   5157  C CB    . GLU B 2 644  ? 110.118 139.420 182.554 1.00 82.22  ? 641  GLU A CB    1 
ATOM   5158  C CG    . GLU B 2 644  ? 110.154 140.929 182.708 1.00 82.22  ? 641  GLU A CG    1 
ATOM   5159  C CD    . GLU B 2 644  ? 110.159 141.352 184.158 1.00 82.22  ? 641  GLU A CD    1 
ATOM   5160  O OE1   . GLU B 2 644  ? 110.336 140.471 185.025 1.00 82.22  ? 641  GLU A OE1   1 
ATOM   5161  O OE2   . GLU B 2 644  ? 109.990 142.559 184.432 1.00 82.22  ? 641  GLU A OE2   1 
ATOM   5162  N N     . ILE B 2 645  ? 112.985 140.325 181.456 1.00 81.42  ? 642  ILE A N     1 
ATOM   5163  C CA    . ILE B 2 645  ? 113.725 140.854 180.313 1.00 81.42  ? 642  ILE A CA    1 
ATOM   5164  C C     . ILE B 2 645  ? 114.874 139.924 179.939 1.00 81.42  ? 642  ILE A C     1 
ATOM   5165  O O     . ILE B 2 645  ? 115.204 139.769 178.757 1.00 81.42  ? 642  ILE A O     1 
ATOM   5166  C CB    . ILE B 2 645  ? 114.211 142.287 180.598 1.00 81.42  ? 642  ILE A CB    1 
ATOM   5167  C CG1   . ILE B 2 645  ? 115.067 142.328 181.861 1.00 81.42  ? 642  ILE A CG1   1 
ATOM   5168  C CG2   . ILE B 2 645  ? 113.029 143.231 180.729 1.00 81.42  ? 642  ILE A CG2   1 
ATOM   5169  C CD1   . ILE B 2 645  ? 115.710 143.660 182.114 1.00 81.42  ? 642  ILE A CD1   1 
ATOM   5170  N N     . TYR B 2 646  ? 115.505 139.295 180.934 1.00 82.33  ? 643  TYR A N     1 
ATOM   5171  C CA    . TYR B 2 646  ? 116.479 138.250 180.637 1.00 82.33  ? 643  TYR A CA    1 
ATOM   5172  C C     . TYR B 2 646  ? 115.808 137.043 179.997 1.00 82.33  ? 643  TYR A C     1 
ATOM   5173  O O     . TYR B 2 646  ? 116.369 136.420 179.087 1.00 82.33  ? 643  TYR A O     1 
ATOM   5174  C CB    . TYR B 2 646  ? 117.223 137.844 181.908 1.00 82.33  ? 643  TYR A CB    1 
ATOM   5175  C CG    . TYR B 2 646  ? 118.134 136.650 181.726 1.00 82.33  ? 643  TYR A CG    1 
ATOM   5176  C CD1   . TYR B 2 646  ? 119.255 136.724 180.910 1.00 82.33  ? 643  TYR A CD1   1 
ATOM   5177  C CD2   . TYR B 2 646  ? 117.878 135.452 182.380 1.00 82.33  ? 643  TYR A CD2   1 
ATOM   5178  C CE1   . TYR B 2 646  ? 120.088 135.636 180.742 1.00 82.33  ? 643  TYR A CE1   1 
ATOM   5179  C CE2   . TYR B 2 646  ? 118.708 134.360 182.220 1.00 82.33  ? 643  TYR A CE2   1 
ATOM   5180  C CZ    . TYR B 2 646  ? 119.811 134.458 181.401 1.00 82.33  ? 643  TYR A CZ    1 
ATOM   5181  O OH    . TYR B 2 646  ? 120.640 133.372 181.239 1.00 82.33  ? 643  TYR A OH    1 
ATOM   5182  N N     . ASP B 2 647  ? 114.607 136.692 180.464 1.00 86.35  ? 644  ASP A N     1 
ATOM   5183  C CA    . ASP B 2 647  ? 113.867 135.595 179.850 1.00 86.35  ? 644  ASP A CA    1 
ATOM   5184  C C     . ASP B 2 647  ? 113.507 135.920 178.406 1.00 86.35  ? 644  ASP A C     1 
ATOM   5185  O O     . ASP B 2 647  ? 113.479 135.029 177.549 1.00 86.35  ? 644  ASP A O     1 
ATOM   5186  C CB    . ASP B 2 647  ? 112.611 135.287 180.664 1.00 86.35  ? 644  ASP A CB    1 
ATOM   5187  C CG    . ASP B 2 647  ? 112.928 134.669 182.012 1.00 86.35  ? 644  ASP A CG    1 
ATOM   5188  O OD1   . ASP B 2 647  ? 113.966 133.983 182.123 1.00 86.35  ? 644  ASP A OD1   1 
ATOM   5189  O OD2   . ASP B 2 647  ? 112.141 134.872 182.960 1.00 86.35  ? 644  ASP A OD2   1 
ATOM   5190  N N     . LEU B 2 648  ? 113.219 137.192 178.120 1.00 84.70  ? 645  LEU A N     1 
ATOM   5191  C CA    . LEU B 2 648  ? 113.012 137.612 176.738 1.00 84.70  ? 645  LEU A CA    1 
ATOM   5192  C C     . LEU B 2 648  ? 114.262 137.383 175.899 1.00 84.70  ? 645  LEU A C     1 
ATOM   5193  O O     . LEU B 2 648  ? 114.176 136.924 174.755 1.00 84.70  ? 645  LEU A O     1 
ATOM   5194  C CB    . LEU B 2 648  ? 112.596 139.084 176.689 1.00 84.70  ? 645  LEU A CB    1 
ATOM   5195  C CG    . LEU B 2 648  ? 111.115 139.484 176.753 1.00 84.70  ? 645  LEU A CG    1 
ATOM   5196  C CD1   . LEU B 2 648  ? 110.381 139.005 175.515 1.00 84.70  ? 645  LEU A CD1   1 
ATOM   5197  C CD2   . LEU B 2 648  ? 110.424 138.964 178.001 1.00 84.70  ? 645  LEU A CD2   1 
ATOM   5198  N N     . ASN B 2 649  ? 115.434 137.693 176.451 1.00 83.44  ? 646  ASN A N     1 
ATOM   5199  C CA    . ASN B 2 649  ? 116.684 137.578 175.714 1.00 83.44  ? 646  ASN A CA    1 
ATOM   5200  C C     . ASN B 2 649  ? 117.241 136.161 175.691 1.00 83.44  ? 646  ASN A C     1 
ATOM   5201  O O     . ASN B 2 649  ? 118.223 135.912 174.983 1.00 83.44  ? 646  ASN A O     1 
ATOM   5202  C CB    . ASN B 2 649  ? 117.733 138.529 176.302 1.00 83.44  ? 646  ASN A CB    1 
ATOM   5203  C CG    . ASN B 2 649  ? 118.740 138.996 175.269 1.00 83.44  ? 646  ASN A CG    1 
ATOM   5204  O OD1   . ASN B 2 649  ? 118.636 138.661 174.089 1.00 83.44  ? 646  ASN A OD1   1 
ATOM   5205  N ND2   . ASN B 2 649  ? 119.719 139.777 175.708 1.00 83.44  ? 646  ASN A ND2   1 
ATOM   5206  N N     . ASN B 2 650  ? 116.647 135.236 176.437 1.00 84.89  ? 647  ASN A N     1 
ATOM   5207  C CA    . ASN B 2 650  ? 117.111 133.855 176.451 1.00 84.89  ? 647  ASN A CA    1 
ATOM   5208  C C     . ASN B 2 650  ? 116.791 133.154 175.135 1.00 84.89  ? 647  ASN A C     1 
ATOM   5209  O O     . ASN B 2 650  ? 117.668 132.561 174.507 1.00 84.89  ? 647  ASN A O     1 
ATOM   5210  C CB    . ASN B 2 650  ? 116.486 133.090 177.619 1.00 84.89  ? 647  ASN A CB    1 
ATOM   5211  C CG    . ASN B 2 650  ? 117.230 133.307 178.920 1.00 84.89  ? 647  ASN A CG    1 
ATOM   5212  O OD1   . ASN B 2 650  ? 116.637 133.673 179.935 1.00 84.89  ? 647  ASN A OD1   1 
ATOM   5213  N ND2   . ASN B 2 650  ? 118.539 133.083 178.898 1.00 84.89  ? 647  ASN A ND2   1 
ATOM   5214  N N     . PRO B 2 655  ? 114.153 132.034 166.146 1.00 90.49  ? 652  PRO A N     1 
ATOM   5215  C CA    . PRO B 2 655  ? 112.993 132.845 166.531 1.00 90.49  ? 652  PRO A CA    1 
ATOM   5216  C C     . PRO B 2 655  ? 113.103 133.391 167.951 1.00 90.49  ? 652  PRO A C     1 
ATOM   5217  O O     . PRO B 2 655  ? 112.285 133.056 168.808 1.00 90.49  ? 652  PRO A O     1 
ATOM   5218  C CB    . PRO B 2 655  ? 111.826 131.862 166.412 1.00 90.49  ? 652  PRO A CB    1 
ATOM   5219  C CG    . PRO B 2 655  ? 112.440 130.527 166.644 1.00 90.49  ? 652  PRO A CG    1 
ATOM   5220  C CD    . PRO B 2 655  ? 113.825 130.600 166.064 1.00 90.49  ? 652  PRO A CD    1 
ATOM   5221  N N     . LYS B 2 656  ? 114.115 134.223 168.188 1.00 87.23  ? 653  LYS A N     1 
ATOM   5222  C CA    . LYS B 2 656  ? 114.291 134.832 169.499 1.00 87.23  ? 653  LYS A CA    1 
ATOM   5223  C C     . LYS B 2 656  ? 113.150 135.793 169.798 1.00 87.23  ? 653  LYS A C     1 
ATOM   5224  O O     . LYS B 2 656  ? 112.520 136.339 168.889 1.00 87.23  ? 653  LYS A O     1 
ATOM   5225  C CB    . LYS B 2 656  ? 115.628 135.570 169.567 1.00 87.23  ? 653  LYS A CB    1 
ATOM   5226  C CG    . LYS B 2 656  ? 116.845 134.664 169.613 1.00 87.23  ? 653  LYS A CG    1 
ATOM   5227  C CD    . LYS B 2 656  ? 118.130 135.476 169.592 1.00 87.23  ? 653  LYS A CD    1 
ATOM   5228  C CE    . LYS B 2 656  ? 118.309 136.265 170.880 1.00 87.23  ? 653  LYS A CE    1 
ATOM   5229  N NZ    . LYS B 2 656  ? 118.552 135.377 172.050 1.00 87.23  ? 653  LYS A NZ    1 
ATOM   5230  N N     . LYS B 2 657  ? 112.883 135.994 171.086 1.00 91.16  ? 654  LYS A N     1 
ATOM   5231  C CA    . LYS B 2 657  ? 111.838 136.918 171.487 1.00 91.16  ? 654  LYS A CA    1 
ATOM   5232  C C     . LYS B 2 657  ? 112.267 138.357 171.197 1.00 91.16  ? 654  LYS A C     1 
ATOM   5233  O O     . LYS B 2 657  ? 113.435 138.644 170.918 1.00 91.16  ? 654  LYS A O     1 
ATOM   5234  C CB    . LYS B 2 657  ? 111.499 136.736 172.965 1.00 91.16  ? 654  LYS A CB    1 
ATOM   5235  C CG    . LYS B 2 657  ? 110.900 135.375 173.289 1.00 91.16  ? 654  LYS A CG    1 
ATOM   5236  C CD    . LYS B 2 657  ? 109.943 135.434 174.470 1.00 91.16  ? 654  LYS A CD    1 
ATOM   5237  C CE    . LYS B 2 657  ? 108.663 136.171 174.110 1.00 91.16  ? 654  LYS A CE    1 
ATOM   5238  N NZ    . LYS B 2 657  ? 107.810 136.419 175.304 1.00 91.16  ? 654  LYS A NZ    1 
ATOM   5239  N N     . PHE B 2 658  ? 111.285 139.261 171.247 1.00 85.39  ? 655  PHE A N     1 
ATOM   5240  C CA    . PHE B 2 658  ? 111.414 140.669 170.871 1.00 85.39  ? 655  PHE A CA    1 
ATOM   5241  C C     . PHE B 2 658  ? 112.187 140.849 169.566 1.00 85.39  ? 655  PHE A C     1 
ATOM   5242  O O     . PHE B 2 658  ? 112.833 141.879 169.355 1.00 85.39  ? 655  PHE A O     1 
ATOM   5243  C CB    . PHE B 2 658  ? 112.036 141.507 172.004 1.00 85.39  ? 655  PHE A CB    1 
ATOM   5244  C CG    . PHE B 2 658  ? 113.425 141.093 172.417 1.00 85.39  ? 655  PHE A CG    1 
ATOM   5245  C CD1   . PHE B 2 658  ? 114.537 141.558 171.735 1.00 85.39  ? 655  PHE A CD1   1 
ATOM   5246  C CD2   . PHE B 2 658  ? 113.620 140.276 173.515 1.00 85.39  ? 655  PHE A CD2   1 
ATOM   5247  C CE1   . PHE B 2 658  ? 115.809 141.191 172.119 1.00 85.39  ? 655  PHE A CE1   1 
ATOM   5248  C CE2   . PHE B 2 658  ? 114.891 139.909 173.903 1.00 85.39  ? 655  PHE A CE2   1 
ATOM   5249  C CZ    . PHE B 2 658  ? 115.986 140.366 173.205 1.00 85.39  ? 655  PHE A CZ    1 
ATOM   5250  N N     . GLN B 2 659  ? 112.096 139.868 168.672 1.00 89.76  ? 656  GLN A N     1 
ATOM   5251  C CA    . GLN B 2 659  ? 112.740 139.929 167.370 1.00 89.76  ? 656  GLN A CA    1 
ATOM   5252  C C     . GLN B 2 659  ? 111.685 139.705 166.296 1.00 89.76  ? 656  GLN A C     1 
ATOM   5253  O O     . GLN B 2 659  ? 110.630 139.119 166.551 1.00 89.76  ? 656  GLN A O     1 
ATOM   5254  C CB    . GLN B 2 659  ? 113.870 138.894 167.251 1.00 89.76  ? 656  GLN A CB    1 
ATOM   5255  C CG    . GLN B 2 659  ? 114.798 139.100 166.063 1.00 89.76  ? 656  GLN A CG    1 
ATOM   5256  C CD    . GLN B 2 659  ? 116.027 138.217 166.125 1.00 89.76  ? 656  GLN A CD    1 
ATOM   5257  O OE1   . GLN B 2 659  ? 116.324 137.620 167.157 1.00 89.76  ? 656  GLN A OE1   1 
ATOM   5258  N NE2   . GLN B 2 659  ? 116.747 138.125 165.012 1.00 89.76  ? 656  GLN A NE2   1 
ATOM   5259  N N     . THR B 2 660  ? 111.983 140.192 165.087 1.00 93.10  ? 657  THR A N     1 
ATOM   5260  C CA    . THR B 2 660  ? 111.004 140.186 164.003 1.00 93.10  ? 657  THR A CA    1 
ATOM   5261  C C     . THR B 2 660  ? 110.448 138.790 163.751 1.00 93.10  ? 657  THR A C     1 
ATOM   5262  O O     . THR B 2 660  ? 109.278 138.636 163.382 1.00 93.10  ? 657  THR A O     1 
ATOM   5263  C CB    . THR B 2 660  ? 111.637 140.733 162.724 1.00 93.10  ? 657  THR A CB    1 
ATOM   5264  O OG1   . THR B 2 660  ? 112.764 139.923 162.369 1.00 93.10  ? 657  THR A OG1   1 
ATOM   5265  C CG2   . THR B 2 660  ? 112.100 142.172 162.926 1.00 93.10  ? 657  THR A CG2   1 
ATOM   5266  N N     . ALA B 2 661  ? 111.273 137.759 163.945 1.00 93.39  ? 658  ALA A N     1 
ATOM   5267  C CA    . ALA B 2 661  ? 110.810 136.391 163.734 1.00 93.39  ? 658  ALA A CA    1 
ATOM   5268  C C     . ALA B 2 661  ? 109.711 136.017 164.721 1.00 93.39  ? 658  ALA A C     1 
ATOM   5269  O O     . ALA B 2 661  ? 108.744 135.338 164.354 1.00 93.39  ? 658  ALA A O     1 
ATOM   5270  C CB    . ALA B 2 661  ? 111.983 135.417 163.843 1.00 93.39  ? 658  ALA A CB    1 
ATOM   5271  N N     . TYR B 2 662  ? 109.844 136.441 165.980 1.00 92.73  ? 659  TYR A N     1 
ATOM   5272  C CA    . TYR B 2 662  ? 108.867 136.061 166.997 1.00 92.73  ? 659  TYR A CA    1 
ATOM   5273  C C     . TYR B 2 662  ? 107.484 136.617 166.674 1.00 92.73  ? 659  TYR A C     1 
ATOM   5274  O O     . TYR B 2 662  ? 106.479 135.905 166.771 1.00 92.73  ? 659  TYR A O     1 
ATOM   5275  C CB    . TYR B 2 662  ? 109.336 136.531 168.374 1.00 92.73  ? 659  TYR A CB    1 
ATOM   5276  C CG    . TYR B 2 662  ? 108.276 136.461 169.449 1.00 92.73  ? 659  TYR A CG    1 
ATOM   5277  C CD1   . TYR B 2 662  ? 107.686 135.252 169.795 1.00 92.73  ? 659  TYR A CD1   1 
ATOM   5278  C CD2   . TYR B 2 662  ? 107.874 137.603 170.125 1.00 92.73  ? 659  TYR A CD2   1 
ATOM   5279  C CE1   . TYR B 2 662  ? 106.717 135.187 170.781 1.00 92.73  ? 659  TYR A CE1   1 
ATOM   5280  C CE2   . TYR B 2 662  ? 106.908 137.549 171.110 1.00 92.73  ? 659  TYR A CE2   1 
ATOM   5281  C CZ    . TYR B 2 662  ? 106.332 136.339 171.434 1.00 92.73  ? 659  TYR A CZ    1 
ATOM   5282  O OH    . TYR B 2 662  ? 105.370 136.286 172.416 1.00 92.73  ? 659  TYR A OH    1 
ATOM   5283  N N     . ALA B 2 663  ? 107.414 137.891 166.279 1.00 96.28  ? 660  ALA A N     1 
ATOM   5284  C CA    . ALA B 2 663  ? 106.127 138.471 165.906 1.00 96.28  ? 660  ALA A CA    1 
ATOM   5285  C C     . ALA B 2 663  ? 105.601 137.880 164.604 1.00 96.28  ? 660  ALA A C     1 
ATOM   5286  O O     . ALA B 2 663  ? 104.386 137.717 164.446 1.00 96.28  ? 660  ALA A O     1 
ATOM   5287  C CB    . ALA B 2 663  ? 106.243 139.990 165.788 1.00 96.28  ? 660  ALA A CB    1 
ATOM   5288  N N     . LYS B 2 664  ? 106.495 137.562 163.665 1.00 95.65  ? 661  LYS A N     1 
ATOM   5289  C CA    . LYS B 2 664  ? 106.068 136.991 162.391 1.00 95.65  ? 661  LYS A CA    1 
ATOM   5290  C C     . LYS B 2 664  ? 105.427 135.622 162.582 1.00 95.65  ? 661  LYS A C     1 
ATOM   5291  O O     . LYS B 2 664  ? 104.432 135.297 161.923 1.00 95.65  ? 661  LYS A O     1 
ATOM   5292  C CB    . LYS B 2 664  ? 107.259 136.897 161.437 1.00 95.65  ? 661  LYS A CB    1 
ATOM   5293  C CG    . LYS B 2 664  ? 106.903 136.412 160.041 1.00 95.65  ? 661  LYS A CG    1 
ATOM   5294  C CD    . LYS B 2 664  ? 106.098 137.455 159.284 1.00 95.65  ? 661  LYS A CD    1 
ATOM   5295  C CE    . LYS B 2 664  ? 105.953 137.085 157.816 1.00 95.65  ? 661  LYS A CE    1 
ATOM   5296  N NZ    . LYS B 2 664  ? 105.294 135.762 157.635 1.00 95.65  ? 661  LYS A NZ    1 
ATOM   5297  N N     . LYS B 2 665  ? 105.981 134.806 163.477 1.00 94.11  ? 662  LYS A N     1 
ATOM   5298  C CA    . LYS B 2 665  ? 105.513 133.435 163.653 1.00 94.11  ? 662  LYS A CA    1 
ATOM   5299  C C     . LYS B 2 665  ? 104.419 133.337 164.713 1.00 94.11  ? 662  LYS A C     1 
ATOM   5300  O O     . LYS B 2 665  ? 103.302 132.896 164.423 1.00 94.11  ? 662  LYS A O     1 
ATOM   5301  C CB    . LYS B 2 665  ? 106.693 132.524 164.012 1.00 94.11  ? 662  LYS A CB    1 
ATOM   5302  C CG    . LYS B 2 665  ? 107.419 131.940 162.809 1.00 94.11  ? 662  LYS A CG    1 
ATOM   5303  C CD    . LYS B 2 665  ? 108.335 132.967 162.160 1.00 94.11  ? 662  LYS A CD    1 
ATOM   5304  C CE    . LYS B 2 665  ? 109.112 132.365 161.002 1.00 94.11  ? 662  LYS A CE    1 
ATOM   5305  N NZ    . LYS B 2 665  ? 109.933 133.389 160.297 1.00 94.11  ? 662  LYS A NZ    1 
ATOM   5306  N N     . THR B 2 666  ? 104.729 133.740 165.948 1.00 97.37  ? 663  THR A N     1 
ATOM   5307  C CA    . THR B 2 666  ? 103.754 133.627 167.030 1.00 97.37  ? 663  THR A CA    1 
ATOM   5308  C C     . THR B 2 666  ? 102.551 134.534 166.796 1.00 97.37  ? 663  THR A C     1 
ATOM   5309  O O     . THR B 2 666  ? 101.404 134.120 167.007 1.00 97.37  ? 663  THR A O     1 
ATOM   5310  C CB    . THR B 2 666  ? 104.414 133.950 168.370 1.00 97.37  ? 663  THR A CB    1 
ATOM   5311  O OG1   . THR B 2 666  ? 105.554 133.102 168.559 1.00 97.37  ? 663  THR A OG1   1 
ATOM   5312  C CG2   . THR B 2 666  ? 103.434 133.733 169.514 1.00 97.37  ? 663  THR A CG2   1 
ATOM   5313  N N     . GLY B 2 667  ? 102.788 135.768 166.358 1.00 96.71  ? 664  GLY A N     1 
ATOM   5314  C CA    . GLY B 2 667  ? 101.714 136.703 166.102 1.00 96.71  ? 664  GLY A CA    1 
ATOM   5315  C C     . GLY B 2 667  ? 101.173 137.421 167.318 1.00 96.71  ? 664  GLY A C     1 
ATOM   5316  O O     . GLY B 2 667  ? 100.190 138.162 167.189 1.00 96.71  ? 664  GLY A O     1 
ATOM   5317  N N     . ASP B 2 668  ? 101.774 137.233 168.493 1.00 95.85  ? 665  ASP A N     1 
ATOM   5318  C CA    . ASP B 2 668  ? 101.327 137.904 169.713 1.00 95.85  ? 665  ASP A CA    1 
ATOM   5319  C C     . ASP B 2 668  ? 101.795 139.356 169.665 1.00 95.85  ? 665  ASP A C     1 
ATOM   5320  O O     . ASP B 2 668  ? 102.795 139.747 170.271 1.00 95.85  ? 665  ASP A O     1 
ATOM   5321  C CB    . ASP B 2 668  ? 101.855 137.186 170.950 1.00 95.85  ? 665  ASP A CB    1 
ATOM   5322  C CG    . ASP B 2 668  ? 101.291 137.752 172.239 1.00 95.85  ? 665  ASP A CG    1 
ATOM   5323  O OD1   . ASP B 2 668  ? 100.330 138.548 172.174 1.00 95.85  ? 665  ASP A OD1   1 
ATOM   5324  O OD2   . ASP B 2 668  ? 101.810 137.401 173.320 1.00 95.85  ? 665  ASP A OD2   1 
ATOM   5325  N N     . GLN B 2 669  ? 101.045 140.171 168.920 1.00 94.89  ? 666  GLN A N     1 
ATOM   5326  C CA    . GLN B 2 669  ? 101.422 141.569 168.737 1.00 94.89  ? 666  GLN A CA    1 
ATOM   5327  C C     . GLN B 2 669  ? 101.342 142.350 170.044 1.00 94.89  ? 666  GLN A C     1 
ATOM   5328  O O     . GLN B 2 669  ? 102.207 143.188 170.324 1.00 94.89  ? 666  GLN A O     1 
ATOM   5329  C CB    . GLN B 2 669  ? 100.537 142.215 167.671 1.00 94.89  ? 666  GLN A CB    1 
ATOM   5330  C CG    . GLN B 2 669  ? 100.901 141.836 166.242 1.00 94.89  ? 666  GLN A CG    1 
ATOM   5331  C CD    . GLN B 2 669  ? 102.397 141.710 166.028 1.00 94.89  ? 666  GLN A CD    1 
ATOM   5332  O OE1   . GLN B 2 669  ? 102.941 140.606 166.001 1.00 94.89  ? 666  GLN A OE1   1 
ATOM   5333  N NE2   . GLN B 2 669  ? 103.070 142.844 165.867 1.00 94.89  ? 666  GLN A NE2   1 
ATOM   5334  N N     . LYS B 2 670  ? 100.305 142.102 170.850 1.00 93.32  ? 667  LYS A N     1 
ATOM   5335  C CA    . LYS B 2 670  ? 100.166 142.822 172.114 1.00 93.32  ? 667  LYS A CA    1 
ATOM   5336  C C     . LYS B 2 670  ? 101.317 142.492 173.056 1.00 93.32  ? 667  LYS A C     1 
ATOM   5337  O O     . LYS B 2 670  ? 101.854 143.378 173.732 1.00 93.32  ? 667  LYS A O     1 
ATOM   5338  C CB    . LYS B 2 670  ? 98.820  142.497 172.765 1.00 93.32  ? 667  LYS A CB    1 
ATOM   5339  C CG    . LYS B 2 670  ? 98.657  143.090 174.156 1.00 93.32  ? 667  LYS A CG    1 
ATOM   5340  C CD    . LYS B 2 670  ? 98.754  144.609 174.111 1.00 93.32  ? 667  LYS A CD    1 
ATOM   5341  C CE    . LYS B 2 670  ? 98.826  145.201 175.509 1.00 93.32  ? 667  LYS A CE    1 
ATOM   5342  N NZ    . LYS B 2 670  ? 100.110 144.853 176.185 1.00 93.32  ? 667  LYS A NZ    1 
ATOM   5343  N N     . GLY B 2 671  ? 101.708 141.218 173.113 1.00 89.50  ? 668  GLY A N     1 
ATOM   5344  C CA    . GLY B 2 671  ? 102.878 140.850 173.892 1.00 89.50  ? 668  GLY A CA    1 
ATOM   5345  C C     . GLY B 2 671  ? 104.154 141.463 173.347 1.00 89.50  ? 668  GLY A C     1 
ATOM   5346  O O     . GLY B 2 671  ? 105.053 141.827 174.108 1.00 89.50  ? 668  GLY A O     1 
ATOM   5347  N N     . TYR B 2 672  ? 104.250 141.577 172.021 1.00 90.53  ? 669  TYR A N     1 
ATOM   5348  C CA    . TYR B 2 672  ? 105.410 142.205 171.397 1.00 90.53  ? 669  TYR A CA    1 
ATOM   5349  C C     . TYR B 2 672  ? 105.589 143.644 171.866 1.00 90.53  ? 669  TYR A C     1 
ATOM   5350  O O     . TYR B 2 672  ? 106.626 143.998 172.437 1.00 90.53  ? 669  TYR A O     1 
ATOM   5351  C CB    . TYR B 2 672  ? 105.254 142.151 169.877 1.00 90.53  ? 669  TYR A CB    1 
ATOM   5352  C CG    . TYR B 2 672  ? 106.541 142.096 169.092 1.00 90.53  ? 669  TYR A CG    1 
ATOM   5353  C CD1   . TYR B 2 672  ? 107.344 140.965 169.101 1.00 90.53  ? 669  TYR A CD1   1 
ATOM   5354  C CD2   . TYR B 2 672  ? 106.932 143.174 168.313 1.00 90.53  ? 669  TYR A CD2   1 
ATOM   5355  C CE1   . TYR B 2 672  ? 108.516 140.923 168.367 1.00 90.53  ? 669  TYR A CE1   1 
ATOM   5356  C CE2   . TYR B 2 672  ? 108.088 143.141 167.580 1.00 90.53  ? 669  TYR A CE2   1 
ATOM   5357  C CZ    . TYR B 2 672  ? 108.877 142.020 167.607 1.00 90.53  ? 669  TYR A CZ    1 
ATOM   5358  O OH    . TYR B 2 672  ? 110.030 142.022 166.863 1.00 90.53  ? 669  TYR A OH    1 
ATOM   5359  N N     . ARG B 2 673  ? 104.568 144.482 171.674 1.00 87.59  ? 670  ARG A N     1 
ATOM   5360  C CA    . ARG B 2 673  ? 104.748 145.917 171.881 1.00 87.59  ? 670  ARG A CA    1 
ATOM   5361  C C     . ARG B 2 673  ? 105.052 146.237 173.341 1.00 87.59  ? 670  ARG A C     1 
ATOM   5362  O O     . ARG B 2 673  ? 105.854 147.131 173.633 1.00 87.59  ? 670  ARG A O     1 
ATOM   5363  C CB    . ARG B 2 673  ? 103.511 146.677 171.401 1.00 87.59  ? 670  ARG A CB    1 
ATOM   5364  C CG    . ARG B 2 673  ? 103.800 148.102 170.948 1.00 87.59  ? 670  ARG A CG    1 
ATOM   5365  C CD    . ARG B 2 673  ? 104.350 148.095 169.525 1.00 87.59  ? 670  ARG A CD    1 
ATOM   5366  N NE    . ARG B 2 673  ? 104.998 149.349 169.157 1.00 87.59  ? 670  ARG A NE    1 
ATOM   5367  C CZ    . ARG B 2 673  ? 105.589 149.568 167.989 1.00 87.59  ? 670  ARG A CZ    1 
ATOM   5368  N NH1   . ARG B 2 673  ? 105.670 148.623 167.067 1.00 87.59  ? 670  ARG A NH1   1 
ATOM   5369  N NH2   . ARG B 2 673  ? 106.118 150.764 167.744 1.00 87.59  ? 670  ARG A NH2   1 
ATOM   5370  N N     . GLU B 2 674  ? 104.414 145.526 174.273 1.00 90.28  ? 671  GLU A N     1 
ATOM   5371  C CA    . GLU B 2 674  ? 104.730 145.715 175.686 1.00 90.28  ? 671  GLU A CA    1 
ATOM   5372  C C     . GLU B 2 674  ? 106.144 145.247 176.010 1.00 90.28  ? 671  GLU A C     1 
ATOM   5373  O O     . GLU B 2 674  ? 106.889 145.943 176.709 1.00 90.28  ? 671  GLU A O     1 
ATOM   5374  C CB    . GLU B 2 674  ? 103.707 144.987 176.558 1.00 90.28  ? 671  GLU A CB    1 
ATOM   5375  C CG    . GLU B 2 674  ? 104.044 144.972 178.044 1.00 90.28  ? 671  GLU A CG    1 
ATOM   5376  C CD    . GLU B 2 674  ? 104.357 146.349 178.600 1.00 90.28  ? 671  GLU A CD    1 
ATOM   5377  O OE1   . GLU B 2 674  ? 103.591 147.296 178.327 1.00 90.28  ? 671  GLU A OE1   1 
ATOM   5378  O OE2   . GLU B 2 674  ? 105.373 146.481 179.315 1.00 90.28  ? 671  GLU A OE2   1 
ATOM   5379  N N     . ALA B 2 675  ? 106.530 144.065 175.522 1.00 86.10  ? 672  ALA A N     1 
ATOM   5380  C CA    . ALA B 2 675  ? 107.868 143.555 175.810 1.00 86.10  ? 672  ALA A CA    1 
ATOM   5381  C C     . ALA B 2 675  ? 108.944 144.441 175.195 1.00 86.10  ? 672  ALA A C     1 
ATOM   5382  O O     . ALA B 2 675  ? 109.969 144.711 175.832 1.00 86.10  ? 672  ALA A O     1 
ATOM   5383  C CB    . ALA B 2 675  ? 108.006 142.117 175.314 1.00 86.10  ? 672  ALA A CB    1 
ATOM   5384  N N     . LEU B 2 676  ? 108.737 144.898 173.957 1.00 83.02  ? 673  LEU A N     1 
ATOM   5385  C CA    . LEU B 2 676  ? 109.700 145.808 173.344 1.00 83.02  ? 673  LEU A CA    1 
ATOM   5386  C C     . LEU B 2 676  ? 109.776 147.127 174.099 1.00 83.02  ? 673  LEU A C     1 
ATOM   5387  O O     . LEU B 2 676  ? 110.862 147.695 174.252 1.00 83.02  ? 673  LEU A O     1 
ATOM   5388  C CB    . LEU B 2 676  ? 109.363 146.050 171.872 1.00 83.02  ? 673  LEU A CB    1 
ATOM   5389  C CG    . LEU B 2 676  ? 109.836 145.036 170.823 1.00 83.02  ? 673  LEU A CG    1 
ATOM   5390  C CD1   . LEU B 2 676  ? 111.350 145.019 170.795 1.00 83.02  ? 673  LEU A CD1   1 
ATOM   5391  C CD2   . LEU B 2 676  ? 109.301 143.636 171.044 1.00 83.02  ? 673  LEU A CD2   1 
ATOM   5392  N N     . CYS B 2 677  ? 108.636 147.637 174.572 1.00 86.16  ? 674  CYS A N     1 
ATOM   5393  C CA    . CYS B 2 677  ? 108.658 148.876 175.341 1.00 86.16  ? 674  CYS A CA    1 
ATOM   5394  C C     . CYS B 2 677  ? 109.490 148.722 176.607 1.00 86.16  ? 674  CYS A C     1 
ATOM   5395  O O     . CYS B 2 677  ? 110.269 149.615 176.958 1.00 86.16  ? 674  CYS A O     1 
ATOM   5396  C CB    . CYS B 2 677  ? 107.235 149.313 175.686 1.00 86.16  ? 674  CYS A CB    1 
ATOM   5397  S SG    . CYS B 2 677  ? 107.140 150.934 176.479 1.00 86.16  ? 674  CYS A SG    1 
ATOM   5398  N N     . LYS B 2 678  ? 109.341 147.594 177.305 1.00 81.64  ? 675  LYS A N     1 
ATOM   5399  C CA    . LYS B 2 678  ? 110.168 147.342 178.480 1.00 81.64  ? 675  LYS A CA    1 
ATOM   5400  C C     . LYS B 2 678  ? 111.629 147.143 178.096 1.00 81.64  ? 675  LYS A C     1 
ATOM   5401  O O     . LYS B 2 678  ? 112.530 147.661 178.766 1.00 81.64  ? 675  LYS A O     1 
ATOM   5402  C CB    . LYS B 2 678  ? 109.642 146.127 179.242 1.00 81.64  ? 675  LYS A CB    1 
ATOM   5403  C CG    . LYS B 2 678  ? 110.430 145.794 180.497 1.00 81.64  ? 675  LYS A CG    1 
ATOM   5404  C CD    . LYS B 2 678  ? 110.268 146.871 181.558 1.00 81.64  ? 675  LYS A CD    1 
ATOM   5405  C CE    . LYS B 2 678  ? 110.925 146.459 182.865 1.00 81.64  ? 675  LYS A CE    1 
ATOM   5406  N NZ    . LYS B 2 678  ? 112.405 146.359 182.736 1.00 81.64  ? 675  LYS A NZ    1 
ATOM   5407  N N     . TRP B 2 679  ? 111.884 146.393 177.020 1.00 75.15  ? 676  TRP A N     1 
ATOM   5408  C CA    . TRP B 2 679  ? 113.260 146.159 176.590 1.00 75.15  ? 676  TRP A CA    1 
ATOM   5409  C C     . TRP B 2 679  ? 113.932 147.452 176.145 1.00 75.15  ? 676  TRP A C     1 
ATOM   5410  O O     . TRP B 2 679  ? 115.070 147.734 176.542 1.00 75.15  ? 676  TRP A O     1 
ATOM   5411  C CB    . TRP B 2 679  ? 113.289 145.123 175.466 1.00 75.15  ? 676  TRP A CB    1 
ATOM   5412  C CG    . TRP B 2 679  ? 114.650 144.906 174.864 1.00 75.15  ? 676  TRP A CG    1 
ATOM   5413  C CD1   . TRP B 2 679  ? 115.017 145.137 173.570 1.00 75.15  ? 676  TRP A CD1   1 
ATOM   5414  C CD2   . TRP B 2 679  ? 115.821 144.412 175.528 1.00 75.15  ? 676  TRP A CD2   1 
ATOM   5415  N NE1   . TRP B 2 679  ? 116.340 144.821 173.389 1.00 75.15  ? 676  TRP A NE1   1 
ATOM   5416  C CE2   . TRP B 2 679  ? 116.857 144.373 174.575 1.00 75.15  ? 676  TRP A CE2   1 
ATOM   5417  C CE3   . TRP B 2 679  ? 116.094 144.000 176.836 1.00 75.15  ? 676  TRP A CE3   1 
ATOM   5418  C CZ2   . TRP B 2 679  ? 118.141 143.939 174.888 1.00 75.15  ? 676  TRP A CZ2   1 
ATOM   5419  C CZ3   . TRP B 2 679  ? 117.371 143.570 177.142 1.00 75.15  ? 676  TRP A CZ3   1 
ATOM   5420  C CH2   . TRP B 2 679  ? 118.377 143.543 176.173 1.00 75.15  ? 676  TRP A CH2   1 
ATOM   5421  N N     . ILE B 2 680  ? 113.247 148.252 175.324 1.00 78.48  ? 677  ILE A N     1 
ATOM   5422  C CA    . ILE B 2 680  ? 113.815 149.525 174.890 1.00 78.48  ? 677  ILE A CA    1 
ATOM   5423  C C     . ILE B 2 680  ? 114.012 150.452 176.081 1.00 78.48  ? 677  ILE A C     1 
ATOM   5424  O O     . ILE B 2 680  ? 115.043 151.126 176.196 1.00 78.48  ? 677  ILE A O     1 
ATOM   5425  C CB    . ILE B 2 680  ? 112.932 150.167 173.805 1.00 78.48  ? 677  ILE A CB    1 
ATOM   5426  C CG1   . ILE B 2 680  ? 112.961 149.326 172.528 1.00 78.48  ? 677  ILE A CG1   1 
ATOM   5427  C CG2   . ILE B 2 680  ? 113.394 151.584 173.507 1.00 78.48  ? 677  ILE A CG2   1 
ATOM   5428  C CD1   . ILE B 2 680  ? 114.350 149.104 171.976 1.00 78.48  ? 677  ILE A CD1   1 
ATOM   5429  N N     . ASP B 2 681  ? 113.033 150.501 176.987 1.00 78.40  ? 678  ASP A N     1 
ATOM   5430  C CA    . ASP B 2 681  ? 113.201 151.282 178.208 1.00 78.40  ? 678  ASP A CA    1 
ATOM   5431  C C     . ASP B 2 681  ? 114.355 150.747 179.042 1.00 78.40  ? 678  ASP A C     1 
ATOM   5432  O O     . ASP B 2 681  ? 115.102 151.522 179.651 1.00 78.40  ? 678  ASP A O     1 
ATOM   5433  C CB    . ASP B 2 681  ? 111.907 151.281 179.022 1.00 78.40  ? 678  ASP A CB    1 
ATOM   5434  C CG    . ASP B 2 681  ? 111.789 152.490 179.928 1.00 78.40  ? 678  ASP A CG    1 
ATOM   5435  O OD1   . ASP B 2 681  ? 112.025 153.619 179.449 1.00 78.40  ? 678  ASP A OD1   1 
ATOM   5436  O OD2   . ASP B 2 681  ? 111.459 152.312 181.119 1.00 78.40  ? 678  ASP A OD2   1 
ATOM   5437  N N     . PHE B 2 682  ? 114.515 149.422 179.086 1.00 76.97  ? 679  PHE A N     1 
ATOM   5438  C CA    . PHE B 2 682  ? 115.634 148.842 179.821 1.00 76.97  ? 679  PHE A CA    1 
ATOM   5439  C C     . PHE B 2 682  ? 116.968 149.256 179.214 1.00 76.97  ? 679  PHE A C     1 
ATOM   5440  O O     . PHE B 2 682  ? 117.915 149.572 179.944 1.00 76.97  ? 679  PHE A O     1 
ATOM   5441  C CB    . PHE B 2 682  ? 115.517 147.321 179.858 1.00 76.97  ? 679  PHE A CB    1 
ATOM   5442  C CG    . PHE B 2 682  ? 116.692 146.646 180.496 1.00 76.97  ? 679  PHE A CG    1 
ATOM   5443  C CD1   . PHE B 2 682  ? 117.017 146.900 181.817 1.00 76.97  ? 679  PHE A CD1   1 
ATOM   5444  C CD2   . PHE B 2 682  ? 117.476 145.762 179.775 1.00 76.97  ? 679  PHE A CD2   1 
ATOM   5445  C CE1   . PHE B 2 682  ? 118.099 146.282 182.410 1.00 76.97  ? 679  PHE A CE1   1 
ATOM   5446  C CE2   . PHE B 2 682  ? 118.559 145.141 180.362 1.00 76.97  ? 679  PHE A CE2   1 
ATOM   5447  C CZ    . PHE B 2 682  ? 118.869 145.401 181.681 1.00 76.97  ? 679  PHE A CZ    1 
ATOM   5448  N N     . THR B 2 683  ? 117.066 149.250 177.882 1.00 72.74  ? 680  THR A N     1 
ATOM   5449  C CA    . THR B 2 683  ? 118.275 149.752 177.240 1.00 72.74  ? 680  THR A CA    1 
ATOM   5450  C C     . THR B 2 683  ? 118.502 151.216 177.587 1.00 72.74  ? 680  THR A C     1 
ATOM   5451  O O     . THR B 2 683  ? 119.589 151.592 178.037 1.00 72.74  ? 680  THR A O     1 
ATOM   5452  C CB    . THR B 2 683  ? 118.191 149.568 175.725 1.00 72.74  ? 680  THR A CB    1 
ATOM   5453  O OG1   . THR B 2 683  ? 116.994 150.179 175.232 1.00 72.74  ? 680  THR A OG1   1 
ATOM   5454  C CG2   . THR B 2 683  ? 118.188 148.091 175.367 1.00 72.74  ? 680  THR A CG2   1 
ATOM   5455  N N     . ARG B 2 684  ? 117.473 152.050 177.418 1.00 74.51  ? 681  ARG A N     1 
ATOM   5456  C CA    . ARG B 2 684  ? 117.582 153.448 177.820 1.00 74.51  ? 681  ARG A CA    1 
ATOM   5457  C C     . ARG B 2 684  ? 117.905 153.564 179.304 1.00 74.51  ? 681  ARG A C     1 
ATOM   5458  O O     . ARG B 2 684  ? 118.616 154.484 179.725 1.00 74.51  ? 681  ARG A O     1 
ATOM   5459  C CB    . ARG B 2 684  ? 116.288 154.190 177.486 1.00 74.51  ? 681  ARG A CB    1 
ATOM   5460  C CG    . ARG B 2 684  ? 116.295 155.661 177.859 1.00 74.51  ? 681  ARG A CG    1 
ATOM   5461  C CD    . ARG B 2 684  ? 117.258 156.444 176.984 1.00 74.51  ? 681  ARG A CD    1 
ATOM   5462  N NE    . ARG B 2 684  ? 117.110 157.883 177.165 1.00 74.51  ? 681  ARG A NE    1 
ATOM   5463  C CZ    . ARG B 2 684  ? 117.637 158.570 178.169 1.00 74.51  ? 681  ARG A CZ    1 
ATOM   5464  N NH1   . ARG B 2 684  ? 118.363 157.981 179.105 1.00 74.51  ? 681  ARG A NH1   1 
ATOM   5465  N NH2   . ARG B 2 684  ? 117.432 159.883 178.234 1.00 74.51  ? 681  ARG A NH2   1 
ATOM   5466  N N     . ASP B 2 685  ? 117.392 152.634 180.113 1.00 70.83  ? 682  ASP A N     1 
ATOM   5467  C CA    . ASP B 2 685  ? 117.780 152.584 181.517 1.00 70.83  ? 682  ASP A CA    1 
ATOM   5468  C C     . ASP B 2 685  ? 119.255 152.230 181.664 1.00 70.83  ? 682  ASP A C     1 
ATOM   5469  O O     . ASP B 2 685  ? 119.949 152.774 182.532 1.00 70.83  ? 682  ASP A O     1 
ATOM   5470  C CB    . ASP B 2 685  ? 116.907 151.580 182.267 1.00 70.83  ? 682  ASP A CB    1 
ATOM   5471  C CG    . ASP B 2 685  ? 116.735 151.937 183.730 1.00 70.83  ? 682  ASP A CG    1 
ATOM   5472  O OD1   . ASP B 2 685  ? 116.893 153.126 184.075 1.00 70.83  ? 682  ASP A OD1   1 
ATOM   5473  O OD2   . ASP B 2 685  ? 116.438 151.028 184.534 1.00 70.83  ? 682  ASP A OD2   1 
ATOM   5474  N N     . PHE B 2 686  ? 119.751 151.317 180.825 1.00 64.48  ? 683  PHE A N     1 
ATOM   5475  C CA    . PHE B 2 686  ? 121.145 150.895 180.923 1.00 64.48  ? 683  PHE A CA    1 
ATOM   5476  C C     . PHE B 2 686  ? 122.098 152.023 180.544 1.00 64.48  ? 683  PHE A C     1 
ATOM   5477  O O     . PHE B 2 686  ? 123.109 152.249 181.220 1.00 64.48  ? 683  PHE A O     1 
ATOM   5478  C CB    . PHE B 2 686  ? 121.388 149.673 180.039 1.00 64.48  ? 683  PHE A CB    1 
ATOM   5479  C CG    . PHE B 2 686  ? 122.826 149.254 179.975 1.00 64.48  ? 683  PHE A CG    1 
ATOM   5480  C CD1   . PHE B 2 686  ? 123.412 148.581 181.031 1.00 64.48  ? 683  PHE A CD1   1 
ATOM   5481  C CD2   . PHE B 2 686  ? 123.594 149.541 178.862 1.00 64.48  ? 683  PHE A CD2   1 
ATOM   5482  C CE1   . PHE B 2 686  ? 124.737 148.196 180.974 1.00 64.48  ? 683  PHE A CE1   1 
ATOM   5483  C CE2   . PHE B 2 686  ? 124.918 149.161 178.800 1.00 64.48  ? 683  PHE A CE2   1 
ATOM   5484  C CZ    . PHE B 2 686  ? 125.490 148.487 179.856 1.00 64.48  ? 683  PHE A CZ    1 
ATOM   5485  N N     . LEU B 2 687  ? 121.799 152.735 179.454 1.00 60.46  ? 684  LEU A N     1 
ATOM   5486  C CA    . LEU B 2 687  ? 122.703 153.782 178.983 1.00 60.46  ? 684  LEU A CA    1 
ATOM   5487  C C     . LEU B 2 687  ? 122.870 154.884 180.020 1.00 60.46  ? 684  LEU A C     1 
ATOM   5488  O O     . LEU B 2 687  ? 123.988 155.352 180.264 1.00 60.46  ? 684  LEU A O     1 
ATOM   5489  C CB    . LEU B 2 687  ? 122.198 154.374 177.667 1.00 60.46  ? 684  LEU A CB    1 
ATOM   5490  C CG    . LEU B 2 687  ? 122.494 153.699 176.324 1.00 60.46  ? 684  LEU A CG    1 
ATOM   5491  C CD1   . LEU B 2 687  ? 123.985 153.688 176.038 1.00 60.46  ? 684  LEU A CD1   1 
ATOM   5492  C CD2   . LEU B 2 687  ? 121.936 152.303 176.253 1.00 60.46  ? 684  LEU A CD2   1 
ATOM   5493  N N     . SER B 2 688  ? 121.772 155.313 180.642 1.00 60.86  ? 685  SER A N     1 
ATOM   5494  C CA    . SER B 2 688  ? 121.849 156.387 181.622 1.00 60.86  ? 685  SER A CA    1 
ATOM   5495  C C     . SER B 2 688  ? 122.498 155.939 182.923 1.00 60.86  ? 685  SER A C     1 
ATOM   5496  O O     . SER B 2 688  ? 122.850 156.788 183.749 1.00 60.86  ? 685  SER A O     1 
ATOM   5497  C CB    . SER B 2 688  ? 120.453 156.946 181.899 1.00 60.86  ? 685  SER A CB    1 
ATOM   5498  O OG    . SER B 2 688  ? 119.587 155.936 182.387 1.00 60.86  ? 685  SER A OG    1 
ATOM   5499  N N     . LYS B 2 689  ? 122.667 154.634 183.123 1.00 64.42  ? 686  LYS A N     1 
ATOM   5500  C CA    . LYS B 2 689  ? 123.222 154.111 184.364 1.00 64.42  ? 686  LYS A CA    1 
ATOM   5501  C C     . LYS B 2 689  ? 124.653 153.614 184.227 1.00 64.42  ? 686  LYS A C     1 
ATOM   5502  O O     . LYS B 2 689  ? 125.363 153.527 185.235 1.00 64.42  ? 686  LYS A O     1 
ATOM   5503  C CB    . LYS B 2 689  ? 122.340 152.976 184.895 1.00 64.42  ? 686  LYS A CB    1 
ATOM   5504  C CG    . LYS B 2 689  ? 121.057 153.459 185.550 1.00 64.42  ? 686  LYS A CG    1 
ATOM   5505  C CD    . LYS B 2 689  ? 120.166 152.301 185.950 1.00 64.42  ? 686  LYS A CD    1 
ATOM   5506  C CE    . LYS B 2 689  ? 118.928 152.786 186.683 1.00 64.42  ? 686  LYS A CE    1 
ATOM   5507  N NZ    . LYS B 2 689  ? 119.142 152.847 188.155 1.00 64.42  ? 686  LYS A NZ    1 
ATOM   5508  N N     . TYR B 2 690  ? 125.095 153.290 183.015 1.00 52.10  ? 687  TYR A N     1 
ATOM   5509  C CA    . TYR B 2 690  ? 126.451 152.796 182.821 1.00 52.10  ? 687  TYR A CA    1 
ATOM   5510  C C     . TYR B 2 690  ? 127.467 153.899 183.096 1.00 52.10  ? 687  TYR A C     1 
ATOM   5511  O O     . TYR B 2 690  ? 127.166 155.092 183.005 1.00 52.10  ? 687  TYR A O     1 
ATOM   5512  C CB    . TYR B 2 690  ? 126.618 152.256 181.402 1.00 52.10  ? 687  TYR A CB    1 
ATOM   5513  C CG    . TYR B 2 690  ? 127.679 151.191 181.275 1.00 52.10  ? 687  TYR A CG    1 
ATOM   5514  C CD1   . TYR B 2 690  ? 127.604 150.023 182.015 1.00 52.10  ? 687  TYR A CD1   1 
ATOM   5515  C CD2   . TYR B 2 690  ? 128.750 151.351 180.409 1.00 52.10  ? 687  TYR A CD2   1 
ATOM   5516  C CE1   . TYR B 2 690  ? 128.567 149.047 181.902 1.00 52.10  ? 687  TYR A CE1   1 
ATOM   5517  C CE2   . TYR B 2 690  ? 129.720 150.379 180.290 1.00 52.10  ? 687  TYR A CE2   1 
ATOM   5518  C CZ    . TYR B 2 690  ? 129.621 149.229 181.038 1.00 52.10  ? 687  TYR A CZ    1 
ATOM   5519  O OH    . TYR B 2 690  ? 130.582 148.254 180.926 1.00 52.10  ? 687  TYR A OH    1 
ATOM   5520  N N     . THR B 2 691  ? 128.689 153.486 183.437 1.00 51.34  ? 688  THR A N     1 
ATOM   5521  C CA    . THR B 2 691  ? 129.698 154.428 183.910 1.00 51.34  ? 688  THR A CA    1 
ATOM   5522  C C     . THR B 2 691  ? 130.230 155.342 182.814 1.00 51.34  ? 688  THR A C     1 
ATOM   5523  O O     . THR B 2 691  ? 130.747 156.419 183.129 1.00 51.34  ? 688  THR A O     1 
ATOM   5524  C CB    . THR B 2 691  ? 130.864 153.674 184.553 1.00 51.34  ? 688  THR A CB    1 
ATOM   5525  O OG1   . THR B 2 691  ? 131.878 154.606 184.946 1.00 51.34  ? 688  THR A OG1   1 
ATOM   5526  C CG2   . THR B 2 691  ? 131.455 152.668 183.575 1.00 51.34  ? 688  THR A CG2   1 
ATOM   5527  N N     . LYS B 2 692  ? 130.129 154.948 181.545 1.00 51.87  ? 689  LYS A N     1 
ATOM   5528  C CA    . LYS B 2 692  ? 130.697 155.740 180.462 1.00 51.87  ? 689  LYS A CA    1 
ATOM   5529  C C     . LYS B 2 692  ? 129.664 156.306 179.501 1.00 51.87  ? 689  LYS A C     1 
ATOM   5530  O O     . LYS B 2 692  ? 129.977 157.246 178.769 1.00 51.87  ? 689  LYS A O     1 
ATOM   5531  C CB    . LYS B 2 692  ? 131.709 154.910 179.663 1.00 51.87  ? 689  LYS A CB    1 
ATOM   5532  C CG    . LYS B 2 692  ? 131.088 153.870 178.754 1.00 51.87  ? 689  LYS A CG    1 
ATOM   5533  C CD    . LYS B 2 692  ? 132.078 153.412 177.699 1.00 51.87  ? 689  LYS A CD    1 
ATOM   5534  C CE    . LYS B 2 692  ? 132.376 154.519 176.705 1.00 51.87  ? 689  LYS A CE    1 
ATOM   5535  N NZ    . LYS B 2 692  ? 131.182 154.863 175.884 1.00 51.87  ? 689  LYS A NZ    1 
ATOM   5536  N N     . THR B 2 693  ? 128.452 155.763 179.480 1.00 56.23  ? 690  THR A N     1 
ATOM   5537  C CA    . THR B 2 693  ? 127.417 156.238 178.573 1.00 56.23  ? 690  THR A CA    1 
ATOM   5538  C C     . THR B 2 693  ? 126.453 157.219 179.227 1.00 56.23  ? 690  THR A C     1 
ATOM   5539  O O     . THR B 2 693  ? 125.495 157.648 178.576 1.00 56.23  ? 690  THR A O     1 
ATOM   5540  C CB    . THR B 2 693  ? 126.631 155.055 178.005 1.00 56.23  ? 690  THR A CB    1 
ATOM   5541  O OG1   . THR B 2 693  ? 125.979 154.355 179.072 1.00 56.23  ? 690  THR A OG1   1 
ATOM   5542  C CG2   . THR B 2 693  ? 127.562 154.100 177.275 1.00 56.23  ? 690  THR A CG2   1 
ATOM   5543  N N     . THR B 2 694  ? 126.678 157.583 180.490 1.00 54.43  ? 691  THR A N     1 
ATOM   5544  C CA    . THR B 2 694  ? 125.760 158.491 181.169 1.00 54.43  ? 691  THR A CA    1 
ATOM   5545  C C     . THR B 2 694  ? 125.951 159.936 180.725 1.00 54.43  ? 691  THR A C     1 
ATOM   5546  O O     . THR B 2 694  ? 125.007 160.731 180.788 1.00 54.43  ? 691  THR A O     1 
ATOM   5547  C CB    . THR B 2 694  ? 125.930 158.377 182.684 1.00 54.43  ? 691  THR A CB    1 
ATOM   5548  O OG1   . THR B 2 694  ? 125.111 159.356 183.335 1.00 54.43  ? 691  THR A OG1   1 
ATOM   5549  C CG2   . THR B 2 694  ? 127.383 158.592 183.080 1.00 54.43  ? 691  THR A CG2   1 
ATOM   5550  N N     . SER B 2 695  ? 127.154 160.296 180.275 1.00 56.26  ? 692  SER A N     1 
ATOM   5551  C CA    . SER B 2 695  ? 127.438 161.687 179.942 1.00 56.26  ? 692  SER A CA    1 
ATOM   5552  C C     . SER B 2 695  ? 126.823 162.111 178.615 1.00 56.26  ? 692  SER A C     1 
ATOM   5553  O O     . SER B 2 695  ? 126.480 163.287 178.448 1.00 56.26  ? 692  SER A O     1 
ATOM   5554  C CB    . SER B 2 695  ? 128.949 161.921 179.909 1.00 56.26  ? 692  SER A CB    1 
ATOM   5555  O OG    . SER B 2 695  ? 129.246 163.304 179.830 1.00 56.26  ? 692  SER A OG    1 
ATOM   5556  N N     . ILE B 2 696  ? 126.680 161.188 177.665 1.00 60.89  ? 693  ILE A N     1 
ATOM   5557  C CA    . ILE B 2 696  ? 126.193 161.549 176.339 1.00 60.89  ? 693  ILE A CA    1 
ATOM   5558  C C     . ILE B 2 696  ? 124.716 161.916 176.414 1.00 60.89  ? 693  ILE A C     1 
ATOM   5559  O O     . ILE B 2 696  ? 123.937 161.293 177.149 1.00 60.89  ? 693  ILE A O     1 
ATOM   5560  C CB    . ILE B 2 696  ? 126.450 160.411 175.339 1.00 60.89  ? 693  ILE A CB    1 
ATOM   5561  C CG1   . ILE B 2 696  ? 125.592 159.189 175.664 1.00 60.89  ? 693  ILE A CG1   1 
ATOM   5562  C CG2   . ILE B 2 696  ? 127.925 160.039 175.326 1.00 60.89  ? 693  ILE A CG2   1 
ATOM   5563  C CD1   . ILE B 2 696  ? 125.872 157.999 174.781 1.00 60.89  ? 693  ILE A CD1   1 
ATOM   5564  N N     . ASP B 2 697  ? 124.330 162.952 175.670 1.00 67.97  ? 694  ASP A N     1 
ATOM   5565  C CA    . ASP B 2 697  ? 122.954 163.433 175.669 1.00 67.97  ? 694  ASP A CA    1 
ATOM   5566  C C     . ASP B 2 697  ? 122.069 162.555 174.795 1.00 67.97  ? 694  ASP A C     1 
ATOM   5567  O O     . ASP B 2 697  ? 122.021 162.731 173.574 1.00 67.97  ? 694  ASP A O     1 
ATOM   5568  C CB    . ASP B 2 697  ? 122.894 164.885 175.194 1.00 67.97  ? 694  ASP A CB    1 
ATOM   5569  C CG    . ASP B 2 697  ? 121.496 165.465 175.271 1.00 67.97  ? 694  ASP A CG    1 
ATOM   5570  O OD1   . ASP B 2 697  ? 121.013 165.708 176.397 1.00 67.97  ? 694  ASP A OD1   1 
ATOM   5571  O OD2   . ASP B 2 697  ? 120.879 165.677 174.206 1.00 67.97  ? 694  ASP A OD2   1 
ATOM   5572  N N     . LEU B 2 698  ? 121.367 161.612 175.412 1.00 71.33  ? 695  LEU A N     1 
ATOM   5573  C CA    . LEU B 2 698  ? 120.491 160.697 174.696 1.00 71.33  ? 695  LEU A CA    1 
ATOM   5574  C C     . LEU B 2 698  ? 119.033 161.134 174.713 1.00 71.33  ? 695  LEU A C     1 
ATOM   5575  O O     . LEU B 2 698  ? 118.164 160.358 174.301 1.00 71.33  ? 695  LEU A O     1 
ATOM   5576  C CB    . LEU B 2 698  ? 120.617 159.290 175.282 1.00 71.33  ? 695  LEU A CB    1 
ATOM   5577  C CG    . LEU B 2 698  ? 122.009 158.677 175.131 1.00 71.33  ? 695  LEU A CG    1 
ATOM   5578  C CD1   . LEU B 2 698  ? 122.115 157.398 175.926 1.00 71.33  ? 695  LEU A CD1   1 
ATOM   5579  C CD2   . LEU B 2 698  ? 122.329 158.426 173.669 1.00 71.33  ? 695  LEU A CD2   1 
ATOM   5580  N N     . SER B 2 699  ? 118.744 162.352 175.177 1.00 75.21  ? 696  SER A N     1 
ATOM   5581  C CA    . SER B 2 699  ? 117.369 162.837 175.207 1.00 75.21  ? 696  SER A CA    1 
ATOM   5582  C C     . SER B 2 699  ? 116.775 162.982 173.813 1.00 75.21  ? 696  SER A C     1 
ATOM   5583  O O     . SER B 2 699  ? 115.549 163.065 173.682 1.00 75.21  ? 696  SER A O     1 
ATOM   5584  C CB    . SER B 2 699  ? 117.299 164.175 175.945 1.00 75.21  ? 696  SER A CB    1 
ATOM   5585  O OG    . SER B 2 699  ? 118.031 164.127 177.157 1.00 75.21  ? 696  SER A OG    1 
ATOM   5586  N N     . SER B 2 700  ? 117.612 163.015 172.773 1.00 75.21  ? 697  SER A N     1 
ATOM   5587  C CA    . SER B 2 700  ? 117.103 163.058 171.407 1.00 75.21  ? 697  SER A CA    1 
ATOM   5588  C C     . SER B 2 700  ? 116.397 161.767 171.016 1.00 75.21  ? 697  SER A C     1 
ATOM   5589  O O     . SER B 2 700  ? 115.678 161.747 170.012 1.00 75.21  ? 697  SER A O     1 
ATOM   5590  C CB    . SER B 2 700  ? 118.244 163.342 170.430 1.00 75.21  ? 697  SER A CB    1 
ATOM   5591  O OG    . SER B 2 700  ? 117.903 162.933 169.118 1.00 75.21  ? 697  SER A OG    1 
ATOM   5592  N N     . LEU B 2 701  ? 116.592 160.693 171.776 1.00 79.53  ? 698  LEU A N     1 
ATOM   5593  C CA    . LEU B 2 701  ? 115.900 159.443 171.497 1.00 79.53  ? 698  LEU A CA    1 
ATOM   5594  C C     . LEU B 2 701  ? 114.413 159.578 171.799 1.00 79.53  ? 698  LEU A C     1 
ATOM   5595  O O     . LEU B 2 701  ? 114.015 160.195 172.790 1.00 79.53  ? 698  LEU A O     1 
ATOM   5596  C CB    . LEU B 2 701  ? 116.502 158.306 172.322 1.00 79.53  ? 698  LEU A CB    1 
ATOM   5597  C CG    . LEU B 2 701  ? 117.921 157.871 171.953 1.00 79.53  ? 698  LEU A CG    1 
ATOM   5598  C CD1   . LEU B 2 701  ? 118.444 156.850 172.951 1.00 79.53  ? 698  LEU A CD1   1 
ATOM   5599  C CD2   . LEU B 2 701  ? 117.962 157.313 170.539 1.00 79.53  ? 698  LEU A CD2   1 
ATOM   5600  N N     . ARG B 2 702  ? 113.591 158.994 170.931 1.00 84.62  ? 699  ARG A N     1 
ATOM   5601  C CA    . ARG B 2 702  ? 112.152 159.029 171.115 1.00 84.62  ? 699  ARG A CA    1 
ATOM   5602  C C     . ARG B 2 702  ? 111.731 158.061 172.219 1.00 84.62  ? 699  ARG A C     1 
ATOM   5603  O O     . ARG B 2 702  ? 112.474 157.142 172.571 1.00 84.62  ? 699  ARG A O     1 
ATOM   5604  C CB    . ARG B 2 702  ? 111.444 158.677 169.809 1.00 84.62  ? 699  ARG A CB    1 
ATOM   5605  C CG    . ARG B 2 702  ? 111.792 159.594 168.650 1.00 84.62  ? 699  ARG A CG    1 
ATOM   5606  C CD    . ARG B 2 702  ? 111.489 158.937 167.314 1.00 84.62  ? 699  ARG A CD    1 
ATOM   5607  N NE    . ARG B 2 702  ? 112.512 157.969 166.935 1.00 84.62  ? 699  ARG A NE    1 
ATOM   5608  C CZ    . ARG B 2 702  ? 112.480 157.241 165.827 1.00 84.62  ? 699  ARG A CZ    1 
ATOM   5609  N NH1   . ARG B 2 702  ? 111.484 157.343 164.962 1.00 84.62  ? 699  ARG A NH1   1 
ATOM   5610  N NH2   . ARG B 2 702  ? 113.472 156.391 165.580 1.00 84.62  ? 699  ARG A NH2   1 
ATOM   5611  N N     . PRO B 2 703  ? 110.549 158.264 172.800 1.00 90.99  ? 700  PRO A N     1 
ATOM   5612  C CA    . PRO B 2 703  ? 110.007 157.261 173.723 1.00 90.99  ? 700  PRO A CA    1 
ATOM   5613  C C     . PRO B 2 703  ? 109.748 155.944 173.006 1.00 90.99  ? 700  PRO A C     1 
ATOM   5614  O O     . PRO B 2 703  ? 109.549 155.898 171.790 1.00 90.99  ? 700  PRO A O     1 
ATOM   5615  C CB    . PRO B 2 703  ? 108.704 157.896 174.227 1.00 90.99  ? 700  PRO A CB    1 
ATOM   5616  C CG    . PRO B 2 703  ? 108.437 159.056 173.316 1.00 90.99  ? 700  PRO A CG    1 
ATOM   5617  C CD    . PRO B 2 703  ? 109.769 159.512 172.823 1.00 90.99  ? 700  PRO A CD    1 
ATOM   5618  N N     . SER B 2 704  ? 109.753 154.860 173.785 1.00 89.47  ? 701  SER A N     1 
ATOM   5619  C CA    . SER B 2 704  ? 109.708 153.509 173.235 1.00 89.47  ? 701  SER A CA    1 
ATOM   5620  C C     . SER B 2 704  ? 108.390 153.176 172.547 1.00 89.47  ? 701  SER A C     1 
ATOM   5621  O O     . SER B 2 704  ? 108.313 152.145 171.870 1.00 89.47  ? 701  SER A O     1 
ATOM   5622  C CB    . SER B 2 704  ? 109.973 152.490 174.343 1.00 89.47  ? 701  SER A CB    1 
ATOM   5623  O OG    . SER B 2 704  ? 108.948 152.524 175.320 1.00 89.47  ? 701  SER A OG    1 
ATOM   5624  N N     . SER B 2 705  ? 107.359 154.008 172.701 1.00 92.01  ? 702  SER A N     1 
ATOM   5625  C CA    . SER B 2 705  ? 106.046 153.678 172.161 1.00 92.01  ? 702  SER A CA    1 
ATOM   5626  C C     . SER B 2 705  ? 106.017 153.645 170.636 1.00 92.01  ? 702  SER A C     1 
ATOM   5627  O O     . SER B 2 705  ? 105.203 152.911 170.066 1.00 92.01  ? 702  SER A O     1 
ATOM   5628  C CB    . SER B 2 705  ? 105.005 154.675 172.673 1.00 92.01  ? 702  SER A CB    1 
ATOM   5629  O OG    . SER B 2 705  ? 104.885 154.609 174.083 1.00 92.01  ? 702  SER A OG    1 
ATOM   5630  N N     . GLN B 2 706  ? 106.875 154.408 169.964 1.00 88.34  ? 703  GLN A N     1 
ATOM   5631  C CA    . GLN B 2 706  ? 106.813 154.556 168.514 1.00 88.34  ? 703  GLN A CA    1 
ATOM   5632  C C     . GLN B 2 706  ? 108.051 153.986 167.828 1.00 88.34  ? 703  GLN A C     1 
ATOM   5633  O O     . GLN B 2 706  ? 108.484 154.475 166.783 1.00 88.34  ? 703  GLN A O     1 
ATOM   5634  C CB    . GLN B 2 706  ? 106.613 156.020 168.127 1.00 88.34  ? 703  GLN A CB    1 
ATOM   5635  C CG    . GLN B 2 706  ? 107.747 156.945 168.536 1.00 88.34  ? 703  GLN A CG    1 
ATOM   5636  C CD    . GLN B 2 706  ? 107.511 157.600 169.879 1.00 88.34  ? 703  GLN A CD    1 
ATOM   5637  O OE1   . GLN B 2 706  ? 106.770 157.084 170.715 1.00 88.34  ? 703  GLN A OE1   1 
ATOM   5638  N NE2   . GLN B 2 706  ? 108.133 158.753 170.089 1.00 88.34  ? 703  GLN A NE2   1 
ATOM   5639  N N     . TYR B 2 707  ? 108.629 152.932 168.396 1.00 86.32  ? 704  TYR A N     1 
ATOM   5640  C CA    . TYR B 2 707  ? 109.759 152.239 167.790 1.00 86.32  ? 704  TYR A CA    1 
ATOM   5641  C C     . TYR B 2 707  ? 109.270 150.924 167.199 1.00 86.32  ? 704  TYR A C     1 
ATOM   5642  O O     . TYR B 2 707  ? 108.744 150.071 167.922 1.00 86.32  ? 704  TYR A O     1 
ATOM   5643  C CB    . TYR B 2 707  ? 110.873 152.005 168.808 1.00 86.32  ? 704  TYR A CB    1 
ATOM   5644  C CG    . TYR B 2 707  ? 111.757 153.214 169.000 1.00 86.32  ? 704  TYR A CG    1 
ATOM   5645  C CD1   . TYR B 2 707  ? 112.780 153.498 168.105 1.00 86.32  ? 704  TYR A CD1   1 
ATOM   5646  C CD2   . TYR B 2 707  ? 111.559 154.081 170.065 1.00 86.32  ? 704  TYR A CD2   1 
ATOM   5647  C CE1   . TYR B 2 707  ? 113.588 154.606 168.271 1.00 86.32  ? 704  TYR A CE1   1 
ATOM   5648  C CE2   . TYR B 2 707  ? 112.361 155.191 170.238 1.00 86.32  ? 704  TYR A CE2   1 
ATOM   5649  C CZ    . TYR B 2 707  ? 113.374 155.450 169.338 1.00 86.32  ? 704  TYR A CZ    1 
ATOM   5650  O OH    . TYR B 2 707  ? 114.175 156.555 169.509 1.00 86.32  ? 704  TYR A OH    1 
ATOM   5651  N N     . LYS B 2 708  ? 109.444 150.767 165.885 1.00 85.17  ? 705  LYS A N     1 
ATOM   5652  C CA    . LYS B 2 708  ? 108.905 149.595 165.202 1.00 85.17  ? 705  LYS A CA    1 
ATOM   5653  C C     . LYS B 2 708  ? 109.663 148.328 165.578 1.00 85.17  ? 705  LYS A C     1 
ATOM   5654  O O     . LYS B 2 708  ? 109.049 147.297 165.876 1.00 85.17  ? 705  LYS A O     1 
ATOM   5655  C CB    . LYS B 2 708  ? 108.938 149.810 163.689 1.00 85.17  ? 705  LYS A CB    1 
ATOM   5656  C CG    . LYS B 2 708  ? 108.273 151.098 163.230 1.00 85.17  ? 705  LYS A CG    1 
ATOM   5657  C CD    . LYS B 2 708  ? 106.760 151.003 163.330 1.00 85.17  ? 705  LYS A CD    1 
ATOM   5658  C CE    . LYS B 2 708  ? 106.223 149.865 162.477 1.00 85.17  ? 705  LYS A CE    1 
ATOM   5659  N NZ    . LYS B 2 708  ? 106.679 149.971 161.063 1.00 85.17  ? 705  LYS A NZ    1 
ATOM   5660  N N     . ASP B 2 709  ? 110.991 148.381 165.573 1.00 83.49  ? 706  ASP A N     1 
ATOM   5661  C CA    . ASP B 2 709  ? 111.799 147.192 165.814 1.00 83.49  ? 706  ASP A CA    1 
ATOM   5662  C C     . ASP B 2 709  ? 113.185 147.625 166.274 1.00 83.49  ? 706  ASP A C     1 
ATOM   5663  O O     . ASP B 2 709  ? 113.457 148.813 166.469 1.00 83.49  ? 706  ASP A O     1 
ATOM   5664  C CB    . ASP B 2 709  ? 111.873 146.314 164.562 1.00 83.49  ? 706  ASP A CB    1 
ATOM   5665  C CG    . ASP B 2 709  ? 112.500 147.032 163.386 1.00 83.49  ? 706  ASP A CG    1 
ATOM   5666  O OD1   . ASP B 2 709  ? 112.128 148.196 163.132 1.00 83.49  ? 706  ASP A OD1   1 
ATOM   5667  O OD2   . ASP B 2 709  ? 113.366 146.432 162.715 1.00 83.49  ? 706  ASP A OD2   1 
ATOM   5668  N N     . LEU B 2 710  ? 114.068 146.637 166.446 1.00 82.57  ? 707  LEU A N     1 
ATOM   5669  C CA    . LEU B 2 710  ? 115.410 146.919 166.944 1.00 82.57  ? 707  LEU A CA    1 
ATOM   5670  C C     . LEU B 2 710  ? 116.273 147.594 165.887 1.00 82.57  ? 707  LEU A C     1 
ATOM   5671  O O     . LEU B 2 710  ? 117.206 148.329 166.230 1.00 82.57  ? 707  LEU A O     1 
ATOM   5672  C CB    . LEU B 2 710  ? 116.090 145.632 167.414 1.00 82.57  ? 707  LEU A CB    1 
ATOM   5673  C CG    . LEU B 2 710  ? 115.782 145.096 168.816 1.00 82.57  ? 707  LEU A CG    1 
ATOM   5674  C CD1   . LEU B 2 710  ? 116.184 146.096 169.889 1.00 82.57  ? 707  LEU A CD1   1 
ATOM   5675  C CD2   . LEU B 2 710  ? 114.328 144.698 168.953 1.00 82.57  ? 707  LEU A CD2   1 
ATOM   5676  N N     . GLY B 2 711  ? 115.985 147.350 164.607 1.00 81.84  ? 708  GLY A N     1 
ATOM   5677  C CA    . GLY B 2 711  ? 116.836 147.880 163.553 1.00 81.84  ? 708  GLY A CA    1 
ATOM   5678  C C     . GLY B 2 711  ? 116.888 149.394 163.547 1.00 81.84  ? 708  GLY A C     1 
ATOM   5679  O O     . GLY B 2 711  ? 117.961 149.992 163.442 1.00 81.84  ? 708  GLY A O     1 
ATOM   5680  N N     . GLU B 2 712  ? 115.725 150.038 163.662 1.00 82.90  ? 709  GLU A N     1 
ATOM   5681  C CA    . GLU B 2 712  ? 115.697 151.496 163.653 1.00 82.90  ? 709  GLU A CA    1 
ATOM   5682  C C     . GLU B 2 712  ? 116.226 152.069 164.961 1.00 82.90  ? 709  GLU A C     1 
ATOM   5683  O O     . GLU B 2 712  ? 116.841 153.142 164.969 1.00 82.90  ? 709  GLU A O     1 
ATOM   5684  C CB    . GLU B 2 712  ? 114.279 151.997 163.377 1.00 82.90  ? 709  GLU A CB    1 
ATOM   5685  C CG    . GLU B 2 712  ? 113.230 151.495 164.354 1.00 82.90  ? 709  GLU A CG    1 
ATOM   5686  C CD    . GLU B 2 712  ? 111.818 151.788 163.889 1.00 82.90  ? 709  GLU A CD    1 
ATOM   5687  O OE1   . GLU B 2 712  ? 111.537 151.605 162.686 1.00 82.90  ? 709  GLU A OE1   1 
ATOM   5688  O OE2   . GLU B 2 712  ? 110.989 152.205 164.726 1.00 82.90  ? 709  GLU A OE2   1 
ATOM   5689  N N     . TYR B 2 713  ? 115.995 151.375 166.078 1.00 71.68  ? 710  TYR A N     1 
ATOM   5690  C CA    . TYR B 2 713  ? 116.442 151.895 167.365 1.00 71.68  ? 710  TYR A CA    1 
ATOM   5691  C C     . TYR B 2 713  ? 117.960 151.836 167.490 1.00 71.68  ? 710  TYR A C     1 
ATOM   5692  O O     . TYR B 2 713  ? 118.593 152.812 167.909 1.00 71.68  ? 710  TYR A O     1 
ATOM   5693  C CB    . TYR B 2 713  ? 115.779 151.125 168.506 1.00 71.68  ? 710  TYR A CB    1 
ATOM   5694  C CG    . TYR B 2 713  ? 116.280 151.524 169.874 1.00 71.68  ? 710  TYR A CG    1 
ATOM   5695  C CD1   . TYR B 2 713  ? 115.800 152.664 170.502 1.00 71.68  ? 710  TYR A CD1   1 
ATOM   5696  C CD2   . TYR B 2 713  ? 117.230 150.761 170.538 1.00 71.68  ? 710  TYR A CD2   1 
ATOM   5697  C CE1   . TYR B 2 713  ? 116.254 153.035 171.752 1.00 71.68  ? 710  TYR A CE1   1 
ATOM   5698  C CE2   . TYR B 2 713  ? 117.690 151.124 171.789 1.00 71.68  ? 710  TYR A CE2   1 
ATOM   5699  C CZ    . TYR B 2 713  ? 117.198 152.261 172.391 1.00 71.68  ? 710  TYR A CZ    1 
ATOM   5700  O OH    . TYR B 2 713  ? 117.652 152.627 173.637 1.00 71.68  ? 710  TYR A OH    1 
ATOM   5701  N N     . TYR B 2 714  ? 118.562 150.698 167.137 1.00 70.86  ? 711  TYR A N     1 
ATOM   5702  C CA    . TYR B 2 714  ? 120.013 150.572 167.234 1.00 70.86  ? 711  TYR A CA    1 
ATOM   5703  C C     . TYR B 2 714  ? 120.719 151.460 166.218 1.00 70.86  ? 711  TYR A C     1 
ATOM   5704  O O     . TYR B 2 714  ? 121.781 152.022 166.511 1.00 70.86  ? 711  TYR A O     1 
ATOM   5705  C CB    . TYR B 2 714  ? 120.431 149.113 167.061 1.00 70.86  ? 711  TYR A CB    1 
ATOM   5706  C CG    . TYR B 2 714  ? 120.111 148.245 168.256 1.00 70.86  ? 711  TYR A CG    1 
ATOM   5707  C CD1   . TYR B 2 714  ? 119.992 148.796 169.524 1.00 70.86  ? 711  TYR A CD1   1 
ATOM   5708  C CD2   . TYR B 2 714  ? 119.939 146.875 168.119 1.00 70.86  ? 711  TYR A CD2   1 
ATOM   5709  C CE1   . TYR B 2 714  ? 119.705 148.010 170.621 1.00 70.86  ? 711  TYR A CE1   1 
ATOM   5710  C CE2   . TYR B 2 714  ? 119.651 146.080 169.211 1.00 70.86  ? 711  TYR A CE2   1 
ATOM   5711  C CZ    . TYR B 2 714  ? 119.537 146.653 170.460 1.00 70.86  ? 711  TYR A CZ    1 
ATOM   5712  O OH    . TYR B 2 714  ? 119.250 145.865 171.550 1.00 70.86  ? 711  TYR A OH    1 
ATOM   5713  N N     . ALA B 2 715  ? 120.152 151.595 165.016 1.00 67.33  ? 712  ALA A N     1 
ATOM   5714  C CA    . ALA B 2 715  ? 120.733 152.498 164.029 1.00 67.33  ? 712  ALA A CA    1 
ATOM   5715  C C     . ALA B 2 715  ? 120.687 153.944 164.502 1.00 67.33  ? 712  ALA A C     1 
ATOM   5716  O O     . ALA B 2 715  ? 121.493 154.768 164.058 1.00 67.33  ? 712  ALA A O     1 
ATOM   5717  C CB    . ALA B 2 715  ? 120.012 152.354 162.689 1.00 67.33  ? 712  ALA A CB    1 
ATOM   5718  N N     . GLU B 2 716  ? 119.746 154.273 165.387 1.00 67.33  ? 713  GLU A N     1 
ATOM   5719  C CA    . GLU B 2 716  ? 119.679 155.616 165.949 1.00 67.33  ? 713  GLU A CA    1 
ATOM   5720  C C     . GLU B 2 716  ? 120.558 155.762 167.183 1.00 67.33  ? 713  GLU A C     1 
ATOM   5721  O O     . GLU B 2 716  ? 121.166 156.820 167.385 1.00 67.33  ? 713  GLU A O     1 
ATOM   5722  C CB    . GLU B 2 716  ? 118.232 155.967 166.294 1.00 67.33  ? 713  GLU A CB    1 
ATOM   5723  C CG    . GLU B 2 716  ? 118.027 157.394 166.769 1.00 67.33  ? 713  GLU A CG    1 
ATOM   5724  C CD    . GLU B 2 716  ? 116.562 157.744 166.940 1.00 67.33  ? 713  GLU A CD    1 
ATOM   5725  O OE1   . GLU B 2 716  ? 115.727 156.816 166.967 1.00 67.33  ? 713  GLU A OE1   1 
ATOM   5726  O OE2   . GLU B 2 716  ? 116.245 158.947 167.048 1.00 67.33  ? 713  GLU A OE2   1 
ATOM   5727  N N     . LEU B 2 717  ? 120.638 154.721 168.013 1.00 62.57  ? 714  LEU A N     1 
ATOM   5728  C CA    . LEU B 2 717  ? 121.402 154.806 169.253 1.00 62.57  ? 714  LEU A CA    1 
ATOM   5729  C C     . LEU B 2 717  ? 122.904 154.743 168.999 1.00 62.57  ? 714  LEU A C     1 
ATOM   5730  O O     . LEU B 2 717  ? 123.684 155.365 169.729 1.00 62.57  ? 714  LEU A O     1 
ATOM   5731  C CB    . LEU B 2 717  ? 120.972 153.690 170.205 1.00 62.57  ? 714  LEU A CB    1 
ATOM   5732  C CG    . LEU B 2 717  ? 121.675 153.612 171.561 1.00 62.57  ? 714  LEU A CG    1 
ATOM   5733  C CD1   . LEU B 2 717  ? 121.589 154.942 172.290 1.00 62.57  ? 714  LEU A CD1   1 
ATOM   5734  C CD2   . LEU B 2 717  ? 121.080 152.498 172.405 1.00 62.57  ? 714  LEU A CD2   1 
ATOM   5735  N N     . ASN B 2 718  ? 123.324 154.003 167.973 1.00 54.85  ? 715  ASN A N     1 
ATOM   5736  C CA    . ASN B 2 718  ? 124.753 153.809 167.729 1.00 54.85  ? 715  ASN A CA    1 
ATOM   5737  C C     . ASN B 2 718  ? 125.510 155.105 167.457 1.00 54.85  ? 715  ASN A C     1 
ATOM   5738  O O     . ASN B 2 718  ? 126.567 155.311 168.078 1.00 54.85  ? 715  ASN A O     1 
ATOM   5739  C CB    . ASN B 2 718  ? 124.944 152.806 166.586 1.00 54.85  ? 715  ASN A CB    1 
ATOM   5740  C CG    . ASN B 2 718  ? 125.186 151.398 167.085 1.00 54.85  ? 715  ASN A CG    1 
ATOM   5741  O OD1   . ASN B 2 718  ? 126.330 150.975 167.250 1.00 54.85  ? 715  ASN A OD1   1 
ATOM   5742  N ND2   . ASN B 2 718  ? 124.109 150.662 167.328 1.00 54.85  ? 715  ASN A ND2   1 
ATOM   5743  N N     . PRO B 2 719  ? 125.066 156.000 166.566 1.00 50.73  ? 716  PRO A N     1 
ATOM   5744  C CA    . PRO B 2 719  ? 125.858 157.215 166.310 1.00 50.73  ? 716  PRO A CA    1 
ATOM   5745  C C     . PRO B 2 719  ? 125.996 158.125 167.515 1.00 50.73  ? 716  PRO A C     1 
ATOM   5746  O O     . PRO B 2 719  ? 126.949 158.911 167.571 1.00 50.73  ? 716  PRO A O     1 
ATOM   5747  C CB    . PRO B 2 719  ? 125.090 157.907 165.176 1.00 50.73  ? 716  PRO A CB    1 
ATOM   5748  C CG    . PRO B 2 719  ? 123.709 157.378 165.280 1.00 50.73  ? 716  PRO A CG    1 
ATOM   5749  C CD    . PRO B 2 719  ? 123.872 155.955 165.705 1.00 50.73  ? 716  PRO A CD    1 
ATOM   5750  N N     . LEU B 2 720  ? 125.079 158.050 168.479 1.00 49.98  ? 717  LEU A N     1 
ATOM   5751  C CA    . LEU B 2 720  ? 125.154 158.937 169.634 1.00 49.98  ? 717  LEU A CA    1 
ATOM   5752  C C     . LEU B 2 720  ? 126.278 158.527 170.578 1.00 49.98  ? 717  LEU A C     1 
ATOM   5753  O O     . LEU B 2 720  ? 126.819 159.366 171.309 1.00 49.98  ? 717  LEU A O     1 
ATOM   5754  C CB    . LEU B 2 720  ? 123.812 158.952 170.365 1.00 49.98  ? 717  LEU A CB    1 
ATOM   5755  C CG    . LEU B 2 720  ? 122.615 159.385 169.517 1.00 49.98  ? 717  LEU A CG    1 
ATOM   5756  C CD1   . LEU B 2 720  ? 121.307 159.059 170.216 1.00 49.98  ? 717  LEU A CD1   1 
ATOM   5757  C CD2   . LEU B 2 720  ? 122.697 160.868 169.189 1.00 49.98  ? 717  LEU A CD2   1 
ATOM   5758  N N     . LEU B 2 721  ? 126.643 157.243 170.580 1.00 44.73  ? 718  LEU A N     1 
ATOM   5759  C CA    . LEU B 2 721  ? 127.661 156.763 171.510 1.00 44.73  ? 718  LEU A CA    1 
ATOM   5760  C C     . LEU B 2 721  ? 129.054 157.233 171.108 1.00 44.73  ? 718  LEU A C     1 
ATOM   5761  O O     . LEU B 2 721  ? 129.842 157.657 171.960 1.00 44.73  ? 718  LEU A O     1 
ATOM   5762  C CB    . LEU B 2 721  ? 127.612 155.238 171.593 1.00 44.73  ? 718  LEU A CB    1 
ATOM   5763  C CG    . LEU B 2 721  ? 126.221 154.601 171.640 1.00 44.73  ? 718  LEU A CG    1 
ATOM   5764  C CD1   . LEU B 2 721  ? 126.299 153.107 171.372 1.00 44.73  ? 718  LEU A CD1   1 
ATOM   5765  C CD2   . LEU B 2 721  ? 125.549 154.870 172.970 1.00 44.73  ? 718  LEU A CD2   1 
ATOM   5766  N N     . TYR B 2 722  ? 129.374 157.166 169.820 1.00 44.73  ? 719  TYR A N     1 
ATOM   5767  C CA    . TYR B 2 722  ? 130.710 157.507 169.351 1.00 44.73  ? 719  TYR A CA    1 
ATOM   5768  C C     . TYR B 2 722  ? 130.900 159.020 169.315 1.00 44.73  ? 719  TYR A C     1 
ATOM   5769  O O     . TYR B 2 722  ? 130.012 159.762 168.886 1.00 44.73  ? 719  TYR A O     1 
ATOM   5770  C CB    . TYR B 2 722  ? 130.933 156.897 167.969 1.00 44.73  ? 719  TYR A CB    1 
ATOM   5771  C CG    . TYR B 2 722  ? 132.084 157.465 167.176 1.00 44.73  ? 719  TYR A CG    1 
ATOM   5772  C CD1   . TYR B 2 722  ? 133.378 157.009 167.367 1.00 44.73  ? 719  TYR A CD1   1 
ATOM   5773  C CD2   . TYR B 2 722  ? 131.869 158.438 166.212 1.00 44.73  ? 719  TYR A CD2   1 
ATOM   5774  C CE1   . TYR B 2 722  ? 134.426 157.517 166.631 1.00 44.73  ? 719  TYR A CE1   1 
ATOM   5775  C CE2   . TYR B 2 722  ? 132.911 158.952 165.477 1.00 44.73  ? 719  TYR A CE2   1 
ATOM   5776  C CZ    . TYR B 2 722  ? 134.185 158.488 165.689 1.00 44.73  ? 719  TYR A CZ    1 
ATOM   5777  O OH    . TYR B 2 722  ? 135.217 159.004 164.946 1.00 44.73  ? 719  TYR A OH    1 
ATOM   5778  N N     . HIS B 2 723  ? 132.069 159.476 169.763 1.00 44.73  ? 720  HIS A N     1 
ATOM   5779  C CA    . HIS B 2 723  ? 132.348 160.904 169.854 1.00 44.73  ? 720  HIS A CA    1 
ATOM   5780  C C     . HIS B 2 723  ? 133.846 161.127 170.003 1.00 44.73  ? 720  HIS A C     1 
ATOM   5781  O O     . HIS B 2 723  ? 134.535 160.332 170.647 1.00 44.73  ? 720  HIS A O     1 
ATOM   5782  C CB    . HIS B 2 723  ? 131.606 161.539 171.035 1.00 44.73  ? 720  HIS A CB    1 
ATOM   5783  C CG    . HIS B 2 723  ? 131.620 163.036 171.022 1.00 44.73  ? 720  HIS A CG    1 
ATOM   5784  N ND1   . HIS B 2 723  ? 131.715 163.789 172.172 1.00 44.73  ? 720  HIS A ND1   1 
ATOM   5785  C CD2   . HIS B 2 723  ? 131.549 163.920 169.999 1.00 44.73  ? 720  HIS A CD2   1 
ATOM   5786  C CE1   . HIS B 2 723  ? 131.704 165.072 171.858 1.00 44.73  ? 720  HIS A CE1   1 
ATOM   5787  N NE2   . HIS B 2 723  ? 131.603 165.179 170.546 1.00 44.73  ? 720  HIS A NE2   1 
ATOM   5788  N N     . ILE B 2 724  ? 134.339 162.210 169.405 1.00 44.73  ? 721  ILE A N     1 
ATOM   5789  C CA    . ILE B 2 724  ? 135.726 162.639 169.544 1.00 44.73  ? 721  ILE A CA    1 
ATOM   5790  C C     . ILE B 2 724  ? 135.748 164.087 170.008 1.00 44.73  ? 721  ILE A C     1 
ATOM   5791  O O     . ILE B 2 724  ? 135.066 164.940 169.428 1.00 44.73  ? 721  ILE A O     1 
ATOM   5792  C CB    . ILE B 2 724  ? 136.521 162.493 168.233 1.00 44.73  ? 721  ILE A CB    1 
ATOM   5793  C CG1   . ILE B 2 724  ? 136.611 161.031 167.808 1.00 44.73  ? 721  ILE A CG1   1 
ATOM   5794  C CG2   . ILE B 2 724  ? 137.908 163.087 168.375 1.00 44.73  ? 721  ILE A CG2   1 
ATOM   5795  C CD1   . ILE B 2 724  ? 137.153 160.862 166.416 1.00 44.73  ? 721  ILE A CD1   1 
ATOM   5796  N N     . SER B 2 725  ? 136.534 164.364 171.043 1.00 44.73  ? 722  SER A N     1 
ATOM   5797  C CA    . SER B 2 725  ? 136.724 165.714 171.549 1.00 44.73  ? 722  SER A CA    1 
ATOM   5798  C C     . SER B 2 725  ? 138.209 165.958 171.774 1.00 44.73  ? 722  SER A C     1 
ATOM   5799  O O     . SER B 2 725  ? 138.986 165.026 171.997 1.00 44.73  ? 722  SER A O     1 
ATOM   5800  C CB    . SER B 2 725  ? 135.945 165.945 172.850 1.00 44.73  ? 722  SER A CB    1 
ATOM   5801  O OG    . SER B 2 725  ? 136.484 167.033 173.581 1.00 44.73  ? 722  SER A OG    1 
ATOM   5802  N N     . PHE B 2 726  ? 138.598 167.227 171.713 1.00 44.73  ? 723  PHE A N     1 
ATOM   5803  C CA    . PHE B 2 726  ? 139.987 167.632 171.867 1.00 44.73  ? 723  PHE A CA    1 
ATOM   5804  C C     . PHE B 2 726  ? 140.132 168.523 173.092 1.00 44.73  ? 723  PHE A C     1 
ATOM   5805  O O     . PHE B 2 726  ? 139.298 169.399 173.336 1.00 44.73  ? 723  PHE A O     1 
ATOM   5806  C CB    . PHE B 2 726  ? 140.486 168.374 170.624 1.00 44.73  ? 723  PHE A CB    1 
ATOM   5807  C CG    . PHE B 2 726  ? 140.876 167.469 169.493 1.00 44.73  ? 723  PHE A CG    1 
ATOM   5808  C CD1   . PHE B 2 726  ? 142.156 166.953 169.411 1.00 44.73  ? 723  PHE A CD1   1 
ATOM   5809  C CD2   . PHE B 2 726  ? 139.964 167.138 168.508 1.00 44.73  ? 723  PHE A CD2   1 
ATOM   5810  C CE1   . PHE B 2 726  ? 142.518 166.122 168.370 1.00 44.73  ? 723  PHE A CE1   1 
ATOM   5811  C CE2   . PHE B 2 726  ? 140.320 166.307 167.464 1.00 44.73  ? 723  PHE A CE2   1 
ATOM   5812  C CZ    . PHE B 2 726  ? 141.599 165.799 167.396 1.00 44.73  ? 723  PHE A CZ    1 
ATOM   5813  N N     . GLN B 2 727  ? 141.194 168.290 173.860 1.00 44.73  ? 724  GLN A N     1 
ATOM   5814  C CA    . GLN B 2 727  ? 141.518 169.114 175.016 1.00 44.73  ? 724  GLN A CA    1 
ATOM   5815  C C     . GLN B 2 727  ? 142.993 169.473 174.968 1.00 44.73  ? 724  GLN A C     1 
ATOM   5816  O O     . GLN B 2 727  ? 143.835 168.612 174.700 1.00 44.73  ? 724  GLN A O     1 
ATOM   5817  C CB    . GLN B 2 727  ? 141.184 168.397 176.329 1.00 44.73  ? 724  GLN A CB    1 
ATOM   5818  C CG    . GLN B 2 727  ? 139.696 168.194 176.557 1.00 44.73  ? 724  GLN A CG    1 
ATOM   5819  C CD    . GLN B 2 727  ? 139.393 167.514 177.876 1.00 44.73  ? 724  GLN A CD    1 
ATOM   5820  O OE1   . GLN B 2 727  ? 140.150 167.636 178.839 1.00 44.73  ? 724  GLN A OE1   1 
ATOM   5821  N NE2   . GLN B 2 727  ? 138.278 166.796 177.930 1.00 44.73  ? 724  GLN A NE2   1 
ATOM   5822  N N     . ARG B 2 728  ? 143.298 170.741 175.226 1.00 44.73  ? 725  ARG A N     1 
ATOM   5823  C CA    . ARG B 2 728  ? 144.668 171.222 175.117 1.00 44.73  ? 725  ARG A CA    1 
ATOM   5824  C C     . ARG B 2 728  ? 145.546 170.630 176.213 1.00 44.73  ? 725  ARG A C     1 
ATOM   5825  O O     . ARG B 2 728  ? 145.157 170.570 177.383 1.00 44.73  ? 725  ARG A O     1 
ATOM   5826  C CB    . ARG B 2 728  ? 144.695 172.748 175.186 1.00 44.73  ? 725  ARG A CB    1 
ATOM   5827  C CG    . ARG B 2 728  ? 146.065 173.341 175.462 1.00 44.73  ? 725  ARG A CG    1 
ATOM   5828  C CD    . ARG B 2 728  ? 146.947 173.274 174.231 1.00 44.73  ? 725  ARG A CD    1 
ATOM   5829  N NE    . ARG B 2 728  ? 146.226 173.649 173.022 1.00 44.73  ? 725  ARG A NE    1 
ATOM   5830  C CZ    . ARG B 2 728  ? 146.064 174.896 172.602 1.00 44.73  ? 725  ARG A CZ    1 
ATOM   5831  N NH1   . ARG B 2 728  ? 146.568 175.920 173.270 1.00 44.73  ? 725  ARG A NH1   1 
ATOM   5832  N NH2   . ARG B 2 728  ? 145.383 175.120 171.482 1.00 44.73  ? 725  ARG A NH2   1 
ATOM   5833  N N     . ILE B 2 729  ? 146.739 170.190 175.824 1.00 44.73  ? 726  ILE A N     1 
ATOM   5834  C CA    . ILE B 2 729  ? 147.749 169.682 176.743 1.00 44.73  ? 726  ILE A CA    1 
ATOM   5835  C C     . ILE B 2 729  ? 148.975 170.575 176.627 1.00 44.73  ? 726  ILE A C     1 
ATOM   5836  O O     . ILE B 2 729  ? 149.427 170.873 175.516 1.00 44.73  ? 726  ILE A O     1 
ATOM   5837  C CB    . ILE B 2 729  ? 148.105 168.214 176.447 1.00 44.73  ? 726  ILE A CB    1 
ATOM   5838  C CG1   . ILE B 2 729  ? 146.859 167.336 176.556 1.00 44.73  ? 726  ILE A CG1   1 
ATOM   5839  C CG2   . ILE B 2 729  ? 149.176 167.722 177.400 1.00 44.73  ? 726  ILE A CG2   1 
ATOM   5840  C CD1   . ILE B 2 729  ? 146.228 167.343 177.930 1.00 44.73  ? 726  ILE A CD1   1 
ATOM   5841  N N     . ALA B 2 730  ? 149.502 171.008 177.771 1.00 44.73  ? 727  ALA A N     1 
ATOM   5842  C CA    . ALA B 2 730  ? 150.592 171.973 177.780 1.00 44.73  ? 727  ALA A CA    1 
ATOM   5843  C C     . ALA B 2 730  ? 151.823 171.415 177.078 1.00 44.73  ? 727  ALA A C     1 
ATOM   5844  O O     . ALA B 2 730  ? 152.128 170.224 177.170 1.00 44.73  ? 727  ALA A O     1 
ATOM   5845  C CB    . ALA B 2 730  ? 150.939 172.365 179.216 1.00 44.73  ? 727  ALA A CB    1 
ATOM   5846  N N     . GLU B 2 731  ? 152.530 172.296 176.365 1.00 44.73  ? 728  GLU A N     1 
ATOM   5847  C CA    . GLU B 2 731  ? 153.710 171.875 175.616 1.00 44.73  ? 728  GLU A CA    1 
ATOM   5848  C C     . GLU B 2 731  ? 154.822 171.390 176.536 1.00 44.73  ? 728  GLU A C     1 
ATOM   5849  O O     . GLU B 2 731  ? 155.605 170.514 176.153 1.00 44.73  ? 728  GLU A O     1 
ATOM   5850  C CB    . GLU B 2 731  ? 154.211 173.025 174.742 1.00 44.73  ? 728  GLU A CB    1 
ATOM   5851  C CG    . GLU B 2 731  ? 155.355 172.653 173.816 1.00 44.73  ? 728  GLU A CG    1 
ATOM   5852  C CD    . GLU B 2 731  ? 155.823 173.819 172.971 1.00 44.73  ? 728  GLU A CD    1 
ATOM   5853  O OE1   . GLU B 2 731  ? 155.270 174.928 173.128 1.00 44.73  ? 728  GLU A OE1   1 
ATOM   5854  O OE2   . GLU B 2 731  ? 156.745 173.628 172.150 1.00 44.73  ? 728  GLU A OE2   1 
ATOM   5855  N N     . LYS B 2 732  ? 154.910 171.946 177.746 1.00 44.73  ? 729  LYS A N     1 
ATOM   5856  C CA    . LYS B 2 732  ? 155.976 171.556 178.662 1.00 44.73  ? 729  LYS A CA    1 
ATOM   5857  C C     . LYS B 2 732  ? 155.869 170.084 179.040 1.00 44.73  ? 729  LYS A C     1 
ATOM   5858  O O     . LYS B 2 732  ? 156.882 169.380 179.116 1.00 44.73  ? 729  LYS A O     1 
ATOM   5859  C CB    . LYS B 2 732  ? 155.941 172.437 179.910 1.00 38.03  ? 729  LYS A CB    1 
ATOM   5860  C CG    . LYS B 2 732  ? 157.069 172.175 180.894 1.00 38.03  ? 729  LYS A CG    1 
ATOM   5861  C CD    . LYS B 2 732  ? 158.403 172.651 180.341 1.00 38.03  ? 729  LYS A CD    1 
ATOM   5862  C CE    . LYS B 2 732  ? 159.508 172.524 181.377 1.00 38.03  ? 729  LYS A CE    1 
ATOM   5863  N NZ    . LYS B 2 732  ? 160.833 172.925 180.828 1.00 38.03  ? 729  LYS A NZ    1 
ATOM   5864  N N     . GLU B 2 733  ? 154.649 169.600 179.285 1.00 44.73  ? 730  GLU A N     1 
ATOM   5865  C CA    . GLU B 2 733  ? 154.465 168.191 179.617 1.00 44.73  ? 730  GLU A CA    1 
ATOM   5866  C C     . GLU B 2 733  ? 154.834 167.295 178.442 1.00 44.73  ? 730  GLU A C     1 
ATOM   5867  O O     . GLU B 2 733  ? 155.482 166.256 178.618 1.00 44.73  ? 730  GLU A O     1 
ATOM   5868  C CB    . GLU B 2 733  ? 153.022 167.935 180.053 1.00 44.73  ? 730  GLU A CB    1 
ATOM   5869  C CG    . GLU B 2 733  ? 152.513 168.878 181.127 1.00 44.73  ? 730  GLU A CG    1 
ATOM   5870  C CD    . GLU B 2 733  ? 151.018 168.755 181.344 1.00 44.73  ? 730  GLU A CD    1 
ATOM   5871  O OE1   . GLU B 2 733  ? 150.572 167.690 181.820 1.00 44.73  ? 730  GLU A OE1   1 
ATOM   5872  O OE2   . GLU B 2 733  ? 150.289 169.721 181.039 1.00 44.73  ? 730  GLU A OE2   1 
ATOM   5873  N N     . ILE B 2 734  ? 154.423 167.678 177.231 1.00 44.73  ? 731  ILE A N     1 
ATOM   5874  C CA    . ILE B 2 734  ? 154.685 166.847 176.058 1.00 44.73  ? 731  ILE A CA    1 
ATOM   5875  C C     . ILE B 2 734  ? 156.179 166.791 175.767 1.00 44.73  ? 731  ILE A C     1 
ATOM   5876  O O     . ILE B 2 734  ? 156.741 165.720 175.510 1.00 44.73  ? 731  ILE A O     1 
ATOM   5877  C CB    . ILE B 2 734  ? 153.894 167.364 174.844 1.00 44.73  ? 731  ILE A CB    1 
ATOM   5878  C CG1   . ILE B 2 734  ? 152.399 167.407 175.158 1.00 44.73  ? 731  ILE A CG1   1 
ATOM   5879  C CG2   . ILE B 2 734  ? 154.153 166.488 173.632 1.00 44.73  ? 731  ILE A CG2   1 
ATOM   5880  C CD1   . ILE B 2 734  ? 151.745 166.048 175.185 1.00 44.73  ? 731  ILE A CD1   1 
ATOM   5881  N N     . MET B 2 735  ? 156.845 167.948 175.797 1.00 44.73  ? 732  MET A N     1 
ATOM   5882  C CA    . MET B 2 735  ? 158.277 167.980 175.523 1.00 44.73  ? 732  MET A CA    1 
ATOM   5883  C C     . MET B 2 735  ? 159.064 167.229 176.589 1.00 44.73  ? 732  MET A C     1 
ATOM   5884  O O     . MET B 2 735  ? 160.021 166.513 176.274 1.00 44.73  ? 732  MET A O     1 
ATOM   5885  C CB    . MET B 2 735  ? 158.759 169.426 175.416 1.00 44.73  ? 732  MET A CB    1 
ATOM   5886  C CG    . MET B 2 735  ? 158.472 170.080 174.072 1.00 44.73  ? 732  MET A CG    1 
ATOM   5887  S SD    . MET B 2 735  ? 159.608 169.551 172.774 1.00 44.73  ? 732  MET A SD    1 
ATOM   5888  C CE    . MET B 2 735  ? 158.591 168.378 171.880 1.00 44.73  ? 732  MET A CE    1 
ATOM   5889  N N     . ASP B 2 736  ? 158.677 167.380 177.858 1.00 44.73  ? 733  ASP A N     1 
ATOM   5890  C CA    . ASP B 2 736  ? 159.368 166.668 178.928 1.00 44.73  ? 733  ASP A CA    1 
ATOM   5891  C C     . ASP B 2 736  ? 159.109 165.169 178.851 1.00 44.73  ? 733  ASP A C     1 
ATOM   5892  O O     . ASP B 2 736  ? 159.985 164.365 179.191 1.00 44.73  ? 733  ASP A O     1 
ATOM   5893  C CB    . ASP B 2 736  ? 158.943 167.216 180.288 1.00 44.73  ? 733  ASP A CB    1 
ATOM   5894  C CG    . ASP B 2 736  ? 159.786 168.396 180.728 1.00 44.73  ? 733  ASP A CG    1 
ATOM   5895  O OD1   . ASP B 2 736  ? 160.982 168.439 180.372 1.00 44.73  ? 733  ASP A OD1   1 
ATOM   5896  O OD2   . ASP B 2 736  ? 159.252 169.278 181.433 1.00 44.73  ? 733  ASP A OD2   1 
ATOM   5897  N N     . ALA B 2 737  ? 157.909 164.773 178.420 1.00 44.73  ? 734  ALA A N     1 
ATOM   5898  C CA    . ALA B 2 737  ? 157.627 163.354 178.232 1.00 44.73  ? 734  ALA A CA    1 
ATOM   5899  C C     . ALA B 2 737  ? 158.525 162.756 177.158 1.00 44.73  ? 734  ALA A C     1 
ATOM   5900  O O     . ALA B 2 737  ? 159.041 161.644 177.317 1.00 44.73  ? 734  ALA A O     1 
ATOM   5901  C CB    . ALA B 2 737  ? 156.155 163.152 177.877 1.00 44.73  ? 734  ALA A CB    1 
ATOM   5902  N N     . VAL B 2 738  ? 158.719 163.479 176.055 1.00 44.73  ? 735  VAL A N     1 
ATOM   5903  C CA    . VAL B 2 738  ? 159.655 163.034 175.028 1.00 44.73  ? 735  VAL A CA    1 
ATOM   5904  C C     . VAL B 2 738  ? 161.086 163.115 175.545 1.00 44.73  ? 735  VAL A C     1 
ATOM   5905  O O     . VAL B 2 738  ? 161.920 162.252 175.244 1.00 44.73  ? 735  VAL A O     1 
ATOM   5906  C CB    . VAL B 2 738  ? 159.461 163.861 173.744 1.00 44.73  ? 735  VAL A CB    1 
ATOM   5907  C CG1   . VAL B 2 738  ? 160.536 163.529 172.721 1.00 44.73  ? 735  VAL A CG1   1 
ATOM   5908  C CG2   . VAL B 2 738  ? 158.077 163.622 173.168 1.00 44.73  ? 735  VAL A CG2   1 
ATOM   5909  N N     . GLU B 2 739  ? 161.391 164.151 176.331 1.00 44.73  ? 736  GLU A N     1 
ATOM   5910  C CA    . GLU B 2 739  ? 162.729 164.309 176.893 1.00 44.73  ? 736  GLU A CA    1 
ATOM   5911  C C     . GLU B 2 739  ? 163.126 163.101 177.732 1.00 44.73  ? 736  GLU A C     1 
ATOM   5912  O O     . GLU B 2 739  ? 164.194 162.513 177.530 1.00 44.73  ? 736  GLU A O     1 
ATOM   5913  C CB    . GLU B 2 739  ? 162.785 165.588 177.730 1.00 44.73  ? 736  GLU A CB    1 
ATOM   5914  C CG    . GLU B 2 739  ? 164.182 166.075 178.076 1.00 44.73  ? 736  GLU A CG    1 
ATOM   5915  C CD    . GLU B 2 739  ? 165.142 165.994 176.911 1.00 44.73  ? 736  GLU A CD    1 
ATOM   5916  O OE1   . GLU B 2 739  ? 165.061 166.853 176.008 1.00 44.73  ? 736  GLU A OE1   1 
ATOM   5917  O OE2   . GLU B 2 739  ? 165.978 165.068 176.900 1.00 44.73  ? 736  GLU A OE2   1 
ATOM   5918  N N     . THR B 2 740  ? 162.273 162.714 178.680 1.00 44.73  ? 737  THR A N     1 
ATOM   5919  C CA    . THR B 2 740  ? 162.586 161.568 179.526 1.00 44.73  ? 737  THR A CA    1 
ATOM   5920  C C     . THR B 2 740  ? 162.409 160.252 178.780 1.00 44.73  ? 737  THR A C     1 
ATOM   5921  O O     . THR B 2 740  ? 163.088 159.268 179.094 1.00 44.73  ? 737  THR A O     1 
ATOM   5922  C CB    . THR B 2 740  ? 161.716 161.589 180.781 1.00 44.73  ? 737  THR A CB    1 
ATOM   5923  O OG1   . THR B 2 740  ? 160.337 161.502 180.408 1.00 44.73  ? 737  THR A OG1   1 
ATOM   5924  C CG2   . THR B 2 740  ? 161.943 162.874 181.562 1.00 44.73  ? 737  THR A CG2   1 
ATOM   5925  N N     . GLY B 2 741  ? 161.513 160.213 177.799 1.00 44.73  ? 738  GLY A N     1 
ATOM   5926  C CA    . GLY B 2 741  ? 161.278 159.017 177.022 1.00 44.73  ? 738  GLY A CA    1 
ATOM   5927  C C     . GLY B 2 741  ? 159.968 158.311 177.286 1.00 44.73  ? 738  GLY A C     1 
ATOM   5928  O O     . GLY B 2 741  ? 159.784 157.191 176.798 1.00 44.73  ? 738  GLY A O     1 
ATOM   5929  N N     . LYS B 2 742  ? 159.052 158.923 178.039 1.00 44.73  ? 739  LYS A N     1 
ATOM   5930  C CA    . LYS B 2 742  ? 157.769 158.285 178.302 1.00 44.73  ? 739  LYS A CA    1 
ATOM   5931  C C     . LYS B 2 742  ? 156.839 158.326 177.098 1.00 44.73  ? 739  LYS A C     1 
ATOM   5932  O O     . LYS B 2 742  ? 155.954 157.472 176.988 1.00 44.73  ? 739  LYS A O     1 
ATOM   5933  C CB    . LYS B 2 742  ? 157.087 158.938 179.505 1.00 35.42  ? 739  LYS A CB    1 
ATOM   5934  C CG    . LYS B 2 742  ? 158.038 159.360 180.609 1.00 35.42  ? 739  LYS A CG    1 
ATOM   5935  C CD    . LYS B 2 742  ? 157.339 159.394 181.957 1.00 35.42  ? 739  LYS A CD    1 
ATOM   5936  C CE    . LYS B 2 742  ? 158.182 160.109 182.999 1.00 35.42  ? 739  LYS A CE    1 
ATOM   5937  N NZ    . LYS B 2 742  ? 158.159 161.586 182.814 1.00 35.42  ? 739  LYS A NZ    1 
ATOM   5938  N N     . LEU B 2 743  ? 157.012 159.292 176.201 1.00 44.73  ? 740  LEU A N     1 
ATOM   5939  C CA    . LEU B 2 743  ? 156.159 159.431 175.031 1.00 44.73  ? 740  LEU A CA    1 
ATOM   5940  C C     . LEU B 2 743  ? 157.016 159.495 173.778 1.00 44.73  ? 740  LEU A C     1 
ATOM   5941  O O     . LEU B 2 743  ? 158.059 160.153 173.762 1.00 44.73  ? 740  LEU A O     1 
ATOM   5942  C CB    . LEU B 2 743  ? 155.280 160.681 175.127 1.00 44.73  ? 740  LEU A CB    1 
ATOM   5943  C CG    . LEU B 2 743  ? 154.356 160.951 173.940 1.00 44.73  ? 740  LEU A CG    1 
ATOM   5944  C CD1   . LEU B 2 743  ? 153.205 159.962 173.930 1.00 44.73  ? 740  LEU A CD1   1 
ATOM   5945  C CD2   . LEU B 2 743  ? 153.840 162.377 173.973 1.00 44.73  ? 740  LEU A CD2   1 
ATOM   5946  N N     . TYR B 2 744  ? 156.570 158.809 172.730 1.00 44.73  ? 741  TYR A N     1 
ATOM   5947  C CA    . TYR B 2 744  ? 157.234 158.818 171.433 1.00 44.73  ? 741  TYR A CA    1 
ATOM   5948  C C     . TYR B 2 744  ? 156.401 159.664 170.479 1.00 44.73  ? 741  TYR A C     1 
ATOM   5949  O O     . TYR B 2 744  ? 155.284 159.281 170.117 1.00 44.73  ? 741  TYR A O     1 
ATOM   5950  C CB    . TYR B 2 744  ? 157.413 157.401 170.896 1.00 44.73  ? 741  TYR A CB    1 
ATOM   5951  C CG    . TYR B 2 744  ? 158.428 156.577 171.650 1.00 44.73  ? 741  TYR A CG    1 
ATOM   5952  C CD1   . TYR B 2 744  ? 159.299 157.167 172.554 1.00 44.73  ? 741  TYR A CD1   1 
ATOM   5953  C CD2   . TYR B 2 744  ? 158.529 155.210 171.443 1.00 44.73  ? 741  TYR A CD2   1 
ATOM   5954  C CE1   . TYR B 2 744  ? 160.231 156.417 173.241 1.00 44.73  ? 741  TYR A CE1   1 
ATOM   5955  C CE2   . TYR B 2 744  ? 159.459 154.453 172.122 1.00 44.73  ? 741  TYR A CE2   1 
ATOM   5956  C CZ    . TYR B 2 744  ? 160.308 155.060 173.019 1.00 44.73  ? 741  TYR A CZ    1 
ATOM   5957  O OH    . TYR B 2 744  ? 161.235 154.307 173.701 1.00 44.73  ? 741  TYR A OH    1 
ATOM   5958  N N     . LEU B 2 745  ? 156.946 160.805 170.069 1.00 44.73  ? 742  LEU A N     1 
ATOM   5959  C CA    . LEU B 2 745  ? 156.236 161.729 169.197 1.00 44.73  ? 742  LEU A CA    1 
ATOM   5960  C C     . LEU B 2 745  ? 156.620 161.474 167.746 1.00 44.73  ? 742  LEU A C     1 
ATOM   5961  O O     . LEU B 2 745  ? 157.806 161.427 167.409 1.00 44.73  ? 742  LEU A O     1 
ATOM   5962  C CB    . LEU B 2 745  ? 156.548 163.176 169.576 1.00 44.73  ? 742  LEU A CB    1 
ATOM   5963  C CG    . LEU B 2 745  ? 155.500 163.905 170.414 1.00 44.73  ? 742  LEU A CG    1 
ATOM   5964  C CD1   . LEU B 2 745  ? 155.920 165.346 170.635 1.00 44.73  ? 742  LEU A CD1   1 
ATOM   5965  C CD2   . LEU B 2 745  ? 154.145 163.841 169.742 1.00 44.73  ? 742  LEU A CD2   1 
ATOM   5966  N N     . PHE B 2 746  ? 155.612 161.312 166.892 1.00 44.73  ? 743  PHE A N     1 
ATOM   5967  C CA    . PHE B 2 746  ? 155.812 161.071 165.467 1.00 44.73  ? 743  PHE A CA    1 
ATOM   5968  C C     . PHE B 2 746  ? 154.913 162.021 164.690 1.00 44.73  ? 743  PHE A C     1 
ATOM   5969  O O     . PHE B 2 746  ? 153.685 161.933 164.787 1.00 44.73  ? 743  PHE A O     1 
ATOM   5970  C CB    . PHE B 2 746  ? 155.502 159.619 165.106 1.00 44.73  ? 743  PHE A CB    1 
ATOM   5971  C CG    . PHE B 2 746  ? 156.589 158.655 165.470 1.00 44.73  ? 743  PHE A CG    1 
ATOM   5972  C CD1   . PHE B 2 746  ? 157.829 158.732 164.865 1.00 44.73  ? 743  PHE A CD1   1 
ATOM   5973  C CD2   . PHE B 2 746  ? 156.369 157.668 166.409 1.00 44.73  ? 743  PHE A CD2   1 
ATOM   5974  C CE1   . PHE B 2 746  ? 158.831 157.844 165.194 1.00 44.73  ? 743  PHE A CE1   1 
ATOM   5975  C CE2   . PHE B 2 746  ? 157.365 156.778 166.742 1.00 44.73  ? 743  PHE A CE2   1 
ATOM   5976  C CZ    . PHE B 2 746  ? 158.596 156.866 166.136 1.00 44.73  ? 743  PHE A CZ    1 
ATOM   5977  N N     . GLN B 2 747  ? 155.517 162.919 163.917 1.00 44.73  ? 744  GLN A N     1 
ATOM   5978  C CA    . GLN B 2 747  ? 154.733 163.827 163.093 1.00 44.73  ? 744  GLN A CA    1 
ATOM   5979  C C     . GLN B 2 747  ? 154.234 163.107 161.847 1.00 44.73  ? 744  GLN A C     1 
ATOM   5980  O O     . GLN B 2 747  ? 154.968 162.332 161.227 1.00 44.73  ? 744  GLN A O     1 
ATOM   5981  C CB    . GLN B 2 747  ? 155.561 165.049 162.701 1.00 44.73  ? 744  GLN A CB    1 
ATOM   5982  C CG    . GLN B 2 747  ? 154.778 166.083 161.909 1.00 44.73  ? 744  GLN A CG    1 
ATOM   5983  C CD    . GLN B 2 747  ? 155.669 167.054 161.166 1.00 44.73  ? 744  GLN A CD    1 
ATOM   5984  O OE1   . GLN B 2 747  ? 156.856 167.180 161.465 1.00 44.73  ? 744  GLN A OE1   1 
ATOM   5985  N NE2   . GLN B 2 747  ? 155.100 167.747 160.189 1.00 44.73  ? 744  GLN A NE2   1 
ATOM   5986  N N     . ILE B 2 748  ? 152.986 163.365 161.483 1.00 44.73  ? 745  ILE A N     1 
ATOM   5987  C CA    . ILE B 2 748  ? 152.383 162.791 160.288 1.00 44.73  ? 745  ILE A CA    1 
ATOM   5988  C C     . ILE B 2 748  ? 152.712 163.691 159.104 1.00 44.73  ? 745  ILE A C     1 
ATOM   5989  O O     . ILE B 2 748  ? 152.456 164.900 159.142 1.00 44.73  ? 745  ILE A O     1 
ATOM   5990  C CB    . ILE B 2 748  ? 150.866 162.630 160.468 1.00 44.73  ? 745  ILE A CB    1 
ATOM   5991  C CG1   . ILE B 2 748  ? 150.570 161.379 161.297 1.00 44.73  ? 745  ILE A CG1   1 
ATOM   5992  C CG2   . ILE B 2 748  ? 150.165 162.567 159.122 1.00 44.73  ? 745  ILE A CG2   1 
ATOM   5993  C CD1   . ILE B 2 748  ? 149.176 161.340 161.867 1.00 44.73  ? 745  ILE A CD1   1 
ATOM   5994  N N     . TYR B 2 749  ? 153.279 163.104 158.051 1.00 44.73  ? 746  TYR A N     1 
ATOM   5995  C CA    . TYR B 2 749  ? 153.853 163.870 156.952 1.00 44.73  ? 746  TYR A CA    1 
ATOM   5996  C C     . TYR B 2 749  ? 153.539 163.184 155.631 1.00 44.73  ? 746  TYR A C     1 
ATOM   5997  O O     . TYR B 2 749  ? 153.906 162.023 155.434 1.00 44.73  ? 746  TYR A O     1 
ATOM   5998  C CB    . TYR B 2 749  ? 155.368 164.006 157.145 1.00 44.73  ? 746  TYR A CB    1 
ATOM   5999  C CG    . TYR B 2 749  ? 156.057 165.032 156.273 1.00 44.73  ? 746  TYR A CG    1 
ATOM   6000  C CD1   . TYR B 2 749  ? 156.197 164.838 154.907 1.00 44.73  ? 746  TYR A CD1   1 
ATOM   6001  C CD2   . TYR B 2 749  ? 156.580 166.192 156.824 1.00 44.73  ? 746  TYR A CD2   1 
ATOM   6002  C CE1   . TYR B 2 749  ? 156.834 165.770 154.117 1.00 44.73  ? 746  TYR A CE1   1 
ATOM   6003  C CE2   . TYR B 2 749  ? 157.217 167.129 156.043 1.00 44.73  ? 746  TYR A CE2   1 
ATOM   6004  C CZ    . TYR B 2 749  ? 157.342 166.914 154.691 1.00 44.73  ? 746  TYR A CZ    1 
ATOM   6005  O OH    . TYR B 2 749  ? 157.978 167.847 153.908 1.00 44.73  ? 746  TYR A OH    1 
ATOM   6006  N N     . ASN B 2 750  ? 152.862 163.900 154.731 1.00 44.73  ? 747  ASN A N     1 
ATOM   6007  C CA    . ASN B 2 750  ? 152.555 163.381 153.400 1.00 44.73  ? 747  ASN A CA    1 
ATOM   6008  C C     . ASN B 2 750  ? 152.730 164.462 152.338 1.00 44.73  ? 747  ASN A C     1 
ATOM   6009  O O     . ASN B 2 750  ? 151.937 164.562 151.396 1.00 44.73  ? 747  ASN A O     1 
ATOM   6010  C CB    . ASN B 2 750  ? 151.146 162.788 153.348 1.00 44.73  ? 747  ASN A CB    1 
ATOM   6011  C CG    . ASN B 2 750  ? 150.066 163.810 153.641 1.00 44.73  ? 747  ASN A CG    1 
ATOM   6012  O OD1   . ASN B 2 750  ? 150.351 164.959 153.976 1.00 44.73  ? 747  ASN A OD1   1 
ATOM   6013  N ND2   . ASN B 2 750  ? 148.812 163.393 153.514 1.00 44.73  ? 747  ASN A ND2   1 
ATOM   6014  N N     . LYS B 2 751  ? 153.754 165.304 152.500 1.00 44.73  ? 748  LYS A N     1 
ATOM   6015  C CA    . LYS B 2 751  ? 154.177 166.297 151.512 1.00 44.73  ? 748  LYS A CA    1 
ATOM   6016  C C     . LYS B 2 751  ? 153.177 167.442 151.393 1.00 44.73  ? 748  LYS A C     1 
ATOM   6017  O O     . LYS B 2 751  ? 153.455 168.452 150.738 1.00 44.73  ? 748  LYS A O     1 
ATOM   6018  C CB    . LYS B 2 751  ? 154.405 165.645 150.142 1.00 30.68  ? 748  LYS A CB    1 
ATOM   6019  C CG    . LYS B 2 751  ? 155.130 166.514 149.126 1.00 30.68  ? 748  LYS A CG    1 
ATOM   6020  C CD    . LYS B 2 751  ? 155.015 165.935 147.728 1.00 30.68  ? 748  LYS A CD    1 
ATOM   6021  C CE    . LYS B 2 751  ? 153.568 165.669 147.354 1.00 30.68  ? 748  LYS A CE    1 
ATOM   6022  N NZ    . LYS B 2 751  ? 153.460 164.755 146.186 1.00 30.68  ? 748  LYS A NZ    1 
ATOM   6023  N N     . ASP B 2 752  ? 152.024 167.314 152.039 1.00 44.73  ? 749  ASP A N     1 
ATOM   6024  C CA    . ASP B 2 752  ? 151.063 168.402 152.111 1.00 44.73  ? 749  ASP A CA    1 
ATOM   6025  C C     . ASP B 2 752  ? 151.242 169.242 153.364 1.00 44.73  ? 749  ASP A C     1 
ATOM   6026  O O     . ASP B 2 752  ? 150.520 170.226 153.549 1.00 44.73  ? 749  ASP A O     1 
ATOM   6027  C CB    . ASP B 2 752  ? 149.636 167.855 152.039 1.00 44.73  ? 749  ASP A CB    1 
ATOM   6028  C CG    . ASP B 2 752  ? 149.282 167.347 150.658 1.00 44.73  ? 749  ASP A CG    1 
ATOM   6029  O OD1   . ASP B 2 752  ? 149.426 168.121 149.689 1.00 44.73  ? 749  ASP A OD1   1 
ATOM   6030  O OD2   . ASP B 2 752  ? 148.861 166.178 150.539 1.00 44.73  ? 749  ASP A OD2   1 
ATOM   6031  N N     . PHE B 2 753  ? 152.188 168.871 154.225 1.00 44.73  ? 750  PHE A N     1 
ATOM   6032  C CA    . PHE B 2 753  ? 152.555 169.661 155.391 1.00 44.73  ? 750  PHE A CA    1 
ATOM   6033  C C     . PHE B 2 753  ? 153.961 170.230 155.268 1.00 44.73  ? 750  PHE A C     1 
ATOM   6034  O O     . PHE B 2 753  ? 154.520 170.703 156.266 1.00 44.73  ? 750  PHE A O     1 
ATOM   6035  C CB    . PHE B 2 753  ? 152.428 168.818 156.661 1.00 44.73  ? 750  PHE A CB    1 
ATOM   6036  C CG    . PHE B 2 753  ? 151.075 168.193 156.837 1.00 44.73  ? 750  PHE A CG    1 
ATOM   6037  C CD1   . PHE B 2 753  ? 150.008 168.942 157.299 1.00 44.73  ? 750  PHE A CD1   1 
ATOM   6038  C CD2   . PHE B 2 753  ? 150.867 166.861 156.533 1.00 44.73  ? 750  PHE A CD2   1 
ATOM   6039  C CE1   . PHE B 2 753  ? 148.762 168.373 157.459 1.00 44.73  ? 750  PHE A CE1   1 
ATOM   6040  C CE2   . PHE B 2 753  ? 149.624 166.287 156.693 1.00 44.73  ? 750  PHE A CE2   1 
ATOM   6041  C CZ    . PHE B 2 753  ? 148.571 167.043 157.156 1.00 44.73  ? 750  PHE A CZ    1 
ATOM   6042  N N     . ALA B 2 754  ? 154.545 170.196 154.074 1.00 44.73  ? 751  ALA A N     1 
ATOM   6043  C CA    . ALA B 2 754  ? 155.885 170.707 153.848 1.00 44.73  ? 751  ALA A CA    1 
ATOM   6044  C C     . ALA B 2 754  ? 155.898 172.231 153.896 1.00 44.73  ? 751  ALA A C     1 
ATOM   6045  O O     . ALA B 2 754  ? 154.882 172.897 153.679 1.00 44.73  ? 751  ALA A O     1 
ATOM   6046  C CB    . ALA B 2 754  ? 156.421 170.223 152.501 1.00 44.73  ? 751  ALA A CB    1 
ATOM   6047  N N     . LYS B 2 755  ? 157.078 172.780 154.192 1.00 44.73  ? 752  LYS A N     1 
ATOM   6048  C CA    . LYS B 2 755  ? 157.222 174.230 154.264 1.00 44.73  ? 752  LYS A CA    1 
ATOM   6049  C C     . LYS B 2 755  ? 156.973 174.878 152.909 1.00 44.73  ? 752  LYS A C     1 
ATOM   6050  O O     . LYS B 2 755  ? 156.298 175.910 152.820 1.00 44.73  ? 752  LYS A O     1 
ATOM   6051  C CB    . LYS B 2 755  ? 158.612 174.591 154.786 1.00 40.72  ? 752  LYS A CB    1 
ATOM   6052  C CG    . LYS B 2 755  ? 158.779 174.408 156.286 1.00 40.72  ? 752  LYS A CG    1 
ATOM   6053  C CD    . LYS B 2 755  ? 159.891 175.289 156.834 1.00 40.72  ? 752  LYS A CD    1 
ATOM   6054  C CE    . LYS B 2 755  ? 161.157 175.165 156.001 1.00 40.72  ? 752  LYS A CE    1 
ATOM   6055  N NZ    . LYS B 2 755  ? 161.753 173.804 156.102 1.00 40.72  ? 752  LYS A NZ    1 
ATOM   6056  N N     . GLY B 2 756  ? 157.505 174.287 151.844 1.00 44.73  ? 753  GLY A N     1 
ATOM   6057  C CA    . GLY B 2 756  ? 157.324 174.809 150.507 1.00 44.73  ? 753  GLY A CA    1 
ATOM   6058  C C     . GLY B 2 756  ? 156.069 174.360 149.802 1.00 44.73  ? 753  GLY A C     1 
ATOM   6059  O O     . GLY B 2 756  ? 155.885 174.675 148.623 1.00 44.73  ? 753  GLY A O     1 
ATOM   6060  N N     . HIS B 2 757  ? 155.201 173.624 150.490 1.00 44.73  ? 754  HIS A N     1 
ATOM   6061  C CA    . HIS B 2 757  ? 153.982 173.122 149.872 1.00 44.73  ? 754  HIS A CA    1 
ATOM   6062  C C     . HIS B 2 757  ? 153.064 174.266 149.460 1.00 44.73  ? 754  HIS A C     1 
ATOM   6063  O O     . HIS B 2 757  ? 152.841 175.212 150.220 1.00 44.73  ? 754  HIS A O     1 
ATOM   6064  C CB    . HIS B 2 757  ? 153.254 172.187 150.836 1.00 44.73  ? 754  HIS A CB    1 
ATOM   6065  C CG    . HIS B 2 757  ? 151.797 172.025 150.536 1.00 44.73  ? 754  HIS A CG    1 
ATOM   6066  N ND1   . HIS B 2 757  ? 150.823 172.781 151.153 1.00 44.73  ? 754  HIS A ND1   1 
ATOM   6067  C CD2   . HIS B 2 757  ? 151.148 171.195 149.687 1.00 44.73  ? 754  HIS A CD2   1 
ATOM   6068  C CE1   . HIS B 2 757  ? 149.637 172.423 150.696 1.00 44.73  ? 754  HIS A CE1   1 
ATOM   6069  N NE2   . HIS B 2 757  ? 149.806 171.463 149.805 1.00 44.73  ? 754  HIS A NE2   1 
ATOM   6070  N N     . HIS B 2 758  ? 152.530 174.169 148.245 1.00 44.73  ? 755  HIS A N     1 
ATOM   6071  C CA    . HIS B 2 758  ? 151.539 175.119 147.757 1.00 44.73  ? 755  HIS A CA    1 
ATOM   6072  C C     . HIS B 2 758  ? 150.766 174.461 146.627 1.00 44.73  ? 755  HIS A C     1 
ATOM   6073  O O     . HIS B 2 758  ? 151.367 173.911 145.700 1.00 44.73  ? 755  HIS A O     1 
ATOM   6074  C CB    . HIS B 2 758  ? 152.192 176.420 147.280 1.00 44.73  ? 755  HIS A CB    1 
ATOM   6075  C CG    . HIS B 2 758  ? 153.026 176.262 146.049 1.00 44.73  ? 755  HIS A CG    1 
ATOM   6076  N ND1   . HIS B 2 758  ? 152.552 176.552 144.788 1.00 44.73  ? 755  HIS A ND1   1 
ATOM   6077  C CD2   . HIS B 2 758  ? 154.305 175.850 145.885 1.00 44.73  ? 755  HIS A CD2   1 
ATOM   6078  C CE1   . HIS B 2 758  ? 153.501 176.320 143.900 1.00 44.73  ? 755  HIS A CE1   1 
ATOM   6079  N NE2   . HIS B 2 758  ? 154.575 175.894 144.539 1.00 44.73  ? 755  HIS A NE2   1 
ATOM   6080  N N     . GLY B 2 759  ? 149.446 174.517 146.704 1.00 44.73  ? 756  GLY A N     1 
ATOM   6081  C CA    . GLY B 2 759  ? 148.584 173.861 145.743 1.00 44.73  ? 756  GLY A CA    1 
ATOM   6082  C C     . GLY B 2 759  ? 147.606 172.916 146.417 1.00 44.73  ? 756  GLY A C     1 
ATOM   6083  O O     . GLY B 2 759  ? 147.682 172.633 147.611 1.00 44.73  ? 756  GLY A O     1 
ATOM   6084  N N     . LYS B 2 760  ? 146.668 172.438 145.609 1.00 44.73  ? 757  LYS A N     1 
ATOM   6085  C CA    . LYS B 2 760  ? 145.634 171.559 146.129 1.00 44.73  ? 757  LYS A CA    1 
ATOM   6086  C C     . LYS B 2 760  ? 146.254 170.245 146.604 1.00 44.73  ? 757  LYS A C     1 
ATOM   6087  O O     . LYS B 2 760  ? 147.119 169.681 145.923 1.00 44.73  ? 757  LYS A O     1 
ATOM   6088  C CB    . LYS B 2 760  ? 144.560 171.311 145.068 1.00 44.73  ? 757  LYS A CB    1 
ATOM   6089  C CG    . LYS B 2 760  ? 145.063 170.701 143.777 1.00 44.73  ? 757  LYS A CG    1 
ATOM   6090  C CD    . LYS B 2 760  ? 143.931 170.562 142.777 1.00 44.73  ? 757  LYS A CD    1 
ATOM   6091  C CE    . LYS B 2 760  ? 143.515 171.911 142.221 1.00 44.73  ? 757  LYS A CE    1 
ATOM   6092  N NZ    . LYS B 2 760  ? 144.587 172.521 141.389 1.00 44.73  ? 757  LYS A NZ    1 
ATOM   6093  N N     . PRO B 2 761  ? 145.858 169.748 147.768 1.00 44.73  ? 758  PRO A N     1 
ATOM   6094  C CA    . PRO B 2 761  ? 146.519 168.584 148.363 1.00 44.73  ? 758  PRO A CA    1 
ATOM   6095  C C     . PRO B 2 761  ? 145.970 167.277 147.804 1.00 44.73  ? 758  PRO A C     1 
ATOM   6096  O O     . PRO B 2 761  ? 145.129 167.252 146.908 1.00 44.73  ? 758  PRO A O     1 
ATOM   6097  C CB    . PRO B 2 761  ? 146.193 168.734 149.849 1.00 44.73  ? 758  PRO A CB    1 
ATOM   6098  C CG    . PRO B 2 761  ? 144.870 169.414 149.860 1.00 44.73  ? 758  PRO A CG    1 
ATOM   6099  C CD    . PRO B 2 761  ? 144.836 170.322 148.660 1.00 44.73  ? 758  PRO A CD    1 
ATOM   6100  N N     . ASN B 2 762  ? 146.472 166.177 148.358 1.00 44.73  ? 759  ASN A N     1 
ATOM   6101  C CA    . ASN B 2 762  ? 146.010 164.855 147.971 1.00 44.73  ? 759  ASN A CA    1 
ATOM   6102  C C     . ASN B 2 762  ? 144.634 164.569 148.564 1.00 44.73  ? 759  ASN A C     1 
ATOM   6103  O O     . ASN B 2 762  ? 144.188 165.214 149.517 1.00 44.73  ? 759  ASN A O     1 
ATOM   6104  C CB    . ASN B 2 762  ? 146.997 163.780 148.427 1.00 44.73  ? 759  ASN A CB    1 
ATOM   6105  C CG    . ASN B 2 762  ? 148.345 163.906 147.758 1.00 44.73  ? 759  ASN A CG    1 
ATOM   6106  O OD1   . ASN B 2 762  ? 148.476 164.541 146.712 1.00 44.73  ? 759  ASN A OD1   1 
ATOM   6107  N ND2   . ASN B 2 762  ? 149.358 163.293 148.354 1.00 44.73  ? 759  ASN A ND2   1 
ATOM   6108  N N     . LEU B 2 763  ? 143.956 163.581 147.977 1.00 44.73  ? 760  LEU A N     1 
ATOM   6109  C CA    . LEU B 2 763  ? 142.657 163.167 148.494 1.00 44.73  ? 760  LEU A CA    1 
ATOM   6110  C C     . LEU B 2 763  ? 142.785 162.559 149.885 1.00 44.73  ? 760  LEU A C     1 
ATOM   6111  O O     . LEU B 2 763  ? 141.938 162.793 150.754 1.00 44.73  ? 760  LEU A O     1 
ATOM   6112  C CB    . LEU B 2 763  ? 142.001 162.179 147.533 1.00 44.73  ? 760  LEU A CB    1 
ATOM   6113  C CG    . LEU B 2 763  ? 141.044 162.790 146.515 1.00 44.73  ? 760  LEU A CG    1 
ATOM   6114  C CD1   . LEU B 2 763  ? 140.424 161.701 145.661 1.00 44.73  ? 760  LEU A CD1   1 
ATOM   6115  C CD2   . LEU B 2 763  ? 139.971 163.602 147.214 1.00 44.73  ? 760  LEU A CD2   1 
ATOM   6116  N N     . HIS B 2 764  ? 143.835 161.767 150.110 1.00 44.73  ? 761  HIS A N     1 
ATOM   6117  C CA    . HIS B 2 764  ? 144.050 161.175 151.426 1.00 44.73  ? 761  HIS A CA    1 
ATOM   6118  C C     . HIS B 2 764  ? 144.328 162.244 152.474 1.00 44.73  ? 761  HIS A C     1 
ATOM   6119  O O     . HIS B 2 764  ? 143.917 162.107 153.632 1.00 44.73  ? 761  HIS A O     1 
ATOM   6120  C CB    . HIS B 2 764  ? 145.194 160.165 151.361 1.00 44.73  ? 761  HIS A CB    1 
ATOM   6121  C CG    . HIS B 2 764  ? 144.805 158.855 150.751 1.00 44.73  ? 761  HIS A CG    1 
ATOM   6122  N ND1   . HIS B 2 764  ? 144.346 158.745 149.457 1.00 44.73  ? 761  HIS A ND1   1 
ATOM   6123  C CD2   . HIS B 2 764  ? 144.813 157.599 151.256 1.00 44.73  ? 761  HIS A CD2   1 
ATOM   6124  C CE1   . HIS B 2 764  ? 144.082 157.478 149.192 1.00 44.73  ? 761  HIS A CE1   1 
ATOM   6125  N NE2   . HIS B 2 764  ? 144.358 156.762 150.267 1.00 44.73  ? 761  HIS A NE2   1 
ATOM   6126  N N     . THR B 2 765  ? 145.032 163.311 152.090 1.00 44.73  ? 762  THR A N     1 
ATOM   6127  C CA    . THR B 2 765  ? 145.237 164.425 153.009 1.00 44.73  ? 762  THR A CA    1 
ATOM   6128  C C     . THR B 2 765  ? 143.915 165.100 153.353 1.00 44.73  ? 762  THR A C     1 
ATOM   6129  O O     . THR B 2 765  ? 143.679 165.465 154.510 1.00 44.73  ? 762  THR A O     1 
ATOM   6130  C CB    . THR B 2 765  ? 146.212 165.434 152.405 1.00 44.73  ? 762  THR A CB    1 
ATOM   6131  O OG1   . THR B 2 765  ? 147.478 164.802 152.184 1.00 44.73  ? 762  THR A OG1   1 
ATOM   6132  C CG2   . THR B 2 765  ? 146.403 166.616 153.339 1.00 44.73  ? 762  THR A CG2   1 
ATOM   6133  N N     . LEU B 2 766  ? 143.039 165.268 152.360 1.00 44.73  ? 763  LEU A N     1 
ATOM   6134  C CA    . LEU B 2 766  ? 141.732 165.862 152.619 1.00 44.73  ? 763  LEU A CA    1 
ATOM   6135  C C     . LEU B 2 766  ? 140.901 164.984 153.545 1.00 44.73  ? 763  LEU A C     1 
ATOM   6136  O O     . LEU B 2 766  ? 140.170 165.494 154.402 1.00 44.73  ? 763  LEU A O     1 
ATOM   6137  C CB    . LEU B 2 766  ? 140.993 166.103 151.306 1.00 44.73  ? 763  LEU A CB    1 
ATOM   6138  C CG    . LEU B 2 766  ? 141.504 167.259 150.448 1.00 44.73  ? 763  LEU A CG    1 
ATOM   6139  C CD1   . LEU B 2 766  ? 140.641 167.404 149.214 1.00 44.73  ? 763  LEU A CD1   1 
ATOM   6140  C CD2   . LEU B 2 766  ? 141.525 168.551 151.247 1.00 44.73  ? 763  LEU A CD2   1 
ATOM   6141  N N     . TYR B 2 767  ? 140.988 163.663 153.379 1.00 44.73  ? 764  TYR A N     1 
ATOM   6142  C CA    . TYR B 2 767  ? 140.305 162.758 154.297 1.00 44.73  ? 764  TYR A CA    1 
ATOM   6143  C C     . TYR B 2 767  ? 140.840 162.914 155.713 1.00 44.73  ? 764  TYR A C     1 
ATOM   6144  O O     . TYR B 2 767  ? 140.071 162.908 156.681 1.00 44.73  ? 764  TYR A O     1 
ATOM   6145  C CB    . TYR B 2 767  ? 140.458 161.313 153.823 1.00 44.73  ? 764  TYR A CB    1 
ATOM   6146  C CG    . TYR B 2 767  ? 139.797 161.020 152.495 1.00 44.73  ? 764  TYR A CG    1 
ATOM   6147  C CD1   . TYR B 2 767  ? 138.764 161.813 152.021 1.00 44.73  ? 764  TYR A CD1   1 
ATOM   6148  C CD2   . TYR B 2 767  ? 140.205 159.945 151.719 1.00 44.73  ? 764  TYR A CD2   1 
ATOM   6149  C CE1   . TYR B 2 767  ? 138.157 161.547 150.811 1.00 44.73  ? 764  TYR A CE1   1 
ATOM   6150  C CE2   . TYR B 2 767  ? 139.604 159.671 150.507 1.00 44.73  ? 764  TYR A CE2   1 
ATOM   6151  C CZ    . TYR B 2 767  ? 138.581 160.475 150.058 1.00 44.73  ? 764  TYR A CZ    1 
ATOM   6152  O OH    . TYR B 2 767  ? 137.978 160.206 148.851 1.00 44.73  ? 764  TYR A OH    1 
ATOM   6153  N N     . TRP B 2 768  ? 142.160 163.050 155.854 1.00 44.73  ? 765  TRP A N     1 
ATOM   6154  C CA    . TRP B 2 768  ? 142.745 163.291 157.168 1.00 44.73  ? 765  TRP A CA    1 
ATOM   6155  C C     . TRP B 2 768  ? 142.359 164.665 157.699 1.00 44.73  ? 765  TRP A C     1 
ATOM   6156  O O     . TRP B 2 768  ? 141.979 164.803 158.868 1.00 44.73  ? 765  TRP A O     1 
ATOM   6157  C CB    . TRP B 2 768  ? 144.265 163.153 157.092 1.00 44.73  ? 765  TRP A CB    1 
ATOM   6158  C CG    . TRP B 2 768  ? 144.928 163.055 158.424 1.00 44.73  ? 765  TRP A CG    1 
ATOM   6159  C CD1   . TRP B 2 768  ? 145.799 163.946 158.974 1.00 44.73  ? 765  TRP A CD1   1 
ATOM   6160  C CD2   . TRP B 2 768  ? 144.776 162.000 159.378 1.00 44.73  ? 765  TRP A CD2   1 
ATOM   6161  N NE1   . TRP B 2 768  ? 146.200 163.512 160.213 1.00 44.73  ? 765  TRP A NE1   1 
ATOM   6162  C CE2   . TRP B 2 768  ? 145.585 162.318 160.484 1.00 44.73  ? 765  TRP A CE2   1 
ATOM   6163  C CE3   . TRP B 2 768  ? 144.034 160.817 159.404 1.00 44.73  ? 765  TRP A CE3   1 
ATOM   6164  C CZ2   . TRP B 2 768  ? 145.673 161.498 161.602 1.00 44.73  ? 765  TRP A CZ2   1 
ATOM   6165  C CZ3   . TRP B 2 768  ? 144.122 160.005 160.515 1.00 44.73  ? 765  TRP A CZ3   1 
ATOM   6166  C CH2   . TRP B 2 768  ? 144.936 160.348 161.598 1.00 44.73  ? 765  TRP A CH2   1 
ATOM   6167  N N     . THR B 2 769  ? 142.457 165.696 156.857 1.00 44.73  ? 766  THR A N     1 
ATOM   6168  C CA    . THR B 2 769  ? 142.072 167.039 157.278 1.00 44.73  ? 766  THR A CA    1 
ATOM   6169  C C     . THR B 2 769  ? 140.581 167.117 157.578 1.00 44.73  ? 766  THR A C     1 
ATOM   6170  O O     . THR B 2 769  ? 140.172 167.733 158.569 1.00 44.73  ? 766  THR A O     1 
ATOM   6171  C CB    . THR B 2 769  ? 142.458 168.056 156.205 1.00 44.73  ? 766  THR A CB    1 
ATOM   6172  O OG1   . THR B 2 769  ? 143.879 168.046 156.026 1.00 44.73  ? 766  THR A OG1   1 
ATOM   6173  C CG2   . THR B 2 769  ? 142.016 169.452 156.607 1.00 44.73  ? 766  THR A CG2   1 
ATOM   6174  N N     . GLY B 2 770  ? 139.752 166.490 156.741 1.00 44.73  ? 767  GLY A N     1 
ATOM   6175  C CA    . GLY B 2 770  ? 138.316 166.522 156.952 1.00 44.73  ? 767  GLY A CA    1 
ATOM   6176  C C     . GLY B 2 770  ? 137.848 165.704 158.136 1.00 44.73  ? 767  GLY A C     1 
ATOM   6177  O O     . GLY B 2 770  ? 136.766 165.970 158.668 1.00 44.73  ? 767  GLY A O     1 
ATOM   6178  N N     . LEU B 2 771  ? 138.635 164.712 158.555 1.00 44.73  ? 768  LEU A N     1 
ATOM   6179  C CA    . LEU B 2 771  ? 138.263 163.915 159.718 1.00 44.73  ? 768  LEU A CA    1 
ATOM   6180  C C     . LEU B 2 771  ? 138.286 164.757 160.987 1.00 44.73  ? 768  LEU A C     1 
ATOM   6181  O O     . LEU B 2 771  ? 137.422 164.606 161.858 1.00 44.73  ? 768  LEU A O     1 
ATOM   6182  C CB    . LEU B 2 771  ? 139.197 162.711 159.845 1.00 44.73  ? 768  LEU A CB    1 
ATOM   6183  C CG    . LEU B 2 771  ? 138.862 161.609 160.855 1.00 44.73  ? 768  LEU A CG    1 
ATOM   6184  C CD1   . LEU B 2 771  ? 139.419 160.286 160.372 1.00 44.73  ? 768  LEU A CD1   1 
ATOM   6185  C CD2   . LEU B 2 771  ? 139.402 161.920 162.241 1.00 44.73  ? 768  LEU A CD2   1 
ATOM   6186  N N     . PHE B 2 772  ? 139.269 165.647 161.109 1.00 44.73  ? 769  PHE A N     1 
ATOM   6187  C CA    . PHE B 2 772  ? 139.436 166.480 162.290 1.00 44.73  ? 769  PHE A CA    1 
ATOM   6188  C C     . PHE B 2 772  ? 138.859 167.878 162.115 1.00 44.73  ? 769  PHE A C     1 
ATOM   6189  O O     . PHE B 2 772  ? 139.114 168.750 162.950 1.00 44.73  ? 769  PHE A O     1 
ATOM   6190  C CB    . PHE B 2 772  ? 140.915 166.566 162.666 1.00 44.73  ? 769  PHE A CB    1 
ATOM   6191  C CG    . PHE B 2 772  ? 141.540 165.236 162.960 1.00 44.73  ? 769  PHE A CG    1 
ATOM   6192  C CD1   . PHE B 2 772  ? 141.237 164.560 164.128 1.00 44.73  ? 769  PHE A CD1   1 
ATOM   6193  C CD2   . PHE B 2 772  ? 142.419 164.656 162.067 1.00 44.73  ? 769  PHE A CD2   1 
ATOM   6194  C CE1   . PHE B 2 772  ? 141.808 163.336 164.404 1.00 44.73  ? 769  PHE A CE1   1 
ATOM   6195  C CE2   . PHE B 2 772  ? 142.991 163.431 162.337 1.00 44.73  ? 769  PHE A CE2   1 
ATOM   6196  C CZ    . PHE B 2 772  ? 142.685 162.770 163.507 1.00 44.73  ? 769  PHE A CZ    1 
ATOM   6197  N N     . SER B 2 773  ? 138.098 168.112 161.050 1.00 44.73  ? 770  SER A N     1 
ATOM   6198  C CA    . SER B 2 773  ? 137.420 169.386 160.893 1.00 44.73  ? 770  SER A CA    1 
ATOM   6199  C C     . SER B 2 773  ? 136.365 169.554 161.985 1.00 44.73  ? 770  SER A C     1 
ATOM   6200  O O     . SER B 2 773  ? 135.802 168.571 162.471 1.00 44.73  ? 770  SER A O     1 
ATOM   6201  C CB    . SER B 2 773  ? 136.765 169.479 159.518 1.00 44.73  ? 770  SER A CB    1 
ATOM   6202  O OG    . SER B 2 773  ? 137.738 169.478 158.488 1.00 44.73  ? 770  SER A OG    1 
ATOM   6203  N N     . PRO B 2 774  ? 136.092 170.793 162.401 1.00 44.73  ? 771  PRO A N     1 
ATOM   6204  C CA    . PRO B 2 774  ? 135.068 171.004 163.435 1.00 44.73  ? 771  PRO A CA    1 
ATOM   6205  C C     . PRO B 2 774  ? 133.697 170.484 163.043 1.00 44.73  ? 771  PRO A C     1 
ATOM   6206  O O     . PRO B 2 774  ? 132.924 170.085 163.923 1.00 44.73  ? 771  PRO A O     1 
ATOM   6207  C CB    . PRO B 2 774  ? 135.064 172.527 163.617 1.00 44.73  ? 771  PRO A CB    1 
ATOM   6208  C CG    . PRO B 2 774  ? 136.413 172.966 163.162 1.00 44.73  ? 771  PRO A CG    1 
ATOM   6209  C CD    . PRO B 2 774  ? 136.786 172.042 162.044 1.00 44.73  ? 771  PRO A CD    1 
ATOM   6210  N N     . GLU B 2 775  ? 133.368 170.481 161.750 1.00 44.73  ? 772  GLU A N     1 
ATOM   6211  C CA    . GLU B 2 775  ? 132.078 169.953 161.318 1.00 44.73  ? 772  GLU A CA    1 
ATOM   6212  C C     . GLU B 2 775  ? 131.975 168.456 161.583 1.00 44.73  ? 772  GLU A C     1 
ATOM   6213  O O     . GLU B 2 775  ? 130.925 167.966 162.015 1.00 44.73  ? 772  GLU A O     1 
ATOM   6214  C CB    . GLU B 2 775  ? 131.859 170.249 159.835 1.00 44.73  ? 772  GLU A CB    1 
ATOM   6215  C CG    . GLU B 2 775  ? 131.738 171.727 159.509 1.00 44.73  ? 772  GLU A CG    1 
ATOM   6216  C CD    . GLU B 2 775  ? 133.072 172.358 159.166 1.00 44.73  ? 772  GLU A CD    1 
ATOM   6217  O OE1   . GLU B 2 775  ? 133.962 171.637 158.667 1.00 44.73  ? 772  GLU A OE1   1 
ATOM   6218  O OE2   . GLU B 2 775  ? 133.233 173.575 159.395 1.00 44.73  ? 772  GLU A OE2   1 
ATOM   6219  N N     . ASN B 2 776  ? 133.052 167.711 161.326 1.00 44.73  ? 773  ASN A N     1 
ATOM   6220  C CA    . ASN B 2 776  ? 133.003 166.262 161.495 1.00 44.73  ? 773  ASN A CA    1 
ATOM   6221  C C     . ASN B 2 776  ? 132.940 165.872 162.966 1.00 44.73  ? 773  ASN A C     1 
ATOM   6222  O O     . ASN B 2 776  ? 132.260 164.905 163.327 1.00 44.73  ? 773  ASN A O     1 
ATOM   6223  C CB    . ASN B 2 776  ? 134.207 165.610 160.821 1.00 44.73  ? 773  ASN A CB    1 
ATOM   6224  C CG    . ASN B 2 776  ? 134.055 164.110 160.692 1.00 44.73  ? 773  ASN A CG    1 
ATOM   6225  O OD1   . ASN B 2 776  ? 132.941 163.593 160.625 1.00 44.73  ? 773  ASN A OD1   1 
ATOM   6226  N ND2   . ASN B 2 776  ? 135.174 163.402 160.664 1.00 44.73  ? 773  ASN A ND2   1 
ATOM   6227  N N     . LEU B 2 777  ? 133.655 166.597 163.828 1.00 44.73  ? 774  LEU A N     1 
ATOM   6228  C CA    . LEU B 2 777  ? 133.592 166.311 165.257 1.00 44.73  ? 774  LEU A CA    1 
ATOM   6229  C C     . LEU B 2 777  ? 132.192 166.552 165.806 1.00 44.73  ? 774  LEU A C     1 
ATOM   6230  O O     . LEU B 2 777  ? 131.698 165.771 166.628 1.00 44.73  ? 774  LEU A O     1 
ATOM   6231  C CB    . LEU B 2 777  ? 134.618 167.156 166.009 1.00 44.73  ? 774  LEU A CB    1 
ATOM   6232  C CG    . LEU B 2 777  ? 136.075 166.980 165.578 1.00 44.73  ? 774  LEU A CG    1 
ATOM   6233  C CD1   . LEU B 2 777  ? 137.009 167.713 166.524 1.00 44.73  ? 774  LEU A CD1   1 
ATOM   6234  C CD2   . LEU B 2 777  ? 136.437 165.507 165.501 1.00 44.73  ? 774  LEU A CD2   1 
ATOM   6235  N N     . ALA B 2 778  ? 131.538 167.630 165.368 1.00 44.73  ? 775  ALA A N     1 
ATOM   6236  C CA    . ALA B 2 778  ? 130.178 167.904 165.820 1.00 44.73  ? 775  ALA A CA    1 
ATOM   6237  C C     . ALA B 2 778  ? 129.189 166.890 165.259 1.00 44.73  ? 775  ALA A C     1 
ATOM   6238  O O     . ALA B 2 778  ? 128.332 166.381 165.990 1.00 44.73  ? 775  ALA A O     1 
ATOM   6239  C CB    . ALA B 2 778  ? 129.771 169.324 165.430 1.00 44.73  ? 775  ALA A CB    1 
ATOM   6240  N N     . LYS B 2 779  ? 129.289 166.584 163.967 1.00 44.73  ? 776  LYS A N     1 
ATOM   6241  C CA    . LYS B 2 779  ? 128.428 165.602 163.315 1.00 44.73  ? 776  LYS A CA    1 
ATOM   6242  C C     . LYS B 2 779  ? 129.318 164.637 162.546 1.00 44.73  ? 776  LYS A C     1 
ATOM   6243  O O     . LYS B 2 779  ? 129.969 165.030 161.574 1.00 44.73  ? 776  LYS A O     1 
ATOM   6244  C CB    . LYS B 2 779  ? 127.417 166.276 162.388 1.00 44.73  ? 776  LYS A CB    1 
ATOM   6245  C CG    . LYS B 2 779  ? 126.417 165.316 161.767 1.00 44.73  ? 776  LYS A CG    1 
ATOM   6246  C CD    . LYS B 2 779  ? 125.270 165.022 162.721 1.00 44.73  ? 776  LYS A CD    1 
ATOM   6247  C CE    . LYS B 2 779  ? 124.569 163.724 162.359 1.00 44.73  ? 776  LYS A CE    1 
ATOM   6248  N NZ    . LYS B 2 779  ? 123.493 163.936 161.352 1.00 44.73  ? 776  LYS A NZ    1 
ATOM   6249  N N     . THR B 2 780  ? 129.337 163.379 162.975 1.00 44.73  ? 777  THR A N     1 
ATOM   6250  C CA    . THR B 2 780  ? 130.300 162.422 162.449 1.00 44.73  ? 777  THR A CA    1 
ATOM   6251  C C     . THR B 2 780  ? 129.886 161.921 161.072 1.00 44.73  ? 777  THR A C     1 
ATOM   6252  O O     . THR B 2 780  ? 128.771 161.424 160.885 1.00 44.73  ? 777  THR A O     1 
ATOM   6253  C CB    . THR B 2 780  ? 130.449 161.243 163.407 1.00 44.73  ? 777  THR A CB    1 
ATOM   6254  O OG1   . THR B 2 780  ? 131.202 161.651 164.557 1.00 44.73  ? 777  THR A OG1   1 
ATOM   6255  C CG2   . THR B 2 780  ? 131.163 160.090 162.721 1.00 44.73  ? 777  THR A CG2   1 
ATOM   6256  N N     . SER B 2 781  ? 130.793 162.056 160.109 1.00 44.73  ? 778  SER A N     1 
ATOM   6257  C CA    . SER B 2 781  ? 130.675 161.392 158.818 1.00 44.73  ? 778  SER A CA    1 
ATOM   6258  C C     . SER B 2 781  ? 131.919 160.610 158.431 1.00 44.73  ? 778  SER A C     1 
ATOM   6259  O O     . SER B 2 781  ? 131.820 159.715 157.583 1.00 44.73  ? 778  SER A O     1 
ATOM   6260  C CB    . SER B 2 781  ? 130.359 162.407 157.711 1.00 44.73  ? 778  SER A CB    1 
ATOM   6261  O OG    . SER B 2 781  ? 129.170 163.121 158.000 1.00 44.73  ? 778  SER A OG    1 
ATOM   6262  N N     . ILE B 2 782  ? 133.076 160.914 159.012 1.00 44.73  ? 779  ILE A N     1 
ATOM   6263  C CA    . ILE B 2 782  ? 134.290 160.123 158.857 1.00 44.73  ? 779  ILE A CA    1 
ATOM   6264  C C     . ILE B 2 782  ? 134.683 159.619 160.237 1.00 44.73  ? 779  ILE A C     1 
ATOM   6265  O O     . ILE B 2 782  ? 134.941 160.420 161.144 1.00 44.73  ? 779  ILE A O     1 
ATOM   6266  C CB    . ILE B 2 782  ? 135.431 160.937 158.229 1.00 44.73  ? 779  ILE A CB    1 
ATOM   6267  C CG1   . ILE B 2 782  ? 134.909 161.784 157.070 1.00 44.73  ? 779  ILE A CG1   1 
ATOM   6268  C CG2   . ILE B 2 782  ? 136.542 160.015 157.761 1.00 44.73  ? 779  ILE A CG2   1 
ATOM   6269  C CD1   . ILE B 2 782  ? 135.989 162.560 156.353 1.00 44.73  ? 779  ILE A CD1   1 
ATOM   6270  N N     . LYS B 2 783  ? 134.730 158.301 160.397 1.00 44.73  ? 780  LYS A N     1 
ATOM   6271  C CA    . LYS B 2 783  ? 135.033 157.676 161.675 1.00 44.73  ? 780  LYS A CA    1 
ATOM   6272  C C     . LYS B 2 783  ? 136.453 157.132 161.662 1.00 44.73  ? 780  LYS A C     1 
ATOM   6273  O O     . LYS B 2 783  ? 136.882 156.512 160.685 1.00 44.73  ? 780  LYS A O     1 
ATOM   6274  C CB    . LYS B 2 783  ? 134.047 156.547 161.986 1.00 44.73  ? 780  LYS A CB    1 
ATOM   6275  C CG    . LYS B 2 783  ? 134.613 155.471 162.898 1.00 44.73  ? 780  LYS A CG    1 
ATOM   6276  C CD    . LYS B 2 783  ? 133.521 154.600 163.487 1.00 44.73  ? 780  LYS A CD    1 
ATOM   6277  C CE    . LYS B 2 783  ? 134.080 153.647 164.526 1.00 44.73  ? 780  LYS A CE    1 
ATOM   6278  N NZ    . LYS B 2 783  ? 135.376 153.057 164.094 1.00 44.73  ? 780  LYS A NZ    1 
ATOM   6279  N N     . LEU B 2 784  ? 137.178 157.366 162.752 1.00 44.73  ? 781  LEU A N     1 
ATOM   6280  C CA    . LEU B 2 784  ? 138.552 156.891 162.892 1.00 44.73  ? 781  LEU A CA    1 
ATOM   6281  C C     . LEU B 2 784  ? 138.509 155.467 163.431 1.00 44.73  ? 781  LEU A C     1 
ATOM   6282  O O     . LEU B 2 784  ? 138.302 155.248 164.627 1.00 44.73  ? 781  LEU A O     1 
ATOM   6283  C CB    . LEU B 2 784  ? 139.346 157.813 163.808 1.00 44.73  ? 781  LEU A CB    1 
ATOM   6284  C CG    . LEU B 2 784  ? 140.794 157.409 164.065 1.00 44.73  ? 781  LEU A CG    1 
ATOM   6285  C CD1   . LEU B 2 784  ? 141.565 157.426 162.768 1.00 44.73  ? 781  LEU A CD1   1 
ATOM   6286  C CD2   . LEU B 2 784  ? 141.430 158.339 165.079 1.00 44.73  ? 781  LEU A CD2   1 
ATOM   6287  N N     . ASN B 2 785  ? 138.700 154.493 162.546 1.00 44.73  ? 782  ASN A N     1 
ATOM   6288  C CA    . ASN B 2 785  ? 138.669 153.098 162.952 1.00 44.73  ? 782  ASN A CA    1 
ATOM   6289  C C     . ASN B 2 785  ? 139.944 152.723 163.702 1.00 44.73  ? 782  ASN A C     1 
ATOM   6290  O O     . ASN B 2 785  ? 141.000 153.340 163.543 1.00 44.73  ? 782  ASN A O     1 
ATOM   6291  C CB    . ASN B 2 785  ? 138.494 152.187 161.738 1.00 44.73  ? 782  ASN A CB    1 
ATOM   6292  C CG    . ASN B 2 785  ? 137.194 152.436 161.006 1.00 44.73  ? 782  ASN A CG    1 
ATOM   6293  O OD1   . ASN B 2 785  ? 136.323 153.154 161.494 1.00 44.73  ? 782  ASN A OD1   1 
ATOM   6294  N ND2   . ASN B 2 785  ? 137.054 151.840 159.828 1.00 44.73  ? 782  ASN A ND2   1 
ATOM   6295  N N     . GLY B 2 786  ? 139.831 151.691 164.529 1.00 44.73  ? 783  GLY A N     1 
ATOM   6296  C CA    . GLY B 2 786  ? 140.957 151.180 165.279 1.00 44.73  ? 783  GLY A CA    1 
ATOM   6297  C C     . GLY B 2 786  ? 141.793 150.226 164.453 1.00 44.73  ? 783  GLY A C     1 
ATOM   6298  O O     . GLY B 2 786  ? 141.689 150.161 163.226 1.00 44.73  ? 783  GLY A O     1 
ATOM   6299  N N     . GLN B 2 787  ? 142.639 149.467 165.152 1.00 44.73  ? 784  GLN A N     1 
ATOM   6300  C CA    . GLN B 2 787  ? 143.544 148.503 164.525 1.00 44.73  ? 784  GLN A CA    1 
ATOM   6301  C C     . GLN B 2 787  ? 144.490 149.183 163.537 1.00 44.73  ? 784  GLN A C     1 
ATOM   6302  O O     . GLN B 2 787  ? 144.735 148.683 162.438 1.00 44.73  ? 784  GLN A O     1 
ATOM   6303  C CB    . GLN B 2 787  ? 142.769 147.371 163.846 1.00 44.73  ? 784  GLN A CB    1 
ATOM   6304  C CG    . GLN B 2 787  ? 142.223 146.329 164.808 1.00 44.73  ? 784  GLN A CG    1 
ATOM   6305  C CD    . GLN B 2 787  ? 140.778 145.976 164.524 1.00 44.73  ? 784  GLN A CD    1 
ATOM   6306  O OE1   . GLN B 2 787  ? 140.325 146.037 163.381 1.00 44.73  ? 784  GLN A OE1   1 
ATOM   6307  N NE2   . GLN B 2 787  ? 140.044 145.603 165.566 1.00 44.73  ? 784  GLN A NE2   1 
ATOM   6308  N N     . ALA B 2 788  ? 145.025 150.335 163.931 1.00 44.73  ? 785  ALA A N     1 
ATOM   6309  C CA    . ALA B 2 788  ? 146.047 150.994 163.135 1.00 44.73  ? 785  ALA A CA    1 
ATOM   6310  C C     . ALA B 2 788  ? 147.367 150.237 163.240 1.00 44.73  ? 785  ALA A C     1 
ATOM   6311  O O     . ALA B 2 788  ? 147.615 149.496 164.195 1.00 44.73  ? 785  ALA A O     1 
ATOM   6312  C CB    . ALA B 2 788  ? 146.229 152.443 163.584 1.00 44.73  ? 785  ALA A CB    1 
ATOM   6313  N N     . GLU B 2 789  ? 148.224 150.431 162.241 1.00 44.73  ? 786  GLU A N     1 
ATOM   6314  C CA    . GLU B 2 789  ? 149.472 149.692 162.141 1.00 44.73  ? 786  GLU A CA    1 
ATOM   6315  C C     . GLU B 2 789  ? 150.635 150.644 161.900 1.00 44.73  ? 786  GLU A C     1 
ATOM   6316  O O     . GLU B 2 789  ? 150.483 151.691 161.266 1.00 44.73  ? 786  GLU A O     1 
ATOM   6317  C CB    . GLU B 2 789  ? 149.407 148.647 161.021 1.00 44.73  ? 786  GLU A CB    1 
ATOM   6318  C CG    . GLU B 2 789  ? 148.425 147.518 161.293 1.00 44.73  ? 786  GLU A CG    1 
ATOM   6319  C CD    . GLU B 2 789  ? 148.362 146.509 160.164 1.00 44.73  ? 786  GLU A CD    1 
ATOM   6320  O OE1   . GLU B 2 789  ? 148.988 146.750 159.112 1.00 44.73  ? 786  GLU A OE1   1 
ATOM   6321  O OE2   . GLU B 2 789  ? 147.684 145.472 160.330 1.00 44.73  ? 786  GLU A OE2   1 
ATOM   6322  N N     . LEU B 2 790  ? 151.800 150.263 162.418 1.00 44.73  ? 787  LEU A N     1 
ATOM   6323  C CA    . LEU B 2 790  ? 153.033 151.022 162.267 1.00 44.73  ? 787  LEU A CA    1 
ATOM   6324  C C     . LEU B 2 790  ? 154.060 150.170 161.536 1.00 44.73  ? 787  LEU A C     1 
ATOM   6325  O O     . LEU B 2 790  ? 154.181 148.969 161.800 1.00 44.73  ? 787  LEU A O     1 
ATOM   6326  C CB    . LEU B 2 790  ? 153.588 151.457 163.625 1.00 44.73  ? 787  LEU A CB    1 
ATOM   6327  C CG    . LEU B 2 790  ? 153.119 152.801 164.182 1.00 44.73  ? 787  LEU A CG    1 
ATOM   6328  C CD1   . LEU B 2 790  ? 151.668 152.730 164.621 1.00 44.73  ? 787  LEU A CD1   1 
ATOM   6329  C CD2   . LEU B 2 790  ? 154.006 153.234 165.333 1.00 44.73  ? 787  LEU A CD2   1 
ATOM   6330  N N     . PHE B 2 791  ? 154.798 150.791 160.618 1.00 44.73  ? 788  PHE A N     1 
ATOM   6331  C CA    . PHE B 2 791  ? 155.755 150.080 159.784 1.00 44.73  ? 788  PHE A CA    1 
ATOM   6332  C C     . PHE B 2 791  ? 157.065 150.848 159.703 1.00 44.73  ? 788  PHE A C     1 
ATOM   6333  O O     . PHE B 2 791  ? 157.091 152.079 159.781 1.00 44.73  ? 788  PHE A O     1 
ATOM   6334  C CB    . PHE B 2 791  ? 155.197 149.846 158.377 1.00 44.73  ? 788  PHE A CB    1 
ATOM   6335  C CG    . PHE B 2 791  ? 154.061 148.873 158.338 1.00 44.73  ? 788  PHE A CG    1 
ATOM   6336  C CD1   . PHE B 2 791  ? 154.303 147.512 158.331 1.00 44.73  ? 788  PHE A CD1   1 
ATOM   6337  C CD2   . PHE B 2 791  ? 152.753 149.316 158.322 1.00 44.73  ? 788  PHE A CD2   1 
ATOM   6338  C CE1   . PHE B 2 791  ? 153.262 146.610 158.299 1.00 44.73  ? 788  PHE A CE1   1 
ATOM   6339  C CE2   . PHE B 2 791  ? 151.707 148.418 158.291 1.00 44.73  ? 788  PHE A CE2   1 
ATOM   6340  C CZ    . PHE B 2 791  ? 151.963 147.064 158.280 1.00 44.73  ? 788  PHE A CZ    1 
ATOM   6341  N N     . TYR B 2 792  ? 158.156 150.101 159.544 1.00 44.73  ? 789  TYR A N     1 
ATOM   6342  C CA    . TYR B 2 792  ? 159.499 150.655 159.445 1.00 44.73  ? 789  TYR A CA    1 
ATOM   6343  C C     . TYR B 2 792  ? 160.175 150.075 158.214 1.00 44.73  ? 789  TYR A C     1 
ATOM   6344  O O     . TYR B 2 792  ? 160.239 148.852 158.057 1.00 44.73  ? 789  TYR A O     1 
ATOM   6345  C CB    . TYR B 2 792  ? 160.310 150.344 160.707 1.00 44.73  ? 789  TYR A CB    1 
ATOM   6346  C CG    . TYR B 2 792  ? 161.754 150.795 160.673 1.00 44.73  ? 789  TYR A CG    1 
ATOM   6347  C CD1   . TYR B 2 792  ? 162.753 149.956 160.207 1.00 44.73  ? 789  TYR A CD1   1 
ATOM   6348  C CD2   . TYR B 2 792  ? 162.118 152.053 161.129 1.00 44.73  ? 789  TYR A CD2   1 
ATOM   6349  C CE1   . TYR B 2 792  ? 164.069 150.357 160.185 1.00 44.73  ? 789  TYR A CE1   1 
ATOM   6350  C CE2   . TYR B 2 792  ? 163.435 152.463 161.110 1.00 44.73  ? 789  TYR A CE2   1 
ATOM   6351  C CZ    . TYR B 2 792  ? 164.405 151.611 160.635 1.00 44.73  ? 789  TYR A CZ    1 
ATOM   6352  O OH    . TYR B 2 792  ? 165.720 152.010 160.613 1.00 44.73  ? 789  TYR A OH    1 
ATOM   6353  N N     . ARG B 2 793  ? 160.677 150.949 157.347 1.00 44.73  ? 790  ARG A N     1 
ATOM   6354  C CA    . ARG B 2 793  ? 161.280 150.526 156.088 1.00 44.73  ? 790  ARG A CA    1 
ATOM   6355  C C     . ARG B 2 793  ? 162.779 150.780 156.107 1.00 44.73  ? 790  ARG A C     1 
ATOM   6356  O O     . ARG B 2 793  ? 163.202 151.945 156.173 1.00 44.73  ? 790  ARG A O     1 
ATOM   6357  C CB    . ARG B 2 793  ? 160.633 151.257 154.913 1.00 44.73  ? 790  ARG A CB    1 
ATOM   6358  C CG    . ARG B 2 793  ? 161.222 150.900 153.565 1.00 44.73  ? 790  ARG A CG    1 
ATOM   6359  C CD    . ARG B 2 793  ? 160.541 151.674 152.456 1.00 44.73  ? 790  ARG A CD    1 
ATOM   6360  N NE    . ARG B 2 793  ? 160.922 153.080 152.463 1.00 44.73  ? 790  ARG A NE    1 
ATOM   6361  C CZ    . ARG B 2 793  ? 160.208 154.050 151.909 1.00 44.73  ? 790  ARG A CZ    1 
ATOM   6362  N NH1   . ARG B 2 793  ? 159.062 153.801 151.299 1.00 44.73  ? 790  ARG A NH1   1 
ATOM   6363  N NH2   . ARG B 2 793  ? 160.655 155.301 151.970 1.00 44.73  ? 790  ARG A NH2   1 
ATOM   6364  N N     . PRO B 2 794  ? 163.616 149.744 156.058 1.00 44.73  ? 791  PRO A N     1 
ATOM   6365  C CA    . PRO B 2 794  ? 165.063 149.970 156.007 1.00 44.73  ? 791  PRO A CA    1 
ATOM   6366  C C     . PRO B 2 794  ? 165.472 150.656 154.713 1.00 44.73  ? 791  PRO A C     1 
ATOM   6367  O O     . PRO B 2 794  ? 164.814 150.530 153.678 1.00 44.73  ? 791  PRO A O     1 
ATOM   6368  C CB    . PRO B 2 794  ? 165.650 148.557 156.100 1.00 44.73  ? 791  PRO A CB    1 
ATOM   6369  C CG    . PRO B 2 794  ? 164.542 147.706 156.633 1.00 44.73  ? 791  PRO A CG    1 
ATOM   6370  C CD    . PRO B 2 794  ? 163.283 148.313 156.114 1.00 44.73  ? 791  PRO A CD    1 
ATOM   6371  N N     . LYS B 2 795  ? 166.577 151.393 154.784 1.00 44.73  ? 792  LYS A N     1 
ATOM   6372  C CA    . LYS B 2 795  ? 167.078 152.116 153.625 1.00 44.73  ? 792  LYS A CA    1 
ATOM   6373  C C     . LYS B 2 795  ? 167.577 151.152 152.556 1.00 44.73  ? 792  LYS A C     1 
ATOM   6374  O O     . LYS B 2 795  ? 167.961 150.014 152.840 1.00 44.73  ? 792  LYS A O     1 
ATOM   6375  C CB    . LYS B 2 795  ? 168.205 153.063 154.036 1.00 38.70  ? 792  LYS A CB    1 
ATOM   6376  C CG    . LYS B 2 795  ? 169.451 152.359 154.543 1.00 38.70  ? 792  LYS A CG    1 
ATOM   6377  C CD    . LYS B 2 795  ? 170.502 153.357 154.994 1.00 38.70  ? 792  LYS A CD    1 
ATOM   6378  C CE    . LYS B 2 795  ? 171.400 153.771 153.843 1.00 38.70  ? 792  LYS A CE    1 
ATOM   6379  N NZ    . LYS B 2 795  ? 172.245 152.642 153.366 1.00 38.70  ? 792  LYS A NZ    1 
ATOM   6380  N N     . SER B 2 796  ? 167.564 151.619 151.311 1.00 44.73  ? 793  SER A N     1 
ATOM   6381  C CA    . SER B 2 796  ? 168.014 150.842 150.161 1.00 44.73  ? 793  SER A CA    1 
ATOM   6382  C C     . SER B 2 796  ? 168.956 151.667 149.300 1.00 44.73  ? 793  SER A C     1 
ATOM   6383  O O     . SER B 2 796  ? 168.846 151.708 148.073 1.00 44.73  ? 793  SER A O     1 
ATOM   6384  C CB    . SER B 2 796  ? 166.831 150.354 149.334 1.00 44.73  ? 793  SER A CB    1 
ATOM   6385  O OG    . SER B 2 796  ? 166.092 151.442 148.812 1.00 44.73  ? 793  SER A OG    1 
ATOM   6386  N N     . ARG B 2 797  ? 169.906 152.342 149.940 1.00 54.52  ? 794  ARG A N     1 
ATOM   6387  C CA    . ARG B 2 797  ? 170.847 153.203 149.227 1.00 54.52  ? 794  ARG A CA    1 
ATOM   6388  C C     . ARG B 2 797  ? 171.930 152.330 148.606 1.00 54.52  ? 794  ARG A C     1 
ATOM   6389  O O     . ARG B 2 797  ? 172.925 151.995 149.252 1.00 54.52  ? 794  ARG A O     1 
ATOM   6390  C CB    . ARG B 2 797  ? 171.440 154.246 150.167 1.00 54.52  ? 794  ARG A CB    1 
ATOM   6391  C CG    . ARG B 2 797  ? 172.483 155.143 149.519 1.00 54.52  ? 794  ARG A CG    1 
ATOM   6392  C CD    . ARG B 2 797  ? 172.625 156.458 150.265 1.00 54.52  ? 794  ARG A CD    1 
ATOM   6393  N NE    . ARG B 2 797  ? 173.831 157.177 149.873 1.00 54.52  ? 794  ARG A NE    1 
ATOM   6394  C CZ    . ARG B 2 797  ? 174.103 158.429 150.218 1.00 54.52  ? 794  ARG A CZ    1 
ATOM   6395  N NH1   . ARG B 2 797  ? 173.270 159.137 150.962 1.00 54.52  ? 794  ARG A NH1   1 
ATOM   6396  N NH2   . ARG B 2 797  ? 175.240 158.983 149.805 1.00 54.52  ? 794  ARG A NH2   1 
ATOM   6397  N N     . MET B 2 798  ? 171.733 151.950 147.342 1.00 54.21  ? 795  MET A N     1 
ATOM   6398  C CA    . MET B 2 798  ? 172.731 151.206 146.591 1.00 54.21  ? 795  MET A CA    1 
ATOM   6399  C C     . MET B 2 798  ? 173.315 151.973 145.416 1.00 54.21  ? 795  MET A C     1 
ATOM   6400  O O     . MET B 2 798  ? 174.431 151.654 144.992 1.00 54.21  ? 795  MET A O     1 
ATOM   6401  C CB    . MET B 2 798  ? 172.146 149.882 146.070 1.00 54.21  ? 795  MET A CB    1 
ATOM   6402  C CG    . MET B 2 798  ? 172.100 148.765 147.102 1.00 54.21  ? 795  MET A CG    1 
ATOM   6403  S SD    . MET B 2 798  ? 170.939 149.068 148.447 1.00 54.21  ? 795  MET A SD    1 
ATOM   6404  C CE    . MET B 2 798  ? 169.445 148.364 147.755 1.00 54.21  ? 795  MET A CE    1 
ATOM   6405  N N     . LYS B 2 799  ? 172.605 152.966 144.882 1.00 51.62  ? 796  LYS A N     1 
ATOM   6406  C CA    . LYS B 2 799  ? 173.119 153.777 143.780 1.00 51.62  ? 796  LYS A CA    1 
ATOM   6407  C C     . LYS B 2 799  ? 172.417 155.129 143.851 1.00 51.62  ? 796  LYS A C     1 
ATOM   6408  O O     . LYS B 2 799  ? 171.259 155.251 143.440 1.00 51.62  ? 796  LYS A O     1 
ATOM   6409  C CB    . LYS B 2 799  ? 172.892 153.097 142.437 1.00 51.62  ? 796  LYS A CB    1 
ATOM   6410  N N     . ARG B 2 800  ? 173.118 156.132 144.371 1.00 57.26  ? 797  ARG A N     1 
ATOM   6411  C CA    . ARG B 2 800  ? 172.545 157.457 144.552 1.00 57.26  ? 797  ARG A CA    1 
ATOM   6412  C C     . ARG B 2 800  ? 172.856 158.331 143.345 1.00 57.26  ? 797  ARG A C     1 
ATOM   6413  O O     . ARG B 2 800  ? 174.023 158.515 142.985 1.00 57.26  ? 797  ARG A O     1 
ATOM   6414  C CB    . ARG B 2 800  ? 173.079 158.114 145.825 1.00 57.26  ? 797  ARG A CB    1 
ATOM   6415  C CG    . ARG B 2 800  ? 172.908 159.626 145.849 1.00 57.26  ? 797  ARG A CG    1 
ATOM   6416  C CD    . ARG B 2 800  ? 173.217 160.212 147.216 1.00 57.26  ? 797  ARG A CD    1 
ATOM   6417  N NE    . ARG B 2 800  ? 173.327 161.665 147.166 1.00 57.26  ? 797  ARG A NE    1 
ATOM   6418  C CZ    . ARG B 2 800  ? 174.173 162.380 147.895 1.00 57.26  ? 797  ARG A CZ    1 
ATOM   6419  N NH1   . ARG B 2 800  ? 175.005 161.807 148.749 1.00 57.26  ? 797  ARG A NH1   1 
ATOM   6420  N NH2   . ARG B 2 800  ? 174.185 163.703 147.764 1.00 57.26  ? 797  ARG A NH2   1 
ATOM   6421  N N     . MET B 2 801  ? 171.808 158.862 142.723 1.00 54.28  ? 798  MET A N     1 
ATOM   6422  C CA    . MET B 2 801  ? 171.928 159.849 141.662 1.00 54.28  ? 798  MET A CA    1 
ATOM   6423  C C     . MET B 2 801  ? 171.365 161.168 142.167 1.00 54.28  ? 798  MET A C     1 
ATOM   6424  O O     . MET B 2 801  ? 170.317 161.195 142.819 1.00 54.28  ? 798  MET A O     1 
ATOM   6425  C CB    . MET B 2 801  ? 171.190 159.404 140.396 1.00 54.28  ? 798  MET A CB    1 
ATOM   6426  C CG    . MET B 2 801  ? 171.405 160.316 139.199 1.00 54.28  ? 798  MET A CG    1 
ATOM   6427  S SD    . MET B 2 801  ? 173.111 160.306 138.616 1.00 54.28  ? 798  MET A SD    1 
ATOM   6428  C CE    . MET B 2 801  ? 173.194 161.890 137.784 1.00 54.28  ? 798  MET A CE    1 
ATOM   6429  N N     . ALA B 2 802  ? 172.068 162.260 141.883 1.00 49.77  ? 799  ALA A N     1 
ATOM   6430  C CA    . ALA B 2 802  ? 171.673 163.553 142.417 1.00 49.77  ? 799  ALA A CA    1 
ATOM   6431  C C     . ALA B 2 802  ? 172.069 164.651 141.445 1.00 49.77  ? 799  ALA A C     1 
ATOM   6432  O O     . ALA B 2 802  ? 172.964 164.483 140.613 1.00 49.77  ? 799  ALA A O     1 
ATOM   6433  C CB    . ALA B 2 802  ? 172.303 163.808 143.790 1.00 49.77  ? 799  ALA A CB    1 
ATOM   6434  N N     . HIS B 2 803  ? 171.385 165.785 141.567 1.00 47.99  ? 800  HIS A N     1 
ATOM   6435  C CA    . HIS B 2 803  ? 171.713 166.982 140.796 1.00 47.99  ? 800  HIS A CA    1 
ATOM   6436  C C     . HIS B 2 803  ? 172.496 167.910 141.714 1.00 47.99  ? 800  HIS A C     1 
ATOM   6437  O O     . HIS B 2 803  ? 171.928 168.706 142.462 1.00 47.99  ? 800  HIS A O     1 
ATOM   6438  C CB    . HIS B 2 803  ? 170.452 167.648 140.263 1.00 47.99  ? 800  HIS A CB    1 
ATOM   6439  C CG    . HIS B 2 803  ? 169.679 166.802 139.300 1.00 47.99  ? 800  HIS A CG    1 
ATOM   6440  N ND1   . HIS B 2 803  ? 169.992 166.726 137.960 1.00 47.99  ? 800  HIS A ND1   1 
ATOM   6441  C CD2   . HIS B 2 803  ? 168.605 165.999 139.482 1.00 47.99  ? 800  HIS A CD2   1 
ATOM   6442  C CE1   . HIS B 2 803  ? 169.145 165.911 137.359 1.00 47.99  ? 800  HIS A CE1   1 
ATOM   6443  N NE2   . HIS B 2 803  ? 168.293 165.455 138.260 1.00 47.99  ? 800  HIS A NE2   1 
ATOM   6444  N N     . ARG B 2 804  ? 173.820 167.798 141.666 1.00 50.59  ? 801  ARG A N     1 
ATOM   6445  C CA    . ARG B 2 804  ? 174.663 168.626 142.511 1.00 50.59  ? 801  ARG A CA    1 
ATOM   6446  C C     . ARG B 2 804  ? 174.602 170.082 142.062 1.00 50.59  ? 801  ARG A C     1 
ATOM   6447  O O     . ARG B 2 804  ? 174.279 170.396 140.913 1.00 50.59  ? 801  ARG A O     1 
ATOM   6448  C CB    . ARG B 2 804  ? 176.106 168.124 142.487 1.00 50.59  ? 801  ARG A CB    1 
ATOM   6449  C CG    . ARG B 2 804  ? 176.331 166.851 143.286 1.00 50.59  ? 801  ARG A CG    1 
ATOM   6450  C CD    . ARG B 2 804  ? 176.290 165.619 142.397 1.00 50.59  ? 801  ARG A CD    1 
ATOM   6451  N NE    . ARG B 2 804  ? 176.438 164.389 143.165 1.00 50.59  ? 801  ARG A NE    1 
ATOM   6452  C CZ    . ARG B 2 804  ? 176.056 163.191 142.742 1.00 50.59  ? 801  ARG A CZ    1 
ATOM   6453  N NH1   . ARG B 2 804  ? 175.497 163.024 141.555 1.00 50.59  ? 801  ARG A NH1   1 
ATOM   6454  N NH2   . ARG B 2 804  ? 176.240 162.136 143.530 1.00 50.59  ? 801  ARG A NH2   1 
ATOM   6455  N N     . LEU B 2 805  ? 174.903 170.979 142.999 1.00 50.96  ? 802  LEU A N     1 
ATOM   6456  C CA    . LEU B 2 805  ? 174.889 172.404 142.698 1.00 50.96  ? 802  LEU A CA    1 
ATOM   6457  C C     . LEU B 2 805  ? 175.924 172.731 141.630 1.00 50.96  ? 802  LEU A C     1 
ATOM   6458  O O     . LEU B 2 805  ? 177.062 172.255 141.674 1.00 50.96  ? 802  LEU A O     1 
ATOM   6459  C CB    . LEU B 2 805  ? 175.157 173.218 143.964 1.00 50.96  ? 802  LEU A CB    1 
ATOM   6460  C CG    . LEU B 2 805  ? 173.950 173.492 144.865 1.00 50.96  ? 802  LEU A CG    1 
ATOM   6461  C CD1   . LEU B 2 805  ? 173.644 172.293 145.750 1.00 50.96  ? 802  LEU A CD1   1 
ATOM   6462  C CD2   . LEU B 2 805  ? 174.182 174.738 145.706 1.00 50.96  ? 802  LEU A CD2   1 
ATOM   6463  N N     . GLY B 2 806  ? 175.520 173.549 140.662 1.00 50.68  ? 803  GLY A N     1 
ATOM   6464  C CA    . GLY B 2 806  ? 176.356 173.891 139.537 1.00 50.68  ? 803  GLY A CA    1 
ATOM   6465  C C     . GLY B 2 806  ? 176.073 173.106 138.275 1.00 50.68  ? 803  GLY A C     1 
ATOM   6466  O O     . GLY B 2 806  ? 176.466 173.545 137.189 1.00 50.68  ? 803  GLY A O     1 
ATOM   6467  N N     . GLU B 2 807  ? 175.406 171.960 138.383 1.00 54.38  ? 804  GLU A N     1 
ATOM   6468  C CA    . GLU B 2 807  ? 175.005 171.220 137.199 1.00 54.38  ? 804  GLU A CA    1 
ATOM   6469  C C     . GLU B 2 807  ? 173.784 171.877 136.560 1.00 54.38  ? 804  GLU A C     1 
ATOM   6470  O O     . GLU B 2 807  ? 173.154 172.774 137.127 1.00 54.38  ? 804  GLU A O     1 
ATOM   6471  C CB    . GLU B 2 807  ? 174.712 169.761 137.548 1.00 54.38  ? 804  GLU A CB    1 
ATOM   6472  C CG    . GLU B 2 807  ? 175.805 169.086 138.357 1.00 54.38  ? 804  GLU A CG    1 
ATOM   6473  C CD    . GLU B 2 807  ? 175.619 167.585 138.444 1.00 54.38  ? 804  GLU A CD    1 
ATOM   6474  O OE1   . GLU B 2 807  ? 174.997 167.008 137.527 1.00 54.38  ? 804  GLU A OE1   1 
ATOM   6475  O OE2   . GLU B 2 807  ? 176.092 166.981 139.429 1.00 54.38  ? 804  GLU A OE2   1 
ATOM   6476  N N     . LYS B 2 808  ? 173.454 171.422 135.357 1.00 53.07  ? 805  LYS A N     1 
ATOM   6477  C CA    . LYS B 2 808  ? 172.402 172.026 134.551 1.00 53.07  ? 805  LYS A CA    1 
ATOM   6478  C C     . LYS B 2 808  ? 171.291 171.007 134.335 1.00 53.07  ? 805  LYS A C     1 
ATOM   6479  O O     . LYS B 2 808  ? 171.503 169.983 133.677 1.00 53.07  ? 805  LYS A O     1 
ATOM   6480  C CB    . LYS B 2 808  ? 172.968 172.514 133.218 1.00 53.07  ? 805  LYS A CB    1 
ATOM   6481  C CG    . LYS B 2 808  ? 173.777 173.800 133.339 1.00 53.07  ? 805  LYS A CG    1 
ATOM   6482  C CD    . LYS B 2 808  ? 174.074 174.422 131.986 1.00 53.07  ? 805  LYS A CD    1 
ATOM   6483  C CE    . LYS B 2 808  ? 172.802 174.795 131.254 1.00 53.07  ? 805  LYS A CE    1 
ATOM   6484  N NZ    . LYS B 2 808  ? 172.406 176.207 131.515 1.00 53.07  ? 805  LYS A NZ    1 
ATOM   6485  N N     . MET B 2 809  ? 170.115 171.288 134.890 1.00 48.89  ? 806  MET A N     1 
ATOM   6486  C CA    . MET B 2 809  ? 168.964 170.419 134.697 1.00 48.89  ? 806  MET A CA    1 
ATOM   6487  C C     . MET B 2 809  ? 168.516 170.440 133.241 1.00 48.89  ? 806  MET A C     1 
ATOM   6488  O O     . MET B 2 809  ? 168.724 171.416 132.517 1.00 48.89  ? 806  MET A O     1 
ATOM   6489  C CB    . MET B 2 809  ? 167.801 170.858 135.587 1.00 48.89  ? 806  MET A CB    1 
ATOM   6490  C CG    . MET B 2 809  ? 168.095 170.891 137.075 1.00 48.89  ? 806  MET A CG    1 
ATOM   6491  S SD    . MET B 2 809  ? 167.577 169.383 137.913 1.00 48.89  ? 806  MET A SD    1 
ATOM   6492  C CE    . MET B 2 809  ? 167.740 169.879 139.625 1.00 48.89  ? 806  MET A CE    1 
ATOM   6493  N N     . LEU B 2 810  ? 167.894 169.345 132.813 1.00 45.29  ? 807  LEU A N     1 
ATOM   6494  C CA    . LEU B 2 810  ? 167.274 169.266 131.496 1.00 45.29  ? 807  LEU A CA    1 
ATOM   6495  C C     . LEU B 2 810  ? 165.831 168.818 131.660 1.00 45.29  ? 807  LEU A C     1 
ATOM   6496  O O     . LEU B 2 810  ? 165.571 167.753 132.229 1.00 45.29  ? 807  LEU A O     1 
ATOM   6497  C CB    . LEU B 2 810  ? 168.027 168.306 130.574 1.00 45.29  ? 807  LEU A CB    1 
ATOM   6498  C CG    . LEU B 2 810  ? 167.527 168.306 129.128 1.00 45.29  ? 807  LEU A CG    1 
ATOM   6499  C CD1   . LEU B 2 810  ? 167.305 169.726 128.633 1.00 45.29  ? 807  LEU A CD1   1 
ATOM   6500  C CD2   . LEU B 2 810  ? 168.483 167.563 128.214 1.00 45.29  ? 807  LEU A CD2   1 
ATOM   6501  N N     . ASN B 2 811  ? 164.902 169.627 131.163 1.00 44.73  ? 808  ASN A N     1 
ATOM   6502  C CA    . ASN B 2 811  ? 163.497 169.253 131.186 1.00 44.73  ? 808  ASN A CA    1 
ATOM   6503  C C     . ASN B 2 811  ? 163.237 168.117 130.206 1.00 44.73  ? 808  ASN A C     1 
ATOM   6504  O O     . ASN B 2 811  ? 163.835 168.054 129.130 1.00 44.73  ? 808  ASN A O     1 
ATOM   6505  C CB    . ASN B 2 811  ? 162.621 170.454 130.839 1.00 44.73  ? 808  ASN A CB    1 
ATOM   6506  C CG    . ASN B 2 811  ? 162.604 171.495 131.934 1.00 44.73  ? 808  ASN A CG    1 
ATOM   6507  O OD1   . ASN B 2 811  ? 163.373 171.419 132.891 1.00 44.73  ? 808  ASN A OD1   1 
ATOM   6508  N ND2   . ASN B 2 811  ? 161.719 172.475 131.803 1.00 44.73  ? 808  ASN A ND2   1 
ATOM   6509  N N     . LYS B 2 812  ? 162.335 167.212 130.587 1.00 44.73  ? 809  LYS A N     1 
ATOM   6510  C CA    . LYS B 2 812  ? 161.956 166.116 129.705 1.00 44.73  ? 809  LYS A CA    1 
ATOM   6511  C C     . LYS B 2 812  ? 161.034 166.562 128.580 1.00 44.73  ? 809  LYS A C     1 
ATOM   6512  O O     . LYS B 2 812  ? 160.753 165.764 127.680 1.00 44.73  ? 809  LYS A O     1 
ATOM   6513  C CB    . LYS B 2 812  ? 161.287 165.001 130.508 1.00 44.73  ? 809  LYS A CB    1 
ATOM   6514  C CG    . LYS B 2 812  ? 162.234 164.253 131.425 1.00 44.73  ? 809  LYS A CG    1 
ATOM   6515  C CD    . LYS B 2 812  ? 161.502 163.197 132.230 1.00 44.73  ? 809  LYS A CD    1 
ATOM   6516  C CE    . LYS B 2 812  ? 162.418 162.559 133.257 1.00 44.73  ? 809  LYS A CE    1 
ATOM   6517  N NZ    . LYS B 2 812  ? 163.473 161.731 132.612 1.00 44.73  ? 809  LYS A NZ    1 
ATOM   6518  N N     . LYS B 2 813  ? 160.560 167.802 128.609 1.00 44.73  ? 810  LYS A N     1 
ATOM   6519  C CA    . LYS B 2 813  ? 159.660 168.327 127.597 1.00 44.73  ? 810  LYS A CA    1 
ATOM   6520  C C     . LYS B 2 813  ? 160.327 169.470 126.843 1.00 44.73  ? 810  LYS A C     1 
ATOM   6521  O O     . LYS B 2 813  ? 161.261 170.110 127.332 1.00 44.73  ? 810  LYS A O     1 
ATOM   6522  C CB    . LYS B 2 813  ? 158.348 168.798 128.230 1.00 41.89  ? 810  LYS A CB    1 
ATOM   6523  C CG    . LYS B 2 813  ? 157.593 167.693 128.949 1.00 41.89  ? 810  LYS A CG    1 
ATOM   6524  C CD    . LYS B 2 813  ? 156.242 168.171 129.443 1.00 41.89  ? 810  LYS A CD    1 
ATOM   6525  C CE    . LYS B 2 813  ? 156.383 169.246 130.505 1.00 41.89  ? 810  LYS A CE    1 
ATOM   6526  N NZ    . LYS B 2 813  ? 155.087 169.511 131.187 1.00 41.89  ? 810  LYS A NZ    1 
ATOM   6527  N N     . LEU B 2 814  ? 159.832 169.716 125.633 1.00 46.47  ? 811  LEU A N     1 
ATOM   6528  C CA    . LEU B 2 814  ? 160.400 170.726 124.751 1.00 46.47  ? 811  LEU A CA    1 
ATOM   6529  C C     . LEU B 2 814  ? 159.874 172.105 125.152 1.00 46.47  ? 811  LEU A C     1 
ATOM   6530  O O     . LEU B 2 814  ? 159.322 172.289 126.241 1.00 46.47  ? 811  LEU A O     1 
ATOM   6531  C CB    . LEU B 2 814  ? 160.094 170.382 123.298 1.00 46.47  ? 811  LEU A CB    1 
ATOM   6532  C CG    . LEU B 2 814  ? 160.766 169.098 122.805 1.00 46.47  ? 811  LEU A CG    1 
ATOM   6533  C CD1   . LEU B 2 814  ? 160.311 168.745 121.394 1.00 46.47  ? 811  LEU A CD1   1 
ATOM   6534  C CD2   . LEU B 2 814  ? 162.284 169.189 122.892 1.00 46.47  ? 811  LEU A CD2   1 
ATOM   6535  N N     . LYS B 2 815  ? 160.056 173.103 124.280 1.00 48.66  ? 812  LYS A N     1 
ATOM   6536  C CA    . LYS B 2 815  ? 159.638 174.460 124.620 1.00 48.66  ? 812  LYS A CA    1 
ATOM   6537  C C     . LYS B 2 815  ? 158.142 174.551 124.877 1.00 48.66  ? 812  LYS A C     1 
ATOM   6538  O O     . LYS B 2 815  ? 157.712 175.379 125.688 1.00 48.66  ? 812  LYS A O     1 
ATOM   6539  C CB    . LYS B 2 815  ? 159.998 175.447 123.508 1.00 48.66  ? 812  LYS A CB    1 
ATOM   6540  C CG    . LYS B 2 815  ? 161.392 175.315 122.939 1.00 48.66  ? 812  LYS A CG    1 
ATOM   6541  C CD    . LYS B 2 815  ? 161.552 176.230 121.732 1.00 48.66  ? 812  LYS A CD    1 
ATOM   6542  C CE    . LYS B 2 815  ? 160.914 175.649 120.478 1.00 48.66  ? 812  LYS A CE    1 
ATOM   6543  N NZ    . LYS B 2 815  ? 161.430 174.313 120.103 1.00 48.66  ? 812  LYS A NZ    1 
ATOM   6544  N N     . ASP B 2 816  ? 157.342 173.722 124.210 1.00 48.13  ? 813  ASP A N     1 
ATOM   6545  C CA    . ASP B 2 816  ? 155.896 173.751 124.368 1.00 48.13  ? 813  ASP A CA    1 
ATOM   6546  C C     . ASP B 2 816  ? 155.422 172.992 125.598 1.00 48.13  ? 813  ASP A C     1 
ATOM   6547  O O     . ASP B 2 816  ? 154.208 172.888 125.804 1.00 48.13  ? 813  ASP A O     1 
ATOM   6548  C CB    . ASP B 2 816  ? 155.219 173.181 123.117 1.00 48.13  ? 813  ASP A CB    1 
ATOM   6549  C CG    . ASP B 2 816  ? 155.845 171.878 122.652 1.00 48.13  ? 813  ASP A CG    1 
ATOM   6550  O OD1   . ASP B 2 816  ? 156.260 171.070 123.509 1.00 48.13  ? 813  ASP A OD1   1 
ATOM   6551  O OD2   . ASP B 2 816  ? 155.923 171.660 121.425 1.00 48.13  ? 813  ASP A OD2   1 
ATOM   6552  N N     . GLN B 2 817  ? 156.350 172.449 126.393 1.00 47.22  ? 814  GLN A N     1 
ATOM   6553  C CA    . GLN B 2 817  ? 156.084 171.691 127.614 1.00 47.22  ? 814  GLN A CA    1 
ATOM   6554  C C     . GLN B 2 817  ? 154.946 170.690 127.439 1.00 47.22  ? 814  GLN A C     1 
ATOM   6555  O O     . GLN B 2 817  ? 154.196 170.416 128.382 1.00 47.22  ? 814  GLN A O     1 
ATOM   6556  C CB    . GLN B 2 817  ? 155.816 172.638 128.797 1.00 47.22  ? 814  GLN A CB    1 
ATOM   6557  C CG    . GLN B 2 817  ? 154.518 173.439 128.763 1.00 47.22  ? 814  GLN A CG    1 
ATOM   6558  C CD    . GLN B 2 817  ? 154.729 174.872 128.314 1.00 47.22  ? 814  GLN A CD    1 
ATOM   6559  O OE1   . GLN B 2 817  ? 155.817 175.243 127.876 1.00 47.22  ? 814  GLN A OE1   1 
ATOM   6560  N NE2   . GLN B 2 817  ? 153.686 175.686 128.424 1.00 47.22  ? 814  GLN A NE2   1 
ATOM   6561  N N     . LYS B 2 818  ? 154.820 170.127 126.237 1.00 46.36  ? 815  LYS A N     1 
ATOM   6562  C CA    . LYS B 2 818  ? 153.817 169.099 125.977 1.00 46.36  ? 815  LYS A CA    1 
ATOM   6563  C C     . LYS B 2 818  ? 154.329 167.907 125.184 1.00 46.36  ? 815  LYS A C     1 
ATOM   6564  O O     . LYS B 2 818  ? 153.707 166.842 125.253 1.00 46.36  ? 815  LYS A O     1 
ATOM   6565  C CB    . LYS B 2 818  ? 152.611 169.700 125.244 1.00 46.36  ? 815  LYS A CB    1 
ATOM   6566  C CG    . LYS B 2 818  ? 152.874 170.069 123.795 1.00 46.36  ? 815  LYS A CG    1 
ATOM   6567  C CD    . LYS B 2 818  ? 151.605 170.558 123.116 1.00 46.36  ? 815  LYS A CD    1 
ATOM   6568  C CE    . LYS B 2 818  ? 150.536 169.478 123.099 1.00 46.36  ? 815  LYS A CE    1 
ATOM   6569  N NZ    . LYS B 2 818  ? 151.002 168.244 122.411 1.00 46.36  ? 815  LYS A NZ    1 
ATOM   6570  N N     . THR B 2 819  ? 155.427 168.027 124.440 1.00 44.73  ? 816  THR A N     1 
ATOM   6571  C CA    . THR B 2 819  ? 155.941 166.926 123.632 1.00 44.73  ? 816  THR A CA    1 
ATOM   6572  C C     . THR B 2 819  ? 157.214 166.378 124.259 1.00 44.73  ? 816  THR A C     1 
ATOM   6573  O O     . THR B 2 819  ? 158.270 167.024 124.170 1.00 44.73  ? 816  THR A O     1 
ATOM   6574  C CB    . THR B 2 819  ? 156.210 167.389 122.199 1.00 44.73  ? 816  THR A CB    1 
ATOM   6575  O OG1   . THR B 2 819  ? 157.200 168.424 122.209 1.00 44.73  ? 816  THR A OG1   1 
ATOM   6576  C CG2   . THR B 2 819  ? 154.935 167.921 121.563 1.00 44.73  ? 816  THR A CG2   1 
ATOM   6577  N N     . PRO B 2 820  ? 157.171 165.211 124.897 1.00 44.73  ? 817  PRO A N     1 
ATOM   6578  C CA    . PRO B 2 820  ? 158.365 164.690 125.570 1.00 44.73  ? 817  PRO A CA    1 
ATOM   6579  C C     . PRO B 2 820  ? 159.467 164.304 124.596 1.00 44.73  ? 817  PRO A C     1 
ATOM   6580  O O     . PRO B 2 820  ? 159.220 163.917 123.452 1.00 44.73  ? 817  PRO A O     1 
ATOM   6581  C CB    . PRO B 2 820  ? 157.840 163.461 126.323 1.00 44.73  ? 817  PRO A CB    1 
ATOM   6582  C CG    . PRO B 2 820  ? 156.572 163.096 125.629 1.00 44.73  ? 817  PRO A CG    1 
ATOM   6583  C CD    . PRO B 2 820  ? 155.982 164.386 125.162 1.00 44.73  ? 817  PRO A CD    1 
ATOM   6584  N N     . ILE B 2 821  ? 160.701 164.418 125.077 1.00 44.73  ? 818  ILE A N     1 
ATOM   6585  C CA    . ILE B 2 821  ? 161.896 163.994 124.353 1.00 44.73  ? 818  ILE A CA    1 
ATOM   6586  C C     . ILE B 2 821  ? 161.943 162.470 124.344 1.00 44.73  ? 818  ILE A C     1 
ATOM   6587  O O     . ILE B 2 821  ? 161.500 161.838 125.313 1.00 44.73  ? 818  ILE A O     1 
ATOM   6588  C CB    . ILE B 2 821  ? 163.161 164.590 124.994 1.00 44.73  ? 818  ILE A CB    1 
ATOM   6589  C CG1   . ILE B 2 821  ? 162.966 166.079 125.270 1.00 44.73  ? 818  ILE A CG1   1 
ATOM   6590  C CG2   . ILE B 2 821  ? 164.385 164.372 124.123 1.00 44.73  ? 818  ILE A CG2   1 
ATOM   6591  C CD1   . ILE B 2 821  ? 164.032 166.672 126.156 1.00 44.73  ? 818  ILE A CD1   1 
ATOM   6592  N N     . PRO B 2 822  ? 162.448 161.839 123.283 1.00 44.92  ? 819  PRO A N     1 
ATOM   6593  C CA    . PRO B 2 822  ? 162.654 160.387 123.326 1.00 44.92  ? 819  PRO A CA    1 
ATOM   6594  C C     . PRO B 2 822  ? 163.611 159.999 124.443 1.00 44.92  ? 819  PRO A C     1 
ATOM   6595  O O     . PRO B 2 822  ? 164.503 160.762 124.821 1.00 44.92  ? 819  PRO A O     1 
ATOM   6596  C CB    . PRO B 2 822  ? 163.244 160.070 121.949 1.00 44.92  ? 819  PRO A CB    1 
ATOM   6597  C CG    . PRO B 2 822  ? 162.733 161.148 121.068 1.00 44.92  ? 819  PRO A CG    1 
ATOM   6598  C CD    . PRO B 2 822  ? 162.598 162.379 121.920 1.00 44.92  ? 819  PRO A CD    1 
ATOM   6599  N N     . ASP B 2 823  ? 163.404 158.794 124.979 1.00 52.59  ? 820  ASP A N     1 
ATOM   6600  C CA    . ASP B 2 823  ? 164.169 158.350 126.140 1.00 52.59  ? 820  ASP A CA    1 
ATOM   6601  C C     . ASP B 2 823  ? 165.661 158.288 125.835 1.00 52.59  ? 820  ASP A C     1 
ATOM   6602  O O     . ASP B 2 823  ? 166.489 158.731 126.640 1.00 52.59  ? 820  ASP A O     1 
ATOM   6603  C CB    . ASP B 2 823  ? 163.658 156.987 126.609 1.00 52.59  ? 820  ASP A CB    1 
ATOM   6604  C CG    . ASP B 2 823  ? 162.271 157.062 127.216 1.00 52.59  ? 820  ASP A CG    1 
ATOM   6605  O OD1   . ASP B 2 823  ? 161.924 158.121 127.782 1.00 52.59  ? 820  ASP A OD1   1 
ATOM   6606  O OD2   . ASP B 2 823  ? 161.526 156.064 127.125 1.00 52.59  ? 820  ASP A OD2   1 
ATOM   6607  N N     . THR B 2 824  ? 166.026 157.737 124.676 1.00 48.09  ? 821  THR A N     1 
ATOM   6608  C CA    . THR B 2 824  ? 167.440 157.621 124.333 1.00 48.09  ? 821  THR A CA    1 
ATOM   6609  C C     . THR B 2 824  ? 168.054 158.983 124.036 1.00 48.09  ? 821  THR A C     1 
ATOM   6610  O O     . THR B 2 824  ? 169.208 159.242 124.396 1.00 48.09  ? 821  THR A O     1 
ATOM   6611  C CB    . THR B 2 824  ? 167.624 156.685 123.139 1.00 48.09  ? 821  THR A CB    1 
ATOM   6612  O OG1   . THR B 2 824  ? 167.167 157.333 121.946 1.00 48.09  ? 821  THR A OG1   1 
ATOM   6613  C CG2   . THR B 2 824  ? 166.845 155.400 123.344 1.00 48.09  ? 821  THR A CG2   1 
ATOM   6614  N N     . LEU B 2 825  ? 167.300 159.867 123.381 1.00 48.80  ? 822  LEU A N     1 
ATOM   6615  C CA    . LEU B 2 825  ? 167.839 161.177 123.035 1.00 48.80  ? 822  LEU A CA    1 
ATOM   6616  C C     . LEU B 2 825  ? 167.958 162.069 124.263 1.00 48.80  ? 822  LEU A C     1 
ATOM   6617  O O     . LEU B 2 825  ? 168.834 162.940 124.324 1.00 48.80  ? 822  LEU A O     1 
ATOM   6618  C CB    . LEU B 2 825  ? 166.966 161.843 121.973 1.00 48.80  ? 822  LEU A CB    1 
ATOM   6619  C CG    . LEU B 2 825  ? 167.285 161.542 120.506 1.00 48.80  ? 822  LEU A CG    1 
ATOM   6620  C CD1   . LEU B 2 825  ? 168.698 161.989 120.173 1.00 48.80  ? 822  LEU A CD1   1 
ATOM   6621  C CD2   . LEU B 2 825  ? 167.087 160.071 120.168 1.00 48.80  ? 822  LEU A CD2   1 
ATOM   6622  N N     . TYR B 2 826  ? 167.080 161.873 125.250 1.00 50.39  ? 823  TYR A N     1 
ATOM   6623  C CA    . TYR B 2 826  ? 167.098 162.724 126.436 1.00 50.39  ? 823  TYR A CA    1 
ATOM   6624  C C     . TYR B 2 826  ? 168.387 162.545 127.228 1.00 50.39  ? 823  TYR A C     1 
ATOM   6625  O O     . TYR B 2 826  ? 168.963 163.523 127.719 1.00 50.39  ? 823  TYR A O     1 
ATOM   6626  C CB    . TYR B 2 826  ? 165.880 162.428 127.310 1.00 50.39  ? 823  TYR A CB    1 
ATOM   6627  C CG    . TYR B 2 826  ? 165.990 162.947 128.726 1.00 50.39  ? 823  TYR A CG    1 
ATOM   6628  C CD1   . TYR B 2 826  ? 165.900 164.305 128.996 1.00 50.39  ? 823  TYR A CD1   1 
ATOM   6629  C CD2   . TYR B 2 826  ? 166.167 162.079 129.794 1.00 50.39  ? 823  TYR A CD2   1 
ATOM   6630  C CE1   . TYR B 2 826  ? 165.993 164.784 130.287 1.00 50.39  ? 823  TYR A CE1   1 
ATOM   6631  C CE2   . TYR B 2 826  ? 166.261 162.550 131.089 1.00 50.39  ? 823  TYR A CE2   1 
ATOM   6632  C CZ    . TYR B 2 826  ? 166.173 163.905 131.328 1.00 50.39  ? 823  TYR A CZ    1 
ATOM   6633  O OH    . TYR B 2 826  ? 166.266 164.379 132.615 1.00 50.39  ? 823  TYR A OH    1 
ATOM   6634  N N     . GLN B 2 827  ? 168.852 161.301 127.370 1.00 51.16  ? 824  GLN A N     1 
ATOM   6635  C CA    . GLN B 2 827  ? 170.089 161.055 128.103 1.00 51.16  ? 824  GLN A CA    1 
ATOM   6636  C C     . GLN B 2 827  ? 171.288 161.667 127.389 1.00 51.16  ? 824  GLN A C     1 
ATOM   6637  O O     . GLN B 2 827  ? 172.169 162.250 128.030 1.00 51.16  ? 824  GLN A O     1 
ATOM   6638  C CB    . GLN B 2 827  ? 170.291 159.553 128.301 1.00 51.16  ? 824  GLN A CB    1 
ATOM   6639  C CG    . GLN B 2 827  ? 171.465 159.190 129.198 1.00 51.16  ? 824  GLN A CG    1 
ATOM   6640  C CD    . GLN B 2 827  ? 171.131 159.275 130.676 1.00 51.16  ? 824  GLN A CD    1 
ATOM   6641  O OE1   . GLN B 2 827  ? 170.167 159.930 131.073 1.00 51.16  ? 824  GLN A OE1   1 
ATOM   6642  N NE2   . GLN B 2 827  ? 171.930 158.608 131.500 1.00 51.16  ? 824  GLN A NE2   1 
ATOM   6643  N N     . GLU B 2 828  ? 171.342 161.536 126.061 1.00 53.67  ? 825  GLU A N     1 
ATOM   6644  C CA    . GLU B 2 828  ? 172.456 162.104 125.309 1.00 53.67  ? 825  GLU A CA    1 
ATOM   6645  C C     . GLU B 2 828  ? 172.468 163.624 125.403 1.00 53.67  ? 825  GLU A C     1 
ATOM   6646  O O     . GLU B 2 828  ? 173.531 164.235 125.568 1.00 53.67  ? 825  GLU A O     1 
ATOM   6647  C CB    . GLU B 2 828  ? 172.385 161.657 123.849 1.00 53.67  ? 825  GLU A CB    1 
ATOM   6648  C CG    . GLU B 2 828  ? 172.912 160.255 123.606 1.00 53.67  ? 825  GLU A CG    1 
ATOM   6649  C CD    . GLU B 2 828  ? 173.452 160.073 122.202 1.00 53.67  ? 825  GLU A CD    1 
ATOM   6650  O OE1   . GLU B 2 828  ? 174.249 160.924 121.756 1.00 53.67  ? 825  GLU A OE1   1 
ATOM   6651  O OE2   . GLU B 2 828  ? 173.079 159.079 121.544 1.00 53.67  ? 825  GLU A OE2   1 
ATOM   6652  N N     . LEU B 2 829  ? 171.296 164.253 125.294 1.00 56.94  ? 826  LEU A N     1 
ATOM   6653  C CA    . LEU B 2 829  ? 171.220 165.703 125.430 1.00 56.94  ? 826  LEU A CA    1 
ATOM   6654  C C     . LEU B 2 829  ? 171.592 166.149 126.839 1.00 56.94  ? 826  LEU A C     1 
ATOM   6655  O O     . LEU B 2 829  ? 172.275 167.164 127.014 1.00 56.94  ? 826  LEU A O     1 
ATOM   6656  C CB    . LEU B 2 829  ? 169.819 166.190 125.065 1.00 56.94  ? 826  LEU A CB    1 
ATOM   6657  C CG    . LEU B 2 829  ? 169.546 166.400 123.576 1.00 56.94  ? 826  LEU A CG    1 
ATOM   6658  C CD1   . LEU B 2 829  ? 168.052 166.380 123.296 1.00 56.94  ? 826  LEU A CD1   1 
ATOM   6659  C CD2   . LEU B 2 829  ? 170.167 167.703 123.100 1.00 56.94  ? 826  LEU A CD2   1 
ATOM   6660  N N     . TYR B 2 830  ? 171.149 165.404 127.856 1.00 57.04  ? 827  TYR A N     1 
ATOM   6661  C CA    . TYR B 2 830  ? 171.449 165.772 129.236 1.00 57.04  ? 827  TYR A CA    1 
ATOM   6662  C C     . TYR B 2 830  ? 172.947 165.727 129.509 1.00 57.04  ? 827  TYR A C     1 
ATOM   6663  O O     . TYR B 2 830  ? 173.487 166.600 130.199 1.00 57.04  ? 827  TYR A O     1 
ATOM   6664  C CB    . TYR B 2 830  ? 170.694 164.852 130.195 1.00 57.04  ? 827  TYR A CB    1 
ATOM   6665  C CG    . TYR B 2 830  ? 171.198 164.884 131.621 1.00 57.04  ? 827  TYR A CG    1 
ATOM   6666  C CD1   . TYR B 2 830  ? 170.959 165.980 132.437 1.00 57.04  ? 827  TYR A CD1   1 
ATOM   6667  C CD2   . TYR B 2 830  ? 171.898 163.811 132.154 1.00 57.04  ? 827  TYR A CD2   1 
ATOM   6668  C CE1   . TYR B 2 830  ? 171.413 166.012 133.741 1.00 57.04  ? 827  TYR A CE1   1 
ATOM   6669  C CE2   . TYR B 2 830  ? 172.355 163.834 133.457 1.00 57.04  ? 827  TYR A CE2   1 
ATOM   6670  C CZ    . TYR B 2 830  ? 172.109 164.937 134.245 1.00 57.04  ? 827  TYR A CZ    1 
ATOM   6671  O OH    . TYR B 2 830  ? 172.563 164.964 135.544 1.00 57.04  ? 827  TYR A OH    1 
ATOM   6672  N N     . ASP B 2 831  ? 173.633 164.711 128.985 1.00 55.42  ? 828  ASP A N     1 
ATOM   6673  C CA    . ASP B 2 831  ? 175.078 164.622 129.167 1.00 55.42  ? 828  ASP A CA    1 
ATOM   6674  C C     . ASP B 2 831  ? 175.797 165.766 128.463 1.00 55.42  ? 828  ASP A C     1 
ATOM   6675  O O     . ASP B 2 831  ? 176.758 166.329 129.000 1.00 55.42  ? 828  ASP A O     1 
ATOM   6676  C CB    . ASP B 2 831  ? 175.584 163.272 128.660 1.00 55.42  ? 828  ASP A CB    1 
ATOM   6677  C CG    . ASP B 2 831  ? 175.270 162.137 129.615 1.00 55.42  ? 828  ASP A CG    1 
ATOM   6678  O OD1   . ASP B 2 831  ? 175.140 162.397 130.829 1.00 55.42  ? 828  ASP A OD1   1 
ATOM   6679  O OD2   . ASP B 2 831  ? 175.152 160.984 129.150 1.00 55.42  ? 828  ASP A OD2   1 
ATOM   6680  N N     . TYR B 2 832  ? 175.349 166.122 127.257 1.00 57.05  ? 829  TYR A N     1 
ATOM   6681  C CA    . TYR B 2 832  ? 176.003 167.193 126.511 1.00 57.05  ? 829  TYR A CA    1 
ATOM   6682  C C     . TYR B 2 832  ? 175.766 168.551 127.161 1.00 57.05  ? 829  TYR A C     1 
ATOM   6683  O O     . TYR B 2 832  ? 176.653 169.413 127.147 1.00 57.05  ? 829  TYR A O     1 
ATOM   6684  C CB    . TYR B 2 832  ? 175.514 167.206 125.064 1.00 57.05  ? 829  TYR A CB    1 
ATOM   6685  C CG    . TYR B 2 832  ? 176.141 168.298 124.228 1.00 57.05  ? 829  TYR A CG    1 
ATOM   6686  C CD1   . TYR B 2 832  ? 177.476 168.229 123.851 1.00 57.05  ? 829  TYR A CD1   1 
ATOM   6687  C CD2   . TYR B 2 832  ? 175.401 169.399 123.819 1.00 57.05  ? 829  TYR A CD2   1 
ATOM   6688  C CE1   . TYR B 2 832  ? 178.056 169.225 123.089 1.00 57.05  ? 829  TYR A CE1   1 
ATOM   6689  C CE2   . TYR B 2 832  ? 175.972 170.400 123.056 1.00 57.05  ? 829  TYR A CE2   1 
ATOM   6690  C CZ    . TYR B 2 832  ? 177.300 170.308 122.694 1.00 57.05  ? 829  TYR A CZ    1 
ATOM   6691  O OH    . TYR B 2 832  ? 177.874 171.301 121.934 1.00 57.05  ? 829  TYR A OH    1 
ATOM   6692  N N     . VAL B 2 833  ? 174.573 168.767 127.720 1.00 56.71  ? 830  VAL A N     1 
ATOM   6693  C CA    . VAL B 2 833  ? 174.287 170.031 128.394 1.00 56.71  ? 830  VAL A CA    1 
ATOM   6694  C C     . VAL B 2 833  ? 175.231 170.226 129.573 1.00 56.71  ? 830  VAL A C     1 
ATOM   6695  O O     . VAL B 2 833  ? 175.775 171.318 129.781 1.00 56.71  ? 830  VAL A O     1 
ATOM   6696  C CB    . VAL B 2 833  ? 172.811 170.084 128.829 1.00 56.71  ? 830  VAL A CB    1 
ATOM   6697  C CG1   . VAL B 2 833  ? 172.593 171.188 129.849 1.00 56.71  ? 830  VAL A CG1   1 
ATOM   6698  C CG2   . VAL B 2 833  ? 171.912 170.296 127.622 1.00 56.71  ? 830  VAL A CG2   1 
ATOM   6699  N N     . ASN B 2 834  ? 175.456 169.170 130.349 1.00 57.98  ? 831  ASN A N     1 
ATOM   6700  C CA    . ASN B 2 834  ? 176.410 169.210 131.448 1.00 57.98  ? 831  ASN A CA    1 
ATOM   6701  C C     . ASN B 2 834  ? 177.851 169.037 130.986 1.00 57.98  ? 831  ASN A C     1 
ATOM   6702  O O     . ASN B 2 834  ? 178.754 169.025 131.829 1.00 57.98  ? 831  ASN A O     1 
ATOM   6703  C CB    . ASN B 2 834  ? 176.068 168.133 132.480 1.00 57.98  ? 831  ASN A CB    1 
ATOM   6704  C CG    . ASN B 2 834  ? 175.012 168.587 133.463 1.00 57.98  ? 831  ASN A CG    1 
ATOM   6705  O OD1   . ASN B 2 834  ? 174.201 169.459 133.157 1.00 57.98  ? 831  ASN A OD1   1 
ATOM   6706  N ND2   . ASN B 2 834  ? 175.014 167.995 134.651 1.00 57.98  ? 831  ASN A ND2   1 
ATOM   6707  N N     . HIS B 2 835  ? 178.079 168.898 129.677 1.00 56.90  ? 832  HIS A N     1 
ATOM   6708  C CA    . HIS B 2 835  ? 179.421 168.753 129.109 1.00 56.90  ? 832  HIS A CA    1 
ATOM   6709  C C     . HIS B 2 835  ? 180.144 167.541 129.691 1.00 56.90  ? 832  HIS A C     1 
ATOM   6710  O O     . HIS B 2 835  ? 181.327 167.601 130.029 1.00 56.90  ? 832  HIS A O     1 
ATOM   6711  C CB    . HIS B 2 835  ? 180.242 170.029 129.305 1.00 56.90  ? 832  HIS A CB    1 
ATOM   6712  C CG    . HIS B 2 835  ? 179.447 171.286 129.139 1.00 56.90  ? 832  HIS A CG    1 
ATOM   6713  N ND1   . HIS B 2 835  ? 178.880 171.655 127.938 1.00 56.90  ? 832  HIS A ND1   1 
ATOM   6714  C CD2   . HIS B 2 835  ? 179.119 172.258 130.023 1.00 56.90  ? 832  HIS A CD2   1 
ATOM   6715  C CE1   . HIS B 2 835  ? 178.240 172.800 128.089 1.00 56.90  ? 832  HIS A CE1   1 
ATOM   6716  N NE2   . HIS B 2 835  ? 178.370 173.188 129.345 1.00 56.90  ? 832  HIS A NE2   1 
ATOM   6717  N N     . ARG B 2 836  ? 179.419 166.429 129.809 1.00 57.21  ? 833  ARG A N     1 
ATOM   6718  C CA    . ARG B 2 836  ? 179.971 165.185 130.322 1.00 57.21  ? 833  ARG A CA    1 
ATOM   6719  C C     . ARG B 2 836  ? 180.143 164.119 129.249 1.00 57.21  ? 833  ARG A C     1 
ATOM   6720  O O     . ARG B 2 836  ? 180.973 163.219 129.420 1.00 57.21  ? 833  ARG A O     1 
ATOM   6721  C CB    . ARG B 2 836  ? 179.075 164.641 131.448 1.00 57.21  ? 833  ARG A CB    1 
ATOM   6722  C CG    . ARG B 2 836  ? 179.596 163.387 132.138 1.00 57.21  ? 833  ARG A CG    1 
ATOM   6723  C CD    . ARG B 2 836  ? 178.988 163.090 133.525 1.00 57.21  ? 833  ARG A CD    1 
ATOM   6724  N NE    . ARG B 2 836  ? 178.976 164.211 134.463 1.00 57.21  ? 833  ARG A NE    1 
ATOM   6725  C CZ    . ARG B 2 836  ? 178.079 165.189 134.485 1.00 57.21  ? 833  ARG A CZ    1 
ATOM   6726  N NH1   . ARG B 2 836  ? 177.021 165.177 133.691 1.00 57.21  ? 833  ARG A NH1   1 
ATOM   6727  N NH2   . ARG B 2 836  ? 178.233 166.190 135.347 1.00 57.21  ? 833  ARG A NH2   1 
ATOM   6728  N N     . LEU B 2 837  ? 179.408 164.208 128.144 1.00 68.25  ? 834  LEU A N     1 
ATOM   6729  C CA    . LEU B 2 837  ? 179.453 163.196 127.098 1.00 68.25  ? 834  LEU A CA    1 
ATOM   6730  C C     . LEU B 2 837  ? 180.779 163.269 126.352 1.00 68.25  ? 834  LEU A C     1 
ATOM   6731  O O     . LEU B 2 837  ? 181.159 164.331 125.847 1.00 68.25  ? 834  LEU A O     1 
ATOM   6732  C CB    . LEU B 2 837  ? 178.289 163.376 126.124 1.00 68.25  ? 834  LEU A CB    1 
ATOM   6733  C CG    . LEU B 2 837  ? 178.233 162.399 124.949 1.00 68.25  ? 834  LEU A CG    1 
ATOM   6734  C CD1   . LEU B 2 837  ? 178.034 160.977 125.447 1.00 68.25  ? 834  LEU A CD1   1 
ATOM   6735  C CD2   . LEU B 2 837  ? 177.130 162.789 123.978 1.00 68.25  ? 834  LEU A CD2   1 
ATOM   6736  N N     . SER B 2 838  ? 181.480 162.136 126.289 1.00 72.95  ? 835  SER A N     1 
ATOM   6737  C CA    . SER B 2 838  ? 182.737 162.070 125.552 1.00 72.95  ? 835  SER A CA    1 
ATOM   6738  C C     . SER B 2 838  ? 182.514 161.996 124.047 1.00 72.95  ? 835  SER A C     1 
ATOM   6739  O O     . SER B 2 838  ? 183.331 162.515 123.278 1.00 72.95  ? 835  SER A O     1 
ATOM   6740  C CB    . SER B 2 838  ? 183.558 160.868 126.020 1.00 72.95  ? 835  SER A CB    1 
ATOM   6741  O OG    . SER B 2 838  ? 182.801 159.672 125.939 1.00 72.95  ? 835  SER A OG    1 
ATOM   6742  N N     . HIS B 2 839  ? 181.428 161.364 123.613 1.00 76.11  ? 836  HIS A N     1 
ATOM   6743  C CA    . HIS B 2 839  ? 181.148 161.193 122.194 1.00 76.11  ? 836  HIS A CA    1 
ATOM   6744  C C     . HIS B 2 839  ? 180.460 162.444 121.650 1.00 76.11  ? 836  HIS A C     1 
ATOM   6745  O O     . HIS B 2 839  ? 180.386 163.484 122.309 1.00 76.11  ? 836  HIS A O     1 
ATOM   6746  C CB    . HIS B 2 839  ? 180.312 159.937 121.969 1.00 76.11  ? 836  HIS A CB    1 
ATOM   6747  C CG    . HIS B 2 839  ? 180.678 158.798 122.870 1.00 76.11  ? 836  HIS A CG    1 
ATOM   6748  N ND1   . HIS B 2 839  ? 180.148 158.648 124.133 1.00 76.11  ? 836  HIS A ND1   1 
ATOM   6749  C CD2   . HIS B 2 839  ? 181.523 157.755 122.690 1.00 76.11  ? 836  HIS A CD2   1 
ATOM   6750  C CE1   . HIS B 2 839  ? 180.650 157.562 124.693 1.00 76.11  ? 836  HIS A CE1   1 
ATOM   6751  N NE2   . HIS B 2 839  ? 181.487 157.002 123.838 1.00 76.11  ? 836  HIS A NE2   1 
ATOM   6752  N N     . ASP B 2 840  ? 179.947 162.352 120.426 1.00 69.21  ? 837  ASP A N     1 
ATOM   6753  C CA    . ASP B 2 840  ? 179.276 163.458 119.765 1.00 69.21  ? 837  ASP A CA    1 
ATOM   6754  C C     . ASP B 2 840  ? 177.799 163.133 119.588 1.00 69.21  ? 837  ASP A C     1 
ATOM   6755  O O     . ASP B 2 840  ? 177.405 161.964 119.542 1.00 69.21  ? 837  ASP A O     1 
ATOM   6756  C CB    . ASP B 2 840  ? 179.912 163.760 118.403 1.00 69.21  ? 837  ASP A CB    1 
ATOM   6757  C CG    . ASP B 2 840  ? 181.399 164.037 118.503 1.00 69.21  ? 837  ASP A CG    1 
ATOM   6758  O OD1   . ASP B 2 840  ? 181.894 164.235 119.632 1.00 69.21  ? 837  ASP A OD1   1 
ATOM   6759  O OD2   . ASP B 2 840  ? 182.073 164.054 117.452 1.00 69.21  ? 837  ASP A OD2   1 
ATOM   6760  N N     . LEU B 2 841  ? 176.986 164.180 119.493 1.00 63.52  ? 838  LEU A N     1 
ATOM   6761  C CA    . LEU B 2 841  ? 175.549 164.000 119.370 1.00 63.52  ? 838  LEU A CA    1 
ATOM   6762  C C     . LEU B 2 841  ? 175.176 163.498 117.978 1.00 63.52  ? 838  LEU A C     1 
ATOM   6763  O O     . LEU B 2 841  ? 175.888 163.711 116.993 1.00 63.52  ? 838  LEU A O     1 
ATOM   6764  C CB    . LEU B 2 841  ? 174.817 165.308 119.664 1.00 63.52  ? 838  LEU A CB    1 
ATOM   6765  C CG    . LEU B 2 841  ? 175.222 166.032 120.946 1.00 63.52  ? 838  LEU A CG    1 
ATOM   6766  C CD1   . LEU B 2 841  ? 174.529 167.381 121.037 1.00 63.52  ? 838  LEU A CD1   1 
ATOM   6767  C CD2   . LEU B 2 841  ? 174.893 165.173 122.155 1.00 63.52  ? 838  LEU A CD2   1 
ATOM   6768  N N     . SER B 2 842  ? 174.034 162.819 117.911 1.00 63.66  ? 839  SER A N     1 
ATOM   6769  C CA    . SER B 2 842  ? 173.513 162.332 116.646 1.00 63.66  ? 839  SER A CA    1 
ATOM   6770  C C     . SER B 2 842  ? 172.908 163.483 115.843 1.00 63.66  ? 839  SER A C     1 
ATOM   6771  O O     . SER B 2 842  ? 172.762 164.609 116.326 1.00 63.66  ? 839  SER A O     1 
ATOM   6772  C CB    . SER B 2 842  ? 172.470 161.241 116.882 1.00 63.66  ? 839  SER A CB    1 
ATOM   6773  O OG    . SER B 2 842  ? 173.023 160.153 117.600 1.00 63.66  ? 839  SER A OG    1 
ATOM   6774  N N     . ASP B 2 843  ? 172.560 163.184 114.589 1.00 66.23  ? 840  ASP A N     1 
ATOM   6775  C CA    . ASP B 2 843  ? 171.960 164.198 113.729 1.00 66.23  ? 840  ASP A CA    1 
ATOM   6776  C C     . ASP B 2 843  ? 170.623 164.673 114.283 1.00 66.23  ? 840  ASP A C     1 
ATOM   6777  O O     . ASP B 2 843  ? 170.332 165.876 114.278 1.00 66.23  ? 840  ASP A O     1 
ATOM   6778  C CB    . ASP B 2 843  ? 171.792 163.652 112.311 1.00 66.23  ? 840  ASP A CB    1 
ATOM   6779  C CG    . ASP B 2 843  ? 171.195 162.260 112.289 1.00 66.23  ? 840  ASP A CG    1 
ATOM   6780  O OD1   . ASP B 2 843  ? 171.084 161.644 113.370 1.00 66.23  ? 840  ASP A OD1   1 
ATOM   6781  O OD2   . ASP B 2 843  ? 170.837 161.781 111.193 1.00 66.23  ? 840  ASP A OD2   1 
ATOM   6782  N N     . GLU B 2 844  ? 169.793 163.745 114.766 1.00 63.44  ? 841  GLU A N     1 
ATOM   6783  C CA    . GLU B 2 844  ? 168.526 164.142 115.371 1.00 63.44  ? 841  GLU A CA    1 
ATOM   6784  C C     . GLU B 2 844  ? 168.734 164.796 116.731 1.00 63.44  ? 841  GLU A C     1 
ATOM   6785  O O     . GLU B 2 844  ? 167.903 165.605 117.160 1.00 63.44  ? 841  GLU A O     1 
ATOM   6786  C CB    . GLU B 2 844  ? 167.594 162.935 115.488 1.00 63.44  ? 841  GLU A CB    1 
ATOM   6787  C CG    . GLU B 2 844  ? 167.982 161.934 116.562 1.00 63.44  ? 841  GLU A CG    1 
ATOM   6788  C CD    . GLU B 2 844  ? 168.555 160.655 115.985 1.00 63.44  ? 841  GLU A CD    1 
ATOM   6789  O OE1   . GLU B 2 844  ? 168.830 160.622 114.768 1.00 63.44  ? 841  GLU A OE1   1 
ATOM   6790  O OE2   . GLU B 2 844  ? 168.729 159.683 116.749 1.00 63.44  ? 841  GLU A OE2   1 
ATOM   6791  N N     . ALA B 2 845  ? 169.827 164.460 117.422 1.00 61.10  ? 842  ALA A N     1 
ATOM   6792  C CA    . ALA B 2 845  ? 170.130 165.115 118.690 1.00 61.10  ? 842  ALA A CA    1 
ATOM   6793  C C     . ALA B 2 845  ? 170.431 166.594 118.489 1.00 61.10  ? 842  ALA A C     1 
ATOM   6794  O O     . ALA B 2 845  ? 169.989 167.439 119.276 1.00 61.10  ? 842  ALA A O     1 
ATOM   6795  C CB    . ALA B 2 845  ? 171.303 164.416 119.376 1.00 61.10  ? 842  ALA A CB    1 
ATOM   6796  N N     . ARG B 2 846  ? 171.190 166.925 117.442 1.00 60.66  ? 843  ARG A N     1 
ATOM   6797  C CA    . ARG B 2 846  ? 171.475 168.324 117.142 1.00 60.66  ? 843  ARG A CA    1 
ATOM   6798  C C     . ARG B 2 846  ? 170.199 169.067 116.763 1.00 60.66  ? 843  ARG A C     1 
ATOM   6799  O O     . ARG B 2 846  ? 169.994 170.217 117.171 1.00 60.66  ? 843  ARG A O     1 
ATOM   6800  C CB    . ARG B 2 846  ? 172.513 168.409 116.019 1.00 60.66  ? 843  ARG A CB    1 
ATOM   6801  C CG    . ARG B 2 846  ? 172.830 169.810 115.484 1.00 60.66  ? 843  ARG A CG    1 
ATOM   6802  C CD    . ARG B 2 846  ? 172.943 170.873 116.580 1.00 60.66  ? 843  ARG A CD    1 
ATOM   6803  N NE    . ARG B 2 846  ? 173.837 170.479 117.663 1.00 60.66  ? 843  ARG A NE    1 
ATOM   6804  C CZ    . ARG B 2 846  ? 175.156 170.390 117.559 1.00 60.66  ? 843  ARG A CZ    1 
ATOM   6805  N NH1   . ARG B 2 846  ? 175.783 170.679 116.430 1.00 60.66  ? 843  ARG A NH1   1 
ATOM   6806  N NH2   . ARG B 2 846  ? 175.866 170.007 118.617 1.00 60.66  ? 843  ARG A NH2   1 
ATOM   6807  N N     . ALA B 2 847  ? 169.323 168.421 115.990 1.00 57.35  ? 844  ALA A N     1 
ATOM   6808  C CA    . ALA B 2 847  ? 168.084 169.068 115.573 1.00 57.35  ? 844  ALA A CA    1 
ATOM   6809  C C     . ALA B 2 847  ? 167.192 169.383 116.766 1.00 57.35  ? 844  ALA A C     1 
ATOM   6810  O O     . ALA B 2 847  ? 166.556 170.442 116.815 1.00 57.35  ? 844  ALA A O     1 
ATOM   6811  C CB    . ALA B 2 847  ? 167.344 168.185 114.568 1.00 57.35  ? 844  ALA A CB    1 
ATOM   6812  N N     . LEU B 2 848  ? 167.130 168.473 117.738 1.00 57.97  ? 845  LEU A N     1 
ATOM   6813  C CA    . LEU B 2 848  ? 166.287 168.673 118.909 1.00 57.97  ? 845  LEU A CA    1 
ATOM   6814  C C     . LEU B 2 848  ? 166.957 169.528 119.977 1.00 57.97  ? 845  LEU A C     1 
ATOM   6815  O O     . LEU B 2 848  ? 166.313 169.864 120.977 1.00 57.97  ? 845  LEU A O     1 
ATOM   6816  C CB    . LEU B 2 848  ? 165.893 167.317 119.499 1.00 57.97  ? 845  LEU A CB    1 
ATOM   6817  C CG    . LEU B 2 848  ? 164.622 167.246 120.345 1.00 57.97  ? 845  LEU A CG    1 
ATOM   6818  C CD1   . LEU B 2 848  ? 163.433 167.773 119.562 1.00 57.97  ? 845  LEU A CD1   1 
ATOM   6819  C CD2   . LEU B 2 848  ? 164.374 165.819 120.795 1.00 57.97  ? 845  LEU A CD2   1 
ATOM   6820  N N     . LEU B 2 849  ? 168.230 169.881 119.791 1.00 56.11  ? 846  LEU A N     1 
ATOM   6821  C CA    . LEU B 2 849  ? 168.947 170.644 120.811 1.00 56.11  ? 846  LEU A CA    1 
ATOM   6822  C C     . LEU B 2 849  ? 168.333 172.013 121.086 1.00 56.11  ? 846  LEU A C     1 
ATOM   6823  O O     . LEU B 2 849  ? 168.144 172.346 122.268 1.00 56.11  ? 846  LEU A O     1 
ATOM   6824  C CB    . LEU B 2 849  ? 170.426 170.754 120.418 1.00 56.11  ? 846  LEU A CB    1 
ATOM   6825  C CG    . LEU B 2 849  ? 171.425 171.357 121.413 1.00 56.11  ? 846  LEU A CG    1 
ATOM   6826  C CD1   . LEU B 2 849  ? 172.810 170.792 121.148 1.00 56.11  ? 846  LEU A CD1   1 
ATOM   6827  C CD2   . LEU B 2 849  ? 171.470 172.878 121.340 1.00 56.11  ? 846  LEU A CD2   1 
ATOM   6828  N N     . PRO B 2 850  ? 168.017 172.852 120.092 1.00 55.59  ? 847  PRO A N     1 
ATOM   6829  C CA    . PRO B 2 850  ? 167.433 174.161 120.424 1.00 55.59  ? 847  PRO A CA    1 
ATOM   6830  C C     . PRO B 2 850  ? 166.069 174.071 121.080 1.00 55.59  ? 847  PRO A C     1 
ATOM   6831  O O     . PRO B 2 850  ? 165.663 175.021 121.760 1.00 55.59  ? 847  PRO A O     1 
ATOM   6832  C CB    . PRO B 2 850  ? 167.361 174.871 119.066 1.00 55.59  ? 847  PRO A CB    1 
ATOM   6833  C CG    . PRO B 2 850  ? 167.262 173.779 118.080 1.00 55.59  ? 847  PRO A CG    1 
ATOM   6834  C CD    . PRO B 2 850  ? 168.092 172.653 118.632 1.00 55.59  ? 847  PRO A CD    1 
ATOM   6835  N N     . ASN B 2 851  ? 165.353 172.962 120.908 1.00 58.18  ? 848  ASN A N     1 
ATOM   6836  C CA    . ASN B 2 851  ? 164.010 172.825 121.456 1.00 58.18  ? 848  ASN A CA    1 
ATOM   6837  C C     . ASN B 2 851  ? 163.990 172.492 122.942 1.00 58.18  ? 848  ASN A C     1 
ATOM   6838  O O     . ASN B 2 851  ? 162.970 172.719 123.601 1.00 58.18  ? 848  ASN A O     1 
ATOM   6839  C CB    . ASN B 2 851  ? 163.233 171.755 120.683 1.00 58.18  ? 848  ASN A CB    1 
ATOM   6840  C CG    . ASN B 2 851  ? 163.295 171.957 119.184 1.00 58.18  ? 848  ASN A CG    1 
ATOM   6841  O OD1   . ASN B 2 851  ? 163.635 173.039 118.706 1.00 58.18  ? 848  ASN A OD1   1 
ATOM   6842  N ND2   . ASN B 2 851  ? 162.954 170.918 118.432 1.00 58.18  ? 848  ASN A ND2   1 
ATOM   6843  N N     . VAL B 2 852  ? 165.078 171.952 123.492 1.00 51.02  ? 849  VAL A N     1 
ATOM   6844  C CA    . VAL B 2 852  ? 165.062 171.599 124.906 1.00 51.02  ? 849  VAL A CA    1 
ATOM   6845  C C     . VAL B 2 852  ? 165.234 172.853 125.759 1.00 51.02  ? 849  VAL A C     1 
ATOM   6846  O O     . VAL B 2 852  ? 165.697 173.903 125.300 1.00 51.02  ? 849  VAL A O     1 
ATOM   6847  C CB    . VAL B 2 852  ? 166.140 170.553 125.229 1.00 51.02  ? 849  VAL A CB    1 
ATOM   6848  C CG1   . VAL B 2 852  ? 165.976 169.333 124.335 1.00 51.02  ? 849  VAL A CG1   1 
ATOM   6849  C CG2   . VAL B 2 852  ? 167.529 171.152 125.102 1.00 51.02  ? 849  VAL A CG2   1 
ATOM   6850  N N     . ILE B 2 853  ? 164.840 172.738 127.025 1.00 44.87  ? 850  ILE A N     1 
ATOM   6851  C CA    . ILE B 2 853  ? 164.926 173.829 127.989 1.00 44.87  ? 850  ILE A CA    1 
ATOM   6852  C C     . ILE B 2 853  ? 165.762 173.357 129.169 1.00 44.87  ? 850  ILE A C     1 
ATOM   6853  O O     . ILE B 2 853  ? 165.529 172.268 129.704 1.00 44.87  ? 850  ILE A O     1 
ATOM   6854  C CB    . ILE B 2 853  ? 163.532 174.289 128.450 1.00 44.87  ? 850  ILE A CB    1 
ATOM   6855  C CG1   . ILE B 2 853  ? 162.704 174.756 127.251 1.00 44.87  ? 850  ILE A CG1   1 
ATOM   6856  C CG2   . ILE B 2 853  ? 163.651 175.397 129.481 1.00 44.87  ? 850  ILE A CG2   1 
ATOM   6857  C CD1   . ILE B 2 853  ? 163.306 175.931 126.511 1.00 44.87  ? 850  ILE A CD1   1 
ATOM   6858  N N     . THR B 2 854  ? 166.734 174.173 129.569 1.00 45.84  ? 851  THR A N     1 
ATOM   6859  C CA    . THR B 2 854  ? 167.657 173.829 130.639 1.00 45.84  ? 851  THR A CA    1 
ATOM   6860  C C     . THR B 2 854  ? 167.496 174.784 131.815 1.00 45.84  ? 851  THR A C     1 
ATOM   6861  O O     . THR B 2 854  ? 167.115 175.947 131.648 1.00 45.84  ? 851  THR A O     1 
ATOM   6862  C CB    . THR B 2 854  ? 169.110 173.848 130.148 1.00 45.84  ? 851  THR A CB    1 
ATOM   6863  O OG1   . THR B 2 854  ? 169.963 173.286 131.152 1.00 45.84  ? 851  THR A OG1   1 
ATOM   6864  C CG2   . THR B 2 854  ? 169.556 175.269 129.837 1.00 45.84  ? 851  THR A CG2   1 
ATOM   6865  N N     . LYS B 2 855  ? 167.771 174.270 133.013 1.00 45.56  ? 852  LYS A N     1 
ATOM   6866  C CA    . LYS B 2 855  ? 167.717 175.050 134.242 1.00 45.56  ? 852  LYS A CA    1 
ATOM   6867  C C     . LYS B 2 855  ? 168.943 174.744 135.086 1.00 45.56  ? 852  LYS A C     1 
ATOM   6868  O O     . LYS B 2 855  ? 169.470 173.629 135.046 1.00 45.56  ? 852  LYS A O     1 
ATOM   6869  C CB    . LYS B 2 855  ? 166.450 174.747 135.053 1.00 45.56  ? 852  LYS A CB    1 
ATOM   6870  C CG    . LYS B 2 855  ? 165.164 174.728 134.249 1.00 45.56  ? 852  LYS A CG    1 
ATOM   6871  C CD    . LYS B 2 855  ? 164.075 173.955 134.973 1.00 45.56  ? 852  LYS A CD    1 
ATOM   6872  C CE    . LYS B 2 855  ? 163.992 174.352 136.436 1.00 45.56  ? 852  LYS A CE    1 
ATOM   6873  N NZ    . LYS B 2 855  ? 163.690 175.801 136.599 1.00 45.56  ? 852  LYS A NZ    1 
ATOM   6874  N N     . GLU B 2 856  ? 169.395 175.735 135.848 1.00 47.20  ? 853  GLU A N     1 
ATOM   6875  C CA    . GLU B 2 856  ? 170.500 175.529 136.772 1.00 47.20  ? 853  GLU A CA    1 
ATOM   6876  C C     . GLU B 2 856  ? 169.992 174.963 138.092 1.00 47.20  ? 853  GLU A C     1 
ATOM   6877  O O     . GLU B 2 856  ? 168.875 175.253 138.529 1.00 47.20  ? 853  GLU A O     1 
ATOM   6878  C CB    . GLU B 2 856  ? 171.253 176.835 137.018 1.00 47.20  ? 853  GLU A CB    1 
ATOM   6879  C CG    . GLU B 2 856  ? 172.066 177.312 135.826 1.00 47.20  ? 853  GLU A CG    1 
ATOM   6880  C CD    . GLU B 2 856  ? 173.383 177.942 136.233 1.00 47.20  ? 853  GLU A CD    1 
ATOM   6881  O OE1   . GLU B 2 856  ? 173.360 178.959 136.958 1.00 47.20  ? 853  GLU A OE1   1 
ATOM   6882  O OE2   . GLU B 2 856  ? 174.443 177.420 135.828 1.00 47.20  ? 853  GLU A OE2   1 
ATOM   6883  N N     . VAL B 2 857  ? 170.830 174.147 138.728 1.00 50.09  ? 854  VAL A N     1 
ATOM   6884  C CA    . VAL B 2 857  ? 170.465 173.473 139.972 1.00 50.09  ? 854  VAL A CA    1 
ATOM   6885  C C     . VAL B 2 857  ? 170.588 174.494 141.100 1.00 50.09  ? 854  VAL A C     1 
ATOM   6886  O O     . VAL B 2 857  ? 171.681 174.743 141.613 1.00 50.09  ? 854  VAL A O     1 
ATOM   6887  C CB    . VAL B 2 857  ? 171.333 172.240 140.229 1.00 50.09  ? 854  VAL A CB    1 
ATOM   6888  C CG1   . VAL B 2 857  ? 171.018 171.645 141.590 1.00 50.09  ? 854  VAL A CG1   1 
ATOM   6889  C CG2   . VAL B 2 857  ? 171.129 171.208 139.132 1.00 50.09  ? 854  VAL A CG2   1 
ATOM   6890  N N     . SER B 2 858  ? 169.463 175.103 141.482 1.00 45.40  ? 855  SER A N     1 
ATOM   6891  C CA    . SER B 2 858  ? 169.469 176.001 142.632 1.00 45.40  ? 855  SER A CA    1 
ATOM   6892  C C     . SER B 2 858  ? 169.702 175.231 143.925 1.00 45.40  ? 855  SER A C     1 
ATOM   6893  O O     . SER B 2 858  ? 170.461 175.677 144.793 1.00 45.40  ? 855  SER A O     1 
ATOM   6894  C CB    . SER B 2 858  ? 168.156 176.779 142.697 1.00 45.40  ? 855  SER A CB    1 
ATOM   6895  O OG    . SER B 2 858  ? 168.008 177.625 141.569 1.00 45.40  ? 855  SER A OG    1 
ATOM   6896  N N     . HIS B 2 859  ? 169.059 174.075 144.068 1.00 45.65  ? 856  HIS A N     1 
ATOM   6897  C CA    . HIS B 2 859  ? 169.238 173.210 145.223 1.00 45.65  ? 856  HIS A CA    1 
ATOM   6898  C C     . HIS B 2 859  ? 169.257 171.766 144.752 1.00 45.65  ? 856  HIS A C     1 
ATOM   6899  O O     . HIS B 2 859  ? 168.639 171.421 143.741 1.00 45.65  ? 856  HIS A O     1 
ATOM   6900  C CB    . HIS B 2 859  ? 168.129 173.410 146.261 1.00 45.65  ? 856  HIS A CB    1 
ATOM   6901  C CG    . HIS B 2 859  ? 166.747 173.258 145.705 1.00 45.65  ? 856  HIS A CG    1 
ATOM   6902  N ND1   . HIS B 2 859  ? 165.961 174.336 145.360 1.00 45.65  ? 856  HIS A ND1   1 
ATOM   6903  C CD2   . HIS B 2 859  ? 166.011 172.154 145.435 1.00 45.65  ? 856  HIS A CD2   1 
ATOM   6904  C CE1   . HIS B 2 859  ? 164.801 173.903 144.901 1.00 45.65  ? 856  HIS A CE1   1 
ATOM   6905  N NE2   . HIS B 2 859  ? 164.806 172.583 144.936 1.00 45.65  ? 856  HIS A NE2   1 
ATOM   6906  N N     . GLU B 2 860  ? 169.968 170.923 145.496 1.00 48.92  ? 857  GLU A N     1 
ATOM   6907  C CA    . GLU B 2 860  ? 170.137 169.538 145.080 1.00 48.92  ? 857  GLU A CA    1 
ATOM   6908  C C     . GLU B 2 860  ? 168.803 168.802 145.097 1.00 48.92  ? 857  GLU A C     1 
ATOM   6909  O O     . GLU B 2 860  ? 167.965 169.008 145.980 1.00 48.92  ? 857  GLU A O     1 
ATOM   6910  C CB    . GLU B 2 860  ? 171.157 168.828 145.976 1.00 48.92  ? 857  GLU A CB    1 
ATOM   6911  C CG    . GLU B 2 860  ? 170.634 168.386 147.333 1.00 48.92  ? 857  GLU A CG    1 
ATOM   6912  C CD    . GLU B 2 860  ? 171.665 167.609 148.128 1.00 48.92  ? 857  GLU A CD    1 
ATOM   6913  O OE1   . GLU B 2 860  ? 172.833 167.547 147.689 1.00 48.92  ? 857  GLU A OE1   1 
ATOM   6914  O OE2   . GLU B 2 860  ? 171.308 167.059 149.191 1.00 48.92  ? 857  GLU A OE2   1 
ATOM   6915  N N     . ILE B 2 861  ? 168.597 167.966 144.086 1.00 45.25  ? 858  ILE A N     1 
ATOM   6916  C CA    . ILE B 2 861  ? 167.431 167.099 143.989 1.00 45.25  ? 858  ILE A CA    1 
ATOM   6917  C C     . ILE B 2 861  ? 167.942 165.667 143.950 1.00 45.25  ? 858  ILE A C     1 
ATOM   6918  O O     . ILE B 2 861  ? 168.683 165.291 143.033 1.00 45.25  ? 858  ILE A O     1 
ATOM   6919  C CB    . ILE B 2 861  ? 166.577 167.426 142.754 1.00 45.25  ? 858  ILE A CB    1 
ATOM   6920  C CG1   . ILE B 2 861  ? 165.663 168.615 143.051 1.00 45.25  ? 858  ILE A CG1   1 
ATOM   6921  C CG2   . ILE B 2 861  ? 165.761 166.222 142.326 1.00 45.25  ? 858  ILE A CG2   1 
ATOM   6922  C CD1   . ILE B 2 861  ? 164.784 169.015 141.895 1.00 45.25  ? 858  ILE A CD1   1 
ATOM   6923  N N     . ILE B 2 862  ? 167.565 164.878 144.950 1.00 44.73  ? 859  ILE A N     1 
ATOM   6924  C CA    . ILE B 2 862  ? 168.077 163.524 145.119 1.00 44.73  ? 859  ILE A CA    1 
ATOM   6925  C C     . ILE B 2 862  ? 167.130 162.569 144.412 1.00 44.73  ? 859  ILE A C     1 
ATOM   6926  O O     . ILE B 2 862  ? 165.931 162.534 144.714 1.00 44.73  ? 859  ILE A O     1 
ATOM   6927  C CB    . ILE B 2 862  ? 168.219 163.158 146.604 1.00 44.73  ? 859  ILE A CB    1 
ATOM   6928  C CG1   . ILE B 2 862  ? 169.094 164.179 147.332 1.00 44.73  ? 859  ILE A CG1   1 
ATOM   6929  C CG2   . ILE B 2 862  ? 168.800 161.762 146.751 1.00 44.73  ? 859  ILE A CG2   1 
ATOM   6930  C CD1   . ILE B 2 862  ? 170.542 164.156 146.913 1.00 44.73  ? 859  ILE A CD1   1 
ATOM   6931  N N     . LYS B 2 863  ? 167.662 161.796 143.469 1.00 44.73  ? 860  LYS A N     1 
ATOM   6932  C CA    . LYS B 2 863  ? 166.851 160.794 142.795 1.00 44.73  ? 860  LYS A CA    1 
ATOM   6933  C C     . LYS B 2 863  ? 166.468 159.696 143.775 1.00 44.73  ? 860  LYS A C     1 
ATOM   6934  O O     . LYS B 2 863  ? 167.330 159.107 144.434 1.00 44.73  ? 860  LYS A O     1 
ATOM   6935  C CB    . LYS B 2 863  ? 167.606 160.203 141.607 1.00 44.73  ? 860  LYS A CB    1 
ATOM   6936  C CG    . LYS B 2 863  ? 166.799 159.205 140.798 1.00 44.73  ? 860  LYS A CG    1 
ATOM   6937  C CD    . LYS B 2 863  ? 167.604 158.654 139.634 1.00 44.73  ? 860  LYS A CD    1 
ATOM   6938  C CE    . LYS B 2 863  ? 166.751 157.765 138.747 1.00 44.73  ? 860  LYS A CE    1 
ATOM   6939  N NZ    . LYS B 2 863  ? 166.317 156.528 139.453 1.00 44.73  ? 860  LYS A NZ    1 
ATOM   6940  N N     . ASP B 2 864  ? 165.166 159.430 143.867 1.00 44.73  ? 861  ASP A N     1 
ATOM   6941  C CA    . ASP B 2 864  ? 164.632 158.385 144.736 1.00 44.73  ? 861  ASP A CA    1 
ATOM   6942  C C     . ASP B 2 864  ? 165.019 158.630 146.193 1.00 44.73  ? 861  ASP A C     1 
ATOM   6943  O O     . ASP B 2 864  ? 165.489 157.731 146.893 1.00 44.73  ? 861  ASP A O     1 
ATOM   6944  C CB    . ASP B 2 864  ? 165.088 157.005 144.266 1.00 38.79  ? 861  ASP A CB    1 
ATOM   6945  C CG    . ASP B 2 864  ? 164.662 156.715 142.844 1.00 38.79  ? 861  ASP A CG    1 
ATOM   6946  O OD1   . ASP B 2 864  ? 163.444 156.755 142.567 1.00 38.79  ? 861  ASP A OD1   1 
ATOM   6947  O OD2   . ASP B 2 864  ? 165.542 156.441 142.001 1.00 38.79  ? 861  ASP A OD2   1 
ATOM   6948  N N     . ARG B 2 865  ? 164.819 159.869 146.649 1.00 44.73  ? 862  ARG A N     1 
ATOM   6949  C CA    . ARG B 2 865  ? 165.144 160.241 148.022 1.00 44.73  ? 862  ARG A CA    1 
ATOM   6950  C C     . ARG B 2 865  ? 164.265 159.530 149.042 1.00 44.73  ? 862  ARG A C     1 
ATOM   6951  O O     . ARG B 2 865  ? 164.603 159.518 150.230 1.00 44.73  ? 862  ARG A O     1 
ATOM   6952  C CB    . ARG B 2 865  ? 165.020 161.757 148.188 1.00 40.58  ? 862  ARG A CB    1 
ATOM   6953  C CG    . ARG B 2 865  ? 165.810 162.337 149.345 1.00 40.58  ? 862  ARG A CG    1 
ATOM   6954  C CD    . ARG B 2 865  ? 165.648 163.846 149.409 1.00 40.58  ? 862  ARG A CD    1 
ATOM   6955  N NE    . ARG B 2 865  ? 164.319 164.239 149.859 1.00 40.58  ? 862  ARG A NE    1 
ATOM   6956  C CZ    . ARG B 2 865  ? 163.815 165.458 149.730 1.00 40.58  ? 862  ARG A CZ    1 
ATOM   6957  N NH1   . ARG B 2 865  ? 164.503 166.432 149.159 1.00 40.58  ? 862  ARG A NH1   1 
ATOM   6958  N NH2   . ARG B 2 865  ? 162.590 165.707 150.185 1.00 40.58  ? 862  ARG A NH2   1 
ATOM   6959  N N     . ARG B 2 866  ? 163.148 158.942 148.607 1.00 44.73  ? 863  ARG A N     1 
ATOM   6960  C CA    . ARG B 2 866  ? 162.260 158.248 149.534 1.00 44.73  ? 863  ARG A CA    1 
ATOM   6961  C C     . ARG B 2 866  ? 162.984 157.115 150.246 1.00 44.73  ? 863  ARG A C     1 
ATOM   6962  O O     . ARG B 2 866  ? 162.830 156.931 151.459 1.00 44.73  ? 863  ARG A O     1 
ATOM   6963  C CB    . ARG B 2 866  ? 161.045 157.696 148.786 1.00 44.73  ? 863  ARG A CB    1 
ATOM   6964  C CG    . ARG B 2 866  ? 160.045 158.735 148.317 1.00 44.73  ? 863  ARG A CG    1 
ATOM   6965  C CD    . ARG B 2 866  ? 160.347 159.199 146.899 1.00 44.73  ? 863  ARG A CD    1 
ATOM   6966  N NE    . ARG B 2 866  ? 160.470 158.090 145.961 1.00 44.73  ? 863  ARG A NE    1 
ATOM   6967  C CZ    . ARG B 2 866  ? 159.445 157.474 145.390 1.00 44.73  ? 863  ARG A CZ    1 
ATOM   6968  N NH1   . ARG B 2 866  ? 158.196 157.824 145.649 1.00 44.73  ? 863  ARG A NH1   1 
ATOM   6969  N NH2   . ARG B 2 866  ? 159.679 156.483 144.535 1.00 44.73  ? 863  ARG A NH2   1 
ATOM   6970  N N     . PHE B 2 867  ? 163.781 156.349 149.507 1.00 44.73  ? 864  PHE A N     1 
ATOM   6971  C CA    . PHE B 2 867  ? 164.403 155.133 150.005 1.00 44.73  ? 864  PHE A CA    1 
ATOM   6972  C C     . PHE B 2 867  ? 165.870 155.320 150.367 1.00 44.73  ? 864  PHE A C     1 
ATOM   6973  O O     . PHE B 2 867  ? 166.552 154.335 150.668 1.00 44.73  ? 864  PHE A O     1 
ATOM   6974  C CB    . PHE B 2 867  ? 164.250 154.024 148.967 1.00 44.73  ? 864  PHE A CB    1 
ATOM   6975  C CG    . PHE B 2 867  ? 162.895 153.987 148.326 1.00 44.73  ? 864  PHE A CG    1 
ATOM   6976  C CD1   . PHE B 2 867  ? 161.807 153.482 149.010 1.00 44.73  ? 864  PHE A CD1   1 
ATOM   6977  C CD2   . PHE B 2 867  ? 162.701 154.498 147.059 1.00 44.73  ? 864  PHE A CD2   1 
ATOM   6978  C CE1   . PHE B 2 867  ? 160.557 153.453 148.428 1.00 44.73  ? 864  PHE A CE1   1 
ATOM   6979  C CE2   . PHE B 2 867  ? 161.453 154.474 146.472 1.00 44.73  ? 864  PHE A CE2   1 
ATOM   6980  C CZ    . PHE B 2 867  ? 160.380 153.952 147.159 1.00 44.73  ? 864  PHE A CZ    1 
ATOM   6981  N N     . THR B 2 868  ? 166.373 156.554 150.336 1.00 44.73  ? 865  THR A N     1 
ATOM   6982  C CA    . THR B 2 868  ? 167.764 156.792 150.707 1.00 44.73  ? 865  THR A CA    1 
ATOM   6983  C C     . THR B 2 868  ? 168.007 156.470 152.176 1.00 44.73  ? 865  THR A C     1 
ATOM   6984  O O     . THR B 2 868  ? 169.023 155.856 152.523 1.00 44.73  ? 865  THR A O     1 
ATOM   6985  C CB    . THR B 2 868  ? 168.145 158.241 150.398 1.00 44.73  ? 865  THR A CB    1 
ATOM   6986  O OG1   . THR B 2 868  ? 168.345 158.392 148.987 1.00 44.73  ? 865  THR A OG1   1 
ATOM   6987  C CG2   . THR B 2 868  ? 169.422 158.635 151.127 1.00 44.73  ? 865  THR A CG2   1 
ATOM   6988  N N     . SER B 2 869  ? 167.079 156.855 153.051 1.00 44.73  ? 866  SER A N     1 
ATOM   6989  C CA    . SER B 2 869  ? 167.249 156.640 154.482 1.00 44.73  ? 866  SER A CA    1 
ATOM   6990  C C     . SER B 2 869  ? 166.135 155.768 155.048 1.00 44.73  ? 866  SER A C     1 
ATOM   6991  O O     . SER B 2 869  ? 165.294 155.258 154.301 1.00 44.73  ? 866  SER A O     1 
ATOM   6992  C CB    . SER B 2 869  ? 167.296 157.979 155.219 1.00 44.73  ? 866  SER A CB    1 
ATOM   6993  O OG    . SER B 2 869  ? 166.118 158.731 154.985 1.00 44.73  ? 866  SER A OG    1 
ATOM   6994  N N     . ASP B 2 870  ? 166.127 155.591 156.366 1.00 44.73  ? 867  ASP A N     1 
ATOM   6995  C CA    . ASP B 2 870  ? 165.124 154.778 157.040 1.00 44.73  ? 867  ASP A CA    1 
ATOM   6996  C C     . ASP B 2 870  ? 163.893 155.623 157.334 1.00 44.73  ? 867  ASP A C     1 
ATOM   6997  O O     . ASP B 2 870  ? 164.011 156.787 157.731 1.00 44.73  ? 867  ASP A O     1 
ATOM   6998  C CB    . ASP B 2 870  ? 165.689 154.198 158.335 1.00 44.73  ? 867  ASP A CB    1 
ATOM   6999  C CG    . ASP B 2 870  ? 166.927 153.354 158.104 1.00 44.73  ? 867  ASP A CG    1 
ATOM   7000  O OD1   . ASP B 2 870  ? 166.785 152.192 157.671 1.00 44.73  ? 867  ASP A OD1   1 
ATOM   7001  O OD2   . ASP B 2 870  ? 168.044 153.853 158.357 1.00 44.73  ? 867  ASP A OD2   1 
ATOM   7002  N N     . LYS B 2 871  ? 162.713 155.037 157.142 1.00 44.73  ? 868  LYS A N     1 
ATOM   7003  C CA    . LYS B 2 871  ? 161.458 155.757 157.294 1.00 44.73  ? 868  LYS A CA    1 
ATOM   7004  C C     . LYS B 2 871  ? 160.486 154.950 158.141 1.00 44.73  ? 868  LYS A C     1 
ATOM   7005  O O     . LYS B 2 871  ? 160.466 153.717 158.076 1.00 44.73  ? 868  LYS A O     1 
ATOM   7006  C CB    . LYS B 2 871  ? 160.820 156.057 155.932 1.00 44.73  ? 868  LYS A CB    1 
ATOM   7007  C CG    . LYS B 2 871  ? 161.695 156.858 154.983 1.00 44.73  ? 868  LYS A CG    1 
ATOM   7008  C CD    . LYS B 2 871  ? 161.872 158.287 155.459 1.00 44.73  ? 868  LYS A CD    1 
ATOM   7009  C CE    . LYS B 2 871  ? 162.336 159.188 154.327 1.00 44.73  ? 868  LYS A CE    1 
ATOM   7010  N NZ    . LYS B 2 871  ? 161.262 159.409 153.323 1.00 44.73  ? 868  LYS A NZ    1 
ATOM   7011  N N     . PHE B 2 872  ? 159.686 155.653 158.935 1.00 44.73  ? 869  PHE A N     1 
ATOM   7012  C CA    . PHE B 2 872  ? 158.567 155.056 159.644 1.00 44.73  ? 869  PHE A CA    1 
ATOM   7013  C C     . PHE B 2 872  ? 157.286 155.246 158.835 1.00 44.73  ? 869  PHE A C     1 
ATOM   7014  O O     . PHE B 2 872  ? 157.242 156.006 157.866 1.00 44.73  ? 869  PHE A O     1 
ATOM   7015  C CB    . PHE B 2 872  ? 158.411 155.671 161.034 1.00 44.73  ? 869  PHE A CB    1 
ATOM   7016  C CG    . PHE B 2 872  ? 159.575 155.419 161.950 1.00 44.73  ? 869  PHE A CG    1 
ATOM   7017  C CD1   . PHE B 2 872  ? 160.737 156.161 161.838 1.00 44.73  ? 869  PHE A CD1   1 
ATOM   7018  C CD2   . PHE B 2 872  ? 159.498 154.452 162.934 1.00 44.73  ? 869  PHE A CD2   1 
ATOM   7019  C CE1   . PHE B 2 872  ? 161.803 155.934 162.683 1.00 44.73  ? 869  PHE A CE1   1 
ATOM   7020  C CE2   . PHE B 2 872  ? 160.562 154.221 163.782 1.00 44.73  ? 869  PHE A CE2   1 
ATOM   7021  C CZ    . PHE B 2 872  ? 161.715 154.963 163.656 1.00 44.73  ? 869  PHE A CZ    1 
ATOM   7022  N N     . PHE B 2 873  ? 156.229 154.550 159.247 1.00 44.73  ? 870  PHE A N     1 
ATOM   7023  C CA    . PHE B 2 873  ? 154.972 154.614 158.517 1.00 44.73  ? 870  PHE A CA    1 
ATOM   7024  C C     . PHE B 2 873  ? 153.811 154.421 159.480 1.00 44.73  ? 870  PHE A C     1 
ATOM   7025  O O     . PHE B 2 873  ? 153.968 153.880 160.578 1.00 44.73  ? 870  PHE A O     1 
ATOM   7026  C CB    . PHE B 2 873  ? 154.924 153.571 157.396 1.00 44.73  ? 870  PHE A CB    1 
ATOM   7027  C CG    . PHE B 2 873  ? 155.820 153.893 156.239 1.00 44.73  ? 870  PHE A CG    1 
ATOM   7028  C CD1   . PHE B 2 873  ? 155.508 154.923 155.372 1.00 44.73  ? 870  PHE A CD1   1 
ATOM   7029  C CD2   . PHE B 2 873  ? 156.985 153.179 156.030 1.00 44.73  ? 870  PHE A CD2   1 
ATOM   7030  C CE1   . PHE B 2 873  ? 156.334 155.227 154.314 1.00 44.73  ? 870  PHE A CE1   1 
ATOM   7031  C CE2   . PHE B 2 873  ? 157.814 153.479 154.972 1.00 44.73  ? 870  PHE A CE2   1 
ATOM   7032  C CZ    . PHE B 2 873  ? 157.488 154.504 154.113 1.00 44.73  ? 870  PHE A CZ    1 
ATOM   7033  N N     . PHE B 2 874  ? 152.633 154.874 159.048 1.00 44.73  ? 871  PHE A N     1 
ATOM   7034  C CA    . PHE B 2 874  ? 151.430 154.811 159.876 1.00 44.73  ? 871  PHE A CA    1 
ATOM   7035  C C     . PHE B 2 874  ? 150.248 154.532 158.954 1.00 44.73  ? 871  PHE A C     1 
ATOM   7036  O O     . PHE B 2 874  ? 149.749 155.445 158.289 1.00 44.73  ? 871  PHE A O     1 
ATOM   7037  C CB    . PHE B 2 874  ? 151.237 156.103 160.657 1.00 44.73  ? 871  PHE A CB    1 
