data_9CJH
# 
_entry.id   9CJH 
# 
_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   9CJH         pdb_00009cjh 10.2210/pdb9cjh/pdb 
WWPDB D_1000285688 ?            ?                   
EMDB  EMD-45631    ?            ?                   
# 
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' 1 1 2025-02-05 ? 
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' 1 2 2025-05-28 ? 
21 'EM metadata'     1 1 2025-05-28 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1  1  'Structure model' repository 'Initial release' ? ? 
2  2  'EM metadata'     repository 'Initial release' ? ? 
3  3  'Additional map'  repository 'Initial release' ? ? 
4  4  '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 12 'Additional map'  repository 'Initial release' ? ? 
12 13 'Additional map'  repository 'Initial release' ? ? 
13 14 FSC               repository 'Initial release' ? ? 
14 15 'Half map'        repository 'Initial release' ? ? 
15 16 'Half map'        repository 'Initial release' ? ? 
16 17 Image             repository 'Initial release' ? ? 
17 18 Mask              repository 'Initial release' ? ? 
18 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' 'Data collection'      
2 11 'Structure model' 'Database references'  
3 20 'Structure model' 'Data collection'      
4 21 'EM metadata'     'Data processing'      
5 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' citation        
2 11 'Structure model' citation_author 
3 11 'Structure model' em_admin        
4 20 'Structure model' em_admin        
5 20 'Structure model' em_software     
6 21 'EM metadata'     em_admin        
7 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' '_citation.journal_volume'          
2 11 'Structure model' '_citation.year'                    
3 11 'Structure model' '_citation_author.identifier_ORCID' 
4 11 'Structure model' '_em_admin.last_update'             
5 20 'Structure model' '_em_admin.last_update'             
6 20 'Structure model' '_em_software.name'                 
7 21 'EM metadata'     '_em_admin.last_update'             
8 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                        9CJH 
_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 'Cas12a:gRNA:DNA (Acidaminococcus sp.) with 0 RNA:DNA base pairs, structure 1' EMD-45631 'associated EM volume' 
PDB  .                                                                              9CJI      unspecified            
EMDB .                                                                              EMD-45632 'consensus EM volume'  
PDB  .                                                                              9CJJ      unspecified            
EMDB .                                                                              EMD-45633 'consensus EM volume'  
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              doudna@berkeley.edu 
_pdbx_contact_author.name_first         Jennifer 
_pdbx_contact_author.name_last          Doudna 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9161-999X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Soczek, K.M.' 1 0000-0003-3803-6079 
'Doudna, J.A.' 2 0000-0001-9161-999X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nucleic Acids Res.' 
_citation.journal_id_ASTM           NARHAD 
_citation.journal_id_CSD            0389 
_citation.journal_id_ISSN           1362-4962 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            53 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'CRISPR-Cas12a bends DNA to destabilize base pairs during target interrogation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1093/nar/gkae1192 
_citation.pdbx_database_id_PubMed   39698811 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Soczek, K.M.' 1 ? 
primary 'Cofsky, J.C.' 2 ? 
primary 'Tuck, O.T.'   3 ? 
primary 'Shi, H.'      4 ? 
primary 'Doudna, J.A.' 5 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer syn '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 with XL1, forming N4-cystamine-2'-deoxycytidine; 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  ?    ?   ?   A . n 
B 2 575  LYS 575  572  ?    ?   ?   A . n 
B 2 576  GLY 576  573  ?    ?   ?   A . n 
B 2 577  ARG 577  574  ?    ?   ?   A . n 
B 2 578  TYR 578  575  ?    ?   ?   A . n 
B 2 579  LYS 579  576  ?    ?   ?   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  648  PRO PRO A . n 
B 2 652  GLU 652  649  649  GLU GLU 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 ALA 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    1    DG  DG  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   31   DC  DC  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                     9CJH 
_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                         9CJH 
_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                   9CJH 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9CJH 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.003  ? 11566 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.563  ? 15888 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 17.407 ? 4416  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.039  ? 1773  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.005  ? 1836  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9CJH 
_struct.title                        'Cas12a:gRNA:DNA (Acidaminococcus sp.) with 0 RNA:DNA base pairs, structure 1' 
_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        9CJH 
_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 9CJH        9CJH   ? 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 9CJH        9CJH   ? 3 ? 1 
4 PDB 9CJH        9CJH   ? 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 9CJH B 1 ? 42   ? 9CJH   1 ? 42   ? 1 42   
2 2 9CJH A 4 ? 1310 ? U2UMQ6 1 ? 1307 ? 1 1307 
3 3 9CJH C 1 ? 31   ? 9CJH   1 ? 31   ? 1 31   
4 4 9CJH D 1 ? 31   ? 9CJH   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 9CJH SER A 1   ? UNP U2UMQ6 ?   ?   'expression tag'      -2  1 
2 9CJH ASN A 2   ? UNP U2UMQ6 ?   ?   'expression tag'      -1  2 
2 9CJH ALA A 3   ? UNP U2UMQ6 ?   ?   'expression tag'      0   3 
2 9CJH CYS A 554 ? UNP U2UMQ6 ASN 551 'engineered mutation' 551 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_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   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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   ? ASP B 48   ? GLY A 35   ASP A 45   1 ? 11 
HELX_P HELX_P4  AA4 GLU B 52   ? LEU B 71   ? GLU A 49   LEU A 68   1 ? 20 
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  ? PHE B 136  ? LEU A 132  PHE A 133  5 ? 2  
HELX_P HELX_P9  AA9 LYS B 137  ? PHE B 141  ? LYS A 134  PHE A 138  5 ? 5  
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  ? SER B 184  ? PHE A 169  SER A 181  1 ? 13 
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  ? MET B 510  ? ASP A 493  MET A 507  1 ? 15 
HELX_P HELX_P30 AD3 GLU B 511  ? LYS B 526  ? GLU A 508  LYS A 523  1 ? 16 
HELX_P HELX_P31 AD4 LYS B 551  ? GLY B 556  ? LYS A 548  GLY A 553  1 ? 6  
HELX_P HELX_P32 AD5 ASP B 603  ? SER B 612  ? ASP A 600  SER A 609  1 ? 10 
HELX_P HELX_P33 AD6 LEU B 615  ? HIS B 625  ? LEU A 612  HIS A 622  1 ? 11 
HELX_P HELX_P34 AD7 THR B 642  ? ASN B 650  ? THR A 639  ASN A 647  1 ? 9  
HELX_P HELX_P35 AD8 THR B 660  ? LYS B 665  ? THR A 657  LYS A 662  1 ? 6  
HELX_P HELX_P36 AD9 ASP B 668  ? TYR B 690  ? ASP A 665  TYR A 687  1 ? 23 
HELX_P HELX_P37 AE1 ASP B 697  ? LEU B 701  ? ASP A 694  LEU A 698  5 ? 5  
HELX_P HELX_P38 AE2 ASP B 709  ? TYR B 722  ? ASP A 706  TYR A 719  1 ? 14 
HELX_P HELX_P39 AE3 GLU B 731  ? THR B 740  ? GLU A 728  THR A 737  1 ? 10 
HELX_P HELX_P40 AE4 ASN B 762  ? PHE B 772  ? ASN A 759  PHE A 769  1 ? 11 
HELX_P HELX_P41 AE5 SER B 773  ? LYS B 779  ? SER A 770  LYS A 776  1 ? 7  
HELX_P HELX_P42 AE6 PRO B 822  ? ASN B 834  ? PRO A 819  ASN A 831  1 ? 13 
HELX_P HELX_P43 AE7 SER B 842  ? LEU B 849  ? SER A 839  LEU A 846  1 ? 8  
HELX_P HELX_P44 AE8 PRO B 850  ? VAL B 852  ? PRO A 847  VAL A 849  5 ? 3  
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 TRP B 961  ? GLN B 990  ? TRP A 958  GLN A 987  1 ? 30 
HELX_P HELX_P49 AF4 VAL B 1014 ? CYS B 1028 ? VAL A 1011 CYS A 1025 1 ? 15 
HELX_P HELX_P50 AF5 ASN B 1093 ? PHE B 1104 ? ASN A 1090 PHE A 1101 1 ? 12 
HELX_P HELX_P51 AF6 TYR B 1180 ? GLY B 1193 ? TYR A 1177 GLY A 1190 1 ? 14 
HELX_P HELX_P52 AF7 ILE B 1202 ? ASP B 1210 ? ILE A 1199 ASP A 1207 1 ? 9  
HELX_P HELX_P53 AF8 ASP B 1211 ? GLN B 1227 ? ASP A 1208 GLN A 1224 1 ? 17 
HELX_P HELX_P54 AF9 ASP B 1253 ? GLN B 1257 ? ASP A 1250 GLN A 1254 5 ? 5  
HELX_P HELX_P55 AG1 ASP B 1264 ? SER B 1287 ? ASP A 1261 SER A 1284 1 ? 24 
HELX_P HELX_P56 AG2 SER B 1297 ? ASN B 1310 ? SER A 1294 ASN A 1307 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale one  ? B CYS 554 SG    ? ? ? 1_555 C 2YR 7  S  ? ? A CYS 551 C 2YR 7  1_555 ? ? ? ? ? ? ?                    2.027 
? ? 
covale2  covale both ? C DG  6   "O3'" ? ? ? 1_555 C 2YR 7  P  ? ? C DG  6   C 2YR 7  1_555 ? ? ? ? ? ? ?                    1.606 
? ? 
covale3  covale both ? C 2YR 7   "O3'" ? ? ? 1_555 C DT  8  P  ? ? C 2YR 7   C DT  8  1_555 ? ? ? ? ? ? ?                    1.609 
? ? 
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 DG  1   N2    ? ? ? 1_555 D DC  31 O2 ? ? C DG  1   D DC  31 1_555 ? ? ? ? ? ? 'DG-DC PAIR'         ?     
? ? 
hydrog18 hydrog ?    ? C DT  2   N3    ? ? ? 1_555 D DA  30 N1 ? ? C DT  2   D DA  30 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog19 hydrog ?    ? C DT  2   O4    ? ? ? 1_555 D DA  30 N6 ? ? C DT  2   D DA  30 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog20 hydrog ?    ? C DA  3   N1    ? ? ? 1_555 D DT  29 N3 ? ? C DA  3   D DT  29 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog21 hydrog ?    ? C DA  3   N6    ? ? ? 1_555 D DT  29 O4 ? ? C DA  3   D DT  29 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog22 hydrog ?    ? C DG  4   N1    ? ? ? 1_555 D DC  28 N3 ? ? C DG  4   D DC  28 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog23 hydrog ?    ? C DG  4   N2    ? ? ? 1_555 D DC  28 O2 ? ? C DG  4   D DC  28 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog24 hydrog ?    ? C DG  4   O6    ? ? ? 1_555 D DC  28 N4 ? ? C DG  4   D DC  28 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog25 hydrog ?    ? C DT  5   N3    ? ? ? 1_555 D DA  27 N1 ? ? C DT  5   D DA  27 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog26 hydrog ?    ? C DT  5   O4    ? ? ? 1_555 D DA  27 N6 ? ? C DT  5   D DA  27 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog27 hydrog ?    ? C DG  6   N1    ? ? ? 1_555 D DC  26 N3 ? ? C DG  6   D DC  26 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog28 hydrog ?    ? C DG  6   N2    ? ? ? 1_555 D DC  26 O2 ? ? C DG  6   D DC  26 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog29 hydrog ?    ? C DG  6   O6    ? ? ? 1_555 D DC  26 N4 ? ? C DG  6   D DC  26 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog30 hydrog ?    ? C DT  8   N3    ? ? ? 1_555 D DA  24 N1 ? ? C DT  8   D DA  24 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog31 hydrog ?    ? C DT  8   O4    ? ? ? 1_555 D DA  24 N6 ? ? C DT  8   D DA  24 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog32 hydrog ?    ? C DT  9   N3    ? ? ? 1_555 D DA  23 N1 ? ? C DT  9   D DA  23 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog33 hydrog ?    ? C DT  9   O4    ? ? ? 1_555 D DA  23 N6 ? ? C DT  9   D DA  23 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog34 hydrog ?    ? C DT  10  N3    ? ? ? 1_555 D DA  22 N1 ? ? C DT  10  D DA  22 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog35 hydrog ?    ? C DT  10  O4    ? ? ? 1_555 D DA  22 N6 ? ? C DT  10  D DA  22 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog36 hydrog ?    ? C DG  11  N1    ? ? ? 1_555 D DC  21 N3 ? ? C DG  11  D DC  21 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog37 hydrog ?    ? C DG  11  N2    ? ? ? 1_555 D DC  21 O2 ? ? C DG  11  D DC  21 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog38 hydrog ?    ? C DG  11  O6    ? ? ? 1_555 D DC  21 N4 ? ? C DG  11  D DC  21 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog39 hydrog ?    ? C DC  13  N3    ? ? ? 1_555 D DG  19 N1 ? ? C DC  13  D DG  19 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog40 hydrog ?    ? C DC  13  N4    ? ? ? 1_555 D DG  19 O6 ? ? C DC  13  D DG  19 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog41 hydrog ?    ? C DC  13  O2    ? ? ? 1_555 D DG  19 N2 ? ? C DC  13  D DG  19 1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
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 DC  16  O2    ? ? ? 1_555 D DG  16 N1 ? ? C DC  16  D DG  16 1_555 ? ? ? ? ? ? 'DC-DG PAIR'         ?     
? ? 
# 
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 ? 7 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 6 ? 
AA9 ? 3 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA8 5 6 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
# 
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  
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 GLY B 592  ? ASP B 599  ? GLY A 589  ASP A 596  
AA4 2 HIS B 723  ? ALA B 730  ? HIS A 720  ALA A 727  
AA5 1 ILE B 629  ? LEU B 631  ? ILE A 626  LEU A 628  
AA5 2 LEU B 639  ? ILE B 641  ? LEU A 636  ILE A 638  
AA6 1 ALA B 802  ? HIS B 803  ? ALA A 799  HIS A 800  
AA6 2 ILE B 861  ? ILE B 862  ? ILE A 858  ILE A 859  
AA7 1 LYS B 808  ? LEU B 810  ? LYS A 805  LEU A 807  
AA7 2 THR B 854  ? GLU B 856  ? THR A 851  GLU A 853  
AA8 1 ILE B 929  ? SER B 934  ? ILE A 926  SER A 931  
AA8 2 TYR B 919  ? ILE B 923  ? TYR A 916  ILE A 920  
AA8 3 ILE B 907  ? ASP B 911  ? ILE A 904  ASP A 908  
AA8 4 VAL B 992  ? ASN B 997  ? VAL A 989  ASN A 994  
AA8 5 LEU B 1065 ? PRO B 1069 ? LEU A 1062 PRO A 1066 
AA8 6 GLN B 1061 ? SER B 1062 ? GLN A 1058 SER A 1059 
AA9 1 PHE B 1106 ? ASP B 1110 ? PHE A 1103 ASP A 1107 
AA9 2 ASP B 1115 ? LYS B 1121 ? ASP A 1112 LYS A 1118 
AA9 3 ALA B 1138 ? PHE B 1143 ? ALA A 1135 PHE A 1140 
AB1 1 THR B 1148 ? PHE B 1150 ? THR A 1145 PHE A 1147 
AB1 2 PRO B 1156 ? ILE B 1158 ? PRO A 1153 ILE A 1155 
AB2 1 ARG B 1162 ? VAL B 1164 ? ARG A 1159 VAL A 1161 
AB2 2 ARG B 1177 ? LEU B 1179 ? ARG A 1174 LEU A 1176 
AB3 1 ARG B 1229 ? ASN B 1232 ? ARG A 1226 ASN A 1229 
AB3 2 GLU B 1237 ? ILE B 1240 ? GLU A 1234 ILE A 1237 
# 
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 GLU B 789  ? N GLU A 786  O HIS B 875  ? O HIS A 872  
AA1 3 4 O ILE B 878  ? O ILE A 875  N LYS B 18   ? N LYS A 15   
AA1 4 5 N GLU B 23   ? N GLU A 20   O TYR B 749  ? O TYR A 746  
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  
AA2 1 2 N PHE B 534  ? N PHE A 531  O TYR B 792  ? O TYR A 789  
AA2 2 3 N GLU B 789  ? N GLU A 786  O HIS B 875  ? O HIS A 872  
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 TYR B 597  ? N TYR A 594  O SER B 725  ? O SER A 722  
AA5 1 2 N LEU B 631  ? N LEU A 628  O LEU B 639  ? O LEU A 636  
AA6 1 2 N HIS B 803  ? N HIS A 800  O ILE B 861  ? O ILE A 858  
AA7 1 2 N MET B 809  ? N MET A 806  O LYS B 855  ? O LYS A 852  
AA8 1 2 O LEU B 930  ? O LEU A 927  N VAL B 922  ? N VAL A 919  
AA8 2 3 O ILE B 923  ? O ILE A 920  N ILE B 907  ? N ILE A 904  
AA8 3 4 N ILE B 908  ? N ILE A 905  O VAL B 994  ? O VAL A 991  
AA8 4 5 N LEU B 995  ? N LEU A 992  O PHE B 1066 ? O PHE A 1063 
AA8 5 6 O LEU B 1065 ? O LEU A 1062 N SER B 1062 ? N SER A 1059 
AA9 1 2 N PHE B 1106 ? N PHE A 1103 O HIS B 1119 ? O HIS A 1116 
AA9 2 3 N LEU B 1118 ? N LEU A 1115 O ILE B 1141 ? O ILE A 1138 
AB1 1 2 N GLN B 1149 ? N GLN A 1146 O PHE B 1157 ? O PHE A 1154 
AB2 1 2 N ARG B 1162 ? N ARG A 1159 O LEU B 1179 ? O LEU A 1176 
AB3 1 2 N ASN B 1232 ? N ASN A 1229 O GLU B 1237 ? O GLU A 1234 
# 
_pdbx_entry_details.entry_id                   9CJH 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 CE2 A PHE 165  ? ? ND2 A ASN 534  ? ? 1.20 
2  1 CE2 A PHE 165  ? ? CG  A ASN 534  ? ? 1.21 
3  1 CB  A LYS 164  ? ? CG  A PRO 538  ? ? 1.27 
4  1 CD2 A PHE 165  ? ? ND2 A ASN 534  ? ? 1.59 
5  1 CE2 A PHE 165  ? ? OD1 A ASN 534  ? ? 1.64 
6  1 CZ  A PHE 165  ? ? OD1 A ASN 534  ? ? 1.69 
7  1 CD  A ARG 43   ? ? O   A SER 161  ? ? 1.70 
8  1 NE  A ARG 43   ? ? O   A SER 161  ? ? 1.75 
9  1 CZ  A PHE 165  ? ? ND2 A ASN 534  ? ? 1.83 
10 1 O   A LYS 164  ? ? CB  A PRO 538  ? ? 1.85 
11 1 NE2 A HIS 381  ? ? NZ  A LYS 1086 ? ? 1.88 
12 1 CZ  A PHE 165  ? ? CG  A ASN 534  ? ? 1.97 
13 1 CZ  A ARG 43   ? ? O   A SER 161  ? ? 2.00 
14 1 O   A LYS 164  ? ? CA  A PRO 538  ? ? 2.09 
15 1 CB  A LYS 164  ? ? CB  A PRO 538  ? ? 2.11 
16 1 NH1 A ARG 43   ? ? O   A SER 161  ? ? 2.13 
17 1 NZ  A LYS 468  ? ? O   A GLN 956  ? ? 2.16 
18 1 O   A LYS 1086 ? ? NZ  A LYS 1089 ? ? 2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_1              700 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             N 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_2              700 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CD 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_3              700 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                99.35 
_pdbx_validate_rmsd_angle.angle_target_value         111.70 
_pdbx_validate_rmsd_angle.angle_deviation            -12.35 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.40 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 87   ? ? -91.68  49.43   
2  1 ARG A 113  ? ? -144.55 36.88   
3  1 LYS A 134  ? ? -153.89 -159.78 
4  1 PHE A 165  ? ? -155.26 23.68   
5  1 ALA A 541  ? ? 57.88   17.69   
6  1 ASP A 694  ? ? 37.83   53.81   
7  1 PRO A 700  ? ? -42.34  153.04  
8  1 LYS A 748  ? ? 68.47   -7.20   
9  1 LYS A 1009 ? ? 67.26   -1.76   
10 1 MET A 1133 ? ? 59.71   74.58   
11 1 LEU A 1287 ? ? -93.72  57.70   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9CJH 
_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                    9CJH 
_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                  3.6 
_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               20031 
_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 1' ? ? ? 1,2,3,4 
2 1 RECOMBINANT        COMPLEX Cas12a                                                                         ? ? ? 2       
3 1 SYNTHETIC          COMPLEX gRNA:DNA                                                                       ? ? ? 1,3,4   
# 
_em_imaging.entry_id                        9CJH 
_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              9CJH 
_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                9CJH 
_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              9CJH 
_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 GLN 571 ? B GLN 574 
85  1 Y 1 A LYS 572 ? B LYS 575 
86  1 Y 1 A GLY 573 ? B GLY 576 
87  1 Y 1 A ARG 574 ? B ARG 577 
88  1 Y 1 A TYR 575 ? B TYR 578 
89  1 Y 1 A LYS 576 ? B LYS 579 
90  1 Y 1 A LYS 650 ? B LYS 653 
91  1 Y 1 A GLU 651 ? B GLU 654 
92  1 Y 1 C DT  17  ? C DT  17  
93  1 Y 1 C DC  18  ? C DC  18  
94  1 Y 1 C DA  19  ? C DA  19  
95  1 Y 1 C DT  20  ? C DT  20  
96  1 Y 1 C DC  21  ? C DC  21  
97  1 Y 1 C DT  22  ? C DT  22  
98  1 Y 1 C DG  23  ? C DG  23  
99  1 Y 1 C DT  24  ? C DT  24  
100 1 Y 1 C DA  25  ? C DA  25  
101 1 Y 1 C DT  26  ? C DT  26  
102 1 Y 1 C DG  27  ? C DG  27  
103 1 Y 1 C DC  28  ? C DC  28  
104 1 Y 1 C DG  29  ? C DG  29  
105 1 Y 1 C DT  30  ? C DT  30  
106 1 Y 1 C DC  31  ? C DC  31  
107 1 Y 1 D DG  1   ? D DG  1   
108 1 Y 1 D DA  2   ? D DA  2   
109 1 Y 1 D DC  3   ? D DC  3   
110 1 Y 1 D DG  4   ? D DG  4   
111 1 Y 1 D DC  5   ? D DC  5   
112 1 Y 1 D DA  6   ? D DA  6   
113 1 Y 1 D DT  7   ? D DT  7   
114 1 Y 1 D DA  8   ? D DA  8   
115 1 Y 1 D DC  9   ? D DC  9   
116 1 Y 1 D DA  10  ? D DA  10  
117 1 Y 1 D DG  11  ? D DG  11  
118 1 Y 1 D DA  12  ? D DA  12  
119 1 Y 1 D DT  13  ? D DT  13  
120 1 Y 1 D DG  14  ? D DG  14  
121 1 Y 1 D DA  15  ? D DA  15  
# 
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           9CJH 
_em_admin.last_update        2025-05-28 
_em_admin.map_release_date   2025-01-08 
_em_admin.title              'Cas12a:gRNA:DNA (Acidaminococcus sp.) with 0 RNA:DNA base pairs, structure 1' 
# 
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 
9CJH 'double helix'         
9CJH 'a-form double helix'  
9CJH 'b-form double helix'  
9CJH 'hairpin loop'         
9CJH '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 -3.863 -1.180 0.085  -18.961 -30.987 -102.415 1  B_A5:U13_B    B 5  ? B 13 ? 24 4 
1 A G  17 1_555 A C  12 1_555 -1.037 0.052  0.027  -13.105 -24.900 7.991    2  B_G17:C12_B   B 17 ? B 12 ? 19 1 
1 A U  18 1_555 A A  11 1_555 -0.237 -0.073 0.202  -1.569  -12.962 -0.122   3  B_U18:A11_B   B 18 ? B 11 ? 20 1 
1 A A  19 1_555 A U  10 1_555 0.582  -0.084 0.029  -7.117  1.472   0.151    4  B_A19:U10_B   B 19 ? B 10 ? 20 1 
1 A G  20 1_555 A C  9  1_555 -0.011 -0.388 -0.278 10.495  -1.361  3.355    5  B_G20:C9_B    B 20 ? B 9  ? 19 1 
1 A A  21 1_555 A U  8  1_555 0.246  -0.415 -1.525 -24.017 -11.926 -5.264   6  B_A21:U8_B    B 21 ? B 8  ? 20 1 
1 A U  22 1_555 A U  7  1_555 2.485  -1.502 -0.733 -9.324  -21.293 8.901    7  B_U22:U7_B    B 22 ? B 7  ? 16 1 
1 C DG 1  1_555 D DC 31 1_555 -0.449 0.281  -1.431 1.672   -2.994  17.136   8  C_DG1:DC31_D  C 1  ? D 31 ? ?  1 
1 C DT 2  1_555 D DA 30 1_555 -0.041 -0.213 -0.533 0.340   -9.103  3.970    9  C_DT2:DA30_D  C 2  ? D 30 ? 20 1 
1 C DA 3  1_555 D DT 29 1_555 0.113  -0.258 -1.098 -7.832  -10.869 2.848    10 C_DA3:DT29_D  C 3  ? D 29 ? 20 1 
1 C DG 4  1_555 D DC 28 1_555 -0.167 -0.433 -1.518 -13.829 -3.441  -0.004   11 C_DG4:DC28_D  C 4  ? D 28 ? 19 1 
1 C DT 5  1_555 D DA 27 1_555 -0.159 -0.468 -1.329 -5.967  0.412   -4.057   12 C_DT5:DA27_D  C 5  ? D 27 ? 20 1 
1 C DG 6  1_555 D DC 26 1_555 -0.202 -0.129 0.024  -0.800  5.716   1.486    13 C_DG6:DC26_D  C 6  ? D 26 ? 19 1 
1 C DT 8  1_555 D DA 24 1_555 -0.061 -0.184 -0.015 2.710   -8.598  1.239    14 C_DT8:DA24_D  C 8  ? D 24 ? 20 1 
1 C DT 9  1_555 D DA 23 1_555 -0.216 -0.163 0.596  -8.915  -11.346 -1.449   15 C_DT9:DA23_D  C 9  ? D 23 ? 20 1 
1 C DT 10 1_555 D DA 22 1_555 -0.236 -0.134 0.574  -7.858  -6.959  -6.929   16 C_DT10:DA22_D C 10 ? D 22 ? 20 1 
1 C DG 11 1_555 D DC 21 1_555 -0.189 -0.130 -0.687 -7.571  3.764   -0.554   17 C_DG11:DC21_D C 11 ? D 21 ? 19 1 
1 C DC 13 1_555 D DG 19 1_555 0.160  -0.182 0.347  1.473   5.125   -1.443   18 C_DC13:DG19_D C 13 ? D 19 ? 19 1 
1 C DG 14 1_555 D DC 18 1_555 -0.167 -0.230 0.443  5.840   2.881   -1.925   19 C_DG14:DC18_D C 14 ? D 18 ? 19 1 
1 C DC 16 1_555 D DG 16 1_555 3.523  -0.316 0.292  2.225   -0.231  33.686   20 C_DC16:DG16_D C 16 ? D 16 ? ?  1 
# 
loop_
_ndb_struct_na_base_pair_step.model_number 
_ndb_struct_na_base_pair_step.i_label_asym_id_1 
_ndb_struct_na_base_pair_step.i_label_comp_id_1 
_ndb_struct_na_base_pair_step.i_label_seq_id_1 
_ndb_struct_na_base_pair_step.i_symmetry_1 
_ndb_struct_na_base_pair_step.j_label_asym_id_1 
_ndb_struct_na_base_pair_step.j_label_comp_id_1 
_ndb_struct_na_base_pair_step.j_label_seq_id_1 
_ndb_struct_na_base_pair_step.j_symmetry_1 
_ndb_struct_na_base_pair_step.i_label_asym_id_2 
_ndb_struct_na_base_pair_step.i_label_comp_id_2 
_ndb_struct_na_base_pair_step.i_label_seq_id_2 
_ndb_struct_na_base_pair_step.i_symmetry_2 
_ndb_struct_na_base_pair_step.j_label_asym_id_2 
_ndb_struct_na_base_pair_step.j_label_comp_id_2 
_ndb_struct_na_base_pair_step.j_label_seq_id_2 
_ndb_struct_na_base_pair_step.j_symmetry_2 
_ndb_struct_na_base_pair_step.shift 
_ndb_struct_na_base_pair_step.slide 
_ndb_struct_na_base_pair_step.rise 
_ndb_struct_na_base_pair_step.tilt 
_ndb_struct_na_base_pair_step.roll 
_ndb_struct_na_base_pair_step.twist 
_ndb_struct_na_base_pair_step.x_displacement 
_ndb_struct_na_base_pair_step.y_displacement 
_ndb_struct_na_base_pair_step.helical_rise 
_ndb_struct_na_base_pair_step.inclination 
_ndb_struct_na_base_pair_step.tip 
_ndb_struct_na_base_pair_step.helical_twist 
_ndb_struct_na_base_pair_step.step_number 
_ndb_struct_na_base_pair_step.step_name 
_ndb_struct_na_base_pair_step.i_auth_asym_id_1 
_ndb_struct_na_base_pair_step.i_auth_seq_id_1 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.j_auth_asym_id_1 
_ndb_struct_na_base_pair_step.j_auth_seq_id_1 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.i_auth_asym_id_2 
_ndb_struct_na_base_pair_step.i_auth_seq_id_2 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_2 
_ndb_struct_na_base_pair_step.j_auth_asym_id_2 
_ndb_struct_na_base_pair_step.j_auth_seq_id_2 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_2 
1 A A  5  1_555 A U  13 1_555 A G  17 1_555 A C  12 1_555 3.576  -2.619 3.578 13.997 20.053 81.007 -2.482 -2.305 3.448 15.131 
-10.561 84.005 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 -1.287 -1.922 3.147 -6.429 -5.080 32.315 -2.468 1.127  3.582 -8.949 
11.325  33.311 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 -0.268 -1.226 3.089 0.542  22.424 36.008 -3.661 0.419  2.018 32.671 
-0.789  42.225 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 0.168  -1.190 2.980 2.951  7.789  25.068 -4.394 0.309  2.506 17.344 
-6.571  26.395 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 0.096  -1.184 4.351 13.313 14.127 36.204 -3.677 1.732  3.502 20.983 
-19.773 40.926 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 0.897  -0.321 3.040 -5.586 17.844 40.720 -1.893 -1.641 2.554 24.166 
7.565   44.641 6  BB_A21U22:U7U8_BB       B 21 ? B 8  ? B 22 ? B 7  ? 
1 C DG 1  1_555 D DC 31 1_555 C DT 2  1_555 D DA 30 1_555 -1.839 0.444  3.963 -0.396 0.697  36.268 0.595  2.886  3.990 1.120  
0.636   36.276 7  CC_DG1DT2:DA30DC31_DD   C 1  ? D 31 ? C 2  ? D 30 ? 
1 C DT 2  1_555 D DA 30 1_555 C DA 3  1_555 D DT 29 1_555 0.833  2.705  3.702 -0.810 -0.965 45.087 3.623  -1.168 3.631 -1.258 
1.056   45.104 8  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 -1.330 1.230  3.329 -4.329 -0.912 41.956 1.806  1.387  3.417 -1.269 
6.026   42.179 9  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 -0.210 0.064  3.368 -6.067 1.459  30.213 -0.174 -0.830 3.345 2.763  
11.486  30.836 10 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 1.297  -0.431 3.342 -1.480 6.213  32.771 -1.782 -2.504 3.149 10.884 
2.592   33.371 11 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 0.708  -1.716 6.230 4.031  4.292  68.003 -1.836 -0.344 6.154 3.830  
-3.597  68.226 12 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 0.224  0.267  3.491 2.204  -0.414 43.726 0.401  -0.076 3.495 -0.555 
-2.957  43.781 13 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 -0.573 -0.141 3.411 -3.816 3.583  35.978 -0.750 0.359  3.422 5.762  
6.138   36.344 14 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 -0.727 0.774  3.587 -2.440 5.057  32.790 0.403  0.813  3.705 8.877  
4.283   33.254 15 CC_DT10DG11:DC21DA22_DD C 10 ? D 22 ? C 11 ? D 21 ? 
1 C DG 11 1_555 D DC 21 1_555 C DC 13 1_555 D DG 19 1_555 1.083  0.446  7.132 -1.737 12.043 49.151 -1.353 -1.538 7.012 14.227 
2.052   50.544 16 CC_DG11DC13:DG19DC21_DD C 11 ? D 21 ? 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 0.438  -0.447 3.051 4.224  7.124  37.296 -1.518 -0.175 2.950 10.974 
-6.506  38.172 17 CC_DC13DG14:DC18DG19_DD C 13 ? D 19 ? C 14 ? D 18 ? 
# 
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                    9CJH 
_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    ? 167.377 160.458 135.809 1.00 47.34  ? 4    A   B P     1 
ATOM   2     O OP1   . A   A 1 4    ? 166.141 160.520 134.989 1.00 47.34  ? 4    A   B OP1   1 
ATOM   3     O OP2   . A   A 1 4    ? 168.567 161.245 135.398 1.00 47.34  ? 4    A   B OP2   1 
ATOM   4     O "O5'" . A   A 1 4    ? 166.999 160.877 137.299 1.00 47.34  ? 4    A   B "O5'" 1 
ATOM   5     C "C5'" . A   A 1 4    ? 165.648 160.868 137.738 1.00 47.34  ? 4    A   B "C5'" 1 
ATOM   6     C "C4'" . A   A 1 4    ? 165.455 161.747 138.948 1.00 47.34  ? 4    A   B "C4'" 1 
ATOM   7     O "O4'" . A   A 1 4    ? 166.026 163.057 138.696 1.00 47.34  ? 4    A   B "O4'" 1 
ATOM   8     C "C3'" . A   A 1 4    ? 164.011 162.030 139.341 1.00 47.34  ? 4    A   B "C3'" 1 
ATOM   9     O "O3'" . A   A 1 4    ? 163.448 160.973 140.107 1.00 47.34  ? 4    A   B "O3'" 1 
ATOM   10    C "C2'" . A   A 1 4    ? 164.120 163.361 140.074 1.00 47.34  ? 4    A   B "C2'" 1 
ATOM   11    O "O2'" . A   A 1 4    ? 164.589 163.165 141.399 1.00 47.34  ? 4    A   B "O2'" 1 
ATOM   12    C "C1'" . A   A 1 4    ? 165.219 164.058 139.274 1.00 47.34  ? 4    A   B "C1'" 1 
ATOM   13    N N9    . A   A 1 4    ? 164.685 164.888 138.177 1.00 47.34  ? 4    A   B N9    1 
ATOM   14    C C8    . A   A 1 4    ? 164.466 164.488 136.882 1.00 47.34  ? 4    A   B C8    1 
ATOM   15    N N7    . A   A 1 4    ? 163.996 165.429 136.103 1.00 47.34  ? 4    A   B N7    1 
ATOM   16    C C5    . A   A 1 4    ? 163.905 166.530 136.940 1.00 47.34  ? 4    A   B C5    1 
ATOM   17    C C6    . A   A 1 4    ? 163.475 167.845 136.710 1.00 47.34  ? 4    A   B C6    1 
ATOM   18    N N6    . A   A 1 4    ? 163.042 168.277 135.523 1.00 47.34  ? 4    A   B N6    1 
ATOM   19    N N1    . A   A 1 4    ? 163.502 168.707 137.747 1.00 47.34  ? 4    A   B N1    1 
ATOM   20    C C2    . A   A 1 4    ? 163.938 168.261 138.931 1.00 47.34  ? 4    A   B C2    1 
ATOM   21    N N3    . A   A 1 4    ? 164.370 167.049 139.273 1.00 47.34  ? 4    A   B N3    1 
ATOM   22    C C4    . A   A 1 4    ? 164.327 166.216 138.219 1.00 47.34  ? 4    A   B C4    1 
ATOM   23    P P     . A   A 1 5    ? 162.161 161.188 141.051 1.00 39.98  ? 5    A   B P     1 
ATOM   24    O OP1   . A   A 1 5    ? 161.537 159.856 141.243 1.00 39.98  ? 5    A   B OP1   1 
ATOM   25    O OP2   . A   A 1 5    ? 161.324 162.299 140.537 1.00 39.98  ? 5    A   B OP2   1 
ATOM   26    O "O5'" . A   A 1 5    ? 162.790 161.613 142.449 1.00 39.98  ? 5    A   B "O5'" 1 
ATOM   27    C "C5'" . A   A 1 5    ? 161.987 161.757 143.612 1.00 39.98  ? 5    A   B "C5'" 1 
ATOM   28    C "C4'" . A   A 1 5    ? 162.737 162.513 144.678 1.00 39.98  ? 5    A   B "C4'" 1 
ATOM   29    O "O4'" . A   A 1 5    ? 163.343 163.688 144.086 1.00 39.98  ? 5    A   B "O4'" 1 
ATOM   30    C "C3'" . A   A 1 5    ? 161.919 163.050 145.845 1.00 39.98  ? 5    A   B "C3'" 1 
ATOM   31    O "O3'" . A   A 1 5    ? 161.711 162.065 146.847 1.00 39.98  ? 5    A   B "O3'" 1 
ATOM   32    C "C2'" . A   A 1 5    ? 162.752 164.237 146.317 1.00 39.98  ? 5    A   B "C2'" 1 
ATOM   33    O "O2'" . A   A 1 5    ? 163.828 163.801 147.136 1.00 39.98  ? 5    A   B "O2'" 1 
ATOM   34    C "C1'" . A   A 1 5    ? 163.328 164.757 145.002 1.00 39.98  ? 5    A   B "C1'" 1 
ATOM   35    N N9    . A   A 1 5    ? 162.525 165.848 144.421 1.00 39.98  ? 5    A   B N9    1 
ATOM   36    C C8    . A   A 1 5    ? 161.513 165.740 143.504 1.00 39.98  ? 5    A   B C8    1 
ATOM   37    N N7    . A   A 1 5    ? 160.993 166.890 143.160 1.00 39.98  ? 5    A   B N7    1 
ATOM   38    C C5    . A   A 1 5    ? 161.710 167.817 143.898 1.00 39.98  ? 5    A   B C5    1 
ATOM   39    C C6    . A   A 1 5    ? 161.640 169.217 143.985 1.00 39.98  ? 5    A   B C6    1 
ATOM   40    N N6    . A   A 1 5    ? 160.772 169.958 143.294 1.00 39.98  ? 5    A   B N6    1 
ATOM   41    N N1    . A   A 1 5    ? 162.501 169.838 144.817 1.00 39.98  ? 5    A   B N1    1 
ATOM   42    C C2    . A   A 1 5    ? 163.370 169.096 145.511 1.00 39.98  ? 5    A   B C2    1 
ATOM   43    N N3    . A   A 1 5    ? 163.533 167.776 145.514 1.00 39.98  ? 5    A   B N3    1 
ATOM   44    C C4    . A   A 1 5    ? 162.661 167.190 144.678 1.00 39.98  ? 5    A   B C4    1 
ATOM   45    P P     . U   A 1 6    ? 160.840 162.362 148.170 1.00 34.55  ? 6    U   B P     1 
ATOM   46    O OP1   . U   A 1 6    ? 161.054 163.736 148.684 1.00 34.55  ? 6    U   B OP1   1 
ATOM   47    O OP2   . U   A 1 6    ? 161.079 161.232 149.095 1.00 34.55  ? 6    U   B OP2   1 
ATOM   48    O "O5'" . U   A 1 6    ? 159.330 162.277 147.679 1.00 34.55  ? 6    U   B "O5'" 1 
ATOM   49    C "C5'" . U   A 1 6    ? 158.337 163.096 148.286 1.00 34.55  ? 6    U   B "C5'" 1 
ATOM   50    C "C4'" . U   A 1 6    ? 156.952 162.511 148.163 1.00 34.55  ? 6    U   B "C4'" 1 
ATOM   51    O "O4'" . U   A 1 6    ? 156.543 162.507 146.767 1.00 34.55  ? 6    U   B "O4'" 1 
ATOM   52    C "C3'" . U   A 1 6    ? 156.782 161.079 148.664 1.00 34.55  ? 6    U   B "C3'" 1 
ATOM   53    O "O3'" . U   A 1 6    ? 155.491 160.947 149.252 1.00 34.55  ? 6    U   B "O3'" 1 
ATOM   54    C "C2'" . U   A 1 6    ? 156.828 160.265 147.375 1.00 34.55  ? 6    U   B "C2'" 1 
ATOM   55    O "O2'" . U   A 1 6    ? 156.178 159.014 147.448 1.00 34.55  ? 6    U   B "O2'" 1 
ATOM   56    C "C1'" . U   A 1 6    ? 156.135 161.206 146.397 1.00 34.55  ? 6    U   B "C1'" 1 
ATOM   57    N N1    . U   A 1 6    ? 156.501 160.989 144.991 1.00 34.55  ? 6    U   B N1    1 
ATOM   58    C C2    . U   A 1 6    ? 155.506 160.582 144.130 1.00 34.55  ? 6    U   B C2    1 
ATOM   59    O O2    . U   A 1 6    ? 154.356 160.400 144.492 1.00 34.55  ? 6    U   B O2    1 
ATOM   60    N N3    . U   A 1 6    ? 155.903 160.395 142.832 1.00 34.55  ? 6    U   B N3    1 
ATOM   61    C C4    . U   A 1 6    ? 157.170 160.570 142.319 1.00 34.55  ? 6    U   B C4    1 
ATOM   62    O O4    . U   A 1 6    ? 157.373 160.362 141.123 1.00 34.55  ? 6    U   B O4    1 
ATOM   63    C C5    . U   A 1 6    ? 158.145 160.994 143.275 1.00 34.55  ? 6    U   B C5    1 
ATOM   64    C C6    . U   A 1 6    ? 157.786 161.185 144.547 1.00 34.55  ? 6    U   B C6    1 
ATOM   65    P P     . U   A 1 7    ? 155.303 161.088 150.841 1.00 29.66  ? 7    U   B P     1 
ATOM   66    O OP1   . U   A 1 7    ? 153.935 161.604 151.089 1.00 29.66  ? 7    U   B OP1   1 
ATOM   67    O OP2   . U   A 1 7    ? 156.475 161.812 151.392 1.00 29.66  ? 7    U   B OP2   1 
ATOM   68    O "O5'" . U   A 1 7    ? 155.357 159.585 151.361 1.00 29.66  ? 7    U   B "O5'" 1 
ATOM   69    C "C5'" . U   A 1 7    ? 155.157 159.270 152.729 1.00 29.66  ? 7    U   B "C5'" 1 
ATOM   70    C "C4'" . U   A 1 7    ? 154.366 157.996 152.874 1.00 29.66  ? 7    U   B "C4'" 1 
ATOM   71    O "O4'" . U   A 1 7    ? 152.976 158.308 153.131 1.00 29.66  ? 7    U   B "O4'" 1 
ATOM   72    C "C3'" . U   A 1 7    ? 154.333 157.110 151.640 1.00 29.66  ? 7    U   B "C3'" 1 
ATOM   73    O "O3'" . U   A 1 7    ? 155.477 156.281 151.542 1.00 29.66  ? 7    U   B "O3'" 1 
ATOM   74    C "C2'" . U   A 1 7    ? 153.036 156.327 151.812 1.00 29.66  ? 7    U   B "C2'" 1 
ATOM   75    O "O2'" . U   A 1 7    ? 153.231 155.220 152.680 1.00 29.66  ? 7    U   B "O2'" 1 
ATOM   76    C "C1'" . U   A 1 7    ? 152.143 157.346 152.524 1.00 29.66  ? 7    U   B "C1'" 1 
ATOM   77    N N1    . U   A 1 7    ? 151.202 158.042 151.616 1.00 29.66  ? 7    U   B N1    1 
ATOM   78    C C2    . U   A 1 7    ? 150.138 157.338 151.085 1.00 29.66  ? 7    U   B C2    1 
ATOM   79    O O2    . U   A 1 7    ? 149.937 156.156 151.296 1.00 29.66  ? 7    U   B O2    1 
ATOM   80    N N3    . U   A 1 7    ? 149.309 158.067 150.273 1.00 29.66  ? 7    U   B N3    1 
ATOM   81    C C4    . U   A 1 7    ? 149.420 159.401 149.954 1.00 29.66  ? 7    U   B C4    1 
ATOM   82    O O4    . U   A 1 7    ? 148.589 159.915 149.203 1.00 29.66  ? 7    U   B O4    1 
ATOM   83    C C5    . U   A 1 7    ? 150.537 160.063 150.548 1.00 29.66  ? 7    U   B C5    1 
ATOM   84    C C6    . U   A 1 7    ? 151.363 159.378 151.343 1.00 29.66  ? 7    U   B C6    1 
ATOM   85    P P     . U   A 1 8    ? 156.496 156.436 150.312 1.00 34.85  ? 8    U   B P     1 
ATOM   86    O OP1   . U   A 1 8    ? 157.849 156.686 150.866 1.00 34.85  ? 8    U   B OP1   1 
ATOM   87    O OP2   . U   A 1 8    ? 155.916 157.394 149.340 1.00 34.85  ? 8    U   B OP2   1 
ATOM   88    O "O5'" . U   A 1 8    ? 156.510 154.992 149.644 1.00 34.85  ? 8    U   B "O5'" 1 
ATOM   89    C "C5'" . U   A 1 8    ? 155.431 154.083 149.838 1.00 34.85  ? 8    U   B "C5'" 1 
ATOM   90    C "C4'" . U   A 1 8    ? 154.826 153.650 148.526 1.00 34.85  ? 8    U   B "C4'" 1 
ATOM   91    O "O4'" . U   A 1 8    ? 153.565 154.349 148.324 1.00 34.85  ? 8    U   B "O4'" 1 
ATOM   92    C "C3'" . U   A 1 8    ? 155.676 153.940 147.289 1.00 34.85  ? 8    U   B "C3'" 1 
ATOM   93    O "O3'" . U   A 1 8    ? 155.475 152.905 146.327 1.00 34.85  ? 8    U   B "O3'" 1 
ATOM   94    C "C2'" . U   A 1 8    ? 155.070 155.240 146.777 1.00 34.85  ? 8    U   B "C2'" 1 
ATOM   95    O "O2'" . U   A 1 8    ? 155.300 155.516 145.412 1.00 34.85  ? 8    U   B "O2'" 1 
ATOM   96    C "C1'" . U   A 1 8    ? 153.594 155.017 147.080 1.00 34.85  ? 8    U   B "C1'" 1 
ATOM   97    N N1    . U   A 1 8    ? 152.820 156.260 147.180 1.00 34.85  ? 8    U   B N1    1 
ATOM   98    C C2    . U   A 1 8    ? 151.483 156.212 146.852 1.00 34.85  ? 8    U   B C2    1 
ATOM   99    O O2    . U   A 1 8    ? 150.923 155.182 146.523 1.00 34.85  ? 8    U   B O2    1 
ATOM   100   N N3    . U   A 1 8    ? 150.828 157.414 146.944 1.00 34.85  ? 8    U   B N3    1 
ATOM   101   C C4    . U   A 1 8    ? 151.369 158.629 147.307 1.00 34.85  ? 8    U   B C4    1 
ATOM   102   O O4    . U   A 1 8    ? 150.653 159.628 147.339 1.00 34.85  ? 8    U   B O4    1 
ATOM   103   C C5    . U   A 1 8    ? 152.763 158.597 147.613 1.00 34.85  ? 8    U   B C5    1 
ATOM   104   C C6    . U   A 1 8    ? 153.423 157.440 147.533 1.00 34.85  ? 8    U   B C6    1 
ATOM   105   P P     . C   A 1 9    ? 156.424 152.794 145.035 1.00 48.55  ? 9    C   B P     1 
ATOM   106   O OP1   . C   A 1 9    ? 156.871 151.384 144.911 1.00 48.55  ? 9    C   B OP1   1 
ATOM   107   O OP2   . C   A 1 9    ? 157.431 153.883 145.094 1.00 48.55  ? 9    C   B OP2   1 
ATOM   108   O "O5'" . C   A 1 9    ? 155.441 153.112 143.823 1.00 48.55  ? 9    C   B "O5'" 1 
ATOM   109   C "C5'" . C   A 1 9    ? 154.416 152.197 143.471 1.00 48.55  ? 9    C   B "C5'" 1 
ATOM   110   C "C4'" . C   A 1 9    ? 153.565 152.708 142.336 1.00 48.55  ? 9    C   B "C4'" 1 
ATOM   111   O "O4'" . C   A 1 9    ? 152.451 153.484 142.844 1.00 48.55  ? 9    C   B "O4'" 1 
ATOM   112   C "C3'" . C   A 1 9    ? 154.234 153.648 141.349 1.00 48.55  ? 9    C   B "C3'" 1 
ATOM   113   O "O3'" . C   A 1 9    ? 155.072 152.982 140.422 1.00 48.55  ? 9    C   B "O3'" 1 
ATOM   114   C "C2'" . C   A 1 9    ? 153.040 154.342 140.706 1.00 48.55  ? 9    C   B "C2'" 1 
ATOM   115   O "O2'" . C   A 1 9    ? 152.437 153.504 139.732 1.00 48.55  ? 9    C   B "O2'" 1 
ATOM   116   C "C1'" . C   A 1 9    ? 152.084 154.465 141.895 1.00 48.55  ? 9    C   B "C1'" 1 
ATOM   117   N N1    . C   A 1 9    ? 152.147 155.805 142.521 1.00 48.55  ? 9    C   B N1    1 
ATOM   118   C C2    . C   A 1 9    ? 151.329 156.808 142.001 1.00 48.55  ? 9    C   B C2    1 
ATOM   119   O O2    . C   A 1 9    ? 150.581 156.534 141.051 1.00 48.55  ? 9    C   B O2    1 
ATOM   120   N N3    . C   A 1 9    ? 151.364 158.045 142.543 1.00 48.55  ? 9    C   B N3    1 
ATOM   121   C C4    . C   A 1 9    ? 152.180 158.300 143.563 1.00 48.55  ? 9    C   B C4    1 
ATOM   122   N N4    . C   A 1 9    ? 152.182 159.536 144.068 1.00 48.55  ? 9    C   B N4    1 
ATOM   123   C C5    . C   A 1 9    ? 153.030 157.299 144.110 1.00 48.55  ? 9    C   B C5    1 
ATOM   124   C C6    . C   A 1 9    ? 152.982 156.078 143.564 1.00 48.55  ? 9    C   B C6    1 
ATOM   125   P P     . U   A 1 10   ? 156.271 153.778 139.711 1.00 33.37  ? 10   U   B P     1 
ATOM   126   O OP1   . U   A 1 10   ? 157.173 152.786 139.075 1.00 33.37  ? 10   U   B OP1   1 
ATOM   127   O OP2   . U   A 1 10   ? 156.822 154.748 140.689 1.00 33.37  ? 10   U   B OP2   1 
ATOM   128   O "O5'" . U   A 1 10   ? 155.552 154.602 138.554 1.00 33.37  ? 10   U   B "O5'" 1 
ATOM   129   C "C5'" . U   A 1 10   ? 154.808 153.935 137.545 1.00 33.37  ? 10   U   B "C5'" 1 
ATOM   130   C "C4'" . U   A 1 10   ? 153.975 154.898 136.738 1.00 33.37  ? 10   U   B "C4'" 1 
ATOM   131   O "O4'" . U   A 1 10   ? 152.953 155.497 137.576 1.00 33.37  ? 10   U   B "O4'" 1 
ATOM   132   C "C3'" . U   A 1 10   ? 154.710 156.092 136.156 1.00 33.37  ? 10   U   B "C3'" 1 
ATOM   133   O "O3'" . U   A 1 10   ? 155.442 155.779 134.987 1.00 33.37  ? 10   U   B "O3'" 1 
ATOM   134   C "C2'" . U   A 1 10   ? 153.583 157.090 135.931 1.00 33.37  ? 10   U   B "C2'" 1 
ATOM   135   O "O2'" . U   A 1 10   ? 152.848 156.761 134.761 1.00 33.37  ? 10   U   B "O2'" 1 
ATOM   136   C "C1'" . U   A 1 10   ? 152.697 156.819 137.147 1.00 33.37  ? 10   U   B "C1'" 1 
ATOM   137   N N1    . U   A 1 10   ? 152.986 157.750 138.262 1.00 33.37  ? 10   U   B N1    1 
ATOM   138   C C2    . U   A 1 10   ? 152.335 158.966 138.258 1.00 33.37  ? 10   U   B C2    1 
ATOM   139   O O2    . U   A 1 10   ? 151.544 159.288 137.389 1.00 33.37  ? 10   U   B O2    1 
ATOM   140   N N3    . U   A 1 10   ? 152.639 159.791 139.311 1.00 33.37  ? 10   U   B N3    1 
ATOM   141   C C4    . U   A 1 10   ? 153.512 159.531 140.346 1.00 33.37  ? 10   U   B C4    1 
ATOM   142   O O4    . U   A 1 10   ? 153.680 160.378 141.224 1.00 33.37  ? 10   U   B O4    1 
ATOM   143   C C5    . U   A 1 10   ? 154.148 158.255 140.278 1.00 33.37  ? 10   U   B C5    1 
ATOM   144   C C6    . U   A 1 10   ? 153.870 157.431 139.264 1.00 33.37  ? 10   U   B C6    1 
ATOM   145   P P     . A   A 1 11   ? 156.866 156.472 134.730 1.00 36.71  ? 11   A   B P     1 
ATOM   146   O OP1   . A   A 1 11   ? 157.522 155.772 133.598 1.00 36.71  ? 11   A   B OP1   1 
ATOM   147   O OP2   . A   A 1 11   ? 157.567 156.578 136.034 1.00 36.71  ? 11   A   B OP2   1 
ATOM   148   O "O5'" . A   A 1 11   ? 156.488 157.942 134.249 1.00 36.71  ? 11   A   B "O5'" 1 
ATOM   149   C "C5'" . A   A 1 11   ? 155.711 158.137 133.079 1.00 36.71  ? 11   A   B "C5'" 1 
ATOM   150   C "C4'" . A   A 1 11   ? 155.100 159.514 133.031 1.00 36.71  ? 11   A   B "C4'" 1 
ATOM   151   O "O4'" . A   A 1 11   ? 154.138 159.676 134.107 1.00 36.71  ? 11   A   B "O4'" 1 
ATOM   152   C "C3'" . A   A 1 11   ? 156.048 160.683 133.224 1.00 36.71  ? 11   A   B "C3'" 1 
ATOM   153   O "O3'" . A   A 1 11   ? 156.811 160.992 132.073 1.00 36.71  ? 11   A   B "O3'" 1 
ATOM   154   C "C2'" . A   A 1 11   ? 155.100 161.793 133.649 1.00 36.71  ? 11   A   B "C2'" 1 
ATOM   155   O "O2'" . A   A 1 11   ? 154.379 162.291 132.532 1.00 36.71  ? 11   A   B "O2'" 1 
ATOM   156   C "C1'" . A   A 1 11   ? 154.132 161.021 134.542 1.00 36.71  ? 11   A   B "C1'" 1 
ATOM   157   N N9    . A   A 1 11   ? 154.559 161.069 135.951 1.00 36.71  ? 11   A   B N9    1 
ATOM   158   C C8    . A   A 1 11   ? 155.157 160.084 136.696 1.00 36.71  ? 11   A   B C8    1 
ATOM   159   N N7    . A   A 1 11   ? 155.426 160.445 137.927 1.00 36.71  ? 11   A   B N7    1 
ATOM   160   C C5    . A   A 1 11   ? 154.982 161.757 137.994 1.00 36.71  ? 11   A   B C5    1 
ATOM   161   C C6    . A   A 1 11   ? 154.979 162.705 139.031 1.00 36.71  ? 11   A   B C6    1 
ATOM   162   N N6    . A   A 1 11   ? 155.458 162.466 140.254 1.00 36.71  ? 11   A   B N6    1 
ATOM   163   N N1    . A   A 1 11   ? 154.460 163.924 138.769 1.00 36.71  ? 11   A   B N1    1 
ATOM   164   C C2    . A   A 1 11   ? 153.979 164.165 137.544 1.00 36.71  ? 11   A   B C2    1 
ATOM   165   N N3    . A   A 1 11   ? 153.926 163.356 136.489 1.00 36.71  ? 11   A   B N3    1 
ATOM   166   C C4    . A   A 1 11   ? 154.449 162.154 136.784 1.00 36.71  ? 11   A   B C4    1 
ATOM   167   P P     . C   A 1 12   ? 158.335 161.470 132.233 1.00 42.17  ? 12   C   B P     1 
ATOM   168   O OP1   . C   A 1 12   ? 158.890 161.685 130.874 1.00 42.17  ? 12   C   B OP1   1 
ATOM   169   O OP2   . C   A 1 12   ? 159.014 160.536 133.166 1.00 42.17  ? 12   C   B OP2   1 
ATOM   170   O "O5'" . C   A 1 12   ? 158.222 162.889 132.948 1.00 42.17  ? 12   C   B "O5'" 1 
ATOM   171   C "C5'" . C   A 1 12   ? 157.618 163.984 132.278 1.00 42.17  ? 12   C   B "C5'" 1 
ATOM   172   C "C4'" . C   A 1 12   ? 157.134 165.045 133.236 1.00 42.17  ? 12   C   B "C4'" 1 
ATOM   173   O "O4'" . C   A 1 12   ? 156.584 164.442 134.432 1.00 42.17  ? 12   C   B "O4'" 1 
ATOM   174   C "C3'" . C   A 1 12   ? 158.178 166.009 133.768 1.00 42.17  ? 12   C   B "C3'" 1 
ATOM   175   O "O3'" . C   A 1 12   ? 158.509 167.016 132.831 1.00 42.17  ? 12   C   B "O3'" 1 
ATOM   176   C "C2'" . C   A 1 12   ? 157.513 166.550 135.027 1.00 42.17  ? 12   C   B "C2'" 1 
ATOM   177   O "O2'" . C   A 1 12   ? 156.566 167.556 134.702 1.00 42.17  ? 12   C   B "O2'" 1 
ATOM   178   C "C1'" . C   A 1 12   ? 156.751 165.319 135.526 1.00 42.17  ? 12   C   B "C1'" 1 
ATOM   179   N N1    . C   A 1 12   ? 157.464 164.618 136.616 1.00 42.17  ? 12   C   B N1    1 
ATOM   180   C C2    . C   A 1 12   ? 157.312 165.110 137.913 1.00 42.17  ? 12   C   B C2    1 
ATOM   181   O O2    . C   A 1 12   ? 156.594 166.105 138.098 1.00 42.17  ? 12   C   B O2    1 
ATOM   182   N N3    . C   A 1 12   ? 157.945 164.496 138.934 1.00 42.17  ? 12   C   B N3    1 
ATOM   183   C C4    . C   A 1 12   ? 158.704 163.431 138.696 1.00 42.17  ? 12   C   B C4    1 
ATOM   184   N N4    . C   A 1 12   ? 159.308 162.859 139.738 1.00 42.17  ? 12   C   B N4    1 
ATOM   185   C C5    . C   A 1 12   ? 158.879 162.905 137.384 1.00 42.17  ? 12   C   B C5    1 
ATOM   186   C C6    . C   A 1 12   ? 158.245 163.523 136.380 1.00 42.17  ? 12   C   B C6    1 
ATOM   187   P P     . U   A 1 13   ? 159.970 167.680 132.839 1.00 44.96  ? 13   U   B P     1 
ATOM   188   O OP1   . U   A 1 13   ? 160.153 168.370 131.538 1.00 44.96  ? 13   U   B OP1   1 
ATOM   189   O OP2   . U   A 1 13   ? 160.949 166.653 133.274 1.00 44.96  ? 13   U   B OP2   1 
ATOM   190   O "O5'" . U   A 1 13   ? 159.875 168.787 133.977 1.00 44.96  ? 13   U   B "O5'" 1 
ATOM   191   C "C5'" . U   A 1 13   ? 158.819 169.742 133.973 1.00 44.96  ? 13   U   B "C5'" 1 
ATOM   192   C "C4'" . U   A 1 13   ? 158.868 170.642 135.182 1.00 44.96  ? 13   U   B "C4'" 1 
ATOM   193   O "O4'" . U   A 1 13   ? 158.727 169.842 136.388 1.00 44.96  ? 13   U   B "O4'" 1 
ATOM   194   C "C3'" . U   A 1 13   ? 160.156 171.444 135.350 1.00 44.96  ? 13   U   B "C3'" 1 
ATOM   195   O "O3'" . U   A 1 13   ? 159.843 172.722 135.895 1.00 44.96  ? 13   U   B "O3'" 1 
ATOM   196   C "C2'" . U   A 1 13   ? 160.935 170.628 136.376 1.00 44.96  ? 13   U   B "C2'" 1 
ATOM   197   O "O2'" . U   A 1 13   ? 161.879 171.366 137.121 1.00 44.96  ? 13   U   B "O2'" 1 
ATOM   198   C "C1'" . U   A 1 13   ? 159.812 170.095 137.258 1.00 44.96  ? 13   U   B "C1'" 1 
ATOM   199   N N1    . U   A 1 13   ? 160.143 168.847 137.960 1.00 44.96  ? 13   U   B N1    1 
ATOM   200   C C2    . U   A 1 13   ? 160.415 168.926 139.310 1.00 44.96  ? 13   U   B C2    1 
ATOM   201   O O2    . U   A 1 13   ? 160.395 169.976 139.928 1.00 44.96  ? 13   U   B O2    1 
ATOM   202   N N3    . U   A 1 13   ? 160.714 167.729 139.910 1.00 44.96  ? 13   U   B N3    1 
ATOM   203   C C4    . U   A 1 13   ? 160.765 166.490 139.311 1.00 44.96  ? 13   U   B C4    1 
ATOM   204   O O4    . U   A 1 13   ? 161.051 165.501 139.987 1.00 44.96  ? 13   U   B O4    1 
ATOM   205   C C5    . U   A 1 13   ? 160.469 166.493 137.913 1.00 44.96  ? 13   U   B C5    1 
ATOM   206   C C6    . U   A 1 13   ? 160.174 167.643 137.301 1.00 44.96  ? 13   U   B C6    1 
ATOM   207   P P     . C   A 1 14   ? 159.477 173.942 134.918 1.00 56.74  ? 14   C   B P     1 
ATOM   208   O OP1   . C   A 1 14   ? 158.059 174.311 135.151 1.00 56.74  ? 14   C   B OP1   1 
ATOM   209   O OP2   . C   A 1 14   ? 159.912 173.579 133.547 1.00 56.74  ? 14   C   B OP2   1 
ATOM   210   O "O5'" . C   A 1 14   ? 160.402 175.132 135.432 1.00 56.74  ? 14   C   B "O5'" 1 
ATOM   211   C "C5'" . C   A 1 14   ? 160.268 175.643 136.750 1.00 56.74  ? 14   C   B "C5'" 1 
ATOM   212   C "C4'" . C   A 1 14   ? 159.640 177.013 136.738 1.00 56.74  ? 14   C   B "C4'" 1 
ATOM   213   O "O4'" . C   A 1 14   ? 158.347 176.946 136.084 1.00 56.74  ? 14   C   B "O4'" 1 
ATOM   214   C "C3'" . C   A 1 14   ? 159.343 177.630 138.097 1.00 56.74  ? 14   C   B "C3'" 1 
ATOM   215   O "O3'" . C   A 1 14   ? 160.495 178.235 138.673 1.00 56.74  ? 14   C   B "O3'" 1 
ATOM   216   C "C2'" . C   A 1 14   ? 158.216 178.604 137.776 1.00 56.74  ? 14   C   B "C2'" 1 
ATOM   217   O "O2'" . C   A 1 14   ? 158.730 179.792 137.192 1.00 56.74  ? 14   C   B "O2'" 1 
ATOM   218   C "C1'" . C   A 1 14   ? 157.445 177.833 136.704 1.00 56.74  ? 14   C   B "C1'" 1 
ATOM   219   N N1    . C   A 1 14   ? 156.327 177.039 137.264 1.00 56.74  ? 14   C   B N1    1 
ATOM   220   C C2    . C   A 1 14   ? 155.146 177.677 137.652 1.00 56.74  ? 14   C   B C2    1 
ATOM   221   O O2    . C   A 1 14   ? 155.053 178.908 137.533 1.00 56.74  ? 14   C   B O2    1 
ATOM   222   N N3    . C   A 1 14   ? 154.132 176.936 138.156 1.00 56.74  ? 14   C   B N3    1 
ATOM   223   C C4    . C   A 1 14   ? 154.260 175.613 138.273 1.00 56.74  ? 14   C   B C4    1 
ATOM   224   N N4    . C   A 1 14   ? 153.234 174.924 138.774 1.00 56.74  ? 14   C   B N4    1 
ATOM   225   C C5    . C   A 1 14   ? 155.448 174.937 137.879 1.00 56.74  ? 14   C   B C5    1 
ATOM   226   C C6    . C   A 1 14   ? 156.441 175.683 137.384 1.00 56.74  ? 14   C   B C6    1 
ATOM   227   P P     . U   A 1 15   ? 160.448 179.012 140.086 1.00 51.15  ? 15   U   B P     1 
ATOM   228   O OP1   . U   A 1 15   ? 159.062 179.311 140.525 1.00 51.15  ? 15   U   B OP1   1 
ATOM   229   O OP2   . U   A 1 15   ? 161.394 180.146 139.950 1.00 51.15  ? 15   U   B OP2   1 
ATOM   230   O "O5'" . U   A 1 15   ? 161.109 177.996 141.123 1.00 51.15  ? 15   U   B "O5'" 1 
ATOM   231   C "C5'" . U   A 1 15   ? 160.635 176.664 141.270 1.00 51.15  ? 15   U   B "C5'" 1 
ATOM   232   C "C4'" . U   A 1 15   ? 159.282 176.623 141.935 1.00 51.15  ? 15   U   B "C4'" 1 
ATOM   233   O "O4'" . U   A 1 15   ? 158.269 176.302 140.949 1.00 51.15  ? 15   U   B "O4'" 1 
ATOM   234   C "C3'" . U   A 1 15   ? 159.098 175.571 143.017 1.00 51.15  ? 15   U   B "C3'" 1 
ATOM   235   O "O3'" . U   A 1 15   ? 159.598 175.993 144.273 1.00 51.15  ? 15   U   B "O3'" 1 
ATOM   236   C "C2'" . U   A 1 15   ? 157.591 175.348 143.016 1.00 51.15  ? 15   U   B "C2'" 1 
ATOM   237   O "O2'" . U   A 1 15   ? 156.935 176.378 143.738 1.00 51.15  ? 15   U   B "O2'" 1 
ATOM   238   C "C1'" . U   A 1 15   ? 157.256 175.514 141.534 1.00 51.15  ? 15   U   B "C1'" 1 
ATOM   239   N N1    . U   A 1 15   ? 157.193 174.219 140.818 1.00 51.15  ? 15   U   B N1    1 
ATOM   240   C C2    . U   A 1 15   ? 156.020 173.498 140.907 1.00 51.15  ? 15   U   B C2    1 
ATOM   241   O O2    . U   A 1 15   ? 155.056 173.880 141.548 1.00 51.15  ? 15   U   B O2    1 
ATOM   242   N N3    . U   A 1 15   ? 156.017 172.311 140.221 1.00 51.15  ? 15   U   B N3    1 
ATOM   243   C C4    . U   A 1 15   ? 157.046 171.784 139.468 1.00 51.15  ? 15   U   B C4    1 
ATOM   244   O O4    . U   A 1 15   ? 156.891 170.699 138.907 1.00 51.15  ? 15   U   B O4    1 
ATOM   245   C C5    . U   A 1 15   ? 158.224 172.592 139.423 1.00 51.15  ? 15   U   B C5    1 
ATOM   246   C C6    . U   A 1 15   ? 158.255 173.754 140.082 1.00 51.15  ? 15   U   B C6    1 
ATOM   247   P P     . U   A 1 16   ? 161.057 175.536 144.764 1.00 45.02  ? 16   U   B P     1 
ATOM   248   O OP1   . U   A 1 16   ? 161.841 176.757 145.075 1.00 45.02  ? 16   U   B OP1   1 
ATOM   249   O OP2   . U   A 1 16   ? 161.589 174.558 143.782 1.00 45.02  ? 16   U   B OP2   1 
ATOM   250   O "O5'" . U   A 1 16   ? 160.780 174.767 146.132 1.00 45.02  ? 16   U   B "O5'" 1 
ATOM   251   C "C5'" . U   A 1 16   ? 160.110 173.513 146.143 1.00 45.02  ? 16   U   B "C5'" 1 
ATOM   252   C "C4'" . U   A 1 16   ? 160.801 172.513 147.039 1.00 45.02  ? 16   U   B "C4'" 1 
ATOM   253   O "O4'" . U   A 1 16   ? 162.230 172.790 147.065 1.00 45.02  ? 16   U   B "O4'" 1 
ATOM   254   C "C3'" . U   A 1 16   ? 160.342 172.501 148.499 1.00 45.02  ? 16   U   B "C3'" 1 
ATOM   255   O "O3'" . U   A 1 16   ? 160.371 171.161 148.987 1.00 45.02  ? 16   U   B "O3'" 1 
ATOM   256   C "C2'" . U   A 1 16   ? 161.429 173.309 149.201 1.00 45.02  ? 16   U   B "C2'" 1 
ATOM   257   O "O2'" . U   A 1 16   ? 161.575 173.027 150.577 1.00 45.02  ? 16   U   B "O2'" 1 
ATOM   258   C "C1'" . U   A 1 16   ? 162.662 172.897 148.406 1.00 45.02  ? 16   U   B "C1'" 1 
ATOM   259   N N1    . U   A 1 16   ? 163.808 173.820 148.482 1.00 45.02  ? 16   U   B N1    1 
ATOM   260   C C2    . U   A 1 16   ? 163.688 175.165 148.163 1.00 45.02  ? 16   U   B C2    1 
ATOM   261   O O2    . U   A 1 16   ? 162.660 175.701 147.793 1.00 45.02  ? 16   U   B O2    1 
ATOM   262   N N3    . U   A 1 16   ? 164.846 175.892 148.285 1.00 45.02  ? 16   U   B N3    1 
ATOM   263   C C4    . U   A 1 16   ? 166.085 175.440 148.684 1.00 45.02  ? 16   U   B C4    1 
ATOM   264   O O4    . U   A 1 16   ? 167.030 176.228 148.743 1.00 45.02  ? 16   U   B O4    1 
ATOM   265   C C5    . U   A 1 16   ? 166.130 174.048 148.999 1.00 45.02  ? 16   U   B C5    1 
ATOM   266   C C6    . U   A 1 16   ? 165.020 173.314 148.889 1.00 45.02  ? 16   U   B C6    1 
ATOM   267   P P     . G   A 1 17   ? 159.066 170.519 149.668 1.00 36.89  ? 17   G   B P     1 
ATOM   268   O OP1   . G   A 1 17   ? 159.082 170.889 151.105 1.00 36.89  ? 17   G   B OP1   1 
ATOM   269   O OP2   . G   A 1 17   ? 158.990 169.088 149.280 1.00 36.89  ? 17   G   B OP2   1 
ATOM   270   O "O5'" . G   A 1 17   ? 157.856 171.283 148.972 1.00 36.89  ? 17   G   B "O5'" 1 
ATOM   271   C "C5'" . G   A 1 17   ? 156.898 170.581 148.193 1.00 36.89  ? 17   G   B "C5'" 1 
ATOM   272   C "C4'" . G   A 1 17   ? 156.883 171.080 146.771 1.00 36.89  ? 17   G   B "C4'" 1 
ATOM   273   O "O4'" . G   A 1 17   ? 158.059 170.596 146.070 1.00 36.89  ? 17   G   B "O4'" 1 
ATOM   274   C "C3'" . G   A 1 17   ? 155.726 170.612 145.905 1.00 36.89  ? 17   G   B "C3'" 1 
ATOM   275   O "O3'" . G   A 1 17   ? 154.534 171.347 146.118 1.00 36.89  ? 17   G   B "O3'" 1 
ATOM   276   C "C2'" . G   A 1 17   ? 156.291 170.762 144.502 1.00 36.89  ? 17   G   B "C2'" 1 
ATOM   277   O "O2'" . G   A 1 17   ? 156.288 172.126 144.106 1.00 36.89  ? 17   G   B "O2'" 1 
ATOM   278   C "C1'" . G   A 1 17   ? 157.738 170.330 144.721 1.00 36.89  ? 17   G   B "C1'" 1 
ATOM   279   N N9    . G   A 1 17   ? 157.912 168.888 144.476 1.00 36.89  ? 17   G   B N9    1 
ATOM   280   C C8    . G   A 1 17   ? 158.254 167.925 145.393 1.00 36.89  ? 17   G   B C8    1 
ATOM   281   N N7    . G   A 1 17   ? 158.326 166.729 144.876 1.00 36.89  ? 17   G   B N7    1 
ATOM   282   C C5    . G   A 1 17   ? 158.009 166.914 143.538 1.00 36.89  ? 17   G   B C5    1 
ATOM   283   C C6    . G   A 1 17   ? 157.928 165.978 142.476 1.00 36.89  ? 17   G   B C6    1 
ATOM   284   O O6    . G   A 1 17   ? 158.122 164.757 142.508 1.00 36.89  ? 17   G   B O6    1 
ATOM   285   N N1    . G   A 1 17   ? 157.577 166.593 141.280 1.00 36.89  ? 17   G   B N1    1 
ATOM   286   C C2    . G   A 1 17   ? 157.338 167.934 141.122 1.00 36.89  ? 17   G   B C2    1 
ATOM   287   N N2    . G   A 1 17   ? 157.012 168.337 139.886 1.00 36.89  ? 17   G   B N2    1 
ATOM   288   N N3    . G   A 1 17   ? 157.414 168.816 142.102 1.00 36.89  ? 17   G   B N3    1 
ATOM   289   C C4    . G   A 1 17   ? 157.753 168.241 143.274 1.00 36.89  ? 17   G   B C4    1 
ATOM   290   P P     . U   A 1 18   ? 153.106 170.656 145.864 1.00 36.27  ? 18   U   B P     1 
ATOM   291   O OP1   . U   A 1 18   ? 152.054 171.584 146.349 1.00 36.27  ? 18   U   B OP1   1 
ATOM   292   O OP2   . U   A 1 18   ? 153.162 169.271 146.392 1.00 36.27  ? 18   U   B OP2   1 
ATOM   293   O "O5'" . U   A 1 18   ? 152.992 170.572 144.278 1.00 36.27  ? 18   U   B "O5'" 1 
ATOM   294   C "C5'" . U   A 1 18   ? 152.959 171.749 143.486 1.00 36.27  ? 18   U   B "C5'" 1 
ATOM   295   C "C4'" . U   A 1 18   ? 152.810 171.428 142.020 1.00 36.27  ? 18   U   B "C4'" 1 
ATOM   296   O "O4'" . U   A 1 18   ? 153.957 170.668 141.561 1.00 36.27  ? 18   U   B "O4'" 1 
ATOM   297   C "C3'" . U   A 1 18   ? 151.622 170.559 141.645 1.00 36.27  ? 18   U   B "C3'" 1 
ATOM   298   O "O3'" . U   A 1 18   ? 150.410 171.285 141.561 1.00 36.27  ? 18   U   B "O3'" 1 
ATOM   299   C "C2'" . U   A 1 18   ? 152.063 169.950 140.321 1.00 36.27  ? 18   U   B "C2'" 1 
ATOM   300   O "O2'" . U   A 1 18   ? 151.902 170.883 139.262 1.00 36.27  ? 18   U   B "O2'" 1 
ATOM   301   C "C1'" . U   A 1 18   ? 153.559 169.750 140.565 1.00 36.27  ? 18   U   B "C1'" 1 
ATOM   302   N N1    . U   A 1 18   ? 153.870 168.380 141.030 1.00 36.27  ? 18   U   B N1    1 
ATOM   303   C C2    . U   A 1 18   ? 153.922 167.379 140.083 1.00 36.27  ? 18   U   B C2    1 
ATOM   304   O O2    . U   A 1 18   ? 153.726 167.576 138.897 1.00 36.27  ? 18   U   B O2    1 
ATOM   305   N N3    . U   A 1 18   ? 154.214 166.133 140.576 1.00 36.27  ? 18   U   B N3    1 
ATOM   306   C C4    . U   A 1 18   ? 154.455 165.793 141.890 1.00 36.27  ? 18   U   B C4    1 
ATOM   307   O O4    . U   A 1 18   ? 154.705 164.621 142.176 1.00 36.27  ? 18   U   B O4    1 
ATOM   308   C C5    . U   A 1 18   ? 154.382 166.884 142.809 1.00 36.27  ? 18   U   B C5    1 
ATOM   309   C C6    . U   A 1 18   ? 154.099 168.109 142.357 1.00 36.27  ? 18   U   B C6    1 
ATOM   310   P P     . A   A 1 19   ? 149.053 170.650 142.137 1.00 35.90  ? 19   A   B P     1 
ATOM   311   O OP1   . A   A 1 19   ? 148.006 171.702 142.102 1.00 35.90  ? 19   A   B OP1   1 
ATOM   312   O OP2   . A   A 1 19   ? 149.371 169.970 143.417 1.00 35.90  ? 19   A   B OP2   1 
ATOM   313   O "O5'" . A   A 1 19   ? 148.665 169.534 141.069 1.00 35.90  ? 19   A   B "O5'" 1 
ATOM   314   C "C5'" . A   A 1 19   ? 148.185 169.895 139.784 1.00 35.90  ? 19   A   B "C5'" 1 
ATOM   315   C "C4'" . A   A 1 19   ? 147.947 168.683 138.920 1.00 35.90  ? 19   A   B "C4'" 1 
ATOM   316   O "O4'" . A   A 1 19   ? 149.214 168.096 138.531 1.00 35.90  ? 19   A   B "O4'" 1 
ATOM   317   C "C3'" . A   A 1 19   ? 147.195 167.534 139.570 1.00 35.90  ? 19   A   B "C3'" 1 
ATOM   318   O "O3'" . A   A 1 19   ? 145.793 167.733 139.594 1.00 35.90  ? 19   A   B "O3'" 1 
ATOM   319   C "C2'" . A   A 1 19   ? 147.627 166.340 138.730 1.00 35.90  ? 19   A   B "C2'" 1 
ATOM   320   O "O2'" . A   A 1 19   ? 146.917 166.309 137.501 1.00 35.90  ? 19   A   B "O2'" 1 
ATOM   321   C "C1'" . A   A 1 19   ? 149.085 166.693 138.436 1.00 35.90  ? 19   A   B "C1'" 1 
ATOM   322   N N9    . A   A 1 19   ? 150.007 166.071 139.402 1.00 35.90  ? 19   A   B N9    1 
ATOM   323   C C8    . A   A 1 19   ? 150.589 166.647 140.502 1.00 35.90  ? 19   A   B C8    1 
ATOM   324   N N7    . A   A 1 19   ? 151.366 165.833 141.174 1.00 35.90  ? 19   A   B N7    1 
ATOM   325   C C5    . A   A 1 19   ? 151.289 164.642 140.468 1.00 35.90  ? 19   A   B C5    1 
ATOM   326   C C6    . A   A 1 19   ? 151.884 163.385 140.665 1.00 35.90  ? 19   A   B C6    1 
ATOM   327   N N6    . A   A 1 19   ? 152.711 163.107 141.675 1.00 35.90  ? 19   A   B N6    1 
ATOM   328   N N1    . A   A 1 19   ? 151.598 162.409 139.777 1.00 35.90  ? 19   A   B N1    1 
ATOM   329   C C2    . A   A 1 19   ? 150.769 162.686 138.765 1.00 35.90  ? 19   A   B C2    1 
ATOM   330   N N3    . A   A 1 19   ? 150.148 163.826 138.475 1.00 35.90  ? 19   A   B N3    1 
ATOM   331   C C4    . A   A 1 19   ? 150.455 164.774 139.375 1.00 35.90  ? 19   A   B C4    1 
ATOM   332   P P     . G   A 1 20   ? 144.917 167.157 140.810 1.00 34.17  ? 20   G   B P     1 
ATOM   333   O OP1   . G   A 1 20   ? 143.556 167.739 140.706 1.00 34.17  ? 20   G   B OP1   1 
ATOM   334   O OP2   . G   A 1 20   ? 145.695 167.310 142.064 1.00 34.17  ? 20   G   B OP2   1 
ATOM   335   O "O5'" . G   A 1 20   ? 144.788 165.604 140.491 1.00 34.17  ? 20   G   B "O5'" 1 
ATOM   336   C "C5'" . G   A 1 20   ? 143.954 165.153 139.436 1.00 34.17  ? 20   G   B "C5'" 1 
ATOM   337   C "C4'" . G   A 1 20   ? 144.228 163.714 139.083 1.00 34.17  ? 20   G   B "C4'" 1 
ATOM   338   O "O4'" . G   A 1 20   ? 145.639 163.535 138.800 1.00 34.17  ? 20   G   B "O4'" 1 
ATOM   339   C "C3'" . G   A 1 20   ? 143.945 162.688 140.166 1.00 34.17  ? 20   G   B "C3'" 1 
ATOM   340   O "O3'" . G   A 1 20   ? 142.573 162.363 140.285 1.00 34.17  ? 20   G   B "O3'" 1 
ATOM   341   C "C2'" . G   A 1 20   ? 144.813 161.516 139.734 1.00 34.17  ? 20   G   B "C2'" 1 
ATOM   342   O "O2'" . G   A 1 20   ? 144.205 160.812 138.661 1.00 34.17  ? 20   G   B "O2'" 1 
ATOM   343   C "C1'" . G   A 1 20   ? 146.046 162.242 139.197 1.00 34.17  ? 20   G   B "C1'" 1 
ATOM   344   N N9    . G   A 1 20   ? 147.094 162.363 140.226 1.00 34.17  ? 20   G   B N9    1 
ATOM   345   C C8    . G   A 1 20   ? 147.315 163.414 141.080 1.00 34.17  ? 20   G   B C8    1 
ATOM   346   N N7    . G   A 1 20   ? 148.322 163.213 141.885 1.00 34.17  ? 20   G   B N7    1 
ATOM   347   C C5    . G   A 1 20   ? 148.789 161.952 141.545 1.00 34.17  ? 20   G   B C5    1 
ATOM   348   C C6    . G   A 1 20   ? 149.865 161.193 142.074 1.00 34.17  ? 20   G   B C6    1 
ATOM   349   O O6    . G   A 1 20   ? 150.649 161.495 142.981 1.00 34.17  ? 20   G   B O6    1 
ATOM   350   N N1    . G   A 1 20   ? 149.987 159.965 141.433 1.00 34.17  ? 20   G   B N1    1 
ATOM   351   C C2    . G   A 1 20   ? 149.179 159.521 140.416 1.00 34.17  ? 20   G   B C2    1 
ATOM   352   N N2    . G   A 1 20   ? 149.453 158.305 139.925 1.00 34.17  ? 20   G   B N2    1 
ATOM   353   N N3    . G   A 1 20   ? 148.174 160.219 139.917 1.00 34.17  ? 20   G   B N3    1 
ATOM   354   C C4    . G   A 1 20   ? 148.039 161.414 140.524 1.00 34.17  ? 20   G   B C4    1 
ATOM   355   P P     . A   A 1 21   ? 141.981 161.875 141.697 1.00 27.82  ? 21   A   B P     1 
ATOM   356   O OP1   . A   A 1 21   ? 140.501 161.869 141.603 1.00 27.82  ? 21   A   B OP1   1 
ATOM   357   O OP2   . A   A 1 21   ? 142.642 162.664 142.767 1.00 27.82  ? 21   A   B OP2   1 
ATOM   358   O "O5'" . A   A 1 21   ? 142.475 160.366 141.824 1.00 27.82  ? 21   A   B "O5'" 1 
ATOM   359   C "C5'" . A   A 1 21   ? 142.064 159.383 140.886 1.00 27.82  ? 21   A   B "C5'" 1 
ATOM   360   C "C4'" . A   A 1 21   ? 142.952 158.165 140.938 1.00 27.82  ? 21   A   B "C4'" 1 
ATOM   361   O "O4'" . A   A 1 21   ? 144.334 158.559 140.747 1.00 27.82  ? 21   A   B "O4'" 1 
ATOM   362   C "C3'" . A   A 1 21   ? 142.963 157.403 142.253 1.00 27.82  ? 21   A   B "C3'" 1 
ATOM   363   O "O3'" . A   A 1 21   ? 141.865 156.517 142.380 1.00 27.82  ? 21   A   B "O3'" 1 
ATOM   364   C "C2'" . A   A 1 21   ? 144.311 156.696 142.217 1.00 27.82  ? 21   A   B "C2'" 1 
ATOM   365   O "O2'" . A   A 1 21   ? 144.249 155.541 141.393 1.00 27.82  ? 21   A   B "O2'" 1 
ATOM   366   C "C1'" . A   A 1 21   ? 145.182 157.739 141.519 1.00 27.82  ? 21   A   B "C1'" 1 
ATOM   367   N N9    . A   A 1 21   ? 145.910 158.588 142.479 1.00 27.82  ? 21   A   B N9    1 
ATOM   368   C C8    . A   A 1 21   ? 145.653 159.895 142.810 1.00 27.82  ? 21   A   B C8    1 
ATOM   369   N N7    . A   A 1 21   ? 146.481 160.387 143.699 1.00 27.82  ? 21   A   B N7    1 
ATOM   370   C C5    . A   A 1 21   ? 147.341 159.333 143.969 1.00 27.82  ? 21   A   B C5    1 
ATOM   371   C C6    . A   A 1 21   ? 148.445 159.211 144.828 1.00 27.82  ? 21   A   B C6    1 
ATOM   372   N N6    . A   A 1 21   ? 148.889 160.199 145.608 1.00 27.82  ? 21   A   B N6    1 
ATOM   373   N N1    . A   A 1 21   ? 149.085 158.023 144.863 1.00 27.82  ? 21   A   B N1    1 
ATOM   374   C C2    . A   A 1 21   ? 148.640 157.031 144.082 1.00 27.82  ? 21   A   B C2    1 
ATOM   375   N N3    . A   A 1 21   ? 147.616 157.025 143.233 1.00 27.82  ? 21   A   B N3    1 
ATOM   376   C C4    . A   A 1 21   ? 147.002 158.220 143.224 1.00 27.82  ? 21   A   B C4    1 
ATOM   377   P P     . U   A 1 22   ? 141.116 156.351 143.790 1.00 31.13  ? 22   U   B P     1 
ATOM   378   O OP1   . U   A 1 22   ? 140.006 155.383 143.609 1.00 31.13  ? 22   U   B OP1   1 
ATOM   379   O OP2   . U   A 1 22   ? 140.832 157.706 144.323 1.00 31.13  ? 22   U   B OP2   1 
ATOM   380   O "O5'" . U   A 1 22   ? 142.208 155.670 144.726 1.00 31.13  ? 22   U   B "O5'" 1 
ATOM   381   C "C5'" . U   A 1 22   ? 142.697 154.367 144.449 1.00 31.13  ? 22   U   B "C5'" 1 
ATOM   382   C "C4'" . U   A 1 22   ? 143.914 154.054 145.280 1.00 31.13  ? 22   U   B "C4'" 1 
ATOM   383   O "O4'" . U   A 1 22   ? 144.995 154.952 144.920 1.00 31.13  ? 22   U   B "O4'" 1 
ATOM   384   C "C3'" . U   A 1 22   ? 143.755 154.251 146.778 1.00 31.13  ? 22   U   B "C3'" 1 
ATOM   385   O "O3'" . U   A 1 22   ? 143.113 153.162 147.415 1.00 31.13  ? 22   U   B "O3'" 1 
ATOM   386   C "C2'" . U   A 1 22   ? 145.189 154.477 147.236 1.00 31.13  ? 22   U   B "C2'" 1 
ATOM   387   O "O2'" . U   A 1 22   ? 145.891 153.245 147.312 1.00 31.13  ? 22   U   B "O2'" 1 
ATOM   388   C "C1'" . U   A 1 22   ? 145.754 155.278 146.064 1.00 31.13  ? 22   U   B "C1'" 1 
ATOM   389   N N1    . U   A 1 22   ? 145.659 156.738 146.292 1.00 31.13  ? 22   U   B N1    1 
ATOM   390   C C2    . U   A 1 22   ? 146.642 157.336 147.053 1.00 31.13  ? 22   U   B C2    1 
ATOM   391   O O2    . U   A 1 22   ? 147.572 156.717 147.538 1.00 31.13  ? 22   U   B O2    1 
ATOM   392   N N3    . U   A 1 22   ? 146.497 158.689 147.227 1.00 31.13  ? 22   U   B N3    1 
ATOM   393   C C4    . U   A 1 22   ? 145.492 159.490 146.730 1.00 31.13  ? 22   U   B C4    1 
ATOM   394   O O4    . U   A 1 22   ? 145.502 160.697 146.976 1.00 31.13  ? 22   U   B O4    1 
ATOM   395   C C5    . U   A 1 22   ? 144.513 158.800 145.952 1.00 31.13  ? 22   U   B C5    1 
ATOM   396   C C6    . U   A 1 22   ? 144.629 157.482 145.764 1.00 31.13  ? 22   U   B C6    1 
ATOM   397   P P     . A   A 1 23   ? 141.607 153.319 147.954 1.00 28.33  ? 23   A   B P     1 
ATOM   398   O OP1   . A   A 1 23   ? 140.700 152.657 146.984 1.00 28.33  ? 23   A   B OP1   1 
ATOM   399   O OP2   . A   A 1 23   ? 141.391 154.743 148.307 1.00 28.33  ? 23   A   B OP2   1 
ATOM   400   O "O5'" . A   A 1 23   ? 141.594 152.470 149.299 1.00 28.33  ? 23   A   B "O5'" 1 
ATOM   401   C "C5'" . A   A 1 23   ? 142.564 152.702 150.314 1.00 28.33  ? 23   A   B "C5'" 1 
ATOM   402   C "C4'" . A   A 1 23   ? 143.218 151.420 150.769 1.00 28.33  ? 23   A   B "C4'" 1 
ATOM   403   O "O4'" . A   A 1 23   ? 142.341 150.728 151.699 1.00 28.33  ? 23   A   B "O4'" 1 
ATOM   404   C "C3'" . A   A 1 23   ? 143.545 150.420 149.661 1.00 28.33  ? 23   A   B "C3'" 1 
ATOM   405   O "O3'" . A   A 1 23   ? 144.767 149.753 149.972 1.00 28.33  ? 23   A   B "O3'" 1 
ATOM   406   C "C2'" . A   A 1 23   ? 142.388 149.428 149.751 1.00 28.33  ? 23   A   B "C2'" 1 
ATOM   407   O "O2'" . A   A 1 23   ? 142.677 148.140 149.249 1.00 28.33  ? 23   A   B "O2'" 1 
ATOM   408   C "C1'" . A   A 1 23   ? 142.123 149.405 151.252 1.00 28.33  ? 23   A   B "C1'" 1 
ATOM   409   N N9    . A   A 1 23   ? 140.762 149.011 151.616 1.00 28.33  ? 23   A   B N9    1 
ATOM   410   C C8    . A   A 1 23   ? 139.641 149.018 150.826 1.00 28.33  ? 23   A   B C8    1 
ATOM   411   N N7    . A   A 1 23   ? 138.560 148.603 151.440 1.00 28.33  ? 23   A   B N7    1 
ATOM   412   C C5    . A   A 1 23   ? 139.000 148.303 152.721 1.00 28.33  ? 23   A   B C5    1 
ATOM   413   C C6    . A   A 1 23   ? 138.337 147.816 153.860 1.00 28.33  ? 23   A   B C6    1 
ATOM   414   N N6    . A   A 1 23   ? 137.033 147.533 153.891 1.00 28.33  ? 23   A   B N6    1 
ATOM   415   N N1    . A   A 1 23   ? 139.067 147.626 154.979 1.00 28.33  ? 23   A   B N1    1 
ATOM   416   C C2    . A   A 1 23   ? 140.374 147.910 154.947 1.00 28.33  ? 23   A   B C2    1 
ATOM   417   N N3    . A   A 1 23   ? 141.109 148.371 153.939 1.00 28.33  ? 23   A   B N3    1 
ATOM   418   C C4    . A   A 1 23   ? 140.354 148.549 152.843 1.00 28.33  ? 23   A   B C4    1 
ATOM   419   P P     . G   A 1 24   ? 146.160 150.326 149.415 1.00 32.60  ? 24   G   B P     1 
ATOM   420   O OP1   . G   A 1 24   ? 145.951 151.734 148.997 1.00 32.60  ? 24   G   B OP1   1 
ATOM   421   O OP2   . G   A 1 24   ? 146.704 149.344 148.445 1.00 32.60  ? 24   G   B OP2   1 
ATOM   422   O "O5'" . G   A 1 24   ? 147.111 150.330 150.692 1.00 32.60  ? 24   G   B "O5'" 1 
ATOM   423   C "C5'" . G   A 1 24   ? 147.569 149.114 151.261 1.00 32.60  ? 24   G   B "C5'" 1 
ATOM   424   C "C4'" . G   A 1 24   ? 147.346 149.081 152.751 1.00 32.60  ? 24   G   B "C4'" 1 
ATOM   425   O "O4'" . G   A 1 24   ? 145.924 149.079 153.029 1.00 32.60  ? 24   G   B "O4'" 1 
ATOM   426   C "C3'" . G   A 1 24   ? 147.867 147.848 153.472 1.00 32.60  ? 24   G   B "C3'" 1 
ATOM   427   O "O3'" . G   A 1 24   ? 149.252 147.924 153.758 1.00 32.60  ? 24   G   B "O3'" 1 
ATOM   428   C "C2'" . G   A 1 24   ? 146.991 147.793 154.715 1.00 32.60  ? 24   G   B "C2'" 1 
ATOM   429   O "O2'" . G   A 1 24   ? 147.445 148.720 155.689 1.00 32.60  ? 24   G   B "O2'" 1 
ATOM   430   C "C1'" . G   A 1 24   ? 145.655 148.288 154.166 1.00 32.60  ? 24   G   B "C1'" 1 
ATOM   431   N N9    . G   A 1 24   ? 144.769 147.180 153.764 1.00 32.60  ? 24   G   B N9    1 
ATOM   432   C C8    . G   A 1 24   ? 144.502 146.763 152.484 1.00 32.60  ? 24   G   B C8    1 
ATOM   433   N N7    . G   A 1 24   ? 143.671 145.759 152.436 1.00 32.60  ? 24   G   B N7    1 
ATOM   434   C C5    . G   A 1 24   ? 143.368 145.501 153.765 1.00 32.60  ? 24   G   B C5    1 
ATOM   435   C C6    . G   A 1 24   ? 142.517 144.522 154.338 1.00 32.60  ? 24   G   B C6    1 
ATOM   436   O O6    . G   A 1 24   ? 141.839 143.660 153.766 1.00 32.60  ? 24   G   B O6    1 
ATOM   437   N N1    . G   A 1 24   ? 142.499 144.610 155.726 1.00 32.60  ? 24   G   B N1    1 
ATOM   438   C C2    . G   A 1 24   ? 143.208 145.522 156.468 1.00 32.60  ? 24   G   B C2    1 
ATOM   439   N N2    . G   A 1 24   ? 143.057 145.447 157.798 1.00 32.60  ? 24   G   B N2    1 
ATOM   440   N N3    . G   A 1 24   ? 144.005 146.440 155.945 1.00 32.60  ? 24   G   B N3    1 
ATOM   441   C C4    . G   A 1 24   ? 144.037 146.371 154.598 1.00 32.60  ? 24   G   B C4    1 
ATOM   442   P P     . C   A 1 25   ? 150.261 146.826 153.163 1.00 39.19  ? 25   C   B P     1 
ATOM   443   O OP1   . C   A 1 25   ? 151.647 147.303 153.393 1.00 39.19  ? 25   C   B OP1   1 
ATOM   444   O OP2   . C   A 1 25   ? 149.818 146.494 151.787 1.00 39.19  ? 25   C   B OP2   1 
ATOM   445   O "O5'" . C   A 1 25   ? 150.024 145.548 154.081 1.00 39.19  ? 25   C   B "O5'" 1 
ATOM   446   C "C5'" . C   A 1 25   ? 150.395 145.560 155.450 1.00 39.19  ? 25   C   B "C5'" 1 
ATOM   447   C "C4'" . C   A 1 25   ? 149.657 144.507 156.238 1.00 39.19  ? 25   C   B "C4'" 1 
ATOM   448   O "O4'" . C   A 1 25   ? 148.228 144.722 156.124 1.00 39.19  ? 25   C   B "O4'" 1 
ATOM   449   C "C3'" . C   A 1 25   ? 149.851 143.070 155.782 1.00 39.19  ? 25   C   B "C3'" 1 
ATOM   450   O "O3'" . C   A 1 25   ? 151.055 142.499 156.262 1.00 39.19  ? 25   C   B "O3'" 1 
ATOM   451   C "C2'" . C   A 1 25   ? 148.598 142.381 156.307 1.00 39.19  ? 25   C   B "C2'" 1 
ATOM   452   O "O2'" . C   A 1 25   ? 148.728 142.092 157.691 1.00 39.19  ? 25   C   B "O2'" 1 
ATOM   453   C "C1'" . C   A 1 25   ? 147.551 143.484 156.142 1.00 39.19  ? 25   C   B "C1'" 1 
ATOM   454   N N1    . C   A 1 25   ? 146.778 143.345 154.888 1.00 39.19  ? 25   C   B N1    1 
ATOM   455   C C2    . C   A 1 25   ? 145.668 142.500 154.881 1.00 39.19  ? 25   C   B C2    1 
ATOM   456   O O2    . C   A 1 25   ? 145.371 141.894 155.920 1.00 39.19  ? 25   C   B O2    1 
ATOM   457   N N3    . C   A 1 25   ? 144.947 142.362 153.746 1.00 39.19  ? 25   C   B N3    1 
ATOM   458   C C4    . C   A 1 25   ? 145.299 143.030 152.648 1.00 39.19  ? 25   C   B C4    1 
ATOM   459   N N4    . C   A 1 25   ? 144.558 142.863 151.550 1.00 39.19  ? 25   C   B N4    1 
ATOM   460   C C5    . C   A 1 25   ? 146.425 143.901 152.626 1.00 39.19  ? 25   C   B C5    1 
ATOM   461   C C6    . C   A 1 25   ? 147.128 144.029 153.758 1.00 39.19  ? 25   C   B C6    1 
ATOM   462   P P     . A   A 1 26   ? 152.225 142.094 155.238 1.00 65.69  ? 26   A   B P     1 
ATOM   463   O OP1   . A   A 1 26   ? 153.519 142.228 155.952 1.00 65.69  ? 26   A   B OP1   1 
ATOM   464   O OP2   . A   A 1 26   ? 152.006 142.834 153.971 1.00 65.69  ? 26   A   B OP2   1 
ATOM   465   O "O5'" . A   A 1 26   ? 151.973 140.548 154.952 1.00 65.69  ? 26   A   B "O5'" 1 
ATOM   466   C "C5'" . A   A 1 26   ? 152.204 139.572 155.958 1.00 65.69  ? 26   A   B "C5'" 1 
ATOM   467   C "C4'" . A   A 1 26   ? 151.389 138.326 155.716 1.00 65.69  ? 26   A   B "C4'" 1 
ATOM   468   O "O4'" . A   A 1 26   ? 149.979 138.669 155.676 1.00 65.69  ? 26   A   B "O4'" 1 
ATOM   469   C "C3'" . A   A 1 26   ? 151.635 137.615 154.394 1.00 65.69  ? 26   A   B "C3'" 1 
ATOM   470   O "O3'" . A   A 1 26   ? 152.774 136.773 154.418 1.00 65.69  ? 26   A   B "O3'" 1 
ATOM   471   C "C2'" . A   A 1 26   ? 150.328 136.868 154.171 1.00 65.69  ? 26   A   B "C2'" 1 
ATOM   472   O "O2'" . A   A 1 26   ? 150.279 135.695 154.969 1.00 65.69  ? 26   A   B "O2'" 1 
ATOM   473   C "C1'" . A   A 1 26   ? 149.314 137.870 154.722 1.00 65.69  ? 26   A   B "C1'" 1 
ATOM   474   N N9    . A   A 1 26   ? 148.787 138.753 153.664 1.00 65.69  ? 26   A   B N9    1 
ATOM   475   C C8    . A   A 1 26   ? 149.338 139.919 153.192 1.00 65.69  ? 26   A   B C8    1 
ATOM   476   N N7    . A   A 1 26   ? 148.641 140.486 152.238 1.00 65.69  ? 26   A   B N7    1 
ATOM   477   C C5    . A   A 1 26   ? 147.559 139.635 152.069 1.00 65.69  ? 26   A   B C5    1 
ATOM   478   C C6    . A   A 1 26   ? 146.451 139.677 151.207 1.00 65.69  ? 26   A   B C6    1 
ATOM   479   N N6    . A   A 1 26   ? 146.246 140.649 150.317 1.00 65.69  ? 26   A   B N6    1 
ATOM   480   N N1    . A   A 1 26   ? 145.551 138.673 151.291 1.00 65.69  ? 26   A   B N1    1 
ATOM   481   C C2    . A   A 1 26   ? 145.759 137.698 152.185 1.00 65.69  ? 26   A   B C2    1 
ATOM   482   N N3    . A   A 1 26   ? 146.760 137.549 153.049 1.00 65.69  ? 26   A   B N3    1 
ATOM   483   C C4    . A   A 1 26   ? 147.636 138.562 152.939 1.00 65.69  ? 26   A   B C4    1 
ATOM   484   P P     . G   A 1 27   ? 153.683 136.608 153.102 1.00 84.97  ? 27   G   B P     1 
ATOM   485   O OP1   . G   A 1 27   ? 154.947 135.936 153.498 1.00 84.97  ? 27   G   B OP1   1 
ATOM   486   O OP2   . G   A 1 27   ? 153.736 137.922 152.413 1.00 84.97  ? 27   G   B OP2   1 
ATOM   487   O "O5'" . G   A 1 27   ? 152.856 135.603 152.184 1.00 84.97  ? 27   G   B "O5'" 1 
ATOM   488   C "C5'" . G   A 1 27   ? 152.621 134.265 152.597 1.00 84.97  ? 27   G   B "C5'" 1 
ATOM   489   C "C4'" . G   A 1 27   ? 151.487 133.637 151.826 1.00 84.97  ? 27   G   B "C4'" 1 
ATOM   490   O "O4'" . G   A 1 27   ? 150.275 134.413 152.020 1.00 84.97  ? 27   G   B "O4'" 1 
ATOM   491   C "C3'" . G   A 1 27   ? 151.654 133.589 150.315 1.00 84.97  ? 27   G   B "C3'" 1 
ATOM   492   O "O3'" . G   A 1 27   ? 152.465 132.513 149.876 1.00 84.97  ? 27   G   B "O3'" 1 
ATOM   493   C "C2'" . G   A 1 27   ? 150.214 133.512 149.828 1.00 84.97  ? 27   G   B "C2'" 1 
ATOM   494   O "O2'" . G   A 1 27   ? 149.699 132.199 149.991 1.00 84.97  ? 27   G   B "O2'" 1 
ATOM   495   C "C1'" . G   A 1 27   ? 149.516 134.429 150.830 1.00 84.97  ? 27   G   B "C1'" 1 
ATOM   496   N N9    . G   A 1 27   ? 149.446 135.819 150.343 1.00 84.97  ? 27   G   B N9    1 
ATOM   497   C C8    . G   A 1 27   ? 150.319 136.841 150.627 1.00 84.97  ? 27   G   B C8    1 
ATOM   498   N N7    . G   A 1 27   ? 150.002 137.966 150.045 1.00 84.97  ? 27   G   B N7    1 
ATOM   499   C C5    . G   A 1 27   ? 148.850 137.668 149.331 1.00 84.97  ? 27   G   B C5    1 
ATOM   500   C C6    . G   A 1 27   ? 148.045 138.491 148.502 1.00 84.97  ? 27   G   B C6    1 
ATOM   501   O O6    . G   A 1 27   ? 148.194 139.688 148.226 1.00 84.97  ? 27   G   B O6    1 
ATOM   502   N N1    . G   A 1 27   ? 146.971 137.785 147.972 1.00 84.97  ? 27   G   B N1    1 
ATOM   503   C C2    . G   A 1 27   ? 146.703 136.460 148.207 1.00 84.97  ? 27   G   B C2    1 
ATOM   504   N N2    . G   A 1 27   ? 145.615 135.960 147.603 1.00 84.97  ? 27   G   B N2    1 
ATOM   505   N N3    . G   A 1 27   ? 147.445 135.682 148.977 1.00 84.97  ? 27   G   B N3    1 
ATOM   506   C C4    . G   A 1 27   ? 148.495 136.347 149.502 1.00 84.97  ? 27   G   B C4    1 
ATOM   507   P P     . A   A 1 28   ? 153.248 132.615 148.476 1.00 103.91 ? 28   A   B P     1 
ATOM   508   O OP1   . A   A 1 28   ? 154.370 131.642 148.499 1.00 103.91 ? 28   A   B OP1   1 
ATOM   509   O OP2   . A   A 1 28   ? 153.527 134.049 148.209 1.00 103.91 ? 28   A   B OP2   1 
ATOM   510   O "O5'" . A   A 1 28   ? 152.182 132.117 147.403 1.00 103.91 ? 28   A   B "O5'" 1 
ATOM   511   C "C5'" . A   A 1 28   ? 152.400 132.308 146.013 1.00 103.91 ? 28   A   B "C5'" 1 
ATOM   512   C "C4'" . A   A 1 28   ? 151.133 132.097 145.224 1.00 103.91 ? 28   A   B "C4'" 1 
ATOM   513   O "O4'" . A   A 1 28   ? 150.044 132.828 145.845 1.00 103.91 ? 28   A   B "O4'" 1 
ATOM   514   C "C3'" . A   A 1 28   ? 151.149 132.602 143.790 1.00 103.91 ? 28   A   B "C3'" 1 
ATOM   515   O "O3'" . A   A 1 28   ? 151.774 131.700 142.892 1.00 103.91 ? 28   A   B "O3'" 1 
ATOM   516   C "C2'" . A   A 1 28   ? 149.672 132.828 143.499 1.00 103.91 ? 28   A   B "C2'" 1 
ATOM   517   O "O2'" . A   A 1 28   ? 149.023 131.598 143.211 1.00 103.91 ? 28   A   B "O2'" 1 
ATOM   518   C "C1'" . A   A 1 28   ? 149.172 133.330 144.854 1.00 103.91 ? 28   A   B "C1'" 1 
ATOM   519   N N9    . A   A 1 28   ? 149.176 134.803 144.934 1.00 103.91 ? 28   A   B N9    1 
ATOM   520   C C8    . A   A 1 28   ? 150.047 135.604 145.630 1.00 103.91 ? 28   A   B C8    1 
ATOM   521   N N7    . A   A 1 28   ? 149.796 136.885 145.510 1.00 103.91 ? 28   A   B N7    1 
ATOM   522   C C5    . A   A 1 28   ? 148.684 136.930 144.680 1.00 103.91 ? 28   A   B C5    1 
ATOM   523   C C6    . A   A 1 28   ? 147.926 137.998 144.169 1.00 103.91 ? 28   A   B C6    1 
ATOM   524   N N6    . A   A 1 28   ? 148.184 139.282 144.432 1.00 103.91 ? 28   A   B N6    1 
ATOM   525   N N1    . A   A 1 28   ? 146.879 137.700 143.369 1.00 103.91 ? 28   A   B N1    1 
ATOM   526   C C2    . A   A 1 28   ? 146.619 136.413 143.106 1.00 103.91 ? 28   A   B C2    1 
ATOM   527   N N3    . A   A 1 28   ? 147.257 135.323 143.526 1.00 103.91 ? 28   A   B N3    1 
ATOM   528   C C4    . A   A 1 28   ? 148.291 135.654 144.318 1.00 103.91 ? 28   A   B C4    1 
ATOM   529   N N     . THR B 2 5    ? 113.712 162.485 143.792 1.00 29.87  ? 2    THR A N     1 
ATOM   530   C CA    . THR B 2 5    ? 114.969 161.752 143.711 1.00 29.87  ? 2    THR A CA    1 
ATOM   531   C C     . THR B 2 5    ? 115.880 162.342 142.641 1.00 29.87  ? 2    THR A C     1 
ATOM   532   O O     . THR B 2 5    ? 115.788 161.984 141.467 1.00 29.87  ? 2    THR A O     1 
ATOM   533   C CB    . THR B 2 5    ? 114.735 160.263 143.407 1.00 29.87  ? 2    THR A CB    1 
ATOM   534   O OG1   . THR B 2 5    ? 113.812 160.134 142.320 1.00 29.87  ? 2    THR A OG1   1 
ATOM   535   C CG2   . THR B 2 5    ? 114.175 159.553 144.629 1.00 29.87  ? 2    THR A CG2   1 
ATOM   536   N N     . GLN B 2 6    ? 116.757 163.251 143.055 1.00 27.84  ? 3    GLN A N     1 
ATOM   537   C CA    . GLN B 2 6    ? 117.677 163.890 142.131 1.00 27.84  ? 3    GLN A CA    1 
ATOM   538   C C     . GLN B 2 6    ? 118.951 163.064 141.979 1.00 27.84  ? 3    GLN A C     1 
ATOM   539   O O     . GLN B 2 6    ? 119.264 162.194 142.796 1.00 27.84  ? 3    GLN A O     1 
ATOM   540   C CB    . GLN B 2 6    ? 118.026 165.300 142.609 1.00 27.84  ? 3    GLN A CB    1 
ATOM   541   C CG    . GLN B 2 6    ? 116.872 166.292 142.558 1.00 27.84  ? 3    GLN A CG    1 
ATOM   542   C CD    . GLN B 2 6    ? 115.906 166.024 141.419 1.00 27.84  ? 3    GLN A CD    1 
ATOM   543   O OE1   . GLN B 2 6    ? 116.293 166.010 140.249 1.00 27.84  ? 3    GLN A OE1   1 
ATOM   544   N NE2   . GLN B 2 6    ? 114.640 165.808 141.756 1.00 27.84  ? 3    GLN A NE2   1 
ATOM   545   N N     . PHE B 2 7    ? 119.687 163.347 140.901 1.00 24.94  ? 4    PHE A N     1 
ATOM   546   C CA    . PHE B 2 7    ? 120.996 162.731 140.712 1.00 24.94  ? 4    PHE A CA    1 
ATOM   547   C C     . PHE B 2 7    ? 121.953 163.088 141.835 1.00 24.94  ? 4    PHE A C     1 
ATOM   548   O O     . PHE B 2 7    ? 122.801 162.272 142.212 1.00 24.94  ? 4    PHE A O     1 
ATOM   549   C CB    . PHE B 2 7    ? 121.600 163.165 139.378 1.00 24.94  ? 4    PHE A CB    1 
ATOM   550   C CG    . PHE B 2 7    ? 122.998 162.663 139.154 1.00 24.94  ? 4    PHE A CG    1 
ATOM   551   C CD1   . PHE B 2 7    ? 123.226 161.372 138.714 1.00 24.94  ? 4    PHE A CD1   1 
ATOM   552   C CD2   . PHE B 2 7    ? 124.086 163.485 139.391 1.00 24.94  ? 4    PHE A CD2   1 
ATOM   553   C CE1   . PHE B 2 7    ? 124.514 160.917 138.511 1.00 24.94  ? 4    PHE A CE1   1 
ATOM   554   C CE2   . PHE B 2 7    ? 125.372 163.033 139.191 1.00 24.94  ? 4    PHE A CE2   1 
ATOM   555   C CZ    . PHE B 2 7    ? 125.587 161.748 138.750 1.00 24.94  ? 4    PHE A CZ    1 
ATOM   556   N N     . GLU B 2 8    ? 121.835 164.298 142.376 1.00 23.90  ? 5    GLU A N     1 
ATOM   557   C CA    . GLU B 2 8    ? 122.810 164.789 143.334 1.00 23.90  ? 5    GLU A CA    1 
ATOM   558   C C     . GLU B 2 8    ? 122.634 164.142 144.703 1.00 23.90  ? 5    GLU A C     1 
ATOM   559   O O     . GLU B 2 8    ? 123.513 164.281 145.560 1.00 23.90  ? 5    GLU A O     1 
ATOM   560   C CB    . GLU B 2 8    ? 122.687 166.315 143.422 1.00 23.90  ? 5    GLU A CB    1 
ATOM   561   C CG    . GLU B 2 8    ? 123.744 167.015 144.246 1.00 23.90  ? 5    GLU A CG    1 
ATOM   562   C CD    . GLU B 2 8    ? 125.119 166.899 143.612 1.00 23.90  ? 5    GLU A CD    1 
ATOM   563   O OE1   . GLU B 2 8    ? 125.190 166.732 142.376 1.00 23.90  ? 5    GLU A OE1   1 
ATOM   564   O OE2   . GLU B 2 8    ? 126.132 166.982 144.336 1.00 23.90  ? 5    GLU A OE2   1 
ATOM   565   N N     . GLY B 2 9    ? 121.536 163.418 144.912 1.00 23.35  ? 6    GLY A N     1 
ATOM   566   C CA    . GLY B 2 9    ? 121.215 162.749 146.154 1.00 23.35  ? 6    GLY A CA    1 
ATOM   567   C C     . GLY B 2 9    ? 121.766 161.352 146.327 1.00 23.35  ? 6    GLY A C     1 
ATOM   568   O O     . GLY B 2 9    ? 121.420 160.685 147.306 1.00 23.35  ? 6    GLY A O     1 
ATOM   569   N N     . PHE B 2 10   ? 122.609 160.877 145.412 1.00 23.85  ? 7    PHE A N     1 
ATOM   570   C CA    . PHE B 2 10   ? 123.242 159.564 145.553 1.00 23.85  ? 7    PHE A CA    1 
ATOM   571   C C     . PHE B 2 10   ? 124.411 159.638 146.536 1.00 23.85  ? 7    PHE A C     1 
ATOM   572   O O     . PHE B 2 10   ? 125.564 159.354 146.212 1.00 23.85  ? 7    PHE A O     1 
ATOM   573   C CB    . PHE B 2 10   ? 123.694 159.041 144.194 1.00 23.85  ? 7    PHE A CB    1 
ATOM   574   C CG    . PHE B 2 10   ? 122.607 158.371 143.407 1.00 23.85  ? 7    PHE A CG    1 
ATOM   575   C CD1   . PHE B 2 10   ? 122.375 157.015 143.542 1.00 23.85  ? 7    PHE A CD1   1 
ATOM   576   C CD2   . PHE B 2 10   ? 121.820 159.095 142.530 1.00 23.85  ? 7    PHE A CD2   1 
ATOM   577   C CE1   . PHE B 2 10   ? 121.378 156.393 142.821 1.00 23.85  ? 7    PHE A CE1   1 
ATOM   578   C CE2   . PHE B 2 10   ? 120.821 158.478 141.806 1.00 23.85  ? 7    PHE A CE2   1 
ATOM   579   C CZ    . PHE B 2 10   ? 120.600 157.126 141.951 1.00 23.85  ? 7    PHE A CZ    1 
ATOM   580   N N     . THR B 2 11   ? 124.087 160.032 147.764 1.00 22.58  ? 8    THR A N     1 
ATOM   581   C CA    . THR B 2 11   ? 125.075 160.168 148.821 1.00 22.58  ? 8    THR A CA    1 
ATOM   582   C C     . THR B 2 11   ? 124.560 159.497 150.084 1.00 22.58  ? 8    THR A C     1 
ATOM   583   O O     . THR B 2 11   ? 123.349 159.408 150.309 1.00 22.58  ? 8    THR A O     1 
ATOM   584   C CB    . THR B 2 11   ? 125.394 161.636 149.113 1.00 22.58  ? 8    THR A CB    1 
ATOM   585   O OG1   . THR B 2 11   ? 126.324 161.717 150.200 1.00 22.58  ? 8    THR A OG1   1 
ATOM   586   C CG2   . THR B 2 11   ? 124.127 162.391 149.481 1.00 22.58  ? 8    THR A CG2   1 
ATOM   587   N N     . ASN B 2 12   ? 125.498 159.029 150.907 1.00 23.54  ? 9    ASN A N     1 
ATOM   588   C CA    . ASN B 2 12   ? 125.186 158.405 152.192 1.00 23.54  ? 9    ASN A CA    1 
ATOM   589   C C     . ASN B 2 12   ? 124.262 157.202 152.008 1.00 23.54  ? 9    ASN A C     1 
ATOM   590   O O     . ASN B 2 12   ? 123.264 157.040 152.712 1.00 23.54  ? 9    ASN A O     1 
ATOM   591   C CB    . ASN B 2 12   ? 124.579 159.427 153.159 1.00 23.54  ? 9    ASN A CB    1 
ATOM   592   C CG    . ASN B 2 12   ? 124.625 158.967 154.600 1.00 23.54  ? 9    ASN A CG    1 
ATOM   593   O OD1   . ASN B 2 12   ? 125.581 158.322 155.028 1.00 23.54  ? 9    ASN A OD1   1 
ATOM   594   N ND2   . ASN B 2 12   ? 123.587 159.298 155.359 1.00 23.54  ? 9    ASN A ND2   1 
ATOM   595   N N     . LEU B 2 13   ? 124.602 156.353 151.038 1.00 23.81  ? 10   LEU A N     1 
ATOM   596   C CA    . LEU B 2 13   ? 123.818 155.149 150.792 1.00 23.81  ? 10   LEU A CA    1 
ATOM   597   C C     . LEU B 2 13   ? 124.347 153.941 151.556 1.00 23.81  ? 10   LEU A C     1 
ATOM   598   O O     . LEU B 2 13   ? 123.555 153.173 152.113 1.00 23.81  ? 10   LEU A O     1 
ATOM   599   C CB    . LEU B 2 13   ? 123.774 154.836 149.294 1.00 23.81  ? 10   LEU A CB    1 
ATOM   600   C CG    . LEU B 2 13   ? 122.639 155.481 148.493 1.00 23.81  ? 10   LEU A CG    1 
ATOM   601   C CD1   . LEU B 2 13   ? 122.874 156.965 148.296 1.00 23.81  ? 10   LEU A CD1   1 
ATOM   602   C CD2   . LEU B 2 13   ? 122.459 154.785 147.156 1.00 23.81  ? 10   LEU A CD2   1 
ATOM   603   N N     . TYR B 2 14   ? 125.664 153.751 151.601 1.00 24.71  ? 11   TYR A N     1 
ATOM   604   C CA    . TYR B 2 14   ? 126.229 152.627 152.330 1.00 24.71  ? 11   TYR A CA    1 
ATOM   605   C C     . TYR B 2 14   ? 127.654 152.950 152.754 1.00 24.71  ? 11   TYR A C     1 
ATOM   606   O O     . TYR B 2 14   ? 128.311 153.818 152.175 1.00 24.71  ? 11   TYR A O     1 
ATOM   607   C CB    . TYR B 2 14   ? 126.191 151.339 151.500 1.00 24.71  ? 11   TYR A CB    1 
ATOM   608   C CG    . TYR B 2 14   ? 126.899 151.432 150.172 1.00 24.71  ? 11   TYR A CG    1 
ATOM   609   C CD1   . TYR B 2 14   ? 126.245 151.911 149.045 1.00 24.71  ? 11   TYR A CD1   1 
ATOM   610   C CD2   . TYR B 2 14   ? 128.214 151.019 150.038 1.00 24.71  ? 11   TYR A CD2   1 
ATOM   611   C CE1   . TYR B 2 14   ? 126.887 151.990 147.829 1.00 24.71  ? 11   TYR A CE1   1 
ATOM   612   C CE2   . TYR B 2 14   ? 128.862 151.092 148.830 1.00 24.71  ? 11   TYR A CE2   1 
ATOM   613   C CZ    . TYR B 2 14   ? 128.197 151.579 147.727 1.00 24.71  ? 11   TYR A CZ    1 
ATOM   614   O OH    . TYR B 2 14   ? 128.845 151.653 146.516 1.00 24.71  ? 11   TYR A OH    1 
ATOM   615   N N     . GLN B 2 15   ? 128.121 152.235 153.774 1.00 25.46  ? 12   GLN A N     1 
ATOM   616   C CA    . GLN B 2 15   ? 129.427 152.494 154.361 1.00 25.46  ? 12   GLN A CA    1 
ATOM   617   C C     . GLN B 2 15   ? 130.551 152.068 153.424 1.00 25.46  ? 12   GLN A C     1 
ATOM   618   O O     . GLN B 2 15   ? 130.448 151.074 152.700 1.00 25.46  ? 12   GLN A O     1 
ATOM   619   C CB    . GLN B 2 15   ? 129.562 151.758 155.694 1.00 25.46  ? 12   GLN A CB    1 
ATOM   620   C CG    . GLN B 2 15   ? 129.251 152.606 156.913 1.00 25.46  ? 12   GLN A CG    1 
ATOM   621   C CD    . GLN B 2 15   ? 129.241 151.798 158.195 1.00 25.46  ? 12   GLN A CD    1 
ATOM   622   O OE1   . GLN B 2 15   ? 130.291 151.411 158.707 1.00 25.46  ? 12   GLN A OE1   1 
ATOM   623   N NE2   . GLN B 2 15   ? 128.051 151.543 158.723 1.00 25.46  ? 12   GLN A NE2   1 
ATOM   624   N N     . VAL B 2 16   ? 131.636 152.838 153.447 1.00 25.06  ? 13   VAL A N     1 
ATOM   625   C CA    . VAL B 2 16   ? 132.850 152.531 152.702 1.00 25.06  ? 13   VAL A CA    1 
ATOM   626   C C     . VAL B 2 16   ? 134.032 152.680 153.648 1.00 25.06  ? 13   VAL A C     1 
ATOM   627   O O     . VAL B 2 16   ? 134.172 153.711 154.314 1.00 25.06  ? 13   VAL A O     1 
ATOM   628   C CB    . VAL B 2 16   ? 133.020 153.446 151.474 1.00 25.06  ? 13   VAL A CB    1 
ATOM   629   C CG1   . VAL B 2 16   ? 134.378 153.225 150.830 1.00 25.06  ? 13   VAL A CG1   1 
ATOM   630   C CG2   . VAL B 2 16   ? 131.906 153.201 150.469 1.00 25.06  ? 13   VAL A CG2   1 
ATOM   631   N N     . SER B 2 17   ? 134.877 151.655 153.709 1.00 25.26  ? 14   SER A N     1 
ATOM   632   C CA    . SER B 2 17   ? 136.037 151.647 154.588 1.00 25.26  ? 14   SER A CA    1 
ATOM   633   C C     . SER B 2 17   ? 137.310 151.806 153.767 1.00 25.26  ? 14   SER A C     1 
ATOM   634   O O     . SER B 2 17   ? 137.519 151.081 152.790 1.00 25.26  ? 14   SER A O     1 
ATOM   635   C CB    . SER B 2 17   ? 136.093 150.356 155.405 1.00 25.26  ? 14   SER A CB    1 
ATOM   636   O OG    . SER B 2 17   ? 134.980 150.255 156.276 1.00 25.26  ? 14   SER A OG    1 
ATOM   637   N N     . LYS B 2 18   ? 138.153 152.755 154.167 1.00 25.65  ? 15   LYS A N     1 
ATOM   638   C CA    . LYS B 2 18   ? 139.421 153.014 153.506 1.00 25.65  ? 15   LYS A CA    1 
ATOM   639   C C     . LYS B 2 18   ? 140.532 153.066 154.544 1.00 25.65  ? 15   LYS A C     1 
ATOM   640   O O     . LYS B 2 18   ? 140.306 153.436 155.699 1.00 25.65  ? 15   LYS A O     1 
ATOM   641   C CB    . LYS B 2 18   ? 139.389 154.328 152.715 1.00 25.65  ? 15   LYS A CB    1 
ATOM   642   C CG    . LYS B 2 18   ? 138.525 154.288 151.468 1.00 25.65  ? 15   LYS A CG    1 
ATOM   643   C CD    . LYS B 2 18   ? 138.726 155.534 150.623 1.00 25.65  ? 15   LYS A CD    1 
ATOM   644   C CE    . LYS B 2 18   ? 137.924 155.466 149.336 1.00 25.65  ? 15   LYS A CE    1 
ATOM   645   N NZ    . LYS B 2 18   ? 138.442 154.427 148.406 1.00 25.65  ? 15   LYS A NZ    1 
ATOM   646   N N     . THR B 2 19   ? 141.736 152.693 154.123 1.00 25.44  ? 16   THR A N     1 
ATOM   647   C CA    . THR B 2 19   ? 142.911 152.695 154.985 1.00 25.44  ? 16   THR A CA    1 
ATOM   648   C C     . THR B 2 19   ? 143.909 153.719 154.462 1.00 25.44  ? 16   THR A C     1 
ATOM   649   O O     . THR B 2 19   ? 144.281 153.683 153.285 1.00 25.44  ? 16   THR A O     1 
ATOM   650   C CB    . THR B 2 19   ? 143.553 151.312 155.052 1.00 25.44  ? 16   THR A CB    1 
ATOM   651   O OG1   . THR B 2 19   ? 142.657 150.399 155.698 1.00 25.44  ? 16   THR A OG1   1 
ATOM   652   C CG2   . THR B 2 19   ? 144.852 151.374 155.837 1.00 25.44  ? 16   THR A CG2   1 
ATOM   653   N N     . LEU B 2 20   ? 144.338 154.620 155.336 1.00 24.84  ? 17   LEU A N     1 
ATOM   654   C CA    . LEU B 2 20   ? 145.292 155.660 154.986 1.00 24.84  ? 17   LEU A CA    1 
ATOM   655   C C     . LEU B 2 20   ? 146.693 155.266 155.439 1.00 24.84  ? 17   LEU A C     1 
ATOM   656   O O     . LEU B 2 20   ? 146.875 154.436 156.333 1.00 24.84  ? 17   LEU A O     1 
ATOM   657   C CB    . LEU B 2 20   ? 144.890 156.992 155.619 1.00 24.84  ? 17   LEU A CB    1 
ATOM   658   C CG    . LEU B 2 20   ? 143.866 157.868 154.894 1.00 24.84  ? 17   LEU A CG    1 
ATOM   659   C CD1   . LEU B 2 20   ? 142.528 157.168 154.754 1.00 24.84  ? 17   LEU A CD1   1 
ATOM   660   C CD2   . LEU B 2 20   ? 143.696 159.185 155.627 1.00 24.84  ? 17   LEU A CD2   1 
ATOM   661   N N     . ARG B 2 21   ? 147.692 155.877 154.809 1.00 25.01  ? 18   ARG A N     1 
ATOM   662   C CA    . ARG B 2 21   ? 149.087 155.626 155.133 1.00 25.01  ? 18   ARG A CA    1 
ATOM   663   C C     . ARG B 2 21   ? 149.824 156.949 155.266 1.00 25.01  ? 18   ARG A C     1 
ATOM   664   O O     . ARG B 2 21   ? 149.549 157.907 154.539 1.00 25.01  ? 18   ARG A O     1 
ATOM   665   C CB    . ARG B 2 21   ? 149.770 154.758 154.072 1.00 25.01  ? 18   ARG A CB    1 
ATOM   666   C CG    . ARG B 2 21   ? 149.332 153.306 154.067 1.00 25.01  ? 18   ARG A CG    1 
ATOM   667   C CD    . ARG B 2 21   ? 149.952 152.565 152.897 1.00 25.01  ? 18   ARG A CD    1 
ATOM   668   N NE    . ARG B 2 21   ? 149.410 153.018 151.622 1.00 25.01  ? 18   ARG A NE    1 