ATOM   7038  C CG    . PHE B 2 874  ? 150.069 156.077 161.597 1.00 44.73  ? 871  PHE A CG    1 
ATOM   7039  C CD1   . PHE B 2 874  ? 149.880 155.013 162.459 1.00 44.73  ? 871  PHE A CD1   1 
ATOM   7040  C CD2   . PHE B 2 874  ? 149.164 157.121 161.623 1.00 44.73  ? 871  PHE A CD2   1 
ATOM   7041  C CE1   . PHE B 2 874  ? 148.809 154.989 163.326 1.00 44.73  ? 871  PHE A CE1   1 
ATOM   7042  C CE2   . PHE B 2 874  ? 148.090 157.102 162.487 1.00 44.73  ? 871  PHE A CE2   1 
ATOM   7043  C CZ    . PHE B 2 874  ? 147.913 156.034 163.339 1.00 44.73  ? 871  PHE A CZ    1 
ATOM   7044  N N     . HIS B 2 875  ? 149.810 153.277 158.918 1.00 44.73  ? 872  HIS A N     1 
ATOM   7045  C CA    . HIS B 2 875  ? 148.637 152.873 158.152 1.00 44.73  ? 872  HIS A CA    1 
ATOM   7046  C C     . HIS B 2 875  ? 147.438 152.894 159.092 1.00 44.73  ? 872  HIS A C     1 
ATOM   7047  O O     . HIS B 2 875  ? 147.316 152.036 159.972 1.00 44.73  ? 872  HIS A O     1 
ATOM   7048  C CB    . HIS B 2 875  ? 148.832 151.487 157.540 1.00 44.73  ? 872  HIS A CB    1 
ATOM   7049  C CG    . HIS B 2 875  ? 149.966 151.408 156.567 1.00 44.73  ? 872  HIS A CG    1 
ATOM   7050  N ND1   . HIS B 2 875  ? 150.333 150.232 155.950 1.00 44.73  ? 872  HIS A ND1   1 
ATOM   7051  C CD2   . HIS B 2 875  ? 150.816 152.355 156.106 1.00 44.73  ? 872  HIS A CD2   1 
ATOM   7052  C CE1   . HIS B 2 875  ? 151.359 150.458 155.150 1.00 44.73  ? 872  HIS A CE1   1 
ATOM   7053  N NE2   . HIS B 2 875  ? 151.672 151.739 155.226 1.00 44.73  ? 872  HIS A NE2   1 
ATOM   7054  N N     . VAL B 2 876  ? 146.555 153.870 158.908 1.00 44.73  ? 873  VAL A N     1 
ATOM   7055  C CA    . VAL B 2 876  ? 145.415 154.089 159.787 1.00 44.73  ? 873  VAL A CA    1 
ATOM   7056  C C     . VAL B 2 876  ? 144.141 153.935 158.966 1.00 44.73  ? 873  VAL A C     1 
ATOM   7057  O O     . VAL B 2 876  ? 144.046 154.504 157.877 1.00 44.73  ? 873  VAL A O     1 
ATOM   7058  C CB    . VAL B 2 876  ? 145.456 155.466 160.474 1.00 44.73  ? 873  VAL A CB    1 
ATOM   7059  C CG1   . VAL B 2 876  ? 145.532 156.596 159.455 1.00 44.73  ? 873  VAL A CG1   1 
ATOM   7060  C CG2   . VAL B 2 876  ? 144.257 155.638 161.379 1.00 44.73  ? 873  VAL A CG2   1 
ATOM   7061  N N     . PRO B 2 877  ? 143.162 153.153 159.422 1.00 44.73  ? 874  PRO A N     1 
ATOM   7062  C CA    . PRO B 2 877  ? 141.913 153.009 158.668 1.00 44.73  ? 874  PRO A CA    1 
ATOM   7063  C C     . PRO B 2 877  ? 140.840 153.985 159.124 1.00 44.73  ? 874  PRO A C     1 
ATOM   7064  O O     . PRO B 2 877  ? 140.683 154.277 160.311 1.00 44.73  ? 874  PRO A O     1 
ATOM   7065  C CB    . PRO B 2 877  ? 141.504 151.564 158.974 1.00 44.73  ? 874  PRO A CB    1 
ATOM   7066  C CG    . PRO B 2 877  ? 142.025 151.324 160.348 1.00 44.73  ? 874  PRO A CG    1 
ATOM   7067  C CD    . PRO B 2 877  ? 143.227 152.219 160.558 1.00 44.73  ? 874  PRO A CD    1 
ATOM   7068  N N     . ILE B 2 878  ? 140.091 154.500 158.150 1.00 44.73  ? 875  ILE A N     1 
ATOM   7069  C CA    . ILE B 2 878  ? 138.980 155.404 158.410 1.00 44.73  ? 875  ILE A CA    1 
ATOM   7070  C C     . ILE B 2 878  ? 137.752 154.887 157.674 1.00 44.73  ? 875  ILE A C     1 
ATOM   7071  O O     . ILE B 2 878  ? 137.849 154.167 156.679 1.00 44.73  ? 875  ILE A O     1 
ATOM   7072  C CB    . ILE B 2 878  ? 139.292 156.860 157.995 1.00 44.73  ? 875  ILE A CB    1 
ATOM   7073  C CG1   . ILE B 2 878  ? 139.301 157.003 156.474 1.00 44.73  ? 875  ILE A CG1   1 
ATOM   7074  C CG2   . ILE B 2 878  ? 140.621 157.312 158.574 1.00 44.73  ? 875  ILE A CG2   1 
ATOM   7075  C CD1   . ILE B 2 878  ? 139.375 158.429 155.997 1.00 44.73  ? 875  ILE A CD1   1 
ATOM   7076  N N     . THR B 2 879  ? 136.582 155.256 158.187 1.00 44.73  ? 876  THR A N     1 
ATOM   7077  C CA    . THR B 2 879  ? 135.308 154.851 157.610 1.00 44.73  ? 876  THR A CA    1 
ATOM   7078  C C     . THR B 2 879  ? 134.548 156.087 157.156 1.00 44.73  ? 876  THR A C     1 
ATOM   7079  O O     . THR B 2 879  ? 134.323 157.008 157.947 1.00 44.73  ? 876  THR A O     1 
ATOM   7080  C CB    . THR B 2 879  ? 134.471 154.053 158.615 1.00 44.73  ? 876  THR A CB    1 
ATOM   7081  O OG1   . THR B 2 879  ? 135.050 152.756 158.798 1.00 44.73  ? 876  THR A OG1   1 
ATOM   7082  C CG2   . THR B 2 879  ? 133.047 153.896 158.116 1.00 44.73  ? 876  THR A CG2   1 
ATOM   7083  N N     . LEU B 2 880  ? 134.153 156.100 155.889 1.00 44.73  ? 877  LEU A N     1 
ATOM   7084  C CA    . LEU B 2 880  ? 133.443 157.219 155.293 1.00 44.73  ? 877  LEU A CA    1 
ATOM   7085  C C     . LEU B 2 880  ? 131.967 156.878 155.135 1.00 44.73  ? 877  LEU A C     1 
ATOM   7086  O O     . LEU B 2 880  ? 131.598 155.716 154.948 1.00 44.73  ? 877  LEU A O     1 
ATOM   7087  C CB    . LEU B 2 880  ? 134.058 157.585 153.941 1.00 44.73  ? 877  LEU A CB    1 
ATOM   7088  C CG    . LEU B 2 880  ? 135.459 158.193 154.028 1.00 44.73  ? 877  LEU A CG    1 
ATOM   7089  C CD1   . LEU B 2 880  ? 136.326 157.746 152.868 1.00 44.73  ? 877  LEU A CD1   1 
ATOM   7090  C CD2   . LEU B 2 880  ? 135.369 159.707 154.069 1.00 44.73  ? 877  LEU A CD2   1 
ATOM   7091  N N     . ASN B 2 881  ? 131.126 157.911 155.220 1.00 44.73  ? 878  ASN A N     1 
ATOM   7092  C CA    . ASN B 2 881  ? 129.671 157.752 155.254 1.00 44.73  ? 878  ASN A CA    1 
ATOM   7093  C C     . ASN B 2 881  ? 129.255 156.852 156.417 1.00 44.73  ? 878  ASN A C     1 
ATOM   7094  O O     . ASN B 2 881  ? 128.559 155.850 156.244 1.00 44.73  ? 878  ASN A O     1 
ATOM   7095  C CB    . ASN B 2 881  ? 129.137 157.220 153.922 1.00 44.73  ? 878  ASN A CB    1 
ATOM   7096  C CG    . ASN B 2 881  ? 129.363 158.185 152.778 1.00 44.73  ? 878  ASN A CG    1 
ATOM   7097  O OD1   . ASN B 2 881  ? 130.160 157.923 151.879 1.00 44.73  ? 878  ASN A OD1   1 
ATOM   7098  N ND2   . ASN B 2 881  ? 128.662 159.310 152.807 1.00 44.73  ? 878  ASN A ND2   1 
ATOM   7099  N N     . TYR B 2 882  ? 129.691 157.230 157.621 1.00 44.73  ? 879  TYR A N     1 
ATOM   7100  C CA    . TYR B 2 882  ? 129.479 156.408 158.807 1.00 44.73  ? 879  TYR A CA    1 
ATOM   7101  C C     . TYR B 2 882  ? 128.009 156.300 159.194 1.00 44.73  ? 879  TYR A C     1 
ATOM   7102  O O     . TYR B 2 882  ? 127.634 155.354 159.894 1.00 44.73  ? 879  TYR A O     1 
ATOM   7103  C CB    . TYR B 2 882  ? 130.295 156.973 159.972 1.00 44.73  ? 879  TYR A CB    1 
ATOM   7104  C CG    . TYR B 2 882  ? 130.033 156.311 161.304 1.00 44.73  ? 879  TYR A CG    1 
ATOM   7105  C CD1   . TYR B 2 882  ? 130.411 154.998 161.535 1.00 44.73  ? 879  TYR A CD1   1 
ATOM   7106  C CD2   . TYR B 2 882  ? 129.408 157.002 162.332 1.00 44.73  ? 879  TYR A CD2   1 
ATOM   7107  C CE1   . TYR B 2 882  ? 130.170 154.389 162.750 1.00 44.73  ? 879  TYR A CE1   1 
ATOM   7108  C CE2   . TYR B 2 882  ? 129.166 156.403 163.551 1.00 44.73  ? 879  TYR A CE2   1 
ATOM   7109  C CZ    . TYR B 2 882  ? 129.549 155.097 163.755 1.00 44.73  ? 879  TYR A CZ    1 
ATOM   7110  O OH    . TYR B 2 882  ? 129.310 154.495 164.968 1.00 44.73  ? 879  TYR A OH    1 
ATOM   7111  N N     . GLN B 2 883  ? 127.169 157.228 158.746 1.00 44.73  ? 880  GLN A N     1 
ATOM   7112  C CA    . GLN B 2 883  ? 125.761 157.244 159.115 1.00 44.73  ? 880  GLN A CA    1 
ATOM   7113  C C     . GLN B 2 883  ? 124.892 156.412 158.180 1.00 44.73  ? 880  GLN A C     1 
ATOM   7114  O O     . GLN B 2 883  ? 123.667 156.413 158.330 1.00 44.73  ? 880  GLN A O     1 
ATOM   7115  C CB    . GLN B 2 883  ? 125.245 158.685 159.155 1.00 44.73  ? 880  GLN A CB    1 
ATOM   7116  C CG    . GLN B 2 883  ? 126.003 159.591 160.108 1.00 44.73  ? 880  GLN A CG    1 
ATOM   7117  C CD    . GLN B 2 883  ? 125.551 159.437 161.547 1.00 44.73  ? 880  GLN A CD    1 
ATOM   7118  O OE1   . GLN B 2 883  ? 124.686 158.619 161.854 1.00 44.73  ? 880  GLN A OE1   1 
ATOM   7119  N NE2   . GLN B 2 883  ? 126.137 160.227 162.438 1.00 44.73  ? 880  GLN A NE2   1 
ATOM   7120  N N     . ALA B 2 884  ? 125.491 155.709 157.226 1.00 44.73  ? 881  ALA A N     1 
ATOM   7121  C CA    . ALA B 2 884  ? 124.758 154.899 156.271 1.00 44.73  ? 881  ALA A CA    1 
ATOM   7122  C C     . ALA B 2 884  ? 124.843 153.425 156.661 1.00 44.73  ? 881  ALA A C     1 
ATOM   7123  O O     . ALA B 2 884  ? 125.418 153.060 157.691 1.00 44.73  ? 881  ALA A O     1 
ATOM   7124  C CB    . ALA B 2 884  ? 125.294 155.146 154.860 1.00 44.73  ? 881  ALA A CB    1 
ATOM   7125  N N     . ALA B 2 885  ? 124.263 152.563 155.832 1.00 44.73  ? 882  ALA A N     1 
ATOM   7126  C CA    . ALA B 2 885  ? 124.252 151.136 156.100 1.00 44.73  ? 882  ALA A CA    1 
ATOM   7127  C C     . ALA B 2 885  ? 125.609 150.514 155.782 1.00 44.73  ? 882  ALA A C     1 
ATOM   7128  O O     . ALA B 2 885  ? 126.455 151.109 155.110 1.00 44.73  ? 882  ALA A O     1 
ATOM   7129  C CB    . ALA B 2 885  ? 123.156 150.444 155.290 1.00 44.73  ? 882  ALA A CB    1 
ATOM   7130  N N     . ASN B 2 886  ? 125.810 149.295 156.289 1.00 44.73  ? 883  ASN A N     1 
ATOM   7131  C CA    . ASN B 2 886  ? 127.070 148.594 156.061 1.00 44.73  ? 883  ASN A CA    1 
ATOM   7132  C C     . ASN B 2 886  ? 127.266 148.263 154.587 1.00 44.73  ? 883  ASN A C     1 
ATOM   7133  O O     . ASN B 2 886  ? 128.368 148.427 154.051 1.00 44.73  ? 883  ASN A O     1 
ATOM   7134  C CB    . ASN B 2 886  ? 127.122 147.323 156.906 1.00 44.73  ? 883  ASN A CB    1 
ATOM   7135  C CG    . ASN B 2 886  ? 127.070 147.609 158.393 1.00 44.73  ? 883  ASN A CG    1 
ATOM   7136  O OD1   . ASN B 2 886  ? 126.869 148.748 158.811 1.00 44.73  ? 883  ASN A OD1   1 
ATOM   7137  N ND2   . ASN B 2 886  ? 127.251 146.571 159.201 1.00 44.73  ? 883  ASN A ND2   1 
ATOM   7138  N N     . SER B 2 887  ? 126.218 147.796 153.919 1.00 44.73  ? 884  SER A N     1 
ATOM   7139  C CA    . SER B 2 887  ? 126.290 147.404 152.521 1.00 44.73  ? 884  SER A CA    1 
ATOM   7140  C C     . SER B 2 887  ? 125.116 148.010 151.768 1.00 44.73  ? 884  SER A C     1 
ATOM   7141  O O     . SER B 2 887  ? 124.051 148.237 152.354 1.00 44.73  ? 884  SER A O     1 
ATOM   7142  C CB    . SER B 2 887  ? 126.272 145.875 152.364 1.00 44.73  ? 884  SER A CB    1 
ATOM   7143  O OG    . SER B 2 887  ? 127.416 145.287 152.959 1.00 44.73  ? 884  SER A OG    1 
ATOM   7144  N N     . PRO B 2 888  ? 125.283 148.291 150.478 1.00 44.73  ? 885  PRO A N     1 
ATOM   7145  C CA    . PRO B 2 888  ? 124.162 148.813 149.691 1.00 44.73  ? 885  PRO A CA    1 
ATOM   7146  C C     . PRO B 2 888  ? 123.047 147.789 149.563 1.00 44.73  ? 885  PRO A C     1 
ATOM   7147  O O     . PRO B 2 888  ? 123.280 146.578 149.538 1.00 44.73  ? 885  PRO A O     1 
ATOM   7148  C CB    . PRO B 2 888  ? 124.796 149.119 148.330 1.00 44.73  ? 885  PRO A CB    1 
ATOM   7149  C CG    . PRO B 2 888  ? 125.993 148.235 148.268 1.00 44.73  ? 885  PRO A CG    1 
ATOM   7150  C CD    . PRO B 2 888  ? 126.506 148.155 149.671 1.00 44.73  ? 885  PRO A CD    1 
ATOM   7151  N N     . SER B 2 889  ? 121.820 148.293 149.481 1.00 44.73  ? 886  SER A N     1 
ATOM   7152  C CA    . SER B 2 889  ? 120.625 147.460 149.364 1.00 44.73  ? 886  SER A CA    1 
ATOM   7153  C C     . SER B 2 889  ? 119.934 147.811 148.051 1.00 44.73  ? 886  SER A C     1 
ATOM   7154  O O     . SER B 2 889  ? 119.215 148.812 147.970 1.00 44.73  ? 886  SER A O     1 
ATOM   7155  C CB    . SER B 2 889  ? 119.695 147.663 150.557 1.00 44.73  ? 886  SER A CB    1 
ATOM   7156  O OG    . SER B 2 889  ? 120.337 147.311 151.770 1.00 44.73  ? 886  SER A OG    1 
ATOM   7157  N N     . LYS B 2 890  ? 120.153 146.982 147.029 1.00 44.73  ? 887  LYS A N     1 
ATOM   7158  C CA    . LYS B 2 890  ? 119.566 147.172 145.703 1.00 44.73  ? 887  LYS A CA    1 
ATOM   7159  C C     . LYS B 2 890  ? 119.927 148.549 145.142 1.00 44.73  ? 887  LYS A C     1 
ATOM   7160  O O     . LYS B 2 890  ? 119.069 149.392 144.874 1.00 44.73  ? 887  LYS A O     1 
ATOM   7161  C CB    . LYS B 2 890  ? 118.048 146.965 145.739 1.00 44.73  ? 887  LYS A CB    1 
ATOM   7162  C CG    . LYS B 2 890  ? 117.614 145.632 146.327 1.00 44.73  ? 887  LYS A CG    1 
ATOM   7163  C CD    . LYS B 2 890  ? 118.407 144.475 145.737 1.00 44.73  ? 887  LYS A CD    1 
ATOM   7164  C CE    . LYS B 2 890  ? 117.906 144.112 144.348 1.00 44.73  ? 887  LYS A CE    1 
ATOM   7165  N NZ    . LYS B 2 890  ? 118.830 143.173 143.653 1.00 44.73  ? 887  LYS A NZ    1 
ATOM   7166  N N     . PHE B 2 891  ? 121.234 148.764 144.976 1.00 44.73  ? 888  PHE A N     1 
ATOM   7167  C CA    . PHE B 2 891  ? 121.714 150.054 144.492 1.00 44.73  ? 888  PHE A CA    1 
ATOM   7168  C C     . PHE B 2 891  ? 121.294 150.299 143.049 1.00 44.73  ? 888  PHE A C     1 
ATOM   7169  O O     . PHE B 2 891  ? 120.982 151.434 142.671 1.00 44.73  ? 888  PHE A O     1 
ATOM   7170  C CB    . PHE B 2 891  ? 123.233 150.134 144.627 1.00 44.73  ? 888  PHE A CB    1 
ATOM   7171  C CG    . PHE B 2 891  ? 123.781 151.510 144.409 1.00 44.73  ? 888  PHE A CG    1 
ATOM   7172  C CD1   . PHE B 2 891  ? 123.268 152.589 145.101 1.00 44.73  ? 888  PHE A CD1   1 
ATOM   7173  C CD2   . PHE B 2 891  ? 124.802 151.726 143.505 1.00 44.73  ? 888  PHE A CD2   1 
ATOM   7174  C CE1   . PHE B 2 891  ? 123.766 153.856 144.898 1.00 44.73  ? 888  PHE A CE1   1 
ATOM   7175  C CE2   . PHE B 2 891  ? 125.301 152.992 143.299 1.00 44.73  ? 888  PHE A CE2   1 
ATOM   7176  C CZ    . PHE B 2 891  ? 124.784 154.058 143.997 1.00 44.73  ? 888  PHE A CZ    1 
ATOM   7177  N N     . ASN B 2 892  ? 121.287 149.249 142.225 1.00 44.73  ? 889  ASN A N     1 
ATOM   7178  C CA    . ASN B 2 892  ? 120.909 149.413 140.826 1.00 44.73  ? 889  ASN A CA    1 
ATOM   7179  C C     . ASN B 2 892  ? 119.456 149.845 140.683 1.00 44.73  ? 889  ASN A C     1 
ATOM   7180  O O     . ASN B 2 892  ? 119.109 150.544 139.724 1.00 44.73  ? 889  ASN A O     1 
ATOM   7181  C CB    . ASN B 2 892  ? 121.157 148.116 140.058 1.00 44.73  ? 889  ASN A CB    1 
ATOM   7182  C CG    . ASN B 2 892  ? 122.624 147.886 139.764 1.00 44.73  ? 889  ASN A CG    1 
ATOM   7183  O OD1   . ASN B 2 892  ? 123.436 148.808 139.843 1.00 44.73  ? 889  ASN A OD1   1 
ATOM   7184  N ND2   . ASN B 2 892  ? 122.973 146.652 139.421 1.00 44.73  ? 889  ASN A ND2   1 
ATOM   7185  N N     . GLN B 2 893  ? 118.594 149.436 141.616 1.00 44.73  ? 890  GLN A N     1 
ATOM   7186  C CA    . GLN B 2 893  ? 117.198 149.861 141.569 1.00 44.73  ? 890  GLN A CA    1 
ATOM   7187  C C     . GLN B 2 893  ? 117.074 151.366 141.766 1.00 44.73  ? 890  GLN A C     1 
ATOM   7188  O O     . GLN B 2 893  ? 116.252 152.019 141.113 1.00 44.73  ? 890  GLN A O     1 
ATOM   7189  C CB    . GLN B 2 893  ? 116.386 149.111 142.623 1.00 44.73  ? 890  GLN A CB    1 
ATOM   7190  C CG    . GLN B 2 893  ? 115.798 147.796 142.136 1.00 44.73  ? 890  GLN A CG    1 
ATOM   7191  C CD    . GLN B 2 893  ? 116.860 146.754 141.840 1.00 44.73  ? 890  GLN A CD    1 
ATOM   7192  O OE1   . GLN B 2 893  ? 117.956 146.790 142.401 1.00 44.73  ? 890  GLN A OE1   1 
ATOM   7193  N NE2   . GLN B 2 893  ? 116.540 145.819 140.954 1.00 44.73  ? 890  GLN A NE2   1 
ATOM   7194  N N     . ARG B 2 894  ? 117.877 151.934 142.669 1.00 44.73  ? 891  ARG A N     1 
ATOM   7195  C CA    . ARG B 2 894  ? 117.857 153.379 142.873 1.00 44.73  ? 891  ARG A CA    1 
ATOM   7196  C C     . ARG B 2 894  ? 118.323 154.120 141.626 1.00 44.73  ? 891  ARG A C     1 
ATOM   7197  O O     . ARG B 2 894  ? 117.730 155.134 141.239 1.00 44.73  ? 891  ARG A O     1 
ATOM   7198  C CB    . ARG B 2 894  ? 118.728 153.754 144.070 1.00 44.73  ? 891  ARG A CB    1 
ATOM   7199  C CG    . ARG B 2 894  ? 117.990 153.780 145.394 1.00 44.73  ? 891  ARG A CG    1 
ATOM   7200  C CD    . ARG B 2 894  ? 118.961 153.863 146.559 1.00 44.73  ? 891  ARG A CD    1 
ATOM   7201  N NE    . ARG B 2 894  ? 119.356 155.239 146.834 1.00 44.73  ? 891  ARG A NE    1 
ATOM   7202  C CZ    . ARG B 2 894  ? 118.609 156.117 147.489 1.00 44.73  ? 891  ARG A CZ    1 
ATOM   7203  N NH1   . ARG B 2 894  ? 117.419 155.792 147.967 1.00 44.73  ? 891  ARG A NH1   1 
ATOM   7204  N NH2   . ARG B 2 894  ? 119.068 157.352 147.669 1.00 44.73  ? 891  ARG A NH2   1 
ATOM   7205  N N     . VAL B 2 895  ? 119.390 153.635 140.989 1.00 44.73  ? 892  VAL A N     1 
ATOM   7206  C CA    . VAL B 2 895  ? 119.901 154.285 139.785 1.00 44.73  ? 892  VAL A CA    1 
ATOM   7207  C C     . VAL B 2 895  ? 118.880 154.189 138.660 1.00 44.73  ? 892  VAL A C     1 
ATOM   7208  O O     . VAL B 2 895  ? 118.617 155.166 137.948 1.00 44.73  ? 892  VAL A O     1 
ATOM   7209  C CB    . VAL B 2 895  ? 121.251 153.672 139.375 1.00 44.73  ? 892  VAL A CB    1 
ATOM   7210  C CG1   . VAL B 2 895  ? 121.696 154.222 138.031 1.00 44.73  ? 892  VAL A CG1   1 
ATOM   7211  C CG2   . VAL B 2 895  ? 122.300 153.937 140.441 1.00 44.73  ? 892  VAL A CG2   1 
ATOM   7212  N N     . ASN B 2 896  ? 118.288 153.006 138.484 1.00 44.73  ? 893  ASN A N     1 
ATOM   7213  C CA    . ASN B 2 896  ? 117.271 152.831 137.454 1.00 44.73  ? 893  ASN A CA    1 
ATOM   7214  C C     . ASN B 2 896  ? 116.048 153.698 137.721 1.00 44.73  ? 893  ASN A C     1 
ATOM   7215  O O     . ASN B 2 896  ? 115.406 154.169 136.775 1.00 44.73  ? 893  ASN A O     1 
ATOM   7216  C CB    . ASN B 2 896  ? 116.872 151.360 137.359 1.00 44.73  ? 893  ASN A CB    1 
ATOM   7217  C CG    . ASN B 2 896  ? 117.911 150.519 136.647 1.00 44.73  ? 893  ASN A CG    1 
ATOM   7218  O OD1   . ASN B 2 896  ? 119.095 150.853 136.635 1.00 44.73  ? 893  ASN A OD1   1 
ATOM   7219  N ND2   . ASN B 2 896  ? 117.474 149.411 136.061 1.00 44.73  ? 893  ASN A ND2   1 
ATOM   7220  N N     . ALA B 2 897  ? 115.708 153.914 138.993 1.00 44.73  ? 894  ALA A N     1 
ATOM   7221  C CA    . ALA B 2 897  ? 114.586 154.787 139.321 1.00 44.73  ? 894  ALA A CA    1 
ATOM   7222  C C     . ALA B 2 897  ? 114.879 156.226 138.918 1.00 44.73  ? 894  ALA A C     1 
ATOM   7223  O O     . ALA B 2 897  ? 114.025 156.910 138.342 1.00 44.73  ? 894  ALA A O     1 
ATOM   7224  C CB    . ALA B 2 897  ? 114.269 154.696 140.813 1.00 44.73  ? 894  ALA A CB    1 
ATOM   7225  N N     . TYR B 2 898  ? 116.088 156.706 139.218 1.00 44.73  ? 895  TYR A N     1 
ATOM   7226  C CA    . TYR B 2 898  ? 116.466 158.061 138.830 1.00 44.73  ? 895  TYR A CA    1 
ATOM   7227  C C     . TYR B 2 898  ? 116.532 158.203 137.315 1.00 44.73  ? 895  TYR A C     1 
ATOM   7228  O O     . TYR B 2 898  ? 116.099 159.219 136.760 1.00 44.73  ? 895  TYR A O     1 
ATOM   7229  C CB    . TYR B 2 898  ? 117.806 158.432 139.462 1.00 44.73  ? 895  TYR A CB    1 
ATOM   7230  C CG    . TYR B 2 898  ? 118.457 159.653 138.858 1.00 44.73  ? 895  TYR A CG    1 
ATOM   7231  C CD1   . TYR B 2 898  ? 117.983 160.925 139.137 1.00 44.73  ? 895  TYR A CD1   1 
ATOM   7232  C CD2   . TYR B 2 898  ? 119.552 159.535 138.014 1.00 44.73  ? 895  TYR A CD2   1 
ATOM   7233  C CE1   . TYR B 2 898  ? 118.577 162.044 138.590 1.00 44.73  ? 895  TYR A CE1   1 
ATOM   7234  C CE2   . TYR B 2 898  ? 120.151 160.649 137.462 1.00 44.73  ? 895  TYR A CE2   1 
ATOM   7235  C CZ    . TYR B 2 898  ? 119.660 161.900 137.754 1.00 44.73  ? 895  TYR A CZ    1 
ATOM   7236  O OH    . TYR B 2 898  ? 120.255 163.012 137.206 1.00 44.73  ? 895  TYR A OH    1 
ATOM   7237  N N     . LEU B 2 899  ? 117.075 157.194 136.630 1.00 44.73  ? 896  LEU A N     1 
ATOM   7238  C CA    . LEU B 2 899  ? 117.188 157.260 135.178 1.00 44.73  ? 896  LEU A CA    1 
ATOM   7239  C C     . LEU B 2 899  ? 115.817 157.261 134.513 1.00 44.73  ? 896  LEU A C     1 
ATOM   7240  O O     . LEU B 2 899  ? 115.611 157.946 133.504 1.00 44.73  ? 896  LEU A O     1 
ATOM   7241  C CB    . LEU B 2 899  ? 118.035 156.096 134.666 1.00 44.73  ? 896  LEU A CB    1 
ATOM   7242  C CG    . LEU B 2 899  ? 119.541 156.217 134.898 1.00 44.73  ? 896  LEU A CG    1 
ATOM   7243  C CD1   . LEU B 2 899  ? 120.228 154.880 134.687 1.00 44.73  ? 896  LEU A CD1   1 
ATOM   7244  C CD2   . LEU B 2 899  ? 120.138 157.277 133.989 1.00 44.73  ? 896  LEU A CD2   1 
ATOM   7245  N N     . LYS B 2 900  ? 114.870 156.493 135.056 1.00 44.73  ? 897  LYS A N     1 
ATOM   7246  C CA    . LYS B 2 900  ? 113.535 156.443 134.468 1.00 44.73  ? 897  LYS A CA    1 
ATOM   7247  C C     . LYS B 2 900  ? 112.837 157.794 134.561 1.00 44.73  ? 897  LYS A C     1 
ATOM   7248  O O     . LYS B 2 900  ? 112.171 158.223 133.611 1.00 44.73  ? 897  LYS A O     1 
ATOM   7249  C CB    . LYS B 2 900  ? 112.701 155.360 135.149 1.00 44.73  ? 897  LYS A CB    1 
ATOM   7250  C CG    . LYS B 2 900  ? 111.314 155.186 134.556 1.00 44.73  ? 897  LYS A CG    1 
ATOM   7251  C CD    . LYS B 2 900  ? 110.707 153.843 134.928 1.00 44.73  ? 897  LYS A CD    1 
ATOM   7252  C CE    . LYS B 2 900  ? 111.736 152.726 134.869 1.00 44.73  ? 897  LYS A CE    1 
ATOM   7253  N NZ    . LYS B 2 900  ? 111.092 151.385 134.911 1.00 44.73  ? 897  LYS A NZ    1 
ATOM   7254  N N     . GLU B 2 901  ? 112.976 158.479 135.695 1.00 44.73  ? 898  GLU A N     1 
ATOM   7255  C CA    . GLU B 2 901  ? 112.375 159.795 135.862 1.00 44.73  ? 898  GLU A CA    1 
ATOM   7256  C C     . GLU B 2 901  ? 113.187 160.904 135.208 1.00 44.73  ? 898  GLU A C     1 
ATOM   7257  O O     . GLU B 2 901  ? 112.721 162.047 135.166 1.00 44.73  ? 898  GLU A O     1 
ATOM   7258  C CB    . GLU B 2 901  ? 112.189 160.109 137.351 1.00 44.73  ? 898  GLU A CB    1 
ATOM   7259  C CG    . GLU B 2 901  ? 111.520 159.014 138.199 1.00 44.73  ? 898  GLU A CG    1 
ATOM   7260  C CD    . GLU B 2 901  ? 110.440 158.209 137.480 1.00 44.73  ? 898  GLU A CD    1 
ATOM   7261  O OE1   . GLU B 2 901  ? 109.709 158.765 136.630 1.00 44.73  ? 898  GLU A OE1   1 
ATOM   7262  O OE2   . GLU B 2 901  ? 110.275 157.020 137.823 1.00 44.73  ? 898  GLU A OE2   1 
ATOM   7263  N N     . HIS B 2 902  ? 114.378 160.599 134.699 1.00 44.73  ? 899  HIS A N     1 
ATOM   7264  C CA    . HIS B 2 902  ? 115.244 161.581 134.048 1.00 44.73  ? 899  HIS A CA    1 
ATOM   7265  C C     . HIS B 2 902  ? 115.640 161.048 132.679 1.00 44.73  ? 899  HIS A C     1 
ATOM   7266  O O     . HIS B 2 902  ? 116.765 160.567 132.486 1.00 44.73  ? 899  HIS A O     1 
ATOM   7267  C CB    . HIS B 2 902  ? 116.477 161.882 134.900 1.00 44.73  ? 899  HIS A CB    1 
ATOM   7268  C CG    . HIS B 2 902  ? 116.210 162.810 136.043 1.00 44.73  ? 899  HIS A CG    1 
ATOM   7269  N ND1   . HIS B 2 902  ? 115.421 162.460 137.117 1.00 44.73  ? 899  HIS A ND1   1 
ATOM   7270  C CD2   . HIS B 2 902  ? 116.628 164.076 136.281 1.00 44.73  ? 899  HIS A CD2   1 
ATOM   7271  C CE1   . HIS B 2 902  ? 115.365 163.470 137.967 1.00 44.73  ? 899  HIS A CE1   1 
ATOM   7272  N NE2   . HIS B 2 902  ? 116.088 164.462 137.483 1.00 44.73  ? 899  HIS A NE2   1 
ATOM   7273  N N     . PRO B 2 903  ? 114.733 161.110 131.700 1.00 44.73  ? 900  PRO A N     1 
ATOM   7274  C CA    . PRO B 2 903  ? 115.083 160.648 130.348 1.00 44.73  ? 900  PRO A CA    1 
ATOM   7275  C C     . PRO B 2 903  ? 116.166 161.478 129.684 1.00 44.73  ? 900  PRO A C     1 
ATOM   7276  O O     . PRO B 2 903  ? 116.788 161.004 128.726 1.00 44.73  ? 900  PRO A O     1 
ATOM   7277  C CB    . PRO B 2 903  ? 113.755 160.750 129.582 1.00 44.73  ? 900  PRO A CB    1 
ATOM   7278  C CG    . PRO B 2 903  ? 112.695 160.888 130.634 1.00 44.73  ? 900  PRO A CG    1 
ATOM   7279  C CD    . PRO B 2 903  ? 113.346 161.592 131.775 1.00 44.73  ? 900  PRO A CD    1 
ATOM   7280  N N     . GLU B 2 904  ? 116.414 162.696 130.158 1.00 44.73  ? 901  GLU A N     1 
ATOM   7281  C CA    . GLU B 2 904  ? 117.389 163.587 129.545 1.00 44.73  ? 901  GLU A CA    1 
ATOM   7282  C C     . GLU B 2 904  ? 118.803 163.373 130.067 1.00 44.73  ? 901  GLU A C     1 
ATOM   7283  O O     . GLU B 2 904  ? 119.680 164.194 129.777 1.00 44.73  ? 901  GLU A O     1 
ATOM   7284  C CB    . GLU B 2 904  ? 116.978 165.047 129.761 1.00 44.73  ? 901  GLU A CB    1 
ATOM   7285  C CG    . GLU B 2 904  ? 117.080 165.522 131.204 1.00 44.73  ? 901  GLU A CG    1 
ATOM   7286  C CD    . GLU B 2 904  ? 115.849 165.191 132.027 1.00 44.73  ? 901  GLU A CD    1 
ATOM   7287  O OE1   . GLU B 2 904  ? 115.043 164.345 131.589 1.00 44.73  ? 901  GLU A OE1   1 
ATOM   7288  O OE2   . GLU B 2 904  ? 115.688 165.781 133.117 1.00 44.73  ? 901  GLU A OE2   1 
ATOM   7289  N N     . THR B 2 905  ? 119.045 162.308 130.821 1.00 44.73  ? 902  THR A N     1 
ATOM   7290  C CA    . THR B 2 905  ? 120.378 162.054 131.359 1.00 44.73  ? 902  THR A CA    1 
ATOM   7291  C C     . THR B 2 905  ? 121.347 161.768 130.221 1.00 44.73  ? 902  THR A C     1 
ATOM   7292  O O     . THR B 2 905  ? 121.119 160.830 129.447 1.00 44.73  ? 902  THR A O     1 
ATOM   7293  C CB    . THR B 2 905  ? 120.349 160.880 132.332 1.00 44.73  ? 902  THR A CB    1 
ATOM   7294  O OG1   . THR B 2 905  ? 119.528 161.210 133.458 1.00 44.73  ? 902  THR A OG1   1 
ATOM   7295  C CG2   . THR B 2 905  ? 121.753 160.557 132.813 1.00 44.73  ? 902  THR A CG2   1 
ATOM   7296  N N     . PRO B 2 906  ? 122.422 162.534 130.076 1.00 44.73  ? 903  PRO A N     1 
ATOM   7297  C CA    . PRO B 2 906  ? 123.358 162.289 128.976 1.00 44.73  ? 903  PRO A CA    1 
ATOM   7298  C C     . PRO B 2 906  ? 124.192 161.039 129.215 1.00 44.73  ? 903  PRO A C     1 
ATOM   7299  O O     . PRO B 2 906  ? 124.225 160.471 130.308 1.00 44.73  ? 903  PRO A O     1 
ATOM   7300  C CB    . PRO B 2 906  ? 124.232 163.547 128.953 1.00 44.73  ? 903  PRO A CB    1 
ATOM   7301  C CG    . PRO B 2 906  ? 124.074 164.166 130.287 1.00 44.73  ? 903  PRO A CG    1 
ATOM   7302  C CD    . PRO B 2 906  ? 122.753 163.744 130.846 1.00 44.73  ? 903  PRO A CD    1 
ATOM   7303  N N     . ILE B 2 907  ? 124.862 160.607 128.152 1.00 44.73  ? 904  ILE A N     1 
ATOM   7304  C CA    . ILE B 2 907  ? 125.680 159.405 128.170 1.00 44.73  ? 904  ILE A CA    1 
ATOM   7305  C C     . ILE B 2 907  ? 127.136 159.814 127.989 1.00 44.73  ? 904  ILE A C     1 
ATOM   7306  O O     . ILE B 2 907  ? 127.447 160.899 127.492 1.00 44.73  ? 904  ILE A O     1 
ATOM   7307  C CB    . ILE B 2 907  ? 125.247 158.408 127.074 1.00 44.73  ? 904  ILE A CB    1 
ATOM   7308  C CG1   . ILE B 2 907  ? 123.724 158.369 126.957 1.00 44.73  ? 904  ILE A CG1   1 
ATOM   7309  C CG2   . ILE B 2 907  ? 125.761 157.016 127.374 1.00 44.73  ? 904  ILE A CG2   1 
ATOM   7310  C CD1   . ILE B 2 907  ? 123.033 157.827 128.174 1.00 44.73  ? 904  ILE A CD1   1 
ATOM   7311  N N     . ILE B 2 908  ? 128.041 158.935 128.413 1.00 44.73  ? 905  ILE A N     1 
ATOM   7312  C CA    . ILE B 2 908  ? 129.475 159.110 128.208 1.00 44.73  ? 905  ILE A CA    1 
ATOM   7313  C C     . ILE B 2 908  ? 130.023 157.791 127.683 1.00 44.73  ? 905  ILE A C     1 
ATOM   7314  O O     . ILE B 2 908  ? 130.058 156.794 128.414 1.00 44.73  ? 905  ILE A O     1 
ATOM   7315  C CB    . ILE B 2 908  ? 130.207 159.530 129.489 1.00 44.73  ? 905  ILE A CB    1 
ATOM   7316  C CG1   . ILE B 2 908  ? 129.768 160.927 129.921 1.00 44.73  ? 905  ILE A CG1   1 
ATOM   7317  C CG2   . ILE B 2 908  ? 131.710 159.492 129.278 1.00 44.73  ? 905  ILE A CG2   1 
ATOM   7318  C CD1   . ILE B 2 908  ? 130.444 161.413 131.178 1.00 44.73  ? 905  ILE A CD1   1 
ATOM   7319  N N     . GLY B 2 909  ? 130.451 157.781 126.424 1.00 44.73  ? 906  GLY A N     1 
ATOM   7320  C CA    . GLY B 2 909  ? 131.007 156.591 125.807 1.00 44.73  ? 906  GLY A CA    1 
ATOM   7321  C C     . GLY B 2 909  ? 132.521 156.674 125.753 1.00 44.73  ? 906  GLY A C     1 
ATOM   7322  O O     . GLY B 2 909  ? 133.084 157.696 125.358 1.00 44.73  ? 906  GLY A O     1 
ATOM   7323  N N     . ILE B 2 910  ? 133.170 155.587 126.156 1.00 44.73  ? 907  ILE A N     1 
ATOM   7324  C CA    . ILE B 2 910  ? 134.624 155.515 126.190 1.00 44.73  ? 907  ILE A CA    1 
ATOM   7325  C C     . ILE B 2 910  ? 135.074 154.333 125.346 1.00 44.73  ? 907  ILE A C     1 
ATOM   7326  O O     . ILE B 2 910  ? 134.591 153.210 125.531 1.00 44.73  ? 907  ILE A O     1 
ATOM   7327  C CB    . ILE B 2 910  ? 135.158 155.392 127.629 1.00 44.73  ? 907  ILE A CB    1 
ATOM   7328  C CG1   . ILE B 2 910  ? 134.839 156.660 128.416 1.00 44.73  ? 907  ILE A CG1   1 
ATOM   7329  C CG2   . ILE B 2 910  ? 136.654 155.158 127.623 1.00 44.73  ? 907  ILE A CG2   1 
ATOM   7330  C CD1   . ILE B 2 910  ? 135.076 156.534 129.903 1.00 44.73  ? 907  ILE A CD1   1 
ATOM   7331  N N     . ASP B 2 911  ? 135.997 154.587 124.422 1.00 44.73  ? 908  ASP A N     1 
ATOM   7332  C CA    . ASP B 2 911  ? 136.531 153.562 123.539 1.00 44.73  ? 908  ASP A CA    1 
ATOM   7333  C C     . ASP B 2 911  ? 138.047 153.678 123.502 1.00 44.73  ? 908  ASP A C     1 
ATOM   7334  O O     . ASP B 2 911  ? 138.606 154.742 123.774 1.00 44.73  ? 908  ASP A O     1 
ATOM   7335  C CB    . ASP B 2 911  ? 135.960 153.685 122.120 1.00 44.73  ? 908  ASP A CB    1 
ATOM   7336  C CG    . ASP B 2 911  ? 136.054 152.390 121.348 1.00 44.73  ? 908  ASP A CG    1 
ATOM   7337  O OD1   . ASP B 2 911  ? 136.240 151.339 121.992 1.00 44.73  ? 908  ASP A OD1   1 
ATOM   7338  O OD2   . ASP B 2 911  ? 135.941 152.416 120.106 1.00 44.73  ? 908  ASP A OD2   1 
ATOM   7339  N N     . ARG B 2 912  ? 138.712 152.570 123.176 1.00 44.73  ? 909  ARG A N     1 
ATOM   7340  C CA    . ARG B 2 912  ? 140.166 152.556 123.026 1.00 44.73  ? 909  ARG A CA    1 
ATOM   7341  C C     . ARG B 2 912  ? 140.505 152.720 121.551 1.00 44.73  ? 909  ARG A C     1 
ATOM   7342  O O     . ARG B 2 912  ? 140.412 151.772 120.768 1.00 44.73  ? 909  ARG A O     1 
ATOM   7343  C CB    . ARG B 2 912  ? 140.773 151.274 123.581 1.00 44.73  ? 909  ARG A CB    1 
ATOM   7344  C CG    . ARG B 2 912  ? 140.622 151.099 125.066 1.00 44.73  ? 909  ARG A CG    1 
ATOM   7345  C CD    . ARG B 2 912  ? 141.401 149.883 125.544 1.00 44.73  ? 909  ARG A CD    1 
ATOM   7346  N NE    . ARG B 2 912  ? 140.944 148.600 125.031 1.00 44.73  ? 909  ARG A NE    1 
ATOM   7347  C CZ    . ARG B 2 912  ? 139.968 147.884 125.566 1.00 44.73  ? 909  ARG A CZ    1 
ATOM   7348  N NH1   . ARG B 2 912  ? 139.268 148.329 126.593 1.00 44.73  ? 909  ARG A NH1   1 
ATOM   7349  N NH2   . ARG B 2 912  ? 139.702 146.681 125.071 1.00 44.73  ? 909  ARG A NH2   1 
ATOM   7350  N N     . GLY B 2 913  ? 140.896 153.929 121.164 1.00 44.73  ? 910  GLY A N     1 
ATOM   7351  C CA    . GLY B 2 913  ? 141.289 154.191 119.799 1.00 44.73  ? 910  GLY A CA    1 
ATOM   7352  C C     . GLY B 2 913  ? 142.704 153.731 119.516 1.00 44.73  ? 910  GLY A C     1 
ATOM   7353  O O     . GLY B 2 913  ? 143.432 153.259 120.388 1.00 44.73  ? 910  GLY A O     1 
ATOM   7354  N N     . GLU B 2 914  ? 143.099 153.872 118.252 1.00 44.73  ? 911  GLU A N     1 
ATOM   7355  C CA    . GLU B 2 914  ? 144.448 153.519 117.831 1.00 44.73  ? 911  GLU A CA    1 
ATOM   7356  C C     . GLU B 2 914  ? 145.384 154.720 117.835 1.00 44.73  ? 911  GLU A C     1 
ATOM   7357  O O     . GLU B 2 914  ? 146.507 154.625 118.338 1.00 44.73  ? 911  GLU A O     1 
ATOM   7358  C CB    . GLU B 2 914  ? 144.418 152.872 116.441 1.00 44.73  ? 911  GLU A CB    1 
ATOM   7359  C CG    . GLU B 2 914  ? 143.728 151.516 116.409 1.00 44.73  ? 911  GLU A CG    1 
ATOM   7360  C CD    . GLU B 2 914  ? 143.700 150.913 115.020 1.00 44.73  ? 911  GLU A CD    1 
ATOM   7361  O OE1   . GLU B 2 914  ? 144.107 151.605 114.064 1.00 44.73  ? 911  GLU A OE1   1 
ATOM   7362  O OE2   . GLU B 2 914  ? 143.265 149.751 114.878 1.00 44.73  ? 911  GLU A OE2   1 
ATOM   7363  N N     . ARG B 2 915  ? 144.943 155.850 117.292 1.00 44.73  ? 912  ARG A N     1 
ATOM   7364  C CA    . ARG B 2 915  ? 145.700 157.090 117.366 1.00 44.73  ? 912  ARG A CA    1 
ATOM   7365  C C     . ARG B 2 915  ? 145.406 157.884 118.632 1.00 44.73  ? 912  ARG A C     1 
ATOM   7366  O O     . ARG B 2 915  ? 146.034 158.925 118.855 1.00 44.73  ? 912  ARG A O     1 
ATOM   7367  C CB    . ARG B 2 915  ? 145.422 157.961 116.137 1.00 44.73  ? 912  ARG A CB    1 
ATOM   7368  C CG    . ARG B 2 915  ? 145.842 157.348 114.805 1.00 44.73  ? 912  ARG A CG    1 
ATOM   7369  C CD    . ARG B 2 915  ? 147.353 157.389 114.592 1.00 44.73  ? 912  ARG A CD    1 
ATOM   7370  N NE    . ARG B 2 915  ? 148.069 156.408 115.398 1.00 44.73  ? 912  ARG A NE    1 
ATOM   7371  C CZ    . ARG B 2 915  ? 148.145 155.115 115.112 1.00 44.73  ? 912  ARG A CZ    1 
ATOM   7372  N NH1   . ARG B 2 915  ? 147.567 154.611 114.033 1.00 44.73  ? 912  ARG A NH1   1 
ATOM   7373  N NH2   . ARG B 2 915  ? 148.815 154.308 115.928 1.00 44.73  ? 912  ARG A NH2   1 
ATOM   7374  N N     . ASN B 2 916  ? 144.471 157.425 119.460 1.00 44.73  ? 913  ASN A N     1 
ATOM   7375  C CA    . ASN B 2 916  ? 144.190 158.041 120.748 1.00 44.73  ? 913  ASN A CA    1 
ATOM   7376  C C     . ASN B 2 916  ? 144.058 156.943 121.789 1.00 44.73  ? 913  ASN A C     1 
ATOM   7377  O O     . ASN B 2 916  ? 143.351 155.957 121.562 1.00 44.73  ? 913  ASN A O     1 
ATOM   7378  C CB    . ASN B 2 916  ? 142.914 158.885 120.695 1.00 44.73  ? 913  ASN A CB    1 
ATOM   7379  C CG    . ASN B 2 916  ? 142.993 159.992 119.668 1.00 44.73  ? 913  ASN A CG    1 
ATOM   7380  O OD1   . ASN B 2 916  ? 143.863 160.859 119.741 1.00 44.73  ? 913  ASN A OD1   1 
ATOM   7381  N ND2   . ASN B 2 916  ? 142.084 159.969 118.702 1.00 44.73  ? 913  ASN A ND2   1 
ATOM   7382  N N     . LEU B 2 917  ? 144.741 157.109 122.924 1.00 44.73  ? 914  LEU A N     1 
ATOM   7383  C CA    . LEU B 2 917  ? 144.720 156.076 123.954 1.00 44.73  ? 914  LEU A CA    1 
ATOM   7384  C C     . LEU B 2 917  ? 143.313 155.879 124.505 1.00 44.73  ? 914  LEU A C     1 
ATOM   7385  O O     . LEU B 2 917  ? 142.790 154.758 124.525 1.00 44.73  ? 914  LEU A O     1 
ATOM   7386  C CB    . LEU B 2 917  ? 145.690 156.440 125.080 1.00 44.73  ? 914  LEU A CB    1 
ATOM   7387  C CG    . LEU B 2 917  ? 147.162 156.081 124.880 1.00 44.73  ? 914  LEU A CG    1 
ATOM   7388  C CD1   . LEU B 2 917  ? 148.036 156.822 125.871 1.00 44.73  ? 914  LEU A CD1   1 
ATOM   7389  C CD2   . LEU B 2 917  ? 147.378 154.581 124.997 1.00 44.73  ? 914  LEU A CD2   1 
ATOM   7390  N N     . ILE B 2 918  ? 142.682 156.961 124.947 1.00 44.73  ? 915  ILE A N     1 
ATOM   7391  C CA    . ILE B 2 918  ? 141.317 156.930 125.459 1.00 44.73  ? 915  ILE A CA    1 
ATOM   7392  C C     . ILE B 2 918  ? 140.560 158.077 124.812 1.00 44.73  ? 915  ILE A C     1 
ATOM   7393  O O     . ILE B 2 918  ? 141.044 159.214 124.803 1.00 44.73  ? 915  ILE A O     1 
ATOM   7394  C CB    . ILE B 2 918  ? 141.270 157.051 126.995 1.00 44.73  ? 915  ILE A CB    1 
ATOM   7395  C CG1   . ILE B 2 918  ? 141.980 155.864 127.649 1.00 44.73  ? 915  ILE A CG1   1 
ATOM   7396  C CG2   . ILE B 2 918  ? 139.833 157.151 127.481 1.00 44.73  ? 915  ILE A CG2   1 
ATOM   7397  C CD1   . ILE B 2 918  ? 141.181 154.587 127.628 1.00 44.73  ? 915  ILE A CD1   1 
ATOM   7398  N N     . TYR B 2 919  ? 139.383 157.789 124.270 1.00 44.73  ? 916  TYR A N     1 
ATOM   7399  C CA    . TYR B 2 919  ? 138.624 158.804 123.562 1.00 44.73  ? 916  TYR A CA    1 
ATOM   7400  C C     . TYR B 2 919  ? 137.222 158.829 124.153 1.00 44.73  ? 916  TYR A C     1 
ATOM   7401  O O     . TYR B 2 919  ? 136.690 157.784 124.538 1.00 44.73  ? 916  TYR A O     1 
ATOM   7402  C CB    . TYR B 2 919  ? 138.543 158.499 122.075 1.00 44.73  ? 916  TYR A CB    1 
ATOM   7403  C CG    . TYR B 2 919  ? 137.831 159.566 121.296 1.00 44.73  ? 916  TYR A CG    1 
ATOM   7404  C CD1   . TYR B 2 919  ? 138.477 160.755 120.997 1.00 44.73  ? 916  TYR A CD1   1 
ATOM   7405  C CD2   . TYR B 2 919  ? 136.500 159.439 120.947 1.00 44.73  ? 916  TYR A CD2   1 
ATOM   7406  C CE1   . TYR B 2 919  ? 137.851 161.751 120.301 1.00 44.73  ? 916  TYR A CE1   1 
ATOM   7407  C CE2   . TYR B 2 919  ? 135.853 160.443 120.274 1.00 44.73  ? 916  TYR A CE2   1 
ATOM   7408  C CZ    . TYR B 2 919  ? 136.535 161.592 119.943 1.00 44.73  ? 916  TYR A CZ    1 
ATOM   7409  O OH    . TYR B 2 919  ? 135.898 162.590 119.254 1.00 44.73  ? 916  TYR A OH    1 
ATOM   7410  N N     . ILE B 2 920  ? 136.618 160.013 124.217 1.00 44.73  ? 917  ILE A N     1 
ATOM   7411  C CA    . ILE B 2 920  ? 135.328 160.178 124.873 1.00 44.73  ? 917  ILE A CA    1 
ATOM   7412  C C     . ILE B 2 920  ? 134.346 160.831 123.910 1.00 44.73  ? 917  ILE A C     1 
ATOM   7413  O O     . ILE B 2 920  ? 134.727 161.540 122.976 1.00 44.73  ? 917  ILE A O     1 
ATOM   7414  C CB    . ILE B 2 920  ? 135.443 161.008 126.166 1.00 44.73  ? 917  ILE A CB    1 
ATOM   7415  C CG1   . ILE B 2 920  ? 135.959 162.408 125.845 1.00 44.73  ? 917  ILE A CG1   1 
ATOM   7416  C CG2   . ILE B 2 920  ? 136.368 160.326 127.151 1.00 44.73  ? 917  ILE A CG2   1 
ATOM   7417  C CD1   . ILE B 2 920  ? 135.901 163.364 127.006 1.00 44.73  ? 917  ILE A CD1   1 
ATOM   7418  N N     . THR B 2 921  ? 133.061 160.574 124.150 1.00 44.73  ? 918  THR A N     1 
ATOM   7419  C CA    . THR B 2 921  ? 131.987 161.191 123.380 1.00 44.73  ? 918  THR A CA    1 
ATOM   7420  C C     . THR B 2 921  ? 130.711 161.158 124.206 1.00 44.73  ? 918  THR A C     1 
ATOM   7421  O O     . THR B 2 921  ? 130.288 160.085 124.647 1.00 44.73  ? 918  THR A O     1 
ATOM   7422  C CB    . THR B 2 921  ? 131.768 160.473 122.046 1.00 44.73  ? 918  THR A CB    1 
ATOM   7423  O OG1   . THR B 2 921  ? 132.939 160.605 121.232 1.00 44.73  ? 918  THR A OG1   1 
ATOM   7424  C CG2   . THR B 2 921  ? 130.577 161.065 121.313 1.00 44.73  ? 918  THR A CG2   1 
ATOM   7425  N N     . VAL B 2 922  ? 130.100 162.323 124.406 1.00 44.73  ? 919  VAL A N     1 
ATOM   7426  C CA    . VAL B 2 922  ? 128.878 162.451 125.191 1.00 44.73  ? 919  VAL A CA    1 
ATOM   7427  C C     . VAL B 2 922  ? 127.708 162.707 124.250 1.00 44.73  ? 919  VAL A C     1 
ATOM   7428  O O     . VAL B 2 922  ? 127.807 163.515 123.319 1.00 44.73  ? 919  VAL A O     1 
ATOM   7429  C CB    . VAL B 2 922  ? 128.993 163.559 126.258 1.00 44.73  ? 919  VAL A CB    1 
ATOM   7430  C CG1   . VAL B 2 922  ? 130.130 163.250 127.213 1.00 44.73  ? 919  VAL A CG1   1 
ATOM   7431  C CG2   . VAL B 2 922  ? 129.206 164.915 125.621 1.00 44.73  ? 919  VAL A CG2   1 
ATOM   7432  N N     . ILE B 2 923  ? 126.609 161.989 124.474 1.00 44.73  ? 920  ILE A N     1 
ATOM   7433  C CA    . ILE B 2 923  ? 125.404 162.127 123.668 1.00 44.73  ? 920  ILE A CA    1 
ATOM   7434  C C     . ILE B 2 923  ? 124.208 162.315 124.589 1.00 44.73  ? 920  ILE A C     1 
ATOM   7435  O O     . ILE B 2 923  ? 124.215 161.886 125.747 1.00 44.73  ? 920  ILE A O     1 
ATOM   7436  C CB    . ILE B 2 923  ? 125.181 160.916 122.737 1.00 44.73  ? 920  ILE A CB    1 
ATOM   7437  C CG1   . ILE B 2 923  ? 124.967 159.644 123.553 1.00 44.73  ? 920  ILE A CG1   1 
ATOM   7438  C CG2   . ILE B 2 923  ? 126.350 160.746 121.786 1.00 44.73  ? 920  ILE A CG2   1 
ATOM   7439  C CD1   . ILE B 2 923  ? 124.474 158.485 122.727 1.00 44.73  ? 920  ILE A CD1   1 
ATOM   7440  N N     . ASP B 2 924  ? 123.175 162.961 124.063 1.00 44.73  ? 921  ASP A N     1 
ATOM   7441  C CA    . ASP B 2 924  ? 121.958 163.246 124.802 1.00 44.73  ? 921  ASP A CA    1 
ATOM   7442  C C     . ASP B 2 924  ? 120.912 162.171 124.516 1.00 44.73  ? 921  ASP A C     1 
ATOM   7443  O O     . ASP B 2 924  ? 121.203 161.128 123.924 1.00 44.73  ? 921  ASP A O     1 
ATOM   7444  C CB    . ASP B 2 924  ? 121.450 164.646 124.452 1.00 44.73  ? 921  ASP A CB    1 
ATOM   7445  C CG    . ASP B 2 924  ? 121.506 164.932 122.966 1.00 44.73  ? 921  ASP A CG    1 
ATOM   7446  O OD1   . ASP B 2 924  ? 121.857 164.015 122.195 1.00 44.73  ? 921  ASP A OD1   1 
ATOM   7447  O OD2   . ASP B 2 924  ? 121.199 166.075 122.569 1.00 44.73  ? 921  ASP A OD2   1 
ATOM   7448  N N     . SER B 2 925  ? 119.675 162.422 124.953 1.00 44.73  ? 922  SER A N     1 
ATOM   7449  C CA    . SER B 2 925  ? 118.605 161.452 124.750 1.00 44.73  ? 922  SER A CA    1 
ATOM   7450  C C     . SER B 2 925  ? 118.334 161.226 123.268 1.00 44.73  ? 922  SER A C     1 
ATOM   7451  O O     . SER B 2 925  ? 118.120 160.087 122.835 1.00 44.73  ? 922  SER A O     1 
ATOM   7452  C CB    . SER B 2 925  ? 117.334 161.915 125.461 1.00 44.73  ? 922  SER A CB    1 
ATOM   7453  O OG    . SER B 2 925  ? 116.829 163.105 124.880 1.00 44.73  ? 922  SER A OG    1 
ATOM   7454  N N     . THR B 2 926  ? 118.339 162.297 122.472 1.00 44.73  ? 923  THR A N     1 
ATOM   7455  C CA    . THR B 2 926  ? 118.090 162.148 121.042 1.00 44.73  ? 923  THR A CA    1 
ATOM   7456  C C     . THR B 2 926  ? 119.271 161.505 120.326 1.00 44.73  ? 923  THR A C     1 
ATOM   7457  O O     . THR B 2 926  ? 119.094 160.912 119.256 1.00 44.73  ? 923  THR A O     1 
ATOM   7458  C CB    . THR B 2 926  ? 117.757 163.505 120.417 1.00 44.73  ? 923  THR A CB    1 
ATOM   7459  O OG1   . THR B 2 926  ? 117.352 163.320 119.055 1.00 44.73  ? 923  THR A OG1   1 
ATOM   7460  C CG2   . THR B 2 926  ? 118.959 164.437 120.467 1.00 44.73  ? 923  THR A CG2   1 
ATOM   7461  N N     . GLY B 2 927  ? 120.471 161.603 120.891 1.00 44.73  ? 924  GLY A N     1 
ATOM   7462  C CA    . GLY B 2 927  ? 121.650 160.973 120.319 1.00 44.73  ? 924  GLY A CA    1 
ATOM   7463  C C     . GLY B 2 927  ? 122.668 161.923 119.720 1.00 44.73  ? 924  GLY A C     1 
ATOM   7464  O O     . GLY B 2 927  ? 123.717 161.456 119.256 1.00 44.73  ? 924  GLY A O     1 
ATOM   7465  N N     . LYS B 2 928  ? 122.422 163.230 119.698 1.00 44.73  ? 925  LYS A N     1 
ATOM   7466  C CA    . LYS B 2 928  ? 123.389 164.164 119.140 1.00 44.73  ? 925  LYS A CA    1 
ATOM   7467  C C     . LYS B 2 928  ? 124.629 164.250 120.023 1.00 44.73  ? 925  LYS A C     1 
ATOM   7468  O O     . LYS B 2 928  ? 124.558 164.126 121.248 1.00 44.73  ? 925  LYS A O     1 
ATOM   7469  C CB    . LYS B 2 928  ? 122.762 165.548 118.983 1.00 26.78  ? 925  LYS A CB    1 
ATOM   7470  C CG    . LYS B 2 928  ? 121.695 165.623 117.904 1.00 26.78  ? 925  LYS A CG    1 
ATOM   7471  C CD    . LYS B 2 928  ? 121.013 166.981 117.891 1.00 26.78  ? 925  LYS A CD    1 
ATOM   7472  C CE    . LYS B 2 928  ? 121.947 168.064 117.378 1.00 26.78  ? 925  LYS A CE    1 
ATOM   7473  N NZ    . LYS B 2 928  ? 121.255 169.376 117.252 1.00 26.78  ? 925  LYS A NZ    1 
ATOM   7474  N N     . ILE B 2 929  ? 125.775 164.468 119.386 1.00 44.73  ? 926  ILE A N     1 
ATOM   7475  C CA    . ILE B 2 929  ? 127.042 164.555 120.104 1.00 44.73  ? 926  ILE A CA    1 
ATOM   7476  C C     . ILE B 2 929  ? 127.165 165.946 120.711 1.00 44.73  ? 926  ILE A C     1 
ATOM   7477  O O     . ILE B 2 929  ? 127.313 166.938 119.991 1.00 44.73  ? 926  ILE A O     1 
ATOM   7478  C CB    . ILE B 2 929  ? 128.228 164.255 119.177 1.00 44.73  ? 926  ILE A CB    1 
ATOM   7479  C CG1   . ILE B 2 929  ? 128.212 162.795 118.732 1.00 44.73  ? 926  ILE A CG1   1 
ATOM   7480  C CG2   . ILE B 2 929  ? 129.541 164.572 119.872 1.00 44.73  ? 926  ILE A CG2   1 
ATOM   7481  C CD1   . ILE B 2 929  ? 129.200 162.490 117.629 1.00 44.73  ? 926  ILE A CD1   1 
ATOM   7482  N N     . LEU B 2 930  ? 127.099 166.022 122.041 1.00 44.73  ? 927  LEU A N     1 
ATOM   7483  C CA    . LEU B 2 930  ? 127.295 167.298 122.719 1.00 44.73  ? 927  LEU A CA    1 
ATOM   7484  C C     . LEU B 2 930  ? 128.768 167.682 122.780 1.00 44.73  ? 927  LEU A C     1 
ATOM   7485  O O     . LEU B 2 930  ? 129.107 168.866 122.672 1.00 44.73  ? 927  LEU A O     1 
ATOM   7486  C CB    . LEU B 2 930  ? 126.701 167.248 124.126 1.00 44.73  ? 927  LEU A CB    1 
ATOM   7487  C CG    . LEU B 2 930  ? 125.182 167.116 124.214 1.00 44.73  ? 927  LEU A CG    1 
ATOM   7488  C CD1   . LEU B 2 930  ? 124.743 166.977 125.659 1.00 44.73  ? 927  LEU A CD1   1 
ATOM   7489  C CD2   . LEU B 2 930  ? 124.518 168.320 123.567 1.00 44.73  ? 927  LEU A CD2   1 
ATOM   7490  N N     . GLU B 2 931  ? 129.653 166.704 122.951 1.00 44.73  ? 928  GLU A N     1 
ATOM   7491  C CA    . GLU B 2 931  ? 131.078 166.977 123.060 1.00 44.73  ? 928  GLU A CA    1 
ATOM   7492  C C     . GLU B 2 931  ? 131.847 165.688 122.825 1.00 44.73  ? 928  GLU A C     1 
ATOM   7493  O O     . GLU B 2 931  ? 131.455 164.628 123.316 1.00 44.73  ? 928  GLU A O     1 
ATOM   7494  C CB    . GLU B 2 931  ? 131.433 167.560 124.432 1.00 44.73  ? 928  GLU A CB    1 
ATOM   7495  C CG    . GLU B 2 931  ? 132.900 167.425 124.798 1.00 44.73  ? 928  GLU A CG    1 
ATOM   7496  C CD    . GLU B 2 931  ? 133.135 167.482 126.289 1.00 44.73  ? 928  GLU A CD    1 
ATOM   7497  O OE1   . GLU B 2 931  ? 132.144 167.493 127.045 1.00 44.73  ? 928  GLU A OE1   1 
ATOM   7498  O OE2   . GLU B 2 931  ? 134.312 167.510 126.707 1.00 44.73  ? 928  GLU A OE2   1 
ATOM   7499  N N     . GLN B 2 932  ? 132.939 165.787 122.073 1.00 44.73  ? 929  GLN A N     1 
ATOM   7500  C CA    . GLN B 2 932  ? 133.828 164.655 121.865 1.00 44.73  ? 929  GLN A CA    1 
ATOM   7501  C C     . GLN B 2 932  ? 135.264 165.132 122.006 1.00 44.73  ? 929  GLN A C     1 
ATOM   7502  O O     . GLN B 2 932  ? 135.631 166.174 121.456 1.00 44.73  ? 929  GLN A O     1 
ATOM   7503  C CB    . GLN B 2 932  ? 133.595 164.018 120.494 1.00 44.73  ? 929  GLN A CB    1 
ATOM   7504  C CG    . GLN B 2 932  ? 133.374 165.004 119.369 1.00 44.73  ? 929  GLN A CG    1 
ATOM   7505  C CD    . GLN B 2 932  ? 133.308 164.321 118.021 1.00 44.73  ? 929  GLN A CD    1 
ATOM   7506  O OE1   . GLN B 2 932  ? 134.258 163.661 117.603 1.00 44.73  ? 929  GLN A OE1   1 
ATOM   7507  N NE2   . GLN B 2 932  ? 132.185 164.477 117.331 1.00 44.73  ? 929  GLN A NE2   1 
ATOM   7508  N N     . ARG B 2 933  ? 136.071 164.369 122.740 1.00 44.73  ? 930  ARG A N     1 
ATOM   7509  C CA    . ARG B 2 933  ? 137.404 164.799 123.132 1.00 44.73  ? 930  ARG A CA    1 
ATOM   7510  C C     . ARG B 2 933  ? 138.346 163.604 123.155 1.00 44.73  ? 930  ARG A C     1 
ATOM   7511  O O     . ARG B 2 933  ? 137.927 162.470 123.394 1.00 44.73  ? 930  ARG A O     1 
ATOM   7512  C CB    . ARG B 2 933  ? 137.385 165.455 124.517 1.00 44.73  ? 930  ARG A CB    1 
ATOM   7513  C CG    . ARG B 2 933  ? 138.530 166.405 124.795 1.00 44.73  ? 930  ARG A CG    1 
ATOM   7514  C CD    . ARG B 2 933  ? 138.055 167.584 125.626 1.00 44.73  ? 930  ARG A CD    1 
ATOM   7515  N NE    . ARG B 2 933  ? 137.259 167.141 126.765 1.00 44.73  ? 930  ARG A NE    1 
ATOM   7516  C CZ    . ARG B 2 933  ? 137.758 166.580 127.858 1.00 44.73  ? 930  ARG A CZ    1 
ATOM   7517  N NH1   . ARG B 2 933  ? 139.058 166.381 128.002 1.00 44.73  ? 930  ARG A NH1   1 
ATOM   7518  N NH2   . ARG B 2 933  ? 136.932 166.204 128.829 1.00 44.73  ? 930  ARG A NH2   1 
ATOM   7519  N N     . SER B 2 934  ? 139.629 163.874 122.931 1.00 44.73  ? 931  SER A N     1 
ATOM   7520  C CA    . SER B 2 934  ? 140.677 162.862 122.990 1.00 44.73  ? 931  SER A CA    1 
ATOM   7521  C C     . SER B 2 934  ? 141.471 163.060 124.273 1.00 44.73  ? 931  SER A C     1 
ATOM   7522  O O     . SER B 2 934  ? 141.947 164.167 124.547 1.00 44.73  ? 931  SER A O     1 
ATOM   7523  C CB    . SER B 2 934  ? 141.593 162.944 121.771 1.00 44.73  ? 931  SER A CB    1 
ATOM   7524  O OG    . SER B 2 934  ? 142.715 162.093 121.923 1.00 44.73  ? 931  SER A OG    1 
ATOM   7525  N N     . LEU B 2 935  ? 141.617 161.990 125.053 1.00 44.73  ? 932  LEU A N     1 
ATOM   7526  C CA    . LEU B 2 935  ? 142.216 162.060 126.377 1.00 44.73  ? 932  LEU A CA    1 
ATOM   7527  C C     . LEU B 2 935  ? 143.694 161.690 126.388 1.00 44.73  ? 932  LEU A C     1 
ATOM   7528  O O     . LEU B 2 935  ? 144.216 161.307 127.441 1.00 44.73  ? 932  LEU A O     1 
ATOM   7529  C CB    . LEU B 2 935  ? 141.450 161.161 127.349 1.00 44.73  ? 932  LEU A CB    1 
ATOM   7530  C CG    . LEU B 2 935  ? 140.101 161.678 127.848 1.00 44.73  ? 932  LEU A CG    1 
ATOM   7531  C CD1   . LEU B 2 935  ? 139.541 160.763 128.922 1.00 44.73  ? 932  LEU A CD1   1 
ATOM   7532  C CD2   . LEU B 2 935  ? 140.232 163.101 128.365 1.00 44.73  ? 932  LEU A CD2   1 
ATOM   7533  N N     . ASN B 2 936  ? 144.382 161.790 125.250 1.00 44.73  ? 933  ASN A N     1 
ATOM   7534  C CA    . ASN B 2 936  ? 145.808 161.488 125.241 1.00 44.73  ? 933  ASN A CA    1 
ATOM   7535  C C     . ASN B 2 936  ? 146.657 162.649 125.741 1.00 44.73  ? 933  ASN A C     1 
ATOM   7536  O O     . ASN B 2 936  ? 147.870 162.480 125.902 1.00 44.73  ? 933  ASN A O     1 
ATOM   7537  C CB    . ASN B 2 936  ? 146.260 161.079 123.838 1.00 44.73  ? 933  ASN A CB    1 
ATOM   7538  C CG    . ASN B 2 936  ? 145.782 162.033 122.769 1.00 44.73  ? 933  ASN A CG    1 
ATOM   7539  O OD1   . ASN B 2 936  ? 145.179 163.065 123.062 1.00 44.73  ? 933  ASN A OD1   1 
ATOM   7540  N ND2   . ASN B 2 936  ? 146.053 161.694 121.515 1.00 44.73  ? 933  ASN A ND2   1 
ATOM   7541  N N     . THR B 2 937  ? 146.059 163.811 125.989 1.00 44.73  ? 934  THR A N     1 
ATOM   7542  C CA    . THR B 2 937  ? 146.760 164.968 126.535 1.00 44.73  ? 934  THR A CA    1 
ATOM   7543  C C     . THR B 2 937  ? 146.086 165.356 127.844 1.00 44.73  ? 934  THR A C     1 
ATOM   7544  O O     . THR B 2 937  ? 145.032 166.001 127.838 1.00 44.73  ? 934  THR A O     1 
ATOM   7545  C CB    . THR B 2 937  ? 146.755 166.135 125.550 1.00 44.73  ? 934  THR A CB    1 
ATOM   7546  O OG1   . THR B 2 937  ? 147.403 165.739 124.335 1.00 44.73  ? 934  THR A OG1   1 
ATOM   7547  C CG2   . THR B 2 937  ? 147.487 167.330 126.138 1.00 44.73  ? 934  THR A CG2   1 
ATOM   7548  N N     . ILE B 2 938  ? 146.693 164.965 128.961 1.00 44.73  ? 935  ILE A N     1 
ATOM   7549  C CA    . ILE B 2 938  ? 146.165 165.240 130.291 1.00 44.73  ? 935  ILE A CA    1 
ATOM   7550  C C     . ILE B 2 938  ? 147.198 166.048 131.061 1.00 44.73  ? 935  ILE A C     1 
ATOM   7551  O O     . ILE B 2 938  ? 148.365 165.648 131.151 1.00 44.73  ? 935  ILE A O     1 
ATOM   7552  C CB    . ILE B 2 938  ? 145.812 163.944 131.043 1.00 44.73  ? 935  ILE A CB    1 
ATOM   7553  C CG1   . ILE B 2 938  ? 144.700 163.191 130.312 1.00 44.73  ? 935  ILE A CG1   1 
ATOM   7554  C CG2   . ILE B 2 938  ? 145.395 164.254 132.471 1.00 44.73  ? 935  ILE A CG2   1 
ATOM   7555  C CD1   . ILE B 2 938  ? 144.468 161.793 130.831 1.00 44.73  ? 935  ILE A CD1   1 
ATOM   7556  N N     . GLN B 2 939  ? 146.764 167.180 131.613 1.00 44.73  ? 936  GLN A N     1 
ATOM   7557  C CA    . GLN B 2 939  ? 147.614 168.071 132.402 1.00 44.73  ? 936  GLN A CA    1 
ATOM   7558  C C     . GLN B 2 939  ? 148.834 168.509 131.587 1.00 44.73  ? 936  GLN A C     1 
ATOM   7559  O O     . GLN B 2 939  ? 149.987 168.346 131.991 1.00 44.73  ? 936  GLN A O     1 
ATOM   7560  C CB    . GLN B 2 939  ? 148.014 167.409 133.727 1.00 44.73  ? 936  GLN A CB    1 
ATOM   7561  C CG    . GLN B 2 939  ? 148.843 168.265 134.693 1.00 44.73  ? 936  GLN A CG    1 
ATOM   7562  C CD    . GLN B 2 939  ? 148.207 169.607 135.020 1.00 44.73  ? 936  GLN A CD    1 
ATOM   7563  O OE1   . GLN B 2 939  ? 147.003 169.802 134.850 1.00 44.73  ? 936  GLN A OE1   1 
ATOM   7564  N NE2   . GLN B 2 939  ? 149.021 170.542 135.495 1.00 44.73  ? 936  GLN A NE2   1 
ATOM   7565  N N     . GLN B 2 940  ? 148.556 169.052 130.400 1.00 44.73  ? 937  GLN A N     1 
ATOM   7566  C CA    . GLN B 2 940  ? 149.578 169.637 129.530 1.00 44.73  ? 937  GLN A CA    1 
ATOM   7567  C C     . GLN B 2 940  ? 150.716 168.659 129.249 1.00 44.73  ? 937  GLN A C     1 
ATOM   7568  O O     . GLN B 2 940  ? 151.893 169.024 129.280 1.00 44.73  ? 937  GLN A O     1 
ATOM   7569  C CB    . GLN B 2 940  ? 150.118 170.942 130.120 1.00 43.78  ? 937  GLN A CB    1 
ATOM   7570  C CG    . GLN B 2 940  ? 149.040 171.949 130.481 1.00 43.78  ? 937  GLN A CG    1 
ATOM   7571  C CD    . GLN B 2 940  ? 149.556 173.375 130.492 1.00 43.78  ? 937  GLN A CD    1 
ATOM   7572  O OE1   . GLN B 2 940  ? 150.764 173.610 130.502 1.00 43.78  ? 937  GLN A OE1   1 
ATOM   7573  N NE2   . GLN B 2 940  ? 148.639 174.336 130.489 1.00 43.78  ? 937  GLN A NE2   1 
ATOM   7574  N N     . PHE B 2 941  ? 150.369 167.404 128.976 1.00 44.73  ? 938  PHE A N     1 
ATOM   7575  C CA    . PHE B 2 941  ? 151.359 166.387 128.657 1.00 44.73  ? 938  PHE A CA    1 
ATOM   7576  C C     . PHE B 2 941  ? 150.760 165.377 127.692 1.00 44.73  ? 938  PHE A C     1 
ATOM   7577  O O     . PHE B 2 941  ? 149.642 164.897 127.900 1.00 44.73  ? 938  PHE A O     1 
ATOM   7578  C CB    . PHE B 2 941  ? 151.853 165.675 129.918 1.00 44.73  ? 938  PHE A CB    1 
ATOM   7579  C CG    . PHE B 2 941  ? 152.978 164.719 129.668 1.00 44.73  ? 938  PHE A CG    1 
ATOM   7580  C CD1   . PHE B 2 941  ? 154.279 165.176 129.553 1.00 44.73  ? 938  PHE A CD1   1 
ATOM   7581  C CD2   . PHE B 2 941  ? 152.738 163.364 129.550 1.00 44.73  ? 938  PHE A CD2   1 
ATOM   7582  C CE1   . PHE B 2 941  ? 155.317 164.299 129.324 1.00 44.73  ? 938  PHE A CE1   1 
ATOM   7583  C CE2   . PHE B 2 941  ? 153.771 162.485 129.322 1.00 44.73  ? 938  PHE A CE2   1 
ATOM   7584  C CZ    . PHE B 2 941  ? 155.063 162.951 129.208 1.00 44.73  ? 938  PHE A CZ    1 
ATOM   7585  N N     . ASP B 2 942  ? 151.512 165.049 126.645 1.00 44.73  ? 939  ASP A N     1 
ATOM   7586  C CA    . ASP B 2 942  ? 151.051 164.125 125.617 1.00 44.73  ? 939  ASP A CA    1 
ATOM   7587  C C     . ASP B 2 942  ? 151.458 162.706 125.993 1.00 44.73  ? 939  ASP A C     1 
ATOM   7588  O O     . ASP B 2 942  ? 152.651 162.409 126.117 1.00 44.73  ? 939  ASP A O     1 
ATOM   7589  C CB    . ASP B 2 942  ? 151.623 164.502 124.253 1.00 44.73  ? 939  ASP A CB    1 
ATOM   7590  C CG    . ASP B 2 942  ? 150.727 164.076 123.110 1.00 44.73  ? 939  ASP A CG    1 
ATOM   7591  O OD1   . ASP B 2 942  ? 150.293 162.906 123.101 1.00 44.73  ? 939  ASP A OD1   1 
ATOM   7592  O OD2   . ASP B 2 942  ? 150.456 164.912 122.223 1.00 44.73  ? 939  ASP A OD2   1 
ATOM   7593  N N     . TYR B 2 943  ? 150.468 161.836 126.177 1.00 44.73  ? 940  TYR A N     1 
ATOM   7594  C CA    . TYR B 2 943  ? 150.728 160.472 126.616 1.00 44.73  ? 940  TYR A CA    1 
ATOM   7595  C C     . TYR B 2 943  ? 150.799 159.472 125.471 1.00 44.73  ? 940  TYR A C     1 
ATOM   7596  O O     . TYR B 2 943  ? 151.391 158.401 125.644 1.00 44.73  ? 940  TYR A O     1 
ATOM   7597  C CB    . TYR B 2 943  ? 149.653 160.026 127.611 1.00 44.73  ? 940  TYR A CB    1 
ATOM   7598  C CG    . TYR B 2 943  ? 149.884 160.523 129.019 1.00 44.73  ? 940  TYR A CG    1 
ATOM   7599  C CD1   . TYR B 2 943  ? 150.739 159.852 129.881 1.00 44.73  ? 940  TYR A CD1   1 
ATOM   7600  C CD2   . TYR B 2 943  ? 149.249 161.664 129.485 1.00 44.73  ? 940  TYR A CD2   1 
ATOM   7601  C CE1   . TYR B 2 943  ? 150.955 160.303 131.166 1.00 44.73  ? 940  TYR A CE1   1 
ATOM   7602  C CE2   . TYR B 2 943  ? 149.459 162.122 130.770 1.00 44.73  ? 940  TYR A CE2   1 
ATOM   7603  C CZ    . TYR B 2 943  ? 150.313 161.438 131.605 1.00 44.73  ? 940  TYR A CZ    1 
ATOM   7604  O OH    . TYR B 2 943  ? 150.525 161.890 132.886 1.00 44.73  ? 940  TYR A OH    1 
ATOM   7605  N N     . GLN B 2 944  ? 150.217 159.786 124.314 1.00 44.73  ? 941  GLN A N     1 
ATOM   7606  C CA    . GLN B 2 944  ? 150.196 158.869 123.182 1.00 44.73  ? 941  GLN A CA    1 
ATOM   7607  C C     . GLN B 2 944  ? 150.995 159.390 121.995 1.00 44.73  ? 941  GLN A C     1 
ATOM   7608  O O     . GLN B 2 944  ? 151.864 158.682 121.480 1.00 44.73  ? 941  GLN A O     1 
ATOM   7609  C CB    . GLN B 2 944  ? 148.752 158.586 122.749 1.00 44.73  ? 941  GLN A CB    1 
ATOM   7610  C CG    . GLN B 2 944  ? 148.601 157.325 121.907 1.00 44.73  ? 941  GLN A CG    1 
ATOM   7611  C CD    . GLN B 2 944  ? 148.896 157.556 120.441 1.00 44.73  ? 941  GLN A CD    1 
ATOM   7612  O OE1   . GLN B 2 944  ? 148.717 158.659 119.926 1.00 44.73  ? 941  GLN A OE1   1 
ATOM   7613  N NE2   . GLN B 2 944  ? 149.358 156.515 119.760 1.00 44.73  ? 941  GLN A NE2   1 
ATOM   7614  N N     . LYS B 2 945  ? 150.707 160.611 121.538 1.00 44.73  ? 942  LYS A N     1 
ATOM   7615  C CA    . LYS B 2 945  ? 151.295 161.096 120.294 1.00 44.73  ? 942  LYS A CA    1 
ATOM   7616  C C     . LYS B 2 945  ? 152.815 161.121 120.358 1.00 44.73  ? 942  LYS A C     1 
ATOM   7617  O O     . LYS B 2 945  ? 153.481 160.909 119.337 1.00 44.73  ? 942  LYS A O     1 
ATOM   7618  C CB    . LYS B 2 945  ? 150.753 162.487 119.963 1.00 42.95  ? 942  LYS A CB    1 
ATOM   7619  C CG    . LYS B 2 945  ? 149.285 162.499 119.568 1.00 42.95  ? 942  LYS A CG    1 
ATOM   7620  C CD    . LYS B 2 945  ? 148.800 163.910 119.278 1.00 42.95  ? 942  LYS A CD    1 
ATOM   7621  C CE    . LYS B 2 945  ? 147.309 163.930 118.981 1.00 42.95  ? 942  LYS A CE    1 
ATOM   7622  N NZ    . LYS B 2 945  ? 146.858 165.259 118.484 1.00 42.95  ? 942  LYS A NZ    1 
ATOM   7623  N N     . LYS B 2 946  ? 153.385 161.376 121.535 1.00 44.73  ? 943  LYS A N     1 
ATOM   7624  C CA    . LYS B 2 946  ? 154.834 161.372 121.688 1.00 44.73  ? 943  LYS A CA    1 
ATOM   7625  C C     . LYS B 2 946  ? 155.322 160.291 122.644 1.00 44.73  ? 943  LYS A C     1 
ATOM   7626  O O     . LYS B 2 946  ? 156.117 159.441 122.235 1.00 44.73  ? 943  LYS A O     1 
ATOM   7627  C CB    . LYS B 2 946  ? 155.311 162.755 122.143 1.00 44.73  ? 943  LYS A CB    1 
ATOM   7628  C CG    . LYS B 2 946  ? 154.985 163.874 121.168 1.00 44.73  ? 943  LYS A CG    1 
ATOM   7629  C CD    . LYS B 2 946  ? 155.542 163.577 119.785 1.00 44.73  ? 943  LYS A CD    1 
ATOM   7630  C CE    . LYS B 2 946  ? 155.239 164.705 118.813 1.00 44.73  ? 943  LYS A CE    1 
ATOM   7631  N NZ    . LYS B 2 946  ? 156.107 165.891 119.052 1.00 44.73  ? 943  LYS A NZ    1 
ATOM   7632  N N     . LEU B 2 947  ? 154.854 160.273 123.895 1.00 44.73  ? 944  LEU A N     1 
ATOM   7633  C CA    . LEU B 2 947  ? 155.506 159.456 124.917 1.00 44.73  ? 944  LEU A CA    1 
ATOM   7634  C C     . LEU B 2 947  ? 155.361 157.966 124.630 1.00 44.73  ? 944  LEU A C     1 
ATOM   7635  O O     . LEU B 2 947  ? 156.349 157.223 124.639 1.00 44.73  ? 944  LEU A O     1 
ATOM   7636  C CB    . LEU B 2 947  ? 154.950 159.787 126.301 1.00 44.73  ? 944  LEU A CB    1 
ATOM   7637  C CG    . LEU B 2 947  ? 155.697 159.064 127.425 1.00 44.73  ? 944  LEU A CG    1 
ATOM   7638  C CD1   . LEU B 2 947  ? 157.167 159.446 127.428 1.00 44.73  ? 944  LEU A CD1   1 
ATOM   7639  C CD2   . LEU B 2 947  ? 155.067 159.340 128.776 1.00 44.73  ? 944  LEU A CD2   1 
ATOM   7640  N N     . ASP B 2 948  ? 154.134 157.506 124.378 1.00 44.73  ? 945  ASP A N     1 
ATOM   7641  C CA    . ASP B 2 948  ? 153.937 156.083 124.125 1.00 44.73  ? 945  ASP A CA    1 
ATOM   7642  C C     . ASP B 2 948  ? 154.546 155.667 122.794 1.00 44.73  ? 945  ASP A C     1 
ATOM   7643  O O     . ASP B 2 948  ? 154.924 154.502 122.622 1.00 44.73  ? 945  ASP A O     1 
ATOM   7644  C CB    . ASP B 2 948  ? 152.450 155.736 124.163 1.00 44.73  ? 945  ASP A CB    1 
ATOM   7645  C CG    . ASP B 2 948  ? 152.197 154.321 124.642 1.00 44.73  ? 945  ASP A CG    1 
ATOM   7646  O OD1   . ASP B 2 948  ? 152.850 153.899 125.617 1.00 44.73  ? 945  ASP A OD1   1 
ATOM   7647  O OD2   . ASP B 2 948  ? 151.346 153.632 124.045 1.00 44.73  ? 945  ASP A OD2   1 
ATOM   7648  N N     . ASN B 2 949  ? 154.646 156.598 121.844 1.00 44.73  ? 946  ASN A N     1 
ATOM   7649  C CA    . ASN B 2 949  ? 155.272 156.285 120.565 1.00 44.73  ? 946  ASN A CA    1 
ATOM   7650  C C     . ASN B 2 949  ? 156.761 156.003 120.729 1.00 44.73  ? 946  ASN A C     1 
ATOM   7651  O O     . ASN B 2 949  ? 157.289 155.065 120.122 1.00 44.73  ? 946  ASN A O     1 
ATOM   7652  C CB    . ASN B 2 949  ? 155.045 157.429 119.579 1.00 44.73  ? 946  ASN A CB    1 
ATOM   7653  C CG    . ASN B 2 949  ? 153.686 157.360 118.913 1.00 44.73  ? 946  ASN A CG    1 
ATOM   7654  O OD1   . ASN B 2 949  ? 152.800 156.633 119.360 1.00 44.73  ? 946  ASN A OD1   1 
ATOM   7655  N ND2   . ASN B 2 949  ? 153.514 158.120 117.838 1.00 44.73  ? 946  ASN A ND2   1 
ATOM   7656  N N     . ARG B 2 950  ? 157.457 156.809 121.537 1.00 44.73  ? 947  ARG A N     1 
ATOM   7657  C CA    . ARG B 2 950  ? 158.875 156.557 121.774 1.00 44.73  ? 947  ARG A CA    1 
ATOM   7658  C C     . ARG B 2 950  ? 159.084 155.239 122.507 1.00 44.73  ? 947  ARG A C     1 
ATOM   7659  O O     . ARG B 2 950  ? 159.997 154.475 122.174 1.00 44.73  ? 947  ARG A O     1 
ATOM   7660  C CB    . ARG B 2 950  ? 159.501 157.709 122.562 1.00 44.73  ? 947  ARG A CB    1 
ATOM   7661  C CG    . ARG B 2 950  ? 159.121 159.093 122.070 1.00 44.73  ? 947  ARG A CG    1 
ATOM   7662  C CD    . ARG B 2 950  ? 159.538 159.322 120.629 1.00 44.73  ? 947  ARG A CD    1 
ATOM   7663  N NE    . ARG B 2 950  ? 159.523 160.739 120.284 1.00 44.73  ? 947  ARG A NE    1 
ATOM   7664  C CZ    . ARG B 2 950  ? 159.798 161.221 119.080 1.00 44.73  ? 947  ARG A CZ    1 
ATOM   7665  N NH1   . ARG B 2 950  ? 160.116 160.424 118.072 1.00 44.73  ? 947  ARG A NH1   1 
ATOM   7666  N NH2   . ARG B 2 950  ? 159.753 162.535 118.881 1.00 44.73  ? 947  ARG A NH2   1 
ATOM   7667  N N     . GLU B 2 951  ? 158.249 154.957 123.510 1.00 44.73  ? 948  GLU A N     1 
ATOM   7668  C CA    . GLU B 2 951  ? 158.355 153.687 124.222 1.00 44.73  ? 948  GLU A CA    1 
ATOM   7669  C C     . GLU B 2 951  ? 158.075 152.511 123.295 1.00 44.73  ? 948  GLU A C     1 
ATOM   7670  O O     . GLU B 2 951  ? 158.752 151.479 123.366 1.00 44.73  ? 948  GLU A O     1 
ATOM   7671  C CB    . GLU B 2 951  ? 157.400 153.671 125.415 1.00 44.73  ? 948  GLU A CB    1 
ATOM   7672  C CG    . GLU B 2 951  ? 157.679 154.747 126.451 1.00 44.73  ? 948  GLU A CG    1 
ATOM   7673  C CD    . GLU B 2 951  ? 158.679 154.306 127.501 1.00 44.73  ? 948  GLU A CD    1 
ATOM   7674  O OE1   . GLU B 2 951  ? 159.741 153.766 127.128 1.00 44.73  ? 948  GLU A OE1   1 
ATOM   7675  O OE2   . GLU B 2 951  ? 158.402 154.500 128.703 1.00 44.73  ? 948  GLU A OE2   1 
ATOM   7676  N N     . LYS B 2 952  ? 157.074 152.646 122.421 1.00 44.73  ? 949  LYS A N     1 
ATOM   7677  C CA    . LYS B 2 952  ? 156.805 151.597 121.443 1.00 44.73  ? 949  LYS A CA    1 
ATOM   7678  C C     . LYS B 2 952  ? 157.938 151.483 120.432 1.00 44.73  ? 949  LYS A C     1 
ATOM   7679  O O     . LYS B 2 952  ? 158.206 150.394 119.912 1.00 44.73  ? 949  LYS A O     1 
ATOM   7680  C CB    . LYS B 2 952  ? 155.477 151.863 120.737 1.00 44.73  ? 949  LYS A CB    1 
ATOM   7681  C CG    . LYS B 2 952  ? 154.258 151.422 121.528 1.00 44.73  ? 949  LYS A CG    1 
ATOM   7682  C CD    . LYS B 2 952  ? 154.131 149.908 121.542 1.00 44.73  ? 949  LYS A CD    1 
ATOM   7683  C CE    . LYS B 2 952  ? 152.948 149.462 122.386 1.00 44.73  ? 949  LYS A CE    1 
ATOM   7684  N NZ    . LYS B 2 952  ? 152.745 147.988 122.324 1.00 44.73  ? 949  LYS A NZ    1 
ATOM   7685  N N     . GLU B 2 953  ? 158.602 152.599 120.125 1.00 44.73  ? 950  GLU A N     1 
ATOM   7686  C CA    . GLU B 2 953  ? 159.755 152.543 119.234 1.00 44.73  ? 950  GLU A CA    1 
ATOM   7687  C C     . GLU B 2 953  ? 160.914 151.793 119.880 1.00 44.73  ? 950  GLU A C     1 
ATOM   7688  O O     . GLU B 2 953  ? 161.625 151.038 119.207 1.00 44.73  ? 950  GLU A O     1 
ATOM   7689  C CB    . GLU B 2 953  ? 160.177 153.955 118.834 1.00 44.73  ? 950  GLU A CB    1 
ATOM   7690  C CG    . GLU B 2 953  ? 159.513 154.456 117.565 1.00 44.73  ? 950  GLU A CG    1 
ATOM   7691  C CD    . GLU B 2 953  ? 159.886 155.887 117.235 1.00 44.73  ? 950  GLU A CD    1 
ATOM   7692  O OE1   . GLU B 2 953  ? 161.095 156.198 117.215 1.00 44.73  ? 950  GLU A OE1   1 
ATOM   7693  O OE2   . GLU B 2 953  ? 158.970 156.701 116.996 1.00 44.73  ? 950  GLU A OE2   1 
ATOM   7694  N N     . ARG B 2 954  ? 161.124 151.993 121.184 1.00 44.73  ? 951  ARG A N     1 
ATOM   7695  C CA    . ARG B 2 954  ? 162.203 151.293 121.874 1.00 44.73  ? 951  ARG A CA    1 
ATOM   7696  C C     . ARG B 2 954  ? 161.940 149.794 121.948 1.00 44.73  ? 951  ARG A C     1 
ATOM   7697  O O     . ARG B 2 954  ? 162.853 148.990 121.728 1.00 44.73  ? 951  ARG A O     1 
ATOM   7698  C CB    . ARG B 2 954  ? 162.395 151.869 123.275 1.00 44.73  ? 951  ARG A CB    1 
ATOM   7699  C CG    . ARG B 2 954  ? 162.756 153.339 123.298 1.00 44.73  ? 951  ARG A CG    1 
ATOM   7700  C CD    . ARG B 2 954  ? 163.900 153.611 124.256 1.00 44.73  ? 951  ARG A CD    1 
ATOM   7701  N NE    . ARG B 2 954  ? 163.807 152.809 125.470 1.00 44.73  ? 951  ARG A NE    1 
ATOM   7702  C CZ    . ARG B 2 954  ? 164.792 152.659 126.345 1.00 44.73  ? 951  ARG A CZ    1 
ATOM   7703  N NH1   . ARG B 2 954  ? 165.966 153.243 126.170 1.00 44.73  ? 951  ARG A NH1   1 
ATOM   7704  N NH2   . ARG B 2 954  ? 164.594 151.905 127.422 1.00 44.73  ? 951  ARG A NH2   1 
ATOM   7705  N N     . VAL B 2 955  ? 160.704 149.397 122.263 1.00 44.73  ? 952  VAL A N     1 
ATOM   7706  C CA    . VAL B 2 955  ? 160.396 147.974 122.362 1.00 44.73  ? 952  VAL A CA    1 
ATOM   7707  C C     . VAL B 2 955  ? 160.492 147.307 120.995 1.00 44.73  ? 952  VAL A C     1 
ATOM   7708  O O     . VAL B 2 955  ? 160.788 146.110 120.901 1.00 44.73  ? 952  VAL A O     1 
ATOM   7709  C CB    . VAL B 2 955  ? 159.014 147.759 123.011 1.00 44.73  ? 952  VAL A CB    1 
ATOM   7710  C CG1   . VAL B 2 955  ? 157.894 148.079 122.041 1.00 44.73  ? 952  VAL A CG1   1 
ATOM   7711  C CG2   . VAL B 2 955  ? 158.885 146.334 123.526 1.00 44.73  ? 952  VAL A CG2   1 
ATOM   7712  N N     . ALA B 2 956  ? 160.251 148.057 119.919 1.00 44.73  ? 953  ALA A N     1 
ATOM   7713  C CA    . ALA B 2 956  ? 160.451 147.526 118.578 1.00 44.73  ? 953  ALA A CA    1 
ATOM   7714  C C     . ALA B 2 956  ? 161.914 147.537 118.163 1.00 44.73  ? 953  ALA A C     1 
ATOM   7715  O O     . ALA B 2 956  ? 162.271 146.877 117.182 1.00 44.73  ? 953  ALA A O     1 
ATOM   7716  C CB    . ALA B 2 956  ? 159.624 148.320 117.565 1.00 44.73  ? 953  ALA A CB    1 
ATOM   7717  N N     . ALA B 2 957  ? 162.764 148.264 118.886 1.00 44.73  ? 954  ALA A N     1 
ATOM   7718  C CA    . ALA B 2 957  ? 164.183 148.338 118.564 1.00 44.73  ? 954  ALA A CA    1 
ATOM   7719  C C     . ALA B 2 957  ? 165.000 147.310 119.339 1.00 44.73  ? 954  ALA A C     1 
ATOM   7720  O O     . ALA B 2 957  ? 165.823 146.599 118.754 1.00 44.73  ? 954  ALA A O     1 
ATOM   7721  C CB    . ALA B 2 957  ? 164.711 149.749 118.838 1.00 44.73  ? 954  ALA A CB    1 
ATOM   7722  N N     . ARG B 2 958  ? 164.786 147.220 120.651 1.00 46.55  ? 955  ARG A N     1 
ATOM   7723  C CA    . ARG B 2 958  ? 165.546 146.314 121.504 1.00 46.55  ? 955  ARG A CA    1 
ATOM   7724  C C     . ARG B 2 958  ? 164.791 145.038 121.848 1.00 46.55  ? 955  ARG A C     1 
ATOM   7725  O O     . ARG B 2 958  ? 165.395 143.961 121.883 1.00 46.55  ? 955  ARG A O     1 
ATOM   7726  C CB    . ARG B 2 958  ? 165.951 147.027 122.799 1.00 46.55  ? 955  ARG A CB    1 
ATOM   7727  C CG    . ARG B 2 958  ? 166.423 148.465 122.612 1.00 46.55  ? 955  ARG A CG    1 
ATOM   7728  C CD    . ARG B 2 958  ? 167.923 148.562 122.342 1.00 46.55  ? 955  ARG A CD    1 
ATOM   7729  N NE    . ARG B 2 958  ? 168.350 147.775 121.191 1.00 46.55  ? 955  ARG A NE    1 
ATOM   7730  C CZ    . ARG B 2 958  ? 168.414 148.236 119.950 1.00 46.55  ? 955  ARG A CZ    1 
ATOM   7731  N NH1   . ARG B 2 958  ? 168.084 149.484 119.658 1.00 46.55  ? 955  ARG A NH1   1 
ATOM   7732  N NH2   . ARG B 2 958  ? 168.820 147.425 118.976 1.00 46.55  ? 955  ARG A NH2   1 
ATOM   7733  N N     . GLN B 2 959  ? 163.484 145.136 122.097 1.00 50.35  ? 956  GLN A N     1 
ATOM   7734  C CA    . GLN B 2 959  ? 162.652 144.002 122.501 1.00 50.35  ? 956  GLN A CA    1 
ATOM   7735  C C     . GLN B 2 959  ? 163.207 143.347 123.768 1.00 50.35  ? 956  GLN A C     1 
ATOM   7736  O O     . GLN B 2 959  ? 163.529 142.158 123.805 1.00 50.35  ? 956  GLN A O     1 
ATOM   7737  C CB    . GLN B 2 959  ? 162.513 142.988 121.359 1.00 50.35  ? 956  GLN A CB    1 
ATOM   7738  C CG    . GLN B 2 959  ? 161.344 142.024 121.512 1.00 50.35  ? 956  GLN A CG    1 
ATOM   7739  C CD    . GLN B 2 959  ? 160.053 142.720 121.899 1.00 50.35  ? 956  GLN A CD    1 
ATOM   7740  O OE1   . GLN B 2 959  ? 159.381 143.317 121.059 1.00 50.35  ? 956  GLN A OE1   1 
ATOM   7741  N NE2   . GLN B 2 959  ? 159.697 142.639 123.175 1.00 50.35  ? 956  GLN A NE2   1 
ATOM   7742  N N     . ALA B 2 960  ? 163.316 144.158 124.814 1.00 53.51  ? 957  ALA A N     1 
ATOM   7743  C CA    . ALA B 2 960  ? 163.835 143.734 126.102 1.00 53.51  ? 957  ALA A CA    1 
ATOM   7744  C C     . ALA B 2 960  ? 162.699 143.670 127.120 1.00 53.51  ? 957  ALA A C     1 
ATOM   7745  O O     . ALA B 2 960  ? 161.526 143.881 126.792 1.00 53.51  ? 957  ALA A O     1 
ATOM   7746  C CB    . ALA B 2 960  ? 164.954 144.675 126.553 1.00 53.51  ? 957  ALA A CB    1 
ATOM   7747  N N     . TRP B 2 961  ? 163.053 143.374 128.370 1.00 61.54  ? 958  TRP A N     1 
ATOM   7748  C CA    . TRP B 2 961  ? 162.066 143.274 129.438 1.00 61.54  ? 958  TRP A CA    1 
ATOM   7749  C C     . TRP B 2 961  ? 161.847 144.602 130.153 1.00 61.54  ? 958  TRP A C     1 
ATOM   7750  O O     . TRP B 2 961  ? 160.734 144.879 130.612 1.00 61.54  ? 958  TRP A O     1 
ATOM   7751  C CB    . TRP B 2 961  ? 162.492 142.207 130.450 1.00 61.54  ? 958  TRP A CB    1 
ATOM   7752  C CG    . TRP B 2 961  ? 162.382 140.809 129.930 1.00 61.54  ? 958  TRP A CG    1 
ATOM   7753  C CD1   . TRP B 2 961  ? 161.406 140.311 129.119 1.00 61.54  ? 958  TRP A CD1   1 
ATOM   7754  C CD2   . TRP B 2 961  ? 163.282 139.725 130.188 1.00 61.54  ? 958  TRP A CD2   1 
ATOM   7755  N NE1   . TRP B 2 961  ? 161.642 138.984 128.855 1.00 61.54  ? 958  TRP A NE1   1 
ATOM   7756  C CE2   . TRP B 2 961  ? 162.788 138.601 129.500 1.00 61.54  ? 958  TRP A CE2   1 
ATOM   7757  C CE3   . TRP B 2 961  ? 164.457 139.597 130.934 1.00 61.54  ? 958  TRP A CE3   1 
ATOM   7758  C CZ2   . TRP B 2 961  ? 163.428 137.365 129.536 1.00 61.54  ? 958  TRP A CZ2   1 
ATOM   7759  C CZ3   . TRP B 2 961  ? 165.090 138.370 130.967 1.00 61.54  ? 958  TRP A CZ3   1 
ATOM   7760  C CH2   . TRP B 2 961  ? 164.575 137.270 130.273 1.00 61.54  ? 958  TRP A CH2   1 
ATOM   7761  N N     . SER B 2 962  ? 162.893 145.425 130.262 1.00 52.21  ? 959  SER A N     1 
ATOM   7762  C CA    . SER B 2 962  ? 162.756 146.709 130.941 1.00 52.21  ? 959  SER A CA    1 
ATOM   7763  C C     . SER B 2 962  ? 161.786 147.626 130.206 1.00 52.21  ? 959  SER A C     1 
ATOM   7764  O O     . SER B 2 962  ? 160.985 148.327 130.835 1.00 52.21  ? 959  SER A O     1 
ATOM   7765  C CB    . SER B 2 962  ? 164.124 147.375 131.081 1.00 52.21  ? 959  SER A CB    1 
ATOM   7766  O OG    . SER B 2 962  ? 164.783 147.452 129.829 1.00 52.21  ? 959  SER A OG    1 
ATOM   7767  N N     . VAL B 2 963  ? 161.846 147.638 128.872 1.00 48.05  ? 960  VAL A N     1 
ATOM   7768  C CA    . VAL B 2 963  ? 160.966 148.506 128.095 1.00 48.05  ? 960  VAL A CA    1 
ATOM   7769  C C     . VAL B 2 963  ? 159.513 148.069 128.239 1.00 48.05  ? 960  VAL A C     1 
ATOM   7770  O O     . VAL B 2 963  ? 158.598 148.901 128.249 1.00 48.05  ? 960  VAL A O     1 
ATOM   7771  C CB    . VAL B 2 963  ? 161.412 148.543 126.621 1.00 48.05  ? 960  VAL A CB    1 
ATOM   7772  C CG1   . VAL B 2 963  ? 162.769 149.210 126.502 1.00 48.05  ? 960  VAL A CG1   1 
ATOM   7773  C CG2   . VAL B 2 963  ? 161.464 147.139 126.040 1.00 48.05  ? 960  VAL A CG2   1 
ATOM   7774  N N     . VAL B 2 964  ? 159.276 146.760 128.344 1.00 48.54  ? 961  VAL A N     1 
ATOM   7775  C CA    . VAL B 2 964  ? 157.916 146.267 128.547 1.00 48.54  ? 961  VAL A CA    1 
ATOM   7776  C C     . VAL B 2 964  ? 157.386 146.711 129.904 1.00 48.54  ? 961  VAL A C     1 
ATOM   7777  O O     . VAL B 2 964  ? 156.229 147.132 130.028 1.00 48.54  ? 961  VAL A O     1 
ATOM   7778  C CB    . VAL B 2 964  ? 157.873 144.735 128.394 1.00 48.54  ? 961  VAL A CB    1 
ATOM   7779  C CG1   . VAL B 2 964  ? 156.480 144.208 128.699 1.00 48.54  ? 961  VAL A CG1   1 
ATOM   7780  C CG2   . VAL B 2 964  ? 158.300 144.333 126.991 1.00 48.54  ? 961  VAL A CG2   1 
ATOM   7781  N N     . GLY B 2 965  ? 158.221 146.624 130.942 1.00 44.73  ? 962  GLY A N     1 
ATOM   7782  C CA    . GLY B 2 965  ? 157.783 147.029 132.269 1.00 44.73  ? 962  GLY A CA    1 
ATOM   7783  C C     . GLY B 2 965  ? 157.451 148.507 132.356 1.00 44.73  ? 962  GLY A C     1 
ATOM   7784  O O     . GLY B 2 965  ? 156.493 148.899 133.025 1.00 44.73  ? 962  GLY A O     1 
ATOM   7785  N N     . THR B 2 966  ? 158.244 149.347 131.688 1.00 44.73  ? 963  THR A N     1 
ATOM   7786  C CA    . THR B 2 966  ? 157.971 150.780 131.692 1.00 44.73  ? 963  THR A CA    1 
ATOM   7787  C C     . THR B 2 966  ? 156.659 151.095 130.984 1.00 44.73  ? 963  THR A C     1 
ATOM   7788  O O     . THR B 2 966  ? 155.917 151.990 131.403 1.00 44.73  ? 963  THR A O     1 
ATOM   7789  C CB    . THR B 2 966  ? 159.125 151.540 131.040 1.00 44.73  ? 963  THR A CB    1 
ATOM   7790  O OG1   . THR B 2 966  ? 159.431 150.951 129.770 1.00 44.73  ? 963  THR A OG1   1 
ATOM   7791  C CG2   . THR B 2 966  ? 160.360 151.492 131.924 1.00 44.73  ? 963  THR A CG2   1 
ATOM   7792  N N     . ILE B 2 967  ? 156.362 150.374 129.900 1.00 44.73  ? 964  ILE A N     1 
ATOM   7793  C CA    . ILE B 2 967  ? 155.131 150.619 129.154 1.00 44.73  ? 964  ILE A CA    1 
ATOM   7794  C C     . ILE B 2 967  ? 153.911 150.287 130.005 1.00 44.73  ? 964  ILE A C     1 
ATOM   7795  O O     . ILE B 2 967  ? 152.939 151.052 130.047 1.00 44.73  ? 964  ILE A O     1 
ATOM   7796  C CB    . ILE B 2 967  ? 155.142 149.825 127.835 1.00 44.73  ? 964  ILE A CB    1 
ATOM   7797  C CG1   . ILE B 2 967  ? 156.025 150.525 126.801 1.00 44.73  ? 964  ILE A CG1   1 
ATOM   7798  C CG2   . ILE B 2 967  ? 153.740 149.656 127.293 1.00 44.73  ? 964  ILE A CG2   1 
ATOM   7799  C CD1   . ILE B 2 967  ? 156.188 149.749 125.515 1.00 44.73  ? 964  ILE A CD1   1 
ATOM   7800  N N     . LYS B 2 968  ? 153.942 149.147 130.699 1.00 44.73  ? 965  LYS A N     1 
ATOM   7801  C CA    . LYS B 2 968  ? 152.808 148.760 131.533 1.00 44.73  ? 965  LYS A CA    1 
ATOM   7802  C C     . LYS B 2 968  ? 152.604 149.739 132.683 1.00 44.73  ? 965  LYS A C     1 
ATOM   7803  O O     . LYS B 2 968  ? 151.465 150.093 133.012 1.00 44.73  ? 965  LYS A O     1 
ATOM   7804  C CB    . LYS B 2 968  ? 153.003 147.342 132.067 1.00 44.73  ? 965  LYS A CB    1 
ATOM   7805  C CG    . LYS B 2 968  ? 151.703 146.602 132.336 1.00 44.73  ? 965  LYS A CG    1 
ATOM   7806  C CD    . LYS B 2 968  ? 151.918 145.424 133.270 1.00 44.73  ? 965  LYS A CD    1 
ATOM   7807  C CE    . LYS B 2 968  ? 150.614 144.694 133.547 1.00 44.73  ? 965  LYS A CE    1 
ATOM   7808  N NZ    . LYS B 2 968  ? 150.709 143.823 134.751 1.00 44.73  ? 965  LYS A NZ    1 
ATOM   7809  N N     . ASP B 2 969  ? 153.695 150.180 133.313 1.00 44.73  ? 966  ASP A N     1 
ATOM   7810  C CA    . ASP B 2 969  ? 153.580 151.159 134.389 1.00 44.73  ? 966  ASP A CA    1 
ATOM   7811  C C     . ASP B 2 969  ? 153.026 152.480 133.874 1.00 44.73  ? 966  ASP A C     1 
ATOM   7812  O O     . ASP B 2 969  ? 152.206 153.120 134.543 1.00 44.73  ? 966  ASP A O     1 
ATOM   7813  C CB    . ASP B 2 969  ? 154.939 151.370 135.055 1.00 44.73  ? 966  ASP A CB    1 
ATOM   7814  C CG    . ASP B 2 969  ? 155.324 150.225 135.971 1.00 44.73  ? 966  ASP A CG    1 
ATOM   7815  O OD1   . ASP B 2 969  ? 154.481 149.329 136.190 1.00 44.73  ? 966  ASP A OD1   1 
ATOM   7816  O OD2   . ASP B 2 969  ? 156.468 150.221 136.472 1.00 44.73  ? 966  ASP A OD2   1 
ATOM   7817  N N     . LEU B 2 970  ? 153.467 152.908 132.689 1.00 44.73  ? 967  LEU A N     1 
ATOM   7818  C CA    . LEU B 2 970  ? 152.964 154.154 132.120 1.00 44.73  ? 967  LEU A CA    1 
ATOM   7819  C C     . LEU B 2 970  ? 151.477 154.056 131.805 1.00 44.73  ? 967  LEU A C     1 
ATOM   7820  O O     . LEU B 2 970  ? 150.722 155.008 132.036 1.00 44.73  ? 967  LEU A O     1 
ATOM   7821  C CB    . LEU B 2 970  ? 153.757 154.517 130.865 1.00 44.73  ? 967  LEU A CB    1 
ATOM   7822  C CG    . LEU B 2 970  ? 153.164 155.612 129.979 1.00 44.73  ? 967  LEU A CG    1 
ATOM   7823  C CD1   . LEU B 2 970  ? 153.100 156.930 130.730 1.00 44.73  ? 967  LEU A CD1   1 
ATOM   7824  C CD2   . LEU B 2 970  ? 153.972 155.762 128.704 1.00 44.73  ? 967  LEU A CD2   1 
ATOM   7825  N N     . LYS B 2 971  ? 151.037 152.913 131.275 1.00 44.73  ? 968  LYS A N     1 
ATOM   7826  C CA    . LYS B 2 971  ? 149.625 152.747 130.943 1.00 44.73  ? 968  LYS A CA    1 
ATOM   7827  C C     . LYS B 2 971  ? 148.753 152.820 132.189 1.00 44.73  ? 968  LYS A C     1 
ATOM   7828  O O     . LYS B 2 971  ? 147.701 153.469 132.181 1.00 44.73  ? 968  LYS A O     1 
ATOM   7829  C CB    . LYS B 2 971  ? 149.410 151.420 130.219 1.00 44.73  ? 968  LYS A CB    1 
ATOM   7830  C CG    . LYS B 2 971  ? 149.878 151.416 128.777 1.00 44.73  ? 968  LYS A CG    1 
ATOM   7831  C CD    . LYS B 2 971  ? 149.435 150.150 128.072 1.00 44.73  ? 968  LYS A CD    1 
ATOM   7832  C CE    . LYS B 2 971  ? 150.235 149.916 126.808 1.00 44.73  ? 968  LYS A CE    1 
ATOM   7833  N NZ    . LYS B 2 971  ? 149.568 148.940 125.904 1.00 44.73  ? 968  LYS A NZ    1 
ATOM   7834  N N     . GLN B 2 972  ? 149.170 152.157 133.270 1.00 44.73  ? 969  GLN A N     1 
ATOM   7835  C CA    . GLN B 2 972  ? 148.420 152.240 134.518 1.00 44.73  ? 969  GLN A CA    1 
ATOM   7836  C C     . GLN B 2 972  ? 148.444 153.656 135.079 1.00 44.73  ? 969  GLN A C     1 
ATOM   7837  O O     . GLN B 2 972  ? 147.430 154.147 135.586 1.00 44.73  ? 969  GLN A O     1 
ATOM   7838  C CB    . GLN B 2 972  ? 148.980 151.248 135.537 1.00 33.12  ? 969  GLN A CB    1 
ATOM   7839  C CG    . GLN B 2 972  ? 148.228 149.929 135.597 1.00 33.12  ? 969  GLN A CG    1 
ATOM   7840  C CD    . GLN B 2 972  ? 148.948 148.885 136.427 1.00 33.12  ? 969  GLN A CD    1 
ATOM   7841  O OE1   . GLN B 2 972  ? 149.969 149.169 137.054 1.00 33.12  ? 969  GLN A OE1   1 
ATOM   7842  N NE2   . GLN B 2 972  ? 148.419 147.667 136.436 1.00 33.12  ? 969  GLN A NE2   1 
ATOM   7843  N N     . GLY B 2 973  ? 149.597 154.323 135.003 1.00 44.73  ? 970  GLY A N     1 
ATOM   7844  C CA    . GLY B 2 973  ? 149.672 155.700 135.456 1.00 44.73  ? 970  GLY A CA    1 
ATOM   7845  C C     . GLY B 2 973  ? 148.823 156.635 134.618 1.00 44.73  ? 970  GLY A C     1 
ATOM   7846  O O     . GLY B 2 973  ? 148.172 157.540 135.146 1.00 44.73  ? 970  GLY A O     1 
ATOM   7847  N N     . TYR B 2 974  ? 148.824 156.436 133.298 1.00 44.73  ? 971  TYR A N     1 
ATOM   7848  C CA    . TYR B 2 974  ? 147.976 157.246 132.431 1.00 44.73  ? 971  TYR A CA    1 
ATOM   7849  C C     . TYR B 2 974  ? 146.502 157.018 132.733 1.00 44.73  ? 971  TYR A C     1 
ATOM   7850  O O     . TYR B 2 974  ? 145.715 157.971 132.781 1.00 44.73  ? 971  TYR A O     1 
ATOM   7851  C CB    . TYR B 2 974  ? 148.268 156.938 130.963 1.00 44.73  ? 971  TYR A CB    1 
ATOM   7852  C CG    . TYR B 2 974  ? 147.183 157.410 130.026 1.00 44.73  ? 971  TYR A CG    1 
ATOM   7853  C CD1   . TYR B 2 974  ? 147.038 158.756 129.727 1.00 44.73  ? 971  TYR A CD1   1 
ATOM   7854  C CD2   . TYR B 2 974  ? 146.301 156.513 129.443 1.00 44.73  ? 971  TYR A CD2   1 
ATOM   7855  C CE1   . TYR B 2 974  ? 146.048 159.194 128.873 1.00 44.73  ? 971  TYR A CE1   1 
ATOM   7856  C CE2   . TYR B 2 974  ? 145.308 156.942 128.589 1.00 44.73  ? 971  TYR A CE2   1 
ATOM   7857  C CZ    . TYR B 2 974  ? 145.186 158.283 128.307 1.00 44.73  ? 971  TYR A CZ    1 
ATOM   7858  O OH    . TYR B 2 974  ? 144.197 158.716 127.455 1.00 44.73  ? 971  TYR A OH    1 
ATOM   7859  N N     . LEU B 2 975  ? 146.109 155.760 132.940 1.00 44.73  ? 972  LEU A N     1 
ATOM   7860  C CA    . LEU B 2 975  ? 144.710 155.455 133.216 1.00 44.73  ? 972  LEU A CA    1 
ATOM   7861  C C     . LEU B 2 975  ? 144.265 156.018 134.560 1.00 44.73  ? 972  LEU A C     1 
ATOM   7862  O O     . LEU B 2 975  ? 143.069 156.251 134.766 1.00 44.73  ? 972  LEU A O     1 
ATOM   7863  C CB    . LEU B 2 975  ? 144.486 153.946 133.159 1.00 44.73  ? 972  LEU A CB    1 
ATOM   7864  C CG    . LEU B 2 975  ? 144.455 153.365 131.743 1.00 44.73  ? 972  LEU A CG    1 
ATOM   7865  C CD1   . LEU B 2 975  ? 144.156 151.878 131.771 1.00 44.73  ? 972  LEU A CD1   1 
ATOM   7866  C CD2   . LEU B 2 975  ? 143.437 154.100 130.888 1.00 44.73  ? 972  LEU A CD2   1 
ATOM   7867  N N     . SER B 2 976  ? 145.204 156.235 135.483 1.00 44.73  ? 973  SER A N     1 
ATOM   7868  C CA    . SER B 2 976  ? 144.871 156.921 136.727 1.00 44.73  ? 973  SER A CA    1 
ATOM   7869  C C     . SER B 2 976  ? 144.452 158.359 136.454 1.00 44.73  ? 973  SER A C     1 
ATOM   7870  O O     . SER B 2 976  ? 143.543 158.890 137.101 1.00 44.73  ? 973  SER A O     1 
ATOM   7871  C CB    . SER B 2 976  ? 146.059 156.876 137.687 1.00 44.73  ? 973  SER A CB    1 
ATOM   7872  O OG    . SER B 2 976  ? 147.161 157.595 137.165 1.00 44.73  ? 973  SER A OG    1 
ATOM   7873  N N     . GLN B 2 977  ? 145.117 159.011 135.498 1.00 44.73  ? 974  GLN A N     1 
ATOM   7874  C CA    . GLN B 2 977  ? 144.734 160.368 135.123 1.00 44.73  ? 974  GLN A CA    1 
ATOM   7875  C C     . GLN B 2 977  ? 143.385 160.384 134.418 1.00 44.73  ? 974  GLN A C     1 
ATOM   7876  O O     . GLN B 2 977  ? 142.667 161.390 134.454 1.00 44.73  ? 974  GLN A O     1 
ATOM   7877  C CB    . GLN B 2 977  ? 145.808 160.986 134.230 1.00 44.73  ? 974  GLN A CB    1 
ATOM   7878  C CG    . GLN B 2 977  ? 147.229 160.599 134.595 1.00 44.73  ? 974  GLN A CG    1 
ATOM   7879  C CD    . GLN B 2 977  ? 147.684 161.216 135.897 1.00 44.73  ? 974  GLN A CD    1 
ATOM   7880  O OE1   . GLN B 2 977  ? 147.309 162.339 136.229 1.00 44.73  ? 974  GLN A OE1   1 
ATOM   7881  N NE2   . GLN B 2 977  ? 148.501 160.484 136.645 1.00 44.73  ? 974  GLN A NE2   1 
ATOM   7882  N N     . VAL B 2 978  ? 143.024 159.276 133.767 1.00 44.73  ? 975  VAL A N     1 
ATOM   7883  C CA    . VAL B 2 978  ? 141.802 159.242 132.970 1.00 44.73  ? 975  VAL A CA    1 
ATOM   7884  C C     . VAL B 2 978  ? 140.566 159.275 133.861 1.00 44.73  ? 975  VAL A C     1 
ATOM   7885  O O     . VAL B 2 978  ? 139.585 159.962 133.552 1.00 44.73  ? 975  VAL A O     1 
ATOM   7886  C CB    . VAL B 2 978  ? 141.805 158.010 132.047 1.00 44.73  ? 975  VAL A CB    1 
ATOM   7887  C CG1   . VAL B 2 978  ? 140.495 157.911 131.288 1.00 44.73  ? 975  VAL A CG1   1 
ATOM   7888  C CG2   . VAL B 2 978  ? 142.972 158.080 131.081 1.00 44.73  ? 975  VAL A CG2   1 
ATOM   7889  N N     . ILE B 2 979  ? 140.586 158.539 134.977 1.00 44.73  ? 976  ILE A N     1 
ATOM   7890  C CA    . ILE B 2 979  ? 139.394 158.460 135.818 1.00 44.73  ? 976  ILE A CA    1 
ATOM   7891  C C     . ILE B 2 979  ? 139.060 159.825 136.406 1.00 44.73  ? 976  ILE A C     1 
ATOM   7892  O O     . ILE B 2 979  ? 137.890 160.132 136.660 1.00 44.73  ? 976  ILE A O     1 
ATOM   7893  C CB    . ILE B 2 979  ? 139.558 157.391 136.915 1.00 44.73  ? 976  ILE A CB    1 
ATOM   7894  C CG1   . ILE B 2 979  ? 140.696 157.734 137.868 1.00 44.73  ? 976  ILE A CG1   1 
ATOM   7895  C CG2   . ILE B 2 979  ? 139.796 156.029 136.308 1.00 44.73  ? 976  ILE A CG2   1 
ATOM   7896  C CD1   . ILE B 2 979  ? 140.763 156.800 139.050 1.00 44.73  ? 976  ILE A CD1   1 
ATOM   7897  N N     . HIS B 2 980  ? 140.071 160.665 136.630 1.00 44.73  ? 977  HIS A N     1 
ATOM   7898  C CA    . HIS B 2 980  ? 139.803 162.035 137.052 1.00 44.73  ? 977  HIS A CA    1 
ATOM   7899  C C     . HIS B 2 980  ? 139.060 162.800 135.966 1.00 44.73  ? 977  HIS A C     1 
ATOM   7900  O O     . HIS B 2 980  ? 138.139 163.574 136.251 1.00 44.73  ? 977  HIS A O     1 
ATOM   7901  C CB    . HIS B 2 980  ? 141.104 162.749 137.409 1.00 44.73  ? 977  HIS A CB    1 
ATOM   7902  C CG    . HIS B 2 980  ? 140.965 164.236 137.502 1.00 44.73  ? 977  HIS A CG    1 
ATOM   7903  N ND1   . HIS B 2 980  ? 141.544 165.096 136.594 1.00 44.73  ? 977  HIS A ND1   1 
ATOM   7904  C CD2   . HIS B 2 980  ? 140.304 165.015 138.390 1.00 44.73  ? 977  HIS A CD2   1 
ATOM   7905  C CE1   . HIS B 2 980  ? 141.251 166.342 136.923 1.00 44.73  ? 977  HIS A CE1   1 
ATOM   7906  N NE2   . HIS B 2 980  ? 140.499 166.320 138.008 1.00 44.73  ? 977  HIS A NE2   1 
ATOM   7907  N N     . GLU B 2 981  ? 139.455 162.599 134.707 1.00 44.73  ? 978  GLU A N     1 
ATOM   7908  C CA    . GLU B 2 981  ? 138.754 163.244 133.604 1.00 44.73  ? 978  GLU A CA    1 
ATOM   7909  C C     . GLU B 2 981  ? 137.332 162.715 133.475 1.00 44.73  ? 978  GLU A C     1 
ATOM   7910  O O     . GLU B 2 981  ? 136.408 163.469 133.148 1.00 44.73  ? 978  GLU A O     1 
ATOM   7911  C CB    . GLU B 2 981  ? 139.524 163.037 132.301 1.00 44.73  ? 978  GLU A CB    1 
ATOM   7912  C CG    . GLU B 2 981  ? 140.815 163.831 132.215 1.00 44.73  ? 978  GLU A CG    1 
ATOM   7913  C CD    . GLU B 2 981  ? 140.615 165.213 131.628 1.00 44.73  ? 978  GLU A CD    1 
ATOM   7914  O OE1   . GLU B 2 981  ? 139.452 165.591 131.371 1.00 44.73  ? 978  GLU A OE1   1 
ATOM   7915  O OE2   . GLU B 2 981  ? 141.621 165.924 131.424 1.00 44.73  ? 978  GLU A OE2   1 
ATOM   7916  N N     . ILE B 2 982  ? 137.138 161.418 133.724 1.00 44.73  ? 979  ILE A N     1 
ATOM   7917  C CA    . ILE B 2 982  ? 135.809 160.825 133.605 1.00 44.73  ? 979  ILE A CA    1 
ATOM   7918  C C     . ILE B 2 982  ? 134.880 161.380 134.676 1.00 44.73  ? 979  ILE A C     1 
ATOM   7919  O O     . ILE B 2 982  ? 133.756 161.808 134.388 1.00 44.73  ? 979  ILE A O     1 
ATOM   7920  C CB    . ILE B 2 982  ? 135.896 159.292 133.684 1.00 44.73  ? 979  ILE A CB    1 
ATOM   7921  C CG1   . ILE B 2 982  ? 136.691 158.737 132.505 1.00 44.73  ? 979  ILE A CG1   1 
ATOM   7922  C CG2   . ILE B 2 982  ? 134.505 158.684 133.720 1.00 44.73  ? 979  ILE A CG2   1 
ATOM   7923  C CD1   . ILE B 2 982  ? 137.199 157.338 132.737 1.00 44.73  ? 979  ILE A CD1   1 
ATOM   7924  N N     . VAL B 2 983  ? 135.335 161.383 135.931 1.00 44.73  ? 980  VAL A N     1 
ATOM   7925  C CA    . VAL B 2 983  ? 134.472 161.829 137.019 1.00 44.73  ? 980  VAL A CA    1 
ATOM   7926  C C     . VAL B 2 983  ? 134.205 163.325 136.914 1.00 44.73  ? 980  VAL A C     1 
ATOM   7927  O O     . VAL B 2 983  ? 133.098 163.792 137.208 1.00 44.73  ? 980  VAL A O     1 
ATOM   7928  C CB    . VAL B 2 983  ? 135.071 161.440 138.385 1.00 44.73  ? 980  VAL A CB    1 
ATOM   7929  C CG1   . VAL B 2 983  ? 135.245 159.933 138.472 1.00 44.73  ? 980  VAL A CG1   1 
ATOM   7930  C CG2   . VAL B 2 983  ? 136.398 162.145 138.629 1.00 44.73  ? 980  VAL A CG2   1 
ATOM   7931  N N     . ASP B 2 984  ? 135.203 164.101 136.488 1.00 44.73  ? 981  ASP A N     1 
ATOM   7932  C CA    . ASP B 2 984  ? 134.992 165.531 136.291 1.00 44.73  ? 981  ASP A CA    1 
ATOM   7933  C C     . ASP B 2 984  ? 134.007 165.782 135.158 1.00 44.73  ? 981  ASP A C     1 
ATOM   7934  O O     . ASP B 2 984  ? 133.162 166.682 135.238 1.00 44.73  ? 981  ASP A O     1 
ATOM   7935  C CB    . ASP B 2 984  ? 136.323 166.225 136.014 1.00 44.73  ? 981  ASP A CB    1 
ATOM   7936  C CG    . ASP B 2 984  ? 136.180 167.727 135.886 1.00 44.73  ? 981  ASP A CG    1 
ATOM   7937  O OD1   . ASP B 2 984  ? 135.357 168.314 136.620 1.00 44.73  ? 981  ASP A OD1   1 
ATOM   7938  O OD2   . ASP B 2 984  ? 136.891 168.321 135.050 1.00 44.73  ? 981  ASP A OD2   1 
ATOM   7939  N N     . LEU B 2 985  ? 134.112 164.999 134.083 1.00 44.73  ? 982  LEU A N     1 
ATOM   7940  C CA    . LEU B 2 985  ? 133.164 165.123 132.983 1.00 44.73  ? 982  LEU A CA    1 
ATOM   7941  C C     . LEU B 2 985  ? 131.775 164.664 133.403 1.00 44.73  ? 982  LEU A C     1 
ATOM   7942  O O     . LEU B 2 985  ? 130.771 165.302 133.064 1.00 44.73  ? 982  LEU A O     1 
ATOM   7943  C CB    . LEU B 2 985  ? 133.653 164.312 131.784 1.00 44.73  ? 982  LEU A CB    1 
ATOM   7944  C CG    . LEU B 2 985  ? 132.817 164.380 130.508 1.00 44.73  ? 982  LEU A CG    1 
ATOM   7945  C CD1   . LEU B 2 985  ? 132.798 165.800 129.976 1.00 44.73  ? 982  LEU A CD1   1 
ATOM   7946  C CD2   . LEU B 2 985  ? 133.341 163.416 129.464 1.00 44.73  ? 982  LEU A CD2   1 
ATOM   7947  N N     . MET B 2 986  ? 131.698 163.557 134.145 1.00 44.73  ? 983  MET A N     1 
ATOM   7948  C CA    . MET B 2 986  ? 130.404 162.973 134.480 1.00 44.73  ? 983  MET A CA    1 
ATOM   7949  C C     . MET B 2 986  ? 129.607 163.865 135.422 1.00 44.73  ? 983  MET A C     1 
ATOM   7950  O O     . MET B 2 986  ? 128.398 164.041 135.240 1.00 44.73  ? 983  MET A O     1 
ATOM   7951  C CB    . MET B 2 986  ? 130.597 161.588 135.092 1.00 44.73  ? 983  MET A CB    1 
ATOM   7952  C CG    . MET B 2 986  ? 129.369 160.707 135.004 1.00 44.73  ? 983  MET A CG    1 
ATOM   7953  S SD    . MET B 2 986  ? 129.341 159.451 136.290 1.00 44.73  ? 983  MET A SD    1 
ATOM   7954  C CE    . MET B 2 986  ? 131.052 158.937 136.260 1.00 44.73  ? 983  MET A CE    1 
ATOM   7955  N N     . ILE B 2 987  ? 130.261 164.434 136.435 1.00 44.73  ? 984  ILE A N     1 
ATOM   7956  C CA    . ILE B 2 987  ? 129.551 165.283 137.386 1.00 44.73  ? 984  ILE A CA    1 
ATOM   7957  C C     . ILE B 2 987  ? 129.094 166.571 136.714 1.00 44.73  ? 984  ILE A C     1 
ATOM   7958  O O     . ILE B 2 987  ? 128.013 167.093 137.012 1.00 44.73  ? 984  ILE A O     1 
ATOM   7959  C CB    . ILE B 2 987  ? 130.431 165.558 138.618 1.00 44.73  ? 984  ILE A CB    1 
ATOM   7960  C CG1   . ILE B 2 987  ? 130.797 164.244 139.311 1.00 44.73  ? 984  ILE A CG1   1 
ATOM   7961  C CG2   . ILE B 2 987  ? 129.725 166.489 139.588 1.00 44.73  ? 984  ILE A CG2   1 
ATOM   7962  C CD1   . ILE B 2 987  ? 129.643 163.272 139.441 1.00 44.73  ? 984  ILE A CD1   1 
ATOM   7963  N N     . HIS B 2 988  ? 129.905 167.102 135.797 1.00 44.73  ? 985  HIS A N     1 
ATOM   7964  C CA    . HIS B 2 988  ? 129.534 168.330 135.102 1.00 44.73  ? 985  HIS A CA    1 
ATOM   7965  C C     . HIS B 2 988  ? 128.267 168.138 134.277 1.00 44.73  ? 985  HIS A C     1 
ATOM   7966  O O     . HIS B 2 988  ? 127.397 169.017 134.249 1.00 44.73  ? 985  HIS A O     1 
ATOM   7967  C CB    . HIS B 2 988  ? 130.689 168.800 134.217 1.00 44.73  ? 985  HIS A CB    1 
ATOM   7968  C CG    . HIS B 2 988  ? 130.328 169.919 133.292 1.00 44.73  ? 985  HIS A CG    1 
ATOM   7969  N ND1   . HIS B 2 988  ? 129.512 170.963 133.669 1.00 44.73  ? 985  HIS A ND1   1 
ATOM   7970  C CD2   . HIS B 2 988  ? 130.677 170.160 132.006 1.00 44.73  ? 985  HIS A CD2   1 
ATOM   7971  C CE1   . HIS B 2 988  ? 129.371 171.797 132.654 1.00 44.73  ? 985  HIS A CE1   1 
ATOM   7972  N NE2   . HIS B 2 988  ? 130.068 171.333 131.633 1.00 44.73  ? 985  HIS A NE2   1 
ATOM   7973  N N     . TYR B 2 989  ? 128.143 166.999 133.599 1.00 44.73  ? 986  TYR A N     1 
ATOM   7974  C CA    . TYR B 2 989  ? 126.963 166.711 132.796 1.00 44.73  ? 986  TYR A CA    1 
ATOM   7975  C C     . TYR B 2 989  ? 125.880 165.957 133.554 1.00 44.73  ? 986  TYR A C     1 
ATOM   7976  O O     . TYR B 2 989  ? 124.777 165.802 133.020 1.00 44.73  ? 986  TYR A O     1 
ATOM   7977  C CB    . TYR B 2 989  ? 127.346 165.901 131.554 1.00 44.73  ? 986  TYR A CB    1 
ATOM   7978  C CG    . TYR B 2 989  ? 127.931 166.724 130.433 1.00 44.73  ? 986  TYR A CG    1 
ATOM   7979  C CD1   . TYR B 2 989  ? 127.159 167.655 129.752 1.00 44.73  ? 986  TYR A CD1   1 
ATOM   7980  C CD2   . TYR B 2 989  ? 129.250 166.558 130.043 1.00 44.73  ? 986  TYR A CD2   1 
ATOM   7981  C CE1   . TYR B 2 989  ? 127.691 168.406 128.723 1.00 44.73  ? 986  TYR A CE1   1 
ATOM   7982  C CE2   . TYR B 2 989  ? 129.788 167.302 129.017 1.00 44.73  ? 986  TYR A CE2   1 
ATOM   7983  C CZ    . TYR B 2 989  ? 129.007 168.225 128.360 1.00 44.73  ? 986  TYR A CZ    1 
ATOM   7984  O OH    . TYR B 2 989  ? 129.544 168.967 127.335 1.00 44.73  ? 986  TYR A OH    1 
ATOM   7985  N N     . GLN B 2 990  ? 126.159 165.496 134.775 1.00 44.73  ? 987  GLN A N     1 
ATOM   7986  C CA    . GLN B 2 990  ? 125.238 164.631 135.516 1.00 44.73  ? 987  GLN A CA    1 
ATOM   7987  C C     . GLN B 2 990  ? 124.858 163.414 134.679 1.00 44.73  ? 987  GLN A C     1 
ATOM   7988  O O     . GLN B 2 990  ? 123.694 163.013 134.612 1.00 44.73  ? 987  GLN A O     1 
ATOM   7989  C CB    . GLN B 2 990  ? 123.994 165.400 135.964 1.00 44.73  ? 987  GLN A CB    1 
ATOM   7990  C CG    . GLN B 2 990  ? 124.297 166.620 136.816 1.00 44.73  ? 987  GLN A CG    1 
ATOM   7991  C CD    . GLN B 2 990  ? 123.114 167.054 137.655 1.00 44.73  ? 987  GLN A CD    1 
ATOM   7992  O OE1   . GLN B 2 990  ? 121.962 166.815 137.295 1.00 44.73  ? 987  GLN A OE1   1 
ATOM   7993  N NE2   . GLN B 2 990  ? 123.393 167.697 138.782 1.00 44.73  ? 987  GLN A NE2   1 
ATOM   7994  N N     . ALA B 2 991  ? 125.858 162.821 134.036 1.00 44.73  ? 988  ALA A N     1 
ATOM   7995  C CA    . ALA B 2 991  ? 125.652 161.817 133.007 1.00 44.73  ? 988  ALA A CA    1 
ATOM   7996  C C     . ALA B 2 991  ? 125.911 160.415 133.547 1.00 44.73  ? 988  ALA A C     1 
ATOM   7997  O O     . ALA B 2 991  ? 126.247 160.212 134.715 1.00 44.73  ? 988  ALA A O     1 
ATOM   7998  C CB    . ALA B 2 991  ? 126.553 162.105 131.805 1.00 44.73  ? 988  ALA A CB    1 
ATOM   7999  N N     . VAL B 2 992  ? 125.739 159.432 132.669 1.00 44.73  ? 989  VAL A N     1 
ATOM   8000  C CA    . VAL B 2 992  ? 126.058 158.039 132.945 1.00 44.73  ? 989  VAL A CA    1 
ATOM   8001  C C     . VAL B 2 992  ? 127.104 157.586 131.936 1.00 44.73  ? 989  VAL A C     1 
ATOM   8002  O O     . VAL B 2 992  ? 126.973 157.835 130.732 1.00 44.73  ? 989  VAL A O     1 
ATOM   8003  C CB    . VAL B 2 992  ? 124.799 157.147 132.905 1.00 44.73  ? 989  VAL A CB    1 
ATOM   8004  C CG1   . VAL B 2 992  ? 124.146 157.173 131.537 1.00 44.73  ? 989  VAL A CG1   1 
ATOM   8005  C CG2   . VAL B 2 992  ? 125.147 155.726 133.294 1.00 44.73  ? 989  VAL A CG2   1 
ATOM   8006  N N     . VAL B 2 993  ? 128.165 156.959 132.432 1.00 44.73  ? 990  VAL A N     1 
ATOM   8007  C CA    . VAL B 2 993  ? 129.305 156.580 131.607 1.00 44.73  ? 990  VAL A CA    1 
ATOM   8008  C C     . VAL B 2 993  ? 129.155 155.123 131.195 1.00 44.73  ? 990  VAL A C     1 
ATOM   8009  O O     . VAL B 2 993  ? 128.851 154.258 132.026 1.00 44.73  ? 990  VAL A O     1 
ATOM   8010  C CB    . VAL B 2 993  ? 130.634 156.831 132.342 1.00 44.73  ? 990  VAL A CB    1 
ATOM   8011  C CG1   . VAL B 2 993  ? 130.677 156.092 133.663 1.00 44.73  ? 990  VAL A CG1   1 
ATOM   8012  C CG2   . VAL B 2 993  ? 131.807 156.437 131.464 1.00 44.73  ? 990  VAL A CG2   1 
ATOM   8013  N N     . VAL B 2 994  ? 129.337 154.857 129.905 1.00 44.73  ? 991  VAL A N     1 
ATOM   8014  C CA    . VAL B 2 994  ? 129.152 153.529 129.333 1.00 44.73  ? 991  VAL A CA    1 
ATOM   8015  C C     . VAL B 2 994  ? 130.514 153.025 128.881 1.00 44.73  ? 991  VAL A C     1 
ATOM   8016  O O     . VAL B 2 994  ? 131.103 153.566 127.936 1.00 44.73  ? 991  VAL A O     1 
ATOM   8017  C CB    . VAL B 2 994  ? 128.156 153.538 128.168 1.00 44.73  ? 991  VAL A CB    1 
ATOM   8018  C CG1   . VAL B 2 994  ? 128.169 152.202 127.454 1.00 44.73  ? 991  VAL A CG1   1 
ATOM   8019  C CG2   . VAL B 2 994  ? 126.763 153.859 128.667 1.00 44.73  ? 991  VAL A CG2   1 
ATOM   8020  N N     . LEU B 2 995  ? 131.012 151.994 129.548 1.00 44.73  ? 992  LEU A N     1 
ATOM   8021  C CA    . LEU B 2 995  ? 132.270 151.366 129.178 1.00 44.73  ? 992  LEU A CA    1 
ATOM   8022  C C     . LEU B 2 995  ? 131.969 150.220 128.212 1.00 44.73  ? 992  LEU A C     1 
ATOM   8023  O O     . LEU B 2 995  ? 130.847 150.094 127.713 1.00 44.73  ? 992  LEU A O     1 
ATOM   8024  C CB    . LEU B 2 995  ? 133.014 150.900 130.435 1.00 44.73  ? 992  LEU A CB    1 
ATOM   8025  C CG    . LEU B 2 995  ? 133.862 151.902 131.225 1.00 44.73  ? 992  LEU A CG    1 
ATOM   8026  C CD1   . LEU B 2 995  ? 135.021 152.410 130.385 1.00 44.73  ? 992  LEU A CD1   1 
ATOM   8027  C CD2   . LEU B 2 995  ? 133.034 153.055 131.771 1.00 44.73  ? 992  LEU A CD2   1 
ATOM   8028  N N     . GLU B 2 996  ? 132.956 149.375 127.930 1.00 44.73  ? 993  GLU A N     1 
ATOM   8029  C CA    . GLU B 2 996  ? 132.742 148.168 127.144 1.00 44.73  ? 993  GLU A CA    1 
ATOM   8030  C C     . GLU B 2 996  ? 133.196 146.966 127.959 1.00 44.73  ? 993  GLU A C     1 
ATOM   8031  O O     . GLU B 2 996  ? 134.290 146.977 128.532 1.00 44.73  ? 993  GLU A O     1 
ATOM   8032  C CB    . GLU B 2 996  ? 133.477 148.239 125.795 1.00 44.73  ? 993  GLU A CB    1 
ATOM   8033  C CG    . GLU B 2 996  ? 134.997 148.186 125.861 1.00 44.73  ? 993  GLU A CG    1 
ATOM   8034  C CD    . GLU B 2 996  ? 135.626 149.543 126.109 1.00 44.73  ? 993  GLU A CD    1 
ATOM   8035  O OE1   . GLU B 2 996  ? 134.902 150.472 126.526 1.00 44.73  ? 993  GLU A OE1   1 
ATOM   8036  O OE2   . GLU B 2 996  ? 136.846 149.682 125.884 1.00 44.73  ? 993  GLU A OE2   1 
ATOM   8037  N N     . ASN B 2 997  ? 132.345 145.946 128.038 1.00 44.73  ? 994  ASN A N     1 
ATOM   8038  C CA    . ASN B 2 997  ? 132.697 144.757 128.800 1.00 44.73  ? 994  ASN A CA    1 
ATOM   8039  C C     . ASN B 2 997  ? 133.733 143.933 128.049 1.00 44.73  ? 994  ASN A C     1 
ATOM   8040  O O     . ASN B 2 997  ? 133.677 143.796 126.824 1.00 44.73  ? 994  ASN A O     1 
ATOM   8041  C CB    . ASN B 2 997  ? 131.457 143.914 129.102 1.00 44.73  ? 994  ASN A CB    1 
ATOM   8042  C CG    . ASN B 2 997  ? 130.619 143.635 127.874 1.00 44.73  ? 994  ASN A CG    1 
ATOM   8043  O OD1   . ASN B 2 997  ? 130.930 144.091 126.775 1.00 44.73  ? 994  ASN A OD1   1 
ATOM   8044  N ND2   . ASN B 2 997  ? 129.545 142.875 128.057 1.00 44.73  ? 994  ASN A ND2   1 
ATOM   8045  N N     . LEU B 2 998  ? 134.690 143.388 128.797 1.00 44.73  ? 995  LEU A N     1 
ATOM   8046  C CA    . LEU B 2 998  ? 135.800 142.658 128.202 1.00 44.73  ? 995  LEU A CA    1 
ATOM   8047  C C     . LEU B 2 998  ? 135.437 141.228 127.831 1.00 44.73  ? 995  LEU A C     1 
ATOM   8048  O O     . LEU B 2 998  ? 136.241 140.553 127.179 1.00 44.73  ? 995  LEU A O     1 
ATOM   8049  C CB    . LEU B 2 998  ? 136.996 142.653 129.158 1.00 44.73  ? 995  LEU A CB    1 
ATOM   8050  C CG    . LEU B 2 998  ? 137.941 143.860 129.123 1.00 44.73  ? 995  LEU A CG    1 
ATOM   8051  C CD1   . LEU B 2 998  ? 138.600 143.993 127.757 1.00 44.73  ? 995  LEU A CD1   1 
ATOM   8052  C CD2   . LEU B 2 998  ? 137.235 145.151 129.513 1.00 44.73  ? 995  LEU A CD2   1 
ATOM   8053  N N     . ASN B 2 999  ? 134.253 140.755 128.223 1.00 37.27  ? 996  ASN A N     1 
ATOM   8054  C CA    . ASN B 2 999  ? 133.865 139.384 127.913 1.00 37.27  ? 996  ASN A CA    1 
ATOM   8055  C C     . ASN B 2 999  ? 133.722 139.168 126.412 1.00 37.27  ? 996  ASN A C     1 
ATOM   8056  O O     . ASN B 2 999  ? 134.095 138.109 125.893 1.00 37.27  ? 996  ASN A O     1 
ATOM   8057  C CB    . ASN B 2 999  ? 132.565 139.036 128.636 1.00 37.27  ? 996  ASN A CB    1 
ATOM   8058  C CG    . ASN B 2 999  ? 132.681 139.177 130.138 1.00 37.27  ? 996  ASN A CG    1 
ATOM   8059  O OD1   . ASN B 2 999  ? 133.766 139.409 130.669 1.00 37.27  ? 996  ASN A OD1   1 
ATOM   8060  N ND2   . ASN B 2 999  ? 131.559 139.039 130.834 1.00 37.27  ? 996  ASN A ND2   1 
ATOM   8061  N N     . PHE B 2 1000 ? 133.190 140.153 125.696 1.00 36.15  ? 997  PHE A N     1 
ATOM   8062  C CA    . PHE B 2 1000 ? 132.881 140.017 124.279 1.00 36.15  ? 997  PHE A CA    1 
ATOM   8063  C C     . PHE B 2 1000 ? 133.873 140.809 123.439 1.00 36.15  ? 997  PHE A C     1 
ATOM   8064  O O     . PHE B 2 1000 ? 134.114 141.991 123.702 1.00 36.15  ? 997  PHE A O     1 
ATOM   8065  C CB    . PHE B 2 1000 ? 131.454 140.486 123.990 1.00 36.15  ? 997  PHE A CB    1 
ATOM   8066  C CG    . PHE B 2 1000 ? 130.420 139.852 124.872 1.00 36.15  ? 997  PHE A CG    1 
ATOM   8067  C CD1   . PHE B 2 1000 ? 130.491 138.507 125.184 1.00 36.15  ? 997  PHE A CD1   1 
ATOM   8068  C CD2   . PHE B 2 1000 ? 129.369 140.597 125.378 1.00 36.15  ? 997  PHE A CD2   1 
ATOM   8069  C CE1   . PHE B 2 1000 ? 129.542 137.917 125.993 1.00 36.15  ? 997  PHE A CE1   1 
ATOM   8070  C CE2   . PHE B 2 1000 ? 128.416 140.013 126.189 1.00 36.15  ? 997  PHE A CE2   1 
ATOM   8071  C CZ    . PHE B 2 1000 ? 128.502 138.671 126.495 1.00 36.15  ? 997  PHE A CZ    1 
ATOM   8072  N N     . GLY B 2 1001 ? 134.446 140.152 122.431 1.00 41.33  ? 998  GLY A N     1 
ATOM   8073  C CA    . GLY B 2 1001 ? 135.284 140.826 121.461 1.00 41.33  ? 998  GLY A CA    1 
ATOM   8074  C C     . GLY B 2 1001 ? 136.718 141.015 121.913 1.00 41.33  ? 998  GLY A C     1 
ATOM   8075  O O     . GLY B 2 1001 ? 137.125 140.652 123.019 1.00 41.33  ? 998  GLY A O     1 
ATOM   8076  N N     . PHE B 2 1002 ? 137.504 141.598 121.010 1.00 46.22  ? 999  PHE A N     1 
ATOM   8077  C CA    . PHE B 2 1002 ? 138.896 141.924 121.277 1.00 46.22  ? 999  PHE A CA    1 
ATOM   8078  C C     . PHE B 2 1002 ? 139.306 143.093 120.389 1.00 46.22  ? 999  PHE A C     1 
ATOM   8079  O O     . PHE B 2 1002 ? 138.669 143.383 119.374 1.00 46.22  ? 999  PHE A O     1 
ATOM   8080  C CB    . PHE B 2 1002 ? 139.791 140.696 121.071 1.00 46.22  ? 999  PHE A CB    1 
ATOM   8081  C CG    . PHE B 2 1002 ? 139.736 140.120 119.678 1.00 46.22  ? 999  PHE A CG    1 
ATOM   8082  C CD1   . PHE B 2 1002 ? 140.441 140.698 118.633 1.00 46.22  ? 999  PHE A CD1   1 
ATOM   8083  C CD2   . PHE B 2 1002 ? 138.979 138.988 119.419 1.00 46.22  ? 999  PHE A CD2   1 
ATOM   8084  C CE1   . PHE B 2 1002 ? 140.386 140.165 117.358 1.00 46.22  ? 999  PHE A CE1   1 
ATOM   8085  C CE2   . PHE B 2 1002 ? 138.922 138.448 118.146 1.00 46.22  ? 999  PHE A CE2   1 
ATOM   8086  C CZ    . PHE B 2 1002 ? 139.626 139.037 117.116 1.00 46.22  ? 999  PHE A CZ    1 
ATOM   8087  N N     . LYS B 2 1003 ? 140.392 143.757 120.773 1.00 42.05  ? 1000 LYS A N     1 
ATOM   8088  C CA    . LYS B 2 1003 ? 140.932 144.893 120.040 1.00 42.05  ? 1000 LYS A CA    1 
ATOM   8089  C C     . LYS B 2 1003 ? 142.297 144.547 119.463 1.00 42.05  ? 1000 LYS A C     1 
ATOM   8090  O O     . LYS B 2 1003 ? 143.034 143.723 120.011 1.00 42.05  ? 1000 LYS A O     1 
ATOM   8091  C CB    . LYS B 2 1003 ? 141.032 146.167 120.916 1.00 42.05  ? 1000 LYS A CB    1 
ATOM   8092  C CG    . LYS B 2 1003 ? 139.840 146.494 121.836 1.00 42.05  ? 1000 LYS A CG    1 
ATOM   8093  C CD    . LYS B 2 1003 ? 138.507 146.138 121.176 1.00 42.05  ? 1000 LYS A CD    1 
ATOM   8094  C CE    . LYS B 2 1003 ? 137.284 146.542 121.987 1.00 42.05  ? 1000 LYS A CE    1 
ATOM   8095  N NZ    . LYS B 2 1003 ? 137.429 146.335 123.450 1.00 42.05  ? 1000 LYS A NZ    1 
ATOM   8096  N N     . SER B 2 1004 ? 142.617 145.193 118.345 1.00 39.41  ? 1001 SER A N     1 
ATOM   8097  C CA    . SER B 2 1004 ? 143.814 144.884 117.584 1.00 39.41  ? 1001 SER A CA    1 
ATOM   8098  C C     . SER B 2 1004 ? 145.071 145.354 118.308 1.00 39.41  ? 1001 SER A C     1 
ATOM   8099  O O     . SER B 2 1004 ? 145.024 146.120 119.274 1.00 39.41  ? 1001 SER A O     1 
ATOM   8100  C CB    . SER B 2 1004 ? 143.753 145.532 116.202 1.00 39.41  ? 1001 SER A CB    1 
ATOM   8101  O OG    . SER B 2 1004 ? 143.785 146.945 116.310 1.00 39.41  ? 1001 SER A OG    1 
ATOM   8102  N N     . LYS B 2 1005 ? 146.214 144.873 117.813 1.00 40.47  ? 1002 LYS A N     1 
ATOM   8103  C CA    . LYS B 2 1005 ? 147.504 145.260 118.370 1.00 40.47  ? 1002 LYS A CA    1 
ATOM   8104  C C     . LYS B 2 1005 ? 147.773 146.749 118.190 1.00 40.47  ? 1002 LYS A C     1 
ATOM   8105  O O     . LYS B 2 1005 ? 148.506 147.347 118.986 1.00 40.47  ? 1002 LYS A O     1 
ATOM   8106  C CB    . LYS B 2 1005 ? 148.612 144.435 117.713 1.00 40.47  ? 1002 LYS A CB    1 
ATOM   8107  C CG    . LYS B 2 1005 ? 150.025 144.757 118.175 1.00 40.47  ? 1002 LYS A CG    1 
ATOM   8108  C CD    . LYS B 2 1005 ? 151.049 143.983 117.354 1.00 40.47  ? 1002 LYS A CD    1 
ATOM   8109  C CE    . LYS B 2 1005 ? 150.678 142.507 117.265 1.00 40.47  ? 1002 LYS A CE    1 
ATOM   8110  N NZ    . LYS B 2 1005 ? 151.846 141.582 117.232 1.00 40.47  ? 1002 LYS A NZ    1 
ATOM   8111  N N     . ARG B 2 1006 ? 147.195 147.366 117.155 1.00 41.99  ? 1003 ARG A N     1 
ATOM   8112  C CA    . ARG B 2 1006 ? 147.415 148.788 116.919 1.00 41.99  ? 1003 ARG A CA    1 
ATOM   8113  C C     . ARG B 2 1006 ? 146.814 149.661 118.013 1.00 41.99  ? 1003 ARG A C     1 
ATOM   8114  O O     . ARG B 2 1006 ? 147.234 150.813 118.167 1.00 41.99  ? 1003 ARG A O     1 
ATOM   8115  C CB    . ARG B 2 1006 ? 146.844 149.198 115.561 1.00 41.99  ? 1003 ARG A CB    1 
ATOM   8116  C CG    . ARG B 2 1006 ? 147.793 148.989 114.393 1.00 41.99  ? 1003 ARG A CG    1 
ATOM   8117  C CD    . ARG B 2 1006 ? 147.268 149.665 113.127 1.00 41.99  ? 1003 ARG A CD    1 
ATOM   8118  N NE    . ARG B 2 1006 ? 145.959 149.195 112.677 1.00 41.99  ? 1003 ARG A NE    1 
ATOM   8119  C CZ    . ARG B 2 1006 ? 145.596 147.927 112.511 1.00 41.99  ? 1003 ARG A CZ    1 
ATOM   8120  N NH1   . ARG B 2 1006 ? 146.453 146.929 112.659 1.00 41.99  ? 1003 ARG A NH1   1 
ATOM   8121  N NH2   . ARG B 2 1006 ? 144.343 147.655 112.157 1.00 41.99  ? 1003 ARG A NH2   1 
ATOM   8122  N N     . THR B 2 1007 ? 145.844 149.150 118.766 1.00 39.00  ? 1004 THR A N     1 
ATOM   8123  C CA    . THR B 2 1007 ? 145.289 149.903 119.880 1.00 39.00  ? 1004 THR A CA    1 
ATOM   8124  C C     . THR B 2 1007 ? 146.336 150.076 120.975 1.00 39.00  ? 1004 THR A C     1 
ATOM   8125  O O     . THR B 2 1007 ? 147.208 149.227 121.174 1.00 39.00  ? 1004 THR A O     1 
ATOM   8126  C CB    . THR B 2 1007 ? 144.053 149.204 120.442 1.00 39.00  ? 1004 THR A CB    1 
ATOM   8127  O OG1   . THR B 2 1007 ? 144.447 148.005 121.120 1.00 39.00  ? 1004 THR A OG1   1 
ATOM   8128  C CG2   . THR B 2 1007 ? 143.081 148.856 119.324 1.00 39.00  ? 1004 THR A CG2   1 
ATOM   8129  N N     . GLY B 2 1008 ? 146.241 151.195 121.691 1.00 38.49  ? 1005 GLY A N     1 
ATOM   8130  C CA    . GLY B 2 1008 ? 147.272 151.555 122.644 1.00 38.49  ? 1005 GLY A CA    1 
ATOM   8131  C C     . GLY B 2 1008 ? 147.205 150.866 123.988 1.00 38.49  ? 1005 GLY A C     1 
ATOM   8132  O O     . GLY B 2 1008 ? 148.145 151.006 124.775 1.00 38.49  ? 1005 GLY A O     1 
ATOM   8133  N N     . ILE B 2 1009 ? 146.139 150.121 124.271 1.00 34.82  ? 1006 ILE A N     1 
ATOM   8134  C CA    . ILE B 2 1009 ? 145.948 149.470 125.563 1.00 34.82  ? 1006 ILE A CA    1 
ATOM   8135  C C     . ILE B 2 1009 ? 145.739 147.978 125.334 1.00 34.82  ? 1006 ILE A C     1 
ATOM   8136  O O     . ILE B 2 1009 ? 144.946 147.583 124.472 1.00 34.82  ? 1006 ILE A O     1 
ATOM   8137  C CB    . ILE B 2 1009 ? 144.755 150.067 126.334 1.00 34.82  ? 1006 ILE A CB    1 
ATOM   8138  C CG1   . ILE B 2 1009 ? 144.981 151.548 126.652 1.00 34.82  ? 1006 ILE A CG1   1 
ATOM   8139  C CG2   . ILE B 2 1009 ? 144.501 149.290 127.618 1.00 34.82  ? 1006 ILE A CG2   1 
ATOM   8140  C CD1   . ILE B 2 1009 ? 146.351 151.862 127.199 1.00 34.82  ? 1006 ILE A CD1   1 
ATOM   8141  N N     . ALA B 2 1010 ? 146.451 147.156 126.101 1.00 40.33  ? 1007 ALA A N     1 
ATOM   8142  C CA    . ALA B 2 1010 ? 146.307 145.711 125.993 1.00 40.33  ? 1007 ALA A CA    1 
ATOM   8143  C C     . ALA B 2 1010 ? 144.928 145.270 126.469 1.00 40.33  ? 1007 ALA A C     1 
ATOM   8144  O O     . ALA B 2 1010 ? 144.412 145.763 127.476 1.00 40.33  ? 1007 ALA A O     1 
ATOM   8145  C CB    . ALA B 2 1010 ? 147.392 145.005 126.804 1.00 40.33  ? 1007 ALA A CB    1 
ATOM   8146  N N     . GLU B 2 1011 ? 144.335 144.331 125.737 1.00 46.52  ? 1008 GLU A N     1 
ATOM   8147  C CA    . GLU B 2 1011 ? 142.978 143.890 126.031 1.00 46.52  ? 1008 GLU A CA    1 
ATOM   8148  C C     . GLU B 2 1011 ? 142.944 143.015 127.279 1.00 46.52  ? 1008 GLU A C     1 
ATOM   8149  O O     . GLU B 2 1011 ? 143.762 142.103 127.436 1.00 46.52  ? 1008 GLU A O     1 
ATOM   8150  C CB    . GLU B 2 1011 ? 142.403 143.127 124.838 1.00 46.52  ? 1008 GLU A CB    1 
ATOM   8151  C CG    . GLU B 2 1011 ? 140.903 142.885 124.915 1.00 46.52  ? 1008 GLU A CG    1 
ATOM   8152  C CD    . GLU B 2 1011 ? 140.561 141.511 125.461 1.00 46.52  ? 1008 GLU A CD    1 
ATOM   8153  O OE1   . GLU B 2 1011 ? 141.457 140.642 125.490 1.00 46.52  ? 1008 GLU A OE1   1 
ATOM   8154  O OE2   . GLU B 2 1011 ? 139.396 141.300 125.859 1.00 46.52  ? 1008 GLU A OE2   1 
ATOM   8155  N N     . LYS B 2 1012 ? 141.995 143.304 128.167 1.00 40.96  ? 1009 LYS A N     1 
ATOM   8156  C CA    . LYS B 2 1012 ? 141.669 142.498 129.341 1.00 40.96  ? 1009 LYS A CA    1 
ATOM   8157  C C     . LYS B 2 1012 ? 142.838 142.342 130.307 1.00 40.96  ? 1009 LYS A C     1 
ATOM   8158  O O     . LYS B 2 1012 ? 142.797 141.470 131.184 1.00 40.96  ? 1009 LYS A O     1 
ATOM   8159  C CB    . LYS B 2 1012 ? 141.141 141.115 128.938 1.00 40.96  ? 1009 LYS A CB    1 
ATOM   8160  C CG    . LYS B 2 1012 ? 140.087 140.553 129.880 1.00 40.96  ? 1009 LYS A CG    1 
ATOM   8161  C CD    . LYS B 2 1012 ? 139.743 139.114 129.534 1.00 40.96  ? 1009 LYS A CD    1 
ATOM   8162  C CE    . LYS B 2 1012 ? 138.829 139.039 128.326 1.00 40.96  ? 1009 LYS A CE    1 
ATOM   8163  N NZ    . LYS B 2 1012 ? 138.331 137.655 128.096 1.00 40.96  ? 1009 LYS A NZ    1 
ATOM   8164  N N     . ALA B 2 1013 ? 143.880 143.160 130.179 1.00 39.56  ? 1010 ALA A N     1 
ATOM   8165  C CA    . ALA B 2 1013 ? 145.024 143.097 131.079 1.00 39.56  ? 1010 ALA A CA    1 
ATOM   8166  C C     . ALA B 2 1013 ? 145.139 144.349 131.938 1.00 39.56  ? 1010 ALA A C     1 
ATOM   8167  O O     . ALA B 2 1013 ? 145.173 144.257 133.168 1.00 39.56  ? 1010 ALA A O     1 
ATOM   8168  C CB    . ALA B 2 1013 ? 146.314 142.872 130.279 1.00 39.56  ? 1010 ALA A CB    1 
ATOM   8169  N N     . VAL B 2 1014 ? 145.190 145.525 131.320 1.00 44.73  ? 1011 VAL A N     1 
ATOM   8170  C CA    . VAL B 2 1014 ? 145.265 146.782 132.049 1.00 44.73  ? 1011 VAL A CA    1 
ATOM   8171  C C     . VAL B 2 1014 ? 143.908 147.470 132.119 1.00 44.73  ? 1011 VAL A C     1 
ATOM   8172  O O     . VAL B 2 1014 ? 143.569 148.076 133.135 1.00 44.73  ? 1011 VAL A O     1 
ATOM   8173  C CB    . VAL B 2 1014 ? 146.326 147.705 131.411 1.00 44.73  ? 1011 VAL A CB    1 
ATOM   8174  C CG1   . VAL B 2 1014 ? 146.510 148.962 132.244 1.00 44.73  ? 1011 VAL A CG1   1 
ATOM   8175  C CG2   . VAL B 2 1014 ? 147.647 146.968 131.260 1.00 44.73  ? 1011 VAL A CG2   1 
ATOM   8176  N N     . TYR B 2 1015 ? 143.114 147.373 131.050 1.00 44.73  ? 1012 TYR A N     1 
ATOM   8177  C CA    . TYR B 2 1015 ? 141.825 148.055 131.018 1.00 44.73  ? 1012 TYR A CA    1 
ATOM   8178  C C     . TYR B 2 1015 ? 140.799 147.382 131.920 1.00 44.73  ? 1012 TYR A C     1 
ATOM   8179  O O     . TYR B 2 1015 ? 139.875 148.045 132.405 1.00 44.73  ? 1012 TYR A O     1 
ATOM   8180  C CB    . TYR B 2 1015 ? 141.318 148.136 129.581 1.00 44.73  ? 1012 TYR A CB    1 
ATOM   8181  C CG    . TYR B 2 1015 ? 140.336 149.254 129.340 1.00 44.73  ? 1012 TYR A CG    1 
ATOM   8182  C CD1   . TYR B 2 1015 ? 138.992 149.109 129.650 1.00 44.73  ? 1012 TYR A CD1   1 
ATOM   8183  C CD2   . TYR B 2 1015 ? 140.747 150.440 128.759 1.00 44.73  ? 1012 TYR A CD2   1 
ATOM   8184  C CE1   . TYR B 2 1015 ? 138.094 150.128 129.412 1.00 44.73  ? 1012 TYR A CE1   1 
ATOM   8185  C CE2   . TYR B 2 1015 ? 139.860 151.462 128.520 1.00 44.73  ? 1012 TYR A CE2   1 
ATOM   8186  C CZ    . TYR B 2 1015 ? 138.534 151.301 128.845 1.00 44.73  ? 1012 TYR A CZ    1 
ATOM   8187  O OH    . TYR B 2 1015 ? 137.651 152.324 128.603 1.00 44.73  ? 1012 TYR A OH    1 
ATOM   8188  N N     . GLN B 2 1016 ? 140.925 146.073 132.141 1.00 44.73  ? 1013 GLN A N     1 
ATOM   8189  C CA    . GLN B 2 1016 ? 140.043 145.403 133.090 1.00 44.73  ? 1013 GLN A CA    1 
ATOM   8190  C C     . GLN B 2 1016 ? 140.250 145.945 134.499 1.00 44.73  ? 1013 GLN A C     1 
ATOM   8191  O O     . GLN B 2 1016 ? 139.283 146.162 135.239 1.00 44.73  ? 1013 GLN A O     1 
ATOM   8192  C CB    . GLN B 2 1016 ? 140.280 143.894 133.037 1.00 44.73  ? 1013 GLN A CB    1 
ATOM   8193  C CG    . GLN B 2 1016 ? 139.400 143.070 133.957 1.00 44.73  ? 1013 GLN A CG    1 
ATOM   8194  C CD    . GLN B 2 1016 ? 139.400 141.600 133.584 1.00 44.73  ? 1013 GLN A CD    1 
ATOM   8195  O OE1   . GLN B 2 1016 ? 138.556 141.143 132.813 1.00 44.73  ? 1013 GLN A OE1   1 
ATOM   8196  N NE2   . GLN B 2 1016 ? 140.363 140.855 134.114 1.00 44.73  ? 1013 GLN A NE2   1 
ATOM   8197  N N     . GLN B 2 1017 ? 141.507 146.174 134.886 1.00 44.73  ? 1014 GLN A N     1 
ATOM   8198  C CA    . GLN B 2 1017 ? 141.796 146.834 136.153 1.00 44.73  ? 1014 GLN A CA    1 
ATOM   8199  C C     . GLN B 2 1017 ? 141.411 148.307 136.124 1.00 44.73  ? 1014 GLN A C     1 
ATOM   8200  O O     . GLN B 2 1017 ? 141.130 148.885 137.178 1.00 44.73  ? 1014 GLN A O     1 
ATOM   8201  C CB    . GLN B 2 1017 ? 143.280 146.673 136.492 1.00 44.73  ? 1014 GLN A CB    1 
ATOM   8202  C CG    . GLN B 2 1017 ? 143.669 147.070 137.907 1.00 44.73  ? 1014 GLN A CG    1 
ATOM   8203  C CD    . GLN B 2 1017 ? 144.062 148.528 138.025 1.00 44.73  ? 1014 GLN A CD    1 
ATOM   8204  O OE1   . GLN B 2 1017 ? 144.530 149.137 137.063 1.00 44.73  ? 1014 GLN A OE1   1 
ATOM   8205  N NE2   . GLN B 2 1017 ? 143.887 149.092 139.213 1.00 44.73  ? 1014 GLN A NE2   1 
ATOM   8206  N N     . PHE B 2 1018 ? 141.393 148.919 134.938 1.00 44.73  ? 1015 PHE A N     1 
ATOM   8207  C CA    . PHE B 2 1018 ? 140.934 150.297 134.808 1.00 44.73  ? 1015 PHE A CA    1 
ATOM   8208  C C     . PHE B 2 1018 ? 139.469 150.432 135.201 1.00 44.73  ? 1015 PHE A C     1 
ATOM   8209  O O     . PHE B 2 1018 ? 139.086 151.392 135.879 1.00 44.73  ? 1015 PHE A O     1 
ATOM   8210  C CB    . PHE B 2 1018 ? 141.156 150.774 133.374 1.00 44.73  ? 1015 PHE A CB    1 
ATOM   8211  C CG    . PHE B 2 1018 ? 140.405 152.022 133.020 1.00 44.73  ? 1015 PHE A CG    1 
ATOM   8212  C CD1   . PHE B 2 1018 ? 140.558 153.180 133.756 1.00 44.73  ? 1015 PHE A CD1   1 
ATOM   8213  C CD2   . PHE B 2 1018 ? 139.534 152.029 131.946 1.00 44.73  ? 1015 PHE A CD2   1 
ATOM   8214  C CE1   . PHE B 2 1018 ? 139.862 154.319 133.418 1.00 44.73  ? 1015 PHE A CE1   1 
ATOM   8215  C CE2   . PHE B 2 1018 ? 138.836 153.167 131.610 1.00 44.73  ? 1015 PHE A CE2   1 
ATOM   8216  C CZ    . PHE B 2 1018 ? 139.000 154.312 132.347 1.00 44.73  ? 1015 PHE A CZ    1 
ATOM   8217  N N     . GLU B 2 1019 ? 138.632 149.481 134.781 1.00 44.73  ? 1016 GLU A N     1 
ATOM   8218  C CA    . GLU B 2 1019 ? 137.224 149.525 135.158 1.00 44.73  ? 1016 GLU A CA    1 
ATOM   8219  C C     . GLU B 2 1019 ? 137.038 149.294 136.651 1.00 44.73  ? 1016 GLU A C     1 
ATOM   8220  O O     . GLU B 2 1019 ? 136.100 149.837 137.247 1.00 44.73  ? 1016 GLU A O     1 
ATOM   8221  C CB    . GLU B 2 1019 ? 136.429 148.500 134.354 1.00 44.73  ? 1016 GLU A CB    1 
ATOM   8222  C CG    . GLU B 2 1019 ? 136.349 148.820 132.874 1.00 44.73  ? 1016 GLU A CG    1 
ATOM   8223  C CD    . GLU B 2 1019 ? 135.553 147.795 132.098 1.00 44.73  ? 1016 GLU A CD    1 
ATOM   8224  O OE1   . GLU B 2 1019 ? 135.205 146.745 132.678 1.00 44.73  ? 1016 GLU A OE1   1 
ATOM   8225  O OE2   . GLU B 2 1019 ? 135.271 148.042 130.908 1.00 44.73  ? 1016 GLU A OE2   1 
ATOM   8226  N N     . LYS B 2 1020 ? 137.907 148.491 137.267 1.00 44.73  ? 1017 LYS A N     1 
ATOM   8227  C CA    . LYS B 2 1020 ? 137.855 148.317 138.715 1.00 44.73  ? 1017 LYS A CA    1 
ATOM   8228  C C     . LYS B 2 1020 ? 138.107 149.634 139.436 1.00 44.73  ? 1017 LYS A C     1 
ATOM   8229  O O     . LYS B 2 1020 ? 137.420 149.957 140.412 1.00 44.73  ? 1017 LYS A O     1 
ATOM   8230  C CB    . LYS B 2 1020 ? 138.873 147.263 139.151 1.00 44.73  ? 1017 LYS A CB    1 
ATOM   8231  C CG    . LYS B 2 1020 ? 139.109 147.207 140.650 1.00 44.73  ? 1017 LYS A CG    1 
ATOM   8232  C CD    . LYS B 2 1020 ? 139.545 145.821 141.087 1.00 44.73  ? 1017 LYS A CD    1 
ATOM   8233  C CE    . LYS B 2 1020 ? 140.581 145.892 142.195 1.00 44.73  ? 1017 LYS A CE    1 
ATOM   8234  N NZ    . LYS B 2 1020 ? 139.954 146.094 143.530 1.00 44.73  ? 1017 LYS A NZ    1 
ATOM   8235  N N     . MET B 2 1021 ? 139.087 150.409 138.968 1.00 44.73  ? 1018 MET A N     1 
ATOM   8236  C CA    . MET B 2 1021 ? 139.389 151.687 139.605 1.00 44.73  ? 1018 MET A CA    1 
ATOM   8237  C C     . MET B 2 1021 ? 138.231 152.665 139.465 1.00 44.73  ? 1018 MET A C     1 
ATOM   8238  O O     . MET B 2 1021 ? 137.922 153.409 140.403 1.00 44.73  ? 1018 MET A O     1 
ATOM   8239  C CB    . MET B 2 1021 ? 140.666 152.281 139.016 1.00 44.73  ? 1018 MET A CB    1 
ATOM   8240  C CG    . MET B 2 1021 ? 141.940 151.662 139.558 1.00 44.73  ? 1018 MET A CG    1 
ATOM   8241  S SD    . MET B 2 1021 ? 143.353 152.775 139.452 1.00 44.73  ? 1018 MET A SD    1 
ATOM   8242  C CE    . MET B 2 1021 ? 143.664 152.759 137.689 1.00 44.73  ? 1018 MET A CE    1 
ATOM   8243  N N     . LEU B 2 1022 ? 137.581 152.685 138.299 1.00 44.73  ? 1019 LEU A N     1 
ATOM   8244  C CA    . LEU B 2 1022 ? 136.468 153.606 138.091 1.00 44.73  ? 1019 LEU A CA    1 
ATOM   8245  C C     . LEU B 2 1022 ? 135.299 153.280 139.013 1.00 44.73  ? 1019 LEU A C     1 
ATOM   8246  O O     . LEU B 2 1022 ? 134.658 154.187 139.556 1.00 44.73  ? 1019 LEU A O     1 
ATOM   8247  C CB    . LEU B 2 1022 ? 136.029 153.573 136.628 1.00 44.73  ? 1019 LEU A CB    1 
ATOM   8248  C CG    . LEU B 2 1022 ? 135.109 154.706 136.181 1.00 44.73  ? 1019 LEU A CG    1 
ATOM   8249  C CD1   . LEU B 2 1022 ? 135.764 156.048 136.444 1.00 44.73  ? 1019 LEU A CD1   1 
ATOM   8250  C CD2   . LEU B 2 1022 ? 134.757 154.560 134.711 1.00 44.73  ? 1019 LEU A CD2   1 
ATOM   8251  N N     . ILE B 2 1023 ? 135.000 151.992 139.195 1.00 44.73  ? 1020 ILE A N     1 
ATOM   8252  C CA    . ILE B 2 1023 ? 133.935 151.597 140.114 1.00 44.73  ? 1020 ILE A CA    1 
ATOM   8253  C C     . ILE B 2 1023 ? 134.306 151.968 141.544 1.00 44.73  ? 1020 ILE A C     1 
ATOM   8254  O O     . ILE B 2 1023 ? 133.491 152.516 142.296 1.00 44.73  ? 1020 ILE A O     1 
ATOM   8255  C CB    . ILE B 2 1023 ? 133.640 150.093 139.983 1.00 44.73  ? 1020 ILE A CB    1 
ATOM   8256  C CG1   . ILE B 2 1023 ? 133.038 149.778 138.614 1.00 44.73  ? 1020 ILE A CG1   1 
ATOM   8257  C CG2   . ILE B 2 1023 ? 132.703 149.633 141.086 1.00 44.73  ? 1020 ILE A CG2   1 
ATOM   8258  C CD1   . ILE B 2 1023 ? 132.966 148.299 138.313 1.00 44.73  ? 1020 ILE A CD1   1 
ATOM   8259  N N     . ASP B 2 1024 ? 135.546 151.673 141.940 1.00 44.73  ? 1021 ASP A N     1 
ATOM   8260  C CA    . ASP B 2 1024 ? 135.982 151.972 143.300 1.00 44.73  ? 1021 ASP A CA    1 
ATOM   8261  C C     . ASP B 2 1024 ? 136.045 153.474 143.547 1.00 44.73  ? 1021 ASP A C     1 
ATOM   8262  O O     . ASP B 2 1024 ? 135.708 153.945 144.638 1.00 44.73  ? 1021 ASP A O     1 
ATOM   8263  C CB    . ASP B 2 1024 ? 137.341 151.326 143.568 1.00 44.73  ? 1021 ASP A CB    1 
ATOM   8264  C CG    . ASP B 2 1024 ? 137.264 149.814 143.629 1.00 44.73  ? 1021 ASP A CG    1 
ATOM   8265  O OD1   . ASP B 2 1024 ? 136.199 149.287 144.014 1.00 44.73  ? 1021 ASP A OD1   1 
ATOM   8266  O OD2   . ASP B 2 1024 ? 138.268 149.152 143.292 1.00 44.73  ? 1021 ASP A OD2   1 
ATOM   8267  N N     . LYS B 2 1025 ? 136.489 154.240 142.548 1.00 44.73  ? 1022 LYS A N     1 
ATOM   8268  C CA    . LYS B 2 1025 ? 136.584 155.687 142.712 1.00 44.73  ? 1022 LYS A CA    1 
ATOM   8269  C C     . LYS B 2 1025 ? 135.214 156.309 142.942 1.00 44.73  ? 1022 LYS A C     1 
ATOM   8270  O O     . LYS B 2 1025 ? 135.060 157.196 143.789 1.00 44.73  ? 1022 LYS A O     1 
ATOM   8271  C CB    . LYS B 2 1025 ? 137.258 156.308 141.489 1.00 44.73  ? 1022 LYS A CB    1 
ATOM   8272  C CG    . LYS B 2 1025 ? 137.145 157.815 141.407 1.00 44.73  ? 1022 LYS A CG    1 
ATOM   8273  C CD    . LYS B 2 1025 ? 137.860 158.489 142.559 1.00 44.73  ? 1022 LYS A CD    1 
ATOM   8274  C CE    . LYS B 2 1025 ? 138.185 159.929 142.224 1.00 44.73  ? 1022 LYS A CE    1 
ATOM   8275  N NZ    . LYS B 2 1025 ? 138.196 160.785 143.438 1.00 44.73  ? 1022 LYS A NZ    1 
ATOM   8276  N N     . LEU B 2 1026 ? 134.204 155.851 142.205 1.00 44.73  ? 1023 LEU A N     1 
ATOM   8277  C CA    . LEU B 2 1026 ? 132.862 156.397 142.340 1.00 44.73  ? 1023 LEU A CA    1 
ATOM   8278  C C     . LEU B 2 1026 ? 132.122 155.858 143.555 1.00 44.73  ? 1023 LEU A C     1 
ATOM   8279  O O     . LEU B 2 1026 ? 131.022 156.338 143.851 1.00 44.73  ? 1023 LEU A O     1 
ATOM   8280  C CB    . LEU B 2 1026 ? 132.056 156.118 141.074 1.00 44.73  ? 1023 LEU A CB    1 
ATOM   8281  C CG    . LEU B 2 1026 ? 132.536 156.891 139.849 1.00 44.73  ? 1023 LEU A CG    1 
ATOM   8282  C CD1   . LEU B 2 1026 ? 131.851 156.372 138.614 1.00 44.73  ? 1023 LEU A CD1   1 
ATOM   8283  C CD2   . LEU B 2 1026 ? 132.273 158.374 140.020 1.00 44.73  ? 1023 LEU A CD2   1 
ATOM   8284  N N     . ASN B 2 1027 ? 132.689 154.874 144.255 1.00 44.73  ? 1024 ASN A N     1 
ATOM   8285  C CA    . ASN B 2 1027 ? 132.112 154.448 145.524 1.00 44.73  ? 1024 ASN A CA    1 
ATOM   8286  C C     . ASN B 2 1027 ? 132.136 155.586 146.535 1.00 44.73  ? 1024 ASN A C     1 
ATOM   8287  O O     . ASN B 2 1027 ? 131.163 155.801 147.267 1.00 44.73  ? 1024 ASN A O     1 
ATOM   8288  C CB    . ASN B 2 1027 ? 132.875 153.240 146.067 1.00 44.73  ? 1024 ASN A CB    1 
ATOM   8289  C CG    . ASN B 2 1027 ? 132.338 151.927 145.544 1.00 44.73  ? 1024 ASN A CG    1 
ATOM   8290  O OD1   . ASN B 2 1027 ? 131.458 151.901 144.685 1.00 44.73  ? 1024 ASN A OD1   1 
ATOM   8291  N ND2   . ASN B 2 1027 ? 132.867 150.825 146.061 1.00 44.73  ? 1024 ASN A ND2   1 
ATOM   8292  N N     . CYS B 2 1028 ? 133.241 156.324 146.589 1.00 44.73  ? 1025 CYS A N     1 
ATOM   8293  C CA    . CYS B 2 1028 ? 133.415 157.438 147.512 1.00 44.73  ? 1025 CYS A CA    1 
ATOM   8294  C C     . CYS B 2 1028 ? 134.017 158.627 146.768 1.00 44.73  ? 1025 CYS A C     1 
ATOM   8295  O O     . CYS B 2 1028 ? 135.043 159.185 147.160 1.00 44.73  ? 1025 CYS A O     1 
ATOM   8296  C CB    . CYS B 2 1028 ? 134.273 157.025 148.706 1.00 44.73  ? 1025 CYS A CB    1 
ATOM   8297  S SG    . CYS B 2 1028 ? 134.467 158.295 149.975 1.00 44.73  ? 1025 CYS A SG    1 
ATOM   8298  N N     . LEU B 2 1029 ? 133.400 158.996 145.647 1.00 44.73  ? 1026 LEU A N     1 
ATOM   8299  C CA    . LEU B 2 1029 ? 133.892 160.112 144.848 1.00 44.73  ? 1026 LEU A CA    1 
ATOM   8300  C C     . LEU B 2 1029 ? 133.948 161.393 145.669 1.00 44.73  ? 1026 LEU A C     1 
ATOM   8301  O O     . LEU B 2 1029 ? 132.938 161.840 146.220 1.00 44.73  ? 1026 LEU A O     1 
ATOM   8302  C CB    . LEU B 2 1029 ? 133.002 160.317 143.624 1.00 44.73  ? 1026 LEU A CB    1 
ATOM   8303  C CG    . LEU B 2 1029 ? 133.425 161.453 142.690 1.00 44.73  ? 1026 LEU A CG    1 
ATOM   8304  C CD1   . LEU B 2 1029 ? 134.791 161.175 142.092 1.00 44.73  ? 1026 LEU A CD1   1 
ATOM   8305  C CD2   . LEU B 2 1029 ? 132.393 161.670 141.597 1.00 44.73  ? 1026 LEU A CD2   1 
ATOM   8306  N N     . VAL B 2 1030 ? 135.139 161.982 145.748 1.00 44.73  ? 1027 VAL A N     1 
ATOM   8307  C CA    . VAL B 2 1030 ? 135.355 163.261 146.412 1.00 44.73  ? 1027 VAL A CA    1 
ATOM   8308  C C     . VAL B 2 1030 ? 136.164 164.148 145.478 1.00 44.73  ? 1027 VAL A C     1 
ATOM   8309  O O     . VAL B 2 1030 ? 137.236 163.748 145.012 1.00 44.73  ? 1027 VAL A O     1 
ATOM   8310  C CB    . VAL B 2 1030 ? 136.083 163.098 147.759 1.00 44.73  ? 1027 VAL A CB    1 
ATOM   8311  C CG1   . VAL B 2 1030 ? 136.370 164.458 148.371 1.00 44.73  ? 1027 VAL A CG1   1 
ATOM   8312  C CG2   . VAL B 2 1030 ? 135.265 162.245 148.711 1.00 44.73  ? 1027 VAL A CG2   1 
ATOM   8313  N N     . LEU B 2 1031 ? 135.655 165.344 145.209 1.00 44.73  ? 1028 LEU A N     1 
ATOM   8314  C CA    . LEU B 2 1031 ? 136.345 166.321 144.380 1.00 44.73  ? 1028 LEU A CA    1 
ATOM   8315  C C     . LEU B 2 1031 ? 137.083 167.299 145.283 1.00 44.73  ? 1028 LEU A C     1 
ATOM   8316  O O     . LEU B 2 1031 ? 136.508 167.815 146.247 1.00 44.73  ? 1028 LEU A O     1 
ATOM   8317  C CB    . LEU B 2 1031 ? 135.363 167.060 143.471 1.00 44.73  ? 1028 LEU A CB    1 
ATOM   8318  C CG    . LEU B 2 1031 ? 134.444 166.177 142.624 1.00 44.73  ? 1028 LEU A CG    1 
ATOM   8319  C CD1   . LEU B 2 1031 ? 133.676 167.015 141.614 1.00 44.73  ? 1028 LEU A CD1   1 
ATOM   8320  C CD2   . LEU B 2 1031 ? 135.237 165.088 141.919 1.00 44.73  ? 1028 LEU A CD2   1 
ATOM   8321  N N     . LYS B 2 1032 ? 138.352 167.552 144.971 1.00 44.73  ? 1029 LYS A N     1 
ATOM   8322  C CA    . LYS B 2 1032 ? 139.226 168.285 145.877 1.00 44.73  ? 1029 LYS A CA    1 
ATOM   8323  C C     . LYS B 2 1032 ? 139.113 169.798 145.745 1.00 44.73  ? 1029 LYS A C     1 
ATOM   8324  O O     . LYS B 2 1032 ? 139.785 170.516 146.493 1.00 44.73  ? 1029 LYS A O     1 
ATOM   8325  C CB    . LYS B 2 1032 ? 140.677 167.848 145.665 1.00 44.73  ? 1029 LYS A CB    1 
ATOM   8326  C CG    . LYS B 2 1032 ? 141.105 167.764 144.220 1.00 44.73  ? 1029 LYS A CG    1 
ATOM   8327  C CD    . LYS B 2 1032 ? 142.586 167.461 144.124 1.00 44.73  ? 1029 LYS A CD    1 
ATOM   8328  C CE    . LYS B 2 1032 ? 142.914 166.127 144.767 1.00 44.73  ? 1029 LYS A CE    1 
ATOM   8329  N NZ    . LYS B 2 1032 ? 144.353 165.783 144.615 1.00 44.73  ? 1029 LYS A NZ    1 
ATOM   8330  N N     . ASP B 2 1033 ? 138.293 170.302 144.829 1.00 44.73  ? 1030 ASP A N     1 
ATOM   8331  C CA    . ASP B 2 1033 ? 138.048 171.733 144.713 1.00 44.73  ? 1030 ASP A CA    1 
ATOM   8332  C C     . ASP B 2 1033 ? 136.718 172.154 145.323 1.00 44.73  ? 1030 ASP A C     1 
ATOM   8333  O O     . ASP B 2 1033 ? 136.336 173.321 145.199 1.00 44.73  ? 1030 ASP A O     1 
ATOM   8334  C CB    . ASP B 2 1033 ? 138.101 172.160 143.243 1.00 44.73  ? 1030 ASP A CB    1 
ATOM   8335  C CG    . ASP B 2 1033 ? 139.513 172.171 142.691 1.00 44.73  ? 1030 ASP A CG    1 
ATOM   8336  O OD1   . ASP B 2 1033 ? 140.447 172.496 143.453 1.00 44.73  ? 1030 ASP A OD1   1 
ATOM   8337  O OD2   . ASP B 2 1033 ? 139.688 171.853 141.496 1.00 44.73  ? 1030 ASP A OD2   1 
ATOM   8338  N N     . TYR B 2 1034 ? 136.007 171.234 145.980 1.00 44.73  ? 1031 TYR A N     1 
ATOM   8339  C CA    . TYR B 2 1034 ? 134.673 171.412 146.523 1.00 44.73  ? 1031 TYR A CA    1 
ATOM   8340  C C     . TYR B 2 1034 ? 134.722 171.641 148.029 1.00 44.73  ? 1031 TYR A C     1 
ATOM   8341  O O     . TYR B 2 1034 ? 135.524 171.020 148.732 1.00 44.73  ? 1031 TYR A O     1 
ATOM   8342  C CB    . TYR B 2 1034 ? 133.808 170.181 146.237 1.00 44.73  ? 1031 TYR A CB    1 
ATOM   8343  C CG    . TYR B 2 1034 ? 133.190 170.148 144.858 1.00 44.73  ? 1031 TYR A CG    1 
ATOM   8344  C CD1   . TYR B 2 1034 ? 133.826 170.735 143.773 1.00 44.73  ? 1031 TYR A CD1   1 
ATOM   8345  C CD2   . TYR B 2 1034 ? 131.975 169.517 144.640 1.00 44.73  ? 1031 TYR A CD2   1 
ATOM   8346  C CE1   . TYR B 2 1034 ? 133.263 170.702 142.513 1.00 44.73  ? 1031 TYR A CE1   1 
ATOM   8347  C CE2   . TYR B 2 1034 ? 131.405 169.478 143.385 1.00 44.73  ? 1031 TYR A CE2   1 
ATOM   8348  C CZ    . TYR B 2 1034 ? 132.053 170.072 142.325 1.00 44.73  ? 1031 TYR A CZ    1 
ATOM   8349  O OH    . TYR B 2 1034 ? 131.488 170.035 141.071 1.00 44.73  ? 1031 TYR A OH    1 
ATOM   8350  N N     . PRO B 2 1035 ? 133.881 172.530 148.551 1.00 44.73  ? 1032 PRO A N     1 
ATOM   8351  C CA    . PRO B 2 1035 ? 133.755 172.650 150.006 1.00 44.73  ? 1032 PRO A CA    1 
ATOM   8352  C C     . PRO B 2 1035 ? 133.140 171.398 150.608 1.00 44.73  ? 1032 PRO A C     1 
ATOM   8353  O O     . PRO B 2 1035 ? 132.357 170.690 149.971 1.00 44.73  ? 1032 PRO A O     1 
ATOM   8354  C CB    . PRO B 2 1035 ? 132.843 173.869 150.190 1.00 44.73  ? 1032 PRO A CB    1 
ATOM   8355  C CG    . PRO B 2 1035 ? 132.132 174.019 148.898 1.00 44.73  ? 1032 PRO A CG    1 
ATOM   8356  C CD    . PRO B 2 1035 ? 133.068 173.528 147.838 1.00 44.73  ? 1032 PRO A CD    1 
ATOM   8357  N N     . ALA B 2 1036 ? 133.510 171.131 151.862 1.00 44.73  ? 1033 ALA A N     1 
ATOM   8358  C CA    . ALA B 2 1036 ? 133.123 169.880 152.504 1.00 44.73  ? 1033 ALA A CA    1 
ATOM   8359  C C     . ALA B 2 1036 ? 131.622 169.797 152.755 1.00 44.73  ? 1033 ALA A C     1 
ATOM   8360  O O     . ALA B 2 1036 ? 131.057 168.698 152.743 1.00 44.73  ? 1033 ALA A O     1 
ATOM   8361  C CB    . ALA B 2 1036 ? 133.885 169.712 153.816 1.00 44.73  ? 1033 ALA A CB    1 
ATOM   8362  N N     . GLU B 2 1037 ? 130.964 170.933 152.991 1.00 44.73  ? 1034 GLU A N     1 
ATOM   8363  C CA    . GLU B 2 1037 ? 129.563 170.897 153.401 1.00 44.73  ? 1034 GLU A CA    1 
ATOM   8364  C C     . GLU B 2 1037 ? 128.650 170.436 152.270 1.00 44.73  ? 1034 GLU A C     1 
ATOM   8365  O O     . GLU B 2 1037 ? 127.654 169.746 152.516 1.00 44.73  ? 1034 GLU A O     1 
ATOM   8366  C CB    . GLU B 2 1037 ? 129.131 172.269 153.924 1.00 32.91  ? 1034 GLU A CB    1 
ATOM   8367  C CG    . GLU B 2 1037 ? 129.151 173.388 152.892 1.00 32.91  ? 1034 GLU A CG    1 
ATOM   8368  C CD    . GLU B 2 1037 ? 130.497 174.083 152.807 1.00 32.91  ? 1034 GLU A CD    1 
ATOM   8369  O OE1   . GLU B 2 1037 ? 131.493 173.521 153.309 1.00 32.91  ? 1034 GLU A OE1   1 
ATOM   8370  O OE2   . GLU B 2 1037 ? 130.557 175.192 152.237 1.00 32.91  ? 1034 GLU A OE2   1 
ATOM   8371  N N     . LYS B 2 1038 ? 128.965 170.798 151.028 1.00 44.73  ? 1035 LYS A N     1 
ATOM   8372  C CA    . LYS B 2 1038 ? 128.079 170.451 149.928 1.00 44.73  ? 1035 LYS A CA    1 
ATOM   8373  C C     . LYS B 2 1038 ? 128.301 169.008 149.488 1.00 44.73  ? 1035 LYS A C     1 
ATOM   8374  O O     . LYS B 2 1038 ? 129.304 168.372 149.823 1.00 44.73  ? 1035 LYS A O     1 
ATOM   8375  C CB    . LYS B 2 1038 ? 128.283 171.389 148.739 1.00 26.16  ? 1035 LYS A CB    1 
ATOM   8376  C CG    . LYS B 2 1038 ? 129.646 171.291 148.086 1.00 26.16  ? 1035 LYS A CG    1 
ATOM   8377  C CD    . LYS B 2 1038 ? 129.765 172.286 146.945 1.00 26.16  ? 1035 LYS A CD    1 
ATOM   8378  C CE    . LYS B 2 1038 ? 129.282 171.690 145.634 1.00 26.16  ? 1035 LYS A CE    1 
ATOM   8379  N NZ    . LYS B 2 1038 ? 130.043 172.224 144.472 1.00 26.16  ? 1035 LYS A NZ    1 
ATOM   8380  N N     . VAL B 2 1039 ? 127.340 168.495 148.722 1.00 44.73  ? 1036 VAL A N     1 
ATOM   8381  C CA    . VAL B 2 1039 ? 127.415 167.123 148.240 1.00 44.73  ? 1036 VAL A CA    1 
ATOM   8382  C C     . VAL B 2 1039 ? 128.534 167.014 147.216 1.00 44.73  ? 1036 VAL A C     1 
ATOM   8383  O O     . VAL B 2 1039 ? 128.683 167.874 146.338 1.00 44.73  ? 1036 VAL A O     1 
ATOM   8384  C CB    . VAL B 2 1039 ? 126.067 166.685 147.649 1.00 44.73  ? 1036 VAL A CB    1 
ATOM   8385  C CG1   . VAL B 2 1039 ? 126.136 165.242 147.193 1.00 44.73  ? 1036 VAL A CG1   1 
ATOM   8386  C CG2   . VAL B 2 1039 ? 124.955 166.874 148.670 1.00 44.73  ? 1036 VAL A CG2   1 
ATOM   8387  N N     . GLY B 2 1040 ? 129.328 165.954 147.324 1.00 44.73  ? 1037 GLY A N     1 
ATOM   8388  C CA    . GLY B 2 1040 ? 130.526 165.796 146.533 1.00 44.73  ? 1037 GLY A CA    1 
ATOM   8389  C C     . GLY B 2 1040 ? 131.803 166.137 147.265 1.00 44.73  ? 1037 GLY A C     1 
ATOM   8390  O O     . GLY B 2 1040 ? 132.889 165.828 146.761 1.00 44.73  ? 1037 GLY A O     1 
ATOM   8391  N N     . GLY B 2 1041 ? 131.705 166.766 148.433 1.00 44.73  ? 1038 GLY A N     1 
ATOM   8392  C CA    . GLY B 2 1041 ? 132.866 167.067 149.237 1.00 44.73  ? 1038 GLY A CA    1 
ATOM   8393  C C     . GLY B 2 1041 ? 133.317 165.873 150.053 1.00 44.73  ? 1038 GLY A C     1 
ATOM   8394  O O     . GLY B 2 1041 ? 132.807 164.760 149.931 1.00 44.73  ? 1038 GLY A O     1 
ATOM   8395  N N     . VAL B 2 1042 ? 134.310 166.122 150.909 1.00 44.73  ? 1039 VAL A N     1 
ATOM   8396  C CA    . VAL B 2 1042 ? 134.865 165.053 151.729 1.00 44.73  ? 1039 VAL A CA    1 
ATOM   8397  C C     . VAL B 2 1042 ? 133.862 164.540 152.756 1.00 44.73  ? 1039 VAL A C     1 
ATOM   8398  O O     . VAL B 2 1042 ? 133.827 163.335 153.031 1.00 44.73  ? 1039 VAL A O     1 
ATOM   8399  C CB    . VAL B 2 1042 ? 136.175 165.525 152.393 1.00 44.73  ? 1039 VAL A CB    1 
ATOM   8400  C CG1   . VAL B 2 1042 ? 135.942 166.767 153.230 1.00 44.73  ? 1039 VAL A CG1   1 
ATOM   8401  C CG2   . VAL B 2 1042 ? 136.778 164.419 153.236 1.00 44.73  ? 1039 VAL A CG2   1 
ATOM   8402  N N     . LEU B 2 1043 ? 133.029 165.413 153.320 1.00 44.73  ? 1040 LEU A N     1 
ATOM   8403  C CA    . LEU B 2 1043 ? 132.037 164.986 154.299 1.00 44.73  ? 1040 LEU A CA    1 
ATOM   8404  C C     . LEU B 2 1043 ? 130.819 164.320 153.674 1.00 44.73  ? 1040 LEU A C     1 
ATOM   8405  O O     . LEU B 2 1043 ? 130.175 163.498 154.337 1.00 44.73  ? 1040 LEU A O     1 
ATOM   8406  C CB    . LEU B 2 1043 ? 131.582 166.176 155.153 1.00 44.73  ? 1040 LEU A CB    1 
ATOM   8407  C CG    . LEU B 2 1043 ? 132.383 166.513 156.416 1.00 44.73  ? 1040 LEU A CG    1 
ATOM   8408  C CD1   . LEU B 2 1043 ? 132.337 165.364 157.405 1.00 44.73  ? 1040 LEU A CD1   1 
ATOM   8409  C CD2   . LEU B 2 1043 ? 133.821 166.882 156.105 1.00 44.73  ? 1040 LEU A CD2   1 
ATOM   8410  N N     . ASN B 2 1044 ? 130.485 164.645 152.426 1.00 44.73  ? 1041 ASN A N     1 
ATOM   8411  C CA    . ASN B 2 1044 ? 129.340 164.060 151.726 1.00 44.73  ? 1041 ASN A CA    1 
ATOM   8412  C C     . ASN B 2 1044 ? 129.779 163.578 150.349 1.00 44.73  ? 1041 ASN A C     1 
ATOM   8413  O O     . ASN B 2 1044 ? 129.443 164.186 149.326 1.00 44.73  ? 1041 ASN A O     1 
ATOM   8414  C CB    . ASN B 2 1044 ? 128.197 165.068 151.610 1.00 44.73  ? 1041 ASN A CB    1 
ATOM   8415  C CG    . ASN B 2 1044 ? 127.398 165.192 152.888 1.00 44.73  ? 1041 ASN A CG    1 
ATOM   8416  O OD1   . ASN B 2 1044 ? 127.060 164.194 153.521 1.00 44.73  ? 1041 ASN A OD1   1 
ATOM   8417  N ND2   . ASN B 2 1044 ? 127.090 166.423 153.275 1.00 44.73  ? 1041 ASN A ND2   1 
ATOM   8418  N N     . PRO B 2 1045 ? 130.536 162.485 150.288 1.00 44.73  ? 1042 PRO A N     1 
ATOM   8419  C CA    . PRO B 2 1045 ? 131.031 162.005 148.994 1.00 44.73  ? 1042 PRO A CA    1 
ATOM   8420  C C     . PRO B 2 1045 ? 129.916 161.481 148.105 1.00 44.73  ? 1042 PRO A C     1 
ATOM   8421  O O     . PRO B 2 1045 ? 128.892 160.980 148.576 1.00 44.73  ? 1042 PRO A O     1 
ATOM   8422  C CB    . PRO B 2 1045 ? 131.999 160.878 149.379 1.00 44.73  ? 1042 PRO A CB    1 
ATOM   8423  C CG    . PRO B 2 1045 ? 132.277 161.072 150.832 1.00 44.73  ? 1042 PRO A CG    1 
ATOM   8424  C CD    . PRO B 2 1045 ? 131.029 161.658 151.398 1.00 44.73  ? 1042 PRO A CD    1 
ATOM   8425  N N     . TYR B 2 1046 ? 130.131 161.606 146.797 1.00 44.73  ? 1043 TYR A N     1 
ATOM   8426  C CA    . TYR B 2 1046 ? 129.275 160.936 145.828 1.00 44.73  ? 1043 TYR A CA    1 
ATOM   8427  C C     . TYR B 2 1046 ? 129.400 159.424 145.954 1.00 44.73  ? 1043 TYR A C     1 
ATOM   8428  O O     . TYR B 2 1046 ? 130.492 158.888 146.162 1.00 44.73  ? 1043 TYR A O     1 
ATOM   8429  C CB    . TYR B 2 1046 ? 129.638 161.369 144.408 1.00 44.73  ? 1043 TYR A CB    1 
ATOM   8430  C CG    . TYR B 2 1046 ? 129.040 162.682 143.965 1.00 44.73  ? 1043 TYR A CG    1 
ATOM   8431  C CD1   . TYR B 2 1046 ? 127.866 163.158 144.525 1.00 44.73  ? 1043 TYR A CD1   1 
ATOM   8432  C CD2   . TYR B 2 1046 ? 129.662 163.456 142.997 1.00 44.73  ? 1043 TYR A CD2   1 
ATOM   8433  C CE1   . TYR B 2 1046 ? 127.318 164.354 144.117 1.00 44.73  ? 1043 TYR A CE1   1 
ATOM   8434  C CE2   . TYR B 2 1046 ? 129.124 164.658 142.591 1.00 44.73  ? 1043 TYR A CE2   1 
ATOM   8435  C CZ    . TYR B 2 1046 ? 127.953 165.103 143.153 1.00 44.73  ? 1043 TYR A CZ    1 
ATOM   8436  O OH    . TYR B 2 1046 ? 127.413 166.302 142.749 1.00 44.73  ? 1043 TYR A OH    1 
ATOM   8437  N N     . GLN B 2 1047 ? 128.270 158.735 145.828 1.00 44.73  ? 1044 GLN A N     1 
ATOM   8438  C CA    . GLN B 2 1047 ? 128.225 157.277 145.783 1.00 44.73  ? 1044 GLN A CA    1 
ATOM   8439  C C     . GLN B 2 1047 ? 127.357 156.893 144.591 1.00 44.73  ? 1044 GLN A C     1 
ATOM   8440  O O     . GLN B 2 1047 ? 126.129 156.837 144.701 1.00 44.73  ? 1044 GLN A O     1 
ATOM   8441  C CB    . GLN B 2 1047 ? 127.682 156.701 147.086 1.00 44.73  ? 1044 GLN A CB    1 
ATOM   8442  C CG    . GLN B 2 1047 ? 128.402 157.195 148.325 1.00 44.73  ? 1044 GLN A CG    1 
ATOM   8443  C CD    . GLN B 2 1047 ? 128.684 156.088 149.315 1.00 44.73  ? 1044 GLN A CD    1 
ATOM   8444  O OE1   . GLN B 2 1047 ? 128.039 155.043 149.292 1.00 44.73  ? 1044 GLN A OE1   1 
ATOM   8445  N NE2   . GLN B 2 1047 ? 129.655 156.310 150.191 1.00 44.73  ? 1044 GLN A NE2   1 
ATOM   8446  N N     . LEU B 2 1048 ? 127.994 156.633 143.449 1.00 44.73  ? 1045 LEU A N     1 
ATOM   8447  C CA    . LEU B 2 1048 ? 127.282 156.349 142.212 1.00 44.73  ? 1045 LEU A CA    1 
ATOM   8448  C C     . LEU B 2 1048 ? 127.517 154.941 141.685 1.00 44.73  ? 1045 LEU A C     1 
ATOM   8449  O O     . LEU B 2 1048 ? 126.986 154.601 140.621 1.00 44.73  ? 1045 LEU A O     1 
ATOM   8450  C CB    . LEU B 2 1048 ? 127.675 157.362 141.128 1.00 44.73  ? 1045 LEU A CB    1 
ATOM   8451  C CG    . LEU B 2 1048 ? 127.640 158.842 141.507 1.00 44.73  ? 1045 LEU A CG    1 
ATOM   8452  C CD1   . LEU B 2 1048 ? 128.503 159.650 140.554 1.00 44.73  ? 1045 LEU A CD1   1 
ATOM   8453  C CD2   . LEU B 2 1048 ? 126.215 159.361 141.510 1.00 44.73  ? 1045 LEU A CD2   1 
ATOM   8454  N N     . THR B 2 1049 ? 128.290 154.115 142.386 1.00 44.73  ? 1046 THR A N     1 
ATOM   8455  C CA    . THR B 2 1049 ? 128.566 152.757 141.943 1.00 44.73  ? 1046 THR A CA    1 
ATOM   8456  C C     . THR B 2 1049 ? 128.370 151.789 143.099 1.00 44.73  ? 1046 THR A C     1 
ATOM   8457  O O     . THR B 2 1049 ? 128.659 152.108 144.255 1.00 44.73  ? 1046 THR A O     1 
ATOM   8458  C CB    . THR B 2 1049 ? 129.989 152.612 141.393 1.00 44.73  ? 1046 THR A CB    1 
ATOM   8459  O OG1   . THR B 2 1049 ? 130.917 153.235 142.290 1.00 44.73  ? 1046 THR A OG1   1 
ATOM   8460  C CG2   . THR B 2 1049 ? 130.098 153.258 140.027 1.00 44.73  ? 1046 THR A CG2   1 
ATOM   8461  N N     . ASP B 2 1050 ? 127.868 150.603 142.773 1.00 44.73  ? 1047 ASP A N     1 
ATOM   8462  C CA    . ASP B 2 1050 ? 127.767 149.537 143.755 1.00 44.73  ? 1047 ASP A CA    1 
ATOM   8463  C C     . ASP B 2 1050 ? 129.154 148.991 144.078 1.00 44.73  ? 1047 ASP A C     1 
ATOM   8464  O O     . ASP B 2 1050 ? 130.113 149.163 143.320 1.00 44.73  ? 1047 ASP A O     1 
ATOM   8465  C CB    . ASP B 2 1050 ? 126.864 148.417 143.240 1.00 44.73  ? 1047 ASP A CB    1 
ATOM   8466  C CG    . ASP B 2 1050 ? 126.237 147.611 144.360 1.00 44.73  ? 1047 ASP A CG    1 
ATOM   8467  O OD1   . ASP B 2 1050 ? 126.974 147.179 145.271 1.00 44.73  ? 1047 ASP A OD1   1 
ATOM   8468  O OD2   . ASP B 2 1050 ? 125.006 147.405 144.328 1.00 44.73  ? 1047 ASP A OD2   1 
ATOM   8469  N N     . GLN B 2 1051 ? 129.255 148.333 145.229 1.00 44.73  ? 1048 GLN A N     1 
ATOM   8470  C CA    . GLN B 2 1051 ? 130.531 147.780 145.660 1.00 44.73  ? 1048 GLN A CA    1 
ATOM   8471  C C     . GLN B 2 1051 ? 131.007 146.717 144.680 1.00 44.73  ? 1048 GLN A C     1 
ATOM   8472  O O     . GLN B 2 1051 ? 130.243 145.831 144.284 1.00 44.73  ? 1048 GLN A O     1 
ATOM   8473  C CB    . GLN B 2 1051 ? 130.401 147.189 147.062 1.00 44.73  ? 1048 GLN A CB    1 
ATOM   8474  C CG    . GLN B 2 1051 ? 130.591 148.202 148.177 1.00 44.73  ? 1048 GLN A CG    1 
ATOM   8475  C CD    . GLN B 2 1051 ? 130.723 147.551 149.537 1.00 44.73  ? 1048 GLN A CD    1 
ATOM   8476  O OE1   . GLN B 2 1051 ? 130.143 146.497 149.793 1.00 44.73  ? 1048 GLN A OE1   1 
ATOM   8477  N NE2   . GLN B 2 1051 ? 131.491 148.178 150.421 1.00 44.73  ? 1048 GLN A NE2   1 
ATOM   8478  N N     . PHE B 2 1052 ? 132.275 146.807 144.287 1.00 44.73  ? 1049 PHE A N     1 
ATOM   8479  C CA    . PHE B 2 1052 ? 132.837 145.834 143.361 1.00 44.73  ? 1049 PHE A CA    1 
ATOM   8480  C C     . PHE B 2 1052 ? 133.110 144.523 144.085 1.00 44.73  ? 1049 PHE A C     1 
ATOM   8481  O O     . PHE B 2 1052 ? 133.755 144.504 145.137 1.00 44.73  ? 1049 PHE A O     1 
ATOM   8482  C CB    . PHE B 2 1052 ? 134.122 146.374 142.737 1.00 44.73  ? 1049 PHE A CB    1 
ATOM   8483  C CG    . PHE B 2 1052 ? 134.830 145.385 141.858 1.00 44.73  ? 1049 PHE A CG    1 
ATOM   8484  C CD1   . PHE B 2 1052 ? 134.329 145.066 140.609 1.00 44.73  ? 1049 PHE A CD1   1 
ATOM   8485  C CD2   . PHE B 2 1052 ? 135.999 144.776 142.279 1.00 44.73  ? 1049 PHE A CD2   1 
ATOM   8486  C CE1   . PHE B 2 1052 ? 134.977 144.158 139.798 1.00 44.73  ? 1049 PHE A CE1   1 
ATOM   8487  C CE2   . PHE B 2 1052 ? 136.651 143.866 141.473 1.00 44.73  ? 1049 PHE A CE2   1 
ATOM   8488  C CZ    . PHE B 2 1052 ? 136.140 143.558 140.231 1.00 44.73  ? 1049 PHE A CZ    1 
ATOM   8489  N N     . THR B 2 1053 ? 132.618 143.424 143.517 1.00 44.73  ? 1050 THR A N     1 
ATOM   8490  C CA    . THR B 2 1053 ? 132.773 142.103 144.109 1.00 44.73  ? 1050 THR A CA    1 
ATOM   8491  C C     . THR B 2 1053 ? 133.702 141.219 143.288 1.00 44.73  ? 1050 THR A C     1 
ATOM   8492  O O     . THR B 2 1053 ? 134.664 140.662 143.826 1.00 44.73  ? 1050 THR A O     1 
ATOM   8493  C CB    . THR B 2 1053 ? 131.403 141.434 144.270 1.00 44.73  ? 1050 THR A CB    1 
ATOM   8494  O OG1   . THR B 2 1053 ? 130.589 142.218 145.151 1.00 44.73  ? 1050 THR A OG1   1 
ATOM   8495  C CG2   . THR B 2 1053 ? 131.563 140.043 144.856 1.00 44.73  ? 1050 THR A CG2   1 
ATOM   8496  N N     . SER B 2 1054 ? 133.440 141.075 141.993 1.00 44.73  ? 1051 SER A N     1 
ATOM   8497  C CA    . SER B 2 1054 ? 134.295 140.287 141.117 1.00 44.73  ? 1051 SER A CA    1 
ATOM   8498  C C     . SER B 2 1054 ? 134.072 140.748 139.684 1.00 44.73  ? 1051 SER A C     1 
ATOM   8499  O O     . SER B 2 1054 ? 133.078 141.407 139.370 1.00 44.73  ? 1051 SER A O     1 
ATOM   8500  C CB    . SER B 2 1054 ? 134.017 138.788 141.259 1.00 44.73  ? 1051 SER A CB    1 
ATOM   8501  O OG    . SER B 2 1054 ? 132.721 138.465 140.789 1.00 44.73  ? 1051 SER A OG    1 
ATOM   8502  N N     . PHE B 2 1055 ? 135.020 140.392 138.815 1.00 44.73  ? 1052 PHE A N     1 
ATOM   8503  C CA    . PHE B 2 1055 ? 134.883 140.727 137.402 1.00 44.73  ? 1052 PHE A CA    1 
ATOM   8504  C C     . PHE B 2 1055 ? 133.720 139.984 136.758 1.00 44.73  ? 1052 PHE A C     1 
ATOM   8505  O O     . PHE B 2 1055 ? 133.073 140.516 135.850 1.00 44.73  ? 1052 PHE A O     1 
ATOM   8506  C CB    . PHE B 2 1055 ? 136.182 140.420 136.656 1.00 44.73  ? 1052 PHE A CB    1 
ATOM   8507  C CG    . PHE B 2 1055 ? 137.363 141.213 137.137 1.00 44.73  ? 1052 PHE A CG    1 
ATOM   8508  C CD1   . PHE B 2 1055 ? 137.402 142.586 136.977 1.00 44.73  ? 1052 PHE A CD1   1 
ATOM   8509  C CD2   . PHE B 2 1055 ? 138.436 140.583 137.743 1.00 44.73  ? 1052 PHE A CD2   1 
ATOM   8510  C CE1   . PHE B 2 1055 ? 138.486 143.317 137.415 1.00 44.73  ? 1052 PHE A CE1   1 
ATOM   8511  C CE2   . PHE B 2 1055 ? 139.524 141.310 138.183 1.00 44.73  ? 1052 PHE A CE2   1 
ATOM   8512  C CZ    . PHE B 2 1055 ? 139.548 142.679 138.018 1.00 44.73  ? 1052 PHE A CZ    1 
ATOM   8513  N N     . ALA B 2 1056 ? 133.445 138.759 137.207 1.00 44.73  ? 1053 ALA A N     1 
ATOM   8514  C CA    . ALA B 2 1056 ? 132.368 137.979 136.609 1.00 44.73  ? 1053 ALA A CA    1 
ATOM   8515  C C     . ALA B 2 1056 ? 130.998 138.489 137.040 1.00 44.73  ? 1053 ALA A C     1 
ATOM   8516  O O     . ALA B 2 1056 ? 130.073 138.561 136.224 1.00 44.73  ? 1053 ALA A O     1 
ATOM   8517  C CB    . ALA B 2 1056 ? 132.528 136.503 136.970 1.00 44.73  ? 1053 ALA A CB    1 
ATOM   8518  N N     . LYS B 2 1057 ? 130.847 138.843 138.319 1.00 44.73  ? 1054 LYS A N     1 
ATOM   8519  C CA    . LYS B 2 1057 ? 129.528 139.198 138.835 1.00 44.73  ? 1054 LYS A CA    1 
ATOM   8520  C C     . LYS B 2 1057 ? 129.010 140.495 138.226 1.00 44.73  ? 1054 LYS A C     1 
ATOM   8521  O O     . LYS B 2 1057 ? 127.806 140.626 137.976 1.00 44.73  ? 1054 LYS A O     1 
ATOM   8522  C CB    . LYS B 2 1057 ? 129.564 139.286 140.360 1.00 44.73  ? 1054 LYS A CB    1 
ATOM   8523  C CG    . LYS B 2 1057 ? 129.346 137.944 141.042 1.00 44.73  ? 1054 LYS A CG    1 
ATOM   8524  C CD    . LYS B 2 1057 ? 129.800 137.957 142.490 1.00 44.73  ? 1054 LYS A CD    1 
ATOM   8525  C CE    . LYS B 2 1057 ? 130.518 136.665 142.847 1.00 44.73  ? 1054 LYS A CE    1 
ATOM   8526  N NZ    . LYS B 2 1057 ? 131.502 136.851 143.948 1.00 44.73  ? 1054 LYS A NZ    1 
ATOM   8527  N N     . MET B 2 1058 ? 129.888 141.467 137.988 1.00 44.73  ? 1055 MET A N     1 
ATOM   8528  C CA    . MET B 2 1058 ? 129.454 142.691 137.327 1.00 44.73  ? 1055 MET A CA    1 
ATOM   8529  C C     . MET B 2 1058 ? 129.044 142.378 135.893 1.00 44.73  ? 1055 MET A C     1 
ATOM   8530  O O     . MET B 2 1058 ? 129.753 141.672 135.169 1.00 44.73  ? 1055 MET A O     1 
ATOM   8531  C CB    . MET B 2 1058 ? 130.555 143.753 137.358 1.00 44.73  ? 1055 MET A CB    1 
ATOM   8532  C CG    . MET B 2 1058 ? 131.813 143.424 136.570 1.00 44.73  ? 1055 MET A CG    1 
ATOM   8533  S SD    . MET B 2 1058 ? 133.062 144.716 136.713 1.00 44.73  ? 1055 MET A SD    1 
ATOM   8534  C CE    . MET B 2 1058 ? 134.380 144.032 135.714 1.00 44.73  ? 1055 MET A CE    1 
ATOM   8535  N N     . GLY B 2 1059 ? 127.883 142.882 135.491 1.00 44.73  ? 1056 GLY A N     1 
ATOM   8536  C CA    . GLY B 2 1059 ? 127.357 142.571 134.179 1.00 44.73  ? 1056 GLY A CA    1 
ATOM   8537  C C     . GLY B 2 1059 ? 127.182 143.781 133.290 1.00 44.73  ? 1056 GLY A C     1 
ATOM   8538  O O     . GLY B 2 1059 ? 128.160 144.429 132.905 1.00 44.73  ? 1056 GLY A O     1 
ATOM   8539  N N     . THR B 2 1060 ? 125.934 144.092 132.956 1.00 44.73  ? 1057 THR A N     1 
ATOM   8540  C CA    . THR B 2 1060 ? 125.613 145.210 132.083 1.00 44.73  ? 1057 THR A CA    1 
ATOM   8541  C C     . THR B 2 1060 ? 125.428 146.520 132.836 1.00 44.73  ? 1057 THR A C     1 
ATOM   8542  O O     . THR B 2 1060 ? 125.214 147.557 132.199 1.00 44.73  ? 1057 THR A O     1 
ATOM   8543  C CB    . THR B 2 1060 ? 124.348 144.900 131.278 1.00 44.73  ? 1057 THR A CB    1 
ATOM   8544  O OG1   . THR B 2 1060 ? 124.221 145.838 130.203 1.00 44.73  ? 1057 THR A OG1   1 
ATOM   8545  C CG2   . THR B 2 1060 ? 123.118 144.986 132.168 1.00 44.73  ? 1057 THR A CG2   1 
ATOM   8546  N N     . GLN B 2 1061 ? 125.506 146.505 134.164 1.00 44.73  ? 1058 GLN A N     1 
ATOM   8547  C CA    . GLN B 2 1061 ? 125.332 147.722 134.942 1.00 44.73  ? 1058 GLN A CA    1 
ATOM   8548  C C     . GLN B 2 1061 ? 126.070 147.582 136.264 1.00 44.73  ? 1058 GLN A C     1 
ATOM   8549  O O     . GLN B 2 1061 ? 126.033 146.522 136.893 1.00 44.73  ? 1058 GLN A O     1 
ATOM   8550  C CB    . GLN B 2 1061 ? 123.849 148.021 135.189 1.00 44.73  ? 1058 GLN A CB    1 
ATOM   8551  C CG    . GLN B 2 1061 ? 123.595 149.297 135.972 1.00 44.73  ? 1058 GLN A CG    1 
ATOM   8552  C CD    . GLN B 2 1061 ? 122.139 149.471 136.345 1.00 44.73  ? 1058 GLN A CD    1 
ATOM   8553  O OE1   . GLN B 2 1061 ? 121.295 148.644 136.003 1.00 44.73  ? 1058 GLN A OE1   1 
ATOM   8554  N NE2   . GLN B 2 1061 ? 121.835 150.554 137.051 1.00 44.73  ? 1058 GLN A NE2   1 
ATOM   8555  N N     . SER B 2 1062 ? 126.736 148.657 136.673 1.00 44.73  ? 1059 SER A N     1 
ATOM   8556  C CA    . SER B 2 1062 ? 127.443 148.722 137.948 1.00 44.73  ? 1059 SER A CA    1 
ATOM   8557  C C     . SER B 2 1062 ? 127.109 150.035 138.648 1.00 44.73  ? 1059 SER A C     1 
ATOM   8558  O O     . SER B 2 1062 ? 127.983 150.743 139.149 1.00 44.73  ? 1059 SER A O     1 
ATOM   8559  C CB    . SER B 2 1062 ? 128.949 148.570 137.747 1.00 44.73  ? 1059 SER A CB    1 
ATOM   8560  O OG    . SER B 2 1062 ? 129.636 148.620 138.984 1.00 44.73  ? 1059 SER A OG    1 
ATOM   8561  N N     . GLY B 2 1063 ? 125.822 150.370 138.685 1.00 44.73  ? 1060 GLY A N     1 
ATOM   8562  C CA    . GLY B 2 1063 ? 125.383 151.639 139.229 1.00 44.73  ? 1060 GLY A CA    1 
ATOM   8563  C C     . GLY B 2 1063 ? 125.182 152.663 138.133 1.00 44.73  ? 1060 GLY A C     1 
ATOM   8564  O O     . GLY B 2 1063 ? 124.304 152.504 137.281 1.00 44.73  ? 1060 GLY A O     1 
ATOM   8565  N N     . PHE B 2 1064 ? 125.994 153.717 138.138 1.00 44.73  ? 1061 PHE A N     1 
ATOM   8566  C CA    . PHE B 2 1064 ? 126.027 154.676 137.043 1.00 44.73  ? 1061 PHE A CA    1 
ATOM   8567  C C     . PHE B 2 1064 ? 127.035 154.299 135.967 1.00 44.73  ? 1061 PHE A C     1 
ATOM   8568  O O     . PHE B 2 1064 ? 127.538 155.183 135.264 1.00 44.73  ? 1061 PHE A O     1 
ATOM   8569  C CB    . PHE B 2 1064 ? 126.326 156.081 137.571 1.00 44.73  ? 1061 PHE A CB    1 
ATOM   8570  C CG    . PHE B 2 1064 ? 125.097 156.879 137.896 1.00 44.73  ? 1061 PHE A CG    1 
ATOM   8571  C CD1   . PHE B 2 1064 ? 124.444 157.595 136.910 1.00 44.73  ? 1061 PHE A CD1   1 
ATOM   8572  C CD2   . PHE B 2 1064 ? 124.597 156.915 139.184 1.00 44.73  ? 1061 PHE A CD2   1 
ATOM   8573  C CE1   . PHE B 2 1064 ? 123.316 158.330 137.201 1.00 44.73  ? 1061 PHE A CE1   1 
ATOM   8574  C CE2   . PHE B 2 1064 ? 123.468 157.649 139.480 1.00 44.73  ? 1061 PHE A CE2   1 
ATOM   8575  C CZ    . PHE B 2 1064 ? 122.828 158.357 138.487 1.00 44.73  ? 1061 PHE A CZ    1 
ATOM   8576  N N     . LEU B 2 1065 ? 127.356 153.016 135.842 1.00 44.73  ? 1062 LEU A N     1 
ATOM   8577  C CA    . LEU B 2 1065 ? 128.222 152.510 134.788 1.00 44.73  ? 1062 LEU A CA    1 
ATOM   8578  C C     . LEU B 2 1065 ? 127.487 151.443 133.993 1.00 44.73  ? 1062 LEU A C     1 
ATOM   8579  O O     . LEU B 2 1065 ? 126.777 150.608 134.563 1.00 44.73  ? 1062 LEU A O     1 
ATOM   8580  C CB    . LEU B 2 1065 ? 129.516 151.922 135.355 1.00 44.73  ? 1062 LEU A CB    1 
ATOM   8581  C CG    . LEU B 2 1065 ? 130.717 152.858 135.469 1.00 44.73  ? 1062 LEU A CG    1 
ATOM   8582  C CD1   . LEU B 2 1065 ? 130.459 153.914 136.515 1.00 44.73  ? 1062 LEU A CD1   1 
ATOM   8583  C CD2   . LEU B 2 1065 ? 131.978 152.075 135.791 1.00 44.73  ? 1062 LEU A CD2   1 
ATOM   8584  N N     . PHE B 2 1066 ? 127.661 151.473 132.677 1.00 44.73  ? 1063 PHE A N     1 
ATOM   8585  C CA    . PHE B 2 1066 ? 127.085 150.477 131.792 1.00 44.73  ? 1063 PHE A CA    1 
ATOM   8586  C C     . PHE B 2 1066 ? 128.197 149.823 130.988 1.00 44.73  ? 1063 PHE A C     1 
ATOM   8587  O O     . PHE B 2 1066 ? 129.222 150.439 130.688 1.00 44.73  ? 1063 PHE A O     1 
ATOM   8588  C CB    . PHE B 2 1066 ? 126.046 151.088 130.850 1.00 44.73  ? 1063 PHE A CB    1 
ATOM   8589  C CG    . PHE B 2 1066 ? 124.844 151.640 131.551 1.00 44.73  ? 1063 PHE A CG    1 
ATOM   8590  C CD1   . PHE B 2 1066 ? 124.306 150.992 132.646 1.00 44.73  ? 1063 PHE A CD1   1 
ATOM   8591  C CD2   . PHE B 2 1066 ? 124.253 152.811 131.116 1.00 44.73  ? 1063 PHE A CD2   1 
ATOM   8592  C CE1   . PHE B 2 1066 ? 123.200 151.500 133.291 1.00 44.73  ? 1063 PHE A CE1   1 
ATOM   8593  C CE2   . PHE B 2 1066 ? 123.149 153.322 131.759 1.00 44.73  ? 1063 PHE A CE2   1 
ATOM   8594  C CZ    . PHE B 2 1066 ? 122.621 152.665 132.849 1.00 44.73  ? 1063 PHE A CZ    1 
ATOM   8595  N N     . TYR B 2 1067 ? 127.980 148.559 130.639 1.00 44.73  ? 1064 TYR A N     1 
ATOM   8596  C CA    . TYR B 2 1067 ? 128.949 147.774 129.879 1.00 44.73  ? 1064 TYR A CA    1 
ATOM   8597  C C     . TYR B 2 1067 ? 128.224 147.176 128.680 1.00 44.73  ? 1064 TYR A C     1 
ATOM   8598  O O     . TYR B 2 1067 ? 127.416 146.254 128.829 1.00 44.73  ? 1064 TYR A O     1 
ATOM   8599  C CB    . TYR B 2 1067 ? 129.583 146.698 130.750 1.00 44.73  ? 1064 TYR A CB    1 
ATOM   8600  C CG    . TYR B 2 1067 ? 130.339 147.257 131.930 1.00 44.73  ? 1064 TYR A CG    1 
ATOM   8601  C CD1   . TYR B 2 1067 ? 131.618 147.770 131.780 1.00 44.73  ? 1064 TYR A CD1   1 
ATOM   8602  C CD2   . TYR B 2 1067 ? 129.769 147.279 133.194 1.00 44.73  ? 1064 TYR A CD2   1 
ATOM   8603  C CE1   . TYR B 2 1067 ? 132.309 148.287 132.855 1.00 44.73  ? 1064 TYR A CE1   1 
ATOM   8604  C CE2   . TYR B 2 1067 ? 130.453 147.793 134.276 1.00 44.73  ? 1064 TYR A CE2   1 
ATOM   8605  C CZ    . TYR B 2 1067 ? 131.722 148.296 134.100 1.00 44.73  ? 1064 TYR A CZ    1 
ATOM   8606  O OH    . TYR B 2 1067 ? 132.411 148.809 135.173 1.00 44.73  ? 1064 TYR A OH    1 
ATOM   8607  N N     . VAL B 2 1068 ? 128.514 147.704 127.497 1.00 44.73  ? 1065 VAL A N     1 
ATOM   8608  C CA    . VAL B 2 1068 ? 127.888 147.248 126.261 1.00 44.73  ? 1065 VAL A CA    1 
ATOM   8609  C C     . VAL B 2 1068 ? 128.906 146.427 125.481 1.00 44.73  ? 1065 VAL A C     1 
ATOM   8610  O O     . VAL B 2 1068 ? 130.117 146.610 125.671 1.00 44.73  ? 1065 VAL A O     1 
ATOM   8611  C CB    . VAL B 2 1068 ? 127.365 148.432 125.435 1.00 44.73  ? 1065 VAL A CB    1 
ATOM   8612  C CG1   . VAL B 2 1068 ? 126.362 149.234 126.243 1.00 44.73  ? 1065 VAL A CG1   1 
ATOM   8613  C CG2   . VAL B 2 1068 ? 128.519 149.313 124.989 1.00 44.73  ? 1065 VAL A CG2   1 
ATOM   8614  N N     . PRO B 2 1069 ? 128.474 145.503 124.624 1.00 44.73  ? 1066 PRO A N     1 
ATOM   8615  C CA    . PRO B 2 1069 ? 129.439 144.704 123.860 1.00 44.73  ? 1066 PRO A CA    1 
ATOM   8616  C C     . PRO B 2 1069 ? 130.330 145.579 122.991 1.00 44.73  ? 1066 PRO A C     1 
ATOM   8617  O O     . PRO B 2 1069 ? 129.866 146.496 122.311 1.00 44.73  ? 1066 PRO A O     1 
ATOM   8618  C CB    . PRO B 2 1069 ? 128.548 143.786 123.016 1.00 44.73  ? 1066 PRO A CB    1 
ATOM   8619  C CG    . PRO B 2 1069 ? 127.272 143.707 123.764 1.00 44.73  ? 1066 PRO A CG    1 
ATOM   8620  C CD    . PRO B 2 1069 ? 127.092 145.038 124.425 1.00 44.73  ? 1066 PRO A CD    1 
ATOM   8621  N N     . ALA B 2 1070 ? 131.626 145.282 123.029 1.00 44.73  ? 1067 ALA A N     1 
ATOM   8622  C CA    . ALA B 2 1070 ? 132.598 146.028 122.233 1.00 44.73  ? 1067 ALA A CA    1 
ATOM   8623  C C     . ALA B 2 1070 ? 132.415 145.872 120.727 1.00 44.73  ? 1067 ALA A C     1 
ATOM   8624  O O     . ALA B 2 1070 ? 132.464 146.893 120.019 1.00 44.73  ? 1067 ALA A O     1 
ATOM   8625  C CB    . ALA B 2 1070 ? 134.010 145.622 122.661 1.00 44.73  ? 1067 ALA A CB    1 
ATOM   8626  N N     . PRO B 2 1071 ? 132.222 144.673 120.169 1.00 44.73  ? 1068 PRO A N     1 
ATOM   8627  C CA    . PRO B 2 1071 ? 132.277 144.535 118.709 1.00 44.73  ? 1068 PRO A CA    1 
ATOM   8628  C C     . PRO B 2 1071 ? 131.142 145.258 118.003 1.00 44.73  ? 1068 PRO A C     1 
ATOM   8629  O O     . PRO B 2 1071 ? 130.091 145.541 118.584 1.00 44.73  ? 1068 PRO A O     1 
ATOM   8630  C CB    . PRO B 2 1071 ? 132.181 143.021 118.490 1.00 44.73  ? 1068 PRO A CB    1 
ATOM   8631  C CG    . PRO B 2 1071 ? 131.485 142.518 119.685 1.00 44.73  ? 1068 PRO A CG    1 
ATOM   8632  C CD    . PRO B 2 1071 ? 131.980 143.367 120.811 1.00 44.73  ? 1068 PRO A CD    1 
ATOM   8633  N N     . TYR B 2 1072 ? 131.391 145.571 116.729 1.00 44.73  ? 1069 TYR A N     1 
ATOM   8634  C CA    . TYR B 2 1072 ? 130.418 146.207 115.842 1.00 44.73  ? 1069 TYR A CA    1 
ATOM   8635  C C     . TYR B 2 1072 ? 130.078 147.606 116.344 1.00 44.73  ? 1069 TYR A C     1 
ATOM   8636  O O     . TYR B 2 1072 ? 128.914 147.964 116.529 1.00 44.73  ? 1069 TYR A O     1 
ATOM   8637  C CB    . TYR B 2 1072 ? 129.161 145.351 115.704 1.00 44.73  ? 1069 TYR A CB    1 
ATOM   8638  C CG    . TYR B 2 1072 ? 129.336 144.226 114.724 1.00 44.73  ? 1069 TYR A CG    1 
ATOM   8639  C CD1   . TYR B 2 1072 ? 129.424 144.460 113.361 1.00 44.73  ? 1069 TYR A CD1   1 
ATOM   8640  C CD2   . TYR B 2 1072 ? 129.441 142.921 115.174 1.00 44.73  ? 1069 TYR A CD2   1 
ATOM   8641  C CE1   . TYR B 2 1072 ? 129.599 143.417 112.476 1.00 44.73  ? 1069 TYR A CE1   1 
ATOM   8642  C CE2   . TYR B 2 1072 ? 129.616 141.881 114.307 1.00 44.73  ? 1069 TYR A CE2   1 
ATOM   8643  C CZ    . TYR B 2 1072 ? 129.694 142.129 112.961 1.00 44.73  ? 1069 TYR A CZ    1 
ATOM   8644  O OH    . TYR B 2 1072 ? 129.868 141.068 112.113 1.00 44.73  ? 1069 TYR A OH    1 
ATOM   8645  N N     . THR B 2 1073 ? 131.111 148.380 116.602 1.00 44.73  ? 1070 THR A N     1 
ATOM   8646  C CA    . THR B 2 1073 ? 130.955 149.718 117.149 1.00 44.73  ? 1070 THR A CA    1 
ATOM   8647  C C     . THR B 2 1073 ? 131.726 150.782 116.382 1.00 44.73  ? 1070 THR A C     1 
ATOM   8648  O O     . THR B 2 1073 ? 131.200 151.876 116.164 1.00 44.73  ? 1070 THR A O     1 
ATOM   8649  C CB    . THR B 2 1073 ? 131.399 149.699 118.619 1.00 44.73  ? 1070 THR A CB    1 
ATOM   8650  O OG1   . THR B 2 1073 ? 130.438 148.980 119.402 1.00 44.73  ? 1070 THR A OG1   1 
ATOM   8651  C CG2   . THR B 2 1073 ? 131.528 151.092 119.153 1.00 44.73  ? 1070 THR A CG2   1 
ATOM   8652  N N     . SER B 2 1074 ? 132.946 150.480 115.937 1.00 44.73  ? 1071 SER A N     1 
ATOM   8653  C CA    . SER B 2 1074 ? 133.822 151.487 115.355 1.00 44.73  ? 1071 SER A CA    1 
ATOM   8654  C C     . SER B 2 1074 ? 133.938 151.397 113.841 1.00 44.73  ? 1071 SER A C     1 
ATOM   8655  O O     . SER B 2 1074 ? 134.419 152.348 113.217 1.00 44.73  ? 1071 SER A O     1 
ATOM   8656  C CB    . SER B 2 1074 ? 135.224 151.382 115.964 1.00 44.73  ? 1071 SER A CB    1 
ATOM   8657  O OG    . SER B 2 1074 ? 135.673 150.039 115.969 1.00 44.73  ? 1071 SER A OG    1 
ATOM   8658  N N     . LYS B 2 1075 ? 133.517 150.287 113.240 1.00 44.73  ? 1072 LYS A N     1 
ATOM   8659  C CA    . LYS B 2 1075 ? 133.620 150.119 111.797 1.00 44.73  ? 1072 LYS A CA    1 
ATOM   8660  C C     . LYS B 2 1075 ? 132.254 150.280 111.147 1.00 44.73  ? 1072 LYS A C     1 
ATOM   8661  O O     . LYS B 2 1075 ? 131.932 149.580 110.182 1.00 44.73  ? 1072 LYS A O     1 
ATOM   8662  C CB    . LYS B 2 1075 ? 134.215 148.752 111.459 1.00 44.73  ? 1072 LYS A CB    1 
ATOM   8663  C CG    . LYS B 2 1075 ? 135.693 148.784 111.111 1.00 44.73  ? 1072 LYS A CG    1 
ATOM   8664  C CD    . LYS B 2 1075 ? 136.324 147.411 111.272 1.00 44.73  ? 1072 LYS A CD    1 
ATOM   8665  C CE    . LYS B 2 1075 ? 137.624 147.304 110.495 1.00 44.73  ? 1072 LYS A CE    1 
ATOM   8666  N NZ    . LYS B 2 1075 ? 137.387 147.170 109.032 1.00 44.73  ? 1072 LYS A NZ    1 
ATOM   8667  N N     . ILE B 2 1076 ? 131.445 151.198 111.668 1.00 44.73  ? 1073 ILE A N     1 
ATOM   8668  C CA    . ILE B 2 1076 ? 130.088 151.421 111.190 1.00 44.73  ? 1073 ILE A CA    1 
ATOM   8669  C C     . ILE B 2 1076 ? 129.970 152.845 110.672 1.00 44.73  ? 1073 ILE A C     1 
ATOM   8670  O O     . ILE B 2 1076 ? 130.500 153.783 111.277 1.00 44.73  ? 1073 ILE A O     1 
ATOM   8671  C CB    . ILE B 2 1076 ? 129.040 151.167 112.293 1.00 44.73  ? 1073 ILE A CB    1 
ATOM   8672  C CG1   . ILE B 2 1076 ? 129.276 149.815 112.958 1.00 44.73  ? 1073 ILE A CG1   1 
ATOM   8673  C CG2   . ILE B 2 1076 ? 127.635 151.236 111.727 1.00 44.73  ? 1073 ILE A CG2   1 
ATOM   8674  C CD1   . ILE B 2 1076 ? 128.175 149.427 113.911 1.00 44.73  ? 1073 ILE A CD1   1 
ATOM   8675  N N     . ASP B 2 1077 ? 129.281 153.000 109.551 1.00 44.73  ? 1074 ASP A N     1 
ATOM   8676  C CA    . ASP B 2 1077 ? 128.910 154.315 109.060 1.00 44.73  ? 1074 ASP A CA    1 
ATOM   8677  C C     . ASP B 2 1077 ? 127.970 154.974 110.062 1.00 44.73  ? 1074 ASP A C     1 
ATOM   8678  O O     . ASP B 2 1077 ? 126.907 154.412 110.363 1.00 44.73  ? 1074 ASP A O     1 
ATOM   8679  C CB    . ASP B 2 1077 ? 128.235 154.186 107.697 1.00 44.73  ? 1074 ASP A CB    1 
ATOM   8680  C CG    . ASP B 2 1077 ? 127.803 155.520 107.121 1.00 44.73  ? 1074 ASP A CG    1 
ATOM   8681  O OD1   . ASP B 2 1077 ? 128.239 156.574 107.627 1.00 44.73  ? 1074 ASP A OD1   1 
ATOM   8682  O OD2   . ASP B 2 1077 ? 127.018 155.513 106.151 1.00 44.73  ? 1074 ASP A OD2   1 
ATOM   8683  N N     . PRO B 2 1078 ? 128.309 156.149 110.600 1.00 44.73  ? 1075 PRO A N     1 
ATOM   8684  C CA    . PRO B 2 1078 ? 127.429 156.786 111.588 1.00 44.73  ? 1075 PRO A CA    1 
ATOM   8685  C C     . PRO B 2 1078 ? 126.222 157.486 110.990 1.00 44.73  ? 1075 PRO A C     1 
ATOM   8686  O O     . PRO B 2 1078 ? 125.447 158.088 111.744 1.00 44.73  ? 1075 PRO A O     1 
ATOM   8687  C CB    . PRO B 2 1078 ? 128.357 157.792 112.278 1.00 44.73  ? 1075 PRO A CB    1 
ATOM   8688  C CG    . PRO B 2 1078 ? 129.372 158.117 111.252 1.00 44.73  ? 1075 PRO A CG    1 
ATOM   8689  C CD    . PRO B 2 1078 ? 129.587 156.865 110.454 1.00 44.73  ? 1075 PRO A CD    1 
ATOM   8690  N N     . LEU B 2 1079 ? 126.039 157.439 109.672 1.00 44.73  ? 1076 LEU A N     1 
ATOM   8691  C CA    . LEU B 2 1079 ? 124.880 158.052 109.037 1.00 44.73  ? 1076 LEU A CA    1 
ATOM   8692  C C     . LEU B 2 1079 ? 123.848 157.040 108.570 1.00 44.73  ? 1076 LEU A C     1 
ATOM   8693  O O     . LEU B 2 1079 ? 122.657 157.361 108.530 1.00 44.73  ? 1076 LEU A O     1 
ATOM   8694  C CB    . LEU B 2 1079 ? 125.315 158.906 107.842 1.00 44.73  ? 1076 LEU A CB    1 
ATOM   8695  C CG    . LEU B 2 1079 ? 126.173 160.134 108.142 1.00 44.73  ? 1076 LEU A CG    1 
ATOM   8696  C CD1   . LEU B 2 1079 ? 126.116 161.112 106.985 1.00 44.73  ? 1076 LEU A CD1   1 
ATOM   8697  C CD2   . LEU B 2 1079 ? 125.729 160.798 109.430 1.00 44.73  ? 1076 LEU A CD2   1 
ATOM   8698  N N     . THR B 2 1080 ? 124.275 155.829 108.211 1.00 44.73  ? 1077 THR A N     1 
ATOM   8699  C CA    . THR B 2 1080 ? 123.366 154.793 107.748 1.00 44.73  ? 1077 THR A CA    1 
ATOM   8700  C C     . THR B 2 1080 ? 123.370 153.541 108.609 1.00 44.73  ? 1077 THR A C     1 
ATOM   8701  O O     . THR B 2 1080 ? 122.484 152.697 108.438 1.00 44.73  ? 1077 THR A O     1 
ATOM   8702  C CB    . THR B 2 1080 ? 123.702 154.389 106.305 1.00 44.73  ? 1077 THR A CB    1 
ATOM   8703  O OG1   . THR B 2 1080 ? 124.916 153.630 106.296 1.00 44.73  ? 1077 THR A OG1   1 
ATOM   8704  C CG2   . THR B 2 1080 ? 123.873 155.616 105.433 1.00 44.73  ? 1077 THR A CG2   1 
ATOM   8705  N N     . GLY B 2 1081 ? 124.326 153.391 109.521 1.00 44.73  ? 1078 GLY A N     1 
ATOM   8706  C CA    . GLY B 2 1081 ? 124.436 152.169 110.287 1.00 44.73  ? 1078 GLY A CA    1 
ATOM   8707  C C     . GLY B 2 1081 ? 124.974 150.992 109.511 1.00 44.73  ? 1078 GLY A C     1 
ATOM   8708  O O     . GLY B 2 1081 ? 124.879 149.857 109.990 1.00 44.73  ? 1078 GLY A O     1 
ATOM   8709  N N     . PHE B 2 1082 ? 125.541 151.227 108.333 1.00 44.73  ? 1079 PHE A N     1 
ATOM   8710  C CA    . PHE B 2 1082 ? 125.995 150.142 107.479 1.00 44.73  ? 1079 PHE A CA    1 
ATOM   8711  C C     . PHE B 2 1082 ? 127.278 149.523 108.018 1.00 44.73  ? 1079 PHE A C     1 
ATOM   8712  O O     . PHE B 2 1082 ? 128.150 150.218 108.547 1.00 44.73  ? 1079 PHE A O     1 
ATOM   8713  C CB    . PHE B 2 1082 ? 126.216 150.660 106.059 1.00 44.73  ? 1079 PHE A CB    1 
ATOM   8714  C CG    . PHE B 2 1082 ? 126.641 149.605 105.083 1.00 44.73  ? 1079 PHE A CG    1 
ATOM   8715  C CD1   . PHE B 2 1082 ? 125.888 148.458 104.911 1.00 44.73  ? 1079 PHE A CD1   1 
ATOM   8716  C CD2   . PHE B 2 1082 ? 127.784 149.770 104.325 1.00 44.73  ? 1079 PHE A CD2   1 
ATOM   8717  C CE1   . PHE B 2 1082 ? 126.274 147.492 104.006 1.00 44.73  ? 1079 PHE A CE1   1 
ATOM   8718  C CE2   . PHE B 2 1082 ? 128.174 148.810 103.421 1.00 44.73  ? 1079 PHE A CE2   1 
ATOM   8719  C CZ    . PHE B 2 1082 ? 127.420 147.668 103.260 1.00 44.73  ? 1079 PHE A CZ    1 
ATOM   8720  N N     . VAL B 2 1083 ? 127.387 148.203 107.880 1.00 44.73  ? 1080 VAL A N     1 
ATOM   8721  C CA    . VAL B 2 1083 ? 128.592 147.465 108.226 1.00 44.73  ? 1080 VAL A CA    1 
ATOM   8722  C C     . VAL B 2 1083 ? 128.989 146.622 107.023 1.00 44.73  ? 1080 VAL A C     1 
ATOM   8723  O O     . VAL B 2 1083 ? 128.167 146.301 106.163 1.00 44.73  ? 1080 VAL A O     1 
ATOM   8724  C CB    . VAL B 2 1083 ? 128.404 146.573 109.473 1.00 44.73  ? 1080 VAL A CB    1 
ATOM   8725  C CG1   . VAL B 2 1083 ? 127.859 147.387 110.632 1.00 44.73  ? 1080 VAL A CG1   1 
ATOM   8726  C CG2   . VAL B 2 1083 ? 127.482 145.408 109.159 1.00 44.73  ? 1080 VAL A CG2   1 
ATOM   8727  N N     . ASP B 2 1084 ? 130.266 146.279 106.963 1.00 44.73  ? 1081 ASP A N     1 
ATOM   8728  C CA    . ASP B 2 1084 ? 130.769 145.455 105.872 1.00 44.73  ? 1081 ASP A CA    1 
ATOM   8729  C C     . ASP B 2 1084 ? 130.135 144.076 105.984 1.00 44.73  ? 1081 ASP A C     1 
ATOM   8730  O O     . ASP B 2 1084 ? 130.486 143.322 106.902 1.00 44.73  ? 1081 ASP A O     1 
ATOM   8731  C CB    . ASP B 2 1084 ? 132.296 145.366 105.934 1.00 44.73  ? 1081 ASP A CB    1 
ATOM   8732  C CG    . ASP B 2 1084 ? 132.897 144.581 104.773 1.00 44.73  ? 1081 ASP A CG    1 
ATOM   8733  O OD1   . ASP B 2 1084 ? 132.152 143.925 104.015 1.00 44.73  ? 1081 ASP A OD1   1 
ATOM   8734  O OD2   . ASP B 2 1084 ? 134.133 144.644 104.606 1.00 44.73  ? 1081 ASP A OD2   1 
ATOM   8735  N N     . PRO B 2 1085 ? 129.216 143.699 105.092 1.00 44.73  ? 1082 PRO A N     1 
ATOM   8736  C CA    . PRO B 2 1085 ? 128.448 142.467 105.291 1.00 44.73  ? 1082 PRO A CA    1 
ATOM   8737  C C     . PRO B 2 1085 ? 129.132 141.202 104.808 1.00 44.73  ? 1082 PRO A C     1 
ATOM   8738  O O     . PRO B 2 1085 ? 128.604 140.109 105.055 1.00 44.73  ? 1082 PRO A O     1 
ATOM   8739  C CB    . PRO B 2 1085 ? 127.178 142.738 104.476 1.00 44.73  ? 1082 PRO A CB    1 
ATOM   8740  C CG    . PRO B 2 1085 ? 127.646 143.608 103.352 1.00 44.73  ? 1082 PRO A CG    1 
ATOM   8741  C CD    . PRO B 2 1085 ? 128.872 144.361 103.822 1.00 44.73  ? 1082 PRO A CD    1 
ATOM   8742  N N     . PHE B 2 1086 ? 130.274 141.307 104.139 1.00 44.73  ? 1083 PHE A N     1 
ATOM   8743  C CA    . PHE B 2 1086 ? 130.952 140.157 103.559 1.00 44.73  ? 1083 PHE A CA    1 
ATOM   8744  C C     . PHE B 2 1086 ? 132.221 139.870 104.346 1.00 44.73  ? 1083 PHE A C     1 
ATOM   8745  O O     . PHE B 2 1086 ? 133.070 140.753 104.504 1.00 44.73  ? 1083 PHE A O     1 
ATOM   8746  C CB    . PHE B 2 1086 ? 131.289 140.404 102.090 1.00 44.73  ? 1083 PHE A CB    1 
ATOM   8747  C CG    . PHE B 2 1086 ? 130.172 141.020 101.308 1.00 44.73  ? 1083 PHE A CG    1 
ATOM   8748  C CD1   . PHE B 2 1086 ? 128.979 140.348 101.136 1.00 44.73  ? 1083 PHE A CD1   1 
ATOM   8749  C CD2   . PHE B 2 1086 ? 130.319 142.272 100.738 1.00 44.73  ? 1083 PHE A CD2   1 
ATOM   8750  C CE1   . PHE B 2 1086 ? 127.952 140.914 100.414 1.00 44.73  ? 1083 PHE A CE1   1 
ATOM   8751  C CE2   . PHE B 2 1086 ? 129.295 142.841 100.016 1.00 44.73  ? 1083 PHE A CE2   1 
ATOM   8752  C CZ    . PHE B 2 1086 ? 128.110 142.162 99.854  1.00 44.73  ? 1083 PHE A CZ    1 
ATOM   8753  N N     . VAL B 2 1087 ? 132.348 138.641 104.835 1.00 44.73  ? 1084 VAL A N     1 
ATOM   8754  C CA    . VAL B 2 1087 ? 133.609 138.175 105.400 1.00 44.73  ? 1084 VAL A CA    1 
ATOM   8755  C C     . VAL B 2 1087 ? 134.515 137.788 104.235 1.00 44.73  ? 1084 VAL A C     1 
ATOM   8756  O O     . VAL B 2 1087 ? 134.135 137.002 103.364 1.00 44.73  ? 1084 VAL A O     1 
ATOM   8757  C CB    . VAL B 2 1087 ? 133.403 137.018 106.388 1.00 44.73  ? 1084 VAL A CB    1 
ATOM   8758  C CG1   . VAL B 2 1087 ? 132.847 135.772 105.707 1.00 44.73  ? 1084 VAL A CG1   1 
ATOM   8759  C CG2   . VAL B 2 1087 ? 134.708 136.699 107.105 1.00 44.73  ? 1084 VAL A CG2   1 
ATOM   8760  N N     . TRP B 2 1088 ? 135.701 138.388 104.183 1.00 44.73  ? 1085 TRP A N     1 
ATOM   8761  C CA    . TRP B 2 1088 ? 136.557 138.218 103.019 1.00 44.73  ? 1085 TRP A CA    1 
ATOM   8762  C C     . TRP B 2 1088 ? 137.387 136.946 103.078 1.00 44.73  ? 1085 TRP A C     1 
ATOM   8763  O O     . TRP B 2 1088 ? 138.153 136.681 102.146 1.00 44.73  ? 1085 TRP A O     1 
ATOM   8764  C CB    . TRP B 2 1088 ? 137.469 139.433 102.852 1.00 44.73  ? 1085 TRP A CB    1 
ATOM   8765  C CG    . TRP B 2 1088 ? 136.714 140.709 102.630 1.00 44.73  ? 1085 TRP A CG    1 
ATOM   8766  C CD1   . TRP B 2 1088 ? 136.694 141.799 103.447 1.00 44.73  ? 1085 TRP A CD1   1 
ATOM   8767  C CD2   . TRP B 2 1088 ? 135.827 141.007 101.544 1.00 44.73  ? 1085 TRP A CD2   1 
ATOM   8768  N NE1   . TRP B 2 1088 ? 135.876 142.769 102.922 1.00 44.73  ? 1085 TRP A NE1   1 
ATOM   8769  C CE2   . TRP B 2 1088 ? 135.333 142.306 101.754 1.00 44.73  ? 1085 TRP A CE2   1 
ATOM   8770  C CE3   . TRP B 2 1088 ? 135.421 140.308 100.404 1.00 44.73  ? 1085 TRP A CE3   1 
ATOM   8771  C CZ2   . TRP B 2 1088 ? 134.449 142.918 100.872 1.00 44.73  ? 1085 TRP A CZ2   1 
ATOM   8772  C CZ3   . TRP B 2 1088 ? 134.548 140.918 99.529  1.00 44.73  ? 1085 TRP A CZ3   1 
ATOM   8773  C CH2   . TRP B 2 1088 ? 134.069 142.209 99.768  1.00 44.73  ? 1085 TRP A CH2   1 
ATOM   8774  N N     . LYS B 2 1089 ? 137.266 136.165 104.148 1.00 44.73  ? 1086 LYS A N     1 
ATOM   8775  C CA    . LYS B 2 1089 ? 137.937 134.877 104.226 1.00 44.73  ? 1086 LYS A CA    1 
ATOM   8776  C C     . LYS B 2 1089 ? 137.240 133.802 103.403 1.00 44.73  ? 1086 LYS A C     1 
ATOM   8777  O O     . LYS B 2 1089 ? 137.783 132.701 103.267 1.00 44.73  ? 1086 LYS A O     1 
ATOM   8778  C CB    . LYS B 2 1089 ? 138.037 134.431 105.686 1.00 44.73  ? 1086 LYS A CB    1 
ATOM   8779  C CG    . LYS B 2 1089 ? 138.883 135.355 106.547 1.00 44.73  ? 1086 LYS A CG    1 
ATOM   8780  C CD    . LYS B 2 1089 ? 138.891 134.913 107.999 1.00 44.73  ? 1086 LYS A CD    1 
ATOM   8781  C CE    . LYS B 2 1089 ? 139.802 133.718 108.210 1.00 44.73  ? 1086 LYS A CE    1 
ATOM   8782  N NZ    . LYS B 2 1089 ? 139.997 133.432 109.657 1.00 44.73  ? 1086 LYS A NZ    1 
ATOM   8783  N N     . THR B 2 1090 ? 136.061 134.091 102.856 1.00 44.73  ? 1087 THR A N     1 
ATOM   8784  C CA    . THR B 2 1090 ? 135.317 133.135 102.050 1.00 44.73  ? 1087 THR A CA    1 
ATOM   8785  C C     . THR B 2 1090 ? 135.571 133.284 100.555 1.00 44.73  ? 1087 THR A C     1 
ATOM   8786  O O     . THR B 2 1090 ? 134.966 132.552 99.765  1.00 44.73  ? 1087 THR A O     1 
ATOM   8787  C CB    . THR B 2 1090 ? 133.816 133.262 102.326 1.00 44.73  ? 1087 THR A CB    1 
ATOM   8788  O OG1   . THR B 2 1090 ? 133.431 134.641 102.272 1.00 44.73  ? 1087 THR A OG1   1 
ATOM   8789  C CG2   . THR B 2 1090 ? 133.479 132.696 103.698 1.00 44.73  ? 1087 THR A CG2   1 
ATOM   8790  N N     . ILE B 2 1091 ? 136.441 134.203 100.145 1.00 44.73  ? 1088 ILE A N     1 
ATOM   8791  C CA    . ILE B 2 1091 ? 136.855 134.331 98.752  1.00 44.73  ? 1088 ILE A CA    1 
ATOM   8792  C C     . ILE B 2 1091 ? 138.323 133.936 98.656  1.00 44.73  ? 1088 ILE A C     1 
ATOM   8793  O O     . ILE B 2 1091 ? 139.197 134.618 99.207  1.00 44.73  ? 1088 ILE A O     1 
ATOM   8794  C CB    . ILE B 2 1091 ? 136.622 135.749 98.204  1.00 44.73  ? 1088 ILE A CB    1 
ATOM   8795  C CG1   . ILE B 2 1091 ? 137.180 136.807 99.156  1.00 44.73  ? 1088 ILE A CG1   1 
ATOM   8796  C CG2   . ILE B 2 1091 ? 135.145 135.989 97.950  1.00 44.73  ? 1088 ILE A CG2   1 
ATOM   8797  C CD1   . ILE B 2 1091 ? 137.405 138.144 98.510  1.00 44.73  ? 1088 ILE A CD1   1 
ATOM   8798  N N     . LYS B 2 1092 ? 138.589 132.829 97.986  1.00 44.73  ? 1089 LYS A N     1 
ATOM   8799  C CA    . LYS B 2 1092 ? 139.961 132.396 97.751  1.00 44.73  ? 1089 LYS A CA    1 
ATOM   8800  C C     . LYS B 2 1092 ? 140.238 132.071 96.292  1.00 44.73  ? 1089 LYS A C     1 
ATOM   8801  O O     . LYS B 2 1092 ? 141.332 132.359 95.803  1.00 44.73  ? 1089 LYS A O     1 
ATOM   8802  C CB    . LYS B 2 1092 ? 140.289 131.172 98.624  1.00 41.33  ? 1089 LYS A CB    1 
ATOM   8803  C CG    . LYS B 2 1092 ? 140.065 131.386 100.113 1.00 41.33  ? 1089 LYS A CG    1 
ATOM   8804  C CD    . LYS B 2 1092 ? 139.510 130.135 100.774 1.00 41.33  ? 1089 LYS A CD    1 
ATOM   8805  C CE    . LYS B 2 1092 ? 138.020 129.987 100.516 1.00 41.33  ? 1089 LYS A CE    1 
ATOM   8806  N NZ    . LYS B 2 1092 ? 137.407 128.954 101.397 1.00 41.33  ? 1089 LYS A NZ    1 
ATOM   8807  N N     . ASN B 2 1093 ? 139.276 131.490 95.586  1.00 44.73  ? 1090 ASN A N     1 
ATOM   8808  C CA    . ASN B 2 1093 ? 139.473 131.010 94.228  1.00 44.73  ? 1090 ASN A CA    1 
ATOM   8809  C C     . ASN B 2 1093 ? 138.668 131.845 93.242  1.00 44.73  ? 1090 ASN A C     1 
ATOM   8810  O O     . ASN B 2 1093 ? 137.874 132.712 93.616  1.00 44.73  ? 1090 ASN A O     1 
ATOM   8811  C CB    . ASN B 2 1093 ? 139.086 129.531 94.116  1.00 44.73  ? 1090 ASN A CB    1 
ATOM   8812  C CG    . ASN B 2 1093 ? 137.687 129.253 94.630  1.00 44.73  ? 1090 ASN A CG    1 
ATOM   8813  O OD1   . ASN B 2 1093 ? 136.697 129.667 94.028  1.00 44.73  ? 1090 ASN A OD1   1 
ATOM   8814  N ND2   . ASN B 2 1093 ? 137.598 128.546 95.751  1.00 44.73  ? 1090 ASN A ND2   1 
ATOM   8815  N N     . HIS B 2 1094 ? 138.896 131.567 91.956  1.00 44.73  ? 1091 HIS A N     1 
ATOM   8816  C CA    . HIS B 2 1094 ? 138.190 132.284 90.901  1.00 44.73  ? 1091 HIS A CA    1 
ATOM   8817  C C     . HIS B 2 1094 ? 136.696 131.992 90.941  1.00 44.73  ? 1091 HIS A C     1 
ATOM   8818  O O     . HIS B 2 1094 ? 135.875 132.886 90.706  1.00 44.73  ? 1091 HIS A O     1 
ATOM   8819  C CB    . HIS B 2 1094 ? 138.774 131.912 89.539  1.00 44.73  ? 1091 HIS A CB    1 
ATOM   8820  C CG    . HIS B 2 1094 ? 138.504 132.921 88.468  1.00 44.73  ? 1091 HIS A CG    1 
ATOM   8821  N ND1   . HIS B 2 1094 ? 138.316 132.573 87.148  1.00 44.73  ? 1091 HIS A ND1   1 
ATOM   8822  C CD2   . HIS B 2 1094 ? 138.401 134.270 88.520  1.00 44.73  ? 1091 HIS A CD2   1 
ATOM   8823  C CE1   . HIS B 2 1094 ? 138.104 133.664 86.434  1.00 44.73  ? 1091 HIS A CE1   1 
ATOM   8824  N NE2   . HIS B 2 1094 ? 138.151 134.707 87.242  1.00 44.73  ? 1091 HIS A NE2   1 
ATOM   8825  N N     . GLU B 2 1095 ? 136.326 130.742 91.227  1.00 47.56  ? 1092 GLU A N     1 
ATOM   8826  C CA    . GLU B 2 1095 ? 134.912 130.389 91.308  1.00 47.56  ? 1092 GLU A CA    1 
ATOM   8827  C C     . GLU B 2 1095 ? 134.224 131.126 92.449  1.00 47.56  ? 1092 GLU A C     1 
ATOM   8828  O O     . GLU B 2 1095 ? 133.076 131.564 92.310  1.00 47.56  ? 1092 GLU A O     1 
ATOM   8829  C CB    . GLU B 2 1095 ? 134.756 128.877 91.471  1.00 47.56  ? 1092 GLU A CB    1 
ATOM   8830  C CG    . GLU B 2 1095 ? 135.274 128.068 90.292  1.00 47.56  ? 1092 GLU A CG    1 
ATOM   8831  C CD    . GLU B 2 1095 ? 135.058 128.765 88.963  1.00 47.56  ? 1092 GLU A CD    1 
ATOM   8832  O OE1   . GLU B 2 1095 ? 133.890 128.896 88.541  1.00 47.56  ? 1092 GLU A OE1   1 
ATOM   8833  O OE2   . GLU B 2 1095 ? 136.057 129.183 88.339  1.00 47.56  ? 1092 GLU A OE2   1 
ATOM   8834  N N     . SER B 2 1096 ? 134.905 131.264 93.589  1.00 44.92  ? 1093 SER A N     1 
ATOM   8835  C CA    . SER B 2 1096 ? 134.345 132.036 94.693  1.00 44.92  ? 1093 SER A CA    1 
ATOM   8836  C C     . SER B 2 1096 ? 134.187 133.503 94.313  1.00 44.92  ? 1093 SER A C     1 
ATOM   8837  O O     . SER B 2 1096 ? 133.165 134.125 94.624  1.00 44.92  ? 1093 SER A O     1 
ATOM   8838  C CB    . SER B 2 1096 ? 135.225 131.893 95.935  1.00 44.92  ? 1093 SER A CB    1 
ATOM   8839  O OG    . SER B 2 1096 ? 136.570 132.237 95.650  1.00 44.92  ? 1093 SER A OG    1 
ATOM   8840  N N     . ARG B 2 1097 ? 135.190 134.072 93.640  1.00 44.73  ? 1094 ARG A N     1 
ATOM   8841  C CA    . ARG B 2 1097 ? 135.101 135.466 93.219  1.00 44.73  ? 1094 ARG A CA    1 
ATOM   8842  C C     . ARG B 2 1097 ? 133.958 135.677 92.236  1.00 44.73  ? 1094 ARG A C     1 
ATOM   8843  O O     . ARG B 2 1097 ? 133.198 136.646 92.355  1.00 44.73  ? 1094 ARG A O     1 
ATOM   8844  C CB    . ARG B 2 1097 ? 136.425 135.914 92.600  1.00 44.73  ? 1094 ARG A CB    1 
ATOM   8845  C CG    . ARG B 2 1097 ? 137.443 136.422 93.603  1.00 44.73  ? 1094 ARG A CG    1 
ATOM   8846  C CD    . ARG B 2 1097 ? 138.616 137.088 92.902  1.00 44.73  ? 1094 ARG A CD    1 
ATOM   8847  N NE    . ARG B 2 1097 ? 139.767 136.199 92.801  1.00 44.73  ? 1094 ARG A NE    1 
ATOM   8848  C CZ    . ARG B 2 1097 ? 140.621 135.964 93.788  1.00 44.73  ? 1094 ARG A CZ    1 
ATOM   8849  N NH1   . ARG B 2 1097 ? 140.491 136.548 94.968  1.00 44.73  ? 1094 ARG A NH1   1 
ATOM   8850  N NH2   . ARG B 2 1097 ? 141.631 135.122 93.586  1.00 44.73  ? 1094 ARG A NH2   1 
ATOM   8851  N N     . LYS B 2 1098 ? 133.822 134.784 91.254  1.00 44.73  ? 1095 LYS A N     1 
ATOM   8852  C CA    . LYS B 2 1098 ? 132.740 134.912 90.284  1.00 44.73  ? 1095 LYS A CA    1 
ATOM   8853  C C     . LYS B 2 1098 ? 131.381 134.717 90.942  1.00 44.73  ? 1095 LYS A C     1 
ATOM   8854  O O     . LYS B 2 1098 ? 130.434 135.459 90.654  1.00 44.73  ? 1095 LYS A O     1 
ATOM   8855  C CB    . LYS B 2 1098 ? 132.932 133.908 89.150  1.00 41.49  ? 1095 LYS A CB    1 
ATOM   8856  C CG    . LYS B 2 1098 ? 133.834 134.392 88.032  1.00 41.49  ? 1095 LYS A CG    1 
ATOM   8857  C CD    . LYS B 2 1098 ? 133.399 133.810 86.698  1.00 41.49  ? 1095 LYS A CD    1 
ATOM   8858  C CE    . LYS B 2 1098 ? 134.074 132.473 86.437  1.00 41.49  ? 1095 LYS A CE    1 
ATOM   8859  N NZ    . LYS B 2 1098 ? 134.120 132.146 84.986  1.00 41.49  ? 1095 LYS A NZ    1 
ATOM   8860  N N     . HIS B 2 1099 ? 131.263 133.723 91.825  1.00 44.73  ? 1096 HIS A N     1 
ATOM   8861  C CA    . HIS B 2 1099 ? 129.996 133.493 92.510  1.00 44.73  ? 1096 HIS A CA    1 
ATOM   8862  C C     . HIS B 2 1099 ? 129.656 134.659 93.430  1.00 44.73  ? 1096 HIS A C     1 
ATOM   8863  O O     . HIS B 2 1099 ? 128.489 135.052 93.545  1.00 44.73  ? 1096 HIS A O     1 
ATOM   8864  C CB    . HIS B 2 1099 ? 130.050 132.180 93.289  1.00 44.73  ? 1096 HIS A CB    1 
ATOM   8865  C CG    . HIS B 2 1099 ? 128.773 131.841 93.992  1.00 44.73  ? 1096 HIS A CG    1 
ATOM   8866  N ND1   . HIS B 2 1099 ? 128.625 131.953 95.358  1.00 44.73  ? 1096 HIS A ND1   1 
ATOM   8867  C CD2   . HIS B 2 1099 ? 127.585 131.396 93.520  1.00 44.73  ? 1096 HIS A CD2   1 
ATOM   8868  C CE1   . HIS B 2 1099 ? 127.401 131.590 95.697  1.00 44.73  ? 1096 HIS A CE1   1 
ATOM   8869  N NE2   . HIS B 2 1099 ? 126.750 131.247 94.601  1.00 44.73  ? 1096 HIS A NE2   1 
ATOM   8870  N N     . PHE B 2 1100 ? 130.665 135.218 94.102  1.00 44.73  ? 1097 PHE A N     1 
ATOM   8871  C CA    . PHE B 2 1100 ? 130.455 136.419 94.904  1.00 44.73  ? 1097 PHE A CA    1 
ATOM   8872  C C     . PHE B 2 1100 ? 130.023 137.589 94.030  1.00 44.73  ? 1097 PHE A C     1 
ATOM   8873  O O     . PHE B 2 1100 ? 129.111 138.344 94.386  1.00 44.73  ? 1097 PHE A O     1 
ATOM   8874  C CB    . PHE B 2 1100 ? 131.734 136.760 95.672  1.00 44.73  ? 1097 PHE A CB    1 
ATOM   8875  C CG    . PHE B 2 1100 ? 131.596 137.928 96.607  1.00 44.73  ? 1097 PHE A CG    1 
ATOM   8876  C CD1   . PHE B 2 1100 ? 131.761 139.225 96.150  1.00 44.73  ? 1097 PHE A CD1   1 
ATOM   8877  C CD2   . PHE B 2 1100 ? 131.314 137.728 97.945  1.00 44.73  ? 1097 PHE A CD2   1 
ATOM   8878  C CE1   . PHE B 2 1100 ? 131.637 140.297 97.006  1.00 44.73  ? 1097 PHE A CE1   1 
ATOM   8879  C CE2   . PHE B 2 1100 ? 131.191 138.797 98.808  1.00 44.73  ? 1097 PHE A CE2   1 
ATOM   8880  C CZ    . PHE B 2 1100 ? 131.353 140.083 98.337  1.00 44.73  ? 1097 PHE A CZ    1 
ATOM   8881  N N     . LEU B 2 1101 ? 130.671 137.754 92.877  1.00 44.73  ? 1098 LEU A N     1 
ATOM   8882  C CA    . LEU B 2 1101 ? 130.372 138.896 92.022  1.00 44.73  ? 1098 LEU A CA    1 
ATOM   8883  C C     . LEU B 2 1101 ? 129.008 138.765 91.359  1.00 44.73  ? 1098 LEU A C     1 
ATOM   8884  O O     . LEU B 2 1101 ? 128.350 139.779 91.098  1.00 44.73  ? 1098 LEU A O     1 
ATOM   8885  C CB    . LEU B 2 1101 ? 131.462 139.059 90.965  1.00 44.73  ? 1098 LEU A CB    1 
ATOM   8886  C CG    . LEU B 2 1101 ? 131.628 140.462 90.385  1.00 44.73  ? 1098 LEU A CG    1 
ATOM   8887  C CD1   . LEU B 2 1101 ? 131.752 141.482 91.500  1.00 44.73  ? 1098 LEU A CD1   1 
ATOM   8888  C CD2   . LEU B 2 1101 ? 132.838 140.515 89.470  1.00 44.73  ? 1098 LEU A CD2   1 
ATOM   8889  N N     . GLU B 2 1102 ? 128.566 137.540 91.079  1.00 44.73  ? 1099 GLU A N     1 
ATOM   8890  C CA    . GLU B 2 1102 ? 127.286 137.343 90.412  1.00 44.73  ? 1099 GLU A CA    1 
ATOM   8891  C C     . GLU B 2 1102 ? 126.098 137.451 91.359  1.00 44.73  ? 1099 GLU A C     1 
ATOM   8892  O O     . GLU B 2 1102 ? 124.956 137.480 90.890  1.00 44.73  ? 1099 GLU A O     1 
ATOM   8893  C CB    . GLU B 2 1102 ? 127.262 135.984 89.707  1.00 44.73  ? 1099 GLU A CB    1 
ATOM   8894  C CG    . GLU B 2 1102 ? 127.086 134.798 90.637  1.00 44.73  ? 1099 GLU A CG    1 
ATOM   8895  C CD    . GLU B 2 1102 ? 127.497 133.489 89.991  1.00 44.73  ? 1099 GLU A CD    1 
ATOM   8896  O OE1   . GLU B 2 1102 ? 127.953 133.516 88.829  1.00 44.73  ? 1099 GLU A OE1   1 
ATOM   8897  O OE2   . GLU B 2 1102 ? 127.364 132.433 90.646  1.00 44.73  ? 1099 GLU A OE2   1 
ATOM   8898  N N     . GLY B 2 1103 ? 126.334 137.509 92.672  1.00 44.73  ? 1100 GLY A N     1 
ATOM   8899  C CA    . GLY B 2 1103 ? 125.243 137.691 93.613  1.00 44.73  ? 1100 GLY A CA    1 
ATOM   8900  C C     . GLY B 2 1103 ? 124.720 139.107 93.700  1.00 44.73  ? 1100 GLY A C     1 
ATOM   8901  O O     . GLY B 2 1103 ? 123.602 139.313 94.183  1.00 44.73  ? 1100 GLY A O     1 
ATOM   8902  N N     . PHE B 2 1104 ? 125.499 140.086 93.247  1.00 44.73  ? 1101 PHE A N     1 
ATOM   8903  C CA    . PHE B 2 1104 ? 125.062 141.472 93.277  1.00 44.73  ? 1101 PHE A CA    1 
ATOM   8904  C C     . PHE B 2 1104 ? 123.972 141.712 92.237  1.00 44.73  ? 1101 PHE A C     1 
ATOM   8905  O O     . PHE B 2 1104 ? 123.792 140.938 91.292  1.00 44.73  ? 1101 PHE A O     1 
ATOM   8906  C CB    . PHE B 2 1104 ? 126.240 142.412 93.025  1.00 44.73  ? 1101 PHE A CB    1 
ATOM   8907  C CG    . PHE B 2 1104 ? 127.098 142.648 94.233  1.00 44.73  ? 1101 PHE A CG    1 
ATOM   8908  C CD1   . PHE B 2 1104 ? 126.788 143.649 95.134  1.00 44.73  ? 1101 PHE A CD1   1 
ATOM   8909  C CD2   . PHE B 2 1104 ? 128.219 141.872 94.462  1.00 44.73  ? 1101 PHE A CD2   1 
ATOM   8910  C CE1   . PHE B 2 1104 ? 127.577 143.870 96.243  1.00 44.73  ? 1101 PHE A CE1   1 
ATOM   8911  C CE2   . PHE B 2 1104 ? 129.011 142.088 95.570  1.00 44.73  ? 1101 PHE A CE2   1 
ATOM   8912  C CZ    . PHE B 2 1104 ? 128.690 143.088 96.461  1.00 44.73  ? 1101 PHE A CZ    1 
ATOM   8913  N N     . ASP B 2 1105 ? 123.236 142.808 92.421  1.00 44.73  ? 1102 ASP A N     1 
ATOM   8914  C CA    . ASP B 2 1105 ? 122.137 143.120 91.512  1.00 44.73  ? 1102 ASP A CA    1 
ATOM   8915  C C     . ASP B 2 1105 ? 122.650 143.757 90.226  1.00 44.73  ? 1102 ASP A C     1 
ATOM   8916  O O     . ASP B 2 1105 ? 122.503 143.189 89.137  1.00 44.73  ? 1102 ASP A O     1 
ATOM   8917  C CB    . ASP B 2 1105 ? 121.129 144.036 92.206  1.00 44.73  ? 1102 ASP A CB    1 
ATOM   8918  C CG    . ASP B 2 1105 ? 119.809 144.114 91.465  1.00 44.73  ? 1102 ASP A CG    1 