ATOM   669   C CZ    . ARG B 2 21   ? 149.729 152.497 150.446 1.00 25.01  ? 18   ARG A CZ    1 
ATOM   670   N NH1   . ARG B 2 21   ? 150.590 151.497 150.344 1.00 25.01  ? 18   ARG A NH1   1 
ATOM   671   N NH2   . ARG B 2 21   ? 149.172 152.991 149.344 1.00 25.01  ? 18   ARG A NH2   1 
ATOM   672   N N     . PHE B 2 22   ? 150.767 156.991 156.203 1.00 24.17  ? 19   PHE A N     1 
ATOM   673   C CA    . PHE B 2 22   ? 151.521 158.204 156.479 1.00 24.17  ? 19   PHE A CA    1 
ATOM   674   C C     . PHE B 2 22   ? 152.922 157.828 156.933 1.00 24.17  ? 19   PHE A C     1 
ATOM   675   O O     . PHE B 2 22   ? 153.174 156.702 157.371 1.00 24.17  ? 19   PHE A O     1 
ATOM   676   C CB    . PHE B 2 22   ? 150.838 159.065 157.545 1.00 24.17  ? 19   PHE A CB    1 
ATOM   677   C CG    . PHE B 2 22   ? 149.458 159.524 157.168 1.00 24.17  ? 19   PHE A CG    1 
ATOM   678   C CD1   . PHE B 2 22   ? 149.281 160.611 156.333 1.00 24.17  ? 19   PHE A CD1   1 
ATOM   679   C CD2   . PHE B 2 22   ? 148.340 158.878 157.663 1.00 24.17  ? 19   PHE A CD2   1 
ATOM   680   C CE1   . PHE B 2 22   ? 148.018 161.040 155.991 1.00 24.17  ? 19   PHE A CE1   1 
ATOM   681   C CE2   . PHE B 2 22   ? 147.072 159.303 157.323 1.00 24.17  ? 19   PHE A CE2   1 
ATOM   682   C CZ    . PHE B 2 22   ? 146.912 160.386 156.485 1.00 24.17  ? 19   PHE A CZ    1 
ATOM   683   N N     . GLU B 2 23   ? 153.834 158.788 156.823 1.00 23.08  ? 20   GLU A N     1 
ATOM   684   C CA    . GLU B 2 23   ? 155.215 158.615 157.252 1.00 23.08  ? 20   GLU A CA    1 
ATOM   685   C C     . GLU B 2 23   ? 155.399 159.286 158.606 1.00 23.08  ? 20   GLU A C     1 
ATOM   686   O O     . GLU B 2 23   ? 155.127 160.483 158.752 1.00 23.08  ? 20   GLU A O     1 
ATOM   687   C CB    . GLU B 2 23   ? 156.186 159.201 156.229 1.00 23.08  ? 20   GLU A CB    1 
ATOM   688   C CG    . GLU B 2 23   ? 157.633 159.203 156.687 1.00 23.08  ? 20   GLU A CG    1 
ATOM   689   C CD    . GLU B 2 23   ? 158.468 160.250 155.976 1.00 23.08  ? 20   GLU A CD    1 
ATOM   690   O OE1   . GLU B 2 23   ? 158.183 160.538 154.795 1.00 23.08  ? 20   GLU A OE1   1 
ATOM   691   O OE2   . GLU B 2 23   ? 159.409 160.785 156.599 1.00 23.08  ? 20   GLU A OE2   1 
ATOM   692   N N     . LEU B 2 24   ? 155.857 158.518 159.589 1.00 22.65  ? 21   LEU A N     1 
ATOM   693   C CA    . LEU B 2 24   ? 156.085 159.048 160.926 1.00 22.65  ? 21   LEU A CA    1 
ATOM   694   C C     . LEU B 2 24   ? 157.516 159.556 161.034 1.00 22.65  ? 21   LEU A C     1 
ATOM   695   O O     . LEU B 2 24   ? 158.469 158.778 160.911 1.00 22.65  ? 21   LEU A O     1 
ATOM   696   C CB    . LEU B 2 24   ? 155.810 157.979 161.979 1.00 22.65  ? 21   LEU A CB    1 
ATOM   697   C CG    . LEU B 2 24   ? 154.377 157.454 162.040 1.00 22.65  ? 21   LEU A CG    1 
ATOM   698   C CD1   . LEU B 2 24   ? 154.180 156.586 163.269 1.00 22.65  ? 21   LEU A CD1   1 
ATOM   699   C CD2   . LEU B 2 24   ? 153.385 158.605 162.030 1.00 22.65  ? 21   LEU A CD2   1 
ATOM   700   N N     . ILE B 2 25   ? 157.667 160.857 161.262 1.00 24.79  ? 22   ILE A N     1 
ATOM   701   C CA    . ILE B 2 25   ? 158.973 161.483 161.439 1.00 24.79  ? 22   ILE A CA    1 
ATOM   702   C C     . ILE B 2 25   ? 159.224 161.603 162.940 1.00 24.79  ? 22   ILE A C     1 
ATOM   703   O O     . ILE B 2 25   ? 158.449 162.284 163.632 1.00 24.79  ? 22   ILE A O     1 
ATOM   704   C CB    . ILE B 2 25   ? 159.040 162.853 160.753 1.00 24.79  ? 22   ILE A CB    1 
ATOM   705   C CG1   . ILE B 2 25   ? 158.645 162.733 159.281 1.00 24.79  ? 22   ILE A CG1   1 
ATOM   706   C CG2   . ILE B 2 25   ? 160.435 163.441 160.883 1.00 24.79  ? 22   ILE A CG2   1 
ATOM   707   C CD1   . ILE B 2 25   ? 158.938 163.972 158.466 1.00 24.79  ? 22   ILE A CD1   1 
ATOM   708   N N     . PRO B 2 26   ? 160.256 160.959 163.482 1.00 27.94  ? 23   PRO A N     1 
ATOM   709   C CA    . PRO B 2 26   ? 160.519 161.066 164.923 1.00 27.94  ? 23   PRO A CA    1 
ATOM   710   C C     . PRO B 2 26   ? 160.762 162.511 165.335 1.00 27.94  ? 23   PRO A C     1 
ATOM   711   O O     . PRO B 2 26   ? 161.618 163.200 164.776 1.00 27.94  ? 23   PRO A O     1 
ATOM   712   C CB    . PRO B 2 26   ? 161.770 160.200 165.121 1.00 27.94  ? 23   PRO A CB    1 
ATOM   713   C CG    . PRO B 2 26   ? 162.359 160.037 163.754 1.00 27.94  ? 23   PRO A CG    1 
ATOM   714   C CD    . PRO B 2 26   ? 161.203 160.055 162.812 1.00 27.94  ? 23   PRO A CD    1 
ATOM   715   N N     . GLN B 2 27   ? 159.996 162.964 166.323 1.00 28.48  ? 24   GLN A N     1 
ATOM   716   C CA    . GLN B 2 27   ? 160.067 164.331 166.820 1.00 28.48  ? 24   GLN A CA    1 
ATOM   717   C C     . GLN B 2 27   ? 160.774 164.346 168.167 1.00 28.48  ? 24   GLN A C     1 
ATOM   718   O O     . GLN B 2 27   ? 160.404 163.596 169.075 1.00 28.48  ? 24   GLN A O     1 
ATOM   719   C CB    . GLN B 2 27   ? 158.670 164.940 166.952 1.00 28.48  ? 24   GLN A CB    1 
ATOM   720   C CG    . GLN B 2 27   ? 158.043 165.388 165.640 1.00 28.48  ? 24   GLN A CG    1 
ATOM   721   C CD    . GLN B 2 27   ? 159.066 165.760 164.582 1.00 28.48  ? 24   GLN A CD    1 
ATOM   722   O OE1   . GLN B 2 27   ? 159.869 166.676 164.768 1.00 28.48  ? 24   GLN A OE1   1 
ATOM   723   N NE2   . GLN B 2 27   ? 159.040 165.049 163.462 1.00 28.48  ? 24   GLN A NE2   1 
ATOM   724   N N     . GLY B 2 28   ? 161.781 165.207 168.295 1.00 28.94  ? 25   GLY A N     1 
ATOM   725   C CA    . GLY B 2 28   ? 162.529 165.284 169.533 1.00 28.94  ? 25   GLY A CA    1 
ATOM   726   C C     . GLY B 2 28   ? 163.477 164.108 169.702 1.00 28.94  ? 25   GLY A C     1 
ATOM   727   O O     . GLY B 2 28   ? 164.025 163.572 168.738 1.00 28.94  ? 25   GLY A O     1 
ATOM   728   N N     . LYS B 2 29   ? 163.666 163.706 170.957 1.00 48.55  ? 26   LYS A N     1 
ATOM   729   C CA    . LYS B 2 29   ? 164.567 162.617 171.302 1.00 48.55  ? 26   LYS A CA    1 
ATOM   730   C C     . LYS B 2 29   ? 163.875 161.260 171.317 1.00 48.55  ? 26   LYS A C     1 
ATOM   731   O O     . LYS B 2 29   ? 164.353 160.339 171.989 1.00 48.55  ? 26   LYS A O     1 
ATOM   732   C CB    . LYS B 2 29   ? 165.223 162.886 172.658 1.00 32.42  ? 26   LYS A CB    1 
ATOM   733   C CG    . LYS B 2 29   ? 166.220 164.033 172.647 1.00 32.42  ? 26   LYS A CG    1 
ATOM   734   C CD    . LYS B 2 29   ? 167.096 164.015 173.889 1.00 32.42  ? 26   LYS A CD    1 
ATOM   735   C CE    . LYS B 2 29   ? 168.027 165.216 173.925 1.00 32.42  ? 26   LYS A CE    1 
ATOM   736   N NZ    . LYS B 2 29   ? 168.954 165.165 175.089 1.00 32.42  ? 26   LYS A NZ    1 
ATOM   737   N N     . THR B 2 30   ? 162.760 161.114 170.596 1.00 48.55  ? 27   THR A N     1 
ATOM   738   C CA    . THR B 2 30   ? 162.080 159.824 170.557 1.00 48.55  ? 27   THR A CA    1 
ATOM   739   C C     . THR B 2 30   ? 162.860 158.798 169.746 1.00 48.55  ? 27   THR A C     1 
ATOM   740   O O     . THR B 2 30   ? 162.686 157.591 169.949 1.00 48.55  ? 27   THR A O     1 
ATOM   741   C CB    . THR B 2 30   ? 160.670 159.980 169.990 1.00 48.55  ? 27   THR A CB    1 
ATOM   742   O OG1   . THR B 2 30   ? 159.998 158.717 170.032 1.00 48.55  ? 27   THR A OG1   1 
ATOM   743   C CG2   . THR B 2 30   ? 160.719 160.467 168.557 1.00 48.55  ? 27   THR A CG2   1 
ATOM   744   N N     . LEU B 2 31   ? 163.716 159.250 168.828 1.00 48.55  ? 28   LEU A N     1 
ATOM   745   C CA    . LEU B 2 31   ? 164.517 158.311 168.052 1.00 48.55  ? 28   LEU A CA    1 
ATOM   746   C C     . LEU B 2 31   ? 165.624 157.701 168.901 1.00 48.55  ? 28   LEU A C     1 
ATOM   747   O O     . LEU B 2 31   ? 165.928 156.509 168.776 1.00 48.55  ? 28   LEU A O     1 
ATOM   748   C CB    . LEU B 2 31   ? 165.102 159.009 166.825 1.00 48.55  ? 28   LEU A CB    1 
ATOM   749   C CG    . LEU B 2 31   ? 165.860 158.112 165.848 1.00 48.55  ? 28   LEU A CG    1 
ATOM   750   C CD1   . LEU B 2 31   ? 164.980 156.960 165.398 1.00 48.55  ? 28   LEU A CD1   1 
ATOM   751   C CD2   . LEU B 2 31   ? 166.351 158.913 164.654 1.00 48.55  ? 28   LEU A CD2   1 
ATOM   752   N N     . LYS B 2 32   ? 166.243 158.506 169.768 1.00 48.55  ? 29   LYS A N     1 
ATOM   753   C CA    . LYS B 2 32   ? 167.296 157.990 170.636 1.00 48.55  ? 29   LYS A CA    1 
ATOM   754   C C     . LYS B 2 32   ? 166.744 156.977 171.630 1.00 48.55  ? 29   LYS A C     1 
ATOM   755   O O     . LYS B 2 32   ? 167.385 155.957 171.909 1.00 48.55  ? 29   LYS A O     1 
ATOM   756   C CB    . LYS B 2 32   ? 167.982 159.142 171.368 1.00 48.55  ? 29   LYS A CB    1 
ATOM   757   C CG    . LYS B 2 32   ? 169.128 158.711 172.266 1.00 48.55  ? 29   LYS A CG    1 
ATOM   758   C CD    . LYS B 2 32   ? 170.253 158.084 171.460 1.00 48.55  ? 29   LYS A CD    1 
ATOM   759   C CE    . LYS B 2 32   ? 170.964 159.121 170.607 1.00 48.55  ? 29   LYS A CE    1 
ATOM   760   N NZ    . LYS B 2 32   ? 172.109 158.534 169.858 1.00 48.55  ? 29   LYS A NZ    1 
ATOM   761   N N     . HIS B 2 33   ? 165.556 157.242 172.179 1.00 48.55  ? 30   HIS A N     1 
ATOM   762   C CA    . HIS B 2 33   ? 164.962 156.320 173.141 1.00 48.55  ? 30   HIS A CA    1 
ATOM   763   C C     . HIS B 2 33   ? 164.605 154.991 172.489 1.00 48.55  ? 30   HIS A C     1 
ATOM   764   O O     . HIS B 2 33   ? 164.774 153.928 173.098 1.00 48.55  ? 30   HIS A O     1 
ATOM   765   C CB    . HIS B 2 33   ? 163.726 156.952 173.780 1.00 48.55  ? 30   HIS A CB    1 
ATOM   766   C CG    . HIS B 2 33   ? 164.041 157.952 174.848 1.00 48.55  ? 30   HIS A CG    1 
ATOM   767   N ND1   . HIS B 2 33   ? 164.749 157.628 175.985 1.00 48.55  ? 30   HIS A ND1   1 
ATOM   768   C CD2   . HIS B 2 33   ? 163.743 159.269 174.954 1.00 48.55  ? 30   HIS A CD2   1 
ATOM   769   C CE1   . HIS B 2 33   ? 164.874 158.702 176.745 1.00 48.55  ? 30   HIS A CE1   1 
ATOM   770   N NE2   . HIS B 2 33   ? 164.272 159.711 176.142 1.00 48.55  ? 30   HIS A NE2   1 
ATOM   771   N N     . ILE B 2 34   ? 164.100 155.029 171.254 1.00 48.55  ? 31   ILE A N     1 
ATOM   772   C CA    . ILE B 2 34   ? 163.723 153.798 170.563 1.00 48.55  ? 31   ILE A CA    1 
ATOM   773   C C     . ILE B 2 34   ? 164.952 152.933 170.310 1.00 48.55  ? 31   ILE A C     1 
ATOM   774   O O     . ILE B 2 34   ? 164.950 151.726 170.576 1.00 48.55  ? 31   ILE A O     1 
ATOM   775   C CB    . ILE B 2 34   ? 162.981 154.123 169.255 1.00 48.55  ? 31   ILE A CB    1 
ATOM   776   C CG1   . ILE B 2 34   ? 161.519 154.459 169.541 1.00 48.55  ? 31   ILE A CG1   1 
ATOM   777   C CG2   . ILE B 2 34   ? 163.072 152.961 168.280 1.00 48.55  ? 31   ILE A CG2   1 
ATOM   778   C CD1   . ILE B 2 34   ? 160.815 155.125 168.385 1.00 48.55  ? 31   ILE A CD1   1 
ATOM   779   N N     . GLN B 2 35   ? 166.022 153.542 169.795 1.00 48.55  ? 32   GLN A N     1 
ATOM   780   C CA    . GLN B 2 35   ? 167.242 152.788 169.526 1.00 48.55  ? 32   GLN A CA    1 
ATOM   781   C C     . GLN B 2 35   ? 167.878 152.284 170.815 1.00 48.55  ? 32   GLN A C     1 
ATOM   782   O O     . GLN B 2 35   ? 168.435 151.180 170.850 1.00 48.55  ? 32   GLN A O     1 
ATOM   783   C CB    . GLN B 2 35   ? 168.231 153.651 168.742 1.00 48.55  ? 32   GLN A CB    1 
ATOM   784   C CG    . GLN B 2 35   ? 168.039 153.601 167.236 1.00 48.55  ? 32   GLN A CG    1 
ATOM   785   C CD    . GLN B 2 35   ? 168.534 154.855 166.545 1.00 48.55  ? 32   GLN A CD    1 
ATOM   786   O OE1   . GLN B 2 35   ? 169.464 155.510 167.015 1.00 48.55  ? 32   GLN A OE1   1 
ATOM   787   N NE2   . GLN B 2 35   ? 167.913 155.196 165.422 1.00 48.55  ? 32   GLN A NE2   1 
ATOM   788   N N     . GLU B 2 36   ? 167.815 153.083 171.883 1.00 48.55  ? 33   GLU A N     1 
ATOM   789   C CA    . GLU B 2 36   ? 168.411 152.671 173.151 1.00 48.55  ? 33   GLU A CA    1 
ATOM   790   C C     . GLU B 2 36   ? 167.733 151.421 173.698 1.00 48.55  ? 33   GLU A C     1 
ATOM   791   O O     . GLU B 2 36   ? 168.407 150.493 174.160 1.00 48.55  ? 33   GLU A O     1 
ATOM   792   C CB    . GLU B 2 36   ? 168.335 153.815 174.162 1.00 48.55  ? 33   GLU A CB    1 
ATOM   793   C CG    . GLU B 2 36   ? 169.151 153.597 175.429 1.00 48.55  ? 33   GLU A CG    1 
ATOM   794   C CD    . GLU B 2 36   ? 168.398 152.818 176.489 1.00 48.55  ? 33   GLU A CD    1 
ATOM   795   O OE1   . GLU B 2 36   ? 167.153 152.908 176.523 1.00 48.55  ? 33   GLU A OE1   1 
ATOM   796   O OE2   . GLU B 2 36   ? 169.051 152.114 177.288 1.00 48.55  ? 33   GLU A OE2   1 
ATOM   797   N N     . GLN B 2 37   ? 166.401 151.376 173.657 1.00 48.55  ? 34   GLN A N     1 
ATOM   798   C CA    . GLN B 2 37   ? 165.683 150.193 174.110 1.00 48.55  ? 34   GLN A CA    1 
ATOM   799   C C     . GLN B 2 37   ? 165.607 149.124 173.023 1.00 48.55  ? 34   GLN A C     1 
ATOM   800   O O     . GLN B 2 37   ? 165.359 147.954 173.331 1.00 48.55  ? 34   GLN A O     1 
ATOM   801   C CB    . GLN B 2 37   ? 164.281 150.597 174.584 1.00 48.55  ? 34   GLN A CB    1 
ATOM   802   C CG    . GLN B 2 37   ? 163.344 149.462 174.994 1.00 48.55  ? 34   GLN A CG    1 
ATOM   803   C CD    . GLN B 2 37   ? 163.999 148.422 175.889 1.00 48.55  ? 34   GLN A CD    1 
ATOM   804   O OE1   . GLN B 2 37   ? 163.770 147.222 175.731 1.00 48.55  ? 34   GLN A OE1   1 
ATOM   805   N NE2   . GLN B 2 37   ? 164.788 148.878 176.857 1.00 48.55  ? 34   GLN A NE2   1 
ATOM   806   N N     . GLY B 2 38   ? 165.866 149.490 171.772 1.00 48.55  ? 35   GLY A N     1 
ATOM   807   C CA    . GLY B 2 38   ? 165.908 148.524 170.688 1.00 48.55  ? 35   GLY A CA    1 
ATOM   808   C C     . GLY B 2 38   ? 164.593 147.868 170.326 1.00 48.55  ? 35   GLY A C     1 
ATOM   809   O O     . GLY B 2 38   ? 164.549 146.645 170.139 1.00 48.55  ? 35   GLY A O     1 
ATOM   810   N N     . PHE B 2 39   ? 163.513 148.647 170.227 1.00 48.55  ? 36   PHE A N     1 
ATOM   811   C CA    . PHE B 2 39   ? 162.258 148.098 169.723 1.00 48.55  ? 36   PHE A CA    1 
ATOM   812   C C     . PHE B 2 39   ? 162.386 147.660 168.269 1.00 48.55  ? 36   PHE A C     1 
ATOM   813   O O     . PHE B 2 39   ? 161.846 146.618 167.881 1.00 48.55  ? 36   PHE A O     1 
ATOM   814   C CB    . PHE B 2 39   ? 161.129 149.118 169.867 1.00 48.55  ? 36   PHE A CB    1 
ATOM   815   C CG    . PHE B 2 39   ? 160.806 149.477 171.287 1.00 48.55  ? 36   PHE A CG    1 
ATOM   816   C CD1   . PHE B 2 39   ? 160.407 148.504 172.186 1.00 48.55  ? 36   PHE A CD1   1 
ATOM   817   C CD2   . PHE B 2 39   ? 160.879 150.789 171.718 1.00 48.55  ? 36   PHE A CD2   1 
ATOM   818   C CE1   . PHE B 2 39   ? 160.099 148.831 173.490 1.00 48.55  ? 36   PHE A CE1   1 
ATOM   819   C CE2   . PHE B 2 39   ? 160.573 151.122 173.021 1.00 48.55  ? 36   PHE A CE2   1 
ATOM   820   C CZ    . PHE B 2 39   ? 160.179 150.142 173.908 1.00 48.55  ? 36   PHE A CZ    1 
ATOM   821   N N     . ILE B 2 40   ? 163.085 148.448 167.449 1.00 48.55  ? 37   ILE A N     1 
ATOM   822   C CA    . ILE B 2 40   ? 163.175 148.151 166.021 1.00 48.55  ? 37   ILE A CA    1 
ATOM   823   C C     . ILE B 2 40   ? 163.910 146.836 165.791 1.00 48.55  ? 37   ILE A C     1 
ATOM   824   O O     . ILE B 2 40   ? 163.502 146.013 164.962 1.00 48.55  ? 37   ILE A O     1 
ATOM   825   C CB    . ILE B 2 40   ? 163.846 149.315 165.270 1.00 48.55  ? 37   ILE A CB    1 
ATOM   826   C CG1   . ILE B 2 40   ? 165.070 149.819 166.037 1.00 48.55  ? 37   ILE A CG1   1 
ATOM   827   C CG2   . ILE B 2 40   ? 162.854 150.442 165.042 1.00 48.55  ? 37   ILE A CG2   1 
ATOM   828   C CD1   . ILE B 2 40   ? 165.871 150.862 165.289 1.00 48.55  ? 37   ILE A CD1   1 
ATOM   829   N N     . GLU B 2 41   ? 165.011 146.620 166.515 1.00 48.55  ? 38   GLU A N     1 
ATOM   830   C CA    . GLU B 2 41   ? 165.779 145.392 166.340 1.00 48.55  ? 38   GLU A CA    1 
ATOM   831   C C     . GLU B 2 41   ? 164.985 144.170 166.785 1.00 48.55  ? 38   GLU A C     1 
ATOM   832   O O     . GLU B 2 41   ? 165.025 143.125 166.126 1.00 48.55  ? 38   GLU A O     1 
ATOM   833   C CB    . GLU B 2 41   ? 167.099 145.485 167.104 1.00 48.55  ? 38   GLU A CB    1 
ATOM   834   C CG    . GLU B 2 41   ? 168.077 146.490 166.522 1.00 48.55  ? 38   GLU A CG    1 
ATOM   835   C CD    . GLU B 2 41   ? 169.211 146.818 167.471 1.00 48.55  ? 38   GLU A CD    1 
ATOM   836   O OE1   . GLU B 2 41   ? 170.163 146.015 167.561 1.00 48.55  ? 38   GLU A OE1   1 
ATOM   837   O OE2   . GLU B 2 41   ? 169.151 147.879 168.127 1.00 48.55  ? 38   GLU A OE2   1 
ATOM   838   N N     . GLU B 2 42   ? 164.264 144.279 167.903 1.00 48.55  ? 39   GLU A N     1 
ATOM   839   C CA    . GLU B 2 42   ? 163.446 143.162 168.363 1.00 48.55  ? 39   GLU A CA    1 
ATOM   840   C C     . GLU B 2 42   ? 162.328 142.861 167.375 1.00 48.55  ? 39   GLU A C     1 
ATOM   841   O O     . GLU B 2 42   ? 162.023 141.693 167.106 1.00 48.55  ? 39   GLU A O     1 
ATOM   842   C CB    . GLU B 2 42   ? 162.879 143.466 169.751 1.00 48.55  ? 39   GLU A CB    1 
ATOM   843   C CG    . GLU B 2 42   ? 162.359 142.251 170.510 1.00 48.55  ? 39   GLU A CG    1 
ATOM   844   C CD    . GLU B 2 42   ? 160.994 141.792 170.036 1.00 48.55  ? 39   GLU A CD    1 
ATOM   845   O OE1   . GLU B 2 42   ? 160.187 142.651 169.621 1.00 48.55  ? 39   GLU A OE1   1 
ATOM   846   O OE2   . GLU B 2 42   ? 160.726 140.573 170.082 1.00 48.55  ? 39   GLU A OE2   1 
ATOM   847   N N     . ASP B 2 43   ? 161.702 143.903 166.824 1.00 48.55  ? 40   ASP A N     1 
ATOM   848   C CA    . ASP B 2 43   ? 160.649 143.697 165.836 1.00 48.55  ? 40   ASP A CA    1 
ATOM   849   C C     . ASP B 2 43   ? 161.209 143.111 164.546 1.00 48.55  ? 40   ASP A C     1 
ATOM   850   O O     . ASP B 2 43   ? 160.531 142.329 163.869 1.00 48.55  ? 40   ASP A O     1 
ATOM   851   C CB    . ASP B 2 43   ? 159.924 145.014 165.564 1.00 48.55  ? 40   ASP A CB    1 
ATOM   852   C CG    . ASP B 2 43   ? 159.090 145.473 166.744 1.00 48.55  ? 40   ASP A CG    1 
ATOM   853   O OD1   . ASP B 2 43   ? 158.567 144.607 167.477 1.00 48.55  ? 40   ASP A OD1   1 
ATOM   854   O OD2   . ASP B 2 43   ? 158.962 146.699 166.944 1.00 48.55  ? 40   ASP A OD2   1 
ATOM   855   N N     . LYS B 2 44   ? 162.440 143.483 164.186 1.00 48.55  ? 41   LYS A N     1 
ATOM   856   C CA    . LYS B 2 44   ? 163.069 142.910 163.000 1.00 48.55  ? 41   LYS A CA    1 
ATOM   857   C C     . LYS B 2 44   ? 163.276 141.410 163.159 1.00 48.55  ? 41   LYS A C     1 
ATOM   858   O O     . LYS B 2 44   ? 163.043 140.640 162.220 1.00 48.55  ? 41   LYS A O     1 
ATOM   859   C CB    . LYS B 2 44   ? 164.401 143.606 162.721 1.00 48.55  ? 41   LYS A CB    1 
ATOM   860   C CG    . LYS B 2 44   ? 165.110 143.107 161.472 1.00 48.55  ? 41   LYS A CG    1 
ATOM   861   C CD    . LYS B 2 44   ? 166.114 144.125 160.959 1.00 48.55  ? 41   LYS A CD    1 
ATOM   862   C CE    . LYS B 2 44   ? 167.307 144.238 161.893 1.00 48.55  ? 41   LYS A CE    1 
ATOM   863   N NZ    . LYS B 2 44   ? 168.124 142.994 161.899 1.00 48.55  ? 41   LYS A NZ    1 
ATOM   864   N N     . ALA B 2 45   ? 163.720 140.978 164.340 1.00 48.55  ? 42   ALA A N     1 
ATOM   865   C CA    . ALA B 2 45   ? 163.918 139.554 164.582 1.00 48.55  ? 42   ALA A CA    1 
ATOM   866   C C     . ALA B 2 45   ? 162.600 138.795 164.514 1.00 48.55  ? 42   ALA A C     1 
ATOM   867   O O     . ALA B 2 45   ? 162.550 137.671 164.001 1.00 48.55  ? 42   ALA A O     1 
ATOM   868   C CB    . ALA B 2 45   ? 164.593 139.340 165.936 1.00 48.55  ? 42   ALA A CB    1 
ATOM   869   N N     . ARG B 2 46   ? 161.523 139.391 165.031 1.00 51.15  ? 43   ARG A N     1 
ATOM   870   C CA    . ARG B 2 46   ? 160.231 138.712 165.039 1.00 51.15  ? 43   ARG A CA    1 
ATOM   871   C C     . ARG B 2 46   ? 159.740 138.435 163.624 1.00 51.15  ? 43   ARG A C     1 
ATOM   872   O O     . ARG B 2 46   ? 159.212 137.353 163.343 1.00 51.15  ? 43   ARG A O     1 
ATOM   873   C CB    . ARG B 2 46   ? 159.209 139.542 165.812 1.00 51.15  ? 43   ARG A CB    1 
ATOM   874   C CG    . ARG B 2 46   ? 157.947 138.786 166.165 1.00 51.15  ? 43   ARG A CG    1 
ATOM   875   C CD    . ARG B 2 46   ? 157.979 138.325 167.610 1.00 51.15  ? 43   ARG A CD    1 
ATOM   876   N NE    . ARG B 2 46   ? 158.073 139.445 168.537 1.00 51.15  ? 43   ARG A NE    1 
ATOM   877   C CZ    . ARG B 2 46   ? 157.047 139.945 169.212 1.00 51.15  ? 43   ARG A CZ    1 
ATOM   878   N NH1   . ARG B 2 46   ? 155.830 139.439 169.093 1.00 51.15  ? 43   ARG A NH1   1 
ATOM   879   N NH2   . ARG B 2 46   ? 157.247 140.977 170.027 1.00 51.15  ? 43   ARG A NH2   1 
ATOM   880   N N     . ASN B 2 47   ? 159.827 139.433 162.746 1.00 52.22  ? 44   ASN A N     1 
ATOM   881   C CA    . ASN B 2 47   ? 159.473 139.214 161.321 1.00 52.22  ? 44   ASN A CA    1 
ATOM   882   C C     . ASN B 2 47   ? 160.493 138.255 160.713 1.00 52.22  ? 44   ASN A C     1 
ATOM   883   O O     . ASN B 2 47   ? 160.119 137.503 159.792 1.00 52.22  ? 44   ASN A O     1 
ATOM   884   C CB    . ASN B 2 47   ? 159.470 140.509 160.520 1.00 52.22  ? 44   ASN A CB    1 
ATOM   885   C CG    . ASN B 2 47   ? 159.081 140.315 159.071 1.00 52.22  ? 44   ASN A CG    1 
ATOM   886   O OD1   . ASN B 2 47   ? 158.409 139.345 158.729 1.00 52.22  ? 44   ASN A OD1   1 
ATOM   887   N ND2   . ASN B 2 47   ? 159.495 141.231 158.212 1.00 52.22  ? 44   ASN A ND2   1 
ATOM   888   N N     . ASP B 2 48   ? 161.729 138.273 161.215 1.00 54.47  ? 45   ASP A N     1 
ATOM   889   C CA    . ASP B 2 48   ? 162.796 137.400 160.664 1.00 54.47  ? 45   ASP A CA    1 
ATOM   890   C C     . ASP B 2 48   ? 162.697 136.044 161.345 1.00 54.47  ? 45   ASP A C     1 
ATOM   891   O O     . ASP B 2 48   ? 163.504 135.163 161.023 1.00 54.47  ? 45   ASP A O     1 
ATOM   892   C CB    . ASP B 2 48   ? 164.175 138.041 160.802 1.00 54.47  ? 45   ASP A CB    1 
ATOM   893   C CG    . ASP B 2 48   ? 164.358 139.255 159.909 1.00 54.47  ? 45   ASP A CG    1 
ATOM   894   O OD1   . ASP B 2 48   ? 163.413 139.580 159.163 1.00 54.47  ? 45   ASP A OD1   1 
ATOM   895   O OD2   . ASP B 2 48   ? 165.441 139.869 159.970 1.00 54.47  ? 45   ASP A OD2   1 
ATOM   896   N N     . HIS B 2 49   ? 161.746 135.891 162.245 1.00 55.19  ? 46   HIS A N     1 
ATOM   897   C CA    . HIS B 2 49   ? 161.509 134.572 162.851 1.00 55.19  ? 46   HIS A CA    1 
ATOM   898   C C     . HIS B 2 49   ? 160.249 134.070 162.185 1.00 55.19  ? 46   HIS A C     1 
ATOM   899   O O     . HIS B 2 49   ? 160.002 132.880 162.223 1.00 55.19  ? 46   HIS A O     1 
ATOM   900   C CB    . HIS B 2 49   ? 161.275 134.664 164.350 1.00 55.19  ? 46   HIS A CB    1 
ATOM   901   C CG    . HIS B 2 49   ? 162.447 135.061 165.176 1.00 55.19  ? 46   HIS A CG    1 
ATOM   902   N ND1   . HIS B 2 49   ? 162.306 135.474 166.479 1.00 55.19  ? 46   HIS A ND1   1 
ATOM   903   C CD2   . HIS B 2 49   ? 163.767 135.085 164.916 1.00 55.19  ? 46   HIS A CD2   1 
ATOM   904   C CE1   . HIS B 2 49   ? 163.488 135.746 166.985 1.00 55.19  ? 46   HIS A CE1   1 
ATOM   905   N NE2   . HIS B 2 49   ? 164.402 135.512 166.045 1.00 55.19  ? 46   HIS A NE2   1 
ATOM   906   N N     . TYR B 2 50   ? 159.469 134.989 161.625 1.00 78.22  ? 47   TYR A N     1 
ATOM   907   C CA    . TYR B 2 50   ? 158.191 134.614 160.965 1.00 73.90  ? 47   TYR A CA    1 
ATOM   908   C C     . TYR B 2 50   ? 158.591 133.695 159.829 1.00 72.72  ? 47   TYR A C     1 
ATOM   909   O O     . TYR B 2 50   ? 157.749 133.188 159.080 1.00 72.10  ? 47   TYR A O     1 
ATOM   910   C CB    . TYR B 2 50   ? 157.396 135.848 160.532 1.00 71.19  ? 47   TYR A CB    1 
ATOM   911   C CG    . TYR B 2 50   ? 156.085 135.546 159.853 1.00 67.71  ? 47   TYR A CG    1 
ATOM   912   C CD1   . TYR B 2 50   ? 155.031 134.985 160.550 1.00 65.48  ? 47   TYR A CD1   1 
ATOM   913   C CD2   . TYR B 2 50   ? 155.898 135.824 158.510 1.00 66.53  ? 47   TYR A CD2   1 
ATOM   914   C CE1   . TYR B 2 50   ? 153.824 134.711 159.932 1.00 64.09  ? 47   TYR A CE1   1 
ATOM   915   C CE2   . TYR B 2 50   ? 154.698 135.552 157.875 1.00 64.91  ? 47   TYR A CE2   1 
ATOM   916   C CZ    . TYR B 2 50   ? 153.657 134.992 158.590 1.00 64.34  ? 47   TYR A CZ    1 
ATOM   917   O OH    . TYR B 2 50   ? 152.469 134.721 157.976 1.00 60.55  ? 47   TYR A OH    1 
ATOM   918   N N     . LYS B 2 51   ? 159.880 133.523 159.705 1.00 72.22  ? 48   LYS A N     1 
ATOM   919   C CA    . LYS B 2 51   ? 160.409 132.577 158.729 1.00 69.41  ? 48   LYS A CA    1 
ATOM   920   C C     . LYS B 2 51   ? 161.114 131.406 159.402 1.00 70.71  ? 48   LYS A C     1 
ATOM   921   O O     . LYS B 2 51   ? 161.143 130.302 158.846 1.00 69.55  ? 48   LYS A O     1 
ATOM   922   C CB    . LYS B 2 51   ? 161.355 133.290 157.765 1.00 68.43  ? 48   LYS A CB    1 
ATOM   923   C CG    . LYS B 2 51   ? 160.674 134.356 156.922 1.00 68.21  ? 48   LYS A CG    1 
ATOM   924   C CD    . LYS B 2 51   ? 161.583 134.867 155.819 1.00 69.74  ? 48   LYS A CD    1 
ATOM   925   C CE    . LYS B 2 51   ? 160.840 135.822 154.899 1.00 69.49  ? 48   LYS A CE    1 
ATOM   926   N NZ    . LYS B 2 51   ? 161.667 136.228 153.729 1.00 69.69  ? 48   LYS A NZ    1 
ATOM   927   N N     . GLU B 2 52   ? 161.688 131.621 160.588 1.00 71.98  ? 49   GLU A N     1 
ATOM   928   C CA    . GLU B 2 52   ? 162.281 130.509 161.326 1.00 74.88  ? 49   GLU A CA    1 
ATOM   929   C C     . GLU B 2 52   ? 161.205 129.640 161.965 1.00 76.15  ? 49   GLU A C     1 
ATOM   930   O O     . GLU B 2 52   ? 161.352 128.414 162.041 1.00 78.41  ? 49   GLU A O     1 
ATOM   931   C CB    . GLU B 2 52   ? 163.241 131.036 162.392 1.00 79.05  ? 49   GLU A CB    1 
ATOM   932   C CG    . GLU B 2 52   ? 164.542 131.607 161.854 1.00 80.27  ? 49   GLU A CG    1 
ATOM   933   C CD    . GLU B 2 52   ? 165.341 132.328 162.924 1.00 82.96  ? 49   GLU A CD    1 
ATOM   934   O OE1   . GLU B 2 52   ? 165.058 133.520 163.176 1.00 82.09  ? 49   GLU A OE1   1 
ATOM   935   O OE2   . GLU B 2 52   ? 166.239 131.701 163.523 1.00 86.24  ? 49   GLU A OE2   1 
ATOM   936   N N     . LEU B 2 53   ? 160.115 130.257 162.425 1.00 74.85  ? 50   LEU A N     1 
ATOM   937   C CA    . LEU B 2 53   ? 159.089 129.531 163.162 1.00 73.79  ? 50   LEU A CA    1 
ATOM   938   C C     . LEU B 2 53   ? 158.119 128.799 162.241 1.00 74.49  ? 50   LEU A C     1 
ATOM   939   O O     . LEU B 2 53   ? 157.559 127.769 162.638 1.00 76.10  ? 50   LEU A O     1 
ATOM   940   C CB    . LEU B 2 53   ? 158.330 130.498 164.072 1.00 72.32  ? 50   LEU A CB    1 
ATOM   941   C CG    . LEU B 2 53   ? 157.208 129.933 164.940 1.00 73.52  ? 50   LEU A CG    1 
ATOM   942   C CD1   . LEU B 2 53   ? 157.721 128.805 165.819 1.00 76.56  ? 50   LEU A CD1   1 
ATOM   943   C CD2   . LEU B 2 53   ? 156.591 131.037 165.780 1.00 76.16  ? 50   LEU A CD2   1 
ATOM   944   N N     . LYS B 2 54   ? 157.910 129.305 161.024 1.00 72.11  ? 51   LYS A N     1 
ATOM   945   C CA    . LYS B 2 54   ? 156.964 128.690 160.093 1.00 67.69  ? 51   LYS A CA    1 
ATOM   946   C C     . LYS B 2 54   ? 157.215 127.203 159.854 1.00 63.77  ? 51   LYS A C     1 
ATOM   947   O O     . LYS B 2 54   ? 156.254 126.422 159.941 1.00 60.79  ? 51   LYS A O     1 
ATOM   948   C CB    . LYS B 2 54   ? 156.974 129.471 158.771 1.00 69.19  ? 51   LYS A CB    1 
ATOM   949   C CG    . LYS B 2 54   ? 156.306 128.741 157.615 1.00 69.43  ? 51   LYS A CG    1 
ATOM   950   C CD    . LYS B 2 54   ? 156.718 129.331 156.278 1.00 69.55  ? 51   LYS A CD    1 
ATOM   951   C CE    . LYS B 2 54   ? 156.248 128.460 155.123 1.00 69.75  ? 51   LYS A CE    1 
ATOM   952   N NZ    . LYS B 2 54   ? 156.821 128.900 153.820 1.00 68.75  ? 51   LYS A NZ    1 
ATOM   953   N N     . PRO B 2 55   ? 158.438 126.740 159.557 1.00 63.44  ? 52   PRO A N     1 
ATOM   954   C CA    . PRO B 2 55   ? 158.626 125.290 159.390 1.00 62.36  ? 52   PRO A CA    1 
ATOM   955   C C     . PRO B 2 55   ? 158.410 124.509 160.672 1.00 67.62  ? 52   PRO A C     1 
ATOM   956   O O     . PRO B 2 55   ? 157.984 123.349 160.612 1.00 66.54  ? 52   PRO A O     1 
ATOM   957   C CB    . PRO B 2 55   ? 160.077 125.173 158.897 1.00 62.28  ? 52   PRO A CB    1 
ATOM   958   C CG    . PRO B 2 55   ? 160.423 126.529 158.379 1.00 63.28  ? 52   PRO A CG    1 
ATOM   959   C CD    . PRO B 2 55   ? 159.680 127.475 159.263 1.00 64.75  ? 52   PRO A CD    1 
ATOM   960   N N     . ILE B 2 56   ? 158.691 125.109 161.831 1.00 72.56  ? 53   ILE A N     1 
ATOM   961   C CA    . ILE B 2 56   ? 158.452 124.427 163.099 1.00 65.78  ? 53   ILE A CA    1 
ATOM   962   C C     . ILE B 2 56   ? 156.958 124.217 163.314 1.00 82.29  ? 53   ILE A C     1 
ATOM   963   O O     . ILE B 2 56   ? 156.516 123.126 163.697 1.00 65.42  ? 53   ILE A O     1 
ATOM   964   C CB    . ILE B 2 56   ? 159.082 125.221 164.259 1.00 85.92  ? 53   ILE A CB    1 
ATOM   965   C CG1   . ILE B 2 56   ? 160.576 125.432 164.002 1.00 86.54  ? 53   ILE A CG1   1 
ATOM   966   C CG2   . ILE B 2 56   ? 158.853 124.507 165.584 1.00 70.77  ? 53   ILE A CG2   1 
ATOM   967   C CD1   . ILE B 2 56   ? 161.234 126.382 164.974 1.00 71.87  ? 53   ILE A CD1   1 
ATOM   968   N N     . ILE B 2 57   ? 156.159 125.258 163.069 1.00 74.06  ? 54   ILE A N     1 
ATOM   969   C CA    . ILE B 2 57   ? 154.710 125.139 163.218 1.00 73.58  ? 54   ILE A CA    1 
ATOM   970   C C     . ILE B 2 57   ? 154.153 124.131 162.221 1.00 73.04  ? 54   ILE A C     1 
ATOM   971   O O     . ILE B 2 57   ? 153.210 123.389 162.528 1.00 73.12  ? 54   ILE A O     1 
ATOM   972   C CB    . ILE B 2 57   ? 154.042 126.519 163.061 1.00 73.25  ? 54   ILE A CB    1 
ATOM   973   C CG1   . ILE B 2 57   ? 154.518 127.472 164.157 1.00 76.27  ? 54   ILE A CG1   1 
ATOM   974   C CG2   . ILE B 2 57   ? 152.525 126.392 163.088 1.00 72.59  ? 54   ILE A CG2   1 
ATOM   975   C CD1   . ILE B 2 57   ? 153.836 128.823 164.122 1.00 76.34  ? 54   ILE A CD1   1 
ATOM   976   N N     . ASP B 2 58   ? 154.732 124.080 161.020 1.00 72.26  ? 55   ASP A N     1 
ATOM   977   C CA    . ASP B 2 58   ? 154.261 123.149 160.001 1.00 73.17  ? 55   ASP A CA    1 
ATOM   978   C C     . ASP B 2 58   ? 154.405 121.695 160.429 1.00 75.72  ? 55   ASP A C     1 
ATOM   979   O O     . ASP B 2 58   ? 153.686 120.838 159.906 1.00 74.53  ? 55   ASP A O     1 
ATOM   980   C CB    . ASP B 2 58   ? 155.006 123.383 158.687 1.00 74.50  ? 55   ASP A CB    1 
ATOM   981   C CG    . ASP B 2 58   ? 154.521 124.621 157.957 1.00 74.93  ? 55   ASP A CG    1 
ATOM   982   O OD1   . ASP B 2 58   ? 153.333 124.970 158.107 1.00 75.35  ? 55   ASP A OD1   1 
ATOM   983   O OD2   . ASP B 2 58   ? 155.330 125.243 157.234 1.00 74.56  ? 55   ASP A OD2   1 
ATOM   984   N N     . ARG B 2 59   ? 155.311 121.397 161.364 1.00 80.59  ? 56   ARG A N     1 
ATOM   985   C CA    . ARG B 2 59   ? 155.422 120.029 161.862 1.00 84.18  ? 56   ARG A CA    1 
ATOM   986   C C     . ARG B 2 59   ? 154.112 119.551 162.471 1.00 85.42  ? 56   ARG A C     1 
ATOM   987   O O     . ARG B 2 59   ? 153.776 118.366 162.368 1.00 86.16  ? 56   ARG A O     1 
ATOM   988   C CB    . ARG B 2 59   ? 156.546 119.926 162.893 1.00 87.61  ? 56   ARG A CB    1 
ATOM   989   C CG    . ARG B 2 59   ? 157.910 120.364 162.392 1.00 88.35  ? 56   ARG A CG    1 
ATOM   990   C CD    . ARG B 2 59   ? 159.016 119.646 163.149 1.00 91.36  ? 56   ARG A CD    1 
ATOM   991   N NE    . ARG B 2 59   ? 160.310 120.303 163.005 1.00 92.31  ? 56   ARG A NE    1 
ATOM   992   C CZ    . ARG B 2 59   ? 160.873 121.051 163.949 1.00 93.28  ? 56   ARG A CZ    1 
ATOM   993   N NH1   . ARG B 2 59   ? 160.257 121.232 165.110 1.00 93.28  ? 56   ARG A NH1   1 
ATOM   994   N NH2   . ARG B 2 59   ? 162.055 121.614 163.735 1.00 93.93  ? 56   ARG A NH2   1 
ATOM   995   N N     . ILE B 2 60   ? 153.359 120.453 163.102 1.00 87.19  ? 57   ILE A N     1 
ATOM   996   C CA    . ILE B 2 60   ? 152.070 120.079 163.677 1.00 87.35  ? 57   ILE A CA    1 
ATOM   997   C C     . ILE B 2 60   ? 151.086 119.701 162.577 1.00 85.46  ? 57   ILE A C     1 
ATOM   998   O O     . ILE B 2 60   ? 150.394 118.680 162.665 1.00 87.46  ? 57   ILE A O     1 
ATOM   999   C CB    . ILE B 2 60   ? 151.524 121.219 164.554 1.00 88.27  ? 57   ILE A CB    1 
ATOM   1000  C CG1   . ILE B 2 60   ? 152.532 121.580 165.645 1.00 91.73  ? 57   ILE A CG1   1 
ATOM   1001  C CG2   . ILE B 2 60   ? 150.188 120.827 165.165 1.00 89.37  ? 57   ILE A CG2   1 
ATOM   1002  C CD1   . ILE B 2 60   ? 152.091 122.722 166.529 1.00 93.85  ? 57   ILE A CD1   1 
ATOM   1003  N N     . TYR B 2 61   ? 151.009 120.519 161.524 1.00 76.75  ? 58   TYR A N     1 
ATOM   1004  C CA    . TYR B 2 61   ? 150.125 120.208 160.408 1.00 70.22  ? 58   TYR A CA    1 
ATOM   1005  C C     . TYR B 2 61   ? 150.565 118.935 159.697 1.00 67.48  ? 58   TYR A C     1 
ATOM   1006  O O     . TYR B 2 61   ? 149.752 118.040 159.441 1.00 64.94  ? 58   TYR A O     1 
ATOM   1007  C CB    . TYR B 2 61   ? 150.083 121.377 159.423 1.00 67.06  ? 58   TYR A CB    1 
ATOM   1008  C CG    . TYR B 2 61   ? 149.471 122.641 159.979 1.00 68.31  ? 58   TYR A CG    1 
ATOM   1009  C CD1   . TYR B 2 61   ? 148.101 122.742 160.179 1.00 70.21  ? 58   TYR A CD1   1 
ATOM   1010  C CD2   . TYR B 2 61   ? 150.262 123.740 160.287 1.00 69.10  ? 58   TYR A CD2   1 
ATOM   1011  C CE1   . TYR B 2 61   ? 147.535 123.898 160.681 1.00 70.75  ? 58   TYR A CE1   1 
ATOM   1012  C CE2   . TYR B 2 61   ? 149.706 124.900 160.791 1.00 70.85  ? 58   TYR A CE2   1 
ATOM   1013  C CZ    . TYR B 2 61   ? 148.342 124.973 160.985 1.00 71.54  ? 58   TYR A CZ    1 
ATOM   1014  O OH    . TYR B 2 61   ? 147.781 126.125 161.483 1.00 72.82  ? 58   TYR A OH    1 
ATOM   1015  N N     . LYS B 2 62   ? 151.858 118.838 159.371 1.00 66.76  ? 59   LYS A N     1 
ATOM   1016  C CA    . LYS B 2 62   ? 152.358 117.681 158.635 1.00 64.88  ? 59   LYS A CA    1 
ATOM   1017  C C     . LYS B 2 62   ? 152.119 116.389 159.407 1.00 69.08  ? 59   LYS A C     1 
ATOM   1018  O O     . LYS B 2 62   ? 151.639 115.398 158.847 1.00 70.16  ? 59   LYS A O     1 
ATOM   1019  C CB    . LYS B 2 62   ? 153.845 117.856 158.327 1.00 64.02  ? 59   LYS A CB    1 
ATOM   1020  C CG    . LYS B 2 62   ? 154.157 118.998 157.370 1.00 62.74  ? 59   LYS A CG    1 
ATOM   1021  C CD    . LYS B 2 62   ? 155.647 119.076 157.066 1.00 63.27  ? 59   LYS A CD    1 
ATOM   1022  C CE    . LYS B 2 62   ? 156.464 119.307 158.327 1.00 66.52  ? 59   LYS A CE    1 
ATOM   1023  N NZ    . LYS B 2 62   ? 157.924 119.385 158.041 1.00 66.37  ? 59   LYS A NZ    1 
ATOM   1024  N N     . THR B 2 63   ? 152.443 116.386 160.703 1.00 73.25  ? 60   THR A N     1 
ATOM   1025  C CA    . THR B 2 63   ? 152.274 115.177 161.503 1.00 76.55  ? 60   THR A CA    1 
ATOM   1026  C C     . THR B 2 63   ? 150.802 114.812 161.642 1.00 78.91  ? 60   THR A C     1 
ATOM   1027  O O     . THR B 2 63   ? 150.414 113.661 161.409 1.00 79.19  ? 60   THR A O     1 
ATOM   1028  C CB    . THR B 2 63   ? 152.915 115.362 162.878 1.00 80.26  ? 60   THR A CB    1 
ATOM   1029  O OG1   . THR B 2 63   ? 154.246 115.870 162.720 1.00 82.54  ? 60   THR A OG1   1 
ATOM   1030  C CG2   . THR B 2 63   ? 152.973 114.035 163.622 1.00 81.68  ? 60   THR A CG2   1 
ATOM   1031  N N     . TYR B 2 64   ? 149.963 115.782 162.016 1.00 81.09  ? 61   TYR A N     1 
ATOM   1032  C CA    . TYR B 2 64   ? 148.547 115.495 162.218 1.00 83.09  ? 61   TYR A CA    1 
ATOM   1033  C C     . TYR B 2 64   ? 147.877 115.059 160.923 1.00 83.80  ? 61   TYR A C     1 
ATOM   1034  O O     . TYR B 2 64   ? 147.075 114.116 160.916 1.00 84.04  ? 61   TYR A O     1 
ATOM   1035  C CB    . TYR B 2 64   ? 147.839 116.713 162.806 1.00 81.79  ? 61   TYR A CB    1 
ATOM   1036  C CG    . TYR B 2 64   ? 146.343 116.540 162.926 1.00 79.80  ? 61   TYR A CG    1 
ATOM   1037  C CD1   . TYR B 2 64   ? 145.791 115.796 163.962 1.00 80.90  ? 61   TYR A CD1   1 
ATOM   1038  C CD2   . TYR B 2 64   ? 145.482 117.120 162.005 1.00 77.87  ? 61   TYR A CD2   1 
ATOM   1039  C CE1   . TYR B 2 64   ? 144.424 115.632 164.072 1.00 81.09  ? 61   TYR A CE1   1 
ATOM   1040  C CE2   . TYR B 2 64   ? 144.115 116.965 162.108 1.00 77.99  ? 61   TYR A CE2   1 
ATOM   1041  C CZ    . TYR B 2 64   ? 143.591 116.219 163.144 1.00 79.63  ? 61   TYR A CZ    1 
ATOM   1042  O OH    . TYR B 2 64   ? 142.228 116.064 163.246 1.00 79.57  ? 61   TYR A OH    1 
ATOM   1043  N N     . ALA B 2 65   ? 148.188 115.732 159.811 1.00 84.26  ? 62   ALA A N     1 
ATOM   1044  C CA    . ALA B 2 65   ? 147.610 115.336 158.531 1.00 84.02  ? 62   ALA A CA    1 
ATOM   1045  C C     . ALA B 2 65   ? 148.091 113.952 158.118 1.00 85.43  ? 62   ALA A C     1 
ATOM   1046  O O     . ALA B 2 65   ? 147.301 113.129 157.642 1.00 86.51  ? 62   ALA A O     1 
ATOM   1047  C CB    . ALA B 2 65   ? 147.947 116.366 157.452 1.00 82.50  ? 62   ALA A CB    1 
ATOM   1048  N N     . ASP B 2 66   ? 149.385 113.675 158.298 1.00 86.48  ? 63   ASP A N     1 
ATOM   1049  C CA    . ASP B 2 66   ? 149.909 112.360 157.951 1.00 88.87  ? 63   ASP A CA    1 
ATOM   1050  C C     . ASP B 2 66   ? 149.282 111.274 158.816 1.00 90.28  ? 63   ASP A C     1 
ATOM   1051  O O     . ASP B 2 66   ? 148.958 110.189 158.323 1.00 91.39  ? 63   ASP A O     1 
ATOM   1052  C CB    . ASP B 2 66   ? 151.434 112.353 158.090 1.00 93.16  ? 63   ASP A CB    1 
ATOM   1053  C CG    . ASP B 2 66   ? 152.089 111.225 157.315 1.00 97.49  ? 63   ASP A CG    1 
ATOM   1054  O OD1   . ASP B 2 66   ? 151.660 110.063 157.465 1.00 100.21 ? 63   ASP A OD1   1 
ATOM   1055  O OD2   . ASP B 2 66   ? 153.034 111.507 156.549 1.00 98.07  ? 63   ASP A OD2   1 
ATOM   1056  N N     . GLN B 2 67   ? 149.089 111.555 160.107 1.00 89.86  ? 64   GLN A N     1 
ATOM   1057  C CA    . GLN B 2 67   ? 148.483 110.566 160.995 1.00 88.06  ? 64   GLN A CA    1 
ATOM   1058  C C     . GLN B 2 67   ? 147.033 110.291 160.613 1.00 83.49  ? 64   GLN A C     1 
ATOM   1059  O O     . GLN B 2 67   ? 146.584 109.139 160.658 1.00 83.81  ? 64   GLN A O     1 
ATOM   1060  C CB    . GLN B 2 67   ? 148.575 111.036 162.447 1.00 88.84  ? 64   GLN A CB    1 
ATOM   1061  C CG    . GLN B 2 67   ? 149.975 110.968 163.033 1.00 90.92  ? 64   GLN A CG    1 
ATOM   1062  C CD    . GLN B 2 67   ? 150.057 111.583 164.416 1.00 94.52  ? 64   GLN A CD    1 
ATOM   1063  O OE1   . GLN B 2 67   ? 149.958 112.798 164.574 1.00 97.42  ? 64   GLN A OE1   1 
ATOM   1064  N NE2   . GLN B 2 67   ? 150.236 110.741 165.427 1.00 94.55  ? 64   GLN A NE2   1 
ATOM   1065  N N     . CYS B 2 68   ? 146.288 111.330 160.230 1.00 79.56  ? 65   CYS A N     1 
ATOM   1066  C CA    . CYS B 2 68   ? 144.895 111.134 159.841 1.00 77.17  ? 65   CYS A CA    1 
ATOM   1067  C C     . CYS B 2 68   ? 144.772 110.370 158.530 1.00 74.34  ? 65   CYS A C     1 
ATOM   1068  O O     . CYS B 2 68   ? 143.814 109.612 158.344 1.00 71.82  ? 65   CYS A O     1 
ATOM   1069  C CB    . CYS B 2 68   ? 144.180 112.481 159.737 1.00 77.04  ? 65   CYS A CB    1 
ATOM   1070  S SG    . CYS B 2 68   ? 143.914 113.309 161.320 1.00 81.69  ? 65   CYS A SG    1 
ATOM   1071  N N     . LEU B 2 69   ? 145.721 110.551 157.612 1.00 73.22  ? 66   LEU A N     1 
ATOM   1072  C CA    . LEU B 2 69   ? 145.675 109.859 156.331 1.00 71.15  ? 66   LEU A CA    1 
ATOM   1073  C C     . LEU B 2 69   ? 146.097 108.399 156.427 1.00 75.33  ? 66   LEU A C     1 
ATOM   1074  O O     . LEU B 2 69   ? 145.899 107.652 155.464 1.00 77.12  ? 66   LEU A O     1 
ATOM   1075  C CB    . LEU B 2 69   ? 146.554 110.584 155.308 1.00 65.00  ? 66   LEU A CB    1 
ATOM   1076  C CG    . LEU B 2 69   ? 146.092 111.990 154.916 1.00 58.74  ? 66   LEU A CG    1 
ATOM   1077  C CD1   . LEU B 2 69   ? 147.046 112.630 153.918 1.00 54.64  ? 66   LEU A CD1   1 
ATOM   1078  C CD2   . LEU B 2 69   ? 144.675 111.961 154.365 1.00 56.42  ? 66   LEU A CD2   1 
ATOM   1079  N N     . GLN B 2 70   ? 146.669 107.970 157.555 1.00 78.16  ? 67   GLN A N     1 
ATOM   1080  C CA    . GLN B 2 70   ? 147.084 106.578 157.688 1.00 82.42  ? 67   GLN A CA    1 
ATOM   1081  C C     . GLN B 2 70   ? 145.905 105.650 157.952 1.00 85.59  ? 67   GLN A C     1 
ATOM   1082  O O     . GLN B 2 70   ? 145.983 104.456 157.641 1.00 87.67  ? 67   GLN A O     1 
ATOM   1083  C CB    . GLN B 2 70   ? 148.121 106.435 158.804 1.00 85.82  ? 67   GLN A CB    1 
ATOM   1084  C CG    . GLN B 2 70   ? 149.457 107.096 158.506 1.00 85.53  ? 67   GLN A CG    1 
ATOM   1085  C CD    . GLN B 2 70   ? 150.450 106.937 159.642 1.00 87.69  ? 67   GLN A CD    1 
ATOM   1086  O OE1   . GLN B 2 70   ? 150.760 105.821 160.056 1.00 89.72  ? 67   GLN A OE1   1 
ATOM   1087  N NE2   . GLN B 2 70   ? 150.947 108.058 160.159 1.00 87.30  ? 67   GLN A NE2   1 
ATOM   1088  N N     . LEU B 2 71   ? 144.818 106.168 158.521 1.00 86.89  ? 68   LEU A N     1 
ATOM   1089  C CA    . LEU B 2 71   ? 143.649 105.358 158.836 1.00 90.18  ? 68   LEU A CA    1 
ATOM   1090  C C     . LEU B 2 71   ? 142.595 105.375 157.737 1.00 90.06  ? 68   LEU A C     1 
ATOM   1091  O O     . LEU B 2 71   ? 141.532 104.771 157.912 1.00 91.05  ? 68   LEU A O     1 
ATOM   1092  C CB    . LEU B 2 71   ? 143.014 105.829 160.148 1.00 92.47  ? 68   LEU A CB    1 
ATOM   1093  C CG    . LEU B 2 71   ? 143.878 105.816 161.410 1.00 94.87  ? 68   LEU A CG    1 
ATOM   1094  C CD1   . LEU B 2 71   ? 144.324 107.222 161.764 1.00 93.49  ? 68   LEU A CD1   1 
ATOM   1095  C CD2   . LEU B 2 71   ? 143.118 105.185 162.566 1.00 98.14  ? 68   LEU A CD2   1 
ATOM   1096  N N     . VAL B 2 72   ? 142.854 106.049 156.618 1.00 88.71  ? 69   VAL A N     1 
ATOM   1097  C CA    . VAL B 2 72   ? 141.839 106.194 155.580 1.00 86.66  ? 69   VAL A CA    1 
ATOM   1098  C C     . VAL B 2 72   ? 141.694 104.878 154.828 1.00 86.87  ? 69   VAL A C     1 
ATOM   1099  O O     . VAL B 2 72   ? 142.653 104.373 154.234 1.00 87.21  ? 69   VAL A O     1 
ATOM   1100  C CB    . VAL B 2 72   ? 142.189 107.342 154.625 1.00 81.61  ? 69   VAL A CB    1 
ATOM   1101  C CG1   . VAL B 2 72   ? 141.116 107.482 153.559 1.00 79.70  ? 69   VAL A CG1   1 
ATOM   1102  C CG2   . VAL B 2 72   ? 142.351 108.642 155.395 1.00 80.65  ? 69   VAL A CG2   1 
ATOM   1103  N N     . GLN B 2 73   ? 140.486 104.319 154.850 1.00 88.38  ? 70   GLN A N     1 
ATOM   1104  C CA    . GLN B 2 73   ? 140.141 103.119 154.091 1.00 88.49  ? 70   GLN A CA    1 
ATOM   1105  C C     . GLN B 2 73   ? 138.807 103.374 153.402 1.00 85.74  ? 70   GLN A C     1 
ATOM   1106  O O     . GLN B 2 73   ? 137.774 103.481 154.070 1.00 87.42  ? 70   GLN A O     1 
ATOM   1107  C CB    . GLN B 2 73   ? 140.062 101.886 154.993 1.00 94.00  ? 70   GLN A CB    1 
ATOM   1108  C CG    . GLN B 2 73   ? 141.305 101.005 154.975 1.00 99.61  ? 70   GLN A CG    1 
ATOM   1109  C CD    . GLN B 2 73   ? 142.483 101.626 155.701 1.00 102.76 ? 70   GLN A CD    1 
ATOM   1110  O OE1   . GLN B 2 73   ? 143.467 102.029 155.080 1.00 104.11 ? 70   GLN A OE1   1 
ATOM   1111  N NE2   . GLN B 2 73   ? 142.386 101.709 157.024 1.00 102.05 ? 70   GLN A NE2   1 
ATOM   1112  N N     . LEU B 2 74   ? 138.828 103.475 152.075 1.00 83.59  ? 71   LEU A N     1 
ATOM   1113  C CA    . LEU B 2 74   ? 137.629 103.759 151.302 1.00 80.35  ? 71   LEU A CA    1 
ATOM   1114  C C     . LEU B 2 74   ? 137.520 102.797 150.129 1.00 78.91  ? 71   LEU A C     1 
ATOM   1115  O O     . LEU B 2 74   ? 138.502 102.187 149.699 1.00 79.78  ? 71   LEU A O     1 
ATOM   1116  C CB    . LEU B 2 74   ? 137.622 105.203 150.782 1.00 74.28  ? 71   LEU A CB    1 
ATOM   1117  C CG    . LEU B 2 74   ? 137.577 106.315 151.827 1.00 71.19  ? 71   LEU A CG    1 
ATOM   1118  C CD1   . LEU B 2 74   ? 137.534 107.668 151.141 1.00 67.32  ? 71   LEU A CD1   1 
ATOM   1119  C CD2   . LEU B 2 74   ? 136.382 106.136 152.749 1.00 71.98  ? 71   LEU A CD2   1 
ATOM   1120  N N     . ASP B 2 75   ? 136.298 102.672 149.615 1.00 78.75  ? 72   ASP A N     1 
ATOM   1121  C CA    . ASP B 2 75   ? 136.013 101.882 148.424 1.00 80.11  ? 72   ASP A CA    1 
ATOM   1122  C C     . ASP B 2 75   ? 135.886 102.843 147.249 1.00 78.86  ? 72   ASP A C     1 
ATOM   1123  O O     . ASP B 2 75   ? 134.891 103.565 147.133 1.00 79.00  ? 72   ASP A O     1 
ATOM   1124  C CB    . ASP B 2 75   ? 134.741 101.056 148.608 1.00 83.64  ? 72   ASP A CB    1 
ATOM   1125  C CG    . ASP B 2 75   ? 134.589 99.970  147.559 1.00 87.93  ? 72   ASP A CG    1 
ATOM   1126  O OD1   . ASP B 2 75   ? 135.185 100.096 146.469 1.00 89.44  ? 72   ASP A OD1   1 
ATOM   1127  O OD2   . ASP B 2 75   ? 133.869 98.986  147.826 1.00 91.11  ? 72   ASP A OD2   1 
ATOM   1128  N N     . TRP B 2 76   ? 136.893 102.852 146.381 1.00 77.19  ? 73   TRP A N     1 
ATOM   1129  C CA    . TRP B 2 76   ? 136.970 103.794 145.273 1.00 74.62  ? 73   TRP A CA    1 
ATOM   1130  C C     . TRP B 2 76   ? 136.238 103.309 144.028 1.00 76.79  ? 73   TRP A C     1 
ATOM   1131  O O     . TRP B 2 76   ? 136.409 103.901 142.957 1.00 76.14  ? 73   TRP A O     1 
ATOM   1132  C CB    . TRP B 2 76   ? 138.433 104.081 144.934 1.00 70.57  ? 73   TRP A CB    1 
ATOM   1133  C CG    . TRP B 2 76   ? 139.246 104.525 146.111 1.00 67.54  ? 73   TRP A CG    1 
ATOM   1134  C CD1   . TRP B 2 76   ? 139.885 103.726 147.014 1.00 67.81  ? 73   TRP A CD1   1 
ATOM   1135  C CD2   . TRP B 2 76   ? 139.507 105.875 146.513 1.00 65.75  ? 73   TRP A CD2   1 
ATOM   1136  N NE1   . TRP B 2 76   ? 140.529 104.493 147.954 1.00 67.17  ? 73   TRP A NE1   1 
ATOM   1137  C CE2   . TRP B 2 76   ? 140.312 105.816 147.669 1.00 66.42  ? 73   TRP A CE2   1 
ATOM   1138  C CE3   . TRP B 2 76   ? 139.140 107.126 146.010 1.00 63.59  ? 73   TRP A CE3   1 
ATOM   1139  C CZ2   . TRP B 2 76   ? 140.756 106.962 148.329 1.00 65.46  ? 73   TRP A CZ2   1 
ATOM   1140  C CZ3   . TRP B 2 76   ? 139.580 108.261 146.666 1.00 61.89  ? 73   TRP A CZ3   1 
ATOM   1141  C CH2   . TRP B 2 76   ? 140.379 108.171 147.812 1.00 63.01  ? 73   TRP A CH2   1 
ATOM   1142  N N     . GLU B 2 77   ? 135.428 102.253 144.141 1.00 83.38  ? 74   GLU A N     1 
ATOM   1143  C CA    . GLU B 2 77   ? 134.753 101.714 142.963 1.00 87.04  ? 74   GLU A CA    1 
ATOM   1144  C C     . GLU B 2 77   ? 133.711 102.687 142.424 1.00 85.01  ? 74   GLU A C     1 
ATOM   1145  O O     . GLU B 2 77   ? 133.540 102.809 141.205 1.00 83.95  ? 74   GLU A O     1 
ATOM   1146  C CB    . GLU B 2 77   ? 134.109 100.368 143.300 1.00 93.55  ? 74   GLU A CB    1 
ATOM   1147  C CG    . GLU B 2 77   ? 133.471 99.672  142.109 1.00 99.07  ? 74   GLU A CG    1 
ATOM   1148  C CD    . GLU B 2 77   ? 134.484 99.284  141.048 1.00 103.74 ? 74   GLU A CD    1 
ATOM   1149  O OE1   . GLU B 2 77   ? 135.645 98.994  141.407 1.00 105.48 ? 74   GLU A OE1   1 
ATOM   1150  O OE2   . GLU B 2 77   ? 134.119 99.273  139.853 1.00 105.20 ? 74   GLU A OE2   1 
ATOM   1151  N N     . ASN B 2 78   ? 133.006 103.390 143.313 1.00 83.74  ? 75   ASN A N     1 
ATOM   1152  C CA    . ASN B 2 78   ? 131.991 104.338 142.865 1.00 81.18  ? 75   ASN A CA    1 
ATOM   1153  C C     . ASN B 2 78   ? 132.619 105.518 142.136 1.00 76.47  ? 75   ASN A C     1 
ATOM   1154  O O     . ASN B 2 78   ? 132.078 105.993 141.131 1.00 75.05  ? 75   ASN A O     1 
ATOM   1155  C CB    . ASN B 2 78   ? 131.161 104.820 144.054 1.00 83.59  ? 75   ASN A CB    1 
ATOM   1156  C CG    . ASN B 2 78   ? 130.330 103.713 144.668 1.00 87.54  ? 75   ASN A CG    1 
ATOM   1157  O OD1   . ASN B 2 78   ? 129.142 103.577 144.376 1.00 88.15  ? 75   ASN A OD1   1 
ATOM   1158  N ND2   . ASN B 2 78   ? 130.953 102.910 145.524 1.00 89.66  ? 75   ASN A ND2   1 
ATOM   1159  N N     . LEU B 2 79   ? 133.761 106.004 142.628 1.00 73.26  ? 76   LEU A N     1 
ATOM   1160  C CA    . LEU B 2 79   ? 134.431 107.121 141.972 1.00 66.85  ? 76   LEU A CA    1 
ATOM   1161  C C     . LEU B 2 79   ? 134.933 106.727 140.588 1.00 62.54  ? 76   LEU A C     1 
ATOM   1162  O O     . LEU B 2 79   ? 134.876 107.530 139.649 1.00 61.31  ? 76   LEU A O     1 
ATOM   1163  C CB    . LEU B 2 79   ? 135.582 107.625 142.842 1.00 62.16  ? 76   LEU A CB    1 
ATOM   1164  C CG    . LEU B 2 79   ? 136.338 108.858 142.346 1.00 54.99  ? 76   LEU A CG    1 
ATOM   1165  C CD1   . LEU B 2 79   ? 135.382 110.018 142.118 1.00 50.61  ? 76   LEU A CD1   1 
ATOM   1166  C CD2   . LEU B 2 79   ? 137.424 109.246 143.336 1.00 53.62  ? 76   LEU A CD2   1 
ATOM   1167  N N     . SER B 2 80   ? 135.420 105.493 140.440 1.00 62.07  ? 77   SER A N     1 
ATOM   1168  C CA    . SER B 2 80   ? 135.887 105.035 139.135 1.00 61.99  ? 77   SER A CA    1 
ATOM   1169  C C     . SER B 2 80   ? 134.743 104.964 138.133 1.00 63.06  ? 77   SER A C     1 
ATOM   1170  O O     . SER B 2 80   ? 134.917 105.304 136.956 1.00 62.63  ? 77   SER A O     1 
ATOM   1171  C CB    . SER B 2 80   ? 136.562 103.671 139.269 1.00 64.84  ? 77   SER A CB    1 
ATOM   1172  O OG    . SER B 2 80   ? 136.922 103.151 138.000 1.00 66.14  ? 77   SER A OG    1 
ATOM   1173  N N     . ALA B 2 81   ? 133.564 104.524 138.580 1.00 63.69  ? 78   ALA A N     1 
ATOM   1174  C CA    . ALA B 2 81   ? 132.429 104.409 137.670 1.00 63.04  ? 78   ALA A CA    1 
ATOM   1175  C C     . ALA B 2 81   ? 131.954 105.781 137.206 1.00 59.75  ? 78   ALA A C     1 
ATOM   1176  O O     . ALA B 2 81   ? 131.513 105.935 136.061 1.00 61.45  ? 78   ALA A O     1 
ATOM   1177  C CB    . ALA B 2 81   ? 131.290 103.645 138.341 1.00 64.74  ? 78   ALA A CB    1 
ATOM   1178  N N     . ALA B 2 82   ? 132.025 106.786 138.083 1.00 56.33  ? 79   ALA A N     1 
ATOM   1179  C CA    . ALA B 2 82   ? 131.648 108.139 137.686 1.00 56.08  ? 79   ALA A CA    1 
ATOM   1180  C C     . ALA B 2 82   ? 132.654 108.735 136.707 1.00 58.12  ? 79   ALA A C     1 
ATOM   1181  O O     . ALA B 2 82   ? 132.272 109.516 135.828 1.00 57.56  ? 79   ALA A O     1 
ATOM   1182  C CB    . ALA B 2 82   ? 131.511 109.029 138.921 1.00 55.90  ? 79   ALA A CB    1 
ATOM   1183  N N     . ILE B 2 83   ? 133.932 108.383 136.845 1.00 60.17  ? 80   ILE A N     1 
ATOM   1184  C CA    . ILE B 2 83   ? 134.933 108.829 135.881 1.00 60.66  ? 80   ILE A CA    1 
ATOM   1185  C C     . ILE B 2 83   ? 134.715 108.148 134.536 1.00 57.88  ? 80   ILE A C     1 
ATOM   1186  O O     . ILE B 2 83   ? 134.807 108.785 133.479 1.00 56.54  ? 80   ILE A O     1 
ATOM   1187  C CB    . ILE B 2 83   ? 136.350 108.573 136.427 1.00 64.17  ? 80   ILE A CB    1 
ATOM   1188  C CG1   . ILE B 2 83   ? 136.582 109.374 137.709 1.00 41.39  ? 80   ILE A CG1   1 
ATOM   1189  C CG2   . ILE B 2 83   ? 137.401 108.925 135.386 1.00 40.42  ? 80   ILE A CG2   1 
ATOM   1190  C CD1   . ILE B 2 83   ? 137.946 109.155 138.325 1.00 41.07  ? 80   ILE A CD1   1 
ATOM   1191  N N     . ASP B 2 84   ? 134.415 106.846 134.553 1.00 57.17  ? 81   ASP A N     1 
ATOM   1192  C CA    . ASP B 2 84   ? 134.188 106.117 133.309 1.00 57.86  ? 81   ASP A CA    1 
ATOM   1193  C C     . ASP B 2 84   ? 132.963 106.642 132.571 1.00 57.68  ? 81   ASP A C     1 
ATOM   1194  O O     . ASP B 2 84   ? 132.991 106.804 131.345 1.00 55.78  ? 81   ASP A O     1 
ATOM   1195  C CB    . ASP B 2 84   ? 134.037 104.623 133.594 1.00 62.59  ? 81   ASP A CB    1 
ATOM   1196  C CG    . ASP B 2 84   ? 135.358 103.953 133.906 1.00 67.37  ? 81   ASP A CG    1 
ATOM   1197  O OD1   . ASP B 2 84   ? 136.342 104.675 134.168 1.00 66.53  ? 81   ASP A OD1   1 
ATOM   1198  O OD2   . ASP B 2 84   ? 135.412 102.705 133.894 1.00 71.57  ? 81   ASP A OD2   1 
ATOM   1199  N N     . SER B 2 85   ? 131.878 106.913 133.301 1.00 60.14  ? 82   SER A N     1 
ATOM   1200  C CA    . SER B 2 85   ? 130.650 107.366 132.657 1.00 61.49  ? 82   SER A CA    1 
ATOM   1201  C C     . SER B 2 85   ? 130.813 108.742 132.026 1.00 60.13  ? 82   SER A C     1 
ATOM   1202  O O     . SER B 2 85   ? 130.205 109.019 130.986 1.00 60.87  ? 82   SER A O     1 
ATOM   1203  C CB    . SER B 2 85   ? 129.499 107.377 133.663 1.00 61.30  ? 82   SER A CB    1 
ATOM   1204  O OG    . SER B 2 85   ? 129.101 106.058 134.000 1.00 61.66  ? 82   SER A OG    1 
ATOM   1205  N N     . TYR B 2 86   ? 131.623 109.615 132.629 1.00 58.96  ? 83   TYR A N     1 
ATOM   1206  C CA    . TYR B 2 86   ? 131.829 110.938 132.046 1.00 59.49  ? 83   TYR A CA    1 
ATOM   1207  C C     . TYR B 2 86   ? 132.699 110.858 130.796 1.00 60.01  ? 83   TYR A C     1 
ATOM   1208  O O     . TYR B 2 86   ? 132.461 111.582 129.823 1.00 60.47  ? 83   TYR A O     1 
ATOM   1209  C CB    . TYR B 2 86   ? 132.445 111.885 133.077 1.00 59.79  ? 83   TYR A CB    1 
ATOM   1210  C CG    . TYR B 2 86   ? 132.640 113.290 132.555 1.00 59.83  ? 83   TYR A CG    1 
ATOM   1211  C CD1   . TYR B 2 86   ? 131.608 113.958 131.908 1.00 61.96  ? 83   TYR A CD1   1 
ATOM   1212  C CD2   . TYR B 2 86   ? 133.850 113.952 132.714 1.00 56.76  ? 83   TYR A CD2   1 
ATOM   1213  C CE1   . TYR B 2 86   ? 131.778 115.242 131.425 1.00 61.29  ? 83   TYR A CE1   1 
ATOM   1214  C CE2   . TYR B 2 86   ? 134.029 115.238 132.238 1.00 56.87  ? 83   TYR A CE2   1 
ATOM   1215  C CZ    . TYR B 2 86   ? 132.989 115.877 131.594 1.00 60.40  ? 83   TYR A CZ    1 
ATOM   1216  O OH    . TYR B 2 86   ? 133.159 117.157 131.118 1.00 61.83  ? 83   TYR A OH    1 
ATOM   1217  N N     . ARG B 2 87   ? 133.711 109.987 130.806 1.00 60.14  ? 84   ARG A N     1 
ATOM   1218  C CA    . ARG B 2 87   ? 134.501 109.770 129.599 1.00 60.01  ? 84   ARG A CA    1 
ATOM   1219  C C     . ARG B 2 87   ? 133.702 109.025 128.536 1.00 61.04  ? 84   ARG A C     1 
ATOM   1220  O O     . ARG B 2 87   ? 133.952 109.200 127.338 1.00 55.45  ? 84   ARG A O     1 
ATOM   1221  C CB    . ARG B 2 87   ? 135.780 109.003 129.935 1.00 59.11  ? 84   ARG A CB    1 
ATOM   1222  C CG    . ARG B 2 87   ? 136.711 109.725 130.896 1.00 59.11  ? 84   ARG A CG    1 
ATOM   1223  C CD    . ARG B 2 87   ? 137.896 108.850 131.268 1.00 59.60  ? 84   ARG A CD    1 
ATOM   1224  N NE    . ARG B 2 87   ? 138.773 109.493 132.240 1.00 59.81  ? 84   ARG A NE    1 
ATOM   1225  C CZ    . ARG B 2 87   ? 139.791 108.888 132.844 1.00 60.93  ? 84   ARG A CZ    1 
ATOM   1226  N NH1   . ARG B 2 87   ? 140.058 107.617 132.577 1.00 61.84  ? 84   ARG A NH1   1 
ATOM   1227  N NH2   . ARG B 2 87   ? 140.538 109.550 133.717 1.00 59.37  ? 84   ARG A NH2   1 
ATOM   1228  N N     . LYS B 2 88   ? 132.746 108.196 128.953 1.00 66.49  ? 85   LYS A N     1 
ATOM   1229  C CA    . LYS B 2 88   ? 131.898 107.453 128.029 1.00 73.50  ? 85   LYS A CA    1 
ATOM   1230  C C     . LYS B 2 88   ? 130.937 108.405 127.325 1.00 78.32  ? 85   LYS A C     1 
ATOM   1231  O O     . LYS B 2 88   ? 131.052 108.631 126.116 1.00 77.46  ? 85   LYS A O     1 
ATOM   1232  C CB    . LYS B 2 88   ? 131.134 106.359 128.779 1.00 74.93  ? 85   LYS A CB    1 
ATOM   1233  C CG    . LYS B 2 88   ? 130.992 105.035 128.036 1.00 73.49  ? 85   LYS A CG    1 
ATOM   1234  C CD    . LYS B 2 88   ? 129.912 105.096 126.969 1.00 74.66  ? 85   LYS A CD    1 
ATOM   1235  C CE    . LYS B 2 88   ? 129.451 103.700 126.574 1.00 77.90  ? 85   LYS A CE    1 
ATOM   1236  N NZ    . LYS B 2 88   ? 130.584 102.826 126.160 1.00 78.09  ? 85   LYS A NZ    1 
ATOM   1237  N N     . GLU B 2 89   ? 129.991 108.967 128.071 1.00 85.09  ? 86   GLU A N     1 
ATOM   1238  C CA    . GLU B 2 89   ? 129.076 109.978 127.557 1.00 87.26  ? 86   GLU A CA    1 
ATOM   1239  C C     . GLU B 2 89   ? 129.529 111.354 128.029 1.00 86.95  ? 86   GLU A C     1 
ATOM   1240  O O     . GLU B 2 89   ? 129.711 111.575 129.231 1.00 87.92  ? 86   GLU A O     1 
ATOM   1241  C CB    . GLU B 2 89   ? 127.640 109.713 128.017 1.00 89.93  ? 86   GLU A CB    1 
ATOM   1242  C CG    . GLU B 2 89   ? 126.818 108.840 127.073 1.00 94.70  ? 86   GLU A CG    1 
ATOM   1243  C CD    . GLU B 2 89   ? 126.814 107.375 127.470 1.00 98.50  ? 86   GLU A CD    1 
ATOM   1244  O OE1   . GLU B 2 89   ? 127.551 107.008 128.410 1.00 99.08  ? 86   GLU A OE1   1 
ATOM   1245  O OE2   . GLU B 2 89   ? 126.066 106.593 126.845 1.00 100.51 ? 86   GLU A OE2   1 
ATOM   1246  N N     . LYS B 2 90   ? 129.709 112.273 127.084 1.00 85.57  ? 87   LYS A N     1 
ATOM   1247  C CA    . LYS B 2 90   ? 130.142 113.635 127.394 1.00 82.07  ? 87   LYS A CA    1 
ATOM   1248  C C     . LYS B 2 90   ? 128.951 114.567 127.604 1.00 81.28  ? 87   LYS A C     1 
ATOM   1249  O O     . LYS B 2 90   ? 128.877 115.653 127.033 1.00 82.27  ? 87   LYS A O     1 
ATOM   1250  C CB    . LYS B 2 90   ? 131.056 114.159 126.290 1.00 79.64  ? 87   LYS A CB    1 
ATOM   1251  C CG    . LYS B 2 90   ? 132.355 113.382 126.106 1.00 77.99  ? 87   LYS A CG    1 
ATOM   1252  C CD    . LYS B 2 90   ? 132.210 112.277 125.069 1.00 80.07  ? 87   LYS A CD    1 
ATOM   1253  C CE    . LYS B 2 90   ? 133.559 111.667 124.717 1.00 81.40  ? 87   LYS A CE    1 
ATOM   1254  N NZ    . LYS B 2 90   ? 134.250 111.108 125.911 1.00 82.33  ? 87   LYS A NZ    1 
ATOM   1255  N N     . THR B 2 91   ? 128.004 114.142 128.431 1.00 82.09  ? 88   THR A N     1 
ATOM   1256  C CA    . THR B 2 91   ? 126.808 114.919 128.714 1.00 83.14  ? 88   THR A CA    1 
ATOM   1257  C C     . THR B 2 91   ? 126.946 115.644 130.047 1.00 82.62  ? 88   THR A C     1 
ATOM   1258  O O     . THR B 2 91   ? 127.700 115.232 130.933 1.00 83.80  ? 88   THR A O     1 
ATOM   1259  C CB    . THR B 2 91   ? 125.562 114.027 128.725 1.00 87.46  ? 88   THR A CB    1 
ATOM   1260  O OG1   . THR B 2 91   ? 124.428 114.788 129.158 1.00 91.55  ? 88   THR A OG1   1 
ATOM   1261  C CG2   . THR B 2 91   ? 125.758 112.840 129.657 1.00 87.64  ? 88   THR A CG2   1 
ATOM   1262  N N     . GLU B 2 92   ? 126.202 116.747 130.175 1.00 81.31  ? 89   GLU A N     1 
ATOM   1263  C CA    . GLU B 2 92   ? 126.244 117.551 131.391 1.00 79.08  ? 89   GLU A CA    1 
ATOM   1264  C C     . GLU B 2 92   ? 125.694 116.806 132.601 1.00 78.11  ? 89   GLU A C     1 
ATOM   1265  O O     . GLU B 2 92   ? 125.986 117.194 133.738 1.00 77.47  ? 89   GLU A O     1 
ATOM   1266  C CB    . GLU B 2 92   ? 125.472 118.855 131.186 1.00 78.95  ? 89   GLU A CB    1 
ATOM   1267  N N     . GLU B 2 93   ? 124.902 115.753 132.385 1.00 76.90  ? 90   GLU A N     1 
ATOM   1268  C CA    . GLU B 2 93   ? 124.400 114.971 133.509 1.00 75.54  ? 90   GLU A CA    1 
ATOM   1269  C C     . GLU B 2 93   ? 125.510 114.135 134.135 1.00 73.52  ? 90   GLU A C     1 
ATOM   1270  O O     . GLU B 2 93   ? 125.591 114.022 135.363 1.00 71.81  ? 90   GLU A O     1 
ATOM   1271  C CB    . GLU B 2 93   ? 123.239 114.085 133.056 1.00 75.97  ? 90   GLU A CB    1 
ATOM   1272  C CG    . GLU B 2 93   ? 122.587 113.273 134.170 1.00 77.60  ? 90   GLU A CG    1 
ATOM   1273  C CD    . GLU B 2 93   ? 123.286 111.950 134.422 1.00 80.21  ? 90   GLU A CD    1 
ATOM   1274  O OE1   . GLU B 2 93   ? 123.801 111.354 133.452 1.00 79.93  ? 90   GLU A OE1   1 
ATOM   1275  O OE2   . GLU B 2 93   ? 123.330 111.514 135.590 1.00 82.82  ? 90   GLU A OE2   1 
ATOM   1276  N N     . THR B 2 94   ? 126.374 113.544 133.307 1.00 73.51  ? 91   THR A N     1 
ATOM   1277  C CA    . THR B 2 94   ? 127.480 112.756 133.838 1.00 73.44  ? 91   THR A CA    1 
ATOM   1278  C C     . THR B 2 94   ? 128.561 113.642 134.443 1.00 71.42  ? 91   THR A C     1 
ATOM   1279  O O     . THR B 2 94   ? 129.309 113.191 135.319 1.00 71.30  ? 91   THR A O     1 
ATOM   1280  C CB    . THR B 2 94   ? 128.072 111.865 132.746 1.00 75.50  ? 91   THR A CB    1 
ATOM   1281  O OG1   . THR B 2 94   ? 128.382 112.662 131.594 1.00 76.80  ? 91   THR A OG1   1 
ATOM   1282  C CG2   . THR B 2 94   ? 127.085 110.775 132.356 1.00 77.65  ? 91   THR A CG2   1 
ATOM   1283  N N     . ARG B 2 95   ? 128.662 114.894 133.994 1.00 72.07  ? 92   ARG A N     1 
ATOM   1284  C CA    . ARG B 2 95   ? 129.616 115.816 134.600 1.00 71.33  ? 92   ARG A CA    1 
ATOM   1285  C C     . ARG B 2 95   ? 129.187 116.187 136.014 1.00 69.67  ? 92   ARG A C     1 
ATOM   1286  O O     . ARG B 2 95   ? 129.987 116.117 136.954 1.00 70.46  ? 92   ARG A O     1 
ATOM   1287  C CB    . ARG B 2 95   ? 129.765 117.070 133.738 1.00 77.35  ? 92   ARG A CB    1 
ATOM   1288  C CG    . ARG B 2 95   ? 131.087 117.799 133.938 1.00 83.35  ? 92   ARG A CG    1 
ATOM   1289  C CD    . ARG B 2 95   ? 130.913 119.313 134.002 1.00 89.54  ? 92   ARG A CD    1 
ATOM   1290  N NE    . ARG B 2 95   ? 130.054 119.828 132.941 1.00 95.56  ? 92   ARG A NE    1 
ATOM   1291  C CZ    . ARG B 2 95   ? 128.834 120.316 133.141 1.00 100.09 ? 92   ARG A CZ    1 
ATOM   1292  N NH1   . ARG B 2 95   ? 128.330 120.366 134.367 1.00 102.26 ? 92   ARG A NH1   1 
ATOM   1293  N NH2   . ARG B 2 95   ? 128.118 120.762 132.116 1.00 100.52 ? 92   ARG A NH2   1 
ATOM   1294  N N     . ASN B 2 96   ? 127.921 116.581 136.181 1.00 67.36  ? 93   ASN A N     1 
ATOM   1295  C CA    . ASN B 2 96   ? 127.418 116.922 137.507 1.00 65.01  ? 93   ASN A CA    1 
ATOM   1296  C C     . ASN B 2 96   ? 127.423 115.714 138.433 1.00 60.28  ? 93   ASN A C     1 
ATOM   1297  O O     . ASN B 2 96   ? 127.587 115.865 139.651 1.00 58.84  ? 93   ASN A O     1 
ATOM   1298  C CB    . ASN B 2 96   ? 126.009 117.505 137.403 1.00 68.48  ? 93   ASN A CB    1 
ATOM   1299  C CG    . ASN B 2 96   ? 125.980 118.830 136.669 1.00 72.30  ? 93   ASN A CG    1 
ATOM   1300  O OD1   . ASN B 2 96   ? 126.971 119.239 136.064 1.00 72.69  ? 93   ASN A OD1   1 
ATOM   1301  N ND2   . ASN B 2 96   ? 124.839 119.506 136.716 1.00 75.13  ? 93   ASN A ND2   1 
ATOM   1302  N N     . ALA B 2 97   ? 127.238 114.513 137.883 1.00 58.13  ? 94   ALA A N     1 
ATOM   1303  C CA    . ALA B 2 97   ? 127.324 113.311 138.703 1.00 56.83  ? 94   ALA A CA    1 
ATOM   1304  C C     . ALA B 2 97   ? 128.744 113.094 139.209 1.00 56.60  ? 94   ALA A C     1 
ATOM   1305  O O     . ALA B 2 97   ? 128.945 112.679 140.356 1.00 57.66  ? 94   ALA A O     1 
ATOM   1306  C CB    . ALA B 2 97   ? 126.842 112.098 137.908 1.00 55.85  ? 94   ALA A CB    1 
ATOM   1307  N N     . LEU B 2 98   ? 129.742 113.376 138.369 1.00 55.31  ? 95   LEU A N     1 
ATOM   1308  C CA    . LEU B 2 98   ? 131.130 113.241 138.802 1.00 55.64  ? 95   LEU A CA    1 
ATOM   1309  C C     . LEU B 2 98   ? 131.507 114.330 139.797 1.00 56.49  ? 95   LEU A C     1 
ATOM   1310  O O     . LEU B 2 98   ? 132.242 114.072 140.756 1.00 57.90  ? 95   LEU A O     1 
ATOM   1311  C CB    . LEU B 2 98   ? 132.061 113.272 137.589 1.00 55.45  ? 95   LEU A CB    1 
ATOM   1312  C CG    . LEU B 2 98   ? 133.560 113.196 137.880 1.00 40.33  ? 95   LEU A CG    1 
ATOM   1313  C CD1   . LEU B 2 98   ? 133.890 111.965 138.707 1.00 43.74  ? 95   LEU A CD1   1 
ATOM   1314  C CD2   . LEU B 2 98   ? 134.356 113.202 136.586 1.00 39.45  ? 95   LEU A CD2   1 
ATOM   1315  N N     . ILE B 2 99   ? 131.011 115.553 139.588 1.00 55.24  ? 96   ILE A N     1 
ATOM   1316  C CA    . ILE B 2 99   ? 131.319 116.652 140.501 1.00 54.80  ? 96   ILE A CA    1 
ATOM   1317  C C     . ILE B 2 99   ? 130.766 116.362 141.891 1.00 57.37  ? 96   ILE A C     1 
ATOM   1318  O O     . ILE B 2 99   ? 131.426 116.623 142.904 1.00 57.51  ? 96   ILE A O     1 
ATOM   1319  C CB    . ILE B 2 99   ? 130.777 117.980 139.938 1.00 52.47  ? 96   ILE A CB    1 
ATOM   1320  C CG1   . ILE B 2 99   ? 131.524 118.358 138.657 1.00 48.58  ? 96   ILE A CG1   1 
ATOM   1321  C CG2   . ILE B 2 99   ? 130.891 119.090 140.972 1.00 52.51  ? 96   ILE A CG2   1 
ATOM   1322  C CD1   . ILE B 2 99   ? 131.028 119.634 138.014 1.00 46.40  ? 96   ILE A CD1   1 
ATOM   1323  N N     . GLU B 2 100  ? 129.552 115.813 141.963 1.00 61.07  ? 97   GLU A N     1 
ATOM   1324  C CA    . GLU B 2 100  ? 128.994 115.440 143.258 1.00 63.16  ? 97   GLU A CA    1 
ATOM   1325  C C     . GLU B 2 100  ? 129.735 114.251 143.857 1.00 61.32  ? 97   GLU A C     1 
ATOM   1326  O O     . GLU B 2 100  ? 129.966 114.205 145.071 1.00 61.31  ? 97   GLU A O     1 
ATOM   1327  C CB    . GLU B 2 100  ? 127.504 115.129 143.127 1.00 70.39  ? 97   GLU A CB    1 
ATOM   1328  C CG    . GLU B 2 100  ? 126.640 116.335 142.804 1.00 76.09  ? 97   GLU A CG    1 
ATOM   1329  C CD    . GLU B 2 100  ? 125.161 116.037 142.942 1.00 82.26  ? 97   GLU A CD    1 
ATOM   1330  O OE1   . GLU B 2 100  ? 124.820 114.924 143.395 1.00 84.96  ? 97   GLU A OE1   1 
ATOM   1331  O OE2   . GLU B 2 100  ? 124.341 116.914 142.598 1.00 83.79  ? 97   GLU A OE2   1 
ATOM   1332  N N     . GLU B 2 101  ? 130.111 113.280 143.022 1.00 60.35  ? 98   GLU A N     1 
ATOM   1333  C CA    . GLU B 2 101  ? 130.832 112.114 143.526 1.00 62.79  ? 98   GLU A CA    1 
ATOM   1334  C C     . GLU B 2 101  ? 132.190 112.510 144.086 1.00 60.33  ? 98   GLU A C     1 
ATOM   1335  O O     . GLU B 2 101  ? 132.635 111.966 145.104 1.00 59.75  ? 98   GLU A O     1 
ATOM   1336  C CB    . GLU B 2 101  ? 130.990 111.073 142.419 1.00 66.23  ? 98   GLU A CB    1 
ATOM   1337  C CG    . GLU B 2 101  ? 131.396 109.699 142.924 1.00 69.85  ? 98   GLU A CG    1 
ATOM   1338  C CD    . GLU B 2 101  ? 130.291 109.027 143.714 1.00 75.65  ? 98   GLU A CD    1 
ATOM   1339  O OE1   . GLU B 2 101  ? 129.113 109.174 143.327 1.00 78.48  ? 98   GLU A OE1   1 
ATOM   1340  O OE2   . GLU B 2 101  ? 130.596 108.357 144.723 1.00 78.09  ? 98   GLU A OE2   1 
ATOM   1341  N N     . GLN B 2 102  ? 132.867 113.460 143.433 1.00 57.89  ? 99   GLN A N     1 
ATOM   1342  C CA    . GLN B 2 102  ? 134.139 113.948 143.952 1.00 53.92  ? 99   GLN A CA    1 
ATOM   1343  C C     . GLN B 2 102  ? 133.948 114.688 145.272 1.00 53.36  ? 99   GLN A C     1 
ATOM   1344  O O     . GLN B 2 102  ? 134.739 114.514 146.206 1.00 53.06  ? 99   GLN A O     1 
ATOM   1345  C CB    . GLN B 2 102  ? 134.816 114.851 142.923 1.00 50.83  ? 99   GLN A CB    1 
ATOM   1346  C CG    . GLN B 2 102  ? 135.260 114.132 141.661 1.00 48.83  ? 99   GLN A CG    1 
ATOM   1347  C CD    . GLN B 2 102  ? 135.616 115.090 140.543 1.00 44.98  ? 99   GLN A CD    1 
ATOM   1348  O OE1   . GLN B 2 102  ? 135.370 116.292 140.639 1.00 46.87  ? 99   GLN A OE1   1 
ATOM   1349  N NE2   . GLN B 2 102  ? 136.198 114.562 139.473 1.00 42.28  ? 99   GLN A NE2   1 
ATOM   1350  N N     . ALA B 2 103  ? 132.903 115.513 145.364 1.00 53.05  ? 100  ALA A N     1 
ATOM   1351  C CA    . ALA B 2 103  ? 132.636 116.232 146.606 1.00 54.63  ? 100  ALA A CA    1 
ATOM   1352  C C     . ALA B 2 103  ? 132.320 115.277 147.750 1.00 57.18  ? 100  ALA A C     1 
ATOM   1353  O O     . ALA B 2 103  ? 132.661 115.559 148.904 1.00 58.73  ? 100  ALA A O     1 
ATOM   1354  C CB    . ALA B 2 103  ? 131.486 117.220 146.407 1.00 53.32  ? 100  ALA A CB    1 
ATOM   1355  N N     . THR B 2 104  ? 131.675 114.148 147.453 1.00 57.84  ? 101  THR A N     1 
ATOM   1356  C CA    . THR B 2 104  ? 131.399 113.159 148.489 1.00 60.57  ? 101  THR A CA    1 
ATOM   1357  C C     . THR B 2 104  ? 132.689 112.528 149.000 1.00 62.07  ? 101  THR A C     1 
ATOM   1358  O O     . THR B 2 104  ? 132.865 112.353 150.213 1.00 63.41  ? 101  THR A O     1 
ATOM   1359  C CB    . THR B 2 104  ? 130.450 112.085 147.954 1.00 61.73  ? 101  THR A CB    1 
ATOM   1360  O OG1   . THR B 2 104  ? 129.207 112.689 147.574 1.00 62.40  ? 101  THR A OG1   1 
ATOM   1361  C CG2   . THR B 2 104  ? 130.187 111.023 149.012 1.00 62.46  ? 101  THR A CG2   1 
ATOM   1362  N N     . TYR B 2 105  ? 133.607 112.189 148.092 1.00 61.96  ? 102  TYR A N     1 
ATOM   1363  C CA    . TYR B 2 105  ? 134.871 111.588 148.511 1.00 63.27  ? 102  TYR A CA    1 
ATOM   1364  C C     . TYR B 2 105  ? 135.750 112.592 149.245 1.00 62.70  ? 102  TYR A C     1 
ATOM   1365  O O     . TYR B 2 105  ? 136.452 112.228 150.195 1.00 63.79  ? 102  TYR A O     1 
ATOM   1366  C CB    . TYR B 2 105  ? 135.605 111.009 147.301 1.00 63.32  ? 102  TYR A CB    1 
ATOM   1367  C CG    . TYR B 2 105  ? 135.207 109.590 146.967 1.00 64.22  ? 102  TYR A CG    1 
ATOM   1368  C CD1   . TYR B 2 105  ? 134.136 109.325 146.124 1.00 64.37  ? 102  TYR A CD1   1 
ATOM   1369  C CD2   . TYR B 2 105  ? 135.905 108.512 147.497 1.00 64.75  ? 102  TYR A CD2   1 
ATOM   1370  C CE1   . TYR B 2 105  ? 133.771 108.028 145.817 1.00 65.84  ? 102  TYR A CE1   1 
ATOM   1371  C CE2   . TYR B 2 105  ? 135.547 107.211 147.195 1.00 66.56  ? 102  TYR A CE2   1 
ATOM   1372  C CZ    . TYR B 2 105  ? 134.481 106.975 146.354 1.00 66.41  ? 102  TYR A CZ    1 
ATOM   1373  O OH    . TYR B 2 105  ? 134.121 105.681 146.052 1.00 66.14  ? 102  TYR A OH    1 
ATOM   1374  N N     . ARG B 2 106  ? 135.730 113.859 148.819 1.00 60.46  ? 103  ARG A N     1 
ATOM   1375  C CA    . ARG B 2 106  ? 136.514 114.876 149.515 1.00 59.30  ? 103  ARG A CA    1 
ATOM   1376  C C     . ARG B 2 106  ? 136.038 115.047 150.953 1.00 61.36  ? 103  ARG A C     1 
ATOM   1377  O O     . ARG B 2 106  ? 136.852 115.229 151.866 1.00 62.56  ? 103  ARG A O     1 
ATOM   1378  C CB    . ARG B 2 106  ? 136.447 116.209 148.767 1.00 56.63  ? 103  ARG A CB    1 
ATOM   1379  C CG    . ARG B 2 106  ? 137.131 116.207 147.408 1.00 51.75  ? 103  ARG A CG    1 
ATOM   1380  C CD    . ARG B 2 106  ? 137.331 117.622 146.886 1.00 47.67  ? 103  ARG A CD    1 
ATOM   1381  N NE    . ARG B 2 106  ? 136.094 118.398 146.892 1.00 49.19  ? 103  ARG A NE    1 
ATOM   1382  C CZ    . ARG B 2 106  ? 135.276 118.513 145.851 1.00 50.08  ? 103  ARG A CZ    1 
ATOM   1383  N NH1   . ARG B 2 106  ? 135.560 117.904 144.708 1.00 50.40  ? 103  ARG A NH1   1 
ATOM   1384  N NH2   . ARG B 2 106  ? 134.173 119.243 145.950 1.00 49.39  ? 103  ARG A NH2   1 
ATOM   1385  N N     . ASN B 2 107  ? 134.722 114.984 151.172 1.00 61.62  ? 104  ASN A N     1 
ATOM   1386  C CA    . ASN B 2 107  ? 134.199 115.066 152.533 1.00 63.17  ? 104  ASN A CA    1 
ATOM   1387  C C     . ASN B 2 107  ? 134.541 113.821 153.340 1.00 65.54  ? 104  ASN A C     1 
ATOM   1388  O O     . ASN B 2 107  ? 134.745 113.912 154.557 1.00 68.30  ? 104  ASN A O     1 
ATOM   1389  C CB    . ASN B 2 107  ? 132.685 115.283 152.505 1.00 65.58  ? 104  ASN A CB    1 
ATOM   1390  C CG    . ASN B 2 107  ? 132.301 116.655 151.985 1.00 68.26  ? 104  ASN A CG    1 
ATOM   1391  O OD1   . ASN B 2 107  ? 132.972 117.649 152.265 1.00 70.18  ? 104  ASN A OD1   1 
ATOM   1392  N ND2   . ASN B 2 107  ? 131.215 116.715 151.221 1.00 68.13  ? 104  ASN A ND2   1 
ATOM   1393  N N     . ALA B 2 108  ? 134.607 112.657 152.689 1.00 67.05  ? 105  ALA A N     1 
ATOM   1394  C CA    . ALA B 2 108  ? 134.991 111.437 153.392 1.00 70.46  ? 105  ALA A CA    1 
ATOM   1395  C C     . ALA B 2 108  ? 136.409 111.539 153.935 1.00 71.65  ? 105  ALA A C     1 
ATOM   1396  O O     . ALA B 2 108  ? 136.695 111.063 155.041 1.00 74.61  ? 105  ALA A O     1 
ATOM   1397  C CB    . ALA B 2 108  ? 134.855 110.230 152.464 1.00 70.09  ? 105  ALA A CB    1 
ATOM   1398  N N     . ILE B 2 109  ? 137.313 112.156 153.171 1.00 68.34  ? 106  ILE A N     1 
ATOM   1399  C CA    . ILE B 2 109  ? 138.657 112.419 153.676 1.00 66.72  ? 106  ILE A CA    1 
ATOM   1400  C C     . ILE B 2 109  ? 138.619 113.514 154.735 1.00 70.90  ? 106  ILE A C     1 
ATOM   1401  O O     . ILE B 2 109  ? 139.336 113.451 155.741 1.00 72.92  ? 106  ILE A O     1 
ATOM   1402  C CB    . ILE B 2 109  ? 139.598 112.791 152.516 1.00 60.73  ? 106  ILE A CB    1 
ATOM   1403  C CG1   . ILE B 2 109  ? 139.469 111.784 151.370 1.00 59.82  ? 106  ILE A CG1   1 
ATOM   1404  C CG2   . ILE B 2 109  ? 141.038 112.871 153.002 1.00 58.67  ? 106  ILE A CG2   1 
ATOM   1405  C CD1   . ILE B 2 109  ? 139.916 110.388 151.726 1.00 61.82  ? 106  ILE A CD1   1 
ATOM   1406  N N     . HIS B 2 110  ? 137.777 114.531 154.526 1.00 71.32  ? 107  HIS A N     1 
ATOM   1407  C CA    . HIS B 2 110  ? 137.690 115.641 155.468 1.00 72.60  ? 107  HIS A CA    1 
ATOM   1408  C C     . HIS B 2 110  ? 137.176 115.188 156.828 1.00 76.50  ? 107  HIS A C     1 
ATOM   1409  O O     . HIS B 2 110  ? 137.573 115.745 157.857 1.00 78.56  ? 107  HIS A O     1 
ATOM   1410  C CB    . HIS B 2 110  ? 136.784 116.733 154.895 1.00 70.77  ? 107  HIS A CB    1 
ATOM   1411  C CG    . HIS B 2 110  ? 136.780 118.003 155.688 1.00 71.02  ? 107  HIS A CG    1 
ATOM   1412  N ND1   . HIS B 2 110  ? 137.852 118.866 155.717 1.00 71.06  ? 107  HIS A ND1   1 
ATOM   1413  C CD2   . HIS B 2 110  ? 135.827 118.559 156.473 1.00 71.82  ? 107  HIS A CD2   1 
ATOM   1414  C CE1   . HIS B 2 110  ? 137.563 119.899 156.489 1.00 71.62  ? 107  HIS A CE1   1 
ATOM   1415  N NE2   . HIS B 2 110  ? 136.340 119.737 156.960 1.00 72.27  ? 107  HIS A NE2   1 
ATOM   1416  N N     . ASP B 2 111  ? 136.296 114.185 156.854 1.00 78.28  ? 108  ASP A N     1 
ATOM   1417  C CA    . ASP B 2 111  ? 135.766 113.694 158.121 1.00 80.94  ? 108  ASP A CA    1 
ATOM   1418  C C     . ASP B 2 111  ? 136.833 113.005 158.965 1.00 84.57  ? 108  ASP A C     1 
ATOM   1419  O O     . ASP B 2 111  ? 136.663 112.899 160.183 1.00 86.53  ? 108  ASP A O     1 
ATOM   1420  C CB    . ASP B 2 111  ? 134.595 112.743 157.868 1.00 81.41  ? 108  ASP A CB    1 
ATOM   1421  C CG    . ASP B 2 111  ? 133.389 113.448 157.272 1.00 80.91  ? 108  ASP A CG    1 
ATOM   1422  O OD1   . ASP B 2 111  ? 133.271 114.681 157.443 1.00 80.12  ? 108  ASP A OD1   1 
ATOM   1423  O OD2   . ASP B 2 111  ? 132.555 112.769 156.635 1.00 81.63  ? 108  ASP A OD2   1 
ATOM   1424  N N     . TYR B 2 112  ? 137.921 112.534 158.350 1.00 84.67  ? 109  TYR A N     1 
ATOM   1425  C CA    . TYR B 2 112  ? 139.047 112.038 159.134 1.00 84.08  ? 109  TYR A CA    1 
ATOM   1426  C C     . TYR B 2 112  ? 139.768 113.171 159.853 1.00 81.45  ? 109  TYR A C     1 
ATOM   1427  O O     . TYR B 2 112  ? 140.275 112.979 160.963 1.00 82.19  ? 109  TYR A O     1 
ATOM   1428  C CB    . TYR B 2 112  ? 140.022 111.274 158.236 1.00 82.25  ? 109  TYR A CB    1 
ATOM   1429  C CG    . TYR B 2 112  ? 139.658 109.821 158.022 1.00 83.64  ? 109  TYR A CG    1 
ATOM   1430  C CD1   . TYR B 2 112  ? 138.683 109.454 157.104 1.00 83.07  ? 109  TYR A CD1   1 
ATOM   1431  C CD2   . TYR B 2 112  ? 140.297 108.815 158.733 1.00 86.48  ? 109  TYR A CD2   1 
ATOM   1432  C CE1   . TYR B 2 112  ? 138.350 108.126 156.905 1.00 84.08  ? 109  TYR A CE1   1 
ATOM   1433  C CE2   . TYR B 2 112  ? 139.972 107.484 158.542 1.00 87.75  ? 109  TYR A CE2   1 
ATOM   1434  C CZ    . TYR B 2 112  ? 138.998 107.146 157.626 1.00 86.17  ? 109  TYR A CZ    1 
ATOM   1435  O OH    . TYR B 2 112  ? 138.672 105.822 157.433 1.00 86.77  ? 109  TYR A OH    1 
ATOM   1436  N N     . PHE B 2 113  ? 139.821 114.355 159.237 1.00 78.56  ? 110  PHE A N     1 
ATOM   1437  C CA    . PHE B 2 113  ? 140.468 115.500 159.870 1.00 74.76  ? 110  PHE A CA    1 
ATOM   1438  C C     . PHE B 2 113  ? 139.623 116.046 161.014 1.00 74.35  ? 110  PHE A C     1 
ATOM   1439  O O     . PHE B 2 113  ? 140.111 116.200 162.141 1.00 73.98  ? 110  PHE A O     1 
ATOM   1440  C CB    . PHE B 2 113  ? 140.729 116.593 158.831 1.00 72.17  ? 110  PHE A CB    1 
ATOM   1441  C CG    . PHE B 2 113  ? 141.742 116.214 157.789 1.00 70.91  ? 110  PHE A CG    1 
ATOM   1442  C CD1   . PHE B 2 113  ? 142.889 115.523 158.137 1.00 72.33  ? 110  PHE A CD1   1 
ATOM   1443  C CD2   . PHE B 2 113  ? 141.545 116.554 156.460 1.00 69.41  ? 110  PHE A CD2   1 
ATOM   1444  C CE1   . PHE B 2 113  ? 143.823 115.175 157.180 1.00 70.99  ? 110  PHE A CE1   1 
ATOM   1445  C CE2   . PHE B 2 113  ? 142.475 116.209 155.497 1.00 68.24  ? 110  PHE A CE2   1 
ATOM   1446  C CZ    . PHE B 2 113  ? 143.616 115.519 155.857 1.00 69.17  ? 110  PHE A CZ    1 
ATOM   1447  N N     . ILE B 2 114  ? 138.351 116.345 160.742 1.00 74.31  ? 111  ILE A N     1 
ATOM   1448  C CA    . ILE B 2 114  ? 137.492 116.970 161.743 1.00 74.06  ? 111  ILE A CA    1 
ATOM   1449  C C     . ILE B 2 114  ? 136.889 115.962 162.711 1.00 75.11  ? 111  ILE A C     1 
ATOM   1450  O O     . ILE B 2 114  ? 136.406 116.354 163.780 1.00 75.36  ? 111  ILE A O     1 
ATOM   1451  C CB    . ILE B 2 114  ? 136.367 117.774 161.071 1.00 69.34  ? 111  ILE A CB    1 
ATOM   1452  C CG1   . ILE B 2 114  ? 135.417 116.841 160.316 1.00 67.28  ? 111  ILE A CG1   1 
ATOM   1453  C CG2   . ILE B 2 114  ? 136.947 118.816 160.130 1.00 65.32  ? 111  ILE A CG2   1 
ATOM   1454  C CD1   . ILE B 2 114  ? 134.244 117.553 159.672 1.00 64.89  ? 111  ILE A CD1   1 
ATOM   1455  N N     . GLY B 2 115  ? 136.894 114.676 162.368 1.00 76.02  ? 112  GLY A N     1 
ATOM   1456  C CA    . GLY B 2 115  ? 136.343 113.664 163.247 1.00 78.49  ? 112  GLY A CA    1 
ATOM   1457  C C     . GLY B 2 115  ? 134.839 113.523 163.145 1.00 81.82  ? 112  GLY A C     1 
ATOM   1458  O O     . GLY B 2 115  ? 134.125 113.732 164.130 1.00 84.29  ? 112  GLY A O     1 
ATOM   1459  N N     . ARG B 2 116  ? 134.344 113.161 161.962 1.00 84.28  ? 113  ARG A N     1 
ATOM   1460  C CA    . ARG B 2 116  ? 132.924 112.890 161.747 1.00 87.18  ? 113  ARG A CA    1 
ATOM   1461  C C     . ARG B 2 116  ? 132.745 111.759 160.743 1.00 88.25  ? 113  ARG A C     1 
ATOM   1462  O O     . ARG B 2 116  ? 131.823 111.774 159.921 1.00 87.26  ? 113  ARG A O     1 
ATOM   1463  C CB    . ARG B 2 116  ? 132.176 114.138 161.277 1.00 86.81  ? 113  ARG A CB    1 
ATOM   1464  C CG    . ARG B 2 116  ? 131.789 115.106 162.384 1.00 89.08  ? 113  ARG A CG    1 
ATOM   1465  C CD    . ARG B 2 116  ? 130.646 116.007 161.940 1.00 90.55  ? 113  ARG A CD    1 
ATOM   1466  N NE    . ARG B 2 116  ? 130.373 117.072 162.900 1.00 94.37  ? 113  ARG A NE    1 
ATOM   1467  C CZ    . ARG B 2 116  ? 129.581 116.944 163.959 1.00 99.89  ? 113  ARG A CZ    1 
ATOM   1468  N NH1   . ARG B 2 116  ? 128.977 115.789 164.205 1.00 102.79 ? 113  ARG A NH1   1 
ATOM   1469  N NH2   . ARG B 2 116  ? 129.393 117.972 164.776 1.00 100.99 ? 113  ARG A NH2   1 
ATOM   1470  N N     . THR B 2 117  ? 133.627 110.766 160.796 1.00 90.66  ? 114  THR A N     1 
ATOM   1471  C CA    . THR B 2 117  ? 133.553 109.600 159.927 1.00 93.05  ? 114  THR A CA    1 
ATOM   1472  C C     . THR B 2 117  ? 133.088 108.392 160.728 1.00 97.06  ? 114  THR A C     1 
ATOM   1473  O O     . THR B 2 117  ? 133.502 108.196 161.875 1.00 97.34  ? 114  THR A O     1 
ATOM   1474  C CB    . THR B 2 117  ? 134.906 109.310 159.267 1.00 93.92  ? 114  THR A CB    1 
ATOM   1475  O OG1   . THR B 2 117  ? 134.841 108.066 158.557 1.00 95.05  ? 114  THR A OG1   1 
ATOM   1476  C CG2   . THR B 2 117  ? 136.017 109.245 160.307 1.00 95.80  ? 114  THR A CG2   1 
ATOM   1477  N N     . ASP B 2 118  ? 132.219 107.583 160.118 1.00 100.12 ? 115  ASP A N     1 
ATOM   1478  C CA    . ASP B 2 118  ? 131.691 106.402 160.787 1.00 104.58 ? 115  ASP A CA    1 
ATOM   1479  C C     . ASP B 2 118  ? 132.705 105.268 160.877 1.00 105.97 ? 115  ASP A C     1 
ATOM   1480  O O     . ASP B 2 118  ? 132.413 104.249 161.509 1.00 107.71 ? 115  ASP A O     1 
ATOM   1481  C CB    . ASP B 2 118  ? 130.433 105.907 160.067 1.00 104.27 ? 115  ASP A CB    1 
ATOM   1482  C CG    . ASP B 2 118  ? 129.318 106.934 160.066 1.00 103.27 ? 115  ASP A CG    1 
ATOM   1483  O OD1   . ASP B 2 118  ? 129.251 107.744 161.015 1.00 103.23 ? 115  ASP A OD1   1 
ATOM   1484  O OD2   . ASP B 2 118  ? 128.506 106.932 159.117 1.00 102.66 ? 115  ASP A OD2   1 
ATOM   1485  N N     . ASN B 2 119  ? 133.882 105.421 160.267 1.00 106.41 ? 116  ASN A N     1 
ATOM   1486  C CA    . ASN B 2 119  ? 134.876 104.356 160.260 1.00 110.52 ? 116  ASN A CA    1 
ATOM   1487  C C     . ASN B 2 119  ? 135.694 104.297 161.546 1.00 114.11 ? 116  ASN A C     1 
ATOM   1488  O O     . ASN B 2 119  ? 136.313 103.265 161.818 1.00 116.13 ? 116  ASN A O     1 
ATOM   1489  C CB    . ASN B 2 119  ? 135.816 104.524 159.064 1.00 110.84 ? 116  ASN A CB    1 
ATOM   1490  C CG    . ASN B 2 119  ? 135.071 104.627 157.747 1.00 111.20 ? 116  ASN A CG    1 
ATOM   1491  O OD1   . ASN B 2 119  ? 133.996 104.049 157.582 1.00 113.05 ? 116  ASN A OD1   1 
ATOM   1492  N ND2   . ASN B 2 119  ? 135.638 105.368 156.801 1.00 108.73 ? 116  ASN A ND2   1 
ATOM   1493  N N     . LEU B 2 120  ? 135.710 105.369 162.331 1.00 114.46 ? 117  LEU A N     1 
ATOM   1494  C CA    . LEU B 2 120  ? 136.490 105.434 163.558 1.00 115.36 ? 117  LEU A CA    1 
ATOM   1495  C C     . LEU B 2 120  ? 135.572 105.536 164.771 1.00 117.05 ? 117  LEU A C     1 
ATOM   1496  O O     . LEU B 2 120  ? 134.471 106.088 164.695 1.00 114.30 ? 117  LEU A O     1 
ATOM   1497  C CB    . LEU B 2 120  ? 137.455 106.622 163.534 1.00 113.00 ? 117  LEU A CB    1 
ATOM   1498  C CG    . LEU B 2 120  ? 138.557 106.556 162.475 1.00 110.16 ? 117  LEU A CG    1 
ATOM   1499  C CD1   . LEU B 2 120  ? 139.472 107.765 162.576 1.00 108.32 ? 117  LEU A CD1   1 
ATOM   1500  C CD2   . LEU B 2 120  ? 139.348 105.265 162.612 1.00 111.92 ? 117  LEU A CD2   1 
ATOM   1501  N N     . THR B 2 121  ? 136.043 104.997 165.893 1.00 120.81 ? 118  THR A N     1 
ATOM   1502  C CA    . THR B 2 121  ? 135.263 104.986 167.120 1.00 122.13 ? 118  THR A CA    1 
ATOM   1503  C C     . THR B 2 121  ? 135.232 106.373 167.758 1.00 120.17 ? 118  THR A C     1 
ATOM   1504  O O     . THR B 2 121  ? 136.043 107.249 167.448 1.00 119.17 ? 118  THR A O     1 
ATOM   1505  C CB    . THR B 2 121  ? 135.829 103.971 168.111 1.00 123.23 ? 118  THR A CB    1 
ATOM   1506  O OG1   . THR B 2 121  ? 137.246 104.164 168.240 1.00 121.30 ? 118  THR A OG1   1 
ATOM   1507  C CG2   . THR B 2 121  ? 135.553 102.551 167.637 1.00 123.88 ? 118  THR A CG2   1 
ATOM   1508  N N     . ASP B 2 122  ? 134.284 106.552 168.685 1.00 120.85 ? 119  ASP A N     1 
ATOM   1509  C CA    . ASP B 2 122  ? 134.039 107.871 169.266 1.00 120.25 ? 119  ASP A CA    1 
ATOM   1510  C C     . ASP B 2 122  ? 135.264 108.397 170.005 1.00 120.86 ? 119  ASP A C     1 
ATOM   1511  O O     . ASP B 2 122  ? 135.540 109.601 169.978 1.00 116.86 ? 119  ASP A O     1 
ATOM   1512  C CB    . ASP B 2 122  ? 132.836 107.809 170.207 1.00 123.00 ? 119  ASP A CB    1 
ATOM   1513  C CG    . ASP B 2 122  ? 131.640 107.125 169.578 1.00 123.51 ? 119  ASP A CG    1 
ATOM   1514  O OD1   . ASP B 2 122  ? 131.845 106.213 168.750 1.00 123.76 ? 119  ASP A OD1   1 
ATOM   1515  O OD2   . ASP B 2 122  ? 130.495 107.496 169.912 1.00 123.23 ? 119  ASP A OD2   1 
ATOM   1516  N N     . ALA B 2 123  ? 136.005 107.513 170.677 1.00 124.96 ? 120  ALA A N     1 
ATOM   1517  C CA    . ALA B 2 123  ? 137.189 107.948 171.412 1.00 125.52 ? 120  ALA A CA    1 
ATOM   1518  C C     . ALA B 2 123  ? 138.236 108.531 170.470 1.00 122.28 ? 120  ALA A C     1 
ATOM   1519  O O     . ALA B 2 123  ? 138.809 109.593 170.739 1.00 123.01 ? 120  ALA A O     1 
ATOM   1520  C CB    . ALA B 2 123  ? 137.768 106.780 172.210 1.00 127.62 ? 120  ALA A CB    1 
ATOM   1521  N N     . ILE B 2 124  ? 138.495 107.846 169.355 1.00 118.43 ? 121  ILE A N     1 
ATOM   1522  C CA    . ILE B 2 124  ? 139.446 108.358 168.375 1.00 113.10 ? 121  ILE A CA    1 
ATOM   1523  C C     . ILE B 2 124  ? 138.829 109.503 167.579 1.00 108.01 ? 121  ILE A C     1 
ATOM   1524  O O     . ILE B 2 124  ? 139.508 110.477 167.233 1.00 106.68 ? 121  ILE A O     1 
ATOM   1525  C CB    . ILE B 2 124  ? 139.923 107.221 167.454 1.00 114.71 ? 121  ILE A CB    1 
ATOM   1526  C CG1   . ILE B 2 124  ? 140.469 106.057 168.283 1.00 118.87 ? 121  ILE A CG1   1 
ATOM   1527  C CG2   . ILE B 2 124  ? 140.977 107.724 166.478 1.00 113.27 ? 121  ILE A CG2   1 
ATOM   1528  C CD1   . ILE B 2 124  ? 140.882 104.860 167.455 1.00 119.43 ? 121  ILE A CD1   1 
ATOM   1529  N N     . ASN B 2 125  ? 137.530 109.408 167.285 1.00 102.76 ? 122  ASN A N     1 
ATOM   1530  C CA    . ASN B 2 125  ? 136.875 110.414 166.458 1.00 97.74  ? 122  ASN A CA    1 
ATOM   1531  C C     . ASN B 2 125  ? 136.796 111.760 167.169 1.00 96.00  ? 122  ASN A C     1 
ATOM   1532  O O     . ASN B 2 125  ? 136.967 112.811 166.539 1.00 96.25  ? 122  ASN A O     1 
ATOM   1533  C CB    . ASN B 2 125  ? 135.480 109.928 166.064 1.00 98.17  ? 122  ASN A CB    1 
ATOM   1534  C CG    . ASN B 2 125  ? 134.823 110.811 165.031 1.00 97.33  ? 122  ASN A CG    1 
ATOM   1535  O OD1   . ASN B 2 125  ? 135.031 110.640 163.829 1.00 95.67  ? 122  ASN A OD1   1 
ATOM   1536  N ND2   . ASN B 2 125  ? 134.013 111.756 165.492 1.00 98.25  ? 122  ASN A ND2   1 
ATOM   1537  N N     . LYS B 2 126  ? 136.541 111.753 168.478 1.00 95.44  ? 123  LYS A N     1 
ATOM   1538  C CA    . LYS B 2 126  ? 136.438 113.006 169.221 1.00 92.61  ? 123  LYS A CA    1 
ATOM   1539  C C     . LYS B 2 126  ? 137.804 113.614 169.510 1.00 91.88  ? 123  LYS A C     1 
ATOM   1540  O O     . LYS B 2 126  ? 137.911 114.836 169.663 1.00 86.71  ? 123  LYS A O     1 
ATOM   1541  C CB    . LYS B 2 126  ? 135.676 112.784 170.529 1.00 94.32  ? 123  LYS A CB    1 
ATOM   1542  N N     . ARG B 2 127  ? 138.851 112.789 169.589 1.00 95.36  ? 124  ARG A N     1 
ATOM   1543  C CA    . ARG B 2 127  ? 140.188 113.312 169.856 1.00 94.83  ? 124  ARG A CA    1 
ATOM   1544  C C     . ARG B 2 127  ? 140.687 114.188 168.715 1.00 92.57  ? 124  ARG A C     1 
ATOM   1545  O O     . ARG B 2 127  ? 141.429 115.149 168.952 1.00 93.81  ? 124  ARG A O     1 
ATOM   1546  C CB    . ARG B 2 127  ? 141.163 112.162 170.108 1.00 94.10  ? 124  ARG A CB    1 
ATOM   1547  N N     . HIS B 2 128  ? 140.295 113.877 167.475 1.00 90.07  ? 125  HIS A N     1 
ATOM   1548  C CA    . HIS B 2 128  ? 140.698 114.703 166.344 1.00 87.44  ? 125  HIS A CA    1 
ATOM   1549  C C     . HIS B 2 128  ? 139.993 116.054 166.354 1.00 88.43  ? 125  HIS A C     1 
ATOM   1550  O O     . HIS B 2 128  ? 140.578 117.058 165.930 1.00 86.28  ? 125  HIS A O     1 
ATOM   1551  C CB    . HIS B 2 128  ? 140.416 113.972 165.032 1.00 88.75  ? 125  HIS A CB    1 
ATOM   1552  C CG    . HIS B 2 128  ? 141.267 112.759 164.821 1.00 93.75  ? 125  HIS A CG    1 
ATOM   1553  N ND1   . HIS B 2 128  ? 140.888 111.717 164.001 1.00 94.52  ? 125  HIS A ND1   1 
ATOM   1554  C CD2   . HIS B 2 128  ? 142.481 112.423 165.317 1.00 96.27  ? 125  HIS A CD2   1 
ATOM   1555  C CE1   . HIS B 2 128  ? 141.829 110.791 164.004 1.00 94.82  ? 125  HIS A CE1   1 
ATOM   1556  N NE2   . HIS B 2 128  ? 142.807 111.195 164.796 1.00 95.91  ? 125  HIS A NE2   1 
ATOM   1557  N N     . ALA B 2 129  ? 138.746 116.100 166.830 1.00 91.97  ? 126  ALA A N     1 
ATOM   1558  C CA    . ALA B 2 129  ? 138.013 117.361 166.863 1.00 92.28  ? 126  ALA A CA    1 
ATOM   1559  C C     . ALA B 2 129  ? 138.634 118.338 167.853 1.00 94.29  ? 126  ALA A C     1 
ATOM   1560  O O     . ALA B 2 129  ? 138.650 119.551 167.610 1.00 91.61  ? 126  ALA A O     1 
ATOM   1561  C CB    . ALA B 2 129  ? 136.547 117.108 167.205 1.00 92.60  ? 126  ALA A CB    1 
ATOM   1562  N N     . GLU B 2 130  ? 139.148 117.832 168.977 1.00 99.36  ? 127  GLU A N     1 
ATOM   1563  C CA    . GLU B 2 130  ? 139.809 118.695 169.948 1.00 103.55 ? 127  GLU A CA    1 
ATOM   1564  C C     . GLU B 2 130  ? 141.095 119.295 169.396 1.00 104.67 ? 127  GLU A C     1 
ATOM   1565  O O     . GLU B 2 130  ? 141.548 120.331 169.894 1.00 104.69 ? 127  GLU A O     1 
ATOM   1566  C CB    . GLU B 2 130  ? 140.102 117.919 171.233 1.00 107.12 ? 127  GLU A CB    1 
ATOM   1567  N N     . ILE B 2 131  ? 141.685 118.666 168.385 1.00 107.27 ? 128  ILE A N     1 
ATOM   1568  C CA    . ILE B 2 131  ? 142.888 119.191 167.744 1.00 105.30 ? 128  ILE A CA    1 
ATOM   1569  C C     . ILE B 2 131  ? 142.537 120.127 166.597 1.00 100.49 ? 128  ILE A C     1 
ATOM   1570  O O     . ILE B 2 131  ? 143.109 121.212 166.470 1.00 100.10 ? 128  ILE A O     1 
ATOM   1571  C CB    . ILE B 2 131  ? 143.775 118.025 167.264 1.00 106.95 ? 128  ILE A CB    1 
ATOM   1572  C CG1   . ILE B 2 131  ? 144.129 117.111 168.437 1.00 110.84 ? 128  ILE A CG1   1 
ATOM   1573  C CG2   . ILE B 2 131  ? 145.029 118.554 166.584 1.00 106.26 ? 128  ILE A CG2   1 
ATOM   1574  C CD1   . ILE B 2 131  ? 144.933 115.897 168.037 1.00 111.75 ? 128  ILE A CD1   1 
ATOM   1575  N N     . TYR B 2 132  ? 141.592 119.722 165.744 1.00 94.08  ? 129  TYR A N     1 
ATOM   1576  C CA    . TYR B 2 132  ? 141.216 120.542 164.599 1.00 86.96  ? 129  TYR A CA    1 
ATOM   1577  C C     . TYR B 2 132  ? 140.560 121.849 165.021 1.00 82.73  ? 129  TYR A C     1 
ATOM   1578  O O     . TYR B 2 132  ? 140.604 122.824 164.264 1.00 81.42  ? 129  TYR A O     1 
ATOM   1579  C CB    . TYR B 2 132  ? 140.282 119.755 163.677 1.00 84.76  ? 129  TYR A CB    1 
ATOM   1580  C CG    . TYR B 2 132  ? 140.042 120.403 162.329 1.00 81.18  ? 129  TYR A CG    1 
ATOM   1581  C CD1   . TYR B 2 132  ? 140.902 120.170 161.263 1.00 78.83  ? 129  TYR A CD1   1 
ATOM   1582  C CD2   . TYR B 2 132  ? 138.951 121.236 162.122 1.00 79.94  ? 129  TYR A CD2   1 
ATOM   1583  C CE1   . TYR B 2 132  ? 140.685 120.755 160.029 1.00 77.71  ? 129  TYR A CE1   1 
ATOM   1584  C CE2   . TYR B 2 132  ? 138.727 121.827 160.891 1.00 77.78  ? 129  TYR A CE2   1 
ATOM   1585  C CZ    . TYR B 2 132  ? 139.595 121.582 159.849 1.00 77.28  ? 129  TYR A CZ    1 
ATOM   1586  O OH    . TYR B 2 132  ? 139.374 122.166 158.621 1.00 75.16  ? 129  TYR A OH    1 
ATOM   1587  N N     . LYS B 2 133  ? 139.960 121.894 166.212 1.00 83.28  ? 130  LYS A N     1 
ATOM   1588  C CA    . LYS B 2 133  ? 139.348 123.130 166.690 1.00 82.82  ? 130  LYS A CA    1 
ATOM   1589  C C     . LYS B 2 133  ? 140.403 124.201 166.940 1.00 83.85  ? 130  LYS A C     1 
ATOM   1590  O O     . LYS B 2 133  ? 140.309 125.315 166.411 1.00 83.27  ? 130  LYS A O     1 
ATOM   1591  C CB    . LYS B 2 133  ? 138.541 122.858 167.959 1.00 84.76  ? 130  LYS A CB    1 
ATOM   1592  N N     . GLY B 2 134  ? 141.419 123.879 167.737 1.00 84.65  ? 131  GLY A N     1 
ATOM   1593  C CA    . GLY B 2 134  ? 142.487 124.818 168.015 1.00 84.56  ? 131  GLY A CA    1 
ATOM   1594  C C     . GLY B 2 134  ? 143.660 124.676 167.068 1.00 81.10  ? 131  GLY A C     1 
ATOM   1595  O O     . GLY B 2 134  ? 144.810 124.911 167.448 1.00 81.11  ? 131  GLY A O     1 
ATOM   1596  N N     . LEU B 2 135  ? 143.378 124.291 165.825 1.00 78.28  ? 132  LEU A N     1 
ATOM   1597  C CA    . LEU B 2 135  ? 144.417 124.083 164.826 1.00 75.48  ? 132  LEU A CA    1 
ATOM   1598  C C     . LEU B 2 135  ? 144.684 125.321 163.980 1.00 73.01  ? 132  LEU A C     1 
ATOM   1599  O O     . LEU B 2 135  ? 145.679 125.347 163.247 1.00 69.06  ? 132  LEU A O     1 
ATOM   1600  C CB    . LEU B 2 135  ? 144.032 122.914 163.911 1.00 72.22  ? 132  LEU A CB    1 
ATOM   1601  C CG    . LEU B 2 135  ? 145.160 122.200 163.165 1.00 70.29  ? 132  LEU A CG    1 
ATOM   1602  C CD1   . LEU B 2 135  ? 146.140 121.577 164.146 1.00 71.12  ? 132  LEU A CD1   1 
ATOM   1603  C CD2   . LEU B 2 135  ? 144.588 121.150 162.229 1.00 69.68  ? 132  LEU A CD2   1 
ATOM   1604  N N     . PHE B 2 136  ? 143.833 126.344 164.068 1.00 77.39  ? 133  PHE A N     1 
ATOM   1605  C CA    . PHE B 2 136  ? 143.964 127.539 163.243 1.00 78.23  ? 133  PHE A CA    1 
ATOM   1606  C C     . PHE B 2 136  ? 143.866 128.808 164.081 1.00 80.21  ? 133  PHE A C     1 
ATOM   1607  O O     . PHE B 2 136  ? 143.373 129.835 163.605 1.00 78.46  ? 133  PHE A O     1 
ATOM   1608  C CB    . PHE B 2 136  ? 142.914 127.548 162.132 1.00 77.98  ? 133  PHE A CB    1 
ATOM   1609  C CG    . PHE B 2 136  ? 142.863 126.273 161.343 1.00 79.56  ? 133  PHE A CG    1 
ATOM   1610  C CD1   . PHE B 2 136  ? 143.762 126.042 160.316 1.00 80.67  ? 133  PHE A CD1   1 
ATOM   1611  C CD2   . PHE B 2 136  ? 141.917 125.303 161.632 1.00 80.49  ? 133  PHE A CD2   1 
ATOM   1612  C CE1   . PHE B 2 136  ? 143.719 124.867 159.590 1.00 80.62  ? 133  PHE A CE1   1 
ATOM   1613  C CE2   . PHE B 2 136  ? 141.870 124.126 160.910 1.00 80.79  ? 133  PHE A CE2   1 
ATOM   1614  C CZ    . PHE B 2 136  ? 142.771 123.907 159.886 1.00 80.86  ? 133  PHE A CZ    1 
ATOM   1615  N N     . LYS B 2 137  ? 144.329 128.756 165.323 1.00 80.68  ? 134  LYS A N     1 
ATOM   1616  C CA    . LYS B 2 137  ? 144.366 129.935 166.180 1.00 82.22  ? 134  LYS A CA    1 
ATOM   1617  C C     . LYS B 2 137  ? 145.479 129.742 167.207 1.00 84.97  ? 134  LYS A C     1 
ATOM   1618  O O     . LYS B 2 137  ? 146.388 128.928 167.011 1.00 86.22  ? 134  LYS A O     1 
ATOM   1619  C CB    . LYS B 2 137  ? 142.982 130.193 166.802 1.00 82.22  ? 134  LYS A CB    1 
ATOM   1620  C CG    . LYS B 2 137  ? 142.220 128.950 167.227 1.00 80.69  ? 134  LYS A CG    1 
ATOM   1621  C CD    . LYS B 2 137  ? 140.807 129.322 167.654 1.00 77.48  ? 134  LYS A CD    1 
ATOM   1622  C CE    . LYS B 2 137  ? 139.981 128.096 167.997 1.00 76.40  ? 134  LYS A CE    1 