ATOM   8919  O OD1   . ASP B 2 1105 ? 119.546 143.231 90.622  1.00 44.73  ? 1102 ASP A OD1   1 
ATOM   8920  O OD2   . ASP B 2 1105 ? 119.033 145.058 91.727  1.00 44.73  ? 1102 ASP A OD2   1 
ATOM   8921  N N     . PHE B 2 1106 ? 123.264 144.933 90.329  1.00 44.73  ? 1103 PHE A N     1 
ATOM   8922  C CA    . PHE B 2 1106 ? 123.770 145.622 89.149  1.00 44.73  ? 1103 PHE A CA    1 
ATOM   8923  C C     . PHE B 2 1106 ? 124.755 146.702 89.567  1.00 44.73  ? 1103 PHE A C     1 
ATOM   8924  O O     . PHE B 2 1106 ? 124.561 147.381 90.579  1.00 44.73  ? 1103 PHE A O     1 
ATOM   8925  C CB    . PHE B 2 1106 ? 122.629 146.229 88.319  1.00 44.73  ? 1103 PHE A CB    1 
ATOM   8926  C CG    . PHE B 2 1106 ? 121.849 147.297 89.034  1.00 44.73  ? 1103 PHE A CG    1 
ATOM   8927  C CD1   . PHE B 2 1106 ? 120.741 146.968 89.796  1.00 44.73  ? 1103 PHE A CD1   1 
ATOM   8928  C CD2   . PHE B 2 1106 ? 122.207 148.632 88.925  1.00 44.73  ? 1103 PHE A CD2   1 
ATOM   8929  C CE1   . PHE B 2 1106 ? 120.013 147.945 90.448  1.00 44.73  ? 1103 PHE A CE1   1 
ATOM   8930  C CE2   . PHE B 2 1106 ? 121.485 149.613 89.578  1.00 44.73  ? 1103 PHE A CE2   1 
ATOM   8931  C CZ    . PHE B 2 1106 ? 120.387 149.270 90.340  1.00 44.73  ? 1103 PHE A CZ    1 
ATOM   8932  N N     . LEU B 2 1107 ? 125.815 146.846 88.773  1.00 44.73  ? 1104 LEU A N     1 
ATOM   8933  C CA    . LEU B 2 1107 ? 126.808 147.901 88.933  1.00 44.73  ? 1104 LEU A CA    1 
ATOM   8934  C C     . LEU B 2 1107 ? 126.835 148.718 87.651  1.00 44.73  ? 1104 LEU A C     1 
ATOM   8935  O O     . LEU B 2 1107 ? 127.075 148.170 86.570  1.00 44.73  ? 1104 LEU A O     1 
ATOM   8936  C CB    . LEU B 2 1107 ? 128.190 147.317 89.236  1.00 44.73  ? 1104 LEU A CB    1 
ATOM   8937  C CG    . LEU B 2 1107 ? 129.313 148.301 89.575  1.00 44.73  ? 1104 LEU A CG    1 
ATOM   8938  C CD1   . LEU B 2 1107 ? 130.215 147.722 90.648  1.00 44.73  ? 1104 LEU A CD1   1 
ATOM   8939  C CD2   . LEU B 2 1107 ? 130.128 148.647 88.345  1.00 44.73  ? 1104 LEU A CD2   1 
ATOM   8940  N N     . HIS B 2 1108 ? 126.591 150.022 87.766  1.00 44.73  ? 1105 HIS A N     1 
ATOM   8941  C CA    . HIS B 2 1108 ? 126.465 150.879 86.598  1.00 44.73  ? 1105 HIS A CA    1 
ATOM   8942  C C     . HIS B 2 1108 ? 127.104 152.238 86.846  1.00 44.73  ? 1105 HIS A C     1 
ATOM   8943  O O     . HIS B 2 1108 ? 127.186 152.713 87.981  1.00 44.73  ? 1105 HIS A O     1 
ATOM   8944  C CB    . HIS B 2 1108 ? 124.993 151.052 86.202  1.00 44.73  ? 1105 HIS A CB    1 
ATOM   8945  C CG    . HIS B 2 1108 ? 124.242 152.016 87.065  1.00 44.73  ? 1105 HIS A CG    1 
ATOM   8946  N ND1   . HIS B 2 1108 ? 123.633 151.639 88.242  1.00 44.73  ? 1105 HIS A ND1   1 
ATOM   8947  C CD2   . HIS B 2 1108 ? 123.990 153.337 86.917  1.00 44.73  ? 1105 HIS A CD2   1 
ATOM   8948  C CE1   . HIS B 2 1108 ? 123.044 152.689 88.785  1.00 44.73  ? 1105 HIS A CE1   1 
ATOM   8949  N NE2   . HIS B 2 1108 ? 123.246 153.732 88.002  1.00 44.73  ? 1105 HIS A NE2   1 
ATOM   8950  N N     . TYR B 2 1109 ? 127.556 152.857 85.756  1.00 44.73  ? 1106 TYR A N     1 
ATOM   8951  C CA    . TYR B 2 1109 ? 128.135 154.197 85.775  1.00 44.73  ? 1106 TYR A CA    1 
ATOM   8952  C C     . TYR B 2 1109 ? 127.023 155.233 85.688  1.00 44.73  ? 1106 TYR A C     1 
ATOM   8953  O O     . TYR B 2 1109 ? 126.195 155.192 84.772  1.00 44.73  ? 1106 TYR A O     1 
ATOM   8954  C CB    . TYR B 2 1109 ? 129.122 154.367 84.623  1.00 44.73  ? 1106 TYR A CB    1 
ATOM   8955  C CG    . TYR B 2 1109 ? 129.802 155.719 84.569  1.00 44.73  ? 1106 TYR A CG    1 
ATOM   8956  C CD1   . TYR B 2 1109 ? 130.820 156.045 85.446  1.00 44.73  ? 1106 TYR A CD1   1 
ATOM   8957  C CD2   . TYR B 2 1109 ? 129.435 156.661 83.619  1.00 44.73  ? 1106 TYR A CD2   1 
ATOM   8958  C CE1   . TYR B 2 1109 ? 131.447 157.273 85.395  1.00 44.73  ? 1106 TYR A CE1   1 
ATOM   8959  C CE2   . TYR B 2 1109 ? 130.058 157.893 83.556  1.00 44.73  ? 1106 TYR A CE2   1 
ATOM   8960  C CZ    . TYR B 2 1109 ? 131.062 158.194 84.448  1.00 44.73  ? 1106 TYR A CZ    1 
ATOM   8961  O OH    . TYR B 2 1109 ? 131.685 159.419 84.393  1.00 44.73  ? 1106 TYR A OH    1 
ATOM   8962  N N     . ASP B 2 1110 ? 127.005 156.161 86.639  1.00 46.91  ? 1107 ASP A N     1 
ATOM   8963  C CA    . ASP B 2 1110 ? 126.101 157.307 86.587  1.00 46.91  ? 1107 ASP A CA    1 
ATOM   8964  C C     . ASP B 2 1110 ? 126.855 158.460 85.939  1.00 46.91  ? 1107 ASP A C     1 
ATOM   8965  O O     . ASP B 2 1110 ? 127.750 159.052 86.546  1.00 46.91  ? 1107 ASP A O     1 
ATOM   8966  C CB    . ASP B 2 1110 ? 125.608 157.670 87.982  1.00 46.91  ? 1107 ASP A CB    1 
ATOM   8967  C CG    . ASP B 2 1110 ? 124.263 158.370 87.962  1.00 46.91  ? 1107 ASP A CG    1 
ATOM   8968  O OD1   . ASP B 2 1110 ? 123.635 158.424 86.883  1.00 46.91  ? 1107 ASP A OD1   1 
ATOM   8969  O OD2   . ASP B 2 1110 ? 123.832 158.865 89.025  1.00 46.91  ? 1107 ASP A OD2   1 
ATOM   8970  N N     . VAL B 2 1111 ? 126.497 158.780 84.694  1.00 45.07  ? 1108 VAL A N     1 
ATOM   8971  C CA    . VAL B 2 1111 ? 127.210 159.825 83.966  1.00 45.07  ? 1108 VAL A CA    1 
ATOM   8972  C C     . VAL B 2 1111 ? 126.971 161.191 84.597  1.00 45.07  ? 1108 VAL A C     1 
ATOM   8973  O O     . VAL B 2 1111 ? 127.835 162.074 84.528  1.00 45.07  ? 1108 VAL A O     1 
ATOM   8974  C CB    . VAL B 2 1111 ? 126.812 159.799 82.477  1.00 45.07  ? 1108 VAL A CB    1 
ATOM   8975  C CG1   . VAL B 2 1111 ? 125.341 160.151 82.301  1.00 45.07  ? 1108 VAL A CG1   1 
ATOM   8976  C CG2   . VAL B 2 1111 ? 127.699 160.735 81.665  1.00 45.07  ? 1108 VAL A CG2   1 
ATOM   8977  N N     . LYS B 2 1112 ? 125.810 161.392 85.224  1.00 46.55  ? 1109 LYS A N     1 
ATOM   8978  C CA    . LYS B 2 1112 ? 125.502 162.690 85.815  1.00 46.55  ? 1109 LYS A CA    1 
ATOM   8979  C C     . LYS B 2 1112 ? 126.433 163.013 86.978  1.00 46.55  ? 1109 LYS A C     1 
ATOM   8980  O O     . LYS B 2 1112 ? 126.888 164.154 87.120  1.00 46.55  ? 1109 LYS A O     1 
ATOM   8981  C CB    . LYS B 2 1112 ? 124.043 162.723 86.270  1.00 46.54  ? 1109 LYS A CB    1 
ATOM   8982  C CG    . LYS B 2 1112 ? 123.576 164.085 86.757  1.00 46.54  ? 1109 LYS A CG    1 
ATOM   8983  C CD    . LYS B 2 1112 ? 122.115 164.051 87.169  1.00 46.54  ? 1109 LYS A CD    1 
ATOM   8984  C CE    . LYS B 2 1112 ? 121.205 163.910 85.959  1.00 46.54  ? 1109 LYS A CE    1 
ATOM   8985  N NZ    . LYS B 2 1112 ? 121.259 165.110 85.080  1.00 46.54  ? 1109 LYS A NZ    1 
ATOM   8986  N N     . THR B 2 1113 ? 126.730 162.023 87.821  1.00 44.73  ? 1110 THR A N     1 
ATOM   8987  C CA    . THR B 2 1113 ? 127.527 162.244 89.019  1.00 44.73  ? 1110 THR A CA    1 
ATOM   8988  C C     . THR B 2 1113 ? 128.923 161.641 88.942  1.00 44.73  ? 1110 THR A C     1 
ATOM   8989  O O     . THR B 2 1113 ? 129.781 162.007 89.752  1.00 44.73  ? 1110 THR A O     1 
ATOM   8990  C CB    . THR B 2 1113 ? 126.807 161.675 90.247  1.00 44.73  ? 1110 THR A CB    1 
ATOM   8991  O OG1   . THR B 2 1113 ? 126.773 160.245 90.163  1.00 44.73  ? 1110 THR A OG1   1 
ATOM   8992  C CG2   . THR B 2 1113 ? 125.384 162.207 90.323  1.00 44.73  ? 1110 THR A CG2   1 
ATOM   8993  N N     . GLY B 2 1114 ? 129.174 160.736 88.000  1.00 44.73  ? 1111 GLY A N     1 
ATOM   8994  C CA    . GLY B 2 1114 ? 130.474 160.108 87.895  1.00 44.73  ? 1111 GLY A CA    1 
ATOM   8995  C C     . GLY B 2 1114 ? 130.747 159.017 88.903  1.00 44.73  ? 1111 GLY A C     1 
ATOM   8996  O O     . GLY B 2 1114 ? 131.902 158.599 89.041  1.00 44.73  ? 1111 GLY A O     1 
ATOM   8997  N N     . ASP B 2 1115 ? 129.729 158.542 89.611  1.00 44.73  ? 1112 ASP A N     1 
ATOM   8998  C CA    . ASP B 2 1115 ? 129.884 157.496 90.609  1.00 44.73  ? 1112 ASP A CA    1 
ATOM   8999  C C     . ASP B 2 1115 ? 129.484 156.144 90.032  1.00 44.73  ? 1112 ASP A C     1 
ATOM   9000  O O     . ASP B 2 1115 ? 128.879 156.046 88.962  1.00 44.73  ? 1112 ASP A O     1 
ATOM   9001  C CB    . ASP B 2 1115 ? 129.040 157.808 91.850  1.00 44.73  ? 1112 ASP A CB    1 
ATOM   9002  C CG    . ASP B 2 1115 ? 129.532 159.028 92.600  1.00 44.73  ? 1112 ASP A CG    1 
ATOM   9003  O OD1   . ASP B 2 1115 ? 130.747 159.306 92.552  1.00 44.73  ? 1112 ASP A OD1   1 
ATOM   9004  O OD2   . ASP B 2 1115 ? 128.703 159.709 93.239  1.00 44.73  ? 1112 ASP A OD2   1 
ATOM   9005  N N     . PHE B 2 1116 ? 129.833 155.088 90.762  1.00 44.73  ? 1113 PHE A N     1 
ATOM   9006  C CA    . PHE B 2 1116 ? 129.373 153.738 90.463  1.00 44.73  ? 1113 PHE A CA    1 
ATOM   9007  C C     . PHE B 2 1116 ? 128.398 153.335 91.557  1.00 44.73  ? 1113 PHE A C     1 
ATOM   9008  O O     . PHE B 2 1116 ? 128.721 153.441 92.745  1.00 44.73  ? 1113 PHE A O     1 
ATOM   9009  C CB    . PHE B 2 1116 ? 130.522 152.727 90.404  1.00 44.73  ? 1113 PHE A CB    1 
ATOM   9010  C CG    . PHE B 2 1116 ? 131.375 152.820 89.170  1.00 44.73  ? 1113 PHE A CG    1 
ATOM   9011  C CD1   . PHE B 2 1116 ? 131.549 154.015 88.502  1.00 44.73  ? 1113 PHE A CD1   1 
ATOM   9012  C CD2   . PHE B 2 1116 ? 132.059 151.708 88.716  1.00 44.73  ? 1113 PHE A CD2   1 
ATOM   9013  C CE1   . PHE B 2 1116 ? 132.358 154.085 87.389  1.00 44.73  ? 1113 PHE A CE1   1 
ATOM   9014  C CE2   . PHE B 2 1116 ? 132.857 151.775 87.595  1.00 44.73  ? 1113 PHE A CE2   1 
ATOM   9015  C CZ    . PHE B 2 1116 ? 133.008 152.966 86.933  1.00 44.73  ? 1113 PHE A CZ    1 
ATOM   9016  N N     . ILE B 2 1117 ? 127.218 152.873 91.166  1.00 44.73  ? 1114 ILE A N     1 
ATOM   9017  C CA    . ILE B 2 1117 ? 126.217 152.398 92.112  1.00 44.73  ? 1114 ILE A CA    1 
ATOM   9018  C C     . ILE B 2 1117 ? 126.170 150.881 92.000  1.00 44.73  ? 1114 ILE A C     1 
ATOM   9019  O O     . ILE B 2 1117 ? 125.762 150.335 90.970  1.00 44.73  ? 1114 ILE A O     1 
ATOM   9020  C CB    . ILE B 2 1117 ? 124.844 153.029 91.847  1.00 44.73  ? 1114 ILE A CB    1 
ATOM   9021  C CG1   . ILE B 2 1117 ? 124.859 154.507 92.242  1.00 44.73  ? 1114 ILE A CG1   1 
ATOM   9022  C CG2   . ILE B 2 1117 ? 123.759 152.284 92.611  1.00 44.73  ? 1114 ILE A CG2   1 
ATOM   9023  C CD1   . ILE B 2 1117 ? 123.505 155.177 92.161  1.00 44.73  ? 1114 ILE A CD1   1 
ATOM   9024  N N     . LEU B 2 1118 ? 126.595 150.196 93.059  1.00 44.73  ? 1115 LEU A N     1 
ATOM   9025  C CA    . LEU B 2 1118 ? 126.613 148.735 93.101  1.00 44.73  ? 1115 LEU A CA    1 
ATOM   9026  C C     . LEU B 2 1118 ? 125.479 148.295 94.019  1.00 44.73  ? 1115 LEU A C     1 
ATOM   9027  O O     . LEU B 2 1118 ? 125.630 148.229 95.239  1.00 44.73  ? 1115 LEU A O     1 
ATOM   9028  C CB    . LEU B 2 1118 ? 127.967 148.220 93.574  1.00 44.73  ? 1115 LEU A CB    1 
ATOM   9029  C CG    . LEU B 2 1118 ? 128.083 146.719 93.842  1.00 44.73  ? 1115 LEU A CG    1 
ATOM   9030  C CD1   . LEU B 2 1118 ? 127.719 145.919 92.604  1.00 44.73  ? 1115 LEU A CD1   1 
ATOM   9031  C CD2   . LEU B 2 1118 ? 129.483 146.368 94.318  1.00 44.73  ? 1115 LEU A CD2   1 
ATOM   9032  N N     . HIS B 2 1119 ? 124.330 148.001 93.421  1.00 44.73  ? 1116 HIS A N     1 
ATOM   9033  C CA    . HIS B 2 1119 ? 123.169 147.592 94.196  1.00 44.73  ? 1116 HIS A CA    1 
ATOM   9034  C C     . HIS B 2 1119 ? 123.376 146.196 94.764  1.00 44.73  ? 1116 HIS A C     1 
ATOM   9035  O O     . HIS B 2 1119 ? 123.968 145.327 94.120  1.00 44.73  ? 1116 HIS A O     1 
ATOM   9036  C CB    . HIS B 2 1119 ? 121.914 147.626 93.329  1.00 44.73  ? 1116 HIS A CB    1 
ATOM   9037  C CG    . HIS B 2 1119 ? 120.640 147.633 94.111  1.00 44.73  ? 1116 HIS A CG    1 
ATOM   9038  N ND1   . HIS B 2 1119 ? 119.858 148.759 94.247  1.00 44.73  ? 1116 HIS A ND1   1 
ATOM   9039  C CD2   . HIS B 2 1119 ? 120.009 146.652 94.798  1.00 44.73  ? 1116 HIS A CD2   1 
ATOM   9040  C CE1   . HIS B 2 1119 ? 118.801 148.472 94.985  1.00 44.73  ? 1116 HIS A CE1   1 
ATOM   9041  N NE2   . HIS B 2 1119 ? 118.868 147.200 95.332  1.00 44.73  ? 1116 HIS A NE2   1 
ATOM   9042  N N     . PHE B 2 1120 ? 122.884 145.984 95.980  1.00 44.73  ? 1117 PHE A N     1 
ATOM   9043  C CA    . PHE B 2 1120 ? 123.007 144.694 96.638  1.00 44.73  ? 1117 PHE A CA    1 
ATOM   9044  C C     . PHE B 2 1120 ? 121.768 144.418 97.472  1.00 44.73  ? 1117 PHE A C     1 
ATOM   9045  O O     . PHE B 2 1120 ? 121.275 145.301 98.179  1.00 44.73  ? 1117 PHE A O     1 
ATOM   9046  C CB    . PHE B 2 1120 ? 124.248 144.636 97.530  1.00 44.73  ? 1117 PHE A CB    1 
ATOM   9047  C CG    . PHE B 2 1120 ? 124.406 143.335 98.250  1.00 44.73  ? 1117 PHE A CG    1 
ATOM   9048  C CD1   . PHE B 2 1120 ? 124.400 142.141 97.553  1.00 44.73  ? 1117 PHE A CD1   1 
ATOM   9049  C CD2   . PHE B 2 1120 ? 124.550 143.302 99.624  1.00 44.73  ? 1117 PHE A CD2   1 
ATOM   9050  C CE1   . PHE B 2 1120 ? 124.543 140.939 98.212  1.00 44.73  ? 1117 PHE A CE1   1 
ATOM   9051  C CE2   . PHE B 2 1120 ? 124.691 142.103 100.289 1.00 44.73  ? 1117 PHE A CE2   1 
ATOM   9052  C CZ    . PHE B 2 1120 ? 124.687 140.919 99.581  1.00 44.73  ? 1117 PHE A CZ    1 
ATOM   9053  N N     . LYS B 2 1121 ? 121.273 143.188 97.385  1.00 44.73  ? 1118 LYS A N     1 
ATOM   9054  C CA    . LYS B 2 1121 ? 120.187 142.707 98.227  1.00 44.73  ? 1118 LYS A CA    1 
ATOM   9055  C C     . LYS B 2 1121 ? 120.759 141.717 99.229  1.00 44.73  ? 1118 LYS A C     1 
ATOM   9056  O O     . LYS B 2 1121 ? 121.477 140.787 98.847  1.00 44.73  ? 1118 LYS A O     1 
ATOM   9057  C CB    . LYS B 2 1121 ? 119.090 142.048 97.391  1.00 44.73  ? 1118 LYS A CB    1 
ATOM   9058  C CG    . LYS B 2 1121 ? 118.658 142.856 96.183  1.00 44.73  ? 1118 LYS A CG    1 
ATOM   9059  C CD    . LYS B 2 1121 ? 117.928 144.119 96.597  1.00 44.73  ? 1118 LYS A CD    1 
ATOM   9060  C CE    . LYS B 2 1121 ? 116.662 144.311 95.781  1.00 44.73  ? 1118 LYS A CE    1 
ATOM   9061  N NZ    . LYS B 2 1121 ? 116.908 144.115 94.325  1.00 44.73  ? 1118 LYS A NZ    1 
ATOM   9062  N N     . MET B 2 1122 ? 120.439 141.913 100.509 1.00 44.73  ? 1119 MET A N     1 
ATOM   9063  C CA    . MET B 2 1122 ? 121.040 141.093 101.553 1.00 44.73  ? 1119 MET A CA    1 
ATOM   9064  C C     . MET B 2 1122 ? 120.589 139.641 101.505 1.00 44.73  ? 1119 MET A C     1 
ATOM   9065  O O     . MET B 2 1122 ? 121.187 138.806 102.191 1.00 44.73  ? 1119 MET A O     1 
ATOM   9066  C CB    . MET B 2 1122 ? 120.746 141.688 102.928 1.00 44.73  ? 1119 MET A CB    1 
ATOM   9067  C CG    . MET B 2 1122 ? 121.260 143.104 103.092 1.00 44.73  ? 1119 MET A CG    1 
ATOM   9068  S SD    . MET B 2 1122 ? 122.992 143.132 103.582 1.00 44.73  ? 1119 MET A SD    1 
ATOM   9069  C CE    . MET B 2 1122 ? 122.867 143.784 105.240 1.00 44.73  ? 1119 MET A CE    1 
ATOM   9070  N N     . ASN B 2 1123 ? 119.564 139.316 100.719 1.00 44.73  ? 1120 ASN A N     1 
ATOM   9071  C CA    . ASN B 2 1123 ? 119.176 137.929 100.510 1.00 44.73  ? 1120 ASN A CA    1 
ATOM   9072  C C     . ASN B 2 1123 ? 120.043 137.231 99.469  1.00 44.73  ? 1120 ASN A C     1 
ATOM   9073  O O     . ASN B 2 1123 ? 119.660 136.168 98.966  1.00 44.73  ? 1120 ASN A O     1 
ATOM   9074  C CB    . ASN B 2 1123 ? 117.699 137.846 100.115 1.00 44.73  ? 1120 ASN A CB    1 
ATOM   9075  C CG    . ASN B 2 1123 ? 117.333 138.810 99.005  1.00 44.73  ? 1120 ASN A CG    1 
ATOM   9076  O OD1   . ASN B 2 1123 ? 118.118 139.050 98.088  1.00 44.73  ? 1120 ASN A OD1   1 
ATOM   9077  N ND2   . ASN B 2 1123 ? 116.132 139.370 99.082  1.00 44.73  ? 1120 ASN A ND2   1 
ATOM   9078  N N     . ARG B 2 1124 ? 121.200 137.806 99.149  1.00 44.73  ? 1121 ARG A N     1 
ATOM   9079  C CA    . ARG B 2 1124 ? 122.154 137.225 98.218  1.00 44.73  ? 1121 ARG A CA    1 
ATOM   9080  C C     . ARG B 2 1124 ? 123.517 137.139 98.890  1.00 44.73  ? 1121 ARG A C     1 
ATOM   9081  O O     . ARG B 2 1124 ? 123.801 137.852 99.856  1.00 44.73  ? 1121 ARG A O     1 
ATOM   9082  C CB    . ARG B 2 1124 ? 122.261 138.046 96.926  1.00 44.73  ? 1121 ARG A CB    1 
ATOM   9083  C CG    . ARG B 2 1124 ? 120.928 138.459 96.326  1.00 44.73  ? 1121 ARG A CG    1 
ATOM   9084  C CD    . ARG B 2 1124 ? 120.067 137.247 95.995  1.00 44.73  ? 1121 ARG A CD    1 
ATOM   9085  N NE    . ARG B 2 1124 ? 120.447 136.592 94.747  1.00 44.73  ? 1121 ARG A NE    1 
ATOM   9086  C CZ    . ARG B 2 1124 ? 120.450 137.167 93.551  1.00 44.73  ? 1121 ARG A CZ    1 
ATOM   9087  N NH1   . ARG B 2 1124 ? 120.037 138.412 93.375  1.00 44.73  ? 1121 ARG A NH1   1 
ATOM   9088  N NH2   . ARG B 2 1124 ? 120.864 136.467 92.498  1.00 44.73  ? 1121 ARG A NH2   1 
ATOM   9089  N N     . ASN B 2 1125 ? 124.359 136.250 98.361  1.00 44.73  ? 1122 ASN A N     1 
ATOM   9090  C CA    . ASN B 2 1125 ? 125.708 136.024 98.884  1.00 44.73  ? 1122 ASN A CA    1 
ATOM   9091  C C     . ASN B 2 1125 ? 125.681 135.663 100.368 1.00 44.73  ? 1122 ASN A C     1 
ATOM   9092  O O     . ASN B 2 1125 ? 126.479 136.165 101.161 1.00 44.73  ? 1122 ASN A O     1 
ATOM   9093  C CB    . ASN B 2 1125 ? 126.608 137.236 98.639  1.00 44.73  ? 1122 ASN A CB    1 
ATOM   9094  C CG    . ASN B 2 1125 ? 127.074 137.334 97.203  1.00 44.73  ? 1122 ASN A CG    1 
ATOM   9095  O OD1   . ASN B 2 1125 ? 127.459 136.337 96.595  1.00 44.73  ? 1122 ASN A OD1   1 
ATOM   9096  N ND2   . ASN B 2 1125 ? 127.044 138.542 96.652  1.00 44.73  ? 1122 ASN A ND2   1 
ATOM   9097  N N     . LEU B 2 1126 ? 124.752 134.781 100.747 1.00 44.73  ? 1123 LEU A N     1 
ATOM   9098  C CA    . LEU B 2 1126 ? 124.663 134.353 102.139 1.00 44.73  ? 1123 LEU A CA    1 
ATOM   9099  C C     . LEU B 2 1126 ? 125.905 133.590 102.577 1.00 44.73  ? 1123 LEU A C     1 
ATOM   9100  O O     . LEU B 2 1126 ? 126.369 133.762 103.710 1.00 44.73  ? 1123 LEU A O     1 
ATOM   9101  C CB    . LEU B 2 1126 ? 123.419 133.491 102.359 1.00 44.73  ? 1123 LEU A CB    1 
ATOM   9102  C CG    . LEU B 2 1126 ? 122.067 134.169 102.603 1.00 44.73  ? 1123 LEU A CG    1 
ATOM   9103  C CD1   . LEU B 2 1126 ? 122.057 134.863 103.958 1.00 44.73  ? 1123 LEU A CD1   1 
ATOM   9104  C CD2   . LEU B 2 1126 ? 121.704 135.142 101.499 1.00 44.73  ? 1123 LEU A CD2   1 
ATOM   9105  N N     . SER B 2 1127 ? 126.452 132.742 101.704 1.00 44.73  ? 1124 SER A N     1 
ATOM   9106  C CA    . SER B 2 1127 ? 127.625 131.957 102.071 1.00 44.73  ? 1124 SER A CA    1 
ATOM   9107  C C     . SER B 2 1127 ? 128.833 132.841 102.345 1.00 44.73  ? 1124 SER A C     1 
ATOM   9108  O O     . SER B 2 1127 ? 129.734 132.443 103.092 1.00 44.73  ? 1124 SER A O     1 
ATOM   9109  C CB    . SER B 2 1127 ? 127.947 130.947 100.969 1.00 44.73  ? 1124 SER A CB    1 
ATOM   9110  O OG    . SER B 2 1127 ? 127.861 131.545 99.688  1.00 44.73  ? 1124 SER A OG    1 
ATOM   9111  N N     . PHE B 2 1128 ? 128.873 134.035 101.757 1.00 44.73  ? 1125 PHE A N     1 
ATOM   9112  C CA    . PHE B 2 1128 ? 129.963 134.975 101.967 1.00 44.73  ? 1125 PHE A CA    1 
ATOM   9113  C C     . PHE B 2 1128 ? 129.637 136.020 103.026 1.00 44.73  ? 1125 PHE A C     1 
ATOM   9114  O O     . PHE B 2 1128 ? 130.430 136.942 103.235 1.00 44.73  ? 1125 PHE A O     1 
ATOM   9115  C CB    . PHE B 2 1128 ? 130.335 135.673 100.655 1.00 44.73  ? 1125 PHE A CB    1 
ATOM   9116  C CG    . PHE B 2 1128 ? 130.733 134.735 99.551  1.00 44.73  ? 1125 PHE A CG    1 
ATOM   9117  C CD1   . PHE B 2 1128 ? 129.789 133.962 98.896  1.00 44.73  ? 1125 PHE A CD1   1 
ATOM   9118  C CD2   . PHE B 2 1128 ? 132.057 134.621 99.173  1.00 44.73  ? 1125 PHE A CD2   1 
ATOM   9119  C CE1   . PHE B 2 1128 ? 130.158 133.101 97.885  1.00 44.73  ? 1125 PHE A CE1   1 
ATOM   9120  C CE2   . PHE B 2 1128 ? 132.432 133.760 98.162  1.00 44.73  ? 1125 PHE A CE2   1 
ATOM   9121  C CZ    . PHE B 2 1128 ? 131.482 133.000 97.517  1.00 44.73  ? 1125 PHE A CZ    1 
ATOM   9122  N N     . GLN B 2 1129 ? 128.497 135.900 103.692 1.00 44.73  ? 1126 GLN A N     1 
ATOM   9123  C CA    . GLN B 2 1129 ? 128.062 136.891 104.662 1.00 44.73  ? 1126 GLN A CA    1 
ATOM   9124  C C     . GLN B 2 1129 ? 128.363 136.434 106.084 1.00 44.73  ? 1126 GLN A C     1 
ATOM   9125  O O     . GLN B 2 1129 ? 128.804 135.310 106.333 1.00 44.73  ? 1126 GLN A O     1 
ATOM   9126  C CB    . GLN B 2 1129 ? 126.568 137.180 104.501 1.00 44.73  ? 1126 GLN A CB    1 
ATOM   9127  C CG    . GLN B 2 1129 ? 126.265 138.315 103.545 1.00 44.73  ? 1126 GLN A CG    1 
ATOM   9128  C CD    . GLN B 2 1129 ? 124.786 138.614 103.454 1.00 44.73  ? 1126 GLN A CD    1 
ATOM   9129  O OE1   . GLN B 2 1129 ? 124.015 138.260 104.344 1.00 44.73  ? 1126 GLN A OE1   1 
ATOM   9130  N NE2   . GLN B 2 1129 ? 124.381 139.271 102.375 1.00 44.73  ? 1126 GLN A NE2   1 
ATOM   9131  N N     . ARG B 2 1130 ? 128.113 137.339 107.024 1.00 44.73  ? 1127 ARG A N     1 
ATOM   9132  C CA    . ARG B 2 1130 ? 128.414 137.144 108.433 1.00 44.73  ? 1127 ARG A CA    1 
ATOM   9133  C C     . ARG B 2 1130 ? 127.194 136.766 109.260 1.00 44.73  ? 1127 ARG A C     1 
ATOM   9134  O O     . ARG B 2 1130 ? 127.302 136.658 110.485 1.00 44.73  ? 1127 ARG A O     1 
ATOM   9135  C CB    . ARG B 2 1130 ? 129.065 138.413 108.985 1.00 44.73  ? 1127 ARG A CB    1 
ATOM   9136  C CG    . ARG B 2 1130 ? 128.247 139.669 108.733 1.00 44.73  ? 1127 ARG A CG    1 
ATOM   9137  C CD    . ARG B 2 1130 ? 128.907 140.947 109.254 1.00 44.73  ? 1127 ARG A CD    1 
ATOM   9138  N NE    . ARG B 2 1130 ? 130.293 141.116 108.825 1.00 44.73  ? 1127 ARG A NE    1 
ATOM   9139  C CZ    . ARG B 2 1130 ? 131.357 140.666 109.480 1.00 44.73  ? 1127 ARG A CZ    1 
ATOM   9140  N NH1   . ARG B 2 1130 ? 131.244 140.040 110.640 1.00 44.73  ? 1127 ARG A NH1   1 
ATOM   9141  N NH2   . ARG B 2 1130 ? 132.566 140.856 108.961 1.00 44.73  ? 1127 ARG A NH2   1 
ATOM   9142  N N     . GLY B 2 1131 ? 126.043 136.559 108.626 1.00 44.73  ? 1128 GLY A N     1 
ATOM   9143  C CA    . GLY B 2 1131 ? 124.865 136.111 109.341 1.00 44.73  ? 1128 GLY A CA    1 
ATOM   9144  C C     . GLY B 2 1131 ? 124.167 137.165 110.166 1.00 44.73  ? 1128 GLY A C     1 
ATOM   9145  O O     . GLY B 2 1131 ? 123.432 136.821 111.094 1.00 44.73  ? 1128 GLY A O     1 
ATOM   9146  N N     . LEU B 2 1132 ? 124.377 138.443 109.861 1.00 44.73  ? 1129 LEU A N     1 
ATOM   9147  C CA    . LEU B 2 1132 ? 123.720 139.549 110.557 1.00 44.73  ? 1129 LEU A CA    1 
ATOM   9148  C C     . LEU B 2 1132 ? 123.070 140.452 109.520 1.00 44.73  ? 1129 LEU A C     1 
ATOM   9149  O O     . LEU B 2 1132 ? 123.668 141.442 109.075 1.00 44.73  ? 1129 LEU A O     1 
ATOM   9150  C CB    . LEU B 2 1132 ? 124.706 140.326 111.430 1.00 44.73  ? 1129 LEU A CB    1 
ATOM   9151  C CG    . LEU B 2 1132 ? 125.599 139.490 112.346 1.00 44.73  ? 1129 LEU A CG    1 
ATOM   9152  C CD1   . LEU B 2 1132 ? 126.771 140.314 112.830 1.00 44.73  ? 1129 LEU A CD1   1 
ATOM   9153  C CD2   . LEU B 2 1132 ? 124.801 138.942 113.519 1.00 44.73  ? 1129 LEU A CD2   1 
ATOM   9154  N N     . PRO B 2 1133 ? 121.847 140.137 109.104 1.00 44.73  ? 1130 PRO A N     1 
ATOM   9155  C CA    . PRO B 2 1133 ? 121.181 140.957 108.085 1.00 44.73  ? 1130 PRO A CA    1 
ATOM   9156  C C     . PRO B 2 1133 ? 120.845 142.355 108.578 1.00 44.73  ? 1130 PRO A C     1 
ATOM   9157  O O     . PRO B 2 1133 ? 121.150 143.346 107.907 1.00 44.73  ? 1130 PRO A O     1 
ATOM   9158  C CB    . PRO B 2 1133 ? 119.915 140.154 107.763 1.00 44.73  ? 1130 PRO A CB    1 
ATOM   9159  C CG    . PRO B 2 1133 ? 119.658 139.344 108.985 1.00 44.73  ? 1130 PRO A CG    1 
ATOM   9160  C CD    . PRO B 2 1133 ? 121.001 139.026 109.572 1.00 44.73  ? 1130 PRO A CD    1 
ATOM   9161  N N     . GLY B 2 1134 ? 120.216 142.450 109.746 1.00 44.73  ? 1131 GLY A N     1 
ATOM   9162  C CA    . GLY B 2 1134 ? 119.815 143.751 110.230 1.00 44.73  ? 1131 GLY A CA    1 
ATOM   9163  C C     . GLY B 2 1134 ? 118.678 144.327 109.399 1.00 44.73  ? 1131 GLY A C     1 
ATOM   9164  O O     . GLY B 2 1134 ? 117.994 143.632 108.644 1.00 44.73  ? 1131 GLY A O     1 
ATOM   9165  N N     . PHE B 2 1135 ? 118.484 145.633 109.554 1.00 44.73  ? 1132 PHE A N     1 
ATOM   9166  C CA    . PHE B 2 1135 ? 117.495 146.362 108.779 1.00 44.73  ? 1132 PHE A CA    1 
ATOM   9167  C C     . PHE B 2 1135 ? 118.066 146.682 107.397 1.00 44.73  ? 1132 PHE A C     1 
ATOM   9168  O O     . PHE B 2 1135 ? 119.181 146.280 107.051 1.00 44.73  ? 1132 PHE A O     1 
ATOM   9169  C CB    . PHE B 2 1135 ? 117.076 147.625 109.528 1.00 44.73  ? 1132 PHE A CB    1 
ATOM   9170  C CG    . PHE B 2 1135 ? 115.639 148.009 109.322 1.00 44.73  ? 1132 PHE A CG    1 
ATOM   9171  C CD1   . PHE B 2 1135 ? 114.633 147.377 110.031 1.00 44.73  ? 1132 PHE A CD1   1 
ATOM   9172  C CD2   . PHE B 2 1135 ? 115.296 149.019 108.439 1.00 44.73  ? 1132 PHE A CD2   1 
ATOM   9173  C CE1   . PHE B 2 1135 ? 113.310 147.731 109.850 1.00 44.73  ? 1132 PHE A CE1   1 
ATOM   9174  C CE2   . PHE B 2 1135 ? 113.975 149.379 108.254 1.00 44.73  ? 1132 PHE A CE2   1 
ATOM   9175  C CZ    . PHE B 2 1135 ? 112.981 148.734 108.960 1.00 44.73  ? 1132 PHE A CZ    1 
ATOM   9176  N N     . MET B 2 1136 ? 117.295 147.425 106.596 1.00 44.73  ? 1133 MET A N     1 
ATOM   9177  C CA    . MET B 2 1136 ? 117.682 147.793 105.237 1.00 44.73  ? 1133 MET A CA    1 
ATOM   9178  C C     . MET B 2 1136 ? 118.057 146.572 104.406 1.00 44.73  ? 1133 MET A C     1 
ATOM   9179  O O     . MET B 2 1136 ? 119.247 146.305 104.197 1.00 44.73  ? 1133 MET A O     1 
ATOM   9180  C CB    . MET B 2 1136 ? 118.837 148.795 105.241 1.00 44.73  ? 1133 MET A CB    1 
ATOM   9181  C CG    . MET B 2 1136 ? 118.617 150.004 106.123 1.00 44.73  ? 1133 MET A CG    1 
ATOM   9182  S SD    . MET B 2 1136 ? 117.945 151.381 105.171 1.00 44.73  ? 1133 MET A SD    1 
ATOM   9183  C CE    . MET B 2 1136 ? 119.446 152.232 104.690 1.00 44.73  ? 1133 MET A CE    1 
ATOM   9184  N N     . PRO B 2 1137 ? 117.075 145.800 103.933 1.00 44.73  ? 1134 PRO A N     1 
ATOM   9185  C CA    . PRO B 2 1137 ? 117.392 144.604 103.134 1.00 44.73  ? 1134 PRO A CA    1 
ATOM   9186  C C     . PRO B 2 1137 ? 118.166 144.895 101.856 1.00 44.73  ? 1134 PRO A C     1 
ATOM   9187  O O     . PRO B 2 1137 ? 118.705 143.954 101.260 1.00 44.73  ? 1134 PRO A O     1 
ATOM   9188  C CB    . PRO B 2 1137 ? 116.009 144.019 102.820 1.00 44.73  ? 1134 PRO A CB    1 
ATOM   9189  C CG    . PRO B 2 1137 ? 115.088 145.191 102.884 1.00 44.73  ? 1134 PRO A CG    1 
ATOM   9190  C CD    . PRO B 2 1137 ? 115.628 146.068 103.978 1.00 44.73  ? 1134 PRO A CD    1 
ATOM   9191  N N     . ALA B 2 1138 ? 118.237 146.148 101.415 1.00 44.73  ? 1135 ALA A N     1 
ATOM   9192  C CA    . ALA B 2 1138 ? 118.999 146.515 100.233 1.00 44.73  ? 1135 ALA A CA    1 
ATOM   9193  C C     . ALA B 2 1138 ? 119.939 147.665 100.561 1.00 44.73  ? 1135 ALA A C     1 
ATOM   9194  O O     . ALA B 2 1138 ? 119.640 148.510 101.409 1.00 44.73  ? 1135 ALA A O     1 
ATOM   9195  C CB    . ALA B 2 1138 ? 118.080 146.910 99.070  1.00 44.73  ? 1135 ALA A CB    1 
ATOM   9196  N N     . TRP B 2 1139 ? 121.081 147.688 99.879  1.00 44.73  ? 1136 TRP A N     1 
ATOM   9197  C CA    . TRP B 2 1139 ? 122.066 148.746 100.040 1.00 44.73  ? 1136 TRP A CA    1 
ATOM   9198  C C     . TRP B 2 1139 ? 122.543 149.202 98.670  1.00 44.73  ? 1136 TRP A C     1 
ATOM   9199  O O     . TRP B 2 1139 ? 122.421 148.484 97.675  1.00 44.73  ? 1136 TRP A O     1 
ATOM   9200  C CB    . TRP B 2 1139 ? 123.265 148.294 100.884 1.00 44.73  ? 1136 TRP A CB    1 
ATOM   9201  C CG    . TRP B 2 1139 ? 122.943 148.012 102.316 1.00 44.73  ? 1136 TRP A CG    1 
ATOM   9202  C CD1   . TRP B 2 1139 ? 122.728 146.792 102.882 1.00 44.73  ? 1136 TRP A CD1   1 
ATOM   9203  C CD2   . TRP B 2 1139 ? 122.812 148.972 103.370 1.00 44.73  ? 1136 TRP A CD2   1 
ATOM   9204  N NE1   . TRP B 2 1139 ? 122.466 146.932 104.223 1.00 44.73  ? 1136 TRP A NE1   1 
ATOM   9205  C CE2   . TRP B 2 1139 ? 122.513 148.261 104.547 1.00 44.73  ? 1136 TRP A CE2   1 
ATOM   9206  C CE3   . TRP B 2 1139 ? 122.917 150.363 103.432 1.00 44.73  ? 1136 TRP A CE3   1 
ATOM   9207  C CZ2   . TRP B 2 1139 ? 122.317 148.894 105.770 1.00 44.73  ? 1136 TRP A CZ2   1 
ATOM   9208  C CZ3   . TRP B 2 1139 ? 122.724 150.989 104.647 1.00 44.73  ? 1136 TRP A CZ3   1 
ATOM   9209  C CH2   . TRP B 2 1139 ? 122.425 150.256 105.799 1.00 44.73  ? 1136 TRP A CH2   1 
ATOM   9210  N N     . ASP B 2 1140 ? 123.089 150.417 98.628  1.00 44.73  ? 1137 ASP A N     1 
ATOM   9211  C CA    . ASP B 2 1140 ? 123.606 151.016 97.398  1.00 44.73  ? 1137 ASP A CA    1 
ATOM   9212  C C     . ASP B 2 1140 ? 125.063 151.404 97.634  1.00 44.73  ? 1137 ASP A C     1 
ATOM   9213  O O     . ASP B 2 1140 ? 125.355 152.537 98.024  1.00 44.73  ? 1137 ASP A O     1 
ATOM   9214  C CB    . ASP B 2 1140 ? 122.764 152.217 96.981  1.00 44.73  ? 1137 ASP A CB    1 
ATOM   9215  C CG    . ASP B 2 1140 ? 121.376 151.823 96.520  1.00 44.73  ? 1137 ASP A CG    1 
ATOM   9216  O OD1   . ASP B 2 1140 ? 121.218 150.700 95.999  1.00 44.73  ? 1137 ASP A OD1   1 
ATOM   9217  O OD2   . ASP B 2 1140 ? 120.442 152.637 96.679  1.00 44.73  ? 1137 ASP A OD2   1 
ATOM   9218  N N     . ILE B 2 1141 ? 125.975 150.462 97.395  1.00 44.73  ? 1138 ILE A N     1 
ATOM   9219  C CA    . ILE B 2 1141 ? 127.398 150.752 97.516  1.00 44.73  ? 1138 ILE A CA    1 
ATOM   9220  C C     . ILE B 2 1141 ? 127.799 151.726 96.419  1.00 44.73  ? 1138 ILE A C     1 
ATOM   9221  O O     . ILE B 2 1141 ? 127.510 151.506 95.236  1.00 44.73  ? 1138 ILE A O     1 
ATOM   9222  C CB    . ILE B 2 1141 ? 128.223 149.460 97.444  1.00 44.73  ? 1138 ILE A CB    1 
ATOM   9223  C CG1   . ILE B 2 1141 ? 127.559 148.351 98.261  1.00 44.73  ? 1138 ILE A CG1   1 
ATOM   9224  C CG2   . ILE B 2 1141 ? 129.640 149.710 97.930  1.00 44.73  ? 1138 ILE A CG2   1 
ATOM   9225  C CD1   . ILE B 2 1141 ? 127.435 148.662 99.736  1.00 44.73  ? 1138 ILE A CD1   1 
ATOM   9226  N N     . VAL B 2 1142 ? 128.467 152.808 96.804  1.00 44.73  ? 1139 VAL A N     1 
ATOM   9227  C CA    . VAL B 2 1142 ? 128.789 153.897 95.890  1.00 44.73  ? 1139 VAL A CA    1 
ATOM   9228  C C     . VAL B 2 1142 ? 130.302 154.008 95.778  1.00 44.73  ? 1139 VAL A C     1 
ATOM   9229  O O     . VAL B 2 1142 ? 130.995 154.174 96.789  1.00 44.73  ? 1139 VAL A O     1 
ATOM   9230  C CB    . VAL B 2 1142 ? 128.176 155.228 96.352  1.00 44.73  ? 1139 VAL A CB    1 
ATOM   9231  C CG1   . VAL B 2 1142 ? 128.841 156.395 95.643  1.00 44.73  ? 1139 VAL A CG1   1 
ATOM   9232  C CG2   . VAL B 2 1142 ? 126.676 155.233 96.104  1.00 44.73  ? 1139 VAL A CG2   1 
ATOM   9233  N N     . PHE B 2 1143 ? 130.810 153.912 94.551  1.00 44.73  ? 1140 PHE A N     1 
ATOM   9234  C CA    . PHE B 2 1143 ? 132.210 154.206 94.254  1.00 44.73  ? 1140 PHE A CA    1 
ATOM   9235  C C     . PHE B 2 1143 ? 132.301 155.703 93.995  1.00 44.73  ? 1140 PHE A C     1 
ATOM   9236  O O     . PHE B 2 1143 ? 132.176 156.168 92.861  1.00 44.73  ? 1140 PHE A O     1 
ATOM   9237  C CB    . PHE B 2 1143 ? 132.698 153.404 93.055  1.00 44.73  ? 1140 PHE A CB    1 
ATOM   9238  C CG    . PHE B 2 1143 ? 132.926 151.947 93.339  1.00 44.73  ? 1140 PHE A CG    1 
ATOM   9239  C CD1   . PHE B 2 1143 ? 131.870 151.112 93.651  1.00 44.73  ? 1140 PHE A CD1   1 
ATOM   9240  C CD2   . PHE B 2 1143 ? 134.197 151.410 93.274  1.00 44.73  ? 1140 PHE A CD2   1 
ATOM   9241  C CE1   . PHE B 2 1143 ? 132.081 149.772 93.904  1.00 44.73  ? 1140 PHE A CE1   1 
ATOM   9242  C CE2   . PHE B 2 1143 ? 134.414 150.073 93.527  1.00 44.73  ? 1140 PHE A CE2   1 
ATOM   9243  C CZ    . PHE B 2 1143 ? 133.355 149.253 93.841  1.00 44.73  ? 1140 PHE A CZ    1 
ATOM   9244  N N     . GLU B 2 1144 ? 132.507 156.467 95.066  1.00 44.73  ? 1141 GLU A N     1 
ATOM   9245  C CA    . GLU B 2 1144 ? 132.443 157.921 94.979  1.00 44.73  ? 1141 GLU A CA    1 
ATOM   9246  C C     . GLU B 2 1144 ? 133.469 158.455 93.991  1.00 44.73  ? 1141 GLU A C     1 
ATOM   9247  O O     . GLU B 2 1144 ? 134.630 158.036 93.994  1.00 44.73  ? 1141 GLU A O     1 
ATOM   9248  C CB    . GLU B 2 1144 ? 132.673 158.540 96.358  1.00 44.73  ? 1141 GLU A CB    1 
ATOM   9249  C CG    . GLU B 2 1144 ? 131.537 158.316 97.340  1.00 44.73  ? 1141 GLU A CG    1 
ATOM   9250  C CD    . GLU B 2 1144 ? 131.987 158.437 98.781  1.00 44.73  ? 1141 GLU A CD    1 
ATOM   9251  O OE1   . GLU B 2 1144 ? 132.437 159.533 99.175  1.00 44.73  ? 1141 GLU A OE1   1 
ATOM   9252  O OE2   . GLU B 2 1144 ? 131.894 157.435 99.520  1.00 44.73  ? 1141 GLU A OE2   1 
ATOM   9253  N N     . LYS B 2 1145 ? 133.034 159.380 93.139  1.00 44.73  ? 1142 LYS A N     1 
ATOM   9254  C CA    . LYS B 2 1145 ? 133.949 160.028 92.212  1.00 44.73  ? 1142 LYS A CA    1 
ATOM   9255  C C     . LYS B 2 1145 ? 134.963 160.854 92.990  1.00 44.73  ? 1142 LYS A C     1 
ATOM   9256  O O     . LYS B 2 1145 ? 134.597 161.634 93.874  1.00 44.73  ? 1142 LYS A O     1 
ATOM   9257  C CB    . LYS B 2 1145 ? 133.179 160.912 91.232  1.00 44.73  ? 1142 LYS A CB    1 
ATOM   9258  C CG    . LYS B 2 1145 ? 133.930 161.210 89.945  1.00 44.73  ? 1142 LYS A CG    1 
ATOM   9259  C CD    . LYS B 2 1145 ? 133.233 162.292 89.135  1.00 44.73  ? 1142 LYS A CD    1 
ATOM   9260  C CE    . LYS B 2 1145 ? 133.562 163.679 89.660  1.00 44.73  ? 1142 LYS A CE    1 
ATOM   9261  N NZ    . LYS B 2 1145 ? 135.005 164.007 89.495  1.00 44.73  ? 1142 LYS A NZ    1 
ATOM   9262  N N     . ASN B 2 1146 ? 136.238 160.681 92.661  1.00 44.73  ? 1143 ASN A N     1 
ATOM   9263  C CA    . ASN B 2 1146 ? 137.292 161.347 93.410  1.00 44.73  ? 1143 ASN A CA    1 
ATOM   9264  C C     . ASN B 2 1146 ? 137.349 162.825 93.049  1.00 44.73  ? 1143 ASN A C     1 
ATOM   9265  O O     . ASN B 2 1146 ? 137.450 163.189 91.874  1.00 44.73  ? 1143 ASN A O     1 
ATOM   9266  C CB    . ASN B 2 1146 ? 138.633 160.674 93.140  1.00 44.73  ? 1143 ASN A CB    1 
ATOM   9267  C CG    . ASN B 2 1146 ? 138.583 159.179 93.368  1.00 44.73  ? 1143 ASN A CG    1 
ATOM   9268  O OD1   . ASN B 2 1146 ? 138.782 158.391 92.445  1.00 44.73  ? 1143 ASN A OD1   1 
ATOM   9269  N ND2   . ASN B 2 1146 ? 138.307 158.779 94.603  1.00 44.73  ? 1143 ASN A ND2   1 
ATOM   9270  N N     . GLU B 2 1147 ? 137.282 163.677 94.069  1.00 44.73  ? 1144 GLU A N     1 
ATOM   9271  C CA    . GLU B 2 1147 ? 137.299 165.119 93.884  1.00 44.73  ? 1144 GLU A CA    1 
ATOM   9272  C C     . GLU B 2 1147 ? 138.006 165.746 95.077  1.00 44.73  ? 1144 GLU A C     1 
ATOM   9273  O O     . GLU B 2 1147 ? 137.972 165.217 96.190  1.00 44.73  ? 1144 GLU A O     1 
ATOM   9274  C CB    . GLU B 2 1147 ? 135.877 165.676 93.728  1.00 44.73  ? 1144 GLU A CB    1 
ATOM   9275  C CG    . GLU B 2 1147 ? 135.799 167.169 93.450  1.00 44.73  ? 1144 GLU A CG    1 
ATOM   9276  C CD    . GLU B 2 1147 ? 134.375 167.649 93.256  1.00 44.73  ? 1144 GLU A CD    1 
ATOM   9277  O OE1   . GLU B 2 1147 ? 133.447 166.819 93.360  1.00 44.73  ? 1144 GLU A OE1   1 
ATOM   9278  O OE2   . GLU B 2 1147 ? 134.182 168.857 93.002  1.00 44.73  ? 1144 GLU A OE2   1 
ATOM   9279  N N     . THR B 2 1148 ? 138.644 166.890 94.834  1.00 44.73  ? 1145 THR A N     1 
ATOM   9280  C CA    . THR B 2 1148 ? 139.413 167.582 95.869  1.00 44.73  ? 1145 THR A CA    1 
ATOM   9281  C C     . THR B 2 1148 ? 138.472 168.372 96.785  1.00 44.73  ? 1145 THR A C     1 
ATOM   9282  O O     . THR B 2 1148 ? 138.421 169.603 96.795  1.00 44.73  ? 1145 THR A O     1 
ATOM   9283  C CB    . THR B 2 1148 ? 140.481 168.465 95.231  1.00 44.73  ? 1145 THR A CB    1 
ATOM   9284  O OG1   . THR B 2 1148 ? 141.163 169.217 96.243  1.00 44.73  ? 1145 THR A OG1   1 
ATOM   9285  C CG2   . THR B 2 1148 ? 139.884 169.400 94.173  1.00 44.73  ? 1145 THR A CG2   1 
ATOM   9286  N N     . GLN B 2 1149 ? 137.722 167.618 97.585  1.00 44.73  ? 1146 GLN A N     1 
ATOM   9287  C CA    . GLN B 2 1149 ? 136.792 168.215 98.531  1.00 44.73  ? 1146 GLN A CA    1 
ATOM   9288  C C     . GLN B 2 1149 ? 137.540 168.957 99.634  1.00 44.73  ? 1146 GLN A C     1 
ATOM   9289  O O     . GLN B 2 1149 ? 138.669 168.613 99.992  1.00 44.73  ? 1146 GLN A O     1 
ATOM   9290  C CB    . GLN B 2 1149 ? 135.892 167.144 99.144  1.00 44.73  ? 1146 GLN A CB    1 
ATOM   9291  C CG    . GLN B 2 1149 ? 134.921 166.510 98.164  1.00 44.73  ? 1146 GLN A CG    1 
ATOM   9292  C CD    . GLN B 2 1149 ? 133.602 167.251 98.093  1.00 44.73  ? 1146 GLN A CD    1 
ATOM   9293  O OE1   . GLN B 2 1149 ? 133.565 168.481 98.116  1.00 44.73  ? 1146 GLN A OE1   1 
ATOM   9294  N NE2   . GLN B 2 1149 ? 132.508 166.503 98.007  1.00 44.73  ? 1146 GLN A NE2   1 
ATOM   9295  N N     . PHE B 2 1150 ? 136.894 169.986 100.173 1.00 44.73  ? 1147 PHE A N     1 
ATOM   9296  C CA    . PHE B 2 1150 ? 137.464 170.813 101.225 1.00 44.73  ? 1147 PHE A CA    1 
ATOM   9297  C C     . PHE B 2 1150 ? 136.680 170.626 102.516 1.00 44.73  ? 1147 PHE A C     1 
ATOM   9298  O O     . PHE B 2 1150 ? 135.450 170.511 102.497 1.00 44.73  ? 1147 PHE A O     1 
ATOM   9299  C CB    . PHE B 2 1150 ? 137.467 172.291 100.822 1.00 44.73  ? 1147 PHE A CB    1 
ATOM   9300  C CG    . PHE B 2 1150 ? 138.133 172.556 99.502  1.00 44.73  ? 1147 PHE A CG    1 
ATOM   9301  C CD1   . PHE B 2 1150 ? 139.512 172.602 99.405  1.00 44.73  ? 1147 PHE A CD1   1 
ATOM   9302  C CD2   . PHE B 2 1150 ? 137.380 172.757 98.359  1.00 44.73  ? 1147 PHE A CD2   1 
ATOM   9303  C CE1   . PHE B 2 1150 ? 140.128 172.845 98.194  1.00 44.73  ? 1147 PHE A CE1   1 
ATOM   9304  C CE2   . PHE B 2 1150 ? 137.991 173.000 97.144  1.00 44.73  ? 1147 PHE A CE2   1 
ATOM   9305  C CZ    . PHE B 2 1150 ? 139.366 173.044 97.062  1.00 44.73  ? 1147 PHE A CZ    1 
ATOM   9306  N N     . ASP B 2 1151 ? 137.397 170.601 103.634 1.00 44.73  ? 1148 ASP A N     1 
ATOM   9307  C CA    . ASP B 2 1151 ? 136.795 170.392 104.941 1.00 44.73  ? 1148 ASP A CA    1 
ATOM   9308  C C     . ASP B 2 1151 ? 136.315 171.724 105.513 1.00 44.73  ? 1148 ASP A C     1 
ATOM   9309  O O     . ASP B 2 1151 ? 136.269 172.744 104.820 1.00 44.73  ? 1148 ASP A O     1 
ATOM   9310  C CB    . ASP B 2 1151 ? 137.789 169.704 105.873 1.00 44.73  ? 1148 ASP A CB    1 
ATOM   9311  C CG    . ASP B 2 1151 ? 138.914 170.621 106.307 1.00 44.73  ? 1148 ASP A CG    1 
ATOM   9312  O OD1   . ASP B 2 1151 ? 139.314 171.495 105.511 1.00 44.73  ? 1148 ASP A OD1   1 
ATOM   9313  O OD2   . ASP B 2 1151 ? 139.400 170.467 107.447 1.00 44.73  ? 1148 ASP A OD2   1 
ATOM   9314  N N     . ALA B 2 1152 ? 135.939 171.721 106.794 1.00 44.73  ? 1149 ALA A N     1 
ATOM   9315  C CA    . ALA B 2 1152 ? 135.540 172.961 107.451 1.00 44.73  ? 1149 ALA A CA    1 
ATOM   9316  C C     . ALA B 2 1152 ? 136.697 173.949 107.504 1.00 44.73  ? 1149 ALA A C     1 
ATOM   9317  O O     . ALA B 2 1152 ? 136.509 175.152 107.289 1.00 44.73  ? 1149 ALA A O     1 
ATOM   9318  C CB    . ALA B 2 1152 ? 135.015 172.669 108.856 1.00 44.73  ? 1149 ALA A CB    1 
ATOM   9319  N N     . LYS B 2 1153 ? 137.905 173.459 107.787 1.00 44.73  ? 1150 LYS A N     1 
ATOM   9320  C CA    . LYS B 2 1153 ? 139.086 174.312 107.774 1.00 44.73  ? 1150 LYS A CA    1 
ATOM   9321  C C     . LYS B 2 1153 ? 139.517 174.699 106.367 1.00 44.73  ? 1150 LYS A C     1 
ATOM   9322  O O     . LYS B 2 1153 ? 140.381 175.570 106.222 1.00 44.73  ? 1150 LYS A O     1 
ATOM   9323  C CB    . LYS B 2 1153 ? 140.242 173.617 108.495 1.00 37.56  ? 1150 LYS A CB    1 
ATOM   9324  C CG    . LYS B 2 1153 ? 139.981 173.341 109.965 1.00 37.56  ? 1150 LYS A CG    1 
ATOM   9325  C CD    . LYS B 2 1153 ? 139.819 174.636 110.744 1.00 37.56  ? 1150 LYS A CD    1 
ATOM   9326  C CE    . LYS B 2 1153 ? 141.145 175.370 110.867 1.00 37.56  ? 1150 LYS A CE    1 
ATOM   9327  N NZ    . LYS B 2 1153 ? 141.028 176.605 111.691 1.00 37.56  ? 1150 LYS A NZ    1 
ATOM   9328  N N     . GLY B 2 1154 ? 138.945 174.082 105.336 1.00 44.73  ? 1151 GLY A N     1 
ATOM   9329  C CA    . GLY B 2 1154 ? 139.312 174.372 103.967 1.00 44.73  ? 1151 GLY A CA    1 
ATOM   9330  C C     . GLY B 2 1154 ? 140.492 173.592 103.431 1.00 44.73  ? 1151 GLY A C     1 
ATOM   9331  O O     . GLY B 2 1154 ? 140.933 173.866 102.307 1.00 44.73  ? 1151 GLY A O     1 
ATOM   9332  N N     . THR B 2 1155 ? 141.022 172.638 104.193 1.00 44.73  ? 1152 THR A N     1 
ATOM   9333  C CA    . THR B 2 1155 ? 142.154 171.854 103.721 1.00 44.73  ? 1152 THR A CA    1 
ATOM   9334  C C     . THR B 2 1155 ? 141.733 170.967 102.552 1.00 44.73  ? 1152 THR A C     1 
ATOM   9335  O O     . THR B 2 1155 ? 140.593 170.494 102.508 1.00 44.73  ? 1152 THR A O     1 
ATOM   9336  C CB    . THR B 2 1155 ? 142.721 170.994 104.850 1.00 44.73  ? 1152 THR A CB    1 
ATOM   9337  O OG1   . THR B 2 1155 ? 141.789 169.956 105.175 1.00 44.73  ? 1152 THR A OG1   1 
ATOM   9338  C CG2   . THR B 2 1155 ? 142.981 171.841 106.086 1.00 44.73  ? 1152 THR A CG2   1 
ATOM   9339  N N     . PRO B 2 1156 ? 142.619 170.730 101.589 1.00 44.73  ? 1153 PRO A N     1 
ATOM   9340  C CA    . PRO B 2 1156 ? 142.250 169.890 100.445 1.00 44.73  ? 1153 PRO A CA    1 
ATOM   9341  C C     . PRO B 2 1156 ? 142.414 168.411 100.750 1.00 44.73  ? 1153 PRO A C     1 
ATOM   9342  O O     . PRO B 2 1156 ? 143.434 167.968 101.283 1.00 44.73  ? 1153 PRO A O     1 
ATOM   9343  C CB    . PRO B 2 1156 ? 143.224 170.338 99.351  1.00 44.73  ? 1153 PRO A CB    1 
ATOM   9344  C CG    . PRO B 2 1156 ? 144.412 170.827 100.104 1.00 44.73  ? 1153 PRO A CG    1 
ATOM   9345  C CD    . PRO B 2 1156 ? 143.885 171.448 101.365 1.00 44.73  ? 1153 PRO A CD    1 
ATOM   9346  N N     . PHE B 2 1157 ? 141.386 167.644 100.399 1.00 44.73  ? 1154 PHE A N     1 
ATOM   9347  C CA    . PHE B 2 1157 ? 141.437 166.195 100.516 1.00 44.73  ? 1154 PHE A CA    1 
ATOM   9348  C C     . PHE B 2 1157 ? 140.617 165.592 99.386  1.00 44.73  ? 1154 PHE A C     1 
ATOM   9349  O O     . PHE B 2 1157 ? 139.626 166.176 98.940  1.00 44.73  ? 1154 PHE A O     1 
ATOM   9350  C CB    . PHE B 2 1157 ? 140.951 165.722 101.897 1.00 44.73  ? 1154 PHE A CB    1 
ATOM   9351  C CG    . PHE B 2 1157 ? 139.468 165.879 102.129 1.00 44.73  ? 1154 PHE A CG    1 
ATOM   9352  C CD1   . PHE B 2 1157 ? 138.559 164.977 101.600 1.00 44.73  ? 1154 PHE A CD1   1 
ATOM   9353  C CD2   . PHE B 2 1157 ? 138.993 166.894 102.940 1.00 44.73  ? 1154 PHE A CD2   1 
ATOM   9354  C CE1   . PHE B 2 1157 ? 137.208 165.119 101.829 1.00 44.73  ? 1154 PHE A CE1   1 
ATOM   9355  C CE2   . PHE B 2 1157 ? 137.641 167.038 103.173 1.00 44.73  ? 1154 PHE A CE2   1 
ATOM   9356  C CZ    . PHE B 2 1157 ? 136.749 166.148 102.619 1.00 44.73  ? 1154 PHE A CZ    1 
ATOM   9357  N N     . ILE B 2 1158 ? 141.046 164.423 98.924  1.00 44.73  ? 1155 ILE A N     1 
ATOM   9358  C CA    . ILE B 2 1158 ? 140.402 163.769 97.791  1.00 44.73  ? 1155 ILE A CA    1 
ATOM   9359  C C     . ILE B 2 1158 ? 139.336 162.804 98.301  1.00 44.73  ? 1155 ILE A C     1 
ATOM   9360  O O     . ILE B 2 1158 ? 139.593 161.979 99.184  1.00 44.73  ? 1155 ILE A O     1 
ATOM   9361  C CB    . ILE B 2 1158 ? 141.435 163.065 96.897  1.00 44.73  ? 1155 ILE A CB    1 
ATOM   9362  C CG1   . ILE B 2 1158 ? 140.790 162.597 95.588  1.00 44.73  ? 1155 ILE A CG1   1 
ATOM   9363  C CG2   . ILE B 2 1158 ? 142.163 161.955 97.641  1.00 44.73  ? 1155 ILE A CG2   1 
ATOM   9364  C CD1   . ILE B 2 1158 ? 141.787 162.187 94.528  1.00 44.73  ? 1155 ILE A CD1   1 
ATOM   9365  N N     . ALA B 2 1159 ? 138.124 162.935 97.769  1.00 44.73  ? 1156 ALA A N     1 
ATOM   9366  C CA    . ALA B 2 1159 ? 137.013 162.107 98.214  1.00 44.73  ? 1156 ALA A CA    1 
ATOM   9367  C C     . ALA B 2 1159 ? 137.156 160.686 97.689  1.00 44.73  ? 1156 ALA A C     1 
ATOM   9368  O O     . ALA B 2 1159 ? 137.631 160.462 96.573  1.00 44.73  ? 1156 ALA A O     1 
ATOM   9369  C CB    . ALA B 2 1159 ? 135.686 162.706 97.753  1.00 44.73  ? 1156 ALA A CB    1 
ATOM   9370  N N     . GLY B 2 1160 ? 136.742 159.722 98.505  1.00 44.73  ? 1157 GLY A N     1 
ATOM   9371  C CA    . GLY B 2 1160 ? 136.792 158.330 98.121  1.00 44.73  ? 1157 GLY A CA    1 
ATOM   9372  C C     . GLY B 2 1160 ? 138.140 157.668 98.272  1.00 44.73  ? 1157 GLY A C     1 
ATOM   9373  O O     . GLY B 2 1160 ? 138.260 156.476 97.963  1.00 44.73  ? 1157 GLY A O     1 
ATOM   9374  N N     . LYS B 2 1161 ? 139.155 158.394 98.732  1.00 44.73  ? 1158 LYS A N     1 
ATOM   9375  C CA    . LYS B 2 1161 ? 140.476 157.807 98.905  1.00 44.73  ? 1158 LYS A CA    1 
ATOM   9376  C C     . LYS B 2 1161 ? 140.428 156.701 99.947  1.00 44.73  ? 1158 LYS A C     1 
ATOM   9377  O O     . LYS B 2 1161 ? 139.853 156.870 101.026 1.00 44.73  ? 1158 LYS A O     1 
ATOM   9378  C CB    . LYS B 2 1161 ? 141.480 158.880 99.319  1.00 44.73  ? 1158 LYS A CB    1 
ATOM   9379  C CG    . LYS B 2 1161 ? 142.847 158.345 99.713  1.00 44.73  ? 1158 LYS A CG    1 
ATOM   9380  C CD    . LYS B 2 1161 ? 143.579 159.336 100.603 1.00 44.73  ? 1158 LYS A CD    1 
ATOM   9381  C CE    . LYS B 2 1161 ? 145.073 159.324 100.340 1.00 44.73  ? 1158 LYS A CE    1 
ATOM   9382  N NZ    . LYS B 2 1161 ? 145.633 157.947 100.401 1.00 44.73  ? 1158 LYS A NZ    1 
ATOM   9383  N N     . ARG B 2 1162 ? 141.035 155.565 99.621  1.00 44.73  ? 1159 ARG A N     1 
ATOM   9384  C CA    . ARG B 2 1162 ? 141.068 154.420 100.514 1.00 44.73  ? 1159 ARG A CA    1 
ATOM   9385  C C     . ARG B 2 1162 ? 142.500 153.932 100.652 1.00 44.73  ? 1159 ARG A C     1 
ATOM   9386  O O     . ARG B 2 1162 ? 143.244 153.878 99.668  1.00 44.73  ? 1159 ARG A O     1 
ATOM   9387  C CB    . ARG B 2 1162 ? 140.184 153.287 99.998  1.00 44.73  ? 1159 ARG A CB    1 
ATOM   9388  C CG    . ARG B 2 1162 ? 138.697 153.594 99.984  1.00 44.73  ? 1159 ARG A CG    1 
ATOM   9389  C CD    . ARG B 2 1162 ? 138.183 153.967 101.358 1.00 44.73  ? 1159 ARG A CD    1 
ATOM   9390  N NE    . ARG B 2 1162 ? 136.743 153.768 101.465 1.00 44.73  ? 1159 ARG A NE    1 
ATOM   9391  C CZ    . ARG B 2 1162 ? 135.832 154.585 100.955 1.00 44.73  ? 1159 ARG A CZ    1 
ATOM   9392  N NH1   . ARG B 2 1162 ? 136.177 155.679 100.295 1.00 44.73  ? 1159 ARG A NH1   1 
ATOM   9393  N NH2   . ARG B 2 1162 ? 134.543 154.298 101.110 1.00 44.73  ? 1159 ARG A NH2   1 
ATOM   9394  N N     . ILE B 2 1163 ? 142.882 153.578 101.874 1.00 44.73  ? 1160 ILE A N     1 
ATOM   9395  C CA    . ILE B 2 1163 ? 144.201 153.031 102.159 1.00 44.73  ? 1160 ILE A CA    1 
ATOM   9396  C C     . ILE B 2 1163 ? 144.062 151.520 102.266 1.00 44.73  ? 1160 ILE A C     1 
ATOM   9397  O O     . ILE B 2 1163 ? 143.408 151.011 103.185 1.00 44.73  ? 1160 ILE A O     1 
ATOM   9398  C CB    . ILE B 2 1163 ? 144.792 153.629 103.444 1.00 44.73  ? 1160 ILE A CB    1 
ATOM   9399  C CG1   . ILE B 2 1163 ? 145.175 155.092 103.222 1.00 44.73  ? 1160 ILE A CG1   1 
ATOM   9400  C CG2   . ILE B 2 1163 ? 145.996 152.826 103.903 1.00 44.73  ? 1160 ILE A CG2   1 
ATOM   9401  C CD1   . ILE B 2 1163 ? 146.401 155.276 102.360 1.00 44.73  ? 1160 ILE A CD1   1 
ATOM   9402  N N     . VAL B 2 1164 ? 144.666 150.803 101.331 1.00 49.71  ? 1161 VAL A N     1 
ATOM   9403  C CA    . VAL B 2 1164 ? 144.593 149.346 101.265 1.00 49.71  ? 1161 VAL A CA    1 
ATOM   9404  C C     . VAL B 2 1164 ? 145.969 148.783 101.599 1.00 49.71  ? 1161 VAL A C     1 
ATOM   9405  O O     . VAL B 2 1164 ? 146.974 149.285 101.083 1.00 49.71  ? 1161 VAL A O     1 
ATOM   9406  C CB    . VAL B 2 1164 ? 144.107 148.853 99.885  1.00 49.71  ? 1161 VAL A CB    1 
ATOM   9407  C CG1   . VAL B 2 1164 ? 145.096 149.204 98.778  1.00 49.71  ? 1161 VAL A CG1   1 
ATOM   9408  C CG2   . VAL B 2 1164 ? 143.847 147.354 99.916  1.00 49.71  ? 1161 VAL A CG2   1 
ATOM   9409  N N     . PRO B 2 1165 ? 146.066 147.796 102.487 1.00 69.88  ? 1162 PRO A N     1 
ATOM   9410  C CA    . PRO B 2 1165 ? 147.370 147.209 102.835 1.00 69.88  ? 1162 PRO A CA    1 
ATOM   9411  C C     . PRO B 2 1165 ? 147.738 145.945 102.069 1.00 69.88  ? 1162 PRO A C     1 
ATOM   9412  O O     . PRO B 2 1165 ? 148.822 145.406 102.314 1.00 69.88  ? 1162 PRO A O     1 
ATOM   9413  C CB    . PRO B 2 1165 ? 147.182 146.890 104.321 1.00 69.88  ? 1162 PRO A CB    1 
ATOM   9414  C CG    . PRO B 2 1165 ? 145.731 146.539 104.438 1.00 69.88  ? 1162 PRO A CG    1 
ATOM   9415  C CD    . PRO B 2 1165 ? 144.989 147.293 103.358 1.00 69.88  ? 1162 PRO A CD    1 
ATOM   9416  N N     . VAL B 2 1166 ? 146.884 145.472 101.165 1.00 80.59  ? 1163 VAL A N     1 
ATOM   9417  C CA    . VAL B 2 1166 ? 147.099 144.189 100.502 1.00 80.59  ? 1163 VAL A CA    1 
ATOM   9418  C C     . VAL B 2 1166 ? 148.300 144.319 99.570  1.00 80.59  ? 1163 VAL A C     1 
ATOM   9419  O O     . VAL B 2 1166 ? 148.220 144.961 98.519  1.00 80.59  ? 1163 VAL A O     1 
ATOM   9420  C CB    . VAL B 2 1166 ? 145.851 143.734 99.739  1.00 80.59  ? 1163 VAL A CB    1 
ATOM   9421  C CG1   . VAL B 2 1166 ? 146.075 142.357 99.131  1.00 80.59  ? 1163 VAL A CG1   1 
ATOM   9422  C CG2   . VAL B 2 1166 ? 144.641 143.724 100.661 1.00 80.59  ? 1163 VAL A CG2   1 
ATOM   9423  N N     . ILE B 2 1167 ? 149.418 143.709 99.958  1.00 86.52  ? 1164 ILE A N     1 
ATOM   9424  C CA    . ILE B 2 1167 ? 150.619 143.674 99.141  1.00 86.52  ? 1164 ILE A CA    1 
ATOM   9425  C C     . ILE B 2 1167 ? 150.951 142.255 98.696  1.00 86.52  ? 1164 ILE A C     1 
ATOM   9426  O O     . ILE B 2 1167 ? 151.362 142.039 97.554  1.00 86.52  ? 1164 ILE A O     1 
ATOM   9427  C CB    . ILE B 2 1167 ? 151.810 144.309 99.891  1.00 86.52  ? 1164 ILE A CB    1 
ATOM   9428  C CG1   . ILE B 2 1167 ? 151.435 145.698 100.409 1.00 86.52  ? 1164 ILE A CG1   1 
ATOM   9429  C CG2   . ILE B 2 1167 ? 153.032 144.389 98.989  1.00 86.52  ? 1164 ILE A CG2   1 
ATOM   9430  C CD1   . ILE B 2 1167 ? 151.084 146.683 99.318  1.00 86.52  ? 1164 ILE A CD1   1 
ATOM   9431  N N     . GLU B 2 1168 ? 150.770 141.277 99.581  1.00 102.62 ? 1165 GLU A N     1 
ATOM   9432  C CA    . GLU B 2 1168 ? 151.038 139.881 99.270  1.00 102.62 ? 1165 GLU A CA    1 
ATOM   9433  C C     . GLU B 2 1168 ? 149.886 139.028 99.783  1.00 102.62 ? 1165 GLU A C     1 
ATOM   9434  O O     . GLU B 2 1168 ? 149.126 139.439 100.663 1.00 102.62 ? 1165 GLU A O     1 
ATOM   9435  C CB    . GLU B 2 1168 ? 152.366 139.410 99.880  1.00 102.62 ? 1165 GLU A CB    1 
ATOM   9436  C CG    . GLU B 2 1168 ? 153.093 138.366 99.049  1.00 102.62 ? 1165 GLU A CG    1 
ATOM   9437  C CD    . GLU B 2 1168 ? 153.484 138.882 97.677  1.00 102.62 ? 1165 GLU A CD    1 
ATOM   9438  O OE1   . GLU B 2 1168 ? 153.859 140.068 97.570  1.00 102.62 ? 1165 GLU A OE1   1 
ATOM   9439  O OE2   . GLU B 2 1168 ? 153.414 138.100 96.705  1.00 102.62 ? 1165 GLU A OE2   1 
ATOM   9440  N N     . ASN B 2 1169 ? 149.758 137.831 99.205  1.00 109.07 ? 1166 ASN A N     1 
ATOM   9441  C CA    . ASN B 2 1169 ? 148.685 136.927 99.610  1.00 109.07 ? 1166 ASN A CA    1 
ATOM   9442  C C     . ASN B 2 1169 ? 148.838 136.499 101.065 1.00 109.07 ? 1166 ASN A C     1 
ATOM   9443  O O     . ASN B 2 1169 ? 147.851 136.434 101.807 1.00 109.07 ? 1166 ASN A O     1 
ATOM   9444  C CB    . ASN B 2 1169 ? 148.652 135.708 98.689  1.00 109.07 ? 1166 ASN A CB    1 
ATOM   9445  C CG    . ASN B 2 1169 ? 149.993 135.007 98.600  1.00 109.07 ? 1166 ASN A CG    1 
ATOM   9446  O OD1   . ASN B 2 1169 ? 151.032 135.649 98.448  1.00 109.07 ? 1166 ASN A OD1   1 
ATOM   9447  N ND2   . ASN B 2 1169 ? 149.977 133.683 98.695  1.00 109.07 ? 1166 ASN A ND2   1 
ATOM   9448  N N     . HIS B 2 1170 ? 150.067 136.201 101.492 1.00 110.37 ? 1167 HIS A N     1 
ATOM   9449  C CA    . HIS B 2 1170 ? 150.290 135.777 102.870 1.00 110.37 ? 1167 HIS A CA    1 
ATOM   9450  C C     . HIS B 2 1170 ? 150.408 136.968 103.814 1.00 110.37 ? 1167 HIS A C     1 
ATOM   9451  O O     . HIS B 2 1170 ? 149.916 136.916 104.947 1.00 110.37 ? 1167 HIS A O     1 
ATOM   9452  C CB    . HIS B 2 1170 ? 151.541 134.903 102.954 1.00 110.37 ? 1167 HIS A CB    1 
ATOM   9453  C CG    . HIS B 2 1170 ? 151.271 133.443 102.769 1.00 110.37 ? 1167 HIS A CG    1 
ATOM   9454  N ND1   . HIS B 2 1170 ? 151.441 132.802 101.561 1.00 110.37 ? 1167 HIS A ND1   1 
ATOM   9455  C CD2   . HIS B 2 1170 ? 150.842 132.498 103.639 1.00 110.37 ? 1167 HIS A CD2   1 
ATOM   9456  C CE1   . HIS B 2 1170 ? 151.128 131.525 101.694 1.00 110.37 ? 1167 HIS A CE1   1 
ATOM   9457  N NE2   . HIS B 2 1170 ? 150.762 131.314 102.946 1.00 110.37 ? 1167 HIS A NE2   1 
ATOM   9458  N N     . ARG B 2 1171 ? 151.053 138.043 103.369 1.00 101.30 ? 1168 ARG A N     1 
ATOM   9459  C CA    . ARG B 2 1171 ? 151.232 139.253 104.167 1.00 101.30 ? 1168 ARG A CA    1 
ATOM   9460  C C     . ARG B 2 1171 ? 150.280 140.313 103.622 1.00 101.30 ? 1168 ARG A C     1 
ATOM   9461  O O     . ARG B 2 1171 ? 150.535 140.912 102.573 1.00 101.30 ? 1168 ARG A O     1 
ATOM   9462  C CB    . ARG B 2 1171 ? 152.685 139.721 104.129 1.00 101.30 ? 1168 ARG A CB    1 
ATOM   9463  C CG    . ARG B 2 1171 ? 152.931 141.155 104.605 1.00 101.30 ? 1168 ARG A CG    1 
ATOM   9464  C CD    . ARG B 2 1171 ? 152.790 141.332 106.118 1.00 101.30 ? 1168 ARG A CD    1 
ATOM   9465  N NE    . ARG B 2 1171 ? 151.413 141.229 106.588 1.00 101.30 ? 1168 ARG A NE    1 
ATOM   9466  C CZ    . ARG B 2 1171 ? 151.036 141.404 107.847 1.00 101.30 ? 1168 ARG A CZ    1 
ATOM   9467  N NH1   . ARG B 2 1171 ? 151.910 141.700 108.795 1.00 101.30 ? 1168 ARG A NH1   1 
ATOM   9468  N NH2   . ARG B 2 1171 ? 149.750 141.281 108.163 1.00 101.30 ? 1168 ARG A NH2   1 
ATOM   9469  N N     . PHE B 2 1172 ? 149.181 140.539 104.338 1.00 97.93  ? 1169 PHE A N     1 
ATOM   9470  C CA    . PHE B 2 1172 ? 148.152 141.473 103.904 1.00 97.93  ? 1169 PHE A CA    1 
ATOM   9471  C C     . PHE B 2 1172 ? 148.320 142.869 104.489 1.00 97.93  ? 1169 PHE A C     1 
ATOM   9472  O O     . PHE B 2 1172 ? 147.496 143.743 104.202 1.00 97.93  ? 1169 PHE A O     1 
ATOM   9473  C CB    . PHE B 2 1172 ? 146.763 140.932 104.264 1.00 97.93  ? 1169 PHE A CB    1 
ATOM   9474  C CG    . PHE B 2 1172 ? 146.691 140.302 105.626 1.00 97.93  ? 1169 PHE A CG    1 
ATOM   9475  C CD1   . PHE B 2 1172 ? 146.565 141.086 106.761 1.00 97.93  ? 1169 PHE A CD1   1 
ATOM   9476  C CD2   . PHE B 2 1172 ? 146.743 138.925 105.772 1.00 97.93  ? 1169 PHE A CD2   1 
ATOM   9477  C CE1   . PHE B 2 1172 ? 146.498 140.510 108.016 1.00 97.93  ? 1169 PHE A CE1   1 
ATOM   9478  C CE2   . PHE B 2 1172 ? 146.676 138.343 107.024 1.00 97.93  ? 1169 PHE A CE2   1 
ATOM   9479  C CZ    . PHE B 2 1172 ? 146.552 139.137 108.147 1.00 97.93  ? 1169 PHE A CZ    1 
ATOM   9480  N N     . THR B 2 1173 ? 149.345 143.101 105.305 1.00 95.15  ? 1170 THR A N     1 
ATOM   9481  C CA    . THR B 2 1173 ? 149.592 144.418 105.889 1.00 95.15  ? 1170 THR A CA    1 
ATOM   9482  C C     . THR B 2 1173 ? 151.096 144.705 105.844 1.00 95.15  ? 1170 THR A C     1 
ATOM   9483  O O     . THR B 2 1173 ? 151.713 145.138 106.818 1.00 95.15  ? 1170 THR A O     1 
ATOM   9484  C CB    . THR B 2 1173 ? 149.010 144.488 107.305 1.00 95.15  ? 1170 THR A CB    1 
ATOM   9485  O OG1   . THR B 2 1173 ? 147.612 144.184 107.248 1.00 95.15  ? 1170 THR A OG1   1 
ATOM   9486  C CG2   . THR B 2 1173 ? 149.125 145.900 107.883 1.00 95.15  ? 1170 THR A CG2   1 
ATOM   9487  N N     . GLY B 2 1174 ? 151.716 144.417 104.698 1.00 85.50  ? 1171 GLY A N     1 
ATOM   9488  C CA    . GLY B 2 1174 ? 153.131 144.715 104.546 1.00 85.50  ? 1171 GLY A CA    1 
ATOM   9489  C C     . GLY B 2 1174 ? 153.421 146.203 104.541 1.00 85.50  ? 1171 GLY A C     1 
ATOM   9490  O O     . GLY B 2 1174 ? 154.351 146.666 105.207 1.00 85.50  ? 1171 GLY A O     1 
ATOM   9491  N N     . ARG B 2 1175 ? 152.630 146.973 103.797 1.00 78.45  ? 1172 ARG A N     1 
ATOM   9492  C CA    . ARG B 2 1175 ? 152.790 148.418 103.739 1.00 78.45  ? 1172 ARG A CA    1 
ATOM   9493  C C     . ARG B 2 1175 ? 151.505 149.030 103.202 1.00 78.45  ? 1172 ARG A C     1 
ATOM   9494  O O     . ARG B 2 1175 ? 150.870 148.468 102.306 1.00 78.45  ? 1172 ARG A O     1 
ATOM   9495  C CB    . ARG B 2 1175 ? 153.982 148.823 102.864 1.00 78.45  ? 1172 ARG A CB    1 
ATOM   9496  C CG    . ARG B 2 1175 ? 154.107 148.040 101.570 1.00 78.45  ? 1172 ARG A CG    1 
ATOM   9497  C CD    . ARG B 2 1175 ? 155.416 148.357 100.867 1.00 78.45  ? 1172 ARG A CD    1 
ATOM   9498  N NE    . ARG B 2 1175 ? 155.778 147.335 99.892  1.00 78.45  ? 1172 ARG A NE    1 
ATOM   9499  C CZ    . ARG B 2 1175 ? 156.348 146.177 100.196 1.00 78.45  ? 1172 ARG A CZ    1 
ATOM   9500  N NH1   . ARG B 2 1175 ? 156.643 145.858 101.446 1.00 78.45  ? 1172 ARG A NH1   1 
ATOM   9501  N NH2   . ARG B 2 1175 ? 156.631 145.317 99.222  1.00 78.45  ? 1172 ARG A NH2   1 
ATOM   9502  N N     . TYR B 2 1176 ? 151.134 150.180 103.755 1.00 60.28  ? 1173 TYR A N     1 
ATOM   9503  C CA    . TYR B 2 1176 ? 149.903 150.844 103.357 1.00 60.28  ? 1173 TYR A CA    1 
ATOM   9504  C C     . TYR B 2 1176 ? 150.074 151.499 101.991 1.00 60.28  ? 1173 TYR A C     1 
ATOM   9505  O O     . TYR B 2 1176 ? 151.094 152.135 101.713 1.00 60.28  ? 1173 TYR A O     1 
ATOM   9506  C CB    . TYR B 2 1176 ? 149.513 151.881 104.407 1.00 60.28  ? 1173 TYR A CB    1 
ATOM   9507  C CG    . TYR B 2 1176 ? 148.758 151.294 105.579 1.00 60.28  ? 1173 TYR A CG    1 
ATOM   9508  C CD1   . TYR B 2 1176 ? 148.356 149.965 105.574 1.00 60.28  ? 1173 TYR A CD1   1 
ATOM   9509  C CD2   . TYR B 2 1176 ? 148.477 152.057 106.703 1.00 60.28  ? 1173 TYR A CD2   1 
ATOM   9510  C CE1   . TYR B 2 1176 ? 147.674 149.420 106.645 1.00 60.28  ? 1173 TYR A CE1   1 
ATOM   9511  C CE2   . TYR B 2 1176 ? 147.799 151.518 107.781 1.00 60.28  ? 1173 TYR A CE2   1 
ATOM   9512  C CZ    . TYR B 2 1176 ? 147.398 150.201 107.745 1.00 60.28  ? 1173 TYR A CZ    1 
ATOM   9513  O OH    . TYR B 2 1176 ? 146.722 149.661 108.815 1.00 60.28  ? 1173 TYR A OH    1 
ATOM   9514  N N     . ARG B 2 1177 ? 149.067 151.340 101.135 1.00 57.19  ? 1174 ARG A N     1 
ATOM   9515  C CA    . ARG B 2 1177 ? 149.128 151.790 99.750  1.00 57.19  ? 1174 ARG A CA    1 
ATOM   9516  C C     . ARG B 2 1177 ? 147.902 152.630 99.421  1.00 57.19  ? 1174 ARG A C     1 
ATOM   9517  O O     . ARG B 2 1177 ? 146.780 152.268 99.788  1.00 57.19  ? 1174 ARG A O     1 
ATOM   9518  C CB    . ARG B 2 1177 ? 149.221 150.596 98.795  1.00 57.19  ? 1174 ARG A CB    1 
ATOM   9519  C CG    . ARG B 2 1177 ? 149.151 150.959 97.321  1.00 57.19  ? 1174 ARG A CG    1 
ATOM   9520  C CD    . ARG B 2 1177 ? 149.617 149.806 96.449  1.00 57.19  ? 1174 ARG A CD    1 
ATOM   9521  N NE    . ARG B 2 1177 ? 148.894 148.574 96.742  1.00 57.19  ? 1174 ARG A NE    1 
ATOM   9522  C CZ    . ARG B 2 1177 ? 147.733 148.237 96.197  1.00 57.19  ? 1174 ARG A CZ    1 
ATOM   9523  N NH1   . ARG B 2 1177 ? 147.128 149.021 95.319  1.00 57.19  ? 1174 ARG A NH1   1 
ATOM   9524  N NH2   . ARG B 2 1177 ? 147.164 147.086 96.542  1.00 57.19  ? 1174 ARG A NH2   1 
ATOM   9525  N N     . ASP B 2 1178 ? 148.120 153.745 98.730  1.00 44.73  ? 1175 ASP A N     1 
ATOM   9526  C CA    . ASP B 2 1178 ? 147.019 154.583 98.281  1.00 44.73  ? 1175 ASP A CA    1 
ATOM   9527  C C     . ASP B 2 1178 ? 146.244 153.887 97.168  1.00 44.73  ? 1175 ASP A C     1 
ATOM   9528  O O     . ASP B 2 1178 ? 146.811 153.173 96.336  1.00 44.73  ? 1175 ASP A O     1 
ATOM   9529  C CB    . ASP B 2 1178 ? 147.544 155.934 97.793  1.00 44.73  ? 1175 ASP A CB    1 
ATOM   9530  C CG    . ASP B 2 1178 ? 146.435 156.938 97.534  1.00 44.73  ? 1175 ASP A CG    1 
ATOM   9531  O OD1   . ASP B 2 1178 ? 145.249 156.591 97.715  1.00 44.73  ? 1175 ASP A OD1   1 
ATOM   9532  O OD2   . ASP B 2 1178 ? 146.752 158.082 97.146  1.00 44.73  ? 1175 ASP A OD2   1 
ATOM   9533  N N     . LEU B 2 1179 ? 144.930 154.104 97.156  1.00 44.73  ? 1176 LEU A N     1 
ATOM   9534  C CA    . LEU B 2 1179 ? 144.069 153.472 96.168  1.00 44.73  ? 1176 LEU A CA    1 
ATOM   9535  C C     . LEU B 2 1179 ? 142.794 154.288 96.026  1.00 44.73  ? 1176 LEU A C     1 
ATOM   9536  O O     . LEU B 2 1179 ? 142.231 154.747 97.023  1.00 44.73  ? 1176 LEU A O     1 
ATOM   9537  C CB    . LEU B 2 1179 ? 143.739 152.028 96.565  1.00 44.73  ? 1176 LEU A CB    1 
ATOM   9538  C CG    . LEU B 2 1179 ? 142.894 151.215 95.586  1.00 44.73  ? 1176 LEU A CG    1 
ATOM   9539  C CD1   . LEU B 2 1179 ? 143.632 151.051 94.271  1.00 44.73  ? 1176 LEU A CD1   1 
ATOM   9540  C CD2   . LEU B 2 1179 ? 142.546 149.861 96.175  1.00 44.73  ? 1176 LEU A CD2   1 
ATOM   9541  N N     . TYR B 2 1180 ? 142.347 154.462 94.788  1.00 44.73  ? 1177 TYR A N     1 
ATOM   9542  C CA    . TYR B 2 1180 ? 141.124 155.205 94.490  1.00 44.73  ? 1177 TYR A CA    1 
ATOM   9543  C C     . TYR B 2 1180 ? 140.160 154.289 93.754  1.00 44.73  ? 1177 TYR A C     1 
ATOM   9544  O O     . TYR B 2 1180 ? 140.366 154.018 92.556  1.00 44.73  ? 1177 TYR A O     1 
ATOM   9545  C CB    . TYR B 2 1180 ? 141.432 156.441 93.648  1.00 44.73  ? 1177 TYR A CB    1 
ATOM   9546  C CG    . TYR B 2 1180 ? 142.412 157.387 94.295  1.00 44.73  ? 1177 TYR A CG    1 
ATOM   9547  C CD1   . TYR B 2 1180 ? 142.022 158.218 95.332  1.00 44.73  ? 1177 TYR A CD1   1 
ATOM   9548  C CD2   . TYR B 2 1180 ? 143.728 157.452 93.864  1.00 44.73  ? 1177 TYR A CD2   1 
ATOM   9549  C CE1   . TYR B 2 1180 ? 142.915 159.083 95.924  1.00 44.73  ? 1177 TYR A CE1   1 
ATOM   9550  C CE2   . TYR B 2 1180 ? 144.628 158.316 94.449  1.00 44.73  ? 1177 TYR A CE2   1 
ATOM   9551  C CZ    . TYR B 2 1180 ? 144.217 159.130 95.478  1.00 44.73  ? 1177 TYR A CZ    1 
ATOM   9552  O OH    . TYR B 2 1180 ? 145.111 159.994 96.067  1.00 44.73  ? 1177 TYR A OH    1 
ATOM   9553  N N     . PRO B 2 1181 ? 139.112 153.785 94.410  1.00 44.73  ? 1178 PRO A N     1 
ATOM   9554  C CA    . PRO B 2 1181 ? 138.245 152.796 93.746  1.00 44.73  ? 1178 PRO A CA    1 
ATOM   9555  C C     . PRO B 2 1181 ? 137.609 153.299 92.463  1.00 44.73  ? 1178 PRO A C     1 
ATOM   9556  O O     . PRO B 2 1181 ? 137.453 152.523 91.512  1.00 44.73  ? 1178 PRO A O     1 
ATOM   9557  C CB    . PRO B 2 1181 ? 137.190 152.485 94.817  1.00 44.73  ? 1178 PRO A CB    1 
ATOM   9558  C CG    . PRO B 2 1181 ? 137.816 152.880 96.109  1.00 44.73  ? 1178 PRO A CG    1 
ATOM   9559  C CD    . PRO B 2 1181 ? 138.707 154.040 95.801  1.00 44.73  ? 1178 PRO A CD    1 
ATOM   9560  N N     . ALA B 2 1182 ? 137.230 154.576 92.406  1.00 44.73  ? 1179 ALA A N     1 
ATOM   9561  C CA    . ALA B 2 1182 ? 136.569 155.094 91.213  1.00 44.73  ? 1179 ALA A CA    1 
ATOM   9562  C C     . ALA B 2 1182 ? 137.536 155.198 90.040  1.00 44.73  ? 1179 ALA A C     1 
ATOM   9563  O O     . ALA B 2 1182 ? 137.233 154.744 88.931  1.00 44.73  ? 1179 ALA A O     1 
ATOM   9564  C CB    . ALA B 2 1182 ? 135.937 156.453 91.511  1.00 44.73  ? 1179 ALA A CB    1 
ATOM   9565  N N     . ASN B 2 1183 ? 138.709 155.795 90.265  1.00 44.73  ? 1180 ASN A N     1 
ATOM   9566  C CA    . ASN B 2 1183 ? 139.652 156.000 89.170  1.00 44.73  ? 1180 ASN A CA    1 
ATOM   9567  C C     . ASN B 2 1183 ? 140.196 154.678 88.644  1.00 44.73  ? 1180 ASN A C     1 
ATOM   9568  O O     . ASN B 2 1183 ? 140.317 154.490 87.428  1.00 44.73  ? 1180 ASN A O     1 
ATOM   9569  C CB    . ASN B 2 1183 ? 140.798 156.905 89.621  1.00 44.73  ? 1180 ASN A CB    1 
ATOM   9570  C CG    . ASN B 2 1183 ? 140.357 158.337 89.841  1.00 44.73  ? 1180 ASN A CG    1 
ATOM   9571  O OD1   . ASN B 2 1183 ? 140.763 158.982 90.807  1.00 44.73  ? 1180 ASN A OD1   1 
ATOM   9572  N ND2   . ASN B 2 1183 ? 139.519 158.842 88.943  1.00 44.73  ? 1180 ASN A ND2   1 
ATOM   9573  N N     . GLU B 2 1184 ? 140.535 153.752 89.542  1.00 44.73  ? 1181 GLU A N     1 
ATOM   9574  C CA    . GLU B 2 1184 ? 141.126 152.490 89.109  1.00 44.73  ? 1181 GLU A CA    1 
ATOM   9575  C C     . GLU B 2 1184 ? 140.128 151.643 88.332  1.00 44.73  ? 1181 GLU A C     1 
ATOM   9576  O O     . GLU B 2 1184 ? 140.502 150.966 87.368  1.00 44.73  ? 1181 GLU A O     1 
ATOM   9577  C CB    . GLU B 2 1184 ? 141.666 151.718 90.311  1.00 44.73  ? 1181 GLU A CB    1 
ATOM   9578  C CG    . GLU B 2 1184 ? 142.720 152.471 91.103  1.00 44.73  ? 1181 GLU A CG    1 
ATOM   9579  C CD    . GLU B 2 1184 ? 143.747 153.145 90.216  1.00 44.73  ? 1181 GLU A CD    1 
ATOM   9580  O OE1   . GLU B 2 1184 ? 144.437 152.434 89.456  1.00 44.73  ? 1181 GLU A OE1   1 
ATOM   9581  O OE2   . GLU B 2 1184 ? 143.865 154.387 90.280  1.00 44.73  ? 1181 GLU A OE2   1 
ATOM   9582  N N     . LEU B 2 1185 ? 138.856 151.662 88.733  1.00 44.73  ? 1182 LEU A N     1 
ATOM   9583  C CA    . LEU B 2 1185 ? 137.874 150.819 88.060  1.00 44.73  ? 1182 LEU A CA    1 
ATOM   9584  C C     . LEU B 2 1185 ? 137.517 151.374 86.687  1.00 44.73  ? 1182 LEU A C     1 
ATOM   9585  O O     . LEU B 2 1185 ? 137.239 150.611 85.755  1.00 44.73  ? 1182 LEU A O     1 
ATOM   9586  C CB    . LEU B 2 1185 ? 136.631 150.656 88.932  1.00 44.73  ? 1182 LEU A CB    1 
ATOM   9587  C CG    . LEU B 2 1185 ? 135.631 149.635 88.400  1.00 44.73  ? 1182 LEU A CG    1 
ATOM   9588  C CD1   . LEU B 2 1185 ? 136.360 148.337 88.156  1.00 44.73  ? 1182 LEU A CD1   1 
ATOM   9589  C CD2   . LEU B 2 1185 ? 134.536 149.412 89.421  1.00 44.73  ? 1182 LEU A CD2   1 
ATOM   9590  N N     . ILE B 2 1186 ? 137.518 152.700 86.541  1.00 44.73  ? 1183 ILE A N     1 
ATOM   9591  C CA    . ILE B 2 1186 ? 137.390 153.290 85.211  1.00 44.73  ? 1183 ILE A CA    1 
ATOM   9592  C C     . ILE B 2 1186 ? 138.588 152.911 84.350  1.00 44.73  ? 1183 ILE A C     1 
ATOM   9593  O O     . ILE B 2 1186 ? 138.440 152.555 83.174  1.00 44.73  ? 1183 ILE A O     1 
ATOM   9594  C CB    . ILE B 2 1186 ? 137.224 154.818 85.312  1.00 44.73  ? 1183 ILE A CB    1 
ATOM   9595  C CG1   . ILE B 2 1186 ? 135.932 155.167 86.052  1.00 44.73  ? 1183 ILE A CG1   1 
ATOM   9596  C CG2   . ILE B 2 1186 ? 137.236 155.449 83.931  1.00 44.73  ? 1183 ILE A CG2   1 
ATOM   9597  C CD1   . ILE B 2 1186 ? 135.818 156.629 86.421  1.00 44.73  ? 1183 ILE A CD1   1 
ATOM   9598  N N     . ALA B 2 1187 ? 139.792 152.979 84.922  1.00 44.73  ? 1184 ALA A N     1 
ATOM   9599  C CA    . ALA B 2 1187 ? 140.990 152.599 84.179  1.00 44.73  ? 1184 ALA A CA    1 
ATOM   9600  C C     . ALA B 2 1187 ? 140.980 151.116 83.831  1.00 44.73  ? 1184 ALA A C     1 
ATOM   9601  O O     . ALA B 2 1187 ? 141.372 150.729 82.724  1.00 44.73  ? 1184 ALA A O     1 
ATOM   9602  C CB    . ALA B 2 1187 ? 142.240 152.954 84.983  1.00 44.73  ? 1184 ALA A CB    1 
ATOM   9603  N N     . LEU B 2 1188 ? 140.547 150.269 84.768  1.00 45.24  ? 1185 LEU A N     1 
ATOM   9604  C CA    . LEU B 2 1188 ? 140.494 148.835 84.503  1.00 45.24  ? 1185 LEU A CA    1 
ATOM   9605  C C     . LEU B 2 1188 ? 139.519 148.523 83.376  1.00 45.24  ? 1185 LEU A C     1 
ATOM   9606  O O     . LEU B 2 1188 ? 139.805 147.698 82.500  1.00 45.24  ? 1185 LEU A O     1 
ATOM   9607  C CB    . LEU B 2 1188 ? 140.105 148.080 85.773  1.00 45.24  ? 1185 LEU A CB    1 
ATOM   9608  C CG    . LEU B 2 1188 ? 139.671 146.626 85.574  1.00 45.24  ? 1185 LEU A CG    1 
ATOM   9609  C CD1   . LEU B 2 1188 ? 140.863 145.754 85.210  1.00 45.24  ? 1185 LEU A CD1   1 
ATOM   9610  C CD2   . LEU B 2 1188 ? 138.967 146.092 86.811  1.00 45.24  ? 1185 LEU A CD2   1 
ATOM   9611  N N     . LEU B 2 1189 ? 138.356 149.177 83.383  1.00 45.21  ? 1186 LEU A N     1 
ATOM   9612  C CA    . LEU B 2 1189 ? 137.366 148.934 82.341  1.00 45.21  ? 1186 LEU A CA    1 
ATOM   9613  C C     . LEU B 2 1189 ? 137.838 149.443 80.985  1.00 45.21  ? 1186 LEU A C     1 
ATOM   9614  O O     . LEU B 2 1189 ? 137.539 148.826 79.956  1.00 45.21  ? 1186 LEU A O     1 
ATOM   9615  C CB    . LEU B 2 1189 ? 136.034 149.580 82.723  1.00 45.21  ? 1186 LEU A CB    1 
ATOM   9616  C CG    . LEU B 2 1189 ? 134.991 148.650 83.346  1.00 45.21  ? 1186 LEU A CG    1 
ATOM   9617  C CD1   . LEU B 2 1189 ? 135.551 147.949 84.572  1.00 45.21  ? 1186 LEU A CD1   1 
ATOM   9618  C CD2   . LEU B 2 1189 ? 133.729 149.417 83.701  1.00 45.21  ? 1186 LEU A CD2   1 
ATOM   9619  N N     . GLU B 2 1190 ? 138.566 150.561 80.961  1.00 48.04  ? 1187 GLU A N     1 
ATOM   9620  C CA    . GLU B 2 1190 ? 139.083 151.080 79.699  1.00 48.04  ? 1187 GLU A CA    1 
ATOM   9621  C C     . GLU B 2 1190 ? 140.071 150.108 79.067  1.00 48.04  ? 1187 GLU A C     1 
ATOM   9622  O O     . GLU B 2 1190 ? 140.056 149.904 77.847  1.00 48.04  ? 1187 GLU A O     1 
ATOM   9623  C CB    . GLU B 2 1190 ? 139.736 152.444 79.920  1.00 48.04  ? 1187 GLU A CB    1 
ATOM   9624  C CG    . GLU B 2 1190 ? 138.749 153.592 80.086  1.00 48.04  ? 1187 GLU A CG    1 
ATOM   9625  C CD    . GLU B 2 1190 ? 137.751 153.678 78.948  1.00 48.04  ? 1187 GLU A CD    1 
ATOM   9626  O OE1   . GLU B 2 1190 ? 138.170 153.558 77.777  1.00 48.04  ? 1187 GLU A OE1   1 
ATOM   9627  O OE2   . GLU B 2 1190 ? 136.548 153.869 79.224  1.00 48.04  ? 1187 GLU A OE2   1 
ATOM   9628  N N     . GLU B 2 1191 ? 140.940 149.504 79.881  1.00 50.01  ? 1188 GLU A N     1 
ATOM   9629  C CA    . GLU B 2 1191 ? 141.882 148.518 79.363  1.00 50.01  ? 1188 GLU A CA    1 
ATOM   9630  C C     . GLU B 2 1191 ? 141.154 147.314 78.785  1.00 50.01  ? 1188 GLU A C     1 
ATOM   9631  O O     . GLU B 2 1191 ? 141.526 146.802 77.722  1.00 50.01  ? 1188 GLU A O     1 
ATOM   9632  C CB    . GLU B 2 1191 ? 142.842 148.080 80.470  1.00 50.01  ? 1188 GLU A CB    1 
ATOM   9633  C CG    . GLU B 2 1191 ? 143.434 146.693 80.266  1.00 50.01  ? 1188 GLU A CG    1 
ATOM   9634  C CD    . GLU B 2 1191 ? 144.133 146.168 81.503  1.00 50.01  ? 1188 GLU A CD    1 
ATOM   9635  O OE1   . GLU B 2 1191 ? 144.150 146.883 82.528  1.00 50.01  ? 1188 GLU A OE1   1 
ATOM   9636  O OE2   . GLU B 2 1191 ? 144.663 145.039 81.452  1.00 50.01  ? 1188 GLU A OE2   1 
ATOM   9637  N N     . LYS B 2 1192 ? 140.105 146.853 79.467  1.00 45.80  ? 1189 LYS A N     1 
ATOM   9638  C CA    . LYS B 2 1192 ? 139.374 145.679 79.010  1.00 45.80  ? 1189 LYS A CA    1 
ATOM   9639  C C     . LYS B 2 1192 ? 138.501 145.979 77.799  1.00 45.80  ? 1189 LYS A C     1 
ATOM   9640  O O     . LYS B 2 1192 ? 137.906 145.054 77.237  1.00 45.80  ? 1189 LYS A O     1 
ATOM   9641  C CB    . LYS B 2 1192 ? 138.518 145.120 80.147  1.00 45.80  ? 1189 LYS A CB    1 
ATOM   9642  C CG    . LYS B 2 1192 ? 139.175 143.989 80.921  1.00 45.80  ? 1189 LYS A CG    1 
ATOM   9643  C CD    . LYS B 2 1192 ? 139.327 142.744 80.068  1.00 45.80  ? 1189 LYS A CD    1 
ATOM   9644  C CE    . LYS B 2 1192 ? 137.981 142.258 79.562  1.00 45.80  ? 1189 LYS A CE    1 
ATOM   9645  N NZ    . LYS B 2 1192 ? 138.126 141.316 78.418  1.00 45.80  ? 1189 LYS A NZ    1 
ATOM   9646  N N     . GLY B 2 1193 ? 138.406 147.241 77.390  1.00 44.73  ? 1190 GLY A N     1 
ATOM   9647  C CA    . GLY B 2 1193 ? 137.550 147.602 76.282  1.00 44.73  ? 1190 GLY A CA    1 
ATOM   9648  C C     . GLY B 2 1193 ? 136.082 147.679 76.622  1.00 44.73  ? 1190 GLY A C     1 
ATOM   9649  O O     . GLY B 2 1193 ? 135.253 147.762 75.708  1.00 44.73  ? 1190 GLY A O     1 
ATOM   9650  N N     . ILE B 2 1194 ? 135.735 147.653 77.908  1.00 44.73  ? 1191 ILE A N     1 
ATOM   9651  C CA    . ILE B 2 1194 ? 134.340 147.676 78.326  1.00 44.73  ? 1191 ILE A CA    1 
ATOM   9652  C C     . ILE B 2 1194 ? 133.783 149.084 78.186  1.00 44.73  ? 1191 ILE A C     1 
ATOM   9653  O O     . ILE B 2 1194 ? 134.322 150.045 78.751  1.00 44.73  ? 1191 ILE A O     1 
ATOM   9654  C CB    . ILE B 2 1194 ? 134.211 147.173 79.770  1.00 44.73  ? 1191 ILE A CB    1 
ATOM   9655  C CG1   . ILE B 2 1194 ? 134.661 145.715 79.856  1.00 44.73  ? 1191 ILE A CG1   1 
ATOM   9656  C CG2   . ILE B 2 1194 ? 132.788 147.359 80.289  1.00 44.73  ? 1191 ILE A CG2   1 
ATOM   9657  C CD1   . ILE B 2 1194 ? 134.814 145.220 81.260  1.00 44.73  ? 1191 ILE A CD1   1 
ATOM   9658  N N     . VAL B 2 1195 ? 132.697 149.213 77.435  1.00 44.73  ? 1192 VAL A N     1 
ATOM   9659  C CA    . VAL B 2 1195 ? 131.997 150.487 77.333  1.00 44.73  ? 1192 VAL A CA    1 
ATOM   9660  C C     . VAL B 2 1195 ? 130.974 150.579 78.458  1.00 44.73  ? 1192 VAL A C     1 
ATOM   9661  O O     . VAL B 2 1195 ? 130.160 149.669 78.657  1.00 44.73  ? 1192 VAL A O     1 
ATOM   9662  C CB    . VAL B 2 1195 ? 131.352 150.650 75.946  1.00 44.73  ? 1192 VAL A CB    1 
ATOM   9663  C CG1   . VAL B 2 1195 ? 130.312 149.567 75.672  1.00 44.73  ? 1192 VAL A CG1   1 
ATOM   9664  C CG2   . VAL B 2 1195 ? 130.736 152.032 75.818  1.00 44.73  ? 1192 VAL A CG2   1 
ATOM   9665  N N     . PHE B 2 1196 ? 131.040 151.665 79.226  1.00 44.73  ? 1193 PHE A N     1 
ATOM   9666  C CA    . PHE B 2 1196 ? 130.153 151.827 80.370  1.00 44.73  ? 1193 PHE A CA    1 
ATOM   9667  C C     . PHE B 2 1196 ? 129.556 153.217 80.504  1.00 44.73  ? 1193 PHE A C     1 
ATOM   9668  O O     . PHE B 2 1196 ? 128.757 153.428 81.421  1.00 44.73  ? 1193 PHE A O     1 
ATOM   9669  C CB    . PHE B 2 1196 ? 130.888 151.476 81.672  1.00 44.73  ? 1193 PHE A CB    1 
ATOM   9670  C CG    . PHE B 2 1196 ? 132.085 152.341 81.949  1.00 44.73  ? 1193 PHE A CG    1 
ATOM   9671  C CD1   . PHE B 2 1196 ? 133.315 152.043 81.391  1.00 44.73  ? 1193 PHE A CD1   1 
ATOM   9672  C CD2   . PHE B 2 1196 ? 131.983 153.440 82.782  1.00 44.73  ? 1193 PHE A CD2   1 
ATOM   9673  C CE1   . PHE B 2 1196 ? 134.416 152.833 81.648  1.00 44.73  ? 1193 PHE A CE1   1 
ATOM   9674  C CE2   . PHE B 2 1196 ? 133.081 154.233 83.043  1.00 44.73  ? 1193 PHE A CE2   1 
ATOM   9675  C CZ    . PHE B 2 1196 ? 134.298 153.929 82.476  1.00 44.73  ? 1193 PHE A CZ    1 
ATOM   9676  N N     . ARG B 2 1197 ? 129.905 154.170 79.639  1.00 46.03  ? 1194 ARG A N     1 
ATOM   9677  C CA    . ARG B 2 1197 ? 129.321 155.502 79.719  1.00 46.03  ? 1194 ARG A CA    1 
ATOM   9678  C C     . ARG B 2 1197 ? 127.841 155.507 79.370  1.00 46.03  ? 1194 ARG A C     1 
ATOM   9679  O O     . ARG B 2 1197 ? 127.153 156.489 79.671  1.00 46.03  ? 1194 ARG A O     1 
ATOM   9680  C CB    . ARG B 2 1197 ? 130.076 156.470 78.803  1.00 46.03  ? 1194 ARG A CB    1 
ATOM   9681  C CG    . ARG B 2 1197 ? 131.537 156.108 78.541  1.00 46.03  ? 1194 ARG A CG    1 
ATOM   9682  C CD    . ARG B 2 1197 ? 132.357 156.058 79.825  1.00 46.03  ? 1194 ARG A CD    1 
ATOM   9683  N NE    . ARG B 2 1197 ? 132.549 157.378 80.410  1.00 46.03  ? 1194 ARG A NE    1 
ATOM   9684  C CZ    . ARG B 2 1197 ? 133.650 158.103 80.275  1.00 46.03  ? 1194 ARG A CZ    1 
ATOM   9685  N NH1   . ARG B 2 1197 ? 134.687 157.662 79.582  1.00 46.03  ? 1194 ARG A NH1   1 
ATOM   9686  N NH2   . ARG B 2 1197 ? 133.715 159.300 80.852  1.00 46.03  ? 1194 ARG A NH2   1 
ATOM   9687  N N     . ASP B 2 1198 ? 127.338 154.441 78.746  1.00 44.73  ? 1195 ASP A N     1 
ATOM   9688  C CA    . ASP B 2 1198 ? 125.922 154.335 78.429  1.00 44.73  ? 1195 ASP A CA    1 
ATOM   9689  C C     . ASP B 2 1198 ? 125.056 154.078 79.655  1.00 44.73  ? 1195 ASP A C     1 
ATOM   9690  O O     . ASP B 2 1198 ? 123.828 154.162 79.550  1.00 44.73  ? 1195 ASP A O     1 
ATOM   9691  C CB    . ASP B 2 1198 ? 125.706 153.235 77.386  1.00 44.73  ? 1195 ASP A CB    1 
ATOM   9692  C CG    . ASP B 2 1198 ? 126.116 151.857 77.884  1.00 44.73  ? 1195 ASP A CG    1 
ATOM   9693  O OD1   . ASP B 2 1198 ? 126.610 151.744 79.026  1.00 44.73  ? 1195 ASP A OD1   1 
ATOM   9694  O OD2   . ASP B 2 1198 ? 125.941 150.880 77.127  1.00 44.73  ? 1195 ASP A OD2   1 
ATOM   9695  N N     . GLY B 2 1199 ? 125.656 153.770 80.802  1.00 44.73  ? 1196 GLY A N     1 
ATOM   9696  C CA    . GLY B 2 1199 ? 124.895 153.483 81.999  1.00 44.73  ? 1196 GLY A CA    1 
ATOM   9697  C C     . GLY B 2 1199 ? 124.391 152.063 82.114  1.00 44.73  ? 1196 GLY A C     1 
ATOM   9698  O O     . GLY B 2 1199 ? 123.671 151.754 83.070  1.00 44.73  ? 1196 GLY A O     1 
ATOM   9699  N N     . SER B 2 1200 ? 124.743 151.190 81.174  1.00 44.73  ? 1197 SER A N     1 
ATOM   9700  C CA    . SER B 2 1200 ? 124.292 149.810 81.225  1.00 44.73  ? 1197 SER A CA    1 
ATOM   9701  C C     . SER B 2 1200 ? 125.024 149.046 82.326  1.00 44.73  ? 1197 SER A C     1 
ATOM   9702  O O     . SER B 2 1200 ? 126.054 149.483 82.846  1.00 44.73  ? 1197 SER A O     1 
ATOM   9703  C CB    . SER B 2 1200 ? 124.509 149.125 79.876  1.00 44.73  ? 1197 SER A CB    1 
ATOM   9704  O OG    . SER B 2 1200 ? 125.887 149.063 79.552  1.00 44.73  ? 1197 SER A OG    1 
ATOM   9705  N N     . ASN B 2 1201 ? 124.471 147.887 82.678  1.00 44.73  ? 1198 ASN A N     1 
ATOM   9706  C CA    . ASN B 2 1201 ? 125.062 147.061 83.721  1.00 44.73  ? 1198 ASN A CA    1 
ATOM   9707  C C     . ASN B 2 1201 ? 126.446 146.581 83.301  1.00 44.73  ? 1198 ASN A C     1 
ATOM   9708  O O     . ASN B 2 1201 ? 126.694 146.291 82.128  1.00 44.73  ? 1198 ASN A O     1 
ATOM   9709  C CB    . ASN B 2 1201 ? 124.157 145.868 84.026  1.00 44.73  ? 1198 ASN A CB    1 
ATOM   9710  C CG    . ASN B 2 1201 ? 124.413 145.277 85.397  1.00 44.73  ? 1198 ASN A CG    1 
ATOM   9711  O OD1   . ASN B 2 1201 ? 125.328 145.697 86.106  1.00 44.73  ? 1198 ASN A OD1   1 
ATOM   9712  N ND2   . ASN B 2 1201 ? 123.609 144.292 85.776  1.00 44.73  ? 1198 ASN A ND2   1 
ATOM   9713  N N     . ILE B 2 1202 ? 127.352 146.500 84.270  1.00 44.73  ? 1199 ILE A N     1 
ATOM   9714  C CA    . ILE B 2 1202 ? 128.747 146.177 84.007  1.00 44.73  ? 1199 ILE A CA    1 
ATOM   9715  C C     . ILE B 2 1202 ? 129.093 144.760 84.444  1.00 44.73  ? 1199 ILE A C     1 
ATOM   9716  O O     . ILE B 2 1202 ? 129.900 144.091 83.798  1.00 44.73  ? 1199 ILE A O     1 
ATOM   9717  C CB    . ILE B 2 1202 ? 129.661 147.215 84.692  1.00 44.73  ? 1199 ILE A CB    1 
ATOM   9718  C CG1   . ILE B 2 1202 ? 129.417 148.603 84.100  1.00 44.73  ? 1199 ILE A CG1   1 
ATOM   9719  C CG2   . ILE B 2 1202 ? 131.124 146.831 84.556  1.00 44.73  ? 1199 ILE A CG2   1 
ATOM   9720  C CD1   . ILE B 2 1202 ? 130.069 149.722 84.871  1.00 44.73  ? 1199 ILE A CD1   1 
ATOM   9721  N N     . LEU B 2 1203 ? 128.482 144.284 85.528  1.00 44.73  ? 1200 LEU A N     1 
ATOM   9722  C CA    . LEU B 2 1203 ? 128.816 142.958 86.043  1.00 44.73  ? 1200 LEU A CA    1 
ATOM   9723  C C     . LEU B 2 1203 ? 128.580 141.826 85.048  1.00 44.73  ? 1200 LEU A C     1 
ATOM   9724  O O     . LEU B 2 1203 ? 129.458 140.950 84.944  1.00 44.73  ? 1200 LEU A O     1 
ATOM   9725  C CB    . LEU B 2 1203 ? 128.048 142.702 87.347  1.00 44.73  ? 1200 LEU A CB    1 
ATOM   9726  C CG    . LEU B 2 1203 ? 128.449 143.553 88.555  1.00 44.73  ? 1200 LEU A CG    1 
ATOM   9727  C CD1   . LEU B 2 1203 ? 127.776 143.034 89.805  1.00 44.73  ? 1200 LEU A CD1   1 
ATOM   9728  C CD2   . LEU B 2 1203 ? 129.956 143.566 88.722  1.00 44.73  ? 1200 LEU A CD2   1 
ATOM   9729  N N     . PRO B 2 1204 ? 127.451 141.751 84.325  1.00 44.73  ? 1201 PRO A N     1 
ATOM   9730  C CA    . PRO B 2 1204 ? 127.313 140.657 83.344  1.00 44.73  ? 1201 PRO A CA    1 
ATOM   9731  C C     . PRO B 2 1204 ? 128.398 140.658 82.284  1.00 44.73  ? 1201 PRO A C     1 
ATOM   9732  O O     . PRO B 2 1204 ? 128.852 139.585 81.868  1.00 44.73  ? 1201 PRO A O     1 
ATOM   9733  C CB    . PRO B 2 1204 ? 125.927 140.882 82.724  1.00 44.73  ? 1201 PRO A CB    1 
ATOM   9734  C CG    . PRO B 2 1204 ? 125.277 141.942 83.488  1.00 44.73  ? 1201 PRO A CG    1 
ATOM   9735  C CD    . PRO B 2 1204 ? 126.225 142.564 84.448  1.00 44.73  ? 1201 PRO A CD    1 
ATOM   9736  N N     . LYS B 2 1205 ? 128.827 141.835 81.831  1.00 44.73  ? 1202 LYS A N     1 
ATOM   9737  C CA    . LYS B 2 1205 ? 129.874 141.881 80.820  1.00 44.73  ? 1202 LYS A CA    1 
ATOM   9738  C C     . LYS B 2 1205 ? 131.214 141.457 81.406  1.00 44.73  ? 1202 LYS A C     1 
ATOM   9739  O O     . LYS B 2 1205 ? 132.040 140.852 80.713  1.00 44.73  ? 1202 LYS A O     1 
ATOM   9740  C CB    . LYS B 2 1205 ? 129.951 143.279 80.200  1.00 44.73  ? 1202 LYS A CB    1 
ATOM   9741  C CG    . LYS B 2 1205 ? 130.922 143.392 79.035  1.00 44.73  ? 1202 LYS A CG    1 
ATOM   9742  C CD    . LYS B 2 1205 ? 130.992 144.811 78.507  1.00 44.73  ? 1202 LYS A CD    1 
ATOM   9743  C CE    . LYS B 2 1205 ? 129.740 145.172 77.724  1.00 44.73  ? 1202 LYS A CE    1 
ATOM   9744  N NZ    . LYS B 2 1205 ? 129.861 146.519 77.110  1.00 44.73  ? 1202 LYS A NZ    1 
ATOM   9745  N N     . LEU B 2 1206 ? 131.444 141.758 82.686  1.00 44.73  ? 1203 LEU A N     1 
ATOM   9746  C CA    . LEU B 2 1206 ? 132.644 141.273 83.360  1.00 44.73  ? 1203 LEU A CA    1 
ATOM   9747  C C     . LEU B 2 1206 ? 132.681 139.751 83.395  1.00 44.73  ? 1203 LEU A C     1 
ATOM   9748  O O     . LEU B 2 1206 ? 133.738 139.144 83.196  1.00 44.73  ? 1203 LEU A O     1 
ATOM   9749  C CB    . LEU B 2 1206 ? 132.709 141.831 84.782  1.00 44.73  ? 1203 LEU A CB    1 
ATOM   9750  C CG    . LEU B 2 1206 ? 132.894 143.336 84.954  1.00 44.73  ? 1203 LEU A CG    1 
ATOM   9751  C CD1   . LEU B 2 1206 ? 132.791 143.720 86.414  1.00 44.73  ? 1203 LEU A CD1   1 
ATOM   9752  C CD2   . LEU B 2 1206 ? 134.242 143.736 84.415  1.00 44.73  ? 1203 LEU A CD2   1 
ATOM   9753  N N     . LEU B 2 1207 ? 131.534 139.120 83.654  1.00 44.73  ? 1204 LEU A N     1 
ATOM   9754  C CA    . LEU B 2 1207 ? 131.498 137.668 83.795  1.00 44.73  ? 1204 LEU A CA    1 
ATOM   9755  C C     . LEU B 2 1207 ? 131.727 136.966 82.461  1.00 44.73  ? 1204 LEU A C     1 
ATOM   9756  O O     . LEU B 2 1207 ? 132.373 135.913 82.411  1.00 44.73  ? 1204 LEU A O     1 
ATOM   9757  C CB    . LEU B 2 1207 ? 130.164 137.242 84.407  1.00 44.73  ? 1204 LEU A CB    1 
ATOM   9758  C CG    . LEU B 2 1207 ? 130.161 136.988 85.915  1.00 44.73  ? 1204 LEU A CG    1 
ATOM   9759  C CD1   . LEU B 2 1207 ? 130.468 138.266 86.681  1.00 44.73  ? 1204 LEU A CD1   1 
ATOM   9760  C CD2   . LEU B 2 1207 ? 128.828 136.407 86.355  1.00 44.73  ? 1204 LEU A CD2   1 
ATOM   9761  N N     . GLU B 2 1208 ? 131.203 137.529 81.368  1.00 45.31  ? 1205 GLU A N     1 
ATOM   9762  C CA    . GLU B 2 1208 ? 131.253 136.829 80.088  1.00 45.31  ? 1205 GLU A CA    1 
ATOM   9763  C C     . GLU B 2 1208 ? 132.651 136.838 79.479  1.00 45.31  ? 1205 GLU A C     1 
ATOM   9764  O O     . GLU B 2 1208 ? 133.024 135.884 78.785  1.00 45.31  ? 1205 GLU A O     1 
ATOM   9765  C CB    . GLU B 2 1208 ? 130.236 137.434 79.119  1.00 45.31  ? 1205 GLU A CB    1 
ATOM   9766  C CG    . GLU B 2 1208 ? 130.555 138.842 78.656  1.00 45.31  ? 1205 GLU A CG    1 
ATOM   9767  C CD    . GLU B 2 1208 ? 129.402 139.478 77.906  1.00 45.31  ? 1205 GLU A CD    1 
ATOM   9768  O OE1   . GLU B 2 1208 ? 128.309 138.875 77.873  1.00 45.31  ? 1205 GLU A OE1   1 
ATOM   9769  O OE2   . GLU B 2 1208 ? 129.588 140.581 77.350  1.00 45.31  ? 1205 GLU A OE2   1 
ATOM   9770  N N     . ASN B 2 1209 ? 133.436 137.893 79.713  1.00 47.63  ? 1206 ASN A N     1 
ATOM   9771  C CA    . ASN B 2 1209 ? 134.807 137.902 79.212  1.00 47.63  ? 1206 ASN A CA    1 
ATOM   9772  C C     . ASN B 2 1209 ? 135.677 136.907 79.970  1.00 47.63  ? 1206 ASN A C     1 
ATOM   9773  O O     . ASN B 2 1209 ? 136.659 136.392 79.424  1.00 47.63  ? 1206 ASN A O     1 
ATOM   9774  C CB    . ASN B 2 1209 ? 135.396 139.308 79.296  1.00 47.63  ? 1206 ASN A CB    1 
ATOM   9775  C CG    . ASN B 2 1209 ? 134.677 140.294 78.402  1.00 47.63  ? 1206 ASN A CG    1 
ATOM   9776  O OD1   . ASN B 2 1209 ? 134.044 141.235 78.877  1.00 47.63  ? 1206 ASN A OD1   1 
ATOM   9777  N ND2   . ASN B 2 1209 ? 134.775 140.085 77.096  1.00 47.63  ? 1206 ASN A ND2   1 
ATOM   9778  N N     . ASP B 2 1210 ? 135.329 136.628 81.228  1.00 47.27  ? 1207 ASP A N     1 
ATOM   9779  C CA    . ASP B 2 1210 ? 136.020 135.631 82.047  1.00 47.27  ? 1207 ASP A CA    1 
ATOM   9780  C C     . ASP B 2 1210 ? 137.515 135.922 82.150  1.00 47.27  ? 1207 ASP A C     1 
ATOM   9781  O O     . ASP B 2 1210 ? 138.349 135.016 82.092  1.00 47.27  ? 1207 ASP A O     1 
ATOM   9782  C CB    . ASP B 2 1210 ? 135.778 134.216 81.517  1.00 47.27  ? 1207 ASP A CB    1 
ATOM   9783  C CG    . ASP B 2 1210 ? 135.915 133.161 82.596  1.00 47.27  ? 1207 ASP A CG    1 
ATOM   9784  O OD1   . ASP B 2 1210 ? 135.998 133.533 83.785  1.00 47.27  ? 1207 ASP A OD1   1 
ATOM   9785  O OD2   . ASP B 2 1210 ? 135.941 131.960 82.255  1.00 47.27  ? 1207 ASP A OD2   1 
ATOM   9786  N N     . ASP B 2 1211 ? 137.860 137.197 82.303  1.00 50.21  ? 1208 ASP A N     1 
ATOM   9787  C CA    . ASP B 2 1211 ? 139.243 137.601 82.510  1.00 50.21  ? 1208 ASP A CA    1 
ATOM   9788  C C     . ASP B 2 1211 ? 139.593 137.400 83.980  1.00 50.21  ? 1208 ASP A C     1 
ATOM   9789  O O     . ASP B 2 1211 ? 139.007 138.047 84.855  1.00 50.21  ? 1208 ASP A O     1 
ATOM   9790  C CB    . ASP B 2 1211 ? 139.452 139.056 82.095  1.00 50.21  ? 1208 ASP A CB    1 
ATOM   9791  C CG    . ASP B 2 1211 ? 140.916 139.456 82.082  1.00 50.21  ? 1208 ASP A CG    1 
ATOM   9792  O OD1   . ASP B 2 1211 ? 141.780 138.569 82.247  1.00 50.21  ? 1208 ASP A OD1   1 
ATOM   9793  O OD2   . ASP B 2 1211 ? 141.202 140.659 81.908  1.00 50.21  ? 1208 ASP A OD2   1 
ATOM   9794  N N     . SER B 2 1212 ? 140.541 136.500 84.247  1.00 50.54  ? 1209 SER A N     1 
ATOM   9795  C CA    . SER B 2 1212 ? 140.901 136.192 85.628  1.00 50.54  ? 1209 SER A CA    1 
ATOM   9796  C C     . SER B 2 1212 ? 141.478 137.411 86.337  1.00 50.54  ? 1209 SER A C     1 
ATOM   9797  O O     . SER B 2 1212 ? 141.152 137.673 87.501  1.00 50.54  ? 1209 SER A O     1 
ATOM   9798  C CB    . SER B 2 1212 ? 141.893 135.030 85.665  1.00 50.54  ? 1209 SER A CB    1 
ATOM   9799  O OG    . SER B 2 1212 ? 143.149 135.414 85.134  1.00 50.54  ? 1209 SER A OG    1 
ATOM   9800  N N     . HIS B 2 1213 ? 142.342 138.165 85.654  1.00 47.34  ? 1210 HIS A N     1 
ATOM   9801  C CA    . HIS B 2 1213 ? 142.934 139.350 86.268  1.00 47.34  ? 1210 HIS A CA    1 
ATOM   9802  C C     . HIS B 2 1213 ? 141.882 140.417 86.544  1.00 47.34  ? 1210 HIS A C     1 
ATOM   9803  O O     . HIS B 2 1213 ? 141.914 141.074 87.592  1.00 47.34  ? 1210 HIS A O     1 
ATOM   9804  C CB    . HIS B 2 1213 ? 144.041 139.905 85.375  1.00 47.34  ? 1210 HIS A CB    1 
ATOM   9805  C CG    . HIS B 2 1213 ? 144.928 140.897 86.059  1.00 47.34  ? 1210 HIS A CG    1 
ATOM   9806  N ND1   . HIS B 2 1213 ? 145.894 140.527 86.970  1.00 47.34  ? 1210 HIS A ND1   1 
ATOM   9807  C CD2   . HIS B 2 1213 ? 144.995 142.246 85.966  1.00 47.34  ? 1210 HIS A CD2   1 
ATOM   9808  C CE1   . HIS B 2 1213 ? 146.518 141.606 87.408  1.00 47.34  ? 1210 HIS A CE1   1 
ATOM   9809  N NE2   . HIS B 2 1213 ? 145.992 142.662 86.815  1.00 47.34  ? 1210 HIS A NE2   1 
ATOM   9810  N N     . ALA B 2 1214 ? 140.947 140.612 85.611  1.00 44.73  ? 1211 ALA A N     1 
ATOM   9811  C CA    . ALA B 2 1214 ? 139.916 141.629 85.796  1.00 44.73  ? 1211 ALA A CA    1 
ATOM   9812  C C     . ALA B 2 1214 ? 139.002 141.288 86.965  1.00 44.73  ? 1211 ALA A C     1 
ATOM   9813  O O     . ALA B 2 1214 ? 138.598 142.175 87.725  1.00 44.73  ? 1211 ALA A O     1 
ATOM   9814  C CB    . ALA B 2 1214 ? 139.106 141.797 84.512  1.00 44.73  ? 1211 ALA A CB    1 
ATOM   9815  N N     . ILE B 2 1215 ? 138.656 140.008 87.119  1.00 44.73  ? 1212 ILE A N     1 
ATOM   9816  C CA    . ILE B 2 1215 ? 137.795 139.597 88.225  1.00 44.73  ? 1212 ILE A CA    1 
ATOM   9817  C C     . ILE B 2 1215 ? 138.489 139.834 89.559  1.00 44.73  ? 1212 ILE A C     1 
ATOM   9818  O O     . ILE B 2 1215 ? 137.879 140.330 90.515  1.00 44.73  ? 1212 ILE A O     1 
ATOM   9819  C CB    . ILE B 2 1215 ? 137.372 138.126 88.055  1.00 44.73  ? 1212 ILE A CB    1 
ATOM   9820  C CG1   . ILE B 2 1215 ? 136.440 137.978 86.852  1.00 44.73  ? 1212 ILE A CG1   1 
ATOM   9821  C CG2   . ILE B 2 1215 ? 136.698 137.612 89.316  1.00 44.73  ? 1212 ILE A CG2   1 
ATOM   9822  C CD1   . ILE B 2 1215 ? 135.229 138.882 86.903  1.00 44.73  ? 1212 ILE A CD1   1 
ATOM   9823  N N     . ASP B 2 1216 ? 139.775 139.488 89.646  1.00 46.09  ? 1213 ASP A N     1 
ATOM   9824  C CA    . ASP B 2 1216 ? 140.523 139.724 90.877  1.00 46.09  ? 1213 ASP A CA    1 
ATOM   9825  C C     . ASP B 2 1216 ? 140.579 141.210 91.209  1.00 46.09  ? 1213 ASP A C     1 
ATOM   9826  O O     . ASP B 2 1216 ? 140.406 141.602 92.368  1.00 46.09  ? 1213 ASP A O     1 
ATOM   9827  C CB    . ASP B 2 1216 ? 141.933 139.149 90.751  1.00 46.09  ? 1213 ASP A CB    1 
ATOM   9828  C CG    . ASP B 2 1216 ? 142.645 139.051 92.086  1.00 46.09  ? 1213 ASP A CG    1 
ATOM   9829  O OD1   . ASP B 2 1216 ? 142.004 139.307 93.127  1.00 46.09  ? 1213 ASP A OD1   1 
ATOM   9830  O OD2   . ASP B 2 1216 ? 143.849 138.717 92.095  1.00 46.09  ? 1213 ASP A OD2   1 
ATOM   9831  N N     . THR B 2 1217 ? 140.819 142.053 90.202  1.00 45.61  ? 1214 THR A N     1 
ATOM   9832  C CA    . THR B 2 1217 ? 140.827 143.494 90.431  1.00 45.61  ? 1214 THR A CA    1 
ATOM   9833  C C     . THR B 2 1217 ? 139.432 144.000 90.778  1.00 45.61  ? 1214 THR A C     1 
ATOM   9834  O O     . THR B 2 1217 ? 139.281 144.931 91.578  1.00 45.61  ? 1214 THR A O     1 
ATOM   9835  C CB    . THR B 2 1217 ? 141.376 144.219 89.203  1.00 45.61  ? 1214 THR A CB    1 
ATOM   9836  O OG1   . THR B 2 1217 ? 142.651 143.666 88.853  1.00 45.61  ? 1214 THR A OG1   1 
ATOM   9837  C CG2   . THR B 2 1217 ? 141.545 145.702 89.488  1.00 45.61  ? 1214 THR A CG2   1 
ATOM   9838  N N     . MET B 2 1218 ? 138.399 143.396 90.184  1.00 44.73  ? 1215 MET A N     1 
ATOM   9839  C CA    . MET B 2 1218 ? 137.028 143.776 90.510  1.00 44.73  ? 1215 MET A CA    1 
ATOM   9840  C C     . MET B 2 1218 ? 136.709 143.506 91.973  1.00 44.73  ? 1215 MET A C     1 
ATOM   9841  O O     . MET B 2 1218 ? 136.124 144.355 92.656  1.00 44.73  ? 1215 MET A O     1 
ATOM   9842  C CB    . MET B 2 1218 ? 136.049 143.026 89.610  1.00 44.73  ? 1215 MET A CB    1 
ATOM   9843  C CG    . MET B 2 1218 ? 134.690 143.681 89.500  1.00 44.73  ? 1215 MET A CG    1 
ATOM   9844  S SD    . MET B 2 1218 ? 134.807 145.453 89.239  1.00 44.73  ? 1215 MET A SD    1 
ATOM   9845  C CE    . MET B 2 1218 ? 133.090 145.931 89.389  1.00 44.73  ? 1215 MET A CE    1 
ATOM   9846  N N     . VAL B 2 1219 ? 137.081 142.327 92.472  1.00 44.73  ? 1216 VAL A N     1 
ATOM   9847  C CA    . VAL B 2 1219 ? 136.816 142.000 93.868  1.00 44.73  ? 1216 VAL A CA    1 
ATOM   9848  C C     . VAL B 2 1219 ? 137.707 142.824 94.787  1.00 44.73  ? 1216 VAL A C     1 
ATOM   9849  O O     . VAL B 2 1219 ? 137.258 143.320 95.828  1.00 44.73  ? 1216 VAL A O     1 
ATOM   9850  C CB    . VAL B 2 1219 ? 136.991 140.490 94.102  1.00 44.73  ? 1216 VAL A CB    1 
ATOM   9851  C CG1   . VAL B 2 1219 ? 137.083 140.189 95.584  1.00 44.73  ? 1216 VAL A CG1   1 
ATOM   9852  C CG2   . VAL B 2 1219 ? 135.839 139.725 93.472  1.00 44.73  ? 1216 VAL A CG2   1 
ATOM   9853  N N     . ALA B 2 1220 ? 138.977 142.997 94.413  1.00 44.73  ? 1217 ALA A N     1 
ATOM   9854  C CA    . ALA B 2 1220 ? 139.903 143.746 95.256  1.00 44.73  ? 1217 ALA A CA    1 
ATOM   9855  C C     . ALA B 2 1220 ? 139.459 145.193 95.423  1.00 44.73  ? 1217 ALA A C     1 
ATOM   9856  O O     . ALA B 2 1220 ? 139.763 145.831 96.437  1.00 44.73  ? 1217 ALA A O     1 
ATOM   9857  C CB    . ALA B 2 1220 ? 141.315 143.683 94.673  1.00 44.73  ? 1217 ALA A CB    1 
ATOM   9858  N N     . LEU B 2 1221 ? 138.750 145.736 94.432  1.00 44.73  ? 1218 LEU A N     1 
ATOM   9859  C CA    . LEU B 2 1221 ? 138.246 147.097 94.562  1.00 44.73  ? 1218 LEU A CA    1 
ATOM   9860  C C     . LEU B 2 1221 ? 137.018 147.145 95.462  1.00 44.73  ? 1218 LEU A C     1 
ATOM   9861  O O     . LEU B 2 1221 ? 136.795 148.137 96.165  1.00 44.73  ? 1218 LEU A O     1 
ATOM   9862  C CB    . LEU B 2 1221 ? 137.944 147.678 93.183  1.00 44.73  ? 1218 LEU A CB    1 
ATOM   9863  C CG    . LEU B 2 1221 ? 139.170 148.269 92.484  1.00 44.73  ? 1218 LEU A CG    1 
ATOM   9864  C CD1   . LEU B 2 1221 ? 138.763 149.116 91.297  1.00 44.73  ? 1218 LEU A CD1   1 
ATOM   9865  C CD2   . LEU B 2 1221 ? 140.010 149.082 93.458  1.00 44.73  ? 1218 LEU A CD2   1 
ATOM   9866  N N     . ILE B 2 1222 ? 136.208 146.085 95.452  1.00 44.73  ? 1219 ILE A N     1 
ATOM   9867  C CA    . ILE B 2 1222 ? 135.111 145.981 96.409  1.00 44.73  ? 1219 ILE A CA    1 
ATOM   9868  C C     . ILE B 2 1222 ? 135.660 145.833 97.823  1.00 44.73  ? 1219 ILE A C     1 
ATOM   9869  O O     . ILE B 2 1222 ? 135.076 146.337 98.790  1.00 44.73  ? 1219 ILE A O     1 
ATOM   9870  C CB    . ILE B 2 1222 ? 134.176 144.819 96.027  1.00 44.73  ? 1219 ILE A CB    1 
ATOM   9871  C CG1   . ILE B 2 1222 ? 133.493 145.111 94.692  1.00 44.73  ? 1219 ILE A CG1   1 
ATOM   9872  C CG2   . ILE B 2 1222 ? 133.133 144.582 97.104  1.00 44.73  ? 1219 ILE A CG2   1 
ATOM   9873  C CD1   . ILE B 2 1222 ? 132.727 143.937 94.132  1.00 44.73  ? 1219 ILE A CD1   1 
ATOM   9874  N N     . ARG B 2 1223 ? 136.792 145.136 97.963  1.00 44.73  ? 1220 ARG A N     1 
ATOM   9875  C CA    . ARG B 2 1223 ? 137.508 145.108 99.235  1.00 44.73  ? 1220 ARG A CA    1 
ATOM   9876  C C     . ARG B 2 1223 ? 137.756 146.518 99.749  1.00 44.73  ? 1220 ARG A C     1 
ATOM   9877  O O     . ARG B 2 1223 ? 137.494 146.830 100.916 1.00 44.73  ? 1220 ARG A O     1 
ATOM   9878  C CB    . ARG B 2 1223 ? 138.849 144.387 99.068  1.00 44.73  ? 1220 ARG A CB    1 
ATOM   9879  C CG    . ARG B 2 1223 ? 138.782 142.949 98.605  1.00 44.73  ? 1220 ARG A CG    1 
ATOM   9880  C CD    . ARG B 2 1223 ? 138.265 142.051 99.694  1.00 44.73  ? 1220 ARG A CD    1 
ATOM   9881  N NE    . ARG B 2 1223 ? 139.106 142.094 100.884 1.00 44.73  ? 1220 ARG A NE    1 
ATOM   9882  C CZ    . ARG B 2 1223 ? 140.176 141.335 101.073 1.00 44.73  ? 1220 ARG A CZ    1 
ATOM   9883  N NH1   . ARG B 2 1223 ? 140.569 140.457 100.165 1.00 44.73  ? 1220 ARG A NH1   1 
ATOM   9884  N NH2   . ARG B 2 1223 ? 140.870 141.460 102.201 1.00 44.73  ? 1220 ARG A NH2   1 
ATOM   9885  N N     . SER B 2 1224 ? 138.267 147.386 98.876  1.00 44.73  ? 1221 SER A N     1 
ATOM   9886  C CA    . SER B 2 1224 ? 138.710 148.708 99.299  1.00 44.73  ? 1221 SER A CA    1 
ATOM   9887  C C     . SER B 2 1224 ? 137.534 149.621 99.624  1.00 44.73  ? 1221 SER A C     1 
ATOM   9888  O O     . SER B 2 1224 ? 137.571 150.357 100.617 1.00 44.73  ? 1221 SER A O     1 
ATOM   9889  C CB    . SER B 2 1224 ? 139.587 149.322 98.210  1.00 44.73  ? 1221 SER A CB    1 
ATOM   9890  O OG    . SER B 2 1224 ? 140.113 150.570 98.614  1.00 44.73  ? 1221 SER A OG    1 
ATOM   9891  N N     . VAL B 2 1225 ? 136.484 149.594 98.800  1.00 44.73  ? 1222 VAL A N     1 
ATOM   9892  C CA    . VAL B 2 1225 ? 135.371 150.519 98.994  1.00 44.73  ? 1222 VAL A CA    1 
ATOM   9893  C C     . VAL B 2 1225 ? 134.590 150.173 100.257 1.00 44.73  ? 1222 VAL A C     1 
ATOM   9894  O O     . VAL B 2 1225 ? 134.126 151.067 100.976 1.00 44.73  ? 1222 VAL A O     1 
ATOM   9895  C CB    . VAL B 2 1225 ? 134.475 150.553 97.741  1.00 44.73  ? 1222 VAL A CB    1 
ATOM   9896  C CG1   . VAL B 2 1225 ? 133.824 149.208 97.490  1.00 44.73  ? 1222 VAL A CG1   1 
ATOM   9897  C CG2   . VAL B 2 1225 ? 133.422 151.640 97.875  1.00 44.73  ? 1222 VAL A CG2   1 
ATOM   9898  N N     . LEU B 2 1226 ? 134.436 148.882 100.558 1.00 44.73  ? 1223 LEU A N     1 
ATOM   9899  C CA    . LEU B 2 1226 ? 133.753 148.489 101.785 1.00 44.73  ? 1223 LEU A CA    1 
ATOM   9900  C C     . LEU B 2 1226 ? 134.588 148.747 103.030 1.00 44.73  ? 1223 LEU A C     1 
ATOM   9901  O O     . LEU B 2 1226 ? 134.059 148.633 104.141 1.00 44.73  ? 1223 LEU A O     1 
ATOM   9902  C CB    . LEU B 2 1226 ? 133.351 147.013 101.734 1.00 44.73  ? 1223 LEU A CB    1 
ATOM   9903  C CG    . LEU B 2 1226 ? 132.034 146.617 101.056 1.00 44.73  ? 1223 LEU A CG    1 
ATOM   9904  C CD1   . LEU B 2 1226 ? 130.860 147.212 101.808 1.00 44.73  ? 1223 LEU A CD1   1 
ATOM   9905  C CD2   . LEU B 2 1226 ? 131.982 147.018 99.597  1.00 44.73  ? 1223 LEU A CD2   1 
ATOM   9906  N N     . GLN B 2 1227 ? 135.864 149.087 102.878 1.00 44.73  ? 1224 GLN A N     1 
ATOM   9907  C CA    . GLN B 2 1227 ? 136.728 149.386 104.011 1.00 44.73  ? 1224 GLN A CA    1 
ATOM   9908  C C     . GLN B 2 1227 ? 136.575 150.858 104.372 1.00 44.73  ? 1224 GLN A C     1 
ATOM   9909  O O     . GLN B 2 1227 ? 137.104 151.732 103.677 1.00 44.73  ? 1224 GLN A O     1 
ATOM   9910  C CB    . GLN B 2 1227 ? 138.181 149.047 103.681 1.00 44.73  ? 1224 GLN A CB    1 
ATOM   9911  C CG    . GLN B 2 1227 ? 139.199 149.562 104.682 1.00 44.73  ? 1224 GLN A CG    1 
ATOM   9912  C CD    . GLN B 2 1227 ? 140.624 149.311 104.235 1.00 44.73  ? 1224 GLN A CD    1 
ATOM   9913  O OE1   . GLN B 2 1227 ? 140.868 148.531 103.316 1.00 44.73  ? 1224 GLN A OE1   1 
ATOM   9914  N NE2   . GLN B 2 1227 ? 141.574 149.971 104.884 1.00 44.73  ? 1224 GLN A NE2   1 
ATOM   9915  N N     . MET B 2 1228 ? 135.844 151.129 105.452 1.00 44.73  ? 1225 MET A N     1 
ATOM   9916  C CA    . MET B 2 1228 ? 135.583 152.497 105.885 1.00 44.73  ? 1225 MET A CA    1 
ATOM   9917  C C     . MET B 2 1228 ? 136.744 153.055 106.702 1.00 44.73  ? 1225 MET A C     1 
ATOM   9918  O O     . MET B 2 1228 ? 137.216 154.167 106.445 1.00 44.73  ? 1225 MET A O     1 
ATOM   9919  C CB    . MET B 2 1228 ? 134.283 152.552 106.696 1.00 44.73  ? 1225 MET A CB    1 
ATOM   9920  C CG    . MET B 2 1228 ? 133.057 152.080 105.944 1.00 44.73  ? 1225 MET A CG    1 
ATOM   9921  S SD    . MET B 2 1228 ? 131.735 151.539 107.040 1.00 44.73  ? 1225 MET A SD    1 
ATOM   9922  C CE    . MET B 2 1228 ? 131.897 149.762 106.908 1.00 44.73  ? 1225 MET A CE    1 
ATOM   9923  N N     . ARG B 2 1229 ? 137.213 152.293 107.684 1.00 44.73  ? 1226 ARG A N     1 
ATOM   9924  C CA    . ARG B 2 1229 ? 138.272 152.748 108.579 1.00 44.73  ? 1226 ARG A CA    1 
ATOM   9925  C C     . ARG B 2 1229 ? 139.597 152.724 107.831 1.00 44.73  ? 1226 ARG A C     1 
ATOM   9926  O O     . ARG B 2 1229 ? 140.240 151.679 107.712 1.00 44.73  ? 1226 ARG A O     1 
ATOM   9927  C CB    . ARG B 2 1229 ? 138.325 151.870 109.823 1.00 44.73  ? 1226 ARG A CB    1 
ATOM   9928  C CG    . ARG B 2 1229 ? 139.151 152.448 110.957 1.00 44.73  ? 1226 ARG A CG    1 
ATOM   9929  C CD    . ARG B 2 1229 ? 138.634 151.976 112.307 1.00 44.73  ? 1226 ARG A CD    1 
ATOM   9930  N NE    . ARG B 2 1229 ? 139.239 152.698 113.420 1.00 44.73  ? 1226 ARG A NE    1 
ATOM   9931  C CZ    . ARG B 2 1229 ? 140.506 152.583 113.794 1.00 44.73  ? 1226 ARG A CZ    1 
ATOM   9932  N NH1   . ARG B 2 1229 ? 141.339 151.764 113.174 1.00 44.73  ? 1226 ARG A NH1   1 
ATOM   9933  N NH2   . ARG B 2 1229 ? 140.947 153.306 114.819 1.00 44.73  ? 1226 ARG A NH2   1 
ATOM   9934  N N     . ASN B 2 1230 ? 140.011 153.880 107.323 1.00 44.73  ? 1227 ASN A N     1 
ATOM   9935  C CA    . ASN B 2 1230 ? 141.278 154.021 106.618 1.00 44.73  ? 1227 ASN A CA    1 
ATOM   9936  C C     . ASN B 2 1230 ? 142.253 154.777 107.510 1.00 44.73  ? 1227 ASN A C     1 
ATOM   9937  O O     . ASN B 2 1230 ? 141.977 155.910 107.917 1.00 44.73  ? 1227 ASN A O     1 
ATOM   9938  C CB    . ASN B 2 1230 ? 141.082 154.750 105.291 1.00 44.73  ? 1227 ASN A CB    1 
ATOM   9939  C CG    . ASN B 2 1230 ? 140.131 154.024 104.368 1.00 44.73  ? 1227 ASN A CG    1 
ATOM   9940  O OD1   . ASN B 2 1230 ? 140.553 153.279 103.484 1.00 44.73  ? 1227 ASN A OD1   1 
ATOM   9941  N ND2   . ASN B 2 1230 ? 138.836 154.235 104.568 1.00 44.73  ? 1227 ASN A ND2   1 
ATOM   9942  N N     . SER B 2 1231 ? 143.388 154.152 107.809 1.00 44.73  ? 1228 SER A N     1 
ATOM   9943  C CA    . SER B 2 1231 ? 144.378 154.705 108.720 1.00 44.73  ? 1228 SER A CA    1 
ATOM   9944  C C     . SER B 2 1231 ? 145.742 154.710 108.047 1.00 44.73  ? 1228 SER A C     1 
ATOM   9945  O O     . SER B 2 1231 ? 146.006 153.885 107.168 1.00 44.73  ? 1228 SER A O     1 
ATOM   9946  C CB    . SER B 2 1231 ? 144.434 153.903 110.023 1.00 44.73  ? 1228 SER A CB    1 
ATOM   9947  O OG    . SER B 2 1231 ? 144.909 152.589 109.792 1.00 44.73  ? 1228 SER A OG    1 
ATOM   9948  N N     . ASN B 2 1232 ? 146.594 155.650 108.451 1.00 44.73  ? 1229 ASN A N     1 
ATOM   9949  C CA    . ASN B 2 1232 ? 147.971 155.735 107.963 1.00 44.73  ? 1229 ASN A CA    1 
ATOM   9950  C C     . ASN B 2 1232 ? 148.774 156.481 109.025 1.00 44.73  ? 1229 ASN A C     1 
ATOM   9951  O O     . ASN B 2 1232 ? 148.646 157.701 109.164 1.00 44.73  ? 1229 ASN A O     1 
ATOM   9952  C CB    . ASN B 2 1232 ? 148.043 156.435 106.612 1.00 44.73  ? 1229 ASN A CB    1 
ATOM   9953  C CG    . ASN B 2 1232 ? 149.407 156.313 105.964 1.00 44.73  ? 1229 ASN A CG    1 
ATOM   9954  O OD1   . ASN B 2 1232 ? 150.324 155.716 106.526 1.00 44.73  ? 1229 ASN A OD1   1 
ATOM   9955  N ND2   . ASN B 2 1232 ? 149.547 156.880 104.772 1.00 44.73  ? 1229 ASN A ND2   1 
ATOM   9956  N N     . ALA B 2 1233 ? 149.592 155.741 109.777 1.00 44.73  ? 1230 ALA A N     1 
ATOM   9957  C CA    . ALA B 2 1233 ? 150.328 156.342 110.885 1.00 44.73  ? 1230 ALA A CA    1 
ATOM   9958  C C     . ALA B 2 1233 ? 151.341 157.370 110.397 1.00 44.73  ? 1230 ALA A C     1 
ATOM   9959  O O     . ALA B 2 1233 ? 151.508 158.428 111.015 1.00 44.73  ? 1230 ALA A O     1 
ATOM   9960  C CB    . ALA B 2 1233 ? 151.021 155.254 111.705 1.00 44.73  ? 1230 ALA A CB    1 
ATOM   9961  N N     . ALA B 2 1234 ? 152.035 157.074 109.296 1.00 46.60  ? 1231 ALA A N     1 
ATOM   9962  C CA    . ALA B 2 1234 ? 153.094 157.962 108.827 1.00 46.60  ? 1231 ALA A CA    1 
ATOM   9963  C C     . ALA B 2 1234 ? 152.546 159.318 108.400 1.00 46.60  ? 1231 ALA A C     1 
ATOM   9964  O O     . ALA B 2 1234 ? 153.126 160.360 108.726 1.00 46.60  ? 1231 ALA A O     1 
ATOM   9965  C CB    . ALA B 2 1234 ? 153.856 157.305 107.676 1.00 46.60  ? 1231 ALA A CB    1 
ATOM   9966  N N     . THR B 2 1235 ? 151.432 159.328 107.673 1.00 44.89  ? 1232 THR A N     1 
ATOM   9967  C CA    . THR B 2 1235 ? 150.864 160.563 107.150 1.00 44.89  ? 1232 THR A CA    1 
ATOM   9968  C C     . THR B 2 1235 ? 149.822 161.182 108.072 1.00 44.89  ? 1232 THR A C     1 
ATOM   9969  O O     . THR B 2 1235 ? 149.304 162.259 107.760 1.00 44.89  ? 1232 THR A O     1 
ATOM   9970  C CB    . THR B 2 1235 ? 150.244 160.318 105.771 1.00 44.89  ? 1232 THR A CB    1 
ATOM   9971  O OG1   . THR B 2 1235 ? 149.148 159.403 105.893 1.00 44.89  ? 1232 THR A OG1   1 
ATOM   9972  C CG2   . THR B 2 1235 ? 151.280 159.737 104.822 1.00 44.89  ? 1232 THR A CG2   1 
ATOM   9973  N N     . GLY B 2 1236 ? 149.506 160.538 109.190 1.00 44.73  ? 1233 GLY A N     1 
ATOM   9974  C CA    . GLY B 2 1236 ? 148.552 161.093 110.135 1.00 44.73  ? 1233 GLY A CA    1 
ATOM   9975  C C     . GLY B 2 1236 ? 147.132 161.199 109.624 1.00 44.73  ? 1233 GLY A C     1 
ATOM   9976  O O     . GLY B 2 1236 ? 146.475 162.226 109.839 1.00 44.73  ? 1233 GLY A O     1 
ATOM   9977  N N     . GLU B 2 1237 ? 146.638 160.164 108.948 1.00 44.73  ? 1234 GLU A N     1 
ATOM   9978  C CA    . GLU B 2 1237 ? 145.263 160.116 108.468 1.00 44.73  ? 1234 GLU A CA    1 
ATOM   9979  C C     . GLU B 2 1237 ? 144.558 158.943 109.131 1.00 44.73  ? 1234 GLU A C     1 
ATOM   9980  O O     . GLU B 2 1237 ? 145.034 157.806 109.053 1.00 44.73  ? 1234 GLU A O     1 
ATOM   9981  C CB    . GLU B 2 1237 ? 145.212 159.981 106.945 1.00 44.73  ? 1234 GLU A CB    1 
ATOM   9982  C CG    . GLU B 2 1237 ? 145.725 161.197 106.194 1.00 44.73  ? 1234 GLU A CG    1 
ATOM   9983  C CD    . GLU B 2 1237 ? 145.675 161.015 104.690 1.00 44.73  ? 1234 GLU A CD    1 
ATOM   9984  O OE1   . GLU B 2 1237 ? 145.357 159.896 104.236 1.00 44.73  ? 1234 GLU A OE1   1 
ATOM   9985  O OE2   . GLU B 2 1237 ? 145.952 161.992 103.962 1.00 44.73  ? 1234 GLU A OE2   1 
ATOM   9986  N N     . ASP B 2 1238 ? 143.435 159.221 109.787 1.00 44.73  ? 1235 ASP A N     1 
ATOM   9987  C CA    . ASP B 2 1238 ? 142.633 158.195 110.447 1.00 44.73  ? 1235 ASP A CA    1 
ATOM   9988  C C     . ASP B 2 1238 ? 141.153 158.457 110.194 1.00 44.73  ? 1235 ASP A C     1 
ATOM   9989  O O     . ASP B 2 1238 ? 140.322 158.414 111.101 1.00 44.73  ? 1235 ASP A O     1 
ATOM   9990  C CB    . ASP B 2 1238 ? 142.937 158.138 111.942 1.00 44.73  ? 1235 ASP A CB    1 
ATOM   9991  C CG    . ASP B 2 1238 ? 142.667 156.771 112.539 1.00 44.73  ? 1235 ASP A CG    1 
ATOM   9992  O OD1   . ASP B 2 1238 ? 142.364 155.835 111.770 1.00 44.73  ? 1235 ASP A OD1   1 
ATOM   9993  O OD2   . ASP B 2 1238 ? 142.756 156.632 113.777 1.00 44.73  ? 1235 ASP A OD2   1 
ATOM   9994  N N     . TYR B 2 1239 ? 140.813 158.749 108.944 1.00 44.73  ? 1236 TYR A N     1 
ATOM   9995  C CA    . TYR B 2 1239 ? 139.447 159.096 108.587 1.00 44.73  ? 1236 TYR A CA    1 
ATOM   9996  C C     . TYR B 2 1239 ? 138.610 157.847 108.332 1.00 44.73  ? 1236 TYR A C     1 
ATOM   9997  O O     . TYR B 2 1239 ? 139.127 156.741 108.155 1.00 44.73  ? 1236 TYR A O     1 
ATOM   9998  C CB    . TYR B 2 1239 ? 139.426 159.991 107.350 1.00 44.73  ? 1236 TYR A CB    1 
ATOM   9999  C CG    . TYR B 2 1239 ? 139.947 159.318 106.102 1.00 44.73  ? 1236 TYR A CG    1 
ATOM   10000 C CD1   . TYR B 2 1239 ? 141.309 159.189 105.879 1.00 44.73  ? 1236 TYR A CD1   1 
ATOM   10001 C CD2   . TYR B 2 1239 ? 139.077 158.809 105.150 1.00 44.73  ? 1236 TYR A CD2   1 
ATOM   10002 C CE1   . TYR B 2 1239 ? 141.790 158.573 104.744 1.00 44.73  ? 1236 TYR A CE1   1 
ATOM   10003 C CE2   . TYR B 2 1239 ? 139.549 158.191 104.011 1.00 44.73  ? 1236 TYR A CE2   1 
ATOM   10004 C CZ    . TYR B 2 1239 ? 140.907 158.077 103.814 1.00 44.73  ? 1236 TYR A CZ    1 
ATOM   10005 O OH    . TYR B 2 1239 ? 141.388 157.464 102.683 1.00 44.73  ? 1236 TYR A OH    1 
ATOM   10006 N N     . ILE B 2 1240 ? 137.294 158.041 108.312 1.00 44.73  ? 1237 ILE A N     1 
ATOM   10007 C CA    . ILE B 2 1240 ? 136.339 156.989 107.984 1.00 44.73  ? 1237 ILE A CA    1 
ATOM   10008 C C     . ILE B 2 1240 ? 135.413 157.499 106.887 1.00 44.73  ? 1237 ILE A C     1 
ATOM   10009 O O     . ILE B 2 1240 ? 134.914 158.628 106.959 1.00 44.73  ? 1237 ILE A O     1 
ATOM   10010 C CB    . ILE B 2 1240 ? 135.554 156.520 109.225 1.00 44.73  ? 1237 ILE A CB    1 
ATOM   10011 C CG1   . ILE B 2 1240 ? 134.702 155.302 108.881 1.00 44.73  ? 1237 ILE A CG1   1 
ATOM   10012 C CG2   . ILE B 2 1240 ? 134.717 157.637 109.820 1.00 44.73  ? 1237 ILE A CG2   1 
ATOM   10013 C CD1   . ILE B 2 1240 ? 134.188 154.563 110.083 1.00 44.73  ? 1237 ILE A CD1   1 
ATOM   10014 N N     . ASN B 2 1241 ? 135.217 156.680 105.856 1.00 44.73  ? 1238 ASN A N     1 
ATOM   10015 C CA    . ASN B 2 1241 ? 134.440 157.048 104.679 1.00 44.73  ? 1238 ASN A CA    1 
ATOM   10016 C C     . ASN B 2 1241 ? 133.325 156.034 104.476 1.00 44.73  ? 1238 ASN A C     1 
ATOM   10017 O O     . ASN B 2 1241 ? 133.586 154.831 104.373 1.00 44.73  ? 1238 ASN A O     1 
ATOM   10018 C CB    . ASN B 2 1241 ? 135.329 157.114 103.437 1.00 44.73  ? 1238 ASN A CB    1 
ATOM   10019 C CG    . ASN B 2 1241 ? 134.917 158.214 102.484 1.00 44.73  ? 1238 ASN A CG    1 
ATOM   10020 O OD1   . ASN B 2 1241 ? 135.726 159.061 102.108 1.00 44.73  ? 1238 ASN A OD1   1 
ATOM   10021 N ND2   . ASN B 2 1241 ? 133.649 158.214 102.095 1.00 44.73  ? 1238 ASN A ND2   1 
ATOM   10022 N N     . SER B 2 1242 ? 132.090 156.520 104.410 1.00 44.73  ? 1239 SER A N     1 
ATOM   10023 C CA    . SER B 2 1242 ? 130.956 155.641 104.194 1.00 44.73  ? 1239 SER A CA    1 
ATOM   10024 C C     . SER B 2 1242 ? 130.927 155.147 102.749 1.00 44.73  ? 1239 SER A C     1 
ATOM   10025 O O     . SER B 2 1242 ? 131.220 155.902 101.819 1.00 44.73  ? 1239 SER A O     1 
ATOM   10026 C CB    . SER B 2 1242 ? 129.654 156.365 104.511 1.00 44.73  ? 1239 SER A CB    1 
ATOM   10027 O OG    . SER B 2 1242 ? 128.534 155.617 104.069 1.00 44.73  ? 1239 SER A OG    1 
ATOM   10028 N N     . PRO B 2 1243 ? 130.576 153.882 102.534 1.00 44.73  ? 1240 PRO A N     1 
ATOM   10029 C CA    . PRO B 2 1243 ? 130.454 153.377 101.163 1.00 44.73  ? 1240 PRO A CA    1 
ATOM   10030 C C     . PRO B 2 1243 ? 129.046 153.527 100.610 1.00 44.73  ? 1240 PRO A C     1 
ATOM   10031 O O     . PRO B 2 1243 ? 128.826 153.356 99.407  1.00 44.73  ? 1240 PRO A O     1 
ATOM   10032 C CB    . PRO B 2 1243 ? 130.846 151.905 101.305 1.00 44.73  ? 1240 PRO A CB    1 
ATOM   10033 C CG    . PRO B 2 1243 ? 130.399 151.548 102.681 1.00 44.73  ? 1240 PRO A CG    1 
ATOM   10034 C CD    . PRO B 2 1243 ? 130.480 152.800 103.529 1.00 44.73  ? 1240 PRO A CD    1 
ATOM   10035 N N     . VAL B 2 1244 ? 128.086 153.844 101.474 1.00 44.73  ? 1241 VAL A N     1 
ATOM   10036 C CA    . VAL B 2 1244 ? 126.680 153.894 101.095 1.00 44.73  ? 1241 VAL A CA    1 
ATOM   10037 C C     . VAL B 2 1244 ? 126.119 155.269 101.430 1.00 44.73  ? 1241 VAL A C     1 
ATOM   10038 O O     . VAL B 2 1244 ? 126.556 155.934 102.376 1.00 44.73  ? 1241 VAL A O     1 
ATOM   10039 C CB    . VAL B 2 1244 ? 125.871 152.774 101.787 1.00 44.73  ? 1241 VAL A CB    1 
ATOM   10040 C CG1   . VAL B 2 1244 ? 125.761 153.034 103.275 1.00 44.73  ? 1241 VAL A CG1   1 
ATOM   10041 C CG2   . VAL B 2 1244 ? 124.494 152.627 101.155 1.00 44.73  ? 1241 VAL A CG2   1 
ATOM   10042 N N     . ARG B 2 1245 ? 125.151 155.701 100.626 1.00 44.73  ? 1242 ARG A N     1 
ATOM   10043 C CA    . ARG B 2 1245 ? 124.548 157.014 100.785 1.00 44.73  ? 1242 ARG A CA    1 
ATOM   10044 C C     . ARG B 2 1245 ? 123.548 157.015 101.939 1.00 44.73  ? 1242 ARG A C     1 
ATOM   10045 O O     . ARG B 2 1245 ? 122.945 155.993 102.280 1.00 44.73  ? 1242 ARG A O     1 
ATOM   10046 C CB    . ARG B 2 1245 ? 123.858 157.437 99.489  1.00 44.73  ? 1242 ARG A CB    1 
ATOM   10047 C CG    . ARG B 2 1245 ? 124.706 158.321 98.592  1.00 44.73  ? 1242 ARG A CG    1 
ATOM   10048 C CD    . ARG B 2 1245 ? 124.335 158.130 97.131  1.00 44.73  ? 1242 ARG A CD    1 
ATOM   10049 N NE    . ARG B 2 1245 ? 125.145 158.957 96.245  1.00 44.73  ? 1242 ARG A NE    1 
ATOM   10050 C CZ    . ARG B 2 1245 ? 124.831 160.193 95.880  1.00 44.73  ? 1242 ARG A CZ    1 
ATOM   10051 N NH1   . ARG B 2 1245 ? 123.725 160.779 96.307  1.00 44.73  ? 1242 ARG A NH1   1 
ATOM   10052 N NH2   . ARG B 2 1245 ? 125.647 160.856 95.066  1.00 44.73  ? 1242 ARG A NH2   1 
ATOM   10053 N N     . ASP B 2 1246 ? 123.375 158.188 102.543 1.00 44.73  ? 1243 ASP A N     1 
ATOM   10054 C CA    . ASP B 2 1246 ? 122.428 158.360 103.636 1.00 44.73  ? 1243 ASP A CA    1 
ATOM   10055 C C     . ASP B 2 1246 ? 121.060 158.748 103.076 1.00 44.73  ? 1243 ASP A C     1 
ATOM   10056 O O     . ASP B 2 1246 ? 120.821 158.708 101.866 1.00 44.73  ? 1243 ASP A O     1 
ATOM   10057 C CB    . ASP B 2 1246 ? 122.963 159.378 104.642 1.00 44.73  ? 1243 ASP A CB    1 
ATOM   10058 C CG    . ASP B 2 1246 ? 123.139 160.767 104.046 1.00 44.73  ? 1243 ASP A CG    1 
ATOM   10059 O OD1   . ASP B 2 1246 ? 122.889 160.950 102.836 1.00 44.73  ? 1243 ASP A OD1   1 
ATOM   10060 O OD2   . ASP B 2 1246 ? 123.532 161.683 104.798 1.00 44.73  ? 1243 ASP A OD2   1 
ATOM   10061 N N     . LEU B 2 1247 ? 120.136 159.130 103.962 1.00 44.73  ? 1244 LEU A N     1 
ATOM   10062 C CA    . LEU B 2 1247 ? 118.806 159.524 103.508 1.00 44.73  ? 1244 LEU A CA    1 
ATOM   10063 C C     . LEU B 2 1247 ? 118.827 160.890 102.829 1.00 44.73  ? 1244 LEU A C     1 
ATOM   10064 O O     . LEU B 2 1247 ? 118.032 161.136 101.916 1.00 44.73  ? 1244 LEU A O     1 
ATOM   10065 C CB    . LEU B 2 1247 ? 117.821 159.492 104.681 1.00 44.73  ? 1244 LEU A CB    1 
ATOM   10066 C CG    . LEU B 2 1247 ? 118.000 160.381 105.916 1.00 44.73  ? 1244 LEU A CG    1 
ATOM   10067 C CD1   . LEU B 2 1247 ? 117.438 161.778 105.700 1.00 44.73  ? 1244 LEU A CD1   1 
ATOM   10068 C CD2   . LEU B 2 1247 ? 117.369 159.734 107.138 1.00 44.73  ? 1244 LEU A CD2   1 
ATOM   10069 N N     . ASN B 2 1248 ? 119.717 161.789 103.261 1.00 44.73  ? 1245 ASN A N     1 
ATOM   10070 C CA    . ASN B 2 1248 ? 119.934 163.025 102.514 1.00 44.73  ? 1245 ASN A CA    1 
ATOM   10071 C C     . ASN B 2 1248 ? 120.475 162.734 101.121 1.00 44.73  ? 1245 ASN A C     1 
ATOM   10072 O O     . ASN B 2 1248 ? 120.048 163.349 100.138 1.00 44.73  ? 1245 ASN A O     1 
ATOM   10073 C CB    . ASN B 2 1248 ? 120.891 163.948 103.270 1.00 44.73  ? 1245 ASN A CB    1 
ATOM   10074 C CG    . ASN B 2 1248 ? 120.223 164.673 104.421 1.00 44.73  ? 1245 ASN A CG    1 
ATOM   10075 O OD1   . ASN B 2 1248 ? 119.248 164.192 104.992 1.00 44.73  ? 1245 ASN A OD1   1 
ATOM   10076 N ND2   . ASN B 2 1248 ? 120.750 165.842 104.767 1.00 44.73  ? 1245 ASN A ND2   1 
ATOM   10077 N N     . GLY B 2 1249 ? 121.418 161.800 101.019 1.00 44.73  ? 1246 GLY A N     1 
ATOM   10078 C CA    . GLY B 2 1249 ? 121.985 161.433 99.738  1.00 44.73  ? 1246 GLY A CA    1 
ATOM   10079 C C     . GLY B 2 1249 ? 123.453 161.778 99.613  1.00 44.73  ? 1246 GLY A C     1 
ATOM   10080 O O     . GLY B 2 1249 ? 123.966 161.939 98.502  1.00 44.73  ? 1246 GLY A O     1 
ATOM   10081 N N     . VAL B 2 1250 ? 124.142 161.895 100.746 1.00 44.73  ? 1247 VAL A N     1 
ATOM   10082 C CA    . VAL B 2 1250 ? 125.562 162.225 100.775 1.00 44.73  ? 1247 VAL A CA    1 
ATOM   10083 C C     . VAL B 2 1250 ? 126.293 161.157 101.577 1.00 44.73  ? 1247 VAL A C     1 
ATOM   10084 O O     . VAL B 2 1250 ? 125.891 160.829 102.698 1.00 44.73  ? 1247 VAL A O     1 
ATOM   10085 C CB    . VAL B 2 1250 ? 125.814 163.625 101.368 1.00 44.73  ? 1247 VAL A CB    1 
ATOM   10086 C CG1   . VAL B 2 1250 ? 125.425 164.698 100.365 1.00 44.73  ? 1247 VAL A CG1   1 
ATOM   10087 C CG2   . VAL B 2 1250 ? 125.036 163.811 102.663 1.00 44.73  ? 1247 VAL A CG2   1 
ATOM   10088 N N     . CYS B 2 1251 ? 127.355 160.608 100.997 1.00 44.73  ? 1248 CYS A N     1 
ATOM   10089 C CA    . CYS B 2 1251 ? 128.161 159.623 101.702 1.00 44.73  ? 1248 CYS A CA    1 
ATOM   10090 C C     . CYS B 2 1251 ? 128.960 160.293 102.812 1.00 44.73  ? 1248 CYS A C     1 
ATOM   10091 O O     . CYS B 2 1251 ? 129.531 161.371 102.626 1.00 44.73  ? 1248 CYS A O     1 
ATOM   10092 C CB    . CYS B 2 1251 ? 129.100 158.909 100.732 1.00 44.73  ? 1248 CYS A CB    1 
ATOM   10093 S SG    . CYS B 2 1251 ? 128.264 157.870 99.512  1.00 44.73  ? 1248 CYS A SG    1 
ATOM   10094 N N     . PHE B 2 1252 ? 128.995 159.647 103.972 1.00 44.73  ? 1249 PHE A N     1 
ATOM   10095 C CA    . PHE B 2 1252 ? 129.702 160.202 105.117 1.00 44.73  ? 1249 PHE A CA    1 
ATOM   10096 C C     . PHE B 2 1252 ? 131.205 160.196 104.880 1.00 44.73  ? 1249 PHE A C     1 
ATOM   10097 O O     . PHE B 2 1252 ? 131.766 159.229 104.358 1.00 44.73  ? 1249 PHE A O     1 
ATOM   10098 C CB    . PHE B 2 1252 ? 129.366 159.410 106.378 1.00 44.73  ? 1249 PHE A CB    1 
ATOM   10099 C CG    . PHE B 2 1252 ? 130.115 159.861 107.596 1.00 44.73  ? 1249 PHE A CG    1 
ATOM   10100 C CD1   . PHE B 2 1252 ? 129.748 161.017 108.261 1.00 44.73  ? 1249 PHE A CD1   1 
ATOM   10101 C CD2   . PHE B 2 1252 ? 131.179 159.125 108.083 1.00 44.73  ? 1249 PHE A CD2   1 
ATOM   10102 C CE1   . PHE B 2 1252 ? 130.434 161.432 109.381 1.00 44.73  ? 1249 PHE A CE1   1 
ATOM   10103 C CE2   . PHE B 2 1252 ? 131.865 159.537 109.203 1.00 44.73  ? 1249 PHE A CE2   1 
ATOM   10104 C CZ    . PHE B 2 1252 ? 131.493 160.691 109.852 1.00 44.73  ? 1249 PHE A CZ    1 
ATOM   10105 N N     . ASP B 2 1253 ? 131.857 161.289 105.268 1.00 44.73  ? 1250 ASP A N     1 
ATOM   10106 C CA    . ASP B 2 1253 ? 133.309 161.411 105.177 1.00 44.73  ? 1250 ASP A CA    1 
ATOM   10107 C C     . ASP B 2 1253 ? 133.785 162.202 106.386 1.00 44.73  ? 1250 ASP A C     1 
ATOM   10108 O O     . ASP B 2 1253 ? 133.528 163.406 106.480 1.00 44.73  ? 1250 ASP A O     1 
ATOM   10109 C CB    . ASP B 2 1253 ? 133.732 162.087 103.875 1.00 44.73  ? 1250 ASP A CB    1 
ATOM   10110 C CG    . ASP B 2 1253 ? 135.166 161.779 103.500 1.00 44.73  ? 1250 ASP A CG    1 
ATOM   10111 O OD1   . ASP B 2 1253 ? 135.718 160.788 104.024 1.00 44.73  ? 1250 ASP A OD1   1 
ATOM   10112 O OD2   . ASP B 2 1253 ? 135.741 162.522 102.679 1.00 44.73  ? 1250 ASP A OD2   1 
ATOM   10113 N N     . SER B 2 1254 ? 134.476 161.529 107.308 1.00 44.73  ? 1251 SER A N     1 
ATOM   10114 C CA    . SER B 2 1254 ? 134.900 162.169 108.546 1.00 44.73  ? 1251 SER A CA    1 
ATOM   10115 C C     . SER B 2 1254 ? 135.954 163.243 108.330 1.00 44.73  ? 1251 SER A C     1 
ATOM   10116 O O     . SER B 2 1254 ? 136.207 164.026 109.252 1.00 44.73  ? 1251 SER A O     1 
ATOM   10117 C CB    . SER B 2 1254 ? 135.431 161.125 109.525 1.00 44.73  ? 1251 SER A CB    1 
ATOM   10118 O OG    . SER B 2 1254 ? 136.622 160.536 109.040 1.00 44.73  ? 1251 SER A OG    1 
ATOM   10119 N N     . ARG B 2 1255 ? 136.572 163.305 107.151 1.00 44.73  ? 1252 ARG A N     1 
ATOM   10120 C CA    . ARG B 2 1255 ? 137.534 164.367 106.888 1.00 44.73  ? 1252 ARG A CA    1 
ATOM   10121 C C     . ARG B 2 1255 ? 136.871 165.733 106.787 1.00 44.73  ? 1252 ARG A C     1 
ATOM   10122 O O     . ARG B 2 1255 ? 137.568 166.749 106.863 1.00 44.73  ? 1252 ARG A O     1 
ATOM   10123 C CB    . ARG B 2 1255 ? 138.318 164.075 105.610 1.00 44.73  ? 1252 ARG A CB    1 
ATOM   10124 C CG    . ARG B 2 1255 ? 139.520 163.174 105.823 1.00 44.73  ? 1252 ARG A CG    1 
ATOM   10125 C CD    . ARG B 2 1255 ? 140.069 162.661 104.505 1.00 44.73  ? 1252 ARG A CD    1 
ATOM   10126 N NE    . ARG B 2 1255 ? 139.077 161.897 103.759 1.00 44.73  ? 1252 ARG A NE    1 
ATOM   10127 C CZ    . ARG B 2 1255 ? 139.184 161.590 102.475 1.00 44.73  ? 1252 ARG A CZ    1 
ATOM   10128 N NH1   . ARG B 2 1255 ? 140.235 161.958 101.762 1.00 44.73  ? 1252 ARG A NH1   1 
ATOM   10129 N NH2   . ARG B 2 1255 ? 138.212 160.895 101.891 1.00 44.73  ? 1252 ARG A NH2   1 
ATOM   10130 N N     . PHE B 2 1256 ? 135.548 165.782 106.613 1.00 44.73  ? 1253 PHE A N     1 
ATOM   10131 C CA    . PHE B 2 1256 ? 134.846 167.059 106.584 1.00 44.73  ? 1253 PHE A CA    1 
ATOM   10132 C C     . PHE B 2 1256 ? 134.902 167.775 107.926 1.00 44.73  ? 1253 PHE A C     1 
ATOM   10133 O O     . PHE B 2 1256 ? 134.678 168.990 107.977 1.00 44.73  ? 1253 PHE A O     1 
ATOM   10134 C CB    . PHE B 2 1256 ? 133.391 166.848 106.167 1.00 44.73  ? 1253 PHE A CB    1 
ATOM   10135 C CG    . PHE B 2 1256 ? 133.189 166.771 104.681 1.00 44.73  ? 1253 PHE A CG    1 
ATOM   10136 C CD1   . PHE B 2 1256 ? 133.475 165.607 103.991 1.00 44.73  ? 1253 PHE A CD1   1 
ATOM   10137 C CD2   . PHE B 2 1256 ? 132.704 167.858 103.977 1.00 44.73  ? 1253 PHE A CD2   1 
ATOM   10138 C CE1   . PHE B 2 1256 ? 133.288 165.531 102.626 1.00 44.73  ? 1253 PHE A CE1   1 
ATOM   10139 C CE2   . PHE B 2 1256 ? 132.515 167.786 102.612 1.00 44.73  ? 1253 PHE A CE2   1 
ATOM   10140 C CZ    . PHE B 2 1256 ? 132.807 166.621 101.937 1.00 44.73  ? 1253 PHE A CZ    1 
ATOM   10141 N N     . GLN B 2 1257 ? 135.192 167.048 109.008 1.00 44.73  ? 1254 GLN A N     1 
ATOM   10142 C CA    . GLN B 2 1257 ? 135.333 167.620 110.348 1.00 44.73  ? 1254 GLN A CA    1 
ATOM   10143 C C     . GLN B 2 1257 ? 134.071 168.362 110.783 1.00 44.73  ? 1254 GLN A C     1 
ATOM   10144 O O     . GLN B 2 1257 ? 134.136 169.450 111.359 1.00 44.73  ? 1254 GLN A O     1 
ATOM   10145 C CB    . GLN B 2 1257 ? 136.557 168.535 110.433 1.00 44.73  ? 1254 GLN A CB    1 
ATOM   10146 C CG    . GLN B 2 1257 ? 137.820 167.941 109.835 1.00 44.73  ? 1254 GLN A CG    1 
ATOM   10147 C CD    . GLN B 2 1257 ? 138.470 166.915 110.739 1.00 44.73  ? 1254 GLN A CD    1 
ATOM   10148 O OE1   . GLN B 2 1257 ? 138.098 165.742 110.733 1.00 44.73  ? 1254 GLN A OE1   1 
ATOM   10149 N NE2   . GLN B 2 1257 ? 139.451 167.350 111.519 1.00 44.73  ? 1254 GLN A NE2   1 
ATOM   10150 N N     . ASN B 2 1258 ? 132.918 167.773 110.509 1.00 44.73  ? 1255 ASN A N     1 
ATOM   10151 C CA    . ASN B 2 1258 ? 131.662 168.324 111.004 1.00 44.73  ? 1255 ASN A CA    1 
ATOM   10152 C C     . ASN B 2 1258 ? 131.507 167.985 112.480 1.00 44.73  ? 1255 ASN A C     1 
ATOM   10153 O O     . ASN B 2 1258 ? 131.572 166.803 112.842 1.00 44.73  ? 1255 ASN A O     1 
ATOM   10154 C CB    . ASN B 2 1258 ? 130.486 167.775 110.205 1.00 44.73  ? 1255 ASN A CB    1 
ATOM   10155 C CG    . ASN B 2 1258 ? 129.309 168.725 110.176 1.00 44.73  ? 1255 ASN A CG    1 
ATOM   10156 O OD1   . ASN B 2 1258 ? 129.437 169.901 110.517 1.00 44.73  ? 1255 ASN A OD1   1 
ATOM   10157 N ND2   . ASN B 2 1258 ? 128.151 168.220 109.769 1.00 44.73  ? 1255 ASN A ND2   1 
ATOM   10158 N N     . PRO B 2 1259 ? 131.318 168.970 113.360 1.00 44.73  ? 1256 PRO A N     1 
ATOM   10159 C CA    . PRO B 2 1259 ? 131.210 168.660 114.797 1.00 44.73  ? 1256 PRO A CA    1 
ATOM   10160 C C     . PRO B 2 1259 ? 130.073 167.712 115.141 1.00 44.73  ? 1256 PRO A C     1 
ATOM   10161 O O     . PRO B 2 1259 ? 130.202 166.929 116.091 1.00 44.73  ? 1256 PRO A O     1 
ATOM   10162 C CB    . PRO B 2 1259 ? 130.998 170.035 115.445 1.00 44.73  ? 1256 PRO A CB    1 
ATOM   10163 C CG    . PRO B 2 1259 ? 131.448 171.036 114.449 1.00 44.73  ? 1256 PRO A CG    1 
ATOM   10164 C CD    . PRO B 2 1259 ? 131.482 170.408 113.092 1.00 44.73  ? 1256 PRO A CD    1 
ATOM   10165 N N     . GLU B 2 1260 ? 128.961 167.757 114.404 1.00 44.73  ? 1257 GLU A N     1 
ATOM   10166 C CA    . GLU B 2 1260 ? 127.801 166.932 114.725 1.00 44.73  ? 1257 GLU A CA    1 
ATOM   10167 C C     . GLU B 2 1260 ? 128.046 165.444 114.507 1.00 44.73  ? 1257 GLU A C     1 
ATOM   10168 O O     . GLU B 2 1260 ? 127.228 164.631 114.950 1.00 44.73  ? 1257 GLU A O     1 
ATOM   10169 C CB    . GLU B 2 1260 ? 126.592 167.373 113.896 1.00 44.73  ? 1257 GLU A CB    1 
ATOM   10170 C CG    . GLU B 2 1260 ? 126.032 168.741 114.260 1.00 44.73  ? 1257 GLU A CG    1 
ATOM   10171 C CD    . GLU B 2 1260 ? 126.883 169.886 113.746 1.00 44.73  ? 1257 GLU A CD    1 
ATOM   10172 O OE1   . GLU B 2 1260 ? 127.228 169.879 112.545 1.00 44.73  ? 1257 GLU A OE1   1 
ATOM   10173 O OE2   . GLU B 2 1260 ? 127.207 170.792 114.541 1.00 44.73  ? 1257 GLU A OE2   1 
ATOM   10174 N N     . TRP B 2 1261 ? 129.133 165.072 113.847 1.00 44.73  ? 1258 TRP A N     1 
ATOM   10175 C CA    . TRP B 2 1261 ? 129.466 163.694 113.531 1.00 44.73  ? 1258 TRP A CA    1 
ATOM   10176 C C     . TRP B 2 1261 ? 130.906 163.424 113.937 1.00 44.73  ? 1258 TRP A C     1 
ATOM   10177 O O     . TRP B 2 1261 ? 131.687 164.361 114.132 1.00 44.73  ? 1258 TRP A O     1 
ATOM   10178 C CB    . TRP B 2 1261 ? 129.268 163.419 112.033 1.00 44.73  ? 1258 TRP A CB    1 
ATOM   10179 C CG    . TRP B 2 1261 ? 127.892 163.756 111.547 1.00 44.73  ? 1258 TRP A CG    1 
ATOM   10180 C CD1   . TRP B 2 1261 ? 127.556 164.730 110.655 1.00 44.73  ? 1258 TRP A CD1   1 
ATOM   10181 C CD2   . TRP B 2 1261 ? 126.665 163.123 111.930 1.00 44.73  ? 1258 TRP A CD2   1 
ATOM   10182 N NE1   . TRP B 2 1261 ? 126.197 164.743 110.456 1.00 44.73  ? 1258 TRP A NE1   1 
ATOM   10183 C CE2   . TRP B 2 1261 ? 125.628 163.766 111.229 1.00 44.73  ? 1258 TRP A CE2   1 
ATOM   10184 C CE3   . TRP B 2 1261 ? 126.344 162.075 112.797 1.00 44.73  ? 1258 TRP A CE3   1 
ATOM   10185 C CZ2   . TRP B 2 1261 ? 124.293 163.395 111.366 1.00 44.73  ? 1258 TRP A CZ2   1 
ATOM   10186 C CZ3   . TRP B 2 1261 ? 125.019 161.708 112.932 1.00 44.73  ? 1258 TRP A CZ3   1 
ATOM   10187 C CH2   . TRP B 2 1261 ? 124.010 162.366 112.221 1.00 44.73  ? 1258 TRP A CH2   1 
ATOM   10188 N N     . PRO B 2 1262 ? 131.284 162.154 114.104 1.00 44.73  ? 1259 PRO A N     1 
ATOM   10189 C CA    . PRO B 2 1262 ? 132.637 161.846 114.584 1.00 44.73  ? 1259 PRO A CA    1 
ATOM   10190 C C     . PRO B 2 1262 ? 133.724 162.432 113.693 1.00 44.73  ? 1259 PRO A C     1 
ATOM   10191 O O     . PRO B 2 1262 ? 133.627 162.427 112.464 1.00 44.73  ? 1259 PRO A O     1 
ATOM   10192 C CB    . PRO B 2 1262 ? 132.671 160.315 114.568 1.00 44.73  ? 1259 PRO A CB    1 
ATOM   10193 C CG    . PRO B 2 1262 ? 131.261 159.925 114.797 1.00 44.73  ? 1259 PRO A CG    1 
ATOM   10194 C CD    . PRO B 2 1262 ? 130.428 160.954 114.086 1.00 44.73  ? 1259 PRO A CD    1 
ATOM   10195 N N     . MET B 2 1263 ? 134.772 162.950 114.341 1.00 44.73  ? 1260 MET A N     1 
ATOM   10196 C CA    . MET B 2 1263 ? 135.858 163.608 113.622 1.00 44.73  ? 1260 MET A CA    1 
ATOM   10197 C C     . MET B 2 1263 ? 136.797 162.623 112.934 1.00 44.73  ? 1260 MET A C     1 
ATOM   10198 O O     . MET B 2 1263 ? 137.188 162.855 111.785 1.00 44.73  ? 1260 MET A O     1 
ATOM   10199 C CB    . MET B 2 1263 ? 136.652 164.504 114.574 1.00 44.73  ? 1260 MET A CB    1 
ATOM   10200 C CG    . MET B 2 1263 ? 135.793 165.423 115.423 1.00 44.73  ? 1260 MET A CG    1 
ATOM   10201 S SD    . MET B 2 1263 ? 134.892 166.644 114.452 1.00 44.73  ? 1260 MET A SD    1 
ATOM   10202 C CE    . MET B 2 1263 ? 136.041 168.017 114.485 1.00 44.73  ? 1260 MET A CE    1 
ATOM   10203 N N     . ASP B 2 1264 ? 137.172 161.537 113.600 1.00 44.73  ? 1261 ASP A N     1 
ATOM   10204 C CA    . ASP B 2 1264 ? 138.110 160.579 113.024 1.00 44.73  ? 1261 ASP A CA    1 
ATOM   10205 C C     . ASP B 2 1264 ? 137.621 159.171 113.343 1.00 44.73  ? 1261 ASP A C     1 
ATOM   10206 O O     . ASP B 2 1264 ? 136.541 158.984 113.913 1.00 44.73  ? 1261 ASP A O     1 
ATOM   10207 C CB    . ASP B 2 1264 ? 139.535 160.835 113.529 1.00 44.73  ? 1261 ASP A CB    1 
ATOM   10208 C CG    . ASP B 2 1264 ? 139.599 161.023 115.030 1.00 44.73  ? 1261 ASP A CG    1 
ATOM   10209 O OD1   . ASP B 2 1264 ? 138.532 161.028 115.674 1.00 44.73  ? 1261 ASP A OD1   1 
ATOM   10210 O OD2   . ASP B 2 1264 ? 140.716 161.174 115.566 1.00 44.73  ? 1261 ASP A OD2   1 
ATOM   10211 N N     . ALA B 2 1265 ? 138.424 158.172 112.967 1.00 44.73  ? 1262 ALA A N     1 
ATOM   10212 C CA    . ALA B 2 1265 ? 138.011 156.782 113.130 1.00 44.73  ? 1262 ALA A CA    1 
ATOM   10213 C C     . ALA B 2 1265 ? 137.803 156.432 114.596 1.00 44.73  ? 1262 ALA A C     1 
ATOM   10214 O O     . ALA B 2 1265 ? 136.839 155.742 114.947 1.00 44.73  ? 1262 ALA A O     1 
ATOM   10215 C CB    . ALA B 2 1265 ? 139.046 155.850 112.501 1.00 44.73  ? 1262 ALA A CB    1 
ATOM   10216 N N     . ASP B 2 1266 ? 138.699 156.897 115.469 1.00 44.73  ? 1263 ASP A N     1 
ATOM   10217 C CA    . ASP B 2 1266 ? 138.560 156.612 116.892 1.00 44.73  ? 1263 ASP A CA    1 
ATOM   10218 C C     . ASP B 2 1266 ? 137.327 157.295 117.468 1.00 44.73  ? 1263 ASP A C     1 
ATOM   10219 O O     . ASP B 2 1266 ? 136.741 156.818 118.446 1.00 44.73  ? 1263 ASP A O     1 
ATOM   10220 C CB    . ASP B 2 1266 ? 139.818 157.053 117.637 1.00 44.73  ? 1263 ASP A CB    1 
ATOM   10221 C CG    . ASP B 2 1266 ? 141.079 156.458 117.048 1.00 44.73  ? 1263 ASP A CG    1 
ATOM   10222 O OD1   . ASP B 2 1266 ? 140.997 155.374 116.434 1.00 44.73  ? 1263 ASP A OD1   1 
ATOM   10223 O OD2   . ASP B 2 1266 ? 142.157 157.072 117.201 1.00 44.73  ? 1263 ASP A OD2   1 
ATOM   10224 N N     . ALA B 2 1267 ? 136.924 158.419 116.873 1.00 44.73  ? 1264 ALA A N     1 
ATOM   10225 C CA    . ALA B 2 1267 ? 135.729 159.116 117.330 1.00 44.73  ? 1264 ALA A CA    1 
ATOM   10226 C C     . ALA B 2 1267 ? 134.477 158.286 117.100 1.00 44.73  ? 1264 ALA A C     1 
ATOM   10227 O O     . ALA B 2 1267 ? 133.524 158.358 117.884 1.00 44.73  ? 1264 ALA A O     1 
ATOM   10228 C CB    . ALA B 2 1267 ? 135.606 160.469 116.631 1.00 44.73  ? 1264 ALA A CB    1 
ATOM   10229 N N     . ASN B 2 1268 ? 134.458 157.500 116.025 1.00 44.73  ? 1265 ASN A N     1 
ATOM   10230 C CA    . ASN B 2 1268 ? 133.259 156.743 115.686 1.00 44.73  ? 1265 ASN A CA    1 
ATOM   10231 C C     . ASN B 2 1268 ? 132.956 155.692 116.747 1.00 44.73  ? 1265 ASN A C     1 
ATOM   10232 O O     . ASN B 2 1268 ? 131.790 155.452 117.079 1.00 44.73  ? 1265 ASN A O     1 
ATOM   10233 C CB    . ASN B 2 1268 ? 133.432 156.093 114.312 1.00 44.73  ? 1265 ASN A CB    1 
ATOM   10234 C CG    . ASN B 2 1268 ? 132.129 155.579 113.739 1.00 44.73  ? 1265 ASN A CG    1 
ATOM   10235 O OD1   . ASN B 2 1268 ? 131.070 155.736 114.338 1.00 44.73  ? 1265 ASN A OD1   1 
ATOM   10236 N ND2   . ASN B 2 1268 ? 132.204 154.950 112.574 1.00 44.73  ? 1265 ASN A ND2   1 
ATOM   10237 N N     . GLY B 2 1269 ? 133.995 155.045 117.280 1.00 44.73  ? 1266 GLY A N     1 
ATOM   10238 C CA    . GLY B 2 1269 ? 133.780 153.977 118.246 1.00 44.73  ? 1266 GLY A CA    1 
ATOM   10239 C C     . GLY B 2 1269 ? 133.171 154.462 119.548 1.00 44.73  ? 1266 GLY A C     1 
ATOM   10240 O O     . GLY B 2 1269 ? 132.222 153.868 120.064 1.00 44.73  ? 1266 GLY A O     1 
ATOM   10241 N N     . ALA B 2 1270 ? 133.714 155.544 120.106 1.00 44.73  ? 1267 ALA A N     1 
ATOM   10242 C CA    . ALA B 2 1270 ? 133.180 156.058 121.362 1.00 44.73  ? 1267 ALA A CA    1 
ATOM   10243 C C     . ALA B 2 1270 ? 131.750 156.549 121.188 1.00 44.73  ? 1267 ALA A C     1 
ATOM   10244 O O     . ALA B 2 1270 ? 130.954 156.518 122.132 1.00 44.73  ? 1267 ALA A O     1 
ATOM   10245 C CB    . ALA B 2 1270 ? 134.074 157.172 121.898 1.00 44.73  ? 1267 ALA A CB    1 
ATOM   10246 N N     . TYR B 2 1271 ? 131.412 157.017 119.986 1.00 44.73  ? 1268 TYR A N     1 
ATOM   10247 C CA    . TYR B 2 1271 ? 130.053 157.475 119.717 1.00 44.73  ? 1268 TYR A CA    1 
ATOM   10248 C C     . TYR B 2 1271 ? 129.053 156.326 119.789 1.00 44.73  ? 1268 TYR A C     1 
ATOM   10249 O O     . TYR B 2 1271 ? 127.963 156.478 120.354 1.00 44.73  ? 1268 TYR A O     1 
ATOM   10250 C CB    . TYR B 2 1271 ? 130.005 158.158 118.350 1.00 44.73  ? 1268 TYR A CB    1 
ATOM   10251 C CG    . TYR B 2 1271 ? 128.630 158.588 117.899 1.00 44.73  ? 1268 TYR A CG    1 
ATOM   10252 C CD1   . TYR B 2 1271 ? 127.790 159.301 118.740 1.00 44.73  ? 1268 TYR A CD1   1 
ATOM   10253 C CD2   . TYR B 2 1271 ? 128.181 158.300 116.619 1.00 44.73  ? 1268 TYR A CD2   1 
ATOM   10254 C CE1   . TYR B 2 1271 ? 126.535 159.701 118.324 1.00 44.73  ? 1268 TYR A CE1   1 
ATOM   10255 C CE2   . TYR B 2 1271 ? 126.930 158.696 116.195 1.00 44.73  ? 1268 TYR A CE2   1 
ATOM   10256 C CZ    . TYR B 2 1271 ? 126.112 159.396 117.050 1.00 44.73  ? 1268 TYR A CZ    1 
ATOM   10257 O OH    . TYR B 2 1271 ? 124.863 159.791 116.628 1.00 44.73  ? 1268 TYR A OH    1 
ATOM   10258 N N     . HIS B 2 1272 ? 129.407 155.165 119.233 1.00 44.73  ? 1269 HIS A N     1 
ATOM   10259 C CA    . HIS B 2 1272 ? 128.460 154.056 119.177 1.00 44.73  ? 1269 HIS A CA    1 
ATOM   10260 C C     . HIS B 2 1272 ? 128.388 153.279 120.485 1.00 44.73  ? 1269 HIS A C     1 
ATOM   10261 O O     . HIS B 2 1272 ? 127.364 152.643 120.761 1.00 44.73  ? 1269 HIS A O     1 
ATOM   10262 C CB    . HIS B 2 1272 ? 128.812 153.119 118.022 1.00 44.73  ? 1269 HIS A CB    1 
ATOM   10263 C CG    . HIS B 2 1272 ? 128.360 153.618 116.685 1.00 44.73  ? 1269 HIS A CG    1 
ATOM   10264 N ND1   . HIS B 2 1272 ? 127.031 153.747 116.348 1.00 44.73  ? 1269 HIS A ND1   1 
ATOM   10265 C CD2   . HIS B 2 1272 ? 129.063 154.022 115.602 1.00 44.73  ? 1269 HIS A CD2   1 
ATOM   10266 C CE1   . HIS B 2 1272 ? 126.933 154.208 115.115 1.00 44.73  ? 1269 HIS A CE1   1 
ATOM   10267 N NE2   . HIS B 2 1272 ? 128.152 154.385 114.640 1.00 44.73  ? 1269 HIS A NE2   1 
ATOM   10268 N N     . ILE B 2 1273 ? 129.449 153.301 121.296 1.00 44.73  ? 1270 ILE A N     1 
ATOM   10269 C CA    . ILE B 2 1273 ? 129.345 152.751 122.645 1.00 44.73  ? 1270 ILE A CA    1 
ATOM   10270 C C     . ILE B 2 1273 ? 128.340 153.550 123.461 1.00 44.73  ? 1270 ILE A C     1 
ATOM   10271 O O     . ILE B 2 1273 ? 127.527 152.984 124.203 1.00 44.73  ? 1270 ILE A O     1 
ATOM   10272 C CB    . ILE B 2 1273 ? 130.727 152.703 123.323 1.00 44.73  ? 1270 ILE A CB    1 
ATOM   10273 C CG1   . ILE B 2 1273 ? 131.627 151.691 122.619 1.00 44.73  ? 1270 ILE A CG1   1 
ATOM   10274 C CG2   . ILE B 2 1273 ? 130.597 152.358 124.791 1.00 44.73  ? 1270 ILE A CG2   1 
ATOM   10275 C CD1   . ILE B 2 1273 ? 133.063 151.741 123.059 1.00 44.73  ? 1270 ILE A CD1   1 
ATOM   10276 N N     . ALA B 2 1274 ? 128.375 154.877 123.335 1.00 44.73  ? 1271 ALA A N     1 
ATOM   10277 C CA    . ALA B 2 1274 ? 127.334 155.700 123.938 1.00 44.73  ? 1271 ALA A CA    1 
ATOM   10278 C C     . ALA B 2 1274 ? 125.978 155.404 123.314 1.00 44.73  ? 1271 ALA A C     1 
ATOM   10279 O O     . ALA B 2 1274 ? 124.954 155.402 124.007 1.00 44.73  ? 1271 ALA A O     1 
ATOM   10280 C CB    . ALA B 2 1274 ? 127.687 157.179 123.795 1.00 44.73  ? 1271 ALA A CB    1 
ATOM   10281 N N     . LEU B 2 1275 ? 125.950 155.156 122.002 1.00 44.73  ? 1272 LEU A N     1 
ATOM   10282 C CA    . LEU B 2 1275 ? 124.700 154.792 121.344 1.00 44.73  ? 1272 LEU A CA    1 
ATOM   10283 C C     . LEU B 2 1275 ? 124.199 153.434 121.819 1.00 44.73  ? 1272 LEU A C     1 
ATOM   10284 O O     . LEU B 2 1275 ? 122.988 153.229 121.960 1.00 44.73  ? 1272 LEU A O     1 
ATOM   10285 C CB    . LEU B 2 1275 ? 124.881 154.799 119.828 1.00 44.73  ? 1272 LEU A CB    1 
ATOM   10286 C CG    . LEU B 2 1275 ? 124.760 156.165 119.156 1.00 44.73  ? 1272 LEU A CG    1 
ATOM   10287 C CD1   . LEU B 2 1275 ? 124.968 156.049 117.656 1.00 44.73  ? 1272 LEU A CD1   1 
ATOM   10288 C CD2   . LEU B 2 1275 ? 123.410 156.785 119.460 1.00 44.73  ? 1272 LEU A CD2   1 
ATOM   10289 N N     . LYS B 2 1276 ? 125.112 152.491 122.061 1.00 44.73  ? 1273 LYS A N     1 
ATOM   10290 C CA    . LYS B 2 1276 ? 124.710 151.210 122.633 1.00 44.73  ? 1273 LYS A CA    1 
ATOM   10291 C C     . LYS B 2 1276 ? 124.152 151.391 124.038 1.00 44.73  ? 1273 LYS A C     1 
ATOM   10292 O O     . LYS B 2 1276 ? 123.304 150.610 124.484 1.00 44.73  ? 1273 LYS A O     1 
ATOM   10293 C CB    . LYS B 2 1276 ? 125.893 150.241 122.642 1.00 44.73  ? 1273 LYS A CB    1 
ATOM   10294 C CG    . LYS B 2 1276 ? 125.957 149.328 121.431 1.00 44.73  ? 1273 LYS A CG    1 
ATOM   10295 C CD    . LYS B 2 1276 ? 127.035 148.269 121.589 1.00 44.73  ? 1273 LYS A CD    1 
ATOM   10296 C CE    . LYS B 2 1276 ? 127.032 147.301 120.417 1.00 44.73  ? 1273 LYS A CE    1 
ATOM   10297 N NZ    . LYS B 2 1276 ? 128.108 146.283 120.535 1.00 44.73  ? 1273 LYS A NZ    1 
ATOM   10298 N N     . GLY B 2 1277 ? 124.622 152.414 124.754 1.00 44.73  ? 1274 GLY A N     1 
ATOM   10299 C CA    . GLY B 2 1277 ? 124.045 152.723 126.051 1.00 44.73  ? 1274 GLY A CA    1 
ATOM   10300 C C     . GLY B 2 1277 ? 122.601 153.173 125.950 1.00 44.73  ? 1274 GLY A C     1 
ATOM   10301 O O     . GLY B 2 1277 ? 121.784 152.874 126.824 1.00 44.73  ? 1274 GLY A O     1 
ATOM   10302 N N     . GLN B 2 1278 ? 122.268 153.908 124.885 1.00 44.73  ? 1275 GLN A N     1 
ATOM   10303 C CA    . GLN B 2 1278 ? 120.883 154.310 124.662 1.00 44.73  ? 1275 GLN A CA    1 
ATOM   10304 C C     . GLN B 2 1278 ? 119.978 153.099 124.491 1.00 44.73  ? 1275 GLN A C     1 
ATOM   10305 O O     . GLN B 2 1278 ? 118.862 153.071 125.023 1.00 44.73  ? 1275 GLN A O     1 
ATOM   10306 C CB    . GLN B 2 1278 ? 120.786 155.219 123.438 1.00 44.73  ? 1275 GLN A CB    1 
ATOM   10307 C CG    . GLN B 2 1278 ? 121.643 156.464 123.506 1.00 44.73  ? 1275 GLN A CG    1 
ATOM   10308 C CD    . GLN B 2 1278 ? 120.950 157.612 124.210 1.00 44.73  ? 1275 GLN A CD    1 
ATOM   10309 O OE1   . GLN B 2 1278 ? 120.578 157.508 125.378 1.00 44.73  ? 1275 GLN A OE1   1 
ATOM   10310 N NE2   . GLN B 2 1278 ? 120.771 158.719 123.498 1.00 44.73  ? 1275 GLN A NE2   1 
ATOM   10311 N N     . LEU B 2 1279 ? 120.441 152.090 123.750 1.00 44.73  ? 1276 LEU A N     1 
ATOM   10312 C CA    . LEU B 2 1279 ? 119.635 150.895 123.527 1.00 44.73  ? 1276 LEU A CA    1 
ATOM   10313 C C     . LEU B 2 1279 ? 119.326 150.194 124.843 1.00 44.73  ? 1276 LEU A C     1 
ATOM   10314 O O     . LEU B 2 1279 ? 118.245 149.619 125.017 1.00 44.73  ? 1276 LEU A O     1 
ATOM   10315 C CB    . LEU B 2 1279 ? 120.359 149.954 122.565 1.00 44.73  ? 1276 LEU A CB    1 
ATOM   10316 C CG    . LEU B 2 1279 ? 119.637 148.664 122.181 1.00 44.73  ? 1276 LEU A CG    1 
ATOM   10317 C CD1   . LEU B 2 1279 ? 118.292 148.981 121.560 1.00 44.73  ? 1276 LEU A CD1   1 
ATOM   10318 C CD2   . LEU B 2 1279 ? 120.486 147.859 121.218 1.00 44.73  ? 1276 LEU A CD2   1 
ATOM   10319 N N     . LEU B 2 1280 ? 120.271 150.226 125.783 1.00 44.73  ? 1277 LEU A N     1 
ATOM   10320 C CA    . LEU B 2 1280 ? 120.016 149.677 127.110 1.00 44.73  ? 1277 LEU A CA    1 
ATOM   10321 C C     . LEU B 2 1280 ? 118.959 150.492 127.847 1.00 44.73  ? 1277 LEU A C     1 
ATOM   10322 O O     . LEU B 2 1280 ? 118.040 149.934 128.456 1.00 44.73  ? 1277 LEU A O     1 
ATOM   10323 C CB    . LEU B 2 1280 ? 121.316 149.626 127.911 1.00 44.73  ? 1277 LEU A CB    1 
ATOM   10324 C CG    . LEU B 2 1280 ? 122.071 148.298 127.871 1.00 44.73  ? 1277 LEU A CG    1 
ATOM   10325 C CD1   . LEU B 2 1280 ? 123.424 148.441 128.538 1.00 44.73  ? 1277 LEU A CD1   1 
ATOM   10326 C CD2   . LEU B 2 1280 ? 121.256 147.206 128.537 1.00 44.73  ? 1277 LEU A CD2   1 
ATOM   10327 N N     . LEU B 2 1281 ? 119.072 151.822 127.799 1.00 44.73  ? 1278 LEU A N     1 
ATOM   10328 C CA    . LEU B 2 1281 ? 118.112 152.671 128.498 1.00 44.73  ? 1278 LEU A CA    1 
ATOM   10329 C C     . LEU B 2 1281 ? 116.783 152.753 127.758 1.00 44.73  ? 1278 LEU A C     1 
ATOM   10330 O O     . LEU B 2 1281 ? 115.725 152.860 128.390 1.00 44.73  ? 1278 LEU A O     1 
ATOM   10331 C CB    . LEU B 2 1281 ? 118.693 154.066 128.711 1.00 44.73  ? 1278 LEU A CB    1 
ATOM   10332 C CG    . LEU B 2 1281 ? 120.043 154.091 129.420 1.00 44.73  ? 1278 LEU A CG    1 
ATOM   10333 C CD1   . LEU B 2 1281 ? 120.609 155.493 129.439 1.00 44.73  ? 1278 LEU A CD1   1 
ATOM   10334 C CD2   . LEU B 2 1281 ? 119.861 153.567 130.830 1.00 44.73  ? 1278 LEU A CD2   1 
ATOM   10335 N N     . ASN B 2 1282 ? 116.812 152.722 126.424 1.00 49.53  ? 1279 ASN A N     1 
ATOM   10336 C CA    . ASN B 2 1282 ? 115.563 152.762 125.671 1.00 49.53  ? 1279 ASN A CA    1 
ATOM   10337 C C     . ASN B 2 1282 ? 114.699 151.550 125.988 1.00 49.53  ? 1279 ASN A C     1 
ATOM   10338 O O     . ASN B 2 1282 ? 113.475 151.667 126.122 1.00 49.53  ? 1279 ASN A O     1 
ATOM   10339 C CB    . ASN B 2 1282 ? 115.847 152.847 124.172 1.00 49.53  ? 1279 ASN A CB    1 
ATOM   10340 C CG    . ASN B 2 1282 ? 115.970 154.277 123.684 1.00 49.53  ? 1279 ASN A CG    1 
ATOM   10341 O OD1   . ASN B 2 1282 ? 115.900 155.221 124.471 1.00 49.53  ? 1279 ASN A OD1   1 
ATOM   10342 N ND2   . ASN B 2 1282 ? 116.153 154.444 122.380 1.00 49.53  ? 1279 ASN A ND2   1 
ATOM   10343 N N     . HIS B 2 1283 ? 115.318 150.376 126.111 1.00 54.65  ? 1280 HIS A N     1 
ATOM   10344 C CA    . HIS B 2 1283 ? 114.589 149.209 126.593 1.00 54.65  ? 1280 HIS A CA    1 
ATOM   10345 C C     . HIS B 2 1283 ? 114.235 149.354 128.067 1.00 54.65  ? 1280 HIS A C     1 
ATOM   10346 O O     . HIS B 2 1283 ? 113.193 148.861 128.513 1.00 54.65  ? 1280 HIS A O     1 
ATOM   10347 C CB    . HIS B 2 1283 ? 115.406 147.939 126.356 1.00 54.65  ? 1280 HIS A CB    1 
ATOM   10348 C CG    . HIS B 2 1283 ? 115.519 147.552 124.914 1.00 54.65  ? 1280 HIS A CG    1 
ATOM   10349 N ND1   . HIS B 2 1283 ? 115.599 146.239 124.502 1.00 54.65  ? 1280 HIS A ND1   1 
ATOM   10350 C CD2   . HIS B 2 1283 ? 115.552 148.302 123.788 1.00 54.65  ? 1280 HIS A CD2   1 
ATOM   10351 C CE1   . HIS B 2 1283 ? 115.683 146.197 123.185 1.00 54.65  ? 1280 HIS A CE1   1 
ATOM   10352 N NE2   . HIS B 2 1283 ? 115.656 147.436 122.726 1.00 54.65  ? 1280 HIS A NE2   1 
ATOM   10353 N N     . LEU B 2 1284 ? 115.094 150.024 128.839 1.00 53.67  ? 1281 LEU A N     1 
ATOM   10354 C CA    . LEU B 2 1284 ? 114.834 150.200 130.265 1.00 53.67  ? 1281 LEU A CA    1 
ATOM   10355 C C     . LEU B 2 1284 ? 113.589 151.048 130.500 1.00 53.67  ? 1281 LEU A C     1 
ATOM   10356 O O     . LEU B 2 1284 ? 112.755 150.723 131.353 1.00 53.67  ? 1281 LEU A O     1 
ATOM   10357 C CB    . LEU B 2 1284 ? 116.054 150.829 130.942 1.00 53.67  ? 1281 LEU A CB    1 
ATOM   10358 C CG    . LEU B 2 1284 ? 115.998 151.085 132.450 1.00 53.67  ? 1281 LEU A CG    1 
ATOM   10359 C CD1   . LEU B 2 1284 ? 117.342 150.775 133.080 1.00 53.67  ? 1281 LEU A CD1   1 
ATOM   10360 C CD2   . LEU B 2 1284 ? 115.600 152.523 132.749 1.00 53.67  ? 1281 LEU A CD2   1 
ATOM   10361 N N     . LYS B 2 1285 ? 113.451 152.148 129.755 1.00 55.22  ? 1282 LYS A N     1 
ATOM   10362 C CA    . LYS B 2 1285 ? 112.316 153.041 129.962 1.00 55.22  ? 1282 LYS A CA    1 
ATOM   10363 C C     . LYS B 2 1285 ? 111.000 152.361 129.606 1.00 55.22  ? 1282 LYS A C     1 
ATOM   10364 O O     . LYS B 2 1285 ? 110.009 152.491 130.335 1.00 55.22  ? 1282 LYS A O     1 
ATOM   10365 C CB    . LYS B 2 1285 ? 112.497 154.320 129.145 1.00 55.22  ? 1282 LYS A CB    1 
ATOM   10366 C CG    . LYS B 2 1285 ? 111.360 155.316 129.300 1.00 55.22  ? 1282 LYS A CG    1 
ATOM   10367 C CD    . LYS B 2 1285 ? 111.324 155.891 130.707 1.00 55.22  ? 1282 LYS A CD    1 
ATOM   10368 C CE    . LYS B 2 1285 ? 110.292 157.001 130.829 1.00 55.22  ? 1282 LYS A CE    1 
ATOM   10369 N NZ    . LYS B 2 1285 ? 108.904 156.489 130.662 1.00 55.22  ? 1282 LYS A NZ    1 
ATOM   10370 N N     . GLU B 2 1286 ? 110.967 151.633 128.489 1.00 62.28  ? 1283 GLU A N     1 
ATOM   10371 C CA    . GLU B 2 1286 ? 109.744 150.948 128.089 1.00 62.28  ? 1283 GLU A CA    1 
ATOM   10372 C C     . GLU B 2 1286 ? 109.461 149.719 128.941 1.00 62.28  ? 1283 GLU A C     1 
ATOM   10373 O O     . GLU B 2 1286 ? 108.300 149.308 129.046 1.00 62.28  ? 1283 GLU A O     1 
ATOM   10374 C CB    . GLU B 2 1286 ? 109.815 150.560 126.609 1.00 62.28  ? 1283 GLU A CB    1 
ATOM   10375 C CG    . GLU B 2 1286 ? 110.970 149.638 126.247 1.00 62.28  ? 1283 GLU A CG    1 
ATOM   10376 C CD    . GLU B 2 1286 ? 110.604 148.169 126.337 1.00 62.28  ? 1283 GLU A CD    1 
ATOM   10377 O OE1   . GLU B 2 1286 ? 109.396 147.853 126.311 1.00 62.28  ? 1283 GLU A OE1   1 
ATOM   10378 O OE2   . GLU B 2 1286 ? 111.524 147.331 126.433 1.00 62.28  ? 1283 GLU A OE2   1 
ATOM   10379 N N     . SER B 2 1287 ? 110.485 149.123 129.546 1.00 64.68  ? 1284 SER A N     1 
ATOM   10380 C CA    . SER B 2 1287 ? 110.281 147.940 130.368 1.00 64.68  ? 1284 SER A CA    1 
ATOM   10381 C C     . SER B 2 1287 ? 109.520 148.292 131.639 1.00 64.68  ? 1284 SER A C     1 
ATOM   10382 O O     . SER B 2 1287 ? 109.743 149.342 132.248 1.00 64.68  ? 1284 SER A O     1 
ATOM   10383 C CB    . SER B 2 1287 ? 111.621 147.298 130.724 1.00 64.68  ? 1284 SER A CB    1 
ATOM   10384 O OG    . SER B 2 1287 ? 111.467 146.334 131.750 1.00 64.68  ? 1284 SER A OG    1 
ATOM   10385 N N     . LYS B 2 1288 ? 108.607 147.403 132.035 1.00 79.24  ? 1285 LYS A N     1 
ATOM   10386 C CA    . LYS B 2 1288 ? 107.868 147.606 133.276 1.00 79.24  ? 1285 LYS A CA    1 
ATOM   10387 C C     . LYS B 2 1288 ? 108.743 147.327 134.492 1.00 79.24  ? 1285 LYS A C     1 
ATOM   10388 O O     . LYS B 2 1288 ? 108.683 148.058 135.487 1.00 79.24  ? 1285 LYS A O     1 
ATOM   10389 C CB    . LYS B 2 1288 ? 106.623 146.719 133.291 1.00 79.24  ? 1285 LYS A CB    1 
ATOM   10390 C CG    . LYS B 2 1288 ? 106.858 145.315 132.756 1.00 79.24  ? 1285 LYS A CG    1 
ATOM   10391 C CD    . LYS B 2 1288 ? 105.661 144.415 133.010 1.00 79.24  ? 1285 LYS A CD    1 
ATOM   10392 C CE    . LYS B 2 1288 ? 105.929 142.997 132.535 1.00 79.24  ? 1285 LYS A CE    1 
ATOM   10393 N NZ    . LYS B 2 1288 ? 105.628 142.830 131.086 1.00 79.24  ? 1285 LYS A NZ    1 
ATOM   10394 N N     . ASP B 2 1289 ? 109.559 146.279 134.430 1.00 84.31  ? 1286 ASP A N     1 
ATOM   10395 C CA    . ASP B 2 1289 ? 110.423 145.917 135.541 1.00 84.31  ? 1286 ASP A CA    1 
ATOM   10396 C C     . ASP B 2 1289 ? 111.690 146.768 135.541 1.00 84.31  ? 1286 ASP A C     1 
ATOM   10397 O O     . ASP B 2 1289 ? 112.090 147.342 134.525 1.00 84.31  ? 1286 ASP A O     1 
ATOM   10398 C CB    . ASP B 2 1289 ? 110.787 144.433 135.474 1.00 84.31  ? 1286 ASP A CB    1 
ATOM   10399 C CG    . ASP B 2 1289 ? 111.174 143.865 136.825 1.00 84.31  ? 1286 ASP A CG    1 
ATOM   10400 O OD1   . ASP B 2 1289 ? 111.341 144.654 137.779 1.00 84.31  ? 1286 ASP A OD1   1 
ATOM   10401 O OD2   . ASP B 2 1289 ? 111.313 142.628 136.933 1.00 84.31  ? 1286 ASP A OD2   1 
ATOM   10402 N N     . LEU B 2 1290 ? 112.323 146.843 136.711 1.00 76.60  ? 1287 LEU A N     1 
ATOM   10403 C CA    . LEU B 2 1290 ? 113.582 147.572 136.870 1.00 76.60  ? 1287 LEU A CA    1 
ATOM   10404 C C     . LEU B 2 1290 ? 114.771 146.637 136.637 1.00 76.60  ? 1287 LEU A C     1 
ATOM   10405 O O     . LEU B 2 1290 ? 115.607 146.403 137.509 1.00 76.60  ? 1287 LEU A O     1 
ATOM   10406 C CB    . LEU B 2 1290 ? 113.646 148.219 138.249 1.00 76.60  ? 1287 LEU A CB    1 
ATOM   10407 C CG    . LEU B 2 1290 ? 112.572 149.259 138.573 1.00 76.60  ? 1287 LEU A CG    1 
ATOM   10408 C CD1   . LEU B 2 1290 ? 112.616 149.633 140.046 1.00 76.60  ? 1287 LEU A CD1   1 
ATOM   10409 C CD2   . LEU B 2 1290 ? 112.743 150.492 137.701 1.00 76.60  ? 1287 LEU A CD2   1 
ATOM   10410 N N     . LYS B 2 1291 ? 114.831 146.098 135.422 1.00 78.96  ? 1288 LYS A N     1 
ATOM   10411 C CA    . LYS B 2 1291 ? 115.868 145.157 135.029 1.00 78.96  ? 1288 LYS A CA    1 
ATOM   10412 C C     . LYS B 2 1291 ? 116.444 145.565 133.680 1.00 78.96  ? 1288 LYS A C     1 
ATOM   10413 O O     . LYS B 2 1291 ? 115.929 146.456 133.000 1.00 78.96  ? 1288 LYS A O     1 
ATOM   10414 C CB    . LYS B 2 1291 ? 115.327 143.721 134.965 1.00 78.96  ? 1288 LYS A CB    1 
ATOM   10415 C CG    . LYS B 2 1291 ? 114.371 143.471 133.810 1.00 78.96  ? 1288 LYS A CG    1 
ATOM   10416 C CD    . LYS B 2 1291 ? 114.372 142.007 133.401 1.00 78.96  ? 1288 LYS A CD    1 
ATOM   10417 C CE    . LYS B 2 1291 ? 113.812 141.125 134.504 1.00 78.96  ? 1288 LYS A CE    1 
ATOM   10418 N NZ    . LYS B 2 1291 ? 113.775 139.691 134.103 1.00 78.96  ? 1288 LYS A NZ    1 
ATOM   10419 N N     . LEU B 2 1292 ? 117.529 144.896 133.298 1.00 66.49  ? 1289 LEU A N     1 
ATOM   10420 C CA    . LEU B 2 1292 ? 118.199 145.161 132.034 1.00 66.49  ? 1289 LEU A CA    1 
ATOM   10421 C C     . LEU B 2 1292 ? 118.548 143.839 131.365 1.00 66.49  ? 1289 LEU A C     1 
ATOM   10422 O O     . LEU B 2 1292 ? 118.701 142.807 132.023 1.00 66.49  ? 1289 LEU A O     1 
ATOM   10423 C CB    . LEU B 2 1292 ? 119.463 146.009 132.231 1.00 66.49  ? 1289 LEU A CB    1 
ATOM   10424 C CG    . LEU B 2 1292 ? 119.235 147.516 132.353 1.00 66.49  ? 1289 LEU A CG    1 
ATOM   10425 C CD1   . LEU B 2 1292 ? 120.522 148.228 132.735 1.00 66.49  ? 1289 LEU A CD1   1 
ATOM   10426 C CD2   . LEU B 2 1292 ? 118.677 148.068 131.054 1.00 66.49  ? 1289 LEU A CD2   1 
ATOM   10427 N N     . GLN B 2 1293 ? 118.668 143.885 130.041 1.00 70.21  ? 1290 GLN A N     1 
ATOM   10428 C CA    . GLN B 2 1293 ? 118.983 142.689 129.275 1.00 70.21  ? 1290 GLN A CA    1 
ATOM   10429 C C     . GLN B 2 1293 ? 120.407 142.223 129.558 1.00 70.21  ? 1290 GLN A C     1 
ATOM   10430 O O     . GLN B 2 1293 ? 121.314 143.025 129.797 1.00 70.21  ? 1290 GLN A O     1 
ATOM   10431 C CB    . GLN B 2 1293 ? 118.808 142.949 127.778 1.00 70.21  ? 1290 GLN A CB    1 
ATOM   10432 C CG    . GLN B 2 1293 ? 117.369 143.186 127.348 1.00 70.21  ? 1290 GLN A CG    1 
ATOM   10433 C CD    . GLN B 2 1293 ? 116.923 144.619 127.559 1.00 70.21  ? 1290 GLN A CD    1 
ATOM   10434 O OE1   . GLN B 2 1293 ? 117.745 145.521 127.717 1.00 70.21  ? 1290 GLN A OE1   1 
ATOM   10435 N NE2   . GLN B 2 1293 ? 115.612 144.835 127.566 1.00 70.21  ? 1290 GLN A NE2   1 
ATOM   10436 N N     . ASN B 2 1294 ? 120.596 140.903 129.529 1.00 67.67  ? 1291 ASN A N     1 
ATOM   10437 C CA    . ASN B 2 1294 ? 121.906 140.295 129.764 1.00 67.67  ? 1291 ASN A CA    1 
ATOM   10438 C C     . ASN B 2 1294 ? 122.739 140.389 128.485 1.00 67.67  ? 1291 ASN A C     1 
ATOM   10439 O O     . ASN B 2 1294 ? 122.995 139.407 127.784 1.00 67.67  ? 1291 ASN A O     1 
ATOM   10440 C CB    . ASN B 2 1294 ? 121.750 138.855 130.230 1.00 67.67  ? 1291 ASN A CB    1 
ATOM   10441 C CG    . ASN B 2 1294 ? 120.979 138.744 131.531 1.00 67.67  ? 1291 ASN A CG    1 
ATOM   10442 O OD1   . ASN B 2 1294 ? 120.697 139.747 132.186 1.00 67.67  ? 1291 ASN A OD1   1 
ATOM   10443 N ND2   . ASN B 2 1294 ? 120.635 137.519 131.912 1.00 67.67  ? 1291 ASN A ND2   1 
ATOM   10444 N N     . GLY B 2 1295 ? 123.164 141.610 128.187 1.00 58.93  ? 1292 GLY A N     1 
ATOM   10445 C CA    . GLY B 2 1295 ? 123.935 141.883 126.994 1.00 58.93  ? 1292 GLY A CA    1 
ATOM   10446 C C     . GLY B 2 1295 ? 123.060 142.221 125.799 1.00 58.93  ? 1292 GLY A C     1 
ATOM   10447 O O     . GLY B 2 1295 ? 121.858 141.960 125.770 1.00 58.93  ? 1292 GLY A O     1 
ATOM   10448 N N     . ILE B 2 1296 ? 123.693 142.817 124.793 1.00 44.73  ? 1293 ILE A N     1 
ATOM   10449 C CA    . ILE B 2 1296 ? 123.025 143.228 123.564 1.00 44.73  ? 1293 ILE A CA    1 
ATOM   10450 C C     . ILE B 2 1296 ? 123.535 142.351 122.430 1.00 44.73  ? 1293 ILE A C     1 
ATOM   10451 O O     . ILE B 2 1296 ? 124.747 142.265 122.198 1.00 44.73  ? 1293 ILE A O     1 
ATOM   10452 C CB    . ILE B 2 1296 ? 123.263 144.714 123.258 1.00 44.73  ? 1293 ILE A CB    1 
ATOM   10453 C CG1   . ILE B 2 1296 ? 122.715 145.589 124.387 1.00 44.73  ? 1293 ILE A CG1   1 
ATOM   10454 C CG2   . ILE B 2 1296 ? 122.641 145.084 121.926 1.00 44.73  ? 1293 ILE A CG2   1 
ATOM   10455 C CD1   . ILE B 2 1296 ? 123.780 146.174 125.283 1.00 44.73  ? 1293 ILE A CD1   1 
ATOM   10456 N N     . SER B 2 1297 ? 122.612 141.700 121.728 1.00 44.73  ? 1294 SER A N     1 
ATOM   10457 C CA    . SER B 2 1297 ? 122.985 140.892 120.578 1.00 44.73  ? 1294 SER A CA    1 
ATOM   10458 C C     . SER B 2 1297 ? 123.540 141.776 119.469 1.00 44.73  ? 1294 SER A C     1 
ATOM   10459 O O     . SER B 2 1297 ? 123.105 142.915 119.275 1.00 44.73  ? 1294 SER A O     1 
ATOM   10460 C CB    . SER B 2 1297 ? 121.780 140.101 120.070 1.00 44.73  ? 1294 SER A CB    1 
ATOM   10461 O OG    . SER B 2 1297 ? 121.267 139.249 121.078 1.00 44.73  ? 1294 SER A OG    1 
ATOM   10462 N N     . ASN B 2 1298 ? 124.523 141.243 118.741 1.00 44.73  ? 1295 ASN A N     1 
ATOM   10463 C CA    . ASN B 2 1298 ? 125.116 141.996 117.642 1.00 44.73  ? 1295 ASN A CA    1 
ATOM   10464 C C     . ASN B 2 1298 ? 124.090 142.284 116.554 1.00 44.73  ? 1295 ASN A C     1 
ATOM   10465 O O     . ASN B 2 1298 ? 124.040 143.396 116.016 1.00 44.73  ? 1295 ASN A O     1 
ATOM   10466 C CB    . ASN B 2 1298 ? 126.309 141.236 117.069 1.00 44.73  ? 1295 ASN A CB    1 
ATOM   10467 C CG    . ASN B 2 1298 ? 127.521 141.293 117.972 1.00 44.73  ? 1295 ASN A CG    1 
ATOM   10468 O OD1   . ASN B 2 1298 ? 127.431 141.721 119.122 1.00 44.73  ? 1295 ASN A OD1   1 
ATOM   10469 N ND2   . ASN B 2 1298 ? 128.663 140.851 117.460 1.00 44.73  ? 1295 ASN A ND2   1 
ATOM   10470 N N     . GLN B 2 1299 ? 123.265 141.293 116.213 1.00 44.73  ? 1296 GLN A N     1 
ATOM   10471 C CA    . GLN B 2 1299 ? 122.220 141.517 115.220 1.00 44.73  ? 1296 GLN A CA    1 
ATOM   10472 C C     . GLN B 2 1299 ? 121.167 142.488 115.736 1.00 44.73  ? 1296 GLN A C     1 
ATOM   10473 O O     . GLN B 2 1299 ? 120.683 143.343 114.985 1.00 44.73  ? 1296 GLN A O     1 
ATOM   10474 C CB    . GLN B 2 1299 ? 121.577 140.190 114.822 1.00 44.73  ? 1296 GLN A CB    1 
ATOM   10475 C CG    . GLN B 2 1299 ? 120.846 140.233 113.490 1.00 44.73  ? 1296 GLN A CG    1 
ATOM   10476 C CD    . GLN B 2 1299 ? 119.430 140.750 113.617 1.00 44.73  ? 1296 GLN A CD    1 
ATOM   10477 O OE1   . GLN B 2 1299 ? 118.771 140.544 114.635 1.00 44.73  ? 1296 GLN A OE1   1 
ATOM   10478 N NE2   . GLN B 2 1299 ? 118.953 141.429 112.582 1.00 44.73  ? 1296 GLN A NE2   1 
ATOM   10479 N N     . ASP B 2 1300 ? 120.792 142.365 117.011 1.00 44.73  ? 1297 ASP A N     1 
ATOM   10480 C CA    . ASP B 2 1300 ? 119.803 143.274 117.580 1.00 44.73  ? 1297 ASP A CA    1 
ATOM   10481 C C     . ASP B 2 1300 ? 120.324 144.704 117.609 1.00 44.73  ? 1297 ASP A C     1 
ATOM   10482 O O     . ASP B 2 1300 ? 119.579 145.650 117.323 1.00 44.73  ? 1297 ASP A O     1 
ATOM   10483 C CB    . ASP B 2 1300 ? 119.412 142.813 118.983 1.00 44.73  ? 1297 ASP A CB    1 
ATOM   10484 C CG    . ASP B 2 1300 ? 117.966 143.116 119.312 1.00 44.73  ? 1297 ASP A CG    1 
ATOM   10485 O OD1   . ASP B 2 1300 ? 117.388 144.021 118.674 1.00 44.73  ? 1297 ASP A OD1   1 
ATOM   10486 O OD2   . ASP B 2 1300 ? 117.405 142.449 120.207 1.00 44.73  ? 1297 ASP A OD2   1 
ATOM   10487 N N     . TRP B 2 1301 ? 121.599 144.884 117.960 1.00 44.73  ? 1298 TRP A N     1 
ATOM   10488 C CA    . TRP B 2 1301 ? 122.195 146.215 117.915 1.00 44.73  ? 1298 TRP A CA    1 
ATOM   10489 C C     . TRP B 2 1301 ? 122.235 146.754 116.492 1.00 44.73  ? 1298 TRP A C     1 
ATOM   10490 O O     . TRP B 2 1301 ? 121.933 147.929 116.257 1.00 44.73  ? 1298 TRP A O     1 
ATOM   10491 C CB    . TRP B 2 1301 ? 123.600 146.183 118.516 1.00 44.73  ? 1298 TRP A CB    1 
ATOM   10492 C CG    . TRP B 2 1301 ? 124.536 147.180 117.905 1.00 44.73  ? 1298 TRP A CG    1 
ATOM   10493 C CD1   . TRP B 2 1301 ? 125.612 146.912 117.114 1.00 44.73  ? 1298 TRP A CD1   1 
ATOM   10494 C CD2   . TRP B 2 1301 ? 124.482 148.605 118.039 1.00 44.73  ? 1298 TRP A CD2   1 
ATOM   10495 N NE1   . TRP B 2 1301 ? 126.231 148.079 116.744 1.00 44.73  ? 1298 TRP A NE1   1 
ATOM   10496 C CE2   . TRP B 2 1301 ? 125.556 149.133 117.298 1.00 44.73  ? 1298 TRP A CE2   1 
ATOM   10497 C CE3   . TRP B 2 1301 ? 123.628 149.484 118.708 1.00 44.73  ? 1298 TRP A CE3   1 
ATOM   10498 C CZ2   . TRP B 2 1301 ? 125.800 150.499 117.209 1.00 44.73  ? 1298 TRP A CZ2   1 
ATOM   10499 C CZ3   . TRP B 2 1301 ? 123.872 150.841 118.620 1.00 44.73  ? 1298 TRP A CZ3   1 
ATOM   10500 C CH2   . TRP B 2 1301 ? 124.949 151.335 117.876 1.00 44.73  ? 1298 TRP A CH2   1 
ATOM   10501 N N     . LEU B 2 1302 ? 122.611 145.910 115.528 1.00 44.73  ? 1299 LEU A N     1 
ATOM   10502 C CA    . LEU B 2 1302 ? 122.657 146.352 114.138 1.00 44.73  ? 1299 LEU A CA    1 
ATOM   10503 C C     . LEU B 2 1302 ? 121.268 146.700 113.622 1.00 44.73  ? 1299 LEU A C     1 
ATOM   10504 O O     . LEU B 2 1302 ? 121.094 147.697 112.912 1.00 44.73  ? 1299 LEU A O     1 
ATOM   10505 C CB    . LEU B 2 1302 ? 123.304 145.278 113.265 1.00 44.73  ? 1299 LEU A CB    1 
ATOM   10506 C CG    . LEU B 2 1302 ? 124.831 145.195 113.321 1.00 44.73  ? 1299 LEU A CG    1 
ATOM   10507 C CD1   . LEU B 2 1302 ? 125.371 144.440 112.120 1.00 44.73  ? 1299 LEU A CD1   1 
ATOM   10508 C CD2   . LEU B 2 1302 ? 125.443 146.583 113.402 1.00 44.73  ? 1299 LEU A CD2   1 
ATOM   10509 N N     . ALA B 2 1303 ? 120.265 145.890 113.967 1.00 44.73  ? 1300 ALA A N     1 
ATOM   10510 C CA    . ALA B 2 1303 ? 118.900 146.186 113.546 1.00 44.73  ? 1300 ALA A CA    1 
ATOM   10511 C C     . ALA B 2 1303 ? 118.406 147.489 114.160 1.00 44.73  ? 1300 ALA A C     1 
ATOM   10512 O O     . ALA B 2 1303 ? 117.701 148.267 113.504 1.00 44.73  ? 1300 ALA A O     1 
ATOM   10513 C CB    . ALA B 2 1303 ? 117.971 145.032 113.919 1.00 44.73  ? 1300 ALA A CB    1 
ATOM   10514 N N     . TYR B 2 1304 ? 118.759 147.741 115.421 1.00 44.73  ? 1301 TYR A N     1 
ATOM   10515 C CA    . TYR B 2 1304 ? 118.341 148.972 116.082 1.00 44.73  ? 1301 TYR A CA    1 
ATOM   10516 C C     . TYR B 2 1304 ? 119.014 150.192 115.465 1.00 44.73  ? 1301 TYR A C     1 
ATOM   10517 O O     . TYR B 2 1304 ? 118.357 151.201 115.184 1.00 44.73  ? 1301 TYR A O     1 
ATOM   10518 C CB    . TYR B 2 1304 ? 118.646 148.885 117.577 1.00 44.73  ? 1301 TYR A CB    1 
ATOM   10519 C CG    . TYR B 2 1304 ? 118.599 150.213 118.297 1.00 44.73  ? 1301 TYR A CG    1 
ATOM   10520 C CD1   . TYR B 2 1304 ? 117.389 150.790 118.651 1.00 44.73  ? 1301 TYR A CD1   1 
ATOM   10521 C CD2   . TYR B 2 1304 ? 119.768 150.877 118.640 1.00 44.73  ? 1301 TYR A CD2   1 
ATOM   10522 C CE1   . TYR B 2 1304 ? 117.343 151.999 119.315 1.00 44.73  ? 1301 TYR A CE1   1 
ATOM   10523 C CE2   . TYR B 2 1304 ? 119.732 152.086 119.304 1.00 44.73  ? 1301 TYR A CE2   1 
ATOM   10524 C CZ    . TYR B 2 1304 ? 118.518 152.642 119.639 1.00 44.73  ? 1301 TYR A CZ    1 
ATOM   10525 O OH    . TYR B 2 1304 ? 118.478 153.847 120.301 1.00 44.73  ? 1301 TYR A OH    1 
ATOM   10526 N N     . ILE B 2 1305 ? 120.330 150.123 115.251 1.00 44.73  ? 1302 ILE A N     1 
ATOM   10527 C CA    . ILE B 2 1305 ? 121.049 151.289 114.748 1.00 44.73  ? 1302 ILE A CA    1 
ATOM   10528 C C     . ILE B 2 1305 ? 120.687 151.563 113.293 1.00 44.73  ? 1302 ILE A C     1 
ATOM   10529 O O     . ILE B 2 1305 ? 120.526 152.720 112.892 1.00 44.73  ? 1302 ILE A O     1 
ATOM   10530 C CB    . ILE B 2 1305 ? 122.569 151.122 114.949 1.00 44.73  ? 1302 ILE A CB    1 
ATOM   10531 C CG1   . ILE B 2 1305 ? 123.285 152.450 114.697 1.00 44.73  ? 1302 ILE A CG1   1 
ATOM   10532 C CG2   . ILE B 2 1305 ? 123.139 150.018 114.067 1.00 44.73  ? 1302 ILE A CG2   1 
ATOM   10533 C CD1   . ILE B 2 1305 ? 122.818 153.573 115.594 1.00 44.73  ? 1302 ILE A CD1   1 
ATOM   10534 N N     . GLN B 2 1306 ? 120.532 150.513 112.482 1.00 44.73  ? 1303 GLN A N     1 
ATOM   10535 C CA    . GLN B 2 1306 ? 120.210 150.723 111.076 1.00 44.73  ? 1303 GLN A CA    1 
ATOM   10536 C C     . GLN B 2 1306 ? 118.823 151.325 110.904 1.00 44.73  ? 1303 GLN A C     1 
ATOM   10537 O O     . GLN B 2 1306 ? 118.585 152.066 109.944 1.00 44.73  ? 1303 GLN A O     1 
ATOM   10538 C CB    . GLN B 2 1306 ? 120.326 149.408 110.307 1.00 44.73  ? 1303 GLN A CB    1 
ATOM   10539 C CG    . GLN B 2 1306 ? 121.759 148.996 110.017 1.00 44.73  ? 1303 GLN A CG    1 
ATOM   10540 C CD    . GLN B 2 1306 ? 121.893 147.521 109.703 1.00 44.73  ? 1303 GLN A CD    1 
ATOM   10541 O OE1   . GLN B 2 1306 ? 121.137 146.696 110.213 1.00 44.73  ? 1303 GLN A OE1   1 
ATOM   10542 N NE2   . GLN B 2 1306 ? 122.863 147.181 108.865 1.00 44.73  ? 1303 GLN A NE2   1 
ATOM   10543 N N     . GLU B 2 1307 ? 117.900 151.021 111.817 1.00 44.73  ? 1304 GLU A N     1 
ATOM   10544 C CA    . GLU B 2 1307 ? 116.579 151.637 111.768 1.00 44.73  ? 1304 GLU A CA    1 
ATOM   10545 C C     . GLU B 2 1307 ? 116.621 153.079 112.257 1.00 44.73  ? 1304 GLU A C     1 
ATOM   10546 O O     . GLU B 2 1307 ? 115.922 153.945 111.718 1.00 44.73  ? 1304 GLU A O     1 
ATOM   10547 C CB    . GLU B 2 1307 ? 115.592 150.818 112.599 1.00 44.73  ? 1304 GLU A CB    1 
ATOM   10548 C CG    . GLU B 2 1307 ? 114.181 151.378 112.625 1.00 44.73  ? 1304 GLU A CG    1 
ATOM   10549 C CD    . GLU B 2 1307 ? 113.219 150.492 113.391 1.00 44.73  ? 1304 GLU A CD    1 
ATOM   10550 O OE1   . GLU B 2 1307 ? 113.620 149.942 114.438 1.00 44.73  ? 1304 GLU A OE1   1 
ATOM   10551 O OE2   . GLU B 2 1307 ? 112.061 150.345 112.947 1.00 44.73  ? 1304 GLU A OE2   1 
ATOM   10552 N N     . LEU B 2 1308 ? 117.438 153.357 113.275 1.00 44.73  ? 1305 LEU A N     1 
ATOM   10553 C CA    . LEU B 2 1308 ? 117.463 154.692 113.867 1.00 44.73  ? 1305 LEU A CA    1 
ATOM   10554 C C     . LEU B 2 1308 ? 118.094 155.708 112.923 1.00 44.73  ? 1305 LEU A C     1 
ATOM   10555 O O     . LEU B 2 1308 ? 117.585 156.825 112.771 1.00 44.73  ? 1305 LEU A O     1 
ATOM   10556 C CB    . LEU B 2 1308 ? 118.210 154.659 115.199 1.00 44.73  ? 1305 LEU A CB    1 
ATOM   10557 C CG    . LEU B 2 1308 ? 118.197 155.956 116.009 1.00 44.73  ? 1305 LEU A CG    1 
ATOM   10558 C CD1   . LEU B 2 1308 ? 116.828 156.188 116.629 1.00 44.73  ? 1305 LEU A CD1   1 
ATOM   10559 C CD2   . LEU B 2 1308 ? 119.278 155.932 117.077 1.00 44.73  ? 1305 LEU A CD2   1 
ATOM   10560 N N     . ARG B 2 1309 ? 119.205 155.343 112.280 1.00 44.73  ? 1306 ARG A N     1 
ATOM   10561 C CA    . ARG B 2 1309 ? 119.884 156.277 111.390 1.00 44.73  ? 1306 ARG A CA    1 
ATOM   10562 C C     . ARG B 2 1309 ? 119.093 156.566 110.122 1.00 44.73  ? 1306 ARG A C     1 
ATOM   10563 O O     . ARG B 2 1309 ? 119.455 157.490 109.386 1.00 44.73  ? 1306 ARG A O     1 
ATOM   10564 C CB    . ARG B 2 1309 ? 121.273 155.752 111.020 1.00 44.73  ? 1306 ARG A CB    1 
ATOM   10565 C CG    . ARG B 2 1309 ? 122.091 155.258 112.199 1.00 44.73  ? 1306 ARG A CG    1 
ATOM   10566 C CD    . ARG B 2 1309 ? 122.978 156.344 112.774 1.00 44.73  ? 1306 ARG A CD    1 
ATOM   10567 N NE    . ARG B 2 1309 ? 122.223 157.296 113.578 1.00 44.73  ? 1306 ARG A NE    1 
ATOM   10568 C CZ    . ARG B 2 1309 ? 122.730 158.405 114.097 1.00 44.73  ? 1306 ARG A CZ    1 
ATOM   10569 N NH1   . ARG B 2 1309 ? 123.998 158.734 113.919 1.00 44.73  ? 1306 ARG A NH1   1 
ATOM   10570 N NH2   . ARG B 2 1309 ? 121.945 159.202 114.816 1.00 44.73  ? 1306 ARG A NH2   1 
ATOM   10571 N N     . ASN B 2 1310 ? 118.037 155.807 109.849 1.00 44.73  ? 1307 ASN A N     1 
ATOM   10572 C CA    . ASN B 2 1310 ? 117.178 156.074 108.704 1.00 44.73  ? 1307 ASN A CA    1 
ATOM   10573 C C     . ASN B 2 1310 ? 116.123 157.120 109.049 1.00 44.73  ? 1307 ASN A C     1 
ATOM   10574 O O     . ASN B 2 1310 ? 116.098 157.655 110.157 1.00 44.73  ? 1307 ASN A O     1 
ATOM   10575 C CB    . ASN B 2 1310 ? 116.506 154.789 108.226 1.00 44.73  ? 1307 ASN A CB    1 
ATOM   10576 C CG    . ASN B 2 1310 ? 117.468 153.859 107.528 1.00 44.73  ? 1307 ASN A CG    1 
ATOM   10577 O OD1   . ASN B 2 1310 ? 118.373 154.303 106.823 1.00 44.73  ? 1307 ASN A OD1   1 
ATOM   10578 N ND2   . ASN B 2 1310 ? 117.276 152.559 107.713 1.00 44.73  ? 1307 ASN A ND2   1 
ATOM   10579 O OXT   . ASN B 2 1310 ? 115.272 157.457 108.225 1.00 31.92  ? 1307 ASN A OXT   1 
ATOM   10580 P P     . DT  C 3 2    ? 140.975 135.148 198.945 1.00 143.24 ? 2    DT  C P     1 
ATOM   10581 O OP1   . DT  C 3 2    ? 141.335 133.714 198.884 1.00 143.24 ? 2    DT  C OP1   1 
ATOM   10582 O OP2   . DT  C 3 2    ? 139.632 135.595 198.512 1.00 143.24 ? 2    DT  C OP2   1 
ATOM   10583 O "O5'" . DT  C 3 2    ? 141.217 135.684 200.434 1.00 143.24 ? 2    DT  C "O5'" 1 
ATOM   10584 C "C5'" . DT  C 3 2    ? 140.782 136.991 200.805 1.00 143.24 ? 2    DT  C "C5'" 1 
ATOM   10585 C "C4'" . DT  C 3 2    ? 141.941 137.973 200.788 1.00 143.24 ? 2    DT  C "C4'" 1 
ATOM   10586 O "O4'" . DT  C 3 2    ? 143.079 137.376 201.448 1.00 143.24 ? 2    DT  C "O4'" 1 
ATOM   10587 C "C3'" . DT  C 3 2    ? 142.438 138.353 199.404 1.00 143.24 ? 2    DT  C "C3'" 1 
ATOM   10588 O "O3'" . DT  C 3 2    ? 141.718 139.475 198.926 1.00 143.24 ? 2    DT  C "O3'" 1 
ATOM   10589 C "C2'" . DT  C 3 2    ? 143.900 138.703 199.652 1.00 143.24 ? 2    DT  C "C2'" 1 
ATOM   10590 C "C1'" . DT  C 3 2    ? 144.276 137.780 200.812 1.00 143.24 ? 2    DT  C "C1'" 1 
ATOM   10591 N N1    . DT  C 3 2    ? 145.035 136.560 200.403 1.00 143.24 ? 2    DT  C N1    1 
ATOM   10592 C C2    . DT  C 3 2    ? 146.317 136.693 199.927 1.00 143.24 ? 2    DT  C C2    1 
ATOM   10593 O O2    . DT  C 3 2    ? 146.870 137.770 199.787 1.00 143.24 ? 2    DT  C O2    1 
ATOM   10594 N N3    . DT  C 3 2    ? 146.924 135.520 199.575 1.00 143.24 ? 2    DT  C N3    1 
ATOM   10595 C C4    . DT  C 3 2    ? 146.403 134.244 199.694 1.00 143.24 ? 2    DT  C C4    1 
ATOM   10596 O O4    . DT  C 3 2    ? 147.035 133.249 199.363 1.00 143.24 ? 2    DT  C O4    1 
ATOM   10597 C C5    . DT  C 3 2    ? 145.058 134.171 200.212 1.00 143.24 ? 2    DT  C C5    1 
ATOM   10598 C C7    . DT  C 3 2    ? 144.382 132.842 200.372 1.00 143.24 ? 2    DT  C C7    1 
ATOM   10599 C C6    . DT  C 3 2    ? 144.447 135.319 200.542 1.00 143.24 ? 2    DT  C C6    1 
ATOM   10600 P P     . DA  C 3 3    ? 141.653 139.767 197.349 1.00 111.15 ? 3    DA  C P     1 
ATOM   10601 O OP1   . DA  C 3 3    ? 140.310 140.308 197.041 1.00 111.15 ? 3    DA  C OP1   1 
ATOM   10602 O OP2   . DA  C 3 3    ? 142.113 138.527 196.686 1.00 111.15 ? 3    DA  C OP2   1 
ATOM   10603 O "O5'" . DA  C 3 3    ? 142.742 140.923 197.117 1.00 111.15 ? 3    DA  C "O5'" 1 
ATOM   10604 C "C5'" . DA  C 3 3    ? 142.370 142.118 196.426 1.00 111.15 ? 3    DA  C "C5'" 1 
ATOM   10605 C "C4'" . DA  C 3 3    ? 143.582 142.975 196.093 1.00 111.15 ? 3    DA  C "C4'" 1 
ATOM   10606 O "O4'" . DA  C 3 3    ? 144.721 142.130 195.818 1.00 111.15 ? 3    DA  C "O4'" 1 
ATOM   10607 C "C3'" . DA  C 3 3    ? 143.446 143.791 194.832 1.00 111.15 ? 3    DA  C "C3'" 1 
ATOM   10608 O "O3'" . DA  C 3 3    ? 144.464 144.778 194.808 1.00 111.15 ? 3    DA  C "O3'" 1 
ATOM   10609 C "C2'" . DA  C 3 3    ? 143.684 142.718 193.772 1.00 111.15 ? 3    DA  C "C2'" 1 
ATOM   10610 C "C1'" . DA  C 3 3    ? 144.813 141.905 194.415 1.00 111.15 ? 3    DA  C "C1'" 1 
ATOM   10611 N N9    . DA  C 3 3    ? 144.717 140.464 194.216 1.00 111.15 ? 3    DA  C N9    1 
ATOM   10612 C C8    . DA  C 3 3    ? 143.658 139.668 194.534 1.00 111.15 ? 3    DA  C C8    1 
ATOM   10613 N N7    . DA  C 3 3    ? 143.857 138.397 194.296 1.00 111.15 ? 3    DA  C N7    1 
ATOM   10614 C C5    . DA  C 3 3    ? 145.144 138.351 193.797 1.00 111.15 ? 3    DA  C C5    1 
ATOM   10615 C C6    . DA  C 3 3    ? 145.943 137.285 193.352 1.00 111.15 ? 3    DA  C C6    1 
ATOM   10616 N N6    . DA  C 3 3    ? 145.529 136.015 193.346 1.00 111.15 ? 3    DA  C N6    1 
ATOM   10617 N N1    . DA  C 3 3    ? 147.185 137.573 192.914 1.00 111.15 ? 3    DA  C N1    1 
ATOM   10618 C C2    . DA  C 3 3    ? 147.592 138.850 192.924 1.00 111.15 ? 3    DA  C C2    1 
ATOM   10619 N N3    . DA  C 3 3    ? 146.928 139.938 193.321 1.00 111.15 ? 3    DA  C N3    1 
ATOM   10620 C C4    . DA  C 3 3    ? 145.698 139.615 193.751 1.00 111.15 ? 3    DA  C C4    1 
ATOM   10621 P P     . DG  C 3 4    ? 144.365 146.033 193.813 1.00 96.86  ? 4    DG  C P     1 
ATOM   10622 O OP1   . DG  C 3 4    ? 144.611 147.256 194.607 1.00 96.86  ? 4    DG  C OP1   1 
ATOM   10623 O OP2   . DG  C 3 4    ? 143.113 145.897 193.036 1.00 96.86  ? 4    DG  C OP2   1 
ATOM   10624 O "O5'" . DG  C 3 4    ? 145.595 145.817 192.816 1.00 96.86  ? 4    DG  C "O5'" 1 
ATOM   10625 C "C5'" . DG  C 3 4    ? 145.881 146.783 191.820 1.00 96.86  ? 4    DG  C "C5'" 1 
ATOM   10626 C "C4'" . DG  C 3 4    ? 147.292 146.607 191.295 1.00 96.86  ? 4    DG  C "C4'" 1 
ATOM   10627 O "O4'" . DG  C 3 4    ? 147.659 145.210 191.364 1.00 96.86  ? 4    DG  C "O4'" 1 
ATOM   10628 C "C3'" . DG  C 3 4    ? 147.473 146.957 189.838 1.00 96.86  ? 4    DG  C "C3'" 1 
ATOM   10629 O "O3'" . DG  C 3 4    ? 148.857 147.124 189.571 1.00 96.86  ? 4    DG  C "O3'" 1 
ATOM   10630 C "C2'" . DG  C 3 4    ? 146.924 145.699 189.172 1.00 96.86  ? 4    DG  C "C2'" 1 
ATOM   10631 C "C1'" . DG  C 3 4    ? 147.494 144.614 190.085 1.00 96.86  ? 4    DG  C "C1'" 1 
ATOM   10632 N N9    . DG  C 3 4    ? 146.637 143.443 190.250 1.00 96.86  ? 4    DG  C N9    1 
ATOM   10633 C C8    . DG  C 3 4    ? 145.388 143.408 190.819 1.00 96.86  ? 4    DG  C C8    1 
ATOM   10634 N N7    . DG  C 3 4    ? 144.869 142.213 190.859 1.00 96.86  ? 4    DG  C N7    1 
ATOM   10635 C C5    . DG  C 3 4    ? 145.841 141.399 190.298 1.00 96.86  ? 4    DG  C C5    1 
ATOM   10636 C C6    . DG  C 3 4    ? 145.842 140.001 190.079 1.00 96.86  ? 4    DG  C C6    1 
ATOM   10637 O O6    . DG  C 3 4    ? 144.953 139.179 190.344 1.00 96.86  ? 4    DG  C O6    1 
ATOM   10638 N N1    . DG  C 3 4    ? 147.025 139.575 189.480 1.00 96.86  ? 4    DG  C N1    1 
ATOM   10639 C C2    . DG  C 3 4    ? 148.077 140.399 189.142 1.00 96.86  ? 4    DG  C C2    1 
ATOM   10640 N N2    . DG  C 3 4    ? 149.138 139.806 188.569 1.00 96.86  ? 4    DG  C N2    1 
ATOM   10641 N N3    . DG  C 3 4    ? 148.087 141.711 189.343 1.00 96.86  ? 4    DG  C N3    1 
ATOM   10642 C C4    . DG  C 3 4    ? 146.940 142.140 189.923 1.00 96.86  ? 4    DG  C C4    1 
ATOM   10643 P P     . DT  C 3 5    ? 149.346 147.895 188.251 1.00 79.33  ? 5    DT  C P     1 
ATOM   10644 O OP1   . DT  C 3 5    ? 150.738 148.339 188.482 1.00 79.33  ? 5    DT  C OP1   1 
ATOM   10645 O OP2   . DT  C 3 5    ? 148.306 148.887 187.900 1.00 79.33  ? 5    DT  C OP2   1 
ATOM   10646 O "O5'" . DT  C 3 5    ? 149.344 146.759 187.128 1.00 79.33  ? 5    DT  C "O5'" 1 
ATOM   10647 C "C5'" . DT  C 3 5    ? 149.996 145.516 187.373 1.00 79.33  ? 5    DT  C "C5'" 1 
ATOM   10648 C "C4'" . DT  C 3 5    ? 149.787 144.566 186.209 1.00 79.33  ? 5    DT  C "C4'" 1 
ATOM   10649 O "O4'" . DT  C 3 5    ? 148.883 143.496 186.598 1.00 79.33  ? 5    DT  C "O4'" 1 
ATOM   10650 C "C3'" . DT  C 3 5    ? 149.169 145.206 184.960 1.00 79.33  ? 5    DT  C "C3'" 1 
ATOM   10651 O "O3'" . DT  C 3 5    ? 149.804 144.730 183.764 1.00 79.33  ? 5    DT  C "O3'" 1 
ATOM   10652 C "C2'" . DT  C 3 5    ? 147.719 144.736 185.030 1.00 79.33  ? 5    DT  C "C2'" 1 
ATOM   10653 C "C1'" . DT  C 3 5    ? 147.917 143.340 185.588 1.00 79.33  ? 5    DT  C "C1'" 1 
ATOM   10654 N N1    . DT  C 3 5    ? 146.688 142.734 186.173 1.00 79.33  ? 5    DT  C N1    1 
ATOM   10655 C C2    . DT  C 3 5    ? 146.511 141.376 186.087 1.00 79.33  ? 5    DT  C C2    1 
ATOM   10656 O O2    . DT  C 3 5    ? 147.318 140.631 185.562 1.00 79.33  ? 5    DT  C O2    1 
ATOM   10657 N N3    . DT  C 3 5    ? 145.350 140.912 186.644 1.00 79.33  ? 5    DT  C N3    1 
ATOM   10658 C C4    . DT  C 3 5    ? 144.367 141.658 187.265 1.00 79.33  ? 5    DT  C C4    1 
ATOM   10659 O O4    . DT  C 3 5    ? 143.356 141.147 187.736 1.00 79.33  ? 5    DT  C O4    1 
ATOM   10660 C C5    . DT  C 3 5    ? 144.612 143.080 187.316 1.00 79.33  ? 5    DT  C C5    1 
ATOM   10661 C C7    . DT  C 3 5    ? 143.615 143.995 187.963 1.00 79.33  ? 5    DT  C C7    1 
ATOM   10662 C C6    . DT  C 3 5    ? 145.747 143.544 186.770 1.00 79.33  ? 5    DT  C C6    1 
ATOM   10663 P P     . DG  C 3 6    ? 151.256 144.035 183.786 1.00 69.24  ? 6    DG  C P     1 
ATOM   10664 O OP1   . DG  C 3 6    ? 151.120 142.652 184.297 1.00 69.24  ? 6    DG  C OP1   1 
ATOM   10665 O OP2   . DG  C 3 6    ? 152.230 144.973 184.387 1.00 69.24  ? 6    DG  C OP2   1 
ATOM   10666 O "O5'" . DG  C 3 6    ? 151.627 143.916 182.238 1.00 69.24  ? 6    DG  C "O5'" 1 
ATOM   10667 C "C5'" . DG  C 3 6    ? 152.148 142.700 181.730 1.00 69.24  ? 6    DG  C "C5'" 1 
ATOM   10668 C "C4'" . DG  C 3 6    ? 151.099 141.951 180.927 1.00 69.24  ? 6    DG  C "C4'" 1 
ATOM   10669 O "O4'" . DG  C 3 6    ? 149.898 141.799 181.706 1.00 69.24  ? 6    DG  C "O4'" 1 
ATOM   10670 C "C3'" . DG  C 3 6    ? 150.664 142.630 179.626 1.00 69.24  ? 6    DG  C "C3'" 1 
ATOM   10671 O "O3'" . DG  C 3 6    ? 151.216 141.921 178.516 1.00 69.24  ? 6    DG  C "O3'" 1 
ATOM   10672 C "C2'" . DG  C 3 6    ? 149.123 142.571 179.651 1.00 69.24  ? 6    DG  C "C2'" 1 
ATOM   10673 C "C1'" . DG  C 3 6    ? 148.823 141.646 180.821 1.00 69.24  ? 6    DG  C "C1'" 1 
ATOM   10674 N N9    . DG  C 3 6    ? 147.593 141.982 181.530 1.00 69.24  ? 6    DG  C N9    1 
ATOM   10675 C C8    . DG  C 3 6    ? 147.190 143.228 181.940 1.00 69.24  ? 6    DG  C C8    1 
ATOM   10676 N N7    . DG  C 3 6    ? 146.044 143.225 182.560 1.00 69.24  ? 6    DG  C N7    1 
ATOM   10677 C C5    . DG  C 3 6    ? 145.662 141.892 182.563 1.00 69.24  ? 6    DG  C C5    1 
ATOM   10678 C C6    . DG  C 3 6    ? 144.506 141.280 183.094 1.00 69.24  ? 6    DG  C C6    1 
ATOM   10679 O O6    . DG  C 3 6    ? 143.562 141.816 183.687 1.00 69.24  ? 6    DG  C O6    1 
ATOM   10680 N N1    . DG  C 3 6    ? 144.507 139.904 182.883 1.00 69.24  ? 6    DG  C N1    1 
ATOM   10681 C C2    . DG  C 3 6    ? 145.502 139.209 182.235 1.00 69.24  ? 6    DG  C C2    1 
ATOM   10682 N N2    . DG  C 3 6    ? 145.331 137.883 182.121 1.00 69.24  ? 6    DG  C N2    1 
ATOM   10683 N N3    . DG  C 3 6    ? 146.592 139.774 181.734 1.00 69.24  ? 6    DG  C N3    1 
ATOM   10684 C C4    . DG  C 3 6    ? 146.604 141.113 181.933 1.00 69.24  ? 6    DG  C C4    1 
HETATM 10685 P P     . 2YR C 3 7    ? 150.605 142.072 177.037 1.00 57.13  ? 7    2YR C P     1 
HETATM 10686 O OP1   . 2YR C 3 7    ? 151.683 141.677 176.105 1.00 57.13  ? 7    2YR C OP1   1 
HETATM 10687 O OP2   . 2YR C 3 7    ? 149.993 143.412 176.885 1.00 57.13  ? 7    2YR C OP2   1 
HETATM 10688 O "O5'" . 2YR C 3 7    ? 149.465 140.950 176.992 1.00 57.13  ? 7    2YR C "O5'" 1 
HETATM 10689 C "C5'" . 2YR C 3 7    ? 149.748 139.653 177.499 1.00 57.13  ? 7    2YR C "C5'" 1 
HETATM 10690 C "C4'" . 2YR C 3 7    ? 148.511 138.772 177.508 1.00 57.13  ? 7    2YR C "C4'" 1 
HETATM 10691 O "O4'" . 2YR C 3 7    ? 147.528 139.306 178.433 1.00 57.13  ? 7    2YR C "O4'" 1 
HETATM 10692 C "C3'" . 2YR C 3 7    ? 147.799 138.624 176.161 1.00 57.13  ? 7    2YR C "C3'" 1 
HETATM 10693 O "O3'" . 2YR C 3 7    ? 147.519 137.252 175.917 1.00 57.13  ? 7    2YR C "O3'" 1 
HETATM 10694 C "C2'" . 2YR C 3 7    ? 146.519 139.432 176.350 1.00 57.13  ? 7    2YR C "C2'" 1 
HETATM 10695 C "C1'" . 2YR C 3 7    ? 146.261 139.257 177.831 1.00 57.13  ? 7    2YR C "C1'" 1 
HETATM 10696 N N1    . 2YR C 3 7    ? 145.425 140.331 178.415 1.00 57.13  ? 7    2YR C N1    1 
HETATM 10697 C C2    . 2YR C 3 7    ? 144.233 140.002 179.067 1.00 57.13  ? 7    2YR C C2    1 
HETATM 10698 O O2    . 2YR C 3 7    ? 143.901 138.813 179.141 1.00 57.13  ? 7    2YR C O2    1 
HETATM 10699 N N3    . 2YR C 3 7    ? 143.481 140.998 179.599 1.00 57.13  ? 7    2YR C N3    1 
HETATM 10700 C C4    . 2YR C 3 7    ? 143.888 142.267 179.492 1.00 57.13  ? 7    2YR C C4    1 
HETATM 10701 N N4    . 2YR C 3 7    ? 143.125 143.221 180.028 1.00 57.13  ? 7    2YR C N4    1 
HETATM 10702 C C5    . 2YR C 3 7    ? 145.100 142.614 178.830 1.00 57.13  ? 7    2YR C C5    1 
HETATM 10703 C C6    . 2YR C 3 7    ? 145.828 141.625 178.312 1.00 57.13  ? 7    2YR C C6    1 
HETATM 10704 S S     . 2YR C 3 7    ? 144.662 146.884 179.359 1.00 52.20  ? 7    2YR C S     1 
HETATM 10705 C C8    . 2YR C 3 7    ? 143.512 145.485 179.351 1.00 52.20  ? 7    2YR C C8    1 
HETATM 10706 C C9    . 2YR C 3 7    ? 143.783 144.453 180.442 1.00 52.20  ? 7    2YR C C9    1 
ATOM   10707 P P     . DT  C 3 8    ? 146.812 136.785 174.551 1.00 52.37  ? 8    DT  C P     1 
ATOM   10708 O OP1   . DT  C 3 8    ? 147.516 135.568 174.096 1.00 52.37  ? 8    DT  C OP1   1 
ATOM   10709 O OP2   . DT  C 3 8    ? 146.691 137.944 173.639 1.00 52.37  ? 8    DT  C OP2   1 
ATOM   10710 O "O5'" . DT  C 3 8    ? 145.349 136.345 175.013 1.00 52.37  ? 8    DT  C "O5'" 1 
ATOM   10711 C "C5'" . DT  C 3 8    ? 145.188 135.170 175.790 1.00 52.37  ? 8    DT  C "C5'" 1 
ATOM   10712 C "C4'" . DT  C 3 8    ? 143.726 134.912 176.107 1.00 52.37  ? 8    DT  C "C4'" 1 
ATOM   10713 O "O4'" . DT  C 3 8    ? 143.141 136.086 176.736 1.00 52.37  ? 8    DT  C "O4'" 1 
ATOM   10714 C "C3'" . DT  C 3 8    ? 142.834 134.611 174.904 1.00 52.37  ? 8    DT  C "C3'" 1 
ATOM   10715 O "O3'" . DT  C 3 8    ? 141.801 133.713 175.315 1.00 52.37  ? 8    DT  C "O3'" 1 
ATOM   10716 C "C2'" . DT  C 3 8    ? 142.277 135.993 174.584 1.00 52.37  ? 8    DT  C "C2'" 1 
ATOM   10717 C "C1'" . DT  C 3 8    ? 142.014 136.496 175.988 1.00 52.37  ? 8    DT  C "C1'" 1 
ATOM   10718 N N1    . DT  C 3 8    ? 141.865 137.981 176.126 1.00 52.37  ? 8    DT  C N1    1 
ATOM   10719 C C2    . DT  C 3 8    ? 140.803 138.472 176.843 1.00 52.37  ? 8    DT  C C2    1 
ATOM   10720 O O2    . DT  C 3 8    ? 139.956 137.760 177.352 1.00 52.37  ? 8    DT  C O2    1 
ATOM   10721 N N3    . DT  C 3 8    ? 140.757 139.834 176.942 1.00 52.37  ? 8    DT  C N3    1 
ATOM   10722 C C4    . DT  C 3 8    ? 141.650 140.740 176.413 1.00 52.37  ? 8    DT  C C4    1 
ATOM   10723 O O4    . DT  C 3 8    ? 141.518 141.950 176.562 1.00 52.37  ? 8    DT  C O4    1 
ATOM   10724 C C5    . DT  C 3 8    ? 142.749 140.167 175.680 1.00 52.37  ? 8    DT  C C5    1 
ATOM   10725 C C7    . DT  C 3 8    ? 143.779 141.061 175.059 1.00 52.37  ? 8    DT  C C7    1 
ATOM   10726 C C6    . DT  C 3 8    ? 142.808 138.826 175.574 1.00 52.37  ? 8    DT  C C6    1 
ATOM   10727 P P     . DT  C 3 9    ? 140.775 133.061 174.262 1.00 57.24  ? 9    DT  C P     1 
ATOM   10728 O OP1   . DT  C 3 9    ? 141.157 131.642 174.102 1.00 57.24  ? 9    DT  C OP1   1 
ATOM   10729 O OP2   . DT  C 3 9    ? 140.667 133.922 173.064 1.00 57.24  ? 9    DT  C OP2   1 
ATOM   10730 O "O5'" . DT  C 3 9    ? 139.378 133.123 175.035 1.00 57.24  ? 9    DT  C "O5'" 1 
ATOM   10731 C "C5'" . DT  C 3 9    ? 139.077 134.252 175.849 1.00 57.24  ? 9    DT  C "C5'" 1 
ATOM   10732 C "C4'" . DT  C 3 9    ? 137.632 134.228 176.308 1.00 57.24  ? 9    DT  C "C4'" 1 
ATOM   10733 O "O4'" . DT  C 3 9    ? 137.210 135.574 176.631 1.00 57.24  ? 9    DT  C "O4'" 1 
ATOM   10734 C "C3'" . DT  C 3 9    ? 136.641 133.777 175.262 1.00 57.24  ? 9    DT  C "C3'" 1 
ATOM   10735 O "O3'" . DT  C 3 9    ? 135.435 133.381 175.895 1.00 57.24  ? 9    DT  C "O3'" 1 
ATOM   10736 C "C2'" . DT  C 3 9    ? 136.457 135.052 174.447 1.00 57.24  ? 9    DT  C "C2'" 1 
ATOM   10737 C "C1'" . DT  C 3 9    ? 136.522 136.138 175.523 1.00 57.24  ? 9    DT  C "C1'" 1 
ATOM   10738 N N1    . DT  C 3 9    ? 137.258 137.384 175.109 1.00 57.24  ? 9    DT  C N1    1 
ATOM   10739 C C2    . DT  C 3 9    ? 136.825 138.604 175.572 1.00 57.24  ? 9    DT  C C2    1 
ATOM   10740 O O2    . DT  C 3 9    ? 135.849 138.740 176.288 1.00 57.24  ? 9    DT  C O2    1 
ATOM   10741 N N3    . DT  C 3 9    ? 137.577 139.672 175.157 1.00 57.24  ? 9    DT  C N3    1 
ATOM   10742 C C4    . DT  C 3 9    ? 138.695 139.646 174.354 1.00 57.24  ? 9    DT  C C4    1 
ATOM   10743 O O4    . DT  C 3 9    ? 139.302 140.665 174.038 1.00 57.24  ? 9    DT  C O4    1 
ATOM   10744 C C5    . DT  C 3 9    ? 139.101 138.342 173.909 1.00 57.24  ? 9    DT  C C5    1 
ATOM   10745 C C7    . DT  C 3 9    ? 140.300 138.202 173.025 1.00 57.24  ? 9    DT  C C7    1 
ATOM   10746 C C6    . DT  C 3 9    ? 138.380 137.283 174.311 1.00 57.24  ? 9    DT  C C6    1 
ATOM   10747 P P     . DT  C 3 10   ? 134.169 132.917 175.024 1.00 63.64  ? 10   DT  C P     1 
ATOM   10748 O OP1   . DT  C 3 10   ? 133.458 131.874 175.795 1.00 63.64  ? 10   DT  C OP1   1 
ATOM   10749 O OP2   . DT  C 3 10   ? 134.633 132.621 173.651 1.00 63.64  ? 10   DT  C OP2   1 
ATOM   10750 O "O5'" . DT  C 3 10   ? 133.254 134.224 174.967 1.00 63.64  ? 10   DT  C "O5'" 1 
ATOM   10751 C "C5'" . DT  C 3 10   ? 132.850 134.864 176.176 1.00 63.64  ? 10   DT  C "C5'" 1 
ATOM   10752 C "C4'" . DT  C 3 10   ? 131.896 136.013 175.895 1.00 63.64  ? 10   DT  C "C4'" 1 
ATOM   10753 O "O4'" . DT  C 3 10   ? 132.648 137.207 175.547 1.00 63.64  ? 10   DT  C "O4'" 1 
ATOM   10754 C "C3'" . DT  C 3 10   ? 130.932 135.786 174.738 1.00 63.64  ? 10   DT  C "C3'" 1 
ATOM   10755 O "O3'" . DT  C 3 10   ? 129.709 136.459 175.004 1.00 63.64  ? 10   DT  C "O3'" 1 
ATOM   10756 C "C2'" . DT  C 3 10   ? 131.679 136.429 173.573 1.00 63.64  ? 10   DT  C "C2'" 1 
ATOM   10757 C "C1'" . DT  C 3 10   ? 132.260 137.651 174.263 1.00 63.64  ? 10   DT  C "C1'" 1 
ATOM   10758 N N1    . DT  C 3 10   ? 133.461 138.242 173.589 1.00 63.64  ? 10   DT  C N1    1 
ATOM   10759 C C2    . DT  C 3 10   ? 133.648 139.603 173.637 1.00 63.64  ? 10   DT  C C2    1 
ATOM   10760 O O2    . DT  C 3 10   ? 132.869 140.364 174.180 1.00 63.64  ? 10   DT  C O2    1 
ATOM   10761 N N3    . DT  C 3 10   ? 134.781 140.049 173.011 1.00 63.64  ? 10   DT  C N3    1 
ATOM   10762 C C4    . DT  C 3 10   ? 135.733 139.286 172.366 1.00 63.64  ? 10   DT  C C4    1 
ATOM   10763 O O4    . DT  C 3 10   ? 136.718 139.780 171.830 1.00 63.64  ? 10   DT  C O4    1 
ATOM   10764 C C5    . DT  C 3 10   ? 135.483 137.868 172.353 1.00 63.64  ? 10   DT  C C5    1 
ATOM   10765 C C7    . DT  C 3 10   ? 136.446 136.946 171.664 1.00 63.64  ? 10   DT  C C7    1 
ATOM   10766 C C6    . DT  C 3 10   ? 134.372 137.416 172.962 1.00 63.64  ? 10   DT  C C6    1 
ATOM   10767 P P     . DG  C 3 11   ? 128.306 135.700 174.823 1.00 65.66  ? 11   DG  C P     1 
ATOM   10768 O OP1   . DG  C 3 11   ? 127.781 135.388 176.170 1.00 65.66  ? 11   DG  C OP1   1 
ATOM   10769 O OP2   . DG  C 3 11   ? 128.515 134.609 173.846 1.00 65.66  ? 11   DG  C OP2   1 
ATOM   10770 O "O5'" . DG  C 3 11   ? 127.355 136.808 174.165 1.00 65.66  ? 11   DG  C "O5'" 1 
ATOM   10771 C "C5'" . DG  C 3 11   ? 127.077 138.022 174.861 1.00 65.66  ? 11   DG  C "C5'" 1 
ATOM   10772 C "C4'" . DG  C 3 11   ? 127.041 139.196 173.898 1.00 65.66  ? 11   DG  C "C4'" 1 
ATOM   10773 O "O4'" . DG  C 3 11   ? 128.382 139.649 173.660 1.00 65.66  ? 11   DG  C "O4'" 1 
ATOM   10774 C "C3'" . DG  C 3 11   ? 126.465 138.871 172.528 1.00 65.66  ? 11   DG  C "C3'" 1 
ATOM   10775 O "O3'" . DG  C 3 11   ? 125.107 139.284 172.467 1.00 65.66  ? 11   DG  C "O3'" 1 
ATOM   10776 C "C2'" . DG  C 3 11   ? 127.336 139.661 171.535 1.00 65.66  ? 11   DG  C "C2'" 1 
ATOM   10777 C "C1'" . DG  C 3 11   ? 128.471 140.236 172.386 1.00 65.66  ? 11   DG  C "C1'" 1 
ATOM   10778 N N9    . DG  C 3 11   ? 129.797 139.940 171.865 1.00 65.66  ? 11   DG  C N9    1 
ATOM   10779 C C8    . DG  C 3 11   ? 130.348 138.701 171.710 1.00 65.66  ? 11   DG  C C8    1 
ATOM   10780 N N7    . DG  C 3 11   ? 131.563 138.724 171.246 1.00 65.66  ? 11   DG  C N7    1 
ATOM   10781 C C5    . DG  C 3 11   ? 131.836 140.070 171.080 1.00 65.66  ? 11   DG  C C5    1 
ATOM   10782 C C6    . DG  C 3 11   ? 133.004 140.703 170.603 1.00 65.66  ? 11   DG  C C6    1 
ATOM   10783 O O6    . DG  C 3 11   ? 134.056 140.177 170.222 1.00 65.66  ? 11   DG  C O6    1 
ATOM   10784 N N1    . DG  C 3 11   ? 132.874 142.085 170.594 1.00 65.66  ? 11   DG  C N1    1 
ATOM   10785 C C2    . DG  C 3 11   ? 131.752 142.771 170.992 1.00 65.66  ? 11   DG  C C2    1 
ATOM   10786 N N2    . DG  C 3 11   ? 131.814 144.108 170.911 1.00 65.66  ? 11   DG  C N2    1 
ATOM   10787 N N3    . DG  C 3 11   ? 130.646 142.188 171.444 1.00 65.66  ? 11   DG  C N3    1 
ATOM   10788 C C4    . DG  C 3 11   ? 130.761 140.838 171.461 1.00 65.66  ? 11   DG  C C4    1 
ATOM   10789 P P     . DT  C 3 12   ? 123.927 138.219 172.694 1.00 68.83  ? 12   DT  C P     1 
ATOM   10790 O OP1   . DT  C 3 12   ? 123.542 138.261 174.119 1.00 68.83  ? 12   DT  C OP1   1 
ATOM   10791 O OP2   . DT  C 3 12   ? 124.349 136.940 172.083 1.00 68.83  ? 12   DT  C OP2   1 
ATOM   10792 O "O5'" . DT  C 3 12   ? 122.719 138.796 171.826 1.00 68.83  ? 12   DT  C "O5'" 1 
ATOM   10793 C "C5'" . DT  C 3 12   ? 122.614 138.463 170.451 1.00 68.83  ? 12   DT  C "C5'" 1 
ATOM   10794 C "C4'" . DT  C 3 12   ? 123.261 139.525 169.582 1.00 68.83  ? 12   DT  C "C4'" 1 
ATOM   10795 O "O4'" . DT  C 3 12   ? 124.688 139.410 169.664 1.00 68.83  ? 12   DT  C "O4'" 1 
ATOM   10796 C "C3'" . DT  C 3 12   ? 122.943 139.403 168.101 1.00 68.83  ? 12   DT  C "C3'" 1 
ATOM   10797 O "O3'" . DT  C 3 12   ? 121.867 140.271 167.768 1.00 68.83  ? 12   DT  C "O3'" 1 
ATOM   10798 C "C2'" . DT  C 3 12   ? 124.248 139.812 167.389 1.00 68.83  ? 12   DT  C "C2'" 1 