ATOM   1623  N NZ    . LYS B 2 137  ? 138.588 128.463 168.370 1.00 75.88  ? 134  LYS A NZ    1 
ATOM   1624  N N     . ALA B 2 138  ? 145.406 130.489 168.312 1.00 86.78  ? 135  ALA A N     1 
ATOM   1625  C CA    . ALA B 2 138  ? 146.510 130.568 169.264 1.00 93.94  ? 135  ALA A CA    1 
ATOM   1626  C C     . ALA B 2 138  ? 146.818 129.249 169.961 1.00 112.24 ? 135  ALA A C     1 
ATOM   1627  O O     . ALA B 2 138  ? 147.845 129.161 170.643 1.00 129.30 ? 135  ALA A O     1 
ATOM   1628  C CB    . ALA B 2 138  ? 146.219 131.641 170.312 1.00 116.29 ? 135  ALA A CB    1 
ATOM   1629  N N     . GLU B 2 139  ? 145.973 128.226 169.814 1.00 109.33 ? 136  GLU A N     1 
ATOM   1630  C CA    . GLU B 2 139  ? 146.226 126.961 170.494 1.00 113.99 ? 136  GLU A CA    1 
ATOM   1631  C C     . GLU B 2 139  ? 147.395 126.186 169.896 1.00 114.10 ? 136  GLU A C     1 
ATOM   1632  O O     . GLU B 2 139  ? 147.848 125.218 170.514 1.00 116.37 ? 136  GLU A O     1 
ATOM   1633  C CB    . GLU B 2 139  ? 144.966 126.094 170.483 1.00 116.25 ? 136  GLU A CB    1 
ATOM   1634  C CG    . GLU B 2 139  ? 143.786 126.719 171.209 1.00 119.26 ? 136  GLU A CG    1 
ATOM   1635  C CD    . GLU B 2 139  ? 142.659 125.734 171.451 1.00 121.80 ? 136  GLU A CD    1 
ATOM   1636  O OE1   . GLU B 2 139  ? 142.929 124.515 171.481 1.00 123.52 ? 136  GLU A OE1   1 
ATOM   1637  O OE2   . GLU B 2 139  ? 141.503 126.178 171.610 1.00 121.83 ? 136  GLU A OE2   1 
ATOM   1638  N N     . LEU B 2 140  ? 147.884 126.578 168.717 1.00 107.02 ? 137  LEU A N     1 
ATOM   1639  C CA    . LEU B 2 140  ? 149.107 125.978 168.189 1.00 101.61 ? 137  LEU A CA    1 
ATOM   1640  C C     . LEU B 2 140  ? 150.292 126.259 169.105 1.00 103.71 ? 137  LEU A C     1 
ATOM   1641  O O     . LEU B 2 140  ? 151.172 125.407 169.275 1.00 107.16 ? 137  LEU A O     1 
ATOM   1642  C CB    . LEU B 2 140  ? 149.397 126.513 166.787 1.00 94.93  ? 137  LEU A CB    1 
ATOM   1643  C CG    . LEU B 2 140  ? 148.546 126.048 165.606 1.00 89.43  ? 137  LEU A CG    1 
ATOM   1644  C CD1   . LEU B 2 140  ? 148.910 126.852 164.372 1.00 86.10  ? 137  LEU A CD1   1 
ATOM   1645  C CD2   . LEU B 2 140  ? 148.742 124.562 165.356 1.00 87.84  ? 137  LEU A CD2   1 
ATOM   1646  N N     . PHE B 2 141  ? 150.324 127.448 169.703 1.00 103.02 ? 138  PHE A N     1 
ATOM   1647  C CA    . PHE B 2 141  ? 151.456 127.900 170.500 1.00 105.69 ? 138  PHE A CA    1 
ATOM   1648  C C     . PHE B 2 141  ? 151.402 127.414 171.940 1.00 110.93 ? 138  PHE A C     1 
ATOM   1649  O O     . PHE B 2 141  ? 152.416 127.496 172.642 1.00 112.12 ? 138  PHE A O     1 
ATOM   1650  C CB    . PHE B 2 141  ? 151.527 129.429 170.472 1.00 105.68 ? 138  PHE A CB    1 
ATOM   1651  C CG    . PHE B 2 141  ? 151.541 130.012 169.083 1.00 103.39 ? 138  PHE A CG    1 
ATOM   1652  C CD1   . PHE B 2 141  ? 150.363 130.171 168.370 1.00 100.97 ? 138  PHE A CD1   1 
ATOM   1653  C CD2   . PHE B 2 141  ? 152.731 130.405 168.494 1.00 103.07 ? 138  PHE A CD2   1 
ATOM   1654  C CE1   . PHE B 2 141  ? 150.371 130.702 167.096 1.00 97.47  ? 138  PHE A CE1   1 
ATOM   1655  C CE2   . PHE B 2 141  ? 152.745 130.941 167.220 1.00 100.07 ? 138  PHE A CE2   1 
ATOM   1656  C CZ    . PHE B 2 141  ? 151.564 131.088 166.520 1.00 96.94  ? 138  PHE A CZ    1 
ATOM   1657  N N     . ASN B 2 142  ? 150.250 126.915 172.397 1.00 114.51 ? 139  ASN A N     1 
ATOM   1658  C CA    . ASN B 2 142  ? 150.145 126.378 173.746 1.00 118.97 ? 139  ASN A CA    1 
ATOM   1659  C C     . ASN B 2 142  ? 151.041 125.166 173.957 1.00 121.33 ? 139  ASN A C     1 
ATOM   1660  O O     . ASN B 2 142  ? 151.329 124.814 175.106 1.00 123.03 ? 139  ASN A O     1 
ATOM   1661  C CB    . ASN B 2 142  ? 148.701 125.976 174.048 1.00 118.90 ? 139  ASN A CB    1 
ATOM   1662  C CG    . ASN B 2 142  ? 147.727 127.118 173.867 1.00 117.27 ? 139  ASN A CG    1 
ATOM   1663  O OD1   . ASN B 2 142  ? 148.118 128.234 173.531 1.00 115.83 ? 139  ASN A OD1   1 
ATOM   1664  N ND2   . ASN B 2 142  ? 146.447 126.841 174.083 1.00 117.24 ? 139  ASN A ND2   1 
ATOM   1665  N N     . GLY B 2 143  ? 151.487 124.527 172.880 1.00 121.35 ? 140  GLY A N     1 
ATOM   1666  C CA    . GLY B 2 143  ? 152.014 123.187 172.978 1.00 124.23 ? 140  GLY A CA    1 
ATOM   1667  C C     . GLY B 2 143  ? 150.964 122.136 173.245 1.00 125.94 ? 140  GLY A C     1 
ATOM   1668  O O     . GLY B 2 143  ? 151.302 120.949 173.306 1.00 127.20 ? 140  GLY A O     1 
ATOM   1669  N N     . LYS B 2 144  ? 149.698 122.538 173.404 1.00 126.32 ? 141  LYS A N     1 
ATOM   1670  C CA    . LYS B 2 144  ? 148.630 121.581 173.661 1.00 127.37 ? 141  LYS A CA    1 
ATOM   1671  C C     . LYS B 2 144  ? 148.452 120.634 172.483 1.00 126.44 ? 141  LYS A C     1 
ATOM   1672  O O     . LYS B 2 144  ? 148.430 119.412 172.658 1.00 128.10 ? 141  LYS A O     1 
ATOM   1673  C CB    . LYS B 2 144  ? 147.326 122.321 173.963 1.00 126.48 ? 141  LYS A CB    1 
ATOM   1674  N N     . VAL B 2 145  ? 148.332 121.181 171.271 1.00 123.65 ? 142  VAL A N     1 
ATOM   1675  C CA    . VAL B 2 145  ? 148.201 120.340 170.083 1.00 121.53 ? 142  VAL A CA    1 
ATOM   1676  C C     . VAL B 2 145  ? 149.425 119.443 169.933 1.00 123.73 ? 142  VAL A C     1 
ATOM   1677  O O     . VAL B 2 145  ? 149.305 118.254 169.614 1.00 122.20 ? 142  VAL A O     1 
ATOM   1678  C CB    . VAL B 2 145  ? 147.961 121.211 168.835 1.00 118.95 ? 142  VAL A CB    1 
ATOM   1679  C CG1   . VAL B 2 145  ? 146.554 121.789 168.862 1.00 118.40 ? 142  VAL A CG1   1 
ATOM   1680  C CG2   . VAL B 2 145  ? 148.980 122.336 168.762 1.00 119.55 ? 142  VAL A CG2   1 
ATOM   1681  N N     . LEU B 2 146  ? 150.614 119.989 170.188 1.00 126.87 ? 143  LEU A N     1 
ATOM   1682  C CA    . LEU B 2 146  ? 151.817 119.170 170.222 1.00 128.66 ? 143  LEU A CA    1 
ATOM   1683  C C     . LEU B 2 146  ? 151.830 118.226 171.418 1.00 134.39 ? 143  LEU A C     1 
ATOM   1684  O O     . LEU B 2 146  ? 152.474 117.173 171.353 1.00 133.38 ? 143  LEU A O     1 
ATOM   1685  C CB    . LEU B 2 146  ? 153.054 120.075 170.216 1.00 125.15 ? 143  LEU A CB    1 
ATOM   1686  C CG    . LEU B 2 146  ? 154.366 119.616 170.850 1.00 124.33 ? 143  LEU A CG    1 
ATOM   1687  C CD1   . LEU B 2 146  ? 155.506 119.720 169.852 1.00 121.41 ? 143  LEU A CD1   1 
ATOM   1688  C CD2   . LEU B 2 146  ? 154.659 120.456 172.081 1.00 126.05 ? 143  LEU A CD2   1 
ATOM   1689  N N     . LYS B 2 147  ? 151.119 118.564 172.496 1.00 142.81 ? 144  LYS A N     1 
ATOM   1690  C CA    . LYS B 2 147  ? 150.990 117.623 173.603 1.00 146.04 ? 144  LYS A CA    1 
ATOM   1691  C C     . LYS B 2 147  ? 150.100 116.441 173.233 1.00 145.97 ? 144  LYS A C     1 
ATOM   1692  O O     . LYS B 2 147  ? 150.312 115.333 173.739 1.00 149.19 ? 144  LYS A O     1 
ATOM   1693  C CB    . LYS B 2 147  ? 150.450 118.325 174.850 1.00 147.77 ? 144  LYS A CB    1 
ATOM   1694  N N     . GLN B 2 148  ? 149.105 116.650 172.362 1.00 137.88 ? 145  GLN A N     1 
ATOM   1695  C CA    . GLN B 2 148  ? 148.329 115.514 171.869 1.00 130.71 ? 145  GLN A CA    1 
ATOM   1696  C C     . GLN B 2 148  ? 149.173 114.621 170.970 1.00 127.34 ? 145  GLN A C     1 
ATOM   1697  O O     . GLN B 2 148  ? 148.901 113.422 170.856 1.00 129.20 ? 145  GLN A O     1 
ATOM   1698  C CB    . GLN B 2 148  ? 147.080 115.977 171.108 1.00 123.13 ? 145  GLN A CB    1 
ATOM   1699  C CG    . GLN B 2 148  ? 146.617 117.392 171.412 1.00 119.79 ? 145  GLN A CG    1 
ATOM   1700  C CD    . GLN B 2 148  ? 145.173 117.469 171.876 1.00 119.01 ? 145  GLN A CD    1 
ATOM   1701  O OE1   . GLN B 2 148  ? 144.514 116.443 172.063 1.00 117.50 ? 145  GLN A OE1   1 
ATOM   1702  N NE2   . GLN B 2 148  ? 144.670 118.683 172.058 1.00 120.01 ? 145  GLN A NE2   1 
ATOM   1703  N N     . LEU B 2 149  ? 150.196 115.185 170.337 1.00 122.10 ? 146  LEU A N     1 
ATOM   1704  C CA    . LEU B 2 149  ? 151.052 114.436 169.426 1.00 117.84 ? 146  LEU A CA    1 
ATOM   1705  C C     . LEU B 2 149  ? 152.303 113.934 170.140 1.00 118.91 ? 146  LEU A C     1 
ATOM   1706  O O     . LEU B 2 149  ? 152.611 112.742 170.112 1.00 119.01 ? 146  LEU A O     1 
ATOM   1707  C CB    . LEU B 2 149  ? 151.441 115.306 168.227 1.00 113.63 ? 146  LEU A CB    1 
ATOM   1708  C CG    . LEU B 2 149  ? 150.491 115.425 167.025 1.00 110.55 ? 146  LEU A CG    1 
ATOM   1709  C CD1   . LEU B 2 149  ? 149.043 115.126 167.386 1.00 111.34 ? 146  LEU A CD1   1 
ATOM   1710  C CD2   . LEU B 2 149  ? 150.606 116.810 166.396 1.00 107.90 ? 146  LEU A CD2   1 
ATOM   1711  N N     . THR B 2 153  ? 157.826 117.528 171.890 1.00 113.34 ? 150  THR A N     1 
ATOM   1712  C CA    . THR B 2 153  ? 158.405 118.350 172.944 1.00 118.25 ? 150  THR A CA    1 
ATOM   1713  C C     . THR B 2 153  ? 159.207 119.504 172.352 1.00 117.75 ? 150  THR A C     1 
ATOM   1714  O O     . THR B 2 153  ? 160.039 119.312 171.467 1.00 116.11 ? 150  THR A O     1 
ATOM   1715  C CB    . THR B 2 153  ? 159.308 117.521 173.884 1.00 122.60 ? 150  THR A CB    1 
ATOM   1716  O OG1   . THR B 2 153  ? 160.273 116.795 173.113 1.00 122.26 ? 150  THR A OG1   1 
ATOM   1717  C CG2   . THR B 2 153  ? 158.476 116.546 174.710 1.00 124.04 ? 150  THR A CG2   1 
ATOM   1718  N N     . THR B 2 154  ? 158.941 120.707 172.850 1.00 119.02 ? 151  THR A N     1 
ATOM   1719  C CA    . THR B 2 154  ? 159.593 121.913 172.366 1.00 118.47 ? 151  THR A CA    1 
ATOM   1720  C C     . THR B 2 154  ? 161.005 122.033 172.937 1.00 121.21 ? 151  THR A C     1 
ATOM   1721  O O     . THR B 2 154  ? 161.274 121.631 174.072 1.00 122.91 ? 151  THR A O     1 
ATOM   1722  C CB    . THR B 2 154  ? 158.761 123.142 172.750 1.00 118.38 ? 151  THR A CB    1 
ATOM   1723  O OG1   . THR B 2 154  ? 157.404 122.953 172.329 1.00 116.23 ? 151  THR A OG1   1 
ATOM   1724  C CG2   . THR B 2 154  ? 159.308 124.403 172.106 1.00 116.75 ? 151  THR A CG2   1 
ATOM   1725  N N     . THR B 2 155  ? 161.914 122.574 172.126 1.00 121.09 ? 152  THR A N     1 
ATOM   1726  C CA    . THR B 2 155  ? 163.270 122.884 172.553 1.00 121.57 ? 152  THR A CA    1 
ATOM   1727  C C     . THR B 2 155  ? 163.360 124.358 172.937 1.00 121.81 ? 152  THR A C     1 
ATOM   1728  O O     . THR B 2 155  ? 162.504 125.168 172.569 1.00 120.92 ? 152  THR A O     1 
ATOM   1729  C CB    . THR B 2 155  ? 164.286 122.564 171.449 1.00 116.03 ? 152  THR A CB    1 
ATOM   1730  O OG1   . THR B 2 155  ? 164.339 123.647 170.511 1.00 112.08 ? 152  THR A OG1   1 
ATOM   1731  C CG2   . THR B 2 155  ? 163.893 121.294 170.710 1.00 112.06 ? 152  THR A CG2   1 
ATOM   1732  N N     . GLU B 2 156  ? 164.417 124.701 173.680 1.00 123.10 ? 153  GLU A N     1 
ATOM   1733  C CA    . GLU B 2 156  ? 164.519 126.038 174.263 1.00 121.92 ? 153  GLU A CA    1 
ATOM   1734  C C     . GLU B 2 156  ? 164.508 127.127 173.194 1.00 118.78 ? 153  GLU A C     1 
ATOM   1735  O O     . GLU B 2 156  ? 163.837 128.154 173.355 1.00 118.51 ? 153  GLU A O     1 
ATOM   1736  C CB    . GLU B 2 156  ? 165.780 126.143 175.122 1.00 124.48 ? 153  GLU A CB    1 
ATOM   1737  N N     . HIS B 2 157  ? 165.249 126.926 172.101 1.00 116.04 ? 154  HIS A N     1 
ATOM   1738  C CA    . HIS B 2 157  ? 165.256 127.928 171.038 1.00 111.24 ? 154  HIS A CA    1 
ATOM   1739  C C     . HIS B 2 157  ? 163.892 128.026 170.363 1.00 109.05 ? 154  HIS A C     1 
ATOM   1740  O O     . HIS B 2 157  ? 163.452 129.123 169.997 1.00 108.24 ? 154  HIS A O     1 
ATOM   1741  C CB    . HIS B 2 157  ? 166.350 127.615 170.015 1.00 106.23 ? 154  HIS A CB    1 
ATOM   1742  C CG    . HIS B 2 157  ? 166.426 128.602 168.892 1.00 101.74 ? 154  HIS A CG    1 
ATOM   1743  N ND1   . HIS B 2 157  ? 166.053 128.291 167.602 1.00 98.32  ? 154  HIS A ND1   1 
ATOM   1744  C CD2   . HIS B 2 157  ? 166.814 129.899 168.870 1.00 101.44 ? 154  HIS A CD2   1 
ATOM   1745  C CE1   . HIS B 2 157  ? 166.213 129.353 166.832 1.00 97.09  ? 154  HIS A CE1   1 
ATOM   1746  N NE2   . HIS B 2 157  ? 166.674 130.342 167.576 1.00 99.06  ? 154  HIS A NE2   1 
ATOM   1747  N N     . GLU B 2 158  ? 163.206 126.892 170.198 1.00 108.15 ? 155  GLU A N     1 
ATOM   1748  C CA    . GLU B 2 158  ? 161.841 126.926 169.680 1.00 106.08 ? 155  GLU A CA    1 
ATOM   1749  C C     . GLU B 2 158  ? 160.904 127.631 170.654 1.00 108.19 ? 155  GLU A C     1 
ATOM   1750  O O     . GLU B 2 158  ? 160.057 128.434 170.243 1.00 108.29 ? 155  GLU A O     1 
ATOM   1751  C CB    . GLU B 2 158  ? 161.351 125.505 169.388 1.00 105.31 ? 155  GLU A CB    1 
ATOM   1752  C CG    . GLU B 2 158  ? 162.046 124.815 168.217 1.00 103.75 ? 155  GLU A CG    1 
ATOM   1753  C CD    . GLU B 2 158  ? 161.757 123.324 168.161 1.00 102.52 ? 155  GLU A CD    1 
ATOM   1754  O OE1   . GLU B 2 158  ? 160.838 122.867 168.873 1.00 102.99 ? 155  GLU A OE1   1 
ATOM   1755  O OE2   . GLU B 2 158  ? 162.454 122.607 167.411 1.00 100.59 ? 155  GLU A OE2   1 
ATOM   1756  N N     . ASN B 2 159  ? 161.047 127.348 171.953 1.00 114.27 ? 156  ASN A N     1 
ATOM   1757  C CA    . ASN B 2 159  ? 160.261 128.064 172.953 1.00 115.87 ? 156  ASN A CA    1 
ATOM   1758  C C     . ASN B 2 159  ? 160.556 129.560 172.915 1.00 114.15 ? 156  ASN A C     1 
ATOM   1759  O O     . ASN B 2 159  ? 159.645 130.384 173.054 1.00 113.05 ? 156  ASN A O     1 
ATOM   1760  C CB    . ASN B 2 159  ? 160.532 127.499 174.352 1.00 123.27 ? 156  ASN A CB    1 
ATOM   1761  C CG    . ASN B 2 159  ? 159.467 126.502 174.810 1.00 125.57 ? 156  ASN A CG    1 
ATOM   1762  O OD1   . ASN B 2 159  ? 158.268 126.712 174.613 1.00 124.81 ? 156  ASN A OD1   1 
ATOM   1763  N ND2   . ASN B 2 159  ? 159.909 125.416 175.434 1.00 127.74 ? 156  ASN A ND2   1 
ATOM   1764  N N     . ALA B 2 160  ? 161.825 129.931 172.719 1.00 114.07 ? 157  ALA A N     1 
ATOM   1765  C CA    . ALA B 2 160  ? 162.164 131.345 172.583 1.00 111.66 ? 157  ALA A CA    1 
ATOM   1766  C C     . ALA B 2 160  ? 161.583 131.939 171.305 1.00 104.25 ? 157  ALA A C     1 
ATOM   1767  O O     . ALA B 2 160  ? 161.305 133.142 171.254 1.00 103.00 ? 157  ALA A O     1 
ATOM   1768  C CB    . ALA B 2 160  ? 163.680 131.535 172.612 1.00 113.69 ? 157  ALA A CB    1 
ATOM   1769  N N     . LEU B 2 161  ? 161.397 131.119 170.268 1.00 98.50  ? 158  LEU A N     1 
ATOM   1770  C CA    . LEU B 2 161  ? 160.774 131.601 169.041 1.00 94.06  ? 158  LEU A CA    1 
ATOM   1771  C C     . LEU B 2 161  ? 159.266 131.761 169.190 1.00 93.31  ? 158  LEU A C     1 
ATOM   1772  O O     . LEU B 2 161  ? 158.682 132.665 168.579 1.00 93.33  ? 158  LEU A O     1 
ATOM   1773  C CB    . LEU B 2 161  ? 161.084 130.655 167.882 1.00 90.41  ? 158  LEU A CB    1 
ATOM   1774  C CG    . LEU B 2 161  ? 162.312 131.002 167.039 1.00 89.99  ? 158  LEU A CG    1 
ATOM   1775  C CD1   . LEU B 2 161  ? 162.447 130.035 165.875 1.00 88.47  ? 158  LEU A CD1   1 
ATOM   1776  C CD2   . LEU B 2 161  ? 162.223 132.436 166.541 1.00 88.47  ? 158  LEU A CD2   1 
ATOM   1777  N N     . LEU B 2 162  ? 158.621 130.900 169.982 1.00 91.16  ? 159  LEU A N     1 
ATOM   1778  C CA    . LEU B 2 162  ? 157.186 131.041 170.208 1.00 86.84  ? 159  LEU A CA    1 
ATOM   1779  C C     . LEU B 2 162  ? 156.870 132.320 170.972 1.00 88.43  ? 159  LEU A C     1 
ATOM   1780  O O     . LEU B 2 162  ? 155.927 133.040 170.626 1.00 84.71  ? 159  LEU A O     1 
ATOM   1781  C CB    . LEU B 2 162  ? 156.646 129.825 170.959 1.00 86.53  ? 159  LEU A CB    1 
ATOM   1782  C CG    . LEU B 2 162  ? 156.626 128.486 170.221 1.00 85.36  ? 159  LEU A CG    1 
ATOM   1783  C CD1   . LEU B 2 162  ? 156.167 127.374 171.150 1.00 86.84  ? 159  LEU A CD1   1 
ATOM   1784  C CD2   . LEU B 2 162  ? 155.733 128.564 168.994 1.00 81.82  ? 159  LEU A CD2   1 
ATOM   1785  N N     . ARG B 2 163  ? 157.650 132.620 172.014 1.00 93.93  ? 160  ARG A N     1 
ATOM   1786  C CA    . ARG B 2 163  ? 157.405 133.808 172.822 1.00 84.24  ? 160  ARG A CA    1 
ATOM   1787  C C     . ARG B 2 163  ? 157.719 135.102 172.085 1.00 83.30  ? 160  ARG A C     1 
ATOM   1788  O O     . ARG B 2 163  ? 157.313 136.171 172.552 1.00 84.04  ? 160  ARG A O     1 
ATOM   1789  C CB    . ARG B 2 163  ? 158.221 133.744 174.114 1.00 96.86  ? 160  ARG A CB    1 
ATOM   1790  C CG    . ARG B 2 163  ? 158.033 132.463 174.906 1.00 98.39  ? 160  ARG A CG    1 
ATOM   1791  C CD    . ARG B 2 163  ? 158.578 132.607 176.316 1.00 93.33  ? 160  ARG A CD    1 
ATOM   1792  N NE    . ARG B 2 163  ? 159.822 133.371 176.346 1.00 101.10 ? 160  ARG A NE    1 
ATOM   1793  C CZ    . ARG B 2 163  ? 161.035 132.835 176.256 1.00 101.24 ? 160  ARG A CZ    1 
ATOM   1794  N NH1   . ARG B 2 163  ? 161.177 131.523 176.130 1.00 96.15  ? 160  ARG A NH1   1 
ATOM   1795  N NH2   . ARG B 2 163  ? 162.108 133.613 176.292 1.00 101.73 ? 160  ARG A NH2   1 
ATOM   1796  N N     . SER B 2 164  ? 158.426 135.037 170.953 1.00 84.68  ? 161  SER A N     1 
ATOM   1797  C CA    . SER B 2 164  ? 158.668 136.239 170.163 1.00 80.84  ? 161  SER A CA    1 
ATOM   1798  C C     . SER B 2 164  ? 157.380 136.810 169.589 1.00 81.53  ? 161  SER A C     1 
ATOM   1799  O O     . SER B 2 164  ? 157.365 137.968 169.157 1.00 77.86  ? 161  SER A O     1 
ATOM   1800  C CB    . SER B 2 164  ? 159.661 135.940 169.037 1.00 79.73  ? 161  SER A CB    1 
ATOM   1801  O OG    . SER B 2 164  ? 159.200 134.882 168.214 1.00 79.34  ? 161  SER A OG    1 
ATOM   1802  N N     . PHE B 2 165  ? 156.304 136.027 169.577 1.00 79.65  ? 162  PHE A N     1 
ATOM   1803  C CA    . PHE B 2 165  ? 154.990 136.463 169.127 1.00 77.85  ? 162  PHE A CA    1 
ATOM   1804  C C     . PHE B 2 165  ? 153.987 136.440 170.274 1.00 78.98  ? 162  PHE A C     1 
ATOM   1805  O O     . PHE B 2 165  ? 152.809 136.127 170.090 1.00 77.33  ? 162  PHE A O     1 
ATOM   1806  C CB    . PHE B 2 165  ? 154.502 135.606 167.962 1.00 76.31  ? 162  PHE A CB    1 
ATOM   1807  C CG    . PHE B 2 165  ? 155.223 135.874 166.673 1.00 76.35  ? 162  PHE A CG    1 
ATOM   1808  C CD1   . PHE B 2 165  ? 154.964 137.025 165.950 1.00 76.27  ? 162  PHE A CD1   1 
ATOM   1809  C CD2   . PHE B 2 165  ? 156.159 134.978 166.186 1.00 76.20  ? 162  PHE A CD2   1 
ATOM   1810  C CE1   . PHE B 2 165  ? 155.623 137.281 164.765 1.00 74.11  ? 162  PHE A CE1   1 
ATOM   1811  C CE2   . PHE B 2 165  ? 156.823 135.227 164.998 1.00 75.44  ? 162  PHE A CE2   1 
ATOM   1812  C CZ    . PHE B 2 165  ? 156.555 136.381 164.288 1.00 74.23  ? 162  PHE A CZ    1 
ATOM   1813  N N     . ASP B 2 166  ? 154.449 136.762 171.480 1.00 82.48  ? 163  ASP A N     1 
ATOM   1814  C CA    . ASP B 2 166  ? 153.536 136.939 172.600 1.00 84.23  ? 163  ASP A CA    1 
ATOM   1815  C C     . ASP B 2 166  ? 152.747 138.228 172.407 1.00 85.21  ? 163  ASP A C     1 
ATOM   1816  O O     . ASP B 2 166  ? 153.319 139.271 172.072 1.00 86.32  ? 163  ASP A O     1 
ATOM   1817  C CB    . ASP B 2 166  ? 154.307 136.971 173.919 1.00 88.02  ? 163  ASP A CB    1 
ATOM   1818  N N     . LYS B 2 167  ? 151.429 138.149 172.606 1.00 84.41  ? 164  LYS A N     1 
ATOM   1819  C CA    . LYS B 2 167  ? 150.512 139.256 172.328 1.00 81.83  ? 164  LYS A CA    1 
ATOM   1820  C C     . LYS B 2 167  ? 150.657 139.757 170.892 1.00 80.33  ? 164  LYS A C     1 
ATOM   1821  O O     . LYS B 2 167  ? 150.521 140.952 170.618 1.00 78.15  ? 164  LYS A O     1 
ATOM   1822  C CB    . LYS B 2 167  ? 150.704 140.407 173.322 1.00 83.32  ? 164  LYS A CB    1 
ATOM   1823  N N     . PHE B 2 168  ? 150.937 138.833 169.963 1.00 83.02  ? 165  PHE A N     1 
ATOM   1824  C CA    . PHE B 2 168  ? 151.112 139.226 168.561 1.00 84.45  ? 165  PHE A CA    1 
ATOM   1825  C C     . PHE B 2 168  ? 150.825 138.080 167.598 1.00 82.33  ? 165  PHE A C     1 
ATOM   1826  O O     . PHE B 2 168  ? 151.342 138.106 166.476 1.00 85.33  ? 165  PHE A O     1 
ATOM   1827  C CB    . PHE B 2 168  ? 152.537 139.755 168.334 1.00 86.22  ? 165  PHE A CB    1 
ATOM   1828  C CG    . PHE B 2 168  ? 152.605 140.980 167.463 1.00 84.41  ? 165  PHE A CG    1 
ATOM   1829  C CD1   . PHE B 2 168  ? 152.421 140.890 166.091 1.00 67.98  ? 165  PHE A CD1   1 
ATOM   1830  C CD2   . PHE B 2 168  ? 152.870 142.223 168.015 1.00 72.30  ? 165  PHE A CD2   1 
ATOM   1831  C CE1   . PHE B 2 168  ? 152.489 142.013 165.291 1.00 67.25  ? 165  PHE A CE1   1 
ATOM   1832  C CE2   . PHE B 2 168  ? 152.942 143.350 167.219 1.00 71.57  ? 165  PHE A CE2   1 
ATOM   1833  C CZ    . PHE B 2 168  ? 152.750 143.245 165.855 1.00 69.05  ? 165  PHE A CZ    1 
ATOM   1834  N N     . THR B 2 169  ? 150.034 137.078 167.986 1.00 77.76  ? 166  THR A N     1 
ATOM   1835  C CA    . THR B 2 169  ? 149.765 135.944 167.110 1.00 76.86  ? 166  THR A CA    1 
ATOM   1836  C C     . THR B 2 169  ? 148.884 136.308 165.922 1.00 75.42  ? 166  THR A C     1 
ATOM   1837  O O     . THR B 2 169  ? 148.699 135.468 165.035 1.00 75.41  ? 166  THR A O     1 
ATOM   1838  C CB    . THR B 2 169  ? 149.111 134.807 167.900 1.00 80.29  ? 166  THR A CB    1 
ATOM   1839  O OG1   . THR B 2 169  ? 147.853 135.247 168.426 1.00 82.78  ? 166  THR A OG1   1 
ATOM   1840  C CG2   . THR B 2 169  ? 150.012 134.371 169.045 1.00 83.41  ? 166  THR A CG2   1 
ATOM   1841  N N     . THR B 2 170  ? 148.339 137.526 165.880 1.00 73.83  ? 167  THR A N     1 
ATOM   1842  C CA    . THR B 2 170  ? 147.617 137.984 164.698 1.00 70.13  ? 167  THR A CA    1 
ATOM   1843  C C     . THR B 2 170  ? 148.537 138.163 163.496 1.00 66.91  ? 167  THR A C     1 
ATOM   1844  O O     . THR B 2 170  ? 148.044 138.335 162.376 1.00 63.17  ? 167  THR A O     1 
ATOM   1845  C CB    . THR B 2 170  ? 146.884 139.296 164.999 1.00 67.72  ? 167  THR A CB    1 
ATOM   1846  O OG1   . THR B 2 170  ? 146.345 139.247 166.324 1.00 67.15  ? 167  THR A OG1   1 
ATOM   1847  C CG2   . THR B 2 170  ? 145.739 139.515 164.018 1.00 63.29  ? 167  THR A CG2   1 
ATOM   1848  N N     . TYR B 2 171  ? 149.856 138.121 163.699 1.00 68.68  ? 168  TYR A N     1 
ATOM   1849  C CA    . TYR B 2 171  ? 150.788 138.140 162.579 1.00 69.23  ? 168  TYR A CA    1 
ATOM   1850  C C     . TYR B 2 171  ? 150.625 136.920 161.683 1.00 64.81  ? 168  TYR A C     1 
ATOM   1851  O O     . TYR B 2 171  ? 150.987 136.975 160.502 1.00 65.00  ? 168  TYR A O     1 
ATOM   1852  C CB    . TYR B 2 171  ? 152.224 138.220 163.102 1.00 73.94  ? 168  TYR A CB    1 
ATOM   1853  C CG    . TYR B 2 171  ? 153.233 138.729 162.097 1.00 61.61  ? 168  TYR A CG    1 
ATOM   1854  C CD1   . TYR B 2 171  ? 153.272 140.071 161.746 1.00 61.69  ? 168  TYR A CD1   1 
ATOM   1855  C CD2   . TYR B 2 171  ? 154.160 137.873 161.520 1.00 61.30  ? 168  TYR A CD2   1 
ATOM   1856  C CE1   . TYR B 2 171  ? 154.198 140.544 160.836 1.00 61.52  ? 168  TYR A CE1   1 
ATOM   1857  C CE2   . TYR B 2 171  ? 155.091 138.337 160.610 1.00 61.05  ? 168  TYR A CE2   1 
ATOM   1858  C CZ    . TYR B 2 171  ? 155.105 139.674 160.272 1.00 61.19  ? 168  TYR A CZ    1 
ATOM   1859  O OH    . TYR B 2 171  ? 156.029 140.143 159.367 1.00 61.09  ? 168  TYR A OH    1 
ATOM   1860  N N     . PHE B 2 172  ? 150.087 135.822 162.220 1.00 62.69  ? 169  PHE A N     1 
ATOM   1861  C CA    . PHE B 2 172  ? 149.780 134.625 161.447 1.00 63.52  ? 169  PHE A CA    1 
ATOM   1862  C C     . PHE B 2 172  ? 148.344 134.612 160.936 1.00 63.33  ? 169  PHE A C     1 
ATOM   1863  O O     . PHE B 2 172  ? 147.783 133.531 160.709 1.00 61.82  ? 169  PHE A O     1 
ATOM   1864  C CB    . PHE B 2 172  ? 150.049 133.375 162.287 1.00 64.12  ? 169  PHE A CB    1 
ATOM   1865  C CG    . PHE B 2 172  ? 151.491 133.197 162.674 1.00 65.56  ? 169  PHE A CG    1 
ATOM   1866  C CD1   . PHE B 2 172  ? 151.998 133.799 163.815 1.00 66.96  ? 169  PHE A CD1   1 
ATOM   1867  C CD2   . PHE B 2 172  ? 152.336 132.413 161.906 1.00 64.94  ? 169  PHE A CD2   1 
ATOM   1868  C CE1   . PHE B 2 172  ? 153.323 133.632 164.175 1.00 67.82  ? 169  PHE A CE1   1 
ATOM   1869  C CE2   . PHE B 2 172  ? 153.661 132.240 162.261 1.00 65.91  ? 169  PHE A CE2   1 
ATOM   1870  C CZ    . PHE B 2 172  ? 154.155 132.852 163.398 1.00 67.72  ? 169  PHE A CZ    1 
ATOM   1871  N N     . SER B 2 173  ? 147.732 135.784 160.749 1.00 63.36  ? 170  SER A N     1 
ATOM   1872  C CA    . SER B 2 173  ? 146.333 135.841 160.335 1.00 61.26  ? 170  SER A CA    1 
ATOM   1873  C C     . SER B 2 173  ? 146.150 135.245 158.943 1.00 59.08  ? 170  SER A C     1 
ATOM   1874  O O     . SER B 2 173  ? 145.348 134.324 158.747 1.00 58.26  ? 170  SER A O     1 
ATOM   1875  C CB    . SER B 2 173  ? 145.833 137.287 160.376 1.00 61.06  ? 170  SER A CB    1 
ATOM   1876  O OG    . SER B 2 173  ? 144.443 137.354 160.115 1.00 61.66  ? 170  SER A OG    1 
ATOM   1877  N N     . GLY B 2 174  ? 146.884 135.767 157.959 1.00 58.91  ? 171  GLY A N     1 
ATOM   1878  C CA    . GLY B 2 174  ? 146.805 135.214 156.619 1.00 59.54  ? 171  GLY A CA    1 
ATOM   1879  C C     . GLY B 2 174  ? 147.353 133.807 156.522 1.00 62.71  ? 171  GLY A C     1 
ATOM   1880  O O     . GLY B 2 174  ? 146.882 133.007 155.705 1.00 63.50  ? 171  GLY A O     1 
ATOM   1881  N N     . PHE B 2 175  ? 148.350 133.480 157.350 1.00 65.06  ? 172  PHE A N     1 
ATOM   1882  C CA    . PHE B 2 175  ? 148.877 132.121 157.389 1.00 64.17  ? 172  PHE A CA    1 
ATOM   1883  C C     . PHE B 2 175  ? 147.827 131.125 157.866 1.00 62.49  ? 172  PHE A C     1 
ATOM   1884  O O     . PHE B 2 175  ? 147.811 129.977 157.405 1.00 60.51  ? 172  PHE A O     1 
ATOM   1885  C CB    . PHE B 2 175  ? 150.115 132.069 158.288 1.00 67.89  ? 172  PHE A CB    1 
ATOM   1886  C CG    . PHE B 2 175  ? 150.598 130.676 158.581 1.00 69.08  ? 172  PHE A CG    1 
ATOM   1887  C CD1   . PHE B 2 175  ? 151.314 129.960 157.633 1.00 68.91  ? 172  PHE A CD1   1 
ATOM   1888  C CD2   . PHE B 2 175  ? 150.351 130.084 159.810 1.00 69.15  ? 172  PHE A CD2   1 
ATOM   1889  C CE1   . PHE B 2 175  ? 151.761 128.680 157.903 1.00 68.25  ? 172  PHE A CE1   1 
ATOM   1890  C CE2   . PHE B 2 175  ? 150.795 128.804 160.085 1.00 68.95  ? 172  PHE A CE2   1 
ATOM   1891  C CZ    . PHE B 2 175  ? 151.503 128.102 159.129 1.00 69.03  ? 172  PHE A CZ    1 
ATOM   1892  N N     . TYR B 2 176  ? 146.950 131.539 158.787 1.00 60.81  ? 173  TYR A N     1 
ATOM   1893  C CA    . TYR B 2 176  ? 145.869 130.660 159.224 1.00 58.36  ? 173  TYR A CA    1 
ATOM   1894  C C     . TYR B 2 176  ? 144.958 130.293 158.061 1.00 53.40  ? 173  TYR A C     1 
ATOM   1895  O O     . TYR B 2 176  ? 144.480 129.158 157.971 1.00 50.06  ? 173  TYR A O     1 
ATOM   1896  C CB    . TYR B 2 176  ? 145.061 131.322 160.341 1.00 60.04  ? 173  TYR A CB    1 
ATOM   1897  C CG    . TYR B 2 176  ? 145.753 131.352 161.685 1.00 63.74  ? 173  TYR A CG    1 
ATOM   1898  C CD1   . TYR B 2 176  ? 146.690 130.386 162.029 1.00 65.55  ? 173  TYR A CD1   1 
ATOM   1899  C CD2   . TYR B 2 176  ? 145.465 132.343 162.615 1.00 64.67  ? 173  TYR A CD2   1 
ATOM   1900  C CE1   . TYR B 2 176  ? 147.323 130.408 163.258 1.00 67.78  ? 173  TYR A CE1   1 
ATOM   1901  C CE2   . TYR B 2 176  ? 146.094 132.375 163.846 1.00 66.57  ? 173  TYR A CE2   1 
ATOM   1902  C CZ    . TYR B 2 176  ? 147.021 131.405 164.162 1.00 69.82  ? 173  TYR A CZ    1 
ATOM   1903  O OH    . TYR B 2 176  ? 147.649 131.434 165.385 1.00 75.30  ? 173  TYR A OH    1 
ATOM   1904  N N     . GLU B 2 177  ? 144.703 131.245 157.160 1.00 54.59  ? 174  GLU A N     1 
ATOM   1905  C CA    . GLU B 2 177  ? 143.869 130.960 155.997 1.00 55.64  ? 174  GLU A CA    1 
ATOM   1906  C C     . GLU B 2 177  ? 144.567 130.006 155.035 1.00 53.07  ? 174  GLU A C     1 
ATOM   1907  O O     . GLU B 2 177  ? 143.924 129.130 154.443 1.00 49.50  ? 174  GLU A O     1 
ATOM   1908  C CB    . GLU B 2 177  ? 143.494 132.261 155.289 1.00 59.70  ? 174  GLU A CB    1 
ATOM   1909  C CG    . GLU B 2 177  ? 142.463 133.090 156.033 1.00 64.70  ? 174  GLU A CG    1 
ATOM   1910  C CD    . GLU B 2 177  ? 141.103 132.423 156.069 1.00 67.31  ? 174  GLU A CD    1 
ATOM   1911  O OE1   . GLU B 2 177  ? 140.775 131.685 155.115 1.00 67.21  ? 174  GLU A OE1   1 
ATOM   1912  O OE2   . GLU B 2 177  ? 140.361 132.633 157.052 1.00 68.49  ? 174  GLU A OE2   1 
ATOM   1913  N N     . ASN B 2 178  ? 145.883 130.159 154.871 1.00 53.77  ? 175  ASN A N     1 
ATOM   1914  C CA    . ASN B 2 178  ? 146.625 129.267 153.985 1.00 52.60  ? 175  ASN A CA    1 
ATOM   1915  C C     . ASN B 2 178  ? 146.610 127.833 154.497 1.00 54.41  ? 175  ASN A C     1 
ATOM   1916  O O     . ASN B 2 178  ? 146.671 126.889 153.699 1.00 54.14  ? 175  ASN A O     1 
ATOM   1917  C CB    . ASN B 2 178  ? 148.060 129.763 153.830 1.00 54.12  ? 175  ASN A CB    1 
ATOM   1918  C CG    . ASN B 2 178  ? 148.131 131.175 153.285 1.00 55.02  ? 175  ASN A CG    1 
ATOM   1919  O OD1   . ASN B 2 178  ? 148.808 132.034 153.848 1.00 58.84  ? 175  ASN A OD1   1 
ATOM   1920  N ND2   . ASN B 2 178  ? 147.443 131.416 152.176 1.00 52.67  ? 175  ASN A ND2   1 
ATOM   1921  N N     . ARG B 2 179  ? 146.527 127.647 155.816 1.00 57.14  ? 176  ARG A N     1 
ATOM   1922  C CA    . ARG B 2 179  ? 146.470 126.301 156.370 1.00 60.11  ? 176  ARG A CA    1 
ATOM   1923  C C     . ARG B 2 179  ? 145.054 125.737 156.360 1.00 62.20  ? 176  ARG A C     1 
ATOM   1924  O O     . ARG B 2 179  ? 144.884 124.513 156.317 1.00 64.76  ? 176  ARG A O     1 
ATOM   1925  C CB    . ARG B 2 179  ? 147.045 126.292 157.786 1.00 61.46  ? 176  ARG A CB    1 
ATOM   1926  C CG    . ARG B 2 179  ? 148.559 126.409 157.816 1.00 61.19  ? 176  ARG A CG    1 
ATOM   1927  C CD    . ARG B 2 179  ? 149.199 125.289 157.006 1.00 58.79  ? 176  ARG A CD    1 
ATOM   1928  N NE    . ARG B 2 179  ? 150.633 125.488 156.814 1.00 57.40  ? 176  ARG A NE    1 
ATOM   1929  C CZ    . ARG B 2 179  ? 151.170 126.082 155.753 1.00 56.21  ? 176  ARG A CZ    1 
ATOM   1930  N NH1   . ARG B 2 179  ? 150.393 126.542 154.781 1.00 57.40  ? 176  ARG A NH1   1 
ATOM   1931  N NH2   . ARG B 2 179  ? 152.487 126.217 155.662 1.00 53.53  ? 176  ARG A NH2   1 
ATOM   1932  N N     . LYS B 2 180  ? 144.034 126.598 156.402 1.00 61.87  ? 177  LYS A N     1 
ATOM   1933  C CA    . LYS B 2 180  ? 142.679 126.117 156.161 1.00 60.62  ? 177  LYS A CA    1 
ATOM   1934  C C     . LYS B 2 180  ? 142.516 125.636 154.727 1.00 58.13  ? 177  LYS A C     1 
ATOM   1935  O O     . LYS B 2 180  ? 141.755 124.695 154.470 1.00 57.87  ? 177  LYS A O     1 
ATOM   1936  C CB    . LYS B 2 180  ? 141.651 127.208 156.465 1.00 62.74  ? 177  LYS A CB    1 
ATOM   1937  C CG    . LYS B 2 180  ? 141.611 127.662 157.912 1.00 67.60  ? 177  LYS A CG    1 
ATOM   1938  C CD    . LYS B 2 180  ? 140.204 128.083 158.302 1.00 69.76  ? 177  LYS A CD    1 
ATOM   1939  C CE    . LYS B 2 180  ? 140.214 129.244 159.281 1.00 70.84  ? 177  LYS A CE    1 
ATOM   1940  N NZ    . LYS B 2 180  ? 140.644 130.507 158.618 1.00 70.07  ? 177  LYS A NZ    1 
ATOM   1941  N N     . ASN B 2 181  ? 143.226 126.260 153.785 1.00 53.03  ? 178  ASN A N     1 
ATOM   1942  C CA    . ASN B 2 181  ? 143.199 125.809 152.399 1.00 51.79  ? 178  ASN A CA    1 
ATOM   1943  C C     . ASN B 2 181  ? 143.824 124.433 152.227 1.00 51.12  ? 178  ASN A C     1 
ATOM   1944  O O     . ASN B 2 181  ? 143.590 123.785 151.203 1.00 49.58  ? 178  ASN A O     1 
ATOM   1945  C CB    . ASN B 2 181  ? 143.923 126.814 151.502 1.00 49.23  ? 178  ASN A CB    1 
ATOM   1946  C CG    . ASN B 2 181  ? 143.264 128.177 151.506 1.00 41.02  ? 178  ASN A CG    1 
ATOM   1947  O OD1   . ASN B 2 181  ? 142.068 128.299 151.768 1.00 47.20  ? 178  ASN A OD1   1 
ATOM   1948  N ND2   . ASN B 2 181  ? 144.043 129.212 151.212 1.00 40.88  ? 178  ASN A ND2   1 
ATOM   1949  N N     . VAL B 2 182  ? 144.613 123.974 153.199 1.00 52.49  ? 179  VAL A N     1 
ATOM   1950  C CA    . VAL B 2 182  ? 145.242 122.662 153.100 1.00 49.03  ? 179  VAL A CA    1 
ATOM   1951  C C     . VAL B 2 182  ? 144.273 121.564 153.520 1.00 51.77  ? 179  VAL A C     1 
ATOM   1952  O O     . VAL B 2 182  ? 144.215 120.499 152.893 1.00 52.43  ? 179  VAL A O     1 
ATOM   1953  C CB    . VAL B 2 182  ? 146.532 122.631 153.940 1.00 47.28  ? 179  VAL A CB    1 
ATOM   1954  C CG1   . VAL B 2 182  ? 147.144 121.238 153.930 1.00 46.11  ? 179  VAL A CG1   1 
ATOM   1955  C CG2   . VAL B 2 182  ? 147.527 123.658 153.423 1.00 44.97  ? 179  VAL A CG2   1 
ATOM   1956  N N     . PHE B 2 183  ? 143.497 121.801 154.575 1.00 52.46  ? 180  PHE A N     1 
ATOM   1957  C CA    . PHE B 2 183  ? 142.576 120.810 155.112 1.00 52.58  ? 180  PHE A CA    1 
ATOM   1958  C C     . PHE B 2 183  ? 141.149 120.988 154.611 1.00 52.59  ? 180  PHE A C     1 
ATOM   1959  O O     . PHE B 2 183  ? 140.272 120.209 154.999 1.00 54.53  ? 180  PHE A O     1 
ATOM   1960  C CB    . PHE B 2 183  ? 142.586 120.855 156.645 1.00 53.74  ? 180  PHE A CB    1 
ATOM   1961  C CG    . PHE B 2 183  ? 143.893 120.433 157.255 1.00 53.51  ? 180  PHE A CG    1 
ATOM   1962  C CD1   . PHE B 2 183  ? 144.923 121.345 157.424 1.00 53.04  ? 180  PHE A CD1   1 
ATOM   1963  C CD2   . PHE B 2 183  ? 144.089 119.126 157.669 1.00 55.35  ? 180  PHE A CD2   1 
ATOM   1964  C CE1   . PHE B 2 183  ? 146.125 120.959 157.987 1.00 54.23  ? 180  PHE A CE1   1 
ATOM   1965  C CE2   . PHE B 2 183  ? 145.288 118.734 158.234 1.00 57.39  ? 180  PHE A CE2   1 
ATOM   1966  C CZ    . PHE B 2 183  ? 146.307 119.650 158.394 1.00 52.39  ? 180  PHE A CZ    1 
ATOM   1967  N N     . SER B 2 184  ? 140.896 121.984 153.767 1.00 52.07  ? 181  SER A N     1 
ATOM   1968  C CA    . SER B 2 184  ? 139.545 122.248 153.295 1.00 50.03  ? 181  SER A CA    1 
ATOM   1969  C C     . SER B 2 184  ? 139.011 121.076 152.481 1.00 51.68  ? 181  SER A C     1 
ATOM   1970  O O     . SER B 2 184  ? 139.761 120.349 151.825 1.00 52.15  ? 181  SER A O     1 
ATOM   1971  C CB    . SER B 2 184  ? 139.517 123.523 152.450 1.00 47.24  ? 181  SER A CB    1 
ATOM   1972  O OG    . SER B 2 184  ? 138.243 123.717 151.859 1.00 46.86  ? 181  SER A OG    1 
ATOM   1973  N N     . ALA B 2 185  ? 137.694 120.895 152.532 1.00 53.19  ? 182  ALA A N     1 
ATOM   1974  C CA    . ALA B 2 185  ? 137.017 119.888 151.728 1.00 53.44  ? 182  ALA A CA    1 
ATOM   1975  C C     . ALA B 2 185  ? 136.486 120.446 150.416 1.00 53.95  ? 182  ALA A C     1 
ATOM   1976  O O     . ALA B 2 185  ? 135.940 119.684 149.613 1.00 55.53  ? 182  ALA A O     1 
ATOM   1977  C CB    . ALA B 2 185  ? 135.867 119.262 152.522 1.00 52.24  ? 182  ALA A CB    1 
ATOM   1978  N N     . GLU B 2 186  ? 136.633 121.746 150.183 1.00 54.32  ? 183  GLU A N     1 
ATOM   1979  C CA    . GLU B 2 186  ? 136.144 122.356 148.958 1.00 55.61  ? 183  GLU A CA    1 
ATOM   1980  C C     . GLU B 2 186  ? 136.979 121.896 147.763 1.00 52.94  ? 183  GLU A C     1 
ATOM   1981  O O     . GLU B 2 186  ? 138.049 121.296 147.900 1.00 50.73  ? 183  GLU A O     1 
ATOM   1982  C CB    . GLU B 2 186  ? 136.172 123.879 149.073 1.00 59.72  ? 183  GLU A CB    1 
ATOM   1983  C CG    . GLU B 2 186  ? 135.287 124.427 150.177 1.00 65.56  ? 183  GLU A CG    1 
ATOM   1984  C CD    . GLU B 2 186  ? 133.816 124.174 149.918 1.00 72.08  ? 183  GLU A CD    1 
ATOM   1985  O OE1   . GLU B 2 186  ? 133.418 124.142 148.735 1.00 75.13  ? 183  GLU A OE1   1 
ATOM   1986  O OE2   . GLU B 2 186  ? 133.058 124.003 150.896 1.00 74.22  ? 183  GLU A OE2   1 
ATOM   1987  N N     . ASP B 2 187  ? 136.468 122.194 146.566 1.00 52.32  ? 184  ASP A N     1 
ATOM   1988  C CA    . ASP B 2 187  ? 137.129 121.812 145.319 1.00 50.47  ? 184  ASP A CA    1 
ATOM   1989  C C     . ASP B 2 187  ? 138.199 122.850 144.976 1.00 47.17  ? 184  ASP A C     1 
ATOM   1990  O O     . ASP B 2 187  ? 138.124 123.580 143.986 1.00 45.93  ? 184  ASP A O     1 
ATOM   1991  C CB    . ASP B 2 187  ? 136.105 121.662 144.202 1.00 51.81  ? 184  ASP A CB    1 
ATOM   1992  C CG    . ASP B 2 187  ? 136.721 121.160 142.912 1.00 53.38  ? 184  ASP A CG    1 
ATOM   1993  O OD1   . ASP B 2 187  ? 137.783 120.509 142.975 1.00 53.32  ? 184  ASP A OD1   1 
ATOM   1994  O OD2   . ASP B 2 187  ? 136.141 121.415 141.836 1.00 55.72  ? 184  ASP A OD2   1 
ATOM   1995  N N     . ILE B 2 188  ? 139.217 122.905 145.833 1.00 46.62  ? 185  ILE A N     1 
ATOM   1996  C CA    . ILE B 2 188  ? 140.341 123.818 145.673 1.00 44.22  ? 185  ILE A CA    1 
ATOM   1997  C C     . ILE B 2 188  ? 141.623 123.002 145.619 1.00 46.68  ? 185  ILE A C     1 
ATOM   1998  O O     . ILE B 2 188  ? 141.794 122.042 146.380 1.00 49.42  ? 185  ILE A O     1 
ATOM   1999  C CB    . ILE B 2 188  ? 140.394 124.865 146.805 1.00 42.86  ? 185  ILE A CB    1 
ATOM   2000  C CG1   . ILE B 2 188  ? 140.522 124.189 148.170 1.00 46.57  ? 185  ILE A CG1   1 
ATOM   2001  C CG2   . ILE B 2 188  ? 139.151 125.742 146.772 1.00 39.40  ? 185  ILE A CG2   1 
ATOM   2002  C CD1   . ILE B 2 188  ? 140.573 125.159 149.328 1.00 39.19  ? 185  ILE A CD1   1 
ATOM   2003  N N     . SER B 2 189  ? 142.527 123.382 144.712 1.00 45.17  ? 186  SER A N     1 
ATOM   2004  C CA    . SER B 2 189  ? 143.729 122.595 144.466 1.00 42.99  ? 186  SER A CA    1 
ATOM   2005  C C     . SER B 2 189  ? 144.762 122.705 145.579 1.00 42.86  ? 186  SER A C     1 
ATOM   2006  O O     . SER B 2 189  ? 145.722 121.926 145.587 1.00 44.80  ? 186  SER A O     1 
ATOM   2007  C CB    . SER B 2 189  ? 144.350 123.009 143.131 1.00 35.22  ? 186  SER A CB    1 
ATOM   2008  O OG    . SER B 2 189  ? 144.212 124.402 142.927 1.00 34.87  ? 186  SER A OG    1 
ATOM   2009  N N     . THR B 2 190  ? 144.595 123.635 146.517 1.00 42.71  ? 187  THR A N     1 
ATOM   2010  C CA    . THR B 2 190  ? 145.516 123.747 147.639 1.00 43.97  ? 187  THR A CA    1 
ATOM   2011  C C     . THR B 2 190  ? 145.287 122.686 148.707 1.00 45.91  ? 187  THR A C     1 
ATOM   2012  O O     . THR B 2 190  ? 146.096 122.582 149.634 1.00 52.52  ? 187  THR A O     1 
ATOM   2013  C CB    . THR B 2 190  ? 145.402 125.133 148.280 1.00 38.89  ? 187  THR A CB    1 
ATOM   2014  O OG1   . THR B 2 190  ? 144.037 125.383 148.638 1.00 38.93  ? 187  THR A OG1   1 
ATOM   2015  C CG2   . THR B 2 190  ? 145.871 126.211 147.317 1.00 41.00  ? 187  THR A CG2   1 
ATOM   2016  N N     . ALA B 2 191  ? 144.223 121.897 148.599 1.00 42.48  ? 188  ALA A N     1 
ATOM   2017  C CA    . ALA B 2 191  ? 143.772 121.044 149.686 1.00 43.86  ? 188  ALA A CA    1 
ATOM   2018  C C     . ALA B 2 191  ? 144.260 119.609 149.526 1.00 47.01  ? 188  ALA A C     1 
ATOM   2019  O O     . ALA B 2 191  ? 144.582 119.148 148.428 1.00 48.54  ? 188  ALA A O     1 
ATOM   2020  C CB    . ALA B 2 191  ? 142.245 121.065 149.786 1.00 44.48  ? 188  ALA A CB    1 
ATOM   2021  N N     . ILE B 2 192  ? 144.300 118.906 150.654 1.00 47.89  ? 189  ILE A N     1 
ATOM   2022  C CA    . ILE B 2 192  ? 144.690 117.500 150.713 1.00 47.84  ? 189  ILE A CA    1 
ATOM   2023  C C     . ILE B 2 192  ? 143.581 116.609 150.156 1.00 50.65  ? 189  ILE A C     1 
ATOM   2024  O O     . ILE B 2 192  ? 143.881 115.707 149.359 1.00 51.63  ? 189  ILE A O     1 
ATOM   2025  C CB    . ILE B 2 192  ? 145.072 117.094 152.149 1.00 46.17  ? 189  ILE A CB    1 
ATOM   2026  C CG1   . ILE B 2 192  ? 146.362 117.796 152.575 1.00 46.62  ? 189  ILE A CG1   1 
ATOM   2027  C CG2   . ILE B 2 192  ? 145.216 115.585 152.264 1.00 46.31  ? 189  ILE A CG2   1 
ATOM   2028  C CD1   . ILE B 2 192  ? 146.822 117.433 153.969 1.00 50.06  ? 189  ILE A CD1   1 
ATOM   2029  N N     . PRO B 2 193  ? 142.304 116.792 150.531 1.00 51.02  ? 190  PRO A N     1 
ATOM   2030  C CA    . PRO B 2 193  ? 141.260 115.948 149.920 1.00 51.20  ? 190  PRO A CA    1 
ATOM   2031  C C     . PRO B 2 193  ? 141.187 116.075 148.408 1.00 51.02  ? 190  PRO A C     1 
ATOM   2032  O O     . PRO B 2 193  ? 140.968 115.072 147.719 1.00 51.30  ? 190  PRO A O     1 
ATOM   2033  C CB    . PRO B 2 193  ? 139.974 116.441 150.595 1.00 52.45  ? 190  PRO A CB    1 
ATOM   2034  C CG    . PRO B 2 193  ? 140.423 116.988 151.892 1.00 53.13  ? 190  PRO A CG    1 
ATOM   2035  C CD    . PRO B 2 193  ? 141.741 117.636 151.603 1.00 52.18  ? 190  PRO A CD    1 
ATOM   2036  N N     . HIS B 2 194  ? 141.370 117.285 147.871 1.00 50.66  ? 191  HIS A N     1 
ATOM   2037  C CA    . HIS B 2 194  ? 141.348 117.458 146.421 1.00 47.97  ? 191  HIS A CA    1 
ATOM   2038  C C     . HIS B 2 194  ? 142.521 116.742 145.759 1.00 46.90  ? 191  HIS A C     1 
ATOM   2039  O O     . HIS B 2 194  ? 142.360 116.124 144.700 1.00 47.43  ? 191  HIS A O     1 
ATOM   2040  C CB    . HIS B 2 194  ? 141.363 118.943 146.067 1.00 47.26  ? 191  HIS A CB    1 
ATOM   2041  C CG    . HIS B 2 194  ? 141.601 119.214 144.615 1.00 48.28  ? 191  HIS A CG    1 
ATOM   2042  N ND1   . HIS B 2 194  ? 142.863 119.358 144.081 1.00 50.95  ? 191  HIS A ND1   1 
ATOM   2043  C CD2   . HIS B 2 194  ? 140.736 119.381 143.586 1.00 46.40  ? 191  HIS A CD2   1 
ATOM   2044  C CE1   . HIS B 2 194  ? 142.767 119.595 142.785 1.00 48.86  ? 191  HIS A CE1   1 
ATOM   2045  N NE2   . HIS B 2 194  ? 141.486 119.614 142.458 1.00 46.58  ? 191  HIS A NE2   1 
ATOM   2046  N N     . ARG B 2 195  ? 143.709 116.825 146.363 1.00 44.20  ? 192  ARG A N     1 
ATOM   2047  C CA    . ARG B 2 195  ? 144.872 116.132 145.818 1.00 42.29  ? 192  ARG A CA    1 
ATOM   2048  C C     . ARG B 2 195  ? 144.657 114.625 145.782 1.00 42.52  ? 192  ARG A C     1 
ATOM   2049  O O     . ARG B 2 195  ? 145.124 113.952 144.856 1.00 44.01  ? 192  ARG A O     1 
ATOM   2050  C CB    . ARG B 2 195  ? 146.114 116.482 146.641 1.00 42.33  ? 192  ARG A CB    1 
ATOM   2051  C CG    . ARG B 2 195  ? 147.380 115.727 146.262 1.00 43.26  ? 192  ARG A CG    1 
ATOM   2052  C CD    . ARG B 2 195  ? 147.736 115.906 144.793 1.00 43.42  ? 192  ARG A CD    1 
ATOM   2053  N NE    . ARG B 2 195  ? 147.836 117.312 144.406 1.00 43.74  ? 192  ARG A NE    1 
ATOM   2054  C CZ    . ARG B 2 195  ? 148.961 118.018 144.431 1.00 37.72  ? 192  ARG A CZ    1 
ATOM   2055  N NH1   . ARG B 2 195  ? 150.092 117.453 144.829 1.00 57.88  ? 192  ARG A NH1   1 
ATOM   2056  N NH2   . ARG B 2 195  ? 148.957 119.289 144.059 1.00 37.06  ? 192  ARG A NH2   1 
ATOM   2057  N N     . ILE B 2 196  ? 143.941 114.079 146.762 1.00 42.60  ? 193  ILE A N     1 
ATOM   2058  C CA    . ILE B 2 196  ? 143.724 112.636 146.816 1.00 44.76  ? 193  ILE A CA    1 
ATOM   2059  C C     . ILE B 2 196  ? 142.657 112.209 145.817 1.00 46.28  ? 193  ILE A C     1 
ATOM   2060  O O     . ILE B 2 196  ? 142.825 111.226 145.087 1.00 48.93  ? 193  ILE A O     1 
ATOM   2061  C CB    . ILE B 2 196  ? 143.357 112.208 148.248 1.00 47.51  ? 193  ILE A CB    1 
ATOM   2062  C CG1   . ILE B 2 196  ? 144.542 112.424 149.188 1.00 47.66  ? 193  ILE A CG1   1 
ATOM   2063  C CG2   . ILE B 2 196  ? 142.895 110.757 148.275 1.00 50.84  ? 193  ILE A CG2   1 
ATOM   2064  C CD1   . ILE B 2 196  ? 144.256 112.056 150.629 1.00 49.08  ? 193  ILE A CD1   1 
ATOM   2065  N N     . VAL B 2 197  ? 141.546 112.945 145.763 1.00 45.11  ? 194  VAL A N     1 
ATOM   2066  C CA    . VAL B 2 197  ? 140.394 112.500 144.991 1.00 45.99  ? 194  VAL A CA    1 
ATOM   2067  C C     . VAL B 2 197  ? 140.544 112.851 143.514 1.00 46.95  ? 194  VAL A C     1 
ATOM   2068  O O     . VAL B 2 197  ? 140.280 112.020 142.640 1.00 51.34  ? 194  VAL A O     1 
ATOM   2069  C CB    . VAL B 2 197  ? 139.106 113.092 145.590 1.00 47.44  ? 194  VAL A CB    1 
ATOM   2070  C CG1   . VAL B 2 197  ? 137.902 112.710 144.744 1.00 46.92  ? 194  VAL A CG1   1 
ATOM   2071  C CG2   . VAL B 2 197  ? 138.926 112.624 147.027 1.00 49.10  ? 194  VAL A CG2   1 
ATOM   2072  N N     . GLN B 2 198  ? 140.969 114.076 143.205 1.00 45.02  ? 195  GLN A N     1 
ATOM   2073  C CA    . GLN B 2 198  ? 140.902 114.581 141.841 1.00 45.99  ? 195  GLN A CA    1 
ATOM   2074  C C     . GLN B 2 198  ? 142.251 114.682 141.140 1.00 51.42  ? 195  GLN A C     1 
ATOM   2075  O O     . GLN B 2 198  ? 142.279 114.977 139.941 1.00 54.12  ? 195  GLN A O     1 
ATOM   2076  C CB    . GLN B 2 198  ? 140.221 115.957 141.827 1.00 42.70  ? 195  GLN A CB    1 
ATOM   2077  C CG    . GLN B 2 198  ? 138.861 115.963 142.506 1.00 42.95  ? 195  GLN A CG    1 
ATOM   2078  C CD    . GLN B 2 198  ? 138.250 117.344 142.588 1.00 43.57  ? 195  GLN A CD    1 
ATOM   2079  O OE1   . GLN B 2 198  ? 137.738 117.747 143.632 1.00 42.98  ? 195  GLN A OE1   1 
ATOM   2080  N NE2   . GLN B 2 198  ? 138.292 118.078 141.482 1.00 44.95  ? 195  GLN A NE2   1 
ATOM   2081  N N     . ASP B 2 199  ? 143.360 114.444 141.839 1.00 52.81  ? 196  ASP A N     1 
ATOM   2082  C CA    . ASP B 2 199  ? 144.683 114.510 141.233 1.00 53.13  ? 196  ASP A CA    1 
ATOM   2083  C C     . ASP B 2 199  ? 145.349 113.141 141.150 1.00 52.75  ? 196  ASP A C     1 
ATOM   2084  O O     . ASP B 2 199  ? 145.700 112.690 140.057 1.00 53.41  ? 196  ASP A O     1 
ATOM   2085  C CB    . ASP B 2 199  ? 145.578 115.487 142.009 1.00 57.35  ? 196  ASP A CB    1 
ATOM   2086  C CG    . ASP B 2 199  ? 145.420 116.922 141.540 1.00 61.57  ? 196  ASP A CG    1 
ATOM   2087  O OD1   . ASP B 2 199  ? 145.059 117.129 140.363 1.00 61.13  ? 196  ASP A OD1   1 
ATOM   2088  O OD2   . ASP B 2 199  ? 145.670 117.843 142.347 1.00 63.77  ? 196  ASP A OD2   1 
ATOM   2089  N N     . ASN B 2 200  ? 145.528 112.460 142.283 1.00 52.35  ? 197  ASN A N     1 
ATOM   2090  C CA    . ASN B 2 200  ? 146.321 111.235 142.285 1.00 50.77  ? 197  ASN A CA    1 
ATOM   2091  C C     . ASN B 2 200  ? 145.502 110.013 141.881 1.00 50.48  ? 197  ASN A C     1 
ATOM   2092  O O     . ASN B 2 200  ? 146.016 109.132 141.183 1.00 50.23  ? 197  ASN A O     1 
ATOM   2093  C CB    . ASN B 2 200  ? 146.955 111.023 143.661 1.00 49.95  ? 197  ASN A CB    1 
ATOM   2094  C CG    . ASN B 2 200  ? 148.163 111.911 143.886 1.00 46.83  ? 197  ASN A CG    1 
ATOM   2095  O OD1   . ASN B 2 200  ? 148.731 112.457 142.939 1.00 40.29  ? 197  ASN A OD1   1 
ATOM   2096  N ND2   . ASN B 2 200  ? 148.570 112.051 145.144 1.00 46.84  ? 197  ASN A ND2   1 
ATOM   2097  N N     . PHE B 2 201  ? 144.240 109.932 142.306 1.00 49.23  ? 198  PHE A N     1 
ATOM   2098  C CA    . PHE B 2 201  ? 143.452 108.742 141.989 1.00 50.96  ? 198  PHE A CA    1 
ATOM   2099  C C     . PHE B 2 201  ? 143.210 108.571 140.494 1.00 48.80  ? 198  PHE A C     1 
ATOM   2100  O O     . PHE B 2 201  ? 143.366 107.442 139.996 1.00 48.44  ? 198  PHE A O     1 
ATOM   2101  C CB    . PHE B 2 201  ? 142.131 108.750 142.764 1.00 51.80  ? 198  PHE A CB    1 
ATOM   2102  C CG    . PHE B 2 201  ? 141.221 107.609 142.402 1.00 53.76  ? 198  PHE A CG    1 
ATOM   2103  C CD1   . PHE B 2 201  ? 141.482 106.329 142.860 1.00 55.29  ? 198  PHE A CD1   1 
ATOM   2104  C CD2   . PHE B 2 201  ? 140.119 107.813 141.587 1.00 55.12  ? 198  PHE A CD2   1 
ATOM   2105  C CE1   . PHE B 2 201  ? 140.655 105.273 142.522 1.00 57.04  ? 198  PHE A CE1   1 
ATOM   2106  C CE2   . PHE B 2 201  ? 139.286 106.761 141.248 1.00 56.41  ? 198  PHE A CE2   1 
ATOM   2107  C CZ    . PHE B 2 201  ? 139.554 105.489 141.716 1.00 57.31  ? 198  PHE A CZ    1 
ATOM   2108  N N     . PRO B 2 202  ? 142.818 109.599 139.729 1.00 45.03  ? 199  PRO A N     1 
ATOM   2109  C CA    . PRO B 2 202  ? 142.752 109.411 138.268 1.00 43.90  ? 199  PRO A CA    1 
ATOM   2110  C C     . PRO B 2 202  ? 144.076 108.980 137.665 1.00 44.03  ? 199  PRO A C     1 
ATOM   2111  O O     . PRO B 2 202  ? 144.083 108.258 136.659 1.00 44.03  ? 199  PRO A O     1 
ATOM   2112  C CB    . PRO B 2 202  ? 142.315 110.793 137.759 1.00 40.33  ? 199  PRO A CB    1 
ATOM   2113  C CG    . PRO B 2 202  ? 141.565 111.380 138.893 1.00 39.75  ? 199  PRO A CG    1 
ATOM   2114  C CD    . PRO B 2 202  ? 142.284 110.916 140.126 1.00 42.11  ? 199  PRO A CD    1 
ATOM   2115  N N     . LYS B 2 203  ? 145.199 109.399 138.253 1.00 41.78  ? 200  LYS A N     1 
ATOM   2116  C CA    . LYS B 2 203  ? 146.495 108.890 137.819 1.00 41.65  ? 200  LYS A CA    1 
ATOM   2117  C C     . LYS B 2 203  ? 146.666 107.430 138.218 1.00 46.11  ? 200  LYS A C     1 
ATOM   2118  O O     . LYS B 2 203  ? 147.091 106.600 137.405 1.00 47.39  ? 200  LYS A O     1 
ATOM   2119  C CB    . LYS B 2 203  ? 147.619 109.746 138.407 1.00 40.83  ? 200  LYS A CB    1 
ATOM   2120  C CG    . LYS B 2 203  ? 147.595 111.197 137.956 1.00 41.28  ? 200  LYS A CG    1 
ATOM   2121  C CD    . LYS B 2 203  ? 148.691 112.008 138.631 1.00 40.85  ? 200  LYS A CD    1 
ATOM   2122  C CE    . LYS B 2 203  ? 148.605 113.477 138.246 1.00 41.63  ? 200  LYS A CE    1 
ATOM   2123  N NZ    . LYS B 2 203  ? 148.680 113.672 136.770 1.00 44.33  ? 200  LYS A NZ    1 
ATOM   2124  N N     . PHE B 2 204  ? 146.334 107.098 139.467 1.00 47.99  ? 201  PHE A N     1 
ATOM   2125  C CA    . PHE B 2 204  ? 146.446 105.714 139.918 1.00 46.10  ? 201  PHE A CA    1 
ATOM   2126  C C     . PHE B 2 204  ? 145.458 104.812 139.186 1.00 46.55  ? 201  PHE A C     1 
ATOM   2127  O O     . PHE B 2 204  ? 145.796 103.681 138.821 1.00 46.01  ? 201  PHE A O     1 
ATOM   2128  C CB    . PHE B 2 204  ? 146.228 105.634 141.428 1.00 43.93  ? 201  PHE A CB    1 
ATOM   2129  C CG    . PHE B 2 204  ? 146.242 104.233 141.967 1.00 46.69  ? 201  PHE A CG    1 
ATOM   2130  C CD1   . PHE B 2 204  ? 147.440 103.590 142.225 1.00 48.40  ? 201  PHE A CD1   1 
ATOM   2131  C CD2   . PHE B 2 204  ? 145.057 103.559 142.215 1.00 48.37  ? 201  PHE A CD2   1 
ATOM   2132  C CE1   . PHE B 2 204  ? 147.456 102.299 142.718 1.00 49.32  ? 201  PHE A CE1   1 
ATOM   2133  C CE2   . PHE B 2 204  ? 145.068 102.268 142.707 1.00 48.68  ? 201  PHE A CE2   1 
ATOM   2134  C CZ    . PHE B 2 204  ? 146.269 101.639 142.960 1.00 48.93  ? 201  PHE A CZ    1 
ATOM   2135  N N     . LYS B 2 205  ? 144.234 105.297 138.970 1.00 47.92  ? 202  LYS A N     1 
ATOM   2136  C CA    . LYS B 2 205  ? 143.243 104.521 138.229 1.00 50.01  ? 202  LYS A CA    1 
ATOM   2137  C C     . LYS B 2 205  ? 143.708 104.251 136.802 1.00 50.96  ? 202  LYS A C     1 
ATOM   2138  O O     . LYS B 2 205  ? 143.505 103.152 136.272 1.00 51.99  ? 202  LYS A O     1 
ATOM   2139  C CB    . LYS B 2 205  ? 141.903 105.257 138.236 1.00 49.07  ? 202  LYS A CB    1 
ATOM   2140  C CG    . LYS B 2 205  ? 140.874 104.726 137.258 1.00 47.14  ? 202  LYS A CG    1 
ATOM   2141  C CD    . LYS B 2 205  ? 139.614 105.574 137.300 1.00 44.43  ? 202  LYS A CD    1 
ATOM   2142  C CE    . LYS B 2 205  ? 138.719 105.296 136.109 1.00 45.83  ? 202  LYS A CE    1 
ATOM   2143  N NZ    . LYS B 2 205  ? 138.265 103.879 136.060 1.00 49.36  ? 202  LYS A NZ    1 
ATOM   2144  N N     . GLU B 2 206  ? 144.340 105.241 136.167 1.00 50.24  ? 203  GLU A N     1 
ATOM   2145  C CA    . GLU B 2 206  ? 144.896 105.026 134.835 1.00 48.73  ? 203  GLU A CA    1 
ATOM   2146  C C     . GLU B 2 206  ? 146.063 104.047 134.866 1.00 48.01  ? 203  GLU A C     1 
ATOM   2147  O O     . GLU B 2 206  ? 146.236 103.263 133.928 1.00 47.75  ? 203  GLU A O     1 
ATOM   2148  C CB    . GLU B 2 206  ? 145.333 106.360 134.230 1.00 48.35  ? 203  GLU A CB    1 
ATOM   2149  C CG    . GLU B 2 206  ? 146.037 106.251 132.884 1.00 51.03  ? 203  GLU A CG    1 
ATOM   2150  C CD    . GLU B 2 206  ? 145.129 105.743 131.777 1.00 55.86  ? 203  GLU A CD    1 
ATOM   2151  O OE1   . GLU B 2 206  ? 143.892 105.801 131.937 1.00 59.20  ? 203  GLU A OE1   1 
ATOM   2152  O OE2   . GLU B 2 206  ? 145.656 105.288 130.739 1.00 56.88  ? 203  GLU A OE2   1 
ATOM   2153  N N     . ASN B 2 207  ? 146.862 104.067 135.937 1.00 49.86  ? 204  ASN A N     1 
ATOM   2154  C CA    . ASN B 2 207  ? 147.984 103.138 136.040 1.00 49.74  ? 204  ASN A CA    1 
ATOM   2155  C C     . ASN B 2 207  ? 147.502 101.692 136.069 1.00 50.71  ? 204  ASN A C     1 
ATOM   2156  O O     . ASN B 2 207  ? 148.126 100.811 135.468 1.00 51.39  ? 204  ASN A O     1 
ATOM   2157  C CB    . ASN B 2 207  ? 148.819 103.450 137.282 1.00 50.18  ? 204  ASN A CB    1 
ATOM   2158  C CG    . ASN B 2 207  ? 149.718 104.660 137.093 1.00 49.25  ? 204  ASN A CG    1 
ATOM   2159  O OD1   . ASN B 2 207  ? 149.676 105.327 136.058 1.00 51.01  ? 204  ASN A OD1   1 
ATOM   2160  N ND2   . ASN B 2 207  ? 150.538 104.950 138.098 1.00 45.34  ? 204  ASN A ND2   1 
ATOM   2161  N N     . CYS B 2 208  ? 146.394 101.431 136.766 1.00 51.88  ? 205  CYS A N     1 
ATOM   2162  C CA    . CYS B 2 208  ? 145.853 100.077 136.810 1.00 54.00  ? 205  CYS A CA    1 
ATOM   2163  C C     . CYS B 2 208  ? 145.376 99.618  135.438 1.00 56.69  ? 205  CYS A C     1 
ATOM   2164  O O     . CYS B 2 208  ? 145.489 98.432  135.107 1.00 60.05  ? 205  CYS A O     1 
ATOM   2165  C CB    . CYS B 2 208  ? 144.708 100.001 137.819 1.00 56.49  ? 205  CYS A CB    1 
ATOM   2166  S SG    . CYS B 2 208  ? 145.136 100.582 139.475 1.00 58.59  ? 205  CYS A SG    1 
ATOM   2167  N N     . HIS B 2 209  ? 144.844 100.537 134.630 1.00 54.86  ? 206  HIS A N     1 
ATOM   2168  C CA    . HIS B 2 209  ? 144.377 100.166 133.299 1.00 53.39  ? 206  HIS A CA    1 
ATOM   2169  C C     . HIS B 2 209  ? 145.547 99.929  132.351 1.00 53.76  ? 206  HIS A C     1 
ATOM   2170  O O     . HIS B 2 209  ? 145.504 99.013  131.522 1.00 55.26  ? 206  HIS A O     1 
ATOM   2171  C CB    . HIS B 2 209  ? 143.445 101.247 132.753 1.00 53.68  ? 206  HIS A CB    1 
ATOM   2172  C CG    . HIS B 2 209  ? 142.805 100.889 131.449 1.00 59.22  ? 206  HIS A CG    1 
ATOM   2173  N ND1   . HIS B 2 209  ? 143.123 101.520 130.265 1.00 62.09  ? 206  HIS A ND1   1 
ATOM   2174  C CD2   . HIS B 2 209  ? 141.865 99.964  131.142 1.00 64.63  ? 206  HIS A CD2   1 
ATOM   2175  C CE1   . HIS B 2 209  ? 142.405 101.000 129.286 1.00 65.48  ? 206  HIS A CE1   1 
ATOM   2176  N NE2   . HIS B 2 209  ? 141.634 100.052 129.791 1.00 66.67  ? 206  HIS A NE2   1 
ATOM   2177  N N     . ILE B 2 210  ? 146.596 100.748 132.454 1.00 50.80  ? 207  ILE A N     1 
ATOM   2178  C CA    . ILE B 2 210  ? 147.794 100.529 131.646 1.00 52.06  ? 207  ILE A CA    1 
ATOM   2179  C C     . ILE B 2 210  ? 148.439 99.198  132.008 1.00 54.26  ? 207  ILE A C     1 
ATOM   2180  O O     . ILE B 2 210  ? 148.965 98.486  131.143 1.00 52.97  ? 207  ILE A O     1 
ATOM   2181  C CB    . ILE B 2 210  ? 148.777 101.702 131.821 1.00 50.86  ? 207  ILE A CB    1 
ATOM   2182  C CG1   . ILE B 2 210  ? 148.138 103.012 131.362 1.00 51.17  ? 207  ILE A CG1   1 
ATOM   2183  C CG2   . ILE B 2 210  ? 150.068 101.445 131.059 1.00 48.81  ? 207  ILE A CG2   1 
ATOM   2184  C CD1   . ILE B 2 210  ? 149.023 104.220 131.565 1.00 50.14  ? 207  ILE A CD1   1 
ATOM   2185  N N     . PHE B 2 211  ? 148.394 98.835  133.292 1.00 56.95  ? 208  PHE A N     1 
ATOM   2186  C CA    . PHE B 2 211  ? 149.023 97.599  133.746 1.00 58.13  ? 208  PHE A CA    1 
ATOM   2187  C C     . PHE B 2 211  ? 148.341 96.377  133.140 1.00 63.71  ? 208  PHE A C     1 
ATOM   2188  O O     . PHE B 2 211  ? 148.996 95.536  132.514 1.00 66.74  ? 208  PHE A O     1 
ATOM   2189  C CB    . PHE B 2 211  ? 148.994 97.539  135.273 1.00 56.09  ? 208  PHE A CB    1 
ATOM   2190  C CG    . PHE B 2 211  ? 149.484 96.238  135.843 1.00 56.86  ? 208  PHE A CG    1 
ATOM   2191  C CD1   . PHE B 2 211  ? 150.839 95.997  135.987 1.00 56.92  ? 208  PHE A CD1   1 
ATOM   2192  C CD2   . PHE B 2 211  ? 148.588 95.264  136.249 1.00 58.33  ? 208  PHE A CD2   1 
ATOM   2193  C CE1   . PHE B 2 211  ? 151.293 94.801  136.517 1.00 58.89  ? 208  PHE A CE1   1 
ATOM   2194  C CE2   . PHE B 2 211  ? 149.033 94.067  136.778 1.00 59.39  ? 208  PHE A CE2   1 
ATOM   2195  C CZ    . PHE B 2 211  ? 150.387 93.835  136.914 1.00 59.60  ? 208  PHE A CZ    1 
ATOM   2196  N N     . THR B 2 212  ? 147.020 96.269  133.306 1.00 65.50  ? 209  THR A N     1 
ATOM   2197  C CA    . THR B 2 212  ? 146.321 95.065  132.865 1.00 66.58  ? 209  THR A CA    1 
ATOM   2198  C C     . THR B 2 212  ? 146.331 94.920  131.347 1.00 64.64  ? 209  THR A C     1 
ATOM   2199  O O     . THR B 2 212  ? 146.302 93.795  130.837 1.00 67.48  ? 209  THR A O     1 
ATOM   2200  C CB    . THR B 2 212  ? 144.883 95.064  133.386 1.00 68.88  ? 209  THR A CB    1 
ATOM   2201  O OG1   . THR B 2 212  ? 144.166 96.170  132.824 1.00 70.87  ? 209  THR A OG1   1 
ATOM   2202  C CG2   . THR B 2 212  ? 144.868 95.175  134.903 1.00 69.33  ? 209  THR A CG2   1 
ATOM   2203  N N     . ARG B 2 213  ? 146.374 96.032  130.609 1.00 61.32  ? 210  ARG A N     1 
ATOM   2204  C CA    . ARG B 2 213  ? 146.440 95.936  129.154 1.00 62.46  ? 210  ARG A CA    1 
ATOM   2205  C C     . ARG B 2 213  ? 147.777 95.366  128.697 1.00 64.13  ? 210  ARG A C     1 
ATOM   2206  O O     . ARG B 2 213  ? 147.828 94.569  127.753 1.00 66.76  ? 210  ARG A O     1 
ATOM   2207  C CB    . ARG B 2 213  ? 146.197 97.302  128.513 1.00 61.76  ? 210  ARG A CB    1 
ATOM   2208  C CG    . ARG B 2 213  ? 144.751 97.759  128.553 1.00 66.62  ? 210  ARG A CG    1 
ATOM   2209  C CD    . ARG B 2 213  ? 144.503 98.851  127.527 1.00 69.61  ? 210  ARG A CD    1 
ATOM   2210  N NE    . ARG B 2 213  ? 144.652 98.354  126.163 1.00 73.49  ? 210  ARG A NE    1 
ATOM   2211  C CZ    . ARG B 2 213  ? 144.573 99.115  125.076 1.00 75.30  ? 210  ARG A CZ    1 
ATOM   2212  N NH1   . ARG B 2 213  ? 144.349 100.417 125.190 1.00 74.58  ? 210  ARG A NH1   1 
ATOM   2213  N NH2   . ARG B 2 213  ? 144.722 98.575  123.873 1.00 75.78  ? 210  ARG A NH2   1 
ATOM   2214  N N     . LEU B 2 214  ? 148.871 95.763  129.353 1.00 60.40  ? 211  LEU A N     1 
ATOM   2215  C CA    . LEU B 2 214  ? 150.181 95.227  128.995 1.00 56.19  ? 211  LEU A CA    1 
ATOM   2216  C C     . LEU B 2 214  ? 150.306 93.760  129.392 1.00 58.63  ? 211  LEU A C     1 
ATOM   2217  O O     . LEU B 2 214  ? 150.833 92.946  128.623 1.00 58.47  ? 211  LEU A O     1 
ATOM   2218  C CB    . LEU B 2 214  ? 151.287 96.054  129.650 1.00 51.00  ? 211  LEU A CB    1 
ATOM   2219  C CG    . LEU B 2 214  ? 151.471 97.494  129.164 1.00 46.48  ? 211  LEU A CG    1 
ATOM   2220  C CD1   . LEU B 2 214  ? 152.533 98.207  129.991 1.00 43.47  ? 211  LEU A CD1   1 
ATOM   2221  C CD2   . LEU B 2 214  ? 151.831 97.527  127.689 1.00 43.76  ? 211  LEU A CD2   1 
ATOM   2222  N N     . ILE B 2 215  ? 149.821 93.402  130.583 1.00 61.06  ? 212  ILE A N     1 
ATOM   2223  C CA    . ILE B 2 215  ? 149.957 92.028  131.060 1.00 64.53  ? 212  ILE A CA    1 
ATOM   2224  C C     . ILE B 2 215  ? 149.117 91.076  130.221 1.00 67.37  ? 212  ILE A C     1 
ATOM   2225  O O     . ILE B 2 215  ? 149.503 89.920  130.006 1.00 71.35  ? 212  ILE A O     1 
ATOM   2226  C CB    . ILE B 2 215  ? 149.590 91.946  132.554 1.00 67.42  ? 212  ILE A CB    1 
ATOM   2227  C CG1   . ILE B 2 215  ? 150.457 92.906  133.371 1.00 67.04  ? 212  ILE A CG1   1 
ATOM   2228  C CG2   . ILE B 2 215  ? 149.743 90.527  133.075 1.00 70.25  ? 212  ILE A CG2   1 
ATOM   2229  C CD1   . ILE B 2 215  ? 151.935 92.818  133.062 1.00 64.77  ? 212  ILE A CD1   1 
ATOM   2230  N N     . THR B 2 216  ? 147.964 91.531  129.729 1.00 67.19  ? 213  THR A N     1 
ATOM   2231  C CA    . THR B 2 216  ? 147.131 90.663  128.903 1.00 69.20  ? 213  THR A CA    1 
ATOM   2232  C C     . THR B 2 216  ? 147.768 90.425  127.538 1.00 68.66  ? 213  THR A C     1 
ATOM   2233  O O     . THR B 2 216  ? 147.769 89.296  127.036 1.00 71.03  ? 213  THR A O     1 
ATOM   2234  C CB    . THR B 2 216  ? 145.733 91.261  128.751 1.00 69.13  ? 213  THR A CB    1 
ATOM   2235  O OG1   . THR B 2 216  ? 145.153 91.452  130.048 1.00 69.23  ? 213  THR A OG1   1 
ATOM   2236  C CG2   . THR B 2 216  ? 144.841 90.333  127.939 1.00 70.97  ? 213  THR A CG2   1 
ATOM   2237  N N     . ALA B 2 217  ? 148.324 91.473  126.929 1.00 66.99  ? 214  ALA A N     1 
ATOM   2238  C CA    . ALA B 2 217  ? 148.962 91.319  125.625 1.00 67.93  ? 214  ALA A CA    1 
ATOM   2239  C C     . ALA B 2 217  ? 150.312 90.622  125.745 1.00 68.20  ? 214  ALA A C     1 
ATOM   2240  O O     . ALA B 2 217  ? 150.611 89.699  124.981 1.00 70.74  ? 214  ALA A O     1 
ATOM   2241  C CB    . ALA B 2 217  ? 149.117 92.683  124.952 1.00 65.45  ? 214  ALA A CB    1 
ATOM   2242  N N     . VAL B 2 218  ? 151.138 91.048  126.697 1.00 64.72  ? 215  VAL A N     1 
ATOM   2243  C CA    . VAL B 2 218  ? 152.452 90.444  126.909 1.00 61.88  ? 215  VAL A CA    1 
ATOM   2244  C C     . VAL B 2 218  ? 152.504 89.872  128.321 1.00 63.91  ? 215  VAL A C     1 
ATOM   2245  O O     . VAL B 2 218  ? 152.927 90.569  129.255 1.00 62.67  ? 215  VAL A O     1 
ATOM   2246  C CB    . VAL B 2 218  ? 153.579 91.463  126.673 1.00 57.65  ? 215  VAL A CB    1 
ATOM   2247  C CG1   . VAL B 2 218  ? 154.936 90.780  126.744 1.00 57.44  ? 215  VAL A CG1   1 
ATOM   2248  C CG2   . VAL B 2 218  ? 153.395 92.158  125.332 1.00 54.60  ? 215  VAL A CG2   1 
ATOM   2249  N N     . PRO B 2 219  ? 152.081 88.622  128.527 1.00 67.37  ? 216  PRO A N     1 
ATOM   2250  C CA    . PRO B 2 219  ? 152.065 88.068  129.891 1.00 70.11  ? 216  PRO A CA    1 
ATOM   2251  C C     . PRO B 2 219  ? 153.441 87.946  130.522 1.00 70.60  ? 216  PRO A C     1 
ATOM   2252  O O     . PRO B 2 219  ? 153.547 87.954  131.755 1.00 72.10  ? 216  PRO A O     1 
ATOM   2253  C CB    . PRO B 2 219  ? 151.406 86.694  129.704 1.00 71.86  ? 216  PRO A CB    1 
ATOM   2254  C CG    . PRO B 2 219  ? 150.633 86.810  128.429 1.00 71.81  ? 216  PRO A CG    1 
ATOM   2255  C CD    . PRO B 2 219  ? 151.442 87.718  127.555 1.00 69.31  ? 216  PRO A CD    1 
ATOM   2256  N N     . SER B 2 220  ? 154.500 87.827  129.717 1.00 70.69  ? 217  SER A N     1 
ATOM   2257  C CA    . SER B 2 220  ? 155.847 87.757  130.272 1.00 70.11  ? 217  SER A CA    1 
ATOM   2258  C C     . SER B 2 220  ? 156.224 89.029  131.018 1.00 72.13  ? 217  SER A C     1 
ATOM   2259  O O     . SER B 2 220  ? 157.120 88.996  131.868 1.00 73.31  ? 217  SER A O     1 
ATOM   2260  C CB    . SER B 2 220  ? 156.862 87.485  129.160 1.00 66.62  ? 217  SER A CB    1 
ATOM   2261  O OG    . SER B 2 220  ? 156.863 88.531  128.203 1.00 64.23  ? 217  SER A OG    1 
ATOM   2262  N N     . LEU B 2 221  ? 155.554 90.144  130.720 1.00 72.36  ? 218  LEU A N     1 
ATOM   2263  C CA    . LEU B 2 221  ? 155.822 91.401  131.406 1.00 70.08  ? 218  LEU A CA    1 
ATOM   2264  C C     . LEU B 2 221  ? 155.361 91.380  132.857 1.00 69.70  ? 218  LEU A C     1 
ATOM   2265  O O     . LEU B 2 221  ? 155.796 92.228  133.644 1.00 66.73  ? 218  LEU A O     1 
ATOM   2266  C CB    . LEU B 2 221  ? 155.146 92.549  130.658 1.00 67.60  ? 218  LEU A CB    1 
ATOM   2267  C CG    . LEU B 2 221  ? 156.014 93.736  130.246 1.00 66.01  ? 218  LEU A CG    1 
ATOM   2268  C CD1   . LEU B 2 221  ? 157.318 93.262  129.629 1.00 65.68  ? 218  LEU A CD1   1 
ATOM   2269  C CD2   . LEU B 2 221  ? 155.248 94.608  129.269 1.00 65.72  ? 218  LEU A CD2   1 
ATOM   2270  N N     . ARG B 2 222  ? 154.491 90.436  133.227 1.00 72.45  ? 219  ARG A N     1 
ATOM   2271  C CA    . ARG B 2 222  ? 154.018 90.354  134.604 1.00 73.88  ? 219  ARG A CA    1 
ATOM   2272  C C     . ARG B 2 222  ? 155.141 89.935  135.542 1.00 74.85  ? 219  ARG A C     1 
ATOM   2273  O O     . ARG B 2 222  ? 155.435 90.621  136.528 1.00 74.50  ? 219  ARG A O     1 
ATOM   2274  C CB    . ARG B 2 222  ? 152.836 89.382  134.696 1.00 75.00  ? 219  ARG A CB    1 
ATOM   2275  C CG    . ARG B 2 222  ? 152.175 89.307  136.070 1.00 77.38  ? 219  ARG A CG    1 
ATOM   2276  C CD    . ARG B 2 222  ? 152.769 88.191  136.923 1.00 81.80  ? 219  ARG A CD    1 
ATOM   2277  N NE    . ARG B 2 222  ? 152.390 88.305  138.327 1.00 85.67  ? 219  ARG A NE    1 
ATOM   2278  C CZ    . ARG B 2 222  ? 152.917 87.574  139.303 1.00 89.55  ? 219  ARG A CZ    1 
ATOM   2279  N NH1   . ARG B 2 222  ? 153.850 86.673  139.028 1.00 90.84  ? 219  ARG A NH1   1 
ATOM   2280  N NH2   . ARG B 2 222  ? 152.512 87.744  140.555 1.00 91.28  ? 219  ARG A NH2   1 
ATOM   2281  N N     . GLU B 2 223  ? 155.779 88.797  135.254 1.00 76.59  ? 220  GLU A N     1 
ATOM   2282  C CA    . GLU B 2 223  ? 156.900 88.357  136.076 1.00 78.48  ? 220  GLU A CA    1 
ATOM   2283  C C     . GLU B 2 223  ? 158.051 89.350  136.022 1.00 78.70  ? 220  GLU A C     1 
ATOM   2284  O O     . GLU B 2 223  ? 158.816 89.468  136.986 1.00 80.10  ? 220  GLU A O     1 
ATOM   2285  C CB    . GLU B 2 223  ? 157.369 86.972  135.629 1.00 80.03  ? 220  GLU A CB    1 
ATOM   2286  N N     . HIS B 2 224  ? 158.184 90.082  134.912 1.00 78.14  ? 221  HIS A N     1 
ATOM   2287  C CA    . HIS B 2 224  ? 159.256 91.064  134.798 1.00 78.04  ? 221  HIS A CA    1 
ATOM   2288  C C     . HIS B 2 224  ? 159.002 92.267  135.700 1.00 76.03  ? 221  HIS A C     1 
ATOM   2289  O O     . HIS B 2 224  ? 159.929 92.776  136.341 1.00 74.48  ? 221  HIS A O     1 
ATOM   2290  C CB    . HIS B 2 224  ? 159.410 91.500  133.340 1.00 79.31  ? 221  HIS A CB    1 
ATOM   2291  C CG    . HIS B 2 224  ? 160.765 92.041  133.011 1.00 81.77  ? 221  HIS A CG    1 
ATOM   2292  N ND1   . HIS B 2 224  ? 161.337 91.905  131.764 1.00 81.94  ? 221  HIS A ND1   1 
ATOM   2293  C CD2   . HIS B 2 224  ? 161.663 92.721  133.764 1.00 82.42  ? 221  HIS A CD2   1 
ATOM   2294  C CE1   . HIS B 2 224  ? 162.529 92.476  131.764 1.00 81.01  ? 221  HIS A CE1   1 
ATOM   2295  N NE2   . HIS B 2 224  ? 162.750 92.980  132.964 1.00 81.38  ? 221  HIS A NE2   1 
ATOM   2296  N N     . PHE B 2 225  ? 157.753 92.737  135.761 1.00 74.16  ? 222  PHE A N     1 
ATOM   2297  C CA    . PHE B 2 225  ? 157.414 93.809  136.693 1.00 70.75  ? 222  PHE A CA    1 
ATOM   2298  C C     . PHE B 2 225  ? 157.584 93.352  138.137 1.00 71.71  ? 222  PHE A C     1 
ATOM   2299  O O     . PHE B 2 225  ? 158.033 94.124  138.993 1.00 69.46  ? 222  PHE A O     1 
ATOM   2300  C CB    . PHE B 2 225  ? 155.982 94.291  136.454 1.00 67.25  ? 222  PHE A CB    1 
ATOM   2301  C CG    . PHE B 2 225  ? 155.796 95.051  135.169 1.00 63.41  ? 222  PHE A CG    1 
ATOM   2302  C CD1   . PHE B 2 225  ? 156.862 95.695  134.562 1.00 62.19  ? 222  PHE A CD1   1 
ATOM   2303  C CD2   . PHE B 2 225  ? 154.547 95.126  134.572 1.00 61.50  ? 222  PHE A CD2   1 
ATOM   2304  C CE1   . PHE B 2 225  ? 156.687 96.397  133.380 1.00 58.48  ? 222  PHE A CE1   1 
ATOM   2305  C CE2   . PHE B 2 225  ? 154.367 95.825  133.390 1.00 58.65  ? 222  PHE A CE2   1 
ATOM   2306  C CZ    . PHE B 2 225  ? 155.437 96.461  132.795 1.00 56.90  ? 222  PHE A CZ    1 
ATOM   2307  N N     . GLU B 2 226  ? 157.225 92.098  138.426 1.00 76.18  ? 223  GLU A N     1 
ATOM   2308  C CA    . GLU B 2 226  ? 157.359 91.575  139.783 1.00 80.68  ? 223  GLU A CA    1 
ATOM   2309  C C     . GLU B 2 226  ? 158.818 91.526  140.216 1.00 81.80  ? 223  GLU A C     1 
ATOM   2310  O O     . GLU B 2 226  ? 159.136 91.778  141.385 1.00 82.47  ? 223  GLU A O     1 
ATOM   2311  C CB    . GLU B 2 226  ? 156.727 90.184  139.871 1.00 85.00  ? 223  GLU A CB    1 
ATOM   2312  C CG    . GLU B 2 226  ? 156.857 89.515  141.233 1.00 90.35  ? 223  GLU A CG    1 
ATOM   2313  C CD    . GLU B 2 226  ? 155.822 90.000  142.229 1.00 94.27  ? 223  GLU A CD    1 
ATOM   2314  O OE1   . GLU B 2 226  ? 154.645 90.152  141.840 1.00 94.85  ? 223  GLU A OE1   1 
ATOM   2315  O OE2   . GLU B 2 226  ? 156.183 90.231  143.403 1.00 96.61  ? 223  GLU A OE2   1 
ATOM   2316  N N     . ASN B 2 227  ? 159.724 91.207  139.287 1.00 84.12  ? 224  ASN A N     1 
ATOM   2317  C CA    . ASN B 2 227  ? 161.142 91.159  139.626 1.00 84.83  ? 224  ASN A CA    1 
ATOM   2318  C C     . ASN B 2 227  ? 161.679 92.546  139.954 1.00 81.88  ? 224  ASN A C     1 
ATOM   2319  O O     . ASN B 2 227  ? 162.529 92.693  140.840 1.00 83.93  ? 224  ASN A O     1 
ATOM   2320  C CB    . ASN B 2 227  ? 161.939 90.531  138.483 1.00 86.11  ? 224  ASN A CB    1 
ATOM   2321  C CG    . ASN B 2 227  ? 161.564 89.084  138.235 1.00 89.01  ? 224  ASN A CG    1 
ATOM   2322  O OD1   . ASN B 2 227  ? 161.289 88.333  139.171 1.00 88.84  ? 224  ASN A OD1   1 
ATOM   2323  N ND2   . ASN B 2 227  ? 161.559 88.683  136.968 1.00 91.13  ? 224  ASN A ND2   1 
ATOM   2324  N N     . VAL B 2 228  ? 161.200 93.573  139.249 1.00 77.14  ? 225  VAL A N     1 
ATOM   2325  C CA    . VAL B 2 228  ? 161.644 94.937  139.530 1.00 73.62  ? 225  VAL A CA    1 
ATOM   2326  C C     . VAL B 2 228  ? 161.207 95.360  140.926 1.00 72.48  ? 225  VAL A C     1 
ATOM   2327  O O     . VAL B 2 228  ? 161.955 96.025  141.653 1.00 72.08  ? 225  VAL A O     1 
ATOM   2328  C CB    . VAL B 2 228  ? 161.121 95.903  138.452 1.00 70.02  ? 225  VAL A CB    1 
ATOM   2329  C CG1   . VAL B 2 228  ? 161.541 97.331  138.764 1.00 67.54  ? 225  VAL A CG1   1 
ATOM   2330  C CG2   . VAL B 2 228  ? 161.625 95.488  137.079 1.00 68.30  ? 225  VAL A CG2   1 
ATOM   2331  N N     . LYS B 2 229  ? 159.994 94.976  141.329 1.00 71.50  ? 226  LYS A N     1 
ATOM   2332  C CA    . LYS B 2 229  ? 159.512 95.331  142.659 1.00 70.90  ? 226  LYS A CA    1 
ATOM   2333  C C     . LYS B 2 229  ? 160.296 94.603  143.742 1.00 74.76  ? 226  LYS A C     1 
ATOM   2334  O O     . LYS B 2 229  ? 160.617 95.188  144.784 1.00 75.26  ? 226  LYS A O     1 
ATOM   2335  C CB    . LYS B 2 229  ? 158.020 95.023  142.778 1.00 68.59  ? 226  LYS A CB    1 
ATOM   2336  C CG    . LYS B 2 229  ? 157.331 95.746  143.923 1.00 67.33  ? 226  LYS A CG    1 
ATOM   2337  C CD    . LYS B 2 229  ? 156.307 94.860  144.608 1.00 68.21  ? 226  LYS A CD    1 
ATOM   2338  C CE    . LYS B 2 229  ? 156.986 93.710  145.333 1.00 72.35  ? 226  LYS A CE    1 
ATOM   2339  N NZ    . LYS B 2 229  ? 156.018 92.887  146.106 1.00 76.36  ? 226  LYS A NZ    1 
ATOM   2340  N N     . LYS B 2 230  ? 160.615 93.325  143.516 1.00 78.69  ? 227  LYS A N     1 
ATOM   2341  C CA    . LYS B 2 230  ? 161.370 92.563  144.504 1.00 82.93  ? 227  LYS A CA    1 
ATOM   2342  C C     . LYS B 2 230  ? 162.830 92.994  144.559 1.00 84.30  ? 227  LYS A C     1 
ATOM   2343  O O     . LYS B 2 230  ? 163.446 92.952  145.630 1.00 82.57  ? 227  LYS A O     1 
ATOM   2344  C CB    . LYS B 2 230  ? 161.275 91.066  144.203 1.00 85.07  ? 227  LYS A CB    1 
ATOM   2345  C CG    . LYS B 2 230  ? 159.891 90.465  144.412 1.00 87.04  ? 227  LYS A CG    1 
ATOM   2346  C CD    . LYS B 2 230  ? 159.899 88.965  144.149 1.00 89.07  ? 227  LYS A CD    1 
ATOM   2347  C CE    . LYS B 2 230  ? 158.556 88.332  144.484 1.00 90.62  ? 227  LYS A CE    1 
ATOM   2348  N NZ    . LYS B 2 230  ? 158.554 86.861  144.250 1.00 91.59  ? 227  LYS A NZ    1 
ATOM   2349  N N     . ALA B 2 231  ? 163.399 93.409  143.424 1.00 89.28  ? 228  ALA A N     1 
ATOM   2350  C CA    . ALA B 2 231  ? 164.805 93.795  143.394 1.00 88.26  ? 228  ALA A CA    1 
ATOM   2351  C C     . ALA B 2 231  ? 165.063 95.118  144.104 1.00 88.39  ? 228  ALA A C     1 
ATOM   2352  O O     . ALA B 2 231  ? 166.207 95.387  144.485 1.00 89.54  ? 228  ALA A O     1 
ATOM   2353  C CB    . ALA B 2 231  ? 165.300 93.880  141.950 1.00 85.51  ? 228  ALA A CB    1 
ATOM   2354  N N     . ILE B 2 232  ? 164.038 95.946  144.288 1.00 87.16  ? 229  ILE A N     1 
ATOM   2355  C CA    . ILE B 2 232  ? 164.214 97.221  144.975 1.00 86.15  ? 229  ILE A CA    1 
ATOM   2356  C C     . ILE B 2 232  ? 163.939 97.093  146.468 1.00 89.54  ? 229  ILE A C     1 
ATOM   2357  O O     . ILE B 2 232  ? 164.682 97.633  147.290 1.00 92.63  ? 229  ILE A O     1 
ATOM   2358  C CB    . ILE B 2 232  ? 163.316 98.294  144.328 1.00 81.39  ? 229  ILE A CB    1 
ATOM   2359  C CG1   . ILE B 2 232  ? 163.707 98.507  142.865 1.00 79.22  ? 229  ILE A CG1   1 
ATOM   2360  C CG2   . ILE B 2 232  ? 163.416 99.601  145.092 1.00 80.39  ? 229  ILE A CG2   1 
ATOM   2361  C CD1   . ILE B 2 232  ? 162.933 99.615  142.187 1.00 75.42  ? 229  ILE A CD1   1 
ATOM   2362  N N     . GLY B 2 233  ? 162.880 96.379  146.839 1.00 88.21  ? 230  GLY A N     1 
ATOM   2363  C CA    . GLY B 2 233  ? 162.511 96.207  148.227 1.00 89.36  ? 230  GLY A CA    1 
ATOM   2364  C C     . GLY B 2 233  ? 161.273 96.960  148.663 1.00 88.96  ? 230  GLY A C     1 
ATOM   2365  O O     . GLY B 2 233  ? 160.966 96.967  149.861 1.00 92.02  ? 230  GLY A O     1 
ATOM   2366  N N     . ILE B 2 234  ? 160.557 97.588  147.742 1.00 85.71  ? 231  ILE A N     1 
ATOM   2367  C CA    . ILE B 2 234  ? 159.361 98.358  148.058 1.00 84.82  ? 231  ILE A CA    1 
ATOM   2368  C C     . ILE B 2 234  ? 158.154 97.433  148.038 1.00 86.47  ? 231  ILE A C     1 
ATOM   2369  O O     . ILE B 2 234  ? 158.039 96.559  147.170 1.00 86.60  ? 231  ILE A O     1 
ATOM   2370  C CB    . ILE B 2 234  ? 159.186 99.521  147.062 1.00 80.76  ? 231  ILE A CB    1 
ATOM   2371  C CG1   . ILE B 2 234  ? 160.444 100.391 147.034 1.00 79.01  ? 231  ILE A CG1   1 
ATOM   2372  C CG2   . ILE B 2 234  ? 157.972 100.359 147.421 1.00 80.92  ? 231  ILE A CG2   1 
ATOM   2373  C CD1   . ILE B 2 234  ? 160.388 101.500 146.011 1.00 76.03  ? 231  ILE A CD1   1 
ATOM   2374  N N     . PHE B 2 235  ? 157.253 97.624  149.002 1.00 87.34  ? 232  PHE A N     1 
ATOM   2375  C CA    . PHE B 2 235  ? 155.986 96.894  149.075 1.00 88.25  ? 232  PHE A CA    1 
ATOM   2376  C C     . PHE B 2 235  ? 156.226 95.384  149.111 1.00 92.75  ? 232  PHE A C     1 
ATOM   2377  O O     . PHE B 2 235  ? 155.779 94.630  148.245 1.00 91.88  ? 232  PHE A O     1 
ATOM   2378  C CB    . PHE B 2 235  ? 155.067 97.279  147.909 1.00 83.62  ? 232  PHE A CB    1 
ATOM   2379  C CG    . PHE B 2 235  ? 154.828 98.759  147.780 1.00 79.27  ? 232  PHE A CG    1 
ATOM   2380  C CD1   . PHE B 2 235  ? 154.765 99.571  148.901 1.00 79.06  ? 232  PHE A CD1   1 
ATOM   2381  C CD2   . PHE B 2 235  ? 154.665 99.339  146.531 1.00 75.89  ? 232  PHE A CD2   1 
ATOM   2382  C CE1   . PHE B 2 235  ? 154.544 100.931 148.779 1.00 76.80  ? 232  PHE A CE1   1 
ATOM   2383  C CE2   . PHE B 2 235  ? 154.445 100.698 146.404 1.00 73.89  ? 232  PHE A CE2   1 
ATOM   2384  C CZ    . PHE B 2 235  ? 154.385 101.494 147.529 1.00 74.14  ? 232  PHE A CZ    1 
ATOM   2385  N N     . VAL B 2 236  ? 156.955 94.950  150.144 1.00 100.14 ? 233  VAL A N     1 
ATOM   2386  C CA    . VAL B 2 236  ? 157.309 93.539  150.250 1.00 101.71 ? 233  VAL A CA    1 
ATOM   2387  C C     . VAL B 2 236  ? 156.083 92.687  150.555 1.00 102.99 ? 233  VAL A C     1 
ATOM   2388  O O     . VAL B 2 236  ? 156.024 91.513  150.168 1.00 104.72 ? 233  VAL A O     1 
ATOM   2389  C CB    . VAL B 2 236  ? 158.412 93.345  151.307 1.00 102.91 ? 233  VAL A CB    1 
ATOM   2390  C CG1   . VAL B 2 236  ? 159.700 94.014  150.854 1.00 100.26 ? 233  VAL A CG1   1 
ATOM   2391  C CG2   . VAL B 2 236  ? 157.967 93.900  152.653 1.00 105.70 ? 233  VAL A CG2   1 
ATOM   2392  N N     . SER B 2 237  ? 155.089 93.251  151.236 1.00 101.44 ? 234  SER A N     1 
ATOM   2393  C CA    . SER B 2 237  ? 153.883 92.522  151.604 1.00 100.90 ? 234  SER A CA    1 
ATOM   2394  C C     . SER B 2 237  ? 152.785 92.625  150.554 1.00 95.14  ? 234  SER A C     1 
ATOM   2395  O O     . SER B 2 237  ? 151.656 92.195  150.812 1.00 92.91  ? 234  SER A O     1 
ATOM   2396  C CB    . SER B 2 237  ? 153.358 93.024  152.951 1.00 104.06 ? 234  SER A CB    1 
ATOM   2397  O OG    . SER B 2 237  ? 152.128 92.404  153.282 1.00 106.64 ? 234  SER A OG    1 
ATOM   2398  N N     . THR B 2 238  ? 153.086 93.177  149.381 1.00 91.81  ? 235  THR A N     1 
ATOM   2399  C CA    . THR B 2 238  ? 152.087 93.420  148.350 1.00 87.05  ? 235  THR A CA    1 
ATOM   2400  C C     . THR B 2 238  ? 152.626 92.959  147.005 1.00 83.66  ? 235  THR A C     1 
ATOM   2401  O O     . THR B 2 238  ? 153.731 93.346  146.611 1.00 86.08  ? 235  THR A O     1 
ATOM   2402  C CB    . THR B 2 238  ? 151.714 94.904  148.288 1.00 82.71  ? 235  THR A CB    1 
ATOM   2403  O OG1   . THR B 2 238  ? 151.630 95.433  149.617 1.00 82.34  ? 235  THR A OG1   1 
ATOM   2404  C CG2   . THR B 2 238  ? 150.375 95.085  147.602 1.00 81.03  ? 235  THR A CG2   1 
ATOM   2405  N N     . SER B 2 239  ? 151.849 92.136  146.304 1.00 80.10  ? 236  SER A N     1 
ATOM   2406  C CA    . SER B 2 239  ? 152.248 91.668  144.986 1.00 78.19  ? 236  SER A CA    1 
ATOM   2407  C C     . SER B 2 239  ? 152.094 92.787  143.957 1.00 77.76  ? 236  SER A C     1 
ATOM   2408  O O     . SER B 2 239  ? 151.581 93.873  144.244 1.00 79.26  ? 236  SER A O     1 
ATOM   2409  C CB    . SER B 2 239  ? 151.424 90.449  144.574 1.00 79.97  ? 236  SER A CB    1 
ATOM   2410  O OG    . SER B 2 239  ? 150.069 90.802  144.364 1.00 81.28  ? 236  SER A OG    1 
ATOM   2411  N N     . ILE B 2 240  ? 152.545 92.508  142.731 1.00 77.51  ? 237  ILE A N     1 
ATOM   2412  C CA    . ILE B 2 240  ? 152.524 93.538  141.697 1.00 75.15  ? 237  ILE A CA    1 
ATOM   2413  C C     . ILE B 2 240  ? 151.110 93.751  141.166 1.00 76.51  ? 237  ILE A C     1 
ATOM   2414  O O     . ILE B 2 240  ? 150.771 94.847  140.708 1.00 75.56  ? 237  ILE A O     1 
ATOM   2415  C CB    . ILE B 2 240  ? 153.513 93.189  140.567 1.00 71.86  ? 237  ILE A CB    1 
ATOM   2416  C CG1   . ILE B 2 240  ? 153.719 94.392  139.643 1.00 67.73  ? 237  ILE A CG1   1 
ATOM   2417  C CG2   . ILE B 2 240  ? 153.025 91.993  139.766 1.00 72.83  ? 237  ILE A CG2   1 
ATOM   2418  C CD1   . ILE B 2 240  ? 154.247 95.621  140.347 1.00 65.15  ? 237  ILE A CD1   1 
ATOM   2419  N N     . GLU B 2 241  ? 150.263 92.722  141.218 1.00 79.70  ? 238  GLU A N     1 
ATOM   2420  C CA    . GLU B 2 241  ? 148.884 92.898  140.776 1.00 79.90  ? 238  GLU A CA    1 
ATOM   2421  C C     . GLU B 2 241  ? 148.076 93.713  141.777 1.00 78.03  ? 238  GLU A C     1 
ATOM   2422  O O     . GLU B 2 241  ? 147.155 94.439  141.384 1.00 76.17  ? 238  GLU A O     1 
ATOM   2423  C CB    . GLU B 2 241  ? 148.219 91.541  140.541 1.00 84.76  ? 238  GLU A CB    1 
ATOM   2424  C CG    . GLU B 2 241  ? 148.668 90.835  139.272 1.00 86.48  ? 238  GLU A CG    1 
ATOM   2425  C CD    . GLU B 2 241  ? 149.837 89.898  139.501 1.00 87.95  ? 238  GLU A CD    1 
ATOM   2426  O OE1   . GLU B 2 241  ? 150.532 90.048  140.527 1.00 86.69  ? 238  GLU A OE1   1 
ATOM   2427  O OE2   . GLU B 2 241  ? 150.055 89.005  138.656 1.00 89.96  ? 238  GLU A OE2   1 
ATOM   2428  N N     . GLU B 2 242  ? 148.408 93.614  143.066 1.00 80.65  ? 239  GLU A N     1 
ATOM   2429  C CA    . GLU B 2 242  ? 147.641 94.323  144.086 1.00 79.11  ? 239  GLU A CA    1 
ATOM   2430  C C     . GLU B 2 242  ? 147.971 95.811  144.109 1.00 76.49  ? 239  GLU A C     1 
ATOM   2431  O O     . GLU B 2 242  ? 147.083 96.637  144.347 1.00 75.59  ? 239  GLU A O     1 
ATOM   2432  C CB    . GLU B 2 242  ? 147.889 93.697  145.459 1.00 82.69  ? 239  GLU A CB    1 
ATOM   2433  C CG    . GLU B 2 242  ? 147.434 92.252  145.572 1.00 87.57  ? 239  GLU A CG    1 
ATOM   2434  C CD    . GLU B 2 242  ? 147.714 91.656  146.937 1.00 91.24  ? 239  GLU A CD    1 
ATOM   2435  O OE1   . GLU B 2 242  ? 148.057 92.424  147.861 1.00 92.19  ? 239  GLU A OE1   1 
ATOM   2436  O OE2   . GLU B 2 242  ? 147.593 90.421  147.085 1.00 93.10  ? 239  GLU A OE2   1 
ATOM   2437  N N     . VAL B 2 243  ? 149.234 96.177  143.864 1.00 75.42  ? 240  VAL A N     1 
ATOM   2438  C CA    . VAL B 2 243  ? 149.579 97.594  143.807 1.00 71.59  ? 240  VAL A CA    1 
ATOM   2439  C C     . VAL B 2 243  ? 148.926 98.271  142.611 1.00 70.55  ? 240  VAL A C     1 
ATOM   2440  O O     . VAL B 2 243  ? 148.860 99.505  142.559 1.00 70.93  ? 240  VAL A O     1 
ATOM   2441  C CB    . VAL B 2 243  ? 151.106 97.802  143.775 1.00 65.07  ? 240  VAL A CB    1 
ATOM   2442  C CG1   . VAL B 2 243  ? 151.773 97.061  144.922 1.00 66.03  ? 240  VAL A CG1   1 
ATOM   2443  C CG2   . VAL B 2 243  ? 151.682 97.369  142.442 1.00 61.88  ? 240  VAL A CG2   1 
ATOM   2444  N N     . PHE B 2 244  ? 148.444 97.494  141.642 1.00 69.97  ? 241  PHE A N     1 
ATOM   2445  C CA    . PHE B 2 244  ? 147.639 98.007  140.542 1.00 68.63  ? 241  PHE A CA    1 
ATOM   2446  C C     . PHE B 2 244  ? 146.174 97.610  140.691 1.00 71.87  ? 241  PHE A C     1 
ATOM   2447  O O     . PHE B 2 244  ? 145.469 97.413  139.697 1.00 74.43  ? 241  PHE A O     1 
ATOM   2448  C CB    . PHE B 2 244  ? 148.197 97.537  139.201 1.00 64.96  ? 241  PHE A CB    1 
ATOM   2449  C CG    . PHE B 2 244  ? 149.495 98.192  138.827 1.00 62.76  ? 241  PHE A CG    1 
ATOM   2450  C CD1   . PHE B 2 244  ? 149.508 99.444  138.232 1.00 60.66  ? 241  PHE A CD1   1 
ATOM   2451  C CD2   . PHE B 2 244  ? 150.703 97.561  139.073 1.00 63.65  ? 241  PHE A CD2   1 
ATOM   2452  C CE1   . PHE B 2 244  ? 150.702 100.053 137.888 1.00 58.22  ? 241  PHE A CE1   1 
ATOM   2453  C CE2   . PHE B 2 244  ? 151.900 98.164  138.731 1.00 61.98  ? 241  PHE A CE2   1 
ATOM   2454  C CZ    . PHE B 2 244  ? 151.899 99.411  138.136 1.00 58.93  ? 241  PHE A CZ    1 
ATOM   2455  N N     . SER B 2 245  ? 145.710 97.483  141.931 1.00 73.77  ? 242  SER A N     1 
ATOM   2456  C CA    . SER B 2 245  ? 144.303 97.291  142.242 1.00 75.29  ? 242  SER A CA    1 
ATOM   2457  C C     . SER B 2 245  ? 143.838 98.426  143.143 1.00 73.80  ? 242  SER A C     1 
ATOM   2458  O O     . SER B 2 245  ? 144.635 99.033  143.864 1.00 72.07  ? 242  SER A O     1 
ATOM   2459  C CB    . SER B 2 245  ? 144.051 95.939  142.923 1.00 82.38  ? 242  SER A CB    1 
ATOM   2460  O OG    . SER B 2 245  ? 144.655 95.892  144.206 1.00 87.41  ? 242  SER A OG    1 
ATOM   2461  N N     . PHE B 2 246  ? 142.536 98.705  143.094 1.00 70.61  ? 243  PHE A N     1 
ATOM   2462  C CA    . PHE B 2 246  ? 141.997 99.855  143.818 1.00 66.42  ? 243  PHE A CA    1 
ATOM   2463  C C     . PHE B 2 246  ? 142.255 99.836  145.323 1.00 66.23  ? 243  PHE A C     1 
ATOM   2464  O O     . PHE B 2 246  ? 142.597 100.901 145.867 1.00 63.91  ? 243  PHE A O     1 
ATOM   2465  C CB    . PHE B 2 246  ? 140.493 99.982  143.536 1.00 64.18  ? 243  PHE A CB    1 
ATOM   2466  C CG    . PHE B 2 246  ? 140.178 100.536 142.178 1.00 60.48  ? 243  PHE A CG    1 
ATOM   2467  C CD1   . PHE B 2 246  ? 141.175 101.091 141.391 1.00 57.82  ? 243  PHE A CD1   1 
ATOM   2468  C CD2   . PHE B 2 246  ? 138.883 100.510 141.689 1.00 60.79  ? 243  PHE A CD2   1 
ATOM   2469  C CE1   . PHE B 2 246  ? 140.887 101.605 140.142 1.00 56.81  ? 243  PHE A CE1   1 
ATOM   2470  C CE2   . PHE B 2 246  ? 138.588 101.021 140.441 1.00 60.39  ? 243  PHE A CE2   1 
ATOM   2471  C CZ    . PHE B 2 246  ? 139.592 101.569 139.666 1.00 58.12  ? 243  PHE A CZ    1 
ATOM   2472  N N     . PRO B 2 247  ? 142.108 98.720  146.050 1.00 68.96  ? 244  PRO A N     1 
ATOM   2473  C CA    . PRO B 2 247  ? 142.304 98.777  147.511 1.00 69.74  ? 244  PRO A CA    1 
ATOM   2474  C C     . PRO B 2 247  ? 143.678 99.267  147.942 1.00 67.62  ? 244  PRO A C     1 
ATOM   2475  O O     . PRO B 2 247  ? 143.809 99.768  149.065 1.00 69.29  ? 244  PRO A O     1 
ATOM   2476  C CB    . PRO B 2 247  ? 142.066 97.327  147.953 1.00 71.56  ? 244  PRO A CB    1 
ATOM   2477  C CG    . PRO B 2 247  ? 141.165 96.772  146.923 1.00 71.35  ? 244  PRO A CG    1 
ATOM   2478  C CD    . PRO B 2 247  ? 141.608 97.396  145.634 1.00 69.97  ? 244  PRO A CD    1 
ATOM   2479  N N     . PHE B 2 248  ? 144.702 99.149  147.095 1.00 64.63  ? 245  PHE A N     1 
ATOM   2480  C CA    . PHE B 2 248  ? 146.035 99.582  147.498 1.00 64.24  ? 245  PHE A CA    1 
ATOM   2481  C C     . PHE B 2 248  ? 146.175 101.099 147.514 1.00 61.40  ? 245  PHE A C     1 
ATOM   2482  O O     . PHE B 2 248  ? 147.091 101.616 148.162 1.00 61.08  ? 245  PHE A O     1 
ATOM   2483  C CB    . PHE B 2 248  ? 147.092 98.969  146.580 1.00 65.73  ? 245  PHE A CB    1 
ATOM   2484  C CG    . PHE B 2 248  ? 148.504 99.212  147.037 1.00 67.57  ? 245  PHE A CG    1 
ATOM   2485  C CD1   . PHE B 2 248  ? 149.005 98.564  148.155 1.00 69.47  ? 245  PHE A CD1   1 
ATOM   2486  C CD2   . PHE B 2 248  ? 149.331 100.084 146.348 1.00 65.14  ? 245  PHE A CD2   1 
ATOM   2487  C CE1   . PHE B 2 248  ? 150.303 98.785  148.580 1.00 68.94  ? 245  PHE A CE1   1 
ATOM   2488  C CE2   . PHE B 2 248  ? 150.631 100.308 146.765 1.00 64.62  ? 245  PHE A CE2   1 
ATOM   2489  C CZ    . PHE B 2 248  ? 151.116 99.656  147.883 1.00 66.68  ? 245  PHE A CZ    1 
ATOM   2490  N N     . TYR B 2 249  ? 145.289 101.825 146.828 1.00 60.14  ? 246  TYR A N     1 
ATOM   2491  C CA    . TYR B 2 249  ? 145.384 103.280 146.805 1.00 58.45  ? 246  TYR A CA    1 
ATOM   2492  C C     . TYR B 2 249  ? 145.154 103.895 148.178 1.00 59.05  ? 246  TYR A C     1 
ATOM   2493  O O     . TYR B 2 249  ? 145.598 105.024 148.421 1.00 58.91  ? 246  TYR A O     1 
ATOM   2494  C CB    . TYR B 2 249  ? 144.391 103.857 145.793 1.00 55.97  ? 246  TYR A CB    1 
ATOM   2495  C CG    . TYR B 2 249  ? 144.461 105.362 145.654 1.00 46.90  ? 246  TYR A CG    1 
ATOM   2496  C CD1   . TYR B 2 249  ? 145.616 105.983 145.194 1.00 45.62  ? 246  TYR A CD1   1 
ATOM   2497  C CD2   . TYR B 2 249  ? 143.372 106.159 145.976 1.00 46.79  ? 246  TYR A CD2   1 
ATOM   2498  C CE1   . TYR B 2 249  ? 145.686 107.357 145.065 1.00 44.34  ? 246  TYR A CE1   1 
ATOM   2499  C CE2   . TYR B 2 249  ? 143.431 107.535 145.850 1.00 45.45  ? 246  TYR A CE2   1 
ATOM   2500  C CZ    . TYR B 2 249  ? 144.590 108.128 145.394 1.00 50.46  ? 246  TYR A CZ    1 
ATOM   2501  O OH    . TYR B 2 249  ? 144.652 109.496 145.268 1.00 49.71  ? 246  TYR A OH    1 
ATOM   2502  N N     . ASN B 2 250  ? 144.479 103.181 149.082 1.00 60.91  ? 247  ASN A N     1 
ATOM   2503  C CA    . ASN B 2 250  ? 144.334 103.671 150.449 1.00 64.66  ? 247  ASN A CA    1 
ATOM   2504  C C     . ASN B 2 250  ? 145.682 103.780 151.148 1.00 69.90  ? 247  ASN A C     1 
ATOM   2505  O O     . ASN B 2 250  ? 145.846 104.604 152.056 1.00 72.91  ? 247  ASN A O     1 
ATOM   2506  C CB    . ASN B 2 250  ? 143.396 102.758 151.239 1.00 67.39  ? 247  ASN A CB    1 
ATOM   2507  C CG    . ASN B 2 250  ? 141.953 102.881 150.791 1.00 69.64  ? 247  ASN A CG    1 
ATOM   2508  O OD1   . ASN B 2 250  ? 141.491 103.965 150.437 1.00 69.29  ? 247  ASN A OD1   1 
ATOM   2509  N ND2   . ASN B 2 250  ? 141.232 101.765 150.802 1.00 72.35  ? 247  ASN A ND2   1 
ATOM   2510  N N     . GLN B 2 251  ? 146.658 102.967 150.741 1.00 73.18  ? 248  GLN A N     1 
ATOM   2511  C CA    . GLN B 2 251  ? 148.015 103.038 151.261 1.00 74.55  ? 248  GLN A CA    1 
ATOM   2512  C C     . GLN B 2 251  ? 148.932 103.875 150.377 1.00 69.59  ? 248  GLN A C     1 
ATOM   2513  O O     . GLN B 2 251  ? 150.154 103.701 150.420 1.00 69.26  ? 248  GLN A O     1 
ATOM   2514  C CB    . GLN B 2 251  ? 148.590 101.633 151.442 1.00 80.28  ? 248  GLN A CB    1 
ATOM   2515  C CG    . GLN B 2 251  ? 148.301 101.025 152.802 1.00 88.93  ? 248  GLN A CG    1 
ATOM   2516  C CD    . GLN B 2 251  ? 148.926 101.822 153.932 1.00 95.38  ? 248  GLN A CD    1 
ATOM   2517  O OE1   . GLN B 2 251  ? 150.149 101.909 154.043 1.00 96.87  ? 248  GLN A OE1   1 
ATOM   2518  N NE2   . GLN B 2 251  ? 148.086 102.416 154.774 1.00 97.77  ? 248  GLN A NE2   1 
ATOM   2519  N N     . LEU B 2 252  ? 148.366 104.772 149.574 1.00 67.16  ? 249  LEU A N     1 
ATOM   2520  C CA    . LEU B 2 252  ? 149.124 105.700 148.742 1.00 63.82  ? 249  LEU A CA    1 
ATOM   2521  C C     . LEU B 2 252  ? 148.675 107.128 149.004 1.00 61.36  ? 249  LEU A C     1 
ATOM   2522  O O     . LEU B 2 252  ? 148.615 107.962 148.096 1.00 58.60  ? 249  LEU A O     1 
ATOM   2523  C CB    . LEU B 2 252  ? 148.982 105.352 147.262 1.00 60.70  ? 249  LEU A CB    1 
ATOM   2524  C CG    . LEU B 2 252  ? 149.551 104.005 146.816 1.00 59.57  ? 249  LEU A CG    1 
ATOM   2525  C CD1   . LEU B 2 252  ? 149.369 103.826 145.319 1.00 58.03  ? 249  LEU A CD1   1 
ATOM   2526  C CD2   . LEU B 2 252  ? 151.017 103.887 147.203 1.00 57.69  ? 249  LEU A CD2   1 
ATOM   2527  N N     . LEU B 2 253  ? 148.354 107.430 150.261 1.00 60.30  ? 250  LEU A N     1 
ATOM   2528  C CA    . LEU B 2 253  ? 147.842 108.737 150.642 1.00 56.71  ? 250  LEU A CA    1 
ATOM   2529  C C     . LEU B 2 253  ? 148.840 109.559 151.445 1.00 58.98  ? 250  LEU A C     1 
ATOM   2530  O O     . LEU B 2 253  ? 148.551 110.716 151.766 1.00 60.11  ? 250  LEU A O     1 
ATOM   2531  C CB    . LEU B 2 253  ? 146.542 108.578 151.438 1.00 54.27  ? 250  LEU A CB    1 
ATOM   2532  C CG    . LEU B 2 253  ? 145.495 107.683 150.772 1.00 54.37  ? 250  LEU A CG    1 
ATOM   2533  C CD1   . LEU B 2 253  ? 144.229 107.627 151.602 1.00 55.48  ? 250  LEU A CD1   1 
ATOM   2534  C CD2   . LEU B 2 253  ? 145.193 108.162 149.360 1.00 54.61  ? 250  LEU A CD2   1 
ATOM   2535  N N     . THR B 2 254  ? 149.998 108.998 151.779 1.00 60.37  ? 251  THR A N     1 
ATOM   2536  C CA    . THR B 2 254  ? 151.037 109.717 152.498 1.00 64.42  ? 251  THR A CA    1 
ATOM   2537  C C     . THR B 2 254  ? 152.266 109.856 151.609 1.00 67.03  ? 251  THR A C     1 
ATOM   2538  O O     . THR B 2 254  ? 152.475 109.076 150.676 1.00 70.78  ? 251  THR A O     1 
ATOM   2539  C CB    . THR B 2 254  ? 151.406 109.010 153.809 1.00 65.68  ? 251  THR A CB    1 
ATOM   2540  O OG1   . THR B 2 254  ? 151.862 107.682 153.531 1.00 65.55  ? 251  THR A OG1   1 
ATOM   2541  C CG2   . THR B 2 254  ? 150.197 108.941 154.731 1.00 65.39  ? 251  THR A CG2   1 
ATOM   2542  N N     . GLN B 2 255  ? 153.085 110.866 151.916 1.00 66.58  ? 252  GLN A N     1 
ATOM   2543  C CA    . GLN B 2 255  ? 154.212 111.197 151.048 1.00 67.12  ? 252  GLN A CA    1 
ATOM   2544  C C     . GLN B 2 255  ? 155.226 110.060 150.986 1.00 71.85  ? 252  GLN A C     1 
ATOM   2545  O O     . GLN B 2 255  ? 155.761 109.758 149.913 1.00 70.80  ? 252  GLN A O     1 
ATOM   2546  C CB    . GLN B 2 255  ? 154.882 112.484 151.525 1.00 65.99  ? 252  GLN A CB    1 
ATOM   2547  C CG    . GLN B 2 255  ? 156.030 112.954 150.643 1.00 65.94  ? 252  GLN A CG    1 
ATOM   2548  C CD    . GLN B 2 255  ? 155.588 113.299 149.234 1.00 67.74  ? 252  GLN A CD    1 
ATOM   2549  O OE1   . GLN B 2 255  ? 154.426 113.633 148.998 1.00 68.38  ? 252  GLN A OE1   1 
ATOM   2550  N NE2   . GLN B 2 255  ? 156.515 113.220 148.286 1.00 68.41  ? 252  GLN A NE2   1 
ATOM   2551  N N     . THR B 2 256  ? 155.511 109.426 152.126 1.00 73.58  ? 253  THR A N     1 
ATOM   2552  C CA    . THR B 2 256  ? 156.467 108.323 152.131 1.00 73.69  ? 253  THR A CA    1 
ATOM   2553  C C     . THR B 2 256  ? 155.996 107.182 151.242 1.00 71.78  ? 253  THR A C     1 
ATOM   2554  O O     . THR B 2 256  ? 156.801 106.546 150.552 1.00 73.59  ? 253  THR A O     1 
ATOM   2555  C CB    . THR B 2 256  ? 156.702 107.830 153.559 1.00 75.01  ? 253  THR A CB    1 
ATOM   2556  O OG1   . THR B 2 256  ? 155.449 107.470 154.156 1.00 75.45  ? 253  THR A OG1   1 
ATOM   2557  C CG2   . THR B 2 256  ? 157.366 108.914 154.396 1.00 75.47  ? 253  THR A CG2   1 
ATOM   2558  N N     . GLN B 2 257  ? 154.689 106.914 151.233 1.00 69.16  ? 254  GLN A N     1 
ATOM   2559  C CA    . GLN B 2 257  ? 154.144 105.891 150.348 1.00 68.31  ? 254  GLN A CA    1 
ATOM   2560  C C     . GLN B 2 257  ? 154.083 106.377 148.905 1.00 67.81  ? 254  GLN A C     1 
ATOM   2561  O O     . GLN B 2 257  ? 154.317 105.597 147.975 1.00 66.41  ? 254  GLN A O     1 
ATOM   2562  C CB    . GLN B 2 257  ? 152.758 105.466 150.831 1.00 69.43  ? 254  GLN A CB    1 
ATOM   2563  C CG    . GLN B 2 257  ? 152.753 104.826 152.213 1.00 75.54  ? 254  GLN A CG    1 
ATOM   2564  C CD    . GLN B 2 257  ? 153.606 103.573 152.280 1.00 79.16  ? 254  GLN A CD    1 
ATOM   2565  O OE1   . GLN B 2 257  ? 154.620 103.537 152.977 1.00 80.83  ? 254  GLN A OE1   1 
ATOM   2566  N NE2   . GLN B 2 257  ? 153.195 102.538 151.559 1.00 79.30  ? 254  GLN A NE2   1 
ATOM   2567  N N     . ILE B 2 258  ? 153.771 107.659 148.698 1.00 65.99  ? 255  ILE A N     1 
ATOM   2568  C CA    . ILE B 2 258  ? 153.771 108.210 147.346 1.00 61.25  ? 255  ILE A CA    1 
ATOM   2569  C C     . ILE B 2 258  ? 155.186 108.229 146.778 1.00 63.78  ? 255  ILE A C     1 
ATOM   2570  O O     . ILE B 2 258  ? 155.395 107.955 145.590 1.00 63.80  ? 255  ILE A O     1 
ATOM   2571  C CB    . ILE B 2 258  ? 153.134 109.612 147.340 1.00 53.09  ? 255  ILE A CB    1 
ATOM   2572  C CG1   . ILE B 2 258  ? 151.634 109.517 147.631 1.00 50.59  ? 255  ILE A CG1   1 
ATOM   2573  C CG2   . ILE B 2 258  ? 153.368 110.313 146.009 1.00 49.91  ? 255  ILE A CG2   1 
ATOM   2574  C CD1   . ILE B 2 258  ? 150.938 110.859 147.699 1.00 44.29  ? 255  ILE A CD1   1 
ATOM   2575  N N     . ASP B 2 259  ? 156.178 108.543 147.615 1.00 67.25  ? 256  ASP A N     1 
ATOM   2576  C CA    . ASP B 2 259  ? 157.564 108.523 147.156 1.00 68.61  ? 256  ASP A CA    1 
ATOM   2577  C C     . ASP B 2 259  ? 158.003 107.113 146.782 1.00 67.87  ? 256  ASP A C     1 