ATOM   10799 C "C1'" . DT  C 3 12   ? 125.250 140.006 168.523 1.00 68.83  ? 12   DT  C "C1'" 1 
ATOM   10800 N N1    . DT  C 3 12   ? 126.583 139.379 168.279 1.00 68.83  ? 12   DT  C N1    1 
ATOM   10801 C C2    . DT  C 3 12   ? 127.638 140.168 167.884 1.00 68.83  ? 12   DT  C C2    1 
ATOM   10802 O O2    . DT  C 3 12   ? 127.542 141.364 167.696 1.00 68.83  ? 12   DT  C O2    1 
ATOM   10803 N N3    . DT  C 3 12   ? 128.820 139.498 167.707 1.00 68.83  ? 12   DT  C N3    1 
ATOM   10804 C C4    . DT  C 3 12   ? 129.048 138.147 167.888 1.00 68.83  ? 12   DT  C C4    1 
ATOM   10805 O O4    . DT  C 3 12   ? 130.148 137.637 167.704 1.00 68.83  ? 12   DT  C O4    1 
ATOM   10806 C C5    . DT  C 3 12   ? 127.900 137.378 168.308 1.00 68.83  ? 12   DT  C C5    1 
ATOM   10807 C C7    . DT  C 3 12   ? 128.024 135.901 168.535 1.00 68.83  ? 12   DT  C C7    1 
ATOM   10808 C C6    . DT  C 3 12   ? 126.738 138.024 168.483 1.00 68.83  ? 12   DT  C C6    1 
ATOM   10809 P P     . DC  C 3 13   ? 120.354 139.730 167.807 1.00 93.81  ? 13   DC  C P     1 
ATOM   10810 O OP1   . DC  C 3 13   ? 119.887 139.785 169.209 1.00 93.81  ? 13   DC  C OP1   1 
ATOM   10811 O OP2   . DC  C 3 13   ? 120.322 138.447 167.072 1.00 93.81  ? 13   DC  C OP2   1 
ATOM   10812 O "O5'" . DC  C 3 13   ? 119.538 140.805 166.950 1.00 93.81  ? 13   DC  C "O5'" 1 
ATOM   10813 C "C5'" . DC  C 3 13   ? 119.617 142.187 167.275 1.00 93.81  ? 13   DC  C "C5'" 1 
ATOM   10814 C "C4'" . DC  C 3 13   ? 120.234 142.970 166.131 1.00 93.81  ? 13   DC  C "C4'" 1 
ATOM   10815 O "O4'" . DC  C 3 13   ? 121.654 142.705 166.087 1.00 93.81  ? 13   DC  C "O4'" 1 
ATOM   10816 C "C3'" . DC  C 3 13   ? 119.702 142.603 164.756 1.00 93.81  ? 13   DC  C "C3'" 1 
ATOM   10817 O "O3'" . DC  C 3 13   ? 118.598 143.439 164.431 1.00 93.81  ? 13   DC  C "O3'" 1 
ATOM   10818 C "C2'" . DC  C 3 13   ? 120.895 142.867 163.836 1.00 93.81  ? 13   DC  C "C2'" 1 
ATOM   10819 C "C1'" . DC  C 3 13   ? 122.100 142.615 164.748 1.00 93.81  ? 13   DC  C "C1'" 1 
ATOM   10820 N N1    . DC  C 3 13   ? 122.755 141.280 164.556 1.00 93.81  ? 13   DC  C N1    1 
ATOM   10821 C C2    . DC  C 3 13   ? 124.123 141.218 164.269 1.00 93.81  ? 13   DC  C C2    1 
ATOM   10822 O O2    . DC  C 3 13   ? 124.767 142.269 164.168 1.00 93.81  ? 13   DC  C O2    1 
ATOM   10823 N N3    . DC  C 3 13   ? 124.706 140.003 164.109 1.00 93.81  ? 13   DC  C N3    1 
ATOM   10824 C C4    . DC  C 3 13   ? 123.977 138.891 164.228 1.00 93.81  ? 13   DC  C C4    1 
ATOM   10825 N N4    . DC  C 3 13   ? 124.595 137.717 164.063 1.00 93.81  ? 13   DC  C N4    1 
ATOM   10826 C C5    . DC  C 3 13   ? 122.583 138.934 164.523 1.00 93.81  ? 13   DC  C C5    1 
ATOM   10827 C C6    . DC  C 3 13   ? 122.019 140.137 164.679 1.00 93.81  ? 13   DC  C C6    1 
ATOM   10828 P P     . DG  C 3 14   ? 117.293 142.821 163.729 1.00 116.65 ? 14   DG  C P     1 
ATOM   10829 O OP1   . DG  C 3 14   ? 116.115 143.554 164.243 1.00 116.65 ? 14   DG  C OP1   1 
ATOM   10830 O OP2   . DG  C 3 14   ? 117.362 141.349 163.868 1.00 116.65 ? 14   DG  C OP2   1 
ATOM   10831 O "O5'" . DG  C 3 14   ? 117.489 143.175 162.182 1.00 116.65 ? 14   DG  C "O5'" 1 
ATOM   10832 C "C5'" . DG  C 3 14   ? 117.701 142.138 161.237 1.00 116.65 ? 14   DG  C "C5'" 1 
ATOM   10833 C "C4'" . DG  C 3 14   ? 118.650 142.592 160.143 1.00 116.65 ? 14   DG  C "C4'" 1 
ATOM   10834 O "O4'" . DG  C 3 14   ? 120.007 142.599 160.658 1.00 116.65 ? 14   DG  C "O4'" 1 
ATOM   10835 C "C3'" . DG  C 3 14   ? 118.662 141.708 158.900 1.00 116.65 ? 14   DG  C "C3'" 1 
ATOM   10836 O "O3'" . DG  C 3 14   ? 117.843 142.299 157.889 1.00 116.65 ? 14   DG  C "O3'" 1 
ATOM   10837 C "C2'" . DG  C 3 14   ? 120.132 141.687 158.489 1.00 116.65 ? 14   DG  C "C2'" 1 
ATOM   10838 C "C1'" . DG  C 3 14   ? 120.856 141.847 159.817 1.00 116.65 ? 14   DG  C "C1'" 1 
ATOM   10839 N N9    . DG  C 3 14   ? 121.172 140.587 160.490 1.00 116.65 ? 14   DG  C N9    1 
ATOM   10840 C C8    . DG  C 3 14   ? 120.360 139.884 161.345 1.00 116.65 ? 14   DG  C C8    1 
ATOM   10841 N N7    . DG  C 3 14   ? 120.909 138.800 161.811 1.00 116.65 ? 14   DG  C N7    1 
ATOM   10842 C C5    . DG  C 3 14   ? 122.173 138.784 161.236 1.00 116.65 ? 14   DG  C C5    1 
ATOM   10843 C C6    . DG  C 3 14   ? 123.218 137.843 161.373 1.00 116.65 ? 14   DG  C C6    1 
ATOM   10844 O O6    . DG  C 3 14   ? 123.231 136.814 162.060 1.00 116.65 ? 14   DG  C O6    1 
ATOM   10845 N N1    . DG  C 3 14   ? 124.335 138.198 160.626 1.00 116.65 ? 14   DG  C N1    1 
ATOM   10846 C C2    . DG  C 3 14   ? 124.428 139.319 159.836 1.00 116.65 ? 14   DG  C C2    1 
ATOM   10847 N N2    . DG  C 3 14   ? 125.587 139.494 159.182 1.00 116.65 ? 14   DG  C N2    1 
ATOM   10848 N N3    . DG  C 3 14   ? 123.451 140.210 159.695 1.00 116.65 ? 14   DG  C N3    1 
ATOM   10849 C C4    . DG  C 3 14   ? 122.356 139.878 160.423 1.00 116.65 ? 14   DG  C C4    1 
ATOM   10850 P P     . DT  C 3 15   ? 117.671 141.593 156.455 1.00 140.57 ? 15   DT  C P     1 
ATOM   10851 O OP1   . DT  C 3 15   ? 116.477 142.185 155.812 1.00 140.57 ? 15   DT  C OP1   1 
ATOM   10852 O OP2   . DT  C 3 15   ? 117.745 140.130 156.652 1.00 140.57 ? 15   DT  C OP2   1 
ATOM   10853 O "O5'" . DT  C 3 15   ? 118.971 142.052 155.641 1.00 140.57 ? 15   DT  C "O5'" 1 
ATOM   10854 C "C5'" . DT  C 3 15   ? 119.460 141.255 154.570 1.00 140.57 ? 15   DT  C "C5'" 1 
ATOM   10855 C "C4'" . DT  C 3 15   ? 120.975 141.159 154.621 1.00 140.57 ? 15   DT  C "C4'" 1 
ATOM   10856 O "O4'" . DT  C 3 15   ? 121.380 140.563 155.883 1.00 140.57 ? 15   DT  C "O4'" 1 
ATOM   10857 C "C3'" . DT  C 3 15   ? 121.599 140.288 153.539 1.00 140.57 ? 15   DT  C "C3'" 1 
ATOM   10858 O "O3'" . DT  C 3 15   ? 122.892 140.777 153.207 1.00 140.57 ? 15   DT  C "O3'" 1 
ATOM   10859 C "C2'" . DT  C 3 15   ? 121.676 138.931 154.223 1.00 140.57 ? 15   DT  C "C2'" 1 
ATOM   10860 C "C1'" . DT  C 3 15   ? 122.037 139.334 155.646 1.00 140.57 ? 15   DT  C "C1'" 1 
ATOM   10861 N N1    . DT  C 3 15   ? 121.591 138.349 156.674 1.00 140.57 ? 15   DT  C N1    1 
ATOM   10862 C C2    . DT  C 3 15   ? 122.447 137.343 157.058 1.00 140.57 ? 15   DT  C C2    1 
ATOM   10863 O O2    . DT  C 3 15   ? 123.568 137.210 156.603 1.00 140.57 ? 15   DT  C O2    1 
ATOM   10864 N N3    . DT  C 3 15   ? 121.940 136.492 158.004 1.00 140.57 ? 15   DT  C N3    1 
ATOM   10865 C C4    . DT  C 3 15   ? 120.690 136.544 158.590 1.00 140.57 ? 15   DT  C C4    1 
ATOM   10866 O O4    . DT  C 3 15   ? 120.325 135.731 159.433 1.00 140.57 ? 15   DT  C O4    1 
ATOM   10867 C C5    . DT  C 3 15   ? 119.842 137.621 158.142 1.00 140.57 ? 15   DT  C C5    1 
ATOM   10868 C C7    . DT  C 3 15   ? 118.462 137.778 158.708 1.00 140.57 ? 15   DT  C C7    1 
ATOM   10869 C C6    . DT  C 3 15   ? 120.328 138.461 157.215 1.00 140.57 ? 15   DT  C C6    1 
ATOM   10870 P P     . DC  C 3 16   ? 123.474 140.583 151.722 1.00 155.26 ? 16   DC  C P     1 
ATOM   10871 O OP1   . DC  C 3 16   ? 124.703 141.399 151.612 1.00 155.26 ? 16   DC  C OP1   1 
ATOM   10872 O OP2   . DC  C 3 16   ? 122.360 140.798 150.773 1.00 155.26 ? 16   DC  C OP2   1 
ATOM   10873 O "O5'" . DC  C 3 16   ? 123.875 139.035 151.664 1.00 155.26 ? 16   DC  C "O5'" 1 
ATOM   10874 C "C5'" . DC  C 3 16   ? 124.842 138.514 152.569 1.00 155.26 ? 16   DC  C "C5'" 1 
ATOM   10875 C "C4'" . DC  C 3 16   ? 124.993 137.014 152.392 1.00 155.26 ? 16   DC  C "C4'" 1 
ATOM   10876 O "O4'" . DC  C 3 16   ? 124.689 136.348 153.634 1.00 155.26 ? 16   DC  C "O4'" 1 
ATOM   10877 C "C3'" . DC  C 3 16   ? 124.043 136.389 151.391 1.00 155.26 ? 16   DC  C "C3'" 1 
ATOM   10878 O "O3'" . DC  C 3 16   ? 124.574 136.508 150.077 1.00 155.26 ? 16   DC  C "O3'" 1 
ATOM   10879 C "C2'" . DC  C 3 16   ? 124.000 134.929 151.848 1.00 155.26 ? 16   DC  C "C2'" 1 
ATOM   10880 C "C1'" . DC  C 3 16   ? 124.254 135.029 153.360 1.00 155.26 ? 16   DC  C "C1'" 1 
ATOM   10881 N N1    . DC  C 3 16   ? 123.051 134.736 154.194 1.00 155.26 ? 16   DC  C N1    1 
ATOM   10882 C C2    . DC  C 3 16   ? 123.077 133.661 155.087 1.00 155.26 ? 16   DC  C C2    1 
ATOM   10883 O O2    . DC  C 3 16   ? 124.104 132.979 155.167 1.00 155.26 ? 16   DC  C O2    1 
ATOM   10884 N N3    . DC  C 3 16   ? 121.976 133.404 155.838 1.00 155.26 ? 16   DC  C N3    1 
ATOM   10885 C C4    . DC  C 3 16   ? 120.891 134.171 155.715 1.00 155.26 ? 16   DC  C C4    1 
ATOM   10886 N N4    . DC  C 3 16   ? 119.827 133.883 156.474 1.00 155.26 ? 16   DC  C N4    1 
ATOM   10887 C C5    . DC  C 3 16   ? 120.847 135.270 154.808 1.00 155.26 ? 16   DC  C C5    1 
ATOM   10888 C C6    . DC  C 3 16   ? 121.937 135.511 154.074 1.00 155.26 ? 16   DC  C C6    1 
ATOM   10889 P P     . DG  D 4 16   ? 121.834 125.240 165.248 1.00 157.97 ? 16   DG  D P     1 
ATOM   10890 O OP1   . DG  D 4 16   ? 121.847 123.765 165.366 1.00 157.97 ? 16   DG  D OP1   1 
ATOM   10891 O OP2   . DG  D 4 16   ? 122.259 126.077 166.392 1.00 157.97 ? 16   DG  D OP2   1 
ATOM   10892 O "O5'" . DG  D 4 16   ? 122.699 125.669 163.971 1.00 157.97 ? 16   DG  D "O5'" 1 
ATOM   10893 C "C5'" . DG  D 4 16   ? 123.162 124.679 163.061 1.00 157.97 ? 16   DG  D "C5'" 1 
ATOM   10894 C "C4'" . DG  D 4 16   ? 123.793 125.322 161.839 1.00 157.97 ? 16   DG  D "C4'" 1 
ATOM   10895 O "O4'" . DG  D 4 16   ? 122.772 125.997 161.066 1.00 157.97 ? 16   DG  D "O4'" 1 
ATOM   10896 C "C3'" . DG  D 4 16   ? 124.864 126.379 162.145 1.00 157.97 ? 16   DG  D "C3'" 1 
ATOM   10897 O "O3'" . DG  D 4 16   ? 126.127 125.984 161.618 1.00 157.97 ? 16   DG  D "O3'" 1 
ATOM   10898 C "C2'" . DG  D 4 16   ? 124.352 127.651 161.464 1.00 157.97 ? 16   DG  D "C2'" 1 
ATOM   10899 C "C1'" . DG  D 4 16   ? 123.354 127.112 160.452 1.00 157.97 ? 16   DG  D "C1'" 1 
ATOM   10900 N N9    . DG  D 4 16   ? 122.314 128.079 160.120 1.00 157.97 ? 16   DG  D N9    1 
ATOM   10901 C C8    . DG  D 4 16   ? 121.056 128.174 160.664 1.00 157.97 ? 16   DG  D C8    1 
ATOM   10902 N N7    . DG  D 4 16   ? 120.354 129.162 160.176 1.00 157.97 ? 16   DG  D N7    1 
ATOM   10903 C C5    . DG  D 4 16   ? 121.208 129.764 159.258 1.00 157.97 ? 16   DG  D C5    1 
ATOM   10904 C C6    . DG  D 4 16   ? 121.004 130.885 158.417 1.00 157.97 ? 16   DG  D C6    1 
ATOM   10905 O O6    . DG  D 4 16   ? 119.994 131.595 158.313 1.00 157.97 ? 16   DG  D O6    1 
ATOM   10906 N N1    . DG  D 4 16   ? 122.130 131.159 157.641 1.00 157.97 ? 16   DG  D N1    1 
ATOM   10907 C C2    . DG  D 4 16   ? 123.301 130.438 157.674 1.00 157.97 ? 16   DG  D C2    1 
ATOM   10908 N N2    . DG  D 4 16   ? 124.284 130.845 156.859 1.00 157.97 ? 16   DG  D N2    1 
ATOM   10909 N N3    . DG  D 4 16   ? 123.501 129.389 158.458 1.00 157.97 ? 16   DG  D N3    1 
ATOM   10910 C C4    . DG  D 4 16   ? 122.417 129.111 159.218 1.00 157.97 ? 16   DG  D C4    1 
ATOM   10911 P P     . DA  D 4 17   ? 127.461 126.760 162.069 1.00 139.42 ? 17   DA  D P     1 
ATOM   10912 O OP1   . DA  D 4 17   ? 128.596 125.823 161.921 1.00 139.42 ? 17   DA  D OP1   1 
ATOM   10913 O OP2   . DA  D 4 17   ? 127.190 127.387 163.381 1.00 139.42 ? 17   DA  D OP2   1 
ATOM   10914 O "O5'" . DA  D 4 17   ? 127.620 127.937 160.993 1.00 139.42 ? 17   DA  D "O5'" 1 
ATOM   10915 C "C5'" . DA  D 4 17   ? 128.392 127.722 159.813 1.00 139.42 ? 17   DA  D "C5'" 1 
ATOM   10916 C "C4'" . DA  D 4 17   ? 128.695 129.033 159.100 1.00 139.42 ? 17   DA  D "C4'" 1 
ATOM   10917 O "O4'" . DA  D 4 17   ? 127.456 129.728 158.798 1.00 139.42 ? 17   DA  D "O4'" 1 
ATOM   10918 C "C3'" . DA  D 4 17   ? 129.553 130.029 159.882 1.00 139.42 ? 17   DA  D "C3'" 1 
ATOM   10919 O "O3'" . DA  D 4 17   ? 130.427 130.709 158.986 1.00 139.42 ? 17   DA  D "O3'" 1 
ATOM   10920 C "C2'" . DA  D 4 17   ? 128.510 130.977 160.467 1.00 139.42 ? 17   DA  D "C2'" 1 
ATOM   10921 C "C1'" . DA  D 4 17   ? 127.506 131.036 159.329 1.00 139.42 ? 17   DA  D "C1'" 1 
ATOM   10922 N N9    . DA  D 4 17   ? 126.159 131.411 159.744 1.00 139.42 ? 17   DA  D N9    1 
ATOM   10923 C C8    . DA  D 4 17   ? 125.354 130.744 160.622 1.00 139.42 ? 17   DA  D C8    1 
ATOM   10924 N N7    . DA  D 4 17   ? 124.182 131.305 160.798 1.00 139.42 ? 17   DA  D N7    1 
ATOM   10925 C C5    . DA  D 4 17   ? 124.221 132.418 159.977 1.00 139.42 ? 17   DA  D C5    1 
ATOM   10926 C C6    . DA  D 4 17   ? 123.281 133.431 159.710 1.00 139.42 ? 17   DA  D C6    1 
ATOM   10927 N N6    . DA  D 4 17   ? 122.072 133.479 160.277 1.00 139.42 ? 17   DA  D N6    1 
ATOM   10928 N N1    . DA  D 4 17   ? 123.634 134.397 158.836 1.00 139.42 ? 17   DA  D N1    1 
ATOM   10929 C C2    . DA  D 4 17   ? 124.846 134.345 158.271 1.00 139.42 ? 17   DA  D C2    1 
ATOM   10930 N N3    . DA  D 4 17   ? 125.812 133.443 158.442 1.00 139.42 ? 17   DA  D N3    1 
ATOM   10931 C C4    . DA  D 4 17   ? 125.431 132.497 159.316 1.00 139.42 ? 17   DA  D C4    1 
ATOM   10932 P P     . DC  D 4 18   ? 131.755 131.437 159.526 1.00 105.89 ? 18   DC  D P     1 
ATOM   10933 O OP1   . DC  D 4 18   ? 132.907 130.586 159.154 1.00 105.89 ? 18   DC  D OP1   1 
ATOM   10934 O OP2   . DC  D 4 18   ? 131.543 131.805 160.943 1.00 105.89 ? 18   DC  D OP2   1 
ATOM   10935 O "O5'" . DC  D 4 18   ? 131.820 132.788 158.671 1.00 105.89 ? 18   DC  D "O5'" 1 
ATOM   10936 C "C5'" . DC  D 4 18   ? 132.702 133.836 159.057 1.00 105.89 ? 18   DC  D "C5'" 1 
ATOM   10937 C "C4'" . DC  D 4 18   ? 132.059 135.192 158.826 1.00 105.89 ? 18   DC  D "C4'" 1 
ATOM   10938 O "O4'" . DC  D 4 18   ? 130.631 135.075 158.989 1.00 105.89 ? 18   DC  D "O4'" 1 
ATOM   10939 C "C3'" . DC  D 4 18   ? 132.516 136.289 159.789 1.00 105.89 ? 18   DC  D "C3'" 1 
ATOM   10940 O "O3'" . DC  D 4 18   ? 133.269 137.277 159.091 1.00 105.89 ? 18   DC  D "O3'" 1 
ATOM   10941 C "C2'" . DC  D 4 18   ? 131.219 136.871 160.377 1.00 105.89 ? 18   DC  D "C2'" 1 
ATOM   10942 C "C1'" . DC  D 4 18   ? 130.119 136.273 159.508 1.00 105.89 ? 18   DC  D "C1'" 1 
ATOM   10943 N N1    . DC  D 4 18   ? 128.885 135.945 160.273 1.00 105.89 ? 18   DC  D N1    1 
ATOM   10944 C C2    . DC  D 4 18   ? 127.767 136.787 160.199 1.00 105.89 ? 18   DC  D C2    1 
ATOM   10945 O O2    . DC  D 4 18   ? 127.821 137.802 159.493 1.00 105.89 ? 18   DC  D O2    1 
ATOM   10946 N N3    . DC  D 4 18   ? 126.655 136.462 160.909 1.00 105.89 ? 18   DC  D N3    1 
ATOM   10947 C C4    . DC  D 4 18   ? 126.642 135.356 161.658 1.00 105.89 ? 18   DC  D C4    1 
ATOM   10948 N N4    . DC  D 4 18   ? 125.530 135.071 162.341 1.00 105.89 ? 18   DC  D N4    1 
ATOM   10949 C C5    . DC  D 4 18   ? 127.771 134.491 161.742 1.00 105.89 ? 18   DC  D C5    1 
ATOM   10950 C C6    . DC  D 4 18   ? 128.857 134.821 161.041 1.00 105.89 ? 18   DC  D C6    1 
ATOM   10951 P P     A DG  D 4 19   ? 134.761 137.636 159.570 0.90 81.69  ? 19   DG  D P     1 
ATOM   10952 P P     B DG  D 4 19   ? 134.743 137.675 159.592 0.10 81.69  ? 19   DG  D P     1 
ATOM   10953 O OP1   A DG  D 4 19   ? 135.703 136.900 158.698 0.90 81.69  ? 19   DG  D OP1   1 
ATOM   10954 O OP1   B DG  D 4 19   ? 135.459 138.279 158.446 0.10 81.69  ? 19   DG  D OP1   1 
ATOM   10955 O OP2   A DG  D 4 19   ? 134.816 137.448 161.036 0.90 81.69  ? 19   DG  D OP2   1 
ATOM   10956 O OP2   B DG  D 4 19   ? 135.316 136.497 160.279 0.10 81.69  ? 19   DG  D OP2   1 
ATOM   10957 O "O5'" A DG  D 4 19   ? 134.900 139.203 159.274 0.90 81.69  ? 19   DG  D "O5'" 1 
ATOM   10958 O "O5'" B DG  D 4 19   ? 134.486 138.807 160.693 0.10 81.69  ? 19   DG  D "O5'" 1 
ATOM   10959 C "C5'" A DG  D 4 19   ? 135.049 140.122 160.353 0.90 81.69  ? 19   DG  D "C5'" 1 
ATOM   10960 C "C5'" B DG  D 4 19   ? 133.812 140.008 160.337 0.10 81.69  ? 19   DG  D "C5'" 1 
ATOM   10961 C "C4'" A DG  D 4 19   ? 133.719 140.758 160.710 0.90 81.69  ? 19   DG  D "C4'" 1 
ATOM   10962 C "C4'" B DG  D 4 19   ? 134.156 141.123 161.306 0.10 81.69  ? 19   DG  D "C4'" 1 
ATOM   10963 O "O4'" A DG  D 4 19   ? 132.745 139.729 160.946 0.90 81.69  ? 19   DG  D "O4'" 1 
ATOM   10964 O "O4'" B DG  D 4 19   ? 135.584 141.372 161.265 0.10 81.69  ? 19   DG  D "O4'" 1 
ATOM   10965 C "C3'" A DG  D 4 19   ? 133.720 141.572 161.991 0.90 81.69  ? 19   DG  D "C3'" 1 
ATOM   10966 C "C3'" B DG  D 4 19   ? 133.472 142.464 161.022 0.10 81.69  ? 19   DG  D "C3'" 1 
ATOM   10967 O "O3'" A DG  D 4 19   ? 134.134 142.924 161.739 0.90 81.69  ? 19   DG  D "O3'" 1 
ATOM   10968 O "O3'" B DG  D 4 19   ? 132.864 142.964 162.207 0.10 81.69  ? 19   DG  D "O3'" 1 
ATOM   10969 C "C2'" A DG  D 4 19   ? 132.260 141.504 162.456 0.90 81.69  ? 19   DG  D "C2'" 1 
ATOM   10970 C "C2'" B DG  D 4 19   ? 134.611 143.370 160.547 0.10 81.69  ? 19   DG  D "C2'" 1 
ATOM   10971 C "C1'" A DG  D 4 19   ? 131.718 140.246 161.766 0.90 81.69  ? 19   DG  D "C1'" 1 
ATOM   10972 C "C1'" B DG  D 4 19   ? 135.817 142.758 161.242 0.10 81.69  ? 19   DG  D "C1'" 1 
ATOM   10973 N N9    A DG  D 4 19   ? 131.298 139.207 162.698 0.90 81.69  ? 19   DG  D N9    1 
ATOM   10974 N N9    B DG  D 4 19   ? 137.081 143.003 160.549 0.10 81.69  ? 19   DG  D N9    1 
ATOM   10975 C C8    A DG  D 4 19   ? 132.106 138.401 163.461 0.90 81.69  ? 19   DG  D C8    1 
ATOM   10976 C C8    B DG  D 4 19   ? 138.207 143.592 161.072 0.10 81.69  ? 19   DG  D C8    1 
ATOM   10977 N N7    A DG  D 4 19   ? 131.444 137.558 164.203 0.90 81.69  ? 19   DG  D N7    1 
ATOM   10978 N N7    B DG  D 4 19   ? 139.190 143.682 160.220 0.10 81.69  ? 19   DG  D N7    1 
ATOM   10979 C C5    A DG  D 4 19   ? 130.112 137.823 163.912 0.90 81.69  ? 19   DG  D C5    1 
ATOM   10980 C C5    B DG  D 4 19   ? 138.686 143.118 159.056 0.10 81.69  ? 19   DG  D C5    1 
ATOM   10981 C C6    A DG  D 4 19   ? 128.933 137.224 164.411 0.90 81.69  ? 19   DG  D C6    1 
ATOM   10982 C C6    B DG  D 4 19   ? 139.298 142.936 157.793 0.10 81.69  ? 19   DG  D C6    1 
ATOM   10983 O O6    A DG  D 4 19   ? 128.828 136.309 165.240 0.90 81.69  ? 19   DG  D O6    1 
ATOM   10984 O O6    B DG  D 4 19   ? 140.444 143.250 157.443 0.10 81.69  ? 19   DG  D O6    1 
ATOM   10985 N N1    A DG  D 4 19   ? 127.790 137.791 163.851 0.90 81.69  ? 19   DG  D N1    1 
ATOM   10986 N N1    B DG  D 4 19   ? 138.437 142.323 156.887 0.10 81.69  ? 19   DG  D N1    1 
ATOM   10987 C C2    A DG  D 4 19   ? 127.791 138.807 162.925 0.90 81.69  ? 19   DG  D C2    1 
ATOM   10988 C C2    B DG  D 4 19   ? 137.149 141.933 157.166 0.10 81.69  ? 19   DG  D C2    1 
ATOM   10989 N N2    A DG  D 4 19   ? 126.591 139.225 162.497 0.90 81.69  ? 19   DG  D N2    1 
ATOM   10990 N N2    B DG  D 4 19   ? 136.472 141.356 156.162 0.10 81.69  ? 19   DG  D N2    1 
ATOM   10991 N N3    A DG  D 4 19   ? 128.890 139.375 162.450 0.90 81.69  ? 19   DG  D N3    1 
ATOM   10992 N N3    B DG  D 4 19   ? 136.563 142.096 158.345 0.10 81.69  ? 19   DG  D N3    1 
ATOM   10993 C C4    A DG  D 4 19   ? 130.008 138.835 162.986 0.90 81.69  ? 19   DG  D C4    1 
ATOM   10994 C C4    B DG  D 4 19   ? 137.388 142.694 159.240 0.10 81.69  ? 19   DG  D C4    1 
ATOM   10995 P P     A DA  D 4 20   ? 133.694 143.711 160.404 0.90 74.56  ? 20   DA  D P     1 
ATOM   10996 P P     B DA  D 4 20   ? 131.364 143.540 162.163 0.10 74.56  ? 20   DA  D P     1 
ATOM   10997 O OP1   A DA  D 4 20   ? 132.277 143.433 160.082 0.90 74.56  ? 20   DA  D OP1   1 
ATOM   10998 O OP1   B DA  D 4 20   ? 130.517 142.634 162.971 0.10 74.56  ? 20   DA  D OP1   1 
ATOM   10999 O OP2   A DA  D 4 20   ? 134.743 143.480 159.387 0.90 74.56  ? 20   DA  D OP2   1 
ATOM   11000 O OP2   B DA  D 4 20   ? 131.023 143.798 160.747 0.10 74.56  ? 20   DA  D OP2   1 
ATOM   11001 O "O5'" A DA  D 4 20   ? 133.784 145.246 160.834 0.90 74.56  ? 20   DA  D "O5'" 1 
ATOM   11002 O "O5'" B DA  D 4 20   ? 131.470 144.952 162.908 0.10 74.56  ? 20   DA  D "O5'" 1 
ATOM   11003 C "C5'" A DA  D 4 20   ? 134.820 145.677 161.705 0.90 74.56  ? 20   DA  D "C5'" 1 
ATOM   11004 C "C5'" B DA  D 4 20   ? 132.495 145.872 162.547 0.10 74.56  ? 20   DA  D "C5'" 1 
ATOM   11005 C "C4'" A DA  D 4 20   ? 134.261 146.075 163.061 0.90 74.56  ? 20   DA  D "C4'" 1 
ATOM   11006 C "C4'" B DA  D 4 20   ? 133.182 146.421 163.784 0.10 74.56  ? 20   DA  D "C4'" 1 
ATOM   11007 O "O4'" A DA  D 4 20   ? 133.581 144.946 163.661 0.90 74.56  ? 20   DA  D "O4'" 1 
ATOM   11008 O "O4'" B DA  D 4 20   ? 133.178 145.410 164.820 0.10 74.56  ? 20   DA  D "O4'" 1 
ATOM   11009 C "C3'" A DA  D 4 20   ? 135.311 146.540 164.070 0.90 74.56  ? 20   DA  D "C3'" 1 
ATOM   11010 C "C3'" B DA  D 4 20   ? 134.642 146.798 163.591 0.10 74.56  ? 20   DA  D "C3'" 1 
ATOM   11011 O "O3'" A DA  D 4 20   ? 135.001 147.850 164.524 0.90 74.56  ? 20   DA  D "O3'" 1 
ATOM   11012 O "O3'" B DA  D 4 20   ? 135.009 147.835 164.498 0.10 74.56  ? 20   DA  D "O3'" 1 
ATOM   11013 C "C2'" A DA  D 4 20   ? 135.245 145.506 165.203 0.90 74.56  ? 20   DA  D "C2'" 1 
ATOM   11014 C "C2'" B DA  D 4 20   ? 135.355 145.492 163.914 0.10 74.56  ? 20   DA  D "C2'" 1 
ATOM   11015 C "C1'" A DA  D 4 20   ? 133.860 144.898 165.038 0.90 74.56  ? 20   DA  D "C1'" 1 
ATOM   11016 C "C1'" B DA  D 4 20   ? 134.494 144.945 165.048 0.10 74.56  ? 20   DA  D "C1'" 1 
ATOM   11017 N N9    A DA  D 4 20   ? 133.792 143.501 165.461 0.90 74.56  ? 20   DA  D N9    1 
ATOM   11018 N N9    B DA  D 4 20   ? 134.474 143.484 165.114 0.10 74.56  ? 20   DA  D N9    1 
ATOM   11019 C C8    A DA  D 4 20   ? 134.847 142.675 165.730 0.90 74.56  ? 20   DA  D C8    1 
ATOM   11020 C C8    B DA  D 4 20   ? 135.504 142.637 164.817 0.10 74.56  ? 20   DA  D C8    1 
ATOM   11021 N N7    A DA  D 4 20   ? 134.494 141.463 166.086 0.90 74.56  ? 20   DA  D N7    1 
ATOM   11022 N N7    B DA  D 4 20   ? 135.209 141.369 164.969 0.10 74.56  ? 20   DA  D N7    1 
ATOM   11023 C C5    A DA  D 4 20   ? 133.111 141.492 166.045 0.90 74.56  ? 20   DA  D C5    1 
ATOM   11024 C C5    B DA  D 4 20   ? 133.894 141.382 165.400 0.10 74.56  ? 20   DA  D C5    1 
ATOM   11025 C C6    A DA  D 4 20   ? 132.133 140.514 166.315 0.90 74.56  ? 20   DA  D C6    1 
ATOM   11026 C C6    B DA  D 4 20   ? 132.997 140.350 165.739 0.10 74.56  ? 20   DA  D C6    1 
ATOM   11027 N N6    A DA  D 4 20   ? 132.429 139.267 166.697 0.90 74.56  ? 20   DA  D N6    1 
ATOM   11028 N N6    B DA  D 4 20   ? 133.316 139.052 165.691 0.10 74.56  ? 20   DA  D N6    1 
ATOM   11029 N N1    A DA  D 4 20   ? 130.838 140.867 166.179 0.90 74.56  ? 20   DA  D N1    1 
ATOM   11030 N N1    B DA  D 4 20   ? 131.756 140.703 166.131 0.10 74.56  ? 20   DA  D N1    1 
ATOM   11031 C C2    A DA  D 4 20   ? 130.549 142.117 165.795 0.90 74.56  ? 20   DA  D C2    1 
ATOM   11032 C C2    B DA  D 4 20   ? 131.440 142.002 166.178 0.10 74.56  ? 20   DA  D C2    1 
ATOM   11033 N N3    A DA  D 4 20   ? 131.381 143.123 165.513 0.90 74.56  ? 20   DA  D N3    1 
ATOM   11034 N N3    B DA  D 4 20   ? 132.196 143.059 165.884 0.10 74.56  ? 20   DA  D N3    1 
ATOM   11035 C C4    A DA  D 4 20   ? 132.659 142.740 165.659 0.90 74.56  ? 20   DA  D C4    1 
ATOM   11036 C C4    B DA  D 4 20   ? 133.423 142.677 165.497 0.10 74.56  ? 20   DA  D C4    1 
ATOM   11037 P P     . DC  D 4 21   ? 135.820 149.114 163.962 1.00 58.81  ? 21   DC  D P     1 
ATOM   11038 O OP1   . DC  D 4 21   ? 134.867 149.976 163.229 1.00 58.81  ? 21   DC  D OP1   1 
ATOM   11039 O OP2   . DC  D 4 21   ? 137.032 148.613 163.280 1.00 58.81  ? 21   DC  D OP2   1 
ATOM   11040 O "O5'" . DC  D 4 21   ? 136.286 149.881 165.283 1.00 58.81  ? 21   DC  D "O5'" 1 
ATOM   11041 C "C5'" . DC  D 4 21   ? 137.143 149.241 166.216 1.00 58.81  ? 21   DC  D "C5'" 1 
ATOM   11042 C "C4'" . DC  D 4 21   ? 136.392 148.923 167.495 1.00 58.81  ? 21   DC  D "C4'" 1 
ATOM   11043 O "O4'" . DC  D 4 21   ? 135.974 147.548 167.479 1.00 58.81  ? 21   DC  D "O4'" 1 
ATOM   11044 C "C3'" . DC  D 4 21   ? 137.204 149.091 168.777 1.00 58.81  ? 21   DC  D "C3'" 1 
ATOM   11045 O "O3'" . DC  D 4 21   ? 136.801 150.273 169.446 1.00 58.81  ? 21   DC  D "O3'" 1 
ATOM   11046 C "C2'" . DC  D 4 21   ? 136.887 147.835 169.609 1.00 58.81  ? 21   DC  D "C2'" 1 
ATOM   11047 C "C1'" . DC  D 4 21   ? 135.807 147.123 168.802 1.00 58.81  ? 21   DC  D "C1'" 1 
ATOM   11048 N N1    . DC  D 4 21   ? 135.931 145.643 168.837 1.00 58.81  ? 21   DC  D N1    1 
ATOM   11049 C C2    . DC  D 4 21   ? 134.818 144.861 169.157 1.00 58.81  ? 21   DC  D C2    1 
ATOM   11050 O O2    . DC  D 4 21   ? 133.742 145.414 169.404 1.00 58.81  ? 21   DC  D O2    1 
ATOM   11051 N N3    . DC  D 4 21   ? 134.949 143.513 169.187 1.00 58.81  ? 21   DC  D N3    1 
ATOM   11052 C C4    . DC  D 4 21   ? 136.129 142.953 168.913 1.00 58.81  ? 21   DC  D C4    1 
ATOM   11053 N N4    . DC  D 4 21   ? 136.214 141.620 168.954 1.00 58.81  ? 21   DC  D N4    1 
ATOM   11054 C C5    . DC  D 4 21   ? 137.275 143.734 168.587 1.00 58.81  ? 21   DC  D C5    1 
ATOM   11055 C C6    . DC  D 4 21   ? 137.132 145.061 168.562 1.00 58.81  ? 21   DC  D C6    1 
ATOM   11056 P P     . DA  D 4 22   ? 137.718 150.907 170.601 1.00 50.10  ? 22   DA  D P     1 
ATOM   11057 O OP1   . DA  D 4 22   ? 138.043 152.294 170.199 1.00 50.10  ? 22   DA  D OP1   1 
ATOM   11058 O OP2   . DA  D 4 22   ? 138.809 149.958 170.908 1.00 50.10  ? 22   DA  D OP2   1 
ATOM   11059 O "O5'" . DA  D 4 22   ? 136.747 150.953 171.866 1.00 50.10  ? 22   DA  D "O5'" 1 
ATOM   11060 C "C5'" . DA  D 4 22   ? 137.160 150.389 173.092 1.00 50.10  ? 22   DA  D "C5'" 1 
ATOM   11061 C "C4'" . DA  D 4 22   ? 135.962 149.973 173.919 1.00 50.10  ? 22   DA  D "C4'" 1 
ATOM   11062 O "O4'" . DA  D 4 22   ? 135.141 149.067 173.142 1.00 50.10  ? 22   DA  D "O4'" 1 
ATOM   11063 C "C3'" . DA  D 4 22   ? 136.305 149.234 175.205 1.00 50.10  ? 22   DA  D "C3'" 1 
ATOM   11064 O "O3'" . DA  D 4 22   ? 136.362 150.159 176.315 1.00 50.10  ? 22   DA  D "O3'" 1 
ATOM   11065 C "C2'" . DA  D 4 22   ? 135.177 148.216 175.338 1.00 50.10  ? 22   DA  D "C2'" 1 
ATOM   11066 C "C1'" . DA  D 4 22   ? 134.865 147.896 173.883 1.00 50.10  ? 22   DA  D "C1'" 1 
ATOM   11067 N N9    . DA  D 4 22   ? 135.656 146.798 173.328 1.00 50.10  ? 22   DA  D N9    1 
ATOM   11068 C C8    . DA  D 4 22   ? 136.909 146.875 172.790 1.00 50.10  ? 22   DA  D C8    1 
ATOM   11069 N N7    . DA  D 4 22   ? 137.370 145.728 172.356 1.00 50.10  ? 22   DA  D N7    1 
ATOM   11070 C C5    . DA  D 4 22   ? 136.351 144.834 172.630 1.00 50.10  ? 22   DA  D C5    1 
ATOM   11071 C C6    . DA  D 4 22   ? 136.221 143.451 172.413 1.00 50.10  ? 22   DA  D C6    1 
ATOM   11072 N N6    . DA  D 4 22   ? 137.173 142.706 171.844 1.00 50.10  ? 22   DA  D N6    1 
ATOM   11073 N N1    . DA  D 4 22   ? 135.075 142.860 172.804 1.00 50.10  ? 22   DA  D N1    1 
ATOM   11074 C C2    . DA  D 4 22   ? 134.126 143.611 173.373 1.00 50.10  ? 22   DA  D C2    1 
ATOM   11075 N N3    . DA  D 4 22   ? 134.134 144.918 173.629 1.00 50.10  ? 22   DA  D N3    1 
ATOM   11076 C C4    . DA  D 4 22   ? 135.286 145.476 173.229 1.00 50.10  ? 22   DA  D C4    1 
ATOM   11077 P P     . DA  D 4 23   ? 135.039 150.639 177.097 1.00 44.73  ? 23   DA  D P     1 
ATOM   11078 O OP1   . DA  D 4 23   ? 133.926 150.845 176.147 1.00 44.73  ? 23   DA  D OP1   1 
ATOM   11079 O OP2   . DA  D 4 23   ? 135.453 151.771 177.950 1.00 44.73  ? 23   DA  D OP2   1 
ATOM   11080 O "O5'" . DA  D 4 23   ? 134.701 149.423 178.075 1.00 44.73  ? 23   DA  D "O5'" 1 
ATOM   11081 C "C5'" . DA  D 4 23   ? 133.376 149.241 178.542 1.00 44.73  ? 23   DA  D "C5'" 1 
ATOM   11082 C "C4'" . DA  D 4 23   ? 133.116 147.781 178.861 1.00 44.73  ? 23   DA  D "C4'" 1 
ATOM   11083 O "O4'" . DA  D 4 23   ? 133.848 146.943 177.928 1.00 44.73  ? 23   DA  D "O4'" 1 
ATOM   11084 C "C3'" . DA  D 4 23   ? 133.558 147.332 180.256 1.00 44.73  ? 23   DA  D "C3'" 1 
ATOM   11085 O "O3'" . DA  D 4 23   ? 132.621 146.402 180.772 1.00 44.73  ? 23   DA  D "O3'" 1 
ATOM   11086 C "C2'" . DA  D 4 23   ? 134.895 146.665 179.974 1.00 44.73  ? 23   DA  D "C2'" 1 
ATOM   11087 C "C1'" . DA  D 4 23   ? 134.581 145.991 178.657 1.00 44.73  ? 23   DA  D "C1'" 1 
ATOM   11088 N N9    . DA  D 4 23   ? 135.760 145.598 177.898 1.00 44.73  ? 23   DA  D N9    1 
ATOM   11089 C C8    . DA  D 4 23   ? 136.849 146.365 177.595 1.00 44.73  ? 23   DA  D C8    1 
ATOM   11090 N N7    . DA  D 4 23   ? 137.762 145.731 176.899 1.00 44.73  ? 23   DA  D N7    1 
ATOM   11091 C C5    . DA  D 4 23   ? 137.236 144.461 176.742 1.00 44.73  ? 23   DA  D C5    1 
ATOM   11092 C C6    . DA  D 4 23   ? 137.714 143.306 176.098 1.00 44.73  ? 23   DA  D C6    1 
ATOM   11093 N N6    . DA  D 4 23   ? 138.889 143.251 175.465 1.00 44.73  ? 23   DA  D N6    1 
ATOM   11094 N N1    . DA  D 4 23   ? 136.937 142.203 176.132 1.00 44.73  ? 23   DA  D N1    1 
ATOM   11095 C C2    . DA  D 4 23   ? 135.763 142.264 176.763 1.00 44.73  ? 23   DA  D C2    1 
ATOM   11096 N N3    . DA  D 4 23   ? 135.211 143.287 177.404 1.00 44.73  ? 23   DA  D N3    1 
ATOM   11097 C C4    . DA  D 4 23   ? 136.005 144.365 177.353 1.00 44.73  ? 23   DA  D C4    1 
ATOM   11098 P P     . DA  D 4 24   ? 132.651 145.984 182.322 1.00 44.73  ? 24   DA  D P     1 
ATOM   11099 O OP1   . DA  D 4 24   ? 131.363 146.402 182.915 1.00 44.73  ? 24   DA  D OP1   1 
ATOM   11100 O OP2   . DA  D 4 24   ? 133.916 146.461 182.919 1.00 44.73  ? 24   DA  D OP2   1 
ATOM   11101 O "O5'" . DA  D 4 24   ? 132.699 144.387 182.280 1.00 44.73  ? 24   DA  D "O5'" 1 
ATOM   11102 C "C5'" . DA  D 4 24   ? 131.620 143.659 181.706 1.00 44.73  ? 24   DA  D "C5'" 1 
ATOM   11103 C "C4'" . DA  D 4 24   ? 132.055 142.263 181.292 1.00 44.73  ? 24   DA  D "C4'" 1 
ATOM   11104 O "O4'" . DA  D 4 24   ? 133.198 142.350 180.401 1.00 44.73  ? 24   DA  D "O4'" 1 
ATOM   11105 C "C3'" . DA  D 4 24   ? 132.506 141.351 182.430 1.00 44.73  ? 24   DA  D "C3'" 1 
ATOM   11106 O "O3'" . DA  D 4 24   ? 132.223 139.999 182.084 1.00 44.73  ? 24   DA  D "O3'" 1 
ATOM   11107 C "C2'" . DA  D 4 24   ? 134.009 141.592 182.438 1.00 44.73  ? 24   DA  D "C2'" 1 
ATOM   11108 C "C1'" . DA  D 4 24   ? 134.259 141.595 180.946 1.00 44.73  ? 24   DA  D "C1'" 1 
ATOM   11109 N N9    . DA  D 4 24   ? 135.517 142.200 180.536 1.00 44.73  ? 24   DA  D N9    1 
ATOM   11110 C C8    . DA  D 4 24   ? 135.910 143.494 180.712 1.00 44.73  ? 24   DA  D C8    1 
ATOM   11111 N N7    . DA  D 4 24   ? 137.095 143.758 180.214 1.00 44.73  ? 24   DA  D N7    1 
ATOM   11112 C C5    . DA  D 4 24   ? 137.499 142.553 179.667 1.00 44.73  ? 24   DA  D C5    1 
ATOM   11113 C C6    . DA  D 4 24   ? 138.667 142.164 178.984 1.00 44.73  ? 24   DA  D C6    1 
ATOM   11114 N N6    . DA  D 4 24   ? 139.685 142.993 178.732 1.00 44.73  ? 24   DA  D N6    1 
ATOM   11115 N N1    . DA  D 4 24   ? 138.751 140.882 178.573 1.00 44.73  ? 24   DA  D N1    1 
ATOM   11116 C C2    . DA  D 4 24   ? 137.731 140.056 178.826 1.00 44.73  ? 24   DA  D C2    1 
ATOM   11117 N N3    . DA  D 4 24   ? 136.588 140.308 179.455 1.00 44.73  ? 24   DA  D N3    1 
ATOM   11118 C C4    . DA  D 4 24   ? 136.535 141.586 179.854 1.00 44.73  ? 24   DA  D C4    1 
ATOM   11119 P P     . DG  D 4 25   ? 131.255 139.099 182.995 1.00 52.65  ? 25   DG  D P     1 
ATOM   11120 O OP1   . DG  D 4 25   ? 130.370 138.352 182.077 1.00 52.65  ? 25   DG  D OP1   1 
ATOM   11121 O OP2   . DG  D 4 25   ? 130.688 139.959 184.055 1.00 52.65  ? 25   DG  D OP2   1 
ATOM   11122 O "O5'" . DG  D 4 25   ? 132.237 138.042 183.683 1.00 52.65  ? 25   DG  D "O5'" 1 
ATOM   11123 C "C5'" . DG  D 4 25   ? 133.602 138.366 183.886 1.00 52.65  ? 25   DG  D "C5'" 1 
ATOM   11124 C "C4'" . DG  D 4 25   ? 134.498 137.432 183.100 1.00 52.65  ? 25   DG  D "C4'" 1 
ATOM   11125 O "O4'" . DG  D 4 25   ? 135.408 138.208 182.273 1.00 52.65  ? 25   DG  D "O4'" 1 
ATOM   11126 C "C3'" . DG  D 4 25   ? 135.386 136.543 183.956 1.00 52.65  ? 25   DG  D "C3'" 1 
ATOM   11127 O "O3'" . DG  D 4 25   ? 135.641 135.328 183.273 1.00 52.65  ? 25   DG  D "O3'" 1 
ATOM   11128 C "C2'" . DG  D 4 25   ? 136.645 137.391 184.075 1.00 52.65  ? 25   DG  D "C2'" 1 
ATOM   11129 C "C1'" . DG  D 4 25   ? 136.740 137.944 182.664 1.00 52.65  ? 25   DG  D "C1'" 1 
ATOM   11130 N N9    . DG  D 4 25   ? 137.515 139.181 182.550 1.00 52.65  ? 25   DG  D N9    1 
ATOM   11131 C C8    . DG  D 4 25   ? 137.167 140.421 183.028 1.00 52.65  ? 25   DG  D C8    1 
ATOM   11132 N N7    . DG  D 4 25   ? 138.048 141.347 182.766 1.00 52.65  ? 25   DG  D N7    1 
ATOM   11133 C C5    . DG  D 4 25   ? 139.045 140.683 182.063 1.00 52.65  ? 25   DG  D C5    1 
ATOM   11134 C C6    . DG  D 4 25   ? 140.257 141.173 181.520 1.00 52.65  ? 25   DG  D C6    1 
ATOM   11135 O O6    . DG  D 4 25   ? 140.699 142.331 181.550 1.00 52.65  ? 25   DG  D O6    1 
ATOM   11136 N N1    . DG  D 4 25   ? 140.979 140.169 180.884 1.00 52.65  ? 25   DG  D N1    1 
ATOM   11137 C C2    . DG  D 4 25   ? 140.583 138.855 180.788 1.00 52.65  ? 25   DG  D C2    1 
ATOM   11138 N N2    . DG  D 4 25   ? 141.413 138.028 180.138 1.00 52.65  ? 25   DG  D N2    1 
ATOM   11139 N N3    . DG  D 4 25   ? 139.451 138.382 181.296 1.00 52.65  ? 25   DG  D N3    1 
ATOM   11140 C C4    . DG  D 4 25   ? 138.732 139.350 181.916 1.00 52.65  ? 25   DG  D C4    1 
ATOM   11141 P P     . DC  D 4 26   ? 136.078 134.013 184.086 1.00 64.76  ? 26   DC  D P     1 
ATOM   11142 O OP1   . DC  D 4 26   ? 134.868 133.186 184.281 1.00 64.76  ? 26   DC  D OP1   1 
ATOM   11143 O OP2   . DC  D 4 26   ? 136.872 134.437 185.259 1.00 64.76  ? 26   DC  D OP2   1 
ATOM   11144 O "O5'" . DC  D 4 26   ? 137.059 133.260 183.075 1.00 64.76  ? 26   DC  D "O5'" 1 
ATOM   11145 C "C5'" . DC  D 4 26   ? 137.949 134.015 182.263 1.00 64.76  ? 26   DC  D "C5'" 1 
ATOM   11146 C "C4'" . DC  D 4 26   ? 139.378 133.563 182.473 1.00 64.76  ? 26   DC  D "C4'" 1 
ATOM   11147 O "O4'" . DC  D 4 26   ? 140.267 134.708 182.352 1.00 64.76  ? 26   DC  D "O4'" 1 
ATOM   11148 C "C3'" . DC  D 4 26   ? 139.663 132.980 183.849 1.00 64.76  ? 26   DC  D "C3'" 1 
ATOM   11149 O "O3'" . DC  D 4 26   ? 140.747 132.065 183.766 1.00 64.76  ? 26   DC  D "O3'" 1 
ATOM   11150 C "C2'" . DC  D 4 26   ? 140.047 134.224 184.632 1.00 64.76  ? 26   DC  D "C2'" 1 
ATOM   11151 C "C1'" . DC  D 4 26   ? 140.887 134.960 183.599 1.00 64.76  ? 26   DC  D "C1'" 1 
ATOM   11152 N N1    . DC  D 4 26   ? 140.941 136.432 183.820 1.00 64.76  ? 26   DC  D N1    1 
ATOM   11153 C C2    . DC  D 4 26   ? 142.018 137.177 183.321 1.00 64.76  ? 26   DC  D C2    1 
ATOM   11154 O O2    . DC  D 4 26   ? 142.913 136.598 182.694 1.00 64.76  ? 26   DC  D O2    1 
ATOM   11155 N N3    . DC  D 4 26   ? 142.044 138.516 183.540 1.00 64.76  ? 26   DC  D N3    1 
ATOM   11156 C C4    . DC  D 4 26   ? 141.057 139.100 184.222 1.00 64.76  ? 26   DC  D C4    1 
ATOM   11157 N N4    . DC  D 4 26   ? 141.119 140.421 184.416 1.00 64.76  ? 26   DC  D N4    1 
ATOM   11158 C C5    . DC  D 4 26   ? 139.961 138.354 184.740 1.00 64.76  ? 26   DC  D C5    1 
ATOM   11159 C C6    . DC  D 4 26   ? 139.946 137.039 184.519 1.00 64.76  ? 26   DC  D C6    1 
ATOM   11160 P P     . DA  D 4 27   ? 141.016 131.004 184.943 1.00 78.47  ? 27   DA  D P     1 
ATOM   11161 O OP1   . DA  D 4 27   ? 140.556 129.685 184.455 1.00 78.47  ? 27   DA  D OP1   1 
ATOM   11162 O OP2   . DA  D 4 27   ? 140.469 131.546 186.207 1.00 78.47  ? 27   DA  D OP2   1 
ATOM   11163 O "O5'" . DA  D 4 27   ? 142.610 130.977 185.068 1.00 78.47  ? 27   DA  D "O5'" 1 
ATOM   11164 C "C5'" . DA  D 4 27   ? 143.392 130.444 184.008 1.00 78.47  ? 27   DA  D "C5'" 1 
ATOM   11165 C "C4'" . DA  D 4 27   ? 144.627 131.292 183.751 1.00 78.47  ? 27   DA  D "C4'" 1 
ATOM   11166 O "O4'" . DA  D 4 27   ? 144.287 132.701 183.830 1.00 78.47  ? 27   DA  D "O4'" 1 
ATOM   11167 C "C3'" . DA  D 4 27   ? 145.770 131.103 184.739 1.00 78.47  ? 27   DA  D "C3'" 1 
ATOM   11168 O "O3'" . DA  D 4 27   ? 146.993 131.368 184.071 1.00 78.47  ? 27   DA  D "O3'" 1 
ATOM   11169 C "C2'" . DA  D 4 27   ? 145.469 132.183 185.774 1.00 78.47  ? 27   DA  D "C2'" 1 
ATOM   11170 C "C1'" . DA  D 4 27   ? 145.058 133.314 184.849 1.00 78.47  ? 27   DA  D "C1'" 1 
ATOM   11171 N N9    . DA  D 4 27   ? 144.240 134.355 185.462 1.00 78.47  ? 27   DA  D N9    1 
ATOM   11172 C C8    . DA  D 4 27   ? 143.039 134.199 186.089 1.00 78.47  ? 27   DA  D C8    1 
ATOM   11173 N N7    . DA  D 4 27   ? 142.510 135.327 186.506 1.00 78.47  ? 27   DA  D N7    1 
ATOM   11174 C C5    . DA  D 4 27   ? 143.427 136.287 186.116 1.00 78.47  ? 27   DA  D C5    1 
ATOM   11175 C C6    . DA  D 4 27   ? 143.457 137.689 186.262 1.00 78.47  ? 27   DA  D C6    1 
ATOM   11176 N N6    . DA  D 4 27   ? 142.494 138.388 186.872 1.00 78.47  ? 27   DA  D N6    1 
ATOM   11177 N N1    . DA  D 4 27   ? 144.522 138.347 185.760 1.00 78.47  ? 27   DA  D N1    1 
ATOM   11178 C C2    . DA  D 4 27   ? 145.483 137.643 185.154 1.00 78.47  ? 27   DA  D C2    1 
ATOM   11179 N N3    . DA  D 4 27   ? 145.563 136.331 184.954 1.00 78.47  ? 27   DA  D N3    1 
ATOM   11180 C C4    . DA  D 4 27   ? 144.495 135.705 185.465 1.00 78.47  ? 27   DA  D C4    1 
ATOM   11181 P P     . DC  D 4 28   ? 148.140 130.249 183.979 1.00 92.62  ? 28   DC  D P     1 
ATOM   11182 O OP1   . DC  D 4 28   ? 148.393 129.985 182.545 1.00 92.62  ? 28   DC  D OP1   1 
ATOM   11183 O OP2   . DC  D 4 28   ? 147.768 129.138 184.882 1.00 92.62  ? 28   DC  D OP2   1 
ATOM   11184 O "O5'" . DC  D 4 28   ? 149.412 130.984 184.598 1.00 92.62  ? 28   DC  D "O5'" 1 
ATOM   11185 C "C5'" . DC  D 4 28   ? 149.251 131.793 185.749 1.00 92.62  ? 28   DC  D "C5'" 1 
ATOM   11186 C "C4'" . DC  D 4 28   ? 150.188 132.982 185.714 1.00 92.62  ? 28   DC  D "C4'" 1 
ATOM   11187 O "O4'" . DC  D 4 28   ? 149.409 134.207 185.775 1.00 92.62  ? 28   DC  D "O4'" 1 
ATOM   11188 C "C3'" . DC  D 4 28   ? 151.133 133.066 186.897 1.00 92.62  ? 28   DC  D "C3'" 1 
ATOM   11189 O "O3'" . DC  D 4 28   ? 152.274 133.834 186.551 1.00 92.62  ? 28   DC  D "O3'" 1 
ATOM   11190 C "C2'" . DC  D 4 28   ? 150.267 133.787 187.915 1.00 92.62  ? 28   DC  D "C2'" 1 
ATOM   11191 C "C1'" . DC  D 4 28   ? 149.607 134.831 187.032 1.00 92.62  ? 28   DC  D "C1'" 1 
ATOM   11192 N N1    . DC  D 4 28   ? 148.291 135.298 187.537 1.00 92.62  ? 28   DC  D N1    1 
ATOM   11193 C C2    . DC  D 4 28   ? 147.998 136.663 187.530 1.00 92.62  ? 28   DC  D C2    1 
ATOM   11194 O O2    . DC  D 4 28   ? 148.848 137.467 187.141 1.00 92.62  ? 28   DC  D O2    1 
ATOM   11195 N N3    . DC  D 4 28   ? 146.805 137.083 188.002 1.00 92.62  ? 28   DC  D N3    1 
ATOM   11196 C C4    . DC  D 4 28   ? 145.908 136.195 188.429 1.00 92.62  ? 28   DC  D C4    1 
ATOM   11197 N N4    . DC  D 4 28   ? 144.741 136.664 188.877 1.00 92.62  ? 28   DC  D N4    1 
ATOM   11198 C C5    . DC  D 4 28   ? 146.180 134.795 188.438 1.00 92.62  ? 28   DC  D C5    1 
ATOM   11199 C C6    . DC  D 4 28   ? 147.374 134.394 187.985 1.00 92.62  ? 28   DC  D C6    1 
ATOM   11200 P P     . DT  D 4 29   ? 153.735 133.171 186.611 1.00 113.05 ? 29   DT  D P     1 
ATOM   11201 O OP1   . DT  D 4 29   ? 154.731 134.236 186.357 1.00 113.05 ? 29   DT  D OP1   1 
ATOM   11202 O OP2   . DT  D 4 29   ? 153.708 131.981 185.732 1.00 113.05 ? 29   DT  D OP2   1 
ATOM   11203 O "O5'" . DT  D 4 29   ? 153.854 132.653 188.122 1.00 113.05 ? 29   DT  D "O5'" 1 
ATOM   11204 C "C5'" . DT  D 4 29   ? 154.715 133.311 189.049 1.00 113.05 ? 29   DT  D "C5'" 1 
ATOM   11205 C "C4'" . DT  D 4 29   ? 154.183 134.686 189.420 1.00 113.05 ? 29   DT  D "C4'" 1 
ATOM   11206 O "O4'" . DT  D 4 29   ? 152.737 134.657 189.471 1.00 113.05 ? 29   DT  D "O4'" 1 
ATOM   11207 C "C3'" . DT  D 4 29   ? 154.646 135.210 190.786 1.00 113.05 ? 29   DT  D "C3'" 1 
ATOM   11208 O "O3'" . DT  D 4 29   ? 155.361 136.429 190.630 1.00 113.05 ? 29   DT  D "O3'" 1 
ATOM   11209 C "C2'" . DT  D 4 29   ? 153.347 135.418 191.574 1.00 113.05 ? 29   DT  D "C2'" 1 
ATOM   11210 C "C1'" . DT  D 4 29   ? 152.312 135.543 190.470 1.00 113.05 ? 29   DT  D "C1'" 1 
ATOM   11211 N N1    . DT  D 4 29   ? 150.943 135.159 190.911 1.00 113.05 ? 29   DT  D N1    1 
ATOM   11212 C C2    . DT  D 4 29   ? 149.972 136.129 191.010 1.00 113.05 ? 29   DT  D C2    1 
ATOM   11213 O O2    . DT  D 4 29   ? 150.167 137.299 190.737 1.00 113.05 ? 29   DT  D O2    1 
ATOM   11214 N N3    . DT  D 4 29   ? 148.753 135.676 191.437 1.00 113.05 ? 29   DT  D N3    1 
ATOM   11215 C C4    . DT  D 4 29   ? 148.418 134.374 191.770 1.00 113.05 ? 29   DT  D C4    1 
ATOM   11216 O O4    . DT  D 4 29   ? 147.294 134.060 192.142 1.00 113.05 ? 29   DT  D O4    1 
ATOM   11217 C C5    . DT  D 4 29   ? 149.486 133.411 191.652 1.00 113.05 ? 29   DT  D C5    1 
ATOM   11218 C C7    . DT  D 4 29   ? 149.241 131.969 191.989 1.00 113.05 ? 29   DT  D C7    1 
ATOM   11219 C C6    . DT  D 4 29   ? 150.684 133.846 191.241 1.00 113.05 ? 29   DT  D C6    1 
ATOM   11220 P P     . DA  D 4 30   ? 156.336 136.944 191.800 1.00 133.54 ? 30   DA  D P     1 
ATOM   11221 O OP1   . DA  D 4 30   ? 157.144 138.054 191.249 1.00 133.54 ? 30   DA  D OP1   1 
ATOM   11222 O OP2   . DA  D 4 30   ? 157.007 135.758 192.376 1.00 133.54 ? 30   DA  D OP2   1 
ATOM   11223 O "O5'" . DA  D 4 30   ? 155.338 137.528 192.908 1.00 133.54 ? 30   DA  D "O5'" 1 
ATOM   11224 C "C5'" . DA  D 4 30   ? 154.501 138.636 192.598 1.00 133.54 ? 30   DA  D "C5'" 1 
ATOM   11225 C "C4'" . DA  D 4 30   ? 153.681 139.057 193.806 1.00 133.54 ? 30   DA  D "C4'" 1 
ATOM   11226 O "O4'" . DA  D 4 30   ? 152.493 138.251 193.901 1.00 133.54 ? 30   DA  D "O4'" 1 
ATOM   11227 C "C3'" . DA  D 4 30   ? 154.358 138.863 195.147 1.00 133.54 ? 30   DA  D "C3'" 1 
ATOM   11228 O "O3'" . DA  D 4 30   ? 155.214 139.963 195.423 1.00 133.54 ? 30   DA  D "O3'" 1 
ATOM   11229 C "C2'" . DA  D 4 30   ? 153.167 138.822 196.112 1.00 133.54 ? 30   DA  D "C2'" 1 
ATOM   11230 C "C1'" . DA  D 4 30   ? 152.009 138.328 195.228 1.00 133.54 ? 30   DA  D "C1'" 1 
ATOM   11231 N N9    . DA  D 4 30   ? 151.488 137.021 195.621 1.00 133.54 ? 30   DA  D N9    1 
ATOM   11232 C C8    . DA  D 4 30   ? 152.168 135.836 195.655 1.00 133.54 ? 30   DA  D C8    1 
ATOM   11233 N N7    . DA  D 4 30   ? 151.441 134.821 196.061 1.00 133.54 ? 30   DA  D N7    1 
ATOM   11234 C C5    . DA  D 4 30   ? 150.199 135.380 196.311 1.00 133.54 ? 30   DA  D C5    1 
ATOM   11235 C C6    . DA  D 4 30   ? 148.983 134.831 196.767 1.00 133.54 ? 30   DA  D C6    1 
ATOM   11236 N N6    . DA  D 4 30   ? 148.826 133.536 197.062 1.00 133.54 ? 30   DA  D N6    1 
ATOM   11237 N N1    . DA  D 4 30   ? 147.934 135.672 196.920 1.00 133.54 ? 30   DA  D N1    1 
ATOM   11238 C C2    . DA  D 4 30   ? 148.097 136.962 196.604 1.00 133.54 ? 30   DA  D C2    1 
ATOM   11239 N N3    . DA  D 4 30   ? 149.188 137.592 196.177 1.00 133.54 ? 30   DA  D N3    1 
ATOM   11240 C C4    . DA  D 4 30   ? 150.212 136.736 196.047 1.00 133.54 ? 30   DA  D C4    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 
728   N N   . LYS B 29   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  26   LYS A N   
729   C CA  . LYS B 29   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  26   LYS A CA  
730   C C   . LYS B 29   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  26   LYS A C   
731   O O   . LYS B 29   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  26   LYS A O   
737   N N   . THR B 30   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  27   THR A N   
738   C CA  . THR B 30   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  27   THR A CA  
739   C C   . THR B 30   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  27   THR A C   
740   O O   . THR B 30   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  27   THR A O   
741   C CB  . THR B 30   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  27   THR A CB  
742   O OG1 . THR B 30   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  27   THR A OG1 
743   C CG2 . THR B 30   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  27   THR A CG2 
744   N N   . LEU B 31   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  28   LEU A N   
745   C CA  . LEU B 31   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  28   LEU A CA  
746   C C   . LEU B 31   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  28   LEU A C   
747   O O   . LEU B 31   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  28   LEU A O   
748   C CB  . LEU B 31   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  28   LEU A CB  
749   C CG  . LEU B 31   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  28   LEU A CG  
750   C CD1 . LEU B 31   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  28   LEU A CD1 
751   C CD2 . LEU B 31   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  28   LEU A CD2 
752   N N   . LYS B 32   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  29   LYS A N   
753   C CA  . LYS B 32   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  29   LYS A CA  
754   C C   . LYS B 32   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  29   LYS A C   
755   O O   . LYS B 32   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  29   LYS A O   
756   C CB  . LYS B 32   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  29   LYS A CB  
757   C CG  . LYS B 32   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  29   LYS A CG  
758   C CD  . LYS B 32   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  29   LYS A CD  
759   C CE  . LYS B 32   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  29   LYS A CE  
760   N NZ  . LYS B 32   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  29   LYS A NZ  
761   N N   . HIS B 33   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  30   HIS A N   
762   C CA  . HIS B 33   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  30   HIS A CA  
763   C C   . HIS B 33   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  30   HIS A C   
764   O O   . HIS B 33   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  30   HIS A O   
765   C CB  . HIS B 33   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  30   HIS A CB  
766   C CG  . HIS B 33   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  30   HIS A CG  
767   N ND1 . HIS B 33   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  30   HIS A ND1 
768   C CD2 . HIS B 33   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  30   HIS A CD2 
769   C CE1 . HIS B 33   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  30   HIS A CE1 
770   N NE2 . HIS B 33   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  30   HIS A NE2 
771   N N   . ILE B 34   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  31   ILE A N   
772   C CA  . ILE B 34   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  31   ILE A CA  
773   C C   . ILE B 34   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  31   ILE A C   
774   O O   . ILE B 34   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  31   ILE A O   
775   C CB  . ILE B 34   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  31   ILE A CB  
776   C CG1 . ILE B 34   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  31   ILE A CG1 
777   C CG2 . ILE B 34   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  31   ILE A CG2 
778   C CD1 . ILE B 34   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  31   ILE A CD1 
779   N N   . GLN B 35   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  32   GLN A N   
780   C CA  . GLN B 35   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  32   GLN A CA  
781   C C   . GLN B 35   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  32   GLN A C   
782   O O   . GLN B 35   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  32   GLN A O   
783   C CB  . GLN B 35   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  32   GLN A CB  
784   C CG  . GLN B 35   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  32   GLN A CG  
785   C CD  . GLN B 35   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  32   GLN A CD  
786   O OE1 . GLN B 35   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  32   GLN A OE1 
787   N NE2 . GLN B 35   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  32   GLN A NE2 
788   N N   . GLU B 36   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  33   GLU A N   
789   C CA  . GLU B 36   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  33   GLU A CA  
790   C C   . GLU B 36   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  33   GLU A C   
791   O O   . GLU B 36   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  33   GLU A O   
792   C CB  . GLU B 36   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  33   GLU A CB  
793   C CG  . GLU B 36   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  33   GLU A CG  
794   C CD  . GLU B 36   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  33   GLU A CD  
795   O OE1 . GLU B 36   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  33   GLU A OE1 
796   O OE2 . GLU B 36   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  33   GLU A OE2 
797   N N   . GLN B 37   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  34   GLN A N   
798   C CA  . GLN B 37   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  34   GLN A CA  
799   C C   . GLN B 37   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  34   GLN A C   
800   O O   . GLN B 37   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  34   GLN A O   
801   C CB  . GLN B 37   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  34   GLN A CB  
802   C CG  . GLN B 37   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  34   GLN A CG  
803   C CD  . GLN B 37   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  34   GLN A CD  
804   O OE1 . GLN B 37   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  34   GLN A OE1 
805   N NE2 . GLN B 37   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  34   GLN A NE2 
806   N N   . GLY B 38   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  35   GLY A N   
807   C CA  . GLY B 38   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  35   GLY A CA  
808   C C   . GLY B 38   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  35   GLY A C   
809   O O   . GLY B 38   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  35   GLY A O   
810   N N   . PHE B 39   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  36   PHE A N   
811   C CA  . PHE B 39   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  36   PHE A CA  
812   C C   . PHE B 39   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  36   PHE A C   
813   O O   . PHE B 39   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  36   PHE A O   
814   C CB  . PHE B 39   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  36   PHE A CB  
815   C CG  . PHE B 39   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  36   PHE A CG  
816   C CD1 . PHE B 39   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  36   PHE A CD1 
817   C CD2 . PHE B 39   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  36   PHE A CD2 
818   C CE1 . PHE B 39   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  36   PHE A CE1 
819   C CE2 . PHE B 39   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  36   PHE A CE2 
820   C CZ  . PHE B 39   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  36   PHE A CZ  
821   N N   . ILE B 40   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  37   ILE A N   
822   C CA  . ILE B 40   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  37   ILE A CA  
823   C C   . ILE B 40   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  37   ILE A C   
824   O O   . ILE B 40   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  37   ILE A O   
825   C CB  . ILE B 40   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  37   ILE A CB  
826   C CG1 . ILE B 40   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  37   ILE A CG1 
827   C CG2 . ILE B 40   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  37   ILE A CG2 
828   C CD1 . ILE B 40   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  37   ILE A CD1 
829   N N   . GLU B 41   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  38   GLU A N   
830   C CA  . GLU B 41   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  38   GLU A CA  
831   C C   . GLU B 41   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  38   GLU A C   
832   O O   . GLU B 41   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  38   GLU A O   
833   C CB  . GLU B 41   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  38   GLU A CB  
834   C CG  . GLU B 41   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  38   GLU A CG  
835   C CD  . GLU B 41   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  38   GLU A CD  
836   O OE1 . GLU B 41   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  38   GLU A OE1 
837   O OE2 . GLU B 41   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  38   GLU A OE2 
838   N N   . GLU B 42   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  39   GLU A N   
839   C CA  . GLU B 42   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  39   GLU A CA  
840   C C   . GLU B 42   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  39   GLU A C   
841   O O   . GLU B 42   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  39   GLU A O   
842   C CB  . GLU B 42   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  39   GLU A CB  
843   C CG  . GLU B 42   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  39   GLU A CG  
844   C CD  . GLU B 42   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  39   GLU A CD  
845   O OE1 . GLU B 42   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  39   GLU A OE1 
846   O OE2 . GLU B 42   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  39   GLU A OE2 
847   N N   . ASP B 43   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  40   ASP A N   
848   C CA  . ASP B 43   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  40   ASP A CA  
849   C C   . ASP B 43   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  40   ASP A C   
850   O O   . ASP B 43   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  40   ASP A O   
851   C CB  . ASP B 43   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  40   ASP A CB  
852   C CG  . ASP B 43   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  40   ASP A CG  
853   O OD1 . ASP B 43   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  40   ASP A OD1 
854   O OD2 . ASP B 43   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  40   ASP A OD2 
855   N N   . LYS B 44   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  41   LYS A N   
856   C CA  . LYS B 44   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  41   LYS A CA  
857   C C   . LYS B 44   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  41   LYS A C   
858   O O   . LYS B 44   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  41   LYS A O   
859   C CB  . LYS B 44   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  41   LYS A CB  
860   C CG  . LYS B 44   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  41   LYS A CG  
861   C CD  . LYS B 44   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  41   LYS A CD  
862   C CE  . LYS B 44   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  41   LYS A CE  
863   N NZ  . LYS B 44   ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  41   LYS A NZ  
864   N N   . ALA B 45   ? 0.5805 0.5805 0.5805 0.0000  0.0000  0.0000  42   ALA A N   
865   C CA  . ALA B 45   ? 0.5805 0.5805 0.5805 0.0000  0.0000  0.0000  42   ALA A CA  
866   C C   . ALA B 45   ? 0.5805 0.5805 0.5805 0.0000  0.0000  0.0000  42   ALA A C   
867   O O   . ALA B 45   ? 0.5805 0.5805 0.5805 0.0000  0.0000  0.0000  42   ALA A O   
868   C CB  . ALA B 45   ? 0.5805 0.5805 0.5805 0.0000  0.0000  0.0000  42   ALA A CB  
869   N N   . ARG B 46   ? 0.5821 0.5821 0.5821 0.0000  0.0000  0.0000  43   ARG A N   
870   C CA  . ARG B 46   ? 0.5821 0.5821 0.5821 0.0000  0.0000  0.0000  43   ARG A CA  
871   C C   . ARG B 46   ? 0.5821 0.5821 0.5821 0.0000  0.0000  0.0000  43   ARG A C   
872   O O   . ARG B 46   ? 0.5821 0.5821 0.5821 0.0000  0.0000  0.0000  43   ARG A O   
873   C CB  . ARG B 46   ? 0.5821 0.5821 0.5821 0.0000  0.0000  0.0000  43   ARG A CB  
874   C CG  . ARG B 46   ? 0.5821 0.5821 0.5821 0.0000  0.0000  0.0000  43   ARG A CG  
875   C CD  . ARG B 46   ? 0.5821 0.5821 0.5821 0.0000  0.0000  0.0000  43   ARG A CD  
876   N NE  . ARG B 46   ? 0.5821 0.5821 0.5821 0.0000  0.0000  0.0000  43   ARG A NE  
877   C CZ  . ARG B 46   ? 0.5821 0.5821 0.5821 0.0000  0.0000  0.0000  43   ARG A CZ  
878   N NH1 . ARG B 46   ? 0.5821 0.5821 0.5821 0.0000  0.0000  0.0000  43   ARG A NH1 
879   N NH2 . ARG B 46   ? 0.5821 0.5821 0.5821 0.0000  0.0000  0.0000  43   ARG A NH2 
880   N N   . ASN B 47   ? 0.5699 0.5699 0.5699 0.0000  0.0000  0.0000  44   ASN A N   
881   C CA  . ASN B 47   ? 0.5699 0.5699 0.5699 0.0000  0.0000  0.0000  44   ASN A CA  
882   C C   . ASN B 47   ? 0.5699 0.5699 0.5699 0.0000  0.0000  0.0000  44   ASN A C   
883   O O   . ASN B 47   ? 0.5699 0.5699 0.5699 0.0000  0.0000  0.0000  44   ASN A O   
884   C CB  . ASN B 47   ? 0.5699 0.5699 0.5699 0.0000  0.0000  0.0000  44   ASN A CB  
885   C CG  . ASN B 47   ? 0.5699 0.5699 0.5699 0.0000  0.0000  0.0000  44   ASN A CG  
886   O OD1 . ASN B 47   ? 0.5699 0.5699 0.5699 0.0000  0.0000  0.0000  44   ASN A OD1 
887   N ND2 . ASN B 47   ? 0.5699 0.5699 0.5699 0.0000  0.0000  0.0000  44   ASN A ND2 
888   N N   . ASP B 48   ? 0.6078 0.6078 0.6078 0.0000  0.0000  0.0000  45   ASP A N   
889   C CA  . ASP B 48   ? 0.6078 0.6078 0.6078 0.0000  0.0000  0.0000  45   ASP A CA  
890   C C   . ASP B 48   ? 0.6078 0.6078 0.6078 0.0000  0.0000  0.0000  45   ASP A C   
891   O O   . ASP B 48   ? 0.6078 0.6078 0.6078 0.0000  0.0000  0.0000  45   ASP A O   
892   C CB  . ASP B 48   ? 0.6078 0.6078 0.6078 0.0000  0.0000  0.0000  45   ASP A CB  
893   C CG  . ASP B 48   ? 0.6078 0.6078 0.6078 0.0000  0.0000  0.0000  45   ASP A CG  
894   O OD1 . ASP B 48   ? 0.6078 0.6078 0.6078 0.0000  0.0000  0.0000  45   ASP A OD1 
895   O OD2 . ASP B 48   ? 0.6078 0.6078 0.6078 0.0000  0.0000  0.0000  45   ASP A OD2 
896   N N   . HIS B 49   ? 0.6625 0.6625 0.6625 0.0000  0.0000  0.0000  46   HIS A N   
897   C CA  . HIS B 49   ? 0.6625 0.6625 0.6625 0.0000  0.0000  0.0000  46   HIS A CA  
898   C C   . HIS B 49   ? 0.6625 0.6625 0.6625 0.0000  0.0000  0.0000  46   HIS A C   
899   O O   . HIS B 49   ? 0.6625 0.6625 0.6625 0.0000  0.0000  0.0000  46   HIS A O   
900   C CB  . HIS B 49   ? 0.6625 0.6625 0.6625 0.0000  0.0000  0.0000  46   HIS A CB  
901   C CG  . HIS B 49   ? 0.6625 0.6625 0.6625 0.0000  0.0000  0.0000  46   HIS A CG  
902   N ND1 . HIS B 49   ? 0.6625 0.6625 0.6625 0.0000  0.0000  0.0000  46   HIS A ND1 
903   C CD2 . HIS B 49   ? 0.6625 0.6625 0.6625 0.0000  0.0000  0.0000  46   HIS A CD2 
904   C CE1 . HIS B 49   ? 0.6625 0.6625 0.6625 0.0000  0.0000  0.0000  46   HIS A CE1 
905   N NE2 . HIS B 49   ? 0.6625 0.6625 0.6625 0.0000  0.0000  0.0000  46   HIS A NE2 
906   N N   . TYR B 50   ? 0.6959 0.6959 0.6959 0.0000  0.0000  0.0000  47   TYR A N   
907   C CA  . TYR B 50   ? 0.6959 0.6959 0.6959 0.0000  0.0000  0.0000  47   TYR A CA  
908   C C   . TYR B 50   ? 0.6959 0.6959 0.6959 0.0000  0.0000  0.0000  47   TYR A C   
909   O O   . TYR B 50   ? 0.6959 0.6959 0.6959 0.0000  0.0000  0.0000  47   TYR A O   
910   C CB  . TYR B 50   ? 0.6959 0.6959 0.6959 0.0000  0.0000  0.0000  47   TYR A CB  
911   C CG  . TYR B 50   ? 0.6959 0.6959 0.6959 0.0000  0.0000  0.0000  47   TYR A CG  
912   C CD1 . TYR B 50   ? 0.6959 0.6959 0.6959 0.0000  0.0000  0.0000  47   TYR A CD1 
913   C CD2 . TYR B 50   ? 0.6959 0.6959 0.6959 0.0000  0.0000  0.0000  47   TYR A CD2 
914   C CE1 . TYR B 50   ? 0.6959 0.6959 0.6959 0.0000  0.0000  0.0000  47   TYR A CE1 
915   C CE2 . TYR B 50   ? 0.6959 0.6959 0.6959 0.0000  0.0000  0.0000  47   TYR A CE2 
916   C CZ  . TYR B 50   ? 0.6959 0.6959 0.6959 0.0000  0.0000  0.0000  47   TYR A CZ  
917   O OH  . TYR B 50   ? 0.6959 0.6959 0.6959 0.0000  0.0000  0.0000  47   TYR A OH  
918   N N   . LYS B 51   ? 0.6633 0.6633 0.6633 0.0000  0.0000  0.0000  48   LYS A N   
919   C CA  . LYS B 51   ? 0.6633 0.6633 0.6633 0.0000  0.0000  0.0000  48   LYS A CA  
920   C C   . LYS B 51   ? 0.6633 0.6633 0.6633 0.0000  0.0000  0.0000  48   LYS A C   
921   O O   . LYS B 51   ? 0.6633 0.6633 0.6633 0.0000  0.0000  0.0000  48   LYS A O   
922   C CB  . LYS B 51   ? 0.6633 0.6633 0.6633 0.0000  0.0000  0.0000  48   LYS A CB  
923   C CG  . LYS B 51   ? 0.6633 0.6633 0.6633 0.0000  0.0000  0.0000  48   LYS A CG  
924   C CD  . LYS B 51   ? 0.6633 0.6633 0.6633 0.0000  0.0000  0.0000  48   LYS A CD  
925   C CE  . LYS B 51   ? 0.6633 0.6633 0.6633 0.0000  0.0000  0.0000  48   LYS A CE  
926   N NZ  . LYS B 51   ? 0.6633 0.6633 0.6633 0.0000  0.0000  0.0000  48   LYS A NZ  
927   N N   . GLU B 52   ? 0.6898 0.6898 0.6898 0.0000  0.0000  0.0000  49   GLU A N   
928   C CA  . GLU B 52   ? 0.6898 0.6898 0.6898 0.0000  0.0000  0.0000  49   GLU A CA  
929   C C   . GLU B 52   ? 0.6898 0.6898 0.6898 0.0000  0.0000  0.0000  49   GLU A C   
930   O O   . GLU B 52   ? 0.6898 0.6898 0.6898 0.0000  0.0000  0.0000  49   GLU A O   
931   C CB  . GLU B 52   ? 0.6898 0.6898 0.6898 0.0000  0.0000  0.0000  49   GLU A CB  
932   C CG  . GLU B 52   ? 0.6898 0.6898 0.6898 0.0000  0.0000  0.0000  49   GLU A CG  
933   C CD  . GLU B 52   ? 0.6898 0.6898 0.6898 0.0000  0.0000  0.0000  49   GLU A CD  
934   O OE1 . GLU B 52   ? 0.6898 0.6898 0.6898 0.0000  0.0000  0.0000  49   GLU A OE1 
935   O OE2 . GLU B 52   ? 0.6898 0.6898 0.6898 0.0000  0.0000  0.0000  49   GLU A OE2 
936   N N   . LEU B 53   ? 0.7524 0.7524 0.7524 0.0000  0.0000  0.0000  50   LEU A N   
937   C CA  . LEU B 53   ? 0.7524 0.7524 0.7524 0.0000  0.0000  0.0000  50   LEU A CA  
938   C C   . LEU B 53   ? 0.7524 0.7524 0.7524 0.0000  0.0000  0.0000  50   LEU A C   
939   O O   . LEU B 53   ? 0.7524 0.7524 0.7524 0.0000  0.0000  0.0000  50   LEU A O   
940   C CB  . LEU B 53   ? 0.7524 0.7524 0.7524 0.0000  0.0000  0.0000  50   LEU A CB  
941   C CG  . LEU B 53   ? 0.7524 0.7524 0.7524 0.0000  0.0000  0.0000  50   LEU A CG  
942   C CD1 . LEU B 53   ? 0.7524 0.7524 0.7524 0.0000  0.0000  0.0000  50   LEU A CD1 
943   C CD2 . LEU B 53   ? 0.7524 0.7524 0.7524 0.0000  0.0000  0.0000  50   LEU A CD2 
944   N N   . LYS B 54   ? 0.8381 0.8381 0.8381 0.0000  0.0000  0.0000  51   LYS A N   
945   C CA  . LYS B 54   ? 0.8381 0.8381 0.8381 0.0000  0.0000  0.0000  51   LYS A CA  
946   C C   . LYS B 54   ? 0.8381 0.8381 0.8381 0.0000  0.0000  0.0000  51   LYS A C   
947   O O   . LYS B 54   ? 0.8381 0.8381 0.8381 0.0000  0.0000  0.0000  51   LYS A O   
948   C CB  . LYS B 54   ? 0.8381 0.8381 0.8381 0.0000  0.0000  0.0000  51   LYS A CB  
949   C CG  . LYS B 54   ? 0.8381 0.8381 0.8381 0.0000  0.0000  0.0000  51   LYS A CG  
950   C CD  . LYS B 54   ? 0.8381 0.8381 0.8381 0.0000  0.0000  0.0000  51   LYS A CD  
951   C CE  . LYS B 54   ? 0.8381 0.8381 0.8381 0.0000  0.0000  0.0000  51   LYS A CE  
952   N NZ  . LYS B 54   ? 0.8381 0.8381 0.8381 0.0000  0.0000  0.0000  51   LYS A NZ  
953   N N   . PRO B 55   ? 0.7618 0.7618 0.7618 0.0000  0.0000  0.0000  52   PRO A N   
954   C CA  . PRO B 55   ? 0.7618 0.7618 0.7618 0.0000  0.0000  0.0000  52   PRO A CA  
955   C C   . PRO B 55   ? 0.7618 0.7618 0.7618 0.0000  0.0000  0.0000  52   PRO A C   
956   O O   . PRO B 55   ? 0.7618 0.7618 0.7618 0.0000  0.0000  0.0000  52   PRO A O   
957   C CB  . PRO B 55   ? 0.7618 0.7618 0.7618 0.0000  0.0000  0.0000  52   PRO A CB  
958   C CG  . PRO B 55   ? 0.7618 0.7618 0.7618 0.0000  0.0000  0.0000  52   PRO A CG  
959   C CD  . PRO B 55   ? 0.7618 0.7618 0.7618 0.0000  0.0000  0.0000  52   PRO A CD  
960   N N   . ILE B 56   ? 0.7805 0.7805 0.7805 0.0000  0.0000  0.0000  53   ILE A N   
961   C CA  . ILE B 56   ? 0.7805 0.7805 0.7805 0.0000  0.0000  0.0000  53   ILE A CA  
962   C C   . ILE B 56   ? 0.7805 0.7805 0.7805 0.0000  0.0000  0.0000  53   ILE A C   
963   O O   . ILE B 56   ? 0.7805 0.7805 0.7805 0.0000  0.0000  0.0000  53   ILE A O   
964   C CB  . ILE B 56   ? 0.7805 0.7805 0.7805 0.0000  0.0000  0.0000  53   ILE A CB  
965   C CG1 . ILE B 56   ? 0.7805 0.7805 0.7805 0.0000  0.0000  0.0000  53   ILE A CG1 
966   C CG2 . ILE B 56   ? 0.7805 0.7805 0.7805 0.0000  0.0000  0.0000  53   ILE A CG2 
967   C CD1 . ILE B 56   ? 0.7805 0.7805 0.7805 0.0000  0.0000  0.0000  53   ILE A CD1 
968   N N   . ILE B 57   ? 0.8285 0.8285 0.8285 0.0000  0.0000  0.0000  54   ILE A N   
969   C CA  . ILE B 57   ? 0.8285 0.8285 0.8285 0.0000  0.0000  0.0000  54   ILE A CA  
970   C C   . ILE B 57   ? 0.8285 0.8285 0.8285 0.0000  0.0000  0.0000  54   ILE A C   
971   O O   . ILE B 57   ? 0.8285 0.8285 0.8285 0.0000  0.0000  0.0000  54   ILE A O   
972   C CB  . ILE B 57   ? 0.8285 0.8285 0.8285 0.0000  0.0000  0.0000  54   ILE A CB  
973   C CG1 . ILE B 57   ? 0.8285 0.8285 0.8285 0.0000  0.0000  0.0000  54   ILE A CG1 
974   C CG2 . ILE B 57   ? 0.8285 0.8285 0.8285 0.0000  0.0000  0.0000  54   ILE A CG2 
975   C CD1 . ILE B 57   ? 0.8285 0.8285 0.8285 0.0000  0.0000  0.0000  54   ILE A CD1 
976   N N   . ASP B 58   ? 0.8332 0.8332 0.8332 0.0000  0.0000  0.0000  55   ASP A N   
977   C CA  . ASP B 58   ? 0.8332 0.8332 0.8332 0.0000  0.0000  0.0000  55   ASP A CA  
978   C C   . ASP B 58   ? 0.8332 0.8332 0.8332 0.0000  0.0000  0.0000  55   ASP A C   
979   O O   . ASP B 58   ? 0.8332 0.8332 0.8332 0.0000  0.0000  0.0000  55   ASP A O   
980   C CB  . ASP B 58   ? 0.8332 0.8332 0.8332 0.0000  0.0000  0.0000  55   ASP A CB  
981   C CG  . ASP B 58   ? 0.8332 0.8332 0.8332 0.0000  0.0000  0.0000  55   ASP A CG  
982   O OD1 . ASP B 58   ? 0.8332 0.8332 0.8332 0.0000  0.0000  0.0000  55   ASP A OD1 
983   O OD2 . ASP B 58   ? 0.8332 0.8332 0.8332 0.0000  0.0000  0.0000  55   ASP A OD2 
984   N N   . ARG B 59   ? 0.8881 0.8881 0.8881 0.0000  0.0000  0.0000  56   ARG A N   
985   C CA  . ARG B 59   ? 0.8881 0.8881 0.8881 0.0000  0.0000  0.0000  56   ARG A CA  
986   C C   . ARG B 59   ? 0.8881 0.8881 0.8881 0.0000  0.0000  0.0000  56   ARG A C   
987   O O   . ARG B 59   ? 0.8881 0.8881 0.8881 0.0000  0.0000  0.0000  56   ARG A O   
988   C CB  . ARG B 59   ? 0.8881 0.8881 0.8881 0.0000  0.0000  0.0000  56   ARG A CB  
989   C CG  . ARG B 59   ? 0.8881 0.8881 0.8881 0.0000  0.0000  0.0000  56   ARG A CG  
990   C CD  . ARG B 59   ? 0.8881 0.8881 0.8881 0.0000  0.0000  0.0000  56   ARG A CD  
991   N NE  . ARG B 59   ? 0.8881 0.8881 0.8881 0.0000  0.0000  0.0000  56   ARG A NE  
992   C CZ  . ARG B 59   ? 0.8881 0.8881 0.8881 0.0000  0.0000  0.0000  56   ARG A CZ  
993   N NH1 . ARG B 59   ? 0.8881 0.8881 0.8881 0.0000  0.0000  0.0000  56   ARG A NH1 
994   N NH2 . ARG B 59   ? 0.8881 0.8881 0.8881 0.0000  0.0000  0.0000  56   ARG A NH2 
995   N N   . ILE B 60   ? 0.8702 0.8702 0.8702 0.0000  0.0000  0.0000  57   ILE A N   
996   C CA  . ILE B 60   ? 0.8702 0.8702 0.8702 0.0000  0.0000  0.0000  57   ILE A CA  
997   C C   . ILE B 60   ? 0.8702 0.8702 0.8702 0.0000  0.0000  0.0000  57   ILE A C   
998   O O   . ILE B 60   ? 0.8702 0.8702 0.8702 0.0000  0.0000  0.0000  57   ILE A O   
999   C CB  . ILE B 60   ? 0.8702 0.8702 0.8702 0.0000  0.0000  0.0000  57   ILE A CB  
1000  C CG1 . ILE B 60   ? 0.8702 0.8702 0.8702 0.0000  0.0000  0.0000  57   ILE A CG1 
1001  C CG2 . ILE B 60   ? 0.8702 0.8702 0.8702 0.0000  0.0000  0.0000  57   ILE A CG2 
1002  C CD1 . ILE B 60   ? 0.8702 0.8702 0.8702 0.0000  0.0000  0.0000  57   ILE A CD1 
1003  N N   . TYR B 61   ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  58   TYR A N   
1004  C CA  . TYR B 61   ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  58   TYR A CA  
1005  C C   . TYR B 61   ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  58   TYR A C   
1006  O O   . TYR B 61   ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  58   TYR A O   
1007  C CB  . TYR B 61   ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  58   TYR A CB  
1008  C CG  . TYR B 61   ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  58   TYR A CG  
1009  C CD1 . TYR B 61   ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  58   TYR A CD1 
1010  C CD2 . TYR B 61   ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  58   TYR A CD2 
1011  C CE1 . TYR B 61   ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  58   TYR A CE1 
1012  C CE2 . TYR B 61   ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  58   TYR A CE2 
1013  C CZ  . TYR B 61   ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  58   TYR A CZ  
1014  O OH  . TYR B 61   ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  58   TYR A OH  
1015  N N   . LYS B 62   ? 1.2002 0.5566 0.7797 0.1169  -0.1480 0.0867  59   LYS A N   
1016  C CA  . LYS B 62   ? 1.1685 0.5408 0.7558 0.1297  -0.1430 0.0780  59   LYS A CA  
1017  C C   . LYS B 62   ? 1.2421 0.5887 0.7939 0.1701  -0.1468 0.0701  59   LYS A C   
1018  O O   . LYS B 62   ? 1.2350 0.6242 0.8064 0.1924  -0.1366 0.0645  59   LYS A O   
1019  C CB  . LYS B 62   ? 1.1718 0.5133 0.7473 0.1043  -0.1509 0.0776  59   LYS A CB  
1020  C CG  . LYS B 62   ? 1.1307 0.5084 0.7447 0.0672  -0.1454 0.0846  59   LYS A CG  
1021  C CD  . LYS B 62   ? 1.1502 0.5016 0.7521 0.0439  -0.1533 0.0843  59   LYS A CD  
1022  C CE  . LYS B 62   ? 1.2359 0.5098 0.7819 0.0360  -0.1725 0.0873  59   LYS A CE  
1023  N NZ  . LYS B 62   ? 1.2466 0.4956 0.7796 0.0111  -0.1811 0.0878  59   LYS A NZ  
1024  N N   . THR B 63   ? 1.3362 0.6134 0.8336 0.1806  -0.1619 0.0700  60   THR A N   
1025  C CA  . THR B 63   ? 1.4012 0.6489 0.8584 0.2221  -0.1669 0.0622  60   THR A CA  
1026  C C   . THR B 63   ? 1.4092 0.7048 0.8843 0.2514  -0.1565 0.0622  60   THR A C   
1027  O O   . THR B 63   ? 1.4004 0.7276 0.8809 0.2815  -0.1494 0.0559  60   THR A O   
1028  C CB  . THR B 63   ? 1.5007 0.6577 0.8912 0.2259  -0.1869 0.0626  60   THR A CB  
1029  O OG1 . THR B 63   ? 1.5475 0.6644 0.9243 0.1919  -0.1971 0.0648  60   THR A OG1 
1030  C CG2 . THR B 63   ? 1.5445 0.6690 0.8899 0.2689  -0.1926 0.0524  60   THR A CG2 
1031  N N   . TYR B 64   ? 1.4305 0.7351 0.9156 0.2423  -0.1554 0.0698  61   TYR A N   
1032  C CA  . TYR B 64   ? 1.4359 0.7849 0.9361 0.2689  -0.1466 0.0706  61   TYR A CA  
1033  C C   . TYR B 64   ? 1.3978 0.8313 0.9550 0.2684  -0.1292 0.0698  61   TYR A C   
1034  O O   . TYR B 64   ? 1.3861 0.8577 0.9495 0.2988  -0.1222 0.0666  61   TYR A O   
1035  C CB  . TYR B 64   ? 1.4215 0.7632 0.9228 0.2553  -0.1490 0.0794  61   TYR A CB  
1036  C CG  . TYR B 64   ? 1.3724 0.7655 0.8943 0.2784  -0.1394 0.0812  61   TYR A CG  
1037  C CD1 . TYR B 64   ? 1.4050 0.7789 0.8899 0.3184  -0.1439 0.0779  61   TYR A CD1 
1038  C CD2 . TYR B 64   ? 1.3073 0.7680 0.8835 0.2607  -0.1262 0.0863  61   TYR A CD2 
1039  C CE1 . TYR B 64   ? 1.3839 0.8089 0.8881 0.3390  -0.1352 0.0802  61   TYR A CE1 
1040  C CE2 . TYR B 64   ? 1.2870 0.7950 0.8813 0.2798  -0.1182 0.0884  61   TYR A CE2 
1041  C CZ  . TYR B 64   ? 1.3246 0.8168 0.8841 0.3183  -0.1225 0.0857  61   TYR A CZ  
1042  O OH  . TYR B 64   ? 1.3005 0.8440 0.8788 0.3368  -0.1145 0.0885  61   TYR A OH  
1043  N N   . ALA B 65   ? 1.3798 0.8442 0.9775 0.2342  -0.1225 0.0730  62   ALA A N   
1044  C CA  . ALA B 65   ? 1.3353 0.8738 0.9834 0.2316  -0.1075 0.0722  62   ALA A CA  
1045  C C   . ALA B 65   ? 1.3513 0.9001 0.9947 0.2518  -0.1048 0.0643  62   ALA A C   
1046  O O   . ALA B 65   ? 1.3395 0.9424 1.0050 0.2698  -0.0949 0.0629  62   ALA A O   
1047  C CB  . ALA B 65   ? 1.2958 0.8574 0.9815 0.1926  -0.1024 0.0767  62   ALA A CB  
1048  N N   . ASP B 66   ? 1.3912 0.8896 1.0050 0.2484  -0.1139 0.0595  63   ASP A N   
1049  C CA  . ASP B 66   ? 1.4220 0.9265 1.0282 0.2685  -0.1121 0.0517  63   ASP A CA  
1050  C C   . ASP B 66   ? 1.4499 0.9532 1.0271 0.3127  -0.1135 0.0475  63   ASP A C   
1051  O O   . ASP B 66   ? 1.4442 0.9927 1.0356 0.3333  -0.1052 0.0440  63   ASP A O   
1052  C CB  . ASP B 66   ? 1.5066 0.9510 1.0820 0.2558  -0.1234 0.0476  63   ASP A CB  
1053  C CG  . ASP B 66   ? 1.5533 1.0153 1.1354 0.2650  -0.1190 0.0404  63   ASP A CG  
1054  O OD1 . ASP B 66   ? 1.5839 1.0658 1.1579 0.2987  -0.1154 0.0357  63   ASP A OD1 
1055  O OD2 . ASP B 66   ? 1.5575 1.0158 1.1530 0.2387  -0.1191 0.0399  63   ASP A OD2 
1056  N N   . GLN B 67   ? 1.4751 0.9288 1.0105 0.3282  -0.1241 0.0484  64   GLN A N   
1057  C CA  . GLN B 67   ? 1.4636 0.9148 0.9674 0.3734  -0.1260 0.0445  64   GLN A CA  
1058  C C   . GLN B 67   ? 1.3661 0.8972 0.9089 0.3868  -0.1123 0.0485  64   GLN A C   
1059  O O   . GLN B 67   ? 1.3598 0.9254 0.8992 0.4201  -0.1075 0.0452  64   GLN A O   
1060  C CB  . GLN B 67   ? 1.5167 0.8936 0.9654 0.3853  -0.1411 0.0451  64   GLN A CB  
1061  C CG  . GLN B 67   ? 1.5889 0.8804 0.9852 0.3819  -0.1573 0.0401  64   GLN A CG  
1062  C CD  . GLN B 67   ? 1.6702 0.9001 1.0209 0.3793  -0.1699 0.0396  64   GLN A CD  
1063  O OE1 . GLN B 67   ? 1.7312 0.9316 1.0386 0.4025  -0.1760 0.0304  64   GLN A OE1 
1064  N NE2 . GLN B 67   ? 1.6734 0.8860 1.0330 0.3496  -0.1738 0.0493  64   GLN A NE2 
1065  N N   . CYS B 68   ? 1.2937 0.8565 0.8727 0.3612  -0.1063 0.0561  65   CYS A N   
1066  C CA  . CYS B 68   ? 1.2263 0.8638 0.8419 0.3702  -0.0943 0.0607  65   CYS A CA  
1067  C C   . CYS B 68   ? 1.1545 0.8584 0.8116 0.3648  -0.0822 0.0598  65   CYS A C   
1068  O O   . CYS B 68   ? 1.0974 0.8603 0.7711 0.3846  -0.0742 0.0615  65   CYS A O   
1069  C CB  . CYS B 68   ? 1.2118 0.8620 0.8534 0.3429  -0.0919 0.0687  65   CYS A CB  
1070  S SG  . CYS B 68   ? 1.3062 0.8943 0.9033 0.3535  -0.1042 0.0718  65   CYS A SG  
1071  N N   . LEU B 69   ? 1.1375 0.8340 0.8107 0.3379  -0.0811 0.0579  66   LEU A N   
1072  C CA  . LEU B 69   ? 1.0796 0.8339 0.7897 0.3309  -0.0705 0.0572  66   LEU A CA  
1073  C C   . LEU B 69   ? 1.1376 0.8968 0.8277 0.3618  -0.0705 0.0507  66   LEU A C   
1074  O O   . LEU B 69   ? 1.1327 0.9463 0.8513 0.3613  -0.0614 0.0509  66   LEU A O   
1075  C CB  . LEU B 69   ? 0.9974 0.7420 0.7302 0.2928  -0.0694 0.0573  66   LEU A CB  
1076  C CG  . LEU B 69   ? 0.9057 0.6600 0.6661 0.2608  -0.0670 0.0641  66   LEU A CG  
1077  C CD1 . LEU B 69   ? 0.8503 0.5963 0.6294 0.2275  -0.0662 0.0637  66   LEU A CD1 
1078  C CD2 . LEU B 69   ? 0.8420 0.6636 0.6380 0.2609  -0.0569 0.0696  66   LEU A CD2 
1079  N N   . GLN B 70   ? 1.2088 0.9121 0.8489 0.3890  -0.0810 0.0451  67   GLN A N   
1080  C CA  . GLN B 70   ? 1.2692 0.9756 0.8867 0.4215  -0.0815 0.0384  67   GLN A CA  
1081  C C   . GLN B 70   ? 1.2879 1.0544 0.9098 0.4563  -0.0746 0.0407  67   GLN A C   
1082  O O   . GLN B 70   ? 1.3027 1.1035 0.9250 0.4779  -0.0701 0.0377  67   GLN A O   
1083  C CB  . GLN B 70   ? 1.3608 0.9819 0.9182 0.4398  -0.0963 0.0313  67   GLN A CB  
1084  C CG  . GLN B 70   ? 1.3784 0.9433 0.9280 0.4074  -0.1039 0.0288  67   GLN A CG  
1085  C CD  . GLN B 70   ? 1.4561 0.9334 0.9422 0.4240  -0.1203 0.0223  67   GLN A CD  
1086  O OE1 . GLN B 70   ? 1.4977 0.9607 0.9506 0.4584  -0.1239 0.0154  67   GLN A OE1 
1087  N NE2 . GLN B 70   ? 1.4776 0.8952 0.9442 0.3995  -0.1309 0.0250  67   GLN A NE2 
1088  N N   . LEU B 71   ? 1.2979 1.0805 0.9231 0.4621  -0.0737 0.0463  68   LEU A N   
1089  C CA  . LEU B 71   ? 1.3182 1.1609 0.9472 0.4947  -0.0677 0.0495  68   LEU A CA  
1090  C C   . LEU B 71   ? 1.2693 1.1982 0.9543 0.4744  -0.0548 0.0578  68   LEU A C   
1091  O O   . LEU B 71   ? 1.2594 1.2472 0.9528 0.4965  -0.0493 0.0623  68   LEU A O   
1092  C CB  . LEU B 71   ? 1.3679 1.1806 0.9651 0.5162  -0.0747 0.0511  68   LEU A CB  
1093  C CG  . LEU B 71   ? 1.4480 1.1733 0.9835 0.5356  -0.0882 0.0428  68   LEU A CG  
1094  C CD1 . LEU B 71   ? 1.4574 1.1142 0.9807 0.5086  -0.0981 0.0455  68   LEU A CD1 
1095  C CD2 . LEU B 71   ? 1.4949 1.2327 1.0012 0.5669  -0.0871 0.0383  68   LEU A CD2 
1096  N N   . VAL B 72   ? 1.2372 1.1748 0.9584 0.4335  -0.0505 0.0602  69   VAL A N   
1097  C CA  . VAL B 72   ? 1.1709 1.1809 0.9408 0.4115  -0.0402 0.0682  69   VAL A CA  
1098  C C   . VAL B 72   ? 1.1472 1.2195 0.9338 0.4229  -0.0326 0.0690  69   VAL A C   
1099  O O   . VAL B 72   ? 1.1555 1.2164 0.9415 0.4179  -0.0322 0.0641  69   VAL A O   
1100  C CB  . VAL B 72   ? 1.1023 1.0979 0.9007 0.3667  -0.0389 0.0700  69   VAL A CB  
1101  C CG1 . VAL B 72   ? 1.0400 1.1048 0.8835 0.3450  -0.0297 0.0779  69   VAL A CG1 
1102  C CG2 . VAL B 72   ? 1.1150 1.0528 0.8966 0.3554  -0.0465 0.0702  69   VAL A CG2 
1103  N N   . GLN B 73   ? 1.1387 1.2791 0.9402 0.4374  -0.0267 0.0758  70   GLN A N   
1104  C CA  . GLN B 73   ? 1.1096 1.3213 0.9314 0.4445  -0.0189 0.0794  70   GLN A CA  
1105  C C   . GLN B 73   ? 1.0385 1.3195 0.8998 0.4232  -0.0121 0.0903  70   GLN A C   
1106  O O   . GLN B 73   ? 1.0511 1.3597 0.9106 0.4375  -0.0119 0.0955  70   GLN A O   
1107  C CB  . GLN B 73   ? 1.1836 1.4135 0.9745 0.4927  -0.0199 0.0770  70   GLN A CB  
1108  C CG  . GLN B 73   ? 1.2730 1.4725 1.0393 0.5102  -0.0225 0.0682  70   GLN A CG  
1109  C CD  . GLN B 73   ? 1.3579 1.4606 1.0860 0.5124  -0.0330 0.0585  70   GLN A CD  
1110  O OE1 . GLN B 73   ? 1.4020 1.4626 1.0912 0.5402  -0.0405 0.0549  70   GLN A OE1 
1111  N NE2 . GLN B 73   ? 1.3579 1.4245 1.0951 0.4828  -0.0343 0.0545  70   GLN A NE2 
1112  N N   . LEU B 74   ? 0.9914 1.2987 0.8859 0.3893  -0.0073 0.0937  71   LEU A N   
1113  C CA  . LEU B 74   ? 0.9190 1.2851 0.8487 0.3644  -0.0023 0.1040  71   LEU A CA  
1114  C C   . LEU B 74   ? 0.8734 1.2981 0.8267 0.3525  0.0036  0.1089  71   LEU A C   
1115  O O   . LEU B 74   ? 0.8908 1.3017 0.8387 0.3546  0.0042  0.1037  71   LEU A O   
1116  C CB  . LEU B 74   ? 0.8485 1.1795 0.7944 0.3273  -0.0040 0.1044  71   LEU A CB  
1117  C CG  . LEU B 74   ? 0.8328 1.1118 0.7603 0.3320  -0.0096 0.1018  71   LEU A CG  
1118  C CD1 . LEU B 74   ? 0.7848 1.0408 0.7321 0.2944  -0.0102 0.1033  71   LEU A CD1 
1119  C CD2 . LEU B 74   ? 0.8327 1.1481 0.7543 0.3555  -0.0094 0.1075  71   LEU A CD2 
1120  N N   . ASP B 75   ? 0.8411 1.3312 0.8197 0.3387  0.0074  0.1196  72   ASP A N   
1121  C CA  . ASP B 75   ? 0.8308 1.3794 0.8335 0.3206  0.0121  0.1268  72   ASP A CA  
1122  C C   . ASP B 75   ? 0.8118 1.3464 0.8380 0.2764  0.0117  0.1293  72   ASP A C   
1123  O O   . ASP B 75   ? 0.8038 1.3544 0.8434 0.2590  0.0110  0.1357  72   ASP A O   
1124  C CB  . ASP B 75   ? 0.8443 1.4768 0.8568 0.3330  0.0153  0.1383  72   ASP A CB  
1125  C CG  . ASP B 75   ? 0.8717 1.5670 0.9024 0.3211  0.0195  0.1460  72   ASP A CG  
1126  O OD1 . ASP B 75   ? 0.8934 1.5696 0.9354 0.2935  0.0199  0.1443  72   ASP A OD1 
1127  O OD2 . ASP B 75   ? 0.8878 1.6533 0.9206 0.3397  0.0223  0.1543  72   ASP A OD2 
1128  N N   . TRP B 76   ? 0.7997 1.3040 0.8290 0.2597  0.0120  0.1240  73   TRP A N   
1129  C CA  . TRP B 76   ? 0.7692 1.2508 0.8154 0.2216  0.0111  0.1244  73   TRP A CA  
1130  C C   . TRP B 76   ? 0.7708 1.3074 0.8395 0.1960  0.0134  0.1343  73   TRP A C   
1131  O O   . TRP B 76   ? 0.7653 1.2829 0.8448 0.1659  0.0124  0.1342  73   TRP A O   
1132  C CB  . TRP B 76   ? 0.7409 1.1625 0.7780 0.2163  0.0098  0.1141  73   TRP A CB  
1133  C CG  . TRP B 76   ? 0.7302 1.0939 0.7423 0.2381  0.0060  0.1050  73   TRP A CG  
1134  C CD1 . TRP B 76   ? 0.7459 1.0967 0.7340 0.2708  0.0049  0.0993  73   TRP A CD1 
1135  C CD2 . TRP B 76   ? 0.7277 1.0371 0.7335 0.2280  0.0020  0.1009  73   TRP A CD2 
1136  N NE1 . TRP B 76   ? 0.7662 1.0543 0.7318 0.2803  -0.0004 0.0922  73   TRP A NE1 
1137  C CE2 . TRP B 76   ? 0.7608 1.0248 0.7380 0.2537  -0.0020 0.0935  73   TRP A CE2 
1138  C CE3 . TRP B 76   ? 0.7005 0.9953 0.7203 0.2001  0.0009  0.1032  73   TRP A CE3 
1139  C CZ2 . TRP B 76   ? 0.7725 0.9789 0.7357 0.2497  -0.0072 0.0892  73   TRP A CZ2 
1140  C CZ3 . TRP B 76   ? 0.7007 0.9422 0.7085 0.1982  -0.0032 0.0987  73   TRP A CZ3 
1141  C CH2 . TRP B 76   ? 0.7384 0.9370 0.7187 0.2216  -0.0073 0.0923  73   TRP A CH2 
1142  N N   . GLU B 77   ? 0.8300 1.4342 0.9040 0.2071  0.0159  0.1433  74   GLU A N   
1143  C CA  . GLU B 77   ? 0.8522 1.5098 0.9452 0.1808  0.0170  0.1540  74   GLU A CA  
1144  C C   . GLU B 77   ? 0.8205 1.4826 0.9270 0.1495  0.0139  0.1608  74   GLU A C   
1145  O O   . GLU B 77   ? 0.8021 1.4684 0.9192 0.1180  0.0123  0.1652  74   GLU A O   
1146  C CB  . GLU B 77   ? 0.9083 1.6427 1.0033 0.2005  0.0201  0.1633  74   GLU A CB  
1147  C CG  . GLU B 77   ? 0.9528 1.7461 1.0653 0.1728  0.0207  0.1757  74   GLU A CG  
1148  C CD  . GLU B 77   ? 1.0187 1.7905 1.1324 0.1583  0.0215  0.1719  74   GLU A CD  
1149  O OE1 . GLU B 77   ? 1.0565 1.7938 1.1575 0.1803  0.0233  0.1614  74   GLU A OE1 
1150  O OE2 . GLU B 77   ? 1.0280 1.8155 1.1535 0.1246  0.0196  0.1793  74   GLU A OE2 
1151  N N   . ASN B 78   ? 0.8064 1.4652 0.9101 0.1582  0.0124  0.1617  75   ASN A N   
1152  C CA  . ASN B 78   ? 0.7692 1.4312 0.8839 0.1302  0.0090  0.1678  75   ASN A CA  
1153  C C   . ASN B 78   ? 0.7312 1.3288 0.8457 0.1067  0.0063  0.1604  75   ASN A C   
1154  O O   . ASN B 78   ? 0.7096 1.3092 0.8328 0.0762  0.0034  0.1653  75   ASN A O   
1155  C CB  . ASN B 78   ? 0.7979 1.4694 0.9087 0.1475  0.0082  0.1698  75   ASN A CB  
1156  C CG  . ASN B 78   ? 0.8229 1.5677 0.9354 0.1685  0.0105  0.1790  75   ASN A CG  
1157  O OD1 . ASN B 78   ? 0.8088 1.6069 0.9335 0.1530  0.0092  0.1906  75   ASN A OD1 
1158  N ND2 . ASN B 78   ? 0.8532 1.6016 0.9517 0.2042  0.0134  0.1742  75   ASN A ND2 
1159  N N   . LEU B 79   ? 0.7135 1.2538 0.8161 0.1206  0.0068  0.1490  76   LEU A N   
1160  C CA  . LEU B 79   ? 0.6514 1.1349 0.7536 0.1004  0.0046  0.1422  76   LEU A CA  
1161  C C   . LEU B 79   ? 0.5951 1.0782 0.7031 0.0791  0.0048  0.1424  76   LEU A C   
1162  O O   . LEU B 79   ? 0.5858 1.0460 0.6976 0.0539  0.0022  0.1421  76   LEU A O   
1163  C CB  . LEU B 79   ? 0.6157 1.0432 0.7030 0.1195  0.0045  0.1313  76   LEU A CB  
1164  C CG  . LEU B 79   ? 0.5441 0.9151 0.6300 0.1017  0.0024  0.1246  76   LEU A CG  
1165  C CD1 . LEU B 79   ? 0.4870 0.8555 0.5803 0.0827  -0.0002 0.1287  76   LEU A CD1 
1166  C CD2 . LEU B 79   ? 0.5486 0.8703 0.6183 0.1203  0.0014  0.1157  76   LEU A CD2 
1167  N N   . SER B 80   ? 0.5812 1.0891 0.6882 0.0900  0.0077  0.1429  77   SER A N   
1168  C CA  . SER B 80   ? 0.5781 1.0875 0.6897 0.0704  0.0078  0.1437  77   SER A CA  
1169  C C   . SER B 80   ? 0.5761 1.1222 0.6977 0.0416  0.0048  0.1549  77   SER A C   
1170  O O   . SER B 80   ? 0.5772 1.1029 0.6996 0.0168  0.0022  0.1548  77   SER A O   
1171  C CB  . SER B 80   ? 0.6072 1.1410 0.7154 0.0897  0.0115  0.1427  77   SER A CB  
1172  O OG  . SER B 80   ? 0.6199 1.1603 0.7327 0.0702  0.0116  0.1448  77   SER A OG  
1173  N N   . ALA B 81   ? 0.5644 1.1640 0.6917 0.0443  0.0046  0.1650  78   ALA A N   
1174  C CA  . ALA B 81   ? 0.5413 1.1777 0.6762 0.0149  0.0005  0.1770  78   ALA A CA  
1175  C C   . ALA B 81   ? 0.5130 1.1109 0.6465 -0.0079 -0.0047 0.1758  78   ALA A C   
1176  O O   . ALA B 81   ? 0.5349 1.1318 0.6680 -0.0370 -0.0096 0.1811  78   ALA A O   
1177  C CB  . ALA B 81   ? 0.5374 1.2437 0.6787 0.0239  0.0013  0.1886  78   ALA A CB  
1178  N N   . ALA B 82   ? 0.4816 1.0467 0.6119 0.0053  -0.0043 0.1690  79   ALA A N   
1179  C CA  . ALA B 82   ? 0.4918 1.0193 0.6197 -0.0134 -0.0088 0.1671  79   ALA A CA  
1180  C C   . ALA B 82   ? 0.5373 1.0119 0.6592 -0.0260 -0.0100 0.1589  79   ALA A C   
1181  O O   . ALA B 82   ? 0.5385 0.9917 0.6567 -0.0485 -0.0150 0.1598  79   ALA A O   
1182  C CB  . ALA B 82   ? 0.4965 1.0050 0.6226 0.0048  -0.0078 0.1626  79   ALA A CB  
1183  N N   . ILE B 83   ? 0.5715 1.0242 0.6904 -0.0109 -0.0060 0.1507  80   ILE A N   
1184  C CA  . ILE B 83   ? 0.5942 1.0028 0.7078 -0.0219 -0.0068 0.1434  80   ILE A CA  
1185  C C   . ILE B 83   ? 0.5536 0.9789 0.6666 -0.0443 -0.0097 0.1495  80   ILE A C   
1186  O O   . ILE B 83   ? 0.5490 0.9439 0.6554 -0.0634 -0.0137 0.1478  80   ILE A O   
1187  C CB  . ILE B 83   ? 0.6483 1.0317 0.7582 -0.0005 -0.0024 0.1338  80   ILE A CB  
1188  C CG1 . ILE B 83   ? 0.3693 0.7279 0.4756 0.0180  -0.0014 0.1282  80   ILE A CG1 
1189  C CG2 . ILE B 83   ? 0.3620 0.7064 0.4672 -0.0117 -0.0030 0.1270  80   ILE A CG2 
1190  C CD1 . ILE B 83   ? 0.3771 0.7072 0.4761 0.0377  0.0014  0.1192  80   ILE A CD1 
1191  N N   . ASP B 84   ? 0.5267 1.0007 0.6447 -0.0418 -0.0080 0.1570  81   ASP A N   
1192  C CA  . ASP B 84   ? 0.5298 1.0225 0.6463 -0.0644 -0.0112 0.1643  81   ASP A CA  
1193  C C   . ASP B 84   ? 0.5273 1.0245 0.6399 -0.0927 -0.0189 0.1729  81   ASP A C   
1194  O O   . ASP B 84   ? 0.5138 0.9887 0.6170 -0.1152 -0.0242 0.1740  81   ASP A O   
1195  C CB  . ASP B 84   ? 0.5679 1.1191 0.6911 -0.0552 -0.0078 0.1721  81   ASP A CB  
1196  C CG  . ASP B 84   ? 0.6319 1.1735 0.7544 -0.0324 -0.0017 0.1638  81   ASP A CG  
1197  O OD1 . ASP B 84   ? 0.6393 1.1314 0.7570 -0.0212 0.0000  0.1521  81   ASP A OD1 
1198  O OD2 . ASP B 84   ? 0.6694 1.2544 0.7954 -0.0260 0.0010  0.1693  81   ASP A OD2 
1199  N N   . SER B 85   ? 0.5480 1.0717 0.6654 -0.0916 -0.0203 0.1788  82   SER A N   
1200  C CA  . SER B 85   ? 0.5647 1.0945 0.6770 -0.1189 -0.0285 0.1876  82   SER A CA  
1201  C C   . SER B 85   ? 0.5718 1.0407 0.6721 -0.1302 -0.0332 0.1799  82   SER A C   
1202  O O   . SER B 85   ? 0.5894 1.0456 0.6779 -0.1561 -0.0414 0.1848  82   SER A O   
1203  C CB  . SER B 85   ? 0.5453 1.1180 0.6660 -0.1129 -0.0286 0.1951  82   SER A CB  
1204  O OG  . SER B 85   ? 0.5251 1.1630 0.6547 -0.1079 -0.0260 0.2052  82   SER A OG  
1205  N N   . TYR B 86   ? 0.5696 1.0003 0.6705 -0.1112 -0.0289 0.1685  83   TYR A N   
1206  C CA  . TYR B 86   ? 0.5978 0.9751 0.6874 -0.1195 -0.0328 0.1614  83   TYR A CA  
1207  C C   . TYR B 86   ? 0.6191 0.9635 0.6975 -0.1297 -0.0347 0.1568  83   TYR A C   
1208  O O   . TYR B 86   ? 0.6407 0.9527 0.7043 -0.1462 -0.0414 0.1559  83   TYR A O   
1209  C CB  . TYR B 86   ? 0.6090 0.9601 0.7027 -0.0977 -0.0278 0.1520  83   TYR A CB  
1210  C CG  . TYR B 86   ? 0.6292 0.9319 0.7123 -0.1041 -0.0313 0.1454  83   TYR A CG  
1211  C CD1 . TYR B 86   ? 0.6624 0.9566 0.7352 -0.1229 -0.0389 0.1496  83   TYR A CD1 
1212  C CD2 . TYR B 86   ? 0.6027 0.8695 0.6844 -0.0912 -0.0274 0.1352  83   TYR A CD2 
1213  C CE1 . TYR B 86   ? 0.6721 0.9235 0.7331 -0.1261 -0.0421 0.1434  83   TYR A CE1 
1214  C CE2 . TYR B 86   ? 0.6201 0.8485 0.6922 -0.0956 -0.0302 0.1299  83   TYR A CE2 
1215  C CZ  . TYR B 86   ? 0.6708 0.8918 0.7323 -0.1118 -0.0373 0.1337  83   TYR A CZ  
1216  O OH  . TYR B 86   ? 0.7051 0.8891 0.7550 -0.1136 -0.0402 0.1282  83   TYR A OH  
1217  N N   . ARG B 87   ? 0.6169 0.9678 0.7003 -0.1188 -0.0293 0.1537  84   ARG A N   
1218  C CA  . ARG B 87   ? 0.6275 0.9521 0.7004 -0.1286 -0.0311 0.1503  84   ARG A CA  
1219  C C   . ARG B 87   ? 0.6371 0.9810 0.7012 -0.1544 -0.0382 0.1611  84   ARG A C   
1220  O O   . ARG B 87   ? 0.5822 0.8944 0.6304 -0.1692 -0.0435 0.1597  84   ARG A O   
1221  C CB  . ARG B 87   ? 0.6125 0.9405 0.6930 -0.1101 -0.0236 0.1444  84   ARG A CB  
1222  C CG  . ARG B 87   ? 0.6193 0.9220 0.7046 -0.0874 -0.0180 0.1339  84   ARG A CG  
1223  C CD  . ARG B 87   ? 0.6223 0.9298 0.7125 -0.0700 -0.0118 0.1288  84   ARG A CD  
1224  N NE  . ARG B 87   ? 0.6326 0.9150 0.7248 -0.0503 -0.0079 0.1198  84   ARG A NE  
1225  C CZ  . ARG B 87   ? 0.6465 0.9278 0.7407 -0.0323 -0.0033 0.1146  84   ARG A CZ  
1226  N NH1 . ARG B 87   ? 0.6491 0.9554 0.7450 -0.0294 -0.0012 0.1170  84   ARG A NH1 
1227  N NH2 . ARG B 87   ? 0.6361 0.8907 0.7288 -0.0177 -0.0014 0.1073  84   ARG A NH2 
1228  N N   . LYS B 88   ? 0.6860 1.0817 0.7585 -0.1601 -0.0390 0.1723  85   LYS A N   
1229  C CA  . LYS B 88   ? 0.7694 1.1894 0.8337 -0.1874 -0.0466 0.1848  85   LYS A CA  
1230  C C   . LYS B 88   ? 0.8461 1.2372 0.8926 -0.2105 -0.0572 0.1878  85   LYS A C   
1231  O O   . LYS B 88   ? 0.8543 1.2082 0.8806 -0.2282 -0.0646 0.1872  85   LYS A O   
1232  C CB  . LYS B 88   ? 0.7593 1.2491 0.8387 -0.1856 -0.0441 0.1966  85   LYS A CB  
1233  C CG  . LYS B 88   ? 0.7288 1.2567 0.8068 -0.2028 -0.0466 0.2078  85   LYS A CG  
1234  C CD  . LYS B 88   ? 0.7498 1.2761 0.8110 -0.2394 -0.0590 0.2194  85   LYS A CD  
1235  C CE  . LYS B 88   ? 0.7705 1.3548 0.8346 -0.2574 -0.0615 0.2348  85   LYS A CE  
1236  N NZ  . LYS B 88   ? 0.7723 1.3567 0.8380 -0.2493 -0.0561 0.2316  85   LYS A NZ  
1237  N N   . GLU B 89   ? 0.9252 1.3311 0.9769 -0.2096 -0.0586 0.1910  86   GLU A N   
1238  C CA  . GLU B 89   ? 0.9682 1.3447 1.0027 -0.2280 -0.0685 0.1926  86   GLU A CA  
1239  C C   . GLU B 89   ? 0.9787 1.3125 1.0125 -0.2096 -0.0653 0.1801  86   GLU A C   
1240  O O   . GLU B 89   ? 0.9802 1.3294 1.0309 -0.1879 -0.0575 0.1764  86   GLU A O   
1241  C CB  . GLU B 89   ? 0.9846 1.4079 1.0243 -0.2417 -0.0733 0.2055  86   GLU A CB  
1242  C CG  . GLU B 89   ? 1.0409 1.4887 1.0686 -0.2742 -0.0833 0.2199  86   GLU A CG  
1243  C CD  . GLU B 89   ? 1.0606 1.5756 1.1062 -0.2720 -0.0778 0.2299  86   GLU A CD  
1244  O OE1 . GLU B 89   ? 1.0544 1.5908 1.1192 -0.2433 -0.0664 0.2242  86   GLU A OE1 
1245  O OE2 . GLU B 89   ? 1.0778 1.6245 1.1166 -0.2992 -0.0856 0.2439  86   GLU A OE2 
1246  N N   . LYS B 90   ? 0.9862 1.2667 0.9985 -0.2179 -0.0716 0.1742  87   LYS A N   
1247  C CA  . LYS B 90   ? 0.9559 1.1969 0.9653 -0.2021 -0.0692 0.1631  87   LYS A CA  
1248  C C   . LYS B 90   ? 0.9504 1.1859 0.9521 -0.2103 -0.0758 0.1662  87   LYS A C   
1249  O O   . LYS B 90   ? 0.9836 1.1760 0.9664 -0.2131 -0.0814 0.1608  87   LYS A O   
1250  C CB  . LYS B 90   ? 0.9489 1.1383 0.9389 -0.2023 -0.0717 0.1544  87   LYS A CB  
1251  C CG  . LYS B 90   ? 0.9251 1.1155 0.9226 -0.1920 -0.0647 0.1497  87   LYS A CG  
1252  C CD  . LYS B 90   ? 0.9526 1.1509 0.9387 -0.2121 -0.0704 0.1573  87   LYS A CD  
1253  C CE  . LYS B 90   ? 0.9709 1.1616 0.9605 -0.2019 -0.0643 0.1514  87   LYS A CE  
1254  N NZ  . LYS B 90   ? 0.9627 1.1866 0.9789 -0.1803 -0.0528 0.1487  87   LYS A NZ  
1255  N N   . THR B 91   ? 0.9410 1.2217 0.9565 -0.2131 -0.0753 0.1749  88   THR A N   
1256  C CA  . THR B 91   ? 0.9557 1.2374 0.9657 -0.2213 -0.0815 0.1789  88   THR A CA  
1257  C C   . THR B 91   ? 0.9410 1.2297 0.9685 -0.1973 -0.0732 0.1734  88   THR A C   
1258  O O   . THR B 91   ? 0.9436 1.2508 0.9895 -0.1769 -0.0635 0.1701  88   THR A O   
1259  C CB  . THR B 91   ? 0.9939 1.3233 1.0060 -0.2423 -0.0876 0.1934  88   THR A CB  
1260  O OG1 . THR B 91   ? 1.0451 1.3789 1.0544 -0.2479 -0.0927 0.1969  88   THR A OG1 
1261  C CG2 . THR B 91   ? 0.9681 1.3561 1.0058 -0.2296 -0.0784 0.1986  88   THR A CG2 
1262  N N   . GLU B 92   ? 0.9332 1.2041 0.9522 -0.2001 -0.0781 0.1725  89   GLU A N   
1263  C CA  . GLU B 92   ? 0.8993 1.1733 0.9319 -0.1797 -0.0715 0.1680  89   GLU A CA  
1264  C C   . GLU B 92   ? 0.8622 1.1900 0.9156 -0.1714 -0.0665 0.1752  89   GLU A C   
1265  O O   . GLU B 92   ? 0.8482 1.1808 0.9144 -0.1505 -0.0595 0.1712  89   GLU A O   
1266  C CB  . GLU B 92   ? 0.9123 1.1579 0.9296 -0.1860 -0.0786 0.1665  89   GLU A CB  
1267  N N   . GLU B 93   ? 0.8325 1.2012 0.8880 -0.1871 -0.0705 0.1862  90   GLU A N   
1268  C CA  . GLU B 93   ? 0.7902 1.2154 0.8647 -0.1768 -0.0654 0.1934  90   GLU A CA  
1269  C C   . GLU B 93   ? 0.7547 1.1953 0.8433 -0.1542 -0.0553 0.1893  90   GLU A C   
1270  O O   . GLU B 93   ? 0.7215 1.1839 0.8229 -0.1320 -0.0486 0.1884  90   GLU A O   
1271  C CB  . GLU B 93   ? 0.7815 1.2511 0.8538 -0.2013 -0.0730 0.2075  90   GLU A CB  
1272  C CG  . GLU B 93   ? 0.7742 1.3094 0.8649 -0.1908 -0.0684 0.2164  90   GLU A CG  
1273  C CD  . GLU B 93   ? 0.7908 1.3630 0.8938 -0.1782 -0.0611 0.2184  90   GLU A CD  
1274  O OE1 . GLU B 93   ? 0.7923 1.3558 0.8887 -0.1909 -0.0630 0.2192  90   GLU A OE1 
1275  O OE2 . GLU B 93   ? 0.8071 1.4152 0.9244 -0.1542 -0.0536 0.2191  90   GLU A OE2 
1276  N N   . THR B 94   ? 0.7605 1.1879 0.8446 -0.1588 -0.0546 0.1868  91   THR A N   
1277  C CA  . THR B 94   ? 0.7524 1.1906 0.8475 -0.1375 -0.0456 0.1823  91   THR A CA  
1278  C C   . THR B 94   ? 0.7402 1.1371 0.8365 -0.1157 -0.0396 0.1699  91   THR A C   
1279  O O   . THR B 94   ? 0.7328 1.1384 0.8378 -0.0937 -0.0325 0.1660  91   THR A O   
1280  C CB  . THR B 94   ? 0.7809 1.2175 0.8704 -0.1498 -0.0469 0.1836  91   THR A CB  
1281  O OG1 . THR B 94   ? 0.8203 1.2052 0.8926 -0.1644 -0.0527 0.1782  91   THR A OG1 
1282  C CG2 . THR B 94   ? 0.7905 1.2786 0.8814 -0.1694 -0.0517 0.1976  91   THR A CG2 
1283  N N   . ARG B 95   ? 0.7668 1.1191 0.8526 -0.1216 -0.0431 0.1639  92   ARG A N   
1284  C CA  . ARG B 95   ? 0.7685 1.0862 0.8556 -0.1033 -0.0380 0.1538  92   ARG A CA  
1285  C C   . ARG B 95   ? 0.7393 1.0723 0.8354 -0.0868 -0.0347 0.1548  92   ARG A C   
1286  O O   . ARG B 95   ? 0.7489 1.0774 0.8507 -0.0665 -0.0288 0.1499  92   ARG A O   
1287  C CB  . ARG B 95   ? 0.8646 1.1368 0.9376 -0.1130 -0.0427 0.1483  92   ARG A CB  
1288  C CG  . ARG B 95   ? 0.9524 1.1896 1.0251 -0.0984 -0.0377 0.1382  92   ARG A CG  
1289  C CD  . ARG B 95   ? 1.0426 1.2511 1.1083 -0.0976 -0.0399 0.1344  92   ARG A CD  
1290  N NE  . ARG B 95   ? 1.1287 1.3235 1.1786 -0.1153 -0.0482 0.1366  92   ARG A NE  
1291  C CZ  . ARG B 95   ? 1.1844 1.3875 1.2309 -0.1226 -0.0531 0.1416  92   ARG A CZ  
1292  N NH1 . ARG B 95   ? 1.2241 1.4092 1.2522 -0.1389 -0.0618 0.1431  92   ARG A NH1 
1293  N NH2 . ARG B 95   ? 1.1775 1.4048 1.2369 -0.1131 -0.0498 0.1448  92   ARG A NH2 
1294  N N   . ASN B 96   ? 0.7048 1.0541 0.8003 -0.0957 -0.0393 0.1611  93   ASN A N   
1295  C CA  . ASN B 96   ? 0.6672 1.0325 0.7702 -0.0804 -0.0366 0.1626  93   ASN A CA  
1296  C C   . ASN B 96   ? 0.5899 0.9973 0.7030 -0.0637 -0.0316 0.1666  93   ASN A C   
1297  O O   . ASN B 96   ? 0.5699 0.9792 0.6866 -0.0427 -0.0275 0.1645  93   ASN A O   
1298  C CB  . ASN B 96   ? 0.7083 1.0857 0.8080 -0.0948 -0.0430 0.1692  93   ASN A CB  
1299  C CG  . ASN B 96   ? 0.7754 1.1090 0.8625 -0.1060 -0.0479 0.1644  93   ASN A CG  
1300  O OD1 . ASN B 96   ? 0.7945 1.0922 0.8750 -0.1053 -0.0469 0.1570  93   ASN A OD1 
1301  N ND2 . ASN B 96   ? 0.8114 1.1492 0.8941 -0.1153 -0.0533 0.1686  93   ASN A ND2 
1302  N N   . ALA B 97   ? 0.5506 0.9918 0.6664 -0.0721 -0.0323 0.1727  94   ALA A N   
1303  C CA  . ALA B 97   ? 0.5172 1.0007 0.6412 -0.0538 -0.0272 0.1763  94   ALA A CA  
1304  C C   . ALA B 97   ? 0.5232 0.9810 0.6462 -0.0317 -0.0211 0.1668  94   ALA A C   
1305  O O   . ALA B 97   ? 0.5315 1.0031 0.6563 -0.0075 -0.0169 0.1658  94   ALA A O   
1306  C CB  . ALA B 97   ? 0.4892 1.0168 0.6160 -0.0697 -0.0296 0.1857  94   ALA A CB  
1307  N N   . LEU B 98   ? 0.5217 0.9405 0.6395 -0.0392 -0.0212 0.1599  95   LEU A N   
1308  C CA  . LEU B 98   ? 0.5356 0.9273 0.6513 -0.0208 -0.0163 0.1510  95   LEU A CA  
1309  C C   . LEU B 98   ? 0.5589 0.9166 0.6710 -0.0068 -0.0150 0.1449  95   LEU A C   
1310  O O   . LEU B 98   ? 0.5808 0.9293 0.6900 0.0144  -0.0117 0.1405  95   LEU A O   
1311  C CB  . LEU B 98   ? 0.5444 0.9067 0.6556 -0.0337 -0.0170 0.1459  95   LEU A CB  
1312  C CG  . LEU B 98   ? 0.3641 0.6958 0.4723 -0.0184 -0.0128 0.1367  95   LEU A CG  
1313  C CD1 . LEU B 98   ? 0.3977 0.7562 0.5080 0.0026  -0.0086 0.1373  95   LEU A CD1 
1314  C CD2 . LEU B 98   ? 0.3623 0.6703 0.4664 -0.0323 -0.0137 0.1327  95   LEU A CD2 
1315  N N   . ILE B 99   ? 0.5503 0.8881 0.6603 -0.0184 -0.0184 0.1447  96   ILE A N   
1316  C CA  . ILE B 99   ? 0.5559 0.8636 0.6625 -0.0074 -0.0176 0.1402  96   ILE A CA  
1317  C C   . ILE B 99   ? 0.5807 0.9105 0.6885 0.0119  -0.0161 0.1435  96   ILE A C   
1318  O O   . ILE B 99   ? 0.5917 0.8994 0.6939 0.0292  -0.0143 0.1392  96   ILE A O   
1319  C CB  . ILE B 99   ? 0.5339 0.8217 0.6379 -0.0235 -0.0216 0.1403  96   ILE A CB  
1320  C CG1 . ILE B 99   ? 0.4960 0.7552 0.5948 -0.0373 -0.0230 0.1354  96   ILE A CG1 
1321  C CG2 . ILE B 99   ? 0.5427 0.8081 0.6442 -0.0130 -0.0209 0.1378  96   ILE A CG2 
1322  C CD1 . ILE B 99   ? 0.4771 0.7159 0.5698 -0.0508 -0.0273 0.1349  96   ILE A CD1 
1323  N N   . GLU B 100  ? 0.6112 0.9846 0.7245 0.0091  -0.0173 0.1516  97   GLU A N   
1324  C CA  . GLU B 100  ? 0.6290 1.0283 0.7425 0.0298  -0.0158 0.1551  97   GLU A CA  
1325  C C   . GLU B 100  ? 0.6029 1.0138 0.7130 0.0521  -0.0120 0.1530  97   GLU A C   
1326  O O   . GLU B 100  ? 0.6080 1.0110 0.7104 0.0757  -0.0106 0.1507  97   GLU A O   
1327  C CB  . GLU B 100  ? 0.7019 1.1502 0.8224 0.0202  -0.0183 0.1651  97   GLU A CB  
1328  C CG  . GLU B 100  ? 0.7778 1.2146 0.8986 0.0025  -0.0227 0.1673  97   GLU A CG  
1329  C CD  . GLU B 100  ? 0.8379 1.3235 0.9642 -0.0040 -0.0256 0.1775  97   GLU A CD  
1330  O OE1 . GLU B 100  ? 0.8553 1.3867 0.9861 0.0075  -0.0235 0.1830  97   GLU A OE1 
1331  O OE2 . GLU B 100  ? 0.8594 1.3393 0.9850 -0.0202 -0.0301 0.1801  97   GLU A OE2 
1332  N N   . GLU B 101  ? 0.5840 1.0117 0.6974 0.0459  -0.0108 0.1537  98   GLU A N   
1333  C CA  . GLU B 101  ? 0.6123 1.0520 0.7215 0.0678  -0.0072 0.1514  98   GLU A CA  
1334  C C   . GLU B 101  ? 0.6026 0.9893 0.7002 0.0820  -0.0062 0.1414  98   GLU A C   
1335  O O   . GLU B 101  ? 0.5998 0.9833 0.6871 0.1075  -0.0048 0.1385  98   GLU A O   
1336  C CB  . GLU B 101  ? 0.6448 1.1116 0.7601 0.0555  -0.0063 0.1545  98   GLU A CB  
1337  C CG  . GLU B 101  ? 0.6817 1.1781 0.7942 0.0786  -0.0027 0.1548  98   GLU A CG  
1338  C CD  . GLU B 101  ? 0.7354 1.2883 0.8508 0.0936  -0.0019 0.1633  98   GLU A CD  
1339  O OE1 . GLU B 101  ? 0.7567 1.3440 0.8812 0.0759  -0.0043 0.1722  98   GLU A OE1 
1340  O OE2 . GLU B 101  ? 0.7660 1.3285 0.8726 0.1236  0.0006  0.1612  98   GLU A OE2 
1341  N N   . GLN B 102  ? 0.5859 0.9307 0.6829 0.0659  -0.0075 0.1362  99   GLN A N   
1342  C CA  . GLN B 102  ? 0.5556 0.8514 0.6416 0.0757  -0.0074 0.1279  99   GLN A CA  
1343  C C   . GLN B 102  ? 0.5582 0.8343 0.6348 0.0900  -0.0090 0.1273  99   GLN A C   
1344  O O   . GLN B 102  ? 0.5677 0.8180 0.6302 0.1087  -0.0094 0.1228  99   GLN A O   
1345  C CB  . GLN B 102  ? 0.5267 0.7895 0.6150 0.0547  -0.0084 0.1237  99   GLN A CB  
1346  C CG  . GLN B 102  ? 0.4967 0.7687 0.5901 0.0426  -0.0073 0.1229  99   GLN A CG  
1347  C CD  . GLN B 102  ? 0.4561 0.7018 0.5510 0.0218  -0.0089 0.1201  99   GLN A CD  
1348  O OE1 . GLN B 102  ? 0.4866 0.7136 0.5805 0.0151  -0.0108 0.1198  99   GLN A OE1 
1349  N NE2 . GLN B 102  ? 0.4218 0.6666 0.5179 0.0126  -0.0083 0.1181  99   GLN A NE2 
1350  N N   . ALA B 103  ? 0.5493 0.8350 0.6314 0.0813  -0.0106 0.1320  100  ALA A N   
1351  C CA  . ALA B 103  ? 0.5780 0.8466 0.6510 0.0943  -0.0123 0.1323  100  ALA A CA  
1352  C C   . ALA B 103  ? 0.6063 0.8960 0.6701 0.1218  -0.0116 0.1340  100  ALA A C   
1353  O O   . ALA B 103  ? 0.6407 0.9020 0.6886 0.1393  -0.0134 0.1315  100  ALA A O   
1354  C CB  . ALA B 103  ? 0.5548 0.8349 0.6364 0.0796  -0.0140 0.1374  100  ALA A CB  
1355  N N   . THR B 104  ? 0.5956 0.9351 0.6670 0.1262  -0.0095 0.1388  101  THR A N   
1356  C CA  . THR B 104  ? 0.6248 0.9900 0.6865 0.1554  -0.0084 0.1405  101  THR A CA  
1357  C C   . THR B 104  ? 0.6602 0.9938 0.7042 0.1758  -0.0083 0.1330  101  THR A C   
1358  O O   . THR B 104  ? 0.6892 1.0064 0.7138 0.2021  -0.0099 0.1307  101  THR A O   
1359  C CB  . THR B 104  ? 0.6128 1.0447 0.6880 0.1533  -0.0062 0.1484  101  THR A CB  
1360  O OG1 . THR B 104  ? 0.6079 1.0666 0.6963 0.1341  -0.0077 0.1557  101  THR A OG1 
1361  C CG2 . THR B 104  ? 0.6148 1.0789 0.6794 0.1864  -0.0047 0.1504  101  THR A CG2 
1362  N N   . TYR B 105  ? 0.6615 0.9833 0.7093 0.1645  -0.0071 0.1290  102  TYR A N   
1363  C CA  . TYR B 105  ? 0.6944 0.9849 0.7248 0.1823  -0.0075 0.1217  102  TYR A CA  
1364  C C   . TYR B 105  ? 0.7142 0.9410 0.7270 0.1842  -0.0116 0.1158  102  TYR A C   
1365  O O   . TYR B 105  ? 0.7457 0.9428 0.7353 0.2066  -0.0143 0.1111  102  TYR A O   
1366  C CB  . TYR B 105  ? 0.6902 0.9857 0.7301 0.1681  -0.0052 0.1194  102  TYR A CB  
1367  C CG  . TYR B 105  ? 0.6812 1.0314 0.7274 0.1778  -0.0018 0.1236  102  TYR A CG  
1368  C CD1 . TYR B 105  ? 0.6593 1.0615 0.7250 0.1606  0.0000  0.1321  102  TYR A CD1 
1369  C CD2 . TYR B 105  ? 0.6930 1.0430 0.7241 0.2038  -0.0009 0.1195  102  TYR A CD2 
1370  C CE1 . TYR B 105  ? 0.6579 1.1142 0.7295 0.1675  0.0028  0.1374  102  TYR A CE1 
1371  C CE2 . TYR B 105  ? 0.6957 1.1003 0.7328 0.2135  0.0025  0.1241  102  TYR A CE2 
1372  C CZ  . TYR B 105  ? 0.6685 1.1280 0.7268 0.1945  0.0045  0.1335  102  TYR A CZ  
1373  O OH  . TYR B 105  ? 0.6436 1.1615 0.7081 0.2021  0.0075  0.1394  102  TYR A OH  
1374  N N   . ARG B 106  ? 0.6902 0.8953 0.7117 0.1608  -0.0129 0.1162  103  ARG A N   
1375  C CA  . ARG B 106  ? 0.6992 0.8490 0.7049 0.1598  -0.0172 0.1124  103  ARG A CA  
1376  C C   . ARG B 106  ? 0.7355 0.8733 0.7226 0.1814  -0.0205 0.1139  103  ARG A C   
1377  O O   . ARG B 106  ? 0.7741 0.8657 0.7371 0.1930  -0.0251 0.1100  103  ARG A O   
1378  C CB  . ARG B 106  ? 0.6646 0.8026 0.6844 0.1320  -0.0174 0.1137  103  ARG A CB  
1379  C CG  . ARG B 106  ? 0.5988 0.7363 0.6312 0.1119  -0.0153 0.1110  103  ARG A CG  
1380  C CD  . ARG B 106  ? 0.5522 0.6679 0.5910 0.0899  -0.0165 0.1111  103  ARG A CD  
1381  N NE  . ARG B 106  ? 0.5622 0.6966 0.6103 0.0824  -0.0166 0.1165  103  ARG A NE  
1382  C CZ  . ARG B 106  ? 0.5588 0.7217 0.6222 0.0674  -0.0150 0.1197  103  ARG A CZ  
1383  N NH1 . ARG B 106  ? 0.5562 0.7317 0.6272 0.0578  -0.0132 0.1182  103  ARG A NH1 
1384  N NH2 . ARG B 106  ? 0.5438 0.7201 0.6128 0.0615  -0.0160 0.1243  103  ARG A NH2 
1385  N N   . ASN B 107  ? 0.7225 0.9002 0.7185 0.1867  -0.0188 0.1199  104  ASN A N   
1386  C CA  . ASN B 107  ? 0.7508 0.9211 0.7284 0.2098  -0.0217 0.1216  104  ASN A CA  
1387  C C   . ASN B 107  ? 0.7880 0.9588 0.7433 0.2426  -0.0226 0.1185  104  ASN A C   
1388  O O   . ASN B 107  ? 0.8434 0.9801 0.7714 0.2640  -0.0273 0.1164  104  ASN A O   
1389  C CB  . ASN B 107  ? 0.7601 0.9776 0.7539 0.2069  -0.0196 0.1291  104  ASN A CB  
1390  C CG  . ASN B 107  ? 0.7922 1.0004 0.8008 0.1796  -0.0202 0.1318  104  ASN A CG  
1391  O OD1 . ASN B 107  ? 0.8350 0.9971 0.8346 0.1715  -0.0233 0.1292  104  ASN A OD1 
1392  N ND2 . ASN B 107  ? 0.7686 1.0214 0.7985 0.1650  -0.0178 0.1373  104  ASN A ND2 
1393  N N   . ALA B 108  ? 0.7918 0.9998 0.7561 0.2476  -0.0187 0.1182  105  ALA A N   
1394  C CA  . ALA B 108  ? 0.8416 1.0519 0.7837 0.2804  -0.0193 0.1148  105  ALA A CA  
1395  C C   . ALA B 108  ? 0.8887 1.0312 0.8023 0.2884  -0.0248 0.1065  105  ALA A C   
1396  O O   . ALA B 108  ? 0.9451 1.0625 0.8273 0.3184  -0.0291 0.1031  105  ALA A O   
1397  C CB  . ALA B 108  ? 0.8129 1.0778 0.7723 0.2803  -0.0139 0.1167  105  ALA A CB  
1398  N N   . ILE B 109  ? 0.8545 0.9660 0.7762 0.2622  -0.0255 0.1034  106  ILE A N   
1399  C CA  . ILE B 109  ? 0.8648 0.9106 0.7598 0.2644  -0.0318 0.0968  106  ILE A CA  
1400  C C   . ILE B 109  ? 0.9396 0.9396 0.8147 0.2648  -0.0383 0.0978  106  ILE A C   
1401  O O   . ILE B 109  ? 0.9939 0.9426 0.8342 0.2811  -0.0456 0.0938  106  ILE A O   
1402  C CB  . ILE B 109  ? 0.7879 0.8204 0.6991 0.2355  -0.0303 0.0941  106  ILE A CB  
1403  C CG1 . ILE B 109  ? 0.7525 0.8343 0.6859 0.2319  -0.0236 0.0944  106  ILE A CG1 
1404  C CG2 . ILE B 109  ? 0.7920 0.7622 0.6751 0.2382  -0.0371 0.0875  106  ILE A CG2 
1405  C CD1 . ILE B 109  ? 0.7819 0.8697 0.6974 0.2601  -0.0236 0.0903  106  ILE A CD1 
1406  N N   . HIS B 110  ? 0.9331 0.9490 0.8278 0.2465  -0.0365 0.1034  107  HIS A N   
1407  C CA  . HIS B 110  ? 0.9680 0.9441 0.8462 0.2443  -0.0423 0.1055  107  HIS A CA  
1408  C C   . HIS B 110  ? 1.0302 0.9972 0.8793 0.2776  -0.0464 0.1058  107  HIS A C   
1409  O O   . HIS B 110  ? 1.0838 0.9978 0.9032 0.2839  -0.0541 0.1050  107  HIS A O   
1410  C CB  . HIS B 110  ? 0.9266 0.9291 0.8331 0.2201  -0.0388 0.1115  107  HIS A CB  
1411  C CG  . HIS B 110  ? 0.9472 0.9106 0.8407 0.2125  -0.0442 0.1142  107  HIS A CG  
1412  N ND1 . HIS B 110  ? 0.9668 0.8828 0.8505 0.1943  -0.0490 0.1129  107  HIS A ND1 
1413  C CD2 . HIS B 110  ? 0.9576 0.9248 0.8465 0.2197  -0.0457 0.1189  107  HIS A CD2 
1414  C CE1 . HIS B 110  ? 0.9852 0.8775 0.8586 0.1901  -0.0534 0.1170  107  HIS A CE1 
1415  N NE2 . HIS B 110  ? 0.9830 0.9041 0.8590 0.2058  -0.0514 0.1203  107  HIS A NE2 
1416  N N   . ASP B 111  ? 1.0335 1.0519 0.8890 0.2993  -0.0418 0.1075  108  ASP A N   
1417  C CA  . ASP B 111  ? 1.0775 1.0929 0.9048 0.3346  -0.0452 0.1078  108  ASP A CA  
1418  C C   . ASP B 111  ? 1.1552 1.1179 0.9401 0.3607  -0.0523 0.1007  108  ASP A C   
1419  O O   . ASP B 111  ? 1.2007 1.1356 0.9513 0.3884  -0.0583 0.0998  108  ASP A O   
1420  C CB  . ASP B 111  ? 1.0521 1.1431 0.8980 0.3509  -0.0383 0.1122  108  ASP A CB  
1421  C CG  . ASP B 111  ? 1.0187 1.1567 0.8990 0.3284  -0.0334 0.1199  108  ASP A CG  
1422  O OD1 . ASP B 111  ? 1.0173 1.1271 0.8997 0.3106  -0.0360 0.1218  108  ASP A OD1 
1423  O OD2 . ASP B 111  ? 0.9980 1.2015 0.9020 0.3282  -0.0274 0.1244  108  ASP A OD2 
1424  N N   . TYR B 112  ? 1.1622 1.1087 0.9462 0.3533  -0.0524 0.0954  109  TYR A N   
1425  C CA  . TYR B 112  ? 1.1892 1.0756 0.9300 0.3738  -0.0608 0.0882  109  TYR A CA  
1426  C C   . TYR B 112  ? 1.1896 1.0013 0.9037 0.3598  -0.0708 0.0876  109  TYR A C   
1427  O O   . TYR B 112  ? 1.2329 0.9886 0.9013 0.3819  -0.0805 0.0839  109  TYR A O   
1428  C CB  . TYR B 112  ? 1.1621 1.0524 0.9106 0.3672  -0.0582 0.0830  109  TYR A CB  
1429  C CG  . TYR B 112  ? 1.1609 1.1040 0.9130 0.3949  -0.0525 0.0817  109  TYR A CG  
1430  C CD1 . TYR B 112  ? 1.1146 1.1349 0.9067 0.3868  -0.0425 0.0874  109  TYR A CD1 
1431  C CD2 . TYR B 112  ? 1.2188 1.1345 0.9324 0.4289  -0.0576 0.0752  109  TYR A CD2 
1432  C CE1 . TYR B 112  ? 1.1085 1.1818 0.9043 0.4105  -0.0374 0.0877  109  TYR A CE1 
1433  C CE2 . TYR B 112  ? 1.2164 1.1847 0.9331 0.4554  -0.0520 0.0745  109  TYR A CE2 
1434  C CZ  . TYR B 112  ? 1.1552 1.2045 0.9142 0.4454  -0.0417 0.0812  109  TYR A CZ  
1435  O OH  . TYR B 112  ? 1.1427 1.2489 0.9052 0.4702  -0.0363 0.0819  109  TYR A OH  
1436  N N   . PHE B 113  ? 1.1451 0.9549 0.8849 0.3234  -0.0692 0.0916  110  PHE A N   
1437  C CA  . PHE B 113  ? 1.1256 0.8717 0.8431 0.3066  -0.0785 0.0929  110  PHE A CA  
1438  C C   . PHE B 113  ? 1.1320 0.8630 0.8298 0.3206  -0.0830 0.0972  110  PHE A C   
1439  O O   . PHE B 113  ? 1.1627 0.8316 0.8165 0.3330  -0.0939 0.0957  110  PHE A O   
1440  C CB  . PHE B 113  ? 1.0778 0.8344 0.8298 0.2656  -0.0747 0.0964  110  PHE A CB  
1441  C CG  . PHE B 113  ? 1.0563 0.8158 0.8221 0.2500  -0.0720 0.0921  110  PHE A CG  
1442  C CD1 . PHE B 113  ? 1.0992 0.8152 0.8338 0.2611  -0.0787 0.0859  110  PHE A CD1 
1443  C CD2 . PHE B 113  ? 1.0086 0.8123 0.8163 0.2249  -0.0635 0.0941  110  PHE A CD2 
1444  C CE1 . PHE B 113  ? 1.0768 0.7963 0.8241 0.2470  -0.0763 0.0820  110  PHE A CE1 
1445  C CE2 . PHE B 113  ? 0.9892 0.7952 0.8083 0.2116  -0.0612 0.0902  110  PHE A CE2 
1446  C CZ  . PHE B 113  ? 1.0242 0.7896 0.8144 0.2224  -0.0673 0.0842  110  PHE A CZ  
1447  N N   . ILE B 114  ? 1.1035 0.8886 0.8313 0.3183  -0.0755 0.1027  111  ILE A N   
1448  C CA  . ILE B 114  ? 1.1085 0.8836 0.8219 0.3288  -0.0791 0.1074  111  ILE A CA  
1449  C C   . ILE B 114  ? 1.1287 0.9111 0.8140 0.3721  -0.0809 0.1055  111  ILE A C   
1450  O O   . ILE B 114  ? 1.1486 0.9062 0.8084 0.3873  -0.0865 0.1079  111  ILE A O   
1451  C CB  . ILE B 114  ? 1.0167 0.8455 0.7725 0.3079  -0.0710 0.1142  111  ILE A CB  
1452  C CG1 . ILE B 114  ? 0.9552 0.8595 0.7418 0.3180  -0.0611 0.1150  111  ILE A CG1 
1453  C CG2 . ILE B 114  ? 0.9598 0.7816 0.7405 0.2681  -0.0695 0.1159  111  ILE A CG2 
1454  C CD1 . ILE B 114  ? 0.8953 0.8508 0.7196 0.2985  -0.0544 0.1216  111  ILE A CD1 
1455  N N   . GLY B 115  ? 1.1277 0.9449 0.8159 0.3934  -0.0763 0.1015  112  GLY A N   
1456  C CA  . GLY B 115  ? 1.1636 0.9938 0.8249 0.4373  -0.0776 0.0997  112  GLY A CA  
1457  C C   . GLY B 115  ? 1.1719 1.0759 0.8608 0.4468  -0.0694 0.1061  112  GLY A C   
1458  O O   . GLY B 115  ? 1.2119 1.1098 0.8808 0.4677  -0.0728 0.1086  112  GLY A O   
1459  N N   . ARG B 116  ? 1.1653 1.1387 0.8984 0.4312  -0.0594 0.1090  113  ARG A N   
1460  C CA  . ARG B 116  ? 1.1672 1.2174 0.9279 0.4379  -0.0519 0.1157  113  ARG A CA  
1461  C C   . ARG B 116  ? 1.1494 1.2664 0.9372 0.4388  -0.0437 0.1164  113  ARG A C   
1462  O O   . ARG B 116  ? 1.1030 1.2840 0.9284 0.4215  -0.0367 0.1228  113  ARG A O   
1463  C CB  . ARG B 116  ? 1.1466 1.2129 0.9390 0.4045  -0.0491 0.1222  113  ARG A CB  
1464  C CG  . ARG B 116  ? 1.1957 1.2233 0.9658 0.4107  -0.0553 0.1246  113  ARG A CG  
1465  C CD  . ARG B 116  ? 1.1890 1.2580 0.9935 0.3875  -0.0507 0.1321  113  ARG A CD  
1466  N NE  . ARG B 116  ? 1.2571 1.2857 1.0427 0.3882  -0.0565 0.1347  113  ARG A NE  
1467  C CZ  . ARG B 116  ? 1.3319 1.3663 1.0971 0.4170  -0.0589 0.1371  113  ARG A CZ  
1468  N NH1 . ARG B 116  ? 1.3540 1.4362 1.1152 0.4486  -0.0558 0.1374  113  ARG A NH1 
1469  N NH2 . ARG B 116  ? 1.3649 1.3592 1.1130 0.4146  -0.0645 0.1396  113  ARG A NH2 
1470  N N   . THR B 117  ? 1.1917 1.2937 0.9592 0.4581  -0.0452 0.1101  114  THR A N   
1471  C CA  . THR B 117  ? 1.1945 1.3576 0.9833 0.4619  -0.0380 0.1108  114  THR A CA  
1472  C C   . THR B 117  ? 1.2414 1.4395 1.0071 0.5085  -0.0376 0.1108  114  THR A C   
1473  O O   . THR B 117  ? 1.2761 1.4246 0.9978 0.5386  -0.0441 0.1046  114  THR A O   
1474  C CB  . THR B 117  ? 1.2184 1.3461 1.0042 0.4490  -0.0390 0.1040  114  THR A CB  
1475  O OG1 . THR B 117  ? 1.2080 1.3942 1.0094 0.4579  -0.0326 0.1046  114  THR A OG1 
1476  C CG2 . THR B 117  ? 1.2855 1.3329 1.0215 0.4716  -0.0488 0.0956  114  THR A CG2 
1477  N N   . ASP B 118  ? 1.2422 1.5256 1.0363 0.5114  -0.0297 0.1172  115  ASP A N   
1478  C CA  . ASP B 118  ? 1.2913 1.6149 1.0673 0.5420  -0.0247 0.1144  115  ASP A CA  
1479  C C   . ASP B 118  ? 1.3238 1.6287 1.0740 0.5609  -0.0241 0.1049  115  ASP A C   
1480  O O   . ASP B 118  ? 1.3450 1.6745 1.0728 0.5870  -0.0198 0.1006  115  ASP A O   
1481  C CB  . ASP B 118  ? 1.2423 1.6629 1.0564 0.5306  -0.0155 0.1243  115  ASP A CB  
1482  C CG  . ASP B 118  ? 1.2147 1.6579 1.0513 0.5137  -0.0160 0.1332  115  ASP A CG  
1483  O OD1 . ASP B 118  ? 1.2380 1.6321 1.0523 0.5227  -0.0213 0.1308  115  ASP A OD1 
1484  O OD2 . ASP B 118  ? 1.1724 1.6809 1.0474 0.4902  -0.0114 0.1428  115  ASP A OD2 
1485  N N   . ASN B 119  ? 1.3431 1.6057 1.0942 0.5491  -0.0284 0.1016  116  ASN A N   
1486  C CA  . ASN B 119  ? 1.4084 1.6540 1.1368 0.5650  -0.0281 0.0927  116  ASN A CA  
1487  C C   . ASN B 119  ? 1.4996 1.6641 1.1720 0.5895  -0.0362 0.0809  116  ASN A C   
1488  O O   . ASN B 119  ? 1.5375 1.6925 1.1825 0.6099  -0.0356 0.0726  116  ASN A O   
1489  C CB  . ASN B 119  ? 1.4087 1.6425 1.1604 0.5418  -0.0295 0.0939  116  ASN A CB  
1490  C CG  . ASN B 119  ? 1.3717 1.6773 1.1760 0.5091  -0.0216 0.1037  116  ASN A CG  
1491  O OD1 . ASN B 119  ? 1.3634 1.7454 1.1866 0.5158  -0.0156 0.1115  116  ASN A OD1 
1492  N ND2 . ASN B 119  ? 1.3420 1.6209 1.1682 0.4688  -0.0211 0.1025  116  ASN A ND2 
1493  N N   . LEU B 120  ? 1.5302 1.6358 1.1830 0.5870  -0.0440 0.0801  117  LEU A N   
1494  C CA  . LEU B 120  ? 1.5877 1.6102 1.1853 0.6055  -0.0533 0.0695  117  LEU A CA  
1495  C C   . LEU B 120  ? 1.6171 1.6405 1.1899 0.6265  -0.0536 0.0685  117  LEU A C   
1496  O O   . LEU B 120  ? 1.5594 1.6248 1.1587 0.6185  -0.0496 0.0770  117  LEU A O   
1497  C CB  . LEU B 120  ? 1.5878 1.5293 1.1762 0.5826  -0.0640 0.0691  117  LEU A CB  
1498  C CG  . LEU B 120  ? 1.5521 1.4779 1.1556 0.5638  -0.0653 0.0684  117  LEU A CG  
1499  C CD1 . LEU B 120  ? 1.5606 1.4051 1.1500 0.5410  -0.0761 0.0685  117  LEU A CD1 
1500  C CD2 . LEU B 120  ? 1.5859 1.5042 1.1625 0.5847  -0.0648 0.0581  117  LEU A CD2 
1501  N N   . THR B 121  ? 1.6984 1.6738 1.2180 0.6536  -0.0587 0.0578  118  THR A N   
1502  C CA  . THR B 121  ? 1.7267 1.6982 1.2156 0.6777  -0.0594 0.0553  118  THR A CA  
1503  C C   . THR B 121  ? 1.7263 1.6360 1.2036 0.6637  -0.0685 0.0575  118  THR A C   
1504  O O   . THR B 121  ? 1.7308 1.5860 1.2112 0.6390  -0.0761 0.0588  118  THR A O   
1505  C CB  . THR B 121  ? 1.7717 1.7077 1.2029 0.7117  -0.0629 0.0426  118  THR A CB  
1506  O OG1 . THR B 121  ? 1.7853 1.6376 1.1860 0.7042  -0.0740 0.0349  118  THR A OG1 
1507  C CG2 . THR B 121  ? 1.7518 1.7624 1.1926 0.7300  -0.0522 0.0419  118  THR A CG2 
1508  N N   . ASP B 122  ? 1.7368 1.6560 1.1989 0.6802  -0.0676 0.0581  119  ASP A N   
1509  C CA  . ASP B 122  ? 1.7467 1.6197 1.2025 0.6668  -0.0749 0.0619  119  ASP A CA  
1510  C C   . ASP B 122  ? 1.8049 1.5737 1.2135 0.6622  -0.0889 0.0545  119  ASP A C   
1511  O O   . ASP B 122  ? 1.7675 1.4914 1.1813 0.6364  -0.0960 0.0595  119  ASP A O   
1512  C CB  . ASP B 122  ? 1.7763 1.6781 1.2191 0.6895  -0.0712 0.0625  119  ASP A CB  
1513  C CG  . ASP B 122  ? 1.7344 1.7409 1.2175 0.6953  -0.0576 0.0694  119  ASP A CG  
1514  O OD1 . ASP B 122  ? 1.7157 1.7685 1.2180 0.6956  -0.0510 0.0695  119  ASP A OD1 
1515  O OD2 . ASP B 122  ? 1.7147 1.7577 1.2098 0.6983  -0.0537 0.0751  119  ASP A OD2 
1516  N N   . ALA B 123  ? 1.8858 1.6158 1.2462 0.6859  -0.0935 0.0429  120  ALA A N   
1517  C CA  . ALA B 123  ? 1.9424 1.5728 1.2539 0.6802  -0.1080 0.0356  120  ALA A CA  
1518  C C   . ALA B 123  ? 1.9047 1.5038 1.2377 0.6457  -0.1126 0.0390  120  ALA A C   
1519  O O   . ALA B 123  ? 1.9398 1.4742 1.2598 0.6222  -0.1228 0.0411  120  ALA A O   
1520  C CB  . ALA B 123  ? 1.9975 1.5983 1.2533 0.7130  -0.1119 0.0223  120  ALA A CB  
1521  N N   . ILE B 124  ? 1.8295 1.4754 1.1949 0.6415  -0.1051 0.0399  121  ILE A N   
1522  C CA  . ILE B 124  ? 1.7621 1.3848 1.1503 0.6098  -0.1083 0.0433  121  ILE A CA  
1523  C C   . ILE B 124  ? 1.6710 1.3239 1.1088 0.5807  -0.1045 0.0562  121  ILE A C   
1524  O O   . ILE B 124  ? 1.6671 1.2760 1.1104 0.5514  -0.1111 0.0604  121  ILE A O   
1525  C CB  . ILE B 124  ? 1.7638 1.4264 1.1684 0.6162  -0.1015 0.0398  121  ILE A CB  
1526  C CG1 . ILE B 124  ? 1.8429 1.4782 1.1953 0.6477  -0.1051 0.0270  121  ILE A CG1 
1527  C CG2 . ILE B 124  ? 1.7485 1.3828 1.1725 0.5849  -0.1053 0.0423  121  ILE A CG2 
1528  C CD1 . ILE B 124  ? 1.8313 1.5092 1.1973 0.6567  -0.0980 0.0235  121  ILE A CD1 
1529  N N   . ASN B 125  ? 1.5676 1.2967 1.0403 0.5877  -0.0942 0.0630  122  ASN A N   
1530  C CA  . ASN B 125  ? 1.4761 1.2409 0.9965 0.5614  -0.0903 0.0753  122  ASN A CA  
1531  C C   . ASN B 125  ? 1.4778 1.1872 0.9824 0.5463  -0.0989 0.0795  122  ASN A C   
1532  O O   . ASN B 125  ? 1.4772 1.1749 1.0049 0.5171  -0.1010 0.0876  122  ASN A O   
1533  C CB  . ASN B 125  ? 1.4376 1.2974 0.9950 0.5721  -0.0782 0.0812  122  ASN A CB  
1534  C CG  . ASN B 125  ? 1.3949 1.2996 1.0035 0.5447  -0.0737 0.0935  122  ASN A CG  
1535  O OD1 . ASN B 125  ? 1.3503 1.2909 0.9940 0.5276  -0.0688 0.0970  122  ASN A OD1 
1536  N ND2 . ASN B 125  ? 1.4058 1.3091 1.0183 0.5389  -0.0752 0.0996  122  ASN A ND2 
1537  N N   . LYS B 126  ? 1.4958 1.1708 0.9596 0.5658  -0.1039 0.0743  123  LYS A N   
1538  C CA  . LYS B 126  ? 1.4829 1.1059 0.9298 0.5516  -0.1122 0.0785  123  LYS A CA  
1539  C C   . LYS B 126  ? 1.5142 1.0485 0.9284 0.5307  -0.1250 0.0756  123  LYS A C   
1540  O O   . LYS B 126  ? 1.4610 0.9586 0.8750 0.5058  -0.1313 0.0824  123  LYS A O   
1541  C CB  . LYS B 126  ? 1.5177 1.1349 0.9310 0.5797  -0.1133 0.0740  123  LYS A CB  
1542  N N   . ARG B 127  ? 1.5787 1.0797 0.9648 0.5388  -0.1293 0.0660  124  ARG A N   
1543  C CA  . ARG B 127  ? 1.6099 1.0290 0.9642 0.5168  -0.1420 0.0633  124  ARG A CA  
1544  C C   . ARG B 127  ? 1.5687 0.9888 0.9597 0.4793  -0.1417 0.0724  124  ARG A C   
1545  O O   . ARG B 127  ? 1.6094 0.9707 0.9841 0.4518  -0.1516 0.0755  124  ARG A O   
1546  C CB  . ARG B 127  ? 1.6227 1.0121 0.9405 0.5345  -0.1461 0.0509  124  ARG A CB  
1547  N N   . HIS B 128  ? 1.4986 0.9860 0.9377 0.4769  -0.1307 0.0770  125  HIS A N   
1548  C CA  . HIS B 128  ? 1.4506 0.9454 0.9263 0.4405  -0.1288 0.0846  125  HIS A CA  
1549  C C   . HIS B 128  ? 1.4513 0.9574 0.9513 0.4132  -0.1268 0.0934  125  HIS A C   
1550  O O   . HIS B 128  ? 1.4257 0.9124 0.9401 0.3749  -0.1286 0.0970  125  HIS A O   
1551  C CB  . HIS B 128  ? 1.4235 0.9984 0.9501 0.4361  -0.1144 0.0833  125  HIS A CB  
1552  C CG  . HIS B 128  ? 1.4958 1.0615 1.0047 0.4550  -0.1156 0.0752  125  HIS A CG  
1553  N ND1 . HIS B 128  ? 1.4723 1.1076 1.0115 0.4677  -0.1044 0.0733  125  HIS A ND1 
1554  C CD2 . HIS B 128  ? 1.5663 1.0618 1.0297 0.4619  -0.1271 0.0686  125  HIS A CD2 
1555  C CE1 . HIS B 128  ? 1.4933 1.1025 1.0070 0.4837  -0.1084 0.0659  125  HIS A CE1 
1556  N NE2 . HIS B 128  ? 1.5500 1.0756 1.0187 0.4786  -0.1216 0.0619  125  HIS A NE2 
1557  N N   . ALA B 129  ? 1.4833 1.0231 0.9881 0.4330  -0.1230 0.0971  126  ALA A N   
1558  C CA  . ALA B 129  ? 1.4756 1.0279 1.0029 0.4093  -0.1209 0.1053  126  ALA A CA  
1559  C C   . ALA B 129  ? 1.5426 1.0124 1.0275 0.3972  -0.1351 0.1082  126  ALA A C   
1560  O O   . ALA B 129  ? 1.5034 0.9694 1.0078 0.3627  -0.1350 0.1147  126  ALA A O   
1561  C CB  . ALA B 129  ? 1.4578 1.0641 0.9965 0.4354  -0.1144 0.1085  126  ALA A CB  
1562  N N   . GLU B 130  ? 1.6452 1.0547 1.0753 0.4203  -0.1459 0.1018  127  GLU A N   
1563  C CA  . GLU B 130  ? 1.7363 1.0708 1.1273 0.4019  -0.1587 0.1024  127  GLU A CA  
1564  C C   . GLU B 130  ? 1.7645 1.0580 1.1546 0.3656  -0.1656 0.1054  127  GLU A C   
1565  O O   . GLU B 130  ? 1.7863 1.0327 1.1589 0.3391  -0.1747 0.1106  127  GLU A O   
1566  C CB  . GLU B 130  ? 1.8144 1.1038 1.1517 0.4284  -0.1662 0.0906  127  GLU A CB  
1567  N N   . ILE B 131  ? 1.7845 1.0978 1.1936 0.3630  -0.1613 0.1027  128  ILE A N   
1568  C CA  . ILE B 131  ? 1.7652 1.0538 1.1821 0.3251  -0.1650 0.1041  128  ILE A CA  
1569  C C   . ILE B 131  ? 1.6630 1.0133 1.1419 0.2884  -0.1528 0.1103  128  ILE A C   
1570  O O   . ILE B 131  ? 1.6637 0.9925 1.1470 0.2530  -0.1572 0.1165  128  ILE A O   
1571  C CB  . ILE B 131  ? 1.7904 1.0741 1.1993 0.3369  -0.1650 0.0951  128  ILE A CB  
1572  C CG1 . ILE B 131  ? 1.8721 1.1110 1.2282 0.3656  -0.1731 0.0838  128  ILE A CG1 
1573  C CG2 . ILE B 131  ? 1.7854 1.0480 1.2039 0.2971  -0.1684 0.0963  128  ILE A CG2 
1574  C CD1 . ILE B 131  ? 1.8866 1.1252 1.2341 0.3795  -0.1723 0.0737  128  ILE A CD1 
1575  N N   . TYR B 132  ? 1.5404 0.9682 1.0660 0.2964  -0.1379 0.1093  129  TYR A N   
1576  C CA  . TYR B 132  ? 1.4126 0.8975 0.9941 0.2644  -0.1267 0.1143  129  TYR A CA  
1577  C C   . TYR B 132  ? 1.3576 0.8407 0.9450 0.2479  -0.1281 0.1231  129  TYR A C   
1578  O O   . TYR B 132  ? 1.3217 0.8292 0.9427 0.2157  -0.1233 0.1281  129  TYR A O   
1579  C CB  . TYR B 132  ? 1.3444 0.9078 0.9682 0.2779  -0.1123 0.1116  129  TYR A CB  
1580  C CG  . TYR B 132  ? 1.2628 0.8810 0.9405 0.2464  -0.1015 0.1149  129  TYR A CG  
1581  C CD1 . TYR B 132  ? 1.2228 0.8522 0.9203 0.2284  -0.0978 0.1115  129  TYR A CD1 
1582  C CD2 . TYR B 132  ? 1.2246 0.8817 0.9310 0.2360  -0.0955 0.1211  129  TYR A CD2 
1583  C CE1 . TYR B 132  ? 1.1780 0.8540 0.9205 0.2019  -0.0887 0.1141  129  TYR A CE1 
1584  C CE2 . TYR B 132  ? 1.1672 0.8700 0.9180 0.2092  -0.0866 0.1236  129  TYR A CE2 
1585  C CZ  . TYR B 132  ? 1.1524 0.8637 0.9202 0.1928  -0.0834 0.1200  129  TYR A CZ  
1586  O OH  . TYR B 132  ? 1.0981 0.8516 0.9062 0.1684  -0.0753 0.1222  129  TYR A OH  
1587  N N   . LYS B 133  ? 1.3851 0.8398 0.9392 0.2705  -0.1347 0.1250  130  LYS A N   
1588  C CA  . LYS B 133  ? 1.3802 0.8299 0.9367 0.2557  -0.1367 0.1336  130  LYS A CA  
1589  C C   . LYS B 133  ? 1.4174 0.8133 0.9554 0.2219  -0.1471 0.1394  130  LYS A C   
1590  O O   . LYS B 133  ? 1.3920 0.8117 0.9603 0.1912  -0.1431 0.1462  130  LYS A O   
1591  C CB  . LYS B 133  ? 1.4246 0.8513 0.9447 0.2898  -0.1424 0.1341  130  LYS A CB  
1592  N N   . GLY B 134  ? 1.4684 0.7925 0.9553 0.2269  -0.1611 0.1372  131  GLY A N   
1593  C CA  . GLY B 134  ? 1.4920 0.7635 0.9574 0.1933  -0.1726 0.1435  131  GLY A CA  
1594  C C   . GLY B 134  ? 1.4416 0.7172 0.9227 0.1695  -0.1715 0.1409  131  GLY A C   
1595  O O   . GLY B 134  ? 1.4719 0.6904 0.9196 0.1515  -0.1843 0.1430  131  GLY A O   
1596  N N   . LEU B 135  ? 1.3671 0.7096 0.8977 0.1685  -0.1569 0.1366  132  LEU A N   
1597  C CA  . LEU B 135  ? 1.3219 0.6750 0.8709 0.1487  -0.1543 0.1334  132  LEU A CA  
1598  C C   . LEU B 135  ? 1.2680 0.6523 0.8539 0.1092  -0.1496 0.1410  132  LEU A C   
1599  O O   . LEU B 135  ? 1.2136 0.6003 0.8101 0.0889  -0.1495 0.1399  132  LEU A O   
1600  C CB  . LEU B 135  ? 1.2530 0.6590 0.8319 0.1699  -0.1419 0.1246  132  LEU A CB  
1601  C CG  . LEU B 135  ? 1.2290 0.6311 0.8107 0.1636  -0.1416 0.1182  132  LEU A CG  
1602  C CD1 . LEU B 135  ? 1.2840 0.6106 0.8076 0.1766  -0.1568 0.1141  132  LEU A CD1 
1603  C CD2 . LEU B 135  ? 1.1899 0.6523 0.8055 0.1828  -0.1283 0.1113  132  LEU A CD2 
1604  N N   . PHE B 136  ? 1.3090 0.7179 0.9135 0.0992  -0.1459 0.1485  133  PHE A N   
1605  C CA  . PHE B 136  ? 1.2958 0.7406 0.9360 0.0657  -0.1405 0.1556  133  PHE A CA  
1606  C C   . PHE B 136  ? 1.3352 0.7540 0.9584 0.0474  -0.1486 0.1668  133  PHE A C   
1607  O O   . PHE B 136  ? 1.2894 0.7482 0.9436 0.0302  -0.1420 0.1732  133  PHE A O   
1608  C CB  . PHE B 136  ? 1.2509 0.7695 0.9424 0.0700  -0.1245 0.1534  133  PHE A CB  
1609  C CG  . PHE B 136  ? 1.2559 0.8031 0.9640 0.0885  -0.1166 0.1435  133  PHE A CG  
1610  C CD1 . PHE B 136  ? 1.2595 0.8206 0.9851 0.0739  -0.1132 0.1400  133  PHE A CD1 
1611  C CD2 . PHE B 136  ? 1.2634 0.8257 0.9691 0.1204  -0.1126 0.1384  133  PHE A CD2 
1612  C CE1 . PHE B 136  ? 1.2453 0.8325 0.9853 0.0901  -0.1061 0.1316  133  PHE A CE1 
1613  C CE2 . PHE B 136  ? 1.2523 0.8443 0.9731 0.1363  -0.1054 0.1306  133  PHE A CE2 
1614  C CZ  . PHE B 136  ? 1.2439 0.8470 0.9816 0.1207  -0.1022 0.1271  133  PHE A CZ  
1615  N N   . LYS B 137  ? 1.3810 0.7318 0.9528 0.0511  -0.1634 0.1694  134  LYS A N   
1616  C CA  . LYS B 137  ? 1.4182 0.7375 0.9682 0.0310  -0.1731 0.1810  134  LYS A CA  
1617  C C   . LYS B 137  ? 1.5000 0.7372 0.9912 0.0248  -0.1917 0.1830  134  LYS A C   
1618  O O   . LYS B 137  ? 1.5289 0.7423 1.0049 0.0275  -0.1959 0.1764  134  LYS A O   
1619  C CB  . LYS B 137  ? 1.4138 0.7453 0.9649 0.0509  -0.1697 0.1833  134  LYS A CB  
1620  C CG  . LYS B 137  ? 1.4006 0.7278 0.9376 0.0929  -0.1674 0.1737  134  LYS A CG  
1621  C CD  . LYS B 137  ? 1.3481 0.7008 0.8950 0.1089  -0.1622 0.1768  134  LYS A CD  
1622  C CE  . LYS B 137  ? 1.3351 0.6954 0.8725 0.1511  -0.1587 0.1681  134  LYS A CE  
1623  N NZ  . LYS B 137  ? 1.3145 0.7049 0.8638 0.1658  -0.1533 0.1716  134  LYS A NZ  
1624  N N   . ALA B 138  ? 1.5500 0.7415 1.0057 0.0162  -0.2037 0.1922  135  ALA A N   
1625  C CA  . ALA B 138  ? 1.6782 0.8050 1.0861 0.0010  -0.2198 0.1927  135  ALA A CA  
1626  C C   . ALA B 138  ? 1.9382 1.0199 1.3066 0.0316  -0.2261 0.1785  135  ALA A C   
1627  O O   . ALA B 138  ? 2.1817 1.2170 1.5141 0.0194  -0.2383 0.1747  135  ALA A O   
1628  C CB  . ALA B 138  ? 1.9733 1.0817 1.3634 -0.0135 -0.2268 0.2006  135  ALA A CB  
1629  N N   . GLU B 139  ? 1.8948 0.9912 1.2679 0.0710  -0.2186 0.1706  136  GLU A N   
1630  C CA  . GLU B 139  ? 1.9788 1.0380 1.3144 0.1025  -0.2238 0.1568  136  GLU A CA  
1631  C C   . GLU B 139  ? 1.9852 1.0333 1.3168 0.0972  -0.2259 0.1496  136  GLU A C   
1632  O O   . GLU B 139  ? 2.0386 1.0493 1.3335 0.1179  -0.2325 0.1382  136  GLU A O   
1633  C CB  . GLU B 139  ? 1.9945 1.0830 1.3396 0.1463  -0.2141 0.1509  136  GLU A CB  
1634  C CG  . GLU B 139  ? 2.0304 1.1267 1.3741 0.1564  -0.2127 0.1563  136  GLU A CG  
1635  C CD  . GLU B 139  ? 2.0547 1.1748 1.3983 0.2021  -0.2053 0.1487  136  GLU A CD  
1636  O OE1 . GLU B 139  ? 2.0835 1.1974 1.4122 0.2281  -0.2048 0.1373  136  GLU A OE1 
1637  O OE2 . GLU B 139  ? 2.0406 1.1890 1.3994 0.2119  -0.1998 0.1541  136  GLU A OE2 
1638  N N   . LEU B 140  ? 1.8731 0.9531 1.2402 0.0710  -0.2207 0.1557  137  LEU A N   
1639  C CA  . LEU B 140  ? 1.8105 0.8777 1.1726 0.0610  -0.2239 0.1498  137  LEU A CA  
1640  C C   . LEU B 140  ? 1.8697 0.8817 1.1891 0.0385  -0.2397 0.1484  137  LEU A C   
1641  O O   . LEU B 140  ? 1.9332 0.9131 1.2253 0.0452  -0.2465 0.1389  137  LEU A O   
1642  C CB  . LEU B 140  ? 1.6946 0.8090 1.1033 0.0339  -0.2154 0.1576  137  LEU A CB  
1643  C CG  . LEU B 140  ? 1.5783 0.7742 1.0453 0.0503  -0.1949 0.1505  137  LEU A CG  
1644  C CD1 . LEU B 140  ? 1.5008 0.7532 1.0175 0.0173  -0.1854 0.1553  137  LEU A CD1 
1645  C CD2 . LEU B 140  ? 1.5620 0.7546 1.0211 0.0808  -0.1922 0.1377  137  LEU A CD2 
1646  N N   . PHE B 141  ? 1.8668 0.8684 1.1790 0.0115  -0.2462 0.1581  138  PHE A N   
1647  C CA  . PHE B 141  ? 1.9286 0.8838 1.2032 -0.0161 -0.2620 0.1592  138  PHE A CA  
1648  C C   . PHE B 141  ? 2.0341 0.9288 1.2520 0.0053  -0.2745 0.1509  138  PHE A C   
1649  O O   . PHE B 141  ? 2.0783 0.9258 1.2559 -0.0121 -0.2896 0.1491  138  PHE A O   
1650  C CB  . PHE B 141  ? 1.9153 0.8916 1.2084 -0.0557 -0.2636 0.1741  138  PHE A CB  
1651  C CG  . PHE B 141  ? 1.8475 0.8860 1.1949 -0.0769 -0.2514 0.1827  138  PHE A CG  
1652  C CD1 . PHE B 141  ? 1.7876 0.8740 1.1747 -0.0630 -0.2371 0.1868  138  PHE A CD1 
1653  C CD2 . PHE B 141  ? 1.8363 0.8863 1.1936 -0.1105 -0.2548 0.1868  138  PHE A CD2 
1654  C CE1 . PHE B 141  ? 1.7094 0.8509 1.1431 -0.0819 -0.2266 0.1943  138  PHE A CE1 
1655  C CE2 . PHE B 141  ? 1.7625 0.8712 1.1684 -0.1286 -0.2435 0.1942  138  PHE A CE2 
1656  C CZ  . PHE B 141  ? 1.6957 0.8488 1.1389 -0.1142 -0.2295 0.1978  138  PHE A CZ  
1657  N N   . ASN B 142  ? 2.0808 0.9769 1.2931 0.0424  -0.2690 0.1459  139  ASN A N   
1658  C CA  . ASN B 142  ? 2.1742 1.0149 1.3314 0.0667  -0.2800 0.1369  139  ASN A CA  
1659  C C   . ASN B 142  ? 2.2295 1.0311 1.3494 0.0832  -0.2878 0.1234  139  ASN A C   
1660  O O   . ASN B 142  ? 2.2882 1.0333 1.3532 0.0947  -0.3011 0.1161  139  ASN A O   
1661  C CB  . ASN B 142  ? 2.1642 1.0252 1.3282 0.1064  -0.2704 0.1337  139  ASN A CB  
1662  C CG  . ASN B 142  ? 2.1191 1.0184 1.3181 0.0935  -0.2627 0.1465  139  ASN A CG  
1663  O OD1 . ASN B 142  ? 2.0903 1.0021 1.3085 0.0552  -0.2641 0.1579  139  ASN A OD1 
1664  N ND2 . ASN B 142  ? 2.1083 1.0301 1.3161 0.1258  -0.2542 0.1448  139  ASN A ND2 
1665  N N   . GLY B 143  ? 2.2117 1.0409 1.3580 0.0848  -0.2803 0.1200  140  GLY A N   
1666  C CA  . GLY B 143  ? 2.2662 1.0703 1.3837 0.1115  -0.2837 0.1061  140  GLY A CA  
1667  C C   . GLY B 143  ? 2.2854 1.1021 1.3977 0.1611  -0.2753 0.0964  140  GLY A C   
1668  O O   . GLY B 143  ? 2.3136 1.1161 1.4035 0.1875  -0.2765 0.0844  140  GLY A O   
1669  N N   . LYS B 144  ? 2.2737 1.1198 1.4061 0.1747  -0.2669 0.1014  141  LYS A N   
1670  C CA  . LYS B 144  ? 2.2810 1.1475 1.4111 0.2216  -0.2584 0.0931  141  LYS A CA  
1671  C C   . LYS B 144  ? 2.2392 1.1576 1.4072 0.2408  -0.2447 0.0888  141  LYS A C   
1672  O O   . LYS B 144  ? 2.2673 1.1839 1.4162 0.2749  -0.2432 0.0773  141  LYS A O   
1673  C CB  . LYS B 144  ? 2.2544 1.1478 1.4035 0.2276  -0.2519 0.1011  141  LYS A CB  
1674  N N   . VAL B 145  ? 2.1706 1.1365 1.3911 0.2191  -0.2348 0.0982  142  VAL A N   
1675  C CA  . VAL B 145  ? 2.1153 1.1302 1.3722 0.2342  -0.2225 0.0949  142  VAL A CA  
1676  C C   . VAL B 145  ? 2.1605 1.1467 1.3941 0.2354  -0.2285 0.0851  142  VAL A C   
1677  O O   . VAL B 145  ? 2.1337 1.1402 1.3693 0.2659  -0.2222 0.0761  142  VAL A O   
1678  C CB  . VAL B 145  ? 2.0483 1.1114 1.3599 0.2065  -0.2131 0.1071  142  VAL A CB  
1679  C CG1 . VAL B 145  ? 2.0198 1.1218 1.3569 0.2158  -0.2048 0.1148  142  VAL A CG1 
1680  C CG2 . VAL B 145  ? 2.0658 1.1019 1.3748 0.1597  -0.2219 0.1154  142  VAL A CG2 
1681  N N   . LEU B 146  ? 2.2233 1.1639 1.4334 0.2024  -0.2410 0.0870  143  LEU A N   
1682  C CA  . LEU B 146  ? 2.2676 1.1734 1.4476 0.2032  -0.2492 0.0774  143  LEU A CA  
1683  C C   . LEU B 146  ? 2.3736 1.2355 1.4972 0.2374  -0.2579 0.0649  143  LEU A C   
1684  O O   . LEU B 146  ? 2.3726 1.2202 1.4752 0.2540  -0.2604 0.0546  143  LEU A O   
1685  C CB  . LEU B 146  ? 2.2378 1.1103 1.4072 0.1570  -0.2611 0.0838  143  LEU A CB  
1686  C CG  . LEU B 146  ? 2.2646 1.0774 1.3821 0.1500  -0.2773 0.0759  143  LEU A CG  
1687  C CD1 . LEU B 146  ? 2.2174 1.0402 1.3555 0.1196  -0.2779 0.0786  143  LEU A CD1 
1688  C CD2 . LEU B 146  ? 2.3186 1.0783 1.3924 0.1302  -0.2935 0.0798  143  LEU A CD2 
1689  N N   . LYS B 147  ? 2.4958 1.3368 1.5934 0.2493  -0.2623 0.0654  144  LYS A N   
1690  C CA  . LYS B 147  ? 2.5667 1.3712 1.6110 0.2862  -0.2692 0.0530  144  LYS A CA  
1691  C C   . LYS B 147  ? 2.5429 1.3976 1.6056 0.3306  -0.2549 0.0455  144  LYS A C   
1692  O O   . LYS B 147  ? 2.6029 1.4379 1.6277 0.3615  -0.2584 0.0335  144  LYS A O   
1693  C CB  . LYS B 147  ? 2.6116 1.3806 1.6225 0.2869  -0.2778 0.0557  144  LYS A CB  
1694  N N   . GLN B 148  ? 2.3995 1.3209 1.5185 0.3342  -0.2393 0.0527  145  GLN A N   
1695  C CA  . GLN B 148  ? 2.2825 1.2601 1.4239 0.3724  -0.2255 0.0468  145  GLN A CA  
1696  C C   . GLN B 148  ? 2.2322 1.2223 1.3840 0.3740  -0.2224 0.0409  145  GLN A C   
1697  O O   . GLN B 148  ? 2.2472 1.2651 1.3967 0.4083  -0.2157 0.0324  145  GLN A O   
1698  C CB  . GLN B 148  ? 2.1442 1.1913 1.3429 0.3732  -0.2106 0.0566  145  GLN A CB  
1699  C CG  . GLN B 148  ? 2.1014 1.1400 1.3102 0.3471  -0.2134 0.0683  145  GLN A CG  
1700  C CD  . GLN B 148  ? 2.0767 1.1499 1.2951 0.3720  -0.2061 0.0707  145  GLN A CD  
1701  O OE1 . GLN B 148  ? 2.0531 1.1279 1.2835 0.3548  -0.2066 0.0803  145  GLN A OE1 
1702  N NE2 . GLN B 148  ? 2.0809 1.1849 1.2939 0.4123  -0.1991 0.0622  145  GLN A NE2 
1703  N N   . LEU B 149  ? 2.1680 1.1402 1.3310 0.3372  -0.2272 0.0455  146  LEU A N   
1704  C CA  . LEU B 149  ? 2.1066 1.0896 1.2813 0.3352  -0.2245 0.0407  146  LEU A CA  
1705  C C   . LEU B 149  ? 2.1607 1.0784 1.2790 0.3341  -0.2398 0.0312  146  LEU A C   
1706  O O   . LEU B 149  ? 2.1675 1.0860 1.2682 0.3605  -0.2389 0.0208  146  LEU A O   
1707  C CB  . LEU B 149  ? 2.0299 1.0363 1.2513 0.2962  -0.2202 0.0513  146  LEU A CB  
1708  C CG  . LEU B 149  ? 1.9464 1.0254 1.2286 0.2989  -0.2037 0.0586  146  LEU A CG  
1709  C CD1 . LEU B 149  ? 1.9398 1.0589 1.2319 0.3321  -0.1948 0.0586  146  LEU A CD1 
1710  C CD2 . LEU B 149  ? 1.9000 0.9860 1.2137 0.2569  -0.2035 0.0718  146  LEU A CD2 
1711  N N   . THR B 153  ? 2.2153 0.8898 1.2014 0.1511  -0.3156 0.0498  150  THR A N   
1712  C CA  . THR B 153  ? 2.3110 0.9300 1.2520 0.1242  -0.3343 0.0543  150  THR A CA  
1713  C C   . THR B 153  ? 2.2914 0.9234 1.2591 0.0724  -0.3378 0.0672  150  THR A C   
1714  O O   . THR B 153  ? 2.2585 0.9072 1.2460 0.0564  -0.3359 0.0676  150  THR A O   
1715  C CB  . THR B 153  ? 2.4124 0.9635 1.2822 0.1371  -0.3525 0.0431  150  THR A CB  
1716  O OG1 . THR B 153  ? 2.4047 0.9610 1.2798 0.1342  -0.3523 0.0383  150  THR A OG1 
1717  C CG2 . THR B 153  ? 2.4481 0.9819 1.2828 0.1873  -0.3512 0.0312  150  THR A CG2 
1718  N N   . THR B 154  ? 2.3091 0.9360 1.2772 0.0469  -0.3427 0.0778  151  THR A N   
1719  C CA  . THR B 154  ? 2.2871 0.9331 1.2811 -0.0021 -0.3456 0.0913  151  THR A CA  
1720  C C   . THR B 154  ? 2.3554 0.9492 1.3007 -0.0298 -0.3667 0.0916  151  THR A C   
1721  O O   . THR B 154  ? 2.4179 0.9503 1.3017 -0.0177 -0.3825 0.0847  151  THR A O   
1722  C CB  . THR B 154  ? 2.2755 0.9368 1.2855 -0.0176 -0.3435 0.1028  151  THR A CB  
1723  O OG1 . THR B 154  ? 2.2208 0.9258 1.2697 0.0115  -0.3254 0.1020  151  THR A OG1 
1724  C CG2 . THR B 154  ? 2.2315 0.9274 1.2769 -0.0657 -0.3432 0.1174  151  THR A CG2 
1725  N N   . THR B 155  ? 2.3365 0.9562 1.3083 -0.0667 -0.3672 0.0997  152  THR A N   
1726  C CA  . THR B 155  ? 2.3685 0.9493 1.3013 -0.0999 -0.3870 0.1033  152  THR A CA  
1727  C C   . THR B 155  ? 2.3681 0.9555 1.3047 -0.1404 -0.3945 0.1183  152  THR A C   
1728  O O   . THR B 155  ? 2.3268 0.9602 1.3074 -0.1468 -0.3819 0.1266  152  THR A O   
1729  C CB  . THR B 155  ? 2.2811 0.8888 1.2389 -0.1159 -0.3837 0.1034  152  THR A CB  
1730  O OG1 . THR B 155  ? 2.1923 0.8605 1.2058 -0.1501 -0.3741 0.1167  152  THR A OG1 
1731  C CG2 . THR B 155  ? 2.2177 0.8445 1.1957 -0.0768 -0.3690 0.0911  152  THR A CG2 
1732  N N   . GLU B 156  ? 2.4157 0.9574 1.3042 -0.1681 -0.4159 0.1221  153  GLU A N   
1733  C CA  . GLU B 156  ? 2.4039 0.9435 1.2850 -0.2047 -0.4262 0.1358  153  GLU A CA  
1734  C C   . GLU B 156  ? 2.3172 0.9322 1.2636 -0.2369 -0.4133 0.1497  153  GLU A C   
1735  O O   . GLU B 156  ? 2.2981 0.9388 1.2658 -0.2500 -0.4091 0.1596  153  GLU A O   
1736  C CB  . GLU B 156  ? 2.4770 0.9574 1.2951 -0.2307 -0.4523 0.1380  153  GLU A CB  
1737  N N   . HIS B 157  ? 2.2596 0.9117 1.2376 -0.2494 -0.4070 0.1508  154  HIS A N   
1738  C CA  . HIS B 157  ? 2.1538 0.8801 1.1929 -0.2778 -0.3943 0.1633  154  HIS A CA  
1739  C C   . HIS B 157  ? 2.0916 0.8677 1.1840 -0.2552 -0.3718 0.1630  154  HIS A C   
1740  O O   . HIS B 157  ? 2.0522 0.8773 1.1830 -0.2746 -0.3637 0.1746  154  HIS A O   
1741  C CB  . HIS B 157  ? 2.0748 0.8281 1.1333 -0.2932 -0.3925 0.1635  154  HIS A CB  
1742  C CG  . HIS B 157  ? 1.9720 0.8030 1.0907 -0.3207 -0.3798 0.1757  154  HIS A CG  
1743  N ND1 . HIS B 157  ? 1.8928 0.7776 1.0654 -0.3081 -0.3598 0.1729  154  HIS A ND1 
1744  C CD2 . HIS B 157  ? 1.9522 0.8175 1.0844 -0.3591 -0.3844 0.1908  154  HIS A CD2 
1745  C CE1 . HIS B 157  ? 1.8418 0.7896 1.0574 -0.3367 -0.3526 0.1853  154  HIS A CE1 
1746  N NE2 . HIS B 157  ? 1.8771 0.8167 1.0702 -0.3674 -0.3669 0.1963  154  HIS A NE2 
1747  N N   . GLU B 158  ? 2.0832 0.8487 1.1773 -0.2138 -0.3619 0.1502  155  GLU A N   
1748  C CA  . GLU B 158  ? 2.0286 0.8355 1.1665 -0.1902 -0.3425 0.1500  155  GLU A CA  
1749  C C   . GLU B 158  ? 2.0648 0.8571 1.1890 -0.1869 -0.3453 0.1549  155  GLU A C   
1750  O O   . GLU B 158  ? 2.0368 0.8756 1.2022 -0.1921 -0.3331 0.1634  155  GLU A O   
1751  C CB  . GLU B 158  ? 2.0222 0.8196 1.1594 -0.1458 -0.3333 0.1354  155  GLU A CB  
1752  C CG  . GLU B 158  ? 1.9853 0.8088 1.1479 -0.1458 -0.3260 0.1308  155  GLU A CG  
1753  C CD  . GLU B 158  ? 1.9811 0.7844 1.1297 -0.1021 -0.3213 0.1156  155  GLU A CD  
1754  O OE1 . GLU B 158  ? 2.0008 0.7826 1.1299 -0.0696 -0.3201 0.1093  155  GLU A OE1 
1755  O OE2 . GLU B 158  ? 1.9512 0.7625 1.1081 -0.0998 -0.3188 0.1101  155  GLU A OE2 
1756  N N   . ASN B 159  ? 2.1835 0.9103 1.2481 -0.1780 -0.3617 0.1496  156  ASN A N   
1757  C CA  . ASN B 159  ? 2.2158 0.9241 1.2626 -0.1776 -0.3664 0.1545  156  ASN A CA  
1758  C C   . ASN B 159  ? 2.1778 0.9162 1.2432 -0.2221 -0.3703 0.1709  156  ASN A C   
1759  O O   . ASN B 159  ? 2.1483 0.9118 1.2354 -0.2245 -0.3635 0.1786  156  ASN A O   
1760  C CB  . ASN B 159  ? 2.3604 0.9891 1.3343 -0.1631 -0.3856 0.1459  156  ASN A CB  
1761  C CG  . ASN B 159  ? 2.4020 1.0090 1.3602 -0.1131 -0.3790 0.1332  156  ASN A CG  
1762  O OD1 . ASN B 159  ? 2.3700 1.0111 1.3613 -0.0956 -0.3645 0.1352  156  ASN A OD1 
1763  N ND2 . ASN B 159  ? 2.4653 1.0170 1.3712 -0.0894 -0.3899 0.1204  156  ASN A ND2 
1764  N N   . ALA B 160  ? 2.1789 0.9187 1.2366 -0.2571 -0.3813 0.1769  157  ALA A N   
1765  C CA  . ALA B 160  ? 2.1285 0.9067 1.2072 -0.2992 -0.3842 0.1930  157  ALA A CA  
1766  C C   . ALA B 160  ? 1.9840 0.8438 1.1334 -0.3043 -0.3629 0.2003  157  ALA A C   
1767  O O   . ALA B 160  ? 1.9473 0.8457 1.1205 -0.3273 -0.3602 0.2129  157  ALA A O   
1768  C CB  . ALA B 160  ? 2.1668 0.9320 1.2210 -0.3340 -0.4008 0.1978  157  ALA A CB  
1769  N N   . LEU B 161  ? 1.8914 0.7782 1.0731 -0.2829 -0.3480 0.1927  158  LEU A N   
1770  C CA  . LEU B 161  ? 1.7894 0.7498 1.0347 -0.2845 -0.3280 0.1987  158  LEU A CA  
1771  C C   . LEU B 161  ? 1.7695 0.7426 1.0334 -0.2598 -0.3159 0.1988  158  LEU A C   
1772  O O   . LEU B 161  ? 1.7369 0.7657 1.0437 -0.2706 -0.3043 0.2085  158  LEU A O   
1773  C CB  . LEU B 161  ? 1.7270 0.7097 0.9983 -0.2706 -0.3172 0.1906  158  LEU A CB  
1774  C CG  . LEU B 161  ? 1.7039 0.7216 0.9937 -0.3022 -0.3189 0.1964  158  LEU A CG  
1775  C CD1 . LEU B 161  ? 1.6682 0.7079 0.9855 -0.2848 -0.3066 0.1878  158  LEU A CD1 
1776  C CD2 . LEU B 161  ? 1.6504 0.7319 0.9793 -0.3325 -0.3129 0.2115  158  LEU A CD2 
1777  N N   . LEU B 162  ? 1.7692 0.6936 1.0008 -0.2257 -0.3185 0.1885  159  LEU A N   
1778  C CA  . LEU B 162  ? 1.7062 0.6415 0.9520 -0.2014 -0.3082 0.1889  159  LEU A CA  
1779  C C   . LEU B 162  ? 1.7281 0.6645 0.9672 -0.2236 -0.3144 0.2006  159  LEU A C   
1780  O O   . LEU B 162  ? 1.6546 0.6344 0.9297 -0.2236 -0.3026 0.2082  159  LEU A O   
1781  C CB  . LEU B 162  ? 1.7316 0.6157 0.9404 -0.1592 -0.3108 0.1751  159  LEU A CB  
1782  C CG  . LEU B 162  ? 1.7119 0.6006 0.9307 -0.1286 -0.3019 0.1630  159  LEU A CG  
1783  C CD1 . LEU B 162  ? 1.7620 0.6000 0.9376 -0.0878 -0.3067 0.1498  159  LEU A CD1 
1784  C CD2 . LEU B 162  ? 1.6261 0.5791 0.9036 -0.1189 -0.2819 0.1664  159  LEU A CD2 
1785  N N   . ARG B 163  ? 1.8293 0.7182 1.0214 -0.2431 -0.3334 0.2025  160  ARG A N   
1786  C CA  . ARG B 163  ? 1.7113 0.5970 0.8924 -0.2649 -0.3411 0.2135  160  ARG A CA  
1787  C C   . ARG B 163  ? 1.6639 0.6142 0.8871 -0.3023 -0.3362 0.2285  160  ARG A C   
1788  O O   . ARG B 163  ? 1.6679 0.6312 0.8942 -0.3182 -0.3383 0.2388  160  ARG A O   
1789  C CB  . ARG B 163  ? 1.9164 0.7317 1.0323 -0.2769 -0.3644 0.2116  160  ARG A CB  
1790  C CG  . ARG B 163  ? 1.9740 0.7228 1.0416 -0.2397 -0.3712 0.1962  160  ARG A CG  
1791  C CD  . ARG B 163  ? 1.9557 0.6339 0.9564 -0.2509 -0.3944 0.1957  160  ARG A CD  
1792  N NE  . ARG B 163  ? 2.0575 0.7370 1.0467 -0.2960 -0.4089 0.2058  160  ARG A NE  
1793  C CZ  . ARG B 163  ? 2.0764 0.7306 1.0395 -0.3076 -0.4206 0.2019  160  ARG A CZ  
1794  N NH1 . ARG B 163  ? 2.0276 0.6524 0.9733 -0.2769 -0.4193 0.1876  160  ARG A NH1 
1795  N NH2 . ARG B 163  ? 2.0836 0.7441 1.0376 -0.3496 -0.4339 0.2128  160  ARG A NH2 
1796  N N   . SER B 164  ? 1.6564 0.6493 0.9116 -0.3156 -0.3297 0.2298  161  SER A N   
1797  C CA  . SER B 164  ? 1.5706 0.6324 0.8684 -0.3470 -0.3232 0.2434  161  SER A CA  
1798  C C   . SER B 164  ? 1.5465 0.6610 0.8904 -0.3353 -0.3051 0.2484  161  SER A C   
1799  O O   . SER B 164  ? 1.4713 0.6409 0.8462 -0.3588 -0.3004 0.2604  161  SER A O   
1800  C CB  . SER B 164  ? 1.5374 0.6333 0.8587 -0.3593 -0.3193 0.2424  161  SER A CB  
1801  O OG  . SER B 164  ? 1.5228 0.6261 0.8658 -0.3288 -0.3054 0.2317  161  SER A OG  
1802  N N   . PHE B 165  ? 1.5261 0.6264 0.8739 -0.2989 -0.2954 0.2398  162  PHE A N   
1803  C CA  . PHE B 165  ? 1.4764 0.6195 0.8621 -0.2846 -0.2796 0.2440  162  PHE A CA  
1804  C C   . PHE B 165  ? 1.5134 0.6161 0.8714 -0.2642 -0.2834 0.2423  162  PHE A C   
1805  O O   . PHE B 165  ? 1.4833 0.5970 0.8580 -0.2361 -0.2720 0.2393  162  PHE A O   
1806  C CB  . PHE B 165  ? 1.4358 0.6078 0.8558 -0.2596 -0.2637 0.2368  162  PHE A CB  
1807  C CG  . PHE B 165  ? 1.4055 0.6322 0.8631 -0.2796 -0.2562 0.2407  162  PHE A CG  
1808  C CD1 . PHE B 165  ? 1.3691 0.6613 0.8675 -0.2982 -0.2468 0.2520  162  PHE A CD1 
1809  C CD2 . PHE B 165  ? 1.4099 0.6240 0.8615 -0.2784 -0.2585 0.2327  162  PHE A CD2 
1810  C CE1 . PHE B 165  ? 1.3130 0.6578 0.8449 -0.3145 -0.2397 0.2551  162  PHE A CE1 
1811  C CE2 . PHE B 165  ? 1.3717 0.6372 0.8576 -0.2960 -0.2515 0.2362  162  PHE A CE2 
1812  C CZ  . PHE B 165  ? 1.3211 0.6523 0.8469 -0.3136 -0.2421 0.2473  162  PHE A CZ  
1813  N N   . ASP B 166  ? 1.5883 0.6435 0.9021 -0.2779 -0.3002 0.2442  163  ASP A N   
1814  C CA  . ASP B 166  ? 1.6308 0.6511 0.9184 -0.2627 -0.3045 0.2443  163  ASP A CA  
1815  C C   . ASP B 166  ? 1.6145 0.6864 0.9366 -0.2764 -0.2958 0.2573  163  ASP A C   
1816  O O   . ASP B 166  ? 1.6094 0.7204 0.9499 -0.3098 -0.2973 0.2683  163  ASP A O   
1817  C CB  . ASP B 166  ? 1.7206 0.6748 0.9489 -0.2761 -0.3260 0.2431  163  ASP A CB  
1818  N N   . LYS B 167  ? 1.6007 0.6753 0.9312 -0.2493 -0.2868 0.2560  164  LYS A N   
1819  C CA  . LYS B 167  ? 1.5392 0.6650 0.9048 -0.2564 -0.2766 0.2672  164  LYS A CA  
1820  C C   . LYS B 167  ? 1.4780 0.6773 0.8969 -0.2715 -0.2632 0.2735  164  LYS A C   
1821  O O   . LYS B 167  ? 1.4261 0.6728 0.8705 -0.2931 -0.2592 0.2851  164  LYS A O   
1822  C CB  . LYS B 167  ? 1.5697 0.6826 0.9134 -0.2831 -0.2886 0.2776  164  LYS A CB  
1823  N N   . PHE B 168  ? 1.5032 0.7129 0.9381 -0.2591 -0.2562 0.2656  165  PHE A N   
1824  C CA  . PHE B 168  ? 1.4827 0.7600 0.9659 -0.2717 -0.2437 0.2704  165  PHE A CA  
1825  C C   . PHE B 168  ? 1.4467 0.7327 0.9489 -0.2457 -0.2330 0.2607  165  PHE A C   
1826  O O   . PHE B 168  ? 1.4609 0.7884 0.9930 -0.2567 -0.2260 0.2617  165  PHE A O   
1827  C CB  . PHE B 168  ? 1.5006 0.7927 0.9826 -0.3070 -0.2518 0.2755  165  PHE A CB  
1828  C CG  . PHE B 168  ? 1.4388 0.8055 0.9628 -0.3306 -0.2433 0.2872  165  PHE A CG  
1829  C CD1 . PHE B 168  ? 1.1981 0.6197 0.7650 -0.3250 -0.2284 0.2866  165  PHE A CD1 
1830  C CD2 . PHE B 168  ? 1.2818 0.6645 0.8009 -0.3576 -0.2506 0.2987  165  PHE A CD2 
1831  C CE1 . PHE B 168  ? 1.1535 0.6448 0.7568 -0.3438 -0.2206 0.2965  165  PHE A CE1 
1832  C CE2 . PHE B 168  ? 1.2360 0.6907 0.7928 -0.3767 -0.2428 0.3091  165  PHE A CE2 
1833  C CZ  . PHE B 168  ? 1.1720 0.6812 0.7705 -0.3688 -0.2276 0.3076  165  PHE A CZ  
1834  N N   . THR B 169  ? 1.4059 0.6567 0.8918 -0.2113 -0.2316 0.2515  166  THR A N   
1835  C CA  . THR B 169  ? 1.3865 0.6454 0.8883 -0.1859 -0.2225 0.2425  166  THR A CA  
1836  C C   . THR B 169  ? 1.3313 0.6530 0.8815 -0.1820 -0.2070 0.2478  166  THR A C   
1837  O O   . THR B 169  ? 1.3144 0.6618 0.8891 -0.1627 -0.1966 0.2371  166  THR A O   
1838  C CB  . THR B 169  ? 1.4569 0.6665 0.9274 -0.1482 -0.2256 0.2316  166  THR A CB  
1839  O OG1 . THR B 169  ? 1.4861 0.7009 0.9583 -0.1337 -0.2222 0.2358  166  THR A OG1 
1840  C CG2 . THR B 169  ? 1.5348 0.6800 0.9543 -0.1503 -0.2415 0.2251  166  THR A CG2 
1841  N N   . THR B 170  ? 1.2918 0.6512 0.8623 -0.1968 -0.2028 0.2588  167  THR A N   
1842  C CA  . THR B 170  ? 1.2019 0.6371 0.8258 -0.1928 -0.1857 0.2580  167  THR A CA  
1843  C C   . THR B 170  ? 1.1363 0.6162 0.7896 -0.2115 -0.1799 0.2579  167  THR A C   
1844  O O   . THR B 170  ? 1.0540 0.5955 0.7507 -0.2039 -0.1652 0.2531  167  THR A O   
1845  C CB  . THR B 170  ? 1.1587 0.6211 0.7932 -0.2045 -0.1839 0.2702  167  THR A CB  
1846  O OG1 . THR B 170  ? 1.1826 0.5904 0.7785 -0.1947 -0.1939 0.2735  167  THR A OG1 
1847  C CG2 . THR B 170  ? 1.0638 0.5940 0.7469 -0.1868 -0.1660 0.2642  167  THR A CG2 
1848  N N   . TYR B 171  ? 1.1773 0.6263 0.8059 -0.2355 -0.1917 0.2631  168  TYR A N   
1849  C CA  . TYR B 171  ? 1.1627 0.6513 0.8166 -0.2506 -0.1867 0.2619  168  TYR A CA  
1850  C C   . TYR B 171  ? 1.0950 0.5978 0.7697 -0.2230 -0.1759 0.2448  168  TYR A C   
1851  O O   . TYR B 171  ? 1.0701 0.6218 0.7777 -0.2275 -0.1665 0.2416  168  TYR A O   
1852  C CB  . TYR B 171  ? 1.2421 0.7001 0.8672 -0.2760 -0.2007 0.2643  168  TYR A CB  
1853  C CG  . TYR B 171  ? 1.0606 0.5690 0.7113 -0.3002 -0.1973 0.2684  168  TYR A CG  
1854  C CD1 . TYR B 171  ? 1.0342 0.6003 0.7095 -0.3211 -0.1932 0.2795  168  TYR A CD1 
1855  C CD2 . TYR B 171  ? 1.0601 0.5598 0.7092 -0.3006 -0.1984 0.2612  168  TYR A CD2 
1856  C CE1 . TYR B 171  ? 1.0080 0.6237 0.7056 -0.3404 -0.1902 0.2831  168  TYR A CE1 
1857  C CE2 . TYR B 171  ? 1.0334 0.5809 0.7052 -0.3215 -0.1954 0.2650  168  TYR A CE2 
1858  C CZ  . TYR B 171  ? 1.0077 0.6137 0.7035 -0.3407 -0.1913 0.2759  168  TYR A CZ  
1859  O OH  . TYR B 171  ? 0.9823 0.6391 0.6997 -0.3586 -0.1883 0.2795  168  TYR A OH  
1860  N N   . PHE B 172  ? 1.0882 0.5504 0.7434 -0.1941 -0.1773 0.2341  169  PHE A N   
1861  C CA  . PHE B 172  ? 1.0872 0.5649 0.7615 -0.1660 -0.1669 0.2186  169  PHE A CA  
1862  C C   . PHE B 172  ? 1.0579 0.5817 0.7666 -0.1422 -0.1522 0.2129  169  PHE A C   
1863  O O   . PHE B 172  ? 1.0365 0.5613 0.7510 -0.1144 -0.1460 0.2012  169  PHE A O   
1864  C CB  . PHE B 172  ? 1.1306 0.5423 0.7633 -0.1466 -0.1768 0.2104  169  PHE A CB  
1865  C CG  . PHE B 172  ? 1.1768 0.5399 0.7741 -0.1679 -0.1915 0.2138  169  PHE A CG  
1866  C CD1 . PHE B 172  ? 1.2265 0.5365 0.7811 -0.1894 -0.2083 0.2254  169  PHE A CD1 
1867  C CD2 . PHE B 172  ? 1.1646 0.5334 0.7695 -0.1673 -0.1894 0.2057  169  PHE A CD2 
1868  C CE1 . PHE B 172  ? 1.2565 0.5357 0.7848 -0.2071 -0.2199 0.2231  169  PHE A CE1 
1869  C CE2 . PHE B 172  ? 1.2032 0.5267 0.7744 -0.1875 -0.2036 0.2088  169  PHE A CE2 
1870  C CZ  . PHE B 172  ? 1.2525 0.5340 0.7867 -0.2072 -0.2185 0.2165  169  PHE A CZ  
1871  N N   . SER B 173  ? 1.0379 0.6010 0.7684 -0.1528 -0.1469 0.2213  170  SER A N   
1872  C CA  . SER B 173  ? 0.9884 0.5914 0.7478 -0.1320 -0.1346 0.2166  170  SER A CA  
1873  C C   . SER B 173  ? 0.9334 0.5824 0.7289 -0.1200 -0.1215 0.2059  170  SER A C   
1874  O O   . SER B 173  ? 0.9184 0.5730 0.7221 -0.0947 -0.1152 0.1962  170  SER A O   
1875  C CB  . SER B 173  ? 0.9704 0.6055 0.7441 -0.1477 -0.1324 0.2282  170  SER A CB  
1876  O OG  . SER B 173  ? 0.9600 0.6266 0.7563 -0.1278 -0.1223 0.2241  170  SER A OG  
1877  N N   . GLY B 174  ? 0.9128 0.5964 0.7293 -0.1382 -0.1176 0.2082  171  GLY A N   
1878  C CA  . GLY B 174  ? 0.8975 0.6202 0.7445 -0.1281 -0.1064 0.1984  171  GLY A CA  
1879  C C   . GLY B 174  ? 0.9505 0.6461 0.7861 -0.1152 -0.1081 0.1880  171  GLY A C   
1880  O O   . GLY B 174  ? 0.9465 0.6647 0.8017 -0.0979 -0.0992 0.1783  171  GLY A O   
1881  N N   . PHE B 175  ? 1.0079 0.6542 0.8100 -0.1240 -0.1200 0.1903  172  PHE A N   
1882  C CA  . PHE B 175  ? 1.0121 0.6275 0.7984 -0.1098 -0.1228 0.1804  172  PHE A CA  
1883  C C   . PHE B 175  ? 0.9981 0.5995 0.7769 -0.0785 -0.1202 0.1723  172  PHE A C   
1884  O O   . PHE B 175  ? 0.9701 0.5749 0.7541 -0.0604 -0.1156 0.1623  172  PHE A O   
1885  C CB  . PHE B 175  ? 1.0912 0.6509 0.8376 -0.1263 -0.1380 0.1853  172  PHE A CB  
1886  C CG  . PHE B 175  ? 1.1286 0.6462 0.8500 -0.1088 -0.1431 0.1753  172  PHE A CG  
1887  C CD1 . PHE B 175  ? 1.1168 0.6496 0.8519 -0.1079 -0.1386 0.1677  172  PHE A CD1 
1888  C CD2 . PHE B 175  ? 1.1610 0.6233 0.8432 -0.0920 -0.1526 0.1735  172  PHE A CD2 
1889  C CE1 . PHE B 175  ? 1.1288 0.6241 0.8403 -0.0909 -0.1432 0.1585  172  PHE A CE1 
1890  C CE2 . PHE B 175  ? 1.1797 0.6037 0.8365 -0.0734 -0.1574 0.1640  172  PHE A CE2 
1891  C CZ  . PHE B 175  ? 1.1698 0.6112 0.8419 -0.0731 -0.1526 0.1566  172  PHE A CZ  
1892  N N   . TYR B 176  ? 0.9854 0.5733 0.7519 -0.0715 -0.1230 0.1771  173  TYR A N   
1893  C CA  . TYR B 176  ? 0.9580 0.5402 0.7193 -0.0409 -0.1200 0.1703  173  TYR A CA  
1894  C C   . TYR B 176  ? 0.8627 0.5019 0.6642 -0.0278 -0.1056 0.1636  173  TYR A C   
1895  O O   . TYR B 176  ? 0.8188 0.4618 0.6213 -0.0042 -0.1017 0.1554  173  TYR A O   
1896  C CB  . TYR B 176  ? 0.9914 0.5546 0.7351 -0.0375 -0.1250 0.1775  173  TYR A CB  
1897  C CG  . TYR B 176  ? 1.0774 0.5726 0.7718 -0.0423 -0.1408 0.1824  173  TYR A CG  
1898  C CD1 . TYR B 176  ? 1.1260 0.5753 0.7894 -0.0361 -0.1493 0.1768  173  TYR A CD1 
1899  C CD2 . TYR B 176  ? 1.1021 0.5766 0.7785 -0.0531 -0.1481 0.1929  173  TYR A CD2 
1900  C CE1 . TYR B 176  ? 1.1936 0.5749 0.8070 -0.0408 -0.1653 0.1812  173  TYR A CE1 
1901  C CE2 . TYR B 176  ? 1.1648 0.5724 0.7920 -0.0589 -0.1639 0.1979  173  TYR A CE2 
1902  C CZ  . TYR B 176  ? 1.2329 0.5924 0.8276 -0.0527 -0.1729 0.1919  173  TYR A CZ  
1903  O OH  . TYR B 176  ? 1.3442 0.6314 0.8853 -0.0586 -0.1902 0.1967  173  TYR A OH  
1904  N N   . GLU B 177  ? 0.8525 0.5363 0.6853 -0.0429 -0.0982 0.1675  174  GLU A N   
1905  C CA  . GLU B 177  ? 0.8376 0.5712 0.7051 -0.0331 -0.0861 0.1616  174  GLU A CA  
1906  C C   . GLU B 177  ? 0.7987 0.5416 0.6761 -0.0304 -0.0822 0.1533  174  GLU A C   
1907  O O   . GLU B 177  ? 0.7410 0.5066 0.6333 -0.0142 -0.0752 0.1463  174  GLU A O   
1908  C CB  . GLU B 177  ? 0.8673 0.6406 0.7603 -0.0489 -0.0806 0.1675  174  GLU A CB  
1909  C CG  . GLU B 177  ? 0.9307 0.7064 0.8211 -0.0470 -0.0815 0.1742  174  GLU A CG  
1910  C CD  . GLU B 177  ? 0.9556 0.7471 0.8547 -0.0240 -0.0760 0.1691  174  GLU A CD  
1911  O OE1 . GLU B 177  ? 0.9390 0.7574 0.8573 -0.0151 -0.0688 0.1619  174  GLU A OE1 
1912  O OE2 . GLU B 177  ? 0.9796 0.7573 0.8655 -0.0155 -0.0792 0.1729  174  GLU A OE2 
1913  N N   . ASN B 178  ? 0.8158 0.5427 0.6847 -0.0471 -0.0871 0.1546  175  ASN A N   
1914  C CA  . ASN B 178  ? 0.7961 0.5298 0.6728 -0.0450 -0.0839 0.1469  175  ASN A CA  
1915  C C   . ASN B 178  ? 0.8345 0.5408 0.6922 -0.0225 -0.0863 0.1392  175  ASN A C   
1916  O O   . ASN B 178  ? 0.8210 0.5446 0.6914 -0.0126 -0.0805 0.1316  175  ASN A O   
1917  C CB  . ASN B 178  ? 0.8223 0.5429 0.6910 -0.0682 -0.0898 0.1509  175  ASN A CB  
1918  C CG  . ASN B 178  ? 0.8164 0.5702 0.7039 -0.0890 -0.0870 0.1590  175  ASN A CG  
1919  O OD1 . ASN B 178  ? 0.8414 0.6376 0.7567 -0.0866 -0.0777 0.1571  175  ASN A OD1 
1920  N ND2 . ASN B 178  ? 0.7989 0.5332 0.6691 -0.1095 -0.0958 0.1684  175  ASN A ND2 
1921  N N   . ARG B 179  ? 0.8938 0.5576 0.7195 -0.0132 -0.0950 0.1411  176  ARG A N   
1922  C CA  . ARG B 179  ? 0.9473 0.5853 0.7514 0.0120  -0.0977 0.1338  176  ARG A CA  
1923  C C   . ARG B 179  ? 0.9594 0.6268 0.7770 0.0361  -0.0901 0.1306  176  ARG A C   
1924  O O   . ARG B 179  ? 0.9923 0.6624 0.8060 0.0577  -0.0878 0.1236  176  ARG A O   
1925  C CB  . ARG B 179  ? 1.0007 0.5756 0.7590 0.0138  -0.1116 0.1366  176  ARG A CB  
1926  C CG  . ARG B 179  ? 1.0152 0.5556 0.7540 -0.0065 -0.1207 0.1379  176  ARG A CG  
1927  C CD  . ARG B 179  ? 0.9796 0.5284 0.7258 0.0017  -0.1168 0.1286  176  ARG A CD  
1928  N NE  . ARG B 179  ? 0.9734 0.4997 0.7080 -0.0206 -0.1239 0.1301  176  ARG A NE  
1929  C CZ  . ARG B 179  ? 0.9374 0.4984 0.6998 -0.0423 -0.1187 0.1324  176  ARG A CZ  
1930  N NH1 . ARG B 179  ? 0.9637 0.5041 0.7133 -0.0620 -0.1260 0.1342  176  ARG A NH1 
1931  N NH2 . ARG B 179  ? 0.8723 0.4881 0.6735 -0.0438 -0.1067 0.1330  176  ARG A NH2 
1932  N N   . LYS B 180  ? 0.9419 0.6338 0.7751 0.0327  -0.0863 0.1360  177  LYS A N   
1933  C CA  . LYS B 180  ? 0.9075 0.6367 0.7592 0.0514  -0.0783 0.1335  177  LYS A CA  
1934  C C   . LYS B 180  ? 0.8500 0.6245 0.7342 0.0494  -0.0685 0.1286  177  LYS A C   
1935  O O   . LYS B 180  ? 0.8353 0.6348 0.7287 0.0670  -0.0632 0.1246  177  LYS A O   
1936  C CB  . LYS B 180  ? 0.9260 0.6710 0.7870 0.0462  -0.0769 0.1405  177  LYS A CB  
1937  C CG  . LYS B 180  ? 1.0126 0.7147 0.8412 0.0500  -0.0864 0.1459  177  LYS A CG  
1938  C CD  . LYS B 180  ? 1.0298 0.7538 0.8668 0.0598  -0.0832 0.1497  177  LYS A CD  
1939  C CE  . LYS B 180  ? 1.0595 0.7545 0.8777 0.0485  -0.0906 0.1584  177  LYS A CE  
1940  N NZ  . LYS B 180  ? 1.0381 0.7496 0.8748 0.0200  -0.0891 0.1643  177  LYS A NZ  
1941  N N   . ASN B 181  ? 0.7762 0.5623 0.6764 0.0282  -0.0663 0.1295  178  ASN A N   
1942  C CA  . ASN B 181  ? 0.7396 0.5621 0.6660 0.0257  -0.0582 0.1246  178  ASN A CA  
1943  C C   . ASN B 181  ? 0.7369 0.5503 0.6553 0.0382  -0.0582 0.1174  178  ASN A C   
1944  O O   . ASN B 181  ? 0.7006 0.5447 0.6384 0.0412  -0.0515 0.1133  178  ASN A O   
1945  C CB  . ASN B 181  ? 0.6987 0.5323 0.6394 0.0024  -0.0568 0.1271  178  ASN A CB  
1946  C CG  . ASN B 181  ? 0.5859 0.4357 0.5370 -0.0089 -0.0557 0.1340  178  ASN A CG  
1947  O OD1 . ASN B 181  ? 0.6575 0.5216 0.6141 0.0000  -0.0534 0.1357  178  ASN A OD1 
1948  N ND2 . ASN B 181  ? 0.5832 0.4332 0.5368 -0.0281 -0.0574 0.1384  178  ASN A ND2 
1949  N N   . VAL B 182  ? 0.7786 0.5489 0.6668 0.0454  -0.0662 0.1161  179  VAL A N   
1950  C CA  . VAL B 182  ? 0.7420 0.5014 0.6195 0.0592  -0.0668 0.1090  179  VAL A CA  
1951  C C   . VAL B 182  ? 0.7737 0.5464 0.6470 0.0868  -0.0641 0.1059  179  VAL A C   
1952  O O   . VAL B 182  ? 0.7712 0.5667 0.6542 0.0977  -0.0591 0.1009  179  VAL A O   
1953  C CB  . VAL B 182  ? 0.7494 0.4542 0.5929 0.0553  -0.0776 0.1085  179  VAL A CB  
1954  C CG1 . VAL B 182  ? 0.7442 0.4348 0.5730 0.0726  -0.0789 0.1007  179  VAL A CG1 
1955  C CG2 . VAL B 182  ? 0.7193 0.4197 0.5696 0.0265  -0.0798 0.1124  179  VAL A CG2 
1956  N N   . PHE B 183  ? 0.7911 0.5523 0.6497 0.0988  -0.0675 0.1093  180  PHE A N   
1957  C CA  . PHE B 183  ? 0.7905 0.5652 0.6420 0.1270  -0.0657 0.1072  180  PHE A CA  
1958  C C   . PHE B 183  ? 0.7637 0.5904 0.6442 0.1282  -0.0576 0.1105  180  PHE A C   
1959  O O   . PHE B 183  ? 0.7822 0.6293 0.6603 0.1503  -0.0555 0.1100  180  PHE A O   
1960  C CB  . PHE B 183  ? 0.8338 0.5617 0.6465 0.1432  -0.0752 0.1086  180  PHE A CB  
1961  C CG  . PHE B 183  ? 0.8613 0.5336 0.6381 0.1469  -0.0848 0.1047  180  PHE A CG  
1962  C CD1 . PHE B 183  ? 0.8725 0.5062 0.6365 0.1227  -0.0923 0.1078  180  PHE A CD1 
1963  C CD2 . PHE B 183  ? 0.8964 0.5559 0.6506 0.1745  -0.0869 0.0983  180  PHE A CD2 
1964  C CE1 . PHE B 183  ? 0.9172 0.4974 0.6458 0.1241  -0.1025 0.1047  180  PHE A CE1 
1965  C CE2 . PHE B 183  ? 0.9529 0.5572 0.6706 0.1784  -0.0968 0.0943  180  PHE A CE2 
1966  C CZ  . PHE B 183  ? 0.9077 0.4708 0.6121 0.1522  -0.1050 0.0975  180  PHE A CZ  
1967  N N   . SER B 184  ? 0.7411 0.5903 0.6472 0.1056  -0.0536 0.1140  181  SER A N   
1968  C CA  . SER B 184  ? 0.6923 0.5859 0.6228 0.1046  -0.0473 0.1173  181  SER A CA  
1969  C C   . SER B 184  ? 0.6937 0.6289 0.6411 0.1141  -0.0409 0.1143  181  SER A C   
1970  O O   . SER B 184  ? 0.6982 0.6348 0.6483 0.1131  -0.0393 0.1098  181  SER A O   
1971  C CB  . SER B 184  ? 0.6461 0.5517 0.5971 0.0792  -0.0449 0.1207  181  SER A CB  
1972  O OG  . SER B 184  ? 0.6203 0.5670 0.5933 0.0773  -0.0396 0.1232  181  SER A OG  
1973  N N   . ALA B 185  ? 0.6973 0.6680 0.6557 0.1226  -0.0376 0.1174  182  ALA A N   
1974  C CA  . ALA B 185  ? 0.6793 0.6959 0.6554 0.1277  -0.0319 0.1168  182  ALA A CA  
1975  C C   . ALA B 185  ? 0.6666 0.7136 0.6695 0.1056  -0.0275 0.1189  182  ALA A C   
1976  O O   . ALA B 185  ? 0.6695 0.7534 0.6870 0.1049  -0.0236 0.1192  182  ALA A O   
1977  C CB  . ALA B 185  ? 0.6570 0.6994 0.6285 0.1498  -0.0313 0.1198  182  ALA A CB  
1978  N N   . GLU B 186  ? 0.6747 0.7069 0.6823 0.0878  -0.0287 0.1206  183  GLU A N   
1979  C CA  . GLU B 186  ? 0.6764 0.7321 0.7045 0.0688  -0.0256 0.1221  183  GLU A CA  
1980  C C   . GLU B 186  ? 0.6391 0.6973 0.6750 0.0590  -0.0233 0.1177  183  GLU A C   
1981  O O   . GLU B 186  ? 0.6207 0.6597 0.6471 0.0643  -0.0242 0.1137  183  GLU A O   
1982  C CB  . GLU B 186  ? 0.7339 0.7730 0.7623 0.0553  -0.0276 0.1249  183  GLU A CB  
1983  C CG  . GLU B 186  ? 0.8106 0.8480 0.8322 0.0633  -0.0298 0.1297  183  GLU A CG  
1984  C CD  . GLU B 186  ? 0.8761 0.9522 0.9103 0.0663  -0.0274 0.1328  183  GLU A CD  
1985  O OE1 . GLU B 186  ? 0.9019 1.0015 0.9511 0.0543  -0.0249 0.1325  183  GLU A OE1 
1986  O OE2 . GLU B 186  ? 0.9034 0.9857 0.9309 0.0803  -0.0286 0.1358  183  GLU A OE2 
1987  N N   . ASP B 187  ? 0.6188 0.6989 0.6701 0.0447  -0.0210 0.1185  184  ASP A N   
1988  C CA  . ASP B 187  ? 0.5919 0.6755 0.6501 0.0348  -0.0190 0.1148  184  ASP A CA  
1989  C C   . ASP B 187  ? 0.5596 0.6172 0.6153 0.0229  -0.0200 0.1127  184  ASP A C   
1990  O O   . ASP B 187  ? 0.5399 0.6025 0.6029 0.0100  -0.0193 0.1126  184  ASP A O   
1991  C CB  . ASP B 187  ? 0.5945 0.7087 0.6653 0.0249  -0.0174 0.1169  184  ASP A CB  
1992  C CG  . ASP B 187  ? 0.6119 0.7289 0.6873 0.0158  -0.0159 0.1133  184  ASP A CG  
1993  O OD1 . ASP B 187  ? 0.6168 0.7215 0.6877 0.0213  -0.0150 0.1094  184  ASP A OD1 
1994  O OD2 . ASP B 187  ? 0.6356 0.7647 0.7169 0.0033  -0.0161 0.1144  184  ASP A OD2 
1995  N N   . ILE B 188  ? 0.5662 0.5957 0.6093 0.0280  -0.0225 0.1112  185  ILE A N   
1996  C CA  . ILE B 188  ? 0.5446 0.5515 0.5839 0.0166  -0.0242 0.1104  185  ILE A CA  
1997  C C   . ILE B 188  ? 0.5842 0.5738 0.6156 0.0195  -0.0249 0.1057  185  ILE A C   
1998  O O   . ILE B 188  ? 0.6258 0.6057 0.6462 0.0334  -0.0264 0.1040  185  ILE A O   
1999  C CB  . ILE B 188  ? 0.5377 0.5241 0.5666 0.0154  -0.0281 0.1147  185  ILE A CB  
2000  C CG1 . ILE B 188  ? 0.5979 0.5628 0.6088 0.0307  -0.0318 0.1148  185  ILE A CG1 
2001  C CG2 . ILE B 188  ? 0.4852 0.4895 0.5225 0.0120  -0.0271 0.1192  185  ILE A CG2 
2002  C CD1 . ILE B 188  ? 0.5171 0.4577 0.5142 0.0290  -0.0367 0.1197  185  ILE A CD1 
2003  N N   . SER B 189  ? 0.5647 0.5510 0.6005 0.0075  -0.0241 0.1035  186  SER A N   
2004  C CA  . SER B 189  ? 0.5433 0.5167 0.5736 0.0088  -0.0245 0.0987  186  SER A CA  
2005  C C   . SER B 189  ? 0.5591 0.4984 0.5708 0.0104  -0.0300 0.0989  186  SER A C   
2006  O O   . SER B 189  ? 0.5914 0.5161 0.5947 0.0139  -0.0313 0.0948  186  SER A O   
2007  C CB  . SER B 189  ? 0.4389 0.4205 0.4788 -0.0040 -0.0221 0.0966  186  SER A CB  
2008  O OG  . SER B 189  ? 0.4320 0.4169 0.4759 -0.0148 -0.0226 0.1002  186  SER A OG  
2009  N N   . THR B 190  ? 0.5649 0.4895 0.5682 0.0073  -0.0338 0.1038  187  THR A N   
2010  C CA  . THR B 190  ? 0.6005 0.4884 0.5818 0.0073  -0.0407 0.1049  187  THR A CA  
2011  C C   . THR B 190  ? 0.6374 0.5066 0.6003 0.0271  -0.0438 0.1028  187  THR A C   
2012  O O   . THR B 190  ? 0.7413 0.5737 0.6807 0.0293  -0.0508 0.1026  187  THR A O   
2013  C CB  . THR B 190  ? 0.5409 0.4192 0.5177 -0.0040 -0.0444 0.1118  187  THR A CB  
2014  O OG1 . THR B 190  ? 0.5344 0.4278 0.5168 0.0036  -0.0424 0.1148  187  THR A OG1 
2015  C CG2 . THR B 190  ? 0.5573 0.4524 0.5480 -0.0222 -0.0422 0.1141  187  THR A CG2 
2016  N N   . ALA B 191  ? 0.5831 0.4767 0.5541 0.0417  -0.0395 0.1014  188  ALA A N   
2017  C CA  . ALA B 191  ? 0.6100 0.4926 0.5637 0.0633  -0.0421 0.1006  188  ALA A CA  
2018  C C   . ALA B 191  ? 0.6522 0.5348 0.5992 0.0780  -0.0412 0.0947  188  ALA A C   
2019  O O   . ALA B 191  ? 0.6602 0.5621 0.6219 0.0723  -0.0367 0.0916  188  ALA A O   
2020  C CB  . ALA B 191  ? 0.6034 0.5177 0.5690 0.0715  -0.0383 0.1041  188  ALA A CB  
2021  N N   . ILE B 192  ? 0.6791 0.5388 0.6016 0.0985  -0.0457 0.0931  189  ILE A N   
2022  C CA  . ILE B 192  ? 0.6827 0.5411 0.5940 0.1175  -0.0455 0.0875  189  ILE A CA  
2023  C C   . ILE B 192  ? 0.6949 0.6040 0.6256 0.1294  -0.0380 0.0879  189  ILE A C   
2024  O O   . ILE B 192  ? 0.6979 0.6264 0.6375 0.1315  -0.0341 0.0845  189  ILE A O   
2025  C CB  . ILE B 192  ? 0.6887 0.5030 0.5627 0.1379  -0.0539 0.0856  189  ILE A CB  
2026  C CG1 . ILE B 192  ? 0.7189 0.4813 0.5713 0.1229  -0.0625 0.0852  189  ILE A CG1 
2027  C CG2 . ILE B 192  ? 0.6923 0.5128 0.5545 0.1631  -0.0529 0.0800  189  ILE A CG2 
2028  C CD1 . ILE B 192  ? 0.7942 0.5039 0.6039 0.1409  -0.0728 0.0833  189  ILE A CD1 
2029  N N   . PRO B 193  ? 0.6893 0.6227 0.6265 0.1365  -0.0361 0.0924  190  PRO A N   
2030  C CA  . PRO B 193  ? 0.6677 0.6534 0.6241 0.1440  -0.0296 0.0941  190  PRO A CA  
2031  C C   . PRO B 193  ? 0.6466 0.6618 0.6301 0.1226  -0.0242 0.0946  190  PRO A C   
2032  O O   . PRO B 193  ? 0.6360 0.6833 0.6299 0.1266  -0.0201 0.0940  190  PRO A O   
2033  C CB  . PRO B 193  ? 0.6775 0.6794 0.6359 0.1500  -0.0297 0.0997  190  PRO A CB  
2034  C CG  . PRO B 193  ? 0.7114 0.6653 0.6421 0.1585  -0.0368 0.0992  190  PRO A CG  
2035  C CD  . PRO B 193  ? 0.7141 0.6294 0.6391 0.1400  -0.0404 0.0966  190  PRO A CD  
2036  N N   . HIS B 194  ? 0.6422 0.6471 0.6356 0.1006  -0.0245 0.0961  191  HIS A N   
2037  C CA  . HIS B 194  ? 0.5937 0.6209 0.6082 0.0819  -0.0204 0.0960  191  HIS A CA  
2038  C C   . HIS B 194  ? 0.5837 0.6020 0.5964 0.0803  -0.0195 0.0907  191  HIS A C   
2039  O O   . HIS B 194  ? 0.5771 0.6218 0.6031 0.0753  -0.0157 0.0901  191  HIS A O   
2040  C CB  . HIS B 194  ? 0.5859 0.6023 0.6075 0.0624  -0.0213 0.0983  191  HIS A CB  
2041  C CG  . HIS B 194  ? 0.5896 0.6185 0.6263 0.0452  -0.0184 0.0970  191  HIS A CG  
2042  N ND1 . HIS B 194  ? 0.6086 0.6670 0.6602 0.0366  -0.0157 0.0997  191  HIS A ND1 
2043  C CD2 . HIS B 194  ? 0.5705 0.5850 0.6074 0.0355  -0.0183 0.0933  191  HIS A CD2 
2044  C CE1 . HIS B 194  ? 0.5798 0.6385 0.6382 0.0236  -0.0143 0.0974  191  HIS A CE1 
2045  N NE2 . HIS B 194  ? 0.5615 0.5959 0.6123 0.0232  -0.0154 0.0936  191  HIS A NE2 
2046  N N   . ARG B 195  ? 0.5681 0.5482 0.5632 0.0832  -0.0238 0.0871  192  ARG A N   
2047  C CA  . ARG B 195  ? 0.5485 0.5183 0.5400 0.0825  -0.0236 0.0818  192  ARG A CA  
2048  C C   . ARG B 195  ? 0.5447 0.5364 0.5345 0.1008  -0.0209 0.0796  192  ARG A C   
2049  O O   . ARG B 195  ? 0.5568 0.5610 0.5544 0.0973  -0.0179 0.0769  192  ARG A O   
2050  C CB  . ARG B 195  ? 0.5721 0.4949 0.5412 0.0826  -0.0302 0.0791  192  ARG A CB  
2051  C CG  . ARG B 195  ? 0.5916 0.4991 0.5529 0.0837  -0.0312 0.0733  192  ARG A CG  
2052  C CD  . ARG B 195  ? 0.5801 0.5075 0.5622 0.0664  -0.0265 0.0723  192  ARG A CD  
2053  N NE  . ARG B 195  ? 0.5824 0.5062 0.5735 0.0464  -0.0270 0.0755  192  ARG A NE  
2054  C CZ  . ARG B 195  ? 0.5166 0.4158 0.5006 0.0340  -0.0308 0.0749  192  ARG A CZ  
2055  N NH1 . ARG B 195  ? 0.7868 0.6588 0.7536 0.0381  -0.0352 0.0710  192  ARG A NH1 
2056  N NH2 . ARG B 195  ? 0.5039 0.4071 0.4970 0.0175  -0.0307 0.0785  192  ARG A NH2 
2057  N N   . ILE B 196  ? 0.5467 0.5458 0.5261 0.1211  -0.0218 0.0812  193  ILE A N   
2058  C CA  . ILE B 196  ? 0.5666 0.5910 0.5430 0.1412  -0.0192 0.0799  193  ILE A CA  
2059  C C   . ILE B 196  ? 0.5600 0.6378 0.5607 0.1340  -0.0132 0.0846  193  ILE A C   
2060  O O   . ILE B 196  ? 0.5833 0.6848 0.5909 0.1356  -0.0099 0.0836  193  ILE A O   
2061  C CB  . ILE B 196  ? 0.6125 0.6266 0.5660 0.1681  -0.0228 0.0800  193  ILE A CB  
2062  C CG1 . ILE B 196  ? 0.6440 0.5996 0.5674 0.1754  -0.0303 0.0749  193  ILE A CG1 
2063  C CG2 . ILE B 196  ? 0.6421 0.6947 0.5950 0.1905  -0.0192 0.0801  193  ILE A CG2 
2064  C CD1 . ILE B 196  ? 0.6781 0.6142 0.5726 0.2032  -0.0353 0.0743  193  ILE A CD1 
2065  N N   . VAL B 197  ? 0.5349 0.6314 0.5477 0.1249  -0.0124 0.0902  194  VAL A N   
2066  C CA  . VAL B 197  ? 0.5231 0.6697 0.5548 0.1187  -0.0083 0.0958  194  VAL A CA  
2067  C C   . VAL B 197  ? 0.5276 0.6807 0.5754 0.0938  -0.0064 0.0960  194  VAL A C   
2068  O O   . VAL B 197  ? 0.5697 0.7538 0.6273 0.0891  -0.0037 0.0980  194  VAL A O   
2069  C CB  . VAL B 197  ? 0.5346 0.6979 0.5700 0.1202  -0.0090 0.1017  194  VAL A CB  
2070  C CG1 . VAL B 197  ? 0.5050 0.7188 0.5588 0.1097  -0.0061 0.1083  194  VAL A CG1 
2071  C CG2 . VAL B 197  ? 0.5632 0.7220 0.5803 0.1478  -0.0110 0.1015  194  VAL A CG2 
2072  N N   . GLN B 198  ? 0.5123 0.6368 0.5615 0.0780  -0.0082 0.0943  195  GLN A N   
2073  C CA  . GLN B 198  ? 0.5182 0.6489 0.5802 0.0562  -0.0070 0.0950  195  GLN A CA  
2074  C C   . GLN B 198  ? 0.5961 0.7021 0.6557 0.0486  -0.0069 0.0893  195  GLN A C   
2075  O O   . GLN B 198  ? 0.6261 0.7365 0.6937 0.0331  -0.0060 0.0892  195  GLN A O   
2076  C CB  . GLN B 198  ? 0.4772 0.6017 0.5436 0.0440  -0.0087 0.0980  195  GLN A CB  
2077  C CG  . GLN B 198  ? 0.4714 0.6201 0.5404 0.0502  -0.0090 0.1038  195  GLN A CG  
2078  C CD  . GLN B 198  ? 0.4813 0.6212 0.5530 0.0397  -0.0109 0.1064  195  GLN A CD  
2079  O OE1 . GLN B 198  ? 0.4763 0.6134 0.5434 0.0483  -0.0123 0.1089  195  GLN A OE1 
2080  N NE2 . GLN B 198  ? 0.4985 0.6336 0.5759 0.0223  -0.0112 0.1059  195  GLN A NE2 
2081  N N   . ASP B 199  ? 0.6268 0.7059 0.6737 0.0592  -0.0085 0.0846  196  ASP A N   
2082  C CA  . ASP B 199  ? 0.6392 0.6963 0.6833 0.0521  -0.0088 0.0794  196  ASP A CA  
2083  C C   . ASP B 199  ? 0.6347 0.6961 0.6735 0.0639  -0.0074 0.0757  196  ASP A C   
2084  O O   . ASP B 199  ? 0.6372 0.7091 0.6832 0.0562  -0.0051 0.0742  196  ASP A O   
2085  C CB  . ASP B 199  ? 0.7092 0.7283 0.7415 0.0501  -0.0129 0.0774  196  ASP A CB  
2086  C CG  . ASP B 199  ? 0.7616 0.7763 0.8015 0.0329  -0.0134 0.0797  196  ASP A CG  
2087  O OD1 . ASP B 199  ? 0.7463 0.7784 0.7980 0.0218  -0.0108 0.0805  196  ASP A OD1 
2088  O OD2 . ASP B 199  ? 0.7992 0.7924 0.8314 0.0309  -0.0167 0.0810  196  ASP A OD2 
2089  N N   . ASN B 200  ? 0.6373 0.6900 0.6617 0.0837  -0.0092 0.0741  197  ASN A N   
2090  C CA  . ASN B 200  ? 0.6206 0.6720 0.6363 0.0968  -0.0086 0.0697  197  ASN A CA  
2091  C C   . ASN B 200  ? 0.5991 0.6953 0.6237 0.1053  -0.0044 0.0729  197  ASN A C   
2092  O O   . ASN B 200  ? 0.5914 0.6987 0.6185 0.1060  -0.0021 0.0708  197  ASN A O   
2093  C CB  . ASN B 200  ? 0.6297 0.6473 0.6209 0.1157  -0.0135 0.0660  197  ASN A CB  
2094  C CG  . ASN B 200  ? 0.6091 0.5814 0.5887 0.1051  -0.0185 0.0624  197  ASN A CG  
2095  O OD1 . ASN B 200  ? 0.5237 0.4933 0.5140 0.0868  -0.0174 0.0615  197  ASN A OD1 
2096  N ND2 . ASN B 200  ? 0.6291 0.5657 0.5850 0.1167  -0.0247 0.0607  197  ASN A ND2 
2097  N N   . PHE B 201  ? 0.5722 0.6969 0.6016 0.1113  -0.0034 0.0787  198  PHE A N   
2098  C CA  . PHE B 201  ? 0.5754 0.7481 0.6128 0.1189  0.0002  0.0832  198  PHE A CA  
2099  C C   . PHE B 201  ? 0.5340 0.7316 0.5884 0.0977  0.0029  0.0863  198  PHE A C   
2100  O O   . PHE B 201  ? 0.5205 0.7428 0.5773 0.1018  0.0054  0.0870  198  PHE A O   
2101  C CB  . PHE B 201  ? 0.5761 0.7769 0.6151 0.1286  0.0002  0.0894  198  PHE A CB  
2102  C CG  . PHE B 201  ? 0.5788 0.8361 0.6278 0.1333  0.0037  0.0960  198  PHE A CG  
2103  C CD1 . PHE B 201  ? 0.5947 0.8714 0.6345 0.1569  0.0053  0.0949  198  PHE A CD1 
2104  C CD2 . PHE B 201  ? 0.5789 0.8706 0.6447 0.1138  0.0047  0.1036  198  PHE A CD2 
2105  C CE1 . PHE B 201  ? 0.5943 0.9289 0.6439 0.1605  0.0085  0.1022  198  PHE A CE1 
2106  C CE2 . PHE B 201  ? 0.5742 0.9206 0.6487 0.1151  0.0070  0.1111  198  PHE A CE2 
2107  C CZ  . PHE B 201  ? 0.5798 0.9503 0.6473 0.1383  0.0093  0.1108  198  PHE A CZ  
2108  N N   . PRO B 202  ? 0.4848 0.6771 0.5490 0.0757  0.0021  0.0885  199  PRO A N   
2109  C CA  . PRO B 202  ? 0.4623 0.6690 0.5367 0.0565  0.0034  0.0905  199  PRO A CA  
2110  C C   . PRO B 202  ? 0.4715 0.6594 0.5419 0.0561  0.0044  0.0842  199  PRO A C   
2111  O O   . PRO B 202  ? 0.4634 0.6705 0.5390 0.0481  0.0059  0.0861  199  PRO A O   
2112  C CB  . PRO B 202  ? 0.4208 0.6119 0.4997 0.0377  0.0012  0.0917  199  PRO A CB  
2113  C CG  . PRO B 202  ? 0.4140 0.6054 0.4911 0.0458  -0.0001 0.0943  199  PRO A CG  
2114  C CD  . PRO B 202  ? 0.4528 0.6292 0.5180 0.0682  -0.0002 0.0901  199  PRO A CD  
2115  N N   . LYS B 203  ? 0.4589 0.6095 0.5191 0.0634  0.0029  0.0775  200  LYS A N   
2116  C CA  . LYS B 203  ? 0.4645 0.5984 0.5196 0.0652  0.0035  0.0715  200  LYS A CA  
2117  C C   . LYS B 203  ? 0.5163 0.6699 0.5657 0.0844  0.0053  0.0708  200  LYS A C   
2118  O O   . LYS B 203  ? 0.5273 0.6936 0.5797 0.0822  0.0074  0.0700  200  LYS A O   
2119  C CB  . LYS B 203  ? 0.4723 0.5624 0.5166 0.0663  0.0003  0.0655  200  LYS A CB  
2120  C CG  . LYS B 203  ? 0.4817 0.5555 0.5313 0.0483  -0.0012 0.0661  200  LYS A CG  
2121  C CD  . LYS B 203  ? 0.4925 0.5283 0.5312 0.0483  -0.0047 0.0619  200  LYS A CD  
2122  C CE  . LYS B 203  ? 0.5038 0.5298 0.5480 0.0321  -0.0059 0.0636  200  LYS A CE  
2123  N NZ  . LYS B 203  ? 0.5314 0.5678 0.5851 0.0185  -0.0036 0.0632  200  LYS A NZ  
2124  N N   . PHE B 204  ? 0.5423 0.6989 0.5821 0.1045  0.0043  0.0713  201  PHE A N   
2125  C CA  . PHE B 204  ? 0.5140 0.6917 0.5460 0.1266  0.0059  0.0707  201  PHE A CA  
2126  C C   . PHE B 204  ? 0.4966 0.7293 0.5428 0.1225  0.0098  0.0785  201  PHE A C   
2127  O O   . PHE B 204  ? 0.4829 0.7367 0.5286 0.1300  0.0122  0.0783  201  PHE A O   
2128  C CB  . PHE B 204  ? 0.4955 0.6629 0.5108 0.1509  0.0033  0.0695  201  PHE A CB  
2129  C CG  . PHE B 204  ? 0.5260 0.7175 0.5305 0.1777  0.0048  0.0690  201  PHE A CG  
2130  C CD1 . PHE B 204  ? 0.5620 0.7276 0.5492 0.1925  0.0032  0.0616  201  PHE A CD1 
2131  C CD2 . PHE B 204  ? 0.5284 0.7704 0.5391 0.1888  0.0076  0.0763  201  PHE A CD2 
2132  C CE1 . PHE B 204  ? 0.5701 0.7583 0.5454 0.2196  0.0045  0.0608  201  PHE A CE1 
2133  C CE2 . PHE B 204  ? 0.5268 0.7958 0.5271 0.2157  0.0092  0.0762  201  PHE A CE2 
2134  C CZ  . PHE B 204  ? 0.5453 0.7866 0.5273 0.2321  0.0077  0.0682  201  PHE A CZ  
2135  N N   . LYS B 205  ? 0.5020 0.7589 0.5599 0.1099  0.0099  0.0858  202  LYS A N   
2136  C CA  . LYS B 205  ? 0.5068 0.8160 0.5773 0.1012  0.0123  0.0947  202  LYS A CA  
2137  C C   . LYS B 205  ? 0.5163 0.8267 0.5934 0.0817  0.0132  0.0949  202  LYS A C   
2138  O O   . LYS B 205  ? 0.5155 0.8630 0.5970 0.0813  0.0153  0.0998  202  LYS A O   
2139  C CB  . LYS B 205  ? 0.4859 0.8131 0.5654 0.0881  0.0108  0.1021  202  LYS A CB  
2140  C CG  . LYS B 205  ? 0.4419 0.8156 0.5335 0.0700  0.0113  0.1122  202  LYS A CG  
2141  C CD  . LYS B 205  ? 0.4019 0.7863 0.4999 0.0563  0.0087  0.1187  202  LYS A CD  
2142  C CE  . LYS B 205  ? 0.4062 0.8227 0.5126 0.0309  0.0070  0.1280  202  LYS A CE  
2143  N NZ  . LYS B 205  ? 0.4304 0.9036 0.5413 0.0362  0.0091  0.1363  202  LYS A NZ  
2144  N N   . GLU B 206  ? 0.5203 0.7915 0.5972 0.0660  0.0114  0.0899  203  GLU A N   
2145  C CA  . GLU B 206  ? 0.5017 0.7682 0.5816 0.0500  0.0119  0.0890  203  GLU A CA  
2146  C C   . GLU B 206  ? 0.4962 0.7581 0.5698 0.0641  0.0140  0.0834  203  GLU A C   
2147  O O   . GLU B 206  ? 0.4859 0.7655 0.5627 0.0568  0.0155  0.0856  203  GLU A O   
2148  C CB  . GLU B 206  ? 0.5104 0.7371 0.5895 0.0339  0.0095  0.0846  203  GLU A CB  
2149  C CG  . GLU B 206  ? 0.5481 0.7636 0.6271 0.0200  0.0096  0.0823  203  GLU A CG  
2150  C CD  . GLU B 206  ? 0.5982 0.8425 0.6816 0.0029  0.0087  0.0905  203  GLU A CD  
2151  O OE1 . GLU B 206  ? 0.6310 0.8999 0.7186 -0.0032 0.0073  0.0981  203  GLU A OE1 
2152  O OE2 . GLU B 206  ? 0.6127 0.8543 0.6942 -0.0055 0.0089  0.0898  203  GLU A OE2 
2153  N N   . ASN B 207  ? 0.5317 0.7684 0.5942 0.0838  0.0135  0.0764  204  ASN A N   
2154  C CA  . ASN B 207  ? 0.5357 0.7649 0.5893 0.0986  0.0147  0.0705  204  ASN A CA  
2155  C C   . ASN B 207  ? 0.5313 0.8088 0.5868 0.1116  0.0178  0.0759  204  ASN A C   
2156  O O   . ASN B 207  ? 0.5369 0.8239 0.5918 0.1133  0.0198  0.0746  204  ASN A O   
2157  C CB  . ASN B 207  ? 0.5598 0.7500 0.5969 0.1171  0.0119  0.0628  204  ASN A CB  
2158  C CG  . ASN B 207  ? 0.5645 0.7081 0.5985 0.1036  0.0089  0.0570  204  ASN A CG  
2159  O OD1 . ASN B 207  ? 0.5842 0.7254 0.6286 0.0828  0.0093  0.0584  204  ASN A OD1 
2160  N ND2 . ASN B 207  ? 0.5328 0.6395 0.5506 0.1155  0.0052  0.0509  204  ASN A ND2 
2161  N N   . CYS B 208  ? 0.5342 0.8452 0.5918 0.1212  0.0184  0.0823  205  CYS A N   
2162  C CA  . CYS B 208  ? 0.5421 0.9073 0.6024 0.1337  0.0215  0.0889  205  CYS A CA  
2163  C C   . CYS B 208  ? 0.5600 0.9600 0.6340 0.1099  0.0230  0.0972  205  CYS A C   
2164  O O   . CYS B 208  ? 0.5906 1.0254 0.6657 0.1160  0.0256  0.1007  205  CYS A O   
2165  C CB  . CYS B 208  ? 0.5632 0.9598 0.6233 0.1479  0.0216  0.0949  205  CYS A CB  
2166  S SG  . CYS B 208  ? 0.6113 0.9636 0.6511 0.1755  0.0185  0.0861  205  CYS A SG  
2167  N N   . HIS B 209  ? 0.5374 0.9273 0.6196 0.0830  0.0207  0.1008  206  HIS A N   
2168  C CA  . HIS B 209  ? 0.5075 0.9229 0.5981 0.0586  0.0204  0.1088  206  HIS A CA  
2169  C C   . HIS B 209  ? 0.5217 0.9122 0.6088 0.0519  0.0210  0.1030  206  HIS A C   
2170  O O   . HIS B 209  ? 0.5303 0.9491 0.6202 0.0436  0.0220  0.1087  206  HIS A O   
2171  C CB  . HIS B 209  ? 0.5125 0.9191 0.6081 0.0337  0.0166  0.1136  206  HIS A CB  
2172  C CG  . HIS B 209  ? 0.5734 1.0036 0.6730 0.0074  0.0143  0.1231  206  HIS A CG  
2173  N ND1 . HIS B 209  ? 0.6224 1.0188 0.7181 -0.0140 0.0112  0.1209  206  HIS A ND1 
2174  C CD2 . HIS B 209  ? 0.6223 1.1060 0.7272 -0.0015 0.0140  0.1352  206  HIS A CD2 
2175  C CE1 . HIS B 209  ? 0.6563 1.0792 0.7526 -0.0352 0.0084  0.1310  206  HIS A CE1 
2176  N NE2 . HIS B 209  ? 0.6511 1.1284 0.7538 -0.0296 0.0100  0.1403  206  HIS A NE2 
2177  N N   . ILE B 210  ? 0.5034 0.8427 0.5841 0.0548  0.0201  0.0925  207  ILE A N   
2178  C CA  . ILE B 210  ? 0.5284 0.8442 0.6053 0.0511  0.0207  0.0863  207  ILE A CA  
2179  C C   . ILE B 210  ? 0.5511 0.8870 0.6236 0.0717  0.0239  0.0844  207  ILE A C   
2180  O O   . ILE B 210  ? 0.5322 0.8757 0.6049 0.0665  0.0252  0.0848  207  ILE A O   
2181  C CB  . ILE B 210  ? 0.5332 0.7950 0.6042 0.0510  0.0188  0.0762  207  ILE A CB  
2182  C CG1 . ILE B 210  ? 0.5416 0.7864 0.6162 0.0314  0.0159  0.0783  207  ILE A CG1 
2183  C CG2 . ILE B 210  ? 0.5161 0.7559 0.5827 0.0490  0.0195  0.0697  207  ILE A CG2 
2184  C CD1 . ILE B 210  ? 0.5455 0.7445 0.6152 0.0309  0.0142  0.0699  207  ILE A CD1 
2185  N N   . PHE B 211  ? 0.5844 0.9286 0.6509 0.0966  0.0248  0.0824  208  PHE A N   
2186  C CA  . PHE B 211  ? 0.5965 0.9571 0.6551 0.1205  0.0273  0.0797  208  PHE A CA  
2187  C C   . PHE B 211  ? 0.6444 1.0649 0.7112 0.1172  0.0303  0.0902  208  PHE A C   
2188  O O   . PHE B 211  ? 0.6801 1.1100 0.7458 0.1181  0.0322  0.0895  208  PHE A O   
2189  C CB  . PHE B 211  ? 0.5768 0.9312 0.6232 0.1491  0.0266  0.0756  208  PHE A CB  
2190  C CG  . PHE B 211  ? 0.5839 0.9579 0.6186 0.1778  0.0286  0.0731  208  PHE A CG  
2191  C CD1 . PHE B 211  ? 0.6019 0.9385 0.6223 0.1900  0.0275  0.0629  208  PHE A CD1 
2192  C CD2 . PHE B 211  ? 0.5827 1.0139 0.6195 0.1934  0.0313  0.0812  208  PHE A CD2 
2193  C CE1 . PHE B 211  ? 0.6261 0.9784 0.6330 0.2182  0.0288  0.0600  208  PHE A CE1 
2194  C CE2 . PHE B 211  ? 0.5937 1.0448 0.6179 0.2226  0.0333  0.0788  208  PHE A CE2 
2195  C CZ  . PHE B 211  ? 0.6155 1.0251 0.6239 0.2355  0.0319  0.0678  208  PHE A CZ  
2196  N N   . THR B 212  ? 0.6500 1.1136 0.7251 0.1124  0.0305  0.1007  209  THR A N   
2197  C CA  . THR B 212  ? 0.6400 1.1675 0.7223 0.1097  0.0329  0.1124  209  THR A CA  
2198  C C   . THR B 212  ? 0.6117 1.1438 0.7005 0.0796  0.0319  0.1181  209  THR A C   
2199  O O   . THR B 212  ? 0.6331 1.2065 0.7245 0.0784  0.0340  0.1250  209  THR A O   
2200  C CB  . THR B 212  ? 0.6514 1.2248 0.7410 0.1089  0.0326  0.1231  209  THR A CB  
2201  O OG1 . THR B 212  ? 0.6803 1.2360 0.7765 0.0806  0.0288  0.1268  209  THR A OG1 
2202  C CG2 . THR B 212  ? 0.6622 1.2296 0.7425 0.1409  0.0332  0.1174  209  THR A CG2 
2203  N N   . ARG B 213  ? 0.5832 1.0738 0.6730 0.0560  0.0284  0.1156  210  ARG A N   
2204  C CA  . ARG B 213  ? 0.5982 1.0856 0.6893 0.0292  0.0265  0.1201  210  ARG A CA  
2205  C C   . ARG B 213  ? 0.6275 1.0961 0.7130 0.0369  0.0287  0.1126  210  ARG A C   
2206  O O   . ARG B 213  ? 0.6534 1.1437 0.7396 0.0248  0.0290  0.1187  210  ARG A O   
2207  C CB  . ARG B 213  ? 0.6041 1.0487 0.6938 0.0063  0.0218  0.1182  210  ARG A CB  
2208  C CG  . ARG B 213  ? 0.6569 1.1233 0.7512 -0.0096 0.0183  0.1282  210  ARG A CG  
2209  C CD  . ARG B 213  ? 0.7091 1.1373 0.7984 -0.0358 0.0128  0.1281  210  ARG A CD  
2210  N NE  . ARG B 213  ? 0.7602 1.1883 0.8439 -0.0562 0.0103  0.1329  210  ARG A NE  
2211  C CZ  . ARG B 213  ? 0.7981 1.1905 0.8724 -0.0777 0.0049  0.1326  210  ARG A CZ  
2212  N NH1 . ARG B 213  ? 0.8019 1.1590 0.8729 -0.0813 0.0020  0.1277  210  ARG A NH1 
2213  N NH2 . ARG B 213  ? 0.8071 1.1986 0.8735 -0.0948 0.0020  0.1372  210  ARG A NH2 
2214  N N   . LEU B 214  ? 0.5960 1.0239 0.6749 0.0557  0.0298  0.0997  211  LEU A N   
2215  C CA  . LEU B 214  ? 0.5509 0.9604 0.6237 0.0641  0.0316  0.0921  211  LEU A CA  
2216  C C   . LEU B 214  ? 0.5675 1.0214 0.6389 0.0846  0.0355  0.0952  211  LEU A C   
2217  O O   . LEU B 214  ? 0.5617 1.0274 0.6324 0.0814  0.0371  0.0964  211  LEU A O   
2218  C CB  . LEU B 214  ? 0.5060 0.8613 0.5706 0.0772  0.0307  0.0785  211  LEU A CB  
2219  C CG  . LEU B 214  ? 0.4638 0.7738 0.5286 0.0589  0.0274  0.0741  211  LEU A CG  
2220  C CD1 . LEU B 214  ? 0.4434 0.7082 0.4999 0.0726  0.0262  0.0625  211  LEU A CD1 
2221  C CD2 . LEU B 214  ? 0.4326 0.7324 0.4978 0.0383  0.0265  0.0752  211  LEU A CD2 
2222  N N   . ILE B 215  ? 0.5902 1.0699 0.6600 0.1071  0.0369  0.0965  212  ILE A N   
2223  C CA  . ILE B 215  ? 0.6210 1.1439 0.6870 0.1316  0.0405  0.0987  212  ILE A CA  
2224  C C   . ILE B 215  ? 0.6326 1.2182 0.7088 0.1160  0.0422  0.1135  212  ILE A C   
2225  O O   . ILE B 215  ? 0.6730 1.2904 0.7475 0.1263  0.0453  0.1159  212  ILE A O   
2226  C CB  . ILE B 215  ? 0.6564 1.1901 0.7150 0.1613  0.0410  0.0965  212  ILE A CB  
2227  C CG1 . ILE B 215  ? 0.6781 1.1455 0.7237 0.1737  0.0380  0.0827  212  ILE A CG1 
2228  C CG2 . ILE B 215  ? 0.6796 1.2583 0.7312 0.1906  0.0446  0.0983  212  ILE A CG2 
2229  C CD1 . ILE B 215  ? 0.6671 1.0913 0.7027 0.1778  0.0374  0.0717  212  ILE A CD1 
2230  N N   . THR B 216  ? 0.6208 1.2255 0.7066 0.0902  0.0398  0.1242  213  THR A N   
2231  C CA  . THR B 216  ? 0.6242 1.2873 0.7179 0.0710  0.0399  0.1398  213  THR A CA  
2232  C C   . THR B 216  ? 0.6234 1.2699 0.7155 0.0495  0.0388  0.1405  213  THR A C   
2233  O O   . THR B 216  ? 0.6384 1.3282 0.7321 0.0470  0.0407  0.1488  213  THR A O   
2234  C CB  . THR B 216  ? 0.6141 1.2970 0.7154 0.0475  0.0361  0.1509  213  THR A CB  
2235  O OG1 . THR B 216  ? 0.6093 1.3093 0.7119 0.0693  0.0374  0.1503  213  THR A OG1 
2236  C CG2 . THR B 216  ? 0.6144 1.3599 0.7221 0.0252  0.0350  0.1686  213  THR A CG2 
2237  N N   . ALA B 217  ? 0.6241 1.2094 0.7119 0.0347  0.0356  0.1321  214  ALA A N   
2238  C CA  . ALA B 217  ? 0.6442 1.2090 0.7280 0.0160  0.0342  0.1319  214  ALA A CA  
2239  C C   . ALA B 217  ? 0.6529 1.2069 0.7315 0.0378  0.0382  0.1223  214  ALA A C   
2240  O O   . ALA B 217  ? 0.6781 1.2540 0.7557 0.0320  0.0394  0.1273  214  ALA A O   
2241  C CB  . ALA B 217  ? 0.6342 1.1393 0.7133 -0.0037 0.0295  0.1259  214  ALA A CB  
2242  N N   . VAL B 218  ? 0.6221 1.1413 0.6957 0.0621  0.0397  0.1089  215  VAL A N   
2243  C CA  . VAL B 218  ? 0.5938 1.0976 0.6597 0.0837  0.0425  0.0988  215  VAL A CA  
2244  C C   . VAL B 218  ? 0.6144 1.1383 0.6755 0.1178  0.0452  0.0952  215  VAL A C   
2245  O O   . VAL B 218  ? 0.6140 1.0993 0.6677 0.1334  0.0438  0.0849  215  VAL A O   
2246  C CB  . VAL B 218  ? 0.5645 1.0018 0.6242 0.0807  0.0404  0.0855  215  VAL A CB  
2247  C CG1 . VAL B 218  ? 0.5695 0.9923 0.6207 0.0992  0.0425  0.0761  215  VAL A CG1 
2248  C CG2 . VAL B 218  ? 0.5322 0.9484 0.5940 0.0495  0.0372  0.0891  215  VAL A CG2 
2249  N N   . PRO B 219  ? 0.6378 1.2212 0.7006 0.1308  0.0485  0.1036  216  PRO A N   
2250  C CA  . PRO B 219  ? 0.6686 1.2721 0.7233 0.1666  0.0506  0.1001  216  PRO A CA  
2251  C C   . PRO B 219  ? 0.6950 1.2542 0.7331 0.1935  0.0505  0.0848  216  PRO A C   
2252  O O   . PRO B 219  ? 0.7217 1.2703 0.7474 0.2216  0.0498  0.0783  216  PRO A O   
2253  C CB  . PRO B 219  ? 0.6628 1.3443 0.7232 0.1719  0.0544  0.1136  216  PRO A CB  
2254  C CG  . PRO B 219  ? 0.6503 1.3542 0.7239 0.1329  0.0528  0.1268  216  PRO A CG  
2255  C CD  . PRO B 219  ? 0.6413 1.2798 0.7125 0.1122  0.0498  0.1182  216  PRO A CD  
2256  N N   . SER B 220  ? 0.7064 1.2378 0.7418 0.1857  0.0505  0.0790  217  SER A N   
2257  C CA  . SER B 220  ? 0.7197 1.2060 0.7382 0.2083  0.0493  0.0646  217  SER A CA  
2258  C C   . SER B 220  ? 0.7684 1.1936 0.7787 0.2099  0.0447  0.0542  217  SER A C   
2259  O O   . SER B 220  ? 0.8013 1.1907 0.7934 0.2326  0.0423  0.0431  217  SER A O   
2260  C CB  . SER B 220  ? 0.6810 1.1502 0.6999 0.1957  0.0499  0.0612  217  SER A CB  
2261  O OG  . SER B 220  ? 0.6580 1.0964 0.6861 0.1643  0.0477  0.0617  217  SER A OG  
2262  N N   . LEU B 221  ? 0.7720 1.1839 0.7933 0.1859  0.0429  0.0578  218  LEU A N   
2263  C CA  . LEU B 221  ? 0.7629 1.1219 0.7778 0.1853  0.0387  0.0497  218  LEU A CA  
2264  C C   . LEU B 221  ? 0.7610 1.1226 0.7647 0.2110  0.0373  0.0481  218  LEU A C   
2265  O O   . LEU B 221  ? 0.7431 1.0571 0.7354 0.2167  0.0331  0.0400  218  LEU A O   
2266  C CB  . LEU B 221  ? 0.7298 1.0795 0.7591 0.1541  0.0373  0.0549  218  LEU A CB  
2267  C CG  . LEU B 221  ? 0.7290 1.0226 0.7565 0.1387  0.0341  0.0466  218  LEU A CG  
2268  C CD1 . LEU B 221  ? 0.7329 1.0083 0.7543 0.1404  0.0346  0.0398  218  LEU A CD1 
2269  C CD2 . LEU B 221  ? 0.7206 1.0155 0.7611 0.1094  0.0334  0.0534  218  LEU A CD2 
2270  N N   . ARG B 222  ? 0.7766 1.1938 0.7823 0.2264  0.0404  0.0562  219  ARG A N   
2271  C CA  . ARG B 222  ? 0.7973 1.2197 0.7902 0.2539  0.0391  0.0548  219  ARG A CA  
2272  C C   . ARG B 222  ? 0.8311 1.2159 0.7970 0.2855  0.0362  0.0425  219  ARG A C   
2273  O O   . ARG B 222  ? 0.8478 1.1859 0.7969 0.2968  0.0312  0.0348  219  ARG A O   
2274  C CB  . ARG B 222  ? 0.7834 1.2813 0.7850 0.2634  0.0435  0.0673  219  ARG A CB  
2275  C CG  . ARG B 222  ? 0.8134 1.3241 0.8027 0.2923  0.0425  0.0674  219  ARG A CG  
2276  C CD  . ARG B 222  ? 0.8747 1.3931 0.8404 0.3334  0.0428  0.0613  219  ARG A CD  
2277  N NE  . ARG B 222  ? 0.9330 1.4427 0.8794 0.3637  0.0401  0.0580  219  ARG A NE  
2278  C CZ  . ARG B 222  ? 0.9948 1.4947 0.9129 0.4033  0.0382  0.0503  219  ARG A CZ  
2279  N NH1 . ARG B 222  ? 1.0152 1.5140 0.9222 0.4170  0.0391  0.0452  219  ARG A NH1 
2280  N NH2 . ARG B 222  ? 1.0270 1.5159 0.9255 0.4302  0.0350  0.0476  219  ARG A NH2 
2281  N N   . GLU B 223  ? 0.8491 1.2525 0.8083 0.2999  0.0385  0.0408  220  GLU A N   
2282  C CA  . GLU B 223  ? 0.8956 1.2601 0.8261 0.3297  0.0348  0.0286  220  GLU A CA  
2283  C C   . GLU B 223  ? 0.9260 1.2171 0.8473 0.3157  0.0290  0.0178  220  GLU A C   
2284  O O   . GLU B 223  ? 0.9689 1.2115 0.8632 0.3355  0.0230  0.0077  220  GLU A O   
2285  C CB  . GLU B 223  ? 0.9045 1.3050 0.8313 0.3451  0.0387  0.0293  220  GLU A CB  
2286  N N   . HIS B 224  ? 0.9151 1.1970 0.8567 0.2818  0.0302  0.0201  221  HIS A N   
2287  C CA  . HIS B 224  ? 0.9368 1.1564 0.8719 0.2672  0.0251  0.0111  221  HIS A CA  
2288  C C   . HIS B 224  ? 0.9266 1.1075 0.8546 0.2641  0.0198  0.0087  221  HIS A C   