ATOM   2578  O O     . ASP B 2 259  ? 158.648 106.915 145.745 1.00 67.13  ? 256  ASP A O     1 
ATOM   2579  C CB    . ASP B 2 259  ? 158.483 109.105 148.230 1.00 73.38  ? 256  ASP A CB    1 
ATOM   2580  C CG    . ASP B 2 259  ? 158.362 110.609 148.349 1.00 79.68  ? 256  ASP A CG    1 
ATOM   2581  O OD1   . ASP B 2 259  ? 158.092 111.270 147.324 1.00 80.20  ? 256  ASP A OD1   1 
ATOM   2582  O OD2   . ASP B 2 259  ? 158.543 111.134 149.468 1.00 84.04  ? 256  ASP A OD2   1 
ATOM   2583  N N     . LEU B 2 260  ? 157.667 106.123 147.611 1.00 67.44  ? 257  LEU A N     1 
ATOM   2584  C CA    . LEU B 2 260  ? 158.014 104.743 147.289 1.00 64.71  ? 257  LEU A CA    1 
ATOM   2585  C C     . LEU B 2 260  ? 157.307 104.278 146.023 1.00 59.16  ? 257  LEU A C     1 
ATOM   2586  O O     . LEU B 2 260  ? 157.885 103.541 145.215 1.00 57.24  ? 257  LEU A O     1 
ATOM   2587  C CB    . LEU B 2 260  ? 157.671 103.828 148.464 1.00 65.29  ? 257  LEU A CB    1 
ATOM   2588  C CG    . LEU B 2 260  ? 158.570 103.949 149.694 1.00 67.07  ? 257  LEU A CG    1 
ATOM   2589  C CD1   . LEU B 2 260  ? 158.047 103.077 150.823 1.00 69.56  ? 257  LEU A CD1   1 
ATOM   2590  C CD2   . LEU B 2 260  ? 160.003 103.576 149.342 1.00 66.65  ? 257  LEU A CD2   1 
ATOM   2591  N N     . TYR B 2 261  ? 156.055 104.700 145.833 1.00 56.17  ? 258  TYR A N     1 
ATOM   2592  C CA    . TYR B 2 261  ? 155.333 104.356 144.613 1.00 54.41  ? 258  TYR A CA    1 
ATOM   2593  C C     . TYR B 2 261  ? 155.982 104.994 143.390 1.00 56.04  ? 258  TYR A C     1 
ATOM   2594  O O     . TYR B 2 261  ? 156.130 104.344 142.349 1.00 57.15  ? 258  TYR A O     1 
ATOM   2595  C CB    . TYR B 2 261  ? 153.871 104.784 144.737 1.00 51.85  ? 258  TYR A CB    1 
ATOM   2596  C CG    . TYR B 2 261  ? 152.992 104.367 143.579 1.00 51.15  ? 258  TYR A CG    1 
ATOM   2597  C CD1   . TYR B 2 261  ? 152.427 103.100 143.534 1.00 53.44  ? 258  TYR A CD1   1 
ATOM   2598  C CD2   . TYR B 2 261  ? 152.710 105.247 142.542 1.00 49.86  ? 258  TYR A CD2   1 
ATOM   2599  C CE1   . TYR B 2 261  ? 151.615 102.715 142.483 1.00 53.30  ? 258  TYR A CE1   1 
ATOM   2600  C CE2   . TYR B 2 261  ? 151.899 104.871 141.485 1.00 47.62  ? 258  TYR A CE2   1 
ATOM   2601  C CZ    . TYR B 2 261  ? 151.355 103.605 141.461 1.00 49.77  ? 258  TYR A CZ    1 
ATOM   2602  O OH    . TYR B 2 261  ? 150.547 103.224 140.415 1.00 50.05  ? 258  TYR A OH    1 
ATOM   2603  N N     . ASN B 2 262  ? 156.381 106.264 143.499 1.00 54.59  ? 259  ASN A N     1 
ATOM   2604  C CA    . ASN B 2 262  ? 157.034 106.928 142.376 1.00 52.61  ? 259  ASN A CA    1 
ATOM   2605  C C     . ASN B 2 262  ? 158.412 106.342 142.096 1.00 53.01  ? 259  ASN A C     1 
ATOM   2606  O O     . ASN B 2 262  ? 158.853 106.328 140.940 1.00 51.79  ? 259  ASN A O     1 
ATOM   2607  C CB    . ASN B 2 262  ? 157.140 108.431 142.635 1.00 51.60  ? 259  ASN A CB    1 
ATOM   2608  C CG    . ASN B 2 262  ? 155.813 109.148 142.475 1.00 51.57  ? 259  ASN A CG    1 
ATOM   2609  O OD1   . ASN B 2 262  ? 154.883 108.625 141.861 1.00 53.47  ? 259  ASN A OD1   1 
ATOM   2610  N ND2   . ASN B 2 262  ? 155.723 110.356 143.018 1.00 50.65  ? 259  ASN A ND2   1 
ATOM   2611  N N     . GLN B 2 263  ? 159.107 105.857 143.127 1.00 54.76  ? 260  GLN A N     1 
ATOM   2612  C CA    . GLN B 2 263  ? 160.427 105.274 142.914 1.00 54.41  ? 260  GLN A CA    1 
ATOM   2613  C C     . GLN B 2 263  ? 160.342 103.865 142.340 1.00 54.43  ? 260  GLN A C     1 
ATOM   2614  O O     . GLN B 2 263  ? 161.287 103.413 141.684 1.00 53.01  ? 260  GLN A O     1 
ATOM   2615  C CB    . GLN B 2 263  ? 161.227 105.279 144.217 1.00 53.89  ? 260  GLN A CB    1 
ATOM   2616  C CG    . GLN B 2 263  ? 161.632 106.674 144.668 1.00 54.92  ? 260  GLN A CG    1 
ATOM   2617  C CD    . GLN B 2 263  ? 162.657 106.656 145.781 1.00 61.21  ? 260  GLN A CD    1 
ATOM   2618  O OE1   . GLN B 2 263  ? 162.312 106.748 146.959 1.00 64.38  ? 260  GLN A OE1   1 
ATOM   2619  N NE2   . GLN B 2 263  ? 163.927 106.543 145.413 1.00 63.27  ? 260  GLN A NE2   1 
ATOM   2620  N N     . LEU B 2 264  ? 159.234 103.159 142.577 1.00 54.91  ? 261  LEU A N     1 
ATOM   2621  C CA    . LEU B 2 264  ? 158.990 101.920 141.848 1.00 55.07  ? 261  LEU A CA    1 
ATOM   2622  C C     . LEU B 2 264  ? 158.843 102.184 140.357 1.00 53.74  ? 261  LEU A C     1 
ATOM   2623  O O     . LEU B 2 264  ? 159.246 101.354 139.533 1.00 52.88  ? 261  LEU A O     1 
ATOM   2624  C CB    . LEU B 2 264  ? 157.739 101.227 142.391 1.00 56.87  ? 261  LEU A CB    1 
ATOM   2625  C CG    . LEU B 2 264  ? 157.273 99.960  141.670 1.00 56.59  ? 261  LEU A CG    1 
ATOM   2626  C CD1   . LEU B 2 264  ? 158.267 98.826  141.863 1.00 57.02  ? 261  LEU A CD1   1 
ATOM   2627  C CD2   . LEU B 2 264  ? 155.883 99.549  142.137 1.00 56.90  ? 261  LEU A CD2   1 
ATOM   2628  N N     . LEU B 2 265  ? 158.281 103.339 139.993 1.00 55.18  ? 262  LEU A N     1 
ATOM   2629  C CA    . LEU B 2 265  ? 158.124 103.700 138.589 1.00 52.92  ? 262  LEU A CA    1 
ATOM   2630  C C     . LEU B 2 265  ? 159.401 104.302 138.017 1.00 51.37  ? 262  LEU A C     1 
ATOM   2631  O O     . LEU B 2 265  ? 159.715 104.094 136.839 1.00 50.02  ? 262  LEU A O     1 
ATOM   2632  C CB    . LEU B 2 265  ? 156.966 104.688 138.426 1.00 53.02  ? 262  LEU A CB    1 
ATOM   2633  C CG    . LEU B 2 265  ? 155.524 104.184 138.302 1.00 53.63  ? 262  LEU A CG    1 
ATOM   2634  C CD1   . LEU B 2 265  ? 155.128 103.302 139.472 1.00 56.55  ? 262  LEU A CD1   1 
ATOM   2635  C CD2   . LEU B 2 265  ? 154.578 105.369 138.185 1.00 53.02  ? 262  LEU A CD2   1 
ATOM   2636  N N     . GLY B 2 266  ? 160.147 105.048 138.830 1.00 48.62  ? 263  GLY A N     1 
ATOM   2637  C CA    . GLY B 2 266  ? 161.276 105.809 138.334 1.00 49.22  ? 263  GLY A CA    1 
ATOM   2638  C C     . GLY B 2 266  ? 162.639 105.217 138.634 1.00 51.70  ? 263  GLY A C     1 
ATOM   2639  O O     . GLY B 2 266  ? 163.629 105.584 137.995 1.00 50.97  ? 263  GLY A O     1 
ATOM   2640  N N     . GLY B 2 267  ? 162.710 104.309 139.603 1.00 53.73  ? 264  GLY A N     1 
ATOM   2641  C CA    . GLY B 2 267  ? 163.973 103.697 139.956 1.00 56.95  ? 264  GLY A CA    1 
ATOM   2642  C C     . GLY B 2 267  ? 164.769 104.531 140.941 1.00 59.64  ? 264  GLY A C     1 
ATOM   2643  O O     . GLY B 2 267  ? 164.358 105.602 141.389 1.00 62.18  ? 264  GLY A O     1 
ATOM   2644  N N     . LYS B 2 327  ? 168.119 136.741 144.218 1.00 105.25 ? 324  LYS A N     1 
ATOM   2645  C CA    . LYS B 2 327  ? 168.562 137.764 145.154 1.00 105.46 ? 324  LYS A CA    1 
ATOM   2646  C C     . LYS B 2 327  ? 169.777 138.557 144.690 1.00 106.48 ? 324  LYS A C     1 
ATOM   2647  O O     . LYS B 2 327  ? 170.052 139.616 145.264 1.00 106.46 ? 324  LYS A O     1 
ATOM   2648  C CB    . LYS B 2 327  ? 168.869 137.128 146.518 1.00 106.73 ? 324  LYS A CB    1 
ATOM   2649  C CG    . LYS B 2 327  ? 167.645 136.567 147.228 1.00 105.20 ? 324  LYS A CG    1 
ATOM   2650  C CD    . LYS B 2 327  ? 166.618 137.658 147.498 1.00 103.53 ? 324  LYS A CD    1 
ATOM   2651  C CE    . LYS B 2 327  ? 165.389 137.110 148.206 1.00 102.73 ? 324  LYS A CE    1 
ATOM   2652  N NZ    . LYS B 2 327  ? 164.379 138.178 148.466 1.00 99.75  ? 324  LYS A NZ    1 
ATOM   2653  N N     . SER B 2 328  ? 170.510 138.093 143.680 1.00 108.92 ? 325  SER A N     1 
ATOM   2654  C CA    . SER B 2 328  ? 171.708 138.801 143.250 1.00 112.73 ? 325  SER A CA    1 
ATOM   2655  C C     . SER B 2 328  ? 171.863 138.671 141.740 1.00 112.17 ? 325  SER A C     1 
ATOM   2656  O O     . SER B 2 328  ? 171.087 137.985 141.068 1.00 110.18 ? 325  SER A O     1 
ATOM   2657  C CB    . SER B 2 328  ? 172.951 138.284 143.984 1.00 117.56 ? 325  SER A CB    1 
ATOM   2658  O OG    . SER B 2 328  ? 173.308 136.985 143.546 1.00 118.93 ? 325  SER A OG    1 
ATOM   2659  N N     . ASP B 2 329  ? 172.885 139.345 141.212 1.00 114.71 ? 326  ASP A N     1 
ATOM   2660  C CA    . ASP B 2 329  ? 173.128 139.364 139.773 1.00 115.09 ? 326  ASP A CA    1 
ATOM   2661  C C     . ASP B 2 329  ? 173.742 138.054 139.296 1.00 117.19 ? 326  ASP A C     1 
ATOM   2662  O O     . ASP B 2 329  ? 173.301 137.482 138.294 1.00 116.07 ? 326  ASP A O     1 
ATOM   2663  C CB    . ASP B 2 329  ? 174.032 140.547 139.418 1.00 117.35 ? 326  ASP A CB    1 
ATOM   2664  C CG    . ASP B 2 329  ? 173.969 140.909 137.950 1.00 116.26 ? 326  ASP A CG    1 
ATOM   2665  O OD1   . ASP B 2 329  ? 174.754 140.341 137.160 1.00 118.06 ? 326  ASP A OD1   1 
ATOM   2666  O OD2   . ASP B 2 329  ? 173.136 141.765 137.587 1.00 113.92 ? 326  ASP A OD2   1 
ATOM   2667  N N     . GLU B 2 330  ? 174.760 137.564 140.003 1.00 120.49 ? 327  GLU A N     1 
ATOM   2668  C CA    . GLU B 2 330  ? 175.414 136.316 139.635 1.00 122.30 ? 327  GLU A CA    1 
ATOM   2669  C C     . GLU B 2 330  ? 174.605 135.085 140.019 1.00 122.50 ? 327  GLU A C     1 
ATOM   2670  O O     . GLU B 2 330  ? 174.915 133.989 139.537 1.00 122.41 ? 327  GLU A O     1 
ATOM   2671  C CB    . GLU B 2 330  ? 176.802 136.240 140.278 1.00 124.73 ? 327  GLU A CB    1 
ATOM   2672  N N     . GLU B 2 331  ? 173.584 135.232 140.869 1.00 121.40 ? 328  GLU A N     1 
ATOM   2673  C CA    . GLU B 2 331  ? 172.775 134.078 141.250 1.00 119.35 ? 328  GLU A CA    1 
ATOM   2674  C C     . GLU B 2 331  ? 171.998 133.534 140.058 1.00 116.34 ? 328  GLU A C     1 
ATOM   2675  O O     . GLU B 2 331  ? 171.815 132.318 139.935 1.00 115.25 ? 328  GLU A O     1 
ATOM   2676  C CB    . GLU B 2 331  ? 171.821 134.451 142.384 1.00 116.65 ? 328  GLU A CB    1 
ATOM   2677  C CG    . GLU B 2 331  ? 171.027 133.276 142.939 1.00 115.81 ? 328  GLU A CG    1 
ATOM   2678  C CD    . GLU B 2 331  ? 170.013 133.697 143.987 1.00 115.55 ? 328  GLU A CD    1 
ATOM   2679  O OE1   . GLU B 2 331  ? 169.850 134.916 144.204 1.00 114.69 ? 328  GLU A OE1   1 
ATOM   2680  O OE2   . GLU B 2 331  ? 169.378 132.809 144.596 1.00 116.52 ? 328  GLU A OE2   1 
ATOM   2681  N N     . VAL B 2 332  ? 171.538 134.415 139.169 1.00 118.09 ? 329  VAL A N     1 
ATOM   2682  C CA    . VAL B 2 332  ? 170.815 133.948 137.992 1.00 114.87 ? 329  VAL A CA    1 
ATOM   2683  C C     . VAL B 2 332  ? 171.772 133.324 136.988 1.00 116.01 ? 329  VAL A C     1 
ATOM   2684  O O     . VAL B 2 332  ? 171.374 132.465 136.194 1.00 116.94 ? 329  VAL A O     1 
ATOM   2685  C CB    . VAL B 2 332  ? 170.002 135.097 137.362 1.00 113.17 ? 329  VAL A CB    1 
ATOM   2686  C CG1   . VAL B 2 332  ? 169.240 135.856 138.434 1.00 112.44 ? 329  VAL A CG1   1 
ATOM   2687  C CG2   . VAL B 2 332  ? 170.902 136.037 136.574 1.00 114.05 ? 329  VAL A CG2   1 
ATOM   2688  N N     . ILE B 2 333  ? 173.043 133.728 137.003 1.00 116.48 ? 330  ILE A N     1 
ATOM   2689  C CA    . ILE B 2 333  ? 174.005 133.160 136.067 1.00 110.83 ? 330  ILE A CA    1 
ATOM   2690  C C     . ILE B 2 333  ? 174.529 131.826 136.579 1.00 108.13 ? 330  ILE A C     1 
ATOM   2691  O O     . ILE B 2 333  ? 174.659 130.866 135.814 1.00 107.26 ? 330  ILE A O     1 
ATOM   2692  C CB    . ILE B 2 333  ? 175.149 134.155 135.808 1.00 104.58 ? 330  ILE A CB    1 
ATOM   2693  C CG1   . ILE B 2 333  ? 174.592 135.517 135.395 1.00 96.96  ? 330  ILE A CG1   1 
ATOM   2694  C CG2   . ILE B 2 333  ? 176.083 133.622 134.732 1.00 103.21 ? 330  ILE A CG2   1 
ATOM   2695  C CD1   . ILE B 2 333  ? 175.660 136.558 135.152 1.00 95.34  ? 330  ILE A CD1   1 
ATOM   2696  N N     . GLN B 2 334  ? 174.832 131.743 137.876 1.00 108.13 ? 331  GLN A N     1 
ATOM   2697  C CA    . GLN B 2 334  ? 175.355 130.499 138.433 1.00 111.56 ? 331  GLN A CA    1 
ATOM   2698  C C     . GLN B 2 334  ? 174.288 129.412 138.460 1.00 112.21 ? 331  GLN A C     1 
ATOM   2699  O O     . GLN B 2 334  ? 174.584 128.238 138.211 1.00 113.89 ? 331  GLN A O     1 
ATOM   2700  C CB    . GLN B 2 334  ? 175.909 130.745 139.835 1.00 113.13 ? 331  GLN A CB    1 
ATOM   2701  N N     . SER B 2 335  ? 173.039 129.782 138.756 1.00 110.88 ? 332  SER A N     1 
ATOM   2702  C CA    . SER B 2 335  ? 171.974 128.785 138.832 1.00 109.08 ? 332  SER A CA    1 
ATOM   2703  C C     . SER B 2 335  ? 171.550 128.320 137.445 1.00 106.57 ? 332  SER A C     1 
ATOM   2704  O O     . SER B 2 335  ? 171.340 127.121 137.225 1.00 105.31 ? 332  SER A O     1 
ATOM   2705  C CB    . SER B 2 335  ? 170.777 129.351 139.597 1.00 107.27 ? 332  SER A CB    1 
ATOM   2706  O OG    . SER B 2 335  ? 169.742 128.390 139.704 1.00 107.23 ? 332  SER A OG    1 
ATOM   2707  N N     . PHE B 2 336  ? 171.409 129.253 136.499 1.00 104.19 ? 333  PHE A N     1 
ATOM   2708  C CA    . PHE B 2 336  ? 171.016 128.872 135.145 1.00 100.04 ? 333  PHE A CA    1 
ATOM   2709  C C     . PHE B 2 336  ? 172.106 128.047 134.476 1.00 102.92 ? 333  PHE A C     1 
ATOM   2710  O O     . PHE B 2 336  ? 171.825 126.994 133.891 1.00 103.05 ? 333  PHE A O     1 
ATOM   2711  C CB    . PHE B 2 336  ? 170.692 130.117 134.319 1.00 94.00  ? 333  PHE A CB    1 
ATOM   2712  C CG    . PHE B 2 336  ? 170.204 129.816 132.930 1.00 90.46  ? 333  PHE A CG    1 
ATOM   2713  C CD1   . PHE B 2 336  ? 169.129 128.970 132.728 1.00 87.98  ? 333  PHE A CD1   1 
ATOM   2714  C CD2   . PHE B 2 336  ? 170.813 130.393 131.827 1.00 90.37  ? 333  PHE A CD2   1 
ATOM   2715  C CE1   . PHE B 2 336  ? 168.675 128.693 131.452 1.00 86.69  ? 333  PHE A CE1   1 
ATOM   2716  C CE2   . PHE B 2 336  ? 170.363 130.122 130.548 1.00 88.66  ? 333  PHE A CE2   1 
ATOM   2717  C CZ    . PHE B 2 336  ? 169.292 129.270 130.361 1.00 86.79  ? 333  PHE A CZ    1 
ATOM   2718  N N     . CYS B 2 337  ? 173.359 128.500 134.564 1.00 107.47 ? 334  CYS A N     1 
ATOM   2719  C CA    . CYS B 2 337  ? 174.463 127.742 133.984 1.00 110.44 ? 334  CYS A CA    1 
ATOM   2720  C C     . CYS B 2 337  ? 174.602 126.372 134.632 1.00 113.43 ? 334  CYS A C     1 
ATOM   2721  O O     . CYS B 2 337  ? 175.055 125.422 133.980 1.00 114.52 ? 334  CYS A O     1 
ATOM   2722  C CB    . CYS B 2 337  ? 175.769 128.528 134.113 1.00 113.73 ? 334  CYS A CB    1 
ATOM   2723  S SG    . CYS B 2 337  ? 177.201 127.750 133.332 1.00 118.68 ? 334  CYS A SG    1 
ATOM   2724  N N     . LYS B 2 338  ? 174.224 126.244 135.906 1.00 115.22 ? 335  LYS A N     1 
ATOM   2725  C CA    . LYS B 2 338  ? 174.211 124.929 136.541 1.00 117.67 ? 335  LYS A CA    1 
ATOM   2726  C C     . LYS B 2 338  ? 173.092 124.061 135.977 1.00 115.38 ? 335  LYS A C     1 
ATOM   2727  O O     . LYS B 2 338  ? 173.295 122.872 135.711 1.00 116.32 ? 335  LYS A O     1 
ATOM   2728  C CB    . LYS B 2 338  ? 174.069 125.075 138.056 1.00 118.16 ? 335  LYS A CB    1 
ATOM   2729  N N     . TYR B 2 339  ? 171.903 124.640 135.791 1.00 111.45 ? 336  TYR A N     1 
ATOM   2730  C CA    . TYR B 2 339  ? 170.828 123.915 135.122 1.00 107.89 ? 336  TYR A CA    1 
ATOM   2731  C C     . TYR B 2 339  ? 171.106 123.762 133.634 1.00 102.25 ? 336  TYR A C     1 
ATOM   2732  O O     . TYR B 2 339  ? 170.701 122.764 133.027 1.00 101.75 ? 336  TYR A O     1 
ATOM   2733  C CB    . TYR B 2 339  ? 169.495 124.630 135.348 1.00 108.02 ? 336  TYR A CB    1 
ATOM   2734  C CG    . TYR B 2 339  ? 168.378 124.177 134.433 1.00 107.66 ? 336  TYR A CG    1 
ATOM   2735  C CD1   . TYR B 2 339  ? 167.686 122.999 134.680 1.00 108.62 ? 336  TYR A CD1   1 
ATOM   2736  C CD2   . TYR B 2 339  ? 168.012 124.932 133.326 1.00 105.60 ? 336  TYR A CD2   1 
ATOM   2737  C CE1   . TYR B 2 339  ? 166.663 122.584 133.847 1.00 106.67 ? 336  TYR A CE1   1 
ATOM   2738  C CE2   . TYR B 2 339  ? 166.992 124.525 132.487 1.00 103.47 ? 336  TYR A CE2   1 
ATOM   2739  C CZ    . TYR B 2 339  ? 166.319 123.351 132.754 1.00 104.20 ? 336  TYR A CZ    1 
ATOM   2740  O OH    . TYR B 2 339  ? 165.303 122.940 131.922 1.00 102.33 ? 336  TYR A OH    1 
ATOM   2741  N N     . LYS B 2 340  ? 171.794 124.735 133.035 1.00 97.81  ? 337  LYS A N     1 
ATOM   2742  C CA    . LYS B 2 340  ? 172.124 124.649 131.618 1.00 94.74  ? 337  LYS A CA    1 
ATOM   2743  C C     . LYS B 2 340  ? 173.131 123.533 131.357 1.00 98.35  ? 337  LYS A C     1 
ATOM   2744  O O     . LYS B 2 340  ? 172.958 122.737 130.428 1.00 98.39  ? 337  LYS A O     1 
ATOM   2745  C CB    . LYS B 2 340  ? 172.658 125.996 131.132 1.00 92.46  ? 337  LYS A CB    1 
ATOM   2746  C CG    . LYS B 2 340  ? 173.008 126.062 129.666 1.00 90.58  ? 337  LYS A CG    1 
ATOM   2747  C CD    . LYS B 2 340  ? 173.176 127.506 129.239 1.00 88.48  ? 337  LYS A CD    1 
ATOM   2748  C CE    . LYS B 2 340  ? 174.045 127.616 128.005 1.00 89.72  ? 337  LYS A CE    1 
ATOM   2749  N NZ    . LYS B 2 340  ? 174.140 129.013 127.508 1.00 88.85  ? 337  LYS A NZ    1 
ATOM   2750  N N     . THR B 2 341  ? 174.181 123.451 132.179 1.00 100.96 ? 338  THR A N     1 
ATOM   2751  C CA    . THR B 2 341  ? 175.161 122.383 132.021 1.00 101.82 ? 338  THR A CA    1 
ATOM   2752  C C     . THR B 2 341  ? 174.588 121.018 132.378 1.00 101.52 ? 338  THR A C     1 
ATOM   2753  O O     . THR B 2 341  ? 175.159 119.995 131.981 1.00 102.56 ? 338  THR A O     1 
ATOM   2754  C CB    . THR B 2 341  ? 176.408 122.667 132.868 1.00 103.05 ? 338  THR A CB    1 
ATOM   2755  O OG1   . THR B 2 341  ? 177.485 121.828 132.432 1.00 106.87 ? 338  THR A OG1   1 
ATOM   2756  C CG2   . THR B 2 341  ? 176.137 122.391 134.341 1.00 102.09 ? 338  THR A CG2   1 
ATOM   2757  N N     . LEU B 2 342  ? 173.473 120.980 133.112 1.00 102.17 ? 339  LEU A N     1 
ATOM   2758  C CA    . LEU B 2 342  ? 172.803 119.718 133.403 1.00 103.53 ? 339  LEU A CA    1 
ATOM   2759  C C     . LEU B 2 342  ? 172.067 119.176 132.185 1.00 102.63 ? 339  LEU A C     1 
ATOM   2760  O O     . LEU B 2 342  ? 171.901 117.957 132.057 1.00 101.63 ? 339  LEU A O     1 
ATOM   2761  C CB    . LEU B 2 342  ? 171.836 119.904 134.576 1.00 104.21 ? 339  LEU A CB    1 
ATOM   2762  C CG    . LEU B 2 342  ? 171.100 118.683 135.132 1.00 106.12 ? 339  LEU A CG    1 
ATOM   2763  C CD1   . LEU B 2 342  ? 171.023 118.766 136.645 1.00 108.19 ? 339  LEU A CD1   1 
ATOM   2764  C CD2   . LEU B 2 342  ? 169.705 118.577 134.542 1.00 104.03 ? 339  LEU A CD2   1 
ATOM   2765  N N     . LEU B 2 343  ? 171.631 120.056 131.280 1.00 102.68 ? 340  LEU A N     1 
ATOM   2766  C CA    . LEU B 2 343  ? 170.947 119.614 130.073 1.00 102.74 ? 340  LEU A CA    1 
ATOM   2767  C C     . LEU B 2 343  ? 171.890 118.938 129.088 1.00 104.95 ? 340  LEU A C     1 
ATOM   2768  O O     . LEU B 2 343  ? 171.436 118.126 128.277 1.00 104.96 ? 340  LEU A O     1 
ATOM   2769  C CB    . LEU B 2 343  ? 170.249 120.799 129.403 1.00 101.14 ? 340  LEU A CB    1 
ATOM   2770  C CG    . LEU B 2 343  ? 169.195 121.523 130.246 1.00 98.30  ? 340  LEU A CG    1 
ATOM   2771  C CD1   . LEU B 2 343  ? 168.730 122.790 129.552 1.00 94.25  ? 340  LEU A CD1   1 
ATOM   2772  C CD2   . LEU B 2 343  ? 168.016 120.609 130.540 1.00 96.62  ? 340  LEU A CD2   1 
ATOM   2773  N N     . ARG B 2 344  ? 173.186 119.255 129.137 1.00 107.33 ? 341  ARG A N     1 
ATOM   2774  C CA    . ARG B 2 344  ? 174.141 118.569 128.273 1.00 110.50 ? 341  ARG A CA    1 
ATOM   2775  C C     . ARG B 2 344  ? 174.396 117.146 128.756 1.00 113.25 ? 341  ARG A C     1 
ATOM   2776  O O     . ARG B 2 344  ? 174.433 116.209 127.951 1.00 113.74 ? 341  ARG A O     1 
ATOM   2777  C CB    . ARG B 2 344  ? 175.460 119.344 128.205 1.00 113.99 ? 341  ARG A CB    1 
ATOM   2778  C CG    . ARG B 2 344  ? 175.427 120.629 127.390 1.00 113.53 ? 341  ARG A CG    1 
ATOM   2779  C CD    . ARG B 2 344  ? 174.946 121.802 128.225 1.00 113.95 ? 341  ARG A CD    1 
ATOM   2780  N NE    . ARG B 2 344  ? 175.621 123.047 127.874 1.00 115.55 ? 341  ARG A NE    1 
ATOM   2781  C CZ    . ARG B 2 344  ? 176.728 123.486 128.463 1.00 118.46 ? 341  ARG A CZ    1 
ATOM   2782  N NH1   . ARG B 2 344  ? 177.291 122.779 129.432 1.00 121.22 ? 341  ARG A NH1   1 
ATOM   2783  N NH2   . ARG B 2 344  ? 177.276 124.633 128.083 1.00 118.53 ? 341  ARG A NH2   1 
ATOM   2784  N N     . ASN B 2 345  ? 174.574 116.970 130.068 1.00 114.62 ? 342  ASN A N     1 
ATOM   2785  C CA    . ASN B 2 345  ? 174.886 115.649 130.605 1.00 116.13 ? 342  ASN A CA    1 
ATOM   2786  C C     . ASN B 2 345  ? 173.724 114.682 130.417 1.00 115.20 ? 342  ASN A C     1 
ATOM   2787  O O     . ASN B 2 345  ? 173.931 113.506 130.098 1.00 116.25 ? 342  ASN A O     1 
ATOM   2788  C CB    . ASN B 2 345  ? 175.263 115.760 132.082 1.00 116.22 ? 342  ASN A CB    1 
ATOM   2789  C CG    . ASN B 2 345  ? 176.419 116.718 132.319 1.00 116.84 ? 342  ASN A CG    1 
ATOM   2790  O OD1   . ASN B 2 345  ? 177.271 116.907 131.452 1.00 117.55 ? 342  ASN A OD1   1 
ATOM   2791  N ND2   . ASN B 2 345  ? 176.450 117.326 133.498 1.00 116.72 ? 342  ASN A ND2   1 
ATOM   2792  N N     . GLU B 2 346  ? 172.491 115.158 130.611 1.00 111.92 ? 343  GLU A N     1 
ATOM   2793  C CA    . GLU B 2 346  ? 171.324 114.321 130.353 1.00 109.11 ? 343  GLU A CA    1 
ATOM   2794  C C     . GLU B 2 346  ? 171.078 114.122 128.864 1.00 107.79 ? 343  GLU A C     1 
ATOM   2795  O O     . GLU B 2 346  ? 170.326 113.215 128.491 1.00 105.60 ? 343  GLU A O     1 
ATOM   2796  C CB    . GLU B 2 346  ? 170.081 114.927 131.007 1.00 104.32 ? 343  GLU A CB    1 
ATOM   2797  C CG    . GLU B 2 346  ? 170.085 114.877 132.525 1.00 103.95 ? 343  GLU A CG    1 
ATOM   2798  C CD    . GLU B 2 346  ? 168.868 115.546 133.135 1.00 101.05 ? 343  GLU A CD    1 
ATOM   2799  O OE1   . GLU B 2 346  ? 168.274 116.424 132.472 1.00 98.91  ? 343  GLU A OE1   1 
ATOM   2800  O OE2   . GLU B 2 346  ? 168.503 115.196 134.277 1.00 101.42 ? 343  GLU A OE2   1 
ATOM   2801  N N     . ASN B 2 347  ? 171.693 114.947 128.013 1.00 109.45 ? 344  ASN A N     1 
ATOM   2802  C CA    . ASN B 2 347  ? 171.531 114.867 126.561 1.00 109.06 ? 344  ASN A CA    1 
ATOM   2803  C C     . ASN B 2 347  ? 170.056 114.952 126.170 1.00 105.87 ? 344  ASN A C     1 
ATOM   2804  O O     . ASN B 2 347  ? 169.555 114.173 125.356 1.00 104.52 ? 344  ASN A O     1 
ATOM   2805  C CB    . ASN B 2 347  ? 172.179 113.594 126.004 1.00 111.26 ? 344  ASN A CB    1 
ATOM   2806  N N     . VAL B 2 348  ? 169.355 115.919 126.766 1.00 105.13 ? 345  VAL A N     1 
ATOM   2807  C CA    . VAL B 2 348  ? 167.930 116.070 126.493 1.00 103.11 ? 345  VAL A CA    1 
ATOM   2808  C C     . VAL B 2 348  ? 167.698 116.589 125.081 1.00 101.24 ? 345  VAL A C     1 
ATOM   2809  O O     . VAL B 2 348  ? 166.659 116.304 124.473 1.00 97.55  ? 345  VAL A O     1 
ATOM   2810  C CB    . VAL B 2 348  ? 167.270 116.982 127.546 1.00 102.40 ? 345  VAL A CB    1 
ATOM   2811  C CG1   . VAL B 2 348  ? 167.367 116.350 128.924 1.00 104.27 ? 345  VAL A CG1   1 
ATOM   2812  C CG2   . VAL B 2 348  ? 167.913 118.359 127.541 1.00 103.47 ? 345  VAL A CG2   1 
ATOM   2813  N N     . LEU B 2 349  ? 168.646 117.351 124.530 1.00 103.31 ? 346  LEU A N     1 
ATOM   2814  C CA    . LEU B 2 349  ? 168.522 117.777 123.139 1.00 101.76 ? 346  LEU A CA    1 
ATOM   2815  C C     . LEU B 2 349  ? 168.629 116.589 122.193 1.00 100.10 ? 346  LEU A C     1 
ATOM   2816  O O     . LEU B 2 349  ? 167.817 116.442 121.273 1.00 97.78  ? 346  LEU A O     1 
ATOM   2817  C CB    . LEU B 2 349  ? 169.576 118.839 122.800 1.00 105.30 ? 346  LEU A CB    1 
ATOM   2818  C CG    . LEU B 2 349  ? 170.909 119.000 123.543 1.00 110.95 ? 346  LEU A CG    1 
ATOM   2819  C CD1   . LEU B 2 349  ? 171.724 117.716 123.624 1.00 113.43 ? 346  LEU A CD1   1 
ATOM   2820  C CD2   . LEU B 2 349  ? 171.724 120.086 122.857 1.00 112.56 ? 346  LEU A CD2   1 
ATOM   2821  N N     . GLU B 2 350  ? 169.619 115.720 122.413 1.00 102.06 ? 347  GLU A N     1 
ATOM   2822  C CA    . GLU B 2 350  ? 169.776 114.548 121.557 1.00 100.49 ? 347  GLU A CA    1 
ATOM   2823  C C     . GLU B 2 350  ? 168.586 113.609 121.690 1.00 96.96  ? 347  GLU A C     1 
ATOM   2824  O O     . GLU B 2 350  ? 168.163 112.987 120.709 1.00 93.08  ? 347  GLU A O     1 
ATOM   2825  C CB    . GLU B 2 350  ? 171.078 113.822 121.898 1.00 102.99 ? 347  GLU A CB    1 
ATOM   2826  N N     . THR B 2 351  ? 168.029 113.496 122.897 1.00 98.00  ? 348  THR A N     1 
ATOM   2827  C CA    . THR B 2 351  ? 166.839 112.674 123.084 1.00 96.48  ? 348  THR A CA    1 
ATOM   2828  C C     . THR B 2 351  ? 165.627 113.300 122.405 1.00 93.15  ? 348  THR A C     1 
ATOM   2829  O O     . THR B 2 351  ? 164.804 112.592 121.814 1.00 92.60  ? 348  THR A O     1 
ATOM   2830  C CB    . THR B 2 351  ? 166.569 112.467 124.574 1.00 95.65  ? 348  THR A CB    1 
ATOM   2831  O OG1   . THR B 2 351  ? 167.773 112.044 125.226 1.00 98.29  ? 348  THR A OG1   1 
ATOM   2832  C CG2   . THR B 2 351  ? 165.494 111.411 124.780 1.00 93.45  ? 348  THR A CG2   1 
ATOM   2833  N N     . ALA B 2 352  ? 165.506 114.628 122.475 1.00 91.33  ? 349  ALA A N     1 
ATOM   2834  C CA    . ALA B 2 352  ? 164.392 115.305 121.819 1.00 88.04  ? 349  ALA A CA    1 
ATOM   2835  C C     . ALA B 2 352  ? 164.536 115.268 120.303 1.00 88.99  ? 349  ALA A C     1 
ATOM   2836  O O     . ALA B 2 352  ? 163.557 115.027 119.587 1.00 86.44  ? 349  ALA A O     1 
ATOM   2837  C CB    . ALA B 2 352  ? 164.286 116.747 122.313 1.00 87.74  ? 349  ALA A CB    1 
ATOM   2838  N N     . GLU B 2 353  ? 165.750 115.501 119.795 1.00 92.33  ? 350  GLU A N     1 
ATOM   2839  C CA    . GLU B 2 353  ? 165.972 115.431 118.353 1.00 92.52  ? 350  GLU A CA    1 
ATOM   2840  C C     . GLU B 2 353  ? 165.722 114.028 117.818 1.00 91.73  ? 350  GLU A C     1 
ATOM   2841  O O     . GLU B 2 353  ? 165.332 113.867 116.656 1.00 90.57  ? 350  GLU A O     1 
ATOM   2842  C CB    . GLU B 2 353  ? 167.392 115.891 118.016 1.00 94.61  ? 350  GLU A CB    1 
ATOM   2843  C CG    . GLU B 2 353  ? 167.661 117.361 118.313 1.00 95.40  ? 350  GLU A CG    1 
ATOM   2844  C CD    . GLU B 2 353  ? 169.138 117.710 118.263 1.00 99.29  ? 350  GLU A CD    1 
ATOM   2845  O OE1   . GLU B 2 353  ? 169.858 117.142 117.413 1.00 100.83 ? 350  GLU A OE1   1 
ATOM   2846  O OE2   . GLU B 2 353  ? 169.582 118.547 119.078 1.00 100.16 ? 350  GLU A OE2   1 
ATOM   2847  N N     . ALA B 2 354  ? 165.935 113.003 118.648 1.00 92.39  ? 351  ALA A N     1 
ATOM   2848  C CA    . ALA B 2 354  ? 165.675 111.632 118.224 1.00 91.05  ? 351  ALA A CA    1 
ATOM   2849  C C     . ALA B 2 354  ? 164.190 111.298 118.242 1.00 87.24  ? 351  ALA A C     1 
ATOM   2850  O O     . ALA B 2 354  ? 163.731 110.500 117.416 1.00 87.35  ? 351  ALA A O     1 
ATOM   2851  C CB    . ALA B 2 354  ? 166.443 110.652 119.112 1.00 94.16  ? 351  ALA A CB    1 
ATOM   2852  N N     . LEU B 2 355  ? 163.427 111.888 119.165 1.00 84.23  ? 352  LEU A N     1 
ATOM   2853  C CA    . LEU B 2 355  ? 161.994 111.622 119.221 1.00 77.51  ? 352  LEU A CA    1 
ATOM   2854  C C     . LEU B 2 355  ? 161.279 112.200 118.009 1.00 73.06  ? 352  LEU A C     1 
ATOM   2855  O O     . LEU B 2 355  ? 160.461 111.521 117.376 1.00 72.80  ? 352  LEU A O     1 
ATOM   2856  C CB    . LEU B 2 355  ? 161.399 112.189 120.511 1.00 73.00  ? 352  LEU A CB    1 
ATOM   2857  C CG    . LEU B 2 355  ? 161.494 111.299 121.747 1.00 73.05  ? 352  LEU A CG    1 
ATOM   2858  C CD1   . LEU B 2 355  ? 160.746 111.931 122.905 1.00 72.47  ? 352  LEU A CD1   1 
ATOM   2859  C CD2   . LEU B 2 355  ? 160.953 109.910 121.445 1.00 72.02  ? 352  LEU A CD2   1 
ATOM   2860  N N     . PHE B 2 356  ? 161.564 113.460 117.673 1.00 71.29  ? 353  PHE A N     1 
ATOM   2861  C CA    . PHE B 2 356  ? 160.925 114.071 116.516 1.00 71.33  ? 353  PHE A CA    1 
ATOM   2862  C C     . PHE B 2 356  ? 161.386 113.445 115.207 1.00 74.85  ? 353  PHE A C     1 
ATOM   2863  O O     . PHE B 2 356  ? 160.661 113.518 114.211 1.00 74.54  ? 353  PHE A O     1 
ATOM   2864  C CB    . PHE B 2 356  ? 161.180 115.577 116.508 1.00 70.58  ? 353  PHE A CB    1 
ATOM   2865  C CG    . PHE B 2 356  ? 160.446 116.317 117.589 1.00 71.19  ? 353  PHE A CG    1 
ATOM   2866  C CD1   . PHE B 2 356  ? 159.119 116.678 117.420 1.00 70.15  ? 353  PHE A CD1   1 
ATOM   2867  C CD2   . PHE B 2 356  ? 161.080 116.648 118.774 1.00 72.74  ? 353  PHE A CD2   1 
ATOM   2868  C CE1   . PHE B 2 356  ? 158.439 117.355 118.415 1.00 69.49  ? 353  PHE A CE1   1 
ATOM   2869  C CE2   . PHE B 2 356  ? 160.406 117.326 119.772 1.00 71.46  ? 353  PHE A CE2   1 
ATOM   2870  C CZ    . PHE B 2 356  ? 159.085 117.680 119.592 1.00 70.08  ? 353  PHE A CZ    1 
ATOM   2871  N N     . ASN B 2 357  ? 162.569 112.830 115.189 1.00 78.80  ? 354  ASN A N     1 
ATOM   2872  C CA    . ASN B 2 357  ? 162.994 112.071 114.020 1.00 80.91  ? 354  ASN A CA    1 
ATOM   2873  C C     . ASN B 2 357  ? 162.290 110.725 113.920 1.00 81.70  ? 354  ASN A C     1 
ATOM   2874  O O     . ASN B 2 357  ? 162.173 110.182 112.816 1.00 80.63  ? 354  ASN A O     1 
ATOM   2875  C CB    . ASN B 2 357  ? 164.510 111.870 114.041 1.00 85.48  ? 354  ASN A CB    1 
ATOM   2876  C CG    . ASN B 2 357  ? 165.033 111.259 112.758 1.00 88.53  ? 354  ASN A CG    1 
ATOM   2877  O OD1   . ASN B 2 357  ? 165.304 110.060 112.693 1.00 90.33  ? 354  ASN A OD1   1 
ATOM   2878  N ND2   . ASN B 2 357  ? 165.171 112.080 111.723 1.00 88.81  ? 354  ASN A ND2   1 
ATOM   2879  N N     . GLU B 2 358  ? 161.813 110.181 115.044 1.00 82.95  ? 355  GLU A N     1 
ATOM   2880  C CA    . GLU B 2 358  ? 161.029 108.950 114.999 1.00 82.30  ? 355  GLU A CA    1 
ATOM   2881  C C     . GLU B 2 358  ? 159.713 109.150 114.261 1.00 75.99  ? 355  GLU A C     1 
ATOM   2882  O O     . GLU B 2 358  ? 159.184 108.201 113.668 1.00 72.20  ? 355  GLU A O     1 
ATOM   2883  C CB    . GLU B 2 358  ? 160.753 108.442 116.416 1.00 85.13  ? 355  GLU A CB    1 
ATOM   2884  C CG    . GLU B 2 358  ? 161.834 107.551 117.000 1.00 89.31  ? 355  GLU A CG    1 
ATOM   2885  C CD    . GLU B 2 358  ? 161.456 107.012 118.366 1.00 91.80  ? 355  GLU A CD    1 
ATOM   2886  O OE1   . GLU B 2 358  ? 160.504 106.206 118.445 1.00 94.59  ? 355  GLU A OE1   1 
ATOM   2887  O OE2   . GLU B 2 358  ? 162.101 107.401 119.364 1.00 90.93  ? 355  GLU A OE2   1 
ATOM   2888  N N     . LEU B 2 359  ? 159.173 110.369 114.277 1.00 75.35  ? 356  LEU A N     1 
ATOM   2889  C CA    . LEU B 2 359  ? 157.865 110.630 113.686 1.00 72.72  ? 356  LEU A CA    1 
ATOM   2890  C C     . LEU B 2 359  ? 157.844 110.438 112.175 1.00 75.05  ? 356  LEU A C     1 
ATOM   2891  O O     . LEU B 2 359  ? 156.759 110.456 111.584 1.00 75.40  ? 356  LEU A O     1 
ATOM   2892  C CB    . LEU B 2 359  ? 157.416 112.052 114.034 1.00 66.63  ? 356  LEU A CB    1 
ATOM   2893  C CG    . LEU B 2 359  ? 157.361 112.389 115.525 1.00 61.22  ? 356  LEU A CG    1 
ATOM   2894  C CD1   . LEU B 2 359  ? 157.052 113.860 115.726 1.00 58.93  ? 356  LEU A CD1   1 
ATOM   2895  C CD2   . LEU B 2 359  ? 156.334 111.521 116.239 1.00 58.90  ? 356  LEU A CD2   1 
ATOM   2896  N N     . ASN B 2 360  ? 159.002 110.251 111.539 1.00 79.90  ? 357  ASN A N     1 
ATOM   2897  C CA    . ASN B 2 360  ? 159.043 110.044 110.098 1.00 80.98  ? 357  ASN A CA    1 
ATOM   2898  C C     . ASN B 2 360  ? 158.757 108.603 109.700 1.00 81.94  ? 357  ASN A C     1 
ATOM   2899  O O     . ASN B 2 360  ? 158.456 108.347 108.528 1.00 83.54  ? 357  ASN A O     1 
ATOM   2900  C CB    . ASN B 2 360  ? 160.408 110.457 109.545 1.00 85.08  ? 357  ASN A CB    1 
ATOM   2901  C CG    . ASN B 2 360  ? 160.815 111.847 109.975 1.00 89.55  ? 357  ASN A CG    1 
ATOM   2902  O OD1   . ASN B 2 360  ? 160.377 112.842 109.401 1.00 90.12  ? 357  ASN A OD1   1 
ATOM   2903  N ND2   . ASN B 2 360  ? 161.659 111.925 110.997 1.00 92.49  ? 357  ASN A ND2   1 
ATOM   2904  N N     . SER B 2 361  ? 158.840 107.660 110.637 1.00 81.07  ? 358  SER A N     1 
ATOM   2905  C CA    . SER B 2 361  ? 158.671 106.248 110.321 1.00 79.32  ? 358  SER A CA    1 
ATOM   2906  C C     . SER B 2 361  ? 157.711 105.502 111.237 1.00 78.85  ? 358  SER A C     1 
ATOM   2907  O O     . SER B 2 361  ? 157.171 104.475 110.812 1.00 76.86  ? 358  SER A O     1 
ATOM   2908  C CB    . SER B 2 361  ? 160.029 105.529 110.346 1.00 80.39  ? 358  SER A CB    1 
ATOM   2909  O OG    . SER B 2 361  ? 160.668 105.690 111.601 1.00 81.35  ? 358  SER A OG    1 
ATOM   2910  N N     . ILE B 2 362  ? 157.476 105.969 112.461 1.00 79.87  ? 359  ILE A N     1 
ATOM   2911  C CA    . ILE B 2 362  ? 156.619 105.246 113.394 1.00 79.86  ? 359  ILE A CA    1 
ATOM   2912  C C     . ILE B 2 362  ? 155.156 105.486 113.048 1.00 80.13  ? 359  ILE A C     1 
ATOM   2913  O O     . ILE B 2 362  ? 154.833 106.344 112.218 1.00 81.13  ? 359  ILE A O     1 
ATOM   2914  C CB    . ILE B 2 362  ? 156.910 105.646 114.852 1.00 74.89  ? 359  ILE A CB    1 
ATOM   2915  C CG1   . ILE B 2 362  ? 156.504 107.099 115.102 1.00 68.22  ? 359  ILE A CG1   1 
ATOM   2916  C CG2   . ILE B 2 362  ? 158.381 105.425 115.181 1.00 76.10  ? 359  ILE A CG2   1 
ATOM   2917  C CD1   . ILE B 2 362  ? 156.685 107.547 116.534 1.00 64.70  ? 359  ILE A CD1   1 
ATOM   2918  N N     . ASP B 2 363  ? 154.267 104.729 113.686 1.00 78.63  ? 360  ASP A N     1 
ATOM   2919  C CA    . ASP B 2 363  ? 152.832 104.839 113.441 1.00 75.85  ? 360  ASP A CA    1 
ATOM   2920  C C     . ASP B 2 363  ? 152.307 106.126 114.069 1.00 73.17  ? 360  ASP A C     1 
ATOM   2921  O O     . ASP B 2 363  ? 152.309 106.273 115.295 1.00 72.35  ? 360  ASP A O     1 
ATOM   2922  C CB    . ASP B 2 363  ? 152.116 103.617 114.009 1.00 78.71  ? 360  ASP A CB    1 
ATOM   2923  C CG    . ASP B 2 363  ? 150.620 103.651 113.765 1.00 80.24  ? 360  ASP A CG    1 
ATOM   2924  O OD1   . ASP B 2 363  ? 150.181 104.330 112.814 1.00 81.36  ? 360  ASP A OD1   1 
ATOM   2925  O OD2   . ASP B 2 363  ? 149.883 102.988 114.525 1.00 80.57  ? 360  ASP A OD2   1 
ATOM   2926  N N     . LEU B 2 364  ? 151.850 107.052 113.230 1.00 71.76  ? 361  LEU A N     1 
ATOM   2927  C CA    . LEU B 2 364  ? 151.400 108.361 113.687 1.00 69.00  ? 361  LEU A CA    1 
ATOM   2928  C C     . LEU B 2 364  ? 149.940 108.381 114.120 1.00 67.77  ? 361  LEU A C     1 
ATOM   2929  O O     . LEU B 2 364  ? 149.460 109.427 114.570 1.00 65.72  ? 361  LEU A O     1 
ATOM   2930  C CB    . LEU B 2 364  ? 151.623 109.407 112.590 1.00 65.30  ? 361  LEU A CB    1 
ATOM   2931  C CG    . LEU B 2 364  ? 153.085 109.703 112.250 1.00 64.67  ? 361  LEU A CG    1 
ATOM   2932  C CD1   . LEU B 2 364  ? 153.185 110.830 111.236 1.00 62.82  ? 361  LEU A CD1   1 
ATOM   2933  C CD2   . LEU B 2 364  ? 153.873 110.036 113.509 1.00 65.38  ? 361  LEU A CD2   1 
ATOM   2934  N N     . THR B 2 365  ? 149.222 107.262 114.002 1.00 67.42  ? 362  THR A N     1 
ATOM   2935  C CA    . THR B 2 365  ? 147.853 107.205 114.493 1.00 64.12  ? 362  THR A CA    1 
ATOM   2936  C C     . THR B 2 365  ? 147.778 107.101 116.010 1.00 64.41  ? 362  THR A C     1 
ATOM   2937  O O     . THR B 2 365  ? 146.676 107.154 116.565 1.00 65.92  ? 362  THR A O     1 
ATOM   2938  C CB    . THR B 2 365  ? 147.105 106.023 113.868 1.00 61.78  ? 362  THR A CB    1 
ATOM   2939  O OG1   . THR B 2 365  ? 147.625 104.793 114.393 1.00 63.34  ? 362  THR A OG1   1 
ATOM   2940  C CG2   . THR B 2 365  ? 147.268 106.028 112.359 1.00 60.52  ? 362  THR A CG2   1 
ATOM   2941  N N     . HIS B 2 366  ? 148.918 106.951 116.688 1.00 65.75  ? 363  HIS A N     1 
ATOM   2942  C CA    . HIS B 2 366  ? 148.961 106.888 118.144 1.00 67.74  ? 363  HIS A CA    1 
ATOM   2943  C C     . HIS B 2 366  ? 149.774 108.023 118.753 1.00 67.04  ? 363  HIS A C     1 
ATOM   2944  O O     . HIS B 2 366  ? 150.031 108.010 119.963 1.00 69.17  ? 363  HIS A O     1 
ATOM   2945  C CB    . HIS B 2 366  ? 149.514 105.534 118.600 1.00 71.85  ? 363  HIS A CB    1 
ATOM   2946  C CG    . HIS B 2 366  ? 148.602 104.381 118.305 1.00 75.11  ? 363  HIS A CG    1 
ATOM   2947  N ND1   . HIS B 2 366  ? 147.567 104.019 119.142 1.00 77.47  ? 363  HIS A ND1   1 
ATOM   2948  C CD2   . HIS B 2 366  ? 148.569 103.512 117.268 1.00 76.03  ? 363  HIS A CD2   1 
ATOM   2949  C CE1   . HIS B 2 366  ? 146.938 102.976 118.632 1.00 77.53  ? 363  HIS A CE1   1 
ATOM   2950  N NE2   . HIS B 2 366  ? 147.524 102.649 117.496 1.00 76.67  ? 363  HIS A NE2   1 
ATOM   2951  N N     . ILE B 2 367  ? 150.190 108.999 117.950 1.00 64.34  ? 364  ILE A N     1 
ATOM   2952  C CA    . ILE B 2 367  ? 150.817 110.221 118.440 1.00 62.36  ? 364  ILE A CA    1 
ATOM   2953  C C     . ILE B 2 367  ? 149.746 111.302 118.421 1.00 57.80  ? 364  ILE A C     1 
ATOM   2954  O O     . ILE B 2 367  ? 149.295 111.724 117.351 1.00 58.18  ? 364  ILE A O     1 
ATOM   2955  C CB    . ILE B 2 367  ? 152.032 110.617 117.592 1.00 61.75  ? 364  ILE A CB    1 
ATOM   2956  C CG1   . ILE B 2 367  ? 153.053 109.481 117.558 1.00 63.65  ? 364  ILE A CG1   1 
ATOM   2957  C CG2   . ILE B 2 367  ? 152.671 111.882 118.139 1.00 58.79  ? 364  ILE A CG2   1 
ATOM   2958  C CD1   . ILE B 2 367  ? 153.599 109.116 118.920 1.00 64.31  ? 364  ILE A CD1   1 
ATOM   2959  N N     . PHE B 2 368  ? 149.330 111.754 119.600 1.00 54.96  ? 365  PHE A N     1 
ATOM   2960  C CA    . PHE B 2 368  ? 148.172 112.622 119.738 1.00 52.26  ? 365  PHE A CA    1 
ATOM   2961  C C     . PHE B 2 368  ? 148.589 114.055 120.040 1.00 52.41  ? 365  PHE A C     1 
ATOM   2962  O O     . PHE B 2 368  ? 149.529 114.297 120.805 1.00 51.82  ? 365  PHE A O     1 
ATOM   2963  C CB    . PHE B 2 368  ? 147.239 112.113 120.839 1.00 52.55  ? 365  PHE A CB    1 
ATOM   2964  C CG    . PHE B 2 368  ? 146.590 110.801 120.514 1.00 56.23  ? 365  PHE A CG    1 
ATOM   2965  C CD1   . PHE B 2 368  ? 147.206 109.605 120.848 1.00 57.64  ? 365  PHE A CD1   1 
ATOM   2966  C CD2   . PHE B 2 368  ? 145.369 110.761 119.862 1.00 56.80  ? 365  PHE A CD2   1 
ATOM   2967  C CE1   . PHE B 2 368  ? 146.613 108.397 120.544 1.00 59.25  ? 365  PHE A CE1   1 
ATOM   2968  C CE2   . PHE B 2 368  ? 144.769 109.556 119.557 1.00 58.05  ? 365  PHE A CE2   1 
ATOM   2969  C CZ    . PHE B 2 368  ? 145.392 108.371 119.899 1.00 60.16  ? 365  PHE A CZ    1 
ATOM   2970  N N     . ILE B 2 369  ? 147.875 115.000 119.431 1.00 52.31  ? 366  ILE A N     1 
ATOM   2971  C CA    . ILE B 2 369  ? 148.055 116.427 119.672 1.00 52.49  ? 366  ILE A CA    1 
ATOM   2972  C C     . ILE B 2 369  ? 146.950 116.902 120.604 1.00 53.71  ? 366  ILE A C     1 
ATOM   2973  O O     . ILE B 2 369  ? 145.780 116.539 120.434 1.00 54.44  ? 366  ILE A O     1 
ATOM   2974  C CB    . ILE B 2 369  ? 148.043 117.217 118.348 1.00 51.28  ? 366  ILE A CB    1 
ATOM   2975  C CG1   . ILE B 2 369  ? 149.206 116.782 117.456 1.00 50.67  ? 366  ILE A CG1   1 
ATOM   2976  C CG2   . ILE B 2 369  ? 148.102 118.709 118.614 1.00 50.77  ? 366  ILE A CG2   1 
ATOM   2977  C CD1   . ILE B 2 369  ? 150.566 116.993 118.082 1.00 49.77  ? 366  ILE A CD1   1 
ATOM   2978  N N     . SER B 2 370  ? 147.319 117.711 121.591 1.00 54.71  ? 367  SER A N     1 
ATOM   2979  C CA    . SER B 2 370  ? 146.344 118.209 122.552 1.00 54.34  ? 367  SER A CA    1 
ATOM   2980  C C     . SER B 2 370  ? 145.410 119.222 121.900 1.00 55.91  ? 367  SER A C     1 
ATOM   2981  O O     . SER B 2 370  ? 145.839 120.066 121.109 1.00 55.68  ? 367  SER A O     1 
ATOM   2982  C CB    . SER B 2 370  ? 147.054 118.844 123.746 1.00 54.51  ? 367  SER A CB    1 
ATOM   2983  O OG    . SER B 2 370  ? 146.117 119.379 124.664 1.00 55.35  ? 367  SER A OG    1 
ATOM   2984  N N     . HIS B 2 371  ? 144.121 119.134 122.243 1.00 57.17  ? 368  HIS A N     1 
ATOM   2985  C CA    . HIS B 2 371  ? 143.148 120.076 121.699 1.00 56.25  ? 368  HIS A CA    1 
ATOM   2986  C C     . HIS B 2 371  ? 143.383 121.488 122.218 1.00 55.12  ? 368  HIS A C     1 
ATOM   2987  O O     . HIS B 2 371  ? 143.042 122.462 121.540 1.00 54.89  ? 368  HIS A O     1 
ATOM   2988  C CB    . HIS B 2 371  ? 141.725 119.619 122.027 1.00 59.84  ? 368  HIS A CB    1 
ATOM   2989  C CG    . HIS B 2 371  ? 141.435 119.538 123.494 1.00 65.77  ? 368  HIS A CG    1 
ATOM   2990  N ND1   . HIS B 2 371  ? 141.453 118.352 124.194 1.00 69.98  ? 368  HIS A ND1   1 
ATOM   2991  C CD2   . HIS B 2 371  ? 141.113 120.499 124.393 1.00 66.18  ? 368  HIS A CD2   1 
ATOM   2992  C CE1   . HIS B 2 371  ? 141.159 118.584 125.458 1.00 68.93  ? 368  HIS A CE1   1 
ATOM   2993  N NE2   . HIS B 2 371  ? 140.947 119.878 125.608 1.00 67.13  ? 368  HIS A NE2   1 
ATOM   2994  N N     . LYS B 2 372  ? 143.964 121.616 123.414 1.00 56.01  ? 369  LYS A N     1 
ATOM   2995  C CA    . LYS B 2 372  ? 144.289 122.927 123.964 1.00 57.47  ? 369  LYS A CA    1 
ATOM   2996  C C     . LYS B 2 372  ? 145.402 123.626 123.195 1.00 58.23  ? 369  LYS A C     1 
ATOM   2997  O O     . LYS B 2 372  ? 145.604 124.829 123.393 1.00 59.14  ? 369  LYS A O     1 
ATOM   2998  C CB    . LYS B 2 372  ? 144.690 122.790 125.435 1.00 58.16  ? 369  LYS A CB    1 
ATOM   2999  C CG    . LYS B 2 372  ? 143.620 122.167 126.316 1.00 58.45  ? 369  LYS A CG    1 
ATOM   3000  C CD    . LYS B 2 372  ? 144.131 121.956 127.734 1.00 59.54  ? 369  LYS A CD    1 
ATOM   3001  C CE    . LYS B 2 372  ? 143.061 121.344 128.622 1.00 58.62  ? 369  LYS A CE    1 
ATOM   3002  N NZ    . LYS B 2 372  ? 143.575 121.065 129.992 1.00 60.64  ? 369  LYS A NZ    1 
ATOM   3003  N N     . LYS B 2 373  ? 146.122 122.911 122.330 1.00 57.16  ? 370  LYS A N     1 
ATOM   3004  C CA    . LYS B 2 373  ? 147.218 123.478 121.561 1.00 53.66  ? 370  LYS A CA    1 
ATOM   3005  C C     . LYS B 2 373  ? 146.979 123.443 120.059 1.00 50.19  ? 370  LYS A C     1 
ATOM   3006  O O     . LYS B 2 373  ? 147.807 123.968 119.306 1.00 51.70  ? 370  LYS A O     1 
ATOM   3007  C CB    . LYS B 2 373  ? 148.528 122.740 121.877 1.00 53.51  ? 370  LYS A CB    1 
ATOM   3008  C CG    . LYS B 2 373  ? 148.819 122.572 123.361 1.00 55.98  ? 370  LYS A CG    1 
ATOM   3009  C CD    . LYS B 2 373  ? 149.078 123.908 124.039 1.00 59.11  ? 370  LYS A CD    1 
ATOM   3010  C CE    . LYS B 2 373  ? 149.411 123.718 125.512 1.00 62.87  ? 370  LYS A CE    1 
ATOM   3011  N NZ    . LYS B 2 373  ? 149.676 125.014 126.200 1.00 65.60  ? 370  LYS A NZ    1 
ATOM   3012  N N     . LEU B 2 374  ? 145.876 122.845 119.598 1.00 46.07  ? 371  LEU A N     1 
ATOM   3013  C CA    . LEU B 2 374  ? 145.673 122.671 118.162 1.00 46.14  ? 371  LEU A CA    1 
ATOM   3014  C C     . LEU B 2 374  ? 145.567 124.012 117.445 1.00 42.45  ? 371  LEU A C     1 
ATOM   3015  O O     . LEU B 2 374  ? 146.114 124.182 116.349 1.00 41.17  ? 371  LEU A O     1 
ATOM   3016  C CB    . LEU B 2 374  ? 144.424 121.829 117.903 1.00 46.66  ? 371  LEU A CB    1 
ATOM   3017  C CG    . LEU B 2 374  ? 144.090 121.581 116.431 1.00 43.67  ? 371  LEU A CG    1 
ATOM   3018  C CD1   . LEU B 2 374  ? 145.222 120.836 115.741 1.00 43.80  ? 371  LEU A CD1   1 
ATOM   3019  C CD2   . LEU B 2 374  ? 142.782 120.819 116.292 1.00 42.51  ? 371  LEU A CD2   1 
ATOM   3020  N N     . GLU B 2 375  ? 144.867 124.977 118.043 1.00 41.71  ? 372  GLU A N     1 
ATOM   3021  C CA    . GLU B 2 375  ? 144.732 126.283 117.405 1.00 45.20  ? 372  GLU A CA    1 
ATOM   3022  C C     . GLU B 2 375  ? 146.056 127.035 117.404 1.00 47.19  ? 372  GLU A C     1 
ATOM   3023  O O     . GLU B 2 375  ? 146.365 127.758 116.448 1.00 48.35  ? 372  GLU A O     1 
ATOM   3024  C CB    . GLU B 2 375  ? 143.642 127.100 118.098 1.00 47.18  ? 372  GLU A CB    1 
ATOM   3025  C CG    . GLU B 2 375  ? 142.241 126.824 117.572 1.00 50.70  ? 372  GLU A CG    1 
ATOM   3026  C CD    . GLU B 2 375  ? 141.818 125.380 117.751 1.00 55.36  ? 372  GLU A CD    1 
ATOM   3027  O OE1   . GLU B 2 375  ? 141.954 124.855 118.877 1.00 59.66  ? 372  GLU A OE1   1 
ATOM   3028  O OE2   . GLU B 2 375  ? 141.358 124.765 116.766 1.00 54.43  ? 372  GLU A OE2   1 
ATOM   3029  N N     . THR B 2 376  ? 146.853 126.880 118.463 1.00 48.75  ? 373  THR A N     1 
ATOM   3030  C CA    . THR B 2 376  ? 148.168 127.513 118.492 1.00 51.15  ? 373  THR A CA    1 
ATOM   3031  C C     . THR B 2 376  ? 149.083 126.921 117.426 1.00 52.59  ? 373  THR A C     1 
ATOM   3032  O O     . THR B 2 376  ? 149.823 127.653 116.759 1.00 53.75  ? 373  THR A O     1 
ATOM   3033  C CB    . THR B 2 376  ? 148.790 127.367 119.880 1.00 53.69  ? 373  THR A CB    1 
ATOM   3034  O OG1   . THR B 2 376  ? 147.908 127.923 120.863 1.00 55.64  ? 373  THR A OG1   1 
ATOM   3035  C CG2   . THR B 2 376  ? 150.128 128.089 119.947 1.00 53.21  ? 373  THR A CG2   1 
ATOM   3036  N N     . ILE B 2 377  ? 149.037 125.600 117.246 1.00 53.59  ? 374  ILE A N     1 
ATOM   3037  C CA    . ILE B 2 377  ? 149.851 124.954 116.221 1.00 53.18  ? 374  ILE A CA    1 
ATOM   3038  C C     . ILE B 2 377  ? 149.405 125.386 114.831 1.00 54.37  ? 374  ILE A C     1 
ATOM   3039  O O     . ILE B 2 377  ? 150.232 125.596 113.935 1.00 55.41  ? 374  ILE A O     1 
ATOM   3040  C CB    . ILE B 2 377  ? 149.795 123.425 116.385 1.00 49.88  ? 374  ILE A CB    1 
ATOM   3041  C CG1   . ILE B 2 377  ? 150.377 123.016 117.737 1.00 49.44  ? 374  ILE A CG1   1 
ATOM   3042  C CG2   . ILE B 2 377  ? 150.537 122.731 115.253 1.00 49.72  ? 374  ILE A CG2   1 
ATOM   3043  C CD1   . ILE B 2 377  ? 150.209 121.550 118.042 1.00 50.33  ? 374  ILE A CD1   1 
ATOM   3044  N N     . SER B 2 378  ? 148.092 125.525 114.628 1.00 54.70  ? 375  SER A N     1 
ATOM   3045  C CA    . SER B 2 378  ? 147.584 125.953 113.329 1.00 53.71  ? 375  SER A CA    1 
ATOM   3046  C C     . SER B 2 378  ? 148.103 127.339 112.966 1.00 53.81  ? 375  SER A C     1 
ATOM   3047  O O     . SER B 2 378  ? 148.466 127.590 111.810 1.00 55.04  ? 375  SER A O     1 
ATOM   3048  C CB    . SER B 2 378  ? 146.058 125.939 113.333 1.00 52.66  ? 375  SER A CB    1 
ATOM   3049  O OG    . SER B 2 378  ? 145.543 126.139 112.028 1.00 52.00  ? 375  SER A OG    1 
ATOM   3050  N N     . SER B 2 379  ? 148.153 128.248 113.940 1.00 55.60  ? 376  SER A N     1 
ATOM   3051  C CA    . SER B 2 379  ? 148.631 129.597 113.673 1.00 56.79  ? 376  SER A CA    1 
ATOM   3052  C C     . SER B 2 379  ? 150.140 129.651 113.475 1.00 56.92  ? 376  SER A C     1 
ATOM   3053  O O     . SER B 2 379  ? 150.631 130.571 112.812 1.00 58.36  ? 376  SER A O     1 
ATOM   3054  C CB    . SER B 2 379  ? 148.218 130.534 114.811 1.00 58.68  ? 376  SER A CB    1 