2289  O O   . HIS B 224  ? 0.9317 1.0582 0.8399 0.2686  0.0133  -0.0002 221  HIS A O   
2290  C CB  . HIS B 224  ? 0.9439 1.1685 0.9012 0.2346  0.0279  0.0147  221  HIS A CB  
2291  C CG  . HIS B 224  ? 0.9943 1.1685 0.9440 0.2247  0.0241  0.0055  221  HIS A CG  
2292  N ND1 . HIS B 224  ? 0.9916 1.1699 0.9520 0.2076  0.0266  0.0057  221  HIS A ND1 
2293  C CD2 . HIS B 224  ? 1.0268 1.1465 0.9584 0.2286  0.0175  -0.0036 221  HIS A CD2 
2294  C CE1 . HIS B 224  ? 0.9986 1.1302 0.9493 0.2025  0.0222  -0.0030 221  HIS A CE1 
2295  N NE2 . HIS B 224  ? 1.0209 1.1169 0.9542 0.2138  0.0164  -0.0084 221  HIS A NE2 
2296  N N   . PHE B 225  ? 0.8888 1.0969 0.8320 0.2552  0.0220  0.0171  222  PHE A N   
2297  C CA  . PHE B 225  ? 0.8589 1.0346 0.7948 0.2547  0.0173  0.0156  222  PHE A CA  
2298  C C   . PHE B 225  ? 0.8877 1.0435 0.7936 0.2888  0.0127  0.0098  222  PHE A C   
2299  O O   . PHE B 225  ? 0.8827 0.9866 0.7700 0.2916  0.0058  0.0038  222  PHE A O   
2300  C CB  . PHE B 225  ? 0.7948 1.0081 0.7523 0.2400  0.0208  0.0261  222  PHE A CB  
2301  C CG  . PHE B 225  ? 0.7370 0.9545 0.7178 0.2057  0.0229  0.0307  222  PHE A CG  
2302  C CD1 . PHE B 225  ? 0.7350 0.9127 0.7153 0.1895  0.0206  0.0245  222  PHE A CD1 
2303  C CD2 . PHE B 225  ? 0.6919 0.9524 0.6925 0.1901  0.0264  0.0413  222  PHE A CD2 
2304  C CE1 . PHE B 225  ? 0.6810 0.8615 0.6793 0.1612  0.0223  0.0283  222  PHE A CE1 
2305  C CE2 . PHE B 225  ? 0.6508 0.9099 0.6678 0.1602  0.0272  0.0451  222  PHE A CE2 
2306  C CZ  . PHE B 225  ? 0.6427 0.8613 0.6578 0.1471  0.0253  0.0383  222  PHE A CZ  
2307  N N   . GLU B 226  ? 0.9329 1.1297 0.8319 0.3154  0.0159  0.0120  223  GLU A N   
2308  C CA  . GLU B 226  ? 1.0066 1.1856 0.8732 0.3523  0.0113  0.0063  223  GLU A CA  
2309  C C   . GLU B 226  ? 1.0519 1.1677 0.8883 0.3628  0.0038  -0.0059 223  GLU A C   
2310  O O   . GLU B 226  ? 1.0866 1.1551 0.8919 0.3811  -0.0041 -0.0125 223  GLU A O   
2311  C CB  . GLU B 226  ? 1.0403 1.2830 0.9064 0.3793  0.0169  0.0116  223  GLU A CB  
2312  C CG  . GLU B 226  ? 1.1251 1.3533 0.9544 0.4227  0.0123  0.0054  223  GLU A CG  
2313  C CD  . GLU B 226  ? 1.1754 1.4079 0.9986 0.4345  0.0105  0.0090  223  GLU A CD  
2314  O OE1 . GLU B 226  ? 1.1557 1.4416 1.0066 0.4209  0.0163  0.0200  223  GLU A OE1 
2315  O OE2 . GLU B 226  ? 1.2335 1.4145 1.0226 0.4569  0.0027  0.0012  223  GLU A OE2 
2316  N N   . ASN B 227  ? 1.0802 1.1926 0.9233 0.3508  0.0054  -0.0089 224  ASN A N   
2317  C CA  . ASN B 227  ? 1.1182 1.1718 0.9331 0.3581  -0.0022 -0.0202 224  ASN A CA  
2318  C C   . ASN B 227  ? 1.1034 1.0962 0.9115 0.3365  -0.0099 -0.0241 224  ASN A C   
2319  O O   . ASN B 227  ? 1.1594 1.0952 0.9342 0.3479  -0.0194 -0.0324 224  ASN A O   
2320  C CB  . ASN B 227  ? 1.1257 1.1940 0.9520 0.3484  0.0017  -0.0217 224  ASN A CB  
2321  C CG  . ASN B 227  ? 1.1424 1.2684 0.9711 0.3715  0.0084  -0.0180 224  ASN A CG  
2322  O OD1 . ASN B 227  ? 1.1194 1.2850 0.9712 0.3574  0.0150  -0.0130 224  ASN A OD1 
2323  N ND2 . ASN B 227  ? 1.1758 1.3076 0.9790 0.4076  0.0063  -0.0202 224  ASN A ND2 
2324  N N   . VAL B 228  ? 1.0299 1.0336 0.8673 0.3051  -0.0066 -0.0179 225  VAL A N   
2325  C CA  . VAL B 228  ? 1.0035 0.9570 0.8367 0.2839  -0.0132 -0.0203 225  VAL A CA  
2326  C C   . VAL B 228  ? 1.0070 0.9305 0.8163 0.2994  -0.0199 -0.0212 225  VAL A C   
2327  O O   . VAL B 228  ? 1.0291 0.8952 0.8143 0.2962  -0.0294 -0.0264 225  VAL A O   
2328  C CB  . VAL B 228  ? 0.9383 0.9150 0.8071 0.2504  -0.0077 -0.0131 225  VAL A CB  
2329  C CG1 . VAL B 228  ? 0.9234 0.8543 0.7884 0.2297  -0.0141 -0.0146 225  VAL A CG1 
2330  C CG2 . VAL B 228  ? 0.9026 0.9023 0.7901 0.2361  -0.0022 -0.0127 225  VAL A CG2 
2331  N N   . LYS B 229  ? 0.9800 0.9423 0.7943 0.3160  -0.0156 -0.0156 226  LYS A N   
2332  C CA  . LYS B 229  ? 0.9891 0.9251 0.7796 0.3333  -0.0217 -0.0163 226  LYS A CA  
2333  C C   . LYS B 229  ? 1.0678 0.9599 0.8128 0.3658  -0.0305 -0.0254 226  LYS A C   
2334  O O   . LYS B 229  ? 1.1030 0.9389 0.8178 0.3709  -0.0405 -0.0295 226  LYS A O   
2335  C CB  . LYS B 229  ? 0.9350 0.9287 0.7423 0.3445  -0.0147 -0.0078 226  LYS A CB  
2336  C CG  . LYS B 229  ? 0.9312 0.9029 0.7242 0.3525  -0.0197 -0.0063 226  LYS A CG  
2337  C CD  . LYS B 229  ? 0.9313 0.9446 0.7159 0.3857  -0.0166 -0.0029 226  LYS A CD  
2338  C CE  . LYS B 229  ? 1.0024 0.9975 0.7490 0.4237  -0.0211 -0.0109 226  LYS A CE  
2339  N NZ  . LYS B 229  ? 1.0439 1.0789 0.7785 0.4600  -0.0187 -0.0078 226  LYS A NZ  
2340  N N   . LYS B 230  ? 1.1125 1.0277 0.8496 0.3880  -0.0276 -0.0285 227  LYS A N   
2341  C CA  . LYS B 230  ? 1.1958 1.0686 0.8864 0.4216  -0.0363 -0.0378 227  LYS A CA  
2342  C C   . LYS B 230  ? 1.2436 1.0481 0.9115 0.4076  -0.0463 -0.0462 227  LYS A C   
2343  O O   . LYS B 230  ? 1.2566 1.0010 0.8798 0.4257  -0.0580 -0.0535 227  LYS A O   
2344  C CB  . LYS B 230  ? 1.2068 1.1289 0.8964 0.4500  -0.0298 -0.0383 227  LYS A CB  
2345  C CG  . LYS B 230  ? 1.2055 1.1941 0.9077 0.4712  -0.0219 -0.0303 227  LYS A CG  
2346  C CD  . LYS B 230  ? 1.2158 1.2541 0.9143 0.4999  -0.0161 -0.0303 227  LYS A CD  
2347  C CE  . LYS B 230  ? 1.2099 1.3164 0.9168 0.5237  -0.0093 -0.0219 227  LYS A CE  
2348  N NZ  . LYS B 230  ? 1.2061 1.3653 0.9085 0.5473  -0.0038 -0.0206 227  LYS A NZ  
2349  N N   . ALA B 231  ? 1.2949 1.1067 0.9906 0.3757  -0.0427 -0.0450 228  ALA A N   
2350  C CA  . ALA B 231  ? 1.3075 1.0617 0.9843 0.3607  -0.0518 -0.0520 228  ALA A CA  
2351  C C   . ALA B 231  ? 1.3327 1.0310 0.9948 0.3411  -0.0619 -0.0520 228  ALA A C   
2352  O O   . ALA B 231  ? 1.3761 1.0166 1.0096 0.3344  -0.0730 -0.0579 228  ALA A O   
2353  C CB  . ALA B 231  ? 1.2517 1.0341 0.9631 0.3332  -0.0446 -0.0501 228  ALA A CB  
2354  N N   . ILE B 232  ? 1.3056 1.0202 0.9858 0.3309  -0.0588 -0.0449 229  ILE A N   
2355  C CA  . ILE B 232  ? 1.3135 0.9791 0.9807 0.3120  -0.0681 -0.0437 229  ILE A CA  
2356  C C   . ILE B 232  ? 1.3850 1.0082 1.0089 0.3394  -0.0779 -0.0466 229  ILE A C   
2357  O O   . ILE B 232  ? 1.4576 1.0155 1.0463 0.3342  -0.0911 -0.0501 229  ILE A O   
2358  C CB  . ILE B 232  ? 1.2267 0.9295 0.9361 0.2842  -0.0600 -0.0346 229  ILE A CB  
2359  C CG1 . ILE B 232  ? 1.1765 0.9113 0.9223 0.2573  -0.0522 -0.0325 229  ILE A CG1 
2360  C CG2 . ILE B 232  ? 1.2338 0.8907 0.9298 0.2664  -0.0691 -0.0325 229  ILE A CG2 
2361  C CD1 . ILE B 232  ? 1.1060 0.8709 0.8886 0.2300  -0.0457 -0.0244 229  ILE A CD1 
2362  N N   . GLY B 233  ? 1.3561 1.0155 0.9798 0.3686  -0.0722 -0.0447 230  GLY A N   
2363  C CA  . GLY B 233  ? 1.3962 1.0205 0.9786 0.3986  -0.0807 -0.0473 230  GLY A CA  
2364  C C   . GLY B 233  ? 1.3803 1.0231 0.9768 0.3955  -0.0777 -0.0398 230  GLY A C   
2365  O O   . GLY B 233  ? 1.4423 1.0510 1.0030 0.4186  -0.0856 -0.0416 230  GLY A O   
2366  N N   . ILE B 234  ? 1.3061 0.9995 0.9509 0.3689  -0.0672 -0.0318 231  ILE A N   
2367  C CA  . ILE B 234  ? 1.2826 0.9964 0.9439 0.3632  -0.0640 -0.0243 231  ILE A CA  
2368  C C   . ILE B 234  ? 1.2776 1.0556 0.9523 0.3899  -0.0545 -0.0203 231  ILE A C   
2369  O O   . ILE B 234  ? 1.2549 1.0842 0.9514 0.3941  -0.0456 -0.0191 231  ILE A O   
2370  C CB  . ILE B 234  ? 1.2101 0.9447 0.9139 0.3216  -0.0583 -0.0177 231  ILE A CB  
2371  C CG1 . ILE B 234  ? 1.2107 0.8893 0.9022 0.2952  -0.0674 -0.0209 231  ILE A CG1 
2372  C CG2 . ILE B 234  ? 1.2012 0.9535 0.9200 0.3155  -0.0557 -0.0103 231  ILE A CG2 
2373  C CD1 . ILE B 234  ? 1.1526 0.8529 0.8834 0.2571  -0.0618 -0.0150 231  ILE A CD1 
2374  N N   . PHE B 235  ? 1.2936 1.0703 0.9546 0.4078  -0.0566 -0.0177 232  PHE A N   
2375  C CA  . PHE B 235  ? 1.2790 1.1204 0.9536 0.4315  -0.0480 -0.0123 232  PHE A CA  
2376  C C   . PHE B 235  ? 1.3336 1.1993 0.9911 0.4667  -0.0459 -0.0167 232  PHE A C   
2377  O O   . PHE B 235  ? 1.2906 1.2230 0.9776 0.4674  -0.0355 -0.0121 232  PHE A O   
2378  C CB  . PHE B 235  ? 1.1804 1.0880 0.9087 0.4028  -0.0362 -0.0026 232  PHE A CB  
2379  C CG  . PHE B 235  ? 1.1259 1.0138 0.8721 0.3691  -0.0377 0.0017  232  PHE A CG  
2380  C CD1 . PHE B 235  ? 1.1486 0.9868 0.8687 0.3729  -0.0465 0.0007  232  PHE A CD1 
2381  C CD2 . PHE B 235  ? 1.0594 0.9779 0.8463 0.3345  -0.0306 0.0069  232  PHE A CD2 
2382  C CE1 . PHE B 235  ? 1.1192 0.9428 0.8561 0.3423  -0.0476 0.0051  232  PHE A CE1 
2383  C CE2 . PHE B 235  ? 1.0343 0.9369 0.8364 0.3059  -0.0319 0.0107  232  PHE A CE2 
2384  C CZ  . PHE B 235  ? 1.0605 0.9176 0.8387 0.3095  -0.0400 0.0100  232  PHE A CZ  
2385  N N   . VAL B 236  ? 1.4632 1.2718 1.0699 0.4960  -0.0566 -0.0255 233  VAL A N   
2386  C CA  . VAL B 236  ? 1.4854 1.3094 1.0697 0.5322  -0.0559 -0.0310 233  VAL A CA  
2387  C C   . VAL B 236  ? 1.4767 1.3699 1.0667 0.5599  -0.0478 -0.0256 233  VAL A C   
2388  O O   . VAL B 236  ? 1.4802 1.4238 1.0750 0.5731  -0.0408 -0.0253 233  VAL A O   
2389  C CB  . VAL B 236  ? 1.5477 1.2897 1.0727 0.5478  -0.0702 -0.0422 233  VAL A CB  
2390  C CG1 . VAL B 236  ? 1.5353 1.2175 1.0565 0.5212  -0.0779 -0.0468 233  VAL A CG1 
2391  C CG2 . VAL B 236  ? 1.6083 1.3086 1.0991 0.5566  -0.0787 -0.0430 233  VAL A CG2 
2392  N N   . SER B 237  ? 1.4549 1.3546 1.0447 0.5637  -0.0481 -0.0207 234  SER A N   
2393  C CA  . SER B 237  ? 1.4248 1.3903 1.0185 0.5837  -0.0404 -0.0153 234  SER A CA  
2394  C C   . SER B 237  ? 1.3049 1.3547 0.9551 0.5686  -0.0283 -0.0027 234  SER A C   
2395  O O   . SER B 237  ? 1.2547 1.3625 0.9128 0.5797  -0.0220 0.0038  234  SER A O   
2396  C CB  . SER B 237  ? 1.4878 1.4172 1.0487 0.5969  -0.0473 -0.0169 234  SER A CB  
2397  O OG  . SER B 237  ? 1.4966 1.4921 1.0631 0.6150  -0.0395 -0.0111 234  SER A OG  
2398  N N   . THR B 238  ? 1.2480 1.3051 0.9352 0.5336  -0.0246 0.0006  235  THR A N   
2399  C CA  . THR B 238  ? 1.1477 1.2744 0.8855 0.5046  -0.0141 0.0121  235  THR A CA  
2400  C C   . THR B 238  ? 1.0864 1.2413 0.8511 0.4824  -0.0079 0.0133  235  THR A C   
2401  O O   . THR B 238  ? 1.1349 1.2405 0.8954 0.4640  -0.0119 0.0068  235  THR A O   
2402  C CB  . THR B 238  ? 1.0956 1.1958 0.8511 0.4704  -0.0160 0.0156  235  THR A CB  
2403  O OG1 . THR B 238  ? 1.1194 1.1686 0.8404 0.4894  -0.0247 0.0117  235  THR A OG1 
2404  C CG2 . THR B 238  ? 1.0364 1.2088 0.8337 0.4515  -0.0070 0.0277  235  THR A CG2 
2405  N N   . SER B 239  ? 1.0057 1.2405 0.7974 0.4835  0.0013  0.0221  236  SER A N   
2406  C CA  . SER B 239  ? 0.9625 1.2282 0.7801 0.4616  0.0073  0.0247  236  SER A CA  
2407  C C   . SER B 239  ? 0.9476 1.2077 0.7994 0.4144  0.0094  0.0294  236  SER A C   
2408  O O   . SER B 239  ? 0.9710 1.2116 0.8290 0.3992  0.0072  0.0315  236  SER A O   
2409  C CB  . SER B 239  ? 0.9500 1.3043 0.7841 0.4756  0.0157  0.0342  236  SER A CB  
2410  O OG  . SER B 239  ? 0.9396 1.3472 0.8013 0.4602  0.0203  0.0461  236  SER A OG  
2411  N N   . ILE B 240  ? 0.9317 1.2089 0.8043 0.3922  0.0137  0.0309  237  ILE A N   
2412  C CA  . ILE B 240  ? 0.8960 1.1629 0.7963 0.3500  0.0150  0.0341  237  ILE A CA  
2413  C C   . ILE B 240  ? 0.8839 1.2092 0.8141 0.3316  0.0204  0.0467  237  ILE A C   
2414  O O   . ILE B 240  ? 0.8707 1.1823 0.8180 0.3022  0.0199  0.0496  237  ILE A O   
2415  C CB  . ILE B 240  ? 0.8533 1.1146 0.7624 0.3337  0.0170  0.0311  237  ILE A CB  
2416  C CG1 . ILE B 240  ? 0.8029 1.0381 0.7323 0.2945  0.0165  0.0318  237  ILE A CG1 
2417  C CG2 . ILE B 240  ? 0.8364 1.1685 0.7623 0.3361  0.0242  0.0393  237  ILE A CG2 
2418  C CD1 . ILE B 240  ? 0.7970 0.9666 0.7119 0.2885  0.0094  0.0250  237  ILE A CD1 
2419  N N   . GLU B 241  ? 0.9001 1.2921 0.8361 0.3480  0.0252  0.0548  238  GLU A N   
2420  C CA  . GLU B 241  ? 0.8751 1.3236 0.8372 0.3297  0.0291  0.0676  238  GLU A CA  
2421  C C   . GLU B 241  ? 0.8570 1.2940 0.8136 0.3367  0.0262  0.0687  238  GLU A C   
2422  O O   . GLU B 241  ? 0.8208 1.2753 0.7979 0.3119  0.0271  0.0764  238  GLU A O   
2423  C CB  . GLU B 241  ? 0.9073 1.4359 0.8774 0.3437  0.0347  0.0773  238  GLU A CB  
2424  C CG  . GLU B 241  ? 0.9159 1.4698 0.9001 0.3261  0.0384  0.0806  238  GLU A CG  
2425  C CD  . GLU B 241  ? 0.9468 1.4851 0.9099 0.3532  0.0383  0.0716  238  GLU A CD  
2426  O OE1 . GLU B 241  ? 0.9154 1.4907 0.8877 0.3481  0.0423  0.0759  238  GLU A OE1 
2427  O OE2 . GLU B 241  ? 0.9982 1.4860 0.9338 0.3793  0.0338  0.0605  238  GLU A OE2 
2428  N N   . GLU B 242  ? 0.9109 1.3160 0.8376 0.3702  0.0220  0.0612  239  GLU A N   
2429  C CA  . GLU B 242  ? 0.8978 1.2918 0.8162 0.3798  0.0189  0.0624  239  GLU A CA  
2430  C C   . GLU B 242  ? 0.8856 1.2156 0.8052 0.3544  0.0141  0.0578  239  GLU A C   
2431  O O   . GLU B 242  ? 0.8691 1.2041 0.7987 0.3433  0.0136  0.0629  239  GLU A O   
2432  C CB  . GLU B 242  ? 0.9608 1.3387 0.8424 0.4257  0.0152  0.0558  239  GLU A CB  
2433  C CG  . GLU B 242  ? 1.0000 1.4484 0.8788 0.4558  0.0202  0.0611  239  GLU A CG  
2434  C CD  . GLU B 242  ? 1.0671 1.4948 0.9047 0.5048  0.0157  0.0536  239  GLU A CD  
2435  O OE1 . GLU B 242  ? 1.1101 1.4709 0.9217 0.5136  0.0083  0.0458  239  GLU A OE1 
2436  O OE2 . GLU B 242  ? 1.0812 1.5503 0.9060 0.5250  0.0195  0.0547  239  GLU A OE2 
2437  N N   . VAL B 243  ? 0.8944 1.1670 0.8042 0.3447  0.0104  0.0489  240  VAL A N   
2438  C CA  . VAL B 243  ? 0.8631 1.0815 0.7756 0.3189  0.0061  0.0457  240  VAL A CA  
2439  C C   . VAL B 243  ? 0.8293 1.0752 0.7762 0.2820  0.0104  0.0535  240  VAL A C   
2440  O O   . VAL B 243  ? 0.8422 1.0573 0.7954 0.2611  0.0078  0.0533  240  VAL A O   
2441  C CB  . VAL B 243  ? 0.8074 0.9632 0.7018 0.3156  0.0009  0.0353  240  VAL A CB  
2442  C CG1 . VAL B 243  ? 0.8428 0.9675 0.6986 0.3525  -0.0046 0.0273  240  VAL A CG1 
2443  C CG2 . VAL B 243  ? 0.7549 0.9285 0.6678 0.2971  0.0053  0.0355  240  VAL A CG2 
2444  N N   . PHE B 244  ? 0.7963 1.0985 0.7636 0.2734  0.0162  0.0606  241  PHE A N   
2445  C CA  . PHE B 244  ? 0.7601 1.0918 0.7558 0.2406  0.0192  0.0692  241  PHE A CA  
2446  C C   . PHE B 244  ? 0.7761 1.1708 0.7840 0.2441  0.0222  0.0804  241  PHE A C   
2447  O O   . PHE B 244  ? 0.7873 1.2249 0.8158 0.2224  0.0252  0.0895  241  PHE A O   
2448  C CB  . PHE B 244  ? 0.7055 1.0489 0.7138 0.2219  0.0221  0.0699  241  PHE A CB  
2449  C CG  . PHE B 244  ? 0.6991 0.9844 0.7012 0.2101  0.0193  0.0606  241  PHE A CG  
2450  C CD1 . PHE B 244  ? 0.6780 0.9359 0.6909 0.1824  0.0176  0.0605  241  PHE A CD1 
2451  C CD2 . PHE B 244  ? 0.7248 0.9844 0.7092 0.2271  0.0179  0.0521  241  PHE A CD2 
2452  C CE1 . PHE B 244  ? 0.6647 0.8749 0.6724 0.1719  0.0151  0.0527  241  PHE A CE1 
2453  C CE2 . PHE B 244  ? 0.7222 0.9315 0.7012 0.2151  0.0149  0.0443  241  PHE A CE2 
2454  C CZ  . PHE B 244  ? 0.6869 0.8737 0.6783 0.1873  0.0137  0.0449  241  PHE A CZ  
2455  N N   . SER B 245  ? 0.8033 1.2032 0.7965 0.2713  0.0209  0.0802  242  SER A N   
2456  C CA  . SER B 245  ? 0.8004 1.2564 0.8037 0.2757  0.0230  0.0906  242  SER A CA  
2457  C C   . SER B 245  ? 0.7945 1.2183 0.7912 0.2772  0.0192  0.0890  242  SER A C   
2458  O O   . SER B 245  ? 0.7995 1.1624 0.7764 0.2866  0.0147  0.0798  242  SER A O   
2459  C CB  . SER B 245  ? 0.8780 1.3827 0.8694 0.3116  0.0255  0.0931  242  SER A CB  
2460  O OG  . SER B 245  ? 0.9660 1.4284 0.9266 0.3459  0.0216  0.0835  242  SER A OG  
2461  N N   . PHE B 246  ? 0.7351 1.2004 0.7475 0.2668  0.0205  0.0988  243  PHE A N   
2462  C CA  . PHE B 246  ? 0.6920 1.1303 0.7014 0.2643  0.0172  0.0984  243  PHE A CA  
2463  C C   . PHE B 246  ? 0.7094 1.1170 0.6902 0.2998  0.0137  0.0919  243  PHE A C   
2464  O O   . PHE B 246  ? 0.7024 1.0536 0.6723 0.2960  0.0092  0.0864  243  PHE A O   
2465  C CB  . PHE B 246  ? 0.6378 1.1330 0.6678 0.2497  0.0191  0.1107  243  PHE A CB  
2466  C CG  . PHE B 246  ? 0.5813 1.0828 0.6337 0.2096  0.0195  0.1159  243  PHE A CG  
2467  C CD1 . PHE B 246  ? 0.5632 1.0169 0.6167 0.1904  0.0183  0.1091  243  PHE A CD1 
2468  C CD2 . PHE B 246  ? 0.5619 1.1160 0.6320 0.1916  0.0203  0.1277  243  PHE A CD2 
2469  C CE1 . PHE B 246  ? 0.5441 1.0004 0.6141 0.1564  0.0180  0.1134  243  PHE A CE1 
2470  C CE2 . PHE B 246  ? 0.5517 1.1055 0.6374 0.1555  0.0192  0.1322  243  PHE A CE2 
2471  C CZ  . PHE B 246  ? 0.5400 1.0437 0.6247 0.1391  0.0181  0.1248  243  PHE A CZ  
2472  N N   . PRO B 247  ? 0.7383 1.1780 0.7039 0.3346  0.0150  0.0925  244  PRO A N   
2473  C CA  . PRO B 247  ? 0.7708 1.1747 0.7043 0.3695  0.0104  0.0860  244  PRO A CA  
2474  C C   . PRO B 247  ? 0.7802 1.1011 0.6878 0.3735  0.0042  0.0739  244  PRO A C   
2475  O O   . PRO B 247  ? 0.8252 1.1006 0.7070 0.3907  -0.0016 0.0691  244  PRO A O   
2476  C CB  . PRO B 247  ? 0.7801 1.2371 0.7017 0.4062  0.0133  0.0883  244  PRO A CB  
2477  C CG  . PRO B 247  ? 0.7402 1.2767 0.6942 0.3867  0.0197  0.1005  244  PRO A CG  
2478  C CD  . PRO B 247  ? 0.7227 1.2373 0.6986 0.3447  0.0203  0.1003  244  PRO A CD  
2479  N N   . PHE B 248  ? 0.7481 1.0472 0.6603 0.3574  0.0046  0.0692  245  PHE A N   
2480  C CA  . PHE B 248  ? 0.7770 0.9999 0.6640 0.3598  -0.0019 0.0584  245  PHE A CA  
2481  C C   . PHE B 248  ? 0.7559 0.9297 0.6474 0.3324  -0.0060 0.0573  245  PHE A C   
2482  O O   . PHE B 248  ? 0.7816 0.8912 0.6481 0.3360  -0.0130 0.0499  245  PHE A O   
2483  C CB  . PHE B 248  ? 0.7962 1.0143 0.6871 0.3514  -0.0002 0.0540  245  PHE A CB  
2484  C CG  . PHE B 248  ? 0.8536 0.9982 0.7156 0.3569  -0.0074 0.0431  245  PHE A CG  
2485  C CD1 . PHE B 248  ? 0.9005 1.0151 0.7240 0.3932  -0.0130 0.0362  245  PHE A CD1 
2486  C CD2 . PHE B 248  ? 0.8327 0.9383 0.7040 0.3260  -0.0093 0.0400  245  PHE A CD2 
2487  C CE1 . PHE B 248  ? 0.9271 0.9712 0.7210 0.3961  -0.0211 0.0267  245  PHE A CE1 
2488  C CE2 . PHE B 248  ? 0.8566 0.8975 0.7012 0.3287  -0.0167 0.0310  245  PHE A CE2 
2489  C CZ  . PHE B 248  ? 0.9065 0.9151 0.7120 0.3625  -0.0229 0.0245  245  PHE A CZ  
2490  N N   . TYR B 249  ? 0.7204 0.9232 0.6416 0.3051  -0.0024 0.0648  246  TYR A N   
2491  C CA  . TYR B 249  ? 0.7111 0.8725 0.6374 0.2801  -0.0058 0.0643  246  TYR A CA  
2492  C C   . TYR B 249  ? 0.7387 0.8640 0.6409 0.2966  -0.0118 0.0628  246  TYR A C   
2493  O O   . TYR B 249  ? 0.7552 0.8319 0.6513 0.2813  -0.0166 0.0604  246  TYR A O   
2494  C CB  . TYR B 249  ? 0.6551 0.8566 0.6150 0.2507  -0.0011 0.0726  246  TYR A CB  
2495  C CG  . TYR B 249  ? 0.5504 0.7147 0.5169 0.2252  -0.0040 0.0724  246  TYR A CG  
2496  C CD1 . TYR B 249  ? 0.5497 0.6699 0.5138 0.2081  -0.0064 0.0668  246  TYR A CD1 
2497  C CD2 . TYR B 249  ? 0.5421 0.7185 0.5171 0.2187  -0.0041 0.0782  246  TYR A CD2 
2498  C CE1 . TYR B 249  ? 0.5411 0.6326 0.5112 0.1859  -0.0088 0.0672  246  TYR A CE1 
2499  C CE2 . TYR B 249  ? 0.5337 0.6788 0.5143 0.1967  -0.0066 0.0782  246  TYR A CE2 
2500  C CZ  . TYR B 249  ? 0.6117 0.7157 0.5898 0.1807  -0.0088 0.0729  246  TYR A CZ  
2501  O OH  . TYR B 249  ? 0.6090 0.6871 0.5926 0.1599  -0.0110 0.0736  246  TYR A OH  
2502  N N   . ASN B 250  ? 0.7592 0.9084 0.6466 0.3280  -0.0118 0.0645  247  ASN A N   
2503  C CA  . ASN B 250  ? 0.8294 0.9392 0.6882 0.3474  -0.0183 0.0624  247  ASN A CA  
2504  C C   . ASN B 250  ? 0.9327 0.9680 0.7550 0.3575  -0.0270 0.0530  247  ASN A C   
2505  O O   . ASN B 250  ? 0.9953 0.9796 0.7954 0.3590  -0.0342 0.0511  247  ASN A O   
2506  C CB  . ASN B 250  ? 0.8532 1.0064 0.7010 0.3829  -0.0165 0.0658  247  ASN A CB  
2507  C CG  . ASN B 250  ? 0.8485 1.0692 0.7283 0.3712  -0.0101 0.0763  247  ASN A CG  
2508  O OD1 . ASN B 250  ? 0.8390 1.0555 0.7382 0.3435  -0.0098 0.0802  247  ASN A OD1 
2509  N ND2 . ASN B 250  ? 0.8598 1.1447 0.7445 0.3923  -0.0054 0.0813  247  ASN A ND2 
2510  N N   . GLN B 251  ? 0.9796 1.0068 0.7941 0.3632  -0.0270 0.0473  248  GLN A N   
2511  C CA  . GLN B 251  ? 1.0319 0.9884 0.8123 0.3686  -0.0358 0.0385  248  GLN A CA  
2512  C C   . GLN B 251  ? 0.9733 0.9014 0.7695 0.3317  -0.0366 0.0369  248  GLN A C   
2513  O O   . GLN B 251  ? 0.9906 0.8747 0.7664 0.3317  -0.0421 0.0301  248  GLN A O   
2514  C CB  . GLN B 251  ? 1.1107 1.0715 0.8682 0.4000  -0.0363 0.0326  248  GLN A CB  
2515  C CG  . GLN B 251  ? 1.2387 1.1845 0.9559 0.4430  -0.0417 0.0297  248  GLN A CG  
2516  C CD  . GLN B 251  ? 1.3617 1.2241 1.0381 0.4466  -0.0542 0.0246  248  GLN A CD  
2517  O OE1 . GLN B 251  ? 1.4082 1.2121 1.0605 0.4413  -0.0619 0.0179  248  GLN A OE1 
2518  N NE2 . GLN B 251  ? 1.3970 1.2533 1.0646 0.4544  -0.0568 0.0284  248  GLN A NE2 
2519  N N   . LEU B 252  ? 0.9227 0.8757 0.7532 0.3013  -0.0317 0.0430  249  LEU A N   
2520  C CA  . LEU B 252  ? 0.8829 0.8131 0.7289 0.2673  -0.0323 0.0423  249  LEU A CA  
2521  C C   . LEU B 252  ? 0.8551 0.7681 0.7082 0.2472  -0.0346 0.0467  249  LEU A C   
2522  O O   . LEU B 252  ? 0.8076 0.7320 0.6869 0.2186  -0.0313 0.0499  249  LEU A O   
2523  C CB  . LEU B 252  ? 0.8155 0.7944 0.6963 0.2491  -0.0236 0.0449  249  LEU A CB  
2524  C CG  . LEU B 252  ? 0.7966 0.7934 0.6735 0.2639  -0.0208 0.0409  249  LEU A CG  
2525  C CD1 . LEU B 252  ? 0.7511 0.7919 0.6619 0.2416  -0.0131 0.0446  249  LEU A CD1 
2526  C CD2 . LEU B 252  ? 0.8015 0.7408 0.6497 0.2690  -0.0282 0.0324  249  LEU A CD2 
2527  N N   . LEU B 253  ? 0.8594 0.7443 0.6873 0.2632  -0.0407 0.0471  250  LEU A N   
2528  C CA  . LEU B 253  ? 0.8173 0.6876 0.6497 0.2472  -0.0431 0.0519  250  LEU A CA  
2529  C C   . LEU B 253  ? 0.8788 0.6804 0.6816 0.2395  -0.0537 0.0492  250  LEU A C   
2530  O O   . LEU B 253  ? 0.8975 0.6837 0.7026 0.2240  -0.0564 0.0535  250  LEU A O   
2531  C CB  . LEU B 253  ? 0.7792 0.6747 0.6081 0.2683  -0.0418 0.0562  250  LEU A CB  
2532  C CG  . LEU B 253  ? 0.7480 0.7148 0.6029 0.2770  -0.0325 0.0602  250  LEU A CG  
2533  C CD1 . LEU B 253  ? 0.7548 0.7472 0.6059 0.2966  -0.0318 0.0651  250  LEU A CD1 
2534  C CD2 . LEU B 253  ? 0.7260 0.7290 0.6201 0.2450  -0.0256 0.0645  250  LEU A CD2 
2535  N N   . THR B 254  ? 0.9199 0.6800 0.6937 0.2490  -0.0604 0.0426  251  THR A N   
2536  C CA  . THR B 254  ? 1.0038 0.6970 0.7469 0.2386  -0.0718 0.0407  251  THR A CA  
2537  C C   . THR B 254  ? 1.0379 0.7192 0.7896 0.2152  -0.0724 0.0378  251  THR A C   
2538  O O   . THR B 254  ? 1.0688 0.7821 0.8385 0.2168  -0.0657 0.0350  251  THR A O   
2539  C CB  . THR B 254  ? 1.0531 0.6965 0.7458 0.2698  -0.0821 0.0354  251  THR A CB  
2540  O OG1 . THR B 254  ? 1.0509 0.7045 0.7352 0.2911  -0.0802 0.0290  251  THR A OG1 
2541  C CG2 . THR B 254  ? 1.0493 0.7037 0.7316 0.2941  -0.0820 0.0385  251  THR A CG2 
2542  N N   . GLN B 255  ? 1.0518 0.6881 0.7899 0.1930  -0.0808 0.0392  252  GLN A N   
2543  C CA  . GLN B 255  ? 1.0571 0.6870 0.8063 0.1675  -0.0813 0.0380  252  GLN A CA  
2544  C C   . GLN B 255  ? 1.1308 0.7401 0.8590 0.1813  -0.0847 0.0302  252  GLN A C   
2545  O O   . GLN B 255  ? 1.1028 0.7353 0.8518 0.1709  -0.0792 0.0280  252  GLN A O   
2546  C CB  . GLN B 255  ? 1.0615 0.6489 0.7968 0.1418  -0.0907 0.0422  252  GLN A CB  
2547  C CG  . GLN B 255  ? 1.0573 0.6430 0.8052 0.1139  -0.0913 0.0422  252  GLN A CG  
2548  C CD  . GLN B 255  ? 1.0451 0.6892 0.8396 0.0988  -0.0788 0.0447  252  GLN A CD  
2549  O OE1 . GLN B 255  ? 1.0337 0.7134 0.8511 0.1001  -0.0715 0.0487  252  GLN A OE1 
2550  N NE2 . GLN B 255  ? 1.0469 0.6992 0.8533 0.0846  -0.0768 0.0423  252  GLN A NE2 
2551  N N   . THR B 256  ? 1.1824 0.7463 0.8670 0.2057  -0.0943 0.0257  253  THR A N   
2552  C CA  . THR B 256  ? 1.1995 0.7406 0.8599 0.2214  -0.0984 0.0178  253  THR A CA  
2553  C C   . THR B 256  ? 1.1471 0.7465 0.8339 0.2384  -0.0862 0.0151  253  THR A C   
2554  O O   . THR B 256  ? 1.1672 0.7712 0.8577 0.2367  -0.0846 0.0105  253  THR A O   
2555  C CB  . THR B 256  ? 1.2545 0.7358 0.8596 0.2489  -0.1112 0.0134  253  THR A CB  
2556  O OG1 . THR B 256  ? 1.2533 0.7574 0.8559 0.2768  -0.1072 0.0149  253  THR A OG1 
2557  C CG2 . THR B 256  ? 1.2920 0.7090 0.8664 0.2280  -0.1253 0.0165  253  THR A CG2 
2558  N N   . GLN B 257  ? 1.0921 0.7381 0.7974 0.2536  -0.0779 0.0185  254  GLN A N   
2559  C CA  . GLN B 257  ? 1.0520 0.7590 0.7845 0.2658  -0.0664 0.0181  254  GLN A CA  
2560  C C   . GLN B 257  ? 1.0165 0.7659 0.7940 0.2354  -0.0572 0.0219  254  GLN A C   
2561  O O   . GLN B 257  ? 0.9830 0.7634 0.7768 0.2361  -0.0508 0.0198  254  GLN A O   
2562  C CB  . GLN B 257  ? 1.0521 0.7973 0.7885 0.2902  -0.0615 0.0217  254  GLN A CB  
2563  C CG  . GLN B 257  ? 1.1572 0.8657 0.8471 0.3265  -0.0699 0.0174  254  GLN A CG  
2564  C CD  . GLN B 257  ? 1.2165 0.9106 0.8807 0.3504  -0.0727 0.0095  254  GLN A CD  
2565  O OE1 . GLN B 257  ? 1.2725 0.9026 0.8962 0.3567  -0.0842 0.0035  254  GLN A OE1 
2566  N NE2 . GLN B 257  ? 1.1911 0.9445 0.8773 0.3634  -0.0628 0.0098  254  GLN A NE2 
2567  N N   . ILE B 258  ? 0.9872 0.7374 0.7828 0.2097  -0.0566 0.0274  255  ILE A N   
2568  C CA  . ILE B 258  ? 0.9033 0.6874 0.7365 0.1821  -0.0491 0.0305  255  ILE A CA  
2569  C C   . ILE B 258  ? 0.9448 0.7046 0.7738 0.1672  -0.0523 0.0261  255  ILE A C   
2570  O O   . ILE B 258  ? 0.9272 0.7172 0.7798 0.1571  -0.0456 0.0254  255  ILE A O   
2571  C CB  . ILE B 258  ? 0.7931 0.5813 0.6426 0.1609  -0.0486 0.0371  255  ILE A CB  
2572  C CG1 . ILE B 258  ? 0.7459 0.5695 0.6066 0.1737  -0.0436 0.0419  255  ILE A CG1 
2573  C CG2 . ILE B 258  ? 0.7349 0.5463 0.6153 0.1330  -0.0431 0.0393  255  ILE A CG2 
2574  C CD1 . ILE B 258  ? 0.6604 0.4876 0.5350 0.1554  -0.0433 0.0482  255  ILE A CD1 
2575  N N   . ASP B 259  ? 1.0180 0.7221 0.8150 0.1652  -0.0632 0.0233  256  ASP A N   
2576  C CA  . ASP B 259  ? 1.0455 0.7258 0.8357 0.1512  -0.0673 0.0193  256  ASP A CA  
2577  C C   . ASP B 259  ? 1.0348 0.7248 0.8191 0.1705  -0.0647 0.0127  256  ASP A C   
2578  O O   . ASP B 259  ? 1.0145 0.7205 0.8155 0.1587  -0.0606 0.0108  256  ASP A O   
2579  C CB  . ASP B 259  ? 1.1395 0.7562 0.8925 0.1444  -0.0812 0.0186  256  ASP A CB  
2580  C CG  . ASP B 259  ? 1.2184 0.8284 0.9808 0.1176  -0.0838 0.0259  256  ASP A CG  
2581  O OD1 . ASP B 259  ? 1.2001 0.8492 0.9978 0.0987  -0.0756 0.0298  256  ASP A OD1 
2582  O OD2 . ASP B 259  ? 1.2986 0.8635 1.0311 0.1160  -0.0944 0.0279  256  ASP A OD2 
2583  N N   . LEU B 260  ? 1.0403 0.7221 0.8002 0.2016  -0.0669 0.0093  257  LEU A N   
2584  C CA  . LEU B 260  ? 1.0030 0.6986 0.7569 0.2227  -0.0640 0.0034  257  LEU A CA  
2585  C C   . LEU B 260  ? 0.8971 0.6593 0.6916 0.2190  -0.0508 0.0065  257  LEU A C   
2586  O O   . LEU B 260  ? 0.8649 0.6426 0.6672 0.2193  -0.0471 0.0032  257  LEU A O   
2587  C CB  . LEU B 260  ? 1.0279 0.7061 0.7468 0.2595  -0.0687 -0.0002 257  LEU A CB  
2588  C CG  . LEU B 260  ? 1.0922 0.6956 0.7606 0.2682  -0.0837 -0.0052 257  LEU A CG  
2589  C CD1 . LEU B 260  ? 1.1399 0.7299 0.7732 0.3082  -0.0877 -0.0085 257  LEU A CD1 
2590  C CD2 . LEU B 260  ? 1.1023 0.6745 0.7555 0.2609  -0.0893 -0.0115 257  LEU A CD2 
2591  N N   . TYR B 261  ? 0.8382 0.6388 0.6572 0.2147  -0.0442 0.0131  258  TYR A N   
2592  C CA  . TYR B 261  ? 0.7839 0.6442 0.6391 0.2072  -0.0332 0.0172  258  TYR A CA  
2593  C C   . TYR B 261  ? 0.7958 0.6600 0.6734 0.1779  -0.0305 0.0175  258  TYR A C   
2594  O O   . TYR B 261  ? 0.7945 0.6883 0.6886 0.1748  -0.0245 0.0169  258  TYR A O   
2595  C CB  . TYR B 261  ? 0.7340 0.6288 0.6071 0.2066  -0.0286 0.0245  258  TYR A CB  
2596  C CG  . TYR B 261  ? 0.6941 0.6492 0.6000 0.1993  -0.0188 0.0297  258  TYR A CG  
2597  C CD1 . TYR B 261  ? 0.7091 0.7047 0.6166 0.2202  -0.0142 0.0309  258  TYR A CD1 
2598  C CD2 . TYR B 261  ? 0.6635 0.6348 0.5963 0.1715  -0.0150 0.0338  258  TYR A CD2 
2599  C CE1 . TYR B 261  ? 0.6799 0.7300 0.6154 0.2106  -0.0064 0.0369  258  TYR A CE1 
2600  C CE2 . TYR B 261  ? 0.6101 0.6308 0.5683 0.1635  -0.0077 0.0389  258  TYR A CE2 
2601  C CZ  . TYR B 261  ? 0.6240 0.6836 0.5836 0.1816  -0.0037 0.0408  258  TYR A CZ  
2602  O OH  . TYR B 261  ? 0.6035 0.7116 0.5864 0.1707  0.0024  0.0470  258  TYR A OH  
2603  N N   . ASN B 262  ? 0.7869 0.6227 0.6644 0.1567  -0.0350 0.0189  259  ASN A N   
2604  C CA  . ASN B 262  ? 0.7541 0.5944 0.6506 0.1310  -0.0328 0.0193  259  ASN A CA  
2605  C C   . ASN B 262  ? 0.7706 0.5892 0.6542 0.1314  -0.0360 0.0129  259  ASN A C   
2606  O O   . ASN B 262  ? 0.7433 0.5797 0.6447 0.1182  -0.0316 0.0123  259  ASN A O   
2607  C CB  . ASN B 262  ? 0.7479 0.5669 0.6459 0.1099  -0.0371 0.0230  259  ASN A CB  
2608  C CG  . ASN B 262  ? 0.7309 0.5790 0.6495 0.1036  -0.0322 0.0296  259  ASN A CG  
2609  O OD1 . ASN B 262  ? 0.7357 0.6234 0.6725 0.1086  -0.0250 0.0318  259  ASN A OD1 
2610  N ND2 . ASN B 262  ? 0.7267 0.5558 0.6420 0.0914  -0.0365 0.0332  259  ASN A ND2 
2611  N N   . GLN B 263  ? 0.8173 0.5955 0.6679 0.1467  -0.0443 0.0080  260  GLN A N   
2612  C CA  . GLN B 263  ? 0.8256 0.5807 0.6612 0.1476  -0.0483 0.0017  260  GLN A CA  
2613  C C   . GLN B 263  ? 0.8138 0.5995 0.6548 0.1663  -0.0418 -0.0017 260  GLN A C   
2614  O O   . GLN B 263  ? 0.7965 0.5798 0.6377 0.1624  -0.0415 -0.0058 260  GLN A O   
2615  C CB  . GLN B 263  ? 0.8525 0.5483 0.6466 0.1563  -0.0610 -0.0024 260  GLN A CB  
2616  C CG  . GLN B 263  ? 0.8789 0.5417 0.6660 0.1322  -0.0688 0.0015  260  GLN A CG  
2617  C CD  . GLN B 263  ? 0.9942 0.5939 0.7376 0.1350  -0.0831 -0.0022 260  GLN A CD  
2618  O OE1 . GLN B 263  ? 1.0544 0.6215 0.7703 0.1471  -0.0905 -0.0018 260  GLN A OE1 
2619  N NE2 . GLN B 263  ? 1.0296 0.6098 0.7645 0.1235  -0.0879 -0.0058 260  GLN A NE2 
2620  N N   . LEU B 264  ? 0.8080 0.6251 0.6533 0.1863  -0.0367 0.0005  261  LEU A N   
2621  C CA  . LEU B 264  ? 0.7922 0.6509 0.6494 0.1995  -0.0291 -0.0002 261  LEU A CA  
2622  C C   . LEU B 264  ? 0.7517 0.6472 0.6431 0.1765  -0.0211 0.0035  261  LEU A C   
2623  O O   . LEU B 264  ? 0.7319 0.6469 0.6304 0.1784  -0.0170 0.0016  261  LEU A O   
2624  C CB  . LEU B 264  ? 0.8040 0.6958 0.6610 0.2229  -0.0252 0.0033  261  LEU A CB  
2625  C CG  . LEU B 264  ? 0.7778 0.7228 0.6494 0.2356  -0.0169 0.0052  261  LEU A CG  
2626  C CD1 . LEU B 264  ? 0.7962 0.7258 0.6445 0.2564  -0.0196 -0.0022 261  LEU A CD1 
2627  C CD2 . LEU B 264  ? 0.7665 0.7522 0.6434 0.2525  -0.0129 0.0112  261  LEU A CD2 
2628  N N   . LEU B 265  ? 0.7609 0.6643 0.6713 0.1555  -0.0193 0.0088  262  LEU A N   
2629  C CA  . LEU B 265  ? 0.7134 0.6456 0.6517 0.1344  -0.0130 0.0121  262  LEU A CA  
2630  C C   . LEU B 265  ? 0.7024 0.6095 0.6399 0.1169  -0.0159 0.0084  262  LEU A C   
2631  O O   . LEU B 265  ? 0.6744 0.5997 0.6263 0.1074  -0.0115 0.0080  262  LEU A O   
2632  C CB  . LEU B 265  ? 0.7026 0.6531 0.6589 0.1211  -0.0104 0.0190  262  LEU A CB  
2633  C CG  . LEU B 265  ? 0.6915 0.6851 0.6612 0.1283  -0.0049 0.0251  262  LEU A CG  
2634  C CD1 . LEU B 265  ? 0.7333 0.7296 0.6857 0.1553  -0.0064 0.0244  262  LEU A CD1 
2635  C CD2 . LEU B 265  ? 0.6764 0.6777 0.6604 0.1126  -0.0041 0.0309  262  LEU A CD2 
2636  N N   . GLY B 266  ? 0.6871 0.5533 0.6069 0.1121  -0.0237 0.0062  263  GLY A N   
2637  C CA  . GLY B 266  ? 0.7007 0.5481 0.6214 0.0926  -0.0269 0.0044  263  GLY A CA  
2638  C C   . GLY B 266  ? 0.7500 0.5659 0.6483 0.0980  -0.0331 -0.0021 263  GLY A C   
2639  O O   . GLY B 266  ? 0.7420 0.5512 0.6436 0.0831  -0.0344 -0.0038 263  GLY A O   
2640  N N   . GLY B 267  ? 0.7905 0.5867 0.6643 0.1200  -0.0374 -0.0060 264  GLY A N   
2641  C CA  . GLY B 267  ? 0.8512 0.6132 0.6993 0.1269  -0.0444 -0.0127 264  GLY A CA  
2642  C C   . GLY B 267  ? 0.9110 0.6221 0.7331 0.1166  -0.0563 -0.0134 264  GLY A C   
2643  O O   . GLY B 267  ? 0.9451 0.6481 0.7692 0.1044  -0.0590 -0.0083 264  GLY A O   
2644  N N   . LYS B 327  ? 1.7072 1.0924 1.1996 -0.4513 -0.2941 0.1632  324  LYS A N   
2645  C CA  . LYS B 327  ? 1.7159 1.0935 1.1975 -0.4586 -0.2988 0.1720  324  LYS A CA  
2646  C C   . LYS B 327  ? 1.7057 1.1400 1.2000 -0.4907 -0.3017 0.1897  324  LYS A C   
2647  O O   . LYS B 327  ? 1.7014 1.1455 1.1982 -0.4963 -0.3019 0.1975  324  LYS A O   
2648  C CB  . LYS B 327  ? 1.7789 1.0740 1.2023 -0.4543 -0.3171 0.1686  324  LYS A CB  
2649  C CG  . LYS B 327  ? 1.7836 1.0224 1.1913 -0.4177 -0.3141 0.1518  324  LYS A CG  
2650  C CD  . LYS B 327  ? 1.7458 1.0029 1.1849 -0.3964 -0.2987 0.1484  324  LYS A CD  
2651  C CE  . LYS B 327  ? 1.7582 0.9637 1.1814 -0.3585 -0.2955 0.1326  324  LYS A CE  
2652  N NZ  . LYS B 327  ? 1.7044 0.9285 1.1573 -0.3381 -0.2808 0.1305  324  LYS A NZ  
2653  N N   . SER B 328  ? 1.7211 1.1945 1.2229 -0.5111 -0.3038 0.1964  325  SER A N   
2654  C CA  . SER B 328  ? 1.7478 1.2769 1.2584 -0.5407 -0.3073 0.2139  325  SER A CA  
2655  C C   . SER B 328  ? 1.7045 1.3058 1.2515 -0.5486 -0.2971 0.2174  325  SER A C   
2656  O O   . SER B 328  ? 1.6733 1.2769 1.2360 -0.5333 -0.2887 0.2062  325  SER A O   
2657  C CB  . SER B 328  ? 1.8407 1.3266 1.2996 -0.5657 -0.3299 0.2236  325  SER A CB  
2658  O OG  . SER B 328  ? 1.8720 1.3379 1.3089 -0.5740 -0.3388 0.2216  325  SER A OG  
2659  N N   . ASP B 329  ? 1.7126 1.3745 1.2715 -0.5722 -0.2981 0.2332  326  ASP A N   
2660  C CA  . ASP B 329  ? 1.6805 1.4188 1.2736 -0.5791 -0.2881 0.2382  326  ASP A CA  
2661  C C   . ASP B 329  ? 1.7192 1.4441 1.2892 -0.5938 -0.2987 0.2394  326  ASP A C   
2662  O O   . ASP B 329  ? 1.6890 1.4405 1.2808 -0.5855 -0.2898 0.2326  326  ASP A O   
2663  C CB  . ASP B 329  ? 1.6798 1.4883 1.2905 -0.5969 -0.2859 0.2551  326  ASP A CB  
2664  C CG  . ASP B 329  ? 1.6225 1.5180 1.2770 -0.5936 -0.2705 0.2580  326  ASP A CG  
2665  O OD1 . ASP B 329  ? 1.6359 1.5635 1.2865 -0.6101 -0.2748 0.2655  326  ASP A OD1 
2666  O OD2 . ASP B 329  ? 1.5686 1.5001 1.2597 -0.5738 -0.2542 0.2529  326  ASP A OD2 
2667  N N   . GLU B 330  ? 1.7901 1.4732 1.3146 -0.6161 -0.3183 0.2481  327  GLU A N   
2668  C CA  . GLU B 330  ? 1.8279 1.4936 1.3254 -0.6322 -0.3302 0.2506  327  GLU A CA  
2669  C C   . GLU B 330  ? 1.8622 1.4553 1.3369 -0.6131 -0.3340 0.2336  327  GLU A C   
2670  O O   . GLU B 330  ? 1.8696 1.4523 1.3292 -0.6210 -0.3404 0.2327  327  GLU A O   
2671  C CB  . GLU B 330  ? 1.8804 1.5249 1.3338 -0.6640 -0.3511 0.2669  327  GLU A CB  
2672  N N   . GLU B 331  ? 1.8659 1.4098 1.3369 -0.5875 -0.3303 0.2204  328  GLU A N   
2673  C CA  . GLU B 331  ? 1.8699 1.3468 1.3182 -0.5661 -0.3335 0.2040  328  GLU A CA  
2674  C C   . GLU B 331  ? 1.8085 1.3201 1.2916 -0.5520 -0.3193 0.1938  328  GLU A C   
2675  O O   . GLU B 331  ? 1.8137 1.2884 1.2768 -0.5462 -0.3249 0.1852  328  GLU A O   
2676  C CB  . GLU B 331  ? 1.8562 1.2808 1.2952 -0.5397 -0.3311 0.1929  328  GLU A CB  
2677  C CG  . GLU B 331  ? 1.8800 1.2315 1.2889 -0.5151 -0.3360 0.1763  328  GLU A CG  
2678  C CD  . GLU B 331  ? 1.8930 1.2014 1.2961 -0.4861 -0.3316 0.1655  328  GLU A CD  
2679  O OE1 . GLU B 331  ? 1.8644 1.2019 1.2913 -0.4850 -0.3233 0.1703  328  GLU A OE1 
2680  O OE2 . GLU B 331  ? 1.9354 1.1823 1.3096 -0.4632 -0.3362 0.1523  328  GLU A OE2 
2681  N N   . VAL B 332  ? 1.7903 1.3726 1.3241 -0.5458 -0.3014 0.1945  329  VAL A N   
2682  C CA  . VAL B 332  ? 1.7263 1.3448 1.2933 -0.5331 -0.2884 0.1852  329  VAL A CA  
2683  C C   . VAL B 332  ? 1.7275 1.3860 1.2944 -0.5557 -0.2929 0.1942  329  VAL A C   
2684  O O   . VAL B 332  ? 1.7337 1.3992 1.3103 -0.5484 -0.2887 0.1857  329  VAL A O   
2685  C CB  . VAL B 332  ? 1.6674 1.3471 1.2856 -0.5184 -0.2685 0.1832  329  VAL A CB  
2686  C CG1 . VAL B 332  ? 1.6710 1.3144 1.2869 -0.5006 -0.2653 0.1780  329  VAL A CG1 
2687  C CG2 . VAL B 332  ? 1.6429 1.4040 1.2866 -0.5379 -0.2638 0.1993  329  VAL A CG2 
2688  N N   . ILE B 333  ? 1.7283 1.4139 1.2834 -0.5832 -0.3018 0.2117  330  ILE A N   
2689  C CA  . ILE B 333  ? 1.6439 1.3699 1.1972 -0.6055 -0.3064 0.2219  330  ILE A CA  
2690  C C   . ILE B 333  ? 1.6489 1.3070 1.1524 -0.6172 -0.3250 0.2211  330  ILE A C   
2691  O O   . ILE B 333  ? 1.6354 1.3019 1.1381 -0.6213 -0.3260 0.2188  330  ILE A O   
2692  C CB  . ILE B 333  ? 1.5413 1.3298 1.1023 -0.6299 -0.3079 0.2419  330  ILE A CB  
2693  C CG1 . ILE B 333  ? 1.4087 1.2594 1.0158 -0.6153 -0.2899 0.2420  330  ILE A CG1 
2694  C CG2 . ILE B 333  ? 1.5064 1.3457 1.0693 -0.6508 -0.3105 0.2528  330  ILE A CG2 
2695  C CD1 . ILE B 333  ? 1.3643 1.2787 0.9794 -0.6356 -0.2906 0.2610  330  ILE A CD1 
2696  N N   . GLN B 334  ? 1.6863 1.2759 1.1464 -0.6219 -0.3402 0.2228  331  GLN A N   
2697  C CA  . GLN B 334  ? 1.7701 1.2910 1.1778 -0.6322 -0.3593 0.2224  331  GLN A CA  
2698  C C   . GLN B 334  ? 1.7970 1.2680 1.1983 -0.6051 -0.3566 0.2027  331  GLN A C   
2699  O O   . GLN B 334  ? 1.8350 1.2800 1.2122 -0.6113 -0.3656 0.2008  331  GLN A O   
2700  C CB  . GLN B 334  ? 1.8258 1.2857 1.1869 -0.6418 -0.3765 0.2287  331  GLN A CB  
2701  N N   . SER B 335  ? 1.7778 1.2356 1.1996 -0.5748 -0.3443 0.1882  332  SER A N   
2702  C CA  . SER B 335  ? 1.7730 1.1841 1.1876 -0.5470 -0.3416 0.1694  332  SER A CA  
2703  C C   . SER B 335  ? 1.7116 1.1741 1.1633 -0.5424 -0.3291 0.1634  332  SER A C   
2704  O O   . SER B 335  ? 1.7117 1.1431 1.1466 -0.5355 -0.3336 0.1544  332  SER A O   
2705  C CB  . SER B 335  ? 1.7564 1.1394 1.1799 -0.5164 -0.3326 0.1569  332  SER A CB  
2706  O OG  . SER B 335  ? 1.7737 1.1124 1.1881 -0.4881 -0.3302 0.1390  332  SER A OG  
2707  N N   . PHE B 336  ? 1.6388 1.1802 1.1399 -0.5449 -0.3135 0.1680  333  PHE A N   
2708  C CA  . PHE B 336  ? 1.5568 1.1509 1.0933 -0.5401 -0.3016 0.1626  333  PHE A CA  
2709  C C   . PHE B 336  ? 1.5923 1.2042 1.1139 -0.5650 -0.3111 0.1723  333  PHE A C   
2710  O O   . PHE B 336  ? 1.5973 1.2010 1.1173 -0.5590 -0.3112 0.1635  333  PHE A O   
2711  C CB  . PHE B 336  ? 1.4359 1.1110 1.0248 -0.5365 -0.2838 0.1665  333  PHE A CB  
2712  C CG  . PHE B 336  ? 1.3600 1.0912 0.9858 -0.5287 -0.2712 0.1601  333  PHE A CG  
2713  C CD1 . PHE B 336  ? 1.3378 1.0390 0.9661 -0.5066 -0.2671 0.1426  333  PHE A CD1 
2714  C CD2 . PHE B 336  ? 1.3208 1.1358 0.9772 -0.5418 -0.2634 0.1716  333  PHE A CD2 
2715  C CE1 . PHE B 336  ? 1.2936 1.0459 0.9544 -0.4996 -0.2563 0.1366  333  PHE A CE1 
2716  C CE2 . PHE B 336  ? 1.2710 1.1381 0.9597 -0.5328 -0.2521 0.1654  333  PHE A CE2 
2717  C CZ  . PHE B 336  ? 1.2571 1.0924 0.9482 -0.5125 -0.2489 0.1479  333  PHE A CZ  
2718  N N   . CYS B 337  ? 1.6460 1.2819 1.1553 -0.5933 -0.3197 0.1908  334  CYS A N   
2719  C CA  . CYS B 337  ? 1.6840 1.3363 1.1760 -0.6193 -0.3298 0.2021  334  CYS A CA  
2720  C C   . CYS B 337  ? 1.7659 1.3362 1.2079 -0.6205 -0.3465 0.1960  334  CYS A C   
2721  O O   . CYS B 337  ? 1.7807 1.3570 1.2136 -0.6319 -0.3515 0.1980  334  CYS A O   
2722  C CB  . CYS B 337  ? 1.7169 1.4046 1.1998 -0.6494 -0.3373 0.2239  334  CYS A CB  
2723  S SG  . CYS B 337  ? 1.7755 1.4948 1.2391 -0.6842 -0.3487 0.2410  334  CYS A SG  
2724  N N   . LYS B 338  ? 1.8254 1.3192 1.2334 -0.6075 -0.3553 0.1887  335  LYS A N   
2725  C CA  . LYS B 338  ? 1.8993 1.3128 1.2588 -0.6022 -0.3704 0.1807  335  LYS A CA  
2726  C C   . LYS B 338  ? 1.8680 1.2723 1.2436 -0.5751 -0.3608 0.1617  335  LYS A C   
2727  O O   . LYS B 338  ? 1.8960 1.2743 1.2493 -0.5780 -0.3688 0.1582  335  LYS A O   
2728  C CB  . LYS B 338  ? 1.9446 1.2819 1.2629 -0.5920 -0.3817 0.1775  335  LYS A CB  
2729  N N   . TYR B 339  ? 1.7989 1.2238 1.2120 -0.5488 -0.3440 0.1494  336  TYR A N   
2730  C CA  . TYR B 339  ? 1.7466 1.1732 1.1795 -0.5244 -0.3338 0.1322  336  TYR A CA  
2731  C C   . TYR B 339  ? 1.6386 1.1392 1.1072 -0.5373 -0.3253 0.1363  336  TYR A C   
2732  O O   . TYR B 339  ? 1.6336 1.1288 1.1036 -0.5278 -0.3239 0.1258  336  TYR A O   
2733  C CB  . TYR B 339  ? 1.7381 1.1670 1.1993 -0.4946 -0.3191 0.1194  336  TYR A CB  
2734  C CG  . TYR B 339  ? 1.7157 1.1669 1.2078 -0.4726 -0.3057 0.1039  336  TYR A CG  
2735  C CD1 . TYR B 339  ? 1.7542 1.1504 1.2224 -0.4504 -0.3095 0.0884  336  TYR A CD1 
2736  C CD2 . TYR B 339  ? 1.6470 1.1748 1.1905 -0.4728 -0.2897 0.1049  336  TYR A CD2 
2737  C CE1 . TYR B 339  ? 1.7140 1.1303 1.2086 -0.4306 -0.2979 0.0743  336  TYR A CE1 
2738  C CE2 . TYR B 339  ? 1.6050 1.1521 1.1743 -0.4535 -0.2788 0.0910  336  TYR A CE2 
2739  C CZ  . TYR B 339  ? 1.6412 1.1320 1.1859 -0.4332 -0.2830 0.0757  336  TYR A CZ  
2740  O OH  . TYR B 339  ? 1.6025 1.1139 1.1717 -0.4126 -0.2718 0.0620  336  TYR A OH  
2741  N N   . LYS B 340  ? 1.5494 1.1207 1.0461 -0.5574 -0.3195 0.1512  337  LYS A N   
2742  C CA  . LYS B 340  ? 1.4745 1.1214 1.0039 -0.5684 -0.3113 0.1563  337  LYS A CA  
2743  C C   . LYS B 340  ? 1.5351 1.1681 1.0338 -0.5905 -0.3251 0.1638  337  LYS A C   
2744  O O   . LYS B 340  ? 1.5246 1.1786 1.0350 -0.5875 -0.3215 0.1577  337  LYS A O   
2745  C CB  . LYS B 340  ? 1.4086 1.1335 0.9710 -0.5818 -0.3022 0.1712  337  LYS A CB  
2746  C CG  . LYS B 340  ? 1.3446 1.1551 0.9418 -0.5899 -0.2923 0.1773  337  LYS A CG  
2747  C CD  . LYS B 340  ? 1.2812 1.1664 0.9144 -0.5917 -0.2801 0.1877  337  LYS A CD  
2748  C CE  . LYS B 340  ? 1.2629 1.2305 0.9157 -0.6075 -0.2755 0.2007  337  LYS A CE  
2749  N NZ  . LYS B 340  ? 1.2149 1.2583 0.9027 -0.6043 -0.2624 0.2095  337  LYS A NZ  
2750  N N   . THR B 341  ? 1.5942 1.1904 1.0515 -0.6133 -0.3416 0.1771  338  THR A N   
2751  C CA  . THR B 341  ? 1.6230 1.1997 1.0461 -0.6361 -0.3565 0.1853  338  THR A CA  
2752  C C   . THR B 341  ? 1.6541 1.1572 1.0460 -0.6191 -0.3644 0.1693  338  THR A C   
2753  O O   . THR B 341  ? 1.6772 1.1708 1.0490 -0.6326 -0.3734 0.1723  338  THR A O   
2754  C CB  . THR B 341  ? 1.6603 1.2122 1.0430 -0.6652 -0.3736 0.2039  338  THR A CB  
2755  O OG1 . THR B 341  ? 1.7153 1.2716 1.0737 -0.6927 -0.3857 0.2160  338  THR A OG1 
2756  C CG2 . THR B 341  ? 1.6951 1.1527 1.0313 -0.6540 -0.3870 0.1970  338  THR A CG2 
2757  N N   . LEU B 342  ? 1.6809 1.1334 1.0678 -0.5889 -0.3612 0.1528  339  LEU A N   
2758  C CA  . LEU B 342  ? 1.7285 1.1165 1.0885 -0.5673 -0.3666 0.1363  339  LEU A CA  
2759  C C   . LEU B 342  ? 1.6916 1.1206 1.0873 -0.5532 -0.3536 0.1241  339  LEU A C   
2760  O O   . LEU B 342  ? 1.6980 1.0911 1.0725 -0.5455 -0.3597 0.1150  339  LEU A O   
2761  C CB  . LEU B 342  ? 1.7633 1.0896 1.1065 -0.5375 -0.3664 0.1232  339  LEU A CB  
2762  C CG  . LEU B 342  ? 1.8235 1.0761 1.1323 -0.5101 -0.3727 0.1061  339  LEU A CG  
2763  C CD1 . LEU B 342  ? 1.8896 1.0676 1.1537 -0.4975 -0.3840 0.1043  339  LEU A CD1 
2764  C CD2 . LEU B 342  ? 1.7783 1.0509 1.1235 -0.4784 -0.3557 0.0877  339  LEU A CD2 
2765  N N   . LEU B 343  ? 1.6499 1.1535 1.0979 -0.5492 -0.3364 0.1238  340  LEU A N   
2766  C CA  . LEU B 343  ? 1.6248 1.1718 1.1069 -0.5364 -0.3244 0.1128  340  LEU A CA  
2767  C C   . LEU B 343  ? 1.6397 1.2255 1.1224 -0.5598 -0.3287 0.1223  340  LEU A C   
2768  O O   . LEU B 343  ? 1.6320 1.2299 1.1260 -0.5496 -0.3245 0.1118  340  LEU A O   
2769  C CB  . LEU B 343  ? 1.5640 1.1798 1.0989 -0.5256 -0.3058 0.1110  340  LEU A CB  
2770  C CG  . LEU B 343  ? 1.5366 1.1216 1.0767 -0.5013 -0.2993 0.1011  340  LEU A CG  
2771  C CD1 . LEU B 343  ? 1.4442 1.1023 1.0346 -0.4965 -0.2825 0.1033  340  LEU A CD1 
2772  C CD2 . LEU B 343  ? 1.5385 1.0676 1.0650 -0.4711 -0.2986 0.0806  340  LEU A CD2 
2773  N N   . ARG B 344  ? 1.6672 1.2737 1.1372 -0.5909 -0.3371 0.1421  341  ARG A N   
2774  C CA  . ARG B 344  ? 1.6974 1.3375 1.1636 -0.6143 -0.3424 0.1523  341  ARG A CA  
2775  C C   . ARG B 344  ? 1.7731 1.3387 1.1910 -0.6175 -0.3589 0.1477  341  ARG A C   
2776  O O   . ARG B 344  ? 1.7742 1.3525 1.1949 -0.6186 -0.3590 0.1433  341  ARG A O   
2777  C CB  . ARG B 344  ? 1.7271 1.4123 1.1916 -0.6468 -0.3468 0.1759  341  ARG A CB  
2778  C CG  . ARG B 344  ? 1.6743 1.4509 1.1885 -0.6463 -0.3299 0.1830  341  ARG A CG  
2779  C CD  . ARG B 344  ? 1.6806 1.4459 1.2029 -0.6349 -0.3251 0.1819  341  ARG A CD  
2780  N NE  . ARG B 344  ? 1.6691 1.5062 1.2152 -0.6495 -0.3183 0.1987  341  ARG A NE  
2781  C CZ  . ARG B 344  ? 1.7155 1.5488 1.2365 -0.6754 -0.3294 0.2168  341  ARG A CZ  
2782  N NH1 . ARG B 344  ? 1.7919 1.5515 1.2623 -0.6903 -0.3483 0.2207  341  ARG A NH1 
2783  N NH2 . ARG B 344  ? 1.6854 1.5885 1.2297 -0.6858 -0.3221 0.2311  341  ARG A NH2 
2784  N N   . ASN B 345  ? 1.8318 1.3193 1.2038 -0.6179 -0.3732 0.1485  342  ASN A N   
2785  C CA  . ASN B 345  ? 1.8930 1.3061 1.2135 -0.6205 -0.3904 0.1454  342  ASN A CA  
2786  C C   . ASN B 345  ? 1.8910 1.2724 1.2136 -0.5881 -0.3853 0.1230  342  ASN A C   
2787  O O   . ASN B 345  ? 1.9185 1.2777 1.2207 -0.5908 -0.3930 0.1196  342  ASN A O   
2788  C CB  . ASN B 345  ? 1.9362 1.2734 1.2061 -0.6243 -0.4065 0.1506  342  ASN A CB  
2789  C CG  . ASN B 345  ? 1.9362 1.3024 1.2009 -0.6568 -0.4126 0.1729  342  ASN A CG  
2790  O OD1 . ASN B 345  ? 1.9185 1.3475 1.2005 -0.6832 -0.4110 0.1876  342  ASN A OD1 
2791  N ND2 . ASN B 345  ? 1.9576 1.2798 1.1976 -0.6542 -0.4197 0.1757  342  ASN A ND2 
2792  N N   . GLU B 346  ? 1.8425 1.2216 1.1885 -0.5572 -0.3726 0.1080  343  GLU A N   
2793  C CA  . GLU B 346  ? 1.8124 1.1697 1.1636 -0.5254 -0.3662 0.0871  343  GLU A CA  
2794  C C   . GLU B 346  ? 1.7575 1.1861 1.1518 -0.5260 -0.3538 0.0831  343  GLU A C   
2795  O O   . GLU B 346  ? 1.7349 1.1482 1.1292 -0.5053 -0.3510 0.0676  343  GLU A O   
2796  C CB  . GLU B 346  ? 1.7552 1.0910 1.1175 -0.4930 -0.3564 0.0734  343  GLU A CB  
2797  C CG  . GLU B 346  ? 1.7928 1.0488 1.1081 -0.4827 -0.3685 0.0726  343  GLU A CG  
2798  C CD  . GLU B 346  ? 1.7562 0.9982 1.0852 -0.4509 -0.3576 0.0602  343  GLU A CD  
2799  O OE1 . GLU B 346  ? 1.6937 0.9940 1.0703 -0.4460 -0.3416 0.0580  343  GLU A OE1 
2800  O OE2 . GLU B 346  ? 1.7963 0.9698 1.0874 -0.4301 -0.3651 0.0531  343  GLU A OE2 
2801  N N   . ASN B 347  ? 1.7408 1.2478 1.1701 -0.5478 -0.3465 0.0968  344  ASN A N   
2802  C CA  . ASN B 347  ? 1.6969 1.2793 1.1677 -0.5483 -0.3345 0.0947  344  ASN A CA  
2803  C C   . ASN B 347  ? 1.6430 1.2360 1.1436 -0.5148 -0.3202 0.0751  344  ASN A C   
2804  O O   . ASN B 347  ? 1.6178 1.2245 1.1291 -0.5030 -0.3160 0.0640  344  ASN A O   
2805  C CB  . ASN B 347  ? 1.7334 1.3094 1.1844 -0.5620 -0.3440 0.0964  344  ASN A CB  
2806  N N   . VAL B 348  ? 1.6318 1.2180 1.1446 -0.4998 -0.3129 0.0713  345  VAL A N   
2807  C CA  . VAL B 348  ? 1.5959 1.1882 1.1337 -0.4689 -0.3000 0.0537  345  VAL A CA  
2808  C C   . VAL B 348  ? 1.5262 1.2075 1.1130 -0.4696 -0.2859 0.0546  345  VAL A C   
2809  O O   . VAL B 348  ? 1.4681 1.1636 1.0748 -0.4431 -0.2743 0.0408  345  VAL A O   
2810  C CB  . VAL B 348  ? 1.5981 1.1585 1.1342 -0.4536 -0.2965 0.0505  345  VAL A CB  
2811  C CG1 . VAL B 348  ? 1.6687 1.1394 1.1538 -0.4463 -0.3102 0.0473  345  VAL A CG1 
2812  C CG2 . VAL B 348  ? 1.5871 1.1979 1.1463 -0.4729 -0.2921 0.0671  345  VAL A CG2 
2813  N N   . LEU B 349  ? 1.5240 1.2698 1.1316 -0.4929 -0.2832 0.0718  346  LEU A N   
2814  C CA  . LEU B 349  ? 1.4606 1.2942 1.1118 -0.4915 -0.2703 0.0735  346  LEU A CA  
2815  C C   . LEU B 349  ? 1.4355 1.2832 1.0846 -0.4918 -0.2724 0.0681  346  LEU A C   
2816  O O   . LEU B 349  ? 1.3854 1.2690 1.0609 -0.4699 -0.2601 0.0578  346  LEU A O   
2817  C CB  . LEU B 349  ? 1.4769 1.3768 1.1472 -0.5137 -0.2668 0.0938  346  LEU A CB  
2818  C CG  . LEU B 349  ? 1.5643 1.4453 1.2061 -0.5426 -0.2789 0.1121  346  LEU A CG  
2819  C CD1 . LEU B 349  ? 1.6203 1.4638 1.2259 -0.5600 -0.2935 0.1156  346  LEU A CD1 
2820  C CD2 . LEU B 349  ? 1.5470 1.5128 1.2169 -0.5579 -0.2711 0.1298  346  LEU A CD2 
2821  N N   . GLU B 350  ? 1.4803 1.2993 1.0982 -0.5118 -0.2854 0.0756  347  GLU A N   
2822  C CA  . GLU B 350  ? 1.4583 1.2878 1.0721 -0.5133 -0.2882 0.0710  347  GLU A CA  
2823  C C   . GLU B 350  ? 1.4349 1.2125 1.0365 -0.4857 -0.2883 0.0494  347  GLU A C   
2824  O O   . GLU B 350  ? 1.3715 1.1779 0.9872 -0.4753 -0.2834 0.0406  347  GLU A O   
2825  C CB  . GLU B 350  ? 1.5110 1.3126 1.0894 -0.5415 -0.3036 0.0841  347  GLU A CB  
2826  N N   . THR B 351  ? 1.4824 1.1845 1.0565 -0.4718 -0.2936 0.0408  348  THR A N   
2827  C CA  . THR B 351  ? 1.4836 1.1372 1.0450 -0.4419 -0.2925 0.0203  348  THR A CA  
2828  C C   . THR B 351  ? 1.4085 1.1135 1.0171 -0.4041 -0.2660 0.0130  348  THR A C   
2829  O O   . THR B 351  ? 1.3965 1.1067 1.0151 -0.3770 -0.2558 0.0012  348  THR A O   
2830  C CB  . THR B 351  ? 1.5153 1.0815 1.0374 -0.4298 -0.3011 0.0150  348  THR A CB  
2831  O OG1 . THR B 351  ? 1.5730 1.1022 1.0592 -0.4532 -0.3163 0.0276  348  THR A OG1 
2832  C CG2 . THR B 351  ? 1.5104 1.0261 1.0141 -0.3967 -0.2999 -0.0045 348  THR A CG2 
2833  N N   . ALA B 352  ? 1.3638 1.1061 1.0001 -0.4021 -0.2551 0.0204  349  ALA A N   
2834  C CA  . ALA B 352  ? 1.2923 1.0819 0.9709 -0.3683 -0.2312 0.0146  349  ALA A CA  
2835  C C   . ALA B 352  ? 1.2687 1.1337 0.9788 -0.3681 -0.2211 0.0173  349  ALA A C   
2836  O O   . ALA B 352  ? 1.2231 1.1075 0.9538 -0.3380 -0.2059 0.0073  349  ALA A O   
2837  C CB  . ALA B 352  ? 1.2767 1.0837 0.9732 -0.3676 -0.2238 0.0220  349  ALA A CB  
2838  N N   . GLU B 353  ? 1.2952 1.2046 1.0083 -0.4013 -0.2296 0.0312  350  GLU A N   
2839  C CA  . GLU B 353  ? 1.2640 1.2473 1.0042 -0.4009 -0.2211 0.0343  350  GLU A CA  
2840  C C   . GLU B 353  ? 1.2639 1.2297 0.9919 -0.3920 -0.2238 0.0238  350  GLU A C   
2841  O O   . GLU B 353  ? 1.2249 1.2391 0.9773 -0.3747 -0.2112 0.0199  350  GLU A O   
2842  C CB  . GLU B 353  ? 1.2726 1.3073 1.0148 -0.4405 -0.2317 0.0526  350  GLU A CB  
2843  C CG  . GLU B 353  ? 1.2654 1.3338 1.0254 -0.4478 -0.2266 0.0642  350  GLU A CG  
2844  C CD  . GLU B 353  ? 1.3038 1.4109 1.0577 -0.4907 -0.2403 0.0836  350  GLU A CD  
2845  O OE1 . GLU B 353  ? 1.3099 1.4556 1.0657 -0.5012 -0.2413 0.0900  350  GLU A OE1 
2846  O OE2 . GLU B 353  ? 1.3208 1.4160 1.0690 -0.5022 -0.2424 0.0939  350  GLU A OE2 
2847  N N   . ALA B 354  ? 1.3088 1.2040 0.9975 -0.4023 -0.2404 0.0187  351  ALA A N   
2848  C CA  . ALA B 354  ? 1.3040 1.1772 0.9781 -0.3927 -0.2437 0.0079  351  ALA A CA  
2849  C C   . ALA B 354  ? 1.2608 1.1102 0.9439 -0.3490 -0.2282 -0.0084 351  ALA A C   
2850  O O   . ALA B 354  ? 1.2550 1.1186 0.9454 -0.3326 -0.2217 -0.0166 351  ALA A O   
2851  C CB  . ALA B 354  ? 1.3834 1.1863 1.0080 -0.4187 -0.2682 0.0082  351  ALA A CB  
2852  N N   . LEU B 355  ? 1.2343 1.0495 0.9165 -0.3306 -0.2224 -0.0127 352  LEU A N   
2853  C CA  . LEU B 355  ? 1.1523 0.9493 0.8435 -0.2906 -0.2078 -0.0267 352  LEU A CA  
2854  C C   . LEU B 355  ? 1.0594 0.9233 0.7933 -0.2696 -0.1869 -0.0276 352  LEU A C   
2855  O O   . LEU B 355  ? 1.0515 0.9210 0.7934 -0.2460 -0.1777 -0.0373 352  LEU A O   
2856  C CB  . LEU B 355  ? 1.1142 0.8644 0.7949 -0.2776 -0.2070 -0.0295 352  LEU A CB  
2857  C CG  . LEU B 355  ? 1.1579 0.8259 0.7918 -0.2785 -0.2236 -0.0360 352  LEU A CG  
2858  C CD1 . LEU B 355  ? 1.1644 0.7959 0.7931 -0.2594 -0.2194 -0.0393 352  LEU A CD1 
2859  C CD2 . LEU B 355  ? 1.1579 0.8016 0.7770 -0.2593 -0.2241 -0.0487 352  LEU A CD2 
2860  N N   . PHE B 356  ? 1.0119 0.9255 0.7714 -0.2772 -0.1797 -0.0176 353  PHE A N   
2861  C CA  . PHE B 356  ? 0.9804 0.9540 0.7759 -0.2568 -0.1612 -0.0183 353  PHE A CA  
2862  C C   . PHE B 356  ? 1.0069 1.0264 0.8106 -0.2620 -0.1607 -0.0171 353  PHE A C   
2863  O O   . PHE B 356  ? 0.9840 1.0385 0.8096 -0.2389 -0.1464 -0.0218 353  PHE A O   
2864  C CB  . PHE B 356  ? 0.9505 0.9640 0.7674 -0.2630 -0.1549 -0.0078 353  PHE A CB  
2865  C CG  . PHE B 356  ? 0.9703 0.9481 0.7864 -0.2502 -0.1506 -0.0103 353  PHE A CG  
2866  C CD1 . PHE B 356  ? 0.9506 0.9305 0.7844 -0.2185 -0.1347 -0.0183 353  PHE A CD1 
2867  C CD2 . PHE B 356  ? 1.0085 0.9504 0.8048 -0.2705 -0.1631 -0.0042 353  PHE A CD2 
2868  C CE1 . PHE B 356  ? 0.9522 0.9025 0.7857 -0.2073 -0.1309 -0.0201 353  PHE A CE1 
2869  C CE2 . PHE B 356  ? 1.0031 0.9136 0.7984 -0.2578 -0.1590 -0.0064 353  PHE A CE2 
2870  C CZ  . PHE B 356  ? 0.9772 0.8937 0.7920 -0.2260 -0.1428 -0.0144 353  PHE A CZ  
2871  N N   . ASN B 357  ? 1.0631 1.0825 0.8484 -0.2921 -0.1767 -0.0106 354  ASN A N   
2872  C CA  . ASN B 357  ? 1.0753 1.1339 0.8652 -0.2969 -0.1775 -0.0103 354  ASN A CA  
2873  C C   . ASN B 357  ? 1.1032 1.1226 0.8784 -0.2786 -0.1777 -0.0240 354  ASN A C   
2874  O O   . ASN B 357  ? 1.0746 1.1284 0.8606 -0.2696 -0.1721 -0.0271 354  ASN A O   
2875  C CB  . ASN B 357  ? 1.1331 1.2073 0.9075 -0.3379 -0.1955 0.0024  354  ASN A CB  
2876  C CG  . ASN B 357  ? 1.1510 1.2788 0.9341 -0.3443 -0.1957 0.0049  354  ASN A CG  
2877  O OD1 . ASN B 357  ? 1.1892 1.2917 0.9513 -0.3531 -0.2063 0.0005  354  ASN A OD1 
2878  N ND2 . ASN B 357  ? 1.1199 1.3220 0.9326 -0.3386 -0.1841 0.0118  354  ASN A ND2 
2879  N N   . GLU B 358  ? 1.1507 1.1004 0.9006 -0.2714 -0.1841 -0.0323 355  GLU A N   
2880  C CA  . GLU B 358  ? 1.1590 1.0726 0.8955 -0.2498 -0.1828 -0.0457 355  GLU A CA  
2881  C C   . GLU B 358  ? 1.0611 1.0010 0.8253 -0.2145 -0.1623 -0.0534 355  GLU A C   
2882  O O   . GLU B 358  ? 1.0140 0.9524 0.7770 -0.1984 -0.1583 -0.0619 355  GLU A O   
2883  C CB  . GLU B 358  ? 1.2321 1.0677 0.9347 -0.2459 -0.1932 -0.0525 355  GLU A CB  
2884  C CG  . GLU B 358  ? 1.3135 1.1038 0.9759 -0.2741 -0.2161 -0.0506 355  GLU A CG  
2885  C CD  . GLU B 358  ? 1.3843 1.0940 1.0095 -0.2639 -0.2259 -0.0590 355  GLU A CD  
2886  O OE1 . GLU B 358  ? 1.4395 1.1128 1.0417 -0.2836 -0.2391 -0.0530 355  GLU A OE1 
2887  O OE2 . GLU B 358  ? 1.3844 1.0680 1.0026 -0.2352 -0.2204 -0.0714 355  GLU A OE2 
2888  N N   . LEU B 359  ? 1.0374 1.0004 0.8251 -0.2030 -0.1498 -0.0503 356  LEU A N   
2889  C CA  . LEU B 359  ? 0.9907 0.9715 0.8008 -0.1711 -0.1317 -0.0570 356  LEU A CA  
2890  C C   . LEU B 359  ? 0.9963 1.0303 0.8248 -0.1638 -0.1233 -0.0569 356  LEU A C   
2891  O O   . LEU B 359  ? 0.9926 1.0371 0.8351 -0.1379 -0.1098 -0.0630 356  LEU A O   
2892  C CB  . LEU B 359  ? 0.9032 0.8968 0.7318 -0.1641 -0.1222 -0.0524 356  LEU A CB  
2893  C CG  . LEU B 359  ? 0.8564 0.8007 0.6688 -0.1688 -0.1289 -0.0521 356  LEU A CG  
2894  C CD1 . LEU B 359  ? 0.8136 0.7790 0.6464 -0.1646 -0.1197 -0.0462 356  LEU A CD1 
2895  C CD2 . LEU B 359  ? 0.8492 0.7430 0.6457 -0.1469 -0.1280 -0.0635 356  LEU A CD2 
2896  N N   . ASN B 360  ? 1.0468 1.1147 0.8743 -0.1860 -0.1313 -0.0498 357  ASN A N   
2897  C CA  . ASN B 360  ? 1.0379 1.1581 0.8809 -0.1781 -0.1240 -0.0496 357  ASN A CA  
2898  C C   . ASN B 360  ? 1.0606 1.1621 0.8908 -0.1696 -0.1265 -0.0589 357  ASN A C   
2899  O O   . ASN B 360  ? 1.0649 1.2016 0.9075 -0.1555 -0.1180 -0.0613 357  ASN A O   
2900  C CB  . ASN B 360  ? 1.0707 1.2429 0.9190 -0.2047 -0.1311 -0.0372 357  ASN A CB  
2901  C CG  . ASN B 360  ? 1.1170 1.3094 0.9762 -0.2155 -0.1301 -0.0270 357  ASN A CG  
2902  O OD1 . ASN B 360  ? 1.1051 1.3337 0.9853 -0.1991 -0.1173 -0.0250 357  ASN A OD1 
2903  N ND2 . ASN B 360  ? 1.1682 1.3351 1.0109 -0.2432 -0.1442 -0.0203 357  ASN A ND2 
2904  N N   . SER B 361  ? 1.0769 1.1227 0.8807 -0.1766 -0.1382 -0.0642 358  SER A N   
2905  C CA  . SER B 361  ? 1.0664 1.0925 0.8549 -0.1701 -0.1422 -0.0729 358  SER A CA  
2906  C C   . SER B 361  ? 1.0868 1.0522 0.8570 -0.1511 -0.1425 -0.0841 358  SER A C   
2907  O O   . SER B 361  ? 1.0665 1.0229 0.8310 -0.1355 -0.1400 -0.0925 358  SER A O   
2908  C CB  . SER B 361  ? 1.0878 1.1114 0.8554 -0.2017 -0.1605 -0.0678 358  SER A CB  
2909  O OG  . SER B 361  ? 1.1221 1.1021 0.8667 -0.2235 -0.1750 -0.0638 358  SER A OG  
2910  N N   . ILE B 362  ? 1.1162 1.0421 0.8764 -0.1507 -0.1454 -0.0842 359  ILE A N   
2911  C CA  . ILE B 362  ? 1.1413 1.0115 0.8814 -0.1315 -0.1465 -0.0943 359  ILE A CA  
2912  C C   . ILE B 362  ? 1.1330 1.0170 0.8946 -0.0998 -0.1282 -0.0999 359  ILE A C   
2913  O O   . ILE B 362  ? 1.1214 1.0504 0.9107 -0.0940 -0.1158 -0.0957 359  ILE A O   
2914  C CB  . ILE B 362  ? 1.1013 0.9237 0.8204 -0.1414 -0.1569 -0.0923 359  ILE A CB  
2915  C CG1 . ILE B 362  ? 1.0018 0.8454 0.7449 -0.1370 -0.1461 -0.0863 359  ILE A CG1 
2916  C CG2 . ILE B 362  ? 1.1300 0.9366 0.8250 -0.1761 -0.1765 -0.0855 359  ILE A CG2 
2917  C CD1 . ILE B 362  ? 0.9789 0.7768 0.7027 -0.1438 -0.1548 -0.0845 359  ILE A CD1 
2918  N N   . ASP B 363  ? 1.1319 0.9770 0.8787 -0.0791 -0.1271 -0.1091 360  ASP A N   
2919  C CA  . ASP B 363  ? 1.0873 0.9433 0.8513 -0.0505 -0.1111 -0.1138 360  ASP A CA  
2920  C C   . ASP B 363  ? 1.0476 0.9063 0.8261 -0.0460 -0.1036 -0.1093 360  ASP A C   
2921  O O   . ASP B 363  ? 1.0549 0.8765 0.8175 -0.0464 -0.1098 -0.1100 360  ASP A O   
2922  C CB  . ASP B 363  ? 1.1439 0.9607 0.8859 -0.0308 -0.1133 -0.1239 360  ASP A CB  
2923  C CG  . ASP B 363  ? 1.1531 0.9838 0.9117 -0.0032 -0.0975 -0.1277 360  ASP A CG  
2924  O OD1 . ASP B 363  ? 1.1449 1.0163 0.9300 0.0004  -0.0856 -0.1238 360  ASP A OD1 
2925  O OD2 . ASP B 363  ? 1.1724 0.9732 0.9156 0.0151  -0.0976 -0.1342 360  ASP A OD2 
2926  N N   . LEU B 364  ? 1.0064 0.9073 0.8129 -0.0407 -0.0908 -0.1049 361  LEU A N   
2927  C CA  . LEU B 364  ? 0.9640 0.8720 0.7856 -0.0379 -0.0837 -0.1000 361  LEU A CA  
2928  C C   . LEU B 364  ? 0.9510 0.8469 0.7771 -0.0136 -0.0735 -0.1045 361  LEU A C   
2929  O O   . LEU B 364  ? 0.9200 0.8195 0.7575 -0.0103 -0.0677 -0.1008 361  LEU A O   
2930  C CB  . LEU B 364  ? 0.8927 0.8497 0.7387 -0.0434 -0.0759 -0.0930 361  LEU A CB  
2931  C CG  . LEU B 364  ? 0.8776 0.8564 0.7230 -0.0687 -0.0850 -0.0857 361  LEU A CG  
2932  C CD1 . LEU B 364  ? 0.8298 0.8585 0.6984 -0.0688 -0.0761 -0.0791 361  LEU A CD1 
2933  C CD2 . LEU B 364  ? 0.9016 0.8504 0.7320 -0.0875 -0.0969 -0.0816 361  LEU A CD2 
2934  N N   . THR B 365  ? 0.9533 0.8375 0.7708 0.0029  -0.0713 -0.1118 362  THR A N   
2935  C CA  . THR B 365  ? 0.9136 0.7890 0.7338 0.0248  -0.0626 -0.1151 362  THR A CA  
2936  C C   . THR B 365  ? 0.9369 0.7725 0.7379 0.0292  -0.0694 -0.1174 362  THR A C   
2937  O O   . THR B 365  ? 0.9568 0.7878 0.7600 0.0470  -0.0626 -0.1190 362  THR A O   
2938  C CB  . THR B 365  ? 0.8838 0.7630 0.7006 0.0414  -0.0580 -0.1215 362  THR A CB  
2939  O OG1 . THR B 365  ? 0.9232 0.7699 0.7136 0.0417  -0.0692 -0.1279 362  THR A OG1 
2940  C CG2 . THR B 365  ? 0.8510 0.7659 0.6825 0.0377  -0.0527 -0.1197 362  THR A CG2 
2941  N N   . HIS B 366  ? 0.9701 0.7773 0.7509 0.0133  -0.0831 -0.1171 363  HIS A N   
2942  C CA  . HIS B 366  ? 1.0171 0.7816 0.7750 0.0172  -0.0913 -0.1192 363  HIS A CA  
2943  C C   . HIS B 366  ? 1.0102 0.7682 0.7690 -0.0021 -0.0971 -0.1119 363  HIS A C   
2944  O O   . HIS B 366  ? 1.0578 0.7765 0.7940 -0.0024 -0.1062 -0.1129 363  HIS A O   
2945  C CB  . HIS B 366  ? 1.0946 0.8176 0.8176 0.0181  -0.1049 -0.1264 363  HIS A CB  
2946  C CG  . HIS B 366  ? 1.1377 0.8607 0.8554 0.0414  -0.0996 -0.1342 363  HIS A CG  
2947  N ND1 . HIS B 366  ? 1.1763 0.8831 0.8842 0.0666  -0.0957 -0.1390 363  HIS A ND1 
2948  C CD2 . HIS B 366  ? 1.1428 0.8826 0.8635 0.0438  -0.0975 -0.1377 363  HIS A CD2 
2949  C CE1 . HIS B 366  ? 1.1754 0.8897 0.8807 0.0830  -0.0914 -0.1447 363  HIS A CE1 
2950  N NE2 . HIS B 366  ? 1.1559 0.8885 0.8687 0.0694  -0.0925 -0.1443 363  HIS A NE2 
2951  N N   . ILE B 367  ? 0.9556 0.7508 0.7381 -0.0172 -0.0924 -0.1045 364  ILE A N   
2952  C CA  . ILE B 367  ? 0.9279 0.7254 0.7162 -0.0337 -0.0954 -0.0967 364  ILE A CA  
2953  C C   . ILE B 367  ? 0.8539 0.6752 0.6670 -0.0205 -0.0814 -0.0939 364  ILE A C   
2954  O O   . ILE B 367  ? 0.8385 0.6976 0.6744 -0.0165 -0.0708 -0.0919 364  ILE A O   
2955  C CB  . ILE B 367  ? 0.9079 0.7339 0.7046 -0.0587 -0.1000 -0.0896 364  ILE A CB  
2956  C CG1 . ILE B 367  ? 0.9478 0.7516 0.7191 -0.0735 -0.1146 -0.0920 364  ILE A CG1 
2957  C CG2 . ILE B 367  ? 0.8671 0.6973 0.6693 -0.0756 -0.1031 -0.0809 364  ILE A CG2 
2958  C CD1 . ILE B 367  ? 0.9858 0.7340 0.7235 -0.0814 -0.1298 -0.0934 364  ILE A CD1 
2959  N N   . PHE B 368  ? 0.8280 0.6258 0.6345 -0.0135 -0.0819 -0.0936 365  PHE A N   
2960  C CA  . PHE B 368  ? 0.7814 0.5968 0.6076 0.0008  -0.0695 -0.0918 365  PHE A CA  
2961  C C   . PHE B 368  ? 0.7757 0.6017 0.6140 -0.0125 -0.0690 -0.0839 365  PHE A C   
2962  O O   . PHE B 368  ? 0.7804 0.5839 0.6045 -0.0271 -0.0795 -0.0809 365  PHE A O   
2963  C CB  . PHE B 368  ? 0.7989 0.5869 0.6108 0.0217  -0.0690 -0.0970 365  PHE A CB  
2964  C CG  . PHE B 368  ? 0.8497 0.6341 0.6528 0.0388  -0.0669 -0.1044 365  PHE A CG  
2965  C CD1 . PHE B 368  ? 0.8880 0.6393 0.6629 0.0391  -0.0782 -0.1104 365  PHE A CD1 
2966  C CD2 . PHE B 368  ? 0.8412 0.6545 0.6626 0.0538  -0.0542 -0.1049 365  PHE A CD2 
2967  C CE1 . PHE B 368  ? 0.9120 0.6610 0.6784 0.0558  -0.0762 -0.1173 365  PHE A CE1 
2968  C CE2 . PHE B 368  ? 0.8598 0.6722 0.6735 0.0691  -0.0521 -0.1109 365  PHE A CE2 
2969  C CZ  . PHE B 368  ? 0.9059 0.6872 0.6928 0.0710  -0.0627 -0.1174 365  PHE A CZ  
2970  N N   . ILE B 369  ? 0.7554 0.6140 0.6182 -0.0075 -0.0574 -0.0802 366  ILE A N   
2971  C CA  . ILE B 369  ? 0.7489 0.6205 0.6250 -0.0162 -0.0550 -0.0731 366  ILE A CA  
2972  C C   . ILE B 369  ? 0.7669 0.6283 0.6457 -0.0015 -0.0494 -0.0735 366  ILE A C   
2973  O O   . ILE B 369  ? 0.7722 0.6401 0.6561 0.0154  -0.0416 -0.0767 366  ILE A O   
2974  C CB  . ILE B 369  ? 0.7125 0.6256 0.6104 -0.0198 -0.0469 -0.0689 366  ILE A CB  
2975  C CG1 . ILE B 369  ? 0.7004 0.6289 0.5958 -0.0343 -0.0527 -0.0677 366  ILE A CG1 
2976  C CG2 . ILE B 369  ? 0.6975 0.6236 0.6081 -0.0257 -0.0438 -0.0621 366  ILE A CG2 
2977  C CD1 . ILE B 369  ? 0.6966 0.6136 0.5808 -0.0561 -0.0645 -0.0627 366  ILE A CD1 
2978  N N   . SER B 370  ? 0.7855 0.6327 0.6607 -0.0084 -0.0536 -0.0695 367  SER A N   
2979  C CA  . SER B 370  ? 0.7829 0.6218 0.6600 0.0049  -0.0490 -0.0692 367  SER A CA  
2980  C C   . SER B 370  ? 0.7836 0.6555 0.6851 0.0097  -0.0372 -0.0654 367  SER A C   
2981  O O   . SER B 370  ? 0.7687 0.6635 0.6835 -0.0009 -0.0348 -0.0609 367  SER A O   
2982  C CB  . SER B 370  ? 0.7970 0.6115 0.6627 -0.0045 -0.0572 -0.0656 367  SER A CB  
2983  O OG  . SER B 370  ? 0.8084 0.6180 0.6768 0.0088  -0.0525 -0.0650 367  SER A OG  
2984  N N   . HIS B 371  ? 0.7975 0.6719 0.7027 0.0261  -0.0304 -0.0670 368  HIS A N   
2985  C CA  . HIS B 371  ? 0.7706 0.6716 0.6952 0.0296  -0.0205 -0.0630 368  HIS A CA  
2986  C C   . HIS B 371  ? 0.7526 0.6566 0.6851 0.0214  -0.0204 -0.0571 368  HIS A C   
2987  O O   . HIS B 371  ? 0.7378 0.6631 0.6847 0.0185  -0.0146 -0.0531 368  HIS A O   
2988  C CB  . HIS B 371  ? 0.8146 0.7192 0.7399 0.0467  -0.0143 -0.0648 368  HIS A CB  
2989  C CG  . HIS B 371  ? 0.8993 0.7854 0.8142 0.0559  -0.0172 -0.0654 368  HIS A CG  
2990  N ND1 . HIS B 371  ? 0.9661 0.8309 0.8621 0.0677  -0.0220 -0.0710 368  HIS A ND1 
2991  C CD2 . HIS B 371  ? 0.9033 0.7889 0.8223 0.0568  -0.0161 -0.0613 368  HIS A CD2 
2992  C CE1 . HIS B 371  ? 0.9597 0.8117 0.8477 0.0765  -0.0238 -0.0704 368  HIS A CE1 
2993  N NE2 . HIS B 371  ? 0.9276 0.7927 0.8302 0.0696  -0.0202 -0.0643 368  HIS A NE2 
2994  N N   . LYS B 372  ? 0.7754 0.6563 0.6966 0.0180  -0.0274 -0.0565 369  LYS A N   
2995  C CA  . LYS B 372  ? 0.7912 0.6736 0.7187 0.0094  -0.0281 -0.0507 369  LYS A CA  
2996  C C   . LYS B 372  ? 0.7937 0.6906 0.7281 -0.0078 -0.0304 -0.0463 369  LYS A C   
2997  O O   . LYS B 372  ? 0.7996 0.7052 0.7424 -0.0146 -0.0294 -0.0410 369  LYS A O   
2998  C CB  . LYS B 372  ? 0.8164 0.6669 0.7264 0.0105  -0.0361 -0.0512 369  LYS A CB  
2999  C CG  . LYS B 372  ? 0.8268 0.6657 0.7283 0.0302  -0.0340 -0.0550 369  LYS A CG  
3000  C CD  . LYS B 372  ? 0.8602 0.6630 0.7390 0.0332  -0.0433 -0.0563 369  LYS A CD  
3001  C CE  . LYS B 372  ? 0.8543 0.6496 0.7234 0.0561  -0.0410 -0.0600 369  LYS A CE  
3002  N NZ  . LYS B 372  ? 0.9021 0.6579 0.7439 0.0622  -0.0509 -0.0621 369  LYS A NZ  
3003  N N   . LYS B 373  ? 0.7795 0.6818 0.7104 -0.0144 -0.0335 -0.0482 370  LYS A N   
3004  C CA  . LYS B 373  ? 0.7267 0.6486 0.6635 -0.0300 -0.0359 -0.0436 370  LYS A CA  
3005  C C   . LYS B 373  ? 0.6691 0.6207 0.6171 -0.0264 -0.0293 -0.0444 370  LYS A C   
3006  O O   . LYS B 373  ? 0.6787 0.6531 0.6325 -0.0362 -0.0301 -0.0404 370  LYS A O   
3007  C CB  . LYS B 373  ? 0.7361 0.6406 0.6566 -0.0447 -0.0474 -0.0435 370  LYS A CB  
3008  C CG  . LYS B 373  ? 0.7861 0.6526 0.6883 -0.0475 -0.0560 -0.0437 370  LYS A CG  
3009  C CD  . LYS B 373  ? 0.8230 0.6917 0.7311 -0.0552 -0.0564 -0.0369 370  LYS A CD  
3010  C CE  . LYS B 373  ? 0.8915 0.7193 0.7781 -0.0574 -0.0659 -0.0370 370  LYS A CE  
3011  N NZ  . LYS B 373  ? 0.9238 0.7531 0.8155 -0.0652 -0.0664 -0.0302 370  LYS A NZ  
3012  N N   . LEU B 374  ? 0.6158 0.5689 0.5657 -0.0121 -0.0231 -0.0490 371  LEU A N   
3013  C CA  . LEU B 374  ? 0.6069 0.5831 0.5631 -0.0080 -0.0180 -0.0502 371  LEU A CA  
3014  C C   . LEU B 374  ? 0.5486 0.5482 0.5160 -0.0084 -0.0128 -0.0455 371  LEU A C   
3015  O O   . LEU B 374  ? 0.5242 0.5458 0.4944 -0.0106 -0.0121 -0.0444 371  LEU A O   
3016  C CB  . LEU B 374  ? 0.6156 0.5868 0.5703 0.0067  -0.0126 -0.0551 371  LEU A CB  
3017  C CG  . LEU B 374  ? 0.5701 0.5607 0.5285 0.0123  -0.0076 -0.0566 371  LEU A CG  
3018  C CD1 . LEU B 374  ? 0.5707 0.5692 0.5244 0.0053  -0.0125 -0.0584 371  LEU A CD1 
3019  C CD2 . LEU B 374  ? 0.5578 0.5431 0.5144 0.0252  -0.0026 -0.0601 371  LEU A CD2 
3020  N N   . GLU B 375  ? 0.5388 0.5346 0.5114 -0.0052 -0.0095 -0.0428 372  GLU A N   
3021  C CA  . GLU B 375  ? 0.5744 0.5885 0.5544 -0.0045 -0.0054 -0.0387 372  GLU A CA  
3022  C C   . GLU B 375  ? 0.5939 0.6226 0.5764 -0.0166 -0.0096 -0.0338 372  GLU A C   
3023  O O   . GLU B 375  ? 0.5997 0.6515 0.5857 -0.0155 -0.0073 -0.0314 372  GLU A O   
3024  C CB  . GLU B 375  ? 0.6012 0.6066 0.5850 0.0006  -0.0017 -0.0368 372  GLU A CB  
3025  C CG  . GLU B 375  ? 0.6464 0.6503 0.6295 0.0115  0.0039  -0.0389 372  GLU A CG  
3026  C CD  . GLU B 375  ? 0.7106 0.7043 0.6887 0.0169  0.0037  -0.0436 372  GLU A CD  
3027  O OE1 . GLU B 375  ? 0.7708 0.7502 0.7457 0.0163  0.0005  -0.0448 372  GLU A OE1 
3028  O OE2 . GLU B 375  ? 0.6979 0.6969 0.6734 0.0227  0.0064  -0.0461 372  GLU A OE2 
3029  N N   . THR B 376  ? 0.6192 0.6350 0.5980 -0.0278 -0.0161 -0.0320 373  THR A N   
3030  C CA  . THR B 376  ? 0.6439 0.6753 0.6242 -0.0421 -0.0211 -0.0261 373  THR A CA  
3031  C C   . THR B 376  ? 0.6552 0.7090 0.6341 -0.0476 -0.0235 -0.0259 373  THR A C   
3032  O O   . THR B 376  ? 0.6582 0.7420 0.6421 -0.0525 -0.0233 -0.0209 373  THR A O   
3033  C CB  . THR B 376  ? 0.6867 0.6939 0.6594 -0.0540 -0.0289 -0.0239 373  THR A CB  
3034  O OG1 . THR B 376  ? 0.7169 0.7060 0.6910 -0.0470 -0.0263 -0.0241 373  THR A OG1 
3035  C CG2 . THR B 376  ? 0.6745 0.6990 0.6484 -0.0713 -0.0345 -0.0162 373  THR A CG2 
3036  N N   . ILE B 377  ? 0.6741 0.7163 0.6458 -0.0462 -0.0258 -0.0311 374  ILE A N   
3037  C CA  . ILE B 377  ? 0.6621 0.7262 0.6322 -0.0511 -0.0282 -0.0312 374  ILE A CA  
3038  C C   . ILE B 377  ? 0.6656 0.7578 0.6423 -0.0380 -0.0205 -0.0319 374  ILE A C   
3039  O O   . ILE B 377  ? 0.6674 0.7915 0.6464 -0.0415 -0.0212 -0.0286 374  ILE A O   
3040  C CB  . ILE B 377  ? 0.6313 0.6731 0.5907 -0.0510 -0.0324 -0.0373 374  ILE A CB  
3041  C CG1 . ILE B 377  ? 0.6402 0.6507 0.5875 -0.0637 -0.0420 -0.0365 374  ILE A CG1 
3042  C CG2 . ILE B 377  ? 0.6217 0.6877 0.5799 -0.0551 -0.0345 -0.0376 374  ILE A CG2 
3043  C CD1 . ILE B 377  ? 0.6656 0.6480 0.5987 -0.0605 -0.0466 -0.0433 374  ILE A CD1 
3044  N N   . SER B 378  ? 0.6732 0.7542 0.6510 -0.0226 -0.0136 -0.0358 375  SER A N   
3045  C CA  . SER B 378  ? 0.6539 0.7539 0.6329 -0.0093 -0.0074 -0.0367 375  SER A CA  
3046  C C   . SER B 378  ? 0.6454 0.7705 0.6286 -0.0097 -0.0062 -0.0310 375  SER A C   
3047  O O   . SER B 378  ? 0.6526 0.8044 0.6344 -0.0031 -0.0045 -0.0302 375  SER A O   
3048  C CB  . SER B 378  ? 0.6480 0.7276 0.6252 0.0037  -0.0018 -0.0404 375  SER A CB  
3049  O OG  . SER B 378  ? 0.6372 0.7280 0.6104 0.0163  0.0027  -0.0419 375  SER A OG  
3050  N N   . SER B 379  ? 0.6693 0.7869 0.6564 -0.0159 -0.0073 -0.0270 376  SER A N   
3051  C CA  . SER B 379  ? 0.6753 0.8166 0.6659 -0.0157 -0.0062 -0.0215 376  SER A CA  
3052  C C   . SER B 379  ? 0.6654 0.8387 0.6587 -0.0286 -0.0110 -0.0157 376  SER A C   
3053  O O   . SER B 379  ? 0.6727 0.8770 0.6676 -0.0247 -0.0094 -0.0115 376  SER A O   
3054  C CB  . SER B 379  ? 0.7038 0.8278 0.6980 -0.0190 -0.0060 -0.0188 376  SER A CB  
3055  O OG  . SER B 379  ? 0.7441 0.8895 0.7405 -0.0164 -0.0044 -0.0140 376  SER A OG  
3056  N N   . ALA B 380  ? 0.6740 0.8408 0.6659 -0.0438 -0.0174 -0.0151 377  ALA A N   
3057  C CA  . ALA B 380  ? 0.7111 0.9080 0.7043 -0.0602 -0.0235 -0.0083 377  ALA A CA  
3058  C C   . ALA B 380  ? 0.7172 0.9436 0.7088 -0.0573 -0.0235 -0.0093 377  ALA A C   
3059  O O   . ALA B 380  ? 0.7454 1.0106 0.7395 -0.0667 -0.0266 -0.0025 377  ALA A O   
3060  C CB  . ALA B 380  ? 0.7309 0.9028 0.7193 -0.0806 -0.0324 -0.0063 377  ALA A CB  
3061  N N   . LEU B 381  ? 0.6969 0.9084 0.6843 -0.0447 -0.0203 -0.0170 378  LEU A N   
3062  C CA  . LEU B 381  ? 0.6825 0.9192 0.6674 -0.0409 -0.0204 -0.0186 378  LEU A CA  
3063  C C   . LEU B 381  ? 0.7255 0.9730 0.7078 -0.0174 -0.0126 -0.0228 378  LEU A C   
3064  O O   . LEU B 381  ? 0.7294 1.0054 0.7095 -0.0117 -0.0121 -0.0231 378  LEU A O   
3065  C CB  . LEU B 381  ? 0.6903 0.9009 0.6693 -0.0474 -0.0247 -0.0240 378  LEU A CB  
3066  C CG  . LEU B 381  ? 0.7349 0.9247 0.7099 -0.0696 -0.0342 -0.0212 378  LEU A CG  
3067  C CD1 . LEU B 381  ? 0.7531 0.9199 0.7188 -0.0729 -0.0388 -0.0271 378  LEU A CD1 
3068  C CD2 . LEU B 381  ? 0.7626 0.9876 0.7402 -0.0888 -0.0404 -0.0113 378  LEU A CD2 
3069  N N   . CYS B 382  ? 0.7845 1.0094 0.7651 -0.0040 -0.0073 -0.0258 379  CYS A N   
3070  C CA  . CYS B 382  ? 0.8348 1.0611 0.8079 0.0174  -0.0015 -0.0300 379  CYS A CA  
3071  C C   . CYS B 382  ? 0.8670 1.0970 0.8375 0.0282  0.0019  -0.0275 379  CYS A C   
3072  O O   . CYS B 382  ? 0.8487 1.0885 0.8255 0.0194  0.0002  -0.0221 379  CYS A O   
3073  C CB  . CYS B 382  ? 0.8256 1.0148 0.7940 0.0240  0.0009  -0.0368 379  CYS A CB  
3074  S SG  . CYS B 382  ? 0.8082 0.9862 0.7774 0.0130  -0.0034 -0.0406 379  CYS A SG  
3075  N N   . ASP B 383  ? 0.9548 1.1747 0.9140 0.0472  0.0060  -0.0315 380  ASP A N   
3076  C CA  . ASP B 383  ? 1.0271 1.2464 0.9789 0.0594  0.0083  -0.0299 380  ASP A CA  
3077  C C   . ASP B 383  ? 1.0285 1.2197 0.9857 0.0511  0.0082  -0.0286 380  ASP A C   
3078  O O   . ASP B 383  ? 1.0317 1.2333 0.9924 0.0483  0.0077  -0.0240 380  ASP A O   
3079  C CB  . ASP B 383  ? 1.0929 1.2984 1.0266 0.0803  0.0110  -0.0347 380  ASP A CB  
3080  C CG  . ASP B 383  ? 1.1402 1.3736 1.0671 0.0910  0.0112  -0.0364 380  ASP A CG  
3081  O OD1 . ASP B 383  ? 1.1665 1.3935 1.0948 0.0878  0.0110  -0.0398 380  ASP A OD1 
3082  O OD2 . ASP B 383  ? 1.1522 1.4151 1.0715 0.1038  0.0116  -0.0342 380  ASP A OD2 
3083  N N   . HIS B 384  ? 0.9846 1.1425 0.9423 0.0476  0.0089  -0.0321 381  HIS A N   
3084  C CA  . HIS B 384  ? 0.9666 1.0992 0.9286 0.0413  0.0090  -0.0309 381  HIS A CA  
3085  C C   . HIS B 384  ? 0.9123 1.0268 0.8825 0.0296  0.0076  -0.0326 381  HIS A C   
3086  O O   . HIS B 384  ? 0.9005 1.0182 0.8713 0.0270  0.0064  -0.0352 381  HIS A O   
3087  C CB  . HIS B 384  ? 0.9878 1.0963 0.9373 0.0531  0.0115  -0.0329 381  HIS A CB  
3088  C CG  . HIS B 384  ? 1.0308 1.1486 0.9640 0.0697  0.0123  -0.0339 381  HIS A CG  
3089  N ND1 . HIS B 384  ? 1.0538 1.1626 0.9730 0.0813  0.0131  -0.0379 381  HIS A ND1 
3090  C CD2 . HIS B 384  ? 1.0503 1.1852 0.9769 0.0784  0.0119  -0.0314 381  HIS A CD2 
3091  C CE1 . HIS B 384  ? 1.0690 1.1863 0.9719 0.0970  0.0130  -0.0382 381  HIS A CE1 
3092  N NE2 . HIS B 384  ? 1.0652 1.1993 0.9721 0.0963  0.0124  -0.0344 381  HIS A NE2 
3093  N N   . TRP B 385  ? 0.8591 0.9543 0.8340 0.0238  0.0075  -0.0311 382  TRP A N   
3094  C CA  . TRP B 385  ? 0.8300 0.9050 0.8091 0.0170  0.0064  -0.0331 382  TRP A CA  
3095  C C   . TRP B 385  ? 0.8675 0.9277 0.8406 0.0254  0.0092  -0.0375 382  TRP A C   
3096  O O   . TRP B 385  ? 0.8938 0.9426 0.8686 0.0227  0.0084  -0.0400 382  TRP A O   
3097  C CB  . TRP B 385  ? 0.7616 0.8223 0.7458 0.0118  0.0061  -0.0302 382  TRP A CB  
3098  C CG  . TRP B 385  ? 0.6957 0.7460 0.6753 0.0196  0.0094  -0.0296 382  TRP A CG  
3099  C CD1 . TRP B 385  ? 0.6679 0.7247 0.6428 0.0247  0.0103  -0.0273 382  TRP A CD1 
3100  C CD2 . TRP B 385  ? 0.6878 0.7197 0.6650 0.0228  0.0115  -0.0309 382  TRP A CD2 
3101  N NE1 . TRP B 385  ? 0.6723 0.7118 0.6405 0.0294  0.0120  -0.0272 382  TRP A NE1 
3102  C CE2 . TRP B 385  ? 0.6774 0.7037 0.6479 0.0273  0.0129  -0.0289 382  TRP A CE2 
3103  C CE3 . TRP B 385  ? 0.6888 0.7099 0.6678 0.0223  0.0120  -0.0333 382  TRP A CE3 
3104  C CZ2 . TRP B 385  ? 0.6874 0.6986 0.6536 0.0286  0.0143  -0.0282 382  TRP A CZ2 
3105  C CZ3 . TRP B 385  ? 0.6733 0.6835 0.6495 0.0253  0.0143  -0.0326 382  TRP A CZ3 
3106  C CH2 . TRP B 385  ? 0.6861 0.6919 0.6564 0.0271  0.0152  -0.0296 382  TRP A CH2 
3107  N N   . ASP B 386  ? 0.8929 0.9520 0.8569 0.0357  0.0118  -0.0382 383  ASP A N   
3108  C CA  . ASP B 386  ? 0.8585 0.9026 0.8150 0.0421  0.0140  -0.0409 383  ASP A CA  
3109  C C   . ASP B 386  ? 0.8327 0.8838 0.7862 0.0458  0.0141  -0.0450 383  ASP A C   
3110  O O   . ASP B 386  ? 0.8348 0.8748 0.7866 0.0473  0.0153  -0.0474 383  ASP A O   
3111  C CB  . ASP B 386  ? 0.9036 0.9394 0.8468 0.0507  0.0153  -0.0398 383  ASP A CB  
3112  C CG  . ASP B 386  ? 0.9971 1.0146 0.9396 0.0472  0.0158  -0.0370 383  ASP A CG  
3113  O OD1 . ASP B 386  ? 1.0408 1.0522 0.9910 0.0419  0.0165  -0.0369 383  ASP A OD1 
3114  O OD2 . ASP B 386  ? 1.0482 1.0579 0.9809 0.0503  0.0152  -0.0348 383  ASP A OD2 
3115  N N   . THR B 387  ? 0.7881 0.8601 0.7407 0.0475  0.0128  -0.0454 384  THR A N   
3116  C CA  . THR B 387  ? 0.7709 0.8512 0.7172 0.0542  0.0132  -0.0490 384  THR A CA  
3117  C C   . THR B 387  ? 0.7469 0.8202 0.6978 0.0489  0.0123  -0.0522 384  THR A C   
3118  O O   . THR B 387  ? 0.7503 0.8178 0.6949 0.0554  0.0139  -0.0555 384  THR A O   
3119  C CB  . THR B 387  ? 0.7802 0.8903 0.7266 0.0556  0.0116  -0.0477 384  THR A CB  
3120  O OG1 . THR B 387  ? 0.8158 0.9376 0.7737 0.0418  0.0083  -0.0445 384  THR A OG1 
3121  C CG2 . THR B 387  ? 0.7570 0.8738 0.6932 0.0673  0.0130  -0.0459 384  THR A CG2 
3122  N N   . LEU B 388  ? 0.7054 0.7769 0.6649 0.0377  0.0091  -0.0514 385  LEU A N   
3123  C CA  . LEU B 388  ? 0.6748 0.7370 0.6348 0.0341  0.0071  -0.0551 385  LEU A CA  
3124  C C   . LEU B 388  ? 0.6687 0.7108 0.6267 0.0396  0.0101  -0.0569 385  LEU A C   
3125  O O   . LEU B 388  ? 0.6843 0.7227 0.6379 0.0450  0.0113  -0.0604 385  LEU A O   
3126  C CB  . LEU B 388  ? 0.6741 0.7338 0.6386 0.0211  0.0016  -0.0536 385  LEU A CB  
3127  C CG  . LEU B 388  ? 0.6850 0.7675 0.6504 0.0125  -0.0029 -0.0517 385  LEU A CG  
3128  C CD1 . LEU B 388  ? 0.6681 0.7398 0.6320 -0.0014 -0.0101 -0.0516 385  LEU A CD1 
3129  C CD2 . LEU B 388  ? 0.7042 0.8031 0.6653 0.0200  -0.0013 -0.0546 385  LEU A CD2 
3130  N N   . ARG B 389  ? 0.6607 0.6924 0.6221 0.0380  0.0112  -0.0539 386  ARG A N   
3131  C CA  . ARG B 389  ? 0.6781 0.6967 0.6383 0.0424  0.0141  -0.0542 386  ARG A CA  
3132  C C   . ARG B 389  ? 0.7156 0.7344 0.6682 0.0501  0.0175  -0.0544 386  ARG A C   
3133  O O   . ARG B 389  ? 0.7474 0.7612 0.6974 0.0539  0.0194  -0.0557 386  ARG A O   
3134  C CB  . ARG B 389  ? 0.7069 0.7189 0.6719 0.0391  0.0146  -0.0500 386  ARG A CB  
3135  C CG  . ARG B 389  ? 0.7361 0.7405 0.7011 0.0426  0.0172  -0.0490 386  ARG A CG  
3136  C CD  . ARG B 389  ? 0.7686 0.7706 0.7366 0.0397  0.0184  -0.0438 386  ARG A CD  
3137  N NE  . ARG B 389  ? 0.7994 0.8024 0.7616 0.0400  0.0193  -0.0414 386  ARG A NE  
3138  C CZ  . ARG B 389  ? 0.8215 0.8205 0.7827 0.0374  0.0196  -0.0369 386  ARG A CZ  
3139  N NH1 . ARG B 389  ? 0.8286 0.8262 0.7967 0.0337  0.0198  -0.0339 386  ARG A NH1 
3140  N NH2 . ARG B 389  ? 0.8177 0.8132 0.7690 0.0392  0.0194  -0.0355 386  ARG A NH2 
3141  N N   . ASN B 390  ? 0.7209 0.7450 0.6680 0.0529  0.0180  -0.0530 387  ASN A N   
3142  C CA  . ASN B 390  ? 0.7309 0.7500 0.6660 0.0604  0.0200  -0.0531 387  ASN A CA  
3143  C C   . ASN B 390  ? 0.7480 0.7733 0.6786 0.0658  0.0202  -0.0575 387  ASN A C   
3144  O O   . ASN B 390  ? 0.7660 0.7844 0.6894 0.0701  0.0220  -0.0582 387  ASN A O   
3145  C CB  . ASN B 390  ? 0.7544 0.7737 0.6803 0.0643  0.0195  -0.0510 387  ASN A CB  
3146  C CG  . ASN B 390  ? 0.7765 0.7857 0.7032 0.0597  0.0193  -0.0465 387  ASN A CG  
3147  O OD1 . ASN B 390  ? 0.8017 0.7970 0.7162 0.0617  0.0192  -0.0441 387  ASN A OD1 
3148  N ND2 . ASN B 390  ? 0.7804 0.7950 0.7196 0.0528  0.0184  -0.0451 387  ASN A ND2 
3149  N N   . ALA B 391  ? 0.7391 0.7790 0.6737 0.0646  0.0182  -0.0599 388  ALA A N   
3150  C CA  . ALA B 391  ? 0.7033 0.7511 0.6339 0.0691  0.0180  -0.0639 388  ALA A CA  
3151  C C   . ALA B 391  ? 0.7295 0.7686 0.6627 0.0679  0.0182  -0.0667 388  ALA A C   
3152  O O   . ALA B 391  ? 0.7478 0.7856 0.6746 0.0741  0.0197  -0.0692 388  ALA A O   
3153  C CB  . ALA B 391  ? 0.6516 0.7197 0.5865 0.0653  0.0148  -0.0647 388  ALA A CB  
3154  N N   . LEU B 392  ? 0.7139 0.7465 0.6546 0.0614  0.0165  -0.0664 389  LEU A N   
3155  C CA  . LEU B 392  ? 0.6909 0.7145 0.6315 0.0631  0.0167  -0.0691 389  LEU A CA  
3156  C C   . LEU B 392  ? 0.6869 0.7047 0.6243 0.0685  0.0209  -0.0669 389  LEU A C   
3157  O O   . LEU B 392  ? 0.6751 0.6917 0.6092 0.0735  0.0223  -0.0690 389  LEU A O   
3158  C CB  . LEU B 392  ? 0.6713 0.6866 0.6168 0.0571  0.0133  -0.0691 389  LEU A CB  
3159  C CG  . LEU B 392  ? 0.6800 0.6976 0.6262 0.0486  0.0075  -0.0705 389  LEU A CG  
3160  C CD1 . LEU B 392  ? 0.7135 0.7167 0.6606 0.0433  0.0036  -0.0699 389  LEU A CD1 
3161  C CD2 . LEU B 392  ? 0.6787 0.6989 0.6191 0.0498  0.0048  -0.0754 389  LEU A CD2 
3162  N N   . TYR B 393  ? 0.6959 0.7108 0.6333 0.0666  0.0225  -0.0620 390  TYR A N   
3163  C CA  . TYR B 393  ? 0.6774 0.6876 0.6103 0.0683  0.0254  -0.0582 390  TYR A CA  
3164  C C   . TYR B 393  ? 0.6830 0.6925 0.6047 0.0738  0.0267  -0.0592 390  TYR A C   
3165  O O   . TYR B 393  ? 0.7001 0.7094 0.6185 0.0761  0.0286  -0.0583 390  TYR A O   
3166  C CB  . TYR B 393  ? 0.6310 0.6362 0.5636 0.0635  0.0255  -0.0527 390  TYR A CB  
3167  C CG  . TYR B 393  ? 0.6445 0.6442 0.5692 0.0624  0.0271  -0.0475 390  TYR A CG  
3168  C CD1 . TYR B 393  ? 0.6507 0.6544 0.5803 0.0599  0.0287  -0.0439 390  TYR A CD1 
3169  C CD2 . TYR B 393  ? 0.6470 0.6374 0.5569 0.0636  0.0262  -0.0457 390  TYR A CD2 
3170  C CE1 . TYR B 393  ? 0.6532 0.6552 0.5754 0.0561  0.0294  -0.0377 390  TYR A CE1 
3171  C CE2 . TYR B 393  ? 0.6381 0.6202 0.5375 0.0598  0.0262  -0.0401 390  TYR A CE2 
3172  C CZ  . TYR B 393  ? 0.6362 0.6256 0.5427 0.0547  0.0278  -0.0356 390  TYR A CZ  
3173  O OH  . TYR B 393  ? 0.6301 0.6146 0.5261 0.0482  0.0271  -0.0285 390  TYR A OH  
3174  N N   . GLU B 394  ? 0.6864 0.6971 0.6012 0.0768  0.0256  -0.0607 391  GLU A N   
3175  C CA  . GLU B 394  ? 0.7132 0.7208 0.6143 0.0835  0.0263  -0.0615 391  GLU A CA  
3176  C C   . GLU B 394  ? 0.7238 0.7383 0.6263 0.0877  0.0271  -0.0662 391  GLU A C   
3177  O O   . GLU B 394  ? 0.7625 0.7732 0.6564 0.0915  0.0286  -0.0658 391  GLU A O   
3178  C CB  . GLU B 394  ? 0.7355 0.7446 0.6273 0.0888  0.0248  -0.0625 391  GLU A CB  
3179  C CG  . GLU B 394  ? 0.7713 0.7704 0.6569 0.0868  0.0236  -0.0582 391  GLU A CG  
3180  C CD  . GLU B 394  ? 0.8125 0.7924 0.6838 0.0852  0.0234  -0.0536 391  GLU A CD  
3181  O OE1 . GLU B 394  ? 0.8072 0.7811 0.6677 0.0887  0.0238  -0.0538 391  GLU A OE1 
3182  O OE2 . GLU B 394  ? 0.8466 0.8172 0.7166 0.0793  0.0222  -0.0492 391  GLU A OE2 
3183  N N   . ARG B 395  ? 0.7094 0.7327 0.6210 0.0863  0.0254  -0.0704 392  ARG A N   
3184  C CA  . ARG B 395  ? 0.6975 0.7255 0.6085 0.0901  0.0252  -0.0752 392  ARG A CA  
3185  C C   . ARG B 395  ? 0.6942 0.7179 0.6073 0.0911  0.0269  -0.0750 392  ARG A C   
3186  O O   . ARG B 395  ? 0.7165 0.7420 0.6250 0.0966  0.0280  -0.0776 392  ARG A O   
3187  C CB  . ARG B 395  ? 0.7124 0.7486 0.6295 0.0862  0.0214  -0.0791 392  ARG A CB  
3188  C CG  . ARG B 395  ? 0.7417 0.7840 0.6548 0.0902  0.0201  -0.0842 392  ARG A CG  
3189  C CD  . ARG B 395  ? 0.7957 0.8446 0.7128 0.0831  0.0149  -0.0870 392  ARG A CD  
3190  N NE  . ARG B 395  ? 0.8561 0.8936 0.7733 0.0809  0.0120  -0.0903 392  ARG A NE  
3191  C CZ  . ARG B 395  ? 0.9008 0.9368 0.8124 0.0841  0.0100  -0.0952 392  ARG A CZ  
3192  N NH1 . ARG B 395  ? 0.8960 0.9436 0.8036 0.0887  0.0111  -0.0970 392  ARG A NH1 
3193  N NH2 . ARG B 395  ? 0.9213 0.9434 0.8294 0.0839  0.0066  -0.0984 392  ARG A NH2 
3194  N N   . ARG B 396  ? 0.6815 0.7016 0.6010 0.0871  0.0272  -0.0719 393  ARG A N   
3195  C CA  . ARG B 396  ? 0.7067 0.7273 0.6276 0.0902  0.0291  -0.0710 393  ARG A CA  
3196  C C   . ARG B 396  ? 0.7263 0.7488 0.6414 0.0909  0.0325  -0.0654 393  ARG A C   
3197  O O   . ARG B 396  ? 0.7461 0.7743 0.6589 0.0956  0.0345  -0.0653 393  ARG A O   
3198  C CB  . ARG B 396  ? 0.7069 0.7252 0.6354 0.0870  0.0281  -0.0693 393  ARG A CB  
3199  C CG  . ARG B 396  ? 0.7384 0.7509 0.6686 0.0862  0.0236  -0.0747 393  ARG A CG  
3200  C CD  . ARG B 396  ? 0.7861 0.7933 0.7200 0.0860  0.0224  -0.0734 393  ARG A CD  
3201  N NE  . ARG B 396  ? 0.8423 0.8383 0.7727 0.0854  0.0167  -0.0787 393  ARG A NE  
3202  C CZ  . ARG B 396  ? 0.8570 0.8429 0.7857 0.0872  0.0140  -0.0793 393  ARG A CZ  
3203  N NH1 . ARG B 396  ? 0.8560 0.8465 0.7888 0.0905  0.0172  -0.0749 393  ARG A NH1 
3204  N NH2 . ARG B 396  ? 0.8536 0.8245 0.7747 0.0853  0.0074  -0.0840 393  ARG A NH2 
3205  N N   . ILE B 397  ? 0.7088 0.7260 0.6197 0.0859  0.0326  -0.0604 394  ILE A N   
3206  C CA  . ILE B 397  ? 0.7045 0.7188 0.6050 0.0843  0.0340  -0.0547 394  ILE A CA  
3207  C C   . ILE B 397  ? 0.7054 0.7185 0.5956 0.0906  0.0344  -0.0580 394  ILE A C   
3208  O O   . ILE B 397  ? 0.7018 0.7157 0.5843 0.0909  0.0358  -0.0545 394  ILE A O   
3209  C CB  . ILE B 397  ? 0.7178 0.7206 0.6111 0.0778  0.0323  -0.0494 394  ILE A CB  
3210  C CG1 . ILE B 397  ? 0.7200 0.7255 0.6240 0.0714  0.0321  -0.0457 394  ILE A CG1 
3211  C CG2 . ILE B 397  ? 0.7432 0.7373 0.6208 0.0743  0.0319  -0.0431 394  ILE A CG2 
3212  C CD1 . ILE B 397  ? 0.7340 0.7510 0.6434 0.0686  0.0343  -0.0406 394  ILE A CD1 
3213  N N   . SER B 398  ? 0.7005 0.7137 0.5902 0.0953  0.0329  -0.0642 395  SER A N   
3214  C CA  . SER B 398  ? 0.7001 0.7141 0.5804 0.1023  0.0331  -0.0679 395  SER A CA  
3215  C C   . SER B 398  ? 0.7156 0.7378 0.5989 0.1066  0.0348  -0.0707 395  SER A C   
3216  O O   . SER B 398  ? 0.7410 0.7638 0.6156 0.1121  0.0355  -0.0724 395  SER A O   
3217  C CB  . SER B 398  ? 0.6763 0.6947 0.5574 0.1057  0.0309  -0.0733 395  SER A CB  
3218  O OG  . SER B 398  ? 0.7054 0.7294 0.5810 0.1128  0.0310  -0.0779 395  SER A OG  
3219  N N   . GLU B 399  ? 0.7255 0.7533 0.6191 0.1058  0.0352  -0.0715 396  GLU A N   
3220  C CA  . GLU B 399  ? 0.7504 0.7852 0.6449 0.1123  0.0363  -0.0750 396  GLU A CA  
3221  C C   . GLU B 399  ? 0.7724 0.8150 0.6699 0.1125  0.0390  -0.0697 396  GLU A C   
3222  O O   . GLU B 399  ? 0.7915 0.8404 0.6914 0.1191  0.0394  -0.0728 396  GLU A O   
3223  C CB  . GLU B 399  ? 0.7875 0.8212 0.6869 0.1144  0.0330  -0.0825 396  GLU A CB  
3224  C CG  . GLU B 399  ? 0.8354 0.8643 0.7425 0.1084  0.0305  -0.0819 396  GLU A CG  
3225  C CD  . GLU B 399  ? 0.8717 0.8966 0.7799 0.1064  0.0256  -0.0881 396  GLU A CD  
3226  O OE1 . GLU B 399  ? 0.8542 0.8820 0.7579 0.1084  0.0241  -0.0923 396  GLU A OE1 
3227  O OE2 . GLU B 399  ? 0.8971 0.9160 0.8095 0.1019  0.0227  -0.0883 396  GLU A OE2 
3228  N N   . LEU B 400  ? 0.7847 0.8277 0.6803 0.1056  0.0403  -0.0614 397  LEU A N   
3229  C CA  . LEU B 400  ? 0.7944 0.8509 0.6921 0.1046  0.0430  -0.0545 397  LEU A CA  
3230  C C   . LEU B 400  ? 0.8537 0.9177 0.7426 0.1070  0.0450  -0.0516 397  LEU A C   
3231  O O   . LEU B 400  ? 0.8819 0.9365 0.7613 0.1080  0.0442  -0.0538 397  LEU A O   
3232  C CB  . LEU B 400  ? 0.7543 0.8093 0.6528 0.0936  0.0426  -0.0458 397  LEU A CB  
3233  C CG  . LEU B 400  ? 0.7229 0.7759 0.6316 0.0909  0.0414  -0.0464 397  LEU A CG  
3234  C CD1 . LEU B 400  ? 0.6842 0.7353 0.5915 0.0794  0.0407  -0.0373 397  LEU A CD1 
3235  C CD2 . LEU B 400  ? 0.7258 0.7923 0.6427 0.0989  0.0427  -0.0485 397  LEU A CD2 
3236  N N   . THR B 401  ? 0.8592 0.9421 0.7507 0.1085  0.0477  -0.0462 398  THR A N   
3237  C CA  . THR B 401  ? 0.8714 0.9665 0.7558 0.1111  0.0499  -0.0427 398  THR A CA  
3238  C C   . THR B 401  ? 0.8983 1.0004 0.7769 0.0982  0.0503  -0.0299 398  THR A C   
3239  O O   . THR B 401  ? 0.8871 1.0003 0.7720 0.0915  0.0505  -0.0230 398  THR A O   
3240  C CB  . THR B 401  ? 0.8787 0.9942 0.7682 0.1238  0.0525  -0.0456 398  THR A CB  
3241  O OG1 . THR B 401  ? 0.9019 1.0058 0.7933 0.1340  0.0505  -0.0573 398  THR A OG1 
3242  C CG2 . THR B 401  ? 0.8705 1.0000 0.7527 0.1274  0.0550  -0.0424 398  THR A CG2 
3243  N N   . GLY B 402  ? 0.9371 1.0319 0.8023 0.0939  0.0496  -0.0263 399  GLY A N   
3244  C CA  . GLY B 402  ? 0.9442 1.0441 0.7998 0.0800  0.0487  -0.0133 399  GLY A CA  
3245  C C   . GLY B 402  ? 0.9301 1.0097 0.7785 0.0660  0.0445  -0.0077 399  GLY A C   
3246  O O   . GLY B 402  ? 0.8954 0.9525 0.7421 0.0680  0.0422  -0.0142 399  GLY A O   
3247  N N   . LYS B 403  ? 0.9596 1.0488 0.8026 0.0512  0.0431  0.0053  400  LYS A N   
3248  C CA  . LYS B 403  ? 0.9875 1.0568 0.8205 0.0359  0.0381  0.0121  400  LYS A CA  
3249  C C   . LYS B 403  ? 0.9948 1.0655 0.8433 0.0380  0.0386  0.0080  400  LYS A C   
3250  O O   . LYS B 403  ? 1.0049 1.1020 0.8676 0.0363  0.0409  0.0124  400  LYS A O   
3251  C CB  . LYS B 403  ? 0.9830 1.0671 0.8079 0.0175  0.0359  0.0280  400  LYS A CB  
3252  N N   . ILE B 404  ? 1.0162 1.0604 0.8613 0.0426  0.0364  -0.0003 401  ILE A N   
3253  C CA  . ILE B 404  ? 1.0408 1.0842 0.8996 0.0446  0.0365  -0.0046 401  ILE A CA  
3254  C C   . ILE B 404  ? 1.0493 1.0888 0.9036 0.0288  0.0331  0.0055  401  ILE A C   
3255  O O   . ILE B 404  ? 1.0785 1.0902 0.9166 0.0218  0.0282  0.0071  401  ILE A O   
3256  C CB  . ILE B 404  ? 1.0765 1.0972 0.9326 0.0536  0.0351  -0.0153 401  ILE A CB  
3257  C CG1 . ILE B 404  ? 1.1318 1.1245 0.9636 0.0511  0.0309  -0.0143 401  ILE A CG1 
3258  C CG2 . ILE B 404  ? 1.0697 1.1006 0.9364 0.0680  0.0384  -0.0254 401  ILE A CG2 
3259  C CD1 . ILE B 404  ? 1.1517 1.1271 0.9798 0.0609  0.0295  -0.0237 401  ILE A CD1 
3260  N N   . THR B 405  ? 1.0728 1.1405 0.9399 0.0239  0.0352  0.0125  402  THR A N   
3261  C CA  . THR B 405  ? 1.0780 1.1466 0.9427 0.0080  0.0319  0.0226  402  THR A CA  
3262  C C   . THR B 405  ? 1.0492 1.1044 0.9217 0.0107  0.0308  0.0168  402  THR A C   
3263  O O   . THR B 405  ? 1.0501 1.1000 0.9318 0.0240  0.0330  0.0059  402  THR A O   
3264  C CB  . THR B 405  ? 1.0353 1.1444 0.9124 0.0034  0.0348  0.0321  402  THR A CB  
3265  O OG1 . THR B 405  ? 1.0078 1.1357 0.9052 0.0173  0.0392  0.0254  402  THR A OG1 
3266  C CG2 . THR B 405  ? 1.0098 1.1389 0.8830 0.0049  0.0372  0.0363  402  THR A CG2 
3267  N N   . LYS B 406  ? 1.0277 1.0777 0.8955 -0.0035 0.0270  0.0248  403  LYS A N   
3268  C CA  . LYS B 406  ? 1.0148 1.0567 0.8915 -0.0016 0.0264  0.0207  403  LYS A CA  
3269  C C   . LYS B 406  ? 1.0028 1.0750 0.9029 0.0064  0.0312  0.0190  403  LYS A C   
3270  O O   . LYS B 406  ? 0.9998 1.0662 0.9095 0.0119  0.0316  0.0131  403  LYS A O   
3271  C CB  . LYS B 406  ? 1.0435 1.0697 0.9068 -0.0188 0.0203  0.0296  403  LYS A CB  
3272  C CG  . LYS B 406  ? 1.0845 1.1396 0.9593 -0.0297 0.0207  0.0398  403  LYS A CG  
3273  C CD  . LYS B 406  ? 1.1127 1.1535 0.9869 -0.0366 0.0170  0.0409  403  LYS A CD  
3274  C CE  . LYS B 406  ? 1.1120 1.1853 1.0000 -0.0454 0.0180  0.0502  403  LYS A CE  
3275  N NZ  . LYS B 406  ? 1.1073 1.1678 0.9969 -0.0503 0.0150  0.0502  403  LYS A NZ  
3276  N N   . SER B 407  ? 0.9423 1.0464 0.8498 0.0079  0.0346  0.0242  404  SER A N   
3277  C CA  . SER B 407  ? 0.8883 1.0191 0.8139 0.0200  0.0389  0.0213  404  SER A CA  
3278  C C   . SER B 407  ? 0.8113 0.9330 0.7421 0.0381  0.0414  0.0080  404  SER A C   
3279  O O   . SER B 407  ? 0.7466 0.8691 0.6875 0.0474  0.0424  0.0020  404  SER A O   
3280  C CB  . SER B 407  ? 0.9088 1.0790 0.8386 0.0189  0.0418  0.0309  404  SER A CB  
3281  O OG  . SER B 407  ? 0.9096 1.1039 0.8530 0.0352  0.0458  0.0268  404  SER A OG  
3282  N N   . ALA B 408  ? 0.7893 0.9012 0.7119 0.0424  0.0417  0.0036  405  ALA A N   
3283  C CA  . ALA B 408  ? 0.7693 0.8717 0.6950 0.0573  0.0430  -0.0086 405  ALA A CA  
3284  C C   . ALA B 408  ? 0.7403 0.8171 0.6666 0.0574  0.0404  -0.0159 405  ALA A C   
3285  O O   . ALA B 408  ? 0.7414 0.8139 0.6739 0.0672  0.0406  -0.0245 405  ALA A O   
3286  C CB  . ALA B 408  ? 0.7863 0.8850 0.7024 0.0608  0.0437  -0.0109 405  ALA A CB  
3287  N N   . LYS B 409  ? 0.7293 0.7889 0.6474 0.0466  0.0374  -0.0122 406  LYS A N   
3288  C CA  . LYS B 409  ? 0.7276 0.7675 0.6462 0.0474  0.0351  -0.0181 406  LYS A CA  
3289  C C   . LYS B 409  ? 0.7024 0.7485 0.6338 0.0471  0.0352  -0.0180 406  LYS A C   
3290  O O   . LYS B 409  ? 0.6891 0.7277 0.6263 0.0524  0.0346  -0.0249 406  LYS A O   
3291  C CB  . LYS B 409  ? 0.7987 0.8176 0.7017 0.0384  0.0314  -0.0144 406  LYS A CB  
3292  C CG  . LYS B 409  ? 0.8630 0.8706 0.7498 0.0401  0.0304  -0.0152 406  LYS A CG  
3293  C CD  . LYS B 409  ? 0.9104 0.8910 0.7777 0.0356  0.0258  -0.0140 406  LYS A CD  
3294  C CE  . LYS B 409  ? 0.9694 0.9363 0.8184 0.0400  0.0245  -0.0158 406  LYS A CE  
3295  N NZ  . LYS B 409  ? 1.0137 0.9516 0.8402 0.0403  0.0196  -0.0162 406  LYS A NZ  
3296  N N   . GLU B 410  ? 0.7098 0.7706 0.6450 0.0404  0.0357  -0.0096 407  GLU A N   
3297  C CA  . GLU B 410  ? 0.7260 0.7939 0.6726 0.0413  0.0359  -0.0091 407  GLU A CA  
3298  C C   . GLU B 410  ? 0.6897 0.7675 0.6447 0.0552  0.0380  -0.0156 407  GLU A C   
3299  O O   . GLU B 410  ? 0.6574 0.7302 0.6187 0.0588  0.0370  -0.0192 407  GLU A O   
3300  C CB  . GLU B 410  ? 0.7937 0.8790 0.7418 0.0311  0.0358  0.0020  407  GLU A CB  
3301  C CG  . GLU B 410  ? 0.8912 0.9607 0.8273 0.0159  0.0318  0.0086  407  GLU A CG  
3302  C CD  . GLU B 410  ? 0.9772 1.0652 0.9137 0.0031  0.0307  0.0206  407  GLU A CD  
3303  O OE1 . GLU B 410  ? 0.9933 1.1115 0.9406 0.0074  0.0339  0.0243  407  GLU A OE1 
3304  O OE2 . GLU B 410  ? 1.0214 1.0942 0.9460 -0.0107 0.0262  0.0266  407  GLU A OE2 
3305  N N   . LYS B 411  ? 0.6749 0.7647 0.6279 0.0633  0.0402  -0.0171 408  LYS A N   
3306  C CA  . LYS B 411  ? 0.6139 0.7073 0.5698 0.0781  0.0410  -0.0243 408  LYS A CA  
3307  C C   . LYS B 411  ? 0.6024 0.6722 0.5562 0.0815  0.0383  -0.0343 408  LYS A C   
3308  O O   . LYS B 411  ? 0.6269 0.6894 0.5822 0.0886  0.0365  -0.0398 408  LYS A O   
3309  C CB  . LYS B 411  ? 0.5959 0.7077 0.5483 0.0866  0.0438  -0.0236 408  LYS A CB  
3310  C CG  . LYS B 411  ? 0.5721 0.7151 0.5275 0.0846  0.0465  -0.0130 408  LYS A CG  
3311  C CD  . LYS B 411  ? 0.5406 0.7048 0.4926 0.0949  0.0495  -0.0126 408  LYS A CD  
3312  C CE  . LYS B 411  ? 0.5128 0.7151 0.4685 0.0930  0.0522  -0.0009 408  LYS A CE  
3313  N NZ  . LYS B 411  ? 0.4997 0.7267 0.4521 0.1047  0.0554  -0.0001 408  LYS A NZ  
3314  N N   . VAL B 412  ? 0.5907 0.6485 0.5394 0.0763  0.0375  -0.0362 409  VAL A N   
3315  C CA  . VAL B 412  ? 0.5728 0.6137 0.5201 0.0778  0.0347  -0.0442 409  VAL A CA  
3316  C C   . VAL B 412  ? 0.6002 0.6316 0.5525 0.0717  0.0323  -0.0439 409  VAL A C   
3317  O O   . VAL B 412  ? 0.6230 0.6452 0.5766 0.0735  0.0296  -0.0494 409  VAL A O   
3318  C CB  . VAL B 412  ? 0.5369 0.5715 0.4766 0.0755  0.0347  -0.0457 409  VAL A CB  
3319  C CG1 . VAL B 412  ? 0.5156 0.5387 0.4547 0.0760  0.0318  -0.0525 409  VAL A CG1 
3320  C CG2 . VAL B 412  ? 0.5184 0.5618 0.4531 0.0821  0.0369  -0.0465 409  VAL A CG2 
3321  N N   . GLN B 413  ? 0.6410 0.6742 0.5948 0.0636  0.0328  -0.0371 410  GLN A N   
3322  C CA  . GLN B 413  ? 0.6967 0.7224 0.6552 0.0582  0.0307  -0.0363 410  GLN A CA  
3323  C C   . GLN B 413  ? 0.7231 0.7513 0.6880 0.0628  0.0300  -0.0375 410  GLN A C   
3324  O O   . GLN B 413  ? 0.7437 0.7616 0.7103 0.0624  0.0272  -0.0414 410  GLN A O   
3325  C CB  . GLN B 413  ? 0.7763 0.8025 0.7329 0.0490  0.0308  -0.0286 410  GLN A CB  
3326  C CG  . GLN B 413  ? 0.8592 0.8752 0.8044 0.0450  0.0298  -0.0276 410  GLN A CG  
3327  C CD  . GLN B 413  ? 0.9096 0.9194 0.8488 0.0354  0.0280  -0.0205 410  GLN A CD  
3328  O OE1 . GLN B 413  ? 0.9540 0.9537 0.8794 0.0316  0.0264  -0.0177 410  GLN A OE1 
3329  N NE2 . GLN B 413  ? 0.8930 0.9062 0.8402 0.0316  0.0275  -0.0176 410  GLN A NE2 
3330  N N   . ARG B 414  ? 0.7372 0.7798 0.7040 0.0673  0.0322  -0.0337 411  ARG A N   
3331  C CA  . ARG B 414  ? 0.7815 0.8260 0.7511 0.0745  0.0314  -0.0348 411  ARG A CA  
3332  C C   . ARG B 414  ? 0.7737 0.8052 0.7374 0.0841  0.0286  -0.0433 411  ARG A C   
3333  O O   . ARG B 414  ? 0.7952 0.8157 0.7574 0.0875  0.0255  -0.0460 411  ARG A O   
3334  C CB  . ARG B 414  ? 0.8604 0.9285 0.8321 0.0796  0.0346  -0.0285 411  ARG A CB  
3335  C CG  . ARG B 414  ? 0.9191 0.9986 0.8967 0.0694  0.0354  -0.0195 411  ARG A CG  
3336  C CD  . ARG B 414  ? 0.9511 1.0535 0.9282 0.0646  0.0381  -0.0111 411  ARG A CD  
3337  N NE  . ARG B 414  ? 0.9797 1.1041 0.9562 0.0774  0.0408  -0.0107 411  ARG A NE  
3338  C CZ  . ARG B 414  ? 0.9983 1.1480 0.9743 0.0750  0.0433  -0.0032 411  ARG A CZ  
3339  N NH1 . ARG B 414  ? 1.0042 1.1560 0.9784 0.0587  0.0427  0.0045  411  ARG A NH1 
3340  N NH2 . ARG B 414  ? 0.9990 1.1713 0.9743 0.0890  0.0459  -0.0032 411  ARG A NH2 
3341  N N   . SER B 415  ? 0.7598 0.7902 0.7182 0.0880  0.0290  -0.0476 412  SER A N   
3342  C CA  . SER B 415  ? 0.7744 0.7902 0.7247 0.0959  0.0253  -0.0557 412  SER A CA  
3343  C C   . SER B 415  ? 0.7700 0.7672 0.7196 0.0873  0.0204  -0.0593 412  SER A C   
3344  O O   . SER B 415  ? 0.7756 0.7566 0.7180 0.0902  0.0154  -0.0639 412  SER A O   
3345  C CB  . SER B 415  ? 0.7668 0.7873 0.7118 0.1011  0.0268  -0.0591 412  SER A CB  
3346  O OG  . SER B 415  ? 0.7447 0.7653 0.6919 0.0919  0.0278  -0.0582 412  SER A OG  
3347  N N   . LEU B 416  ? 0.7453 0.7447 0.7004 0.0767  0.0213  -0.0567 413  LEU A N   
3348  C CA  . LEU B 416  ? 0.7352 0.7241 0.6907 0.0684  0.0171  -0.0589 413  LEU A CA  
3349  C C   . LEU B 416  ? 0.7399 0.7215 0.6986 0.0638  0.0145  -0.0564 413  LEU A C   
3350  O O   . LEU B 416  ? 0.7531 0.7261 0.7109 0.0566  0.0102  -0.0578 413  LEU A O   
3351  C CB  . LEU B 416  ? 0.7185 0.7144 0.6768 0.0618  0.0190  -0.0568 413  LEU A CB  
3352  C CG  . LEU B 416  ? 0.7287 0.7292 0.6821 0.0656  0.0207  -0.0596 413  LEU A CG  
3353  C CD1 . LEU B 416  ? 0.7281 0.7330 0.6808 0.0615  0.0221  -0.0573 413  LEU A CD1 
3354  C CD2 . LEU B 416  ? 0.7463 0.7403 0.6945 0.0671  0.0166  -0.0661 413  LEU A CD2 
3355  N N   . LYS B 417  ? 0.7618 0.7487 0.7240 0.0671  0.0169  -0.0523 414  LYS A N   
3356  C CA  . LYS B 417  ? 0.8157 0.7958 0.7806 0.0633  0.0145  -0.0498 414  LYS A CA  
3357  C C   . LYS B 417  ? 0.9180 0.8808 0.8732 0.0695  0.0093  -0.0540 414  LYS A C   
3358  O O   . LYS B 417  ? 0.9752 0.9249 0.9286 0.0634  0.0048  -0.0537 414  LYS A O   
3359  C CB  . LYS B 417  ? 0.8243 0.8179 0.7961 0.0640  0.0185  -0.0433 414  LYS A CB  
3360  C CG  . LYS B 417  ? 0.8344 0.8369 0.8120 0.0551  0.0213  -0.0384 414  LYS A CG  
3361  C CD  . LYS B 417  ? 0.8708 0.8840 0.8536 0.0532  0.0236  -0.0315 414  LYS A CD  
3362  C CE  . LYS B 417  ? 0.9067 0.9237 0.8904 0.0442  0.0250  -0.0266 414  LYS A CE  
3363  N NZ  . LYS B 417  ? 0.9233 0.9497 0.9111 0.0399  0.0260  -0.0195 414  LYS A NZ  
3364  N N   . HIS B 418  ? 0.9582 0.9192 0.9047 0.0820  0.0093  -0.0577 415  HIS A N   
3365  C CA  . HIS B 418  ? 1.0316 0.9724 0.9638 0.0913  0.0037  -0.0619 415  HIS A CA  
3366  C C   . HIS B 418  ? 1.0748 1.0044 0.9933 0.0994  0.0006  -0.0689 415  HIS A C   
3367  O O   . HIS B 418  ? 1.0947 1.0230 1.0030 0.1151  0.0007  -0.0716 415  HIS A O   
3368  C CB  . HIS B 418  ? 1.0827 1.0331 1.0149 0.1037  0.0065  -0.0588 415  HIS A CB  
3369  C CG  . HIS B 418  ? 1.1127 1.0899 1.0503 0.1125  0.0132  -0.0562 415  HIS A CG  
3370  N ND1 . HIS B 418  ? 1.1260 1.1054 1.0551 0.1233  0.0137  -0.0606 415  HIS A ND1 
3371  C CD2 . HIS B 418  ? 1.1178 1.1215 1.0673 0.1109  0.0191  -0.0489 415  HIS A CD2 
3372  C CE1 . HIS B 418  ? 1.1295 1.1373 1.0660 0.1280  0.0201  -0.0557 415  HIS A CE1 
3373  N NE2 . HIS B 418  ? 1.1242 1.1468 1.0727 0.1197  0.0231  -0.0483 415  HIS A NE2 
3374  N N   . GLU B 419  ? 1.1167 1.0393 1.0339 0.0893  -0.0025 -0.0716 416  GLU A N   
3375  C CA  . GLU B 419  ? 1.1248 1.0320 1.0268 0.0944  -0.0074 -0.0785 416  GLU A CA  
3376  C C   . GLU B 419  ? 1.0624 0.9589 0.9623 0.0784  -0.0135 -0.0798 416  GLU A C   
3377  O O   . GLU B 419  ? 1.0459 0.9565 0.9592 0.0662  -0.0111 -0.0757 416  GLU A O   
3378  C CB  . GLU B 419  ? 1.1670 1.0924 1.0718 0.1035  -0.0016 -0.0800 416  GLU A CB  
3379  C CG  . GLU B 419  ? 1.1903 1.1303 1.1056 0.0930  0.0016  -0.0789 416  GLU A CG  
3380  C CD  . GLU B 419  ? 1.2305 1.1766 1.1408 0.1012  0.0035  -0.0830 416  GLU A CD  
3381  O OE1 . GLU B 419  ? 1.2523 1.1835 1.1512 0.1005  -0.0023 -0.0887 416  GLU A OE1 
3382  O OE2 . GLU B 419  ? 1.2357 1.2012 1.1524 0.1074  0.0102  -0.0801 416  GLU A OE2 
3383  N N   . ASP B 420  ? 0.9844 0.8563 0.8656 0.0789  -0.0219 -0.0854 417  ASP A N   
3384  C CA  . ASP B 420  ? 0.9165 0.7799 0.7938 0.0621  -0.0290 -0.0859 417  ASP A CA  
3385  C C   . ASP B 420  ? 0.8789 0.7595 0.7615 0.0606  -0.0260 -0.0881 417  ASP A C   
3386  O O   . ASP B 420  ? 0.9096 0.7888 0.7850 0.0729  -0.0246 -0.0928 417  ASP A O   
3387  C CB  . ASP B 420  ? 0.9377 0.7636 0.7891 0.0605  -0.0411 -0.0902 417  ASP A CB  
3388  C CG  . ASP B 420  ? 0.9547 0.7602 0.7976 0.0626  -0.0450 -0.0881 417  ASP A CG  
3389  O OD1 . ASP B 420  ? 0.9124 0.7318 0.7709 0.0549  -0.0411 -0.0821 417  ASP A OD1 
3390  O OD2 . ASP B 420  ? 1.0178 0.7918 0.8363 0.0732  -0.0522 -0.0927 417  ASP A OD2 
3391  N N   . ILE B 421  ? 0.8359 0.7343 0.7305 0.0469  -0.0249 -0.0846 418  ILE A N   
3392  C CA  . ILE B 421  ? 0.8327 0.7494 0.7323 0.0456  -0.0221 -0.0861 418  ILE A CA  
3393  C C   . ILE B 421  ? 0.8741 0.7796 0.7614 0.0339  -0.0318 -0.0886 418  ILE A C   
3394  O O   . ILE B 421  ? 0.9286 0.8265 0.8124 0.0193  -0.0388 -0.0855 418  ILE A O   
3395  C CB  . ILE B 421  ? 0.8353 0.7794 0.7525 0.0403  -0.0154 -0.0808 418  ILE A CB  
3396  C CG1 . ILE B 421  ? 0.8087 0.7584 0.7356 0.0466  -0.0085 -0.0768 418  ILE A CG1 
3397  C CG2 . ILE B 421  ? 0.8517 0.8136 0.7721 0.0446  -0.0111 -0.0827 418  ILE A CG2 
3398  C CD1 . ILE B 421  ? 0.7989 0.7522 0.7257 0.0609  -0.0025 -0.0783 418  ILE A CD1 
3399  N N   . ASN B 422  ? 0.8695 0.7747 0.7494 0.0390  -0.0328 -0.0937 419  ASN A N   
3400  C CA  . ASN B 422  ? 0.8666 0.7645 0.7350 0.0264  -0.0422 -0.0956 419  ASN A CA  
3401  C C   . ASN B 422  ? 0.8145 0.7438 0.6971 0.0137  -0.0403 -0.0908 419  ASN A C   
3402  O O   . ASN B 422  ? 0.7726 0.7269 0.6705 0.0197  -0.0311 -0.0885 419  ASN A O   
3403  C CB  . ASN B 422  ? 0.9103 0.7988 0.7659 0.0365  -0.0440 -0.1027 419  ASN A CB  
3404  C CG  . ASN B 422  ? 0.9324 0.8485 0.8013 0.0467  -0.0338 -0.1034 419  ASN A CG  
3405  O OD1 . ASN B 422  ? 0.9222 0.8605 0.7990 0.0396  -0.0325 -0.1018 419  ASN A OD1 
3406  N ND2 . ASN B 422  ? 0.9646 0.8801 0.8345 0.0636  -0.0270 -0.1054 419  ASN A ND2 
3407  N N   . LEU B 423  ? 0.8213 0.7488 0.6964 -0.0038 -0.0499 -0.0890 420  LEU A N   
3408  C CA  . LEU B 423  ? 0.7780 0.7394 0.6657 -0.0161 -0.0489 -0.0833 420  LEU A CA  
3409  C C   . LEU B 423  ? 0.7380 0.7262 0.6330 -0.0077 -0.0426 -0.0856 420  LEU A C   
3410  O O   . LEU B 423  ? 0.7313 0.7510 0.6391 -0.0084 -0.0374 -0.0815 420  LEU A O   
3411  C CB  . LEU B 423  ? 0.7642 0.7204 0.6408 -0.0385 -0.0615 -0.0799 420  LEU A CB  
3412  C CG  . LEU B 423  ? 0.7076 0.7030 0.5967 -0.0533 -0.0617 -0.0722 420  LEU A CG  
3413  C CD1 . LEU B 423  ? 0.6673 0.6786 0.5721 -0.0501 -0.0542 -0.0669 420  LEU A CD1 
3414  C CD2 . LEU B 423  ? 0.7210 0.7096 0.5969 -0.0781 -0.0755 -0.0677 420  LEU A CD2 
3415  N N   . GLN B 424  ? 0.7324 0.7081 0.6179 0.0018  -0.0430 -0.0921 421  GLN A N   
3416  C CA  . GLN B 424  ? 0.7696 0.7690 0.6604 0.0099  -0.0375 -0.0942 421  GLN A CA  
3417  C C   . GLN B 424  ? 0.7528 0.7661 0.6560 0.0250  -0.0257 -0.0932 421  GLN A C   
3418  O O   . GLN B 424  ? 0.7513 0.7909 0.6621 0.0281  -0.0208 -0.0914 421  GLN A O   
3419  C CB  . GLN B 424  ? 0.8353 0.8167 0.7117 0.0163  -0.0412 -0.1014 421  GLN A CB  
3420  C CG  . GLN B 424  ? 0.8746 0.8796 0.7548 0.0233  -0.0367 -0.1037 421  GLN A CG  
3421  C CD  . GLN B 424  ? 0.9162 0.9521 0.8017 0.0101  -0.0399 -0.0994 421  GLN A CD  
3422  O OE1 . GLN B 424  ? 0.9687 1.0021 0.8473 -0.0075 -0.0498 -0.0971 421  GLN A OE1 
3423  N NE2 . GLN B 424  ? 0.8735 0.9388 0.7695 0.0185  -0.0319 -0.0976 421  GLN A NE2 
3424  N N   . GLU B 425  ? 0.7296 0.7255 0.6332 0.0346  -0.0216 -0.0941 422  GLU A N   
3425  C CA  . GLU B 425  ? 0.7099 0.7167 0.6231 0.0460  -0.0117 -0.0920 422  GLU A CA  
3426  C C   . GLU B 425  ? 0.6823 0.7064 0.6059 0.0404  -0.0091 -0.0860 422  GLU A C   
3427  O O   . GLU B 425  ? 0.6543 0.6914 0.5826 0.0479  -0.0026 -0.0842 422  GLU A O   
3428  C CB  . GLU B 425  ? 0.7513 0.7398 0.6627 0.0553  -0.0088 -0.0929 422  GLU A CB  
3429  C CG  . GLU B 425  ? 0.7908 0.7892 0.7092 0.0656  0.0003  -0.0906 422  GLU A CG  
3430  C CD  . GLU B 425  ? 0.8669 0.8538 0.7845 0.0735  0.0030  -0.0901 422  GLU A CD  
3431  O OE1 . GLU B 425  ? 0.9351 0.9060 0.8479 0.0719  -0.0016 -0.0912 422  GLU A OE1 
3432  O OE2 . GLU B 425  ? 0.8546 0.8489 0.7750 0.0812  0.0094  -0.0882 422  GLU A OE2 
3433  N N   . ILE B 426  ? 0.6874 0.7102 0.6122 0.0275  -0.0147 -0.0827 423  ILE A N   
3434  C CA  . ILE B 426  ? 0.7035 0.7454 0.6375 0.0226  -0.0125 -0.0769 423  ILE A CA  
3435  C C   . ILE B 426  ? 0.7322 0.8036 0.6681 0.0218  -0.0121 -0.0757 423  ILE A C   
3436  O O   . ILE B 426  ? 0.7409 0.8292 0.6811 0.0289  -0.0067 -0.0733 423  ILE A O   
3437  C CB  . ILE B 426  ? 0.6643 0.6981 0.5986 0.0084  -0.0189 -0.0730 423  ILE A CB  
3438  C CG1 . ILE B 426  ? 0.6735 0.6783 0.6042 0.0121  -0.0192 -0.0744 423  ILE A CG1 
3439  C CG2 . ILE B 426  ? 0.5970 0.6529 0.5408 0.0043  -0.0164 -0.0668 423  ILE A CG2 
3440  C CD1 . ILE B 426  ? 0.6793 0.6719 0.6079 -0.0007 -0.0257 -0.0707 423  ILE A CD1 
3441  N N   . ILE B 427  ? 0.7446 0.8221 0.6752 0.0138  -0.0183 -0.0774 424  ILE A N   
3442  C CA  . ILE B 427  ? 0.7483 0.8583 0.6806 0.0131  -0.0183 -0.0759 424  ILE A CA  
3443  C C   . ILE B 427  ? 0.7518 0.8679 0.6824 0.0305  -0.0112 -0.0795 424  ILE A C   
3444  O O   . ILE B 427  ? 0.7500 0.8902 0.6823 0.0378  -0.0074 -0.0775 424  ILE A O   
3445  C CB  . ILE B 427  ? 0.7651 0.8796 0.6911 -0.0017 -0.0276 -0.0763 424  ILE A CB  
3446  C CG1 . ILE B 427  ? 0.7565 0.8647 0.6816 -0.0211 -0.0357 -0.0712 424  ILE A CG1 
3447  C CG2 . ILE B 427  ? 0.7789 0.9316 0.7069 -0.0012 -0.0273 -0.0746 424  ILE A CG2 
3448  C CD1 . ILE B 427  ? 0.7615 0.8699 0.6770 -0.0393 -0.0469 -0.0705 424  ILE A CD1 
3449  N N   . SER B 428  ? 0.7518 0.8459 0.6771 0.0382  -0.0095 -0.0847 425  SER A N   
3450  C CA  . SER B 428  ? 0.7565 0.8539 0.6786 0.0532  -0.0034 -0.0877 425  SER A CA  
3451  C C   . SER B 428  ? 0.7583 0.8541 0.6822 0.0632  0.0035  -0.0850 425  SER A C   
3452  O O   . SER B 428  ? 0.7702 0.8713 0.6891 0.0746  0.0077  -0.0859 425  SER A O   
3453  C CB  . SER B 428  ? 0.7796 0.8553 0.6955 0.0584  -0.0034 -0.0930 425  SER A CB  
3454  O OG  . SER B 428  ? 0.8173 0.8907 0.7276 0.0502  -0.0107 -0.0962 425  SER A OG  
3455  N N   . ALA B 429  ? 0.7352 0.8218 0.6641 0.0587  0.0039  -0.0815 426  ALA A N   
3456  C CA  . ALA B 429  ? 0.7150 0.7967 0.6438 0.0663  0.0092  -0.0786 426  ALA A CA  
3457  C C   . ALA B 429  ? 0.7095 0.8086 0.6403 0.0655  0.0093  -0.0744 426  ALA A C   
3458  O O   . ALA B 429  ? 0.6873 0.7849 0.6127 0.0747  0.0130  -0.0729 426  ALA A O   
3459  C CB  . ALA B 429  ? 0.6991 0.7596 0.6313 0.0636  0.0102  -0.0775 426  ALA A CB  
3460  N N   . ALA B 430  ? 0.7199 0.8349 0.6563 0.0548  0.0049  -0.0721 427  ALA A N   
3461  C CA  . ALA B 430  ? 0.7352 0.8704 0.6743 0.0541  0.0050  -0.0674 427  ALA A CA  
3462  C C   . ALA B 430  ? 0.7665 0.9343 0.7025 0.0590  0.0044  -0.0668 427  ALA A C   
3463  O O   . ALA B 430  ? 0.7823 0.9674 0.7159 0.0665  0.0062  -0.0638 427  ALA A O   
3464  C CB  . ALA B 430  ? 0.7341 0.8702 0.6812 0.0383  0.0004  -0.0636 427  ALA A CB  
3465  N N   . GLY B 431  ? 0.7823 0.9600 0.7171 0.0559  0.0016  -0.0694 428  GLY A N   
3466  C CA  . GLY B 431  ? 0.7982 1.0108 0.7305 0.0603  0.0008  -0.0685 428  GLY A CA  
3467  C C   . GLY B 431  ? 0.8352 1.0738 0.7743 0.0423  -0.0058 -0.0644 428  GLY A C   
3468  O O   . GLY B 431  ? 0.8477 1.0747 0.7920 0.0263  -0.0102 -0.0620 428  GLY A O   
3469  N N   . LYS B 432  ? 0.8794 1.1544 0.8170 0.0448  -0.0070 -0.0631 429  LYS A N   
3470  C CA  . LYS B 432  ? 0.9060 1.2111 0.8489 0.0259  -0.0141 -0.0580 429  LYS A CA  
3471  C C   . LYS B 432  ? 0.9439 1.2716 0.8936 0.0170  -0.0156 -0.0502 429  LYS A C   
3472  O O   . LYS B 432  ? 0.9718 1.3165 0.9259 -0.0039 -0.0227 -0.0446 429  LYS A O   
3473  C CB  . LYS B 432  ? 0.8824 1.2262 0.8222 0.0317  -0.0147 -0.0579 429  LYS A CB  
3474  C CG  . LYS B 432  ? 0.8564 1.2352 0.7933 0.0512  -0.0094 -0.0554 429  LYS A CG  
3475  C CD  . LYS B 432  ? 0.8459 1.2659 0.7795 0.0574  -0.0103 -0.0550 429  LYS A CD  
3476  C CE  . LYS B 432  ? 0.8306 1.2880 0.7586 0.0791  -0.0057 -0.0523 429  LYS A CE  
3477  N NZ  . LYS B 432  ? 0.8165 1.3168 0.7405 0.0875  -0.0063 -0.0519 429  LYS A NZ  
3478  N N   . GLU B 433  ? 0.9675 1.2948 0.9166 0.0317  -0.0098 -0.0492 430  GLU A N   
3479  C CA  . GLU B 433  ? 0.9643 1.3143 0.9196 0.0251  -0.0107 -0.0418 430  GLU A CA  
3480  C C   . GLU B 433  ? 0.9274 1.2481 0.8883 0.0069  -0.0144 -0.0397 430  GLU A C   
3481  O O   . GLU B 433  ? 0.9200 1.2602 0.8868 -0.0040 -0.0169 -0.0327 430  GLU A O   
3482  C CB  . GLU B 433  ? 1.0137 1.3687 0.9633 0.0479  -0.0040 -0.0421 430  GLU A CB  
3483  C CG  . GLU B 433  ? 1.0680 1.4627 1.0100 0.0664  -0.0015 -0.0419 430  GLU A CG  
3484  C CD  . GLU B 433  ? 1.1039 1.5548 1.0531 0.0543  -0.0059 -0.0343 430  GLU A CD  
3485  O OE1 . GLU B 433  ? 1.1100 1.5777 1.0601 0.0469  -0.0093 -0.0347 430  GLU A OE1 
3486  O OE2 . GLU B 433  ? 1.1154 1.5950 1.0691 0.0515  -0.0064 -0.0274 430  GLU A OE2 
3487  N N   . LEU B 434  ? 0.8873 1.1637 0.8460 0.0045  -0.0148 -0.0453 431  LEU A N   
3488  C CA  . LEU B 434  ? 0.8601 1.1089 0.8216 -0.0122 -0.0195 -0.0435 431  LEU A CA  
3489  C C   . LEU B 434  ? 0.8779 1.1336 0.8382 -0.0353 -0.0292 -0.0402 431  LEU A C   
3490  O O   . LEU B 434  ? 0.8571 1.1105 0.8192 -0.0527 -0.0348 -0.0345 431  LEU A O   
3491  C CB  . LEU B 434  ? 0.8244 1.0267 0.7822 -0.0050 -0.0168 -0.0503 431  LEU A CB  
3492  C CG  . LEU B 434  ? 0.7938 0.9640 0.7519 -0.0180 -0.0213 -0.0495 431  LEU A CG  
3493  C CD1 . LEU B 434  ? 0.7686 0.9094 0.7270 -0.0054 -0.0152 -0.0529 431  LEU A CD1 
3494  C CD2 . LEU B 434  ? 0.8141 0.9637 0.7645 -0.0299 -0.0290 -0.0526 431  LEU A CD2 
3495  N N   . SER B 435  ? 0.9037 1.1658 0.8591 -0.0365 -0.0320 -0.0435 432  SER A N   
3496  C CA  . SER B 435  ? 0.9241 1.1921 0.8752 -0.0599 -0.0426 -0.0400 432  SER A CA  
3497  C C   . SER B 435  ? 0.9326 1.2474 0.8897 -0.0750 -0.0466 -0.0294 432  SER A C   
3498  O O   . SER B 435  ? 0.9671 1.2783 0.9216 -0.0990 -0.0559 -0.0234 432  SER A O   
3499  C CB  . SER B 435  ? 0.9081 1.1808 0.8532 -0.0565 -0.0442 -0.0451 432  SER A CB  
3500  O OG  . SER B 435  ? 0.8806 1.1145 0.8206 -0.0414 -0.0398 -0.0542 432  SER A OG  
3501  N N   . GLU B 436  ? 0.9214 1.2804 0.8847 -0.0608 -0.0401 -0.0266 433  GLU A N   
3502  C CA  . GLU B 436  ? 0.9357 1.3457 0.9054 -0.0723 -0.0429 -0.0159 433  GLU A CA  
3503  C C   . GLU B 436  ? 0.9110 1.3099 0.8851 -0.0804 -0.0433 -0.0107 433  GLU A C   
3504  O O   . GLU B 436  ? 0.9339 1.3566 0.9105 -0.1022 -0.0502 -0.0011 433  GLU A O   
3505  C CB  . GLU B 436  ? 0.9603 1.4179 0.9328 -0.0498 -0.0352 -0.0151 433  GLU A CB  
3506  C CG  . GLU B 436  ? 1.0180 1.4966 0.9863 -0.0430 -0.0354 -0.0185 433  GLU A CG  
3507  C CD  . GLU B 436  ? 1.0913 1.5921 1.0592 -0.0710 -0.0461 -0.0125 433  GLU A CD  
3508  O OE1 . GLU B 436  ? 1.1170 1.5824 1.0782 -0.0811 -0.0515 -0.0177 433  GLU A OE1 
3509  O OE2 . GLU B 436  ? 1.1049 1.6587 1.0779 -0.0831 -0.0497 -0.0022 433  GLU A OE2 
3510  N N   . ALA B 437  ? 0.8766 1.2404 0.8510 -0.0643 -0.0366 -0.0162 434  ALA A N   
3511  C CA  . ALA B 437  ? 0.8210 1.1697 0.7991 -0.0717 -0.0371 -0.0120 434  ALA A CA  
3512  C C   . ALA B 437  ? 0.7931 1.1039 0.7658 -0.0949 -0.0465 -0.0111 434  ALA A C   
3513  O O   . ALA B 437  ? 0.8216 1.1352 0.7956 -0.1124 -0.0517 -0.0035 434  ALA A O   
3514  C CB  . ALA B 437  ? 0.7691 1.0897 0.7478 -0.0492 -0.0281 -0.0181 434  ALA A CB  
3515  N N   . PHE B 438  ? 0.7489 1.0228 0.7132 -0.0946 -0.0491 -0.0187 435  PHE A N   
3516  C CA  . PHE B 438  ? 0.7538 0.9872 0.7076 -0.1139 -0.0591 -0.0188 435  PHE A CA  
3517  C C   . PHE B 438  ? 0.7907 1.0466 0.7392 -0.1420 -0.0708 -0.0103 435  PHE A C   
3518  O O   . PHE B 438  ? 0.8539 1.0909 0.7953 -0.1628 -0.0798 -0.0048 435  PHE A O   
3519  C CB  . PHE B 438  ? 0.8017 0.9937 0.7459 -0.1039 -0.0590 -0.0293 435  PHE A CB  
3520  C CG  . PHE B 438  ? 0.8725 1.0126 0.8036 -0.1138 -0.0667 -0.0318 435  PHE A CG  
3521  C CD1 . PHE B 438  ? 0.9224 1.0469 0.8385 -0.1363 -0.0799 -0.0294 435  PHE A CD1 
3522  C CD2 . PHE B 438  ? 0.8844 0.9906 0.8159 -0.1001 -0.0614 -0.0364 435  PHE A CD2 
3523  C CE1 . PHE B 438  ? 0.9468 1.0192 0.8461 -0.1429 -0.0878 -0.0322 435  PHE A CE1 
3524  C CE2 . PHE B 438  ? 0.9189 0.9785 0.8362 -0.1060 -0.0685 -0.0389 435  PHE A CE2 
3525  C CZ  . PHE B 438  ? 0.9443 0.9851 0.8444 -0.1264 -0.0818 -0.0372 435  PHE A CZ  
3526  N N   . LYS B 439  ? 0.7873 1.0837 0.7377 -0.1436 -0.0716 -0.0084 436  LYS A N   
3527  C CA  . LYS B 439  ? 0.8214 1.1460 0.7671 -0.1722 -0.0831 0.0011  436  LYS A CA  
3528  C C   . LYS B 439  ? 0.8468 1.2106 0.8011 -0.1857 -0.0844 0.0135  436  LYS A C   
3529  O O   . LYS B 439  ? 0.8919 1.2514 0.8388 -0.2141 -0.0957 0.0220  436  LYS A O   
3530  C CB  . LYS B 439  ? 0.8377 1.2039 0.7854 -0.1685 -0.0824 0.0007  436  LYS A CB  
3531  C CG  . LYS B 439  ? 0.8712 1.2023 0.8084 -0.1610 -0.0838 -0.0099 436  LYS A CG  
3532  C CD  . LYS B 439  ? 0.8720 1.2494 0.8127 -0.1552 -0.0820 -0.0099 436  LYS A CD  
3533  C CE  . LYS B 439  ? 0.8838 1.2280 0.8154 -0.1436 -0.0814 -0.0211 436  LYS A CE  
3534  N NZ  . LYS B 439  ? 0.9207 1.2182 0.8346 -0.1649 -0.0944 -0.0230 436  LYS A NZ  
3535  N N   . GLN B 440  ? 0.8162 1.2174 0.7840 -0.1655 -0.0734 0.0148  437  GLN A N   
3536  C CA  . GLN B 440  ? 0.7846 1.2299 0.7609 -0.1753 -0.0737 0.0267  437  GLN A CA  
3537  C C   . GLN B 440  ? 0.7846 1.1921 0.7584 -0.1868 -0.0771 0.0295  437  GLN A C   
3538  O O   . GLN B 440  ? 0.7777 1.2040 0.7510 -0.2112 -0.0848 0.0409  437  GLN A O   
3539  C CB  . GLN B 440  ? 0.7393 1.2267 0.7266 -0.1467 -0.0613 0.0259  437  GLN A CB  
3540  N N   . LYS B 441  ? 0.7973 1.1530 0.7690 -0.1700 -0.0716 0.0198  438  LYS A N   
3541  C CA  . LYS B 441  ? 0.8339 1.1533 0.8028 -0.1784 -0.0744 0.0219  438  LYS A CA  
3542  C C   . LYS B 441  ? 0.8882 1.1697 0.8407 -0.2063 -0.0887 0.0246  438  LYS A C   
3543  O O   . LYS B 441  ? 0.9244 1.1955 0.8726 -0.2247 -0.0953 0.0322  438  LYS A O   
3544  C CB  . LYS B 441  ? 0.8399 1.1170 0.8103 -0.1533 -0.0653 0.0112  438  LYS A CB  
3545  C CG  . LYS B 441  ? 0.8490 1.1000 0.8202 -0.1559 -0.0651 0.0137  438  LYS A CG  
3546  C CD  . LYS B 441  ? 0.8406 1.1309 0.8249 -0.1451 -0.0571 0.0188  438  LYS A CD  
3547  C CE  . LYS B 441  ? 0.8665 1.1335 0.8518 -0.1493 -0.0574 0.0220  438  LYS A CE  
3548  N NZ  . LYS B 441  ? 0.9136 1.1801 0.8925 -0.1790 -0.0689 0.0321  438  LYS A NZ  
3549  N N   . THR B 442  ? 0.9286 1.1864 0.8693 -0.2095 -0.0941 0.0185  439  THR A N   
3550  C CA  . THR B 442  ? 0.9924 1.2073 0.9120 -0.2344 -0.1091 0.0200  439  THR A CA  
3551  C C   . THR B 442  ? 1.0274 1.2776 0.9428 -0.2679 -0.1209 0.0342  439  THR A C   
3552  O O   . THR B 442  ? 1.0579 1.2822 0.9599 -0.2912 -0.1319 0.0410  439  THR A O   
3553  C CB  . THR B 442  ? 1.0211 1.2049 0.9279 -0.2280 -0.1120 0.0098  439  THR A CB  
3554  O OG1 . THR B 442  ? 1.0274 1.1791 0.9375 -0.1987 -0.1016 -0.0021 439  THR A OG1 
3555  C CG2 . THR B 442  ? 1.0704 1.2054 0.9505 -0.2527 -0.1288 0.0109  439  THR A CG2 
3556  N N   . SER B 443  ? 1.0105 1.3212 0.9361 -0.2711 -0.1192 0.0395  440  SER A N   
3557  C CA  . SER B 443  ? 1.0200 1.3740 0.9433 -0.3038 -0.1301 0.0546  440  SER A CA  
3558  C C   . SER B 443  ? 0.9755 1.3597 0.9096 -0.3107 -0.1278 0.0657  440  SER A C   
3559  O O   . SER B 443  ? 1.0072 1.4013 0.9333 -0.3427 -0.1397 0.0785  440  SER A O   
3560  C CB  . SER B 443  ? 1.0184 1.4370 0.9516 -0.3021 -0.1275 0.0578  440  SER A CB  
3561  O OG  . SER B 443  ? 0.9891 1.4580 0.9430 -0.2748 -0.1126 0.0573  440  SER A OG  
3562  N N   . GLU B 444  ? 0.9127 1.3108 0.8634 -0.2820 -0.1133 0.0614  441  GLU A N   
3563  C CA  . GLU B 444  ? 0.8905 1.3152 0.8510 -0.2856 -0.1104 0.0709  441  GLU A CA  
3564  C C   . GLU B 444  ? 0.8755 1.2437 0.8223 -0.3034 -0.1193 0.0732  441  GLU A C   
3565  O O   . GLU B 444  ? 0.8391 1.2254 0.7841 -0.3277 -0.1266 0.0861  441  GLU A O   
3566  C CB  . GLU B 444  ? 0.9169 1.3572 0.8936 -0.2494 -0.0940 0.0639  441  GLU A CB  
3567  C CG  . GLU B 444  ? 0.9733 1.4525 0.9613 -0.2488 -0.0896 0.0736  441  GLU A CG  
3568  C CD  . GLU B 444  ? 1.0007 1.4793 0.9991 -0.2132 -0.0751 0.0652  441  GLU A CD  
3569  O OE1 . GLU B 444  ? 1.0008 1.4245 0.9960 -0.2021 -0.0720 0.0566  441  GLU A OE1 
3570  O OE2 . GLU B 444  ? 1.0064 1.5391 1.0142 -0.1962 -0.0674 0.0673  441  GLU A OE2 
3571  N N   . ILE B 445  ? 0.9011 1.2016 0.8371 -0.2908 -0.1189 0.0610  442  ILE A N   
3572  C CA  . ILE B 445  ? 0.9272 1.1698 0.8469 -0.3042 -0.1275 0.0619  442  ILE A CA  
3573  C C   . ILE B 445  ? 0.9907 1.2113 0.8865 -0.3402 -0.1463 0.0694  442  ILE A C   
3574  O O   . ILE B 445  ? 1.0327 1.2380 0.9168 -0.3642 -0.1564 0.0791  442  ILE A O   
3575  C CB  . ILE B 445  ? 0.8757 1.0571 0.7896 -0.2783 -0.1217 0.0468  442  ILE A CB  
3576  C CG1 . ILE B 445  ? 0.8180 1.0183 0.7532 -0.2473 -0.1050 0.0414  442  ILE A CG1 
3577  C CG2 . ILE B 445  ? 0.8874 1.0060 0.7800 -0.2908 -0.1321 0.0471  442  ILE A CG2 
3578  C CD1 . ILE B 445  ? 0.8077 0.9568 0.7394 -0.2225 -0.0986 0.0280  442  ILE A CD1 
3579  N N   . LEU B 446  ? 1.0229 1.2397 0.9089 -0.3454 -0.1519 0.0655  443  LEU A N   
3580  C CA  . LEU B 446  ? 1.0637 1.2545 0.9231 -0.3803 -0.1711 0.0721  443  LEU A CA  
3581  C C   . LEU B 446  ? 1.0561 1.3045 0.9191 -0.4138 -0.1793 0.0906  443  LEU A C   
3582  O O   . LEU B 446  ? 1.0753 1.2977 0.9159 -0.4471 -0.1958 0.1003  443  LEU A O   
3583  C CB  . LEU B 446  ? 1.0885 1.2676 0.9380 -0.3768 -0.1745 0.0636  443  LEU A CB  
3584  C CG  . LEU B 446  ? 1.1227 1.2329 0.9583 -0.3525 -0.1723 0.0469  443  LEU A CG  
3585  C CD1 . LEU B 446  ? 1.1345 1.2451 0.9643 -0.3475 -0.1739 0.0392  443  LEU A CD1 
3586  C CD2 . LEU B 446  ? 1.1746 1.2104 0.9782 -0.3675 -0.1869 0.0465  443  LEU A CD2 
3587  N N   . SER B 447  ? 1.0442 1.3714 0.9335 -0.4055 -0.1687 0.0964  444  SER A N   
3588  C CA  . SER B 447  ? 1.0587 1.4505 0.9535 -0.4354 -0.1754 0.1150  444  SER A CA  
3589  C C   . SER B 447  ? 1.0546 1.4422 0.9501 -0.4466 -0.1770 0.1245  444  SER A C   
3590  O O   . SER B 447  ? 1.0832 1.4764 0.9651 -0.4761 -0.1866 0.1397  444  SER A O   
3591  C CB  . SER B 447  ? 1.0506 1.5290 0.9720 -0.4182 -0.1626 0.1179  444  SER A CB  
3592  O OG  . SER B 447  ? 1.0518 1.5420 0.9929 -0.3819 -0.1452 0.1105  444  SER A OG  
3593  N N   . HIS B 448  ? 1.0156 1.3856 0.9233 -0.4167 -0.1638 0.1161  445  HIS A N   
3594  C CA  . HIS B 448  ? 1.0170 1.3807 0.9255 -0.4251 -0.1647 0.1242  445  HIS A CA  
3595  C C   . HIS B 448  ? 1.0814 1.3695 0.9593 -0.4501 -0.1812 0.1259  445  HIS A C   
3596  O O   . HIS B 448  ? 1.0351 1.3263 0.9044 -0.4773 -0.1905 0.1396  445  HIS A O   
3597  C CB  . HIS B 448  ? 0.9912 1.3488 0.9177 -0.3868 -0.1474 0.1138  445  HIS A CB  
3598  C CG  . HIS B 448  ? 0.9521 1.3864 0.9049 -0.3667 -0.1334 0.1167  445  HIS A CG  
3599  N ND1 . HIS B 448  ? 0.9175 1.3546 0.8845 -0.3282 -0.1178 0.1040  445  HIS A ND1 
3600  C CD2 . HIS B 448  ? 0.9410 1.4513 0.9058 -0.3789 -0.1331 0.1312  445  HIS A CD2 
3601  C CE1 . HIS B 448  ? 0.8862 1.3935 0.8706 -0.3163 -0.1090 0.1096  445  HIS A CE1 
3602  N NE2 . HIS B 448  ? 0.8993 1.4545 0.8837 -0.3455 -0.1175 0.1260  445  HIS A NE2 
3603  N N   . ALA B 449  ? 1.2491 1.4678 1.1081 -0.4400 -0.1849 0.1122  446  ALA A N   
3604  C CA  . ALA B 449  ? 1.3746 1.5172 1.1988 -0.4616 -0.2020 0.1129  446  ALA A CA  
3605  C C   . ALA B 449  ? 1.4471 1.5927 1.2481 -0.4989 -0.2187 0.1259  446  ALA A C   
3606  O O   . ALA B 449  ? 1.4986 1.6035 1.2726 -0.5174 -0.2290 0.1353  446  ALA A O   
3607  C CB  . ALA B 449  ? 1.3430 1.4143 1.1517 -0.4363 -0.2006 0.0947  446  ALA A CB  
3608  N N   . HIS B 450  ? 1.4583 1.6479 1.2670 -0.5011 -0.2170 0.1271  447  HIS A N   
3609  C CA  . HIS B 450  ? 1.5024 1.6986 1.2898 -0.5274 -0.2266 0.1410  447  HIS A CA  
3610  C C   . HIS B 450  ? 1.4859 1.7382 1.2804 -0.5434 -0.2237 0.1611  447  HIS A C   
3611  O O   . HIS B 450  ? 1.5353 1.7687 1.3027 -0.5694 -0.2350 0.1750  447  HIS A O   
3612  C CB  . HIS B 450  ? 1.5248 1.7574 1.3205 -0.5239 -0.2243 0.1369  447  HIS A CB  
3613  C CG  . HIS B 450  ? 1.6029 1.8779 1.3904 -0.5481 -0.2285 0.1543  447  HIS A CG  
3614  N ND1 . HIS B 450  ? 1.6933 1.9254 1.4450 -0.5765 -0.2434 0.1658  447  HIS A ND1 
3615  C CD2 . HIS B 450  ? 1.6038 1.9604 1.4120 -0.5477 -0.2198 0.1627  447  HIS A CD2 
3616  C CE1 . HIS B 450  ? 1.7111 1.9977 1.4628 -0.5946 -0.2438 0.1810  447  HIS A CE1 
3617  N NE2 . HIS B 450  ? 1.6600 2.0233 1.4460 -0.5771 -0.2293 0.1793  447  HIS A NE2 
3618  N N   . ALA B 451  ? 1.3983 1.7191 1.2265 -0.5274 -0.2092 0.1631  448  ALA A N   
3619  C CA  . ALA B 451  ? 1.3358 1.7125 1.1707 -0.5386 -0.2054 0.1813  448  ALA A CA  
3620  C C   . ALA B 451  ? 1.2941 1.6320 1.1173 -0.5461 -0.2098 0.1866  448  ALA A C   
3621  O O   . ALA B 451  ? 1.3190 1.6926 1.1403 -0.5597 -0.2099 0.2029  448  ALA A O   
3622  C CB  . ALA B 451  ? 1.2439 1.7048 1.1157 -0.5149 -0.1882 0.1808  448  ALA A CB  
3623  N N   . ALA B 452  ? 1.2404 1.5075 1.0544 -0.5368 -0.2136 0.1735  449  ALA A N   
3624  C CA  . ALA B 452  ? 1.2300 1.4550 1.0311 -0.5421 -0.2181 0.1774  449  ALA A CA  
3625  C C   . ALA B 452  ? 1.2938 1.4423 1.0508 -0.5642 -0.2360 0.1817  449  ALA A C   
3626  O O   . ALA B 452  ? 1.2983 1.4269 1.0390 -0.5771 -0.2422 0.1920  449  ALA A O   
3627  C CB  . ALA B 452  ? 1.1998 1.3950 1.0167 -0.5165 -0.2105 0.1612  449  ALA A CB  
3628  N N   . LEU B 453  ? 1.3513 1.4558 1.0868 -0.5680 -0.2449 0.1742  450  LEU A N   
3629  C CA  . LEU B 453  ? 1.4296 1.4576 1.1191 -0.5866 -0.2627 0.1778  450  LEU A CA  
3630  C C   . LEU B 453  ? 1.5237 1.5772 1.1936 -0.6182 -0.2721 0.1993  450  LEU A C   
3631  O O   . LEU B 453  ? 1.5873 1.5891 1.2214 -0.6357 -0.2861 0.2075  450  LEU A O   
3632  C CB  . LEU B 453  ? 1.4112 1.3868 1.0818 -0.5801 -0.2695 0.1637  450  LEU A CB  
3633  C CG  . LEU B 453  ? 1.3614 1.2756 1.0293 -0.5534 -0.2675 0.1433  450  LEU A CG  
3634  C CD1 . LEU B 453  ? 1.3785 1.2380 1.0202 -0.5492 -0.2765 0.1314  450  LEU A CD1 
3635  C CD2 . LEU B 453  ? 1.3697 1.2262 1.0160 -0.5524 -0.2735 0.1444  450  LEU A CD2 
3636  N N   . ASP B 454  ? 1.5919 1.7241 1.2826 -0.6254 -0.2652 0.2089  451  ASP A N   
3637  C CA  . ASP B 454  ? 1.6560 1.8202 1.3290 -0.6558 -0.2733 0.2305  451  ASP A CA  
3638  C C   . ASP B 454  ? 1.6497 1.8683 1.3377 -0.6602 -0.2669 0.2447  451  ASP A C   
3639  O O   . ASP B 454  ? 1.6981 1.9308 1.3650 -0.6869 -0.2761 0.2635  451  ASP A O   
3640  C CB  . ASP B 454  ? 1.6610 1.8827 1.3444 -0.6623 -0.2698 0.2350  451  ASP A CB  
3641  C CG  . ASP B 454  ? 1.6353 1.9318 1.3645 -0.6361 -0.2506 0.2273  451  ASP A CG  
3642  O OD1 . ASP B 454  ? 1.6336 1.9250 1.3850 -0.6113 -0.2409 0.2148  451  ASP A OD1 
3643  O OD2 . ASP B 454  ? 1.6274 1.9872 1.3687 -0.6397 -0.2454 0.2338  451  ASP A OD2 
3644  N N   . GLN B 455  ? 1.5203 1.7692 1.2422 -0.6352 -0.2522 0.2365  452  GLN A N   
3645  C CA  . GLN B 455  ? 1.4741 1.7705 1.2095 -0.6364 -0.2461 0.2485  452  GLN A CA  
3646  C C   . GLN B 455  ? 1.5073 1.7385 1.2149 -0.6476 -0.2578 0.2522  452  GLN A C   
3647  O O   . GLN B 455  ? 1.5052 1.6735 1.2086 -0.6325 -0.2587 0.2377  452  GLN A O   
3648  C CB  . GLN B 455  ? 1.3993 1.7422 1.1771 -0.6046 -0.2274 0.2377  452  GLN A CB  
3649  C CG  . GLN B 455  ? 1.3815 1.7807 1.1755 -0.6023 -0.2196 0.2494  452  GLN A CG  
3650  C CD  . GLN B 455  ? 1.3285 1.7564 1.1590 -0.5698 -0.2030 0.2371  452  GLN A CD  
3651  O OE1 . GLN B 455  ? 1.3100 1.6893 1.1464 -0.5531 -0.2009 0.2209  452  GLN A OE1 
3652  N NE2 . GLN B 455  ? 1.3064 1.8132 1.1593 -0.5599 -0.1915 0.2452  452  GLN A NE2 
3653  N N   . PRO B 456  ? 1.5359 1.7794 1.2225 -0.6730 -0.2671 0.2712  453  PRO A N   
3654  C CA  . PRO B 456  ? 1.5784 1.7567 1.2346 -0.6843 -0.2799 0.2749  453  PRO A CA  
3655  C C   . PRO B 456  ? 1.5301 1.7187 1.2092 -0.6658 -0.2698 0.2709  453  PRO A C   
3656  O O   . PRO B 456  ? 1.4949 1.7563 1.2078 -0.6538 -0.2556 0.2740  453  PRO A O   
3657  C CB  . PRO B 456  ? 1.6239 1.8249 1.2524 -0.7188 -0.2928 0.2981  453  PRO A CB  
3658  C CG  . PRO B 456  ? 1.5776 1.8785 1.2362 -0.7176 -0.2801 0.3075  453  PRO A CG  
3659  C CD  . PRO B 456  ? 1.5311 1.8481 1.2178 -0.6933 -0.2674 0.2907  453  PRO A CD  
3660  N N   . LEU B 457  ? 1.5316 1.6446 1.1899 -0.6625 -0.2776 0.2640  454  LEU A N   
3661  C CA  . LEU B 457  ? 1.5031 1.6166 1.1781 -0.6475 -0.2701 0.2610  454  LEU A CA  
3662  C C   . LEU B 457  ? 1.5215 1.6752 1.1903 -0.6672 -0.2743 0.2807  454  LEU A C   
3663  O O   . LEU B 457  ? 1.5720 1.7278 1.2122 -0.6953 -0.2877 0.2961  454  LEU A O   
3664  C CB  . LEU B 457  ? 1.5574 1.5776 1.2080 -0.6386 -0.2781 0.2487  454  LEU A CB  
3665  C CG  . LEU B 457  ? 1.5517 1.5379 1.2182 -0.6096 -0.2691 0.2270  454  LEU A CG  
3666  C CD1 . LEU B 457  ? 1.4754 1.5304 1.1914 -0.5874 -0.2489 0.2212  454  LEU A CD1 
3667  C CD2 . LEU B 457  ? 1.5965 1.5513 1.2461 -0.6117 -0.2756 0.2193  454  LEU A CD2 
3668  N N   . PRO B 458  ? 1.4875 1.6743 1.1818 -0.6532 -0.2635 0.2809  455  PRO A N   
3669  C CA  . PRO B 458  ? 1.5063 1.7302 1.1942 -0.6706 -0.2679 0.2991  455  PRO A CA  
3670  C C   . PRO B 458  ? 1.5629 1.7151 1.2102 -0.6889 -0.2857 0.3045  455  PRO A C   
3671  O O   . PRO B 458  ? 1.6179 1.6903 1.2408 -0.6860 -0.2943 0.2937  455  PRO A O   
3672  C CB  . PRO B 458  ? 1.4311 1.7029 1.1586 -0.6455 -0.2504 0.2944  455  PRO A CB  
3673  C CG  . PRO B 458  ? 1.3897 1.6122 1.1303 -0.6196 -0.2428 0.2736  455  PRO A CG  
3674  C CD  . PRO B 458  ? 1.4173 1.6127 1.1474 -0.6213 -0.2469 0.2654  455  PRO A CD  
3675  N N   . THR B 459  ? 1.5574 1.7375 1.1956 -0.7065 -0.2916 0.3210  456  THR A N   
3676  C CA  . THR B 459  ? 1.6099 1.7251 1.2077 -0.7250 -0.3096 0.3272  456  THR A CA  
3677  C C   . THR B 459  ? 1.5975 1.6717 1.2032 -0.7045 -0.3047 0.3160  456  THR A C   
3678  O O   . THR B 459  ? 1.6367 1.6304 1.2103 -0.7063 -0.3167 0.3104  456  THR A O   
3679  C CB  . THR B 459  ? 1.6444 1.8055 1.2266 -0.7543 -0.3195 0.3503  456  THR A CB  
3680  O OG1 . THR B 459  ? 1.6038 1.8429 1.2228 -0.7425 -0.3049 0.3552  456  THR A OG1 
3681  C CG2 . THR B 459  ? 1.6655 1.8578 1.2325 -0.7778 -0.3269 0.3626  456  THR A CG2 
3682  N N   . THR B 460  ? 1.5468 1.6745 1.1930 -0.6840 -0.2875 0.3128  457  THR A N   
3683  C CA  . THR B 460  ? 1.5306 1.6270 1.1875 -0.6644 -0.2813 0.3032  457  THR A CA  
3684  C C   . THR B 460  ? 1.4601 1.5956 1.1628 -0.6333 -0.2600 0.2900  457  THR A C   
3685  O O   . THR B 460  ? 1.4020 1.5954 1.1285 -0.6272 -0.2501 0.2898  457  THR A O   
3686  C CB  . THR B 460  ? 1.5415 1.6613 1.1943 -0.6766 -0.2856 0.3172  457  THR A CB  
3687  O OG1 . THR B 460  ? 1.5212 1.7328 1.1959 -0.6832 -0.2787 0.3307  457  THR A OG1 
3688  C CG2 . THR B 460  ? 1.6202 1.6829 1.2235 -0.7047 -0.3081 0.3274  457  THR A CG2 
3689  N N   . LEU B 461  ? 1.4492 1.5516 1.1624 -0.6133 -0.2534 0.2793  458  LEU A N   
3690  C CA  . LEU B 461  ? 1.3624 1.4979 1.1168 -0.5844 -0.2341 0.2679  458  LEU A CA  
3691  C C   . LEU B 461  ? 1.3302 1.5171 1.1073 -0.5780 -0.2250 0.2753  458  LEU A C   
3692  O O   . LEU B 461  ? 1.3018 1.4931 1.1043 -0.5548 -0.2120 0.2659  458  LEU A O   
3693  C CB  . LEU B 461  ? 1.3345 1.3985 1.0855 -0.5647 -0.2319 0.2502  458  LEU A CB  
3694  C CG  . LEU B 461  ? 1.2996 1.3441 1.0557 -0.5525 -0.2281 0.2361  458  LEU A CG  
3695  C CD1 . LEU B 461  ? 1.3366 1.3672 1.0647 -0.5735 -0.2414 0.2412  458  LEU A CD1 
3696  C CD2 . LEU B 461  ? 1.2969 1.2662 1.0432 -0.5342 -0.2282 0.2206  458  LEU A CD2 
3697  N N   . LYS B 462  ? 1.3581 1.5843 1.1254 -0.5985 -0.2322 0.2924  459  LYS A N   
3698  C CA  . LYS B 462  ? 1.3280 1.6005 1.1131 -0.5933 -0.2253 0.3001  459  LYS A CA  
3699  C C   . LYS B 462  ? 1.2607 1.6112 1.0854 -0.5712 -0.2069 0.2976  459  LYS A C   
3700  O O   . LYS B 462  ? 1.1955 1.5618 1.0435 -0.5508 -0.1951 0.2926  459  LYS A O   
3701  C CB  . LYS B 462  ? 1.3817 1.6769 1.1435 -0.6220 -0.2391 0.3195  459  LYS A CB  
3702  N N   . LYS B 463  ? 1.2760 1.6753 1.1069 -0.5740 -0.2044 0.3011  460  LYS A N   
3703  C CA  . LYS B 463  ? 1.2344 1.7087 1.0983 -0.5518 -0.1880 0.2990  460  LYS A CA  
3704  C C   . LYS B 463  ? 1.2012 1.6575 1.0847 -0.5281 -0.1770 0.2809  460  LYS A C   
3705  O O   . LYS B 463  ? 1.2518 1.6516 1.1217 -0.5332 -0.1832 0.2723  460  LYS A O   
3706  C CB  . LYS B 463  ? 1.2333 1.7739 1.0932 -0.5648 -0.1904 0.3124  460  LYS A CB  
3707  N N   . GLN B 464  ? 1.1198 1.6244 1.0339 -0.5014 -0.1610 0.2750  461  GLN A N   
3708  C CA  . GLN B 464  ? 1.0567 1.5524 0.9905 -0.4783 -0.1503 0.2586  461  GLN A CA  
3709  C C   . GLN B 464  ? 1.0510 1.5705 0.9840 -0.4813 -0.1509 0.2573  461  GLN A C   
3710  O O   . GLN B 464  ? 1.0149 1.5026 0.9521 -0.4729 -0.1489 0.2443  461  GLN A O   
3711  C CB  . GLN B 464  ? 1.0219 1.5650 0.9853 -0.4490 -0.1341 0.2538  461  GLN A CB  
3712  C CG  . GLN B 464  ? 1.0103 1.5429 0.9938 -0.4246 -0.1233 0.2370  461  GLN A CG  
3713  C CD  . GLN B 464  ? 1.0372 1.4919 1.0157 -0.4241 -0.1260 0.2261  461  GLN A CD  
3714  O OE1 . GLN B 464  ? 1.0592 1.4812 1.0303 -0.4287 -0.1291 0.2289  461  GLN A OE1 
3715  N NE2 . GLN B 464  ? 1.0190 1.4438 1.0001 -0.4177 -0.1251 0.2138  461  GLN A NE2 
3716  N N   . GLU B 465  ? 1.1040 1.6803 1.0309 -0.4930 -0.1536 0.2710  462  GLU A N   
3717  C CA  . GLU B 465  ? 1.0902 1.6897 1.0138 -0.4980 -0.1548 0.2713  462  GLU A CA  
3718  C C   . GLU B 465  ? 1.1054 1.6361 1.0032 -0.5205 -0.1689 0.2689  462  GLU A C   
3719  O O   . GLU B 465  ? 1.1232 1.6499 1.0211 -0.5193 -0.1688 0.2624  462  GLU A O   
3720  C CB  . GLU B 465  ? 1.0580 1.7310 0.9764 -0.5082 -0.1559 0.2884  462  GLU A CB  
3721  N N   . GLU B 466  ? 1.0934 1.5682 0.9671 -0.5398 -0.1814 0.2739  463  GLU A N   
3722  C CA  . GLU B 466  ? 1.1645 1.5651 1.0090 -0.5579 -0.1956 0.2705  463  GLU A CA  
3723  C C   . GLU B 466  ? 1.1761 1.5112 1.0252 -0.5405 -0.1925 0.2518  463  GLU A C   
3724  O O   . GLU B 466  ? 1.1612 1.4445 0.9930 -0.5460 -0.2002 0.2443  463  GLU A O   
3725  C CB  . GLU B 466  ? 1.2488 1.6153 1.0609 -0.5848 -0.2116 0.2837  463  GLU A CB  
3726  C CG  . GLU B 466  ? 1.3055 1.7294 1.1058 -0.6077 -0.2181 0.3035  463  GLU A CG  
3727  C CD  . GLU B 466  ? 1.3728 1.7682 1.1427 -0.6333 -0.2336 0.3172  463  GLU A CD  
3728  O OE1 . GLU B 466  ? 1.3691 1.7332 1.1397 -0.6266 -0.2334 0.3139  463  GLU A OE1 
3729  O OE2 . GLU B 466  ? 1.4176 1.8219 1.1620 -0.6605 -0.2464 0.3316  463  GLU A OE2 
3730  N N   . LYS B 467  ? 1.2059 1.5424 1.0765 -0.5195 -0.1817 0.2446  464  LYS A N   
3731  C CA  . LYS B 467  ? 1.2099 1.4939 1.0877 -0.5011 -0.1771 0.2273  464  LYS A CA  
3732  C C   . LYS B 467  ? 1.1860 1.4975 1.0853 -0.4843 -0.1675 0.2163  464  LYS A C   
3733  O O   . LYS B 467  ? 1.1673 1.4294 1.0625 -0.4772 -0.1689 0.2031  464  LYS A O   
3734  C CB  . LYS B 467  ? 1.1627 1.4451 1.0578 -0.4841 -0.1679 0.2240  464  LYS A CB  
3735  C CG  . LYS B 467  ? 1.1798 1.4241 1.0535 -0.4974 -0.1772 0.2320  464  LYS A CG  
3736  C CD  . LYS B 467  ? 1.1275 1.3676 1.0195 -0.4786 -0.1671 0.2272  464  LYS A CD  
3737  C CE  . LYS B 467  ? 1.1559 1.3589 1.0268 -0.4907 -0.1763 0.2349  464  LYS A CE  
3738  N NZ  . LYS B 467  ? 1.1284 1.3253 1.0164 -0.4722 -0.1664 0.2302  464  LYS A NZ  
3739  N N   . GLU B 468  ? 1.2179 1.6076 1.1382 -0.4767 -0.1582 0.2215  465  GLU A N   
3740  C CA  . GLU B 468  ? 1.2038 1.6244 1.1452 -0.4578 -0.1485 0.2109  465  GLU A CA  
3741  C C   . GLU B 468  ? 1.1882 1.5846 1.1129 -0.4708 -0.1574 0.2079  465  GLU A C   
3742  O O   . GLU B 468  ? 1.1667 1.5422 1.0986 -0.4585 -0.1546 0.1942  465  GLU A O   
3743  C CB  . GLU B 468  ? 1.2324 1.7414 1.1951 -0.4444 -0.1372 0.2177  465  GLU A CB  
3744  C CG  . GLU B 468  ? 1.2460 1.7910 1.2302 -0.4210 -0.1266 0.2068  465  GLU A CG  
3745  C CD  . GLU B 468  ? 1.2676 1.8970 1.2664 -0.4056 -0.1165 0.2138  465  GLU A CD  
3746  O OE1 . GLU B 468  ? 1.2952 1.9579 1.2846 -0.4183 -0.1195 0.2286  465  GLU A OE1 
3747  O OE2 . GLU B 468  ? 1.2508 1.9127 1.2682 -0.3798 -0.1060 0.2044  465  GLU A OE2 
3748  N N   . ILE B 469  ? 1.1730 1.5721 1.0742 -0.4960 -0.1686 0.2209  466  ILE A N   
3749  C CA  . ILE B 469  ? 1.1610 1.5393 1.0450 -0.5092 -0.1774 0.2192  466  ILE A CA  
3750  C C   . ILE B 469  ? 1.1367 1.4235 0.9976 -0.5135 -0.1877 0.2082  466  ILE A C   
3751  O O   . ILE B 469  ? 1.1337 1.3948 0.9872 -0.5132 -0.1913 0.1994  466  ILE A O   
3752  C CB  . ILE B 469  ? 1.2170 1.6241 1.0803 -0.5362 -0.1870 0.2374  466  ILE A CB  
3753  C CG1 . ILE B 469  ? 1.2655 1.6421 1.1057 -0.5554 -0.1975 0.2491  466  ILE A CG1 
3754  C CG2 . ILE B 469  ? 1.1935 1.6940 1.0781 -0.5280 -0.1760 0.2461  466  ILE A CG2 
3755  C CD1 . ILE B 469  ? 1.3055 1.7162 1.1254 -0.5829 -0.2072 0.2688  466  ILE A CD1 
3756  N N   . LEU B 470  ? 1.1084 1.3445 0.9558 -0.5161 -0.1926 0.2083  467  LEU A N   
3757  C CA  . LEU B 470  ? 1.1049 1.2535 0.9295 -0.5140 -0.2010 0.1964  467  LEU A CA  
3758  C C   . LEU B 470  ? 1.0181 1.1563 0.8649 -0.4880 -0.1904 0.1788  467  LEU A C   
3759  O O   . LEU B 470  ? 1.0250 1.1136 0.8580 -0.4842 -0.1955 0.1672  467  LEU A O   
3760  C CB  . LEU B 470  ? 1.1361 1.2366 0.9413 -0.5196 -0.2078 0.2007  467  LEU A CB  
3761  C CG  . LEU B 470  ? 1.1689 1.1783 0.9489 -0.5121 -0.2154 0.1880  467  LEU A CG  
3762  C CD1 . LEU B 470  ? 0.9331 0.8938 0.6785 -0.5251 -0.2297 0.1860  467  LEU A CD1 
3763  C CD2 . LEU B 470  ? 0.9093 0.8790 0.6723 -0.5149 -0.2208 0.1927  467  LEU A CD2 
3764  N N   . LYS B 471  ? 0.9273 1.1115 0.8068 -0.4698 -0.1761 0.1766  468  LYS A N   
3765  C CA  . LYS B 471  ? 0.8756 1.0494 0.7711 -0.4302 -0.1612 0.1586  468  LYS A CA  
3766  C C   . LYS B 471  ? 0.8188 1.0253 0.7240 -0.4224 -0.1569 0.1529  468  LYS A C   
3767  O O   . LYS B 471  ? 0.7983 0.9705 0.7014 -0.4004 -0.1523 0.1379  468  LYS A O   
3768  C CB  . LYS B 471  ? 0.8915 1.1033 0.8133 -0.4052 -0.1454 0.1574  468  LYS A CB  
3769  C CG  . LYS B 471  ? 0.9088 1.1102 0.8455 -0.3654 -0.1303 0.1400  468  LYS A CG  
3770  C CD  . LYS B 471  ? 0.8782 1.1371 0.8415 -0.3435 -0.1154 0.1406  468  LYS A CD  
3771  C CE  . LYS B 471  ? 0.8443 1.0974 0.8198 -0.3078 -0.1021 0.1245  468  LYS A CE  
3772  N NZ  . LYS B 471  ? 0.8025 1.1132 0.7994 -0.2871 -0.0893 0.1251  468  LYS A NZ  
3773  N N   . SER B 472  ? 0.8028 1.0780 0.7184 -0.4401 -0.1583 0.1651  469  SER A N   
3774  C CA  . SER B 472  ? 0.7791 1.0914 0.7045 -0.4321 -0.1540 0.1606  469  SER A CA  
3775  C C   . SER B 472  ? 0.7937 1.0525 0.6946 -0.4453 -0.1662 0.1547  469  SER A C   
3776  O O   . SER B 472  ? 0.7853 1.0359 0.6902 -0.4246 -0.1601 0.1419  469  SER A O   
3777  C CB  . SER B 472  ? 0.7714 1.1691 0.7094 -0.4497 -0.1544 0.1766  469  SER A CB  
3778  O OG  . SER B 472  ? 0.7582 1.1945 0.7051 -0.4429 -0.1510 0.1728  469  SER A OG  
3779  N N   . GLN B 473  ? 0.8333 1.0521 0.7058 -0.4776 -0.1834 0.1637  470  GLN A N   
3780  C CA  . GLN B 473  ? 0.8925 1.0528 0.7360 -0.4877 -0.1958 0.1577  470  GLN A CA  
3781  C C   . GLN B 473  ? 0.9498 1.0354 0.7821 -0.4640 -0.1943 0.1402  470  GLN A C   
3782  O O   . GLN B 473  ? 0.9560 1.0085 0.7765 -0.4557 -0.1968 0.1293  470  GLN A O   
3783  C CB  . GLN B 473  ? 0.9596 1.0884 0.7678 -0.5148 -0.2105 0.1714  470  GLN A CB  
3784  C CG  . GLN B 473  ? 0.9661 1.1641 0.7786 -0.5325 -0.2103 0.1891  470  GLN A CG  
3785  C CD  . GLN B 473  ? 0.9999 1.1657 0.7754 -0.5611 -0.2260 0.2036  470  GLN A CD  
3786  O OE1 . GLN B 473  ? 1.0144 1.1034 0.7574 -0.5682 -0.2386 0.1994  470  GLN A OE1 
3787  N NE2 . GLN B 473  ? 1.0116 1.2360 0.7898 -0.5768 -0.2258 0.2211  470  GLN A NE2 
3788  N N   . LEU B 474  ? 0.9922 1.0514 0.8269 -0.4487 -0.1887 0.1372  471  LEU A N   
3789  C CA  . LEU B 474  ? 1.0362 1.0319 0.8620 -0.4194 -0.1840 0.1208  471  LEU A CA  
3790  C C   . LEU B 474  ? 0.9509 0.9725 0.8029 -0.3834 -0.1663 0.1073  471  LEU A C   
3791  O O   . LEU B 474  ? 0.9599 0.9376 0.8027 -0.3636 -0.1645 0.0936  471  LEU A O   
3792  C CB  . LEU B 474  ? 1.0887 1.0561 0.9117 -0.4128 -0.1824 0.1223  471  LEU A CB  
3793  C CG  . LEU B 474  ? 0.8450 0.7595 0.6326 -0.4424 -0.2014 0.1317  471  LEU A CG  
3794  C CD1 . LEU B 474  ? 0.8693 0.7701 0.6599 -0.4345 -0.1975 0.1343  471  LEU A CD1 
3795  C CD2 . LEU B 474  ? 0.8918 0.7276 0.6427 -0.4409 -0.2137 0.1217  471  LEU A CD2 
3796  N N   . ASP B 475  ? 0.8781 0.9694 0.7604 -0.3741 -0.1536 0.1110  472  ASP A N   
3797  C CA  . ASP B 475  ? 0.8332 0.9484 0.7369 -0.3420 -0.1381 0.0991  472  ASP A CA  
3798  C C   . ASP B 475  ? 0.8323 0.9477 0.7293 -0.3446 -0.1419 0.0938  472  ASP A C   
3799  O O   . ASP B 475  ? 0.8240 0.9205 0.7240 -0.3198 -0.1344 0.0805  472  ASP A O   
3800  C CB  . ASP B 475  ? 0.8289 1.0168 0.7608 -0.3324 -0.1258 0.1049  472  ASP A CB  
3801  C CG  . ASP B 475  ? 0.8881 1.0757 0.8283 -0.3248 -0.1203 0.1081  472  ASP A CG  
3802  O OD1 . ASP B 475  ? 0.9197 1.0529 0.8506 -0.3145 -0.1204 0.1011  472  ASP A OD1 
3803  O OD2 . ASP B 475  ? 0.9058 1.1495 0.8612 -0.3282 -0.1158 0.1178  472  ASP A OD2 
3804  N N   . SER B 476  ? 0.8472 0.9853 0.7347 -0.3753 -0.1537 0.1048  473  SER A N   
3805  C CA  . SER B 476  ? 0.8550 0.9920 0.7340 -0.3806 -0.1589 0.1006  473  SER A CA  
3806  C C   . SER B 476  ? 0.8772 0.9339 0.7268 -0.3796 -0.1687 0.0904  473  SER A C   
3807  O O   . SER B 476  ? 0.8648 0.9069 0.7119 -0.3647 -0.1662 0.0794  473  SER A O   
3808  C CB  . SER B 476  ? 0.8538 1.0355 0.7282 -0.4168 -0.1706 0.1164  473  SER A CB  
3809  O OG  . SER B 476  ? 0.8090 1.0684 0.7092 -0.4158 -0.1615 0.1263  473  SER A OG  
3810  N N   . LEU B 477  ? 0.9093 0.9127 0.7348 -0.3939 -0.1802 0.0939  474  LEU A N   
3811  C CA  . LEU B 477  ? 0.9641 0.8880 0.7579 -0.3892 -0.1898 0.0838  474  LEU A CA  
3812  C C   . LEU B 477  ? 0.9343 0.8339 0.7382 -0.3493 -0.1757 0.0682  474  LEU A C   
3813  O O   . LEU B 477  ? 0.9591 0.8206 0.7493 -0.3347 -0.1770 0.0565  474  LEU A O   
3814  C CB  . LEU B 477  ? 1.0503 0.9227 0.8130 -0.4129 -0.2059 0.0919  474  LEU A CB  
3815  C CG  . LEU B 477  ? 1.1199 0.9683 0.8492 -0.4521 -0.2277 0.1015  474  LEU A CG  
3816  C CD1 . LEU B 477  ? 1.1715 0.9692 0.8752 -0.4449 -0.2352 0.0895  474  LEU A CD1 
3817  C CD2 . LEU B 477  ? 1.0938 1.0188 0.8417 -0.4790 -0.2287 0.1161  474  LEU A CD2 
3818  N N   . LEU B 478  ? 0.9032 0.8253 0.7301 -0.3319 -0.1627 0.0682  475  LEU A N   
3819  C CA  . LEU B 478  ? 0.8759 0.7815 0.7140 -0.2961 -0.1493 0.0549  475  LEU A CA  
3820  C C   . LEU B 478  ? 0.8576 0.8006 0.7170 -0.2767 -0.1371 0.0472  475  LEU A C   
3821  O O   . LEU B 478  ? 0.8597 0.7800 0.7201 -0.2515 -0.1300 0.0352  475  LEU A O   
3822  C CB  . LEU B 478  ? 0.8297 0.7498 0.6853 -0.2852 -0.1398 0.0579  475  LEU A CB  
3823  C CG  . LEU B 478  ? 0.7921 0.6864 0.6538 -0.2527 -0.1289 0.0461  475  LEU A CG  
3824  C CD1 . LEU B 478  ? 0.8422 0.6666 0.6727 -0.2490 -0.1389 0.0398  475  LEU A CD1 
3825  C CD2 . LEU B 478  ? 0.7429 0.6600 0.6240 -0.2442 -0.1194 0.0501  475  LEU A CD2 
3826  N N   . GLY B 479  ? 0.8277 0.8293 0.7033 -0.2877 -0.1346 0.0543  476  GLY A N   
3827  C CA  . GLY B 479  ? 0.8043 0.8394 0.6965 -0.2698 -0.1243 0.0473  476  GLY A CA  
3828  C C   . GLY B 479  ? 0.8531 0.8554 0.7272 -0.2698 -0.1311 0.0392  476  GLY A C   
3829  O O   . GLY B 479  ? 0.8623 0.8598 0.7429 -0.2459 -0.1223 0.0283  476  GLY A O   
3830  N N   . LEU B 480  ? 0.8939 0.8723 0.7434 -0.2974 -0.1475 0.0448  477  LEU A N   
3831  C CA  . LEU B 480  ? 0.9017 0.8409 0.7290 -0.2979 -0.1559 0.0368  477  LEU A CA  
3832  C C   . LEU B 480  ? 0.9255 0.8003 0.7355 -0.2764 -0.1558 0.0251  477  LEU A C   
3833  O O   . LEU B 480  ? 0.9359 0.7909 0.7403 -0.2588 -0.1533 0.0141  477  LEU A O   
3834  C CB  . LEU B 480  ? 0.9027 0.8279 0.7039 -0.3347 -0.1752 0.0464  477  LEU A CB  
3835  C CG  . LEU B 480  ? 0.9225 0.8009 0.6947 -0.3388 -0.1869 0.0389  477  LEU A CG  
3836  C CD1 . LEU B 480  ? 0.9005 0.8134 0.6900 -0.3221 -0.1771 0.0313  477  LEU A CD1 
3837  C CD2 . LEU B 480  ? 0.9686 0.8329 0.7130 -0.3790 -0.2075 0.0503  477  LEU A CD2 
3838  N N   . TYR B 481  ? 0.9449 0.7889 0.7461 -0.2767 -0.1585 0.0275  478  TYR A N   
3839  C CA  . TYR B 481  ? 0.9800 0.7691 0.7660 -0.2535 -0.1574 0.0170  478  TYR A CA  
3840  C C   . TYR B 481  ? 0.9118 0.7235 0.7243 -0.2205 -0.1391 0.0077  478  TYR A C   
3841  O O   . TYR B 481  ? 0.9054 0.6856 0.7086 -0.1990 -0.1367 -0.0029 478  TYR A O   
3842  C CB  . TYR B 481  ? 1.0760 0.8338 0.8488 -0.2604 -0.1634 0.0225  478  TYR A CB  
3843  C CG  . TYR B 481  ? 1.1807 0.8915 0.9417 -0.2334 -0.1603 0.0127  478  TYR A CG  
3844  C CD1 . TYR B 481  ? 1.2683 0.9162 0.9924 -0.2288 -0.1722 0.0057  478  TYR A CD1 
3845  C CD2 . TYR B 481  ? 1.1956 0.9258 0.9807 -0.2121 -0.1459 0.0106  478  TYR A CD2 
3846  C CE1 . TYR B 481  ? 1.3049 0.9146 1.0175 -0.2020 -0.1692 -0.0030 478  TYR A CE1 
3847  C CE2 . TYR B 481  ? 1.2267 0.9197 1.0017 -0.1878 -0.1431 0.0026  478  TYR A CE2 
3848  C CZ  . TYR B 481  ? 1.2765 0.9114 1.0159 -0.1821 -0.1544 -0.0041 478  TYR A CZ  
3849  O OH  . TYR B 481  ? 1.2898 0.8923 1.0186 -0.1558 -0.1513 -0.0117 478  TYR A OH  
3850  N N   . HIS B 482  ? 0.8559 0.7218 0.6995 -0.2162 -0.1268 0.0121  479  HIS A N   
3851  C CA  . HIS B 482  ? 0.8051 0.6927 0.6716 -0.1879 -0.1106 0.0043  479  HIS A CA  
3852  C C   . HIS B 482  ? 0.8025 0.7007 0.6710 -0.1789 -0.1076 -0.0029 479  HIS A C   
3853  O O   . HIS B 482  ? 0.8074 0.6956 0.6799 -0.1555 -0.0994 -0.0122 479  HIS A O   
3854  C CB  . HIS B 482  ? 0.7420 0.6816 0.6360 -0.1864 -0.1001 0.0108  479  HIS A CB  
3855  C CG  . HIS B 482  ? 0.7505 0.6800 0.6477 -0.1843 -0.0981 0.0146  479  HIS A CG  
3856  N ND1 . HIS B 482  ? 0.7374 0.7051 0.6508 -0.1918 -0.0942 0.0235  479  HIS A ND1 
3857  C CD2 . HIS B 482  ? 0.7669 0.6540 0.6528 -0.1743 -0.0994 0.0107  479  HIS A CD2 
3858  C CE1 . HIS B 482  ? 0.7469 0.6946 0.6591 -0.1877 -0.0933 0.0249  479  HIS A CE1 
3859  N NE2 . HIS B 482  ? 0.7647 0.6641 0.6606 -0.1771 -0.0964 0.0173  479  HIS A NE2 
3860  N N   . LEU B 483  ? 0.8073 0.7276 0.6729 -0.1980 -0.1143 0.0018  480  LEU A N   
3861  C CA  . LEU B 483  ? 0.7989 0.7334 0.6673 -0.1903 -0.1114 -0.0045 480  LEU A CA  
3862  C C   . LEU B 483  ? 0.8405 0.7226 0.6850 -0.1812 -0.1176 -0.0143 480  LEU A C   
3863  O O   . LEU B 483  ? 0.8472 0.7310 0.6969 -0.1615 -0.1101 -0.0230 480  LEU A O   
3864  C CB  . LEU B 483  ? 0.7839 0.7548 0.6528 -0.2146 -0.1185 0.0038  480  LEU A CB  
3865  C CG  . LEU B 483  ? 0.7510 0.7389 0.6210 -0.2101 -0.1173 -0.0015 480  LEU A CG  
3866  C CD1 . LEU B 483  ? 0.7158 0.7344 0.6090 -0.1827 -0.1009 -0.0077 480  LEU A CD1 
3867  C CD2 . LEU B 483  ? 0.7371 0.7644 0.6071 -0.2367 -0.1255 0.0085  480  LEU A CD2 
3868  N N   . LEU B 484  ? 0.8766 0.7105 0.6927 -0.1946 -0.1316 -0.0131 481  LEU A N   
3869  C CA  . LEU B 484  ? 0.9138 0.6955 0.7022 -0.1853 -0.1392 -0.0225 481  LEU A CA  
3870  C C   . LEU B 484  ? 0.9330 0.6947 0.7246 -0.1539 -0.1291 -0.0318 481  LEU A C   
3871  O O   . LEU B 484  ? 0.9878 0.7261 0.7672 -0.1376 -0.1291 -0.0411 481  LEU A O   
3872  C CB  . LEU B 484  ? 0.9457 0.6761 0.6979 -0.2069 -0.1581 -0.0186 481  LEU A CB  
3873  C CG  . LEU B 484  ? 0.9606 0.7054 0.7035 -0.2418 -0.1712 -0.0088 481  LEU A CG  
3874  C CD1 . LEU B 484  ? 1.0389 0.7228 0.7400 -0.2628 -0.1914 -0.0055 481  LEU A CD1 
3875  C CD2 . LEU B 484  ? 0.9206 0.6877 0.6671 -0.2425 -0.1707 -0.0127 481  LEU A CD2 
3876  N N   . ASP B 485  ? 0.8988 0.6717 0.7067 -0.1453 -0.1206 -0.0291 482  ASP A N   
3877  C CA  . ASP B 485  ? 0.8961 0.6569 0.7091 -0.1173 -0.1108 -0.0362 482  ASP A CA  
3878  C C   . ASP B 485  ? 0.8713 0.6691 0.7093 -0.0989 -0.0961 -0.0409 482  ASP A C   
3879  O O   . ASP B 485  ? 0.8396 0.6357 0.6853 -0.0775 -0.0870 -0.0454 482  ASP A O   
3880  C CB  . ASP B 485  ? 0.9016 0.6622 0.7225 -0.1162 -0.1075 -0.0310 482  ASP A CB  
3881  C CG  . ASP B 485  ? 0.9898 0.6969 0.7795 -0.1201 -0.1201 -0.0308 482  ASP A CG  
3882  O OD1 . ASP B 485  ? 1.0546 0.7291 0.8164 -0.1352 -0.1344 -0.0306 482  ASP A OD1 
3883  O OD2 . ASP B 485  ? 1.0164 0.7124 0.8076 -0.1080 -0.1163 -0.0308 482  ASP A OD2 
3884  N N   . TRP B 486  ? 0.8563 0.6878 0.7059 -0.1070 -0.0940 -0.0395 483  TRP A N   
3885  C CA  . TRP B 486  ? 0.8074 0.6686 0.6759 -0.0896 -0.0816 -0.0443 483  TRP A CA  
3886  C C   . TRP B 486  ? 0.8446 0.6804 0.6993 -0.0731 -0.0819 -0.0538 483  TRP A C   
3887  O O   . TRP B 486  ? 0.8415 0.6907 0.7084 -0.0541 -0.0713 -0.0583 483  TRP A O   
3888  C CB  . TRP B 486  ? 0.7805 0.6841 0.6622 -0.1013 -0.0800 -0.0402 483  TRP A CB  
3889  C CG  . TRP B 486  ? 0.7736 0.7144 0.6741 -0.1095 -0.0754 -0.0317 483  TRP A CG  
3890  C CD1 . TRP B 486  ? 0.7692 0.7065 0.6745 -0.1115 -0.0741 -0.0269 483  TRP A CD1 
3891  C CD2 . TRP B 486  ? 0.7408 0.7292 0.6566 -0.1150 -0.0713 -0.0272 483  TRP A CD2 
3892  N NE1 . TRP B 486  ? 0.7207 0.7000 0.6432 -0.1180 -0.0696 -0.0198 483  TRP A NE1 
3893  C CE2 . TRP B 486  ? 0.7135 0.7252 0.6421 -0.1194 -0.0678 -0.0198 483  TRP A CE2 
3894  C CE3 . TRP B 486  ? 0.7286 0.7431 0.6475 -0.1152 -0.0703 -0.0287 483  TRP A CE3 
3895  C CZ2 . TRP B 486  ? 0.6994 0.7595 0.6424 -0.1226 -0.0634 -0.0141 483  TRP A CZ2 
3896  C CZ3 . TRP B 486  ? 0.7208 0.7840 0.6544 -0.1184 -0.0659 -0.0229 483  TRP A CZ3 
3897  C CH2 . TRP B 486  ? 0.7008 0.7865 0.6458 -0.1214 -0.0625 -0.0157 483  TRP A CH2 
3898  N N   . PHE B 487  ? 0.9087 0.7071 0.7361 -0.0803 -0.0946 -0.0566 484  PHE A N   
3899  C CA  . PHE B 487  ? 0.9846 0.7597 0.7961 -0.0652 -0.0962 -0.0658 484  PHE A CA  
3900  C C   . PHE B 487  ? 1.0938 0.8340 0.8908 -0.0450 -0.0960 -0.0710 484  PHE A C   
3901  O O   . PHE B 487  ? 1.0731 0.7876 0.8577 -0.0489 -0.1020 -0.0682 484  PHE A O   
3902  C CB  . PHE B 487  ? 1.0041 0.7548 0.7901 -0.0824 -0.1111 -0.0667 484  PHE A CB  
3903  C CG  . PHE B 487  ? 0.9723 0.7609 0.7712 -0.1032 -0.1123 -0.0607 484  PHE A CG  
3904  C CD1 . PHE B 487  ? 0.9091 0.7304 0.7230 -0.0958 -0.1045 -0.0637 484  PHE A CD1 
3905  C CD2 . PHE B 487  ? 0.9943 0.7883 0.7898 -0.1298 -0.1214 -0.0514 484  PHE A CD2 
3906  C CE1 . PHE B 487  ? 0.8827 0.7422 0.7078 -0.1128 -0.1055 -0.0582 484  PHE A CE1 
3907  C CE2 . PHE B 487  ? 0.9701 0.8054 0.7779 -0.1481 -0.1223 -0.0450 484  PHE A CE2 
3908  C CZ  . PHE B 487  ? 0.9131 0.7816 0.7357 -0.1386 -0.1143 -0.0487 484  PHE A CZ  
3909  N N   . ALA B 488  ? 1.2088 0.9500 1.0067 -0.0229 -0.0891 -0.0781 485  ALA A N   
3910  C CA  . ALA B 488  ? 1.3154 1.0312 1.1004 -0.0006 -0.0877 -0.0829 485  ALA A CA  
3911  C C   . ALA B 488  ? 1.4235 1.0851 1.1692 -0.0010 -0.1031 -0.0871 485  ALA A C   
3912  O O   . ALA B 488  ? 1.4177 1.0606 1.1444 -0.0100 -0.1129 -0.0901 485  ALA A O   
3913  C CB  . ALA B 488  ? 1.2917 1.0256 1.0859 0.0216  -0.0774 -0.0887 485  ALA A CB  
3914  N N   . VAL B 489  ? 1.5436 1.1781 1.2750 0.0094  -0.1060 -0.0873 486  VAL A N   
3915  C CA  . VAL B 489  ? 1.6347 1.2116 1.3242 0.0102  -0.1217 -0.0909 486  VAL A CA  
3916  C C   . VAL B 489  ? 1.6463 1.2019 1.3157 0.0418  -0.1207 -0.0998 486  VAL A C   
3917  O O   . VAL B 489  ? 1.6974 1.2057 1.3283 0.0477  -0.1335 -0.1059 486  VAL A O   
3918  C CB  . VAL B 489  ? 1.6741 1.2308 1.3557 0.0003  -0.1275 -0.0847 486  VAL A CB  
3919  C CG1 . VAL B 489  ? 1.7521 1.2445 1.3861 -0.0053 -0.1467 -0.0872 486  VAL A CG1 
3920  C CG2 . VAL B 489  ? 1.6404 1.2322 1.3497 -0.0267 -0.1246 -0.0750 486  VAL A CG2 
3921  N N   . ASP B 490  ? 1.5708 1.1615 1.2645 0.0622  -0.1059 -0.1004 487  ASP A N   
3922  C CA  . ASP B 490  ? 1.5809 1.1606 1.2584 0.0935  -0.1035 -0.1075 487  ASP A CA  
3923  C C   . ASP B 490  ? 1.5989 1.1677 1.2600 0.1009  -0.1073 -0.1150 487  ASP A C   
3924  O O   . ASP B 490  ? 1.5858 1.1797 1.2648 0.0878  -0.1037 -0.1143 487  ASP A O   
3925  C CB  . ASP B 490  ? 1.5319 1.1598 1.2422 0.1090  -0.0867 -0.1047 487  ASP A CB  
3926  N N   . GLU B 491  ? 1.6124 1.1431 1.2374 0.1236  -0.1149 -0.1226 488  GLU A N   
3927  C CA  . GLU B 491  ? 1.5851 1.1007 1.1895 0.1344  -0.1195 -0.1306 488  GLU A CA  
3928  C C   . GLU B 491  ? 1.5081 1.0692 1.1361 0.1554  -0.1044 -0.1327 488  GLU A C   
3929  O O   . GLU B 491  ? 1.5161 1.0677 1.1268 0.1699  -0.1068 -0.1397 488  GLU A O   
3930  C CB  . GLU B 491  ? 1.6263 1.0799 1.1783 0.1527  -0.1345 -0.1383 488  GLU A CB  
3931  N N   . SER B 492  ? 1.4303 1.0395 1.0954 0.1567  -0.0898 -0.1264 489  SER A N   
3932  C CA  . SER B 492  ? 1.3676 1.0213 1.0552 0.1728  -0.0760 -0.1267 489  SER A CA  
3933  C C   . SER B 492  ? 1.3431 1.0176 1.0465 0.1591  -0.0728 -0.1272 489  SER A C   
3934  O O   . SER B 492  ? 1.3384 1.0354 1.0476 0.1735  -0.0658 -0.1300 489  SER A O   
3935  C CB  . SER B 492  ? 1.2993 0.9953 1.0197 0.1739  -0.0630 -0.1188 489  SER A CB  
3936  O OG  . SER B 492  ? 1.2465 0.9535 0.9892 0.1474  -0.0618 -0.1121 489  SER A OG  
3937  N N   . ASN B 493  ? 1.3319 1.0015 1.0419 0.1320  -0.0779 -0.1243 490  ASN A N   
3938  C CA  . ASN B 493  ? 1.2982 0.9880 1.0220 0.1187  -0.0757 -0.1246 490  ASN A CA  
3939  C C   . ASN B 493  ? 1.3496 1.0011 1.0412 0.1152  -0.0893 -0.1315 490  ASN A C   
3940  O O   . ASN B 493  ? 1.3685 0.9735 1.0272 0.1150  -0.1026 -0.1345 490  ASN A O   
3941  C CB  . ASN B 493  ? 1.2453 0.9580 0.9948 0.0922  -0.0731 -0.1170 490  ASN A CB  
3942  C CG  . ASN B 493  ? 1.1991 0.9369 0.9728 0.0929  -0.0635 -0.1101 490  ASN A CG  
3943  O OD1 . ASN B 493  ? 1.1632 0.9371 0.9606 0.0999  -0.0513 -0.1075 490  ASN A OD1 
3944  N ND2 . ASN B 493  ? 1.1987 0.9161 0.9649 0.0845  -0.0696 -0.1069 490  ASN A ND2 
3945  N N   . GLU B 494  ? 1.3700 1.0395 1.0694 0.1122  -0.0866 -0.1338 491  GLU A N   
3946  C CA  . GLU B 494  ? 1.4022 1.0402 1.0736 0.1067  -0.0992 -0.1400 491  GLU A CA  
3947  C C   . GLU B 494  ? 1.4309 1.0615 1.1026 0.0746  -0.1085 -0.1351 491  GLU A C   
3948  O O   . GLU B 494  ? 1.3924 1.0525 1.0836 0.0589  -0.1053 -0.1321 491  GLU A O   
3949  C CB  . GLU B 494  ? 1.3354 0.9983 1.0157 0.1162  -0.0923 -0.1440 491  GLU A CB  
3950  C CG  . GLU B 494  ? 1.3008 0.9640 0.9710 0.1477  -0.0868 -0.1497 491  GLU A CG  
3951  C CD  . GLU B 494  ? 1.2667 0.9496 0.9412 0.1557  -0.0820 -0.1538 491  GLU A CD  
3952  O OE1 . GLU B 494  ? 1.2222 0.9414 0.9249 0.1435  -0.0738 -0.1496 491  GLU A OE1 
3953  O OE2 . GLU B 494  ? 1.2959 0.9568 0.9438 0.1753  -0.0868 -0.1614 491  GLU A OE2 
3954  N N   . VAL B 495  ? 1.5313 1.1227 1.1796 0.0651  -0.1207 -0.1337 492  VAL A N   
3955  C CA  . VAL B 495  ? 1.5186 1.1028 1.1650 0.0331  -0.1307 -0.1275 492  VAL A CA  
3956  C C   . VAL B 495  ? 1.5240 1.0790 1.1416 0.0202  -0.1454 -0.1316 492  VAL A C   
3957  O O   . VAL B 495  ? 1.5515 1.0710 1.1381 0.0366  -0.1525 -0.1401 492  VAL A O   
3958  C CB  . VAL B 495  ? 1.5544 1.1068 1.1854 0.0265  -0.1386 -0.1235 492  VAL A CB  
3959  C CG1 . VAL B 495  ? 1.5153 1.1030 1.1790 0.0346  -0.1239 -0.1181 492  VAL A CG1 
3960  C CG2 . VAL B 495  ? 1.6277 1.1214 1.2138 0.0455  -0.1502 -0.1313 492  VAL A CG2 
3961  N N   . ASP B 496  ? 1.4977 1.0697 1.1250 -0.0093 -0.1503 -0.1252 493  ASP A N   
3962  C CA  . ASP B 496  ? 1.5117 1.0603 1.1133 -0.0266 -0.1651 -0.1273 493  ASP A CA  
3963  C C   . ASP B 496  ? 1.5745 1.0545 1.1276 -0.0331 -0.1850 -0.1296 493  ASP A C   
3964  O O   . ASP B 496  ? 1.6017 1.0631 1.1484 -0.0392 -0.1888 -0.1249 493  ASP A O   
3965  C CB  . ASP B 496  ? 1.4591 1.0475 1.0832 -0.0578 -0.1657 -0.1181 493  ASP A CB  
3966  C CG  . ASP B 496  ? 1.4838 1.0597 1.0866 -0.0763 -0.1793 -0.1195 493  ASP A CG  
3967  O OD1 . ASP B 496  ? 1.4621 1.0659 1.0778 -0.0687 -0.1726 -0.1233 493  ASP A OD1 
3968  O OD2 . ASP B 496  ? 1.5343 1.0720 1.1065 -0.0994 -0.1973 -0.1164 493  ASP A OD2 
3969  N N   . PRO B 497  ? 1.6125 1.0511 1.1284 -0.0312 -0.1984 -0.1369 494  PRO A N   
3970  C CA  . PRO B 497  ? 1.6591 1.0249 1.1222 -0.0373 -0.2194 -0.1394 494  PRO A CA  
3971  C C   . PRO B 497  ? 1.6340 0.9888 1.0894 -0.0760 -0.2327 -0.1287 494  PRO A C   
3972  O O   . PRO B 497  ? 1.6387 0.9638 1.0795 -0.0794 -0.2385 -0.1252 494  PRO A O   
3973  C CB  . PRO B 497  ? 1.7207 1.0550 1.1507 -0.0325 -0.2305 -0.1483 494  PRO A CB  
3974  C CG  . PRO B 497  ? 1.6755 1.0593 1.1385 -0.0087 -0.2119 -0.1532 494  PRO A CG  
3975  C CD  . PRO B 497  ? 1.6084 1.0608 1.1256 -0.0195 -0.1949 -0.1440 494  PRO A CD  
3976  N N   . GLU B 498  ? 1.6055 0.9869 1.0709 -0.1055 -0.2376 -0.1229 495  GLU A N   
3977  C CA  . GLU B 498  ? 1.5952 0.9688 1.0508 -0.1451 -0.2519 -0.1117 495  GLU A CA  
3978  C C   . GLU B 498  ? 1.5294 0.9517 1.0255 -0.1543 -0.2394 -0.1012 495  GLU A C   
3979  O O   . GLU B 498  ? 1.5569 0.9567 1.0394 -0.1738 -0.2492 -0.0936 495  GLU A O   
3980  C CB  . GLU B 498  ? 1.5919 0.9868 1.0474 -0.1733 -0.2603 -0.1078 495  GLU A CB  
3981  N N   . PHE B 499  ? 1.4145 0.9012 0.9585 -0.1405 -0.2184 -0.1006 496  PHE A N   
3982  C CA  . PHE B 499  ? 1.3064 0.8419 0.8884 -0.1499 -0.2070 -0.0907 496  PHE A CA  
3983  C C   . PHE B 499  ? 1.2769 0.7860 0.8539 -0.1363 -0.2044 -0.0905 496  PHE A C   
3984  O O   . PHE B 499  ? 1.2856 0.7990 0.8673 -0.1555 -0.2077 -0.0812 496  PHE A O   
3985  C CB  . PHE B 499  ? 1.2080 0.8103 0.8361 -0.1350 -0.1861 -0.0912 496  PHE A CB  
3986  C CG  . PHE B 499  ? 1.1456 0.8011 0.8107 -0.1464 -0.1757 -0.0809 496  PHE A CG  
3987  C CD1 . PHE B 499  ? 1.1158 0.7796 0.7994 -0.1303 -0.1639 -0.0800 496  PHE A CD1 
3988  C CD2 . PHE B 499  ? 1.1326 0.8314 0.8130 -0.1724 -0.1778 -0.0720 496  PHE A CD2 
3989  C CE1 . PHE B 499  ? 1.0676 0.7779 0.7826 -0.1397 -0.1549 -0.0710 496  PHE A CE1 
3990  C CE2 . PHE B 499  ? 1.0855 0.8339 0.7977 -0.1804 -0.1683 -0.0627 496  PHE A CE2 
3991  C CZ  . PHE B 499  ? 1.0509 0.8030 0.7797 -0.1638 -0.1570 -0.0626 496  PHE A CZ  
3992  N N   . SER B 500  ? 1.2536 0.7383 0.8214 -0.1029 -0.1984 -0.1003 497  SER A N   
3993  C CA  . SER B 500  ? 1.2545 0.7178 0.8180 -0.0875 -0.1954 -0.1003 497  SER A CA  
3994  C C   . SER B 500  ? 1.3516 0.7504 0.8699 -0.1032 -0.2159 -0.0981 497  SER A C   
3995  O O   . SER B 500  ? 1.3242 0.7135 0.8429 -0.1047 -0.2158 -0.0932 497  SER A O   
3996  C CB  . SER B 500  ? 1.2520 0.7064 0.8130 -0.0481 -0.1855 -0.1108 497  SER A CB  
3997  O OG  . SER B 500  ? 1.2719 0.7102 0.8297 -0.0323 -0.1822 -0.1105 497  SER A OG  
3998  N N   . ALA B 501  ? 1.4421 0.7942 0.9192 -0.1153 -0.2342 -0.1013 498  ALA A N   
3999  C CA  . ALA B 501  ? 1.5059 0.7903 0.9342 -0.1321 -0.2558 -0.0989 498  ALA A CA  
4000  C C   . ALA B 501  ? 1.4961 0.7992 0.9337 -0.1739 -0.2634 -0.0846 498  ALA A C   
4001  O O   . ALA B 501  ? 1.5223 0.7960 0.9434 -0.1848 -0.2716 -0.0787 498  ALA A O   
4002  C CB  . ALA B 501  ? 1.5644 0.7888 0.9416 -0.1321 -0.2743 -0.1070 498  ALA A CB  
4003  N N   . ARG B 502  ? 1.4772 0.8312 0.9408 -0.1970 -0.2608 -0.0785 499  ARG A N   
4004  C CA  . ARG B 502  ? 1.4963 0.8775 0.9707 -0.2364 -0.2674 -0.0639 499  ARG A CA  
4005  C C   . ARG B 502  ? 1.4594 0.8901 0.9761 -0.2330 -0.2510 -0.0567 499  ARG A C   
4006  O O   . ARG B 502  ? 1.4785 0.9100 0.9930 -0.2587 -0.2581 -0.0455 499  ARG A O   
4007  C CB  . ARG B 502  ? 1.5143 0.9428 1.0058 -0.2588 -0.2681 -0.0594 499  ARG A CB  
4008  C CG  . ARG B 502  ? 1.6346 1.0182 1.0857 -0.2647 -0.2845 -0.0661 499  ARG A CG  
4009  C CD  . ARG B 502  ? 1.6806 1.1139 1.1478 -0.2929 -0.2872 -0.0589 499  ARG A CD  
4010  N NE  . ARG B 502  ? 1.7556 1.1987 1.2165 -0.3359 -0.3008 -0.0435 499  ARG A NE  
4011  C CZ  . ARG B 502  ? 1.7802 1.2785 1.2596 -0.3652 -0.3029 -0.0332 499  ARG A CZ  
4012  N NH1 . ARG B 502  ? 1.7581 1.3042 1.2629 -0.3549 -0.2921 -0.0375 499  ARG A NH1 
4013  N NH2 . ARG B 502  ? 1.8060 1.3176 1.2819 -0.4005 -0.3125 -0.0169 499  ARG A NH2 
4014  N N   . LEU B 503  ? 1.4217 0.8931 0.9754 -0.2027 -0.2298 -0.0624 500  LEU A N   
4015  C CA  . LEU B 503  ? 1.3550 0.8702 0.9465 -0.1977 -0.2146 -0.0563 500  LEU A CA  
4016  C C   . LEU B 503  ? 1.3643 0.8338 0.9358 -0.1880 -0.2186 -0.0566 500  LEU A C   
4017  O O   . LEU B 503  ? 1.3555 0.8366 0.9366 -0.2036 -0.2189 -0.0471 500  LEU A O   
4018  C CB  . LEU B 503  ? 1.2583 0.8232 0.8896 -0.1690 -0.1926 -0.0623 500  LEU A CB  
4019  C CG  . LEU B 503  ? 1.1896 0.7959 0.8579 -0.1597 -0.1764 -0.0575 500  LEU A CG  
4020  C CD1 . LEU B 503  ? 1.1739 0.8243 0.8631 -0.1887 -0.1768 -0.0447 500  LEU A CD1 
4021  C CD2 . LEU B 503  ? 1.1385 0.7838 0.8382 -0.1317 -0.1573 -0.0640 500  LEU A CD2 
4022  N N   . THR B 504  ? 1.3906 0.8093 0.9332 -0.1611 -0.2216 -0.0675 501  THR A N   
4023  C CA  . THR B 504  ? 1.4200 0.7941 0.9405 -0.1482 -0.2257 -0.0686 501  THR A CA  
4024  C C   . THR B 504  ? 1.4611 0.7856 0.9429 -0.1787 -0.2470 -0.0608 501  THR A C   
4025  O O   . THR B 504  ? 1.4765 0.7807 0.9504 -0.1789 -0.2494 -0.0566 501  THR A O   
4026  C CB  . THR B 504  ? 1.4698 0.8007 0.9629 -0.1120 -0.2260 -0.0819 501  THR A CB  
4027  O OG1 . THR B 504  ? 1.4319 0.8080 0.9565 -0.0896 -0.2091 -0.0883 501  THR A OG1 
4028  C CG2 . THR B 504  ? 1.5102 0.8172 0.9950 -0.0901 -0.2229 -0.0833 501  THR A CG2 
4029  N N   . GLY B 505  ? 1.4958 0.8002 0.9522 -0.2058 -0.2633 -0.0582 502  GLY A N   
4030  C CA  . GLY B 505  ? 1.5440 0.8016 0.9618 -0.2392 -0.2852 -0.0492 502  GLY A CA  
4031  C C   . GLY B 505  ? 1.4747 0.7806 0.9232 -0.2685 -0.2816 -0.0342 502  GLY A C   
4032  O O   . GLY B 505  ? 1.5000 0.7781 0.9327 -0.2786 -0.2890 -0.0277 502  GLY A O   
4033  N N   . ILE B 506  ? 1.3983 0.7779 0.8900 -0.2810 -0.2702 -0.0283 503  ILE A N   
4034  C CA  . ILE B 506  ? 1.3730 0.8053 0.8950 -0.3065 -0.2659 -0.0140 503  ILE A CA  
4035  C C   . ILE B 506  ? 1.3795 0.8423 0.9361 -0.2832 -0.2473 -0.0143 503  ILE A C   
4036  O O   . ILE B 506  ? 1.3653 0.8538 0.9372 -0.3005 -0.2460 -0.0031 503  ILE A O   
4037  C CB  . ILE B 506  ? 1.3046 0.8073 0.8589 -0.3249 -0.2602 -0.0078 503  ILE A CB  
4038  C CG1 . ILE B 506  ? 1.2414 0.7907 0.8339 -0.2922 -0.2387 -0.0174 503  ILE A CG1 
4039  C CG2 . ILE B 506  ? 1.3591 0.8332 0.8784 -0.3518 -0.2800 -0.0060 503  ILE A CG2 
4040  C CD1 . ILE B 506  ? 1.1947 0.8124 0.8174 -0.3056 -0.2323 -0.0124 503  ILE A CD1 
4041  N N   . LYS B 507  ? 1.4025 0.8647 0.9714 -0.2451 -0.2331 -0.0262 504  LYS A N   
4042  C CA  . LYS B 507  ? 1.3885 0.8747 0.9863 -0.2236 -0.2169 -0.0265 504  LYS A CA  
4043  C C   . LYS B 507  ? 1.4823 0.9138 1.0499 -0.2227 -0.2268 -0.0247 504  LYS A C   
4044  O O   . LYS B 507  ? 1.4299 0.8823 1.0168 -0.2254 -0.2203 -0.0179 504  LYS A O   
4045  C CB  . LYS B 507  ? 1.3405 0.8413 0.9572 -0.1855 -0.2005 -0.0385 504  LYS A CB  
4046  C CG  . LYS B 507  ? 1.3133 0.8362 0.9571 -0.1629 -0.1846 -0.0391 504  LYS A CG  
4047  C CD  . LYS B 507  ? 1.2926 0.8329 0.9542 -0.1288 -0.1693 -0.0496 504  LYS A CD  
4048  C CE  . LYS B 507  ? 1.2579 0.8545 0.9521 -0.1311 -0.1583 -0.0495 504  LYS A CE  
4049  N NZ  . LYS B 507  ? 1.2185 0.8349 0.9316 -0.1000 -0.1430 -0.0580 504  LYS A NZ  
4050  N N   . LEU B 508  ? 1.2241 1.2241 1.2241 0.0000  0.0000  0.0000  505  LEU A N   
4051  C CA  . LEU B 508  ? 1.2241 1.2241 1.2241 0.0000  0.0000  0.0000  505  LEU A CA  
4052  C C   . LEU B 508  ? 1.2241 1.2241 1.2241 0.0000  0.0000  0.0000  505  LEU A C   
4053  O O   . LEU B 508  ? 1.2241 1.2241 1.2241 0.0000  0.0000  0.0000  505  LEU A O   
4054  C CB  . LEU B 508  ? 1.2241 1.2241 1.2241 0.0000  0.0000  0.0000  505  LEU A CB  
4055  C CG  . LEU B 508  ? 1.2241 1.2241 1.2241 0.0000  0.0000  0.0000  505  LEU A CG  
4056  C CD1 . LEU B 508  ? 1.2241 1.2241 1.2241 0.0000  0.0000  0.0000  505  LEU A CD1 
4057  C CD2 . LEU B 508  ? 1.2241 1.2241 1.2241 0.0000  0.0000  0.0000  505  LEU A CD2 
4058  N N   . GLU B 509  ? 1.2059 1.2059 1.2059 0.0000  0.0000  0.0000  506  GLU A N   
4059  C CA  . GLU B 509  ? 1.2059 1.2059 1.2059 0.0000  0.0000  0.0000  506  GLU A CA  
4060  C C   . GLU B 509  ? 1.2059 1.2059 1.2059 0.0000  0.0000  0.0000  506  GLU A C   
4061  O O   . GLU B 509  ? 1.2059 1.2059 1.2059 0.0000  0.0000  0.0000  506  GLU A O   
4062  C CB  . GLU B 509  ? 1.2059 1.2059 1.2059 0.0000  0.0000  0.0000  506  GLU A CB  
4063  C CG  . GLU B 509  ? 1.2059 1.2059 1.2059 0.0000  0.0000  0.0000  506  GLU A CG  
4064  C CD  . GLU B 509  ? 1.2059 1.2059 1.2059 0.0000  0.0000  0.0000  506  GLU A CD  
4065  O OE1 . GLU B 509  ? 1.2059 1.2059 1.2059 0.0000  0.0000  0.0000  506  GLU A OE1 
4066  O OE2 . GLU B 509  ? 1.2059 1.2059 1.2059 0.0000  0.0000  0.0000  506  GLU A OE2 
4067  N N   . MET B 510  ? 1.1349 1.1349 1.1349 0.0000  0.0000  0.0000  507  MET A N   
4068  C CA  . MET B 510  ? 1.1349 1.1349 1.1349 0.0000  0.0000  0.0000  507  MET A CA  
4069  C C   . MET B 510  ? 1.1349 1.1349 1.1349 0.0000  0.0000  0.0000  507  MET A C   
4070  O O   . MET B 510  ? 1.1349 1.1349 1.1349 0.0000  0.0000  0.0000  507  MET A O   
4071  C CB  . MET B 510  ? 1.1349 1.1349 1.1349 0.0000  0.0000  0.0000  507  MET A CB  
4072  C CG  . MET B 510  ? 1.1349 1.1349 1.1349 0.0000  0.0000  0.0000  507  MET A CG  
4073  S SD  . MET B 510  ? 1.1349 1.1349 1.1349 0.0000  0.0000  0.0000  507  MET A SD  
4074  C CE  . MET B 510  ? 1.1349 1.1349 1.1349 0.0000  0.0000  0.0000  507  MET A CE  
4075  N N   . GLU B 511  ? 1.1296 1.1296 1.1296 0.0000  0.0000  0.0000  508  GLU A N   
4076  C CA  . GLU B 511  ? 1.1296 1.1296 1.1296 0.0000  0.0000  0.0000  508  GLU A CA  
4077  C C   . GLU B 511  ? 1.1296 1.1296 1.1296 0.0000  0.0000  0.0000  508  GLU A C   
4078  O O   . GLU B 511  ? 1.1296 1.1296 1.1296 0.0000  0.0000  0.0000  508  GLU A O   
4079  C CB  . GLU B 511  ? 1.1296 1.1296 1.1296 0.0000  0.0000  0.0000  508  GLU A CB  
4080  C CG  . GLU B 511  ? 1.1296 1.1296 1.1296 0.0000  0.0000  0.0000  508  GLU A CG  
4081  C CD  . GLU B 511  ? 1.1296 1.1296 1.1296 0.0000  0.0000  0.0000  508  GLU A CD  
4082  O OE1 . GLU B 511  ? 1.1296 1.1296 1.1296 0.0000  0.0000  0.0000  508  GLU A OE1 
4083  O OE2 . GLU B 511  ? 1.1296 1.1296 1.1296 0.0000  0.0000  0.0000  508  GLU A OE2 
4084  N N   . PRO B 512  ? 1.1164 1.1164 1.1164 0.0000  0.0000  0.0000  509  PRO A N   
4085  C CA  . PRO B 512  ? 1.1164 1.1164 1.1164 0.0000  0.0000  0.0000  509  PRO A CA  
4086  C C   . PRO B 512  ? 1.1164 1.1164 1.1164 0.0000  0.0000  0.0000  509  PRO A C   
4087  O O   . PRO B 512  ? 1.1164 1.1164 1.1164 0.0000  0.0000  0.0000  509  PRO A O   
4088  C CB  . PRO B 512  ? 1.1164 1.1164 1.1164 0.0000  0.0000  0.0000  509  PRO A CB  
4089  C CG  . PRO B 512  ? 1.1164 1.1164 1.1164 0.0000  0.0000  0.0000  509  PRO A CG  
4090  C CD  . PRO B 512  ? 1.1164 1.1164 1.1164 0.0000  0.0000  0.0000  509  PRO A CD  
4091  N N   . SER B 513  ? 1.0548 1.0548 1.0548 0.0000  0.0000  0.0000  510  SER A N   
4092  C CA  . SER B 513  ? 1.0548 1.0548 1.0548 0.0000  0.0000  0.0000  510  SER A CA  
4093  C C   . SER B 513  ? 1.0548 1.0548 1.0548 0.0000  0.0000  0.0000  510  SER A C   
4094  O O   . SER B 513  ? 1.0548 1.0548 1.0548 0.0000  0.0000  0.0000  510  SER A O   
4095  C CB  . SER B 513  ? 1.0548 1.0548 1.0548 0.0000  0.0000  0.0000  510  SER A CB  
4096  O OG  . SER B 513  ? 1.0548 1.0548 1.0548 0.0000  0.0000  0.0000  510  SER A OG  
4097  N N   . LEU B 514  ? 1.0481 1.0481 1.0481 0.0000  0.0000  0.0000  511  LEU A N   
4098  C CA  . LEU B 514  ? 1.0481 1.0481 1.0481 0.0000  0.0000  0.0000  511  LEU A CA  
4099  C C   . LEU B 514  ? 1.0481 1.0481 1.0481 0.0000  0.0000  0.0000  511  LEU A C   
4100  O O   . LEU B 514  ? 1.0481 1.0481 1.0481 0.0000  0.0000  0.0000  511  LEU A O   
4101  C CB  . LEU B 514  ? 1.0481 1.0481 1.0481 0.0000  0.0000  0.0000  511  LEU A CB  
4102  C CG  . LEU B 514  ? 1.0481 1.0481 1.0481 0.0000  0.0000  0.0000  511  LEU A CG  
4103  C CD1 . LEU B 514  ? 1.0481 1.0481 1.0481 0.0000  0.0000  0.0000  511  LEU A CD1 
4104  C CD2 . LEU B 514  ? 1.0481 1.0481 1.0481 0.0000  0.0000  0.0000  511  LEU A CD2 
4105  N N   . SER B 515  ? 1.0248 1.0248 1.0248 0.0000  0.0000  0.0000  512  SER A N   
4106  C CA  . SER B 515  ? 1.0248 1.0248 1.0248 0.0000  0.0000  0.0000  512  SER A CA  
4107  C C   . SER B 515  ? 1.0248 1.0248 1.0248 0.0000  0.0000  0.0000  512  SER A C   
4108  O O   . SER B 515  ? 1.0248 1.0248 1.0248 0.0000  0.0000  0.0000  512  SER A O   
4109  C CB  . SER B 515  ? 1.0248 1.0248 1.0248 0.0000  0.0000  0.0000  512  SER A CB  
4110  O OG  . SER B 515  ? 1.0248 1.0248 1.0248 0.0000  0.0000  0.0000  512  SER A OG  
4111  N N   . PHE B 516  ? 0.9642 0.9642 0.9642 0.0000  0.0000  0.0000  513  PHE A N   
4112  C CA  . PHE B 516  ? 0.9642 0.9642 0.9642 0.0000  0.0000  0.0000  513  PHE A CA  
4113  C C   . PHE B 516  ? 0.9642 0.9642 0.9642 0.0000  0.0000  0.0000  513  PHE A C   
4114  O O   . PHE B 516  ? 0.9642 0.9642 0.9642 0.0000  0.0000  0.0000  513  PHE A O   
4115  C CB  . PHE B 516  ? 0.9642 0.9642 0.9642 0.0000  0.0000  0.0000  513  PHE A CB  
4116  C CG  . PHE B 516  ? 0.9642 0.9642 0.9642 0.0000  0.0000  0.0000  513  PHE A CG  
4117  C CD1 . PHE B 516  ? 0.9642 0.9642 0.9642 0.0000  0.0000  0.0000  513  PHE A CD1 
4118  C CD2 . PHE B 516  ? 0.9642 0.9642 0.9642 0.0000  0.0000  0.0000  513  PHE A CD2 
4119  C CE1 . PHE B 516  ? 0.9642 0.9642 0.9642 0.0000  0.0000  0.0000  513  PHE A CE1 
4120  C CE2 . PHE B 516  ? 0.9642 0.9642 0.9642 0.0000  0.0000  0.0000  513  PHE A CE2 
4121  C CZ  . PHE B 516  ? 0.9642 0.9642 0.9642 0.0000  0.0000  0.0000  513  PHE A CZ  
4122  N N   . TYR B 517  ? 0.9656 0.9656 0.9656 0.0000  0.0000  0.0000  514  TYR A N   
4123  C CA  . TYR B 517  ? 0.9656 0.9656 0.9656 0.0000  0.0000  0.0000  514  TYR A CA  
4124  C C   . TYR B 517  ? 0.9656 0.9656 0.9656 0.0000  0.0000  0.0000  514  TYR A C   
4125  O O   . TYR B 517  ? 0.9656 0.9656 0.9656 0.0000  0.0000  0.0000  514  TYR A O   
4126  C CB  . TYR B 517  ? 0.9656 0.9656 0.9656 0.0000  0.0000  0.0000  514  TYR A CB  
4127  C CG  . TYR B 517  ? 0.9656 0.9656 0.9656 0.0000  0.0000  0.0000  514  TYR A CG  
4128  C CD1 . TYR B 517  ? 0.9656 0.9656 0.9656 0.0000  0.0000  0.0000  514  TYR A CD1 
4129  C CD2 . TYR B 517  ? 0.9656 0.9656 0.9656 0.0000  0.0000  0.0000  514  TYR A CD2 
4130  C CE1 . TYR B 517  ? 0.9656 0.9656 0.9656 0.0000  0.0000  0.0000  514  TYR A CE1 
4131  C CE2 . TYR B 517  ? 0.9656 0.9656 0.9656 0.0000  0.0000  0.0000  514  TYR A CE2 
4132  C CZ  . TYR B 517  ? 0.9656 0.9656 0.9656 0.0000  0.0000  0.0000  514  TYR A CZ  
4133  O OH  . TYR B 517  ? 0.9656 0.9656 0.9656 0.0000  0.0000  0.0000  514  TYR A OH  
4134  N N   . ASN B 518  ? 0.8857 0.8857 0.8857 0.0000  0.0000  0.0000  515  ASN A N   
4135  C CA  . ASN B 518  ? 0.8857 0.8857 0.8857 0.0000  0.0000  0.0000  515  ASN A CA  
4136  C C   . ASN B 518  ? 0.8857 0.8857 0.8857 0.0000  0.0000  0.0000  515  ASN A C   
4137  O O   . ASN B 518  ? 0.8857 0.8857 0.8857 0.0000  0.0000  0.0000  515  ASN A O   
4138  C CB  . ASN B 518  ? 0.8857 0.8857 0.8857 0.0000  0.0000  0.0000  515  ASN A CB  
4139  C CG  . ASN B 518  ? 0.8857 0.8857 0.8857 0.0000  0.0000  0.0000  515  ASN A CG  
4140  O OD1 . ASN B 518  ? 0.8857 0.8857 0.8857 0.0000  0.0000  0.0000  515  ASN A OD1 
4141  N ND2 . ASN B 518  ? 0.8857 0.8857 0.8857 0.0000  0.0000  0.0000  515  ASN A ND2 
4142  N N   . LYS B 519  ? 0.8271 0.8271 0.8271 0.0000  0.0000  0.0000  516  LYS A N   
4143  C CA  . LYS B 519  ? 0.8271 0.8271 0.8271 0.0000  0.0000  0.0000  516  LYS A CA  
4144  C C   . LYS B 519  ? 0.8271 0.8271 0.8271 0.0000  0.0000  0.0000  516  LYS A C   
4145  O O   . LYS B 519  ? 0.8271 0.8271 0.8271 0.0000  0.0000  0.0000  516  LYS A O   
4146  C CB  . LYS B 519  ? 0.8271 0.8271 0.8271 0.0000  0.0000  0.0000  516  LYS A CB  
4147  C CG  . LYS B 519  ? 0.8271 0.8271 0.8271 0.0000  0.0000  0.0000  516  LYS A CG  
4148  C CD  . LYS B 519  ? 0.8271 0.8271 0.8271 0.0000  0.0000  0.0000  516  LYS A CD  
4149  C CE  . LYS B 519  ? 0.8271 0.8271 0.8271 0.0000  0.0000  0.0000  516  LYS A CE  
4150  N NZ  . LYS B 519  ? 0.8271 0.8271 0.8271 0.0000  0.0000  0.0000  516  LYS A NZ  
4151  N N   . ALA B 520  ? 0.8019 0.8019 0.8019 0.0000  0.0000  0.0000  517  ALA A N   
4152  C CA  . ALA B 520  ? 0.8019 0.8019 0.8019 0.0000  0.0000  0.0000  517  ALA A CA  
4153  C C   . ALA B 520  ? 0.8019 0.8019 0.8019 0.0000  0.0000  0.0000  517  ALA A C   
4154  O O   . ALA B 520  ? 0.8019 0.8019 0.8019 0.0000  0.0000  0.0000  517  ALA A O   
4155  C CB  . ALA B 520  ? 0.8019 0.8019 0.8019 0.0000  0.0000  0.0000  517  ALA A CB  
4156  N N   . ARG B 521  ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  518  ARG A N   
4157  C CA  . ARG B 521  ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  518  ARG A CA  
4158  C C   . ARG B 521  ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  518  ARG A C   
4159  O O   . ARG B 521  ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  518  ARG A O   
4160  C CB  . ARG B 521  ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  518  ARG A CB  
4161  C CG  . ARG B 521  ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  518  ARG A CG  
4162  C CD  . ARG B 521  ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  518  ARG A CD  
4163  N NE  . ARG B 521  ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  518  ARG A NE  
4164  C CZ  . ARG B 521  ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  518  ARG A CZ  
4165  N NH1 . ARG B 521  ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  518  ARG A NH1 
4166  N NH2 . ARG B 521  ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  518  ARG A NH2 
4167  N N   . ASN B 522  ? 0.7227 0.7227 0.7227 0.0000  0.0000  0.0000  519  ASN A N   
4168  C CA  . ASN B 522  ? 0.7227 0.7227 0.7227 0.0000  0.0000  0.0000  519  ASN A CA  
4169  C C   . ASN B 522  ? 0.7227 0.7227 0.7227 0.0000  0.0000  0.0000  519  ASN A C   
4170  O O   . ASN B 522  ? 0.7227 0.7227 0.7227 0.0000  0.0000  0.0000  519  ASN A O   
4171  C CB  . ASN B 522  ? 0.7227 0.7227 0.7227 0.0000  0.0000  0.0000  519  ASN A CB  
4172  C CG  . ASN B 522  ? 0.7227 0.7227 0.7227 0.0000  0.0000  0.0000  519  ASN A CG  
4173  O OD1 . ASN B 522  ? 0.7227 0.7227 0.7227 0.0000  0.0000  0.0000  519  ASN A OD1 
4174  N ND2 . ASN B 522  ? 0.7227 0.7227 0.7227 0.0000  0.0000  0.0000  519  ASN A ND2 
4175  N N   . TYR B 523  ? 0.7468 0.7468 0.7468 0.0000  0.0000  0.0000  520  TYR A N   
4176  C CA  . TYR B 523  ? 0.7468 0.7468 0.7468 0.0000  0.0000  0.0000  520  TYR A CA  
4177  C C   . TYR B 523  ? 0.7468 0.7468 0.7468 0.0000  0.0000  0.0000  520  TYR A C   
4178  O O   . TYR B 523  ? 0.7468 0.7468 0.7468 0.0000  0.0000  0.0000  520  TYR A O   
4179  C CB  . TYR B 523  ? 0.7468 0.7468 0.7468 0.0000  0.0000  0.0000  520  TYR A CB  
4180  C CG  . TYR B 523  ? 0.7468 0.7468 0.7468 0.0000  0.0000  0.0000  520  TYR A CG  
4181  C CD1 . TYR B 523  ? 0.7468 0.7468 0.7468 0.0000  0.0000  0.0000  520  TYR A CD1 
4182  C CD2 . TYR B 523  ? 0.7468 0.7468 0.7468 0.0000  0.0000  0.0000  520  TYR A CD2 
4183  C CE1 . TYR B 523  ? 0.7468 0.7468 0.7468 0.0000  0.0000  0.0000  520  TYR A CE1 
4184  C CE2 . TYR B 523  ? 0.7468 0.7468 0.7468 0.0000  0.0000  0.0000  520  TYR A CE2 
4185  C CZ  . TYR B 523  ? 0.7468 0.7468 0.7468 0.0000  0.0000  0.0000  520  TYR A CZ  
4186  O OH  . TYR B 523  ? 0.7468 0.7468 0.7468 0.0000  0.0000  0.0000  520  TYR A OH  
4187  N N   . ALA B 524  ? 0.7056 0.7056 0.7056 0.0000  0.0000  0.0000  521  ALA A N   
4188  C CA  . ALA B 524  ? 0.7056 0.7056 0.7056 0.0000  0.0000  0.0000  521  ALA A CA  
4189  C C   . ALA B 524  ? 0.7056 0.7056 0.7056 0.0000  0.0000  0.0000  521  ALA A C   
4190  O O   . ALA B 524  ? 0.7056 0.7056 0.7056 0.0000  0.0000  0.0000  521  ALA A O   
4191  C CB  . ALA B 524  ? 0.7056 0.7056 0.7056 0.0000  0.0000  0.0000  521  ALA A CB  
4192  N N   . THR B 525  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  522  THR A N   
4193  C CA  . THR B 525  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  522  THR A CA  
4194  C C   . THR B 525  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  522  THR A C   
4195  O O   . THR B 525  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  522  THR A O   
4196  C CB  . THR B 525  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  522  THR A CB  
4197  O OG1 . THR B 525  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  522  THR A OG1 
4198  C CG2 . THR B 525  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  522  THR A CG2 
4199  N N   . LYS B 526  ? 0.6555 0.6555 0.6555 0.0000  0.0000  0.0000  523  LYS A N   
4200  C CA  . LYS B 526  ? 0.6555 0.6555 0.6555 0.0000  0.0000  0.0000  523  LYS A CA  
4201  C C   . LYS B 526  ? 0.6555 0.6555 0.6555 0.0000  0.0000  0.0000  523  LYS A C   
4202  O O   . LYS B 526  ? 0.6555 0.6555 0.6555 0.0000  0.0000  0.0000  523  LYS A O   
4203  C CB  . LYS B 526  ? 0.6555 0.6555 0.6555 0.0000  0.0000  0.0000  523  LYS A CB  
4204  C CG  . LYS B 526  ? 0.6555 0.6555 0.6555 0.0000  0.0000  0.0000  523  LYS A CG  
4205  C CD  . LYS B 526  ? 0.6555 0.6555 0.6555 0.0000  0.0000  0.0000  523  LYS A CD  
4206  C CE  . LYS B 526  ? 0.6555 0.6555 0.6555 0.0000  0.0000  0.0000  523  LYS A CE  
4207  N NZ  . LYS B 526  ? 0.6555 0.6555 0.6555 0.0000  0.0000  0.0000  523  LYS A NZ  
4208  N N   . LYS B 527  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  524  LYS A N   
4209  C CA  . LYS B 527  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  524  LYS A CA  
4210  C C   . LYS B 527  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  524  LYS A C   
4211  O O   . LYS B 527  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  524  LYS A O   
4217  N N   . PRO B 528  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  525  PRO A N   
4218  C CA  . PRO B 528  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  525  PRO A CA  
4219  C C   . PRO B 528  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  525  PRO A C   
4220  O O   . PRO B 528  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  525  PRO A O   
4221  C CB  . PRO B 528  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  525  PRO A CB  
4222  C CG  . PRO B 528  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  525  PRO A CG  
4223  C CD  . PRO B 528  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  525  PRO A CD  
4224  N N   . TYR B 529  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  526  TYR A N   
4225  C CA  . TYR B 529  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  526  TYR A CA  
4226  C C   . TYR B 529  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  526  TYR A C   
4227  O O   . TYR B 529  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  526  TYR A O   
4228  C CB  . TYR B 529  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  526  TYR A CB  
4229  C CG  . TYR B 529  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  526  TYR A CG  
4230  C CD1 . TYR B 529  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  526  TYR A CD1 
4231  C CD2 . TYR B 529  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  526  TYR A CD2 
4232  C CE1 . TYR B 529  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  526  TYR A CE1 
4233  C CE2 . TYR B 529  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  526  TYR A CE2 
4234  C CZ  . TYR B 529  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  526  TYR A CZ  
4235  O OH  . TYR B 529  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  526  TYR A OH  
4236  N N   . SER B 530  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  527  SER A N   
4237  C CA  . SER B 530  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  527  SER A CA  
4238  C C   . SER B 530  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  527  SER A C   
4239  O O   . SER B 530  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  527  SER A O   
4240  C CB  . SER B 530  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  527  SER A CB  
4241  O OG  . SER B 530  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  527  SER A OG  
4242  N N   . VAL B 531  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  528  VAL A N   
4243  C CA  . VAL B 531  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  528  VAL A CA  
4244  C C   . VAL B 531  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  528  VAL A C   
4245  O O   . VAL B 531  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  528  VAL A O   
4246  C CB  . VAL B 531  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  528  VAL A CB  
4247  C CG1 . VAL B 531  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  528  VAL A CG1 
4248  C CG2 . VAL B 531  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  528  VAL A CG2 
4249  N N   . GLU B 532  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  529  GLU A N   
4250  C CA  . GLU B 532  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  529  GLU A CA  
4251  C C   . GLU B 532  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  529  GLU A C   
4252  O O   . GLU B 532  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  529  GLU A O   
4253  C CB  . GLU B 532  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  529  GLU A CB  
4254  C CG  . GLU B 532  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  529  GLU A CG  
4255  C CD  . GLU B 532  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  529  GLU A CD  
4256  O OE1 . GLU B 532  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  529  GLU A OE1 
4257  O OE2 . GLU B 532  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  529  GLU A OE2 
4258  N N   . LYS B 533  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  530  LYS A N   
4259  C CA  . LYS B 533  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  530  LYS A CA  
4260  C C   . LYS B 533  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  530  LYS A C   
4261  O O   . LYS B 533  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  530  LYS A O   
4262  C CB  . LYS B 533  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  530  LYS A CB  
4263  C CG  . LYS B 533  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  530  LYS A CG  
4264  C CD  . LYS B 533  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  530  LYS A CD  
4265  C CE  . LYS B 533  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  530  LYS A CE  
4266  N NZ  . LYS B 533  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  530  LYS A NZ  
4267  N N   . PHE B 534  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  531  PHE A N   
4268  C CA  . PHE B 534  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  531  PHE A CA  
4269  C C   . PHE B 534  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  531  PHE A C   
4270  O O   . PHE B 534  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  531  PHE A O   
4271  C CB  . PHE B 534  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  531  PHE A CB  
4272  C CG  . PHE B 534  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  531  PHE A CG  
4273  C CD1 . PHE B 534  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  531  PHE A CD1 
4274  C CD2 . PHE B 534  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  531  PHE A CD2 
4275  C CE1 . PHE B 534  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  531  PHE A CE1 
4276  C CE2 . PHE B 534  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  531  PHE A CE2 
4277  C CZ  . PHE B 534  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  531  PHE A CZ  
4278  N N   . LYS B 535  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  532  LYS A N   
4279  C CA  . LYS B 535  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  532  LYS A CA  
4280  C C   . LYS B 535  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  532  LYS A C   
4281  O O   . LYS B 535  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  532  LYS A O   
4282  C CB  . LYS B 535  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  532  LYS A CB  
4283  C CG  . LYS B 535  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  532  LYS A CG  
4284  C CD  . LYS B 535  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  532  LYS A CD  
4285  C CE  . LYS B 535  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  532  LYS A CE  
4286  N NZ  . LYS B 535  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  532  LYS A NZ  
4287  N N   . LEU B 536  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  533  LEU A N   
4288  C CA  . LEU B 536  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  533  LEU A CA  
4289  C C   . LEU B 536  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  533  LEU A C   
4290  O O   . LEU B 536  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  533  LEU A O   
4291  C CB  . LEU B 536  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  533  LEU A CB  
4292  C CG  . LEU B 536  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  533  LEU A CG  
4293  C CD1 . LEU B 536  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  533  LEU A CD1 
4294  C CD2 . LEU B 536  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  533  LEU A CD2 
4295  N N   . ASN B 537  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  534  ASN A N   
4296  C CA  . ASN B 537  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  534  ASN A CA  
4297  C C   . ASN B 537  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  534  ASN A C   
4298  O O   . ASN B 537  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  534  ASN A O   
4299  C CB  . ASN B 537  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  534  ASN A CB  
4300  C CG  . ASN B 537  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  534  ASN A CG  
4301  O OD1 . ASN B 537  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  534  ASN A OD1 
4302  N ND2 . ASN B 537  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  534  ASN A ND2 
4303  N N   . PHE B 538  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  535  PHE A N   
4304  C CA  . PHE B 538  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  535  PHE A CA  
4305  C C   . PHE B 538  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  535  PHE A C   
4306  O O   . PHE B 538  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  535  PHE A O   
4307  C CB  . PHE B 538  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  535  PHE A CB  
4308  C CG  . PHE B 538  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  535  PHE A CG  
4309  C CD1 . PHE B 538  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  535  PHE A CD1 
4310  C CD2 . PHE B 538  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  535  PHE A CD2 
4311  C CE1 . PHE B 538  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  535  PHE A CE1 
4312  C CE2 . PHE B 538  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  535  PHE A CE2 
4313  C CZ  . PHE B 538  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  535  PHE A CZ  
4314  N N   . GLN B 539  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  536  GLN A N   
4315  C CA  . GLN B 539  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  536  GLN A CA  
4316  C C   . GLN B 539  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  536  GLN A C   
4317  O O   . GLN B 539  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  536  GLN A O   
4318  C CB  . GLN B 539  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  536  GLN A CB  
4319  C CG  . GLN B 539  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  536  GLN A CG  
4320  C CD  . GLN B 539  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  536  GLN A CD  
4321  O OE1 . GLN B 539  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  536  GLN A OE1 
4322  N NE2 . GLN B 539  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  536  GLN A NE2 
4323  N N   . MET B 540  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  537  MET A N   
4324  C CA  . MET B 540  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  537  MET A CA  
4325  C C   . MET B 540  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  537  MET A C   
4326  O O   . MET B 540  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  537  MET A O   
4327  C CB  . MET B 540  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  537  MET A CB  
4328  C CG  . MET B 540  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  537  MET A CG  
4329  S SD  . MET B 540  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  537  MET A SD  
4330  C CE  . MET B 540  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  537  MET A CE  
4331  N N   . PRO B 541  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  538  PRO A N   
4332  C CA  . PRO B 541  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  538  PRO A CA  
4333  C C   . PRO B 541  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  538  PRO A C   
4334  O O   . PRO B 541  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  538  PRO A O   
4335  C CB  . PRO B 541  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  538  PRO A CB  
4336  C CG  . PRO B 541  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  538  PRO A CG  
4337  C CD  . PRO B 541  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  538  PRO A CD  
4338  N N   . THR B 542  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  539  THR A N   
4339  C CA  . THR B 542  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  539  THR A CA  
4340  C C   . THR B 542  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  539  THR A C   
4341  O O   . THR B 542  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  539  THR A O   
4342  C CB  . THR B 542  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  539  THR A CB  
4343  O OG1 . THR B 542  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  539  THR A OG1 
4344  C CG2 . THR B 542  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  539  THR A CG2 
4345  N N   . LEU B 543  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  540  LEU A N   
4346  C CA  . LEU B 543  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  540  LEU A CA  
4347  C C   . LEU B 543  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  540  LEU A C   
4348  O O   . LEU B 543  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  540  LEU A O   
4349  C CB  . LEU B 543  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  540  LEU A CB  
4350  C CG  . LEU B 543  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  540  LEU A CG  
4351  C CD1 . LEU B 543  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  540  LEU A CD1 
4352  C CD2 . LEU B 543  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  540  LEU A CD2 
4353  N N   . ALA B 544  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  541  ALA A N   
4354  C CA  . ALA B 544  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  541  ALA A CA  
4355  C C   . ALA B 544  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  541  ALA A C   
4356  O O   . ALA B 544  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  541  ALA A O   
4357  C CB  . ALA B 544  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  541  ALA A CB  
4358  N N   . SER B 545  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  542  SER A N   
4359  C CA  . SER B 545  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  542  SER A CA  
4360  C C   . SER B 545  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  542  SER A C   
4361  O O   . SER B 545  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  542  SER A O   
4362  C CB  . SER B 545  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  542  SER A CB  
4363  O OG  . SER B 545  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  542  SER A OG  
4364  N N   . GLY B 546  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  543  GLY A N   
4365  C CA  . GLY B 546  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  543  GLY A CA  
4366  C C   . GLY B 546  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  543  GLY A C   
4367  O O   . GLY B 546  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  543  GLY A O   
4368  N N   . TRP B 547  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  544  TRP A N   
4369  C CA  . TRP B 547  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  544  TRP A CA  
4370  C C   . TRP B 547  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  544  TRP A C   
4371  O O   . TRP B 547  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  544  TRP A O   
4372  C CB  . TRP B 547  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  544  TRP A CB  
4373  C CG  . TRP B 547  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  544  TRP A CG  
4374  C CD1 . TRP B 547  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  544  TRP A CD1 
4375  C CD2 . TRP B 547  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  544  TRP A CD2 
4376  N NE1 . TRP B 547  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  544  TRP A NE1 
4377  C CE2 . TRP B 547  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  544  TRP A CE2 
4378  C CE3 . TRP B 547  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  544  TRP A CE3 
4379  C CZ2 . TRP B 547  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  544  TRP A CZ2 
4380  C CZ3 . TRP B 547  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  544  TRP A CZ3 
4381  C CH2 . TRP B 547  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  544  TRP A CH2 
4382  N N   . ASP B 548  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  545  ASP A N   
4383  C CA  . ASP B 548  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  545  ASP A CA  
4384  C C   . ASP B 548  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  545  ASP A C   
4385  O O   . ASP B 548  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  545  ASP A O   
4386  C CB  . ASP B 548  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  545  ASP A CB  
4387  C CG  . ASP B 548  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  545  ASP A CG  
4388  O OD1 . ASP B 548  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  545  ASP A OD1 
4389  O OD2 . ASP B 548  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  545  ASP A OD2 
4390  N N   . VAL B 549  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  546  VAL A N   
4391  C CA  . VAL B 549  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  546  VAL A CA  
4392  C C   . VAL B 549  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  546  VAL A C   
4393  O O   . VAL B 549  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  546  VAL A O   
4394  C CB  . VAL B 549  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  546  VAL A CB  
4395  C CG1 . VAL B 549  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  546  VAL A CG1 
4396  C CG2 . VAL B 549  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  546  VAL A CG2 
4397  N N   . ASN B 550  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  547  ASN A N   
4398  C CA  . ASN B 550  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  547  ASN A CA  
4399  C C   . ASN B 550  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  547  ASN A C   
4400  O O   . ASN B 550  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  547  ASN A O   
4401  C CB  . ASN B 550  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  547  ASN A CB  
4402  C CG  . ASN B 550  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  547  ASN A CG  
4403  O OD1 . ASN B 550  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  547  ASN A OD1 
4404  N ND2 . ASN B 550  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  547  ASN A ND2 
4405  N N   . LYS B 551  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  548  LYS A N   
4406  C CA  . LYS B 551  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  548  LYS A CA  
4407  C C   . LYS B 551  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  548  LYS A C   
4408  O O   . LYS B 551  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  548  LYS A O   
4409  C CB  . LYS B 551  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  548  LYS A CB  
4410  C CG  . LYS B 551  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  548  LYS A CG  
4411  C CD  . LYS B 551  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  548  LYS A CD  
4412  C CE  . LYS B 551  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  548  LYS A CE  
4413  N NZ  . LYS B 551  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  548  LYS A NZ  
4414  N N   . GLU B 552  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  549  GLU A N   
4415  C CA  . GLU B 552  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  549  GLU A CA  
4416  C C   . GLU B 552  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  549  GLU A C   
4417  O O   . GLU B 552  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  549  GLU A O   
4418  C CB  . GLU B 552  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  549  GLU A CB  
4419  C CG  . GLU B 552  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  549  GLU A CG  
4420  C CD  . GLU B 552  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  549  GLU A CD  
4421  O OE1 . GLU B 552  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  549  GLU A OE1 
4422  O OE2 . GLU B 552  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  549  GLU A OE2 
4423  N N   . LYS B 553  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  550  LYS A N   
4424  C CA  . LYS B 553  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  550  LYS A CA  
4425  C C   . LYS B 553  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  550  LYS A C   
4426  O O   . LYS B 553  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  550  LYS A O   
4427  C CB  . LYS B 553  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  550  LYS A CB  
4428  C CG  . LYS B 553  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  550  LYS A CG  
4429  C CD  . LYS B 553  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  550  LYS A CD  
4430  C CE  . LYS B 553  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  550  LYS A CE  
4431  N NZ  . LYS B 553  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  550  LYS A NZ  
4432  N N   . CYS B 554  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  551  CYS A N   
4433  C CA  . CYS B 554  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  551  CYS A CA  
4434  C C   . CYS B 554  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  551  CYS A C   
4435  O O   . CYS B 554  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  551  CYS A O   
4438  N N   . ASN B 555  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  552  ASN A N   
4439  C CA  . ASN B 555  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  552  ASN A CA  
4440  C C   . ASN B 555  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  552  ASN A C   
4441  O O   . ASN B 555  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  552  ASN A O   
4442  C CB  . ASN B 555  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  552  ASN A CB  
4443  C CG  . ASN B 555  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  552  ASN A CG  
4444  O OD1 . ASN B 555  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  552  ASN A OD1 
4445  N ND2 . ASN B 555  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  552  ASN A ND2 
4446  N N   . GLY B 556  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  553  GLY A N   
4447  C CA  . GLY B 556  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  553  GLY A CA  
4448  C C   . GLY B 556  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  553  GLY A C   
4449  O O   . GLY B 556  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  553  GLY A O   
4450  N N   . ALA B 557  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  554  ALA A N   
4451  C CA  . ALA B 557  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  554  ALA A CA  
4452  C C   . ALA B 557  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  554  ALA A C   
4453  O O   . ALA B 557  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  554  ALA A O   
4454  C CB  . ALA B 557  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  554  ALA A CB  
4455  N N   . ILE B 558  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  555  ILE A N   
4456  C CA  . ILE B 558  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  555  ILE A CA  
4457  C C   . ILE B 558  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  555  ILE A C   
4458  O O   . ILE B 558  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  555  ILE A O   
4459  C CB  . ILE B 558  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  555  ILE A CB  
4460  C CG1 . ILE B 558  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  555  ILE A CG1 
4461  C CG2 . ILE B 558  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  555  ILE A CG2 
4462  C CD1 . ILE B 558  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  555  ILE A CD1 
4463  N N   . LEU B 559  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  556  LEU A N   
4464  C CA  . LEU B 559  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  556  LEU A CA  
4465  C C   . LEU B 559  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  556  LEU A C   
4466  O O   . LEU B 559  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  556  LEU A O   
4467  C CB  . LEU B 559  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  556  LEU A CB  
4468  C CG  . LEU B 559  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  556  LEU A CG  
4469  C CD1 . LEU B 559  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  556  LEU A CD1 
4470  C CD2 . LEU B 559  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  556  LEU A CD2 
4471  N N   . PHE B 560  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  557  PHE A N   
4472  C CA  . PHE B 560  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  557  PHE A CA  
4473  C C   . PHE B 560  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  557  PHE A C   
4474  O O   . PHE B 560  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  557  PHE A O   
4475  C CB  . PHE B 560  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  557  PHE A CB  
4476  C CG  . PHE B 560  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  557  PHE A CG  
4477  C CD1 . PHE B 560  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  557  PHE A CD1 
4478  C CD2 . PHE B 560  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  557  PHE A CD2 
4479  C CE1 . PHE B 560  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  557  PHE A CE1 
4480  C CE2 . PHE B 560  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  557  PHE A CE2 
4481  C CZ  . PHE B 560  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  557  PHE A CZ  
4482  N N   . VAL B 561  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  558  VAL A N   
4483  C CA  . VAL B 561  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  558  VAL A CA  
4484  C C   . VAL B 561  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  558  VAL A C   
4485  O O   . VAL B 561  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  558  VAL A O   
4486  C CB  . VAL B 561  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  558  VAL A CB  
4487  C CG1 . VAL B 561  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  558  VAL A CG1 
4488  C CG2 . VAL B 561  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  558  VAL A CG2 
4489  N N   . LYS B 562  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  559  LYS A N   
4490  C CA  . LYS B 562  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  559  LYS A CA  
4491  C C   . LYS B 562  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  559  LYS A C   
4492  O O   . LYS B 562  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  559  LYS A O   
4493  C CB  . LYS B 562  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  559  LYS A CB  
4494  C CG  . LYS B 562  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  559  LYS A CG  
4495  C CD  . LYS B 562  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  559  LYS A CD  
4496  C CE  . LYS B 562  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  559  LYS A CE  
4497  N NZ  . LYS B 562  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  559  LYS A NZ  
4498  N N   . ASN B 563  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  560  ASN A N   
4499  C CA  . ASN B 563  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  560  ASN A CA  
4500  C C   . ASN B 563  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  560  ASN A C   
4501  O O   . ASN B 563  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  560  ASN A O   
4502  C CB  . ASN B 563  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  560  ASN A CB  
4503  C CG  . ASN B 563  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  560  ASN A CG  
4504  O OD1 . ASN B 563  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  560  ASN A OD1 
4505  N ND2 . ASN B 563  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  560  ASN A ND2 
4506  N N   . GLY B 564  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  561  GLY A N   
4507  C CA  . GLY B 564  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  561  GLY A CA  
4508  C C   . GLY B 564  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  561  GLY A C   
4509  O O   . GLY B 564  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  561  GLY A O   
4510  N N   . LEU B 565  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  562  LEU A N   
4511  C CA  . LEU B 565  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  562  LEU A CA  
4512  C C   . LEU B 565  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  562  LEU A C   
4513  O O   . LEU B 565  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  562  LEU A O   
4514  C CB  . LEU B 565  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  562  LEU A CB  
4515  C CG  . LEU B 565  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  562  LEU A CG  
4516  C CD1 . LEU B 565  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  562  LEU A CD1 
4517  C CD2 . LEU B 565  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  562  LEU A CD2 
4518  N N   . TYR B 566  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  563  TYR A N   
4519  C CA  . TYR B 566  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  563  TYR A CA  
4520  C C   . TYR B 566  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  563  TYR A C   
4521  O O   . TYR B 566  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  563  TYR A O   
4522  C CB  . TYR B 566  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  563  TYR A CB  
4523  C CG  . TYR B 566  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  563  TYR A CG  
4524  C CD1 . TYR B 566  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  563  TYR A CD1 
4525  C CD2 . TYR B 566  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  563  TYR A CD2 
4526  C CE1 . TYR B 566  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  563  TYR A CE1 
4527  C CE2 . TYR B 566  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  563  TYR A CE2 
4528  C CZ  . TYR B 566  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  563  TYR A CZ  
4529  O OH  . TYR B 566  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  563  TYR A OH  
4530  N N   . TYR B 567  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  564  TYR A N   
4531  C CA  . TYR B 567  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  564  TYR A CA  
4532  C C   . TYR B 567  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  564  TYR A C   
4533  O O   . TYR B 567  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  564  TYR A O   
4534  C CB  . TYR B 567  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  564  TYR A CB  
4535  C CG  . TYR B 567  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  564  TYR A CG  
4536  C CD1 . TYR B 567  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  564  TYR A CD1 
4537  C CD2 . TYR B 567  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  564  TYR A CD2 
4538  C CE1 . TYR B 567  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  564  TYR A CE1 
4539  C CE2 . TYR B 567  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  564  TYR A CE2 
4540  C CZ  . TYR B 567  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  564  TYR A CZ  
4541  O OH  . TYR B 567  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  564  TYR A OH  
4542  N N   . LEU B 568  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  565  LEU A N   
4543  C CA  . LEU B 568  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  565  LEU A CA  
4544  C C   . LEU B 568  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  565  LEU A C   
4545  O O   . LEU B 568  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  565  LEU A O   
4546  C CB  . LEU B 568  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  565  LEU A CB  
4547  C CG  . LEU B 568  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  565  LEU A CG  
4548  C CD1 . LEU B 568  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  565  LEU A CD1 
4549  C CD2 . LEU B 568  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  565  LEU A CD2 
4550  N N   . GLY B 569  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  566  GLY A N   
4551  C CA  . GLY B 569  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  566  GLY A CA  
4552  C C   . GLY B 569  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  566  GLY A C   
4553  O O   . GLY B 569  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  566  GLY A O   
4554  N N   . ILE B 570  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  567  ILE A N   
4555  C CA  . ILE B 570  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  567  ILE A CA  
4556  C C   . ILE B 570  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  567  ILE A C   
4557  O O   . ILE B 570  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  567  ILE A O   
4558  C CB  . ILE B 570  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  567  ILE A CB  
4559  C CG1 . ILE B 570  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  567  ILE A CG1 
4560  C CG2 . ILE B 570  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  567  ILE A CG2 
4561  C CD1 . ILE B 570  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  567  ILE A CD1 
4562  N N   . MET B 571  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  568  MET A N   
4563  C CA  . MET B 571  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  568  MET A CA  
4564  C C   . MET B 571  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  568  MET A C   
4565  O O   . MET B 571  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  568  MET A O   
4566  C CB  . MET B 571  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  568  MET A CB  
4567  C CG  . MET B 571  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  568  MET A CG  
4568  S SD  . MET B 571  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  568  MET A SD  
4569  C CE  . MET B 571  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  568  MET A CE  
4570  N N   . PRO B 572  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  569  PRO A N   
4571  C CA  . PRO B 572  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  569  PRO A CA  
4572  C C   . PRO B 572  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  569  PRO A C   
4573  O O   . PRO B 572  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  569  PRO A O   
4574  C CB  . PRO B 572  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  569  PRO A CB  
4575  C CG  . PRO B 572  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  569  PRO A CG  
4576  C CD  . PRO B 572  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  569  PRO A CD  
4577  N N   . LYS B 573  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  570  LYS A N   
4578  C CA  . LYS B 573  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  570  LYS A CA  
4579  C C   . LYS B 573  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  570  LYS A C   
4580  O O   . LYS B 573  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  570  LYS A O   
4581  C CB  . LYS B 573  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  570  LYS A CB  
4582  C CG  . LYS B 573  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  570  LYS A CG  
4583  C CD  . LYS B 573  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  570  LYS A CD  
4584  C CE  . LYS B 573  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  570  LYS A CE  
4585  N NZ  . LYS B 573  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  570  LYS A NZ  
4586  N N   . GLN B 574  ? 0.7695 0.7695 0.7695 0.0000  0.0000  0.0000  571  GLN A N   
4587  C CA  . GLN B 574  ? 0.7695 0.7695 0.7695 0.0000  0.0000  0.0000  571  GLN A CA  
4588  C C   . GLN B 574  ? 0.7695 0.7695 0.7695 0.0000  0.0000  0.0000  571  GLN A C   
4589  O O   . GLN B 574  ? 0.7695 0.7695 0.7695 0.0000  0.0000  0.0000  571  GLN A O   
4590  C CB  . GLN B 574  ? 0.7695 0.7695 0.7695 0.0000  0.0000  0.0000  571  GLN A CB  
4591  C CG  . GLN B 574  ? 0.7695 0.7695 0.7695 0.0000  0.0000  0.0000  571  GLN A CG  
4592  C CD  . GLN B 574  ? 0.7695 0.7695 0.7695 0.0000  0.0000  0.0000  571  GLN A CD  
4593  O OE1 . GLN B 574  ? 0.7695 0.7695 0.7695 0.0000  0.0000  0.0000  571  GLN A OE1 
4594  N NE2 . GLN B 574  ? 0.7695 0.7695 0.7695 0.0000  0.0000  0.0000  571  GLN A NE2 
4595  N N   . LYS B 575  ? 0.8135 0.8135 0.8135 0.0000  0.0000  0.0000  572  LYS A N   
4596  C CA  . LYS B 575  ? 0.8135 0.8135 0.8135 0.0000  0.0000  0.0000  572  LYS A CA  
4597  C C   . LYS B 575  ? 0.8135 0.8135 0.8135 0.0000  0.0000  0.0000  572  LYS A C   
4598  O O   . LYS B 575  ? 0.8135 0.8135 0.8135 0.0000  0.0000  0.0000  572  LYS A O   
4604  N N   . GLY B 576  ? 0.8189 0.8189 0.8189 0.0000  0.0000  0.0000  573  GLY A N   
4605  C CA  . GLY B 576  ? 0.8189 0.8189 0.8189 0.0000  0.0000  0.0000  573  GLY A CA  
4606  C C   . GLY B 576  ? 0.8189 0.8189 0.8189 0.0000  0.0000  0.0000  573  GLY A C   
4607  O O   . GLY B 576  ? 0.8189 0.8189 0.8189 0.0000  0.0000  0.0000  573  GLY A O   
4608  N N   . ARG B 577  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  574  ARG A N   
4609  C CA  . ARG B 577  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  574  ARG A CA  
4610  C C   . ARG B 577  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  574  ARG A C   
4611  O O   . ARG B 577  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  574  ARG A O   
4619  N N   . TYR B 578  ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  575  TYR A N   
4620  C CA  . TYR B 578  ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  575  TYR A CA  
4621  C C   . TYR B 578  ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  575  TYR A C   
4622  O O   . TYR B 578  ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  575  TYR A O   
4623  C CB  . TYR B 578  ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  575  TYR A CB  
4624  C CG  . TYR B 578  ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  575  TYR A CG  
4625  C CD1 . TYR B 578  ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  575  TYR A CD1 
4626  C CD2 . TYR B 578  ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  575  TYR A CD2 
4627  C CE1 . TYR B 578  ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  575  TYR A CE1 
4628  C CE2 . TYR B 578  ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  575  TYR A CE2 
4629  C CZ  . TYR B 578  ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  575  TYR A CZ  
4630  O OH  . TYR B 578  ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  575  TYR A OH  
4631  N N   . LYS B 579  ? 0.6703 0.6703 0.6703 0.0000  0.0000  0.0000  576  LYS A N   
4632  C CA  . LYS B 579  ? 0.6703 0.6703 0.6703 0.0000  0.0000  0.0000  576  LYS A CA  
4633  C C   . LYS B 579  ? 0.6703 0.6703 0.6703 0.0000  0.0000  0.0000  576  LYS A C   
4634  O O   . LYS B 579  ? 0.6703 0.6703 0.6703 0.0000  0.0000  0.0000  576  LYS A O   
4640  N N   . ALA B 580  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  577  ALA A N   
4641  C CA  . ALA B 580  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  577  ALA A CA  
4642  C C   . ALA B 580  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  577  ALA A C   
4643  O O   . ALA B 580  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  577  ALA A O   
4644  C CB  . ALA B 580  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  577  ALA A CB  
4645  N N   . LEU B 581  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  578  LEU A N   
4646  C CA  . LEU B 581  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  578  LEU A CA  
4647  C C   . LEU B 581  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  578  LEU A C   
4648  O O   . LEU B 581  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  578  LEU A O   
4653  N N   . SER B 582  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  579  SER A N   
4654  C CA  . SER B 582  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  579  SER A CA  
4655  C C   . SER B 582  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  579  SER A C   
4656  O O   . SER B 582  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  579  SER A O   
4657  C CB  . SER B 582  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  579  SER A CB  
4658  O OG  . SER B 582  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  579  SER A OG  
4659  N N   . PHE B 583  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  580  PHE A N   
4660  C CA  . PHE B 583  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  580  PHE A CA  
4661  C C   . PHE B 583  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  580  PHE A C   
4662  O O   . PHE B 583  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  580  PHE A O   
4663  C CB  . PHE B 583  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  580  PHE A CB  
4664  C CG  . PHE B 583  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  580  PHE A CG  
4665  C CD1 . PHE B 583  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  580  PHE A CD1 
4666  C CD2 . PHE B 583  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  580  PHE A CD2 
4667  C CE1 . PHE B 583  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  580  PHE A CE1 
4668  C CE2 . PHE B 583  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  580  PHE A CE2 
4669  C CZ  . PHE B 583  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  580  PHE A CZ  
4670  N N   . GLU B 584  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  581  GLU A N   
4671  C CA  . GLU B 584  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  581  GLU A CA  
4672  C C   . GLU B 584  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  581  GLU A C   
4673  O O   . GLU B 584  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  581  GLU A O   
4679  N N   . PRO B 585  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  582  PRO A N   
4680  C CA  . PRO B 585  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  582  PRO A CA  
4681  C C   . PRO B 585  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  582  PRO A C   
4682  O O   . PRO B 585  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  582  PRO A O   
4683  C CB  . PRO B 585  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  582  PRO A CB  
4684  C CG  . PRO B 585  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  582  PRO A CG  
4685  C CD  . PRO B 585  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  582  PRO A CD  
4686  N N   . THR B 586  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  583  THR A N   
4687  C CA  . THR B 586  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  583  THR A CA  
4688  C C   . THR B 586  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  583  THR A C   
4689  O O   . THR B 586  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  583  THR A O   
4690  C CB  . THR B 586  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  583  THR A CB  
4691  O OG1 . THR B 586  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  583  THR A OG1 
4692  C CG2 . THR B 586  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  583  THR A CG2 
4693  N N   . GLU B 587  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  584  GLU A N   
4694  C CA  . GLU B 587  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  584  GLU A CA  
4695  C C   . GLU B 587  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  584  GLU A C   
4696  O O   . GLU B 587  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  584  GLU A O   
4697  C CB  . GLU B 587  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  584  GLU A CB  
4698  C CG  . GLU B 587  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  584  GLU A CG  
4699  C CD  . GLU B 587  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  584  GLU A CD  
4700  O OE1 . GLU B 587  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  584  GLU A OE1 
4701  O OE2 . GLU B 587  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  584  GLU A OE2 
4702  N N   . LYS B 588  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  585  LYS A N   
4703  C CA  . LYS B 588  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  585  LYS A CA  
4704  C C   . LYS B 588  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  585  LYS A C   
4705  O O   . LYS B 588  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  585  LYS A O   
4711  N N   . THR B 589  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  586  THR A N   
4712  C CA  . THR B 589  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  586  THR A CA  
4713  C C   . THR B 589  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  586  THR A C   
4714  O O   . THR B 589  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  586  THR A O   
4715  C CB  . THR B 589  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  586  THR A CB  
4716  O OG1 . THR B 589  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  586  THR A OG1 
4717  C CG2 . THR B 589  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  586  THR A CG2 
4718  N N   . SER B 590  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  587  SER A N   
4719  C CA  . SER B 590  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  587  SER A CA  
4720  C C   . SER B 590  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  587  SER A C   
4721  O O   . SER B 590  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  587  SER A O   
4722  C CB  . SER B 590  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  587  SER A CB  
4723  O OG  . SER B 590  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  587  SER A OG  
4724  N N   . GLU B 591  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  588  GLU A N   
4725  C CA  . GLU B 591  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  588  GLU A CA  
4726  C C   . GLU B 591  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  588  GLU A C   
4727  O O   . GLU B 591  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  588  GLU A O   
4728  C CB  . GLU B 591  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  588  GLU A CB  
4729  C CG  . GLU B 591  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  588  GLU A CG  
4730  C CD  . GLU B 591  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  588  GLU A CD  
4731  O OE1 . GLU B 591  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  588  GLU A OE1 
4732  O OE2 . GLU B 591  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  588  GLU A OE2 
4733  N N   . GLY B 592  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  589  GLY A N   
4734  C CA  . GLY B 592  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  589  GLY A CA  
4735  C C   . GLY B 592  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  589  GLY A C   
4736  O O   . GLY B 592  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  589  GLY A O   
4737  N N   . PHE B 593  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  590  PHE A N   
4738  C CA  . PHE B 593  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  590  PHE A CA  
4739  C C   . PHE B 593  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  590  PHE A C   
4740  O O   . PHE B 593  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  590  PHE A O   
4741  C CB  . PHE B 593  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  590  PHE A CB  
4742  C CG  . PHE B 593  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  590  PHE A CG  
4743  C CD1 . PHE B 593  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  590  PHE A CD1 
4744  C CD2 . PHE B 593  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  590  PHE A CD2 
4745  C CE1 . PHE B 593  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  590  PHE A CE1 
4746  C CE2 . PHE B 593  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  590  PHE A CE2 
4747  C CZ  . PHE B 593  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  590  PHE A CZ  
4748  N N   . ASP B 594  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  591  ASP A N   
4749  C CA  . ASP B 594  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  591  ASP A CA  
4750  C C   . ASP B 594  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  591  ASP A C   
4751  O O   . ASP B 594  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  591  ASP A O   
4752  C CB  . ASP B 594  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  591  ASP A CB  
4753  C CG  . ASP B 594  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  591  ASP A CG  
4754  O OD1 . ASP B 594  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  591  ASP A OD1 
4755  O OD2 . ASP B 594  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  591  ASP A OD2 
4756  N N   . LYS B 595  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  592  LYS A N   
4757  C CA  . LYS B 595  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  592  LYS A CA  
4758  C C   . LYS B 595  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  592  LYS A C   
4759  O O   . LYS B 595  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  592  LYS A O   
4760  C CB  . LYS B 595  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  592  LYS A CB  
4761  C CG  . LYS B 595  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  592  LYS A CG  
4762  C CD  . LYS B 595  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  592  LYS A CD  
4763  C CE  . LYS B 595  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  592  LYS A CE  
4764  N NZ  . LYS B 595  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  592  LYS A NZ  
4765  N N   . MET B 596  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  593  MET A N   
4766  C CA  . MET B 596  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  593  MET A CA  
4767  C C   . MET B 596  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  593  MET A C   
4768  O O   . MET B 596  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  593  MET A O   
4769  C CB  . MET B 596  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  593  MET A CB  
4770  C CG  . MET B 596  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  593  MET A CG  
4771  S SD  . MET B 596  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  593  MET A SD  
4772  C CE  . MET B 596  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  593  MET A CE  
4773  N N   . TYR B 597  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  594  TYR A N   
4774  C CA  . TYR B 597  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  594  TYR A CA  
4775  C C   . TYR B 597  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  594  TYR A C   
4776  O O   . TYR B 597  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  594  TYR A O   
4777  C CB  . TYR B 597  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  594  TYR A CB  
4778  C CG  . TYR B 597  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  594  TYR A CG  
4779  C CD1 . TYR B 597  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  594  TYR A CD1 
4780  C CD2 . TYR B 597  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  594  TYR A CD2 
4781  C CE1 . TYR B 597  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  594  TYR A CE1 
4782  C CE2 . TYR B 597  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  594  TYR A CE2 
4783  C CZ  . TYR B 597  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  594  TYR A CZ  
4784  O OH  . TYR B 597  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  594  TYR A OH  
4785  N N   . TYR B 598  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  595  TYR A N   
4786  C CA  . TYR B 598  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  595  TYR A CA  
4787  C C   . TYR B 598  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  595  TYR A C   
4788  O O   . TYR B 598  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  595  TYR A O   
4789  C CB  . TYR B 598  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  595  TYR A CB  
4790  C CG  . TYR B 598  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  595  TYR A CG  
4791  C CD1 . TYR B 598  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  595  TYR A CD1 
4792  C CD2 . TYR B 598  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  595  TYR A CD2 
4793  C CE1 . TYR B 598  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  595  TYR A CE1 
4794  C CE2 . TYR B 598  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  595  TYR A CE2 
4795  C CZ  . TYR B 598  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  595  TYR A CZ  
4796  O OH  . TYR B 598  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  595  TYR A OH  
4797  N N   . ASP B 599  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  596  ASP A N   
4798  C CA  . ASP B 599  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  596  ASP A CA  
4799  C C   . ASP B 599  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  596  ASP A C   
4800  O O   . ASP B 599  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  596  ASP A O   
4801  C CB  . ASP B 599  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  596  ASP A CB  
4802  C CG  . ASP B 599  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  596  ASP A CG  
4803  O OD1 . ASP B 599  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  596  ASP A OD1 
4804  O OD2 . ASP B 599  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  596  ASP A OD2 
4805  N N   . TYR B 600  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  597  TYR A N   
4806  C CA  . TYR B 600  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  597  TYR A CA  
4807  C C   . TYR B 600  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  597  TYR A C   
4808  O O   . TYR B 600  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  597  TYR A O   
4809  C CB  . TYR B 600  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  597  TYR A CB  
4810  C CG  . TYR B 600  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  597  TYR A CG  
4811  C CD1 . TYR B 600  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  597  TYR A CD1 
4812  C CD2 . TYR B 600  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  597  TYR A CD2 
4813  C CE1 . TYR B 600  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  597  TYR A CE1 
4814  C CE2 . TYR B 600  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  597  TYR A CE2 
4815  C CZ  . TYR B 600  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  597  TYR A CZ  
4816  O OH  . TYR B 600  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  597  TYR A OH  
4817  N N   . PHE B 601  ? 0.5907 0.5907 0.5907 0.0000  0.0000  0.0000  598  PHE A N   
4818  C CA  . PHE B 601  ? 0.5907 0.5907 0.5907 0.0000  0.0000  0.0000  598  PHE A CA  
4819  C C   . PHE B 601  ? 0.5907 0.5907 0.5907 0.0000  0.0000  0.0000  598  PHE A C   
4820  O O   . PHE B 601  ? 0.5907 0.5907 0.5907 0.0000  0.0000  0.0000  598  PHE A O   
4821  C CB  . PHE B 601  ? 0.5907 0.5907 0.5907 0.0000  0.0000  0.0000  598  PHE A CB  
4822  C CG  . PHE B 601  ? 0.5907 0.5907 0.5907 0.0000  0.0000  0.0000  598  PHE A CG  
4823  C CD1 . PHE B 601  ? 0.5907 0.5907 0.5907 0.0000  0.0000  0.0000  598  PHE A CD1 
4824  C CD2 . PHE B 601  ? 0.5907 0.5907 0.5907 0.0000  0.0000  0.0000  598  PHE A CD2 
4825  C CE1 . PHE B 601  ? 0.5907 0.5907 0.5907 0.0000  0.0000  0.0000  598  PHE A CE1 
4826  C CE2 . PHE B 601  ? 0.5907 0.5907 0.5907 0.0000  0.0000  0.0000  598  PHE A CE2 
4827  C CZ  . PHE B 601  ? 0.5907 0.5907 0.5907 0.0000  0.0000  0.0000  598  PHE A CZ  
4828  N N   . PRO B 602  ? 0.6124 0.6124 0.6124 0.0000  0.0000  0.0000  599  PRO A N   
4829  C CA  . PRO B 602  ? 0.6124 0.6124 0.6124 0.0000  0.0000  0.0000  599  PRO A CA  
4830  C C   . PRO B 602  ? 0.6124 0.6124 0.6124 0.0000  0.0000  0.0000  599  PRO A C   
4831  O O   . PRO B 602  ? 0.6124 0.6124 0.6124 0.0000  0.0000  0.0000  599  PRO A O   
4832  C CB  . PRO B 602  ? 0.6124 0.6124 0.6124 0.0000  0.0000  0.0000  599  PRO A CB  
4833  C CG  . PRO B 602  ? 0.6124 0.6124 0.6124 0.0000  0.0000  0.0000  599  PRO A CG  
4834  C CD  . PRO B 602  ? 0.6124 0.6124 0.6124 0.0000  0.0000  0.0000  599  PRO A CD  
4835  N N   . ASP B 603  ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  600  ASP A N   
4836  C CA  . ASP B 603  ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  600  ASP A CA  
4837  C C   . ASP B 603  ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  600  ASP A C   
4838  O O   . ASP B 603  ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  600  ASP A O   
4839  C CB  . ASP B 603  ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  600  ASP A CB  
4840  C CG  . ASP B 603  ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  600  ASP A CG  
4841  O OD1 . ASP B 603  ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  600  ASP A OD1 
4842  O OD2 . ASP B 603  ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  600  ASP A OD2 
4843  N N   . ALA B 604  ? 0.7298 0.7298 0.7298 0.0000  0.0000  0.0000  601  ALA A N   
4844  C CA  . ALA B 604  ? 0.7298 0.7298 0.7298 0.0000  0.0000  0.0000  601  ALA A CA  
4845  C C   . ALA B 604  ? 0.7298 0.7298 0.7298 0.0000  0.0000  0.0000  601  ALA A C   
4846  O O   . ALA B 604  ? 0.7298 0.7298 0.7298 0.0000  0.0000  0.0000  601  ALA A O   
4847  C CB  . ALA B 604  ? 0.7298 0.7298 0.7298 0.0000  0.0000  0.0000  601  ALA A CB  
4848  N N   . ALA B 605  ? 0.7408 0.7408 0.7408 0.0000  0.0000  0.0000  602  ALA A N   
4849  C CA  . ALA B 605  ? 0.7408 0.7408 0.7408 0.0000  0.0000  0.0000  602  ALA A CA  
4850  C C   . ALA B 605  ? 0.7408 0.7408 0.7408 0.0000  0.0000  0.0000  602  ALA A C   
4851  O O   . ALA B 605  ? 0.7408 0.7408 0.7408 0.0000  0.0000  0.0000  602  ALA A O   
4852  C CB  . ALA B 605  ? 0.7408 0.7408 0.7408 0.0000  0.0000  0.0000  602  ALA A CB  
4853  N N   . LYS B 606  ? 0.7298 0.7298 0.7298 0.0000  0.0000  0.0000  603  LYS A N   
4854  C CA  . LYS B 606  ? 0.7298 0.7298 0.7298 0.0000  0.0000  0.0000  603  LYS A CA  
4855  C C   . LYS B 606  ? 0.7298 0.7298 0.7298 0.0000  0.0000  0.0000  603  LYS A C   
4856  O O   . LYS B 606  ? 0.7298 0.7298 0.7298 0.0000  0.0000  0.0000  603  LYS A O   
4857  C CB  . LYS B 606  ? 0.7298 0.7298 0.7298 0.0000  0.0000  0.0000  603  LYS A CB  
4858  C CG  . LYS B 606  ? 0.7298 0.7298 0.7298 0.0000  0.0000  0.0000  603  LYS A CG  
4859  C CD  . LYS B 606  ? 0.7298 0.7298 0.7298 0.0000  0.0000  0.0000  603  LYS A CD  
4860  C CE  . LYS B 606  ? 0.7298 0.7298 0.7298 0.0000  0.0000  0.0000  603  LYS A CE  
4861  N NZ  . LYS B 606  ? 0.7298 0.7298 0.7298 0.0000  0.0000  0.0000  603  LYS A NZ  
4862  N N   . MET B 607  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  604  MET A N   
4863  C CA  . MET B 607  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  604  MET A CA  
4864  C C   . MET B 607  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  604  MET A C   
4865  O O   . MET B 607  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  604  MET A O   
4866  C CB  . MET B 607  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  604  MET A CB  
4867  C CG  . MET B 607  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  604  MET A CG  
4868  S SD  . MET B 607  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  604  MET A SD  
4869  C CE  . MET B 607  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  604  MET A CE  
4870  N N   . ILE B 608  ? 0.7158 0.7158 0.7158 0.0000  0.0000  0.0000  605  ILE A N   
4871  C CA  . ILE B 608  ? 0.7158 0.7158 0.7158 0.0000  0.0000  0.0000  605  ILE A CA  
4872  C C   . ILE B 608  ? 0.7158 0.7158 0.7158 0.0000  0.0000  0.0000  605  ILE A C   
4873  O O   . ILE B 608  ? 0.7158 0.7158 0.7158 0.0000  0.0000  0.0000  605  ILE A O   
4874  C CB  . ILE B 608  ? 0.7158 0.7158 0.7158 0.0000  0.0000  0.0000  605  ILE A CB  
4875  C CG1 . ILE B 608  ? 0.7158 0.7158 0.7158 0.0000  0.0000  0.0000  605  ILE A CG1 
4876  C CG2 . ILE B 608  ? 0.7158 0.7158 0.7158 0.0000  0.0000  0.0000  605  ILE A CG2 
4877  C CD1 . ILE B 608  ? 0.7158 0.7158 0.7158 0.0000  0.0000  0.0000  605  ILE A CD1 
4878  N N   . PRO B 609  ? 0.7217 0.7217 0.7217 0.0000  0.0000  0.0000  606  PRO A N   
4879  C CA  . PRO B 609  ? 0.7217 0.7217 0.7217 0.0000  0.0000  0.0000  606  PRO A CA  
4880  C C   . PRO B 609  ? 0.7217 0.7217 0.7217 0.0000  0.0000  0.0000  606  PRO A C   
4881  O O   . PRO B 609  ? 0.7217 0.7217 0.7217 0.0000  0.0000  0.0000  606  PRO A O   
4882  C CB  . PRO B 609  ? 0.7217 0.7217 0.7217 0.0000  0.0000  0.0000  606  PRO A CB  
4883  C CG  . PRO B 609  ? 0.7217 0.7217 0.7217 0.0000  0.0000  0.0000  606  PRO A CG  
4884  C CD  . PRO B 609  ? 0.7217 0.7217 0.7217 0.0000  0.0000  0.0000  606  PRO A CD  
4885  N N   . LYS B 610  ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  607  LYS A N   
4886  C CA  . LYS B 610  ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  607  LYS A CA  
4887  C C   . LYS B 610  ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  607  LYS A C   
4888  O O   . LYS B 610  ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  607  LYS A O   
4889  C CB  . LYS B 610  ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  607  LYS A CB  
4890  C CG  . LYS B 610  ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  607  LYS A CG  
4891  C CD  . LYS B 610  ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  607  LYS A CD  
4892  C CE  . LYS B 610  ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  607  LYS A CE  
4893  N NZ  . LYS B 610  ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  607  LYS A NZ  
4894  N N   . CYS B 611  ? 0.7408 0.7408 0.7408 0.0000  0.0000  0.0000  608  CYS A N   
4895  C CA  . CYS B 611  ? 0.7408 0.7408 0.7408 0.0000  0.0000  0.0000  608  CYS A CA  
4896  C C   . CYS B 611  ? 0.7408 0.7408 0.7408 0.0000  0.0000  0.0000  608  CYS A C   
4897  O O   . CYS B 611  ? 0.7408 0.7408 0.7408 0.0000  0.0000  0.0000  608  CYS A O   
4898  C CB  . CYS B 611  ? 0.7408 0.7408 0.7408 0.0000  0.0000  0.0000  608  CYS A CB  
4899  S SG  . CYS B 611  ? 0.7408 0.7408 0.7408 0.0000  0.0000  0.0000  608  CYS A SG  
4900  N N   . SER B 612  ? 0.7961 0.7961 0.7961 0.0000  0.0000  0.0000  609  SER A N   
4901  C CA  . SER B 612  ? 0.7961 0.7961 0.7961 0.0000  0.0000  0.0000  609  SER A CA  
4902  C C   . SER B 612  ? 0.7961 0.7961 0.7961 0.0000  0.0000  0.0000  609  SER A C   
4903  O O   . SER B 612  ? 0.7961 0.7961 0.7961 0.0000  0.0000  0.0000  609  SER A O   
4904  C CB  . SER B 612  ? 0.7961 0.7961 0.7961 0.0000  0.0000  0.0000  609  SER A CB  
4905  O OG  . SER B 612  ? 0.7961 0.7961 0.7961 0.0000  0.0000  0.0000  609  SER A OG  
4906  N N   . THR B 613  ? 0.8397 0.8397 0.8397 0.0000  0.0000  0.0000  610  THR A N   
4907  C CA  . THR B 613  ? 0.8397 0.8397 0.8397 0.0000  0.0000  0.0000  610  THR A CA  
4908  C C   . THR B 613  ? 0.8397 0.8397 0.8397 0.0000  0.0000  0.0000  610  THR A C   
4909  O O   . THR B 613  ? 0.8397 0.8397 0.8397 0.0000  0.0000  0.0000  610  THR A O   
4910  C CB  . THR B 613  ? 0.8397 0.8397 0.8397 0.0000  0.0000  0.0000  610  THR A CB  
4911  O OG1 . THR B 613  ? 0.8397 0.8397 0.8397 0.0000  0.0000  0.0000  610  THR A OG1 
4912  C CG2 . THR B 613  ? 0.8397 0.8397 0.8397 0.0000  0.0000  0.0000  610  THR A CG2 
4913  N N   . GLN B 614  ? 0.7793 0.7793 0.7793 0.0000  0.0000  0.0000  611  GLN A N   
4914  C CA  . GLN B 614  ? 0.7793 0.7793 0.7793 0.0000  0.0000  0.0000  611  GLN A CA  
4915  C C   . GLN B 614  ? 0.7793 0.7793 0.7793 0.0000  0.0000  0.0000  611  GLN A C   
4916  O O   . GLN B 614  ? 0.7793 0.7793 0.7793 0.0000  0.0000  0.0000  611  GLN A O   
4917  C CB  . GLN B 614  ? 0.7793 0.7793 0.7793 0.0000  0.0000  0.0000  611  GLN A CB  
4918  C CG  . GLN B 614  ? 0.7793 0.7793 0.7793 0.0000  0.0000  0.0000  611  GLN A CG  
4919  C CD  . GLN B 614  ? 0.7793 0.7793 0.7793 0.0000  0.0000  0.0000  611  GLN A CD  
4920  O OE1 . GLN B 614  ? 0.7793 0.7793 0.7793 0.0000  0.0000  0.0000  611  GLN A OE1 
4921  N NE2 . GLN B 614  ? 0.7793 0.7793 0.7793 0.0000  0.0000  0.0000  611  GLN A NE2 
4922  N N   . LEU B 615  ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  612  LEU A N   
4923  C CA  . LEU B 615  ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  612  LEU A CA  
4924  C C   . LEU B 615  ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  612  LEU A C   
4925  O O   . LEU B 615  ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  612  LEU A O   
4926  C CB  . LEU B 615  ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  612  LEU A CB  
4927  C CG  . LEU B 615  ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  612  LEU A CG  
4928  C CD1 . LEU B 615  ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  612  LEU A CD1 
4929  C CD2 . LEU B 615  ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  612  LEU A CD2 
4930  N N   . LYS B 616  ? 0.7063 0.7063 0.7063 0.0000  0.0000  0.0000  613  LYS A N   
4931  C CA  . LYS B 616  ? 0.7063 0.7063 0.7063 0.0000  0.0000  0.0000  613  LYS A CA  
4932  C C   . LYS B 616  ? 0.7063 0.7063 0.7063 0.0000  0.0000  0.0000  613  LYS A C   
4933  O O   . LYS B 616  ? 0.7063 0.7063 0.7063 0.0000  0.0000  0.0000  613  LYS A O   
4934  C CB  . LYS B 616  ? 0.7063 0.7063 0.7063 0.0000  0.0000  0.0000  613  LYS A CB  
4935  C CG  . LYS B 616  ? 0.7063 0.7063 0.7063 0.0000  0.0000  0.0000  613  LYS A CG  
4936  C CD  . LYS B 616  ? 0.7063 0.7063 0.7063 0.0000  0.0000  0.0000  613  LYS A CD  
4937  C CE  . LYS B 616  ? 0.7063 0.7063 0.7063 0.0000  0.0000  0.0000  613  LYS A CE  
4938  N NZ  . LYS B 616  ? 0.7063 0.7063 0.7063 0.0000  0.0000  0.0000  613  LYS A NZ  
4939  N N   . ALA B 617  ? 0.7965 0.7965 0.7965 0.0000  0.0000  0.0000  614  ALA A N   
4940  C CA  . ALA B 617  ? 0.7965 0.7965 0.7965 0.0000  0.0000  0.0000  614  ALA A CA  
4941  C C   . ALA B 617  ? 0.7965 0.7965 0.7965 0.0000  0.0000  0.0000  614  ALA A C   
4942  O O   . ALA B 617  ? 0.7965 0.7965 0.7965 0.0000  0.0000  0.0000  614  ALA A O   
4943  C CB  . ALA B 617  ? 0.7965 0.7965 0.7965 0.0000  0.0000  0.0000  614  ALA A CB  
4944  N N   . VAL B 618  ? 0.9127 0.9127 0.9127 0.0000  0.0000  0.0000  615  VAL A N   
4945  C CA  . VAL B 618  ? 0.9127 0.9127 0.9127 0.0000  0.0000  0.0000  615  VAL A CA  
4946  C C   . VAL B 618  ? 0.9127 0.9127 0.9127 0.0000  0.0000  0.0000  615  VAL A C   
4947  O O   . VAL B 618  ? 0.9127 0.9127 0.9127 0.0000  0.0000  0.0000  615  VAL A O   
4948  C CB  . VAL B 618  ? 0.9127 0.9127 0.9127 0.0000  0.0000  0.0000  615  VAL A CB  
4949  C CG1 . VAL B 618  ? 0.9127 0.9127 0.9127 0.0000  0.0000  0.0000  615  VAL A CG1 
4950  C CG2 . VAL B 618  ? 0.9127 0.9127 0.9127 0.0000  0.0000  0.0000  615  VAL A CG2 
4951  N N   . THR B 619  ? 0.8511 0.8511 0.8511 0.0000  0.0000  0.0000  616  THR A N   
4952  C CA  . THR B 619  ? 0.8511 0.8511 0.8511 0.0000  0.0000  0.0000  616  THR A CA  
4953  C C   . THR B 619  ? 0.8511 0.8511 0.8511 0.0000  0.0000  0.0000  616  THR A C   
4954  O O   . THR B 619  ? 0.8511 0.8511 0.8511 0.0000  0.0000  0.0000  616  THR A O   
4955  C CB  . THR B 619  ? 0.8511 0.8511 0.8511 0.0000  0.0000  0.0000  616  THR A CB  
4956  O OG1 . THR B 619  ? 0.8511 0.8511 0.8511 0.0000  0.0000  0.0000  616  THR A OG1 
4957  C CG2 . THR B 619  ? 0.8511 0.8511 0.8511 0.0000  0.0000  0.0000  616  THR A CG2 
4958  N N   . ALA B 620  ? 0.8807 0.8807 0.8807 0.0000  0.0000  0.0000  617  ALA A N   
4959  C CA  . ALA B 620  ? 0.8807 0.8807 0.8807 0.0000  0.0000  0.0000  617  ALA A CA  
4960  C C   . ALA B 620  ? 0.8807 0.8807 0.8807 0.0000  0.0000  0.0000  617  ALA A C   
4961  O O   . ALA B 620  ? 0.8807 0.8807 0.8807 0.0000  0.0000  0.0000  617  ALA A O   
4962  C CB  . ALA B 620  ? 0.8807 0.8807 0.8807 0.0000  0.0000  0.0000  617  ALA A CB  
4963  N N   . HIS B 621  ? 0.9444 0.9444 0.9444 0.0000  0.0000  0.0000  618  HIS A N   
4964  C CA  . HIS B 621  ? 0.9444 0.9444 0.9444 0.0000  0.0000  0.0000  618  HIS A CA  
4965  C C   . HIS B 621  ? 0.9444 0.9444 0.9444 0.0000  0.0000  0.0000  618  HIS A C   
4966  O O   . HIS B 621  ? 0.9444 0.9444 0.9444 0.0000  0.0000  0.0000  618  HIS A O   
4967  C CB  . HIS B 621  ? 0.9444 0.9444 0.9444 0.0000  0.0000  0.0000  618  HIS A CB  
4968  C CG  . HIS B 621  ? 0.9444 0.9444 0.9444 0.0000  0.0000  0.0000  618  HIS A CG  
4969  N ND1 . HIS B 621  ? 0.9444 0.9444 0.9444 0.0000  0.0000  0.0000  618  HIS A ND1 
4970  C CD2 . HIS B 621  ? 0.9444 0.9444 0.9444 0.0000  0.0000  0.0000  618  HIS A CD2 
4971  C CE1 . HIS B 621  ? 0.9444 0.9444 0.9444 0.0000  0.0000  0.0000  618  HIS A CE1 
4972  N NE2 . HIS B 621  ? 0.9444 0.9444 0.9444 0.0000  0.0000  0.0000  618  HIS A NE2 
4973  N N   . PHE B 622  ? 0.9850 0.9850 0.9850 0.0000  0.0000  0.0000  619  PHE A N   
4974  C CA  . PHE B 622  ? 0.9850 0.9850 0.9850 0.0000  0.0000  0.0000  619  PHE A CA  
4975  C C   . PHE B 622  ? 0.9850 0.9850 0.9850 0.0000  0.0000  0.0000  619  PHE A C   
4976  O O   . PHE B 622  ? 0.9850 0.9850 0.9850 0.0000  0.0000  0.0000  619  PHE A O   
4977  C CB  . PHE B 622  ? 0.9850 0.9850 0.9850 0.0000  0.0000  0.0000  619  PHE A CB  
4978  C CG  . PHE B 622  ? 0.9850 0.9850 0.9850 0.0000  0.0000  0.0000  619  PHE A CG  
4979  C CD1 . PHE B 622  ? 0.9850 0.9850 0.9850 0.0000  0.0000  0.0000  619  PHE A CD1 
4980  C CD2 . PHE B 622  ? 0.9850 0.9850 0.9850 0.0000  0.0000  0.0000  619  PHE A CD2 
4981  C CE1 . PHE B 622  ? 0.9850 0.9850 0.9850 0.0000  0.0000  0.0000  619  PHE A CE1 
4982  C CE2 . PHE B 622  ? 0.9850 0.9850 0.9850 0.0000  0.0000  0.0000  619  PHE A CE2 
4983  C CZ  . PHE B 622  ? 0.9850 0.9850 0.9850 0.0000  0.0000  0.0000  619  PHE A CZ  
4984  N N   . GLN B 623  ? 0.9231 0.9231 0.9231 0.0000  0.0000  0.0000  620  GLN A N   
4985  C CA  . GLN B 623  ? 0.9231 0.9231 0.9231 0.0000  0.0000  0.0000  620  GLN A CA  
4986  C C   . GLN B 623  ? 0.9231 0.9231 0.9231 0.0000  0.0000  0.0000  620  GLN A C   
4987  O O   . GLN B 623  ? 0.9231 0.9231 0.9231 0.0000  0.0000  0.0000  620  GLN A O   
4988  C CB  . GLN B 623  ? 0.9231 0.9231 0.9231 0.0000  0.0000  0.0000  620  GLN A CB  
4989  C CG  . GLN B 623  ? 0.9231 0.9231 0.9231 0.0000  0.0000  0.0000  620  GLN A CG  
4990  C CD  . GLN B 623  ? 0.9231 0.9231 0.9231 0.0000  0.0000  0.0000  620  GLN A CD  
4991  O OE1 . GLN B 623  ? 0.9231 0.9231 0.9231 0.0000  0.0000  0.0000  620  GLN A OE1 
4992  N NE2 . GLN B 623  ? 0.9231 0.9231 0.9231 0.0000  0.0000  0.0000  620  GLN A NE2 
4993  N N   . THR B 624  ? 0.9527 0.9527 0.9527 0.0000  0.0000  0.0000  621  THR A N   
4994  C CA  . THR B 624  ? 0.9527 0.9527 0.9527 0.0000  0.0000  0.0000  621  THR A CA  
4995  C C   . THR B 624  ? 0.9527 0.9527 0.9527 0.0000  0.0000  0.0000  621  THR A C   
4996  O O   . THR B 624  ? 0.9527 0.9527 0.9527 0.0000  0.0000  0.0000  621  THR A O   
4997  C CB  . THR B 624  ? 0.9527 0.9527 0.9527 0.0000  0.0000  0.0000  621  THR A CB  
4998  O OG1 . THR B 624  ? 0.9527 0.9527 0.9527 0.0000  0.0000  0.0000  621  THR A OG1 
4999  C CG2 . THR B 624  ? 0.9527 0.9527 0.9527 0.0000  0.0000  0.0000  621  THR A CG2 
5000  N N   . HIS B 625  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  622  HIS A N   
5001  C CA  . HIS B 625  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  622  HIS A CA  
5002  C C   . HIS B 625  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  622  HIS A C   
5003  O O   . HIS B 625  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  622  HIS A O   
5004  C CB  . HIS B 625  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  622  HIS A CB  
5005  C CG  . HIS B 625  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  622  HIS A CG  
5006  N ND1 . HIS B 625  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  622  HIS A ND1 
5007  C CD2 . HIS B 625  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  622  HIS A CD2 
5008  C CE1 . HIS B 625  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  622  HIS A CE1 
5009  N NE2 . HIS B 625  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  622  HIS A NE2 
5010  N N   . THR B 626  ? 1.0502 1.0502 1.0502 0.0000  0.0000  0.0000  623  THR A N   
5011  C CA  . THR B 626  ? 1.0502 1.0502 1.0502 0.0000  0.0000  0.0000  623  THR A CA  
5012  C C   . THR B 626  ? 1.0502 1.0502 1.0502 0.0000  0.0000  0.0000  623  THR A C   
5013  O O   . THR B 626  ? 1.0502 1.0502 1.0502 0.0000  0.0000  0.0000  623  THR A O   
5014  C CB  . THR B 626  ? 1.0502 1.0502 1.0502 0.0000  0.0000  0.0000  623  THR A CB  
5015  O OG1 . THR B 626  ? 1.0502 1.0502 1.0502 0.0000  0.0000  0.0000  623  THR A OG1 
5016  C CG2 . THR B 626  ? 1.0502 1.0502 1.0502 0.0000  0.0000  0.0000  623  THR A CG2 
5017  N N   . THR B 627  ? 1.0355 1.0355 1.0355 0.0000  0.0000  0.0000  624  THR A N   
5018  C CA  . THR B 627  ? 1.0355 1.0355 1.0355 0.0000  0.0000  0.0000  624  THR A CA  
5019  C C   . THR B 627  ? 1.0355 1.0355 1.0355 0.0000  0.0000  0.0000  624  THR A C   
5020  O O   . THR B 627  ? 1.0355 1.0355 1.0355 0.0000  0.0000  0.0000  624  THR A O   
5021  C CB  . THR B 627  ? 1.0355 1.0355 1.0355 0.0000  0.0000  0.0000  624  THR A CB  
5022  O OG1 . THR B 627  ? 1.0355 1.0355 1.0355 0.0000  0.0000  0.0000  624  THR A OG1 
5023  C CG2 . THR B 627  ? 1.0355 1.0355 1.0355 0.0000  0.0000  0.0000  624  THR A CG2 
5024  N N   . PRO B 628  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  625  PRO A N   
5025  C CA  . PRO B 628  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  625  PRO A CA  
5026  C C   . PRO B 628  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  625  PRO A C   
5027  O O   . PRO B 628  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  625  PRO A O   
5028  C CB  . PRO B 628  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  625  PRO A CB  
5029  C CG  . PRO B 628  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  625  PRO A CG  
5030  C CD  . PRO B 628  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  625  PRO A CD  
5031  N N   . ILE B 629  ? 0.9944 0.9944 0.9944 0.0000  0.0000  0.0000  626  ILE A N   
5032  C CA  . ILE B 629  ? 0.9944 0.9944 0.9944 0.0000  0.0000  0.0000  626  ILE A CA  
5033  C C   . ILE B 629  ? 0.9944 0.9944 0.9944 0.0000  0.0000  0.0000  626  ILE A C   
5034  O O   . ILE B 629  ? 0.9944 0.9944 0.9944 0.0000  0.0000  0.0000  626  ILE A O   
5035  C CB  . ILE B 629  ? 0.9944 0.9944 0.9944 0.0000  0.0000  0.0000  626  ILE A CB  
5036  C CG1 . ILE B 629  ? 0.9944 0.9944 0.9944 0.0000  0.0000  0.0000  626  ILE A CG1 
5037  C CG2 . ILE B 629  ? 0.9944 0.9944 0.9944 0.0000  0.0000  0.0000  626  ILE A CG2 
5038  C CD1 . ILE B 629  ? 0.9944 0.9944 0.9944 0.0000  0.0000  0.0000  626  ILE A CD1 
5039  N N   . LEU B 630  ? 0.9578 0.9578 0.9578 0.0000  0.0000  0.0000  627  LEU A N   
5040  C CA  . LEU B 630  ? 0.9578 0.9578 0.9578 0.0000  0.0000  0.0000  627  LEU A CA  
5041  C C   . LEU B 630  ? 0.9578 0.9578 0.9578 0.0000  0.0000  0.0000  627  LEU A C   
5042  O O   . LEU B 630  ? 0.9578 0.9578 0.9578 0.0000  0.0000  0.0000  627  LEU A O   
5043  C CB  . LEU B 630  ? 0.9578 0.9578 0.9578 0.0000  0.0000  0.0000  627  LEU A CB  
5044  C CG  . LEU B 630  ? 0.9578 0.9578 0.9578 0.0000  0.0000  0.0000  627  LEU A CG  
5045  C CD1 . LEU B 630  ? 0.9578 0.9578 0.9578 0.0000  0.0000  0.0000  627  LEU A CD1 
5046  C CD2 . LEU B 630  ? 0.9578 0.9578 0.9578 0.0000  0.0000  0.0000  627  LEU A CD2 
5047  N N   . LEU B 631  ? 0.8498 0.8498 0.8498 0.0000  0.0000  0.0000  628  LEU A N   
5048  C CA  . LEU B 631  ? 0.8498 0.8498 0.8498 0.0000  0.0000  0.0000  628  LEU A CA  
5049  C C   . LEU B 631  ? 0.8498 0.8498 0.8498 0.0000  0.0000  0.0000  628  LEU A C   
5050  O O   . LEU B 631  ? 0.8498 0.8498 0.8498 0.0000  0.0000  0.0000  628  LEU A O   
5051  C CB  . LEU B 631  ? 0.8498 0.8498 0.8498 0.0000  0.0000  0.0000  628  LEU A CB  
5052  C CG  . LEU B 631  ? 0.8498 0.8498 0.8498 0.0000  0.0000  0.0000  628  LEU A CG  
5053  C CD1 . LEU B 631  ? 0.8498 0.8498 0.8498 0.0000  0.0000  0.0000  628  LEU A CD1 
5054  C CD2 . LEU B 631  ? 0.8498 0.8498 0.8498 0.0000  0.0000  0.0000  628  LEU A CD2 
5055  N N   . SER B 632  ? 0.8490 0.8490 0.8490 0.0000  0.0000  0.0000  629  SER A N   
5056  C CA  . SER B 632  ? 0.8490 0.8490 0.8490 0.0000  0.0000  0.0000  629  SER A CA  
5057  C C   . SER B 632  ? 0.8490 0.8490 0.8490 0.0000  0.0000  0.0000  629  SER A C   
5058  O O   . SER B 632  ? 0.8490 0.8490 0.8490 0.0000  0.0000  0.0000  629  SER A O   
5059  C CB  . SER B 632  ? 0.8490 0.8490 0.8490 0.0000  0.0000  0.0000  629  SER A CB  
5060  O OG  . SER B 632  ? 0.8490 0.8490 0.8490 0.0000  0.0000  0.0000  629  SER A OG  
5061  N N   . ASN B 633  ? 0.7878 0.7878 0.7878 0.0000  0.0000  0.0000  630  ASN A N   
5062  C CA  . ASN B 633  ? 0.7878 0.7878 0.7878 0.0000  0.0000  0.0000  630  ASN A CA  
5063  C C   . ASN B 633  ? 0.7878 0.7878 0.7878 0.0000  0.0000  0.0000  630  ASN A C   
5064  O O   . ASN B 633  ? 0.7878 0.7878 0.7878 0.0000  0.0000  0.0000  630  ASN A O   
5065  C CB  . ASN B 633  ? 0.7878 0.7878 0.7878 0.0000  0.0000  0.0000  630  ASN A CB  
5066  C CG  . ASN B 633  ? 0.7878 0.7878 0.7878 0.0000  0.0000  0.0000  630  ASN A CG  
5067  O OD1 . ASN B 633  ? 0.7878 0.7878 0.7878 0.0000  0.0000  0.0000  630  ASN A OD1 
5068  N ND2 . ASN B 633  ? 0.7878 0.7878 0.7878 0.0000  0.0000  0.0000  630  ASN A ND2 
5069  N N   . ASN B 634  ? 0.7790 0.7790 0.7790 0.0000  0.0000  0.0000  631  ASN A N   
5070  C CA  . ASN B 634  ? 0.7790 0.7790 0.7790 0.0000  0.0000  0.0000  631  ASN A CA  
5071  C C   . ASN B 634  ? 0.7790 0.7790 0.7790 0.0000  0.0000  0.0000  631  ASN A C   
5072  O O   . ASN B 634  ? 0.7790 0.7790 0.7790 0.0000  0.0000  0.0000  631  ASN A O   
5073  C CB  . ASN B 634  ? 0.7790 0.7790 0.7790 0.0000  0.0000  0.0000  631  ASN A CB  
5074  C CG  . ASN B 634  ? 0.7790 0.7790 0.7790 0.0000  0.0000  0.0000  631  ASN A CG  
5075  O OD1 . ASN B 634  ? 0.7790 0.7790 0.7790 0.0000  0.0000  0.0000  631  ASN A OD1 
5076  N ND2 . ASN B 634  ? 0.7790 0.7790 0.7790 0.0000  0.0000  0.0000  631  ASN A ND2 
5077  N N   . PHE B 635  ? 0.7616 0.7616 0.7616 0.0000  0.0000  0.0000  632  PHE A N   
5078  C CA  . PHE B 635  ? 0.7616 0.7616 0.7616 0.0000  0.0000  0.0000  632  PHE A CA  
5079  C C   . PHE B 635  ? 0.7616 0.7616 0.7616 0.0000  0.0000  0.0000  632  PHE A C   
5080  O O   . PHE B 635  ? 0.7616 0.7616 0.7616 0.0000  0.0000  0.0000  632  PHE A O   
5081  C CB  . PHE B 635  ? 0.7616 0.7616 0.7616 0.0000  0.0000  0.0000  632  PHE A CB  
5082  C CG  . PHE B 635  ? 0.7616 0.7616 0.7616 0.0000  0.0000  0.0000  632  PHE A CG  
5083  C CD1 . PHE B 635  ? 0.7616 0.7616 0.7616 0.0000  0.0000  0.0000  632  PHE A CD1 
5084  C CD2 . PHE B 635  ? 0.7616 0.7616 0.7616 0.0000  0.0000  0.0000  632  PHE A CD2 
5085  C CE1 . PHE B 635  ? 0.7616 0.7616 0.7616 0.0000  0.0000  0.0000  632  PHE A CE1 
5086  C CE2 . PHE B 635  ? 0.7616 0.7616 0.7616 0.0000  0.0000  0.0000  632  PHE A CE2 
5087  C CZ  . PHE B 635  ? 0.7616 0.7616 0.7616 0.0000  0.0000  0.0000  632  PHE A CZ  
5088  N N   . ILE B 636  ? 0.8642 0.8642 0.8642 0.0000  0.0000  0.0000  633  ILE A N   
5089  C CA  . ILE B 636  ? 0.8642 0.8642 0.8642 0.0000  0.0000  0.0000  633  ILE A CA  
5090  C C   . ILE B 636  ? 0.8642 0.8642 0.8642 0.0000  0.0000  0.0000  633  ILE A C   
5091  O O   . ILE B 636  ? 0.8642 0.8642 0.8642 0.0000  0.0000  0.0000  633  ILE A O   
5092  C CB  . ILE B 636  ? 0.8642 0.8642 0.8642 0.0000  0.0000  0.0000  633  ILE A CB  
5093  C CG1 . ILE B 636  ? 0.8642 0.8642 0.8642 0.0000  0.0000  0.0000  633  ILE A CG1 
5094  C CG2 . ILE B 636  ? 0.8642 0.8642 0.8642 0.0000  0.0000  0.0000  633  ILE A CG2 
5095  C CD1 . ILE B 636  ? 0.8642 0.8642 0.8642 0.0000  0.0000  0.0000  633  ILE A CD1 
5096  N N   . GLU B 637  ? 0.8606 0.8606 0.8606 0.0000  0.0000  0.0000  634  GLU A N   
5097  C CA  . GLU B 637  ? 0.8606 0.8606 0.8606 0.0000  0.0000  0.0000  634  GLU A CA  
5098  C C   . GLU B 637  ? 0.8606 0.8606 0.8606 0.0000  0.0000  0.0000  634  GLU A C   
5099  O O   . GLU B 637  ? 0.8606 0.8606 0.8606 0.0000  0.0000  0.0000  634  GLU A O   
5100  C CB  . GLU B 637  ? 0.8606 0.8606 0.8606 0.0000  0.0000  0.0000  634  GLU A CB  
5101  C CG  . GLU B 637  ? 0.8606 0.8606 0.8606 0.0000  0.0000  0.0000  634  GLU A CG  
5102  C CD  . GLU B 637  ? 0.8606 0.8606 0.8606 0.0000  0.0000  0.0000  634  GLU A CD  
5103  O OE1 . GLU B 637  ? 0.8606 0.8606 0.8606 0.0000  0.0000  0.0000  634  GLU A OE1 
5104  O OE2 . GLU B 637  ? 0.8606 0.8606 0.8606 0.0000  0.0000  0.0000  634  GLU A OE2 
5105  N N   . PRO B 638  ? 0.8935 0.8935 0.8935 0.0000  0.0000  0.0000  635  PRO A N   
5106  C CA  . PRO B 638  ? 0.8935 0.8935 0.8935 0.0000  0.0000  0.0000  635  PRO A CA  
5107  C C   . PRO B 638  ? 0.8935 0.8935 0.8935 0.0000  0.0000  0.0000  635  PRO A C   
5108  O O   . PRO B 638  ? 0.8935 0.8935 0.8935 0.0000  0.0000  0.0000  635  PRO A O   
5109  C CB  . PRO B 638  ? 0.8935 0.8935 0.8935 0.0000  0.0000  0.0000  635  PRO A CB  
5110  C CG  . PRO B 638  ? 0.8935 0.8935 0.8935 0.0000  0.0000  0.0000  635  PRO A CG  
5111  C CD  . PRO B 638  ? 0.8935 0.8935 0.8935 0.0000  0.0000  0.0000  635  PRO A CD  
5112  N N   . LEU B 639  ? 0.8980 0.8980 0.8980 0.0000  0.0000  0.0000  636  LEU A N   
5113  C CA  . LEU B 639  ? 0.8980 0.8980 0.8980 0.0000  0.0000  0.0000  636  LEU A CA  
5114  C C   . LEU B 639  ? 0.8980 0.8980 0.8980 0.0000  0.0000  0.0000  636  LEU A C   
5115  O O   . LEU B 639  ? 0.8980 0.8980 0.8980 0.0000  0.0000  0.0000  636  LEU A O   
5116  C CB  . LEU B 639  ? 0.8980 0.8980 0.8980 0.0000  0.0000  0.0000  636  LEU A CB  
5117  C CG  . LEU B 639  ? 0.8980 0.8980 0.8980 0.0000  0.0000  0.0000  636  LEU A CG  
5118  C CD1 . LEU B 639  ? 0.8980 0.8980 0.8980 0.0000  0.0000  0.0000  636  LEU A CD1 
5119  C CD2 . LEU B 639  ? 0.8980 0.8980 0.8980 0.0000  0.0000  0.0000  636  LEU A CD2 
5120  N N   . GLU B 640  ? 1.0156 1.0156 1.0156 0.0000  0.0000  0.0000  637  GLU A N   
5121  C CA  . GLU B 640  ? 1.0156 1.0156 1.0156 0.0000  0.0000  0.0000  637  GLU A CA  
5122  C C   . GLU B 640  ? 1.0156 1.0156 1.0156 0.0000  0.0000  0.0000  637  GLU A C   
5123  O O   . GLU B 640  ? 1.0156 1.0156 1.0156 0.0000  0.0000  0.0000  637  GLU A O   
5124  C CB  . GLU B 640  ? 1.0156 1.0156 1.0156 0.0000  0.0000  0.0000  637  GLU A CB  
5125  C CG  . GLU B 640  ? 1.0156 1.0156 1.0156 0.0000  0.0000  0.0000  637  GLU A CG  
5126  C CD  . GLU B 640  ? 1.0156 1.0156 1.0156 0.0000  0.0000  0.0000  637  GLU A CD  
5127  O OE1 . GLU B 640  ? 1.0156 1.0156 1.0156 0.0000  0.0000  0.0000  637  GLU A OE1 
5128  O OE2 . GLU B 640  ? 1.0156 1.0156 1.0156 0.0000  0.0000  0.0000  637  GLU A OE2 
5129  N N   . ILE B 641  ? 0.9717 0.9717 0.9717 0.0000  0.0000  0.0000  638  ILE A N   
5130  C CA  . ILE B 641  ? 0.9717 0.9717 0.9717 0.0000  0.0000  0.0000  638  ILE A CA  
5131  C C   . ILE B 641  ? 0.9717 0.9717 0.9717 0.0000  0.0000  0.0000  638  ILE A C   
5132  O O   . ILE B 641  ? 0.9717 0.9717 0.9717 0.0000  0.0000  0.0000  638  ILE A O   
5133  C CB  . ILE B 641  ? 0.9717 0.9717 0.9717 0.0000  0.0000  0.0000  638  ILE A CB  
5134  C CG1 . ILE B 641  ? 0.9717 0.9717 0.9717 0.0000  0.0000  0.0000  638  ILE A CG1 
5135  C CG2 . ILE B 641  ? 0.9717 0.9717 0.9717 0.0000  0.0000  0.0000  638  ILE A CG2 
5136  C CD1 . ILE B 641  ? 0.9717 0.9717 0.9717 0.0000  0.0000  0.0000  638  ILE A CD1 
5137  N N   . THR B 642  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  639  THR A N   
5138  C CA  . THR B 642  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  639  THR A CA  
5139  C C   . THR B 642  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  639  THR A C   
5140  O O   . THR B 642  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  639  THR A O   
5141  C CB  . THR B 642  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  639  THR A CB  
5142  O OG1 . THR B 642  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  639  THR A OG1 
5143  C CG2 . THR B 642  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  639  THR A CG2 
5144  N N   . LYS B 643  ? 1.0419 1.0419 1.0419 0.0000  0.0000  0.0000  640  LYS A N   
5145  C CA  . LYS B 643  ? 1.0419 1.0419 1.0419 0.0000  0.0000  0.0000  640  LYS A CA  
5146  C C   . LYS B 643  ? 1.0419 1.0419 1.0419 0.0000  0.0000  0.0000  640  LYS A C   
5147  O O   . LYS B 643  ? 1.0419 1.0419 1.0419 0.0000  0.0000  0.0000  640  LYS A O   
5148  C CB  . LYS B 643  ? 1.0419 1.0419 1.0419 0.0000  0.0000  0.0000  640  LYS A CB  
5149  C CG  . LYS B 643  ? 1.0419 1.0419 1.0419 0.0000  0.0000  0.0000  640  LYS A CG  
5150  C CD  . LYS B 643  ? 1.0419 1.0419 1.0419 0.0000  0.0000  0.0000  640  LYS A CD  
5151  C CE  . LYS B 643  ? 1.0419 1.0419 1.0419 0.0000  0.0000  0.0000  640  LYS A CE  
5152  N NZ  . LYS B 643  ? 1.0419 1.0419 1.0419 0.0000  0.0000  0.0000  640  LYS A NZ  
5153  N N   . GLU B 644  ? 1.0413 1.0413 1.0413 0.0000  0.0000  0.0000  641  GLU A N   
5154  C CA  . GLU B 644  ? 1.0413 1.0413 1.0413 0.0000  0.0000  0.0000  641  GLU A CA  
5155  C C   . GLU B 644  ? 1.0413 1.0413 1.0413 0.0000  0.0000  0.0000  641  GLU A C   
5156  O O   . GLU B 644  ? 1.0413 1.0413 1.0413 0.0000  0.0000  0.0000  641  GLU A O   
5157  C CB  . GLU B 644  ? 1.0413 1.0413 1.0413 0.0000  0.0000  0.0000  641  GLU A CB  
5158  C CG  . GLU B 644  ? 1.0413 1.0413 1.0413 0.0000  0.0000  0.0000  641  GLU A CG  
5159  C CD  . GLU B 644  ? 1.0413 1.0413 1.0413 0.0000  0.0000  0.0000  641  GLU A CD  
5160  O OE1 . GLU B 644  ? 1.0413 1.0413 1.0413 0.0000  0.0000  0.0000  641  GLU A OE1 
5161  O OE2 . GLU B 644  ? 1.0413 1.0413 1.0413 0.0000  0.0000  0.0000  641  GLU A OE2 
5162  N N   . ILE B 645  ? 1.0312 1.0312 1.0312 0.0000  0.0000  0.0000  642  ILE A N   
5163  C CA  . ILE B 645  ? 1.0312 1.0312 1.0312 0.0000  0.0000  0.0000  642  ILE A CA  
5164  C C   . ILE B 645  ? 1.0312 1.0312 1.0312 0.0000  0.0000  0.0000  642  ILE A C   
5165  O O   . ILE B 645  ? 1.0312 1.0312 1.0312 0.0000  0.0000  0.0000  642  ILE A O   
5166  C CB  . ILE B 645  ? 1.0312 1.0312 1.0312 0.0000  0.0000  0.0000  642  ILE A CB  
5167  C CG1 . ILE B 645  ? 1.0312 1.0312 1.0312 0.0000  0.0000  0.0000  642  ILE A CG1 
5168  C CG2 . ILE B 645  ? 1.0312 1.0312 1.0312 0.0000  0.0000  0.0000  642  ILE A CG2 
5169  C CD1 . ILE B 645  ? 1.0312 1.0312 1.0312 0.0000  0.0000  0.0000  642  ILE A CD1 
5170  N N   . TYR B 646  ? 1.0427 1.0427 1.0427 0.0000  0.0000  0.0000  643  TYR A N   
5171  C CA  . TYR B 646  ? 1.0427 1.0427 1.0427 0.0000  0.0000  0.0000  643  TYR A CA  
5172  C C   . TYR B 646  ? 1.0427 1.0427 1.0427 0.0000  0.0000  0.0000  643  TYR A C   
5173  O O   . TYR B 646  ? 1.0427 1.0427 1.0427 0.0000  0.0000  0.0000  643  TYR A O   
5174  C CB  . TYR B 646  ? 1.0427 1.0427 1.0427 0.0000  0.0000  0.0000  643  TYR A CB  
5175  C CG  . TYR B 646  ? 1.0427 1.0427 1.0427 0.0000  0.0000  0.0000  643  TYR A CG  
5176  C CD1 . TYR B 646  ? 1.0427 1.0427 1.0427 0.0000  0.0000  0.0000  643  TYR A CD1 
5177  C CD2 . TYR B 646  ? 1.0427 1.0427 1.0427 0.0000  0.0000  0.0000  643  TYR A CD2 
5178  C CE1 . TYR B 646  ? 1.0427 1.0427 1.0427 0.0000  0.0000  0.0000  643  TYR A CE1 
5179  C CE2 . TYR B 646  ? 1.0427 1.0427 1.0427 0.0000  0.0000  0.0000  643  TYR A CE2 
5180  C CZ  . TYR B 646  ? 1.0427 1.0427 1.0427 0.0000  0.0000  0.0000  643  TYR A CZ  
5181  O OH  . TYR B 646  ? 1.0427 1.0427 1.0427 0.0000  0.0000  0.0000  643  TYR A OH  
5182  N N   . ASP B 647  ? 1.0936 1.0936 1.0936 0.0000  0.0000  0.0000  644  ASP A N   
5183  C CA  . ASP B 647  ? 1.0936 1.0936 1.0936 0.0000  0.0000  0.0000  644  ASP A CA  
5184  C C   . ASP B 647  ? 1.0936 1.0936 1.0936 0.0000  0.0000  0.0000  644  ASP A C   
5185  O O   . ASP B 647  ? 1.0936 1.0936 1.0936 0.0000  0.0000  0.0000  644  ASP A O   
5186  C CB  . ASP B 647  ? 1.0936 1.0936 1.0936 0.0000  0.0000  0.0000  644  ASP A CB  
5187  C CG  . ASP B 647  ? 1.0936 1.0936 1.0936 0.0000  0.0000  0.0000  644  ASP A CG  
5188  O OD1 . ASP B 647  ? 1.0936 1.0936 1.0936 0.0000  0.0000  0.0000  644  ASP A OD1 
5189  O OD2 . ASP B 647  ? 1.0936 1.0936 1.0936 0.0000  0.0000  0.0000  644  ASP A OD2 
5190  N N   . LEU B 648  ? 1.0728 1.0728 1.0728 0.0000  0.0000  0.0000  645  LEU A N   
5191  C CA  . LEU B 648  ? 1.0728 1.0728 1.0728 0.0000  0.0000  0.0000  645  LEU A CA  
5192  C C   . LEU B 648  ? 1.0728 1.0728 1.0728 0.0000  0.0000  0.0000  645  LEU A C   
5193  O O   . LEU B 648  ? 1.0728 1.0728 1.0728 0.0000  0.0000  0.0000  645  LEU A O   
5194  C CB  . LEU B 648  ? 1.0728 1.0728 1.0728 0.0000  0.0000  0.0000  645  LEU A CB  
5195  C CG  . LEU B 648  ? 1.0728 1.0728 1.0728 0.0000  0.0000  0.0000  645  LEU A CG  
5196  C CD1 . LEU B 648  ? 1.0728 1.0728 1.0728 0.0000  0.0000  0.0000  645  LEU A CD1 
5197  C CD2 . LEU B 648  ? 1.0728 1.0728 1.0728 0.0000  0.0000  0.0000  645  LEU A CD2 
5198  N N   . ASN B 649  ? 1.0568 1.0568 1.0568 0.0000  0.0000  0.0000  646  ASN A N   
5199  C CA  . ASN B 649  ? 1.0568 1.0568 1.0568 0.0000  0.0000  0.0000  646  ASN A CA  
5200  C C   . ASN B 649  ? 1.0568 1.0568 1.0568 0.0000  0.0000  0.0000  646  ASN A C   
5201  O O   . ASN B 649  ? 1.0568 1.0568 1.0568 0.0000  0.0000  0.0000  646  ASN A O   
5202  C CB  . ASN B 649  ? 1.0568 1.0568 1.0568 0.0000  0.0000  0.0000  646  ASN A CB  
5203  C CG  . ASN B 649  ? 1.0568 1.0568 1.0568 0.0000  0.0000  0.0000  646  ASN A CG  
5204  O OD1 . ASN B 649  ? 1.0568 1.0568 1.0568 0.0000  0.0000  0.0000  646  ASN A OD1 
5205  N ND2 . ASN B 649  ? 1.0568 1.0568 1.0568 0.0000  0.0000  0.0000  646  ASN A ND2 
5206  N N   . ASN B 650  ? 1.0752 1.0752 1.0752 0.0000  0.0000  0.0000  647  ASN A N   
5207  C CA  . ASN B 650  ? 1.0752 1.0752 1.0752 0.0000  0.0000  0.0000  647  ASN A CA  
5208  C C   . ASN B 650  ? 1.0752 1.0752 1.0752 0.0000  0.0000  0.0000  647  ASN A C   
5209  O O   . ASN B 650  ? 1.0752 1.0752 1.0752 0.0000  0.0000  0.0000  647  ASN A O   
5210  C CB  . ASN B 650  ? 1.0752 1.0752 1.0752 0.0000  0.0000  0.0000  647  ASN A CB  
5211  C CG  . ASN B 650  ? 1.0752 1.0752 1.0752 0.0000  0.0000  0.0000  647  ASN A CG  
5212  O OD1 . ASN B 650  ? 1.0752 1.0752 1.0752 0.0000  0.0000  0.0000  647  ASN A OD1 
5213  N ND2 . ASN B 650  ? 1.0752 1.0752 1.0752 0.0000  0.0000  0.0000  647  ASN A ND2 
5214  N N   . PRO B 655  ? 1.1461 1.1461 1.1461 0.0000  0.0000  0.0000  652  PRO A N   
5215  C CA  . PRO B 655  ? 1.1461 1.1461 1.1461 0.0000  0.0000  0.0000  652  PRO A CA  
5216  C C   . PRO B 655  ? 1.1461 1.1461 1.1461 0.0000  0.0000  0.0000  652  PRO A C   
5217  O O   . PRO B 655  ? 1.1461 1.1461 1.1461 0.0000  0.0000  0.0000  652  PRO A O   
5218  C CB  . PRO B 655  ? 1.1461 1.1461 1.1461 0.0000  0.0000  0.0000  652  PRO A CB  
5219  C CG  . PRO B 655  ? 1.1461 1.1461 1.1461 0.0000  0.0000  0.0000  652  PRO A CG  
5220  C CD  . PRO B 655  ? 1.1461 1.1461 1.1461 0.0000  0.0000  0.0000  652  PRO A CD  
5221  N N   . LYS B 656  ? 1.1048 1.1048 1.1048 0.0000  0.0000  0.0000  653  LYS A N   
5222  C CA  . LYS B 656  ? 1.1048 1.1048 1.1048 0.0000  0.0000  0.0000  653  LYS A CA  
5223  C C   . LYS B 656  ? 1.1048 1.1048 1.1048 0.0000  0.0000  0.0000  653  LYS A C   
5224  O O   . LYS B 656  ? 1.1048 1.1048 1.1048 0.0000  0.0000  0.0000  653  LYS A O   
5225  C CB  . LYS B 656  ? 1.1048 1.1048 1.1048 0.0000  0.0000  0.0000  653  LYS A CB  
5226  C CG  . LYS B 656  ? 1.1048 1.1048 1.1048 0.0000  0.0000  0.0000  653  LYS A CG  
5227  C CD  . LYS B 656  ? 1.1048 1.1048 1.1048 0.0000  0.0000  0.0000  653  LYS A CD  
5228  C CE  . LYS B 656  ? 1.1048 1.1048 1.1048 0.0000  0.0000  0.0000  653  LYS A CE  
5229  N NZ  . LYS B 656  ? 1.1048 1.1048 1.1048 0.0000  0.0000  0.0000  653  LYS A NZ  
5230  N N   . LYS B 657  ? 1.1546 1.1546 1.1546 0.0000  0.0000  0.0000  654  LYS A N   
5231  C CA  . LYS B 657  ? 1.1546 1.1546 1.1546 0.0000  0.0000  0.0000  654  LYS A CA  
5232  C C   . LYS B 657  ? 1.1546 1.1546 1.1546 0.0000  0.0000  0.0000  654  LYS A C   
5233  O O   . LYS B 657  ? 1.1546 1.1546 1.1546 0.0000  0.0000  0.0000  654  LYS A O   
5234  C CB  . LYS B 657  ? 1.1546 1.1546 1.1546 0.0000  0.0000  0.0000  654  LYS A CB  
5235  C CG  . LYS B 657  ? 1.1546 1.1546 1.1546 0.0000  0.0000  0.0000  654  LYS A CG  
5236  C CD  . LYS B 657  ? 1.1546 1.1546 1.1546 0.0000  0.0000  0.0000  654  LYS A CD  
5237  C CE  . LYS B 657  ? 1.1546 1.1546 1.1546 0.0000  0.0000  0.0000  654  LYS A CE  
5238  N NZ  . LYS B 657  ? 1.1546 1.1546 1.1546 0.0000  0.0000  0.0000  654  LYS A NZ  
5239  N N   . PHE B 658  ? 1.0815 1.0815 1.0815 0.0000  0.0000  0.0000  655  PHE A N   
5240  C CA  . PHE B 658  ? 1.0815 1.0815 1.0815 0.0000  0.0000  0.0000  655  PHE A CA  
5241  C C   . PHE B 658  ? 1.0815 1.0815 1.0815 0.0000  0.0000  0.0000  655  PHE A C   
5242  O O   . PHE B 658  ? 1.0815 1.0815 1.0815 0.0000  0.0000  0.0000  655  PHE A O   
5243  C CB  . PHE B 658  ? 1.0815 1.0815 1.0815 0.0000  0.0000  0.0000  655  PHE A CB  
5244  C CG  . PHE B 658  ? 1.0815 1.0815 1.0815 0.0000  0.0000  0.0000  655  PHE A CG  
5245  C CD1 . PHE B 658  ? 1.0815 1.0815 1.0815 0.0000  0.0000  0.0000  655  PHE A CD1 
5246  C CD2 . PHE B 658  ? 1.0815 1.0815 1.0815 0.0000  0.0000  0.0000  655  PHE A CD2 
5247  C CE1 . PHE B 658  ? 1.0815 1.0815 1.0815 0.0000  0.0000  0.0000  655  PHE A CE1 
5248  C CE2 . PHE B 658  ? 1.0815 1.0815 1.0815 0.0000  0.0000  0.0000  655  PHE A CE2 
5249  C CZ  . PHE B 658  ? 1.0815 1.0815 1.0815 0.0000  0.0000  0.0000  655  PHE A CZ  
5250  N N   . GLN B 659  ? 1.1368 1.1368 1.1368 0.0000  0.0000  0.0000  656  GLN A N   
5251  C CA  . GLN B 659  ? 1.1368 1.1368 1.1368 0.0000  0.0000  0.0000  656  GLN A CA  
5252  C C   . GLN B 659  ? 1.1368 1.1368 1.1368 0.0000  0.0000  0.0000  656  GLN A C   
5253  O O   . GLN B 659  ? 1.1368 1.1368 1.1368 0.0000  0.0000  0.0000  656  GLN A O   
5254  C CB  . GLN B 659  ? 1.1368 1.1368 1.1368 0.0000  0.0000  0.0000  656  GLN A CB  
5255  C CG  . GLN B 659  ? 1.1368 1.1368 1.1368 0.0000  0.0000  0.0000  656  GLN A CG  
5256  C CD  . GLN B 659  ? 1.1368 1.1368 1.1368 0.0000  0.0000  0.0000  656  GLN A CD  
5257  O OE1 . GLN B 659  ? 1.1368 1.1368 1.1368 0.0000  0.0000  0.0000  656  GLN A OE1 
5258  N NE2 . GLN B 659  ? 1.1368 1.1368 1.1368 0.0000  0.0000  0.0000  656  GLN A NE2 
5259  N N   . THR B 660  ? 1.1791 1.1791 1.1791 0.0000  0.0000  0.0000  657  THR A N   
5260  C CA  . THR B 660  ? 1.1791 1.1791 1.1791 0.0000  0.0000  0.0000  657  THR A CA  
5261  C C   . THR B 660  ? 1.1791 1.1791 1.1791 0.0000  0.0000  0.0000  657  THR A C   
5262  O O   . THR B 660  ? 1.1791 1.1791 1.1791 0.0000  0.0000  0.0000  657  THR A O   
5263  C CB  . THR B 660  ? 1.1791 1.1791 1.1791 0.0000  0.0000  0.0000  657  THR A CB  
5264  O OG1 . THR B 660  ? 1.1791 1.1791 1.1791 0.0000  0.0000  0.0000  657  THR A OG1 
5265  C CG2 . THR B 660  ? 1.1791 1.1791 1.1791 0.0000  0.0000  0.0000  657  THR A CG2 
5266  N N   . ALA B 661  ? 1.1828 1.1828 1.1828 0.0000  0.0000  0.0000  658  ALA A N   
5267  C CA  . ALA B 661  ? 1.1828 1.1828 1.1828 0.0000  0.0000  0.0000  658  ALA A CA  
5268  C C   . ALA B 661  ? 1.1828 1.1828 1.1828 0.0000  0.0000  0.0000  658  ALA A C   
5269  O O   . ALA B 661  ? 1.1828 1.1828 1.1828 0.0000  0.0000  0.0000  658  ALA A O   
5270  C CB  . ALA B 661  ? 1.1828 1.1828 1.1828 0.0000  0.0000  0.0000  658  ALA A CB  
5271  N N   . TYR B 662  ? 1.1745 1.1745 1.1745 0.0000  0.0000  0.0000  659  TYR A N   
5272  C CA  . TYR B 662  ? 1.1745 1.1745 1.1745 0.0000  0.0000  0.0000  659  TYR A CA  
5273  C C   . TYR B 662  ? 1.1745 1.1745 1.1745 0.0000  0.0000  0.0000  659  TYR A C   
5274  O O   . TYR B 662  ? 1.1745 1.1745 1.1745 0.0000  0.0000  0.0000  659  TYR A O   
5275  C CB  . TYR B 662  ? 1.1745 1.1745 1.1745 0.0000  0.0000  0.0000  659  TYR A CB  
5276  C CG  . TYR B 662  ? 1.1745 1.1745 1.1745 0.0000  0.0000  0.0000  659  TYR A CG  
5277  C CD1 . TYR B 662  ? 1.1745 1.1745 1.1745 0.0000  0.0000  0.0000  659  TYR A CD1 
5278  C CD2 . TYR B 662  ? 1.1745 1.1745 1.1745 0.0000  0.0000  0.0000  659  TYR A CD2 
5279  C CE1 . TYR B 662  ? 1.1745 1.1745 1.1745 0.0000  0.0000  0.0000  659  TYR A CE1 
5280  C CE2 . TYR B 662  ? 1.1745 1.1745 1.1745 0.0000  0.0000  0.0000  659  TYR A CE2 
5281  C CZ  . TYR B 662  ? 1.1745 1.1745 1.1745 0.0000  0.0000  0.0000  659  TYR A CZ  
5282  O OH  . TYR B 662  ? 1.1745 1.1745 1.1745 0.0000  0.0000  0.0000  659  TYR A OH  
5283  N N   . ALA B 663  ? 1.2194 1.2194 1.2194 0.0000  0.0000  0.0000  660  ALA A N   
5284  C CA  . ALA B 663  ? 1.2194 1.2194 1.2194 0.0000  0.0000  0.0000  660  ALA A CA  
5285  C C   . ALA B 663  ? 1.2194 1.2194 1.2194 0.0000  0.0000  0.0000  660  ALA A C   
5286  O O   . ALA B 663  ? 1.2194 1.2194 1.2194 0.0000  0.0000  0.0000  660  ALA A O   
5287  C CB  . ALA B 663  ? 1.2194 1.2194 1.2194 0.0000  0.0000  0.0000  660  ALA A CB  
5288  N N   . LYS B 664  ? 1.2114 1.2114 1.2114 0.0000  0.0000  0.0000  661  LYS A N   
5289  C CA  . LYS B 664  ? 1.2114 1.2114 1.2114 0.0000  0.0000  0.0000  661  LYS A CA  
5290  C C   . LYS B 664  ? 1.2114 1.2114 1.2114 0.0000  0.0000  0.0000  661  LYS A C   
5291  O O   . LYS B 664  ? 1.2114 1.2114 1.2114 0.0000  0.0000  0.0000  661  LYS A O   
5292  C CB  . LYS B 664  ? 1.2114 1.2114 1.2114 0.0000  0.0000  0.0000  661  LYS A CB  
5293  C CG  . LYS B 664  ? 1.2114 1.2114 1.2114 0.0000  0.0000  0.0000  661  LYS A CG  
5294  C CD  . LYS B 664  ? 1.2114 1.2114 1.2114 0.0000  0.0000  0.0000  661  LYS A CD  
5295  C CE  . LYS B 664  ? 1.2114 1.2114 1.2114 0.0000  0.0000  0.0000  661  LYS A CE  
5296  N NZ  . LYS B 664  ? 1.2114 1.2114 1.2114 0.0000  0.0000  0.0000  661  LYS A NZ  
5297  N N   . LYS B 665  ? 1.1919 1.1919 1.1919 0.0000  0.0000  0.0000  662  LYS A N   
5298  C CA  . LYS B 665  ? 1.1919 1.1919 1.1919 0.0000  0.0000  0.0000  662  LYS A CA  
5299  C C   . LYS B 665  ? 1.1919 1.1919 1.1919 0.0000  0.0000  0.0000  662  LYS A C   
5300  O O   . LYS B 665  ? 1.1919 1.1919 1.1919 0.0000  0.0000  0.0000  662  LYS A O   
5301  C CB  . LYS B 665  ? 1.1919 1.1919 1.1919 0.0000  0.0000  0.0000  662  LYS A CB  
5302  C CG  . LYS B 665  ? 1.1919 1.1919 1.1919 0.0000  0.0000  0.0000  662  LYS A CG  
5303  C CD  . LYS B 665  ? 1.1919 1.1919 1.1919 0.0000  0.0000  0.0000  662  LYS A CD  
5304  C CE  . LYS B 665  ? 1.1919 1.1919 1.1919 0.0000  0.0000  0.0000  662  LYS A CE  
5305  N NZ  . LYS B 665  ? 1.1919 1.1919 1.1919 0.0000  0.0000  0.0000  662  LYS A NZ  
5306  N N   . THR B 666  ? 1.2332 1.2332 1.2332 0.0000  0.0000  0.0000  663  THR A N   
5307  C CA  . THR B 666  ? 1.2332 1.2332 1.2332 0.0000  0.0000  0.0000  663  THR A CA  
5308  C C   . THR B 666  ? 1.2332 1.2332 1.2332 0.0000  0.0000  0.0000  663  THR A C   
5309  O O   . THR B 666  ? 1.2332 1.2332 1.2332 0.0000  0.0000  0.0000  663  THR A O   
5310  C CB  . THR B 666  ? 1.2332 1.2332 1.2332 0.0000  0.0000  0.0000  663  THR A CB  
5311  O OG1 . THR B 666  ? 1.2332 1.2332 1.2332 0.0000  0.0000  0.0000  663  THR A OG1 
5312  C CG2 . THR B 666  ? 1.2332 1.2332 1.2332 0.0000  0.0000  0.0000  663  THR A CG2 
5313  N N   . GLY B 667  ? 1.2249 1.2249 1.2249 0.0000  0.0000  0.0000  664  GLY A N   
5314  C CA  . GLY B 667  ? 1.2249 1.2249 1.2249 0.0000  0.0000  0.0000  664  GLY A CA  
5315  C C   . GLY B 667  ? 1.2249 1.2249 1.2249 0.0000  0.0000  0.0000  664  GLY A C   
5316  O O   . GLY B 667  ? 1.2249 1.2249 1.2249 0.0000  0.0000  0.0000  664  GLY A O   
5317  N N   . ASP B 668  ? 1.2140 1.2140 1.2140 0.0000  0.0000  0.0000  665  ASP A N   
5318  C CA  . ASP B 668  ? 1.2140 1.2140 1.2140 0.0000  0.0000  0.0000  665  ASP A CA  
5319  C C   . ASP B 668  ? 1.2140 1.2140 1.2140 0.0000  0.0000  0.0000  665  ASP A C   
5320  O O   . ASP B 668  ? 1.2140 1.2140 1.2140 0.0000  0.0000  0.0000  665  ASP A O   
5321  C CB  . ASP B 668  ? 1.2140 1.2140 1.2140 0.0000  0.0000  0.0000  665  ASP A CB  
5322  C CG  . ASP B 668  ? 1.2140 1.2140 1.2140 0.0000  0.0000  0.0000  665  ASP A CG  
5323  O OD1 . ASP B 668  ? 1.2140 1.2140 1.2140 0.0000  0.0000  0.0000  665  ASP A OD1 
5324  O OD2 . ASP B 668  ? 1.2140 1.2140 1.2140 0.0000  0.0000  0.0000  665  ASP A OD2 
5325  N N   . GLN B 669  ? 1.2018 1.2018 1.2018 0.0000  0.0000  0.0000  666  GLN A N   
5326  C CA  . GLN B 669  ? 1.2018 1.2018 1.2018 0.0000  0.0000  0.0000  666  GLN A CA  
5327  C C   . GLN B 669  ? 1.2018 1.2018 1.2018 0.0000  0.0000  0.0000  666  GLN A C   
5328  O O   . GLN B 669  ? 1.2018 1.2018 1.2018 0.0000  0.0000  0.0000  666  GLN A O   
5329  C CB  . GLN B 669  ? 1.2018 1.2018 1.2018 0.0000  0.0000  0.0000  666  GLN A CB  
5330  C CG  . GLN B 669  ? 1.2018 1.2018 1.2018 0.0000  0.0000  0.0000  666  GLN A CG  
5331  C CD  . GLN B 669  ? 1.2018 1.2018 1.2018 0.0000  0.0000  0.0000  666  GLN A CD  
5332  O OE1 . GLN B 669  ? 1.2018 1.2018 1.2018 0.0000  0.0000  0.0000  666  GLN A OE1 
5333  N NE2 . GLN B 669  ? 1.2018 1.2018 1.2018 0.0000  0.0000  0.0000  666  GLN A NE2 
5334  N N   . LYS B 670  ? 1.1819 1.1819 1.1819 0.0000  0.0000  0.0000  667  LYS A N   
5335  C CA  . LYS B 670  ? 1.1819 1.1819 1.1819 0.0000  0.0000  0.0000  667  LYS A CA  
5336  C C   . LYS B 670  ? 1.1819 1.1819 1.1819 0.0000  0.0000  0.0000  667  LYS A C   
5337  O O   . LYS B 670  ? 1.1819 1.1819 1.1819 0.0000  0.0000  0.0000  667  LYS A O   
5343  N N   . GLY B 671  ? 1.1335 1.1335 1.1335 0.0000  0.0000  0.0000  668  GLY A N   
5344  C CA  . GLY B 671  ? 1.1335 1.1335 1.1335 0.0000  0.0000  0.0000  668  GLY A CA  
5345  C C   . GLY B 671  ? 1.1335 1.1335 1.1335 0.0000  0.0000  0.0000  668  GLY A C   
5346  O O   . GLY B 671  ? 1.1335 1.1335 1.1335 0.0000  0.0000  0.0000  668  GLY A O   
5347  N N   . TYR B 672  ? 1.1466 1.1466 1.1466 0.0000  0.0000  0.0000  669  TYR A N   
5348  C CA  . TYR B 672  ? 1.1466 1.1466 1.1466 0.0000  0.0000  0.0000  669  TYR A CA  
5349  C C   . TYR B 672  ? 1.1466 1.1466 1.1466 0.0000  0.0000  0.0000  669  TYR A C   
5350  O O   . TYR B 672  ? 1.1466 1.1466 1.1466 0.0000  0.0000  0.0000  669  TYR A O   
5351  C CB  . TYR B 672  ? 1.1466 1.1466 1.1466 0.0000  0.0000  0.0000  669  TYR A CB  
5352  C CG  . TYR B 672  ? 1.1466 1.1466 1.1466 0.0000  0.0000  0.0000  669  TYR A CG  
5353  C CD1 . TYR B 672  ? 1.1466 1.1466 1.1466 0.0000  0.0000  0.0000  669  TYR A CD1 
5354  C CD2 . TYR B 672  ? 1.1466 1.1466 1.1466 0.0000  0.0000  0.0000  669  TYR A CD2 
5355  C CE1 . TYR B 672  ? 1.1466 1.1466 1.1466 0.0000  0.0000  0.0000  669  TYR A CE1 
5356  C CE2 . TYR B 672  ? 1.1466 1.1466 1.1466 0.0000  0.0000  0.0000  669  TYR A CE2 
5357  C CZ  . TYR B 672  ? 1.1466 1.1466 1.1466 0.0000  0.0000  0.0000  669  TYR A CZ  
5358  O OH  . TYR B 672  ? 1.1466 1.1466 1.1466 0.0000  0.0000  0.0000  669  TYR A OH  
5359  N N   . ARG B 673  ? 1.1094 1.1094 1.1094 0.0000  0.0000  0.0000  670  ARG A N   
5360  C CA  . ARG B 673  ? 1.1094 1.1094 1.1094 0.0000  0.0000  0.0000  670  ARG A CA  
5361  C C   . ARG B 673  ? 1.1094 1.1094 1.1094 0.0000  0.0000  0.0000  670  ARG A C   
5362  O O   . ARG B 673  ? 1.1094 1.1094 1.1094 0.0000  0.0000  0.0000  670  ARG A O   
5363  C CB  . ARG B 673  ? 1.1094 1.1094 1.1094 0.0000  0.0000  0.0000  670  ARG A CB  
5364  C CG  . ARG B 673  ? 1.1094 1.1094 1.1094 0.0000  0.0000  0.0000  670  ARG A CG  
5365  C CD  . ARG B 673  ? 1.1094 1.1094 1.1094 0.0000  0.0000  0.0000  670  ARG A CD  
5366  N NE  . ARG B 673  ? 1.1094 1.1094 1.1094 0.0000  0.0000  0.0000  670  ARG A NE  
5367  C CZ  . ARG B 673  ? 1.1094 1.1094 1.1094 0.0000  0.0000  0.0000  670  ARG A CZ  
5368  N NH1 . ARG B 673  ? 1.1094 1.1094 1.1094 0.0000  0.0000  0.0000  670  ARG A NH1 
5369  N NH2 . ARG B 673  ? 1.1094 1.1094 1.1094 0.0000  0.0000  0.0000  670  ARG A NH2 
5370  N N   . GLU B 674  ? 1.1434 1.1434 1.1434 0.0000  0.0000  0.0000  671  GLU A N   
5371  C CA  . GLU B 674  ? 1.1434 1.1434 1.1434 0.0000  0.0000  0.0000  671  GLU A CA  
5372  C C   . GLU B 674  ? 1.1434 1.1434 1.1434 0.0000  0.0000  0.0000  671  GLU A C   
5373  O O   . GLU B 674  ? 1.1434 1.1434 1.1434 0.0000  0.0000  0.0000  671  GLU A O   
5374  C CB  . GLU B 674  ? 1.1434 1.1434 1.1434 0.0000  0.0000  0.0000  671  GLU A CB  
5375  C CG  . GLU B 674  ? 1.1434 1.1434 1.1434 0.0000  0.0000  0.0000  671  GLU A CG  
5376  C CD  . GLU B 674  ? 1.1434 1.1434 1.1434 0.0000  0.0000  0.0000  671  GLU A CD  
5377  O OE1 . GLU B 674  ? 1.1434 1.1434 1.1434 0.0000  0.0000  0.0000  671  GLU A OE1 
5378  O OE2 . GLU B 674  ? 1.1434 1.1434 1.1434 0.0000  0.0000  0.0000  671  GLU A OE2 
5379  N N   . ALA B 675  ? 1.0905 1.0905 1.0905 0.0000  0.0000  0.0000  672  ALA A N   
5380  C CA  . ALA B 675  ? 1.0905 1.0905 1.0905 0.0000  0.0000  0.0000  672  ALA A CA  
5381  C C   . ALA B 675  ? 1.0905 1.0905 1.0905 0.0000  0.0000  0.0000  672  ALA A C   
5382  O O   . ALA B 675  ? 1.0905 1.0905 1.0905 0.0000  0.0000  0.0000  672  ALA A O   
5383  C CB  . ALA B 675  ? 1.0905 1.0905 1.0905 0.0000  0.0000  0.0000  672  ALA A CB  
5384  N N   . LEU B 676  ? 1.0514 1.0514 1.0514 0.0000  0.0000  0.0000  673  LEU A N   
5385  C CA  . LEU B 676  ? 1.0514 1.0514 1.0514 0.0000  0.0000  0.0000  673  LEU A CA  
5386  C C   . LEU B 676  ? 1.0514 1.0514 1.0514 0.0000  0.0000  0.0000  673  LEU A C   
5387  O O   . LEU B 676  ? 1.0514 1.0514 1.0514 0.0000  0.0000  0.0000  673  LEU A O   
5388  C CB  . LEU B 676  ? 1.0514 1.0514 1.0514 0.0000  0.0000  0.0000  673  LEU A CB  
5389  C CG  . LEU B 676  ? 1.0514 1.0514 1.0514 0.0000  0.0000  0.0000  673  LEU A CG  
5390  C CD1 . LEU B 676  ? 1.0514 1.0514 1.0514 0.0000  0.0000  0.0000  673  LEU A CD1 
5391  C CD2 . LEU B 676  ? 1.0514 1.0514 1.0514 0.0000  0.0000  0.0000  673  LEU A CD2 
5392  N N   . CYS B 677  ? 1.0912 1.0912 1.0912 0.0000  0.0000  0.0000  674  CYS A N   
5393  C CA  . CYS B 677  ? 1.0912 1.0912 1.0912 0.0000  0.0000  0.0000  674  CYS A CA  
5394  C C   . CYS B 677  ? 1.0912 1.0912 1.0912 0.0000  0.0000  0.0000  674  CYS A C   
5395  O O   . CYS B 677  ? 1.0912 1.0912 1.0912 0.0000  0.0000  0.0000  674  CYS A O   
5396  C CB  . CYS B 677  ? 1.0912 1.0912 1.0912 0.0000  0.0000  0.0000  674  CYS A CB  
5397  S SG  . CYS B 677  ? 1.0912 1.0912 1.0912 0.0000  0.0000  0.0000  674  CYS A SG  
5398  N N   . LYS B 678  ? 1.0340 1.0340 1.0340 0.0000  0.0000  0.0000  675  LYS A N   
5399  C CA  . LYS B 678  ? 1.0340 1.0340 1.0340 0.0000  0.0000  0.0000  675  LYS A CA  
5400  C C   . LYS B 678  ? 1.0340 1.0340 1.0340 0.0000  0.0000  0.0000  675  LYS A C   
5401  O O   . LYS B 678  ? 1.0340 1.0340 1.0340 0.0000  0.0000  0.0000  675  LYS A O   
5402  C CB  . LYS B 678  ? 1.0340 1.0340 1.0340 0.0000  0.0000  0.0000  675  LYS A CB  
5403  C CG  . LYS B 678  ? 1.0340 1.0340 1.0340 0.0000  0.0000  0.0000  675  LYS A CG  
5404  C CD  . LYS B 678  ? 1.0340 1.0340 1.0340 0.0000  0.0000  0.0000  675  LYS A CD  
5405  C CE  . LYS B 678  ? 1.0340 1.0340 1.0340 0.0000  0.0000  0.0000  675  LYS A CE  
5406  N NZ  . LYS B 678  ? 1.0340 1.0340 1.0340 0.0000  0.0000  0.0000  675  LYS A NZ  
5407  N N   . TRP B 679  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  676  TRP A N   
5408  C CA  . TRP B 679  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  676  TRP A CA  
5409  C C   . TRP B 679  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  676  TRP A C   
5410  O O   . TRP B 679  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  676  TRP A O   
5411  C CB  . TRP B 679  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  676  TRP A CB  
5412  C CG  . TRP B 679  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  676  TRP A CG  
5413  C CD1 . TRP B 679  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  676  TRP A CD1 
5414  C CD2 . TRP B 679  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  676  TRP A CD2 
5415  N NE1 . TRP B 679  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  676  TRP A NE1 
5416  C CE2 . TRP B 679  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  676  TRP A CE2 
5417  C CE3 . TRP B 679  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  676  TRP A CE3 
5418  C CZ2 . TRP B 679  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  676  TRP A CZ2 
5419  C CZ3 . TRP B 679  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  676  TRP A CZ3 
5420  C CH2 . TRP B 679  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  676  TRP A CH2 
5421  N N   . ILE B 680  ? 0.9940 0.9940 0.9940 0.0000  0.0000  0.0000  677  ILE A N   
5422  C CA  . ILE B 680  ? 0.9940 0.9940 0.9940 0.0000  0.0000  0.0000  677  ILE A CA  
5423  C C   . ILE B 680  ? 0.9940 0.9940 0.9940 0.0000  0.0000  0.0000  677  ILE A C   
5424  O O   . ILE B 680  ? 0.9940 0.9940 0.9940 0.0000  0.0000  0.0000  677  ILE A O   
5425  C CB  . ILE B 680  ? 0.9940 0.9940 0.9940 0.0000  0.0000  0.0000  677  ILE A CB  
5426  C CG1 . ILE B 680  ? 0.9940 0.9940 0.9940 0.0000  0.0000  0.0000  677  ILE A CG1 
5427  C CG2 . ILE B 680  ? 0.9940 0.9940 0.9940 0.0000  0.0000  0.0000  677  ILE A CG2 
5428  C CD1 . ILE B 680  ? 0.9940 0.9940 0.9940 0.0000  0.0000  0.0000  677  ILE A CD1 
5429  N N   . ASP B 681  ? 0.9930 0.9930 0.9930 0.0000  0.0000  0.0000  678  ASP A N   
5430  C CA  . ASP B 681  ? 0.9930 0.9930 0.9930 0.0000  0.0000  0.0000  678  ASP A CA  
5431  C C   . ASP B 681  ? 0.9930 0.9930 0.9930 0.0000  0.0000  0.0000  678  ASP A C   
5432  O O   . ASP B 681  ? 0.9930 0.9930 0.9930 0.0000  0.0000  0.0000  678  ASP A O   
5433  C CB  . ASP B 681  ? 0.9930 0.9930 0.9930 0.0000  0.0000  0.0000  678  ASP A CB  
5434  C CG  . ASP B 681  ? 0.9930 0.9930 0.9930 0.0000  0.0000  0.0000  678  ASP A CG  
5435  O OD1 . ASP B 681  ? 0.9930 0.9930 0.9930 0.0000  0.0000  0.0000  678  ASP A OD1 
5436  O OD2 . ASP B 681  ? 0.9930 0.9930 0.9930 0.0000  0.0000  0.0000  678  ASP A OD2 
5437  N N   . PHE B 682  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  679  PHE A N   
5438  C CA  . PHE B 682  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  679  PHE A CA  
5439  C C   . PHE B 682  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  679  PHE A C   
5440  O O   . PHE B 682  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  679  PHE A O   
5441  C CB  . PHE B 682  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  679  PHE A CB  
5442  C CG  . PHE B 682  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  679  PHE A CG  
5443  C CD1 . PHE B 682  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  679  PHE A CD1 
5444  C CD2 . PHE B 682  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  679  PHE A CD2 
5445  C CE1 . PHE B 682  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  679  PHE A CE1 
5446  C CE2 . PHE B 682  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  679  PHE A CE2 
5447  C CZ  . PHE B 682  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  679  PHE A CZ  
5448  N N   . THR B 683  ? 0.9213 0.9213 0.9213 0.0000  0.0000  0.0000  680  THR A N   
5449  C CA  . THR B 683  ? 0.9213 0.9213 0.9213 0.0000  0.0000  0.0000  680  THR A CA  
5450  C C   . THR B 683  ? 0.9213 0.9213 0.9213 0.0000  0.0000  0.0000  680  THR A C   
5451  O O   . THR B 683  ? 0.9213 0.9213 0.9213 0.0000  0.0000  0.0000  680  THR A O   
5452  C CB  . THR B 683  ? 0.9213 0.9213 0.9213 0.0000  0.0000  0.0000  680  THR A CB  
5453  O OG1 . THR B 683  ? 0.9213 0.9213 0.9213 0.0000  0.0000  0.0000  680  THR A OG1 
5454  C CG2 . THR B 683  ? 0.9213 0.9213 0.9213 0.0000  0.0000  0.0000  680  THR A CG2 
5455  N N   . ARG B 684  ? 0.9437 0.9437 0.9437 0.0000  0.0000  0.0000  681  ARG A N   
5456  C CA  . ARG B 684  ? 0.9437 0.9437 0.9437 0.0000  0.0000  0.0000  681  ARG A CA  
5457  C C   . ARG B 684  ? 0.9437 0.9437 0.9437 0.0000  0.0000  0.0000  681  ARG A C   
5458  O O   . ARG B 684  ? 0.9437 0.9437 0.9437 0.0000  0.0000  0.0000  681  ARG A O   
5459  C CB  . ARG B 684  ? 0.9437 0.9437 0.9437 0.0000  0.0000  0.0000  681  ARG A CB  
5460  C CG  . ARG B 684  ? 0.9437 0.9437 0.9437 0.0000  0.0000  0.0000  681  ARG A CG  
5461  C CD  . ARG B 684  ? 0.9437 0.9437 0.9437 0.0000  0.0000  0.0000  681  ARG A CD  
5462  N NE  . ARG B 684  ? 0.9437 0.9437 0.9437 0.0000  0.0000  0.0000  681  ARG A NE  
5463  C CZ  . ARG B 684  ? 0.9437 0.9437 0.9437 0.0000  0.0000  0.0000  681  ARG A CZ  
5464  N NH1 . ARG B 684  ? 0.9437 0.9437 0.9437 0.0000  0.0000  0.0000  681  ARG A NH1 
5465  N NH2 . ARG B 684  ? 0.9437 0.9437 0.9437 0.0000  0.0000  0.0000  681  ARG A NH2 
5466  N N   . ASP B 685  ? 0.8971 0.8971 0.8971 0.0000  0.0000  0.0000  682  ASP A N   
5467  C CA  . ASP B 685  ? 0.8971 0.8971 0.8971 0.0000  0.0000  0.0000  682  ASP A CA  
5468  C C   . ASP B 685  ? 0.8971 0.8971 0.8971 0.0000  0.0000  0.0000  682  ASP A C   
5469  O O   . ASP B 685  ? 0.8971 0.8971 0.8971 0.0000  0.0000  0.0000  682  ASP A O   
5470  C CB  . ASP B 685  ? 0.8971 0.8971 0.8971 0.0000  0.0000  0.0000  682  ASP A CB  
5471  C CG  . ASP B 685  ? 0.8971 0.8971 0.8971 0.0000  0.0000  0.0000  682  ASP A CG  
5472  O OD1 . ASP B 685  ? 0.8971 0.8971 0.8971 0.0000  0.0000  0.0000  682  ASP A OD1 
5473  O OD2 . ASP B 685  ? 0.8971 0.8971 0.8971 0.0000  0.0000  0.0000  682  ASP A OD2 
5474  N N   . PHE B 686  ? 0.8166 0.8166 0.8166 0.0000  0.0000  0.0000  683  PHE A N   
5475  C CA  . PHE B 686  ? 0.8166 0.8166 0.8166 0.0000  0.0000  0.0000  683  PHE A CA  
5476  C C   . PHE B 686  ? 0.8166 0.8166 0.8166 0.0000  0.0000  0.0000  683  PHE A C   
5477  O O   . PHE B 686  ? 0.8166 0.8166 0.8166 0.0000  0.0000  0.0000  683  PHE A O   
5478  C CB  . PHE B 686  ? 0.8166 0.8166 0.8166 0.0000  0.0000  0.0000  683  PHE A CB  
5479  C CG  . PHE B 686  ? 0.8166 0.8166 0.8166 0.0000  0.0000  0.0000  683  PHE A CG  
5480  C CD1 . PHE B 686  ? 0.8166 0.8166 0.8166 0.0000  0.0000  0.0000  683  PHE A CD1 
5481  C CD2 . PHE B 686  ? 0.8166 0.8166 0.8166 0.0000  0.0000  0.0000  683  PHE A CD2 
5482  C CE1 . PHE B 686  ? 0.8166 0.8166 0.8166 0.0000  0.0000  0.0000  683  PHE A CE1 
5483  C CE2 . PHE B 686  ? 0.8166 0.8166 0.8166 0.0000  0.0000  0.0000  683  PHE A CE2 
5484  C CZ  . PHE B 686  ? 0.8166 0.8166 0.8166 0.0000  0.0000  0.0000  683  PHE A CZ  
5485  N N   . LEU B 687  ? 0.7657 0.7657 0.7657 0.0000  0.0000  0.0000  684  LEU A N   
5486  C CA  . LEU B 687  ? 0.7657 0.7657 0.7657 0.0000  0.0000  0.0000  684  LEU A CA  
5487  C C   . LEU B 687  ? 0.7657 0.7657 0.7657 0.0000  0.0000  0.0000  684  LEU A C   
5488  O O   . LEU B 687  ? 0.7657 0.7657 0.7657 0.0000  0.0000  0.0000  684  LEU A O   
5489  C CB  . LEU B 687  ? 0.7657 0.7657 0.7657 0.0000  0.0000  0.0000  684  LEU A CB  
5490  C CG  . LEU B 687  ? 0.7657 0.7657 0.7657 0.0000  0.0000  0.0000  684  LEU A CG  
5491  C CD1 . LEU B 687  ? 0.7657 0.7657 0.7657 0.0000  0.0000  0.0000  684  LEU A CD1 
5492  C CD2 . LEU B 687  ? 0.7657 0.7657 0.7657 0.0000  0.0000  0.0000  684  LEU A CD2 
5493  N N   . SER B 688  ? 0.7708 0.7708 0.7708 0.0000  0.0000  0.0000  685  SER A N   
5494  C CA  . SER B 688  ? 0.7708 0.7708 0.7708 0.0000  0.0000  0.0000  685  SER A CA  
5495  C C   . SER B 688  ? 0.7708 0.7708 0.7708 0.0000  0.0000  0.0000  685  SER A C   
5496  O O   . SER B 688  ? 0.7708 0.7708 0.7708 0.0000  0.0000  0.0000  685  SER A O   
5497  C CB  . SER B 688  ? 0.7708 0.7708 0.7708 0.0000  0.0000  0.0000  685  SER A CB  
5498  O OG  . SER B 688  ? 0.7708 0.7708 0.7708 0.0000  0.0000  0.0000  685  SER A OG  
5499  N N   . LYS B 689  ? 0.8159 0.8159 0.8159 0.0000  0.0000  0.0000  686  LYS A N   
5500  C CA  . LYS B 689  ? 0.8159 0.8159 0.8159 0.0000  0.0000  0.0000  686  LYS A CA  
5501  C C   . LYS B 689  ? 0.8159 0.8159 0.8159 0.0000  0.0000  0.0000  686  LYS A C   
5502  O O   . LYS B 689  ? 0.8159 0.8159 0.8159 0.0000  0.0000  0.0000  686  LYS A O   
5503  C CB  . LYS B 689  ? 0.8159 0.8159 0.8159 0.0000  0.0000  0.0000  686  LYS A CB  
5504  C CG  . LYS B 689  ? 0.8159 0.8159 0.8159 0.0000  0.0000  0.0000  686  LYS A CG  
5505  C CD  . LYS B 689  ? 0.8159 0.8159 0.8159 0.0000  0.0000  0.0000  686  LYS A CD  
5506  C CE  . LYS B 689  ? 0.8159 0.8159 0.8159 0.0000  0.0000  0.0000  686  LYS A CE  
5507  N NZ  . LYS B 689  ? 0.8159 0.8159 0.8159 0.0000  0.0000  0.0000  686  LYS A NZ  
5508  N N   . TYR B 690  ? 0.6598 0.6598 0.6598 0.0000  0.0000  0.0000  687  TYR A N   
5509  C CA  . TYR B 690  ? 0.6598 0.6598 0.6598 0.0000  0.0000  0.0000  687  TYR A CA  
5510  C C   . TYR B 690  ? 0.6598 0.6598 0.6598 0.0000  0.0000  0.0000  687  TYR A C   
5511  O O   . TYR B 690  ? 0.6598 0.6598 0.6598 0.0000  0.0000  0.0000  687  TYR A O   
5512  C CB  . TYR B 690  ? 0.6598 0.6598 0.6598 0.0000  0.0000  0.0000  687  TYR A CB  
5513  C CG  . TYR B 690  ? 0.6598 0.6598 0.6598 0.0000  0.0000  0.0000  687  TYR A CG  
5514  C CD1 . TYR B 690  ? 0.6598 0.6598 0.6598 0.0000  0.0000  0.0000  687  TYR A CD1 
5515  C CD2 . TYR B 690  ? 0.6598 0.6598 0.6598 0.0000  0.0000  0.0000  687  TYR A CD2 
5516  C CE1 . TYR B 690  ? 0.6598 0.6598 0.6598 0.0000  0.0000  0.0000  687  TYR A CE1 
5517  C CE2 . TYR B 690  ? 0.6598 0.6598 0.6598 0.0000  0.0000  0.0000  687  TYR A CE2 
5518  C CZ  . TYR B 690  ? 0.6598 0.6598 0.6598 0.0000  0.0000  0.0000  687  TYR A CZ  
5519  O OH  . TYR B 690  ? 0.6598 0.6598 0.6598 0.0000  0.0000  0.0000  687  TYR A OH  
5520  N N   . THR B 691  ? 0.6502 0.6502 0.6502 0.0000  0.0000  0.0000  688  THR A N   
5521  C CA  . THR B 691  ? 0.6502 0.6502 0.6502 0.0000  0.0000  0.0000  688  THR A CA  
5522  C C   . THR B 691  ? 0.6502 0.6502 0.6502 0.0000  0.0000  0.0000  688  THR A C   
5523  O O   . THR B 691  ? 0.6502 0.6502 0.6502 0.0000  0.0000  0.0000  688  THR A O   
5524  C CB  . THR B 691  ? 0.6502 0.6502 0.6502 0.0000  0.0000  0.0000  688  THR A CB  
5525  O OG1 . THR B 691  ? 0.6502 0.6502 0.6502 0.0000  0.0000  0.0000  688  THR A OG1 
5526  C CG2 . THR B 691  ? 0.6502 0.6502 0.6502 0.0000  0.0000  0.0000  688  THR A CG2 
5527  N N   . LYS B 692  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  689  LYS A N   
5528  C CA  . LYS B 692  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  689  LYS A CA  
5529  C C   . LYS B 692  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  689  LYS A C   
5530  O O   . LYS B 692  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  689  LYS A O   
5531  C CB  . LYS B 692  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  689  LYS A CB  
5532  C CG  . LYS B 692  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  689  LYS A CG  
5533  C CD  . LYS B 692  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  689  LYS A CD  
5534  C CE  . LYS B 692  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  689  LYS A CE  
5535  N NZ  . LYS B 692  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  689  LYS A NZ  
5536  N N   . THR B 693  ? 0.7121 0.7121 0.7121 0.0000  0.0000  0.0000  690  THR A N   
5537  C CA  . THR B 693  ? 0.7121 0.7121 0.7121 0.0000  0.0000  0.0000  690  THR A CA  
5538  C C   . THR B 693  ? 0.7121 0.7121 0.7121 0.0000  0.0000  0.0000  690  THR A C   
5539  O O   . THR B 693  ? 0.7121 0.7121 0.7121 0.0000  0.0000  0.0000  690  THR A O   
5540  C CB  . THR B 693  ? 0.7121 0.7121 0.7121 0.0000  0.0000  0.0000  690  THR A CB  
5541  O OG1 . THR B 693  ? 0.7121 0.7121 0.7121 0.0000  0.0000  0.0000  690  THR A OG1 
5542  C CG2 . THR B 693  ? 0.7121 0.7121 0.7121 0.0000  0.0000  0.0000  690  THR A CG2 
5543  N N   . THR B 694  ? 0.6894 0.6894 0.6894 0.0000  0.0000  0.0000  691  THR A N   
5544  C CA  . THR B 694  ? 0.6894 0.6894 0.6894 0.0000  0.0000  0.0000  691  THR A CA  
5545  C C   . THR B 694  ? 0.6894 0.6894 0.6894 0.0000  0.0000  0.0000  691  THR A C   
5546  O O   . THR B 694  ? 0.6894 0.6894 0.6894 0.0000  0.0000  0.0000  691  THR A O   
5547  C CB  . THR B 694  ? 0.6894 0.6894 0.6894 0.0000  0.0000  0.0000  691  THR A CB  
5548  O OG1 . THR B 694  ? 0.6894 0.6894 0.6894 0.0000  0.0000  0.0000  691  THR A OG1 
5549  C CG2 . THR B 694  ? 0.6894 0.6894 0.6894 0.0000  0.0000  0.0000  691  THR A CG2 
5550  N N   . SER B 695  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  692  SER A N   
5551  C CA  . SER B 695  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  692  SER A CA  
5552  C C   . SER B 695  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  692  SER A C   
5553  O O   . SER B 695  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  692  SER A O   
5554  C CB  . SER B 695  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  692  SER A CB  
5555  O OG  . SER B 695  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  692  SER A OG  
5556  N N   . ILE B 696  ? 0.7712 0.7712 0.7712 0.0000  0.0000  0.0000  693  ILE A N   
5557  C CA  . ILE B 696  ? 0.7712 0.7712 0.7712 0.0000  0.0000  0.0000  693  ILE A CA  
5558  C C   . ILE B 696  ? 0.7712 0.7712 0.7712 0.0000  0.0000  0.0000  693  ILE A C   
5559  O O   . ILE B 696  ? 0.7712 0.7712 0.7712 0.0000  0.0000  0.0000  693  ILE A O   
5560  C CB  . ILE B 696  ? 0.7712 0.7712 0.7712 0.0000  0.0000  0.0000  693  ILE A CB  
5561  C CG1 . ILE B 696  ? 0.7712 0.7712 0.7712 0.0000  0.0000  0.0000  693  ILE A CG1 
5562  C CG2 . ILE B 696  ? 0.7712 0.7712 0.7712 0.0000  0.0000  0.0000  693  ILE A CG2 
5563  C CD1 . ILE B 696  ? 0.7712 0.7712 0.7712 0.0000  0.0000  0.0000  693  ILE A CD1 
5564  N N   . ASP B 697  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  694  ASP A N   
5565  C CA  . ASP B 697  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  694  ASP A CA  
5566  C C   . ASP B 697  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  694  ASP A C   
5567  O O   . ASP B 697  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  694  ASP A O   
5568  C CB  . ASP B 697  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  694  ASP A CB  
5569  C CG  . ASP B 697  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  694  ASP A CG  
5570  O OD1 . ASP B 697  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  694  ASP A OD1 
5571  O OD2 . ASP B 697  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  694  ASP A OD2 
5572  N N   . LEU B 698  ? 0.9034 0.9034 0.9034 0.0000  0.0000  0.0000  695  LEU A N   
5573  C CA  . LEU B 698  ? 0.9034 0.9034 0.9034 0.0000  0.0000  0.0000  695  LEU A CA  
5574  C C   . LEU B 698  ? 0.9034 0.9034 0.9034 0.0000  0.0000  0.0000  695  LEU A C   
5575  O O   . LEU B 698  ? 0.9034 0.9034 0.9034 0.0000  0.0000  0.0000  695  LEU A O   
5576  C CB  . LEU B 698  ? 0.9034 0.9034 0.9034 0.0000  0.0000  0.0000  695  LEU A CB  
5577  C CG  . LEU B 698  ? 0.9034 0.9034 0.9034 0.0000  0.0000  0.0000  695  LEU A CG  
5578  C CD1 . LEU B 698  ? 0.9034 0.9034 0.9034 0.0000  0.0000  0.0000  695  LEU A CD1 
5579  C CD2 . LEU B 698  ? 0.9034 0.9034 0.9034 0.0000  0.0000  0.0000  695  LEU A CD2 
5580  N N   . SER B 699  ? 0.9525 0.9525 0.9525 0.0000  0.0000  0.0000  696  SER A N   
5581  C CA  . SER B 699  ? 0.9525 0.9525 0.9525 0.0000  0.0000  0.0000  696  SER A CA  
5582  C C   . SER B 699  ? 0.9525 0.9525 0.9525 0.0000  0.0000  0.0000  696  SER A C   
5583  O O   . SER B 699  ? 0.9525 0.9525 0.9525 0.0000  0.0000  0.0000  696  SER A O   
5584  C CB  . SER B 699  ? 0.9525 0.9525 0.9525 0.0000  0.0000  0.0000  696  SER A CB  
5585  O OG  . SER B 699  ? 0.9525 0.9525 0.9525 0.0000  0.0000  0.0000  696  SER A OG  
5586  N N   . SER B 700  ? 0.9525 0.9525 0.9525 0.0000  0.0000  0.0000  697  SER A N   
5587  C CA  . SER B 700  ? 0.9525 0.9525 0.9525 0.0000  0.0000  0.0000  697  SER A CA  
5588  C C   . SER B 700  ? 0.9525 0.9525 0.9525 0.0000  0.0000  0.0000  697  SER A C   
5589  O O   . SER B 700  ? 0.9525 0.9525 0.9525 0.0000  0.0000  0.0000  697  SER A O   
5590  C CB  . SER B 700  ? 0.9525 0.9525 0.9525 0.0000  0.0000  0.0000  697  SER A CB  
5591  O OG  . SER B 700  ? 0.9525 0.9525 0.9525 0.0000  0.0000  0.0000  697  SER A OG  
5592  N N   . LEU B 701  ? 1.0072 1.0072 1.0072 0.0000  0.0000  0.0000  698  LEU A N   
5593  C CA  . LEU B 701  ? 1.0072 1.0072 1.0072 0.0000  0.0000  0.0000  698  LEU A CA  
5594  C C   . LEU B 701  ? 1.0072 1.0072 1.0072 0.0000  0.0000  0.0000  698  LEU A C   
5595  O O   . LEU B 701  ? 1.0072 1.0072 1.0072 0.0000  0.0000  0.0000  698  LEU A O   
5596  C CB  . LEU B 701  ? 1.0072 1.0072 1.0072 0.0000  0.0000  0.0000  698  LEU A CB  
5597  C CG  . LEU B 701  ? 1.0072 1.0072 1.0072 0.0000  0.0000  0.0000  698  LEU A CG  
5598  C CD1 . LEU B 701  ? 1.0072 1.0072 1.0072 0.0000  0.0000  0.0000  698  LEU A CD1 
5599  C CD2 . LEU B 701  ? 1.0072 1.0072 1.0072 0.0000  0.0000  0.0000  698  LEU A CD2 
5600  N N   . ARG B 702  ? 1.0717 1.0717 1.0717 0.0000  0.0000  0.0000  699  ARG A N   
5601  C CA  . ARG B 702  ? 1.0717 1.0717 1.0717 0.0000  0.0000  0.0000  699  ARG A CA  
5602  C C   . ARG B 702  ? 1.0717 1.0717 1.0717 0.0000  0.0000  0.0000  699  ARG A C   
5603  O O   . ARG B 702  ? 1.0717 1.0717 1.0717 0.0000  0.0000  0.0000  699  ARG A O   
5604  C CB  . ARG B 702  ? 1.0717 1.0717 1.0717 0.0000  0.0000  0.0000  699  ARG A CB  
5605  C CG  . ARG B 702  ? 1.0717 1.0717 1.0717 0.0000  0.0000  0.0000  699  ARG A CG  
5606  C CD  . ARG B 702  ? 1.0717 1.0717 1.0717 0.0000  0.0000  0.0000  699  ARG A CD  
5607  N NE  . ARG B 702  ? 1.0717 1.0717 1.0717 0.0000  0.0000  0.0000  699  ARG A NE  
5608  C CZ  . ARG B 702  ? 1.0717 1.0717 1.0717 0.0000  0.0000  0.0000  699  ARG A CZ  
5609  N NH1 . ARG B 702  ? 1.0717 1.0717 1.0717 0.0000  0.0000  0.0000  699  ARG A NH1 
5610  N NH2 . ARG B 702  ? 1.0717 1.0717 1.0717 0.0000  0.0000  0.0000  699  ARG A NH2 
5611  N N   . PRO B 703  ? 1.1524 1.1524 1.1524 0.0000  0.0000  0.0000  700  PRO A N   
5612  C CA  . PRO B 703  ? 1.1524 1.1524 1.1524 0.0000  0.0000  0.0000  700  PRO A CA  
5613  C C   . PRO B 703  ? 1.1524 1.1524 1.1524 0.0000  0.0000  0.0000  700  PRO A C   
5614  O O   . PRO B 703  ? 1.1524 1.1524 1.1524 0.0000  0.0000  0.0000  700  PRO A O   
5615  C CB  . PRO B 703  ? 1.1524 1.1524 1.1524 0.0000  0.0000  0.0000  700  PRO A CB  
5616  C CG  . PRO B 703  ? 1.1524 1.1524 1.1524 0.0000  0.0000  0.0000  700  PRO A CG  
5617  C CD  . PRO B 703  ? 1.1524 1.1524 1.1524 0.0000  0.0000  0.0000  700  PRO A CD  
5618  N N   . SER B 704  ? 1.1332 1.1332 1.1332 0.0000  0.0000  0.0000  701  SER A N   
5619  C CA  . SER B 704  ? 1.1332 1.1332 1.1332 0.0000  0.0000  0.0000  701  SER A CA  
5620  C C   . SER B 704  ? 1.1332 1.1332 1.1332 0.0000  0.0000  0.0000  701  SER A C   
5621  O O   . SER B 704  ? 1.1332 1.1332 1.1332 0.0000  0.0000  0.0000  701  SER A O   
5622  C CB  . SER B 704  ? 1.1332 1.1332 1.1332 0.0000  0.0000  0.0000  701  SER A CB  
5623  O OG  . SER B 704  ? 1.1332 1.1332 1.1332 0.0000  0.0000  0.0000  701  SER A OG  
5624  N N   . SER B 705  ? 1.1653 1.1653 1.1653 0.0000  0.0000  0.0000  702  SER A N   
5625  C CA  . SER B 705  ? 1.1653 1.1653 1.1653 0.0000  0.0000  0.0000  702  SER A CA  
5626  C C   . SER B 705  ? 1.1653 1.1653 1.1653 0.0000  0.0000  0.0000  702  SER A C   
5627  O O   . SER B 705  ? 1.1653 1.1653 1.1653 0.0000  0.0000  0.0000  702  SER A O   
5628  C CB  . SER B 705  ? 1.1653 1.1653 1.1653 0.0000  0.0000  0.0000  702  SER A CB  
5629  O OG  . SER B 705  ? 1.1653 1.1653 1.1653 0.0000  0.0000  0.0000  702  SER A OG  
5630  N N   . GLN B 706  ? 1.1188 1.1188 1.1188 0.0000  0.0000  0.0000  703  GLN A N   
5631  C CA  . GLN B 706  ? 1.1188 1.1188 1.1188 0.0000  0.0000  0.0000  703  GLN A CA  
5632  C C   . GLN B 706  ? 1.1188 1.1188 1.1188 0.0000  0.0000  0.0000  703  GLN A C   
5633  O O   . GLN B 706  ? 1.1188 1.1188 1.1188 0.0000  0.0000  0.0000  703  GLN A O   
5634  C CB  . GLN B 706  ? 1.1188 1.1188 1.1188 0.0000  0.0000  0.0000  703  GLN A CB  
5635  C CG  . GLN B 706  ? 1.1188 1.1188 1.1188 0.0000  0.0000  0.0000  703  GLN A CG  
5636  C CD  . GLN B 706  ? 1.1188 1.1188 1.1188 0.0000  0.0000  0.0000  703  GLN A CD  
5637  O OE1 . GLN B 706  ? 1.1188 1.1188 1.1188 0.0000  0.0000  0.0000  703  GLN A OE1 
5638  N NE2 . GLN B 706  ? 1.1188 1.1188 1.1188 0.0000  0.0000  0.0000  703  GLN A NE2 
5639  N N   . TYR B 707  ? 1.0933 1.0933 1.0933 0.0000  0.0000  0.0000  704  TYR A N   
5640  C CA  . TYR B 707  ? 1.0933 1.0933 1.0933 0.0000  0.0000  0.0000  704  TYR A CA  
5641  C C   . TYR B 707  ? 1.0933 1.0933 1.0933 0.0000  0.0000  0.0000  704  TYR A C   
5642  O O   . TYR B 707  ? 1.0933 1.0933 1.0933 0.0000  0.0000  0.0000  704  TYR A O   
5643  C CB  . TYR B 707  ? 1.0933 1.0933 1.0933 0.0000  0.0000  0.0000  704  TYR A CB  
5644  C CG  . TYR B 707  ? 1.0933 1.0933 1.0933 0.0000  0.0000  0.0000  704  TYR A CG  
5645  C CD1 . TYR B 707  ? 1.0933 1.0933 1.0933 0.0000  0.0000  0.0000  704  TYR A CD1 
5646  C CD2 . TYR B 707  ? 1.0933 1.0933 1.0933 0.0000  0.0000  0.0000  704  TYR A CD2 
5647  C CE1 . TYR B 707  ? 1.0933 1.0933 1.0933 0.0000  0.0000  0.0000  704  TYR A CE1 
5648  C CE2 . TYR B 707  ? 1.0933 1.0933 1.0933 0.0000  0.0000  0.0000  704  TYR A CE2 
5649  C CZ  . TYR B 707  ? 1.0933 1.0933 1.0933 0.0000  0.0000  0.0000  704  TYR A CZ  
5650  O OH  . TYR B 707  ? 1.0933 1.0933 1.0933 0.0000  0.0000  0.0000  704  TYR A OH  
5651  N N   . LYS B 708  ? 1.0787 1.0787 1.0787 0.0000  0.0000  0.0000  705  LYS A N   
5652  C CA  . LYS B 708  ? 1.0787 1.0787 1.0787 0.0000  0.0000  0.0000  705  LYS A CA  
5653  C C   . LYS B 708  ? 1.0787 1.0787 1.0787 0.0000  0.0000  0.0000  705  LYS A C   
5654  O O   . LYS B 708  ? 1.0787 1.0787 1.0787 0.0000  0.0000  0.0000  705  LYS A O   
5655  C CB  . LYS B 708  ? 1.0787 1.0787 1.0787 0.0000  0.0000  0.0000  705  LYS A CB  
5656  C CG  . LYS B 708  ? 1.0787 1.0787 1.0787 0.0000  0.0000  0.0000  705  LYS A CG  
5657  C CD  . LYS B 708  ? 1.0787 1.0787 1.0787 0.0000  0.0000  0.0000  705  LYS A CD  
5658  C CE  . LYS B 708  ? 1.0787 1.0787 1.0787 0.0000  0.0000  0.0000  705  LYS A CE  
5659  N NZ  . LYS B 708  ? 1.0787 1.0787 1.0787 0.0000  0.0000  0.0000  705  LYS A NZ  
5660  N N   . ASP B 709  ? 1.0574 1.0574 1.0574 0.0000  0.0000  0.0000  706  ASP A N   
5661  C CA  . ASP B 709  ? 1.0574 1.0574 1.0574 0.0000  0.0000  0.0000  706  ASP A CA  
5662  C C   . ASP B 709  ? 1.0574 1.0574 1.0574 0.0000  0.0000  0.0000  706  ASP A C   
5663  O O   . ASP B 709  ? 1.0574 1.0574 1.0574 0.0000  0.0000  0.0000  706  ASP A O   
5664  C CB  . ASP B 709  ? 1.0574 1.0574 1.0574 0.0000  0.0000  0.0000  706  ASP A CB  
5665  C CG  . ASP B 709  ? 1.0574 1.0574 1.0574 0.0000  0.0000  0.0000  706  ASP A CG  
5666  O OD1 . ASP B 709  ? 1.0574 1.0574 1.0574 0.0000  0.0000  0.0000  706  ASP A OD1 
5667  O OD2 . ASP B 709  ? 1.0574 1.0574 1.0574 0.0000  0.0000  0.0000  706  ASP A OD2 
5668  N N   . LEU B 710  ? 1.0457 1.0457 1.0457 0.0000  0.0000  0.0000  707  LEU A N   
5669  C CA  . LEU B 710  ? 1.0457 1.0457 1.0457 0.0000  0.0000  0.0000  707  LEU A CA  
5670  C C   . LEU B 710  ? 1.0457 1.0457 1.0457 0.0000  0.0000  0.0000  707  LEU A C   
5671  O O   . LEU B 710  ? 1.0457 1.0457 1.0457 0.0000  0.0000  0.0000  707  LEU A O   
5672  C CB  . LEU B 710  ? 1.0457 1.0457 1.0457 0.0000  0.0000  0.0000  707  LEU A CB  
5673  C CG  . LEU B 710  ? 1.0457 1.0457 1.0457 0.0000  0.0000  0.0000  707  LEU A CG  
5674  C CD1 . LEU B 710  ? 1.0457 1.0457 1.0457 0.0000  0.0000  0.0000  707  LEU A CD1 
5675  C CD2 . LEU B 710  ? 1.0457 1.0457 1.0457 0.0000  0.0000  0.0000  707  LEU A CD2 
5676  N N   . GLY B 711  ? 1.0365 1.0365 1.0365 0.0000  0.0000  0.0000  708  GLY A N   
5677  C CA  . GLY B 711  ? 1.0365 1.0365 1.0365 0.0000  0.0000  0.0000  708  GLY A CA  
5678  C C   . GLY B 711  ? 1.0365 1.0365 1.0365 0.0000  0.0000  0.0000  708  GLY A C   
5679  O O   . GLY B 711  ? 1.0365 1.0365 1.0365 0.0000  0.0000  0.0000  708  GLY A O   
5680  N N   . GLU B 712  ? 1.0499 1.0499 1.0499 0.0000  0.0000  0.0000  709  GLU A N   
5681  C CA  . GLU B 712  ? 1.0499 1.0499 1.0499 0.0000  0.0000  0.0000  709  GLU A CA  
5682  C C   . GLU B 712  ? 1.0499 1.0499 1.0499 0.0000  0.0000  0.0000  709  GLU A C   
5683  O O   . GLU B 712  ? 1.0499 1.0499 1.0499 0.0000  0.0000  0.0000  709  GLU A O   
5684  C CB  . GLU B 712  ? 1.0499 1.0499 1.0499 0.0000  0.0000  0.0000  709  GLU A CB  
5685  C CG  . GLU B 712  ? 1.0499 1.0499 1.0499 0.0000  0.0000  0.0000  709  GLU A CG  
5686  C CD  . GLU B 712  ? 1.0499 1.0499 1.0499 0.0000  0.0000  0.0000  709  GLU A CD  
5687  O OE1 . GLU B 712  ? 1.0499 1.0499 1.0499 0.0000  0.0000  0.0000  709  GLU A OE1 
5688  O OE2 . GLU B 712  ? 1.0499 1.0499 1.0499 0.0000  0.0000  0.0000  709  GLU A OE2 
5689  N N   . TYR B 713  ? 0.9079 0.9079 0.9079 0.0000  0.0000  0.0000  710  TYR A N   
5690  C CA  . TYR B 713  ? 0.9079 0.9079 0.9079 0.0000  0.0000  0.0000  710  TYR A CA  
5691  C C   . TYR B 713  ? 0.9079 0.9079 0.9079 0.0000  0.0000  0.0000  710  TYR A C   
5692  O O   . TYR B 713  ? 0.9079 0.9079 0.9079 0.0000  0.0000  0.0000  710  TYR A O   
5693  C CB  . TYR B 713  ? 0.9079 0.9079 0.9079 0.0000  0.0000  0.0000  710  TYR A CB  
5694  C CG  . TYR B 713  ? 0.9079 0.9079 0.9079 0.0000  0.0000  0.0000  710  TYR A CG  
5695  C CD1 . TYR B 713  ? 0.9079 0.9079 0.9079 0.0000  0.0000  0.0000  710  TYR A CD1 
5696  C CD2 . TYR B 713  ? 0.9079 0.9079 0.9079 0.0000  0.0000  0.0000  710  TYR A CD2 
5697  C CE1 . TYR B 713  ? 0.9079 0.9079 0.9079 0.0000  0.0000  0.0000  710  TYR A CE1 
5698  C CE2 . TYR B 713  ? 0.9079 0.9079 0.9079 0.0000  0.0000  0.0000  710  TYR A CE2 
5699  C CZ  . TYR B 713  ? 0.9079 0.9079 0.9079 0.0000  0.0000  0.0000  710  TYR A CZ  
5700  O OH  . TYR B 713  ? 0.9079 0.9079 0.9079 0.0000  0.0000  0.0000  710  TYR A OH  
5701  N N   . TYR B 714  ? 0.8974 0.8974 0.8974 0.0000  0.0000  0.0000  711  TYR A N   
5702  C CA  . TYR B 714  ? 0.8974 0.8974 0.8974 0.0000  0.0000  0.0000  711  TYR A CA  
5703  C C   . TYR B 714  ? 0.8974 0.8974 0.8974 0.0000  0.0000  0.0000  711  TYR A C   
5704  O O   . TYR B 714  ? 0.8974 0.8974 0.8974 0.0000  0.0000  0.0000  711  TYR A O   
5705  C CB  . TYR B 714  ? 0.8974 0.8974 0.8974 0.0000  0.0000  0.0000  711  TYR A CB  
5706  C CG  . TYR B 714  ? 0.8974 0.8974 0.8974 0.0000  0.0000  0.0000  711  TYR A CG  
5707  C CD1 . TYR B 714  ? 0.8974 0.8974 0.8974 0.0000  0.0000  0.0000  711  TYR A CD1 
5708  C CD2 . TYR B 714  ? 0.8974 0.8974 0.8974 0.0000  0.0000  0.0000  711  TYR A CD2 
5709  C CE1 . TYR B 714  ? 0.8974 0.8974 0.8974 0.0000  0.0000  0.0000  711  TYR A CE1 
5710  C CE2 . TYR B 714  ? 0.8974 0.8974 0.8974 0.0000  0.0000  0.0000  711  TYR A CE2 
5711  C CZ  . TYR B 714  ? 0.8974 0.8974 0.8974 0.0000  0.0000  0.0000  711  TYR A CZ  
5712  O OH  . TYR B 714  ? 0.8974 0.8974 0.8974 0.0000  0.0000  0.0000  711  TYR A OH  
5713  N N   . ALA B 715  ? 0.8527 0.8527 0.8527 0.0000  0.0000  0.0000  712  ALA A N   
5714  C CA  . ALA B 715  ? 0.8527 0.8527 0.8527 0.0000  0.0000  0.0000  712  ALA A CA  
5715  C C   . ALA B 715  ? 0.8527 0.8527 0.8527 0.0000  0.0000  0.0000  712  ALA A C   
5716  O O   . ALA B 715  ? 0.8527 0.8527 0.8527 0.0000  0.0000  0.0000  712  ALA A O   
5717  C CB  . ALA B 715  ? 0.8527 0.8527 0.8527 0.0000  0.0000  0.0000  712  ALA A CB  
5718  N N   . GLU B 716  ? 0.8528 0.8528 0.8528 0.0000  0.0000  0.0000  713  GLU A N   
5719  C CA  . GLU B 716  ? 0.8528 0.8528 0.8528 0.0000  0.0000  0.0000  713  GLU A CA  
5720  C C   . GLU B 716  ? 0.8528 0.8528 0.8528 0.0000  0.0000  0.0000  713  GLU A C   
5721  O O   . GLU B 716  ? 0.8528 0.8528 0.8528 0.0000  0.0000  0.0000  713  GLU A O   
5722  C CB  . GLU B 716  ? 0.8528 0.8528 0.8528 0.0000  0.0000  0.0000  713  GLU A CB  
5723  C CG  . GLU B 716  ? 0.8528 0.8528 0.8528 0.0000  0.0000  0.0000  713  GLU A CG  
5724  C CD  . GLU B 716  ? 0.8528 0.8528 0.8528 0.0000  0.0000  0.0000  713  GLU A CD  
5725  O OE1 . GLU B 716  ? 0.8528 0.8528 0.8528 0.0000  0.0000  0.0000  713  GLU A OE1 
5726  O OE2 . GLU B 716  ? 0.8528 0.8528 0.8528 0.0000  0.0000  0.0000  713  GLU A OE2 
5727  N N   . LEU B 717  ? 0.7925 0.7925 0.7925 0.0000  0.0000  0.0000  714  LEU A N   
5728  C CA  . LEU B 717  ? 0.7925 0.7925 0.7925 0.0000  0.0000  0.0000  714  LEU A CA  
5729  C C   . LEU B 717  ? 0.7925 0.7925 0.7925 0.0000  0.0000  0.0000  714  LEU A C   
5730  O O   . LEU B 717  ? 0.7925 0.7925 0.7925 0.0000  0.0000  0.0000  714  LEU A O   
5731  C CB  . LEU B 717  ? 0.7925 0.7925 0.7925 0.0000  0.0000  0.0000  714  LEU A CB  
5732  C CG  . LEU B 717  ? 0.7925 0.7925 0.7925 0.0000  0.0000  0.0000  714  LEU A CG  
5733  C CD1 . LEU B 717  ? 0.7925 0.7925 0.7925 0.0000  0.0000  0.0000  714  LEU A CD1 
5734  C CD2 . LEU B 717  ? 0.7925 0.7925 0.7925 0.0000  0.0000  0.0000  714  LEU A CD2 
5735  N N   . ASN B 718  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  715  ASN A N   
5736  C CA  . ASN B 718  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  715  ASN A CA  
5737  C C   . ASN B 718  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  715  ASN A C   
5738  O O   . ASN B 718  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  715  ASN A O   
5739  C CB  . ASN B 718  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  715  ASN A CB  
5740  C CG  . ASN B 718  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  715  ASN A CG  
5741  O OD1 . ASN B 718  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  715  ASN A OD1 
5742  N ND2 . ASN B 718  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  715  ASN A ND2 
5743  N N   . PRO B 719  ? 0.6425 0.6425 0.6425 0.0000  0.0000  0.0000  716  PRO A N   
5744  C CA  . PRO B 719  ? 0.6425 0.6425 0.6425 0.0000  0.0000  0.0000  716  PRO A CA  
5745  C C   . PRO B 719  ? 0.6425 0.6425 0.6425 0.0000  0.0000  0.0000  716  PRO A C   
5746  O O   . PRO B 719  ? 0.6425 0.6425 0.6425 0.0000  0.0000  0.0000  716  PRO A O   
5747  C CB  . PRO B 719  ? 0.6425 0.6425 0.6425 0.0000  0.0000  0.0000  716  PRO A CB  
5748  C CG  . PRO B 719  ? 0.6425 0.6425 0.6425 0.0000  0.0000  0.0000  716  PRO A CG  
5749  C CD  . PRO B 719  ? 0.6425 0.6425 0.6425 0.0000  0.0000  0.0000  716  PRO A CD  
5750  N N   . LEU B 720  ? 0.6330 0.6330 0.6330 0.0000  0.0000  0.0000  717  LEU A N   
5751  C CA  . LEU B 720  ? 0.6330 0.6330 0.6330 0.0000  0.0000  0.0000  717  LEU A CA  
5752  C C   . LEU B 720  ? 0.6330 0.6330 0.6330 0.0000  0.0000  0.0000  717  LEU A C   
5753  O O   . LEU B 720  ? 0.6330 0.6330 0.6330 0.0000  0.0000  0.0000  717  LEU A O   
5754  C CB  . LEU B 720  ? 0.6330 0.6330 0.6330 0.0000  0.0000  0.0000  717  LEU A CB  
5755  C CG  . LEU B 720  ? 0.6330 0.6330 0.6330 0.0000  0.0000  0.0000  717  LEU A CG  
5756  C CD1 . LEU B 720  ? 0.6330 0.6330 0.6330 0.0000  0.0000  0.0000  717  LEU A CD1 
5757  C CD2 . LEU B 720  ? 0.6330 0.6330 0.6330 0.0000  0.0000  0.0000  717  LEU A CD2 
5758  N N   . LEU B 721  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  718  LEU A N   
5759  C CA  . LEU B 721  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  718  LEU A CA  
5760  C C   . LEU B 721  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  718  LEU A C   
5761  O O   . LEU B 721  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  718  LEU A O   
5762  C CB  . LEU B 721  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  718  LEU A CB  
5763  C CG  . LEU B 721  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  718  LEU A CG  
5764  C CD1 . LEU B 721  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  718  LEU A CD1 
5765  C CD2 . LEU B 721  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  718  LEU A CD2 
5766  N N   . TYR B 722  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  719  TYR A N   
5767  C CA  . TYR B 722  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  719  TYR A CA  
5768  C C   . TYR B 722  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  719  TYR A C   
5769  O O   . TYR B 722  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  719  TYR A O   
5770  C CB  . TYR B 722  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  719  TYR A CB  
5771  C CG  . TYR B 722  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  719  TYR A CG  
5772  C CD1 . TYR B 722  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  719  TYR A CD1 
5773  C CD2 . TYR B 722  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  719  TYR A CD2 
5774  C CE1 . TYR B 722  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  719  TYR A CE1 
5775  C CE2 . TYR B 722  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  719  TYR A CE2 
5776  C CZ  . TYR B 722  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  719  TYR A CZ  
5777  O OH  . TYR B 722  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  719  TYR A OH  
5778  N N   . HIS B 723  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  720  HIS A N   
5779  C CA  . HIS B 723  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  720  HIS A CA  
5780  C C   . HIS B 723  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  720  HIS A C   
5781  O O   . HIS B 723  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  720  HIS A O   
5782  C CB  . HIS B 723  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  720  HIS A CB  
5783  C CG  . HIS B 723  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  720  HIS A CG  
5784  N ND1 . HIS B 723  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  720  HIS A ND1 
5785  C CD2 . HIS B 723  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  720  HIS A CD2 
5786  C CE1 . HIS B 723  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  720  HIS A CE1 
5787  N NE2 . HIS B 723  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  720  HIS A NE2 
5788  N N   . ILE B 724  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  721  ILE A N   
5789  C CA  . ILE B 724  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  721  ILE A CA  
5790  C C   . ILE B 724  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  721  ILE A C   
5791  O O   . ILE B 724  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  721  ILE A O   
5792  C CB  . ILE B 724  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  721  ILE A CB  
5793  C CG1 . ILE B 724  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  721  ILE A CG1 
5794  C CG2 . ILE B 724  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  721  ILE A CG2 
5795  C CD1 . ILE B 724  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  721  ILE A CD1 
5796  N N   . SER B 725  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  722  SER A N   
5797  C CA  . SER B 725  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  722  SER A CA  
5798  C C   . SER B 725  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  722  SER A C   
5799  O O   . SER B 725  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  722  SER A O   
5800  C CB  . SER B 725  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  722  SER A CB  
5801  O OG  . SER B 725  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  722  SER A OG  
5802  N N   . PHE B 726  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  723  PHE A N   
5803  C CA  . PHE B 726  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  723  PHE A CA  
5804  C C   . PHE B 726  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  723  PHE A C   
5805  O O   . PHE B 726  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  723  PHE A O   
5806  C CB  . PHE B 726  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  723  PHE A CB  
5807  C CG  . PHE B 726  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  723  PHE A CG  
5808  C CD1 . PHE B 726  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  723  PHE A CD1 
5809  C CD2 . PHE B 726  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  723  PHE A CD2 
5810  C CE1 . PHE B 726  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  723  PHE A CE1 
5811  C CE2 . PHE B 726  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  723  PHE A CE2 
5812  C CZ  . PHE B 726  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  723  PHE A CZ  
5813  N N   . GLN B 727  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  724  GLN A N   
5814  C CA  . GLN B 727  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  724  GLN A CA  
5815  C C   . GLN B 727  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  724  GLN A C   
5816  O O   . GLN B 727  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  724  GLN A O   
5817  C CB  . GLN B 727  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  724  GLN A CB  
5818  C CG  . GLN B 727  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  724  GLN A CG  
5819  C CD  . GLN B 727  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  724  GLN A CD  
5820  O OE1 . GLN B 727  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  724  GLN A OE1 
5821  N NE2 . GLN B 727  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  724  GLN A NE2 
5822  N N   . ARG B 728  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  725  ARG A N   
5823  C CA  . ARG B 728  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  725  ARG A CA  
5824  C C   . ARG B 728  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  725  ARG A C   
5825  O O   . ARG B 728  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  725  ARG A O   
5826  C CB  . ARG B 728  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  725  ARG A CB  
5827  C CG  . ARG B 728  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  725  ARG A CG  
5828  C CD  . ARG B 728  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  725  ARG A CD  
5829  N NE  . ARG B 728  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  725  ARG A NE  
5830  C CZ  . ARG B 728  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  725  ARG A CZ  
5831  N NH1 . ARG B 728  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  725  ARG A NH1 
5832  N NH2 . ARG B 728  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  725  ARG A NH2 
5833  N N   . ILE B 729  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  726  ILE A N   
5834  C CA  . ILE B 729  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  726  ILE A CA  
5835  C C   . ILE B 729  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  726  ILE A C   
5836  O O   . ILE B 729  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  726  ILE A O   
5837  C CB  . ILE B 729  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  726  ILE A CB  
5838  C CG1 . ILE B 729  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  726  ILE A CG1 
5839  C CG2 . ILE B 729  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  726  ILE A CG2 
5840  C CD1 . ILE B 729  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  726  ILE A CD1 
5841  N N   . ALA B 730  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  727  ALA A N   
5842  C CA  . ALA B 730  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  727  ALA A CA  
5843  C C   . ALA B 730  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  727  ALA A C   
5844  O O   . ALA B 730  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  727  ALA A O   
5845  C CB  . ALA B 730  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  727  ALA A CB  
5846  N N   . GLU B 731  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  728  GLU A N   
5847  C CA  . GLU B 731  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  728  GLU A CA  
5848  C C   . GLU B 731  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  728  GLU A C   
5849  O O   . GLU B 731  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  728  GLU A O   
5850  C CB  . GLU B 731  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  728  GLU A CB  
5851  C CG  . GLU B 731  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  728  GLU A CG  
5852  C CD  . GLU B 731  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  728  GLU A CD  
5853  O OE1 . GLU B 731  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  728  GLU A OE1 
5854  O OE2 . GLU B 731  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  728  GLU A OE2 
5855  N N   . LYS B 732  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  729  LYS A N   
5856  C CA  . LYS B 732  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  729  LYS A CA  
5857  C C   . LYS B 732  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  729  LYS A C   
5858  O O   . LYS B 732  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  729  LYS A O   
5864  N N   . GLU B 733  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  730  GLU A N   
5865  C CA  . GLU B 733  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  730  GLU A CA  
5866  C C   . GLU B 733  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  730  GLU A C   
5867  O O   . GLU B 733  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  730  GLU A O   
5868  C CB  . GLU B 733  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  730  GLU A CB  
5869  C CG  . GLU B 733  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  730  GLU A CG  
5870  C CD  . GLU B 733  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  730  GLU A CD  
5871  O OE1 . GLU B 733  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  730  GLU A OE1 
5872  O OE2 . GLU B 733  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  730  GLU A OE2 
5873  N N   . ILE B 734  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  731  ILE A N   
5874  C CA  . ILE B 734  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  731  ILE A CA  
5875  C C   . ILE B 734  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  731  ILE A C   
5876  O O   . ILE B 734  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  731  ILE A O   
5877  C CB  . ILE B 734  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  731  ILE A CB  
5878  C CG1 . ILE B 734  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  731  ILE A CG1 
5879  C CG2 . ILE B 734  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  731  ILE A CG2 
5880  C CD1 . ILE B 734  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  731  ILE A CD1 
5881  N N   . MET B 735  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  732  MET A N   
5882  C CA  . MET B 735  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  732  MET A CA  
5883  C C   . MET B 735  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  732  MET A C   
5884  O O   . MET B 735  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  732  MET A O   
5885  C CB  . MET B 735  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  732  MET A CB  
5886  C CG  . MET B 735  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  732  MET A CG  
5887  S SD  . MET B 735  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  732  MET A SD  
5888  C CE  . MET B 735  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  732  MET A CE  
5889  N N   . ASP B 736  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  733  ASP A N   
5890  C CA  . ASP B 736  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  733  ASP A CA  
5891  C C   . ASP B 736  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  733  ASP A C   
5892  O O   . ASP B 736  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  733  ASP A O   
5893  C CB  . ASP B 736  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  733  ASP A CB  
5894  C CG  . ASP B 736  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  733  ASP A CG  
5895  O OD1 . ASP B 736  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  733  ASP A OD1 
5896  O OD2 . ASP B 736  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  733  ASP A OD2 
5897  N N   . ALA B 737  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  734  ALA A N   
5898  C CA  . ALA B 737  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  734  ALA A CA  
5899  C C   . ALA B 737  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  734  ALA A C   
5900  O O   . ALA B 737  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  734  ALA A O   
5901  C CB  . ALA B 737  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  734  ALA A CB  
5902  N N   . VAL B 738  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  735  VAL A N   
5903  C CA  . VAL B 738  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  735  VAL A CA  
5904  C C   . VAL B 738  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  735  VAL A C   
5905  O O   . VAL B 738  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  735  VAL A O   
5906  C CB  . VAL B 738  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  735  VAL A CB  
5907  C CG1 . VAL B 738  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  735  VAL A CG1 
5908  C CG2 . VAL B 738  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  735  VAL A CG2 
5909  N N   . GLU B 739  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  736  GLU A N   
5910  C CA  . GLU B 739  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  736  GLU A CA  
5911  C C   . GLU B 739  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  736  GLU A C   
5912  O O   . GLU B 739  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  736  GLU A O   
5913  C CB  . GLU B 739  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  736  GLU A CB  
5914  C CG  . GLU B 739  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  736  GLU A CG  
5915  C CD  . GLU B 739  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  736  GLU A CD  
5916  O OE1 . GLU B 739  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  736  GLU A OE1 
5917  O OE2 . GLU B 739  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  736  GLU A OE2 
5918  N N   . THR B 740  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  737  THR A N   
5919  C CA  . THR B 740  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  737  THR A CA  
5920  C C   . THR B 740  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  737  THR A C   
5921  O O   . THR B 740  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  737  THR A O   
5922  C CB  . THR B 740  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  737  THR A CB  
5923  O OG1 . THR B 740  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  737  THR A OG1 
5924  C CG2 . THR B 740  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  737  THR A CG2 
5925  N N   . GLY B 741  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  738  GLY A N   
5926  C CA  . GLY B 741  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  738  GLY A CA  
5927  C C   . GLY B 741  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  738  GLY A C   
5928  O O   . GLY B 741  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  738  GLY A O   
5929  N N   . LYS B 742  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  739  LYS A N   
5930  C CA  . LYS B 742  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  739  LYS A CA  
5931  C C   . LYS B 742  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  739  LYS A C   
5932  O O   . LYS B 742  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  739  LYS A O   
5938  N N   . LEU B 743  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  740  LEU A N   
5939  C CA  . LEU B 743  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  740  LEU A CA  
5940  C C   . LEU B 743  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  740  LEU A C   
5941  O O   . LEU B 743  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  740  LEU A O   
5942  C CB  . LEU B 743  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  740  LEU A CB  
5943  C CG  . LEU B 743  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  740  LEU A CG  
5944  C CD1 . LEU B 743  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  740  LEU A CD1 
5945  C CD2 . LEU B 743  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  740  LEU A CD2 
5946  N N   . TYR B 744  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  741  TYR A N   
5947  C CA  . TYR B 744  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  741  TYR A CA  
5948  C C   . TYR B 744  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  741  TYR A C   
5949  O O   . TYR B 744  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  741  TYR A O   
5950  C CB  . TYR B 744  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  741  TYR A CB  
5951  C CG  . TYR B 744  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  741  TYR A CG  
5952  C CD1 . TYR B 744  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  741  TYR A CD1 
5953  C CD2 . TYR B 744  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  741  TYR A CD2 
5954  C CE1 . TYR B 744  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  741  TYR A CE1 
5955  C CE2 . TYR B 744  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  741  TYR A CE2 
5956  C CZ  . TYR B 744  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  741  TYR A CZ  
5957  O OH  . TYR B 744  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  741  TYR A OH  
5958  N N   . LEU B 745  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  742  LEU A N   
5959  C CA  . LEU B 745  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  742  LEU A CA  
5960  C C   . LEU B 745  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  742  LEU A C   
5961  O O   . LEU B 745  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  742  LEU A O   
5962  C CB  . LEU B 745  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  742  LEU A CB  
5963  C CG  . LEU B 745  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  742  LEU A CG  
5964  C CD1 . LEU B 745  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  742  LEU A CD1 
5965  C CD2 . LEU B 745  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  742  LEU A CD2 
5966  N N   . PHE B 746  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  743  PHE A N   
5967  C CA  . PHE B 746  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  743  PHE A CA  
5968  C C   . PHE B 746  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  743  PHE A C   
5969  O O   . PHE B 746  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  743  PHE A O   
5970  C CB  . PHE B 746  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  743  PHE A CB  
5971  C CG  . PHE B 746  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  743  PHE A CG  
5972  C CD1 . PHE B 746  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  743  PHE A CD1 
5973  C CD2 . PHE B 746  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  743  PHE A CD2 
5974  C CE1 . PHE B 746  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  743  PHE A CE1 
5975  C CE2 . PHE B 746  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  743  PHE A CE2 
5976  C CZ  . PHE B 746  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  743  PHE A CZ  
5977  N N   . GLN B 747  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  744  GLN A N   
5978  C CA  . GLN B 747  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  744  GLN A CA  
5979  C C   . GLN B 747  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  744  GLN A C   
5980  O O   . GLN B 747  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  744  GLN A O   
5981  C CB  . GLN B 747  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  744  GLN A CB  
5982  C CG  . GLN B 747  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  744  GLN A CG  
5983  C CD  . GLN B 747  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  744  GLN A CD  
5984  O OE1 . GLN B 747  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  744  GLN A OE1 
5985  N NE2 . GLN B 747  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  744  GLN A NE2 
5986  N N   . ILE B 748  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  745  ILE A N   
5987  C CA  . ILE B 748  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  745  ILE A CA  
5988  C C   . ILE B 748  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  745  ILE A C   
5989  O O   . ILE B 748  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  745  ILE A O   
5990  C CB  . ILE B 748  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  745  ILE A CB  
5991  C CG1 . ILE B 748  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  745  ILE A CG1 
5992  C CG2 . ILE B 748  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  745  ILE A CG2 
5993  C CD1 . ILE B 748  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  745  ILE A CD1 
5994  N N   . TYR B 749  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  746  TYR A N   
5995  C CA  . TYR B 749  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  746  TYR A CA  
5996  C C   . TYR B 749  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  746  TYR A C   
5997  O O   . TYR B 749  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  746  TYR A O   
5998  C CB  . TYR B 749  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  746  TYR A CB  
5999  C CG  . TYR B 749  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  746  TYR A CG  
6000  C CD1 . TYR B 749  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  746  TYR A CD1 
6001  C CD2 . TYR B 749  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  746  TYR A CD2 
6002  C CE1 . TYR B 749  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  746  TYR A CE1 
6003  C CE2 . TYR B 749  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  746  TYR A CE2 
6004  C CZ  . TYR B 749  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  746  TYR A CZ  
6005  O OH  . TYR B 749  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  746  TYR A OH  
6006  N N   . ASN B 750  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  747  ASN A N   
6007  C CA  . ASN B 750  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  747  ASN A CA  
6008  C C   . ASN B 750  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  747  ASN A C   
6009  O O   . ASN B 750  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  747  ASN A O   
6010  C CB  . ASN B 750  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  747  ASN A CB  
6011  C CG  . ASN B 750  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  747  ASN A CG  
6012  O OD1 . ASN B 750  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  747  ASN A OD1 
6013  N ND2 . ASN B 750  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  747  ASN A ND2 
6014  N N   . LYS B 751  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  748  LYS A N   
6015  C CA  . LYS B 751  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  748  LYS A CA  
6016  C C   . LYS B 751  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  748  LYS A C   
6017  O O   . LYS B 751  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  748  LYS A O   
6023  N N   . ASP B 752  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  749  ASP A N   
6024  C CA  . ASP B 752  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  749  ASP A CA  
6025  C C   . ASP B 752  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  749  ASP A C   
6026  O O   . ASP B 752  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  749  ASP A O   
6027  C CB  . ASP B 752  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  749  ASP A CB  
6028  C CG  . ASP B 752  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  749  ASP A CG  
6029  O OD1 . ASP B 752  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  749  ASP A OD1 
6030  O OD2 . ASP B 752  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  749  ASP A OD2 
6031  N N   . PHE B 753  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  750  PHE A N   
6032  C CA  . PHE B 753  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  750  PHE A CA  
6033  C C   . PHE B 753  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  750  PHE A C   
6034  O O   . PHE B 753  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  750  PHE A O   
6035  C CB  . PHE B 753  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  750  PHE A CB  
6036  C CG  . PHE B 753  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  750  PHE A CG  
6037  C CD1 . PHE B 753  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  750  PHE A CD1 
6038  C CD2 . PHE B 753  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  750  PHE A CD2 
6039  C CE1 . PHE B 753  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  750  PHE A CE1 
6040  C CE2 . PHE B 753  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  750  PHE A CE2 
6041  C CZ  . PHE B 753  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  750  PHE A CZ  
6042  N N   . ALA B 754  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  751  ALA A N   
6043  C CA  . ALA B 754  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  751  ALA A CA  
6044  C C   . ALA B 754  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  751  ALA A C   
6045  O O   . ALA B 754  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  751  ALA A O   
6046  C CB  . ALA B 754  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  751  ALA A CB  
6047  N N   . LYS B 755  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  752  LYS A N   
6048  C CA  . LYS B 755  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  752  LYS A CA  
6049  C C   . LYS B 755  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  752  LYS A C   
6050  O O   . LYS B 755  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  752  LYS A O   
6056  N N   . GLY B 756  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  753  GLY A N   
6057  C CA  . GLY B 756  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  753  GLY A CA  
6058  C C   . GLY B 756  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  753  GLY A C   
6059  O O   . GLY B 756  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  753  GLY A O   
6060  N N   . HIS B 757  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  754  HIS A N   
6061  C CA  . HIS B 757  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  754  HIS A CA  
6062  C C   . HIS B 757  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  754  HIS A C   
6063  O O   . HIS B 757  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  754  HIS A O   
6064  C CB  . HIS B 757  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  754  HIS A CB  
6065  C CG  . HIS B 757  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  754  HIS A CG  
6066  N ND1 . HIS B 757  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  754  HIS A ND1 
6067  C CD2 . HIS B 757  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  754  HIS A CD2 
6068  C CE1 . HIS B 757  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  754  HIS A CE1 
6069  N NE2 . HIS B 757  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  754  HIS A NE2 
6070  N N   . HIS B 758  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  755  HIS A N   
6071  C CA  . HIS B 758  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  755  HIS A CA  
6072  C C   . HIS B 758  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  755  HIS A C   
6073  O O   . HIS B 758  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  755  HIS A O   
6074  C CB  . HIS B 758  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  755  HIS A CB  
6075  C CG  . HIS B 758  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  755  HIS A CG  
6076  N ND1 . HIS B 758  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  755  HIS A ND1 
6077  C CD2 . HIS B 758  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  755  HIS A CD2 
6078  C CE1 . HIS B 758  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  755  HIS A CE1 
6079  N NE2 . HIS B 758  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  755  HIS A NE2 
6080  N N   . GLY B 759  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  756  GLY A N   
6081  C CA  . GLY B 759  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  756  GLY A CA  
6082  C C   . GLY B 759  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  756  GLY A C   
6083  O O   . GLY B 759  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  756  GLY A O   
6084  N N   . LYS B 760  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  757  LYS A N   
6085  C CA  . LYS B 760  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  757  LYS A CA  
6086  C C   . LYS B 760  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  757  LYS A C   
6087  O O   . LYS B 760  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  757  LYS A O   
6088  C CB  . LYS B 760  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  757  LYS A CB  
6089  C CG  . LYS B 760  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  757  LYS A CG  
6090  C CD  . LYS B 760  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  757  LYS A CD  
6091  C CE  . LYS B 760  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  757  LYS A CE  
6092  N NZ  . LYS B 760  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  757  LYS A NZ  
6093  N N   . PRO B 761  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  758  PRO A N   
6094  C CA  . PRO B 761  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  758  PRO A CA  
6095  C C   . PRO B 761  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  758  PRO A C   
6096  O O   . PRO B 761  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  758  PRO A O   
6097  C CB  . PRO B 761  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  758  PRO A CB  
6098  C CG  . PRO B 761  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  758  PRO A CG  
6099  C CD  . PRO B 761  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  758  PRO A CD  
6100  N N   . ASN B 762  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  759  ASN A N   
6101  C CA  . ASN B 762  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  759  ASN A CA  
6102  C C   . ASN B 762  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  759  ASN A C   
6103  O O   . ASN B 762  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  759  ASN A O   
6104  C CB  . ASN B 762  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  759  ASN A CB  
6105  C CG  . ASN B 762  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  759  ASN A CG  
6106  O OD1 . ASN B 762  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  759  ASN A OD1 
6107  N ND2 . ASN B 762  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  759  ASN A ND2 
6108  N N   . LEU B 763  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  760  LEU A N   
6109  C CA  . LEU B 763  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  760  LEU A CA  
6110  C C   . LEU B 763  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  760  LEU A C   
6111  O O   . LEU B 763  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  760  LEU A O   
6112  C CB  . LEU B 763  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  760  LEU A CB  
6113  C CG  . LEU B 763  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  760  LEU A CG  
6114  C CD1 . LEU B 763  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  760  LEU A CD1 
6115  C CD2 . LEU B 763  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  760  LEU A CD2 
6116  N N   . HIS B 764  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  761  HIS A N   
6117  C CA  . HIS B 764  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  761  HIS A CA  
6118  C C   . HIS B 764  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  761  HIS A C   
6119  O O   . HIS B 764  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  761  HIS A O   
6120  C CB  . HIS B 764  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  761  HIS A CB  
6121  C CG  . HIS B 764  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  761  HIS A CG  
6122  N ND1 . HIS B 764  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  761  HIS A ND1 
6123  C CD2 . HIS B 764  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  761  HIS A CD2 
6124  C CE1 . HIS B 764  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  761  HIS A CE1 
6125  N NE2 . HIS B 764  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  761  HIS A NE2 
6126  N N   . THR B 765  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  762  THR A N   
6127  C CA  . THR B 765  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  762  THR A CA  
6128  C C   . THR B 765  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  762  THR A C   
6129  O O   . THR B 765  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  762  THR A O   
6130  C CB  . THR B 765  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  762  THR A CB  
6131  O OG1 . THR B 765  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  762  THR A OG1 
6132  C CG2 . THR B 765  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  762  THR A CG2 
6133  N N   . LEU B 766  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  763  LEU A N   
6134  C CA  . LEU B 766  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  763  LEU A CA  
6135  C C   . LEU B 766  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  763  LEU A C   
6136  O O   . LEU B 766  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  763  LEU A O   
6137  C CB  . LEU B 766  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  763  LEU A CB  
6138  C CG  . LEU B 766  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  763  LEU A CG  
6139  C CD1 . LEU B 766  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  763  LEU A CD1 
6140  C CD2 . LEU B 766  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  763  LEU A CD2 
6141  N N   . TYR B 767  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  764  TYR A N   
6142  C CA  . TYR B 767  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  764  TYR A CA  
6143  C C   . TYR B 767  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  764  TYR A C   
6144  O O   . TYR B 767  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  764  TYR A O   
6145  C CB  . TYR B 767  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  764  TYR A CB  
6146  C CG  . TYR B 767  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  764  TYR A CG  
6147  C CD1 . TYR B 767  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  764  TYR A CD1 
6148  C CD2 . TYR B 767  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  764  TYR A CD2 
6149  C CE1 . TYR B 767  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  764  TYR A CE1 
6150  C CE2 . TYR B 767  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  764  TYR A CE2 
6151  C CZ  . TYR B 767  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  764  TYR A CZ  
6152  O OH  . TYR B 767  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  764  TYR A OH  
6153  N N   . TRP B 768  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  765  TRP A N   
6154  C CA  . TRP B 768  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  765  TRP A CA  
6155  C C   . TRP B 768  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  765  TRP A C   
6156  O O   . TRP B 768  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  765  TRP A O   
6157  C CB  . TRP B 768  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  765  TRP A CB  
6158  C CG  . TRP B 768  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  765  TRP A CG  
6159  C CD1 . TRP B 768  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  765  TRP A CD1 
6160  C CD2 . TRP B 768  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  765  TRP A CD2 
6161  N NE1 . TRP B 768  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  765  TRP A NE1 
6162  C CE2 . TRP B 768  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  765  TRP A CE2 
6163  C CE3 . TRP B 768  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  765  TRP A CE3 
6164  C CZ2 . TRP B 768  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  765  TRP A CZ2 
6165  C CZ3 . TRP B 768  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  765  TRP A CZ3 
6166  C CH2 . TRP B 768  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  765  TRP A CH2 
6167  N N   . THR B 769  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  766  THR A N   
6168  C CA  . THR B 769  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  766  THR A CA  
6169  C C   . THR B 769  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  766  THR A C   
6170  O O   . THR B 769  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  766  THR A O   
6171  C CB  . THR B 769  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  766  THR A CB  
6172  O OG1 . THR B 769  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  766  THR A OG1 
6173  C CG2 . THR B 769  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  766  THR A CG2 
6174  N N   . GLY B 770  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  767  GLY A N   
6175  C CA  . GLY B 770  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  767  GLY A CA  
6176  C C   . GLY B 770  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  767  GLY A C   
6177  O O   . GLY B 770  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  767  GLY A O   
6178  N N   . LEU B 771  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  768  LEU A N   
6179  C CA  . LEU B 771  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  768  LEU A CA  
6180  C C   . LEU B 771  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  768  LEU A C   
6181  O O   . LEU B 771  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  768  LEU A O   
6182  C CB  . LEU B 771  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  768  LEU A CB  
6183  C CG  . LEU B 771  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  768  LEU A CG  
6184  C CD1 . LEU B 771  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  768  LEU A CD1 
6185  C CD2 . LEU B 771  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  768  LEU A CD2 
6186  N N   . PHE B 772  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  769  PHE A N   
6187  C CA  . PHE B 772  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  769  PHE A CA  
6188  C C   . PHE B 772  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  769  PHE A C   
6189  O O   . PHE B 772  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  769  PHE A O   
6190  C CB  . PHE B 772  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  769  PHE A CB  
6191  C CG  . PHE B 772  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  769  PHE A CG  
6192  C CD1 . PHE B 772  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  769  PHE A CD1 
6193  C CD2 . PHE B 772  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  769  PHE A CD2 
6194  C CE1 . PHE B 772  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  769  PHE A CE1 
6195  C CE2 . PHE B 772  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  769  PHE A CE2 
6196  C CZ  . PHE B 772  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  769  PHE A CZ  
6197  N N   . SER B 773  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  770  SER A N   
6198  C CA  . SER B 773  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  770  SER A CA  
6199  C C   . SER B 773  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  770  SER A C   
6200  O O   . SER B 773  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  770  SER A O   
6201  C CB  . SER B 773  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  770  SER A CB  
6202  O OG  . SER B 773  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  770  SER A OG  
6203  N N   . PRO B 774  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  771  PRO A N   
6204  C CA  . PRO B 774  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  771  PRO A CA  
6205  C C   . PRO B 774  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  771  PRO A C   
6206  O O   . PRO B 774  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  771  PRO A O   
6207  C CB  . PRO B 774  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  771  PRO A CB  
6208  C CG  . PRO B 774  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  771  PRO A CG  
6209  C CD  . PRO B 774  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  771  PRO A CD  
6210  N N   . GLU B 775  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  772  GLU A N   
6211  C CA  . GLU B 775  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  772  GLU A CA  
6212  C C   . GLU B 775  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  772  GLU A C   
6213  O O   . GLU B 775  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  772  GLU A O   
6214  C CB  . GLU B 775  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  772  GLU A CB  
6215  C CG  . GLU B 775  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  772  GLU A CG  
6216  C CD  . GLU B 775  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  772  GLU A CD  
6217  O OE1 . GLU B 775  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  772  GLU A OE1 
6218  O OE2 . GLU B 775  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  772  GLU A OE2 
6219  N N   . ASN B 776  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  773  ASN A N   
6220  C CA  . ASN B 776  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  773  ASN A CA  
6221  C C   . ASN B 776  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  773  ASN A C   
6222  O O   . ASN B 776  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  773  ASN A O   
6223  C CB  . ASN B 776  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  773  ASN A CB  
6224  C CG  . ASN B 776  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  773  ASN A CG  
6225  O OD1 . ASN B 776  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  773  ASN A OD1 
6226  N ND2 . ASN B 776  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  773  ASN A ND2 
6227  N N   . LEU B 777  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  774  LEU A N   
6228  C CA  . LEU B 777  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  774  LEU A CA  
6229  C C   . LEU B 777  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  774  LEU A C   
6230  O O   . LEU B 777  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  774  LEU A O   
6231  C CB  . LEU B 777  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  774  LEU A CB  
6232  C CG  . LEU B 777  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  774  LEU A CG  
6233  C CD1 . LEU B 777  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  774  LEU A CD1 
6234  C CD2 . LEU B 777  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  774  LEU A CD2 
6235  N N   . ALA B 778  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  775  ALA A N   
6236  C CA  . ALA B 778  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  775  ALA A CA  
6237  C C   . ALA B 778  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  775  ALA A C   
6238  O O   . ALA B 778  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  775  ALA A O   
6239  C CB  . ALA B 778  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  775  ALA A CB  
6240  N N   . LYS B 779  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  776  LYS A N   
6241  C CA  . LYS B 779  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  776  LYS A CA  
6242  C C   . LYS B 779  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  776  LYS A C   
6243  O O   . LYS B 779  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  776  LYS A O   
6244  C CB  . LYS B 779  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  776  LYS A CB  
6245  C CG  . LYS B 779  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  776  LYS A CG  
6246  C CD  . LYS B 779  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  776  LYS A CD  
6247  C CE  . LYS B 779  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  776  LYS A CE  
6248  N NZ  . LYS B 779  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  776  LYS A NZ  
6249  N N   . THR B 780  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  777  THR A N   
6250  C CA  . THR B 780  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  777  THR A CA  
6251  C C   . THR B 780  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  777  THR A C   
6252  O O   . THR B 780  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  777  THR A O   
6253  C CB  . THR B 780  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  777  THR A CB  
6254  O OG1 . THR B 780  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  777  THR A OG1 
6255  C CG2 . THR B 780  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  777  THR A CG2 
6256  N N   . SER B 781  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  778  SER A N   
6257  C CA  . SER B 781  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  778  SER A CA  
6258  C C   . SER B 781  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  778  SER A C   
6259  O O   . SER B 781  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  778  SER A O   
6260  C CB  . SER B 781  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  778  SER A CB  
6261  O OG  . SER B 781  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  778  SER A OG  
6262  N N   . ILE B 782  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  779  ILE A N   
6263  C CA  . ILE B 782  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  779  ILE A CA  
6264  C C   . ILE B 782  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  779  ILE A C   
6265  O O   . ILE B 782  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  779  ILE A O   
6266  C CB  . ILE B 782  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  779  ILE A CB  
6267  C CG1 . ILE B 782  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  779  ILE A CG1 
6268  C CG2 . ILE B 782  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  779  ILE A CG2 
6269  C CD1 . ILE B 782  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  779  ILE A CD1 
6270  N N   . LYS B 783  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  780  LYS A N   
6271  C CA  . LYS B 783  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  780  LYS A CA  
6272  C C   . LYS B 783  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  780  LYS A C   
6273  O O   . LYS B 783  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  780  LYS A O   
6274  C CB  . LYS B 783  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  780  LYS A CB  
6275  C CG  . LYS B 783  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  780  LYS A CG  
6276  C CD  . LYS B 783  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  780  LYS A CD  
6277  C CE  . LYS B 783  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  780  LYS A CE  
6278  N NZ  . LYS B 783  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  780  LYS A NZ  
6279  N N   . LEU B 784  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  781  LEU A N   
6280  C CA  . LEU B 784  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  781  LEU A CA  
6281  C C   . LEU B 784  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  781  LEU A C   
6282  O O   . LEU B 784  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  781  LEU A O   
6283  C CB  . LEU B 784  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  781  LEU A CB  
6284  C CG  . LEU B 784  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  781  LEU A CG  
6285  C CD1 . LEU B 784  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  781  LEU A CD1 
6286  C CD2 . LEU B 784  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  781  LEU A CD2 
6287  N N   . ASN B 785  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  782  ASN A N   
6288  C CA  . ASN B 785  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  782  ASN A CA  
6289  C C   . ASN B 785  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  782  ASN A C   
6290  O O   . ASN B 785  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  782  ASN A O   
6291  C CB  . ASN B 785  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  782  ASN A CB  
6292  C CG  . ASN B 785  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  782  ASN A CG  
6293  O OD1 . ASN B 785  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  782  ASN A OD1 
6294  N ND2 . ASN B 785  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  782  ASN A ND2 
6295  N N   . GLY B 786  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  783  GLY A N   
6296  C CA  . GLY B 786  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  783  GLY A CA  
6297  C C   . GLY B 786  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  783  GLY A C   
6298  O O   . GLY B 786  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  783  GLY A O   
6299  N N   . GLN B 787  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  784  GLN A N   
6300  C CA  . GLN B 787  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  784  GLN A CA  
6301  C C   . GLN B 787  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  784  GLN A C   
6302  O O   . GLN B 787  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  784  GLN A O   
6303  C CB  . GLN B 787  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  784  GLN A CB  
6304  C CG  . GLN B 787  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  784  GLN A CG  
6305  C CD  . GLN B 787  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  784  GLN A CD  
6306  O OE1 . GLN B 787  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  784  GLN A OE1 
6307  N NE2 . GLN B 787  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  784  GLN A NE2 
6308  N N   . ALA B 788  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  785  ALA A N   
6309  C CA  . ALA B 788  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  785  ALA A CA  
6310  C C   . ALA B 788  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  785  ALA A C   
6311  O O   . ALA B 788  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  785  ALA A O   
6312  C CB  . ALA B 788  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  785  ALA A CB  
6313  N N   . GLU B 789  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  786  GLU A N   
6314  C CA  . GLU B 789  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  786  GLU A CA  
6315  C C   . GLU B 789  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  786  GLU A C   
6316  O O   . GLU B 789  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  786  GLU A O   
6317  C CB  . GLU B 789  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  786  GLU A CB  
6318  C CG  . GLU B 789  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  786  GLU A CG  
6319  C CD  . GLU B 789  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  786  GLU A CD  
6320  O OE1 . GLU B 789  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  786  GLU A OE1 
6321  O OE2 . GLU B 789  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  786  GLU A OE2 
6322  N N   . LEU B 790  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  787  LEU A N   
6323  C CA  . LEU B 790  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  787  LEU A CA  
6324  C C   . LEU B 790  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  787  LEU A C   
6325  O O   . LEU B 790  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  787  LEU A O   
6326  C CB  . LEU B 790  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  787  LEU A CB  
6327  C CG  . LEU B 790  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  787  LEU A CG  
6328  C CD1 . LEU B 790  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  787  LEU A CD1 
6329  C CD2 . LEU B 790  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  787  LEU A CD2 
6330  N N   . PHE B 791  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  788  PHE A N   
6331  C CA  . PHE B 791  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  788  PHE A CA  
6332  C C   . PHE B 791  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  788  PHE A C   
6333  O O   . PHE B 791  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  788  PHE A O   
6334  C CB  . PHE B 791  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  788  PHE A CB  
6335  C CG  . PHE B 791  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  788  PHE A CG  
6336  C CD1 . PHE B 791  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  788  PHE A CD1 
6337  C CD2 . PHE B 791  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  788  PHE A CD2 
6338  C CE1 . PHE B 791  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  788  PHE A CE1 
6339  C CE2 . PHE B 791  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  788  PHE A CE2 
6340  C CZ  . PHE B 791  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  788  PHE A CZ  
6341  N N   . TYR B 792  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  789  TYR A N   
6342  C CA  . TYR B 792  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  789  TYR A CA  
6343  C C   . TYR B 792  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  789  TYR A C   
6344  O O   . TYR B 792  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  789  TYR A O   
6345  C CB  . TYR B 792  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  789  TYR A CB  
6346  C CG  . TYR B 792  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  789  TYR A CG  
6347  C CD1 . TYR B 792  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  789  TYR A CD1 
6348  C CD2 . TYR B 792  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  789  TYR A CD2 
6349  C CE1 . TYR B 792  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  789  TYR A CE1 
6350  C CE2 . TYR B 792  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  789  TYR A CE2 
6351  C CZ  . TYR B 792  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  789  TYR A CZ  
6352  O OH  . TYR B 792  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  789  TYR A OH  
6353  N N   . ARG B 793  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  790  ARG A N   
6354  C CA  . ARG B 793  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  790  ARG A CA  
6355  C C   . ARG B 793  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  790  ARG A C   
6356  O O   . ARG B 793  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  790  ARG A O   
6357  C CB  . ARG B 793  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  790  ARG A CB  
6358  C CG  . ARG B 793  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  790  ARG A CG  
6359  C CD  . ARG B 793  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  790  ARG A CD  
6360  N NE  . ARG B 793  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  790  ARG A NE  
6361  C CZ  . ARG B 793  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  790  ARG A CZ  
6362  N NH1 . ARG B 793  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  790  ARG A NH1 
6363  N NH2 . ARG B 793  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  790  ARG A NH2 
6364  N N   . PRO B 794  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  791  PRO A N   
6365  C CA  . PRO B 794  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  791  PRO A CA  
6366  C C   . PRO B 794  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  791  PRO A C   
6367  O O   . PRO B 794  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  791  PRO A O   
6368  C CB  . PRO B 794  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  791  PRO A CB  
6369  C CG  . PRO B 794  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  791  PRO A CG  
6370  C CD  . PRO B 794  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  791  PRO A CD  
6371  N N   . LYS B 795  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  792  LYS A N   
6372  C CA  . LYS B 795  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  792  LYS A CA  
6373  C C   . LYS B 795  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  792  LYS A C   
6374  O O   . LYS B 795  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  792  LYS A O   
6380  N N   . SER B 796  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  793  SER A N   
6381  C CA  . SER B 796  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  793  SER A CA  
6382  C C   . SER B 796  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  793  SER A C   
6383  O O   . SER B 796  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  793  SER A O   
6384  C CB  . SER B 796  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  793  SER A CB  
6385  O OG  . SER B 796  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  793  SER A OG  
6386  N N   . ARG B 797  ? 0.6905 0.6905 0.6905 0.0000  0.0000  0.0000  794  ARG A N   
6387  C CA  . ARG B 797  ? 0.6905 0.6905 0.6905 0.0000  0.0000  0.0000  794  ARG A CA  
6388  C C   . ARG B 797  ? 0.6905 0.6905 0.6905 0.0000  0.0000  0.0000  794  ARG A C   
6389  O O   . ARG B 797  ? 0.6905 0.6905 0.6905 0.0000  0.0000  0.0000  794  ARG A O   
6390  C CB  . ARG B 797  ? 0.6905 0.6905 0.6905 0.0000  0.0000  0.0000  794  ARG A CB  
6391  C CG  . ARG B 797  ? 0.6905 0.6905 0.6905 0.0000  0.0000  0.0000  794  ARG A CG  
6392  C CD  . ARG B 797  ? 0.6905 0.6905 0.6905 0.0000  0.0000  0.0000  794  ARG A CD  
6393  N NE  . ARG B 797  ? 0.6905 0.6905 0.6905 0.0000  0.0000  0.0000  794  ARG A NE  
6394  C CZ  . ARG B 797  ? 0.6905 0.6905 0.6905 0.0000  0.0000  0.0000  794  ARG A CZ  
6395  N NH1 . ARG B 797  ? 0.6905 0.6905 0.6905 0.0000  0.0000  0.0000  794  ARG A NH1 
6396  N NH2 . ARG B 797  ? 0.6905 0.6905 0.6905 0.0000  0.0000  0.0000  794  ARG A NH2 
6397  N N   . MET B 798  ? 0.6866 0.6866 0.6866 0.0000  0.0000  0.0000  795  MET A N   
6398  C CA  . MET B 798  ? 0.6866 0.6866 0.6866 0.0000  0.0000  0.0000  795  MET A CA  
6399  C C   . MET B 798  ? 0.6866 0.6866 0.6866 0.0000  0.0000  0.0000  795  MET A C   
6400  O O   . MET B 798  ? 0.6866 0.6866 0.6866 0.0000  0.0000  0.0000  795  MET A O   
6401  C CB  . MET B 798  ? 0.6866 0.6866 0.6866 0.0000  0.0000  0.0000  795  MET A CB  
6402  C CG  . MET B 798  ? 0.6866 0.6866 0.6866 0.0000  0.0000  0.0000  795  MET A CG  
6403  S SD  . MET B 798  ? 0.6866 0.6866 0.6866 0.0000  0.0000  0.0000  795  MET A SD  
6404  C CE  . MET B 798  ? 0.6866 0.6866 0.6866 0.0000  0.0000  0.0000  795  MET A CE  
6467  N N   . GLU B 807  ? 0.6887 0.6887 0.6887 0.0000  0.0000  0.0000  804  GLU A N   
6468  C CA  . GLU B 807  ? 0.6887 0.6887 0.6887 0.0000  0.0000  0.0000  804  GLU A CA  
6469  C C   . GLU B 807  ? 0.6887 0.6887 0.6887 0.0000  0.0000  0.0000  804  GLU A C   
6470  O O   . GLU B 807  ? 0.6887 0.6887 0.6887 0.0000  0.0000  0.0000  804  GLU A O   
6476  N N   . LYS B 808  ? 0.6721 0.6721 0.6721 0.0000  0.0000  0.0000  805  LYS A N   
6477  C CA  . LYS B 808  ? 0.6721 0.6721 0.6721 0.0000  0.0000  0.0000  805  LYS A CA  
6478  C C   . LYS B 808  ? 0.6721 0.6721 0.6721 0.0000  0.0000  0.0000  805  LYS A C   
6479  O O   . LYS B 808  ? 0.6721 0.6721 0.6721 0.0000  0.0000  0.0000  805  LYS A O   
6480  C CB  . LYS B 808  ? 0.6721 0.6721 0.6721 0.0000  0.0000  0.0000  805  LYS A CB  
6481  C CG  . LYS B 808  ? 0.6721 0.6721 0.6721 0.0000  0.0000  0.0000  805  LYS A CG  
6482  C CD  . LYS B 808  ? 0.6721 0.6721 0.6721 0.0000  0.0000  0.0000  805  LYS A CD  
6483  C CE  . LYS B 808  ? 0.6721 0.6721 0.6721 0.0000  0.0000  0.0000  805  LYS A CE  
6484  N NZ  . LYS B 808  ? 0.6721 0.6721 0.6721 0.0000  0.0000  0.0000  805  LYS A NZ  
6485  N N   . MET B 809  ? 0.6192 0.6192 0.6192 0.0000  0.0000  0.0000  806  MET A N   
6486  C CA  . MET B 809  ? 0.6192 0.6192 0.6192 0.0000  0.0000  0.0000  806  MET A CA  
6487  C C   . MET B 809  ? 0.6192 0.6192 0.6192 0.0000  0.0000  0.0000  806  MET A C   
6488  O O   . MET B 809  ? 0.6192 0.6192 0.6192 0.0000  0.0000  0.0000  806  MET A O   
6489  C CB  . MET B 809  ? 0.6192 0.6192 0.6192 0.0000  0.0000  0.0000  806  MET A CB  
6490  C CG  . MET B 809  ? 0.6192 0.6192 0.6192 0.0000  0.0000  0.0000  806  MET A CG  
6491  S SD  . MET B 809  ? 0.6192 0.6192 0.6192 0.0000  0.0000  0.0000  806  MET A SD  
6492  C CE  . MET B 809  ? 0.6192 0.6192 0.6192 0.0000  0.0000  0.0000  806  MET A CE  
6493  N N   . LEU B 810  ? 0.5736 0.5736 0.5736 0.0000  0.0000  0.0000  807  LEU A N   
6494  C CA  . LEU B 810  ? 0.5736 0.5736 0.5736 0.0000  0.0000  0.0000  807  LEU A CA  
6495  C C   . LEU B 810  ? 0.5736 0.5736 0.5736 0.0000  0.0000  0.0000  807  LEU A C   
6496  O O   . LEU B 810  ? 0.5736 0.5736 0.5736 0.0000  0.0000  0.0000  807  LEU A O   
6497  C CB  . LEU B 810  ? 0.5736 0.5736 0.5736 0.0000  0.0000  0.0000  807  LEU A CB  
6498  C CG  . LEU B 810  ? 0.5736 0.5736 0.5736 0.0000  0.0000  0.0000  807  LEU A CG  
6499  C CD1 . LEU B 810  ? 0.5736 0.5736 0.5736 0.0000  0.0000  0.0000  807  LEU A CD1 
6500  C CD2 . LEU B 810  ? 0.5736 0.5736 0.5736 0.0000  0.0000  0.0000  807  LEU A CD2 
6501  N N   . ASN B 811  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  808  ASN A N   
6502  C CA  . ASN B 811  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  808  ASN A CA  
6503  C C   . ASN B 811  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  808  ASN A C   
6504  O O   . ASN B 811  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  808  ASN A O   
6505  C CB  . ASN B 811  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  808  ASN A CB  
6506  C CG  . ASN B 811  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  808  ASN A CG  
6507  O OD1 . ASN B 811  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  808  ASN A OD1 
6508  N ND2 . ASN B 811  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  808  ASN A ND2 
6509  N N   . LYS B 812  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  809  LYS A N   
6510  C CA  . LYS B 812  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  809  LYS A CA  
6511  C C   . LYS B 812  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  809  LYS A C   
6512  O O   . LYS B 812  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  809  LYS A O   
6513  C CB  . LYS B 812  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  809  LYS A CB  
6514  C CG  . LYS B 812  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  809  LYS A CG  
6515  C CD  . LYS B 812  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  809  LYS A CD  
6516  C CE  . LYS B 812  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  809  LYS A CE  
6517  N NZ  . LYS B 812  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  809  LYS A NZ  
6518  N N   . LYS B 813  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  810  LYS A N   
6519  C CA  . LYS B 813  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  810  LYS A CA  
6520  C C   . LYS B 813  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  810  LYS A C   
6521  O O   . LYS B 813  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  810  LYS A O   
6527  N N   . LEU B 814  ? 0.5886 0.5886 0.5886 0.0000  0.0000  0.0000  811  LEU A N   
6528  C CA  . LEU B 814  ? 0.5886 0.5886 0.5886 0.0000  0.0000  0.0000  811  LEU A CA  
6529  C C   . LEU B 814  ? 0.5886 0.5886 0.5886 0.0000  0.0000  0.0000  811  LEU A C   
6530  O O   . LEU B 814  ? 0.5886 0.5886 0.5886 0.0000  0.0000  0.0000  811  LEU A O   
6531  C CB  . LEU B 814  ? 0.5886 0.5886 0.5886 0.0000  0.0000  0.0000  811  LEU A CB  
6532  C CG  . LEU B 814  ? 0.5886 0.5886 0.5886 0.0000  0.0000  0.0000  811  LEU A CG  
6533  C CD1 . LEU B 814  ? 0.5886 0.5886 0.5886 0.0000  0.0000  0.0000  811  LEU A CD1 
6534  C CD2 . LEU B 814  ? 0.5886 0.5886 0.5886 0.0000  0.0000  0.0000  811  LEU A CD2 
6535  N N   . LYS B 815  ? 0.6163 0.6163 0.6163 0.0000  0.0000  0.0000  812  LYS A N   
6536  C CA  . LYS B 815  ? 0.6163 0.6163 0.6163 0.0000  0.0000  0.0000  812  LYS A CA  
6537  C C   . LYS B 815  ? 0.6163 0.6163 0.6163 0.0000  0.0000  0.0000  812  LYS A C   
6538  O O   . LYS B 815  ? 0.6163 0.6163 0.6163 0.0000  0.0000  0.0000  812  LYS A O   
6539  C CB  . LYS B 815  ? 0.6163 0.6163 0.6163 0.0000  0.0000  0.0000  812  LYS A CB  
6540  C CG  . LYS B 815  ? 0.6163 0.6163 0.6163 0.0000  0.0000  0.0000  812  LYS A CG  
6541  C CD  . LYS B 815  ? 0.6163 0.6163 0.6163 0.0000  0.0000  0.0000  812  LYS A CD  
6542  C CE  . LYS B 815  ? 0.6163 0.6163 0.6163 0.0000  0.0000  0.0000  812  LYS A CE  
6543  N NZ  . LYS B 815  ? 0.6163 0.6163 0.6163 0.0000  0.0000  0.0000  812  LYS A NZ  
6544  N N   . ASP B 816  ? 0.6096 0.6096 0.6096 0.0000  0.0000  0.0000  813  ASP A N   
6545  C CA  . ASP B 816  ? 0.6096 0.6096 0.6096 0.0000  0.0000  0.0000  813  ASP A CA  
6546  C C   . ASP B 816  ? 0.6096 0.6096 0.6096 0.0000  0.0000  0.0000  813  ASP A C   
6547  O O   . ASP B 816  ? 0.6096 0.6096 0.6096 0.0000  0.0000  0.0000  813  ASP A O   
6548  C CB  . ASP B 816  ? 0.6096 0.6096 0.6096 0.0000  0.0000  0.0000  813  ASP A CB  
6549  C CG  . ASP B 816  ? 0.6096 0.6096 0.6096 0.0000  0.0000  0.0000  813  ASP A CG  
6550  O OD1 . ASP B 816  ? 0.6096 0.6096 0.6096 0.0000  0.0000  0.0000  813  ASP A OD1 
6551  O OD2 . ASP B 816  ? 0.6096 0.6096 0.6096 0.0000  0.0000  0.0000  813  ASP A OD2 
6552  N N   . GLN B 817  ? 0.5981 0.5981 0.5981 0.0000  0.0000  0.0000  814  GLN A N   
6553  C CA  . GLN B 817  ? 0.5981 0.5981 0.5981 0.0000  0.0000  0.0000  814  GLN A CA  
6554  C C   . GLN B 817  ? 0.5981 0.5981 0.5981 0.0000  0.0000  0.0000  814  GLN A C   
6555  O O   . GLN B 817  ? 0.5981 0.5981 0.5981 0.0000  0.0000  0.0000  814  GLN A O   
6556  C CB  . GLN B 817  ? 0.5981 0.5981 0.5981 0.0000  0.0000  0.0000  814  GLN A CB  
6557  C CG  . GLN B 817  ? 0.5981 0.5981 0.5981 0.0000  0.0000  0.0000  814  GLN A CG  
6558  C CD  . GLN B 817  ? 0.5981 0.5981 0.5981 0.0000  0.0000  0.0000  814  GLN A CD  
6559  O OE1 . GLN B 817  ? 0.5981 0.5981 0.5981 0.0000  0.0000  0.0000  814  GLN A OE1 
6560  N NE2 . GLN B 817  ? 0.5981 0.5981 0.5981 0.0000  0.0000  0.0000  814  GLN A NE2 
6561  N N   . LYS B 818  ? 0.5872 0.5872 0.5872 0.0000  0.0000  0.0000  815  LYS A N   
6562  C CA  . LYS B 818  ? 0.5872 0.5872 0.5872 0.0000  0.0000  0.0000  815  LYS A CA  
6563  C C   . LYS B 818  ? 0.5872 0.5872 0.5872 0.0000  0.0000  0.0000  815  LYS A C   
6564  O O   . LYS B 818  ? 0.5872 0.5872 0.5872 0.0000  0.0000  0.0000  815  LYS A O   
6570  N N   . THR B 819  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  816  THR A N   
6571  C CA  . THR B 819  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  816  THR A CA  
6572  C C   . THR B 819  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  816  THR A C   
6573  O O   . THR B 819  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  816  THR A O   
6574  C CB  . THR B 819  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  816  THR A CB  
6575  O OG1 . THR B 819  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  816  THR A OG1 
6576  C CG2 . THR B 819  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  816  THR A CG2 
6577  N N   . PRO B 820  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  817  PRO A N   
6578  C CA  . PRO B 820  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  817  PRO A CA  
6579  C C   . PRO B 820  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  817  PRO A C   
6580  O O   . PRO B 820  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  817  PRO A O   
6581  C CB  . PRO B 820  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  817  PRO A CB  
6582  C CG  . PRO B 820  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  817  PRO A CG  
6583  C CD  . PRO B 820  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  817  PRO A CD  
6584  N N   . ILE B 821  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  818  ILE A N   
6585  C CA  . ILE B 821  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  818  ILE A CA  
6586  C C   . ILE B 821  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  818  ILE A C   
6587  O O   . ILE B 821  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  818  ILE A O   
6588  C CB  . ILE B 821  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  818  ILE A CB  
6589  C CG1 . ILE B 821  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  818  ILE A CG1 
6590  C CG2 . ILE B 821  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  818  ILE A CG2 
6591  C CD1 . ILE B 821  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  818  ILE A CD1 
6592  N N   . PRO B 822  ? 0.5689 0.5689 0.5689 0.0000  0.0000  0.0000  819  PRO A N   
6593  C CA  . PRO B 822  ? 0.5689 0.5689 0.5689 0.0000  0.0000  0.0000  819  PRO A CA  
6594  C C   . PRO B 822  ? 0.5689 0.5689 0.5689 0.0000  0.0000  0.0000  819  PRO A C   
6595  O O   . PRO B 822  ? 0.5689 0.5689 0.5689 0.0000  0.0000  0.0000  819  PRO A O   
6596  C CB  . PRO B 822  ? 0.5689 0.5689 0.5689 0.0000  0.0000  0.0000  819  PRO A CB  
6597  C CG  . PRO B 822  ? 0.5689 0.5689 0.5689 0.0000  0.0000  0.0000  819  PRO A CG  
6598  C CD  . PRO B 822  ? 0.5689 0.5689 0.5689 0.0000  0.0000  0.0000  819  PRO A CD  
6599  N N   . ASP B 823  ? 0.6660 0.6660 0.6660 0.0000  0.0000  0.0000  820  ASP A N   
6600  C CA  . ASP B 823  ? 0.6660 0.6660 0.6660 0.0000  0.0000  0.0000  820  ASP A CA  
6601  C C   . ASP B 823  ? 0.6660 0.6660 0.6660 0.0000  0.0000  0.0000  820  ASP A C   
6602  O O   . ASP B 823  ? 0.6660 0.6660 0.6660 0.0000  0.0000  0.0000  820  ASP A O   
6603  C CB  . ASP B 823  ? 0.6660 0.6660 0.6660 0.0000  0.0000  0.0000  820  ASP A CB  
6604  C CG  . ASP B 823  ? 0.6660 0.6660 0.6660 0.0000  0.0000  0.0000  820  ASP A CG  
6605  O OD1 . ASP B 823  ? 0.6660 0.6660 0.6660 0.0000  0.0000  0.0000  820  ASP A OD1 
6606  O OD2 . ASP B 823  ? 0.6660 0.6660 0.6660 0.0000  0.0000  0.0000  820  ASP A OD2 
6607  N N   . THR B 824  ? 0.6091 0.6091 0.6091 0.0000  0.0000  0.0000  821  THR A N   
6608  C CA  . THR B 824  ? 0.6091 0.6091 0.6091 0.0000  0.0000  0.0000  821  THR A CA  
6609  C C   . THR B 824  ? 0.6091 0.6091 0.6091 0.0000  0.0000  0.0000  821  THR A C   
6610  O O   . THR B 824  ? 0.6091 0.6091 0.6091 0.0000  0.0000  0.0000  821  THR A O   
6611  C CB  . THR B 824  ? 0.6091 0.6091 0.6091 0.0000  0.0000  0.0000  821  THR A CB  
6612  O OG1 . THR B 824  ? 0.6091 0.6091 0.6091 0.0000  0.0000  0.0000  821  THR A OG1 
6613  C CG2 . THR B 824  ? 0.6091 0.6091 0.6091 0.0000  0.0000  0.0000  821  THR A CG2 
6614  N N   . LEU B 825  ? 0.6180 0.6180 0.6180 0.0000  0.0000  0.0000  822  LEU A N   
6615  C CA  . LEU B 825  ? 0.6180 0.6180 0.6180 0.0000  0.0000  0.0000  822  LEU A CA  
6616  C C   . LEU B 825  ? 0.6180 0.6180 0.6180 0.0000  0.0000  0.0000  822  LEU A C   
6617  O O   . LEU B 825  ? 0.6180 0.6180 0.6180 0.0000  0.0000  0.0000  822  LEU A O   
6618  C CB  . LEU B 825  ? 0.6180 0.6180 0.6180 0.0000  0.0000  0.0000  822  LEU A CB  
6619  C CG  . LEU B 825  ? 0.6180 0.6180 0.6180 0.0000  0.0000  0.0000  822  LEU A CG  
6620  C CD1 . LEU B 825  ? 0.6180 0.6180 0.6180 0.0000  0.0000  0.0000  822  LEU A CD1 
6621  C CD2 . LEU B 825  ? 0.6180 0.6180 0.6180 0.0000  0.0000  0.0000  822  LEU A CD2 
6622  N N   . TYR B 826  ? 0.6382 0.6382 0.6382 0.0000  0.0000  0.0000  823  TYR A N   
6623  C CA  . TYR B 826  ? 0.6382 0.6382 0.6382 0.0000  0.0000  0.0000  823  TYR A CA  
6624  C C   . TYR B 826  ? 0.6382 0.6382 0.6382 0.0000  0.0000  0.0000  823  TYR A C   
6625  O O   . TYR B 826  ? 0.6382 0.6382 0.6382 0.0000  0.0000  0.0000  823  TYR A O   
6626  C CB  . TYR B 826  ? 0.6382 0.6382 0.6382 0.0000  0.0000  0.0000  823  TYR A CB  
6627  C CG  . TYR B 826  ? 0.6382 0.6382 0.6382 0.0000  0.0000  0.0000  823  TYR A CG  
6628  C CD1 . TYR B 826  ? 0.6382 0.6382 0.6382 0.0000  0.0000  0.0000  823  TYR A CD1 
6629  C CD2 . TYR B 826  ? 0.6382 0.6382 0.6382 0.0000  0.0000  0.0000  823  TYR A CD2 
6630  C CE1 . TYR B 826  ? 0.6382 0.6382 0.6382 0.0000  0.0000  0.0000  823  TYR A CE1 
6631  C CE2 . TYR B 826  ? 0.6382 0.6382 0.6382 0.0000  0.0000  0.0000  823  TYR A CE2 
6632  C CZ  . TYR B 826  ? 0.6382 0.6382 0.6382 0.0000  0.0000  0.0000  823  TYR A CZ  
6633  O OH  . TYR B 826  ? 0.6382 0.6382 0.6382 0.0000  0.0000  0.0000  823  TYR A OH  
6634  N N   . GLN B 827  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  824  GLN A N   
6635  C CA  . GLN B 827  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  824  GLN A CA  
6636  C C   . GLN B 827  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  824  GLN A C   
6637  O O   . GLN B 827  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  824  GLN A O   
6638  C CB  . GLN B 827  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  824  GLN A CB  
6639  C CG  . GLN B 827  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  824  GLN A CG  
6640  C CD  . GLN B 827  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  824  GLN A CD  
6641  O OE1 . GLN B 827  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  824  GLN A OE1 
6642  N NE2 . GLN B 827  ? 0.6480 0.6480 0.6480 0.0000  0.0000  0.0000  824  GLN A NE2 
6643  N N   . GLU B 828  ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  825  GLU A N   
6644  C CA  . GLU B 828  ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  825  GLU A CA  
6645  C C   . GLU B 828  ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  825  GLU A C   
6646  O O   . GLU B 828  ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  825  GLU A O   
6647  C CB  . GLU B 828  ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  825  GLU A CB  
6648  C CG  . GLU B 828  ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  825  GLU A CG  
6649  C CD  . GLU B 828  ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  825  GLU A CD  
6650  O OE1 . GLU B 828  ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  825  GLU A OE1 
6651  O OE2 . GLU B 828  ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  825  GLU A OE2 
6652  N N   . LEU B 829  ? 0.7211 0.7211 0.7211 0.0000  0.0000  0.0000  826  LEU A N   
6653  C CA  . LEU B 829  ? 0.7211 0.7211 0.7211 0.0000  0.0000  0.0000  826  LEU A CA  
6654  C C   . LEU B 829  ? 0.7211 0.7211 0.7211 0.0000  0.0000  0.0000  826  LEU A C   
6655  O O   . LEU B 829  ? 0.7211 0.7211 0.7211 0.0000  0.0000  0.0000  826  LEU A O   
6656  C CB  . LEU B 829  ? 0.7211 0.7211 0.7211 0.0000  0.0000  0.0000  826  LEU A CB  
6657  C CG  . LEU B 829  ? 0.7211 0.7211 0.7211 0.0000  0.0000  0.0000  826  LEU A CG  
6658  C CD1 . LEU B 829  ? 0.7211 0.7211 0.7211 0.0000  0.0000  0.0000  826  LEU A CD1 
6659  C CD2 . LEU B 829  ? 0.7211 0.7211 0.7211 0.0000  0.0000  0.0000  826  LEU A CD2 
6660  N N   . TYR B 830  ? 0.7224 0.7224 0.7224 0.0000  0.0000  0.0000  827  TYR A N   
6661  C CA  . TYR B 830  ? 0.7224 0.7224 0.7224 0.0000  0.0000  0.0000  827  TYR A CA  
6662  C C   . TYR B 830  ? 0.7224 0.7224 0.7224 0.0000  0.0000  0.0000  827  TYR A C   
6663  O O   . TYR B 830  ? 0.7224 0.7224 0.7224 0.0000  0.0000  0.0000  827  TYR A O   
6664  C CB  . TYR B 830  ? 0.7224 0.7224 0.7224 0.0000  0.0000  0.0000  827  TYR A CB  
6665  C CG  . TYR B 830  ? 0.7224 0.7224 0.7224 0.0000  0.0000  0.0000  827  TYR A CG  
6666  C CD1 . TYR B 830  ? 0.7224 0.7224 0.7224 0.0000  0.0000  0.0000  827  TYR A CD1 
6667  C CD2 . TYR B 830  ? 0.7224 0.7224 0.7224 0.0000  0.0000  0.0000  827  TYR A CD2 
6668  C CE1 . TYR B 830  ? 0.7224 0.7224 0.7224 0.0000  0.0000  0.0000  827  TYR A CE1 
6669  C CE2 . TYR B 830  ? 0.7224 0.7224 0.7224 0.0000  0.0000  0.0000  827  TYR A CE2 
6670  C CZ  . TYR B 830  ? 0.7224 0.7224 0.7224 0.0000  0.0000  0.0000  827  TYR A CZ  
6671  O OH  . TYR B 830  ? 0.7224 0.7224 0.7224 0.0000  0.0000  0.0000  827  TYR A OH  
6672  N N   . ASP B 831  ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  828  ASP A N   
6673  C CA  . ASP B 831  ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  828  ASP A CA  
6674  C C   . ASP B 831  ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  828  ASP A C   
6675  O O   . ASP B 831  ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  828  ASP A O   
6676  C CB  . ASP B 831  ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  828  ASP A CB  
6677  C CG  . ASP B 831  ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  828  ASP A CG  
6678  O OD1 . ASP B 831  ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  828  ASP A OD1 
6679  O OD2 . ASP B 831  ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  828  ASP A OD2 
6680  N N   . TYR B 832  ? 0.7225 0.7225 0.7225 0.0000  0.0000  0.0000  829  TYR A N   
6681  C CA  . TYR B 832  ? 0.7225 0.7225 0.7225 0.0000  0.0000  0.0000  829  TYR A CA  
6682  C C   . TYR B 832  ? 0.7225 0.7225 0.7225 0.0000  0.0000  0.0000  829  TYR A C   
6683  O O   . TYR B 832  ? 0.7225 0.7225 0.7225 0.0000  0.0000  0.0000  829  TYR A O   
6684  C CB  . TYR B 832  ? 0.7225 0.7225 0.7225 0.0000  0.0000  0.0000  829  TYR A CB  
6685  C CG  . TYR B 832  ? 0.7225 0.7225 0.7225 0.0000  0.0000  0.0000  829  TYR A CG  
6686  C CD1 . TYR B 832  ? 0.7225 0.7225 0.7225 0.0000  0.0000  0.0000  829  TYR A CD1 
6687  C CD2 . TYR B 832  ? 0.7225 0.7225 0.7225 0.0000  0.0000  0.0000  829  TYR A CD2 
6688  C CE1 . TYR B 832  ? 0.7225 0.7225 0.7225 0.0000  0.0000  0.0000  829  TYR A CE1 
6689  C CE2 . TYR B 832  ? 0.7225 0.7225 0.7225 0.0000  0.0000  0.0000  829  TYR A CE2 
6690  C CZ  . TYR B 832  ? 0.7225 0.7225 0.7225 0.0000  0.0000  0.0000  829  TYR A CZ  
6691  O OH  . TYR B 832  ? 0.7225 0.7225 0.7225 0.0000  0.0000  0.0000  829  TYR A OH  
6692  N N   . VAL B 833  ? 0.7183 0.7183 0.7183 0.0000  0.0000  0.0000  830  VAL A N   
6693  C CA  . VAL B 833  ? 0.7183 0.7183 0.7183 0.0000  0.0000  0.0000  830  VAL A CA  
6694  C C   . VAL B 833  ? 0.7183 0.7183 0.7183 0.0000  0.0000  0.0000  830  VAL A C   
6695  O O   . VAL B 833  ? 0.7183 0.7183 0.7183 0.0000  0.0000  0.0000  830  VAL A O   
6696  C CB  . VAL B 833  ? 0.7183 0.7183 0.7183 0.0000  0.0000  0.0000  830  VAL A CB  
6697  C CG1 . VAL B 833  ? 0.7183 0.7183 0.7183 0.0000  0.0000  0.0000  830  VAL A CG1 
6698  C CG2 . VAL B 833  ? 0.7183 0.7183 0.7183 0.0000  0.0000  0.0000  830  VAL A CG2 
6699  N N   . ASN B 834  ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  831  ASN A N   
6700  C CA  . ASN B 834  ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  831  ASN A CA  
6701  C C   . ASN B 834  ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  831  ASN A C   
6702  O O   . ASN B 834  ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  831  ASN A O   
6703  C CB  . ASN B 834  ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  831  ASN A CB  
6704  C CG  . ASN B 834  ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  831  ASN A CG  
6705  O OD1 . ASN B 834  ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  831  ASN A OD1 
6706  N ND2 . ASN B 834  ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  831  ASN A ND2 
6707  N N   . HIS B 835  ? 0.7207 0.7207 0.7207 0.0000  0.0000  0.0000  832  HIS A N   
6708  C CA  . HIS B 835  ? 0.7207 0.7207 0.7207 0.0000  0.0000  0.0000  832  HIS A CA  
6709  C C   . HIS B 835  ? 0.7207 0.7207 0.7207 0.0000  0.0000  0.0000  832  HIS A C   
6710  O O   . HIS B 835  ? 0.7207 0.7207 0.7207 0.0000  0.0000  0.0000  832  HIS A O   
6711  C CB  . HIS B 835  ? 0.7207 0.7207 0.7207 0.0000  0.0000  0.0000  832  HIS A CB  
6712  C CG  . HIS B 835  ? 0.7207 0.7207 0.7207 0.0000  0.0000  0.0000  832  HIS A CG  
6713  N ND1 . HIS B 835  ? 0.7207 0.7207 0.7207 0.0000  0.0000  0.0000  832  HIS A ND1 
6714  C CD2 . HIS B 835  ? 0.7207 0.7207 0.7207 0.0000  0.0000  0.0000  832  HIS A CD2 
6715  C CE1 . HIS B 835  ? 0.7207 0.7207 0.7207 0.0000  0.0000  0.0000  832  HIS A CE1 
6716  N NE2 . HIS B 835  ? 0.7207 0.7207 0.7207 0.0000  0.0000  0.0000  832  HIS A NE2 
6717  N N   . ARG B 836  ? 0.7246 0.7246 0.7246 0.0000  0.0000  0.0000  833  ARG A N   
6718  C CA  . ARG B 836  ? 0.7246 0.7246 0.7246 0.0000  0.0000  0.0000  833  ARG A CA  
6719  C C   . ARG B 836  ? 0.7246 0.7246 0.7246 0.0000  0.0000  0.0000  833  ARG A C   
6720  O O   . ARG B 836  ? 0.7246 0.7246 0.7246 0.0000  0.0000  0.0000  833  ARG A O   
6721  C CB  . ARG B 836  ? 0.7246 0.7246 0.7246 0.0000  0.0000  0.0000  833  ARG A CB  
6722  C CG  . ARG B 836  ? 0.7246 0.7246 0.7246 0.0000  0.0000  0.0000  833  ARG A CG  
6723  C CD  . ARG B 836  ? 0.7246 0.7246 0.7246 0.0000  0.0000  0.0000  833  ARG A CD  
6724  N NE  . ARG B 836  ? 0.7246 0.7246 0.7246 0.0000  0.0000  0.0000  833  ARG A NE  
6725  C CZ  . ARG B 836  ? 0.7246 0.7246 0.7246 0.0000  0.0000  0.0000  833  ARG A CZ  
6726  N NH1 . ARG B 836  ? 0.7246 0.7246 0.7246 0.0000  0.0000  0.0000  833  ARG A NH1 
6727  N NH2 . ARG B 836  ? 0.7246 0.7246 0.7246 0.0000  0.0000  0.0000  833  ARG A NH2 
6728  N N   . LEU B 837  ? 0.8644 0.8644 0.8644 0.0000  0.0000  0.0000  834  LEU A N   
6729  C CA  . LEU B 837  ? 0.8644 0.8644 0.8644 0.0000  0.0000  0.0000  834  LEU A CA  
6730  C C   . LEU B 837  ? 0.8644 0.8644 0.8644 0.0000  0.0000  0.0000  834  LEU A C   
6731  O O   . LEU B 837  ? 0.8644 0.8644 0.8644 0.0000  0.0000  0.0000  834  LEU A O   
6732  C CB  . LEU B 837  ? 0.8644 0.8644 0.8644 0.0000  0.0000  0.0000  834  LEU A CB  
6733  C CG  . LEU B 837  ? 0.8644 0.8644 0.8644 0.0000  0.0000  0.0000  834  LEU A CG  
6734  C CD1 . LEU B 837  ? 0.8644 0.8644 0.8644 0.0000  0.0000  0.0000  834  LEU A CD1 
6735  C CD2 . LEU B 837  ? 0.8644 0.8644 0.8644 0.0000  0.0000  0.0000  834  LEU A CD2 
6736  N N   . SER B 838  ? 0.9239 0.9239 0.9239 0.0000  0.0000  0.0000  835  SER A N   
6737  C CA  . SER B 838  ? 0.9239 0.9239 0.9239 0.0000  0.0000  0.0000  835  SER A CA  
6738  C C   . SER B 838  ? 0.9239 0.9239 0.9239 0.0000  0.0000  0.0000  835  SER A C   
6739  O O   . SER B 838  ? 0.9239 0.9239 0.9239 0.0000  0.0000  0.0000  835  SER A O   
6740  C CB  . SER B 838  ? 0.9239 0.9239 0.9239 0.0000  0.0000  0.0000  835  SER A CB  
6741  O OG  . SER B 838  ? 0.9239 0.9239 0.9239 0.0000  0.0000  0.0000  835  SER A OG  
6742  N N   . HIS B 839  ? 0.9640 0.9640 0.9640 0.0000  0.0000  0.0000  836  HIS A N   
6743  C CA  . HIS B 839  ? 0.9640 0.9640 0.9640 0.0000  0.0000  0.0000  836  HIS A CA  
6744  C C   . HIS B 839  ? 0.9640 0.9640 0.9640 0.0000  0.0000  0.0000  836  HIS A C   
6745  O O   . HIS B 839  ? 0.9640 0.9640 0.9640 0.0000  0.0000  0.0000  836  HIS A O   
6746  C CB  . HIS B 839  ? 0.9640 0.9640 0.9640 0.0000  0.0000  0.0000  836  HIS A CB  
6747  C CG  . HIS B 839  ? 0.9640 0.9640 0.9640 0.0000  0.0000  0.0000  836  HIS A CG  
6748  N ND1 . HIS B 839  ? 0.9640 0.9640 0.9640 0.0000  0.0000  0.0000  836  HIS A ND1 
6749  C CD2 . HIS B 839  ? 0.9640 0.9640 0.9640 0.0000  0.0000  0.0000  836  HIS A CD2 
6750  C CE1 . HIS B 839  ? 0.9640 0.9640 0.9640 0.0000  0.0000  0.0000  836  HIS A CE1 
6751  N NE2 . HIS B 839  ? 0.9640 0.9640 0.9640 0.0000  0.0000  0.0000  836  HIS A NE2 
6752  N N   . ASP B 840  ? 0.8765 0.8765 0.8765 0.0000  0.0000  0.0000  837  ASP A N   
6753  C CA  . ASP B 840  ? 0.8765 0.8765 0.8765 0.0000  0.0000  0.0000  837  ASP A CA  
6754  C C   . ASP B 840  ? 0.8765 0.8765 0.8765 0.0000  0.0000  0.0000  837  ASP A C   
6755  O O   . ASP B 840  ? 0.8765 0.8765 0.8765 0.0000  0.0000  0.0000  837  ASP A O   
6756  C CB  . ASP B 840  ? 0.8765 0.8765 0.8765 0.0000  0.0000  0.0000  837  ASP A CB  
6757  C CG  . ASP B 840  ? 0.8765 0.8765 0.8765 0.0000  0.0000  0.0000  837  ASP A CG  
6758  O OD1 . ASP B 840  ? 0.8765 0.8765 0.8765 0.0000  0.0000  0.0000  837  ASP A OD1 
6759  O OD2 . ASP B 840  ? 0.8765 0.8765 0.8765 0.0000  0.0000  0.0000  837  ASP A OD2 
6760  N N   . LEU B 841  ? 0.8045 0.8045 0.8045 0.0000  0.0000  0.0000  838  LEU A N   
6761  C CA  . LEU B 841  ? 0.8045 0.8045 0.8045 0.0000  0.0000  0.0000  838  LEU A CA  
6762  C C   . LEU B 841  ? 0.8045 0.8045 0.8045 0.0000  0.0000  0.0000  838  LEU A C   
6763  O O   . LEU B 841  ? 0.8045 0.8045 0.8045 0.0000  0.0000  0.0000  838  LEU A O   
6764  C CB  . LEU B 841  ? 0.8045 0.8045 0.8045 0.0000  0.0000  0.0000  838  LEU A CB  
6765  C CG  . LEU B 841  ? 0.8045 0.8045 0.8045 0.0000  0.0000  0.0000  838  LEU A CG  
6766  C CD1 . LEU B 841  ? 0.8045 0.8045 0.8045 0.0000  0.0000  0.0000  838  LEU A CD1 
6767  C CD2 . LEU B 841  ? 0.8045 0.8045 0.8045 0.0000  0.0000  0.0000  838  LEU A CD2 
6768  N N   . SER B 842  ? 0.8062 0.8062 0.8062 0.0000  0.0000  0.0000  839  SER A N   
6769  C CA  . SER B 842  ? 0.8062 0.8062 0.8062 0.0000  0.0000  0.0000  839  SER A CA  
6770  C C   . SER B 842  ? 0.8062 0.8062 0.8062 0.0000  0.0000  0.0000  839  SER A C   
6771  O O   . SER B 842  ? 0.8062 0.8062 0.8062 0.0000  0.0000  0.0000  839  SER A O   
6772  C CB  . SER B 842  ? 0.8062 0.8062 0.8062 0.0000  0.0000  0.0000  839  SER A CB  
6773  O OG  . SER B 842  ? 0.8062 0.8062 0.8062 0.0000  0.0000  0.0000  839  SER A OG  
6774  N N   . ASP B 843  ? 0.8388 0.8388 0.8388 0.0000  0.0000  0.0000  840  ASP A N   
6775  C CA  . ASP B 843  ? 0.8388 0.8388 0.8388 0.0000  0.0000  0.0000  840  ASP A CA  
6776  C C   . ASP B 843  ? 0.8388 0.8388 0.8388 0.0000  0.0000  0.0000  840  ASP A C   
6777  O O   . ASP B 843  ? 0.8388 0.8388 0.8388 0.0000  0.0000  0.0000  840  ASP A O   
6778  C CB  . ASP B 843  ? 0.8388 0.8388 0.8388 0.0000  0.0000  0.0000  840  ASP A CB  
6779  C CG  . ASP B 843  ? 0.8388 0.8388 0.8388 0.0000  0.0000  0.0000  840  ASP A CG  
6780  O OD1 . ASP B 843  ? 0.8388 0.8388 0.8388 0.0000  0.0000  0.0000  840  ASP A OD1 
6781  O OD2 . ASP B 843  ? 0.8388 0.8388 0.8388 0.0000  0.0000  0.0000  840  ASP A OD2 
6782  N N   . GLU B 844  ? 0.8035 0.8035 0.8035 0.0000  0.0000  0.0000  841  GLU A N   
6783  C CA  . GLU B 844  ? 0.8035 0.8035 0.8035 0.0000  0.0000  0.0000  841  GLU A CA  
6784  C C   . GLU B 844  ? 0.8035 0.8035 0.8035 0.0000  0.0000  0.0000  841  GLU A C   
6785  O O   . GLU B 844  ? 0.8035 0.8035 0.8035 0.0000  0.0000  0.0000  841  GLU A O   
6786  C CB  . GLU B 844  ? 0.8035 0.8035 0.8035 0.0000  0.0000  0.0000  841  GLU A CB  
6787  C CG  . GLU B 844  ? 0.8035 0.8035 0.8035 0.0000  0.0000  0.0000  841  GLU A CG  
6788  C CD  . GLU B 844  ? 0.8035 0.8035 0.8035 0.0000  0.0000  0.0000  841  GLU A CD  
6789  O OE1 . GLU B 844  ? 0.8035 0.8035 0.8035 0.0000  0.0000  0.0000  841  GLU A OE1 
6790  O OE2 . GLU B 844  ? 0.8035 0.8035 0.8035 0.0000  0.0000  0.0000  841  GLU A OE2 
6791  N N   . ALA B 845  ? 0.7739 0.7739 0.7739 0.0000  0.0000  0.0000  842  ALA A N   
6792  C CA  . ALA B 845  ? 0.7739 0.7739 0.7739 0.0000  0.0000  0.0000  842  ALA A CA  
6793  C C   . ALA B 845  ? 0.7739 0.7739 0.7739 0.0000  0.0000  0.0000  842  ALA A C   
6794  O O   . ALA B 845  ? 0.7739 0.7739 0.7739 0.0000  0.0000  0.0000  842  ALA A O   
6795  C CB  . ALA B 845  ? 0.7739 0.7739 0.7739 0.0000  0.0000  0.0000  842  ALA A CB  
6796  N N   . ARG B 846  ? 0.7683 0.7683 0.7683 0.0000  0.0000  0.0000  843  ARG A N   
6797  C CA  . ARG B 846  ? 0.7683 0.7683 0.7683 0.0000  0.0000  0.0000  843  ARG A CA  
6798  C C   . ARG B 846  ? 0.7683 0.7683 0.7683 0.0000  0.0000  0.0000  843  ARG A C   
6799  O O   . ARG B 846  ? 0.7683 0.7683 0.7683 0.0000  0.0000  0.0000  843  ARG A O   
6800  C CB  . ARG B 846  ? 0.7683 0.7683 0.7683 0.0000  0.0000  0.0000  843  ARG A CB  
6801  C CG  . ARG B 846  ? 0.7683 0.7683 0.7683 0.0000  0.0000  0.0000  843  ARG A CG  
6802  C CD  . ARG B 846  ? 0.7683 0.7683 0.7683 0.0000  0.0000  0.0000  843  ARG A CD  
6803  N NE  . ARG B 846  ? 0.7683 0.7683 0.7683 0.0000  0.0000  0.0000  843  ARG A NE  
6804  C CZ  . ARG B 846  ? 0.7683 0.7683 0.7683 0.0000  0.0000  0.0000  843  ARG A CZ  
6805  N NH1 . ARG B 846  ? 0.7683 0.7683 0.7683 0.0000  0.0000  0.0000  843  ARG A NH1 
6806  N NH2 . ARG B 846  ? 0.7683 0.7683 0.7683 0.0000  0.0000  0.0000  843  ARG A NH2 
6807  N N   . ALA B 847  ? 0.7263 0.7263 0.7263 0.0000  0.0000  0.0000  844  ALA A N   
6808  C CA  . ALA B 847  ? 0.7263 0.7263 0.7263 0.0000  0.0000  0.0000  844  ALA A CA  
6809  C C   . ALA B 847  ? 0.7263 0.7263 0.7263 0.0000  0.0000  0.0000  844  ALA A C   
6810  O O   . ALA B 847  ? 0.7263 0.7263 0.7263 0.0000  0.0000  0.0000  844  ALA A O   
6811  C CB  . ALA B 847  ? 0.7263 0.7263 0.7263 0.0000  0.0000  0.0000  844  ALA A CB  
6812  N N   . LEU B 848  ? 0.7342 0.7342 0.7342 0.0000  0.0000  0.0000  845  LEU A N   
6813  C CA  . LEU B 848  ? 0.7342 0.7342 0.7342 0.0000  0.0000  0.0000  845  LEU A CA  
6814  C C   . LEU B 848  ? 0.7342 0.7342 0.7342 0.0000  0.0000  0.0000  845  LEU A C   
6815  O O   . LEU B 848  ? 0.7342 0.7342 0.7342 0.0000  0.0000  0.0000  845  LEU A O   
6816  C CB  . LEU B 848  ? 0.7342 0.7342 0.7342 0.0000  0.0000  0.0000  845  LEU A CB  
6817  C CG  . LEU B 848  ? 0.7342 0.7342 0.7342 0.0000  0.0000  0.0000  845  LEU A CG  
6818  C CD1 . LEU B 848  ? 0.7342 0.7342 0.7342 0.0000  0.0000  0.0000  845  LEU A CD1 
6819  C CD2 . LEU B 848  ? 0.7342 0.7342 0.7342 0.0000  0.0000  0.0000  845  LEU A CD2 
6820  N N   . LEU B 849  ? 0.7106 0.7106 0.7106 0.0000  0.0000  0.0000  846  LEU A N   
6821  C CA  . LEU B 849  ? 0.7106 0.7106 0.7106 0.0000  0.0000  0.0000  846  LEU A CA  
6822  C C   . LEU B 849  ? 0.7106 0.7106 0.7106 0.0000  0.0000  0.0000  846  LEU A C   
6823  O O   . LEU B 849  ? 0.7106 0.7106 0.7106 0.0000  0.0000  0.0000  846  LEU A O   
6824  C CB  . LEU B 849  ? 0.7106 0.7106 0.7106 0.0000  0.0000  0.0000  846  LEU A CB  
6825  C CG  . LEU B 849  ? 0.7106 0.7106 0.7106 0.0000  0.0000  0.0000  846  LEU A CG  
6826  C CD1 . LEU B 849  ? 0.7106 0.7106 0.7106 0.0000  0.0000  0.0000  846  LEU A CD1 
6827  C CD2 . LEU B 849  ? 0.7106 0.7106 0.7106 0.0000  0.0000  0.0000  846  LEU A CD2 
6828  N N   . PRO B 850  ? 0.7041 0.7041 0.7041 0.0000  0.0000  0.0000  847  PRO A N   
6829  C CA  . PRO B 850  ? 0.7041 0.7041 0.7041 0.0000  0.0000  0.0000  847  PRO A CA  
6830  C C   . PRO B 850  ? 0.7041 0.7041 0.7041 0.0000  0.0000  0.0000  847  PRO A C   
6831  O O   . PRO B 850  ? 0.7041 0.7041 0.7041 0.0000  0.0000  0.0000  847  PRO A O   
6832  C CB  . PRO B 850  ? 0.7041 0.7041 0.7041 0.0000  0.0000  0.0000  847  PRO A CB  
6833  C CG  . PRO B 850  ? 0.7041 0.7041 0.7041 0.0000  0.0000  0.0000  847  PRO A CG  
6834  C CD  . PRO B 850  ? 0.7041 0.7041 0.7041 0.0000  0.0000  0.0000  847  PRO A CD  
6835  N N   . ASN B 851  ? 0.7369 0.7369 0.7369 0.0000  0.0000  0.0000  848  ASN A N   
6836  C CA  . ASN B 851  ? 0.7369 0.7369 0.7369 0.0000  0.0000  0.0000  848  ASN A CA  
6837  C C   . ASN B 851  ? 0.7369 0.7369 0.7369 0.0000  0.0000  0.0000  848  ASN A C   
6838  O O   . ASN B 851  ? 0.7369 0.7369 0.7369 0.0000  0.0000  0.0000  848  ASN A O   
6839  C CB  . ASN B 851  ? 0.7369 0.7369 0.7369 0.0000  0.0000  0.0000  848  ASN A CB  
6840  C CG  . ASN B 851  ? 0.7369 0.7369 0.7369 0.0000  0.0000  0.0000  848  ASN A CG  
6841  O OD1 . ASN B 851  ? 0.7369 0.7369 0.7369 0.0000  0.0000  0.0000  848  ASN A OD1 
6842  N ND2 . ASN B 851  ? 0.7369 0.7369 0.7369 0.0000  0.0000  0.0000  848  ASN A ND2 
6843  N N   . VAL B 852  ? 0.6462 0.6462 0.6462 0.0000  0.0000  0.0000  849  VAL A N   
6844  C CA  . VAL B 852  ? 0.6462 0.6462 0.6462 0.0000  0.0000  0.0000  849  VAL A CA  
6845  C C   . VAL B 852  ? 0.6462 0.6462 0.6462 0.0000  0.0000  0.0000  849  VAL A C   
6846  O O   . VAL B 852  ? 0.6462 0.6462 0.6462 0.0000  0.0000  0.0000  849  VAL A O   
6847  C CB  . VAL B 852  ? 0.6462 0.6462 0.6462 0.0000  0.0000  0.0000  849  VAL A CB  
6848  C CG1 . VAL B 852  ? 0.6462 0.6462 0.6462 0.0000  0.0000  0.0000  849  VAL A CG1 
6849  C CG2 . VAL B 852  ? 0.6462 0.6462 0.6462 0.0000  0.0000  0.0000  849  VAL A CG2 
6850  N N   . ILE B 853  ? 0.5683 0.5683 0.5683 0.0000  0.0000  0.0000  850  ILE A N   
6851  C CA  . ILE B 853  ? 0.5683 0.5683 0.5683 0.0000  0.0000  0.0000  850  ILE A CA  
6852  C C   . ILE B 853  ? 0.5683 0.5683 0.5683 0.0000  0.0000  0.0000  850  ILE A C   
6853  O O   . ILE B 853  ? 0.5683 0.5683 0.5683 0.0000  0.0000  0.0000  850  ILE A O   
6854  C CB  . ILE B 853  ? 0.5683 0.5683 0.5683 0.0000  0.0000  0.0000  850  ILE A CB  
6855  C CG1 . ILE B 853  ? 0.5683 0.5683 0.5683 0.0000  0.0000  0.0000  850  ILE A CG1 
6856  C CG2 . ILE B 853  ? 0.5683 0.5683 0.5683 0.0000  0.0000  0.0000  850  ILE A CG2 
6857  C CD1 . ILE B 853  ? 0.5683 0.5683 0.5683 0.0000  0.0000  0.0000  850  ILE A CD1 
6858  N N   . THR B 854  ? 0.5806 0.5806 0.5806 0.0000  0.0000  0.0000  851  THR A N   
6859  C CA  . THR B 854  ? 0.5806 0.5806 0.5806 0.0000  0.0000  0.0000  851  THR A CA  
6860  C C   . THR B 854  ? 0.5806 0.5806 0.5806 0.0000  0.0000  0.0000  851  THR A C   
6861  O O   . THR B 854  ? 0.5806 0.5806 0.5806 0.0000  0.0000  0.0000  851  THR A O   
6862  C CB  . THR B 854  ? 0.5806 0.5806 0.5806 0.0000  0.0000  0.0000  851  THR A CB  
6863  O OG1 . THR B 854  ? 0.5806 0.5806 0.5806 0.0000  0.0000  0.0000  851  THR A OG1 
6864  C CG2 . THR B 854  ? 0.5806 0.5806 0.5806 0.0000  0.0000  0.0000  851  THR A CG2 
6865  N N   . LYS B 855  ? 0.5770 0.5770 0.5770 0.0000  0.0000  0.0000  852  LYS A N   
6866  C CA  . LYS B 855  ? 0.5770 0.5770 0.5770 0.0000  0.0000  0.0000  852  LYS A CA  
6867  C C   . LYS B 855  ? 0.5770 0.5770 0.5770 0.0000  0.0000  0.0000  852  LYS A C   
6868  O O   . LYS B 855  ? 0.5770 0.5770 0.5770 0.0000  0.0000  0.0000  852  LYS A O   
6869  C CB  . LYS B 855  ? 0.5770 0.5770 0.5770 0.0000  0.0000  0.0000  852  LYS A CB  
6870  C CG  . LYS B 855  ? 0.5770 0.5770 0.5770 0.0000  0.0000  0.0000  852  LYS A CG  
6871  C CD  . LYS B 855  ? 0.5770 0.5770 0.5770 0.0000  0.0000  0.0000  852  LYS A CD  
6872  C CE  . LYS B 855  ? 0.5770 0.5770 0.5770 0.0000  0.0000  0.0000  852  LYS A CE  
6873  N NZ  . LYS B 855  ? 0.5770 0.5770 0.5770 0.0000  0.0000  0.0000  852  LYS A NZ  
6874  N N   . GLU B 856  ? 0.5978 0.5978 0.5978 0.0000  0.0000  0.0000  853  GLU A N   
6875  C CA  . GLU B 856  ? 0.5978 0.5978 0.5978 0.0000  0.0000  0.0000  853  GLU A CA  
6876  C C   . GLU B 856  ? 0.5978 0.5978 0.5978 0.0000  0.0000  0.0000  853  GLU A C   
6877  O O   . GLU B 856  ? 0.5978 0.5978 0.5978 0.0000  0.0000  0.0000  853  GLU A O   
6883  N N   . VAL B 857  ? 0.6344 0.6344 0.6344 0.0000  0.0000  0.0000  854  VAL A N   
6884  C CA  . VAL B 857  ? 0.6344 0.6344 0.6344 0.0000  0.0000  0.0000  854  VAL A CA  
6885  C C   . VAL B 857  ? 0.6344 0.6344 0.6344 0.0000  0.0000  0.0000  854  VAL A C   
6886  O O   . VAL B 857  ? 0.6344 0.6344 0.6344 0.0000  0.0000  0.0000  854  VAL A O   
6887  C CB  . VAL B 857  ? 0.6344 0.6344 0.6344 0.0000  0.0000  0.0000  854  VAL A CB  
6888  C CG1 . VAL B 857  ? 0.6344 0.6344 0.6344 0.0000  0.0000  0.0000  854  VAL A CG1 
6889  C CG2 . VAL B 857  ? 0.6344 0.6344 0.6344 0.0000  0.0000  0.0000  854  VAL A CG2 
6890  N N   . SER B 858  ? 0.5750 0.5750 0.5750 0.0000  0.0000  0.0000  855  SER A N   
6891  C CA  . SER B 858  ? 0.5750 0.5750 0.5750 0.0000  0.0000  0.0000  855  SER A CA  
6892  C C   . SER B 858  ? 0.5750 0.5750 0.5750 0.0000  0.0000  0.0000  855  SER A C   
6893  O O   . SER B 858  ? 0.5750 0.5750 0.5750 0.0000  0.0000  0.0000  855  SER A O   
6894  C CB  . SER B 858  ? 0.5750 0.5750 0.5750 0.0000  0.0000  0.0000  855  SER A CB  
6895  O OG  . SER B 858  ? 0.5750 0.5750 0.5750 0.0000  0.0000  0.0000  855  SER A OG  
6896  N N   . HIS B 859  ? 0.5782 0.5782 0.5782 0.0000  0.0000  0.0000  856  HIS A N   
6897  C CA  . HIS B 859  ? 0.5782 0.5782 0.5782 0.0000  0.0000  0.0000  856  HIS A CA  
6898  C C   . HIS B 859  ? 0.5782 0.5782 0.5782 0.0000  0.0000  0.0000  856  HIS A C   
6899  O O   . HIS B 859  ? 0.5782 0.5782 0.5782 0.0000  0.0000  0.0000  856  HIS A O   
6900  C CB  . HIS B 859  ? 0.5782 0.5782 0.5782 0.0000  0.0000  0.0000  856  HIS A CB  
6901  C CG  . HIS B 859  ? 0.5782 0.5782 0.5782 0.0000  0.0000  0.0000  856  HIS A CG  
6902  N ND1 . HIS B 859  ? 0.5782 0.5782 0.5782 0.0000  0.0000  0.0000  856  HIS A ND1 
6903  C CD2 . HIS B 859  ? 0.5782 0.5782 0.5782 0.0000  0.0000  0.0000  856  HIS A CD2 
6904  C CE1 . HIS B 859  ? 0.5782 0.5782 0.5782 0.0000  0.0000  0.0000  856  HIS A CE1 
6905  N NE2 . HIS B 859  ? 0.5782 0.5782 0.5782 0.0000  0.0000  0.0000  856  HIS A NE2 
6906  N N   . GLU B 860  ? 0.6196 0.6196 0.6196 0.0000  0.0000  0.0000  857  GLU A N   
6907  C CA  . GLU B 860  ? 0.6196 0.6196 0.6196 0.0000  0.0000  0.0000  857  GLU A CA  
6908  C C   . GLU B 860  ? 0.6196 0.6196 0.6196 0.0000  0.0000  0.0000  857  GLU A C   
6909  O O   . GLU B 860  ? 0.6196 0.6196 0.6196 0.0000  0.0000  0.0000  857  GLU A O   
6910  C CB  . GLU B 860  ? 0.6196 0.6196 0.6196 0.0000  0.0000  0.0000  857  GLU A CB  
6911  C CG  . GLU B 860  ? 0.6196 0.6196 0.6196 0.0000  0.0000  0.0000  857  GLU A CG  
6912  C CD  . GLU B 860  ? 0.6196 0.6196 0.6196 0.0000  0.0000  0.0000  857  GLU A CD  
6913  O OE1 . GLU B 860  ? 0.6196 0.6196 0.6196 0.0000  0.0000  0.0000  857  GLU A OE1 
6914  O OE2 . GLU B 860  ? 0.6196 0.6196 0.6196 0.0000  0.0000  0.0000  857  GLU A OE2 
6915  N N   . ILE B 861  ? 0.5731 0.5731 0.5731 0.0000  0.0000  0.0000  858  ILE A N   
6916  C CA  . ILE B 861  ? 0.5731 0.5731 0.5731 0.0000  0.0000  0.0000  858  ILE A CA  
6917  C C   . ILE B 861  ? 0.5731 0.5731 0.5731 0.0000  0.0000  0.0000  858  ILE A C   
6918  O O   . ILE B 861  ? 0.5731 0.5731 0.5731 0.0000  0.0000  0.0000  858  ILE A O   
6919  C CB  . ILE B 861  ? 0.5731 0.5731 0.5731 0.0000  0.0000  0.0000  858  ILE A CB  
6920  C CG1 . ILE B 861  ? 0.5731 0.5731 0.5731 0.0000  0.0000  0.0000  858  ILE A CG1 
6921  C CG2 . ILE B 861  ? 0.5731 0.5731 0.5731 0.0000  0.0000  0.0000  858  ILE A CG2 
6922  C CD1 . ILE B 861  ? 0.5731 0.5731 0.5731 0.0000  0.0000  0.0000  858  ILE A CD1 
6923  N N   . ILE B 862  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  859  ILE A N   
6924  C CA  . ILE B 862  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  859  ILE A CA  
6925  C C   . ILE B 862  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  859  ILE A C   
6926  O O   . ILE B 862  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  859  ILE A O   
6927  C CB  . ILE B 862  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  859  ILE A CB  
6928  C CG1 . ILE B 862  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  859  ILE A CG1 
6929  C CG2 . ILE B 862  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  859  ILE A CG2 
6930  C CD1 . ILE B 862  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  859  ILE A CD1 
6931  N N   . LYS B 863  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  860  LYS A N   
6932  C CA  . LYS B 863  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  860  LYS A CA  
6933  C C   . LYS B 863  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  860  LYS A C   
6934  O O   . LYS B 863  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  860  LYS A O   
6935  C CB  . LYS B 863  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  860  LYS A CB  
6936  C CG  . LYS B 863  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  860  LYS A CG  
6937  C CD  . LYS B 863  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  860  LYS A CD  
6938  C CE  . LYS B 863  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  860  LYS A CE  
6939  N NZ  . LYS B 863  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  860  LYS A NZ  
6940  N N   . ASP B 864  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  861  ASP A N   
6941  C CA  . ASP B 864  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  861  ASP A CA  
6942  C C   . ASP B 864  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  861  ASP A C   
6943  O O   . ASP B 864  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  861  ASP A O   
6948  N N   . ARG B 865  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  862  ARG A N   
6949  C CA  . ARG B 865  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  862  ARG A CA  
6950  C C   . ARG B 865  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  862  ARG A C   
6951  O O   . ARG B 865  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  862  ARG A O   
6959  N N   . ARG B 866  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  863  ARG A N   
6960  C CA  . ARG B 866  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  863  ARG A CA  
6961  C C   . ARG B 866  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  863  ARG A C   
6962  O O   . ARG B 866  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  863  ARG A O   
6963  C CB  . ARG B 866  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  863  ARG A CB  
6964  C CG  . ARG B 866  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  863  ARG A CG  
6965  C CD  . ARG B 866  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  863  ARG A CD  
6966  N NE  . ARG B 866  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  863  ARG A NE  
6967  C CZ  . ARG B 866  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  863  ARG A CZ  
6968  N NH1 . ARG B 866  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  863  ARG A NH1 
6969  N NH2 . ARG B 866  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  863  ARG A NH2 
6970  N N   . PHE B 867  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  864  PHE A N   
6971  C CA  . PHE B 867  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  864  PHE A CA  
6972  C C   . PHE B 867  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  864  PHE A C   
6973  O O   . PHE B 867  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  864  PHE A O   
6974  C CB  . PHE B 867  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  864  PHE A CB  
6975  C CG  . PHE B 867  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  864  PHE A CG  
6976  C CD1 . PHE B 867  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  864  PHE A CD1 
6977  C CD2 . PHE B 867  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  864  PHE A CD2 
6978  C CE1 . PHE B 867  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  864  PHE A CE1 
6979  C CE2 . PHE B 867  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  864  PHE A CE2 
6980  C CZ  . PHE B 867  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  864  PHE A CZ  
6981  N N   . THR B 868  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  865  THR A N   
6982  C CA  . THR B 868  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  865  THR A CA  
6983  C C   . THR B 868  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  865  THR A C   
6984  O O   . THR B 868  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  865  THR A O   
6985  C CB  . THR B 868  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  865  THR A CB  
6986  O OG1 . THR B 868  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  865  THR A OG1 
6987  C CG2 . THR B 868  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  865  THR A CG2 
6988  N N   . SER B 869  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  866  SER A N   
6989  C CA  . SER B 869  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  866  SER A CA  
6990  C C   . SER B 869  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  866  SER A C   
6991  O O   . SER B 869  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  866  SER A O   
6992  C CB  . SER B 869  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  866  SER A CB  
6993  O OG  . SER B 869  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  866  SER A OG  
6994  N N   . ASP B 870  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  867  ASP A N   
6995  C CA  . ASP B 870  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  867  ASP A CA  
6996  C C   . ASP B 870  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  867  ASP A C   
6997  O O   . ASP B 870  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  867  ASP A O   
6998  C CB  . ASP B 870  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  867  ASP A CB  
6999  C CG  . ASP B 870  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  867  ASP A CG  
7000  O OD1 . ASP B 870  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  867  ASP A OD1 
7001  O OD2 . ASP B 870  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  867  ASP A OD2 
7002  N N   . LYS B 871  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  868  LYS A N   
7003  C CA  . LYS B 871  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  868  LYS A CA  
7004  C C   . LYS B 871  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  868  LYS A C   
7005  O O   . LYS B 871  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  868  LYS A O   
7006  C CB  . LYS B 871  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  868  LYS A CB  
7007  C CG  . LYS B 871  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  868  LYS A CG  
7008  C CD  . LYS B 871  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  868  LYS A CD  
7009  C CE  . LYS B 871  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  868  LYS A CE  
7010  N NZ  . LYS B 871  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  868  LYS A NZ  
7011  N N   . PHE B 872  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  869  PHE A N   
7012  C CA  . PHE B 872  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  869  PHE A CA  
7013  C C   . PHE B 872  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  869  PHE A C   
7014  O O   . PHE B 872  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  869  PHE A O   
7015  C CB  . PHE B 872  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  869  PHE A CB  
7016  C CG  . PHE B 872  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  869  PHE A CG  
7017  C CD1 . PHE B 872  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  869  PHE A CD1 
7018  C CD2 . PHE B 872  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  869  PHE A CD2 
7019  C CE1 . PHE B 872  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  869  PHE A CE1 
7020  C CE2 . PHE B 872  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  869  PHE A CE2 
7021  C CZ  . PHE B 872  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  869  PHE A CZ  
7022  N N   . PHE B 873  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  870  PHE A N   
7023  C CA  . PHE B 873  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  870  PHE A CA  
7024  C C   . PHE B 873  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  870  PHE A C   
7025  O O   . PHE B 873  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  870  PHE A O   
7026  C CB  . PHE B 873  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  870  PHE A CB  
7027  C CG  . PHE B 873  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  870  PHE A CG  
7028  C CD1 . PHE B 873  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  870  PHE A CD1 
7029  C CD2 . PHE B 873  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  870  PHE A CD2 
7030  C CE1 . PHE B 873  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  870  PHE A CE1 
7031  C CE2 . PHE B 873  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  870  PHE A CE2 
7032  C CZ  . PHE B 873  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  870  PHE A CZ  
7033  N N   . PHE B 874  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  871  PHE A N   
7034  C CA  . PHE B 874  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  871  PHE A CA  
7035  C C   . PHE B 874  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  871  PHE A C   
7036  O O   . PHE B 874  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  871  PHE A O   
7037  C CB  . PHE B 874  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  871  PHE A CB  
7038  C CG  . PHE B 874  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  871  PHE A CG  
7039  C CD1 . PHE B 874  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  871  PHE A CD1 
7040  C CD2 . PHE B 874  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  871  PHE A CD2 
7041  C CE1 . PHE B 874  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  871  PHE A CE1 
7042  C CE2 . PHE B 874  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  871  PHE A CE2 
7043  C CZ  . PHE B 874  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  871  PHE A CZ  
7044  N N   . HIS B 875  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  872  HIS A N   
7045  C CA  . HIS B 875  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  872  HIS A CA  
7046  C C   . HIS B 875  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  872  HIS A C   
7047  O O   . HIS B 875  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  872  HIS A O   
7048  C CB  . HIS B 875  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  872  HIS A CB  
7049  C CG  . HIS B 875  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  872  HIS A CG  
7050  N ND1 . HIS B 875  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  872  HIS A ND1 
7051  C CD2 . HIS B 875  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  872  HIS A CD2 
7052  C CE1 . HIS B 875  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  872  HIS A CE1 
7053  N NE2 . HIS B 875  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  872  HIS A NE2 
7054  N N   . VAL B 876  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  873  VAL A N   
7055  C CA  . VAL B 876  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  873  VAL A CA  
7056  C C   . VAL B 876  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  873  VAL A C   
7057  O O   . VAL B 876  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  873  VAL A O   
7058  C CB  . VAL B 876  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  873  VAL A CB  
7059  C CG1 . VAL B 876  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  873  VAL A CG1 
7060  C CG2 . VAL B 876  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  873  VAL A CG2 
7061  N N   . PRO B 877  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  874  PRO A N   
7062  C CA  . PRO B 877  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  874  PRO A CA  
7063  C C   . PRO B 877  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  874  PRO A C   
7064  O O   . PRO B 877  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  874  PRO A O   
7065  C CB  . PRO B 877  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  874  PRO A CB  
7066  C CG  . PRO B 877  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  874  PRO A CG  
7067  C CD  . PRO B 877  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  874  PRO A CD  
7068  N N   . ILE B 878  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  875  ILE A N   
7069  C CA  . ILE B 878  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  875  ILE A CA  
7070  C C   . ILE B 878  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  875  ILE A C   
7071  O O   . ILE B 878  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  875  ILE A O   
7072  C CB  . ILE B 878  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  875  ILE A CB  
7073  C CG1 . ILE B 878  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  875  ILE A CG1 
7074  C CG2 . ILE B 878  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  875  ILE A CG2 
7075  C CD1 . ILE B 878  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  875  ILE A CD1 
7076  N N   . THR B 879  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  876  THR A N   
7077  C CA  . THR B 879  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  876  THR A CA  
7078  C C   . THR B 879  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  876  THR A C   
7079  O O   . THR B 879  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  876  THR A O   
7080  C CB  . THR B 879  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  876  THR A CB  
7081  O OG1 . THR B 879  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  876  THR A OG1 
7082  C CG2 . THR B 879  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  876  THR A CG2 
7083  N N   . LEU B 880  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  877  LEU A N   
7084  C CA  . LEU B 880  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  877  LEU A CA  
7085  C C   . LEU B 880  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  877  LEU A C   
7086  O O   . LEU B 880  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  877  LEU A O   
7087  C CB  . LEU B 880  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  877  LEU A CB  
7088  C CG  . LEU B 880  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  877  LEU A CG  
7089  C CD1 . LEU B 880  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  877  LEU A CD1 
7090  C CD2 . LEU B 880  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  877  LEU A CD2 
7091  N N   . ASN B 881  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  878  ASN A N   
7092  C CA  . ASN B 881  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  878  ASN A CA  
7093  C C   . ASN B 881  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  878  ASN A C   
7094  O O   . ASN B 881  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  878  ASN A O   
7095  C CB  . ASN B 881  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  878  ASN A CB  
7096  C CG  . ASN B 881  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  878  ASN A CG  
7097  O OD1 . ASN B 881  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  878  ASN A OD1 
7098  N ND2 . ASN B 881  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  878  ASN A ND2 
7099  N N   . TYR B 882  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  879  TYR A N   
7100  C CA  . TYR B 882  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  879  TYR A CA  
7101  C C   . TYR B 882  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  879  TYR A C   
7102  O O   . TYR B 882  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  879  TYR A O   
7103  C CB  . TYR B 882  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  879  TYR A CB  
7104  C CG  . TYR B 882  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  879  TYR A CG  
7105  C CD1 . TYR B 882  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  879  TYR A CD1 
7106  C CD2 . TYR B 882  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  879  TYR A CD2 
7107  C CE1 . TYR B 882  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  879  TYR A CE1 
7108  C CE2 . TYR B 882  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  879  TYR A CE2 
7109  C CZ  . TYR B 882  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  879  TYR A CZ  
7110  O OH  . TYR B 882  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  879  TYR A OH  
7111  N N   . GLN B 883  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  880  GLN A N   
7112  C CA  . GLN B 883  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  880  GLN A CA  
7113  C C   . GLN B 883  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  880  GLN A C   
7114  O O   . GLN B 883  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  880  GLN A O   
7115  C CB  . GLN B 883  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  880  GLN A CB  
7116  C CG  . GLN B 883  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  880  GLN A CG  
7117  C CD  . GLN B 883  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  880  GLN A CD  
7118  O OE1 . GLN B 883  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  880  GLN A OE1 
7119  N NE2 . GLN B 883  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  880  GLN A NE2 
7120  N N   . ALA B 884  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  881  ALA A N   
7121  C CA  . ALA B 884  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  881  ALA A CA  
7122  C C   . ALA B 884  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  881  ALA A C   
7123  O O   . ALA B 884  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  881  ALA A O   
7124  C CB  . ALA B 884  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  881  ALA A CB  
7125  N N   . ALA B 885  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  882  ALA A N   
7126  C CA  . ALA B 885  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  882  ALA A CA  
7127  C C   . ALA B 885  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  882  ALA A C   
7128  O O   . ALA B 885  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  882  ALA A O   
7129  C CB  . ALA B 885  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  882  ALA A CB  
7130  N N   . ASN B 886  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  883  ASN A N   
7131  C CA  . ASN B 886  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  883  ASN A CA  
7132  C C   . ASN B 886  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  883  ASN A C   
7133  O O   . ASN B 886  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  883  ASN A O   
7134  C CB  . ASN B 886  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  883  ASN A CB  
7135  C CG  . ASN B 886  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  883  ASN A CG  
7136  O OD1 . ASN B 886  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  883  ASN A OD1 
7137  N ND2 . ASN B 886  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  883  ASN A ND2 
7138  N N   . SER B 887  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  884  SER A N   
7139  C CA  . SER B 887  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  884  SER A CA  
7140  C C   . SER B 887  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  884  SER A C   
7141  O O   . SER B 887  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  884  SER A O   
7142  C CB  . SER B 887  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  884  SER A CB  
7143  O OG  . SER B 887  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  884  SER A OG  
7144  N N   . PRO B 888  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  885  PRO A N   
7145  C CA  . PRO B 888  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  885  PRO A CA  
7146  C C   . PRO B 888  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  885  PRO A C   
7147  O O   . PRO B 888  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  885  PRO A O   
7148  C CB  . PRO B 888  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  885  PRO A CB  
7149  C CG  . PRO B 888  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  885  PRO A CG  
7150  C CD  . PRO B 888  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  885  PRO A CD  
7151  N N   . SER B 889  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  886  SER A N   
7152  C CA  . SER B 889  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  886  SER A CA  
7153  C C   . SER B 889  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  886  SER A C   
7154  O O   . SER B 889  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  886  SER A O   
7155  C CB  . SER B 889  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  886  SER A CB  
7156  O OG  . SER B 889  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  886  SER A OG  
7157  N N   . LYS B 890  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  887  LYS A N   
7158  C CA  . LYS B 890  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  887  LYS A CA  
7159  C C   . LYS B 890  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  887  LYS A C   
7160  O O   . LYS B 890  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  887  LYS A O   
7161  C CB  . LYS B 890  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  887  LYS A CB  
7162  C CG  . LYS B 890  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  887  LYS A CG  
7163  C CD  . LYS B 890  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  887  LYS A CD  
7164  C CE  . LYS B 890  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  887  LYS A CE  
7165  N NZ  . LYS B 890  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  887  LYS A NZ  
7166  N N   . PHE B 891  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  888  PHE A N   
7167  C CA  . PHE B 891  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  888  PHE A CA  
7168  C C   . PHE B 891  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  888  PHE A C   
7169  O O   . PHE B 891  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  888  PHE A O   
7170  C CB  . PHE B 891  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  888  PHE A CB  
7171  C CG  . PHE B 891  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  888  PHE A CG  
7172  C CD1 . PHE B 891  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  888  PHE A CD1 
7173  C CD2 . PHE B 891  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  888  PHE A CD2 
7174  C CE1 . PHE B 891  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  888  PHE A CE1 
7175  C CE2 . PHE B 891  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  888  PHE A CE2 
7176  C CZ  . PHE B 891  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  888  PHE A CZ  
7177  N N   . ASN B 892  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  889  ASN A N   
7178  C CA  . ASN B 892  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  889  ASN A CA  
7179  C C   . ASN B 892  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  889  ASN A C   
7180  O O   . ASN B 892  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  889  ASN A O   
7181  C CB  . ASN B 892  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  889  ASN A CB  
7182  C CG  . ASN B 892  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  889  ASN A CG  
7183  O OD1 . ASN B 892  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  889  ASN A OD1 
7184  N ND2 . ASN B 892  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  889  ASN A ND2 
7185  N N   . GLN B 893  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  890  GLN A N   
7186  C CA  . GLN B 893  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  890  GLN A CA  
7187  C C   . GLN B 893  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  890  GLN A C   
7188  O O   . GLN B 893  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  890  GLN A O   
7189  C CB  . GLN B 893  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  890  GLN A CB  
7190  C CG  . GLN B 893  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  890  GLN A CG  
7191  C CD  . GLN B 893  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  890  GLN A CD  
7192  O OE1 . GLN B 893  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  890  GLN A OE1 
7193  N NE2 . GLN B 893  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  890  GLN A NE2 
7194  N N   . ARG B 894  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  891  ARG A N   
7195  C CA  . ARG B 894  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  891  ARG A CA  
7196  C C   . ARG B 894  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  891  ARG A C   
7197  O O   . ARG B 894  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  891  ARG A O   
7198  C CB  . ARG B 894  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  891  ARG A CB  
7199  C CG  . ARG B 894  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  891  ARG A CG  
7200  C CD  . ARG B 894  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  891  ARG A CD  
7201  N NE  . ARG B 894  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  891  ARG A NE  
7202  C CZ  . ARG B 894  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  891  ARG A CZ  
7203  N NH1 . ARG B 894  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  891  ARG A NH1 
7204  N NH2 . ARG B 894  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  891  ARG A NH2 
7205  N N   . VAL B 895  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  892  VAL A N   
7206  C CA  . VAL B 895  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  892  VAL A CA  
7207  C C   . VAL B 895  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  892  VAL A C   
7208  O O   . VAL B 895  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  892  VAL A O   
7209  C CB  . VAL B 895  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  892  VAL A CB  
7210  C CG1 . VAL B 895  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  892  VAL A CG1 
7211  C CG2 . VAL B 895  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  892  VAL A CG2 
7212  N N   . ASN B 896  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  893  ASN A N   
7213  C CA  . ASN B 896  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  893  ASN A CA  
7214  C C   . ASN B 896  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  893  ASN A C   
7215  O O   . ASN B 896  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  893  ASN A O   
7216  C CB  . ASN B 896  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  893  ASN A CB  
7217  C CG  . ASN B 896  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  893  ASN A CG  
7218  O OD1 . ASN B 896  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  893  ASN A OD1 
7219  N ND2 . ASN B 896  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  893  ASN A ND2 
7220  N N   . ALA B 897  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  894  ALA A N   
7221  C CA  . ALA B 897  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  894  ALA A CA  
7222  C C   . ALA B 897  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  894  ALA A C   
7223  O O   . ALA B 897  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  894  ALA A O   
7224  C CB  . ALA B 897  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  894  ALA A CB  
7225  N N   . TYR B 898  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  895  TYR A N   
7226  C CA  . TYR B 898  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  895  TYR A CA  
7227  C C   . TYR B 898  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  895  TYR A C   
7228  O O   . TYR B 898  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  895  TYR A O   
7229  C CB  . TYR B 898  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  895  TYR A CB  
7230  C CG  . TYR B 898  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  895  TYR A CG  
7231  C CD1 . TYR B 898  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  895  TYR A CD1 
7232  C CD2 . TYR B 898  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  895  TYR A CD2 
7233  C CE1 . TYR B 898  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  895  TYR A CE1 
7234  C CE2 . TYR B 898  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  895  TYR A CE2 
7235  C CZ  . TYR B 898  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  895  TYR A CZ  
7236  O OH  . TYR B 898  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  895  TYR A OH  
7237  N N   . LEU B 899  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  896  LEU A N   
7238  C CA  . LEU B 899  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  896  LEU A CA  
7239  C C   . LEU B 899  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  896  LEU A C   
7240  O O   . LEU B 899  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  896  LEU A O   
7241  C CB  . LEU B 899  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  896  LEU A CB  
7242  C CG  . LEU B 899  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  896  LEU A CG  
7243  C CD1 . LEU B 899  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  896  LEU A CD1 
7244  C CD2 . LEU B 899  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  896  LEU A CD2 
7245  N N   . LYS B 900  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  897  LYS A N   
7246  C CA  . LYS B 900  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  897  LYS A CA  
7247  C C   . LYS B 900  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  897  LYS A C   
7248  O O   . LYS B 900  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  897  LYS A O   
7249  C CB  . LYS B 900  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  897  LYS A CB  
7250  C CG  . LYS B 900  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  897  LYS A CG  
7251  C CD  . LYS B 900  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  897  LYS A CD  
7252  C CE  . LYS B 900  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  897  LYS A CE  
7253  N NZ  . LYS B 900  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  897  LYS A NZ  
7254  N N   . GLU B 901  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  898  GLU A N   
7255  C CA  . GLU B 901  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  898  GLU A CA  
7256  C C   . GLU B 901  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  898  GLU A C   
7257  O O   . GLU B 901  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  898  GLU A O   
7258  C CB  . GLU B 901  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  898  GLU A CB  
7259  C CG  . GLU B 901  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  898  GLU A CG  
7260  C CD  . GLU B 901  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  898  GLU A CD  
7261  O OE1 . GLU B 901  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  898  GLU A OE1 
7262  O OE2 . GLU B 901  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  898  GLU A OE2 
7263  N N   . HIS B 902  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  899  HIS A N   
7264  C CA  . HIS B 902  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  899  HIS A CA  
7265  C C   . HIS B 902  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  899  HIS A C   
7266  O O   . HIS B 902  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  899  HIS A O   
7267  C CB  . HIS B 902  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  899  HIS A CB  
7268  C CG  . HIS B 902  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  899  HIS A CG  
7269  N ND1 . HIS B 902  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  899  HIS A ND1 
7270  C CD2 . HIS B 902  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  899  HIS A CD2 
7271  C CE1 . HIS B 902  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  899  HIS A CE1 
7272  N NE2 . HIS B 902  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  899  HIS A NE2 
7273  N N   . PRO B 903  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  900  PRO A N   
7274  C CA  . PRO B 903  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  900  PRO A CA  
7275  C C   . PRO B 903  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  900  PRO A C   
7276  O O   . PRO B 903  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  900  PRO A O   
7277  C CB  . PRO B 903  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  900  PRO A CB  
7278  C CG  . PRO B 903  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  900  PRO A CG  
7279  C CD  . PRO B 903  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  900  PRO A CD  
7280  N N   . GLU B 904  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  901  GLU A N   
7281  C CA  . GLU B 904  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  901  GLU A CA  
7282  C C   . GLU B 904  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  901  GLU A C   
7283  O O   . GLU B 904  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  901  GLU A O   
7284  C CB  . GLU B 904  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  901  GLU A CB  
7285  C CG  . GLU B 904  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  901  GLU A CG  
7286  C CD  . GLU B 904  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  901  GLU A CD  
7287  O OE1 . GLU B 904  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  901  GLU A OE1 
7288  O OE2 . GLU B 904  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  901  GLU A OE2 
7289  N N   . THR B 905  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  902  THR A N   
7290  C CA  . THR B 905  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  902  THR A CA  
7291  C C   . THR B 905  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  902  THR A C   
7292  O O   . THR B 905  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  902  THR A O   
7293  C CB  . THR B 905  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  902  THR A CB  
7294  O OG1 . THR B 905  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  902  THR A OG1 
7295  C CG2 . THR B 905  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  902  THR A CG2 
7296  N N   . PRO B 906  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  903  PRO A N   
7297  C CA  . PRO B 906  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  903  PRO A CA  
7298  C C   . PRO B 906  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  903  PRO A C   
7299  O O   . PRO B 906  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  903  PRO A O   
7300  C CB  . PRO B 906  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  903  PRO A CB  
7301  C CG  . PRO B 906  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  903  PRO A CG  
7302  C CD  . PRO B 906  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  903  PRO A CD  
7303  N N   . ILE B 907  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  904  ILE A N   
7304  C CA  . ILE B 907  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  904  ILE A CA  
7305  C C   . ILE B 907  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  904  ILE A C   
7306  O O   . ILE B 907  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  904  ILE A O   
7307  C CB  . ILE B 907  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  904  ILE A CB  
7308  C CG1 . ILE B 907  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  904  ILE A CG1 
7309  C CG2 . ILE B 907  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  904  ILE A CG2 
7310  C CD1 . ILE B 907  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  904  ILE A CD1 
7311  N N   . ILE B 908  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  905  ILE A N   
7312  C CA  . ILE B 908  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  905  ILE A CA  
7313  C C   . ILE B 908  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  905  ILE A C   
7314  O O   . ILE B 908  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  905  ILE A O   
7315  C CB  . ILE B 908  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  905  ILE A CB  
7316  C CG1 . ILE B 908  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  905  ILE A CG1 
7317  C CG2 . ILE B 908  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  905  ILE A CG2 
7318  C CD1 . ILE B 908  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  905  ILE A CD1 
7319  N N   . GLY B 909  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  906  GLY A N   
7320  C CA  . GLY B 909  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  906  GLY A CA  
7321  C C   . GLY B 909  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  906  GLY A C   
7322  O O   . GLY B 909  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  906  GLY A O   
7323  N N   . ILE B 910  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  907  ILE A N   
7324  C CA  . ILE B 910  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  907  ILE A CA  
7325  C C   . ILE B 910  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  907  ILE A C   
7326  O O   . ILE B 910  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  907  ILE A O   
7327  C CB  . ILE B 910  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  907  ILE A CB  
7328  C CG1 . ILE B 910  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  907  ILE A CG1 
7329  C CG2 . ILE B 910  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  907  ILE A CG2 
7330  C CD1 . ILE B 910  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  907  ILE A CD1 
7331  N N   . ASP B 911  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  908  ASP A N   
7332  C CA  . ASP B 911  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  908  ASP A CA  
7333  C C   . ASP B 911  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  908  ASP A C   
7334  O O   . ASP B 911  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  908  ASP A O   
7335  C CB  . ASP B 911  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  908  ASP A CB  
7336  C CG  . ASP B 911  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  908  ASP A CG  
7337  O OD1 . ASP B 911  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  908  ASP A OD1 
7338  O OD2 . ASP B 911  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  908  ASP A OD2 
7339  N N   . ARG B 912  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  909  ARG A N   
7340  C CA  . ARG B 912  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  909  ARG A CA  
7341  C C   . ARG B 912  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  909  ARG A C   
7342  O O   . ARG B 912  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  909  ARG A O   
7343  C CB  . ARG B 912  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  909  ARG A CB  
7344  C CG  . ARG B 912  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  909  ARG A CG  
7345  C CD  . ARG B 912  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  909  ARG A CD  
7346  N NE  . ARG B 912  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  909  ARG A NE  
7347  C CZ  . ARG B 912  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  909  ARG A CZ  
7348  N NH1 . ARG B 912  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  909  ARG A NH1 
7349  N NH2 . ARG B 912  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  909  ARG A NH2 
7350  N N   . GLY B 913  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  910  GLY A N   
7351  C CA  . GLY B 913  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  910  GLY A CA  
7352  C C   . GLY B 913  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  910  GLY A C   
7353  O O   . GLY B 913  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  910  GLY A O   
7354  N N   . GLU B 914  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  911  GLU A N   
7355  C CA  . GLU B 914  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  911  GLU A CA  
7356  C C   . GLU B 914  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  911  GLU A C   
7357  O O   . GLU B 914  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  911  GLU A O   
7358  C CB  . GLU B 914  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  911  GLU A CB  
7359  C CG  . GLU B 914  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  911  GLU A CG  
7360  C CD  . GLU B 914  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  911  GLU A CD  
7361  O OE1 . GLU B 914  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  911  GLU A OE1 
7362  O OE2 . GLU B 914  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  911  GLU A OE2 
7363  N N   . ARG B 915  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  912  ARG A N   
7364  C CA  . ARG B 915  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  912  ARG A CA  
7365  C C   . ARG B 915  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  912  ARG A C   
7366  O O   . ARG B 915  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  912  ARG A O   
7367  C CB  . ARG B 915  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  912  ARG A CB  
7368  C CG  . ARG B 915  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  912  ARG A CG  
7369  C CD  . ARG B 915  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  912  ARG A CD  
7370  N NE  . ARG B 915  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  912  ARG A NE  
7371  C CZ  . ARG B 915  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  912  ARG A CZ  
7372  N NH1 . ARG B 915  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  912  ARG A NH1 
7373  N NH2 . ARG B 915  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  912  ARG A NH2 
7374  N N   . ASN B 916  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  913  ASN A N   
7375  C CA  . ASN B 916  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  913  ASN A CA  
7376  C C   . ASN B 916  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  913  ASN A C   
7377  O O   . ASN B 916  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  913  ASN A O   
7378  C CB  . ASN B 916  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  913  ASN A CB  
7379  C CG  . ASN B 916  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  913  ASN A CG  
7380  O OD1 . ASN B 916  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  913  ASN A OD1 
7381  N ND2 . ASN B 916  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  913  ASN A ND2 
7382  N N   . LEU B 917  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  914  LEU A N   
7383  C CA  . LEU B 917  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  914  LEU A CA  
7384  C C   . LEU B 917  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  914  LEU A C   
7385  O O   . LEU B 917  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  914  LEU A O   
7386  C CB  . LEU B 917  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  914  LEU A CB  
7387  C CG  . LEU B 917  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  914  LEU A CG  
7388  C CD1 . LEU B 917  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  914  LEU A CD1 
7389  C CD2 . LEU B 917  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  914  LEU A CD2 
7390  N N   . ILE B 918  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  915  ILE A N   
7391  C CA  . ILE B 918  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  915  ILE A CA  
7392  C C   . ILE B 918  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  915  ILE A C   
7393  O O   . ILE B 918  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  915  ILE A O   
7394  C CB  . ILE B 918  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  915  ILE A CB  
7395  C CG1 . ILE B 918  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  915  ILE A CG1 
7396  C CG2 . ILE B 918  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  915  ILE A CG2 
7397  C CD1 . ILE B 918  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  915  ILE A CD1 
7398  N N   . TYR B 919  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  916  TYR A N   
7399  C CA  . TYR B 919  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  916  TYR A CA  
7400  C C   . TYR B 919  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  916  TYR A C   
7401  O O   . TYR B 919  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  916  TYR A O   
7402  C CB  . TYR B 919  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  916  TYR A CB  
7403  C CG  . TYR B 919  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  916  TYR A CG  
7404  C CD1 . TYR B 919  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  916  TYR A CD1 
7405  C CD2 . TYR B 919  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  916  TYR A CD2 
7406  C CE1 . TYR B 919  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  916  TYR A CE1 
7407  C CE2 . TYR B 919  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  916  TYR A CE2 
7408  C CZ  . TYR B 919  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  916  TYR A CZ  
7409  O OH  . TYR B 919  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  916  TYR A OH  
7410  N N   . ILE B 920  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  917  ILE A N   
7411  C CA  . ILE B 920  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  917  ILE A CA  
7412  C C   . ILE B 920  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  917  ILE A C   
7413  O O   . ILE B 920  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  917  ILE A O   
7414  C CB  . ILE B 920  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  917  ILE A CB  
7415  C CG1 . ILE B 920  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  917  ILE A CG1 
7416  C CG2 . ILE B 920  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  917  ILE A CG2 
7417  C CD1 . ILE B 920  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  917  ILE A CD1 
7418  N N   . THR B 921  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  918  THR A N   
7419  C CA  . THR B 921  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  918  THR A CA  
7420  C C   . THR B 921  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  918  THR A C   
7421  O O   . THR B 921  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  918  THR A O   
7422  C CB  . THR B 921  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  918  THR A CB  
7423  O OG1 . THR B 921  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  918  THR A OG1 
7424  C CG2 . THR B 921  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  918  THR A CG2 
7425  N N   . VAL B 922  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  919  VAL A N   
7426  C CA  . VAL B 922  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  919  VAL A CA  
7427  C C   . VAL B 922  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  919  VAL A C   
7428  O O   . VAL B 922  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  919  VAL A O   
7429  C CB  . VAL B 922  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  919  VAL A CB  
7430  C CG1 . VAL B 922  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  919  VAL A CG1 
7431  C CG2 . VAL B 922  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  919  VAL A CG2 
7432  N N   . ILE B 923  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  920  ILE A N   
7433  C CA  . ILE B 923  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  920  ILE A CA  
7434  C C   . ILE B 923  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  920  ILE A C   
7435  O O   . ILE B 923  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  920  ILE A O   
7436  C CB  . ILE B 923  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  920  ILE A CB  
7437  C CG1 . ILE B 923  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  920  ILE A CG1 
7438  C CG2 . ILE B 923  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  920  ILE A CG2 
7439  C CD1 . ILE B 923  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  920  ILE A CD1 
7440  N N   . ASP B 924  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  921  ASP A N   
7441  C CA  . ASP B 924  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  921  ASP A CA  
7442  C C   . ASP B 924  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  921  ASP A C   
7443  O O   . ASP B 924  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  921  ASP A O   
7444  C CB  . ASP B 924  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  921  ASP A CB  
7445  C CG  . ASP B 924  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  921  ASP A CG  
7446  O OD1 . ASP B 924  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  921  ASP A OD1 
7447  O OD2 . ASP B 924  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  921  ASP A OD2 
7448  N N   . SER B 925  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  922  SER A N   
7449  C CA  . SER B 925  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  922  SER A CA  
7450  C C   . SER B 925  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  922  SER A C   
7451  O O   . SER B 925  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  922  SER A O   
7452  C CB  . SER B 925  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  922  SER A CB  
7453  O OG  . SER B 925  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  922  SER A OG  
7454  N N   . THR B 926  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  923  THR A N   
7455  C CA  . THR B 926  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  923  THR A CA  
7456  C C   . THR B 926  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  923  THR A C   
7457  O O   . THR B 926  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  923  THR A O   
7458  C CB  . THR B 926  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  923  THR A CB  
7459  O OG1 . THR B 926  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  923  THR A OG1 
7460  C CG2 . THR B 926  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  923  THR A CG2 
7461  N N   . GLY B 927  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  924  GLY A N   
7462  C CA  . GLY B 927  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  924  GLY A CA  
7463  C C   . GLY B 927  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  924  GLY A C   
7464  O O   . GLY B 927  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  924  GLY A O   
7465  N N   . LYS B 928  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  925  LYS A N   
7466  C CA  . LYS B 928  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  925  LYS A CA  
7467  C C   . LYS B 928  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  925  LYS A C   
7468  O O   . LYS B 928  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  925  LYS A O   
7474  N N   . ILE B 929  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  926  ILE A N   
7475  C CA  . ILE B 929  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  926  ILE A CA  
7476  C C   . ILE B 929  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  926  ILE A C   
7477  O O   . ILE B 929  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  926  ILE A O   
7478  C CB  . ILE B 929  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  926  ILE A CB  
7479  C CG1 . ILE B 929  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  926  ILE A CG1 
7480  C CG2 . ILE B 929  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  926  ILE A CG2 
7481  C CD1 . ILE B 929  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  926  ILE A CD1 
7482  N N   . LEU B 930  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  927  LEU A N   
7483  C CA  . LEU B 930  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  927  LEU A CA  
7484  C C   . LEU B 930  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  927  LEU A C   
7485  O O   . LEU B 930  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  927  LEU A O   
7486  C CB  . LEU B 930  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  927  LEU A CB  
7487  C CG  . LEU B 930  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  927  LEU A CG  
7488  C CD1 . LEU B 930  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  927  LEU A CD1 
7489  C CD2 . LEU B 930  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  927  LEU A CD2 
7490  N N   . GLU B 931  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  928  GLU A N   
7491  C CA  . GLU B 931  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  928  GLU A CA  
7492  C C   . GLU B 931  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  928  GLU A C   
7493  O O   . GLU B 931  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  928  GLU A O   
7494  C CB  . GLU B 931  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  928  GLU A CB  
7495  C CG  . GLU B 931  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  928  GLU A CG  
7496  C CD  . GLU B 931  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  928  GLU A CD  
7497  O OE1 . GLU B 931  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  928  GLU A OE1 
7498  O OE2 . GLU B 931  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  928  GLU A OE2 
7499  N N   . GLN B 932  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  929  GLN A N   
7500  C CA  . GLN B 932  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  929  GLN A CA  
7501  C C   . GLN B 932  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  929  GLN A C   
7502  O O   . GLN B 932  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  929  GLN A O   
7503  C CB  . GLN B 932  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  929  GLN A CB  
7504  C CG  . GLN B 932  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  929  GLN A CG  
7505  C CD  . GLN B 932  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  929  GLN A CD  
7506  O OE1 . GLN B 932  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  929  GLN A OE1 
7507  N NE2 . GLN B 932  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  929  GLN A NE2 
7508  N N   . ARG B 933  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  930  ARG A N   
7509  C CA  . ARG B 933  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  930  ARG A CA  
7510  C C   . ARG B 933  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  930  ARG A C   
7511  O O   . ARG B 933  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  930  ARG A O   
7512  C CB  . ARG B 933  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  930  ARG A CB  
7513  C CG  . ARG B 933  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  930  ARG A CG  
7514  C CD  . ARG B 933  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  930  ARG A CD  
7515  N NE  . ARG B 933  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  930  ARG A NE  
7516  C CZ  . ARG B 933  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  930  ARG A CZ  
7517  N NH1 . ARG B 933  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  930  ARG A NH1 
7518  N NH2 . ARG B 933  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  930  ARG A NH2 
7519  N N   . SER B 934  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  931  SER A N   
7520  C CA  . SER B 934  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  931  SER A CA  
7521  C C   . SER B 934  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  931  SER A C   
7522  O O   . SER B 934  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  931  SER A O   
7523  C CB  . SER B 934  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  931  SER A CB  
7524  O OG  . SER B 934  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  931  SER A OG  
7525  N N   . LEU B 935  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  932  LEU A N   
7526  C CA  . LEU B 935  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  932  LEU A CA  
7527  C C   . LEU B 935  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  932  LEU A C   
7528  O O   . LEU B 935  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  932  LEU A O   
7529  C CB  . LEU B 935  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  932  LEU A CB  
7530  C CG  . LEU B 935  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  932  LEU A CG  
7531  C CD1 . LEU B 935  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  932  LEU A CD1 
7532  C CD2 . LEU B 935  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  932  LEU A CD2 
7533  N N   . ASN B 936  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  933  ASN A N   
7534  C CA  . ASN B 936  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  933  ASN A CA  
7535  C C   . ASN B 936  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  933  ASN A C   
7536  O O   . ASN B 936  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  933  ASN A O   
7537  C CB  . ASN B 936  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  933  ASN A CB  
7538  C CG  . ASN B 936  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  933  ASN A CG  
7539  O OD1 . ASN B 936  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  933  ASN A OD1 
7540  N ND2 . ASN B 936  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  933  ASN A ND2 
7541  N N   . THR B 937  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  934  THR A N   
7542  C CA  . THR B 937  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  934  THR A CA  
7543  C C   . THR B 937  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  934  THR A C   
7544  O O   . THR B 937  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  934  THR A O   
7545  C CB  . THR B 937  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  934  THR A CB  
7546  O OG1 . THR B 937  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  934  THR A OG1 
7547  C CG2 . THR B 937  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  934  THR A CG2 
7548  N N   . ILE B 938  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  935  ILE A N   
7549  C CA  . ILE B 938  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  935  ILE A CA  
7550  C C   . ILE B 938  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  935  ILE A C   
7551  O O   . ILE B 938  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  935  ILE A O   
7552  C CB  . ILE B 938  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  935  ILE A CB  
7553  C CG1 . ILE B 938  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  935  ILE A CG1 
7554  C CG2 . ILE B 938  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  935  ILE A CG2 
7555  C CD1 . ILE B 938  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  935  ILE A CD1 
7556  N N   . GLN B 939  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  936  GLN A N   
7557  C CA  . GLN B 939  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  936  GLN A CA  
7558  C C   . GLN B 939  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  936  GLN A C   
7559  O O   . GLN B 939  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  936  GLN A O   
7560  C CB  . GLN B 939  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  936  GLN A CB  
7561  C CG  . GLN B 939  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  936  GLN A CG  
7562  C CD  . GLN B 939  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  936  GLN A CD  
7563  O OE1 . GLN B 939  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  936  GLN A OE1 
7564  N NE2 . GLN B 939  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  936  GLN A NE2 
7565  N N   . GLN B 940  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  937  GLN A N   
7566  C CA  . GLN B 940  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  937  GLN A CA  
7567  C C   . GLN B 940  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  937  GLN A C   
7568  O O   . GLN B 940  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  937  GLN A O   
7574  N N   . PHE B 941  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  938  PHE A N   
7575  C CA  . PHE B 941  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  938  PHE A CA  
7576  C C   . PHE B 941  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  938  PHE A C   
7577  O O   . PHE B 941  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  938  PHE A O   
7578  C CB  . PHE B 941  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  938  PHE A CB  
7579  C CG  . PHE B 941  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  938  PHE A CG  
7580  C CD1 . PHE B 941  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  938  PHE A CD1 
7581  C CD2 . PHE B 941  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  938  PHE A CD2 
7582  C CE1 . PHE B 941  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  938  PHE A CE1 
7583  C CE2 . PHE B 941  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  938  PHE A CE2 
7584  C CZ  . PHE B 941  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  938  PHE A CZ  
7585  N N   . ASP B 942  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  939  ASP A N   
7586  C CA  . ASP B 942  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  939  ASP A CA  
7587  C C   . ASP B 942  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  939  ASP A C   
7588  O O   . ASP B 942  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  939  ASP A O   
7589  C CB  . ASP B 942  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  939  ASP A CB  
7590  C CG  . ASP B 942  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  939  ASP A CG  
7591  O OD1 . ASP B 942  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  939  ASP A OD1 
7592  O OD2 . ASP B 942  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  939  ASP A OD2 
7593  N N   . TYR B 943  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  940  TYR A N   
7594  C CA  . TYR B 943  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  940  TYR A CA  
7595  C C   . TYR B 943  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  940  TYR A C   
7596  O O   . TYR B 943  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  940  TYR A O   
7597  C CB  . TYR B 943  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  940  TYR A CB  
7598  C CG  . TYR B 943  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  940  TYR A CG  
7599  C CD1 . TYR B 943  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  940  TYR A CD1 
7600  C CD2 . TYR B 943  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  940  TYR A CD2 
7601  C CE1 . TYR B 943  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  940  TYR A CE1 
7602  C CE2 . TYR B 943  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  940  TYR A CE2 
7603  C CZ  . TYR B 943  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  940  TYR A CZ  
7604  O OH  . TYR B 943  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  940  TYR A OH  
7605  N N   . GLN B 944  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  941  GLN A N   
7606  C CA  . GLN B 944  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  941  GLN A CA  
7607  C C   . GLN B 944  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  941  GLN A C   
7608  O O   . GLN B 944  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  941  GLN A O   
7609  C CB  . GLN B 944  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  941  GLN A CB  
7610  C CG  . GLN B 944  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  941  GLN A CG  
7611  C CD  . GLN B 944  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  941  GLN A CD  
7612  O OE1 . GLN B 944  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  941  GLN A OE1 
7613  N NE2 . GLN B 944  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  941  GLN A NE2 
7614  N N   . LYS B 945  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  942  LYS A N   
7615  C CA  . LYS B 945  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  942  LYS A CA  
7616  C C   . LYS B 945  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  942  LYS A C   
7617  O O   . LYS B 945  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  942  LYS A O   
7623  N N   . LYS B 946  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  943  LYS A N   
7624  C CA  . LYS B 946  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  943  LYS A CA  
7625  C C   . LYS B 946  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  943  LYS A C   
7626  O O   . LYS B 946  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  943  LYS A O   
7627  C CB  . LYS B 946  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  943  LYS A CB  
7628  C CG  . LYS B 946  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  943  LYS A CG  
7629  C CD  . LYS B 946  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  943  LYS A CD  
7630  C CE  . LYS B 946  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  943  LYS A CE  
7631  N NZ  . LYS B 946  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  943  LYS A NZ  
7632  N N   . LEU B 947  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  944  LEU A N   
7633  C CA  . LEU B 947  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  944  LEU A CA  
7634  C C   . LEU B 947  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  944  LEU A C   
7635  O O   . LEU B 947  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  944  LEU A O   
7636  C CB  . LEU B 947  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  944  LEU A CB  
7637  C CG  . LEU B 947  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  944  LEU A CG  
7638  C CD1 . LEU B 947  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  944  LEU A CD1 
7639  C CD2 . LEU B 947  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  944  LEU A CD2 
7640  N N   . ASP B 948  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  945  ASP A N   
7641  C CA  . ASP B 948  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  945  ASP A CA  
7642  C C   . ASP B 948  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  945  ASP A C   
7643  O O   . ASP B 948  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  945  ASP A O   
7644  C CB  . ASP B 948  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  945  ASP A CB  
7645  C CG  . ASP B 948  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  945  ASP A CG  
7646  O OD1 . ASP B 948  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  945  ASP A OD1 
7647  O OD2 . ASP B 948  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  945  ASP A OD2 
7648  N N   . ASN B 949  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  946  ASN A N   
7649  C CA  . ASN B 949  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  946  ASN A CA  
7650  C C   . ASN B 949  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  946  ASN A C   
7651  O O   . ASN B 949  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  946  ASN A O   
7652  C CB  . ASN B 949  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  946  ASN A CB  
7653  C CG  . ASN B 949  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  946  ASN A CG  
7654  O OD1 . ASN B 949  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  946  ASN A OD1 
7655  N ND2 . ASN B 949  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  946  ASN A ND2 
7656  N N   . ARG B 950  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  947  ARG A N   
7657  C CA  . ARG B 950  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  947  ARG A CA  
7658  C C   . ARG B 950  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  947  ARG A C   
7659  O O   . ARG B 950  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  947  ARG A O   
7660  C CB  . ARG B 950  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  947  ARG A CB  
7661  C CG  . ARG B 950  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  947  ARG A CG  
7662  C CD  . ARG B 950  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  947  ARG A CD  
7663  N NE  . ARG B 950  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  947  ARG A NE  
7664  C CZ  . ARG B 950  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  947  ARG A CZ  
7665  N NH1 . ARG B 950  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  947  ARG A NH1 
7666  N NH2 . ARG B 950  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  947  ARG A NH2 
7667  N N   . GLU B 951  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  948  GLU A N   
7668  C CA  . GLU B 951  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  948  GLU A CA  
7669  C C   . GLU B 951  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  948  GLU A C   
7670  O O   . GLU B 951  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  948  GLU A O   
7671  C CB  . GLU B 951  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  948  GLU A CB  
7672  C CG  . GLU B 951  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  948  GLU A CG  
7673  C CD  . GLU B 951  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  948  GLU A CD  
7674  O OE1 . GLU B 951  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  948  GLU A OE1 
7675  O OE2 . GLU B 951  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  948  GLU A OE2 
7676  N N   . LYS B 952  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  949  LYS A N   
7677  C CA  . LYS B 952  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  949  LYS A CA  
7678  C C   . LYS B 952  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  949  LYS A C   
7679  O O   . LYS B 952  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  949  LYS A O   
7680  C CB  . LYS B 952  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  949  LYS A CB  
7681  C CG  . LYS B 952  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  949  LYS A CG  
7682  C CD  . LYS B 952  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  949  LYS A CD  
7683  C CE  . LYS B 952  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  949  LYS A CE  
7684  N NZ  . LYS B 952  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  949  LYS A NZ  
7685  N N   . GLU B 953  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  950  GLU A N   
7686  C CA  . GLU B 953  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  950  GLU A CA  
7687  C C   . GLU B 953  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  950  GLU A C   
7688  O O   . GLU B 953  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  950  GLU A O   
7689  C CB  . GLU B 953  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  950  GLU A CB  
7690  C CG  . GLU B 953  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  950  GLU A CG  
7691  C CD  . GLU B 953  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  950  GLU A CD  
7692  O OE1 . GLU B 953  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  950  GLU A OE1 
7693  O OE2 . GLU B 953  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  950  GLU A OE2 
7694  N N   . ARG B 954  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  951  ARG A N   
7695  C CA  . ARG B 954  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  951  ARG A CA  
7696  C C   . ARG B 954  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  951  ARG A C   
7697  O O   . ARG B 954  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  951  ARG A O   
7698  C CB  . ARG B 954  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  951  ARG A CB  
7699  C CG  . ARG B 954  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  951  ARG A CG  
7700  C CD  . ARG B 954  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  951  ARG A CD  
7701  N NE  . ARG B 954  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  951  ARG A NE  
7702  C CZ  . ARG B 954  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  951  ARG A CZ  
7703  N NH1 . ARG B 954  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  951  ARG A NH1 
7704  N NH2 . ARG B 954  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  951  ARG A NH2 
7705  N N   . VAL B 955  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  952  VAL A N   
7706  C CA  . VAL B 955  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  952  VAL A CA  
7707  C C   . VAL B 955  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  952  VAL A C   
7708  O O   . VAL B 955  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  952  VAL A O   
7709  C CB  . VAL B 955  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  952  VAL A CB  
7710  C CG1 . VAL B 955  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  952  VAL A CG1 
7711  C CG2 . VAL B 955  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  952  VAL A CG2 
7712  N N   . ALA B 956  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  953  ALA A N   
7713  C CA  . ALA B 956  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  953  ALA A CA  
7714  C C   . ALA B 956  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  953  ALA A C   
7715  O O   . ALA B 956  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  953  ALA A O   
7716  C CB  . ALA B 956  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  953  ALA A CB  
7717  N N   . ALA B 957  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  954  ALA A N   
7718  C CA  . ALA B 957  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  954  ALA A CA  
7719  C C   . ALA B 957  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  954  ALA A C   
7720  O O   . ALA B 957  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  954  ALA A O   
7721  C CB  . ALA B 957  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  954  ALA A CB  
7722  N N   . ARG B 958  ? 0.5896 0.5896 0.5896 0.0000  0.0000  0.0000  955  ARG A N   
7723  C CA  . ARG B 958  ? 0.5896 0.5896 0.5896 0.0000  0.0000  0.0000  955  ARG A CA  
7724  C C   . ARG B 958  ? 0.5896 0.5896 0.5896 0.0000  0.0000  0.0000  955  ARG A C   
7725  O O   . ARG B 958  ? 0.5896 0.5896 0.5896 0.0000  0.0000  0.0000  955  ARG A O   
7726  C CB  . ARG B 958  ? 0.5896 0.5896 0.5896 0.0000  0.0000  0.0000  955  ARG A CB  
7727  C CG  . ARG B 958  ? 0.5896 0.5896 0.5896 0.0000  0.0000  0.0000  955  ARG A CG  
7728  C CD  . ARG B 958  ? 0.5896 0.5896 0.5896 0.0000  0.0000  0.0000  955  ARG A CD  
7729  N NE  . ARG B 958  ? 0.5896 0.5896 0.5896 0.0000  0.0000  0.0000  955  ARG A NE  
7730  C CZ  . ARG B 958  ? 0.5896 0.5896 0.5896 0.0000  0.0000  0.0000  955  ARG A CZ  
7731  N NH1 . ARG B 958  ? 0.5896 0.5896 0.5896 0.0000  0.0000  0.0000  955  ARG A NH1 
7732  N NH2 . ARG B 958  ? 0.5896 0.5896 0.5896 0.0000  0.0000  0.0000  955  ARG A NH2 
7733  N N   . GLN B 959  ? 0.6377 0.6377 0.6377 0.0000  0.0000  0.0000  956  GLN A N   
7734  C CA  . GLN B 959  ? 0.6377 0.6377 0.6377 0.0000  0.0000  0.0000  956  GLN A CA  
7735  C C   . GLN B 959  ? 0.6377 0.6377 0.6377 0.0000  0.0000  0.0000  956  GLN A C   
7736  O O   . GLN B 959  ? 0.6377 0.6377 0.6377 0.0000  0.0000  0.0000  956  GLN A O   
7737  C CB  . GLN B 959  ? 0.6377 0.6377 0.6377 0.0000  0.0000  0.0000  956  GLN A CB  
7738  C CG  . GLN B 959  ? 0.6377 0.6377 0.6377 0.0000  0.0000  0.0000  956  GLN A CG  
7739  C CD  . GLN B 959  ? 0.6377 0.6377 0.6377 0.0000  0.0000  0.0000  956  GLN A CD  
7740  O OE1 . GLN B 959  ? 0.6377 0.6377 0.6377 0.0000  0.0000  0.0000  956  GLN A OE1 
7741  N NE2 . GLN B 959  ? 0.6377 0.6377 0.6377 0.0000  0.0000  0.0000  956  GLN A NE2 
7747  N N   . TRP B 961  ? 0.7794 0.7794 0.7794 0.0000  0.0000  0.0000  958  TRP A N   
7748  C CA  . TRP B 961  ? 0.7794 0.7794 0.7794 0.0000  0.0000  0.0000  958  TRP A CA  
7749  C C   . TRP B 961  ? 0.7794 0.7794 0.7794 0.0000  0.0000  0.0000  958  TRP A C   
7750  O O   . TRP B 961  ? 0.7794 0.7794 0.7794 0.0000  0.0000  0.0000  958  TRP A O   
7761  N N   . SER B 962  ? 0.6613 0.6613 0.6613 0.0000  0.0000  0.0000  959  SER A N   
7762  C CA  . SER B 962  ? 0.6613 0.6613 0.6613 0.0000  0.0000  0.0000  959  SER A CA  
7763  C C   . SER B 962  ? 0.6613 0.6613 0.6613 0.0000  0.0000  0.0000  959  SER A C   
7764  O O   . SER B 962  ? 0.6613 0.6613 0.6613 0.0000  0.0000  0.0000  959  SER A O   
7765  C CB  . SER B 962  ? 0.6613 0.6613 0.6613 0.0000  0.0000  0.0000  959  SER A CB  
7766  O OG  . SER B 962  ? 0.6613 0.6613 0.6613 0.0000  0.0000  0.0000  959  SER A OG  
7767  N N   . VAL B 963  ? 0.6086 0.6086 0.6086 0.0000  0.0000  0.0000  960  VAL A N   
7768  C CA  . VAL B 963  ? 0.6086 0.6086 0.6086 0.0000  0.0000  0.0000  960  VAL A CA  
7769  C C   . VAL B 963  ? 0.6086 0.6086 0.6086 0.0000  0.0000  0.0000  960  VAL A C   
7770  O O   . VAL B 963  ? 0.6086 0.6086 0.6086 0.0000  0.0000  0.0000  960  VAL A O   
7771  C CB  . VAL B 963  ? 0.6086 0.6086 0.6086 0.0000  0.0000  0.0000  960  VAL A CB  
7772  C CG1 . VAL B 963  ? 0.6086 0.6086 0.6086 0.0000  0.0000  0.0000  960  VAL A CG1 
7773  C CG2 . VAL B 963  ? 0.6086 0.6086 0.6086 0.0000  0.0000  0.0000  960  VAL A CG2 
7774  N N   . VAL B 964  ? 0.6148 0.6148 0.6148 0.0000  0.0000  0.0000  961  VAL A N   
7775  C CA  . VAL B 964  ? 0.6148 0.6148 0.6148 0.0000  0.0000  0.0000  961  VAL A CA  
7776  C C   . VAL B 964  ? 0.6148 0.6148 0.6148 0.0000  0.0000  0.0000  961  VAL A C   
7777  O O   . VAL B 964  ? 0.6148 0.6148 0.6148 0.0000  0.0000  0.0000  961  VAL A O   
7778  C CB  . VAL B 964  ? 0.6148 0.6148 0.6148 0.0000  0.0000  0.0000  961  VAL A CB  
7779  C CG1 . VAL B 964  ? 0.6148 0.6148 0.6148 0.0000  0.0000  0.0000  961  VAL A CG1 
7780  C CG2 . VAL B 964  ? 0.6148 0.6148 0.6148 0.0000  0.0000  0.0000  961  VAL A CG2 
7781  N N   . GLY B 965  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  962  GLY A N   
7782  C CA  . GLY B 965  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  962  GLY A CA  
7783  C C   . GLY B 965  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  962  GLY A C   
7784  O O   . GLY B 965  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  962  GLY A O   
7785  N N   . THR B 966  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  963  THR A N   
7786  C CA  . THR B 966  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  963  THR A CA  
7787  C C   . THR B 966  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  963  THR A C   
7788  O O   . THR B 966  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  963  THR A O   
7789  C CB  . THR B 966  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  963  THR A CB  
7790  O OG1 . THR B 966  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  963  THR A OG1 
7791  C CG2 . THR B 966  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  963  THR A CG2 
7792  N N   . ILE B 967  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  964  ILE A N   
7793  C CA  . ILE B 967  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  964  ILE A CA  
7794  C C   . ILE B 967  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  964  ILE A C   
7795  O O   . ILE B 967  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  964  ILE A O   
7796  C CB  . ILE B 967  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  964  ILE A CB  
7797  C CG1 . ILE B 967  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  964  ILE A CG1 
7798  C CG2 . ILE B 967  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  964  ILE A CG2 
7799  C CD1 . ILE B 967  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  964  ILE A CD1 
7800  N N   . LYS B 968  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  965  LYS A N   
7801  C CA  . LYS B 968  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  965  LYS A CA  
7802  C C   . LYS B 968  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  965  LYS A C   
7803  O O   . LYS B 968  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  965  LYS A O   
7804  C CB  . LYS B 968  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  965  LYS A CB  
7805  C CG  . LYS B 968  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  965  LYS A CG  
7806  C CD  . LYS B 968  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  965  LYS A CD  
7807  C CE  . LYS B 968  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  965  LYS A CE  
7808  N NZ  . LYS B 968  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  965  LYS A NZ  
7809  N N   . ASP B 969  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  966  ASP A N   
7810  C CA  . ASP B 969  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  966  ASP A CA  
7811  C C   . ASP B 969  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  966  ASP A C   
7812  O O   . ASP B 969  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  966  ASP A O   
7813  C CB  . ASP B 969  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  966  ASP A CB  
7814  C CG  . ASP B 969  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  966  ASP A CG  
7815  O OD1 . ASP B 969  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  966  ASP A OD1 
7816  O OD2 . ASP B 969  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  966  ASP A OD2 
7817  N N   . LEU B 970  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  967  LEU A N   
7818  C CA  . LEU B 970  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  967  LEU A CA  
7819  C C   . LEU B 970  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  967  LEU A C   
7820  O O   . LEU B 970  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  967  LEU A O   
7821  C CB  . LEU B 970  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  967  LEU A CB  
7822  C CG  . LEU B 970  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  967  LEU A CG  
7823  C CD1 . LEU B 970  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  967  LEU A CD1 
7824  C CD2 . LEU B 970  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  967  LEU A CD2 
7825  N N   . LYS B 971  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  968  LYS A N   
7826  C CA  . LYS B 971  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  968  LYS A CA  
7827  C C   . LYS B 971  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  968  LYS A C   
7828  O O   . LYS B 971  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  968  LYS A O   
7829  C CB  . LYS B 971  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  968  LYS A CB  
7830  C CG  . LYS B 971  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  968  LYS A CG  
7831  C CD  . LYS B 971  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  968  LYS A CD  
7832  C CE  . LYS B 971  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  968  LYS A CE  
7833  N NZ  . LYS B 971  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  968  LYS A NZ  
7834  N N   . GLN B 972  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  969  GLN A N   
7835  C CA  . GLN B 972  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  969  GLN A CA  
7836  C C   . GLN B 972  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  969  GLN A C   
7837  O O   . GLN B 972  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  969  GLN A O   
7843  N N   . GLY B 973  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  970  GLY A N   
7844  C CA  . GLY B 973  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  970  GLY A CA  
7845  C C   . GLY B 973  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  970  GLY A C   
7846  O O   . GLY B 973  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  970  GLY A O   
7847  N N   . TYR B 974  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  971  TYR A N   
7848  C CA  . TYR B 974  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  971  TYR A CA  
7849  C C   . TYR B 974  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  971  TYR A C   
7850  O O   . TYR B 974  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  971  TYR A O   
7851  C CB  . TYR B 974  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  971  TYR A CB  
7852  C CG  . TYR B 974  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  971  TYR A CG  
7853  C CD1 . TYR B 974  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  971  TYR A CD1 
7854  C CD2 . TYR B 974  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  971  TYR A CD2 
7855  C CE1 . TYR B 974  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  971  TYR A CE1 
7856  C CE2 . TYR B 974  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  971  TYR A CE2 
7857  C CZ  . TYR B 974  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  971  TYR A CZ  
7858  O OH  . TYR B 974  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  971  TYR A OH  
7859  N N   . LEU B 975  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  972  LEU A N   
7860  C CA  . LEU B 975  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  972  LEU A CA  
7861  C C   . LEU B 975  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  972  LEU A C   
7862  O O   . LEU B 975  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  972  LEU A O   
7863  C CB  . LEU B 975  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  972  LEU A CB  
7864  C CG  . LEU B 975  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  972  LEU A CG  
7865  C CD1 . LEU B 975  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  972  LEU A CD1 
7866  C CD2 . LEU B 975  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  972  LEU A CD2 
7867  N N   . SER B 976  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  973  SER A N   
7868  C CA  . SER B 976  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  973  SER A CA  
7869  C C   . SER B 976  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  973  SER A C   
7870  O O   . SER B 976  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  973  SER A O   
7871  C CB  . SER B 976  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  973  SER A CB  
7872  O OG  . SER B 976  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  973  SER A OG  
7873  N N   . GLN B 977  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  974  GLN A N   
7874  C CA  . GLN B 977  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  974  GLN A CA  
7875  C C   . GLN B 977  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  974  GLN A C   
7876  O O   . GLN B 977  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  974  GLN A O   
7877  C CB  . GLN B 977  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  974  GLN A CB  
7878  C CG  . GLN B 977  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  974  GLN A CG  
7879  C CD  . GLN B 977  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  974  GLN A CD  
7880  O OE1 . GLN B 977  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  974  GLN A OE1 
7881  N NE2 . GLN B 977  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  974  GLN A NE2 
7882  N N   . VAL B 978  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  975  VAL A N   
7883  C CA  . VAL B 978  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  975  VAL A CA  
7884  C C   . VAL B 978  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  975  VAL A C   
7885  O O   . VAL B 978  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  975  VAL A O   
7886  C CB  . VAL B 978  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  975  VAL A CB  
7887  C CG1 . VAL B 978  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  975  VAL A CG1 
7888  C CG2 . VAL B 978  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  975  VAL A CG2 
7889  N N   . ILE B 979  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  976  ILE A N   
7890  C CA  . ILE B 979  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  976  ILE A CA  
7891  C C   . ILE B 979  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  976  ILE A C   
7892  O O   . ILE B 979  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  976  ILE A O   
7893  C CB  . ILE B 979  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  976  ILE A CB  
7894  C CG1 . ILE B 979  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  976  ILE A CG1 
7895  C CG2 . ILE B 979  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  976  ILE A CG2 
7896  C CD1 . ILE B 979  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  976  ILE A CD1 
7897  N N   . HIS B 980  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  977  HIS A N   
7898  C CA  . HIS B 980  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  977  HIS A CA  
7899  C C   . HIS B 980  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  977  HIS A C   
7900  O O   . HIS B 980  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  977  HIS A O   
7901  C CB  . HIS B 980  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  977  HIS A CB  
7902  C CG  . HIS B 980  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  977  HIS A CG  
7903  N ND1 . HIS B 980  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  977  HIS A ND1 
7904  C CD2 . HIS B 980  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  977  HIS A CD2 
7905  C CE1 . HIS B 980  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  977  HIS A CE1 
7906  N NE2 . HIS B 980  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  977  HIS A NE2 
7907  N N   . GLU B 981  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  978  GLU A N   
7908  C CA  . GLU B 981  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  978  GLU A CA  
7909  C C   . GLU B 981  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  978  GLU A C   
7910  O O   . GLU B 981  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  978  GLU A O   
7911  C CB  . GLU B 981  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  978  GLU A CB  
7912  C CG  . GLU B 981  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  978  GLU A CG  
7913  C CD  . GLU B 981  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  978  GLU A CD  
7914  O OE1 . GLU B 981  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  978  GLU A OE1 
7915  O OE2 . GLU B 981  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  978  GLU A OE2 
7916  N N   . ILE B 982  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  979  ILE A N   
7917  C CA  . ILE B 982  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  979  ILE A CA  
7918  C C   . ILE B 982  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  979  ILE A C   
7919  O O   . ILE B 982  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  979  ILE A O   
7920  C CB  . ILE B 982  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  979  ILE A CB  
7921  C CG1 . ILE B 982  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  979  ILE A CG1 
7922  C CG2 . ILE B 982  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  979  ILE A CG2 
7923  C CD1 . ILE B 982  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  979  ILE A CD1 
7924  N N   . VAL B 983  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  980  VAL A N   
7925  C CA  . VAL B 983  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  980  VAL A CA  
7926  C C   . VAL B 983  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  980  VAL A C   
7927  O O   . VAL B 983  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  980  VAL A O   
7928  C CB  . VAL B 983  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  980  VAL A CB  
7929  C CG1 . VAL B 983  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  980  VAL A CG1 
7930  C CG2 . VAL B 983  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  980  VAL A CG2 
7931  N N   . ASP B 984  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  981  ASP A N   
7932  C CA  . ASP B 984  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  981  ASP A CA  
7933  C C   . ASP B 984  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  981  ASP A C   
7934  O O   . ASP B 984  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  981  ASP A O   
7935  C CB  . ASP B 984  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  981  ASP A CB  
7936  C CG  . ASP B 984  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  981  ASP A CG  
7937  O OD1 . ASP B 984  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  981  ASP A OD1 
7938  O OD2 . ASP B 984  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  981  ASP A OD2 
7939  N N   . LEU B 985  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  982  LEU A N   
7940  C CA  . LEU B 985  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  982  LEU A CA  
7941  C C   . LEU B 985  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  982  LEU A C   
7942  O O   . LEU B 985  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  982  LEU A O   
7943  C CB  . LEU B 985  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  982  LEU A CB  
7944  C CG  . LEU B 985  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  982  LEU A CG  
7945  C CD1 . LEU B 985  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  982  LEU A CD1 
7946  C CD2 . LEU B 985  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  982  LEU A CD2 
7947  N N   . MET B 986  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  983  MET A N   
7948  C CA  . MET B 986  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  983  MET A CA  
7949  C C   . MET B 986  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  983  MET A C   
7950  O O   . MET B 986  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  983  MET A O   
7951  C CB  . MET B 986  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  983  MET A CB  
7952  C CG  . MET B 986  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  983  MET A CG  
7953  S SD  . MET B 986  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  983  MET A SD  
7954  C CE  . MET B 986  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  983  MET A CE  
7955  N N   . ILE B 987  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  984  ILE A N   
7956  C CA  . ILE B 987  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  984  ILE A CA  
7957  C C   . ILE B 987  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  984  ILE A C   
7958  O O   . ILE B 987  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  984  ILE A O   
7959  C CB  . ILE B 987  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  984  ILE A CB  
7960  C CG1 . ILE B 987  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  984  ILE A CG1 
7961  C CG2 . ILE B 987  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  984  ILE A CG2 
7962  C CD1 . ILE B 987  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  984  ILE A CD1 
7963  N N   . HIS B 988  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  985  HIS A N   
7964  C CA  . HIS B 988  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  985  HIS A CA  
7965  C C   . HIS B 988  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  985  HIS A C   
7966  O O   . HIS B 988  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  985  HIS A O   
7967  C CB  . HIS B 988  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  985  HIS A CB  
7968  C CG  . HIS B 988  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  985  HIS A CG  
7969  N ND1 . HIS B 988  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  985  HIS A ND1 
7970  C CD2 . HIS B 988  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  985  HIS A CD2 
7971  C CE1 . HIS B 988  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  985  HIS A CE1 
7972  N NE2 . HIS B 988  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  985  HIS A NE2 
7973  N N   . TYR B 989  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  986  TYR A N   
7974  C CA  . TYR B 989  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  986  TYR A CA  
7975  C C   . TYR B 989  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  986  TYR A C   
7976  O O   . TYR B 989  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  986  TYR A O   
7977  C CB  . TYR B 989  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  986  TYR A CB  
7978  C CG  . TYR B 989  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  986  TYR A CG  
7979  C CD1 . TYR B 989  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  986  TYR A CD1 
7980  C CD2 . TYR B 989  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  986  TYR A CD2 
7981  C CE1 . TYR B 989  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  986  TYR A CE1 
7982  C CE2 . TYR B 989  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  986  TYR A CE2 
7983  C CZ  . TYR B 989  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  986  TYR A CZ  
7984  O OH  . TYR B 989  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  986  TYR A OH  
7985  N N   . GLN B 990  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  987  GLN A N   
7986  C CA  . GLN B 990  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  987  GLN A CA  
7987  C C   . GLN B 990  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  987  GLN A C   
7988  O O   . GLN B 990  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  987  GLN A O   
7989  C CB  . GLN B 990  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  987  GLN A CB  
7990  C CG  . GLN B 990  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  987  GLN A CG  
7991  C CD  . GLN B 990  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  987  GLN A CD  
7992  O OE1 . GLN B 990  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  987  GLN A OE1 
7993  N NE2 . GLN B 990  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  987  GLN A NE2 
7994  N N   . ALA B 991  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  988  ALA A N   
7995  C CA  . ALA B 991  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  988  ALA A CA  
7996  C C   . ALA B 991  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  988  ALA A C   
7997  O O   . ALA B 991  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  988  ALA A O   
7998  C CB  . ALA B 991  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  988  ALA A CB  
7999  N N   . VAL B 992  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  989  VAL A N   
8000  C CA  . VAL B 992  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  989  VAL A CA  
8001  C C   . VAL B 992  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  989  VAL A C   
8002  O O   . VAL B 992  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  989  VAL A O   
8003  C CB  . VAL B 992  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  989  VAL A CB  
8004  C CG1 . VAL B 992  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  989  VAL A CG1 
8005  C CG2 . VAL B 992  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  989  VAL A CG2 
8006  N N   . VAL B 993  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  990  VAL A N   
8007  C CA  . VAL B 993  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  990  VAL A CA  
8008  C C   . VAL B 993  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  990  VAL A C   
8009  O O   . VAL B 993  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  990  VAL A O   
8010  C CB  . VAL B 993  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  990  VAL A CB  
8011  C CG1 . VAL B 993  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  990  VAL A CG1 
8012  C CG2 . VAL B 993  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  990  VAL A CG2 
8013  N N   . VAL B 994  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  991  VAL A N   
8014  C CA  . VAL B 994  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  991  VAL A CA  
8015  C C   . VAL B 994  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  991  VAL A C   
8016  O O   . VAL B 994  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  991  VAL A O   
8017  C CB  . VAL B 994  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  991  VAL A CB  
8018  C CG1 . VAL B 994  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  991  VAL A CG1 
8019  C CG2 . VAL B 994  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  991  VAL A CG2 
8020  N N   . LEU B 995  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  992  LEU A N   
8021  C CA  . LEU B 995  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  992  LEU A CA  
8022  C C   . LEU B 995  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  992  LEU A C   
8023  O O   . LEU B 995  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  992  LEU A O   
8024  C CB  . LEU B 995  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  992  LEU A CB  
8025  C CG  . LEU B 995  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  992  LEU A CG  
8026  C CD1 . LEU B 995  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  992  LEU A CD1 
8027  C CD2 . LEU B 995  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  992  LEU A CD2 
8028  N N   . GLU B 996  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  993  GLU A N   
8029  C CA  . GLU B 996  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  993  GLU A CA  
8030  C C   . GLU B 996  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  993  GLU A C   
8031  O O   . GLU B 996  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  993  GLU A O   
8032  C CB  . GLU B 996  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  993  GLU A CB  
8033  C CG  . GLU B 996  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  993  GLU A CG  
8034  C CD  . GLU B 996  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  993  GLU A CD  
8035  O OE1 . GLU B 996  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  993  GLU A OE1 
8036  O OE2 . GLU B 996  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  993  GLU A OE2 
8037  N N   . ASN B 997  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  994  ASN A N   
8038  C CA  . ASN B 997  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  994  ASN A CA  
8039  C C   . ASN B 997  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  994  ASN A C   
8040  O O   . ASN B 997  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  994  ASN A O   
8041  C CB  . ASN B 997  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  994  ASN A CB  
8042  C CG  . ASN B 997  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  994  ASN A CG  
8043  O OD1 . ASN B 997  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  994  ASN A OD1 
8044  N ND2 . ASN B 997  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  994  ASN A ND2 
8045  N N   . LEU B 998  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  995  LEU A N   
8046  C CA  . LEU B 998  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  995  LEU A CA  
8047  C C   . LEU B 998  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  995  LEU A C   
8048  O O   . LEU B 998  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  995  LEU A O   
8049  C CB  . LEU B 998  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  995  LEU A CB  
8050  C CG  . LEU B 998  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  995  LEU A CG  
8051  C CD1 . LEU B 998  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  995  LEU A CD1 
8052  C CD2 . LEU B 998  ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  995  LEU A CD2 
8169  N N   . VAL B 1014 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1011 VAL A N   
8170  C CA  . VAL B 1014 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1011 VAL A CA  
8171  C C   . VAL B 1014 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1011 VAL A C   
8172  O O   . VAL B 1014 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1011 VAL A O   
8173  C CB  . VAL B 1014 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1011 VAL A CB  
8174  C CG1 . VAL B 1014 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1011 VAL A CG1 
8175  C CG2 . VAL B 1014 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1011 VAL A CG2 
8176  N N   . TYR B 1015 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1012 TYR A N   
8177  C CA  . TYR B 1015 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1012 TYR A CA  
8178  C C   . TYR B 1015 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1012 TYR A C   
8179  O O   . TYR B 1015 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1012 TYR A O   
8180  C CB  . TYR B 1015 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1012 TYR A CB  
8181  C CG  . TYR B 1015 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1012 TYR A CG  
8182  C CD1 . TYR B 1015 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1012 TYR A CD1 
8183  C CD2 . TYR B 1015 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1012 TYR A CD2 
8184  C CE1 . TYR B 1015 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1012 TYR A CE1 
8185  C CE2 . TYR B 1015 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1012 TYR A CE2 
8186  C CZ  . TYR B 1015 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1012 TYR A CZ  
8187  O OH  . TYR B 1015 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1012 TYR A OH  
8188  N N   . GLN B 1016 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1013 GLN A N   
8189  C CA  . GLN B 1016 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1013 GLN A CA  
8190  C C   . GLN B 1016 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1013 GLN A C   
8191  O O   . GLN B 1016 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1013 GLN A O   
8192  C CB  . GLN B 1016 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1013 GLN A CB  
8193  C CG  . GLN B 1016 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1013 GLN A CG  
8194  C CD  . GLN B 1016 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1013 GLN A CD  
8195  O OE1 . GLN B 1016 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1013 GLN A OE1 
8196  N NE2 . GLN B 1016 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1013 GLN A NE2 
8197  N N   . GLN B 1017 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1014 GLN A N   
8198  C CA  . GLN B 1017 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1014 GLN A CA  
8199  C C   . GLN B 1017 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1014 GLN A C   
8200  O O   . GLN B 1017 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1014 GLN A O   
8201  C CB  . GLN B 1017 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1014 GLN A CB  
8202  C CG  . GLN B 1017 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1014 GLN A CG  
8203  C CD  . GLN B 1017 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1014 GLN A CD  
8204  O OE1 . GLN B 1017 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1014 GLN A OE1 
8205  N NE2 . GLN B 1017 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1014 GLN A NE2 
8206  N N   . PHE B 1018 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1015 PHE A N   
8207  C CA  . PHE B 1018 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1015 PHE A CA  
8208  C C   . PHE B 1018 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1015 PHE A C   
8209  O O   . PHE B 1018 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1015 PHE A O   
8210  C CB  . PHE B 1018 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1015 PHE A CB  
8211  C CG  . PHE B 1018 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1015 PHE A CG  
8212  C CD1 . PHE B 1018 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1015 PHE A CD1 
8213  C CD2 . PHE B 1018 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1015 PHE A CD2 
8214  C CE1 . PHE B 1018 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1015 PHE A CE1 
8215  C CE2 . PHE B 1018 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1015 PHE A CE2 
8216  C CZ  . PHE B 1018 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1015 PHE A CZ  
8217  N N   . GLU B 1019 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1016 GLU A N   
8218  C CA  . GLU B 1019 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1016 GLU A CA  
8219  C C   . GLU B 1019 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1016 GLU A C   
8220  O O   . GLU B 1019 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1016 GLU A O   
8221  C CB  . GLU B 1019 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1016 GLU A CB  
8222  C CG  . GLU B 1019 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1016 GLU A CG  
8223  C CD  . GLU B 1019 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1016 GLU A CD  
8224  O OE1 . GLU B 1019 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1016 GLU A OE1 
8225  O OE2 . GLU B 1019 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1016 GLU A OE2 
8226  N N   . LYS B 1020 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1017 LYS A N   
8227  C CA  . LYS B 1020 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1017 LYS A CA  
8228  C C   . LYS B 1020 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1017 LYS A C   
8229  O O   . LYS B 1020 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1017 LYS A O   
8230  C CB  . LYS B 1020 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1017 LYS A CB  
8231  C CG  . LYS B 1020 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1017 LYS A CG  
8232  C CD  . LYS B 1020 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1017 LYS A CD  
8233  C CE  . LYS B 1020 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1017 LYS A CE  
8234  N NZ  . LYS B 1020 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1017 LYS A NZ  
8235  N N   . MET B 1021 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1018 MET A N   
8236  C CA  . MET B 1021 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1018 MET A CA  
8237  C C   . MET B 1021 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1018 MET A C   
8238  O O   . MET B 1021 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1018 MET A O   
8239  C CB  . MET B 1021 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1018 MET A CB  
8240  C CG  . MET B 1021 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1018 MET A CG  
8241  S SD  . MET B 1021 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1018 MET A SD  
8242  C CE  . MET B 1021 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1018 MET A CE  
8243  N N   . LEU B 1022 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1019 LEU A N   
8244  C CA  . LEU B 1022 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1019 LEU A CA  
8245  C C   . LEU B 1022 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1019 LEU A C   
8246  O O   . LEU B 1022 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1019 LEU A O   
8247  C CB  . LEU B 1022 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1019 LEU A CB  
8248  C CG  . LEU B 1022 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1019 LEU A CG  
8249  C CD1 . LEU B 1022 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1019 LEU A CD1 
8250  C CD2 . LEU B 1022 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1019 LEU A CD2 
8251  N N   . ILE B 1023 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1020 ILE A N   
8252  C CA  . ILE B 1023 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1020 ILE A CA  
8253  C C   . ILE B 1023 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1020 ILE A C   
8254  O O   . ILE B 1023 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1020 ILE A O   
8255  C CB  . ILE B 1023 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1020 ILE A CB  
8256  C CG1 . ILE B 1023 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1020 ILE A CG1 
8257  C CG2 . ILE B 1023 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1020 ILE A CG2 
8258  C CD1 . ILE B 1023 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1020 ILE A CD1 
8259  N N   . ASP B 1024 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1021 ASP A N   
8260  C CA  . ASP B 1024 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1021 ASP A CA  
8261  C C   . ASP B 1024 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1021 ASP A C   
8262  O O   . ASP B 1024 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1021 ASP A O   
8263  C CB  . ASP B 1024 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1021 ASP A CB  
8264  C CG  . ASP B 1024 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1021 ASP A CG  
8265  O OD1 . ASP B 1024 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1021 ASP A OD1 
8266  O OD2 . ASP B 1024 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1021 ASP A OD2 
8267  N N   . LYS B 1025 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1022 LYS A N   
8268  C CA  . LYS B 1025 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1022 LYS A CA  
8269  C C   . LYS B 1025 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1022 LYS A C   
8270  O O   . LYS B 1025 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1022 LYS A O   
8271  C CB  . LYS B 1025 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1022 LYS A CB  
8272  C CG  . LYS B 1025 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1022 LYS A CG  
8273  C CD  . LYS B 1025 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1022 LYS A CD  
8274  C CE  . LYS B 1025 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1022 LYS A CE  
8275  N NZ  . LYS B 1025 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1022 LYS A NZ  
8276  N N   . LEU B 1026 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1023 LEU A N   
8277  C CA  . LEU B 1026 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1023 LEU A CA  
8278  C C   . LEU B 1026 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1023 LEU A C   
8279  O O   . LEU B 1026 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1023 LEU A O   
8280  C CB  . LEU B 1026 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1023 LEU A CB  
8281  C CG  . LEU B 1026 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1023 LEU A CG  
8282  C CD1 . LEU B 1026 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1023 LEU A CD1 
8283  C CD2 . LEU B 1026 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1023 LEU A CD2 
8284  N N   . ASN B 1027 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1024 ASN A N   
8285  C CA  . ASN B 1027 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1024 ASN A CA  
8286  C C   . ASN B 1027 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1024 ASN A C   
8287  O O   . ASN B 1027 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1024 ASN A O   
8288  C CB  . ASN B 1027 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1024 ASN A CB  
8289  C CG  . ASN B 1027 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1024 ASN A CG  
8290  O OD1 . ASN B 1027 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1024 ASN A OD1 
8291  N ND2 . ASN B 1027 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1024 ASN A ND2 
8292  N N   . CYS B 1028 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1025 CYS A N   
8293  C CA  . CYS B 1028 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1025 CYS A CA  
8294  C C   . CYS B 1028 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1025 CYS A C   
8295  O O   . CYS B 1028 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1025 CYS A O   
8296  C CB  . CYS B 1028 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1025 CYS A CB  
8297  S SG  . CYS B 1028 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1025 CYS A SG  
8298  N N   . LEU B 1029 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1026 LEU A N   
8299  C CA  . LEU B 1029 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1026 LEU A CA  
8300  C C   . LEU B 1029 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1026 LEU A C   
8301  O O   . LEU B 1029 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1026 LEU A O   
8302  C CB  . LEU B 1029 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1026 LEU A CB  
8303  C CG  . LEU B 1029 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1026 LEU A CG  
8304  C CD1 . LEU B 1029 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1026 LEU A CD1 
8305  C CD2 . LEU B 1029 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1026 LEU A CD2 
8306  N N   . VAL B 1030 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1027 VAL A N   
8307  C CA  . VAL B 1030 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1027 VAL A CA  
8308  C C   . VAL B 1030 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1027 VAL A C   
8309  O O   . VAL B 1030 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1027 VAL A O   
8310  C CB  . VAL B 1030 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1027 VAL A CB  
8311  C CG1 . VAL B 1030 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1027 VAL A CG1 
8312  C CG2 . VAL B 1030 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1027 VAL A CG2 
8313  N N   . LEU B 1031 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1028 LEU A N   
8314  C CA  . LEU B 1031 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1028 LEU A CA  
8315  C C   . LEU B 1031 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1028 LEU A C   
8316  O O   . LEU B 1031 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1028 LEU A O   
8317  C CB  . LEU B 1031 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1028 LEU A CB  
8318  C CG  . LEU B 1031 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1028 LEU A CG  
8319  C CD1 . LEU B 1031 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1028 LEU A CD1 
8320  C CD2 . LEU B 1031 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1028 LEU A CD2 
8321  N N   . LYS B 1032 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1029 LYS A N   
8322  C CA  . LYS B 1032 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1029 LYS A CA  
8323  C C   . LYS B 1032 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1029 LYS A C   
8324  O O   . LYS B 1032 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1029 LYS A O   
8325  C CB  . LYS B 1032 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1029 LYS A CB  
8326  C CG  . LYS B 1032 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1029 LYS A CG  
8327  C CD  . LYS B 1032 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1029 LYS A CD  
8328  C CE  . LYS B 1032 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1029 LYS A CE  
8329  N NZ  . LYS B 1032 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1029 LYS A NZ  
8330  N N   . ASP B 1033 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1030 ASP A N   
8331  C CA  . ASP B 1033 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1030 ASP A CA  
8332  C C   . ASP B 1033 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1030 ASP A C   
8333  O O   . ASP B 1033 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1030 ASP A O   
8334  C CB  . ASP B 1033 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1030 ASP A CB  
8335  C CG  . ASP B 1033 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1030 ASP A CG  
8336  O OD1 . ASP B 1033 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1030 ASP A OD1 
8337  O OD2 . ASP B 1033 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1030 ASP A OD2 
8338  N N   . TYR B 1034 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1031 TYR A N   
8339  C CA  . TYR B 1034 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1031 TYR A CA  
8340  C C   . TYR B 1034 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1031 TYR A C   
8341  O O   . TYR B 1034 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1031 TYR A O   
8342  C CB  . TYR B 1034 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1031 TYR A CB  
8343  C CG  . TYR B 1034 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1031 TYR A CG  
8344  C CD1 . TYR B 1034 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1031 TYR A CD1 
8345  C CD2 . TYR B 1034 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1031 TYR A CD2 
8346  C CE1 . TYR B 1034 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1031 TYR A CE1 
8347  C CE2 . TYR B 1034 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1031 TYR A CE2 
8348  C CZ  . TYR B 1034 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1031 TYR A CZ  
8349  O OH  . TYR B 1034 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1031 TYR A OH  
8350  N N   . PRO B 1035 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1032 PRO A N   
8351  C CA  . PRO B 1035 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1032 PRO A CA  
8352  C C   . PRO B 1035 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1032 PRO A C   
8353  O O   . PRO B 1035 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1032 PRO A O   
8354  C CB  . PRO B 1035 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1032 PRO A CB  
8355  C CG  . PRO B 1035 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1032 PRO A CG  
8356  C CD  . PRO B 1035 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1032 PRO A CD  
8357  N N   . ALA B 1036 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1033 ALA A N   
8358  C CA  . ALA B 1036 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1033 ALA A CA  
8359  C C   . ALA B 1036 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1033 ALA A C   
8360  O O   . ALA B 1036 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1033 ALA A O   
8361  C CB  . ALA B 1036 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1033 ALA A CB  
8362  N N   . GLU B 1037 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1034 GLU A N   
8363  C CA  . GLU B 1037 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1034 GLU A CA  
8364  C C   . GLU B 1037 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1034 GLU A C   
8365  O O   . GLU B 1037 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1034 GLU A O   
8371  N N   . LYS B 1038 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1035 LYS A N   
8372  C CA  . LYS B 1038 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1035 LYS A CA  
8373  C C   . LYS B 1038 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1035 LYS A C   
8374  O O   . LYS B 1038 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1035 LYS A O   
8380  N N   . VAL B 1039 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1036 VAL A N   
8381  C CA  . VAL B 1039 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1036 VAL A CA  
8382  C C   . VAL B 1039 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1036 VAL A C   
8383  O O   . VAL B 1039 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1036 VAL A O   
8384  C CB  . VAL B 1039 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1036 VAL A CB  
8385  C CG1 . VAL B 1039 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1036 VAL A CG1 
8386  C CG2 . VAL B 1039 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1036 VAL A CG2 
8387  N N   . GLY B 1040 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1037 GLY A N   
8388  C CA  . GLY B 1040 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1037 GLY A CA  
8389  C C   . GLY B 1040 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1037 GLY A C   
8390  O O   . GLY B 1040 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1037 GLY A O   
8391  N N   . GLY B 1041 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1038 GLY A N   
8392  C CA  . GLY B 1041 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1038 GLY A CA  
8393  C C   . GLY B 1041 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1038 GLY A C   
8394  O O   . GLY B 1041 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1038 GLY A O   
8395  N N   . VAL B 1042 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1039 VAL A N   
8396  C CA  . VAL B 1042 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1039 VAL A CA  
8397  C C   . VAL B 1042 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1039 VAL A C   
8398  O O   . VAL B 1042 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1039 VAL A O   
8399  C CB  . VAL B 1042 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1039 VAL A CB  
8400  C CG1 . VAL B 1042 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1039 VAL A CG1 
8401  C CG2 . VAL B 1042 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1039 VAL A CG2 
8402  N N   . LEU B 1043 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1040 LEU A N   
8403  C CA  . LEU B 1043 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1040 LEU A CA  
8404  C C   . LEU B 1043 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1040 LEU A C   
8405  O O   . LEU B 1043 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1040 LEU A O   
8406  C CB  . LEU B 1043 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1040 LEU A CB  
8407  C CG  . LEU B 1043 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1040 LEU A CG  
8408  C CD1 . LEU B 1043 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1040 LEU A CD1 
8409  C CD2 . LEU B 1043 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1040 LEU A CD2 
8410  N N   . ASN B 1044 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1041 ASN A N   
8411  C CA  . ASN B 1044 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1041 ASN A CA  
8412  C C   . ASN B 1044 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1041 ASN A C   
8413  O O   . ASN B 1044 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1041 ASN A O   
8414  C CB  . ASN B 1044 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1041 ASN A CB  
8415  C CG  . ASN B 1044 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1041 ASN A CG  
8416  O OD1 . ASN B 1044 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1041 ASN A OD1 
8417  N ND2 . ASN B 1044 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1041 ASN A ND2 
8418  N N   . PRO B 1045 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1042 PRO A N   
8419  C CA  . PRO B 1045 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1042 PRO A CA  
8420  C C   . PRO B 1045 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1042 PRO A C   
8421  O O   . PRO B 1045 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1042 PRO A O   
8422  C CB  . PRO B 1045 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1042 PRO A CB  
8423  C CG  . PRO B 1045 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1042 PRO A CG  
8424  C CD  . PRO B 1045 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1042 PRO A CD  
8425  N N   . TYR B 1046 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1043 TYR A N   
8426  C CA  . TYR B 1046 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1043 TYR A CA  
8427  C C   . TYR B 1046 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1043 TYR A C   
8428  O O   . TYR B 1046 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1043 TYR A O   
8429  C CB  . TYR B 1046 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1043 TYR A CB  
8430  C CG  . TYR B 1046 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1043 TYR A CG  
8431  C CD1 . TYR B 1046 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1043 TYR A CD1 
8432  C CD2 . TYR B 1046 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1043 TYR A CD2 
8433  C CE1 . TYR B 1046 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1043 TYR A CE1 
8434  C CE2 . TYR B 1046 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1043 TYR A CE2 
8435  C CZ  . TYR B 1046 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1043 TYR A CZ  
8436  O OH  . TYR B 1046 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1043 TYR A OH  
8437  N N   . GLN B 1047 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1044 GLN A N   
8438  C CA  . GLN B 1047 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1044 GLN A CA  
8439  C C   . GLN B 1047 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1044 GLN A C   
8440  O O   . GLN B 1047 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1044 GLN A O   
8441  C CB  . GLN B 1047 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1044 GLN A CB  
8442  C CG  . GLN B 1047 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1044 GLN A CG  
8443  C CD  . GLN B 1047 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1044 GLN A CD  
8444  O OE1 . GLN B 1047 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1044 GLN A OE1 
8445  N NE2 . GLN B 1047 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1044 GLN A NE2 
8446  N N   . LEU B 1048 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1045 LEU A N   
8447  C CA  . LEU B 1048 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1045 LEU A CA  
8448  C C   . LEU B 1048 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1045 LEU A C   
8449  O O   . LEU B 1048 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1045 LEU A O   
8450  C CB  . LEU B 1048 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1045 LEU A CB  
8451  C CG  . LEU B 1048 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1045 LEU A CG  
8452  C CD1 . LEU B 1048 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1045 LEU A CD1 
8453  C CD2 . LEU B 1048 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1045 LEU A CD2 
8454  N N   . THR B 1049 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1046 THR A N   
8455  C CA  . THR B 1049 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1046 THR A CA  
8456  C C   . THR B 1049 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1046 THR A C   
8457  O O   . THR B 1049 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1046 THR A O   
8458  C CB  . THR B 1049 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1046 THR A CB  
8459  O OG1 . THR B 1049 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1046 THR A OG1 
8460  C CG2 . THR B 1049 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1046 THR A CG2 
8461  N N   . ASP B 1050 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1047 ASP A N   
8462  C CA  . ASP B 1050 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1047 ASP A CA  
8463  C C   . ASP B 1050 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1047 ASP A C   
8464  O O   . ASP B 1050 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1047 ASP A O   
8465  C CB  . ASP B 1050 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1047 ASP A CB  
8466  C CG  . ASP B 1050 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1047 ASP A CG  
8467  O OD1 . ASP B 1050 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1047 ASP A OD1 
8468  O OD2 . ASP B 1050 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1047 ASP A OD2 
8469  N N   . GLN B 1051 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1048 GLN A N   
8470  C CA  . GLN B 1051 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1048 GLN A CA  
8471  C C   . GLN B 1051 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1048 GLN A C   
8472  O O   . GLN B 1051 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1048 GLN A O   
8473  C CB  . GLN B 1051 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1048 GLN A CB  
8474  C CG  . GLN B 1051 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1048 GLN A CG  
8475  C CD  . GLN B 1051 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1048 GLN A CD  
8476  O OE1 . GLN B 1051 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1048 GLN A OE1 
8477  N NE2 . GLN B 1051 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1048 GLN A NE2 
8478  N N   . PHE B 1052 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1049 PHE A N   
8479  C CA  . PHE B 1052 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1049 PHE A CA  
8480  C C   . PHE B 1052 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1049 PHE A C   
8481  O O   . PHE B 1052 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1049 PHE A O   
8482  C CB  . PHE B 1052 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1049 PHE A CB  
8483  C CG  . PHE B 1052 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1049 PHE A CG  
8484  C CD1 . PHE B 1052 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1049 PHE A CD1 
8485  C CD2 . PHE B 1052 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1049 PHE A CD2 
8486  C CE1 . PHE B 1052 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1049 PHE A CE1 
8487  C CE2 . PHE B 1052 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1049 PHE A CE2 
8488  C CZ  . PHE B 1052 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1049 PHE A CZ  
8489  N N   . THR B 1053 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1050 THR A N   
8490  C CA  . THR B 1053 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1050 THR A CA  
8491  C C   . THR B 1053 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1050 THR A C   
8492  O O   . THR B 1053 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1050 THR A O   
8493  C CB  . THR B 1053 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1050 THR A CB  
8494  O OG1 . THR B 1053 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1050 THR A OG1 
8495  C CG2 . THR B 1053 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1050 THR A CG2 
8496  N N   . SER B 1054 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1051 SER A N   
8497  C CA  . SER B 1054 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1051 SER A CA  
8498  C C   . SER B 1054 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1051 SER A C   
8499  O O   . SER B 1054 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1051 SER A O   
8500  C CB  . SER B 1054 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1051 SER A CB  
8501  O OG  . SER B 1054 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1051 SER A OG  
8502  N N   . PHE B 1055 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1052 PHE A N   
8503  C CA  . PHE B 1055 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1052 PHE A CA  
8504  C C   . PHE B 1055 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1052 PHE A C   
8505  O O   . PHE B 1055 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1052 PHE A O   
8506  C CB  . PHE B 1055 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1052 PHE A CB  
8507  C CG  . PHE B 1055 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1052 PHE A CG  
8508  C CD1 . PHE B 1055 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1052 PHE A CD1 
8509  C CD2 . PHE B 1055 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1052 PHE A CD2 
8510  C CE1 . PHE B 1055 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1052 PHE A CE1 
8511  C CE2 . PHE B 1055 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1052 PHE A CE2 
8512  C CZ  . PHE B 1055 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1052 PHE A CZ  
8513  N N   . ALA B 1056 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1053 ALA A N   
8514  C CA  . ALA B 1056 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1053 ALA A CA  
8515  C C   . ALA B 1056 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1053 ALA A C   
8516  O O   . ALA B 1056 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1053 ALA A O   
8517  C CB  . ALA B 1056 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1053 ALA A CB  
8518  N N   . LYS B 1057 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1054 LYS A N   
8519  C CA  . LYS B 1057 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1054 LYS A CA  
8520  C C   . LYS B 1057 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1054 LYS A C   
8521  O O   . LYS B 1057 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1054 LYS A O   
8522  C CB  . LYS B 1057 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1054 LYS A CB  
8523  C CG  . LYS B 1057 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1054 LYS A CG  
8524  C CD  . LYS B 1057 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1054 LYS A CD  
8525  C CE  . LYS B 1057 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1054 LYS A CE  
8526  N NZ  . LYS B 1057 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1054 LYS A NZ  
8527  N N   . MET B 1058 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1055 MET A N   
8528  C CA  . MET B 1058 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1055 MET A CA  
8529  C C   . MET B 1058 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1055 MET A C   
8530  O O   . MET B 1058 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1055 MET A O   
8531  C CB  . MET B 1058 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1055 MET A CB  
8532  C CG  . MET B 1058 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1055 MET A CG  
8533  S SD  . MET B 1058 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1055 MET A SD  
8534  C CE  . MET B 1058 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1055 MET A CE  
8535  N N   . GLY B 1059 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1056 GLY A N   
8536  C CA  . GLY B 1059 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1056 GLY A CA  
8537  C C   . GLY B 1059 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1056 GLY A C   
8538  O O   . GLY B 1059 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1056 GLY A O   
8539  N N   . THR B 1060 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1057 THR A N   
8540  C CA  . THR B 1060 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1057 THR A CA  
8541  C C   . THR B 1060 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1057 THR A C   
8542  O O   . THR B 1060 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1057 THR A O   
8543  C CB  . THR B 1060 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1057 THR A CB  
8544  O OG1 . THR B 1060 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1057 THR A OG1 
8545  C CG2 . THR B 1060 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1057 THR A CG2 
8546  N N   . GLN B 1061 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1058 GLN A N   
8547  C CA  . GLN B 1061 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1058 GLN A CA  
8548  C C   . GLN B 1061 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1058 GLN A C   
8549  O O   . GLN B 1061 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1058 GLN A O   
8550  C CB  . GLN B 1061 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1058 GLN A CB  
8551  C CG  . GLN B 1061 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1058 GLN A CG  
8552  C CD  . GLN B 1061 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1058 GLN A CD  
8553  O OE1 . GLN B 1061 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1058 GLN A OE1 
8554  N NE2 . GLN B 1061 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1058 GLN A NE2 
8555  N N   . SER B 1062 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1059 SER A N   
8556  C CA  . SER B 1062 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1059 SER A CA  
8557  C C   . SER B 1062 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1059 SER A C   
8558  O O   . SER B 1062 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1059 SER A O   
8559  C CB  . SER B 1062 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1059 SER A CB  
8560  O OG  . SER B 1062 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1059 SER A OG  
8561  N N   . GLY B 1063 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1060 GLY A N   
8562  C CA  . GLY B 1063 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1060 GLY A CA  
8563  C C   . GLY B 1063 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1060 GLY A C   
8564  O O   . GLY B 1063 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1060 GLY A O   
8565  N N   . PHE B 1064 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1061 PHE A N   
8566  C CA  . PHE B 1064 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1061 PHE A CA  
8567  C C   . PHE B 1064 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1061 PHE A C   
8568  O O   . PHE B 1064 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1061 PHE A O   
8569  C CB  . PHE B 1064 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1061 PHE A CB  
8570  C CG  . PHE B 1064 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1061 PHE A CG  
8571  C CD1 . PHE B 1064 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1061 PHE A CD1 
8572  C CD2 . PHE B 1064 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1061 PHE A CD2 
8573  C CE1 . PHE B 1064 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1061 PHE A CE1 
8574  C CE2 . PHE B 1064 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1061 PHE A CE2 
8575  C CZ  . PHE B 1064 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1061 PHE A CZ  
8576  N N   . LEU B 1065 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1062 LEU A N   
8577  C CA  . LEU B 1065 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1062 LEU A CA  
8578  C C   . LEU B 1065 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1062 LEU A C   
8579  O O   . LEU B 1065 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1062 LEU A O   
8580  C CB  . LEU B 1065 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1062 LEU A CB  
8581  C CG  . LEU B 1065 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1062 LEU A CG  
8582  C CD1 . LEU B 1065 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1062 LEU A CD1 
8583  C CD2 . LEU B 1065 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1062 LEU A CD2 
8584  N N   . PHE B 1066 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1063 PHE A N   
8585  C CA  . PHE B 1066 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1063 PHE A CA  
8586  C C   . PHE B 1066 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1063 PHE A C   
8587  O O   . PHE B 1066 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1063 PHE A O   
8588  C CB  . PHE B 1066 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1063 PHE A CB  
8589  C CG  . PHE B 1066 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1063 PHE A CG  
8590  C CD1 . PHE B 1066 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1063 PHE A CD1 
8591  C CD2 . PHE B 1066 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1063 PHE A CD2 
8592  C CE1 . PHE B 1066 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1063 PHE A CE1 
8593  C CE2 . PHE B 1066 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1063 PHE A CE2 
8594  C CZ  . PHE B 1066 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1063 PHE A CZ  
8595  N N   . TYR B 1067 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1064 TYR A N   
8596  C CA  . TYR B 1067 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1064 TYR A CA  
8597  C C   . TYR B 1067 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1064 TYR A C   
8598  O O   . TYR B 1067 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1064 TYR A O   
8599  C CB  . TYR B 1067 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1064 TYR A CB  
8600  C CG  . TYR B 1067 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1064 TYR A CG  
8601  C CD1 . TYR B 1067 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1064 TYR A CD1 
8602  C CD2 . TYR B 1067 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1064 TYR A CD2 
8603  C CE1 . TYR B 1067 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1064 TYR A CE1 
8604  C CE2 . TYR B 1067 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1064 TYR A CE2 
8605  C CZ  . TYR B 1067 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1064 TYR A CZ  
8606  O OH  . TYR B 1067 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1064 TYR A OH  
8607  N N   . VAL B 1068 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1065 VAL A N   
8608  C CA  . VAL B 1068 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1065 VAL A CA  
8609  C C   . VAL B 1068 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1065 VAL A C   
8610  O O   . VAL B 1068 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1065 VAL A O   
8611  C CB  . VAL B 1068 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1065 VAL A CB  
8612  C CG1 . VAL B 1068 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1065 VAL A CG1 
8613  C CG2 . VAL B 1068 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1065 VAL A CG2 
8614  N N   . PRO B 1069 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1066 PRO A N   
8615  C CA  . PRO B 1069 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1066 PRO A CA  
8616  C C   . PRO B 1069 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1066 PRO A C   
8617  O O   . PRO B 1069 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1066 PRO A O   
8618  C CB  . PRO B 1069 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1066 PRO A CB  
8619  C CG  . PRO B 1069 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1066 PRO A CG  
8620  C CD  . PRO B 1069 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1066 PRO A CD  
8621  N N   . ALA B 1070 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1067 ALA A N   
8622  C CA  . ALA B 1070 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1067 ALA A CA  
8623  C C   . ALA B 1070 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1067 ALA A C   
8624  O O   . ALA B 1070 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1067 ALA A O   
8625  C CB  . ALA B 1070 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1067 ALA A CB  
8626  N N   . PRO B 1071 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1068 PRO A N   
8627  C CA  . PRO B 1071 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1068 PRO A CA  
8628  C C   . PRO B 1071 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1068 PRO A C   
8629  O O   . PRO B 1071 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1068 PRO A O   
8630  C CB  . PRO B 1071 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1068 PRO A CB  
8631  C CG  . PRO B 1071 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1068 PRO A CG  
8632  C CD  . PRO B 1071 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1068 PRO A CD  
8633  N N   . TYR B 1072 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1069 TYR A N   
8634  C CA  . TYR B 1072 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1069 TYR A CA  
8635  C C   . TYR B 1072 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1069 TYR A C   
8636  O O   . TYR B 1072 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1069 TYR A O   
8637  C CB  . TYR B 1072 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1069 TYR A CB  
8638  C CG  . TYR B 1072 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1069 TYR A CG  
8639  C CD1 . TYR B 1072 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1069 TYR A CD1 
8640  C CD2 . TYR B 1072 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1069 TYR A CD2 
8641  C CE1 . TYR B 1072 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1069 TYR A CE1 
8642  C CE2 . TYR B 1072 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1069 TYR A CE2 
8643  C CZ  . TYR B 1072 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1069 TYR A CZ  
8644  O OH  . TYR B 1072 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1069 TYR A OH  
8645  N N   . THR B 1073 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1070 THR A N   
8646  C CA  . THR B 1073 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1070 THR A CA  
8647  C C   . THR B 1073 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1070 THR A C   
8648  O O   . THR B 1073 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1070 THR A O   
8649  C CB  . THR B 1073 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1070 THR A CB  
8650  O OG1 . THR B 1073 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1070 THR A OG1 
8651  C CG2 . THR B 1073 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1070 THR A CG2 
8652  N N   . SER B 1074 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1071 SER A N   
8653  C CA  . SER B 1074 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1071 SER A CA  
8654  C C   . SER B 1074 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1071 SER A C   
8655  O O   . SER B 1074 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1071 SER A O   
8656  C CB  . SER B 1074 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1071 SER A CB  
8657  O OG  . SER B 1074 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1071 SER A OG  
8658  N N   . LYS B 1075 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1072 LYS A N   
8659  C CA  . LYS B 1075 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1072 LYS A CA  
8660  C C   . LYS B 1075 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1072 LYS A C   
8661  O O   . LYS B 1075 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1072 LYS A O   
8662  C CB  . LYS B 1075 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1072 LYS A CB  
8663  C CG  . LYS B 1075 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1072 LYS A CG  
8664  C CD  . LYS B 1075 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1072 LYS A CD  
8665  C CE  . LYS B 1075 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1072 LYS A CE  
8666  N NZ  . LYS B 1075 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1072 LYS A NZ  
8667  N N   . ILE B 1076 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1073 ILE A N   
8668  C CA  . ILE B 1076 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1073 ILE A CA  
8669  C C   . ILE B 1076 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1073 ILE A C   
8670  O O   . ILE B 1076 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1073 ILE A O   
8671  C CB  . ILE B 1076 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1073 ILE A CB  
8672  C CG1 . ILE B 1076 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1073 ILE A CG1 
8673  C CG2 . ILE B 1076 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1073 ILE A CG2 
8674  C CD1 . ILE B 1076 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1073 ILE A CD1 
8675  N N   . ASP B 1077 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1074 ASP A N   
8676  C CA  . ASP B 1077 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1074 ASP A CA  
8677  C C   . ASP B 1077 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1074 ASP A C   
8678  O O   . ASP B 1077 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1074 ASP A O   
8679  C CB  . ASP B 1077 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1074 ASP A CB  
8680  C CG  . ASP B 1077 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1074 ASP A CG  
8681  O OD1 . ASP B 1077 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1074 ASP A OD1 
8682  O OD2 . ASP B 1077 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1074 ASP A OD2 
8683  N N   . PRO B 1078 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1075 PRO A N   
8684  C CA  . PRO B 1078 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1075 PRO A CA  
8685  C C   . PRO B 1078 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1075 PRO A C   
8686  O O   . PRO B 1078 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1075 PRO A O   
8687  C CB  . PRO B 1078 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1075 PRO A CB  
8688  C CG  . PRO B 1078 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1075 PRO A CG  
8689  C CD  . PRO B 1078 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1075 PRO A CD  
8690  N N   . LEU B 1079 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1076 LEU A N   
8691  C CA  . LEU B 1079 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1076 LEU A CA  
8692  C C   . LEU B 1079 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1076 LEU A C   
8693  O O   . LEU B 1079 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1076 LEU A O   
8694  C CB  . LEU B 1079 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1076 LEU A CB  
8695  C CG  . LEU B 1079 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1076 LEU A CG  
8696  C CD1 . LEU B 1079 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1076 LEU A CD1 
8697  C CD2 . LEU B 1079 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1076 LEU A CD2 
8698  N N   . THR B 1080 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1077 THR A N   
8699  C CA  . THR B 1080 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1077 THR A CA  
8700  C C   . THR B 1080 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1077 THR A C   
8701  O O   . THR B 1080 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1077 THR A O   
8702  C CB  . THR B 1080 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1077 THR A CB  
8703  O OG1 . THR B 1080 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1077 THR A OG1 
8704  C CG2 . THR B 1080 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1077 THR A CG2 
8705  N N   . GLY B 1081 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1078 GLY A N   
8706  C CA  . GLY B 1081 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1078 GLY A CA  
8707  C C   . GLY B 1081 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1078 GLY A C   
8708  O O   . GLY B 1081 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1078 GLY A O   
8709  N N   . PHE B 1082 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1079 PHE A N   
8710  C CA  . PHE B 1082 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1079 PHE A CA  
8711  C C   . PHE B 1082 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1079 PHE A C   
8712  O O   . PHE B 1082 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1079 PHE A O   
8713  C CB  . PHE B 1082 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1079 PHE A CB  
8714  C CG  . PHE B 1082 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1079 PHE A CG  
8715  C CD1 . PHE B 1082 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1079 PHE A CD1 
8716  C CD2 . PHE B 1082 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1079 PHE A CD2 
8717  C CE1 . PHE B 1082 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1079 PHE A CE1 
8718  C CE2 . PHE B 1082 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1079 PHE A CE2 
8719  C CZ  . PHE B 1082 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1079 PHE A CZ  
8720  N N   . VAL B 1083 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1080 VAL A N   
8721  C CA  . VAL B 1083 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1080 VAL A CA  
8722  C C   . VAL B 1083 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1080 VAL A C   
8723  O O   . VAL B 1083 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1080 VAL A O   
8724  C CB  . VAL B 1083 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1080 VAL A CB  
8725  C CG1 . VAL B 1083 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1080 VAL A CG1 
8726  C CG2 . VAL B 1083 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1080 VAL A CG2 
8727  N N   . ASP B 1084 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1081 ASP A N   
8728  C CA  . ASP B 1084 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1081 ASP A CA  
8729  C C   . ASP B 1084 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1081 ASP A C   
8730  O O   . ASP B 1084 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1081 ASP A O   
8731  C CB  . ASP B 1084 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1081 ASP A CB  
8732  C CG  . ASP B 1084 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1081 ASP A CG  
8733  O OD1 . ASP B 1084 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1081 ASP A OD1 
8734  O OD2 . ASP B 1084 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1081 ASP A OD2 
8735  N N   . PRO B 1085 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1082 PRO A N   
8736  C CA  . PRO B 1085 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1082 PRO A CA  
8737  C C   . PRO B 1085 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1082 PRO A C   
8738  O O   . PRO B 1085 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1082 PRO A O   
8739  C CB  . PRO B 1085 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1082 PRO A CB  
8740  C CG  . PRO B 1085 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1082 PRO A CG  
8741  C CD  . PRO B 1085 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1082 PRO A CD  
8742  N N   . PHE B 1086 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1083 PHE A N   
8743  C CA  . PHE B 1086 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1083 PHE A CA  
8744  C C   . PHE B 1086 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1083 PHE A C   
8745  O O   . PHE B 1086 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1083 PHE A O   
8746  C CB  . PHE B 1086 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1083 PHE A CB  
8747  C CG  . PHE B 1086 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1083 PHE A CG  
8748  C CD1 . PHE B 1086 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1083 PHE A CD1 
8749  C CD2 . PHE B 1086 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1083 PHE A CD2 
8750  C CE1 . PHE B 1086 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1083 PHE A CE1 
8751  C CE2 . PHE B 1086 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1083 PHE A CE2 
8752  C CZ  . PHE B 1086 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1083 PHE A CZ  
8753  N N   . VAL B 1087 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1084 VAL A N   
8754  C CA  . VAL B 1087 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1084 VAL A CA  
8755  C C   . VAL B 1087 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1084 VAL A C   
8756  O O   . VAL B 1087 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1084 VAL A O   
8757  C CB  . VAL B 1087 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1084 VAL A CB  
8758  C CG1 . VAL B 1087 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1084 VAL A CG1 
8759  C CG2 . VAL B 1087 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1084 VAL A CG2 
8760  N N   . TRP B 1088 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1085 TRP A N   
8761  C CA  . TRP B 1088 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1085 TRP A CA  
8762  C C   . TRP B 1088 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1085 TRP A C   
8763  O O   . TRP B 1088 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1085 TRP A O   
8764  C CB  . TRP B 1088 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1085 TRP A CB  
8765  C CG  . TRP B 1088 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1085 TRP A CG  
8766  C CD1 . TRP B 1088 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1085 TRP A CD1 
8767  C CD2 . TRP B 1088 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1085 TRP A CD2 
8768  N NE1 . TRP B 1088 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1085 TRP A NE1 
8769  C CE2 . TRP B 1088 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1085 TRP A CE2 
8770  C CE3 . TRP B 1088 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1085 TRP A CE3 
8771  C CZ2 . TRP B 1088 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1085 TRP A CZ2 
8772  C CZ3 . TRP B 1088 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1085 TRP A CZ3 
8773  C CH2 . TRP B 1088 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1085 TRP A CH2 
8774  N N   . LYS B 1089 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1086 LYS A N   
8775  C CA  . LYS B 1089 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1086 LYS A CA  
8776  C C   . LYS B 1089 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1086 LYS A C   
8777  O O   . LYS B 1089 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1086 LYS A O   
8778  C CB  . LYS B 1089 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1086 LYS A CB  
8779  C CG  . LYS B 1089 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1086 LYS A CG  
8780  C CD  . LYS B 1089 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1086 LYS A CD  
8781  C CE  . LYS B 1089 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1086 LYS A CE  
8782  N NZ  . LYS B 1089 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1086 LYS A NZ  
8783  N N   . THR B 1090 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1087 THR A N   
8784  C CA  . THR B 1090 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1087 THR A CA  
8785  C C   . THR B 1090 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1087 THR A C   
8786  O O   . THR B 1090 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1087 THR A O   
8787  C CB  . THR B 1090 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1087 THR A CB  
8788  O OG1 . THR B 1090 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1087 THR A OG1 
8789  C CG2 . THR B 1090 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1087 THR A CG2 
8790  N N   . ILE B 1091 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1088 ILE A N   
8791  C CA  . ILE B 1091 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1088 ILE A CA  
8792  C C   . ILE B 1091 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1088 ILE A C   
8793  O O   . ILE B 1091 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1088 ILE A O   
8794  C CB  . ILE B 1091 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1088 ILE A CB  
8795  C CG1 . ILE B 1091 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1088 ILE A CG1 
8796  C CG2 . ILE B 1091 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1088 ILE A CG2 
8797  C CD1 . ILE B 1091 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1088 ILE A CD1 
8798  N N   . LYS B 1092 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1089 LYS A N   
8799  C CA  . LYS B 1092 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1089 LYS A CA  
8800  C C   . LYS B 1092 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1089 LYS A C   
8801  O O   . LYS B 1092 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1089 LYS A O   
8807  N N   . ASN B 1093 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1090 ASN A N   
8808  C CA  . ASN B 1093 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1090 ASN A CA  
8809  C C   . ASN B 1093 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1090 ASN A C   
8810  O O   . ASN B 1093 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1090 ASN A O   
8811  C CB  . ASN B 1093 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1090 ASN A CB  
8812  C CG  . ASN B 1093 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1090 ASN A CG  
8813  O OD1 . ASN B 1093 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1090 ASN A OD1 
8814  N ND2 . ASN B 1093 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1090 ASN A ND2 
8815  N N   . HIS B 1094 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1091 HIS A N   
8816  C CA  . HIS B 1094 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1091 HIS A CA  
8817  C C   . HIS B 1094 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1091 HIS A C   
8818  O O   . HIS B 1094 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1091 HIS A O   
8819  C CB  . HIS B 1094 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1091 HIS A CB  
8820  C CG  . HIS B 1094 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1091 HIS A CG  
8821  N ND1 . HIS B 1094 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1091 HIS A ND1 
8822  C CD2 . HIS B 1094 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1091 HIS A CD2 
8823  C CE1 . HIS B 1094 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1091 HIS A CE1 
8824  N NE2 . HIS B 1094 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1091 HIS A NE2 
8825  N N   . GLU B 1095 ? 0.6023 0.6023 0.6023 0.0000  0.0000  0.0000  1092 GLU A N   
8826  C CA  . GLU B 1095 ? 0.6023 0.6023 0.6023 0.0000  0.0000  0.0000  1092 GLU A CA  
8827  C C   . GLU B 1095 ? 0.6023 0.6023 0.6023 0.0000  0.0000  0.0000  1092 GLU A C   
8828  O O   . GLU B 1095 ? 0.6023 0.6023 0.6023 0.0000  0.0000  0.0000  1092 GLU A O   
8829  C CB  . GLU B 1095 ? 0.6023 0.6023 0.6023 0.0000  0.0000  0.0000  1092 GLU A CB  
8830  C CG  . GLU B 1095 ? 0.6023 0.6023 0.6023 0.0000  0.0000  0.0000  1092 GLU A CG  
8831  C CD  . GLU B 1095 ? 0.6023 0.6023 0.6023 0.0000  0.0000  0.0000  1092 GLU A CD  
8832  O OE1 . GLU B 1095 ? 0.6023 0.6023 0.6023 0.0000  0.0000  0.0000  1092 GLU A OE1 
8833  O OE2 . GLU B 1095 ? 0.6023 0.6023 0.6023 0.0000  0.0000  0.0000  1092 GLU A OE2 
8834  N N   . SER B 1096 ? 0.5689 0.5689 0.5689 0.0000  0.0000  0.0000  1093 SER A N   
8835  C CA  . SER B 1096 ? 0.5689 0.5689 0.5689 0.0000  0.0000  0.0000  1093 SER A CA  
8836  C C   . SER B 1096 ? 0.5689 0.5689 0.5689 0.0000  0.0000  0.0000  1093 SER A C   
8837  O O   . SER B 1096 ? 0.5689 0.5689 0.5689 0.0000  0.0000  0.0000  1093 SER A O   
8838  C CB  . SER B 1096 ? 0.5689 0.5689 0.5689 0.0000  0.0000  0.0000  1093 SER A CB  
8839  O OG  . SER B 1096 ? 0.5689 0.5689 0.5689 0.0000  0.0000  0.0000  1093 SER A OG  
8840  N N   . ARG B 1097 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1094 ARG A N   
8841  C CA  . ARG B 1097 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1094 ARG A CA  
8842  C C   . ARG B 1097 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1094 ARG A C   
8843  O O   . ARG B 1097 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1094 ARG A O   
8844  C CB  . ARG B 1097 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1094 ARG A CB  
8845  C CG  . ARG B 1097 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1094 ARG A CG  
8846  C CD  . ARG B 1097 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1094 ARG A CD  
8847  N NE  . ARG B 1097 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1094 ARG A NE  
8848  C CZ  . ARG B 1097 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1094 ARG A CZ  
8849  N NH1 . ARG B 1097 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1094 ARG A NH1 
8850  N NH2 . ARG B 1097 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1094 ARG A NH2 
8851  N N   . LYS B 1098 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1095 LYS A N   
8852  C CA  . LYS B 1098 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1095 LYS A CA  
8853  C C   . LYS B 1098 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1095 LYS A C   
8854  O O   . LYS B 1098 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1095 LYS A O   
8860  N N   . HIS B 1099 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1096 HIS A N   
8861  C CA  . HIS B 1099 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1096 HIS A CA  
8862  C C   . HIS B 1099 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1096 HIS A C   
8863  O O   . HIS B 1099 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1096 HIS A O   
8864  C CB  . HIS B 1099 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1096 HIS A CB  
8865  C CG  . HIS B 1099 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1096 HIS A CG  
8866  N ND1 . HIS B 1099 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1096 HIS A ND1 
8867  C CD2 . HIS B 1099 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1096 HIS A CD2 
8868  C CE1 . HIS B 1099 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1096 HIS A CE1 
8869  N NE2 . HIS B 1099 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1096 HIS A NE2 
8870  N N   . PHE B 1100 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1097 PHE A N   
8871  C CA  . PHE B 1100 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1097 PHE A CA  
8872  C C   . PHE B 1100 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1097 PHE A C   
8873  O O   . PHE B 1100 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1097 PHE A O   
8874  C CB  . PHE B 1100 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1097 PHE A CB  
8875  C CG  . PHE B 1100 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1097 PHE A CG  
8876  C CD1 . PHE B 1100 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1097 PHE A CD1 
8877  C CD2 . PHE B 1100 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1097 PHE A CD2 
8878  C CE1 . PHE B 1100 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1097 PHE A CE1 
8879  C CE2 . PHE B 1100 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1097 PHE A CE2 
8880  C CZ  . PHE B 1100 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1097 PHE A CZ  
8881  N N   . LEU B 1101 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1098 LEU A N   
8882  C CA  . LEU B 1101 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1098 LEU A CA  
8883  C C   . LEU B 1101 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1098 LEU A C   
8884  O O   . LEU B 1101 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1098 LEU A O   
8885  C CB  . LEU B 1101 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1098 LEU A CB  
8886  C CG  . LEU B 1101 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1098 LEU A CG  
8887  C CD1 . LEU B 1101 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1098 LEU A CD1 
8888  C CD2 . LEU B 1101 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1098 LEU A CD2 
8889  N N   . GLU B 1102 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1099 GLU A N   
8890  C CA  . GLU B 1102 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1099 GLU A CA  
8891  C C   . GLU B 1102 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1099 GLU A C   
8892  O O   . GLU B 1102 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1099 GLU A O   
8893  C CB  . GLU B 1102 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1099 GLU A CB  
8894  C CG  . GLU B 1102 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1099 GLU A CG  
8895  C CD  . GLU B 1102 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1099 GLU A CD  
8896  O OE1 . GLU B 1102 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1099 GLU A OE1 
8897  O OE2 . GLU B 1102 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1099 GLU A OE2 
8898  N N   . GLY B 1103 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1100 GLY A N   
8899  C CA  . GLY B 1103 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1100 GLY A CA  
8900  C C   . GLY B 1103 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1100 GLY A C   
8901  O O   . GLY B 1103 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1100 GLY A O   
8902  N N   . PHE B 1104 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1101 PHE A N   
8903  C CA  . PHE B 1104 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1101 PHE A CA  
8904  C C   . PHE B 1104 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1101 PHE A C   
8905  O O   . PHE B 1104 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1101 PHE A O   
8906  C CB  . PHE B 1104 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1101 PHE A CB  
8907  C CG  . PHE B 1104 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1101 PHE A CG  
8908  C CD1 . PHE B 1104 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1101 PHE A CD1 
8909  C CD2 . PHE B 1104 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1101 PHE A CD2 
8910  C CE1 . PHE B 1104 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1101 PHE A CE1 
8911  C CE2 . PHE B 1104 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1101 PHE A CE2 
8912  C CZ  . PHE B 1104 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1101 PHE A CZ  
8913  N N   . ASP B 1105 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1102 ASP A N   
8914  C CA  . ASP B 1105 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1102 ASP A CA  
8915  C C   . ASP B 1105 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1102 ASP A C   
8916  O O   . ASP B 1105 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1102 ASP A O   
8917  C CB  . ASP B 1105 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1102 ASP A CB  
8918  C CG  . ASP B 1105 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1102 ASP A CG  
8919  O OD1 . ASP B 1105 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1102 ASP A OD1 
8920  O OD2 . ASP B 1105 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1102 ASP A OD2 
8921  N N   . PHE B 1106 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1103 PHE A N   
8922  C CA  . PHE B 1106 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1103 PHE A CA  
8923  C C   . PHE B 1106 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1103 PHE A C   
8924  O O   . PHE B 1106 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1103 PHE A O   
8925  C CB  . PHE B 1106 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1103 PHE A CB  
8926  C CG  . PHE B 1106 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1103 PHE A CG  
8927  C CD1 . PHE B 1106 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1103 PHE A CD1 
8928  C CD2 . PHE B 1106 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1103 PHE A CD2 
8929  C CE1 . PHE B 1106 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1103 PHE A CE1 
8930  C CE2 . PHE B 1106 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1103 PHE A CE2 
8931  C CZ  . PHE B 1106 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1103 PHE A CZ  
8932  N N   . LEU B 1107 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1104 LEU A N   
8933  C CA  . LEU B 1107 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1104 LEU A CA  
8934  C C   . LEU B 1107 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1104 LEU A C   
8935  O O   . LEU B 1107 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1104 LEU A O   
8936  C CB  . LEU B 1107 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1104 LEU A CB  
8937  C CG  . LEU B 1107 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1104 LEU A CG  
8938  C CD1 . LEU B 1107 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1104 LEU A CD1 
8939  C CD2 . LEU B 1107 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1104 LEU A CD2 
8940  N N   . HIS B 1108 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1105 HIS A N   
8941  C CA  . HIS B 1108 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1105 HIS A CA  
8942  C C   . HIS B 1108 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1105 HIS A C   
8943  O O   . HIS B 1108 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1105 HIS A O   
8944  C CB  . HIS B 1108 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1105 HIS A CB  
8945  C CG  . HIS B 1108 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1105 HIS A CG  
8946  N ND1 . HIS B 1108 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1105 HIS A ND1 
8947  C CD2 . HIS B 1108 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1105 HIS A CD2 
8948  C CE1 . HIS B 1108 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1105 HIS A CE1 
8949  N NE2 . HIS B 1108 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1105 HIS A NE2 
8950  N N   . TYR B 1109 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1106 TYR A N   
8951  C CA  . TYR B 1109 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1106 TYR A CA  
8952  C C   . TYR B 1109 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1106 TYR A C   
8953  O O   . TYR B 1109 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1106 TYR A O   
8954  C CB  . TYR B 1109 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1106 TYR A CB  
8955  C CG  . TYR B 1109 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1106 TYR A CG  
8956  C CD1 . TYR B 1109 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1106 TYR A CD1 
8957  C CD2 . TYR B 1109 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1106 TYR A CD2 
8958  C CE1 . TYR B 1109 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1106 TYR A CE1 
8959  C CE2 . TYR B 1109 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1106 TYR A CE2 
8960  C CZ  . TYR B 1109 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1106 TYR A CZ  
8961  O OH  . TYR B 1109 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1106 TYR A OH  
8962  N N   . ASP B 1110 ? 0.5941 0.5941 0.5941 0.0000  0.0000  0.0000  1107 ASP A N   
8963  C CA  . ASP B 1110 ? 0.5941 0.5941 0.5941 0.0000  0.0000  0.0000  1107 ASP A CA  
8964  C C   . ASP B 1110 ? 0.5941 0.5941 0.5941 0.0000  0.0000  0.0000  1107 ASP A C   
8965  O O   . ASP B 1110 ? 0.5941 0.5941 0.5941 0.0000  0.0000  0.0000  1107 ASP A O   
8966  C CB  . ASP B 1110 ? 0.5941 0.5941 0.5941 0.0000  0.0000  0.0000  1107 ASP A CB  
8967  C CG  . ASP B 1110 ? 0.5941 0.5941 0.5941 0.0000  0.0000  0.0000  1107 ASP A CG  
8968  O OD1 . ASP B 1110 ? 0.5941 0.5941 0.5941 0.0000  0.0000  0.0000  1107 ASP A OD1 
8969  O OD2 . ASP B 1110 ? 0.5941 0.5941 0.5941 0.0000  0.0000  0.0000  1107 ASP A OD2 
8970  N N   . VAL B 1111 ? 0.5708 0.5708 0.5708 0.0000  0.0000  0.0000  1108 VAL A N   
8971  C CA  . VAL B 1111 ? 0.5708 0.5708 0.5708 0.0000  0.0000  0.0000  1108 VAL A CA  
8972  C C   . VAL B 1111 ? 0.5708 0.5708 0.5708 0.0000  0.0000  0.0000  1108 VAL A C   
8973  O O   . VAL B 1111 ? 0.5708 0.5708 0.5708 0.0000  0.0000  0.0000  1108 VAL A O   
8974  C CB  . VAL B 1111 ? 0.5708 0.5708 0.5708 0.0000  0.0000  0.0000  1108 VAL A CB  
8975  C CG1 . VAL B 1111 ? 0.5708 0.5708 0.5708 0.0000  0.0000  0.0000  1108 VAL A CG1 
8976  C CG2 . VAL B 1111 ? 0.5708 0.5708 0.5708 0.0000  0.0000  0.0000  1108 VAL A CG2 
8977  N N   . LYS B 1112 ? 0.5895 0.5895 0.5895 0.0000  0.0000  0.0000  1109 LYS A N   
8978  C CA  . LYS B 1112 ? 0.5895 0.5895 0.5895 0.0000  0.0000  0.0000  1109 LYS A CA  
8979  C C   . LYS B 1112 ? 0.5895 0.5895 0.5895 0.0000  0.0000  0.0000  1109 LYS A C   
8980  O O   . LYS B 1112 ? 0.5895 0.5895 0.5895 0.0000  0.0000  0.0000  1109 LYS A O   
8986  N N   . THR B 1113 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1110 THR A N   
8987  C CA  . THR B 1113 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1110 THR A CA  
8988  C C   . THR B 1113 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1110 THR A C   
8989  O O   . THR B 1113 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1110 THR A O   
8990  C CB  . THR B 1113 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1110 THR A CB  
8991  O OG1 . THR B 1113 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1110 THR A OG1 
8992  C CG2 . THR B 1113 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1110 THR A CG2 
8993  N N   . GLY B 1114 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1111 GLY A N   
8994  C CA  . GLY B 1114 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1111 GLY A CA  
8995  C C   . GLY B 1114 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1111 GLY A C   
8996  O O   . GLY B 1114 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1111 GLY A O   
8997  N N   . ASP B 1115 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1112 ASP A N   
8998  C CA  . ASP B 1115 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1112 ASP A CA  
8999  C C   . ASP B 1115 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1112 ASP A C   
9000  O O   . ASP B 1115 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1112 ASP A O   
9001  C CB  . ASP B 1115 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1112 ASP A CB  
9002  C CG  . ASP B 1115 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1112 ASP A CG  
9003  O OD1 . ASP B 1115 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1112 ASP A OD1 
9004  O OD2 . ASP B 1115 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1112 ASP A OD2 
9005  N N   . PHE B 1116 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1113 PHE A N   
9006  C CA  . PHE B 1116 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1113 PHE A CA  
9007  C C   . PHE B 1116 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1113 PHE A C   
9008  O O   . PHE B 1116 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1113 PHE A O   
9009  C CB  . PHE B 1116 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1113 PHE A CB  
9010  C CG  . PHE B 1116 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1113 PHE A CG  
9011  C CD1 . PHE B 1116 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1113 PHE A CD1 
9012  C CD2 . PHE B 1116 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1113 PHE A CD2 
9013  C CE1 . PHE B 1116 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1113 PHE A CE1 
9014  C CE2 . PHE B 1116 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1113 PHE A CE2 
9015  C CZ  . PHE B 1116 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1113 PHE A CZ  
9016  N N   . ILE B 1117 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1114 ILE A N   
9017  C CA  . ILE B 1117 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1114 ILE A CA  
9018  C C   . ILE B 1117 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1114 ILE A C   
9019  O O   . ILE B 1117 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1114 ILE A O   
9020  C CB  . ILE B 1117 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1114 ILE A CB  
9021  C CG1 . ILE B 1117 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1114 ILE A CG1 
9022  C CG2 . ILE B 1117 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1114 ILE A CG2 
9023  C CD1 . ILE B 1117 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1114 ILE A CD1 
9024  N N   . LEU B 1118 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1115 LEU A N   
9025  C CA  . LEU B 1118 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1115 LEU A CA  
9026  C C   . LEU B 1118 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1115 LEU A C   
9027  O O   . LEU B 1118 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1115 LEU A O   
9028  C CB  . LEU B 1118 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1115 LEU A CB  
9029  C CG  . LEU B 1118 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1115 LEU A CG  
9030  C CD1 . LEU B 1118 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1115 LEU A CD1 
9031  C CD2 . LEU B 1118 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1115 LEU A CD2 
9032  N N   . HIS B 1119 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1116 HIS A N   
9033  C CA  . HIS B 1119 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1116 HIS A CA  
9034  C C   . HIS B 1119 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1116 HIS A C   
9035  O O   . HIS B 1119 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1116 HIS A O   
9036  C CB  . HIS B 1119 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1116 HIS A CB  
9037  C CG  . HIS B 1119 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1116 HIS A CG  
9038  N ND1 . HIS B 1119 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1116 HIS A ND1 
9039  C CD2 . HIS B 1119 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1116 HIS A CD2 
9040  C CE1 . HIS B 1119 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1116 HIS A CE1 
9041  N NE2 . HIS B 1119 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1116 HIS A NE2 
9042  N N   . PHE B 1120 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1117 PHE A N   
9043  C CA  . PHE B 1120 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1117 PHE A CA  
9044  C C   . PHE B 1120 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1117 PHE A C   
9045  O O   . PHE B 1120 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1117 PHE A O   
9046  C CB  . PHE B 1120 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1117 PHE A CB  
9047  C CG  . PHE B 1120 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1117 PHE A CG  
9048  C CD1 . PHE B 1120 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1117 PHE A CD1 
9049  C CD2 . PHE B 1120 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1117 PHE A CD2 
9050  C CE1 . PHE B 1120 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1117 PHE A CE1 
9051  C CE2 . PHE B 1120 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1117 PHE A CE2 
9052  C CZ  . PHE B 1120 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1117 PHE A CZ  
9053  N N   . LYS B 1121 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1118 LYS A N   
9054  C CA  . LYS B 1121 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1118 LYS A CA  
9055  C C   . LYS B 1121 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1118 LYS A C   
9056  O O   . LYS B 1121 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1118 LYS A O   
9057  C CB  . LYS B 1121 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1118 LYS A CB  
9058  C CG  . LYS B 1121 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1118 LYS A CG  
9059  C CD  . LYS B 1121 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1118 LYS A CD  
9060  C CE  . LYS B 1121 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1118 LYS A CE  
9061  N NZ  . LYS B 1121 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1118 LYS A NZ  
9062  N N   . MET B 1122 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1119 MET A N   
9063  C CA  . MET B 1122 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1119 MET A CA  
9064  C C   . MET B 1122 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1119 MET A C   
9065  O O   . MET B 1122 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1119 MET A O   
9066  C CB  . MET B 1122 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1119 MET A CB  
9067  C CG  . MET B 1122 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1119 MET A CG  
9068  S SD  . MET B 1122 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1119 MET A SD  
9069  C CE  . MET B 1122 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1119 MET A CE  
9070  N N   . ASN B 1123 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1120 ASN A N   
9071  C CA  . ASN B 1123 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1120 ASN A CA  
9072  C C   . ASN B 1123 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1120 ASN A C   
9073  O O   . ASN B 1123 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1120 ASN A O   
9074  C CB  . ASN B 1123 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1120 ASN A CB  
9075  C CG  . ASN B 1123 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1120 ASN A CG  
9076  O OD1 . ASN B 1123 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1120 ASN A OD1 
9077  N ND2 . ASN B 1123 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1120 ASN A ND2 
9078  N N   . ARG B 1124 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1121 ARG A N   
9079  C CA  . ARG B 1124 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1121 ARG A CA  
9080  C C   . ARG B 1124 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1121 ARG A C   
9081  O O   . ARG B 1124 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1121 ARG A O   
9082  C CB  . ARG B 1124 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1121 ARG A CB  
9083  C CG  . ARG B 1124 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1121 ARG A CG  
9084  C CD  . ARG B 1124 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1121 ARG A CD  
9085  N NE  . ARG B 1124 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1121 ARG A NE  
9086  C CZ  . ARG B 1124 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1121 ARG A CZ  
9087  N NH1 . ARG B 1124 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1121 ARG A NH1 
9088  N NH2 . ARG B 1124 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1121 ARG A NH2 
9089  N N   . ASN B 1125 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1122 ASN A N   
9090  C CA  . ASN B 1125 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1122 ASN A CA  
9091  C C   . ASN B 1125 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1122 ASN A C   
9092  O O   . ASN B 1125 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1122 ASN A O   
9093  C CB  . ASN B 1125 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1122 ASN A CB  
9094  C CG  . ASN B 1125 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1122 ASN A CG  
9095  O OD1 . ASN B 1125 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1122 ASN A OD1 
9096  N ND2 . ASN B 1125 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1122 ASN A ND2 
9097  N N   . LEU B 1126 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1123 LEU A N   
9098  C CA  . LEU B 1126 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1123 LEU A CA  
9099  C C   . LEU B 1126 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1123 LEU A C   
9100  O O   . LEU B 1126 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1123 LEU A O   
9101  C CB  . LEU B 1126 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1123 LEU A CB  
9102  C CG  . LEU B 1126 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1123 LEU A CG  
9103  C CD1 . LEU B 1126 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1123 LEU A CD1 
9104  C CD2 . LEU B 1126 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1123 LEU A CD2 
9105  N N   . SER B 1127 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1124 SER A N   
9106  C CA  . SER B 1127 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1124 SER A CA  
9107  C C   . SER B 1127 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1124 SER A C   
9108  O O   . SER B 1127 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1124 SER A O   
9109  C CB  . SER B 1127 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1124 SER A CB  
9110  O OG  . SER B 1127 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1124 SER A OG  
9111  N N   . PHE B 1128 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1125 PHE A N   
9112  C CA  . PHE B 1128 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1125 PHE A CA  
9113  C C   . PHE B 1128 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1125 PHE A C   
9114  O O   . PHE B 1128 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1125 PHE A O   
9115  C CB  . PHE B 1128 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1125 PHE A CB  
9116  C CG  . PHE B 1128 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1125 PHE A CG  
9117  C CD1 . PHE B 1128 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1125 PHE A CD1 
9118  C CD2 . PHE B 1128 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1125 PHE A CD2 
9119  C CE1 . PHE B 1128 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1125 PHE A CE1 
9120  C CE2 . PHE B 1128 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1125 PHE A CE2 
9121  C CZ  . PHE B 1128 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1125 PHE A CZ  
9122  N N   . GLN B 1129 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1126 GLN A N   
9123  C CA  . GLN B 1129 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1126 GLN A CA  
9124  C C   . GLN B 1129 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1126 GLN A C   
9125  O O   . GLN B 1129 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1126 GLN A O   
9126  C CB  . GLN B 1129 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1126 GLN A CB  
9127  C CG  . GLN B 1129 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1126 GLN A CG  
9128  C CD  . GLN B 1129 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1126 GLN A CD  
9129  O OE1 . GLN B 1129 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1126 GLN A OE1 
9130  N NE2 . GLN B 1129 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1126 GLN A NE2 
9131  N N   . ARG B 1130 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1127 ARG A N   
9132  C CA  . ARG B 1130 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1127 ARG A CA  
9133  C C   . ARG B 1130 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1127 ARG A C   
9134  O O   . ARG B 1130 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1127 ARG A O   
9135  C CB  . ARG B 1130 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1127 ARG A CB  
9136  C CG  . ARG B 1130 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1127 ARG A CG  
9137  C CD  . ARG B 1130 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1127 ARG A CD  
9138  N NE  . ARG B 1130 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1127 ARG A NE  
9139  C CZ  . ARG B 1130 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1127 ARG A CZ  
9140  N NH1 . ARG B 1130 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1127 ARG A NH1 
9141  N NH2 . ARG B 1130 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1127 ARG A NH2 
9142  N N   . GLY B 1131 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1128 GLY A N   
9143  C CA  . GLY B 1131 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1128 GLY A CA  
9144  C C   . GLY B 1131 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1128 GLY A C   
9145  O O   . GLY B 1131 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1128 GLY A O   
9146  N N   . LEU B 1132 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1129 LEU A N   
9147  C CA  . LEU B 1132 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1129 LEU A CA  
9148  C C   . LEU B 1132 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1129 LEU A C   
9149  O O   . LEU B 1132 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1129 LEU A O   
9150  C CB  . LEU B 1132 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1129 LEU A CB  
9151  C CG  . LEU B 1132 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1129 LEU A CG  
9152  C CD1 . LEU B 1132 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1129 LEU A CD1 
9153  C CD2 . LEU B 1132 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1129 LEU A CD2 
9154  N N   . PRO B 1133 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1130 PRO A N   
9155  C CA  . PRO B 1133 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1130 PRO A CA  
9156  C C   . PRO B 1133 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1130 PRO A C   
9157  O O   . PRO B 1133 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1130 PRO A O   
9158  C CB  . PRO B 1133 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1130 PRO A CB  
9159  C CG  . PRO B 1133 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1130 PRO A CG  
9160  C CD  . PRO B 1133 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1130 PRO A CD  
9161  N N   . GLY B 1134 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1131 GLY A N   
9162  C CA  . GLY B 1134 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1131 GLY A CA  
9163  C C   . GLY B 1134 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1131 GLY A C   
9164  O O   . GLY B 1134 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1131 GLY A O   
9165  N N   . PHE B 1135 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1132 PHE A N   
9166  C CA  . PHE B 1135 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1132 PHE A CA  
9167  C C   . PHE B 1135 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1132 PHE A C   
9168  O O   . PHE B 1135 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1132 PHE A O   
9169  C CB  . PHE B 1135 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1132 PHE A CB  
9170  C CG  . PHE B 1135 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1132 PHE A CG  
9171  C CD1 . PHE B 1135 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1132 PHE A CD1 
9172  C CD2 . PHE B 1135 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1132 PHE A CD2 
9173  C CE1 . PHE B 1135 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1132 PHE A CE1 
9174  C CE2 . PHE B 1135 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1132 PHE A CE2 
9175  C CZ  . PHE B 1135 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1132 PHE A CZ  
9176  N N   . MET B 1136 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1133 MET A N   
9177  C CA  . MET B 1136 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1133 MET A CA  
9178  C C   . MET B 1136 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1133 MET A C   
9179  O O   . MET B 1136 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1133 MET A O   
9180  C CB  . MET B 1136 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1133 MET A CB  
9181  C CG  . MET B 1136 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1133 MET A CG  
9182  S SD  . MET B 1136 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1133 MET A SD  
9183  C CE  . MET B 1136 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1133 MET A CE  
9184  N N   . PRO B 1137 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1134 PRO A N   
9185  C CA  . PRO B 1137 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1134 PRO A CA  
9186  C C   . PRO B 1137 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1134 PRO A C   
9187  O O   . PRO B 1137 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1134 PRO A O   
9188  C CB  . PRO B 1137 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1134 PRO A CB  
9189  C CG  . PRO B 1137 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1134 PRO A CG  
9190  C CD  . PRO B 1137 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1134 PRO A CD  
9191  N N   . ALA B 1138 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1135 ALA A N   
9192  C CA  . ALA B 1138 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1135 ALA A CA  
9193  C C   . ALA B 1138 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1135 ALA A C   
9194  O O   . ALA B 1138 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1135 ALA A O   
9195  C CB  . ALA B 1138 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1135 ALA A CB  
9196  N N   . TRP B 1139 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1136 TRP A N   
9197  C CA  . TRP B 1139 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1136 TRP A CA  
9198  C C   . TRP B 1139 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1136 TRP A C   
9199  O O   . TRP B 1139 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1136 TRP A O   
9200  C CB  . TRP B 1139 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1136 TRP A CB  
9201  C CG  . TRP B 1139 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1136 TRP A CG  
9202  C CD1 . TRP B 1139 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1136 TRP A CD1 
9203  C CD2 . TRP B 1139 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1136 TRP A CD2 
9204  N NE1 . TRP B 1139 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1136 TRP A NE1 
9205  C CE2 . TRP B 1139 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1136 TRP A CE2 
9206  C CE3 . TRP B 1139 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1136 TRP A CE3 
9207  C CZ2 . TRP B 1139 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1136 TRP A CZ2 
9208  C CZ3 . TRP B 1139 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1136 TRP A CZ3 
9209  C CH2 . TRP B 1139 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1136 TRP A CH2 
9210  N N   . ASP B 1140 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1137 ASP A N   
9211  C CA  . ASP B 1140 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1137 ASP A CA  
9212  C C   . ASP B 1140 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1137 ASP A C   
9213  O O   . ASP B 1140 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1137 ASP A O   
9214  C CB  . ASP B 1140 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1137 ASP A CB  
9215  C CG  . ASP B 1140 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1137 ASP A CG  
9216  O OD1 . ASP B 1140 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1137 ASP A OD1 
9217  O OD2 . ASP B 1140 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1137 ASP A OD2 
9218  N N   . ILE B 1141 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1138 ILE A N   
9219  C CA  . ILE B 1141 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1138 ILE A CA  
9220  C C   . ILE B 1141 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1138 ILE A C   
9221  O O   . ILE B 1141 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1138 ILE A O   
9222  C CB  . ILE B 1141 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1138 ILE A CB  
9223  C CG1 . ILE B 1141 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1138 ILE A CG1 
9224  C CG2 . ILE B 1141 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1138 ILE A CG2 
9225  C CD1 . ILE B 1141 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1138 ILE A CD1 
9226  N N   . VAL B 1142 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1139 VAL A N   
9227  C CA  . VAL B 1142 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1139 VAL A CA  
9228  C C   . VAL B 1142 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1139 VAL A C   
9229  O O   . VAL B 1142 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1139 VAL A O   
9230  C CB  . VAL B 1142 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1139 VAL A CB  
9231  C CG1 . VAL B 1142 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1139 VAL A CG1 
9232  C CG2 . VAL B 1142 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1139 VAL A CG2 
9233  N N   . PHE B 1143 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1140 PHE A N   
9234  C CA  . PHE B 1143 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1140 PHE A CA  
9235  C C   . PHE B 1143 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1140 PHE A C   
9236  O O   . PHE B 1143 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1140 PHE A O   
9237  C CB  . PHE B 1143 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1140 PHE A CB  
9238  C CG  . PHE B 1143 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1140 PHE A CG  
9239  C CD1 . PHE B 1143 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1140 PHE A CD1 
9240  C CD2 . PHE B 1143 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1140 PHE A CD2 
9241  C CE1 . PHE B 1143 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1140 PHE A CE1 
9242  C CE2 . PHE B 1143 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1140 PHE A CE2 
9243  C CZ  . PHE B 1143 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1140 PHE A CZ  
9244  N N   . GLU B 1144 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1141 GLU A N   
9245  C CA  . GLU B 1144 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1141 GLU A CA  
9246  C C   . GLU B 1144 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1141 GLU A C   
9247  O O   . GLU B 1144 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1141 GLU A O   
9248  C CB  . GLU B 1144 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1141 GLU A CB  
9249  C CG  . GLU B 1144 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1141 GLU A CG  
9250  C CD  . GLU B 1144 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1141 GLU A CD  
9251  O OE1 . GLU B 1144 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1141 GLU A OE1 
9252  O OE2 . GLU B 1144 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1141 GLU A OE2 
9253  N N   . LYS B 1145 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1142 LYS A N   
9254  C CA  . LYS B 1145 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1142 LYS A CA  
9255  C C   . LYS B 1145 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1142 LYS A C   
9256  O O   . LYS B 1145 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1142 LYS A O   
9257  C CB  . LYS B 1145 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1142 LYS A CB  
9258  C CG  . LYS B 1145 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1142 LYS A CG  
9259  C CD  . LYS B 1145 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1142 LYS A CD  
9260  C CE  . LYS B 1145 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1142 LYS A CE  
9261  N NZ  . LYS B 1145 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1142 LYS A NZ  
9262  N N   . ASN B 1146 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1143 ASN A N   
9263  C CA  . ASN B 1146 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1143 ASN A CA  
9264  C C   . ASN B 1146 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1143 ASN A C   
9265  O O   . ASN B 1146 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1143 ASN A O   
9266  C CB  . ASN B 1146 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1143 ASN A CB  
9267  C CG  . ASN B 1146 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1143 ASN A CG  
9268  O OD1 . ASN B 1146 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1143 ASN A OD1 
9269  N ND2 . ASN B 1146 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1143 ASN A ND2 
9270  N N   . GLU B 1147 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1144 GLU A N   
9271  C CA  . GLU B 1147 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1144 GLU A CA  
9272  C C   . GLU B 1147 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1144 GLU A C   
9273  O O   . GLU B 1147 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1144 GLU A O   
9274  C CB  . GLU B 1147 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1144 GLU A CB  
9275  C CG  . GLU B 1147 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1144 GLU A CG  
9276  C CD  . GLU B 1147 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1144 GLU A CD  
9277  O OE1 . GLU B 1147 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1144 GLU A OE1 
9278  O OE2 . GLU B 1147 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1144 GLU A OE2 
9279  N N   . THR B 1148 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1145 THR A N   
9280  C CA  . THR B 1148 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1145 THR A CA  
9281  C C   . THR B 1148 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1145 THR A C   
9282  O O   . THR B 1148 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1145 THR A O   
9283  C CB  . THR B 1148 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1145 THR A CB  
9284  O OG1 . THR B 1148 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1145 THR A OG1 
9285  C CG2 . THR B 1148 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1145 THR A CG2 
9286  N N   . GLN B 1149 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1146 GLN A N   
9287  C CA  . GLN B 1149 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1146 GLN A CA  
9288  C C   . GLN B 1149 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1146 GLN A C   
9289  O O   . GLN B 1149 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1146 GLN A O   
9290  C CB  . GLN B 1149 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1146 GLN A CB  
9291  C CG  . GLN B 1149 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1146 GLN A CG  
9292  C CD  . GLN B 1149 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1146 GLN A CD  
9293  O OE1 . GLN B 1149 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1146 GLN A OE1 
9294  N NE2 . GLN B 1149 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1146 GLN A NE2 
9295  N N   . PHE B 1150 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1147 PHE A N   
9296  C CA  . PHE B 1150 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1147 PHE A CA  
9297  C C   . PHE B 1150 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1147 PHE A C   
9298  O O   . PHE B 1150 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1147 PHE A O   
9299  C CB  . PHE B 1150 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1147 PHE A CB  
9300  C CG  . PHE B 1150 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1147 PHE A CG  
9301  C CD1 . PHE B 1150 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1147 PHE A CD1 
9302  C CD2 . PHE B 1150 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1147 PHE A CD2 
9303  C CE1 . PHE B 1150 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1147 PHE A CE1 
9304  C CE2 . PHE B 1150 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1147 PHE A CE2 
9305  C CZ  . PHE B 1150 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1147 PHE A CZ  
9306  N N   . ASP B 1151 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1148 ASP A N   
9307  C CA  . ASP B 1151 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1148 ASP A CA  
9308  C C   . ASP B 1151 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1148 ASP A C   
9309  O O   . ASP B 1151 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1148 ASP A O   
9310  C CB  . ASP B 1151 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1148 ASP A CB  
9311  C CG  . ASP B 1151 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1148 ASP A CG  
9312  O OD1 . ASP B 1151 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1148 ASP A OD1 
9313  O OD2 . ASP B 1151 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1148 ASP A OD2 
9314  N N   . ALA B 1152 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1149 ALA A N   
9315  C CA  . ALA B 1152 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1149 ALA A CA  
9316  C C   . ALA B 1152 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1149 ALA A C   
9317  O O   . ALA B 1152 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1149 ALA A O   
9318  C CB  . ALA B 1152 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1149 ALA A CB  
9319  N N   . LYS B 1153 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1150 LYS A N   
9320  C CA  . LYS B 1153 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1150 LYS A CA  
9321  C C   . LYS B 1153 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1150 LYS A C   
9322  O O   . LYS B 1153 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1150 LYS A O   
9328  N N   . GLY B 1154 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1151 GLY A N   
9329  C CA  . GLY B 1154 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1151 GLY A CA  
9330  C C   . GLY B 1154 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1151 GLY A C   
9331  O O   . GLY B 1154 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1151 GLY A O   
9332  N N   . THR B 1155 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1152 THR A N   
9333  C CA  . THR B 1155 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1152 THR A CA  
9334  C C   . THR B 1155 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1152 THR A C   
9335  O O   . THR B 1155 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1152 THR A O   
9336  C CB  . THR B 1155 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1152 THR A CB  
9337  O OG1 . THR B 1155 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1152 THR A OG1 
9338  C CG2 . THR B 1155 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1152 THR A CG2 
9339  N N   . PRO B 1156 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1153 PRO A N   
9340  C CA  . PRO B 1156 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1153 PRO A CA  
9341  C C   . PRO B 1156 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1153 PRO A C   
9342  O O   . PRO B 1156 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1153 PRO A O   
9343  C CB  . PRO B 1156 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1153 PRO A CB  
9344  C CG  . PRO B 1156 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1153 PRO A CG  
9345  C CD  . PRO B 1156 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1153 PRO A CD  
9346  N N   . PHE B 1157 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1154 PHE A N   
9347  C CA  . PHE B 1157 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1154 PHE A CA  
9348  C C   . PHE B 1157 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1154 PHE A C   
9349  O O   . PHE B 1157 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1154 PHE A O   
9350  C CB  . PHE B 1157 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1154 PHE A CB  
9351  C CG  . PHE B 1157 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1154 PHE A CG  
9352  C CD1 . PHE B 1157 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1154 PHE A CD1 
9353  C CD2 . PHE B 1157 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1154 PHE A CD2 
9354  C CE1 . PHE B 1157 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1154 PHE A CE1 
9355  C CE2 . PHE B 1157 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1154 PHE A CE2 
9356  C CZ  . PHE B 1157 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1154 PHE A CZ  
9357  N N   . ILE B 1158 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1155 ILE A N   
9358  C CA  . ILE B 1158 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1155 ILE A CA  
9359  C C   . ILE B 1158 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1155 ILE A C   
9360  O O   . ILE B 1158 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1155 ILE A O   
9361  C CB  . ILE B 1158 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1155 ILE A CB  
9362  C CG1 . ILE B 1158 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1155 ILE A CG1 
9363  C CG2 . ILE B 1158 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1155 ILE A CG2 
9364  C CD1 . ILE B 1158 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1155 ILE A CD1 
9365  N N   . ALA B 1159 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1156 ALA A N   
9366  C CA  . ALA B 1159 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1156 ALA A CA  
9367  C C   . ALA B 1159 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1156 ALA A C   
9368  O O   . ALA B 1159 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1156 ALA A O   
9369  C CB  . ALA B 1159 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1156 ALA A CB  
9370  N N   . GLY B 1160 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1157 GLY A N   
9371  C CA  . GLY B 1160 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1157 GLY A CA  
9372  C C   . GLY B 1160 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1157 GLY A C   
9373  O O   . GLY B 1160 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1157 GLY A O   
9374  N N   . LYS B 1161 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1158 LYS A N   
9375  C CA  . LYS B 1161 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1158 LYS A CA  
9376  C C   . LYS B 1161 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1158 LYS A C   
9377  O O   . LYS B 1161 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1158 LYS A O   
9378  C CB  . LYS B 1161 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1158 LYS A CB  
9379  C CG  . LYS B 1161 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1158 LYS A CG  
9380  C CD  . LYS B 1161 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1158 LYS A CD  
9381  C CE  . LYS B 1161 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1158 LYS A CE  
9382  N NZ  . LYS B 1161 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1158 LYS A NZ  
9383  N N   . ARG B 1162 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1159 ARG A N   
9384  C CA  . ARG B 1162 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1159 ARG A CA  
9385  C C   . ARG B 1162 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1159 ARG A C   
9386  O O   . ARG B 1162 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1159 ARG A O   
9387  C CB  . ARG B 1162 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1159 ARG A CB  
9388  C CG  . ARG B 1162 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1159 ARG A CG  
9389  C CD  . ARG B 1162 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1159 ARG A CD  
9390  N NE  . ARG B 1162 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1159 ARG A NE  
9391  C CZ  . ARG B 1162 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1159 ARG A CZ  
9392  N NH1 . ARG B 1162 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1159 ARG A NH1 
9393  N NH2 . ARG B 1162 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1159 ARG A NH2 
9394  N N   . ILE B 1163 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1160 ILE A N   
9395  C CA  . ILE B 1163 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1160 ILE A CA  
9396  C C   . ILE B 1163 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1160 ILE A C   
9397  O O   . ILE B 1163 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1160 ILE A O   
9398  C CB  . ILE B 1163 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1160 ILE A CB  
9399  C CG1 . ILE B 1163 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1160 ILE A CG1 
9400  C CG2 . ILE B 1163 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1160 ILE A CG2 
9401  C CD1 . ILE B 1163 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1160 ILE A CD1 
9402  N N   . VAL B 1164 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1161 VAL A N   
9403  C CA  . VAL B 1164 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1161 VAL A CA  
9404  C C   . VAL B 1164 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1161 VAL A C   
9405  O O   . VAL B 1164 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1161 VAL A O   
9406  C CB  . VAL B 1164 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1161 VAL A CB  
9407  C CG1 . VAL B 1164 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1161 VAL A CG1 
9408  C CG2 . VAL B 1164 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1161 VAL A CG2 
9409  N N   . PRO B 1165 ? 0.8851 0.8851 0.8851 0.0000  0.0000  0.0000  1162 PRO A N   
9410  C CA  . PRO B 1165 ? 0.8851 0.8851 0.8851 0.0000  0.0000  0.0000  1162 PRO A CA  
9411  C C   . PRO B 1165 ? 0.8851 0.8851 0.8851 0.0000  0.0000  0.0000  1162 PRO A C   
9412  O O   . PRO B 1165 ? 0.8851 0.8851 0.8851 0.0000  0.0000  0.0000  1162 PRO A O   
9413  C CB  . PRO B 1165 ? 0.8851 0.8851 0.8851 0.0000  0.0000  0.0000  1162 PRO A CB  
9414  C CG  . PRO B 1165 ? 0.8851 0.8851 0.8851 0.0000  0.0000  0.0000  1162 PRO A CG  
9415  C CD  . PRO B 1165 ? 0.8851 0.8851 0.8851 0.0000  0.0000  0.0000  1162 PRO A CD  
9502  N N   . TYR B 1176 ? 0.7635 0.7635 0.7635 0.0000  0.0000  0.0000  1173 TYR A N   
9503  C CA  . TYR B 1176 ? 0.7635 0.7635 0.7635 0.0000  0.0000  0.0000  1173 TYR A CA  
9504  C C   . TYR B 1176 ? 0.7635 0.7635 0.7635 0.0000  0.0000  0.0000  1173 TYR A C   
9505  O O   . TYR B 1176 ? 0.7635 0.7635 0.7635 0.0000  0.0000  0.0000  1173 TYR A O   
9506  C CB  . TYR B 1176 ? 0.7635 0.7635 0.7635 0.0000  0.0000  0.0000  1173 TYR A CB  
9507  C CG  . TYR B 1176 ? 0.7635 0.7635 0.7635 0.0000  0.0000  0.0000  1173 TYR A CG  
9508  C CD1 . TYR B 1176 ? 0.7635 0.7635 0.7635 0.0000  0.0000  0.0000  1173 TYR A CD1 
9509  C CD2 . TYR B 1176 ? 0.7635 0.7635 0.7635 0.0000  0.0000  0.0000  1173 TYR A CD2 
9510  C CE1 . TYR B 1176 ? 0.7635 0.7635 0.7635 0.0000  0.0000  0.0000  1173 TYR A CE1 
9511  C CE2 . TYR B 1176 ? 0.7635 0.7635 0.7635 0.0000  0.0000  0.0000  1173 TYR A CE2 
9512  C CZ  . TYR B 1176 ? 0.7635 0.7635 0.7635 0.0000  0.0000  0.0000  1173 TYR A CZ  
9513  O OH  . TYR B 1176 ? 0.7635 0.7635 0.7635 0.0000  0.0000  0.0000  1173 TYR A OH  
9514  N N   . ARG B 1177 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1174 ARG A N   
9515  C CA  . ARG B 1177 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1174 ARG A CA  
9516  C C   . ARG B 1177 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1174 ARG A C   
9517  O O   . ARG B 1177 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1174 ARG A O   
9518  C CB  . ARG B 1177 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1174 ARG A CB  
9519  C CG  . ARG B 1177 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1174 ARG A CG  
9520  C CD  . ARG B 1177 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1174 ARG A CD  
9521  N NE  . ARG B 1177 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1174 ARG A NE  
9522  C CZ  . ARG B 1177 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1174 ARG A CZ  
9523  N NH1 . ARG B 1177 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1174 ARG A NH1 
9524  N NH2 . ARG B 1177 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1174 ARG A NH2 
9525  N N   . ASP B 1178 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1175 ASP A N   
9526  C CA  . ASP B 1178 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1175 ASP A CA  
9527  C C   . ASP B 1178 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1175 ASP A C   
9528  O O   . ASP B 1178 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1175 ASP A O   
9529  C CB  . ASP B 1178 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1175 ASP A CB  
9530  C CG  . ASP B 1178 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1175 ASP A CG  
9531  O OD1 . ASP B 1178 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1175 ASP A OD1 
9532  O OD2 . ASP B 1178 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1175 ASP A OD2 
9533  N N   . LEU B 1179 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1176 LEU A N   
9534  C CA  . LEU B 1179 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1176 LEU A CA  
9535  C C   . LEU B 1179 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1176 LEU A C   
9536  O O   . LEU B 1179 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1176 LEU A O   
9537  C CB  . LEU B 1179 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1176 LEU A CB  
9538  C CG  . LEU B 1179 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1176 LEU A CG  
9539  C CD1 . LEU B 1179 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1176 LEU A CD1 
9540  C CD2 . LEU B 1179 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1176 LEU A CD2 
9541  N N   . TYR B 1180 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1177 TYR A N   
9542  C CA  . TYR B 1180 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1177 TYR A CA  
9543  C C   . TYR B 1180 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1177 TYR A C   
9544  O O   . TYR B 1180 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1177 TYR A O   
9545  C CB  . TYR B 1180 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1177 TYR A CB  
9546  C CG  . TYR B 1180 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1177 TYR A CG  
9547  C CD1 . TYR B 1180 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1177 TYR A CD1 
9548  C CD2 . TYR B 1180 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1177 TYR A CD2 
9549  C CE1 . TYR B 1180 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1177 TYR A CE1 
9550  C CE2 . TYR B 1180 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1177 TYR A CE2 
9551  C CZ  . TYR B 1180 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1177 TYR A CZ  
9552  O OH  . TYR B 1180 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1177 TYR A OH  
9553  N N   . PRO B 1181 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1178 PRO A N   
9554  C CA  . PRO B 1181 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1178 PRO A CA  
9555  C C   . PRO B 1181 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1178 PRO A C   
9556  O O   . PRO B 1181 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1178 PRO A O   
9557  C CB  . PRO B 1181 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1178 PRO A CB  
9558  C CG  . PRO B 1181 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1178 PRO A CG  
9559  C CD  . PRO B 1181 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1178 PRO A CD  
9560  N N   . ALA B 1182 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1179 ALA A N   
9561  C CA  . ALA B 1182 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1179 ALA A CA  
9562  C C   . ALA B 1182 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1179 ALA A C   
9563  O O   . ALA B 1182 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1179 ALA A O   
9564  C CB  . ALA B 1182 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1179 ALA A CB  
9565  N N   . ASN B 1183 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1180 ASN A N   
9566  C CA  . ASN B 1183 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1180 ASN A CA  
9567  C C   . ASN B 1183 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1180 ASN A C   
9568  O O   . ASN B 1183 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1180 ASN A O   
9569  C CB  . ASN B 1183 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1180 ASN A CB  
9570  C CG  . ASN B 1183 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1180 ASN A CG  
9571  O OD1 . ASN B 1183 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1180 ASN A OD1 
9572  N ND2 . ASN B 1183 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1180 ASN A ND2 
9573  N N   . GLU B 1184 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1181 GLU A N   
9574  C CA  . GLU B 1184 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1181 GLU A CA  
9575  C C   . GLU B 1184 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1181 GLU A C   
9576  O O   . GLU B 1184 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1181 GLU A O   
9577  C CB  . GLU B 1184 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1181 GLU A CB  
9578  C CG  . GLU B 1184 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1181 GLU A CG  
9579  C CD  . GLU B 1184 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1181 GLU A CD  
9580  O OE1 . GLU B 1184 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1181 GLU A OE1 
9581  O OE2 . GLU B 1184 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1181 GLU A OE2 
9582  N N   . LEU B 1185 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1182 LEU A N   
9583  C CA  . LEU B 1185 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1182 LEU A CA  
9584  C C   . LEU B 1185 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1182 LEU A C   
9585  O O   . LEU B 1185 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1182 LEU A O   
9586  C CB  . LEU B 1185 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1182 LEU A CB  
9587  C CG  . LEU B 1185 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1182 LEU A CG  
9588  C CD1 . LEU B 1185 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1182 LEU A CD1 
9589  C CD2 . LEU B 1185 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1182 LEU A CD2 
9590  N N   . ILE B 1186 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1183 ILE A N   
9591  C CA  . ILE B 1186 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1183 ILE A CA  
9592  C C   . ILE B 1186 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1183 ILE A C   
9593  O O   . ILE B 1186 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1183 ILE A O   
9594  C CB  . ILE B 1186 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1183 ILE A CB  
9595  C CG1 . ILE B 1186 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1183 ILE A CG1 
9596  C CG2 . ILE B 1186 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1183 ILE A CG2 
9597  C CD1 . ILE B 1186 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1183 ILE A CD1 
9598  N N   . ALA B 1187 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1184 ALA A N   
9599  C CA  . ALA B 1187 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1184 ALA A CA  
9600  C C   . ALA B 1187 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1184 ALA A C   
9601  O O   . ALA B 1187 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1184 ALA A O   
9602  C CB  . ALA B 1187 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1184 ALA A CB  
9603  N N   . LEU B 1188 ? 0.5730 0.5730 0.5730 0.0000  0.0000  0.0000  1185 LEU A N   
9604  C CA  . LEU B 1188 ? 0.5730 0.5730 0.5730 0.0000  0.0000  0.0000  1185 LEU A CA  
9605  C C   . LEU B 1188 ? 0.5730 0.5730 0.5730 0.0000  0.0000  0.0000  1185 LEU A C   
9606  O O   . LEU B 1188 ? 0.5730 0.5730 0.5730 0.0000  0.0000  0.0000  1185 LEU A O   
9607  C CB  . LEU B 1188 ? 0.5730 0.5730 0.5730 0.0000  0.0000  0.0000  1185 LEU A CB  
9608  C CG  . LEU B 1188 ? 0.5730 0.5730 0.5730 0.0000  0.0000  0.0000  1185 LEU A CG  
9609  C CD1 . LEU B 1188 ? 0.5730 0.5730 0.5730 0.0000  0.0000  0.0000  1185 LEU A CD1 
9610  C CD2 . LEU B 1188 ? 0.5730 0.5730 0.5730 0.0000  0.0000  0.0000  1185 LEU A CD2 
9611  N N   . LEU B 1189 ? 0.5726 0.5726 0.5726 0.0000  0.0000  0.0000  1186 LEU A N   
9612  C CA  . LEU B 1189 ? 0.5726 0.5726 0.5726 0.0000  0.0000  0.0000  1186 LEU A CA  
9613  C C   . LEU B 1189 ? 0.5726 0.5726 0.5726 0.0000  0.0000  0.0000  1186 LEU A C   
9614  O O   . LEU B 1189 ? 0.5726 0.5726 0.5726 0.0000  0.0000  0.0000  1186 LEU A O   
9615  C CB  . LEU B 1189 ? 0.5726 0.5726 0.5726 0.0000  0.0000  0.0000  1186 LEU A CB  
9616  C CG  . LEU B 1189 ? 0.5726 0.5726 0.5726 0.0000  0.0000  0.0000  1186 LEU A CG  
9617  C CD1 . LEU B 1189 ? 0.5726 0.5726 0.5726 0.0000  0.0000  0.0000  1186 LEU A CD1 
9618  C CD2 . LEU B 1189 ? 0.5726 0.5726 0.5726 0.0000  0.0000  0.0000  1186 LEU A CD2 
9619  N N   . GLU B 1190 ? 0.6084 0.6084 0.6084 0.0000  0.0000  0.0000  1187 GLU A N   
9620  C CA  . GLU B 1190 ? 0.6084 0.6084 0.6084 0.0000  0.0000  0.0000  1187 GLU A CA  
9621  C C   . GLU B 1190 ? 0.6084 0.6084 0.6084 0.0000  0.0000  0.0000  1187 GLU A C   
9622  O O   . GLU B 1190 ? 0.6084 0.6084 0.6084 0.0000  0.0000  0.0000  1187 GLU A O   
9623  C CB  . GLU B 1190 ? 0.6084 0.6084 0.6084 0.0000  0.0000  0.0000  1187 GLU A CB  
9624  C CG  . GLU B 1190 ? 0.6084 0.6084 0.6084 0.0000  0.0000  0.0000  1187 GLU A CG  
9625  C CD  . GLU B 1190 ? 0.6084 0.6084 0.6084 0.0000  0.0000  0.0000  1187 GLU A CD  
9626  O OE1 . GLU B 1190 ? 0.6084 0.6084 0.6084 0.0000  0.0000  0.0000  1187 GLU A OE1 
9627  O OE2 . GLU B 1190 ? 0.6084 0.6084 0.6084 0.0000  0.0000  0.0000  1187 GLU A OE2 
9628  N N   . GLU B 1191 ? 0.6334 0.6334 0.6334 0.0000  0.0000  0.0000  1188 GLU A N   
9629  C CA  . GLU B 1191 ? 0.6334 0.6334 0.6334 0.0000  0.0000  0.0000  1188 GLU A CA  
9630  C C   . GLU B 1191 ? 0.6334 0.6334 0.6334 0.0000  0.0000  0.0000  1188 GLU A C   
9631  O O   . GLU B 1191 ? 0.6334 0.6334 0.6334 0.0000  0.0000  0.0000  1188 GLU A O   
9632  C CB  . GLU B 1191 ? 0.6334 0.6334 0.6334 0.0000  0.0000  0.0000  1188 GLU A CB  
9633  C CG  . GLU B 1191 ? 0.6334 0.6334 0.6334 0.0000  0.0000  0.0000  1188 GLU A CG  
9634  C CD  . GLU B 1191 ? 0.6334 0.6334 0.6334 0.0000  0.0000  0.0000  1188 GLU A CD  
9635  O OE1 . GLU B 1191 ? 0.6334 0.6334 0.6334 0.0000  0.0000  0.0000  1188 GLU A OE1 
9636  O OE2 . GLU B 1191 ? 0.6334 0.6334 0.6334 0.0000  0.0000  0.0000  1188 GLU A OE2 
9637  N N   . LYS B 1192 ? 0.5801 0.5801 0.5801 0.0000  0.0000  0.0000  1189 LYS A N   
9638  C CA  . LYS B 1192 ? 0.5801 0.5801 0.5801 0.0000  0.0000  0.0000  1189 LYS A CA  
9639  C C   . LYS B 1192 ? 0.5801 0.5801 0.5801 0.0000  0.0000  0.0000  1189 LYS A C   
9640  O O   . LYS B 1192 ? 0.5801 0.5801 0.5801 0.0000  0.0000  0.0000  1189 LYS A O   
9641  C CB  . LYS B 1192 ? 0.5801 0.5801 0.5801 0.0000  0.0000  0.0000  1189 LYS A CB  
9642  C CG  . LYS B 1192 ? 0.5801 0.5801 0.5801 0.0000  0.0000  0.0000  1189 LYS A CG  
9643  C CD  . LYS B 1192 ? 0.5801 0.5801 0.5801 0.0000  0.0000  0.0000  1189 LYS A CD  
9644  C CE  . LYS B 1192 ? 0.5801 0.5801 0.5801 0.0000  0.0000  0.0000  1189 LYS A CE  
9645  N NZ  . LYS B 1192 ? 0.5801 0.5801 0.5801 0.0000  0.0000  0.0000  1189 LYS A NZ  
9646  N N   . GLY B 1193 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1190 GLY A N   
9647  C CA  . GLY B 1193 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1190 GLY A CA  
9648  C C   . GLY B 1193 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1190 GLY A C   
9649  O O   . GLY B 1193 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1190 GLY A O   
9650  N N   . ILE B 1194 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1191 ILE A N   
9651  C CA  . ILE B 1194 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1191 ILE A CA  
9652  C C   . ILE B 1194 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1191 ILE A C   
9653  O O   . ILE B 1194 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1191 ILE A O   
9654  C CB  . ILE B 1194 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1191 ILE A CB  
9655  C CG1 . ILE B 1194 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1191 ILE A CG1 
9656  C CG2 . ILE B 1194 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1191 ILE A CG2 
9657  C CD1 . ILE B 1194 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1191 ILE A CD1 
9658  N N   . VAL B 1195 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1192 VAL A N   
9659  C CA  . VAL B 1195 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1192 VAL A CA  
9660  C C   . VAL B 1195 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1192 VAL A C   
9661  O O   . VAL B 1195 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1192 VAL A O   
9662  C CB  . VAL B 1195 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1192 VAL A CB  
9663  C CG1 . VAL B 1195 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1192 VAL A CG1 
9664  C CG2 . VAL B 1195 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1192 VAL A CG2 
9665  N N   . PHE B 1196 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1193 PHE A N   
9666  C CA  . PHE B 1196 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1193 PHE A CA  
9667  C C   . PHE B 1196 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1193 PHE A C   
9668  O O   . PHE B 1196 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1193 PHE A O   
9669  C CB  . PHE B 1196 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1193 PHE A CB  
9670  C CG  . PHE B 1196 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1193 PHE A CG  
9671  C CD1 . PHE B 1196 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1193 PHE A CD1 
9672  C CD2 . PHE B 1196 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1193 PHE A CD2 
9673  C CE1 . PHE B 1196 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1193 PHE A CE1 
9674  C CE2 . PHE B 1196 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1193 PHE A CE2 
9675  C CZ  . PHE B 1196 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1193 PHE A CZ  
9676  N N   . ARG B 1197 ? 0.5830 0.5830 0.5830 0.0000  0.0000  0.0000  1194 ARG A N   
9677  C CA  . ARG B 1197 ? 0.5830 0.5830 0.5830 0.0000  0.0000  0.0000  1194 ARG A CA  
9678  C C   . ARG B 1197 ? 0.5830 0.5830 0.5830 0.0000  0.0000  0.0000  1194 ARG A C   
9679  O O   . ARG B 1197 ? 0.5830 0.5830 0.5830 0.0000  0.0000  0.0000  1194 ARG A O   
9680  C CB  . ARG B 1197 ? 0.5830 0.5830 0.5830 0.0000  0.0000  0.0000  1194 ARG A CB  
9681  C CG  . ARG B 1197 ? 0.5830 0.5830 0.5830 0.0000  0.0000  0.0000  1194 ARG A CG  
9682  C CD  . ARG B 1197 ? 0.5830 0.5830 0.5830 0.0000  0.0000  0.0000  1194 ARG A CD  
9683  N NE  . ARG B 1197 ? 0.5830 0.5830 0.5830 0.0000  0.0000  0.0000  1194 ARG A NE  
9684  C CZ  . ARG B 1197 ? 0.5830 0.5830 0.5830 0.0000  0.0000  0.0000  1194 ARG A CZ  
9685  N NH1 . ARG B 1197 ? 0.5830 0.5830 0.5830 0.0000  0.0000  0.0000  1194 ARG A NH1 
9686  N NH2 . ARG B 1197 ? 0.5830 0.5830 0.5830 0.0000  0.0000  0.0000  1194 ARG A NH2 
9687  N N   . ASP B 1198 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1195 ASP A N   
9688  C CA  . ASP B 1198 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1195 ASP A CA  
9689  C C   . ASP B 1198 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1195 ASP A C   
9690  O O   . ASP B 1198 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1195 ASP A O   
9691  C CB  . ASP B 1198 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1195 ASP A CB  
9692  C CG  . ASP B 1198 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1195 ASP A CG  
9693  O OD1 . ASP B 1198 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1195 ASP A OD1 
9694  O OD2 . ASP B 1198 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1195 ASP A OD2 
9695  N N   . GLY B 1199 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1196 GLY A N   
9696  C CA  . GLY B 1199 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1196 GLY A CA  
9697  C C   . GLY B 1199 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1196 GLY A C   
9698  O O   . GLY B 1199 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1196 GLY A O   
9699  N N   . SER B 1200 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1197 SER A N   
9700  C CA  . SER B 1200 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1197 SER A CA  
9701  C C   . SER B 1200 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1197 SER A C   
9702  O O   . SER B 1200 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1197 SER A O   
9703  C CB  . SER B 1200 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1197 SER A CB  
9704  O OG  . SER B 1200 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1197 SER A OG  
9705  N N   . ASN B 1201 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1198 ASN A N   
9706  C CA  . ASN B 1201 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1198 ASN A CA  
9707  C C   . ASN B 1201 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1198 ASN A C   
9708  O O   . ASN B 1201 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1198 ASN A O   
9709  C CB  . ASN B 1201 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1198 ASN A CB  
9710  C CG  . ASN B 1201 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1198 ASN A CG  
9711  O OD1 . ASN B 1201 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1198 ASN A OD1 
9712  N ND2 . ASN B 1201 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1198 ASN A ND2 
9713  N N   . ILE B 1202 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1199 ILE A N   
9714  C CA  . ILE B 1202 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1199 ILE A CA  
9715  C C   . ILE B 1202 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1199 ILE A C   
9716  O O   . ILE B 1202 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1199 ILE A O   
9717  C CB  . ILE B 1202 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1199 ILE A CB  
9718  C CG1 . ILE B 1202 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1199 ILE A CG1 
9719  C CG2 . ILE B 1202 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1199 ILE A CG2 
9720  C CD1 . ILE B 1202 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1199 ILE A CD1 
9721  N N   . LEU B 1203 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1200 LEU A N   
9722  C CA  . LEU B 1203 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1200 LEU A CA  
9723  C C   . LEU B 1203 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1200 LEU A C   
9724  O O   . LEU B 1203 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1200 LEU A O   
9725  C CB  . LEU B 1203 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1200 LEU A CB  
9726  C CG  . LEU B 1203 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1200 LEU A CG  
9727  C CD1 . LEU B 1203 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1200 LEU A CD1 
9728  C CD2 . LEU B 1203 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1200 LEU A CD2 
9729  N N   . PRO B 1204 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1201 PRO A N   
9730  C CA  . PRO B 1204 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1201 PRO A CA  
9731  C C   . PRO B 1204 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1201 PRO A C   
9732  O O   . PRO B 1204 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1201 PRO A O   
9733  C CB  . PRO B 1204 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1201 PRO A CB  
9734  C CG  . PRO B 1204 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1201 PRO A CG  
9735  C CD  . PRO B 1204 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1201 PRO A CD  
9736  N N   . LYS B 1205 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1202 LYS A N   
9737  C CA  . LYS B 1205 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1202 LYS A CA  
9738  C C   . LYS B 1205 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1202 LYS A C   
9739  O O   . LYS B 1205 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1202 LYS A O   
9740  C CB  . LYS B 1205 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1202 LYS A CB  
9741  C CG  . LYS B 1205 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1202 LYS A CG  
9742  C CD  . LYS B 1205 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1202 LYS A CD  
9743  C CE  . LYS B 1205 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1202 LYS A CE  
9744  N NZ  . LYS B 1205 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1202 LYS A NZ  
9745  N N   . LEU B 1206 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1203 LEU A N   
9746  C CA  . LEU B 1206 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1203 LEU A CA  
9747  C C   . LEU B 1206 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1203 LEU A C   
9748  O O   . LEU B 1206 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1203 LEU A O   
9749  C CB  . LEU B 1206 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1203 LEU A CB  
9750  C CG  . LEU B 1206 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1203 LEU A CG  
9751  C CD1 . LEU B 1206 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1203 LEU A CD1 
9752  C CD2 . LEU B 1206 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1203 LEU A CD2 
9753  N N   . LEU B 1207 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1204 LEU A N   
9754  C CA  . LEU B 1207 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1204 LEU A CA  
9755  C C   . LEU B 1207 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1204 LEU A C   
9756  O O   . LEU B 1207 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1204 LEU A O   
9757  C CB  . LEU B 1207 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1204 LEU A CB  
9758  C CG  . LEU B 1207 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1204 LEU A CG  
9759  C CD1 . LEU B 1207 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1204 LEU A CD1 
9760  C CD2 . LEU B 1207 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1204 LEU A CD2 
9761  N N   . GLU B 1208 ? 0.5739 0.5739 0.5739 0.0000  0.0000  0.0000  1205 GLU A N   
9762  C CA  . GLU B 1208 ? 0.5739 0.5739 0.5739 0.0000  0.0000  0.0000  1205 GLU A CA  
9763  C C   . GLU B 1208 ? 0.5739 0.5739 0.5739 0.0000  0.0000  0.0000  1205 GLU A C   
9764  O O   . GLU B 1208 ? 0.5739 0.5739 0.5739 0.0000  0.0000  0.0000  1205 GLU A O   
9770  N N   . ASN B 1209 ? 0.6032 0.6032 0.6032 0.0000  0.0000  0.0000  1206 ASN A N   
9771  C CA  . ASN B 1209 ? 0.6032 0.6032 0.6032 0.0000  0.0000  0.0000  1206 ASN A CA  
9772  C C   . ASN B 1209 ? 0.6032 0.6032 0.6032 0.0000  0.0000  0.0000  1206 ASN A C   
9773  O O   . ASN B 1209 ? 0.6032 0.6032 0.6032 0.0000  0.0000  0.0000  1206 ASN A O   
9774  C CB  . ASN B 1209 ? 0.6032 0.6032 0.6032 0.0000  0.0000  0.0000  1206 ASN A CB  
9775  C CG  . ASN B 1209 ? 0.6032 0.6032 0.6032 0.0000  0.0000  0.0000  1206 ASN A CG  
9776  O OD1 . ASN B 1209 ? 0.6032 0.6032 0.6032 0.0000  0.0000  0.0000  1206 ASN A OD1 
9777  N ND2 . ASN B 1209 ? 0.6032 0.6032 0.6032 0.0000  0.0000  0.0000  1206 ASN A ND2 
9778  N N   . ASP B 1210 ? 0.5987 0.5987 0.5987 0.0000  0.0000  0.0000  1207 ASP A N   
9779  C CA  . ASP B 1210 ? 0.5987 0.5987 0.5987 0.0000  0.0000  0.0000  1207 ASP A CA  
9780  C C   . ASP B 1210 ? 0.5987 0.5987 0.5987 0.0000  0.0000  0.0000  1207 ASP A C   
9781  O O   . ASP B 1210 ? 0.5987 0.5987 0.5987 0.0000  0.0000  0.0000  1207 ASP A O   
9782  C CB  . ASP B 1210 ? 0.5987 0.5987 0.5987 0.0000  0.0000  0.0000  1207 ASP A CB  
9783  C CG  . ASP B 1210 ? 0.5987 0.5987 0.5987 0.0000  0.0000  0.0000  1207 ASP A CG  
9784  O OD1 . ASP B 1210 ? 0.5987 0.5987 0.5987 0.0000  0.0000  0.0000  1207 ASP A OD1 
9785  O OD2 . ASP B 1210 ? 0.5987 0.5987 0.5987 0.0000  0.0000  0.0000  1207 ASP A OD2 
9786  N N   . ASP B 1211 ? 0.6359 0.6359 0.6359 0.0000  0.0000  0.0000  1208 ASP A N   
9787  C CA  . ASP B 1211 ? 0.6359 0.6359 0.6359 0.0000  0.0000  0.0000  1208 ASP A CA  
9788  C C   . ASP B 1211 ? 0.6359 0.6359 0.6359 0.0000  0.0000  0.0000  1208 ASP A C   
9789  O O   . ASP B 1211 ? 0.6359 0.6359 0.6359 0.0000  0.0000  0.0000  1208 ASP A O   
9790  C CB  . ASP B 1211 ? 0.6359 0.6359 0.6359 0.0000  0.0000  0.0000  1208 ASP A CB  
9791  C CG  . ASP B 1211 ? 0.6359 0.6359 0.6359 0.0000  0.0000  0.0000  1208 ASP A CG  
9792  O OD1 . ASP B 1211 ? 0.6359 0.6359 0.6359 0.0000  0.0000  0.0000  1208 ASP A OD1 
9793  O OD2 . ASP B 1211 ? 0.6359 0.6359 0.6359 0.0000  0.0000  0.0000  1208 ASP A OD2 
9794  N N   . SER B 1212 ? 0.6401 0.6401 0.6401 0.0000  0.0000  0.0000  1209 SER A N   
9795  C CA  . SER B 1212 ? 0.6401 0.6401 0.6401 0.0000  0.0000  0.0000  1209 SER A CA  
9796  C C   . SER B 1212 ? 0.6401 0.6401 0.6401 0.0000  0.0000  0.0000  1209 SER A C   
9797  O O   . SER B 1212 ? 0.6401 0.6401 0.6401 0.0000  0.0000  0.0000  1209 SER A O   
9798  C CB  . SER B 1212 ? 0.6401 0.6401 0.6401 0.0000  0.0000  0.0000  1209 SER A CB  
9799  O OG  . SER B 1212 ? 0.6401 0.6401 0.6401 0.0000  0.0000  0.0000  1209 SER A OG  
9800  N N   . HIS B 1213 ? 0.5996 0.5996 0.5996 0.0000  0.0000  0.0000  1210 HIS A N   
9801  C CA  . HIS B 1213 ? 0.5996 0.5996 0.5996 0.0000  0.0000  0.0000  1210 HIS A CA  
9802  C C   . HIS B 1213 ? 0.5996 0.5996 0.5996 0.0000  0.0000  0.0000  1210 HIS A C   
9803  O O   . HIS B 1213 ? 0.5996 0.5996 0.5996 0.0000  0.0000  0.0000  1210 HIS A O   
9804  C CB  . HIS B 1213 ? 0.5996 0.5996 0.5996 0.0000  0.0000  0.0000  1210 HIS A CB  
9805  C CG  . HIS B 1213 ? 0.5996 0.5996 0.5996 0.0000  0.0000  0.0000  1210 HIS A CG  
9806  N ND1 . HIS B 1213 ? 0.5996 0.5996 0.5996 0.0000  0.0000  0.0000  1210 HIS A ND1 
9807  C CD2 . HIS B 1213 ? 0.5996 0.5996 0.5996 0.0000  0.0000  0.0000  1210 HIS A CD2 
9808  C CE1 . HIS B 1213 ? 0.5996 0.5996 0.5996 0.0000  0.0000  0.0000  1210 HIS A CE1 
9809  N NE2 . HIS B 1213 ? 0.5996 0.5996 0.5996 0.0000  0.0000  0.0000  1210 HIS A NE2 
9810  N N   . ALA B 1214 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1211 ALA A N   
9811  C CA  . ALA B 1214 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1211 ALA A CA  
9812  C C   . ALA B 1214 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1211 ALA A C   
9813  O O   . ALA B 1214 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1211 ALA A O   
9814  C CB  . ALA B 1214 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1211 ALA A CB  
9815  N N   . ILE B 1215 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1212 ILE A N   
9816  C CA  . ILE B 1215 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1212 ILE A CA  
9817  C C   . ILE B 1215 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1212 ILE A C   
9818  O O   . ILE B 1215 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1212 ILE A O   
9819  C CB  . ILE B 1215 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1212 ILE A CB  
9820  C CG1 . ILE B 1215 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1212 ILE A CG1 
9821  C CG2 . ILE B 1215 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1212 ILE A CG2 
9822  C CD1 . ILE B 1215 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1212 ILE A CD1 
9823  N N   . ASP B 1216 ? 0.5837 0.5837 0.5837 0.0000  0.0000  0.0000  1213 ASP A N   
9824  C CA  . ASP B 1216 ? 0.5837 0.5837 0.5837 0.0000  0.0000  0.0000  1213 ASP A CA  
9825  C C   . ASP B 1216 ? 0.5837 0.5837 0.5837 0.0000  0.0000  0.0000  1213 ASP A C   
9826  O O   . ASP B 1216 ? 0.5837 0.5837 0.5837 0.0000  0.0000  0.0000  1213 ASP A O   
9827  C CB  . ASP B 1216 ? 0.5837 0.5837 0.5837 0.0000  0.0000  0.0000  1213 ASP A CB  
9828  C CG  . ASP B 1216 ? 0.5837 0.5837 0.5837 0.0000  0.0000  0.0000  1213 ASP A CG  
9829  O OD1 . ASP B 1216 ? 0.5837 0.5837 0.5837 0.0000  0.0000  0.0000  1213 ASP A OD1 
9830  O OD2 . ASP B 1216 ? 0.5837 0.5837 0.5837 0.0000  0.0000  0.0000  1213 ASP A OD2 
9831  N N   . THR B 1217 ? 0.5776 0.5776 0.5776 0.0000  0.0000  0.0000  1214 THR A N   
9832  C CA  . THR B 1217 ? 0.5776 0.5776 0.5776 0.0000  0.0000  0.0000  1214 THR A CA  
9833  C C   . THR B 1217 ? 0.5776 0.5776 0.5776 0.0000  0.0000  0.0000  1214 THR A C   
9834  O O   . THR B 1217 ? 0.5776 0.5776 0.5776 0.0000  0.0000  0.0000  1214 THR A O   
9835  C CB  . THR B 1217 ? 0.5776 0.5776 0.5776 0.0000  0.0000  0.0000  1214 THR A CB  
9836  O OG1 . THR B 1217 ? 0.5776 0.5776 0.5776 0.0000  0.0000  0.0000  1214 THR A OG1 
9837  C CG2 . THR B 1217 ? 0.5776 0.5776 0.5776 0.0000  0.0000  0.0000  1214 THR A CG2 
9838  N N   . MET B 1218 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1215 MET A N   
9839  C CA  . MET B 1218 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1215 MET A CA  
9840  C C   . MET B 1218 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1215 MET A C   
9841  O O   . MET B 1218 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1215 MET A O   
9842  C CB  . MET B 1218 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1215 MET A CB  
9843  C CG  . MET B 1218 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1215 MET A CG  
9844  S SD  . MET B 1218 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1215 MET A SD  
9845  C CE  . MET B 1218 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1215 MET A CE  
9846  N N   . VAL B 1219 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1216 VAL A N   
9847  C CA  . VAL B 1219 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1216 VAL A CA  
9848  C C   . VAL B 1219 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1216 VAL A C   
9849  O O   . VAL B 1219 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1216 VAL A O   
9850  C CB  . VAL B 1219 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1216 VAL A CB  
9851  C CG1 . VAL B 1219 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1216 VAL A CG1 
9852  C CG2 . VAL B 1219 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1216 VAL A CG2 
9853  N N   . ALA B 1220 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1217 ALA A N   
9854  C CA  . ALA B 1220 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1217 ALA A CA  
9855  C C   . ALA B 1220 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1217 ALA A C   
9856  O O   . ALA B 1220 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1217 ALA A O   
9857  C CB  . ALA B 1220 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1217 ALA A CB  
9858  N N   . LEU B 1221 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1218 LEU A N   
9859  C CA  . LEU B 1221 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1218 LEU A CA  
9860  C C   . LEU B 1221 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1218 LEU A C   
9861  O O   . LEU B 1221 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1218 LEU A O   
9862  C CB  . LEU B 1221 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1218 LEU A CB  
9863  C CG  . LEU B 1221 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1218 LEU A CG  
9864  C CD1 . LEU B 1221 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1218 LEU A CD1 
9865  C CD2 . LEU B 1221 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1218 LEU A CD2 
9866  N N   . ILE B 1222 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1219 ILE A N   
9867  C CA  . ILE B 1222 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1219 ILE A CA  
9868  C C   . ILE B 1222 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1219 ILE A C   
9869  O O   . ILE B 1222 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1219 ILE A O   
9870  C CB  . ILE B 1222 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1219 ILE A CB  
9871  C CG1 . ILE B 1222 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1219 ILE A CG1 
9872  C CG2 . ILE B 1222 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1219 ILE A CG2 
9873  C CD1 . ILE B 1222 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1219 ILE A CD1 
9874  N N   . ARG B 1223 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1220 ARG A N   
9875  C CA  . ARG B 1223 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1220 ARG A CA  
9876  C C   . ARG B 1223 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1220 ARG A C   
9877  O O   . ARG B 1223 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1220 ARG A O   
9878  C CB  . ARG B 1223 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1220 ARG A CB  
9879  C CG  . ARG B 1223 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1220 ARG A CG  
9880  C CD  . ARG B 1223 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1220 ARG A CD  
9881  N NE  . ARG B 1223 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1220 ARG A NE  
9882  C CZ  . ARG B 1223 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1220 ARG A CZ  
9883  N NH1 . ARG B 1223 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1220 ARG A NH1 
9884  N NH2 . ARG B 1223 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1220 ARG A NH2 
9885  N N   . SER B 1224 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1221 SER A N   
9886  C CA  . SER B 1224 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1221 SER A CA  
9887  C C   . SER B 1224 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1221 SER A C   
9888  O O   . SER B 1224 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1221 SER A O   
9889  C CB  . SER B 1224 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1221 SER A CB  
9890  O OG  . SER B 1224 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1221 SER A OG  
9891  N N   . VAL B 1225 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1222 VAL A N   
9892  C CA  . VAL B 1225 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1222 VAL A CA  
9893  C C   . VAL B 1225 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1222 VAL A C   
9894  O O   . VAL B 1225 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1222 VAL A O   
9895  C CB  . VAL B 1225 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1222 VAL A CB  
9896  C CG1 . VAL B 1225 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1222 VAL A CG1 
9897  C CG2 . VAL B 1225 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1222 VAL A CG2 
9898  N N   . LEU B 1226 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1223 LEU A N   
9899  C CA  . LEU B 1226 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1223 LEU A CA  
9900  C C   . LEU B 1226 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1223 LEU A C   
9901  O O   . LEU B 1226 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1223 LEU A O   
9902  C CB  . LEU B 1226 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1223 LEU A CB  
9903  C CG  . LEU B 1226 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1223 LEU A CG  
9904  C CD1 . LEU B 1226 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1223 LEU A CD1 
9905  C CD2 . LEU B 1226 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1223 LEU A CD2 
9906  N N   . GLN B 1227 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1224 GLN A N   
9907  C CA  . GLN B 1227 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1224 GLN A CA  
9908  C C   . GLN B 1227 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1224 GLN A C   
9909  O O   . GLN B 1227 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1224 GLN A O   
9910  C CB  . GLN B 1227 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1224 GLN A CB  
9911  C CG  . GLN B 1227 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1224 GLN A CG  
9912  C CD  . GLN B 1227 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1224 GLN A CD  
9913  O OE1 . GLN B 1227 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1224 GLN A OE1 
9914  N NE2 . GLN B 1227 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1224 GLN A NE2 
9915  N N   . MET B 1228 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1225 MET A N   
9916  C CA  . MET B 1228 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1225 MET A CA  
9917  C C   . MET B 1228 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1225 MET A C   
9918  O O   . MET B 1228 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1225 MET A O   
9919  C CB  . MET B 1228 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1225 MET A CB  
9920  C CG  . MET B 1228 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1225 MET A CG  
9921  S SD  . MET B 1228 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1225 MET A SD  
9922  C CE  . MET B 1228 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1225 MET A CE  
9923  N N   . ARG B 1229 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1226 ARG A N   
9924  C CA  . ARG B 1229 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1226 ARG A CA  
9925  C C   . ARG B 1229 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1226 ARG A C   
9926  O O   . ARG B 1229 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1226 ARG A O   
9927  C CB  . ARG B 1229 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1226 ARG A CB  
9928  C CG  . ARG B 1229 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1226 ARG A CG  
9929  C CD  . ARG B 1229 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1226 ARG A CD  
9930  N NE  . ARG B 1229 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1226 ARG A NE  
9931  C CZ  . ARG B 1229 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1226 ARG A CZ  
9932  N NH1 . ARG B 1229 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1226 ARG A NH1 
9933  N NH2 . ARG B 1229 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1226 ARG A NH2 
9934  N N   . ASN B 1230 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1227 ASN A N   
9935  C CA  . ASN B 1230 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1227 ASN A CA  
9936  C C   . ASN B 1230 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1227 ASN A C   
9937  O O   . ASN B 1230 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1227 ASN A O   
9938  C CB  . ASN B 1230 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1227 ASN A CB  
9939  C CG  . ASN B 1230 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1227 ASN A CG  
9940  O OD1 . ASN B 1230 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1227 ASN A OD1 
9941  N ND2 . ASN B 1230 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1227 ASN A ND2 
9942  N N   . SER B 1231 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1228 SER A N   
9943  C CA  . SER B 1231 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1228 SER A CA  
9944  C C   . SER B 1231 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1228 SER A C   
9945  O O   . SER B 1231 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1228 SER A O   
9946  C CB  . SER B 1231 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1228 SER A CB  
9947  O OG  . SER B 1231 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1228 SER A OG  
9948  N N   . ASN B 1232 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1229 ASN A N   
9949  C CA  . ASN B 1232 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1229 ASN A CA  
9950  C C   . ASN B 1232 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1229 ASN A C   
9951  O O   . ASN B 1232 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1229 ASN A O   
9952  C CB  . ASN B 1232 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1229 ASN A CB  
9953  C CG  . ASN B 1232 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1229 ASN A CG  
9954  O OD1 . ASN B 1232 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1229 ASN A OD1 
9955  N ND2 . ASN B 1232 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1229 ASN A ND2 
9956  N N   . ALA B 1233 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1230 ALA A N   
9957  C CA  . ALA B 1233 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1230 ALA A CA  
9958  C C   . ALA B 1233 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1230 ALA A C   
9959  O O   . ALA B 1233 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1230 ALA A O   
9960  C CB  . ALA B 1233 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1230 ALA A CB  
9961  N N   . ALA B 1234 ? 0.5902 0.5902 0.5902 0.0000  0.0000  0.0000  1231 ALA A N   
9962  C CA  . ALA B 1234 ? 0.5902 0.5902 0.5902 0.0000  0.0000  0.0000  1231 ALA A CA  
9963  C C   . ALA B 1234 ? 0.5902 0.5902 0.5902 0.0000  0.0000  0.0000  1231 ALA A C   
9964  O O   . ALA B 1234 ? 0.5902 0.5902 0.5902 0.0000  0.0000  0.0000  1231 ALA A O   
9965  C CB  . ALA B 1234 ? 0.5902 0.5902 0.5902 0.0000  0.0000  0.0000  1231 ALA A CB  
9966  N N   . THR B 1235 ? 0.5685 0.5685 0.5685 0.0000  0.0000  0.0000  1232 THR A N   
9967  C CA  . THR B 1235 ? 0.5685 0.5685 0.5685 0.0000  0.0000  0.0000  1232 THR A CA  
9968  C C   . THR B 1235 ? 0.5685 0.5685 0.5685 0.0000  0.0000  0.0000  1232 THR A C   
9969  O O   . THR B 1235 ? 0.5685 0.5685 0.5685 0.0000  0.0000  0.0000  1232 THR A O   
9970  C CB  . THR B 1235 ? 0.5685 0.5685 0.5685 0.0000  0.0000  0.0000  1232 THR A CB  
9971  O OG1 . THR B 1235 ? 0.5685 0.5685 0.5685 0.0000  0.0000  0.0000  1232 THR A OG1 
9972  C CG2 . THR B 1235 ? 0.5685 0.5685 0.5685 0.0000  0.0000  0.0000  1232 THR A CG2 
9973  N N   . GLY B 1236 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1233 GLY A N   
9974  C CA  . GLY B 1236 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1233 GLY A CA  
9975  C C   . GLY B 1236 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1233 GLY A C   
9976  O O   . GLY B 1236 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1233 GLY A O   
9977  N N   . GLU B 1237 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1234 GLU A N   
9978  C CA  . GLU B 1237 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1234 GLU A CA  
9979  C C   . GLU B 1237 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1234 GLU A C   
9980  O O   . GLU B 1237 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1234 GLU A O   
9981  C CB  . GLU B 1237 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1234 GLU A CB  
9982  C CG  . GLU B 1237 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1234 GLU A CG  
9983  C CD  . GLU B 1237 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1234 GLU A CD  
9984  O OE1 . GLU B 1237 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1234 GLU A OE1 
9985  O OE2 . GLU B 1237 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1234 GLU A OE2 
9986  N N   . ASP B 1238 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1235 ASP A N   
9987  C CA  . ASP B 1238 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1235 ASP A CA  
9988  C C   . ASP B 1238 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1235 ASP A C   
9989  O O   . ASP B 1238 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1235 ASP A O   
9990  C CB  . ASP B 1238 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1235 ASP A CB  
9991  C CG  . ASP B 1238 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1235 ASP A CG  
9992  O OD1 . ASP B 1238 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1235 ASP A OD1 
9993  O OD2 . ASP B 1238 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1235 ASP A OD2 
9994  N N   . TYR B 1239 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1236 TYR A N   
9995  C CA  . TYR B 1239 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1236 TYR A CA  
9996  C C   . TYR B 1239 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1236 TYR A C   
9997  O O   . TYR B 1239 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1236 TYR A O   
9998  C CB  . TYR B 1239 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1236 TYR A CB  
9999  C CG  . TYR B 1239 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1236 TYR A CG  
10000 C CD1 . TYR B 1239 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1236 TYR A CD1 
10001 C CD2 . TYR B 1239 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1236 TYR A CD2 
10002 C CE1 . TYR B 1239 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1236 TYR A CE1 
10003 C CE2 . TYR B 1239 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1236 TYR A CE2 
10004 C CZ  . TYR B 1239 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1236 TYR A CZ  
10005 O OH  . TYR B 1239 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1236 TYR A OH  
10006 N N   . ILE B 1240 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1237 ILE A N   
10007 C CA  . ILE B 1240 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1237 ILE A CA  
10008 C C   . ILE B 1240 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1237 ILE A C   
10009 O O   . ILE B 1240 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1237 ILE A O   
10010 C CB  . ILE B 1240 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1237 ILE A CB  
10011 C CG1 . ILE B 1240 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1237 ILE A CG1 
10012 C CG2 . ILE B 1240 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1237 ILE A CG2 
10013 C CD1 . ILE B 1240 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1237 ILE A CD1 
10014 N N   . ASN B 1241 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1238 ASN A N   
10015 C CA  . ASN B 1241 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1238 ASN A CA  
10016 C C   . ASN B 1241 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1238 ASN A C   
10017 O O   . ASN B 1241 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1238 ASN A O   
10018 C CB  . ASN B 1241 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1238 ASN A CB  
10019 C CG  . ASN B 1241 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1238 ASN A CG  
10020 O OD1 . ASN B 1241 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1238 ASN A OD1 
10021 N ND2 . ASN B 1241 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1238 ASN A ND2 
10022 N N   . SER B 1242 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1239 SER A N   
10023 C CA  . SER B 1242 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1239 SER A CA  
10024 C C   . SER B 1242 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1239 SER A C   
10025 O O   . SER B 1242 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1239 SER A O   
10026 C CB  . SER B 1242 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1239 SER A CB  
10027 O OG  . SER B 1242 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1239 SER A OG  
10028 N N   . PRO B 1243 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1240 PRO A N   
10029 C CA  . PRO B 1243 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1240 PRO A CA  
10030 C C   . PRO B 1243 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1240 PRO A C   
10031 O O   . PRO B 1243 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1240 PRO A O   
10032 C CB  . PRO B 1243 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1240 PRO A CB  
10033 C CG  . PRO B 1243 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1240 PRO A CG  
10034 C CD  . PRO B 1243 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1240 PRO A CD  
10035 N N   . VAL B 1244 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1241 VAL A N   
10036 C CA  . VAL B 1244 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1241 VAL A CA  
10037 C C   . VAL B 1244 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1241 VAL A C   
10038 O O   . VAL B 1244 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1241 VAL A O   
10039 C CB  . VAL B 1244 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1241 VAL A CB  
10040 C CG1 . VAL B 1244 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1241 VAL A CG1 
10041 C CG2 . VAL B 1244 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1241 VAL A CG2 
10042 N N   . ARG B 1245 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1242 ARG A N   
10043 C CA  . ARG B 1245 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1242 ARG A CA  
10044 C C   . ARG B 1245 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1242 ARG A C   
10045 O O   . ARG B 1245 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1242 ARG A O   
10046 C CB  . ARG B 1245 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1242 ARG A CB  
10047 C CG  . ARG B 1245 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1242 ARG A CG  
10048 C CD  . ARG B 1245 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1242 ARG A CD  
10049 N NE  . ARG B 1245 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1242 ARG A NE  
10050 C CZ  . ARG B 1245 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1242 ARG A CZ  
10051 N NH1 . ARG B 1245 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1242 ARG A NH1 
10052 N NH2 . ARG B 1245 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1242 ARG A NH2 
10053 N N   . ASP B 1246 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1243 ASP A N   
10054 C CA  . ASP B 1246 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1243 ASP A CA  
10055 C C   . ASP B 1246 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1243 ASP A C   
10056 O O   . ASP B 1246 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1243 ASP A O   
10057 C CB  . ASP B 1246 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1243 ASP A CB  
10058 C CG  . ASP B 1246 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1243 ASP A CG  
10059 O OD1 . ASP B 1246 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1243 ASP A OD1 
10060 O OD2 . ASP B 1246 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1243 ASP A OD2 
10061 N N   . LEU B 1247 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1244 LEU A N   
10062 C CA  . LEU B 1247 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1244 LEU A CA  
10063 C C   . LEU B 1247 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1244 LEU A C   
10064 O O   . LEU B 1247 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1244 LEU A O   
10065 C CB  . LEU B 1247 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1244 LEU A CB  
10066 C CG  . LEU B 1247 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1244 LEU A CG  
10067 C CD1 . LEU B 1247 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1244 LEU A CD1 
10068 C CD2 . LEU B 1247 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1244 LEU A CD2 
10069 N N   . ASN B 1248 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1245 ASN A N   
10070 C CA  . ASN B 1248 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1245 ASN A CA  
10071 C C   . ASN B 1248 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1245 ASN A C   
10072 O O   . ASN B 1248 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1245 ASN A O   
10073 C CB  . ASN B 1248 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1245 ASN A CB  
10074 C CG  . ASN B 1248 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1245 ASN A CG  
10075 O OD1 . ASN B 1248 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1245 ASN A OD1 
10076 N ND2 . ASN B 1248 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1245 ASN A ND2 
10077 N N   . GLY B 1249 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1246 GLY A N   
10078 C CA  . GLY B 1249 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1246 GLY A CA  
10079 C C   . GLY B 1249 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1246 GLY A C   
10080 O O   . GLY B 1249 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1246 GLY A O   
10081 N N   . VAL B 1250 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1247 VAL A N   
10082 C CA  . VAL B 1250 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1247 VAL A CA  
10083 C C   . VAL B 1250 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1247 VAL A C   
10084 O O   . VAL B 1250 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1247 VAL A O   
10085 C CB  . VAL B 1250 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1247 VAL A CB  
10086 C CG1 . VAL B 1250 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1247 VAL A CG1 
10087 C CG2 . VAL B 1250 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1247 VAL A CG2 
10088 N N   . CYS B 1251 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1248 CYS A N   
10089 C CA  . CYS B 1251 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1248 CYS A CA  
10090 C C   . CYS B 1251 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1248 CYS A C   
10091 O O   . CYS B 1251 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1248 CYS A O   
10092 C CB  . CYS B 1251 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1248 CYS A CB  
10093 S SG  . CYS B 1251 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1248 CYS A SG  
10094 N N   . PHE B 1252 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1249 PHE A N   
10095 C CA  . PHE B 1252 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1249 PHE A CA  
10096 C C   . PHE B 1252 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1249 PHE A C   
10097 O O   . PHE B 1252 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1249 PHE A O   
10098 C CB  . PHE B 1252 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1249 PHE A CB  
10099 C CG  . PHE B 1252 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1249 PHE A CG  
10100 C CD1 . PHE B 1252 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1249 PHE A CD1 
10101 C CD2 . PHE B 1252 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1249 PHE A CD2 
10102 C CE1 . PHE B 1252 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1249 PHE A CE1 
10103 C CE2 . PHE B 1252 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1249 PHE A CE2 
10104 C CZ  . PHE B 1252 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1249 PHE A CZ  
10105 N N   . ASP B 1253 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1250 ASP A N   
10106 C CA  . ASP B 1253 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1250 ASP A CA  
10107 C C   . ASP B 1253 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1250 ASP A C   
10108 O O   . ASP B 1253 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1250 ASP A O   
10109 C CB  . ASP B 1253 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1250 ASP A CB  
10110 C CG  . ASP B 1253 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1250 ASP A CG  
10111 O OD1 . ASP B 1253 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1250 ASP A OD1 
10112 O OD2 . ASP B 1253 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1250 ASP A OD2 
10113 N N   . SER B 1254 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1251 SER A N   
10114 C CA  . SER B 1254 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1251 SER A CA  
10115 C C   . SER B 1254 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1251 SER A C   
10116 O O   . SER B 1254 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1251 SER A O   
10117 C CB  . SER B 1254 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1251 SER A CB  
10118 O OG  . SER B 1254 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1251 SER A OG  
10119 N N   . ARG B 1255 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1252 ARG A N   
10120 C CA  . ARG B 1255 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1252 ARG A CA  
10121 C C   . ARG B 1255 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1252 ARG A C   
10122 O O   . ARG B 1255 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1252 ARG A O   
10123 C CB  . ARG B 1255 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1252 ARG A CB  
10124 C CG  . ARG B 1255 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1252 ARG A CG  
10125 C CD  . ARG B 1255 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1252 ARG A CD  
10126 N NE  . ARG B 1255 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1252 ARG A NE  
10127 C CZ  . ARG B 1255 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1252 ARG A CZ  
10128 N NH1 . ARG B 1255 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1252 ARG A NH1 
10129 N NH2 . ARG B 1255 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1252 ARG A NH2 
10130 N N   . PHE B 1256 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1253 PHE A N   
10131 C CA  . PHE B 1256 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1253 PHE A CA  
10132 C C   . PHE B 1256 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1253 PHE A C   
10133 O O   . PHE B 1256 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1253 PHE A O   
10134 C CB  . PHE B 1256 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1253 PHE A CB  
10135 C CG  . PHE B 1256 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1253 PHE A CG  
10136 C CD1 . PHE B 1256 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1253 PHE A CD1 
10137 C CD2 . PHE B 1256 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1253 PHE A CD2 
10138 C CE1 . PHE B 1256 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1253 PHE A CE1 
10139 C CE2 . PHE B 1256 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1253 PHE A CE2 
10140 C CZ  . PHE B 1256 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1253 PHE A CZ  
10141 N N   . GLN B 1257 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1254 GLN A N   
10142 C CA  . GLN B 1257 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1254 GLN A CA  
10143 C C   . GLN B 1257 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1254 GLN A C   
10144 O O   . GLN B 1257 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1254 GLN A O   
10145 C CB  . GLN B 1257 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1254 GLN A CB  
10146 C CG  . GLN B 1257 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1254 GLN A CG  
10147 C CD  . GLN B 1257 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1254 GLN A CD  
10148 O OE1 . GLN B 1257 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1254 GLN A OE1 
10149 N NE2 . GLN B 1257 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1254 GLN A NE2 
10150 N N   . ASN B 1258 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1255 ASN A N   
10151 C CA  . ASN B 1258 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1255 ASN A CA  
10152 C C   . ASN B 1258 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1255 ASN A C   
10153 O O   . ASN B 1258 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1255 ASN A O   
10154 C CB  . ASN B 1258 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1255 ASN A CB  
10155 C CG  . ASN B 1258 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1255 ASN A CG  
10156 O OD1 . ASN B 1258 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1255 ASN A OD1 
10157 N ND2 . ASN B 1258 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1255 ASN A ND2 
10158 N N   . PRO B 1259 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1256 PRO A N   
10159 C CA  . PRO B 1259 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1256 PRO A CA  
10160 C C   . PRO B 1259 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1256 PRO A C   
10161 O O   . PRO B 1259 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1256 PRO A O   
10162 C CB  . PRO B 1259 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1256 PRO A CB  
10163 C CG  . PRO B 1259 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1256 PRO A CG  
10164 C CD  . PRO B 1259 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1256 PRO A CD  
10165 N N   . GLU B 1260 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1257 GLU A N   
10166 C CA  . GLU B 1260 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1257 GLU A CA  
10167 C C   . GLU B 1260 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1257 GLU A C   
10168 O O   . GLU B 1260 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1257 GLU A O   
10169 C CB  . GLU B 1260 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1257 GLU A CB  
10170 C CG  . GLU B 1260 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1257 GLU A CG  
10171 C CD  . GLU B 1260 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1257 GLU A CD  
10172 O OE1 . GLU B 1260 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1257 GLU A OE1 
10173 O OE2 . GLU B 1260 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1257 GLU A OE2 
10174 N N   . TRP B 1261 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1258 TRP A N   
10175 C CA  . TRP B 1261 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1258 TRP A CA  
10176 C C   . TRP B 1261 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1258 TRP A C   
10177 O O   . TRP B 1261 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1258 TRP A O   
10178 C CB  . TRP B 1261 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1258 TRP A CB  
10179 C CG  . TRP B 1261 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1258 TRP A CG  
10180 C CD1 . TRP B 1261 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1258 TRP A CD1 
10181 C CD2 . TRP B 1261 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1258 TRP A CD2 
10182 N NE1 . TRP B 1261 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1258 TRP A NE1 
10183 C CE2 . TRP B 1261 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1258 TRP A CE2 
10184 C CE3 . TRP B 1261 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1258 TRP A CE3 
10185 C CZ2 . TRP B 1261 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1258 TRP A CZ2 
10186 C CZ3 . TRP B 1261 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1258 TRP A CZ3 
10187 C CH2 . TRP B 1261 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1258 TRP A CH2 
10188 N N   . PRO B 1262 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1259 PRO A N   
10189 C CA  . PRO B 1262 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1259 PRO A CA  
10190 C C   . PRO B 1262 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1259 PRO A C   
10191 O O   . PRO B 1262 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1259 PRO A O   
10192 C CB  . PRO B 1262 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1259 PRO A CB  
10193 C CG  . PRO B 1262 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1259 PRO A CG  
10194 C CD  . PRO B 1262 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1259 PRO A CD  
10195 N N   . MET B 1263 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1260 MET A N   
10196 C CA  . MET B 1263 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1260 MET A CA  
10197 C C   . MET B 1263 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1260 MET A C   
10198 O O   . MET B 1263 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1260 MET A O   
10199 C CB  . MET B 1263 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1260 MET A CB  
10200 C CG  . MET B 1263 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1260 MET A CG  
10201 S SD  . MET B 1263 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1260 MET A SD  
10202 C CE  . MET B 1263 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1260 MET A CE  
10203 N N   . ASP B 1264 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1261 ASP A N   
10204 C CA  . ASP B 1264 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1261 ASP A CA  
10205 C C   . ASP B 1264 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1261 ASP A C   
10206 O O   . ASP B 1264 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1261 ASP A O   
10207 C CB  . ASP B 1264 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1261 ASP A CB  
10208 C CG  . ASP B 1264 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1261 ASP A CG  
10209 O OD1 . ASP B 1264 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1261 ASP A OD1 
10210 O OD2 . ASP B 1264 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1261 ASP A OD2 
10211 N N   . ALA B 1265 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1262 ALA A N   
10212 C CA  . ALA B 1265 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1262 ALA A CA  
10213 C C   . ALA B 1265 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1262 ALA A C   
10214 O O   . ALA B 1265 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1262 ALA A O   
10215 C CB  . ALA B 1265 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1262 ALA A CB  
10216 N N   . ASP B 1266 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1263 ASP A N   
10217 C CA  . ASP B 1266 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1263 ASP A CA  
10218 C C   . ASP B 1266 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1263 ASP A C   
10219 O O   . ASP B 1266 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1263 ASP A O   
10220 C CB  . ASP B 1266 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1263 ASP A CB  
10221 C CG  . ASP B 1266 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1263 ASP A CG  
10222 O OD1 . ASP B 1266 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1263 ASP A OD1 
10223 O OD2 . ASP B 1266 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1263 ASP A OD2 
10224 N N   . ALA B 1267 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1264 ALA A N   
10225 C CA  . ALA B 1267 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1264 ALA A CA  
10226 C C   . ALA B 1267 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1264 ALA A C   
10227 O O   . ALA B 1267 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1264 ALA A O   
10228 C CB  . ALA B 1267 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1264 ALA A CB  
10229 N N   . ASN B 1268 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1265 ASN A N   
10230 C CA  . ASN B 1268 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1265 ASN A CA  
10231 C C   . ASN B 1268 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1265 ASN A C   
10232 O O   . ASN B 1268 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1265 ASN A O   
10233 C CB  . ASN B 1268 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1265 ASN A CB  
10234 C CG  . ASN B 1268 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1265 ASN A CG  
10235 O OD1 . ASN B 1268 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1265 ASN A OD1 
10236 N ND2 . ASN B 1268 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1265 ASN A ND2 
10237 N N   . GLY B 1269 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1266 GLY A N   
10238 C CA  . GLY B 1269 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1266 GLY A CA  
10239 C C   . GLY B 1269 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1266 GLY A C   
10240 O O   . GLY B 1269 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1266 GLY A O   
10241 N N   . ALA B 1270 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1267 ALA A N   
10242 C CA  . ALA B 1270 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1267 ALA A CA  
10243 C C   . ALA B 1270 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1267 ALA A C   
10244 O O   . ALA B 1270 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1267 ALA A O   
10245 C CB  . ALA B 1270 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1267 ALA A CB  
10246 N N   . TYR B 1271 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1268 TYR A N   
10247 C CA  . TYR B 1271 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1268 TYR A CA  
10248 C C   . TYR B 1271 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1268 TYR A C   
10249 O O   . TYR B 1271 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1268 TYR A O   
10250 C CB  . TYR B 1271 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1268 TYR A CB  
10251 C CG  . TYR B 1271 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1268 TYR A CG  
10252 C CD1 . TYR B 1271 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1268 TYR A CD1 
10253 C CD2 . TYR B 1271 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1268 TYR A CD2 
10254 C CE1 . TYR B 1271 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1268 TYR A CE1 
10255 C CE2 . TYR B 1271 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1268 TYR A CE2 
10256 C CZ  . TYR B 1271 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1268 TYR A CZ  
10257 O OH  . TYR B 1271 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1268 TYR A OH  
10258 N N   . HIS B 1272 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1269 HIS A N   
10259 C CA  . HIS B 1272 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1269 HIS A CA  
10260 C C   . HIS B 1272 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1269 HIS A C   
10261 O O   . HIS B 1272 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1269 HIS A O   
10262 C CB  . HIS B 1272 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1269 HIS A CB  
10263 C CG  . HIS B 1272 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1269 HIS A CG  
10264 N ND1 . HIS B 1272 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1269 HIS A ND1 
10265 C CD2 . HIS B 1272 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1269 HIS A CD2 
10266 C CE1 . HIS B 1272 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1269 HIS A CE1 
10267 N NE2 . HIS B 1272 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1269 HIS A NE2 
10268 N N   . ILE B 1273 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1270 ILE A N   
10269 C CA  . ILE B 1273 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1270 ILE A CA  
10270 C C   . ILE B 1273 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1270 ILE A C   
10271 O O   . ILE B 1273 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1270 ILE A O   
10272 C CB  . ILE B 1273 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1270 ILE A CB  
10273 C CG1 . ILE B 1273 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1270 ILE A CG1 
10274 C CG2 . ILE B 1273 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1270 ILE A CG2 
10275 C CD1 . ILE B 1273 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1270 ILE A CD1 
10276 N N   . ALA B 1274 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1271 ALA A N   
10277 C CA  . ALA B 1274 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1271 ALA A CA  
10278 C C   . ALA B 1274 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1271 ALA A C   
10279 O O   . ALA B 1274 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1271 ALA A O   
10280 C CB  . ALA B 1274 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1271 ALA A CB  
10281 N N   . LEU B 1275 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1272 LEU A N   
10282 C CA  . LEU B 1275 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1272 LEU A CA  
10283 C C   . LEU B 1275 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1272 LEU A C   
10284 O O   . LEU B 1275 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1272 LEU A O   
10285 C CB  . LEU B 1275 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1272 LEU A CB  
10286 C CG  . LEU B 1275 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1272 LEU A CG  
10287 C CD1 . LEU B 1275 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1272 LEU A CD1 
10288 C CD2 . LEU B 1275 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1272 LEU A CD2 
10289 N N   . LYS B 1276 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1273 LYS A N   
10290 C CA  . LYS B 1276 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1273 LYS A CA  
10291 C C   . LYS B 1276 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1273 LYS A C   
10292 O O   . LYS B 1276 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1273 LYS A O   
10293 C CB  . LYS B 1276 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1273 LYS A CB  
10294 C CG  . LYS B 1276 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1273 LYS A CG  
10295 C CD  . LYS B 1276 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1273 LYS A CD  
10296 C CE  . LYS B 1276 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1273 LYS A CE  
10297 N NZ  . LYS B 1276 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1273 LYS A NZ  
10298 N N   . GLY B 1277 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1274 GLY A N   
10299 C CA  . GLY B 1277 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1274 GLY A CA  
10300 C C   . GLY B 1277 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1274 GLY A C   
10301 O O   . GLY B 1277 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1274 GLY A O   
10302 N N   . GLN B 1278 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1275 GLN A N   
10303 C CA  . GLN B 1278 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1275 GLN A CA  
10304 C C   . GLN B 1278 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1275 GLN A C   
10305 O O   . GLN B 1278 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1275 GLN A O   
10306 C CB  . GLN B 1278 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1275 GLN A CB  
10307 C CG  . GLN B 1278 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1275 GLN A CG  
10308 C CD  . GLN B 1278 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1275 GLN A CD  
10309 O OE1 . GLN B 1278 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1275 GLN A OE1 
10310 N NE2 . GLN B 1278 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1275 GLN A NE2 
10311 N N   . LEU B 1279 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1276 LEU A N   
10312 C CA  . LEU B 1279 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1276 LEU A CA  
10313 C C   . LEU B 1279 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1276 LEU A C   
10314 O O   . LEU B 1279 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1276 LEU A O   
10315 C CB  . LEU B 1279 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1276 LEU A CB  
10316 C CG  . LEU B 1279 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1276 LEU A CG  
10317 C CD1 . LEU B 1279 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1276 LEU A CD1 
10318 C CD2 . LEU B 1279 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1276 LEU A CD2 
10319 N N   . LEU B 1280 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1277 LEU A N   
10320 C CA  . LEU B 1280 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1277 LEU A CA  
10321 C C   . LEU B 1280 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1277 LEU A C   
10322 O O   . LEU B 1280 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1277 LEU A O   
10323 C CB  . LEU B 1280 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1277 LEU A CB  
10324 C CG  . LEU B 1280 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1277 LEU A CG  
10325 C CD1 . LEU B 1280 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1277 LEU A CD1 
10326 C CD2 . LEU B 1280 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1277 LEU A CD2 
10327 N N   . LEU B 1281 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1278 LEU A N   
10328 C CA  . LEU B 1281 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1278 LEU A CA  
10329 C C   . LEU B 1281 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1278 LEU A C   
10330 O O   . LEU B 1281 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1278 LEU A O   
10331 C CB  . LEU B 1281 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1278 LEU A CB  
10332 C CG  . LEU B 1281 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1278 LEU A CG  
10333 C CD1 . LEU B 1281 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1278 LEU A CD1 
10334 C CD2 . LEU B 1281 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1278 LEU A CD2 
10335 N N   . ASN B 1282 ? 0.6273 0.6273 0.6273 0.0000  0.0000  0.0000  1279 ASN A N   
10336 C CA  . ASN B 1282 ? 0.6273 0.6273 0.6273 0.0000  0.0000  0.0000  1279 ASN A CA  
10337 C C   . ASN B 1282 ? 0.6273 0.6273 0.6273 0.0000  0.0000  0.0000  1279 ASN A C   
10338 O O   . ASN B 1282 ? 0.6273 0.6273 0.6273 0.0000  0.0000  0.0000  1279 ASN A O   
10339 C CB  . ASN B 1282 ? 0.6273 0.6273 0.6273 0.0000  0.0000  0.0000  1279 ASN A CB  
10340 C CG  . ASN B 1282 ? 0.6273 0.6273 0.6273 0.0000  0.0000  0.0000  1279 ASN A CG  
10341 O OD1 . ASN B 1282 ? 0.6273 0.6273 0.6273 0.0000  0.0000  0.0000  1279 ASN A OD1 
10342 N ND2 . ASN B 1282 ? 0.6273 0.6273 0.6273 0.0000  0.0000  0.0000  1279 ASN A ND2 
10343 N N   . HIS B 1283 ? 0.6921 0.6921 0.6921 0.0000  0.0000  0.0000  1280 HIS A N   
10344 C CA  . HIS B 1283 ? 0.6921 0.6921 0.6921 0.0000  0.0000  0.0000  1280 HIS A CA  
10345 C C   . HIS B 1283 ? 0.6921 0.6921 0.6921 0.0000  0.0000  0.0000  1280 HIS A C   
10346 O O   . HIS B 1283 ? 0.6921 0.6921 0.6921 0.0000  0.0000  0.0000  1280 HIS A O   
10347 C CB  . HIS B 1283 ? 0.6921 0.6921 0.6921 0.0000  0.0000  0.0000  1280 HIS A CB  
10348 C CG  . HIS B 1283 ? 0.6921 0.6921 0.6921 0.0000  0.0000  0.0000  1280 HIS A CG  
10349 N ND1 . HIS B 1283 ? 0.6921 0.6921 0.6921 0.0000  0.0000  0.0000  1280 HIS A ND1 
10350 C CD2 . HIS B 1283 ? 0.6921 0.6921 0.6921 0.0000  0.0000  0.0000  1280 HIS A CD2 
10351 C CE1 . HIS B 1283 ? 0.6921 0.6921 0.6921 0.0000  0.0000  0.0000  1280 HIS A CE1 
10352 N NE2 . HIS B 1283 ? 0.6921 0.6921 0.6921 0.0000  0.0000  0.0000  1280 HIS A NE2 
10353 N N   . LEU B 1284 ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  1281 LEU A N   
10354 C CA  . LEU B 1284 ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  1281 LEU A CA  
10355 C C   . LEU B 1284 ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  1281 LEU A C   
10356 O O   . LEU B 1284 ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  1281 LEU A O   
10357 C CB  . LEU B 1284 ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  1281 LEU A CB  
10358 C CG  . LEU B 1284 ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  1281 LEU A CG  
10359 C CD1 . LEU B 1284 ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  1281 LEU A CD1 
10360 C CD2 . LEU B 1284 ? 0.6797 0.6797 0.6797 0.0000  0.0000  0.0000  1281 LEU A CD2 
10361 N N   . LYS B 1285 ? 0.6994 0.6994 0.6994 0.0000  0.0000  0.0000  1282 LYS A N   
10362 C CA  . LYS B 1285 ? 0.6994 0.6994 0.6994 0.0000  0.0000  0.0000  1282 LYS A CA  
10363 C C   . LYS B 1285 ? 0.6994 0.6994 0.6994 0.0000  0.0000  0.0000  1282 LYS A C   
10364 O O   . LYS B 1285 ? 0.6994 0.6994 0.6994 0.0000  0.0000  0.0000  1282 LYS A O   
10365 C CB  . LYS B 1285 ? 0.6994 0.6994 0.6994 0.0000  0.0000  0.0000  1282 LYS A CB  
10366 C CG  . LYS B 1285 ? 0.6994 0.6994 0.6994 0.0000  0.0000  0.0000  1282 LYS A CG  
10367 C CD  . LYS B 1285 ? 0.6994 0.6994 0.6994 0.0000  0.0000  0.0000  1282 LYS A CD  
10368 C CE  . LYS B 1285 ? 0.6994 0.6994 0.6994 0.0000  0.0000  0.0000  1282 LYS A CE  
10369 N NZ  . LYS B 1285 ? 0.6994 0.6994 0.6994 0.0000  0.0000  0.0000  1282 LYS A NZ  
10370 N N   . GLU B 1286 ? 0.7888 0.7888 0.7888 0.0000  0.0000  0.0000  1283 GLU A N   
10371 C CA  . GLU B 1286 ? 0.7888 0.7888 0.7888 0.0000  0.0000  0.0000  1283 GLU A CA  
10372 C C   . GLU B 1286 ? 0.7888 0.7888 0.7888 0.0000  0.0000  0.0000  1283 GLU A C   
10373 O O   . GLU B 1286 ? 0.7888 0.7888 0.7888 0.0000  0.0000  0.0000  1283 GLU A O   
10374 C CB  . GLU B 1286 ? 0.7888 0.7888 0.7888 0.0000  0.0000  0.0000  1283 GLU A CB  
10375 C CG  . GLU B 1286 ? 0.7888 0.7888 0.7888 0.0000  0.0000  0.0000  1283 GLU A CG  
10376 C CD  . GLU B 1286 ? 0.7888 0.7888 0.7888 0.0000  0.0000  0.0000  1283 GLU A CD  
10377 O OE1 . GLU B 1286 ? 0.7888 0.7888 0.7888 0.0000  0.0000  0.0000  1283 GLU A OE1 
10378 O OE2 . GLU B 1286 ? 0.7888 0.7888 0.7888 0.0000  0.0000  0.0000  1283 GLU A OE2 
10379 N N   . SER B 1287 ? 0.8192 0.8192 0.8192 0.0000  0.0000  0.0000  1284 SER A N   
10380 C CA  . SER B 1287 ? 0.8192 0.8192 0.8192 0.0000  0.0000  0.0000  1284 SER A CA  
10381 C C   . SER B 1287 ? 0.8192 0.8192 0.8192 0.0000  0.0000  0.0000  1284 SER A C   
10382 O O   . SER B 1287 ? 0.8192 0.8192 0.8192 0.0000  0.0000  0.0000  1284 SER A O   
10383 C CB  . SER B 1287 ? 0.8192 0.8192 0.8192 0.0000  0.0000  0.0000  1284 SER A CB  
10384 O OG  . SER B 1287 ? 0.8192 0.8192 0.8192 0.0000  0.0000  0.0000  1284 SER A OG  
10385 N N   . LYS B 1288 ? 1.0036 1.0036 1.0036 0.0000  0.0000  0.0000  1285 LYS A N   
10386 C CA  . LYS B 1288 ? 1.0036 1.0036 1.0036 0.0000  0.0000  0.0000  1285 LYS A CA  
10387 C C   . LYS B 1288 ? 1.0036 1.0036 1.0036 0.0000  0.0000  0.0000  1285 LYS A C   
10388 O O   . LYS B 1288 ? 1.0036 1.0036 1.0036 0.0000  0.0000  0.0000  1285 LYS A O   
10394 N N   . ASP B 1289 ? 1.0678 1.0678 1.0678 0.0000  0.0000  0.0000  1286 ASP A N   
10395 C CA  . ASP B 1289 ? 1.0678 1.0678 1.0678 0.0000  0.0000  0.0000  1286 ASP A CA  
10396 C C   . ASP B 1289 ? 1.0678 1.0678 1.0678 0.0000  0.0000  0.0000  1286 ASP A C   
10397 O O   . ASP B 1289 ? 1.0678 1.0678 1.0678 0.0000  0.0000  0.0000  1286 ASP A O   
10398 C CB  . ASP B 1289 ? 1.0678 1.0678 1.0678 0.0000  0.0000  0.0000  1286 ASP A CB  
10399 C CG  . ASP B 1289 ? 1.0678 1.0678 1.0678 0.0000  0.0000  0.0000  1286 ASP A CG  
10400 O OD1 . ASP B 1289 ? 1.0678 1.0678 1.0678 0.0000  0.0000  0.0000  1286 ASP A OD1 
10401 O OD2 . ASP B 1289 ? 1.0678 1.0678 1.0678 0.0000  0.0000  0.0000  1286 ASP A OD2 
10402 N N   . LEU B 1290 ? 0.9701 0.9701 0.9701 0.0000  0.0000  0.0000  1287 LEU A N   
10403 C CA  . LEU B 1290 ? 0.9701 0.9701 0.9701 0.0000  0.0000  0.0000  1287 LEU A CA  
10404 C C   . LEU B 1290 ? 0.9701 0.9701 0.9701 0.0000  0.0000  0.0000  1287 LEU A C   
10405 O O   . LEU B 1290 ? 0.9701 0.9701 0.9701 0.0000  0.0000  0.0000  1287 LEU A O   
10406 C CB  . LEU B 1290 ? 0.9701 0.9701 0.9701 0.0000  0.0000  0.0000  1287 LEU A CB  
10407 C CG  . LEU B 1290 ? 0.9701 0.9701 0.9701 0.0000  0.0000  0.0000  1287 LEU A CG  
10408 C CD1 . LEU B 1290 ? 0.9701 0.9701 0.9701 0.0000  0.0000  0.0000  1287 LEU A CD1 
10409 C CD2 . LEU B 1290 ? 0.9701 0.9701 0.9701 0.0000  0.0000  0.0000  1287 LEU A CD2 
10410 N N   . LYS B 1291 ? 1.0000 1.0000 1.0000 0.0000  0.0000  0.0000  1288 LYS A N   
10411 C CA  . LYS B 1291 ? 1.0000 1.0000 1.0000 0.0000  0.0000  0.0000  1288 LYS A CA  
10412 C C   . LYS B 1291 ? 1.0000 1.0000 1.0000 0.0000  0.0000  0.0000  1288 LYS A C   
10413 O O   . LYS B 1291 ? 1.0000 1.0000 1.0000 0.0000  0.0000  0.0000  1288 LYS A O   
10414 C CB  . LYS B 1291 ? 1.0000 1.0000 1.0000 0.0000  0.0000  0.0000  1288 LYS A CB  
10415 C CG  . LYS B 1291 ? 1.0000 1.0000 1.0000 0.0000  0.0000  0.0000  1288 LYS A CG  
10416 C CD  . LYS B 1291 ? 1.0000 1.0000 1.0000 0.0000  0.0000  0.0000  1288 LYS A CD  
10417 C CE  . LYS B 1291 ? 1.0000 1.0000 1.0000 0.0000  0.0000  0.0000  1288 LYS A CE  
10418 N NZ  . LYS B 1291 ? 1.0000 1.0000 1.0000 0.0000  0.0000  0.0000  1288 LYS A NZ  
10419 N N   . LEU B 1292 ? 0.8421 0.8421 0.8421 0.0000  0.0000  0.0000  1289 LEU A N   
10420 C CA  . LEU B 1292 ? 0.8421 0.8421 0.8421 0.0000  0.0000  0.0000  1289 LEU A CA  
10421 C C   . LEU B 1292 ? 0.8421 0.8421 0.8421 0.0000  0.0000  0.0000  1289 LEU A C   
10422 O O   . LEU B 1292 ? 0.8421 0.8421 0.8421 0.0000  0.0000  0.0000  1289 LEU A O   
10423 C CB  . LEU B 1292 ? 0.8421 0.8421 0.8421 0.0000  0.0000  0.0000  1289 LEU A CB  
10424 C CG  . LEU B 1292 ? 0.8421 0.8421 0.8421 0.0000  0.0000  0.0000  1289 LEU A CG  
10425 C CD1 . LEU B 1292 ? 0.8421 0.8421 0.8421 0.0000  0.0000  0.0000  1289 LEU A CD1 
10426 C CD2 . LEU B 1292 ? 0.8421 0.8421 0.8421 0.0000  0.0000  0.0000  1289 LEU A CD2 
10427 N N   . GLN B 1293 ? 0.8892 0.8892 0.8892 0.0000  0.0000  0.0000  1290 GLN A N   
10428 C CA  . GLN B 1293 ? 0.8892 0.8892 0.8892 0.0000  0.0000  0.0000  1290 GLN A CA  
10429 C C   . GLN B 1293 ? 0.8892 0.8892 0.8892 0.0000  0.0000  0.0000  1290 GLN A C   
10430 O O   . GLN B 1293 ? 0.8892 0.8892 0.8892 0.0000  0.0000  0.0000  1290 GLN A O   
10431 C CB  . GLN B 1293 ? 0.8892 0.8892 0.8892 0.0000  0.0000  0.0000  1290 GLN A CB  
10432 C CG  . GLN B 1293 ? 0.8892 0.8892 0.8892 0.0000  0.0000  0.0000  1290 GLN A CG  
10433 C CD  . GLN B 1293 ? 0.8892 0.8892 0.8892 0.0000  0.0000  0.0000  1290 GLN A CD  
10434 O OE1 . GLN B 1293 ? 0.8892 0.8892 0.8892 0.0000  0.0000  0.0000  1290 GLN A OE1 
10435 N NE2 . GLN B 1293 ? 0.8892 0.8892 0.8892 0.0000  0.0000  0.0000  1290 GLN A NE2 
10436 N N   . ASN B 1294 ? 0.8570 0.8570 0.8570 0.0000  0.0000  0.0000  1291 ASN A N   
10437 C CA  . ASN B 1294 ? 0.8570 0.8570 0.8570 0.0000  0.0000  0.0000  1291 ASN A CA  
10438 C C   . ASN B 1294 ? 0.8570 0.8570 0.8570 0.0000  0.0000  0.0000  1291 ASN A C   
10439 O O   . ASN B 1294 ? 0.8570 0.8570 0.8570 0.0000  0.0000  0.0000  1291 ASN A O   
10440 C CB  . ASN B 1294 ? 0.8570 0.8570 0.8570 0.0000  0.0000  0.0000  1291 ASN A CB  
10441 C CG  . ASN B 1294 ? 0.8570 0.8570 0.8570 0.0000  0.0000  0.0000  1291 ASN A CG  
10442 O OD1 . ASN B 1294 ? 0.8570 0.8570 0.8570 0.0000  0.0000  0.0000  1291 ASN A OD1 
10443 N ND2 . ASN B 1294 ? 0.8570 0.8570 0.8570 0.0000  0.0000  0.0000  1291 ASN A ND2 
10444 N N   . GLY B 1295 ? 0.7464 0.7464 0.7464 0.0000  0.0000  0.0000  1292 GLY A N   
10445 C CA  . GLY B 1295 ? 0.7464 0.7464 0.7464 0.0000  0.0000  0.0000  1292 GLY A CA  
10446 C C   . GLY B 1295 ? 0.7464 0.7464 0.7464 0.0000  0.0000  0.0000  1292 GLY A C   
10447 O O   . GLY B 1295 ? 0.7464 0.7464 0.7464 0.0000  0.0000  0.0000  1292 GLY A O   
10448 N N   . ILE B 1296 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1293 ILE A N   
10449 C CA  . ILE B 1296 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1293 ILE A CA  
10450 C C   . ILE B 1296 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1293 ILE A C   
10451 O O   . ILE B 1296 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1293 ILE A O   
10452 C CB  . ILE B 1296 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1293 ILE A CB  
10453 C CG1 . ILE B 1296 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1293 ILE A CG1 
10454 C CG2 . ILE B 1296 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1293 ILE A CG2 
10455 C CD1 . ILE B 1296 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1293 ILE A CD1 
10456 N N   . SER B 1297 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1294 SER A N   
10457 C CA  . SER B 1297 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1294 SER A CA  
10458 C C   . SER B 1297 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1294 SER A C   
10459 O O   . SER B 1297 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1294 SER A O   
10460 C CB  . SER B 1297 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1294 SER A CB  
10461 O OG  . SER B 1297 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1294 SER A OG  
10462 N N   . ASN B 1298 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1295 ASN A N   
10463 C CA  . ASN B 1298 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1295 ASN A CA  
10464 C C   . ASN B 1298 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1295 ASN A C   
10465 O O   . ASN B 1298 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1295 ASN A O   
10466 C CB  . ASN B 1298 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1295 ASN A CB  
10467 C CG  . ASN B 1298 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1295 ASN A CG  
10468 O OD1 . ASN B 1298 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1295 ASN A OD1 
10469 N ND2 . ASN B 1298 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1295 ASN A ND2 
10470 N N   . GLN B 1299 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1296 GLN A N   
10471 C CA  . GLN B 1299 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1296 GLN A CA  
10472 C C   . GLN B 1299 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1296 GLN A C   
10473 O O   . GLN B 1299 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1296 GLN A O   
10474 C CB  . GLN B 1299 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1296 GLN A CB  
10475 C CG  . GLN B 1299 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1296 GLN A CG  
10476 C CD  . GLN B 1299 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1296 GLN A CD  
10477 O OE1 . GLN B 1299 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1296 GLN A OE1 
10478 N NE2 . GLN B 1299 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1296 GLN A NE2 
10479 N N   . ASP B 1300 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1297 ASP A N   
10480 C CA  . ASP B 1300 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1297 ASP A CA  
10481 C C   . ASP B 1300 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1297 ASP A C   
10482 O O   . ASP B 1300 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1297 ASP A O   
10483 C CB  . ASP B 1300 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1297 ASP A CB  
10484 C CG  . ASP B 1300 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1297 ASP A CG  
10485 O OD1 . ASP B 1300 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1297 ASP A OD1 
10486 O OD2 . ASP B 1300 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1297 ASP A OD2 
10487 N N   . TRP B 1301 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1298 TRP A N   
10488 C CA  . TRP B 1301 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1298 TRP A CA  
10489 C C   . TRP B 1301 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1298 TRP A C   
10490 O O   . TRP B 1301 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1298 TRP A O   
10491 C CB  . TRP B 1301 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1298 TRP A CB  
10492 C CG  . TRP B 1301 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1298 TRP A CG  
10493 C CD1 . TRP B 1301 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1298 TRP A CD1 
10494 C CD2 . TRP B 1301 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1298 TRP A CD2 
10495 N NE1 . TRP B 1301 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1298 TRP A NE1 
10496 C CE2 . TRP B 1301 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1298 TRP A CE2 
10497 C CE3 . TRP B 1301 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1298 TRP A CE3 
10498 C CZ2 . TRP B 1301 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1298 TRP A CZ2 
10499 C CZ3 . TRP B 1301 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1298 TRP A CZ3 
10500 C CH2 . TRP B 1301 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1298 TRP A CH2 
10501 N N   . LEU B 1302 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1299 LEU A N   
10502 C CA  . LEU B 1302 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1299 LEU A CA  
10503 C C   . LEU B 1302 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1299 LEU A C   
10504 O O   . LEU B 1302 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1299 LEU A O   
10505 C CB  . LEU B 1302 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1299 LEU A CB  
10506 C CG  . LEU B 1302 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1299 LEU A CG  
10507 C CD1 . LEU B 1302 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1299 LEU A CD1 
10508 C CD2 . LEU B 1302 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1299 LEU A CD2 
10509 N N   . ALA B 1303 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1300 ALA A N   
10510 C CA  . ALA B 1303 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1300 ALA A CA  
10511 C C   . ALA B 1303 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1300 ALA A C   
10512 O O   . ALA B 1303 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1300 ALA A O   
10513 C CB  . ALA B 1303 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1300 ALA A CB  
10514 N N   . TYR B 1304 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1301 TYR A N   
10515 C CA  . TYR B 1304 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1301 TYR A CA  
10516 C C   . TYR B 1304 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1301 TYR A C   
10517 O O   . TYR B 1304 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1301 TYR A O   
10518 C CB  . TYR B 1304 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1301 TYR A CB  
10519 C CG  . TYR B 1304 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1301 TYR A CG  
10520 C CD1 . TYR B 1304 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1301 TYR A CD1 
10521 C CD2 . TYR B 1304 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1301 TYR A CD2 
10522 C CE1 . TYR B 1304 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1301 TYR A CE1 
10523 C CE2 . TYR B 1304 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1301 TYR A CE2 
10524 C CZ  . TYR B 1304 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1301 TYR A CZ  
10525 O OH  . TYR B 1304 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1301 TYR A OH  
10526 N N   . ILE B 1305 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1302 ILE A N   
10527 C CA  . ILE B 1305 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1302 ILE A CA  
10528 C C   . ILE B 1305 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1302 ILE A C   
10529 O O   . ILE B 1305 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1302 ILE A O   
10530 C CB  . ILE B 1305 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1302 ILE A CB  
10531 C CG1 . ILE B 1305 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1302 ILE A CG1 
10532 C CG2 . ILE B 1305 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1302 ILE A CG2 
10533 C CD1 . ILE B 1305 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1302 ILE A CD1 
10534 N N   . GLN B 1306 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1303 GLN A N   
10535 C CA  . GLN B 1306 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1303 GLN A CA  
10536 C C   . GLN B 1306 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1303 GLN A C   
10537 O O   . GLN B 1306 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1303 GLN A O   
10538 C CB  . GLN B 1306 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1303 GLN A CB  
10539 C CG  . GLN B 1306 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1303 GLN A CG  
10540 C CD  . GLN B 1306 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1303 GLN A CD  
10541 O OE1 . GLN B 1306 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1303 GLN A OE1 
10542 N NE2 . GLN B 1306 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1303 GLN A NE2 
10543 N N   . GLU B 1307 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1304 GLU A N   
10544 C CA  . GLU B 1307 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1304 GLU A CA  
10545 C C   . GLU B 1307 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1304 GLU A C   
10546 O O   . GLU B 1307 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1304 GLU A O   
10547 C CB  . GLU B 1307 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1304 GLU A CB  
10548 C CG  . GLU B 1307 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1304 GLU A CG  
10549 C CD  . GLU B 1307 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1304 GLU A CD  
10550 O OE1 . GLU B 1307 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1304 GLU A OE1 
10551 O OE2 . GLU B 1307 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1304 GLU A OE2 
10552 N N   . LEU B 1308 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1305 LEU A N   
10553 C CA  . LEU B 1308 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1305 LEU A CA  
10554 C C   . LEU B 1308 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1305 LEU A C   
10555 O O   . LEU B 1308 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1305 LEU A O   
10556 C CB  . LEU B 1308 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1305 LEU A CB  
10557 C CG  . LEU B 1308 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1305 LEU A CG  
10558 C CD1 . LEU B 1308 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1305 LEU A CD1 
10559 C CD2 . LEU B 1308 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1305 LEU A CD2 
10560 N N   . ARG B 1309 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1306 ARG A N   
10561 C CA  . ARG B 1309 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1306 ARG A CA  
10562 C C   . ARG B 1309 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1306 ARG A C   
10563 O O   . ARG B 1309 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1306 ARG A O   
10564 C CB  . ARG B 1309 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1306 ARG A CB  
10565 C CG  . ARG B 1309 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1306 ARG A CG  
10566 C CD  . ARG B 1309 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1306 ARG A CD  
10567 N NE  . ARG B 1309 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1306 ARG A NE  
10568 C CZ  . ARG B 1309 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1306 ARG A CZ  
10569 N NH1 . ARG B 1309 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1306 ARG A NH1 
10570 N NH2 . ARG B 1309 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1306 ARG A NH2 
10571 N N   . ASN B 1310 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1307 ASN A N   
10572 C CA  . ASN B 1310 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1307 ASN A CA  
10573 C C   . ASN B 1310 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1307 ASN A C   
10574 O O   . ASN B 1310 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1307 ASN A O   
10575 C CB  . ASN B 1310 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1307 ASN A CB  
10576 C CG  . ASN B 1310 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1307 ASN A CG  
10577 O OD1 . ASN B 1310 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1307 ASN A OD1 
10578 N ND2 . ASN B 1310 ? 0.5665 0.5665 0.5665 0.0000  0.0000  0.0000  1307 ASN A ND2 
# 