ATOM   3055  O OG    . SER B 2 379  ? 148.540 131.880 114.510 1.00 62.48  ? 376  SER A OG    1 
ATOM   3056  N N     . ALA B 2 380  ? 150.881 128.690 114.023 1.00 57.39  ? 377  ALA A N     1 
ATOM   3057  C CA    . ALA B 2 380  ? 152.332 128.683 113.904 1.00 61.15  ? 377  ALA A CA    1 
ATOM   3058  C C     . ALA B 2 380  ? 152.830 127.960 112.661 1.00 62.37  ? 377  ALA A C     1 
ATOM   3059  O O     . ALA B 2 380  ? 153.953 128.225 112.217 1.00 65.68  ? 377  ALA A O     1 
ATOM   3060  C CB    . ALA B 2 380  ? 152.962 128.039 115.145 1.00 61.93  ? 377  ALA A CB    1 
ATOM   3061  N N     . LEU B 2 381  ? 152.028 127.061 112.090 1.00 60.26  ? 378  LEU A N     1 
ATOM   3062  C CA    . LEU B 2 381  ? 152.441 126.284 110.934 1.00 59.72  ? 378  LEU A CA    1 
ATOM   3063  C C     . LEU B 2 381  ? 151.630 126.567 109.679 1.00 63.33  ? 378  LEU A C     1 
ATOM   3064  O O     . LEU B 2 381  ? 152.057 126.170 108.591 1.00 64.33  ? 378  LEU A O     1 
ATOM   3065  C CB    . LEU B 2 381  ? 152.361 124.782 111.241 1.00 59.49  ? 378  LEU A CB    1 
ATOM   3066  C CG    . LEU B 2 381  ? 153.112 124.299 112.480 1.00 62.36  ? 378  LEU A CG    1 
ATOM   3067  C CD1   . LEU B 2 381  ? 153.084 122.783 112.567 1.00 62.95  ? 378  LEU A CD1   1 
ATOM   3068  C CD2   . LEU B 2 381  ? 154.538 124.812 112.468 1.00 65.54  ? 378  LEU A CD2   1 
ATOM   3069  N N     . CYS B 2 382  ? 150.480 127.229 109.793 1.00 67.35  ? 379  CYS A N     1 
ATOM   3070  C CA    . CYS B 2 382  ? 149.623 127.437 108.633 1.00 71.16  ? 379  CYS A CA    1 
ATOM   3071  C C     . CYS B 2 382  ? 149.243 128.904 108.472 1.00 73.73  ? 379  CYS A C     1 
ATOM   3072  O O     . CYS B 2 382  ? 149.790 129.776 109.156 1.00 72.71  ? 379  CYS A O     1 
ATOM   3073  C CB    . CYS B 2 382  ? 148.364 126.577 108.746 1.00 69.33  ? 379  CYS A CB    1 
ATOM   3074  S SG    . CYS B 2 382  ? 148.677 124.834 109.098 1.00 67.69  ? 379  CYS A SG    1 
ATOM   3075  N N     . ASP B 2 383  ? 148.302 129.179 107.566 1.00 80.10  ? 380  ASP A N     1 
ATOM   3076  C CA    . ASP B 2 383  ? 147.895 130.553 107.304 1.00 85.60  ? 380  ASP A CA    1 
ATOM   3077  C C     . ASP B 2 383  ? 147.247 131.178 108.533 1.00 85.11  ? 380  ASP A C     1 
ATOM   3078  O O     . ASP B 2 383  ? 147.637 132.266 108.971 1.00 85.73  ? 380  ASP A O     1 
ATOM   3079  C CB    . ASP B 2 383  ? 146.942 130.599 106.108 1.00 89.96  ? 380  ASP A CB    1 
ATOM   3080  C CG    . ASP B 2 383  ? 147.543 129.986 104.856 1.00 94.25  ? 380  ASP A CG    1 
ATOM   3081  O OD1   . ASP B 2 383  ? 147.414 128.757 104.672 1.00 96.19  ? 380  ASP A OD1   1 
ATOM   3082  O OD2   . ASP B 2 383  ? 148.138 130.735 104.053 1.00 95.77  ? 380  ASP A OD2   1 
ATOM   3083  N N     . HIS B 2 384  ? 146.251 130.503 109.105 1.00 80.78  ? 381  HIS A N     1 
ATOM   3084  C CA    . HIS B 2 384  ? 145.515 131.028 110.242 1.00 78.81  ? 381  HIS A CA    1 
ATOM   3085  C C     . HIS B 2 384  ? 145.326 129.930 111.278 1.00 74.26  ? 381  HIS A C     1 
ATOM   3086  O O     . HIS B 2 384  ? 145.660 128.763 111.058 1.00 73.43  ? 381  HIS A O     1 
ATOM   3087  C CB    . HIS B 2 384  ? 144.149 131.589 109.824 1.00 79.52  ? 381  HIS A CB    1 
ATOM   3088  C CG    . HIS B 2 384  ? 144.139 132.198 108.457 1.00 82.73  ? 381  HIS A CG    1 
ATOM   3089  N ND1   . HIS B 2 384  ? 143.555 131.579 107.373 1.00 83.94  ? 381  HIS A ND1   1 
ATOM   3090  C CD2   . HIS B 2 384  ? 144.646 133.366 107.996 1.00 84.55  ? 381  HIS A CD2   1 
ATOM   3091  C CE1   . HIS B 2 384  ? 143.699 132.341 106.303 1.00 84.94  ? 381  HIS A CE1   1 
ATOM   3092  N NE2   . HIS B 2 384  ? 144.358 133.431 106.653 1.00 85.18  ? 381  HIS A NE2   1 
ATOM   3093  N N     . TRP B 2 385  ? 144.772 130.328 112.425 1.00 69.68  ? 382  TRP A N     1 
ATOM   3094  C CA    . TRP B 2 385  ? 144.367 129.368 113.445 1.00 66.96  ? 382  TRP A CA    1 
ATOM   3095  C C     . TRP B 2 385  ? 143.221 128.485 112.972 1.00 69.37  ? 382  TRP A C     1 
ATOM   3096  O O     . TRP B 2 385  ? 142.993 127.417 113.550 1.00 71.19  ? 382  TRP A O     1 
ATOM   3097  C CB    . TRP B 2 385  ? 143.947 130.113 114.709 1.00 61.32  ? 382  TRP A CB    1 
ATOM   3098  C CG    . TRP B 2 385  ? 142.724 130.938 114.481 1.00 55.72  ? 382  TRP A CG    1 
ATOM   3099  C CD1   . TRP B 2 385  ? 142.665 132.184 113.928 1.00 53.57  ? 382  TRP A CD1   1 
ATOM   3100  C CD2   . TRP B 2 385  ? 141.373 130.565 114.773 1.00 54.55  ? 382  TRP A CD2   1 
ATOM   3101  N NE1   . TRP B 2 385  ? 141.362 132.614 113.868 1.00 53.29  ? 382  TRP A NE1   1 
ATOM   3102  C CE2   . TRP B 2 385  ? 140.549 131.637 114.381 1.00 53.40  ? 382  TRP A CE2   1 
ATOM   3103  C CE3   . TRP B 2 385  ? 140.781 129.428 115.334 1.00 54.39  ? 382  TRP A CE3   1 
ATOM   3104  C CZ2   . TRP B 2 385  ? 139.165 131.608 114.533 1.00 53.68  ? 382  TRP A CZ2   1 
ATOM   3105  C CZ3   . TRP B 2 385  ? 139.407 129.401 115.484 1.00 52.80  ? 382  TRP A CZ3   1 
ATOM   3106  C CH2   . TRP B 2 385  ? 138.614 130.484 115.085 1.00 53.54  ? 382  TRP A CH2   1 
ATOM   3107  N N     . ASP B 2 386  ? 142.496 128.913 111.937 1.00 71.11  ? 383  ASP A N     1 
ATOM   3108  C CA    . ASP B 2 386  ? 141.310 128.202 111.475 1.00 67.80  ? 383  ASP A CA    1 
ATOM   3109  C C     . ASP B 2 386  ? 141.644 126.949 110.681 1.00 65.87  ? 383  ASP A C     1 
ATOM   3110  O O     . ASP B 2 386  ? 140.899 125.965 110.750 1.00 65.70  ? 383  ASP A O     1 
ATOM   3111  C CB    . ASP B 2 386  ? 140.456 129.128 110.609 1.00 70.79  ? 383  ASP A CB    1 
ATOM   3112  C CG    . ASP B 2 386  ? 139.245 129.653 111.336 1.00 77.68  ? 383  ASP A CG    1 
ATOM   3113  O OD1   . ASP B 2 386  ? 138.742 128.946 112.235 1.00 81.17  ? 383  ASP A OD1   1 
ATOM   3114  O OD2   . ASP B 2 386  ? 138.793 130.771 111.008 1.00 81.25  ? 383  ASP A OD2   1 
ATOM   3115  N N     . THR B 2 387  ? 142.752 126.963 109.936 1.00 62.87  ? 384  THR A N     1 
ATOM   3116  C CA    . THR B 2 387  ? 142.944 126.000 108.856 1.00 61.57  ? 384  THR A CA    1 
ATOM   3117  C C     . THR B 2 387  ? 142.933 124.561 109.357 1.00 59.61  ? 384  THR A C     1 
ATOM   3118  O O     . THR B 2 387  ? 142.344 123.682 108.716 1.00 59.56  ? 384  THR A O     1 
ATOM   3119  C CB    . THR B 2 387  ? 144.246 126.298 108.116 1.00 63.09  ? 384  THR A CB    1 
ATOM   3120  O OG1   . THR B 2 387  ? 145.304 126.457 109.069 1.00 66.51  ? 384  THR A OG1   1 
ATOM   3121  C CG2   . THR B 2 387  ? 144.112 127.572 107.295 1.00 61.17  ? 384  THR A CG2   1 
ATOM   3122  N N     . LEU B 2 388  ? 143.571 124.296 110.499 1.00 56.51  ? 385  LEU A N     1 
ATOM   3123  C CA    . LEU B 2 388  ? 143.642 122.920 110.988 1.00 53.86  ? 385  LEU A CA    1 
ATOM   3124  C C     . LEU B 2 388  ? 142.279 122.421 111.446 1.00 52.80  ? 385  LEU A C     1 
ATOM   3125  O O     . LEU B 2 388  ? 141.829 121.351 111.021 1.00 53.82  ? 385  LEU A O     1 
ATOM   3126  C CB    . LEU B 2 388  ? 144.663 122.809 112.120 1.00 53.86  ? 385  LEU A CB    1 
ATOM   3127  C CG    . LEU B 2 388  ? 146.119 122.800 111.657 1.00 55.35  ? 385  LEU A CG    1 
ATOM   3128  C CD1   . LEU B 2 388  ? 147.005 122.122 112.690 1.00 53.69  ? 385  LEU A CD1   1 
ATOM   3129  C CD2   . LEU B 2 388  ? 146.236 122.126 110.302 1.00 57.18  ? 385  LEU A CD2   1 
ATOM   3130  N N     . ARG B 2 389  ? 141.611 123.177 112.320 1.00 51.99  ? 386  ARG A N     1 
ATOM   3131  C CA    . ARG B 2 389  ? 140.291 122.769 112.788 1.00 52.98  ? 386  ARG A CA    1 
ATOM   3132  C C     . ARG B 2 389  ? 139.315 122.627 111.628 1.00 55.75  ? 386  ARG A C     1 
ATOM   3133  O O     . ARG B 2 389  ? 138.456 121.738 111.631 1.00 58.06  ? 386  ARG A O     1 
ATOM   3134  C CB    . ARG B 2 389  ? 139.766 123.775 113.811 1.00 55.21  ? 386  ARG A CB    1 
ATOM   3135  C CG    . ARG B 2 389  ? 138.426 123.401 114.420 1.00 57.31  ? 386  ARG A CG    1 
ATOM   3136  C CD    . ARG B 2 389  ? 137.721 124.626 114.974 1.00 59.90  ? 386  ARG A CD    1 
ATOM   3137  N NE    . ARG B 2 389  ? 137.418 125.591 113.922 1.00 62.20  ? 386  ARG A NE    1 
ATOM   3138  C CZ    . ARG B 2 389  ? 136.757 126.726 114.118 1.00 63.82  ? 386  ARG A CZ    1 
ATOM   3139  N NH1   . ARG B 2 389  ? 136.326 127.046 115.332 1.00 64.52  ? 386  ARG A NH1   1 
ATOM   3140  N NH2   . ARG B 2 389  ? 136.524 127.545 113.101 1.00 63.16  ? 386  ARG A NH2   1 
ATOM   3141  N N     . ASN B 2 390  ? 139.441 123.491 110.617 1.00 56.16  ? 387  ASN A N     1 
ATOM   3142  C CA    . ASN B 2 390  ? 138.555 123.414 109.460 1.00 56.50  ? 387  ASN A CA    1 
ATOM   3143  C C     . ASN B 2 390  ? 138.886 122.210 108.586 1.00 57.90  ? 387  ASN A C     1 
ATOM   3144  O O     . ASN B 2 390  ? 137.981 121.530 108.089 1.00 58.95  ? 387  ASN A O     1 
ATOM   3145  C CB    . ASN B 2 390  ? 138.639 124.709 108.652 1.00 58.12  ? 387  ASN A CB    1 
ATOM   3146  C CG    . ASN B 2 390  ? 137.995 125.884 109.365 1.00 59.62  ? 387  ASN A CG    1 
ATOM   3147  O OD1   . ASN B 2 390  ? 136.969 126.402 108.926 1.00 60.93  ? 387  ASN A OD1   1 
ATOM   3148  N ND2   . ASN B 2 390  ? 138.592 126.304 110.473 1.00 60.40  ? 387  ASN A ND2   1 
ATOM   3149  N N     . ALA B 2 391  ? 140.178 121.930 108.387 1.00 57.69  ? 388  ALA A N     1 
ATOM   3150  C CA    . ALA B 2 391  ? 140.568 120.786 107.567 1.00 54.96  ? 388  ALA A CA    1 
ATOM   3151  C C     . ALA B 2 391  ? 140.120 119.475 108.198 1.00 56.87  ? 388  ALA A C     1 
ATOM   3152  O O     . ALA B 2 391  ? 139.654 118.569 107.498 1.00 58.11  ? 388  ALA A O     1 
ATOM   3153  C CB    . ALA B 2 391  ? 142.081 120.787 107.345 1.00 51.53  ? 388  ALA A CB    1 
ATOM   3154  N N     . LEU B 2 392  ? 140.258 119.355 109.520 1.00 55.66  ? 389  LEU A N     1 
ATOM   3155  C CA    . LEU B 2 392  ? 139.753 118.171 110.208 1.00 53.61  ? 389  LEU A CA    1 
ATOM   3156  C C     . LEU B 2 392  ? 138.238 118.086 110.111 1.00 53.06  ? 389  LEU A C     1 
ATOM   3157  O O     . LEU B 2 392  ? 137.672 116.990 110.014 1.00 52.01  ? 389  LEU A O     1 
ATOM   3158  C CB    . LEU B 2 392  ? 140.195 118.182 111.672 1.00 51.97  ? 389  LEU A CB    1 
ATOM   3159  C CG    . LEU B 2 392  ? 141.697 118.109 111.946 1.00 52.74  ? 389  LEU A CG    1 
ATOM   3160  C CD1   . LEU B 2 392  ? 141.965 118.222 113.437 1.00 55.03  ? 389  LEU A CD1   1 
ATOM   3161  C CD2   . LEU B 2 392  ? 142.280 116.821 111.389 1.00 52.55  ? 389  LEU A CD2   1 
ATOM   3162  N N     . TYR B 2 393  ? 137.562 119.238 110.133 1.00 53.69  ? 390  TYR A N     1 
ATOM   3163  C CA    . TYR B 2 393  ? 136.107 119.251 110.023 1.00 51.99  ? 390  TYR A CA    1 
ATOM   3164  C C     . TYR B 2 393  ? 135.654 118.709 108.674 1.00 52.12  ? 390  TYR A C     1 
ATOM   3165  O O     . TYR B 2 393  ? 134.735 117.888 108.598 1.00 53.37  ? 390  TYR A O     1 
ATOM   3166  C CB    . TYR B 2 393  ? 135.578 120.669 110.237 1.00 48.18  ? 390  TYR A CB    1 
ATOM   3167  C CG    . TYR B 2 393  ? 134.106 120.823 109.923 1.00 48.90  ? 390  TYR A CG    1 
ATOM   3168  C CD1   . TYR B 2 393  ? 133.138 120.449 110.844 1.00 49.62  ? 390  TYR A CD1   1 
ATOM   3169  C CD2   . TYR B 2 393  ? 133.686 121.345 108.705 1.00 48.46  ? 390  TYR A CD2   1 
ATOM   3170  C CE1   . TYR B 2 393  ? 131.792 120.585 110.561 1.00 49.58  ? 390  TYR A CE1   1 
ATOM   3171  C CE2   . TYR B 2 393  ? 132.342 121.484 108.413 1.00 47.26  ? 390  TYR A CE2   1 
ATOM   3172  C CZ    . TYR B 2 393  ? 131.399 121.103 109.346 1.00 47.49  ? 390  TYR A CZ    1 
ATOM   3173  O OH    . TYR B 2 393  ? 130.059 121.241 109.066 1.00 46.61  ? 390  TYR A OH    1 
ATOM   3174  N N     . GLU B 2 394  ? 136.298 119.156 107.594 1.00 52.24  ? 391  GLU A N     1 
ATOM   3175  C CA    . GLU B 2 394  ? 135.881 118.730 106.263 1.00 53.91  ? 391  GLU A CA    1 
ATOM   3176  C C     . GLU B 2 394  ? 136.137 117.245 106.047 1.00 54.96  ? 391  GLU A C     1 
ATOM   3177  O O     . GLU B 2 394  ? 135.320 116.555 105.426 1.00 57.69  ? 391  GLU A O     1 
ATOM   3178  C CB    . GLU B 2 394  ? 136.593 119.565 105.198 1.00 55.46  ? 391  GLU A CB    1 
ATOM   3179  C CG    . GLU B 2 394  ? 136.245 121.046 105.241 1.00 57.86  ? 391  GLU A CG    1 
ATOM   3180  C CD    . GLU B 2 394  ? 134.779 121.314 104.945 1.00 60.24  ? 391  GLU A CD    1 
ATOM   3181  O OE1   . GLU B 2 394  ? 134.160 120.518 104.208 1.00 59.38  ? 391  GLU A OE1   1 
ATOM   3182  O OE2   . GLU B 2 394  ? 134.245 122.324 105.453 1.00 62.65  ? 391  GLU A OE2   1 
ATOM   3183  N N     . ARG B 2 395  ? 137.257 116.728 106.556 1.00 54.30  ? 392  ARG A N     1 
ATOM   3184  C CA    . ARG B 2 395  ? 137.558 115.314 106.353 1.00 53.47  ? 392  ARG A CA    1 
ATOM   3185  C C     . ARG B 2 395  ? 136.647 114.421 107.184 1.00 53.15  ? 392  ARG A C     1 
ATOM   3186  O O     . ARG B 2 395  ? 136.340 113.297 106.768 1.00 54.84  ? 392  ARG A O     1 
ATOM   3187  C CB    . ARG B 2 395  ? 139.021 115.022 106.682 1.00 55.02  ? 392  ARG A CB    1 
ATOM   3188  C CG    . ARG B 2 395  ? 139.525 113.721 106.080 1.00 57.39  ? 392  ARG A CG    1 
ATOM   3189  C CD    . ARG B 2 395  ? 140.960 113.439 106.479 1.00 61.93  ? 392  ARG A CD    1 
ATOM   3190  N NE    . ARG B 2 395  ? 141.046 112.471 107.568 1.00 66.40  ? 392  ARG A NE    1 
ATOM   3191  C CZ    . ARG B 2 395  ? 141.260 111.172 107.393 1.00 69.75  ? 392  ARG A CZ    1 
ATOM   3192  N NH1   . ARG B 2 395  ? 141.417 110.683 106.170 1.00 69.57  ? 392  ARG A NH1   1 
ATOM   3193  N NH2   . ARG B 2 395  ? 141.323 110.360 108.441 1.00 70.91  ? 392  ARG A NH2   1 
ATOM   3194  N N     . ARG B 2 396  ? 136.206 114.894 108.352 1.00 52.22  ? 393  ARG A N     1 
ATOM   3195  C CA    . ARG B 2 396  ? 135.298 114.097 109.167 1.00 54.26  ? 393  ARG A CA    1 
ATOM   3196  C C     . ARG B 2 396  ? 133.882 114.115 108.604 1.00 55.70  ? 393  ARG A C     1 
ATOM   3197  O O     . ARG B 2 396  ? 133.186 113.094 108.635 1.00 57.36  ? 393  ARG A O     1 
ATOM   3198  C CB    . ARG B 2 396  ? 135.315 114.592 110.615 1.00 54.41  ? 393  ARG A CB    1 
ATOM   3199  C CG    . ARG B 2 396  ? 136.604 114.251 111.351 1.00 56.79  ? 393  ARG A CG    1 
ATOM   3200  C CD    . ARG B 2 396  ? 136.491 114.503 112.846 1.00 60.52  ? 393  ARG A CD    1 
ATOM   3201  N NE    . ARG B 2 396  ? 137.661 113.999 113.563 1.00 64.57  ? 393  ARG A NE    1 
ATOM   3202  C CZ    . ARG B 2 396  ? 137.787 114.003 114.887 1.00 65.42  ? 393  ARG A CZ    1 
ATOM   3203  N NH1   . ARG B 2 396  ? 136.814 114.483 115.649 1.00 65.57  ? 393  ARG A NH1   1 
ATOM   3204  N NH2   . ARG B 2 396  ? 138.888 113.522 115.450 1.00 64.56  ? 393  ARG A NH2   1 
ATOM   3205  N N     . ILE B 2 397  ? 133.438 115.263 108.085 1.00 54.07  ? 394  ILE A N     1 
ATOM   3206  C CA    . ILE B 2 397  ? 132.177 115.300 107.350 1.00 53.38  ? 394  ILE A CA    1 
ATOM   3207  C C     . ILE B 2 397  ? 132.265 114.417 106.114 1.00 53.15  ? 394  ILE A C     1 
ATOM   3208  O O     . ILE B 2 397  ? 131.265 113.827 105.683 1.00 52.69  ? 394  ILE A O     1 
ATOM   3209  C CB    . ILE B 2 397  ? 131.812 116.756 106.989 1.00 53.94  ? 394  ILE A CB    1 
ATOM   3210  C CG1   . ILE B 2 397  ? 131.636 117.590 108.256 1.00 54.47  ? 394  ILE A CG1   1 
ATOM   3211  C CG2   . ILE B 2 397  ? 130.539 116.810 106.161 1.00 55.30  ? 394  ILE A CG2   1 
ATOM   3212  C CD1   . ILE B 2 397  ? 130.541 117.092 109.161 1.00 56.02  ? 394  ILE A CD1   1 
ATOM   3213  N N     . SER B 2 398  ? 133.464 114.287 105.541 1.00 52.75  ? 395  SER A N     1 
ATOM   3214  C CA    . SER B 2 398  ? 133.671 113.446 104.369 1.00 52.50  ? 395  SER A CA    1 
ATOM   3215  C C     . SER B 2 398  ? 133.451 111.967 104.655 1.00 54.01  ? 395  SER A C     1 
ATOM   3216  O O     . SER B 2 398  ? 133.295 111.187 103.710 1.00 55.81  ? 395  SER A O     1 
ATOM   3217  C CB    . SER B 2 398  ? 135.084 113.660 103.821 1.00 50.75  ? 395  SER A CB    1 
ATOM   3218  O OG    . SER B 2 398  ? 135.460 112.611 102.946 1.00 53.05  ? 395  SER A OG    1 
ATOM   3219  N N     . GLU B 2 399  ? 133.436 111.558 105.924 1.00 55.21  ? 396  GLU A N     1 
ATOM   3220  C CA    . GLU B 2 399  ? 133.316 110.151 106.283 1.00 57.39  ? 396  GLU A CA    1 
ATOM   3221  C C     . GLU B 2 399  ? 132.119 109.893 107.197 1.00 59.41  ? 396  GLU A C     1 
ATOM   3222  O O     . GLU B 2 399  ? 132.128 108.949 107.992 1.00 61.15  ? 396  GLU A O     1 
ATOM   3223  C CB    . GLU B 2 399  ? 134.609 109.651 106.926 1.00 60.42  ? 396  GLU A CB    1 
ATOM   3224  C CG    . GLU B 2 399  ? 135.192 110.574 107.981 1.00 64.28  ? 396  GLU A CG    1 
ATOM   3225  C CD    . GLU B 2 399  ? 136.678 110.342 108.200 1.00 67.07  ? 396  GLU A CD    1 
ATOM   3226  O OE1   . GLU B 2 399  ? 137.311 109.684 107.347 1.00 65.64  ? 396  GLU A OE1   1 
ATOM   3227  O OE2   . GLU B 2 399  ? 137.215 110.819 109.223 1.00 69.02  ? 396  GLU A OE2   1 
ATOM   3228  N N     . LEU B 2 400  ? 131.079 110.715 107.089 1.00 60.34  ? 397  LEU A N     1 
ATOM   3229  C CA    . LEU B 2 400  ? 129.828 110.438 107.777 1.00 61.52  ? 397  LEU A CA    1 
ATOM   3230  C C     . LEU B 2 400  ? 128.973 109.479 106.952 1.00 66.17  ? 397  LEU A C     1 
ATOM   3231  O O     . LEU B 2 400  ? 129.194 109.278 105.756 1.00 67.89  ? 397  LEU A O     1 
ATOM   3232  C CB    . LEU B 2 400  ? 129.058 111.728 108.054 1.00 58.33  ? 397  LEU A CB    1 
ATOM   3233  C CG    . LEU B 2 400  ? 129.565 112.646 109.168 1.00 56.07  ? 397  LEU A CG    1 
ATOM   3234  C CD1   . LEU B 2 400  ? 128.703 113.893 109.257 1.00 52.93  ? 397  LEU A CD1   1 
ATOM   3235  C CD2   . LEU B 2 400  ? 129.582 111.919 110.501 1.00 56.87  ? 397  LEU A CD2   1 
ATOM   3236  N N     . THR B 2 401  ? 127.975 108.893 107.609 1.00 67.17  ? 398  THR A N     1 
ATOM   3237  C CA    . THR B 2 401  ? 127.133 107.867 107.010 1.00 68.26  ? 398  THR A CA    1 
ATOM   3238  C C     . THR B 2 401  ? 125.743 108.422 106.729 1.00 70.42  ? 398  THR A C     1 
ATOM   3239  O O     . THR B 2 401  ? 125.142 109.071 107.592 1.00 69.99  ? 398  THR A O     1 
ATOM   3240  C CB    . THR B 2 401  ? 127.025 106.645 107.923 1.00 69.51  ? 398  THR A CB    1 
ATOM   3241  O OG1   . THR B 2 401  ? 128.336 106.165 108.237 1.00 71.09  ? 398  THR A OG1   1 
ATOM   3242  C CG2   . THR B 2 401  ? 126.238 105.538 107.242 1.00 69.04  ? 398  THR A CG2   1 
ATOM   3243  N N     . GLY B 2 402  ? 125.237 108.160 105.524 1.00 72.94  ? 399  GLY A N     1 
ATOM   3244  C CA    . GLY B 2 402  ? 123.869 108.489 105.182 1.00 73.38  ? 399  GLY A CA    1 
ATOM   3245  C C     . GLY B 2 402  ? 123.633 109.978 104.989 1.00 71.54  ? 399  GLY A C     1 
ATOM   3246  O O     . GLY B 2 402  ? 124.544 110.764 104.705 1.00 68.17  ? 399  GLY A O     1 
ATOM   3247  N N     . LYS B 2 403  ? 122.365 110.361 105.146 1.00 73.98  ? 400  LYS A N     1 
ATOM   3248  C CA    . LYS B 2 403  ? 121.947 111.747 104.988 1.00 75.40  ? 400  LYS A CA    1 
ATOM   3249  C C     . LYS B 2 403  ? 122.609 112.632 106.037 1.00 76.42  ? 400  LYS A C     1 
ATOM   3250  O O     . LYS B 2 403  ? 122.202 112.638 107.201 1.00 78.29  ? 400  LYS A O     1 
ATOM   3251  C CB    . LYS B 2 403  ? 120.423 111.860 105.079 1.00 75.22  ? 400  LYS A CB    1 
ATOM   3252  N N     . ILE B 2 404  ? 123.635 113.377 105.628 1.00 77.32  ? 401  ILE A N     1 
ATOM   3253  C CA    . ILE B 2 404  ? 124.377 114.236 106.542 1.00 79.60  ? 401  ILE A CA    1 
ATOM   3254  C C     . ILE B 2 404  ? 123.528 115.448 106.910 1.00 80.05  ? 401  ILE A C     1 
ATOM   3255  O O     . ILE B 2 404  ? 123.499 116.450 106.189 1.00 81.20  ? 401  ILE A O     1 
ATOM   3256  C CB    . ILE B 2 404  ? 125.730 114.657 105.935 1.00 81.75  ? 401  ILE A CB    1 
ATOM   3257  C CG1   . ILE B 2 404  ? 125.577 115.053 104.464 1.00 84.74  ? 401  ILE A CG1   1 
ATOM   3258  C CG2   . ILE B 2 404  ? 126.735 113.526 106.054 1.00 81.77  ? 401  ILE A CG2   1 
ATOM   3259  C CD1   . ILE B 2 404  ? 126.861 115.555 103.834 1.00 85.76  ? 401  ILE A CD1   1 
ATOM   3260  N N     . THR B 2 405  ? 122.824 115.359 108.036 1.00 82.99  ? 402  THR A N     1 
ATOM   3261  C CA    . THR B 2 405  ? 122.007 116.470 108.493 1.00 83.36  ? 402  THR A CA    1 
ATOM   3262  C C     . THR B 2 405  ? 122.894 117.584 109.050 1.00 80.94  ? 402  THR A C     1 
ATOM   3263  O O     . THR B 2 405  ? 124.107 117.430 109.218 1.00 81.11  ? 402  THR A O     1 
ATOM   3264  C CB    . THR B 2 405  ? 121.021 116.009 109.565 1.00 81.38  ? 402  THR A CB    1 
ATOM   3265  O OG1   . THR B 2 405  ? 121.720 115.795 110.798 1.00 80.24  ? 402  THR A OG1   1 
ATOM   3266  C CG2   . THR B 2 405  ? 120.344 114.712 109.143 1.00 79.79  ? 402  THR A CG2   1 
ATOM   3267  N N     . LYS B 2 406  ? 122.268 118.727 109.340 1.00 78.98  ? 403  LYS A N     1 
ATOM   3268  C CA    . LYS B 2 406  ? 122.995 119.793 110.015 1.00 77.98  ? 403  LYS A CA    1 
ATOM   3269  C C     . LYS B 2 406  ? 123.250 119.459 111.479 1.00 78.45  ? 403  LYS A C     1 
ATOM   3270  O O     . LYS B 2 406  ? 124.124 120.075 112.100 1.00 78.31  ? 403  LYS A O     1 
ATOM   3271  C CB    . LYS B 2 406  ? 122.237 121.119 109.900 1.00 79.48  ? 403  LYS A CB    1 
ATOM   3272  C CG    . LYS B 2 406  ? 121.332 121.435 111.081 1.00 83.78  ? 403  LYS A CG    1 
ATOM   3273  C CD    . LYS B 2 406  ? 121.499 122.882 111.516 1.00 85.62  ? 403  LYS A CD    1 
ATOM   3274  C CE    . LYS B 2 406  ? 120.715 123.181 112.784 1.00 86.78  ? 403  LYS A CE    1 
ATOM   3275  N NZ    . LYS B 2 406  ? 120.992 124.554 113.290 1.00 86.12  ? 403  LYS A NZ    1 
ATOM   3276  N N     . SER B 2 407  ? 122.507 118.502 112.039 1.00 74.71  ? 404  SER A N     1 
ATOM   3277  C CA    . SER B 2 407  ? 122.793 118.036 113.390 1.00 71.62  ? 404  SER A CA    1 
ATOM   3278  C C     . SER B 2 407  ? 124.079 117.224 113.429 1.00 65.44  ? 404  SER A C     1 
ATOM   3279  O O     . SER B 2 407  ? 124.864 117.336 114.378 1.00 60.62  ? 404  SER A O     1 
ATOM   3280  C CB    . SER B 2 407  ? 121.620 117.208 113.917 1.00 74.39  ? 404  SER A CB    1 
ATOM   3281  O OG    . SER B 2 407  ? 121.939 116.611 115.163 1.00 75.44  ? 404  SER A OG    1 
ATOM   3282  N N     . ALA B 2 408  ? 124.314 116.401 112.402 1.00 63.23  ? 405  ALA A N     1 
ATOM   3283  C CA    . ALA B 2 408  ? 125.548 115.626 112.343 1.00 61.48  ? 405  ALA A CA    1 
ATOM   3284  C C     . ALA B 2 408  ? 126.767 116.523 112.165 1.00 58.53  ? 405  ALA A C     1 
ATOM   3285  O O     . ALA B 2 408  ? 127.856 116.185 112.639 1.00 58.67  ? 405  ALA A O     1 
ATOM   3286  C CB    . ALA B 2 408  ? 125.473 114.603 111.207 1.00 62.47  ? 405  ALA A CB    1 
ATOM   3287  N N     . LYS B 2 409  ? 126.606 117.663 111.491 1.00 57.00  ? 406  LYS A N     1 
ATOM   3288  C CA    . LYS B 2 409  ? 127.724 118.586 111.338 1.00 56.36  ? 406  LYS A CA    1 
ATOM   3289  C C     . LYS B 2 409  ? 128.059 119.267 112.658 1.00 54.87  ? 406  LYS A C     1 
ATOM   3290  O O     . LYS B 2 409  ? 129.237 119.448 112.989 1.00 53.77  ? 406  LYS A O     1 
ATOM   3291  C CB    . LYS B 2 409  ? 127.411 119.621 110.257 1.00 61.01  ? 406  LYS A CB    1 
ATOM   3292  C CG    . LYS B 2 409  ? 127.195 119.023 108.876 1.00 65.36  ? 406  LYS A CG    1 
ATOM   3293  C CD    . LYS B 2 409  ? 127.174 120.099 107.804 1.00 67.88  ? 406  LYS A CD    1 
ATOM   3294  C CE    . LYS B 2 409  ? 127.078 119.488 106.416 1.00 71.70  ? 406  LYS A CE    1 
ATOM   3295  N NZ    . LYS B 2 409  ? 127.222 120.514 105.344 1.00 73.84  ? 406  LYS A NZ    1 
ATOM   3296  N N     . GLU B 2 410  ? 127.038 119.649 113.428 1.00 55.94  ? 407  GLU A N     1 
ATOM   3297  C CA    . GLU B 2 410  ? 127.286 120.270 114.723 1.00 57.70  ? 407  GLU A CA    1 
ATOM   3298  C C     . GLU B 2 410  ? 127.923 119.292 115.702 1.00 55.32  ? 407  GLU A C     1 
ATOM   3299  O O     . GLU B 2 410  ? 128.688 119.708 116.580 1.00 52.80  ? 407  GLU A O     1 
ATOM   3300  C CB    . GLU B 2 410  ? 125.983 120.831 115.293 1.00 63.55  ? 407  GLU A CB    1 
ATOM   3301  C CG    . GLU B 2 410  ? 125.384 121.947 114.453 1.00 70.51  ? 407  GLU A CG    1 
ATOM   3302  C CD    . GLU B 2 410  ? 124.075 122.460 115.015 1.00 77.80  ? 407  GLU A CD    1 
ATOM   3303  O OE1   . GLU B 2 410  ? 123.582 121.877 116.005 1.00 80.15  ? 407  GLU A OE1   1 
ATOM   3304  O OE2   . GLU B 2 410  ? 123.540 123.448 114.468 1.00 80.58  ? 407  GLU A OE2   1 
ATOM   3305  N N     . LYS B 2 411  ? 127.622 117.997 115.568 1.00 54.41  ? 408  LYS A N     1 
ATOM   3306  C CA    . LYS B 2 411  ? 128.281 116.999 116.405 1.00 49.77  ? 408  LYS A CA    1 
ATOM   3307  C C     . LYS B 2 411  ? 129.763 116.892 116.066 1.00 48.18  ? 408  LYS A C     1 
ATOM   3308  O O     . LYS B 2 411  ? 130.597 116.711 116.962 1.00 49.97  ? 408  LYS A O     1 
ATOM   3309  C CB    . LYS B 2 411  ? 127.594 115.642 116.245 1.00 48.74  ? 408  LYS A CB    1 
ATOM   3310  C CG    . LYS B 2 411  ? 126.174 115.594 116.782 1.00 47.76  ? 408  LYS A CG    1 
ATOM   3311  C CD    . LYS B 2 411  ? 125.591 114.195 116.670 1.00 45.74  ? 408  LYS A CD    1 
ATOM   3312  C CE    . LYS B 2 411  ? 124.195 114.128 117.270 1.00 44.65  ? 408  LYS A CE    1 
ATOM   3313  N NZ    . LYS B 2 411  ? 123.641 112.746 117.230 1.00 44.18  ? 408  LYS A NZ    1 
ATOM   3314  N N     . VAL B 2 412  ? 130.108 117.004 114.783 1.00 46.81  ? 409  VAL A N     1 
ATOM   3315  C CA    . VAL B 2 412  ? 131.512 116.987 114.388 1.00 44.92  ? 409  VAL A CA    1 
ATOM   3316  C C     . VAL B 2 412  ? 132.223 118.240 114.891 1.00 46.96  ? 409  VAL A C     1 
ATOM   3317  O O     . VAL B 2 412  ? 133.388 118.189 115.300 1.00 48.55  ? 409  VAL A O     1 
ATOM   3318  C CB    . VAL B 2 412  ? 131.634 116.830 112.861 1.00 41.72  ? 409  VAL A CB    1 
ATOM   3319  C CG1   . VAL B 2 412  ? 133.085 116.949 112.418 1.00 39.72  ? 409  VAL A CG1   1 
ATOM   3320  C CG2   . VAL B 2 412  ? 131.051 115.494 112.418 1.00 40.35  ? 409  VAL A CG2   1 
ATOM   3321  N N     . GLN B 2 413  ? 131.527 119.380 114.887 1.00 50.27  ? 410  GLN A N     1 
ATOM   3322  C CA    . GLN B 2 413  ? 132.118 120.614 115.398 1.00 54.59  ? 410  GLN A CA    1 
ATOM   3323  C C     . GLN B 2 413  ? 132.423 120.501 116.885 1.00 56.91  ? 410  GLN A C     1 
ATOM   3324  O O     . GLN B 2 413  ? 133.540 120.799 117.327 1.00 58.31  ? 410  GLN A O     1 
ATOM   3325  C CB    . GLN B 2 413  ? 131.181 121.796 115.138 1.00 60.84  ? 410  GLN A CB    1 
ATOM   3326  C CG    . GLN B 2 413  ? 130.986 122.149 113.676 1.00 66.82  ? 410  GLN A CG    1 
ATOM   3327  C CD    . GLN B 2 413  ? 130.187 123.426 113.490 1.00 70.48  ? 410  GLN A CD    1 
ATOM   3328  O OE1   . GLN B 2 413  ? 130.104 124.259 114.392 1.00 73.35  ? 410  GLN A OE1   1 
ATOM   3329  N NE2   . GLN B 2 413  ? 129.590 123.584 112.312 1.00 69.47  ? 410  GLN A NE2   1 
ATOM   3330  N N     . ARG B 2 414  ? 131.437 120.072 117.679 1.00 58.45  ? 411  ARG A N     1 
ATOM   3331  C CA    . ARG B 2 414  ? 131.638 119.975 119.120 1.00 62.08  ? 411  ARG A CA    1 
ATOM   3332  C C     . ARG B 2 414  ? 132.692 118.936 119.476 1.00 60.96  ? 411  ARG A C     1 
ATOM   3333  O O     . ARG B 2 414  ? 133.387 119.081 120.488 1.00 62.33  ? 411  ARG A O     1 
ATOM   3334  C CB    . ARG B 2 414  ? 130.312 119.652 119.813 1.00 68.98  ? 411  ARG A CB    1 
ATOM   3335  C CG    . ARG B 2 414  ? 129.434 120.869 120.077 1.00 74.07  ? 411  ARG A CG    1 
ATOM   3336  C CD    . ARG B 2 414  ? 127.997 120.631 119.643 1.00 77.19  ? 411  ARG A CD    1 
ATOM   3337  N NE    . ARG B 2 414  ? 127.431 119.422 120.232 1.00 80.01  ? 411  ARG A NE    1 
ATOM   3338  C CZ    . ARG B 2 414  ? 126.220 118.950 119.950 1.00 82.13  ? 411  ARG A CZ    1 
ATOM   3339  N NH1   . ARG B 2 414  ? 125.445 119.588 119.083 1.00 82.60  ? 411  ARG A NH1   1 
ATOM   3340  N NH2   . ARG B 2 414  ? 125.787 117.841 120.532 1.00 82.76  ? 411  ARG A NH2   1 
ATOM   3341  N N     . SER B 2 415  ? 132.833 117.889 118.660 1.00 59.70  ? 412  SER A N     1 
ATOM   3342  C CA    . SER B 2 415  ? 133.837 116.869 118.940 1.00 60.25  ? 412  SER A CA    1 
ATOM   3343  C C     . SER B 2 415  ? 135.248 117.428 118.798 1.00 59.40  ? 412  SER A C     1 
ATOM   3344  O O     . SER B 2 415  ? 136.149 117.055 119.559 1.00 59.22  ? 412  SER A O     1 
ATOM   3345  C CB    . SER B 2 415  ? 133.637 115.666 118.019 1.00 59.64  ? 412  SER A CB    1 
ATOM   3346  O OG    . SER B 2 415  ? 133.784 116.032 116.658 1.00 57.95  ? 412  SER A OG    1 
ATOM   3347  N N     . LEU B 2 416  ? 135.457 118.330 117.839 1.00 57.65  ? 413  LEU A N     1 
ATOM   3348  C CA    . LEU B 2 416  ? 136.782 118.895 117.605 1.00 56.59  ? 413  LEU A CA    1 
ATOM   3349  C C     . LEU B 2 416  ? 137.209 119.883 118.682 1.00 56.85  ? 413  LEU A C     1 
ATOM   3350  O O     . LEU B 2 416  ? 138.389 120.245 118.729 1.00 57.64  ? 413  LEU A O     1 
ATOM   3351  C CB    . LEU B 2 416  ? 136.824 119.580 116.237 1.00 55.53  ? 413  LEU A CB    1 
ATOM   3352  C CG    . LEU B 2 416  ? 136.665 118.667 115.021 1.00 56.32  ? 413  LEU A CG    1 
ATOM   3353  C CD1   . LEU B 2 416  ? 136.642 119.477 113.735 1.00 56.37  ? 413  LEU A CD1   1 
ATOM   3354  C CD2   . LEU B 2 416  ? 137.781 117.633 114.984 1.00 57.40  ? 413  LEU A CD2   1 
ATOM   3355  N N     . LYS B 2 417  ? 136.293 120.329 119.544 1.00 58.81  ? 414  LYS A N     1 
ATOM   3356  C CA    . LYS B 2 417  ? 136.662 121.294 120.572 1.00 62.96  ? 414  LYS A CA    1 
ATOM   3357  C C     . LYS B 2 417  ? 137.339 120.638 121.768 1.00 70.32  ? 414  LYS A C     1 
ATOM   3358  O O     . LYS B 2 417  ? 138.235 121.239 122.370 1.00 74.45  ? 414  LYS A O     1 
ATOM   3359  C CB    . LYS B 2 417  ? 135.433 122.072 121.044 1.00 64.17  ? 414  LYS A CB    1 
ATOM   3360  C CG    . LYS B 2 417  ? 134.909 123.093 120.051 1.00 65.36  ? 414  LYS A CG    1 
ATOM   3361  C CD    . LYS B 2 417  ? 133.825 123.948 120.683 1.00 68.65  ? 414  LYS A CD    1 
ATOM   3362  C CE    . LYS B 2 417  ? 133.225 124.921 119.685 1.00 71.61  ? 414  LYS A CE    1 
ATOM   3363  N NZ    . LYS B 2 417  ? 132.224 125.817 120.329 1.00 73.27  ? 414  LYS A NZ    1 
ATOM   3364  N N     . HIS B 2 418  ? 136.934 119.418 122.129 1.00 73.22  ? 415  HIS A N     1 
ATOM   3365  C CA    . HIS B 2 418  ? 137.420 118.772 123.346 1.00 78.11  ? 415  HIS A CA    1 
ATOM   3366  C C     . HIS B 2 418  ? 137.764 117.301 123.092 1.00 80.86  ? 415  HIS A C     1 
ATOM   3367  O O     . HIS B 2 418  ? 137.224 116.389 123.708 1.00 82.13  ? 415  HIS A O     1 
ATOM   3368  C CB    . HIS B 2 418  ? 136.394 118.914 124.470 1.00 82.40  ? 415  HIS A CB    1 
ATOM   3369  C CG    . HIS B 2 418  ? 135.035 118.386 124.128 1.00 85.61  ? 415  HIS A CG    1 
ATOM   3370  N ND1   . HIS B 2 418  ? 134.804 117.062 123.821 1.00 86.50  ? 415  HIS A ND1   1 
ATOM   3371  C CD2   . HIS B 2 418  ? 133.831 119.002 124.054 1.00 87.03  ? 415  HIS A CD2   1 
ATOM   3372  C CE1   . HIS B 2 418  ? 133.518 116.887 123.567 1.00 87.72  ? 415  HIS A CE1   1 
ATOM   3373  N NE2   . HIS B 2 418  ? 132.906 118.050 123.701 1.00 88.00  ? 415  HIS A NE2   1 
ATOM   3374  N N     . GLU B 2 419  ? 138.696 117.061 122.174 1.00 83.95  ? 416  GLU A N     1 
ATOM   3375  C CA    . GLU B 2 419  ? 139.259 115.727 122.012 1.00 83.79  ? 416  GLU A CA    1 
ATOM   3376  C C     . GLU B 2 419  ? 140.638 115.856 121.382 1.00 78.53  ? 416  GLU A C     1 
ATOM   3377  O O     . GLU B 2 419  ? 140.909 116.802 120.639 1.00 77.95  ? 416  GLU A O     1 
ATOM   3378  C CB    . GLU B 2 419  ? 138.366 114.813 121.161 1.00 87.67  ? 416  GLU A CB    1 
ATOM   3379  C CG    . GLU B 2 419  ? 138.522 114.981 119.658 1.00 90.17  ? 416  GLU A CG    1 
ATOM   3380  C CD    . GLU B 2 419  ? 138.166 113.718 118.897 1.00 93.38  ? 416  GLU A CD    1 
ATOM   3381  O OE1   . GLU B 2 419  ? 139.058 112.861 118.716 1.00 94.41  ? 416  GLU A OE1   1 
ATOM   3382  O OE2   . GLU B 2 419  ? 136.994 113.574 118.491 1.00 94.47  ? 416  GLU A OE2   1 
ATOM   3383  N N     . ASP B 2 420  ? 141.506 114.898 121.694 1.00 71.23  ? 417  ASP A N     1 
ATOM   3384  C CA    . ASP B 2 420  ? 142.859 114.905 121.162 1.00 65.54  ? 417  ASP A CA    1 
ATOM   3385  C C     . ASP B 2 420  ? 142.879 114.243 119.792 1.00 63.16  ? 417  ASP A C     1 
ATOM   3386  O O     . ASP B 2 420  ? 142.348 113.143 119.617 1.00 65.36  ? 417  ASP A O     1 
ATOM   3387  C CB    . ASP B 2 420  ? 143.814 114.189 122.115 1.00 65.54  ? 417  ASP A CB    1 
ATOM   3388  C CG    . ASP B 2 420  ? 143.859 114.834 123.483 1.00 66.13  ? 417  ASP A CG    1 
ATOM   3389  O OD1   . ASP B 2 420  ? 143.786 116.080 123.560 1.00 63.56  ? 417  ASP A OD1   1 
ATOM   3390  O OD2   . ASP B 2 420  ? 143.962 114.096 124.484 1.00 69.64  ? 417  ASP A OD2   1 
ATOM   3391  N N     . ILE B 2 421  ? 143.484 114.921 118.820 1.00 60.55  ? 418  ILE A N     1 
ATOM   3392  C CA    . ILE B 2 421  ? 143.576 114.429 117.453 1.00 60.91  ? 418  ILE A CA    1 
ATOM   3393  C C     . ILE B 2 421  ? 144.926 113.750 117.277 1.00 63.56  ? 418  ILE A C     1 
ATOM   3394  O O     . ILE B 2 421  ? 145.958 114.288 117.695 1.00 67.57  ? 418  ILE A O     1 
ATOM   3395  C CB    . ILE B 2 421  ? 143.404 115.568 116.434 1.00 62.30  ? 418  ILE A CB    1 
ATOM   3396  C CG1   . ILE B 2 421  ? 142.266 116.504 116.853 1.00 60.60  ? 418  ILE A CG1   1 
ATOM   3397  C CG2   . ILE B 2 421  ? 143.147 115.001 115.044 1.00 64.15  ? 418  ILE A CG2   1 
ATOM   3398  C CD1   . ILE B 2 421  ? 140.898 115.859 116.835 1.00 59.92  ? 418  ILE A CD1   1 
ATOM   3399  N N     . ASN B 2 422  ? 144.926 112.569 116.662 1.00 63.00  ? 419  ASN A N     1 
ATOM   3400  C CA    . ASN B 2 422  ? 146.184 111.908 116.358 1.00 62.27  ? 419  ASN A CA    1 
ATOM   3401  C C     . ASN B 2 422  ? 146.867 112.602 115.184 1.00 59.36  ? 419  ASN A C     1 
ATOM   3402  O O     . ASN B 2 422  ? 146.218 113.216 114.332 1.00 57.11  ? 419  ASN A O     1 
ATOM   3403  C CB    . ASN B 2 422  ? 145.966 110.425 116.052 1.00 65.14  ? 419  ASN A CB    1 
ATOM   3404  C CG    . ASN B 2 422  ? 145.110 110.198 114.823 1.00 67.96  ? 419  ASN A CG    1 
ATOM   3405  O OD1   . ASN B 2 422  ? 145.579 110.327 113.692 1.00 67.95  ? 419  ASN A OD1   1 
ATOM   3406  N ND2   . ASN B 2 422  ? 143.849 109.840 115.039 1.00 70.51  ? 419  ASN A ND2   1 
ATOM   3407  N N     . LEU B 2 423  ? 148.198 112.499 115.148 1.00 59.65  ? 420  LEU A N     1 
ATOM   3408  C CA    . LEU B 2 423  ? 148.974 113.230 114.152 1.00 57.46  ? 420  LEU A CA    1 
ATOM   3409  C C     . LEU B 2 423  ? 148.668 112.761 112.732 1.00 55.20  ? 420  LEU A C     1 
ATOM   3410  O O     . LEU B 2 423  ? 148.794 113.545 111.786 1.00 55.83  ? 420  LEU A O     1 
ATOM   3411  C CB    . LEU B 2 423  ? 150.468 113.094 114.451 1.00 55.94  ? 420  LEU A CB    1 
ATOM   3412  C CG    . LEU B 2 423  ? 151.421 113.958 113.623 1.00 52.83  ? 420  LEU A CG    1 
ATOM   3413  C CD1   . LEU B 2 423  ? 151.037 115.427 113.720 1.00 50.48  ? 420  LEU A CD1   1 
ATOM   3414  C CD2   . LEU B 2 423  ? 152.861 113.749 114.068 1.00 53.36  ? 420  LEU A CD2   1 
ATOM   3415  N N     . GLN B 2 424  ? 148.259 111.502 112.562 1.00 54.17  ? 421  GLN A N     1 
ATOM   3416  C CA    . GLN B 2 424  ? 147.987 111.001 111.218 1.00 57.88  ? 421  GLN A CA    1 
ATOM   3417  C C     . GLN B 2 424  ? 146.738 111.646 110.627 1.00 57.24  ? 421  GLN A C     1 
ATOM   3418  O O     . GLN B 2 424  ? 146.724 112.008 109.445 1.00 58.01  ? 421  GLN A O     1 
ATOM   3419  C CB    . GLN B 2 424  ? 147.845 109.479 111.238 1.00 62.21  ? 421  GLN A CB    1 
ATOM   3420  C CG    . GLN B 2 424  ? 147.695 108.866 109.855 1.00 66.03  ? 421  GLN A CG    1 
ATOM   3421  C CD    . GLN B 2 424  ? 148.841 109.231 108.931 1.00 70.27  ? 421  GLN A CD    1 
ATOM   3422  O OE1   . GLN B 2 424  ? 150.012 109.133 109.305 1.00 74.17  ? 421  GLN A OE1   1 
ATOM   3423  N NE2   . GLN B 2 424  ? 148.512 109.668 107.720 1.00 67.95  ? 421  GLN A NE2   1 
ATOM   3424  N N     . GLU B 2 425  ? 145.682 111.799 111.431 1.00 54.96  ? 422  GLU A N     1 
ATOM   3425  C CA    . GLU B 2 425  ? 144.469 112.435 110.933 1.00 53.95  ? 422  GLU A CA    1 
ATOM   3426  C C     . GLU B 2 425  ? 144.707 113.898 110.581 1.00 52.50  ? 422  GLU A C     1 
ATOM   3427  O O     . GLU B 2 425  ? 144.029 114.442 109.702 1.00 50.75  ? 422  GLU A O     1 
ATOM   3428  C CB    . GLU B 2 425  ? 143.345 112.314 111.964 1.00 56.69  ? 422  GLU A CB    1 
ATOM   3429  C CG    . GLU B 2 425  ? 141.976 112.719 111.434 1.00 60.25  ? 422  GLU A CG    1 
ATOM   3430  C CD    . GLU B 2 425  ? 140.885 112.619 112.485 1.00 65.93  ? 422  GLU A CD    1 
ATOM   3431  O OE1   . GLU B 2 425  ? 141.218 112.551 113.687 1.00 70.77  ? 422  GLU A OE1   1 
ATOM   3432  O OE2   . GLU B 2 425  ? 139.693 112.609 112.106 1.00 65.23  ? 422  GLU A OE2   1 
ATOM   3433  N N     . ILE B 2 426  ? 145.668 114.546 111.243 1.00 52.90  ? 423  ILE A N     1 
ATOM   3434  C CA    . ILE B 2 426  ? 145.998 115.924 110.898 1.00 54.91  ? 423  ILE A CA    1 
ATOM   3435  C C     . ILE B 2 426  ? 146.694 115.983 109.545 1.00 58.00  ? 423  ILE A C     1 
ATOM   3436  O O     . ILE B 2 426  ? 146.373 116.830 108.702 1.00 59.25  ? 423  ILE A O     1 
ATOM   3437  C CB    . ILE B 2 426  ? 146.856 116.562 112.006 1.00 51.61  ? 423  ILE A CB    1 
ATOM   3438  C CG1   . ILE B 2 426  ? 146.129 116.498 113.350 1.00 51.48  ? 423  ILE A CG1   1 
ATOM   3439  C CG2   . ILE B 2 426  ? 147.197 118.003 111.658 1.00 47.13  ? 423  ILE A CG2   1 
ATOM   3440  C CD1   . ILE B 2 426  ? 146.897 117.137 114.488 1.00 51.56  ? 423  ILE A CD1   1 
ATOM   3441  N N     . ILE B 2 427  ? 147.650 115.081 109.311 1.00 59.00  ? 424  ILE A N     1 
ATOM   3442  C CA    . ILE B 2 427  ? 148.381 115.078 108.048 1.00 60.20  ? 424  ILE A CA    1 
ATOM   3443  C C     . ILE B 2 427  ? 147.462 114.688 106.897 1.00 60.59  ? 424  ILE A C     1 
ATOM   3444  O O     . ILE B 2 427  ? 147.517 115.280 105.812 1.00 61.13  ? 424  ILE A O     1 
ATOM   3445  C CB    . ILE B 2 427  ? 149.600 114.142 108.142 1.00 61.48  ? 424  ILE A CB    1 
ATOM   3446  C CG1   . ILE B 2 427  ? 150.571 114.641 109.214 1.00 60.61  ? 424  ILE A CG1   1 
ATOM   3447  C CG2   . ILE B 2 427  ? 150.298 114.027 106.796 1.00 63.62  ? 424  ILE A CG2   1 
ATOM   3448  C CD1   . ILE B 2 427  ? 151.793 113.766 109.384 1.00 60.75  ? 424  ILE A CD1   1 
ATOM   3449  N N     . SER B 2 428  ? 146.595 113.696 107.114 1.00 59.87  ? 425  SER A N     1 
ATOM   3450  C CA    . SER B 2 428  ? 145.683 113.255 106.064 1.00 60.24  ? 425  SER A CA    1 
ATOM   3451  C C     . SER B 2 428  ? 144.642 114.309 105.714 1.00 60.39  ? 425  SER A C     1 
ATOM   3452  O O     . SER B 2 428  ? 144.042 114.233 104.637 1.00 61.34  ? 425  SER A O     1 
ATOM   3453  C CB    . SER B 2 428  ? 144.985 111.962 106.485 1.00 61.33  ? 425  SER A CB    1 
ATOM   3454  O OG    . SER B 2 428  ? 145.923 110.930 106.730 1.00 64.10  ? 425  SER A OG    1 
ATOM   3455  N N     . ALA B 2 429  ? 144.416 115.287 106.590 1.00 58.46  ? 426  ALA A N     1 
ATOM   3456  C CA    . ALA B 2 429  ? 143.410 116.314 106.358 1.00 56.73  ? 426  ALA A CA    1 
ATOM   3457  C C     . ALA B 2 429  ? 143.993 117.645 105.906 1.00 56.81  ? 426  ALA A C     1 
ATOM   3458  O O     . ALA B 2 429  ? 143.295 118.418 105.241 1.00 54.87  ? 426  ALA A O     1 
ATOM   3459  C CB    . ALA B 2 429  ? 142.581 116.540 107.627 1.00 55.01  ? 426  ALA A CB    1 
ATOM   3460  N N     . ALA B 2 430  ? 145.248 117.933 106.246 1.00 58.19  ? 427  ALA A N     1 
ATOM   3461  C CA    . ALA B 2 430  ? 145.851 119.222 105.933 1.00 60.00  ? 427  ALA A CA    1 
ATOM   3462  C C     . ALA B 2 430  ? 146.725 119.197 104.689 1.00 63.25  ? 427  ALA A C     1 
ATOM   3463  O O     . ALA B 2 430  ? 146.890 120.239 104.048 1.00 64.89  ? 427  ALA A O     1 
ATOM   3464  C CB    . ALA B 2 430  ? 146.685 119.718 107.119 1.00 60.15  ? 427  ALA A CB    1 
ATOM   3465  N N     . GLY B 2 431  ? 147.283 118.051 104.335 1.00 64.73  ? 428  GLY A N     1 
ATOM   3466  C CA    . GLY B 2 431  ? 148.139 117.928 103.174 1.00 66.84  ? 428  GLY A CA    1 
ATOM   3467  C C     . GLY B 2 431  ? 149.604 117.791 103.556 1.00 70.62  ? 428  GLY A C     1 
ATOM   3468  O O     . GLY B 2 431  ? 149.998 117.913 104.716 1.00 71.44  ? 428  GLY A O     1 
ATOM   3469  N N     . LYS B 2 432  ? 150.419 117.536 102.530 1.00 75.03  ? 429  LYS A N     1 
ATOM   3470  C CA    . LYS B 2 432  ? 151.845 117.326 102.747 1.00 78.06  ? 429  LYS A CA    1 
ATOM   3471  C C     . LYS B 2 432  ? 152.566 118.602 103.157 1.00 81.83  ? 429  LYS A C     1 
ATOM   3472  O O     . LYS B 2 432  ? 153.677 118.524 103.694 1.00 84.59  ? 429  LYS A O     1 
ATOM   3473  C CB    . LYS B 2 432  ? 152.492 116.748 101.487 1.00 77.14  ? 429  LYS A CB    1 
ATOM   3474  C CG    . LYS B 2 432  ? 152.529 117.705 100.306 1.00 75.93  ? 429  LYS A CG    1 
ATOM   3475  C CD    . LYS B 2 432  ? 153.219 117.070 99.108  1.00 76.10  ? 429  LYS A CD    1 
ATOM   3476  C CE    . LYS B 2 432  ? 153.352 118.055 97.958  1.00 75.72  ? 429  LYS A CE    1 
ATOM   3477  N NZ    . LYS B 2 432  ? 154.000 117.437 96.768  1.00 75.64  ? 429  LYS A NZ    1 
ATOM   3478  N N     . GLU B 2 433  ? 151.968 119.772 102.924 1.00 83.67  ? 430  GLU A N     1 
ATOM   3479  C CA    . GLU B 2 433  ? 152.617 121.024 103.288 1.00 84.17  ? 430  GLU A CA    1 
ATOM   3480  C C     . GLU B 2 433  ? 152.622 121.275 104.789 1.00 80.64  ? 430  GLU A C     1 
ATOM   3481  O O     . GLU B 2 433  ? 153.364 122.150 105.248 1.00 80.72  ? 430  GLU A O     1 
ATOM   3482  C CB    . GLU B 2 433  ? 151.950 122.195 102.563 1.00 88.06  ? 430  GLU A CB    1 
ATOM   3483  C CG    . GLU B 2 433  ? 152.297 122.286 101.083 1.00 93.19  ? 430  GLU A CG    1 
ATOM   3484  C CD    . GLU B 2 433  ? 153.797 122.295 100.832 1.00 97.69  ? 430  GLU A CD    1 
ATOM   3485  O OE1   . GLU B 2 433  ? 154.422 123.365 100.998 1.00 98.64  ? 430  GLU A OE1   1 
ATOM   3486  O OE2   . GLU B 2 433  ? 154.352 121.235 100.478 1.00 99.47  ? 430  GLU A OE2   1 
ATOM   3487  N N     . LEU B 2 434  ? 151.819 120.542 105.562 1.00 76.25  ? 431  LEU A N     1 
ATOM   3488  C CA    . LEU B 2 434  ? 151.927 120.636 107.013 1.00 73.45  ? 431  LEU A CA    1 
ATOM   3489  C C     . LEU B 2 434  ? 153.146 119.882 107.522 1.00 75.00  ? 431  LEU A C     1 
ATOM   3490  O O     . LEU B 2 434  ? 153.826 120.346 108.446 1.00 73.35  ? 431  LEU A O     1 
ATOM   3491  C CB    . LEU B 2 434  ? 150.657 120.104 107.682 1.00 69.31  ? 431  LEU A CB    1 
ATOM   3492  C CG    . LEU B 2 434  ? 150.624 120.139 109.212 1.00 66.05  ? 431  LEU A CG    1 
ATOM   3493  C CD1   . LEU B 2 434  ? 149.237 120.482 109.686 1.00 63.30  ? 431  LEU A CD1   1 
ATOM   3494  C CD2   . LEU B 2 434  ? 151.062 118.811 109.822 1.00 66.91  ? 431  LEU A CD2   1 
ATOM   3495  N N     . SER B 2 435  ? 153.431 118.716 106.937 1.00 77.08  ? 432  SER A N     1 
ATOM   3496  C CA    . SER B 2 435  ? 154.614 117.961 107.329 1.00 78.73  ? 432  SER A CA    1 
ATOM   3497  C C     . SER B 2 435  ? 155.880 118.780 107.115 1.00 80.79  ? 432  SER A C     1 
ATOM   3498  O O     . SER B 2 435  ? 156.779 118.780 107.965 1.00 83.35  ? 432  SER A O     1 
ATOM   3499  C CB    . SER B 2 435  ? 154.681 116.649 106.548 1.00 77.43  ? 432  SER A CB    1 
ATOM   3500  O OG    . SER B 2 435  ? 153.475 115.915 106.684 1.00 74.11  ? 432  SER A OG    1 
ATOM   3501  N N     . GLU B 2 436  ? 155.963 119.495 105.991 1.00 81.23  ? 433  GLU A N     1 
ATOM   3502  C CA    . GLU B 2 436  ? 157.113 120.364 105.753 1.00 83.87  ? 433  GLU A CA    1 
ATOM   3503  C C     . GLU B 2 436  ? 157.159 121.503 106.763 1.00 81.75  ? 433  GLU A C     1 
ATOM   3504  O O     . GLU B 2 436  ? 158.239 121.903 107.208 1.00 84.25  ? 433  GLU A O     1 
ATOM   3505  C CB    . GLU B 2 436  ? 157.075 120.909 104.326 1.00 87.14  ? 433  GLU A CB    1 
ATOM   3506  C CG    . GLU B 2 436  ? 157.248 119.851 103.249 1.00 92.14  ? 433  GLU A CG    1 
ATOM   3507  C CD    . GLU B 2 436  ? 158.500 119.017 103.449 1.00 98.50  ? 433  GLU A CD    1 
ATOM   3508  O OE1   . GLU B 2 436  ? 159.606 119.530 103.179 1.00 99.42  ? 433  GLU A OE1   1 
ATOM   3509  O OE2   . GLU B 2 436  ? 158.378 117.852 103.883 1.00 101.10 ? 433  GLU A OE2   1 
ATOM   3510  N N     . ALA B 2 437  ? 155.994 122.038 107.137 1.00 78.11  ? 434  ALA A N     1 
ATOM   3511  C CA    . ALA B 2 437  ? 155.954 123.060 108.179 1.00 73.42  ? 434  ALA A CA    1 
ATOM   3512  C C     . ALA B 2 437  ? 156.306 122.470 109.537 1.00 70.08  ? 434  ALA A C     1 
ATOM   3513  O O     . ALA B 2 437  ? 156.983 123.118 110.345 1.00 72.44  ? 434  ALA A O     1 
ATOM   3514  C CB    . ALA B 2 437  ? 154.575 123.718 108.217 1.00 68.60  ? 434  ALA A CB    1 
ATOM   3515  N N     . PHE B 2 438  ? 155.856 121.242 109.804 1.00 65.40  ? 435  PHE A N     1 
ATOM   3516  C CA    . PHE B 2 438  ? 156.185 120.590 111.069 1.00 64.44  ? 435  PHE A CA    1 
ATOM   3517  C C     . PHE B 2 438  ? 157.670 120.266 111.147 1.00 67.81  ? 435  PHE A C     1 
ATOM   3518  O O     . PHE B 2 438  ? 158.293 120.443 112.200 1.00 72.12  ? 435  PHE A O     1 
ATOM   3519  C CB    . PHE B 2 438  ? 155.345 119.322 111.237 1.00 66.88  ? 435  PHE A CB    1 
ATOM   3520  C CG    . PHE B 2 438  ? 155.256 118.834 112.656 1.00 70.76  ? 435  PHE A CG    1 
ATOM   3521  C CD1   . PHE B 2 438  ? 156.258 118.047 113.202 1.00 73.90  ? 435  PHE A CD1   1 
ATOM   3522  C CD2   . PHE B 2 438  ? 154.160 119.154 113.443 1.00 70.82  ? 435  PHE A CD2   1 
ATOM   3523  C CE1   . PHE B 2 438  ? 156.174 117.595 114.505 1.00 74.01  ? 435  PHE A CE1   1 
ATOM   3524  C CE2   . PHE B 2 438  ? 154.071 118.705 114.749 1.00 71.95  ? 435  PHE A CE2   1 
ATOM   3525  C CZ    . PHE B 2 438  ? 155.080 117.924 115.280 1.00 73.00  ? 435  PHE A CZ    1 
ATOM   3526  N N     . LYS B 2 439  ? 158.255 119.786 110.046 1.00 68.66  ? 436  LYS A N     1 
ATOM   3527  C CA    . LYS B 2 439  ? 159.685 119.491 110.031 1.00 71.97  ? 436  LYS A CA    1 
ATOM   3528  C C     . LYS B 2 439  ? 160.509 120.762 110.194 1.00 75.23  ? 436  LYS A C     1 
ATOM   3529  O O     . LYS B 2 439  ? 161.463 120.802 110.980 1.00 78.49  ? 436  LYS A O     1 
ATOM   3530  C CB    . LYS B 2 439  ? 160.064 118.775 108.736 1.00 74.40  ? 436  LYS A CB    1 
ATOM   3531  C CG    . LYS B 2 439  ? 159.512 117.367 108.588 1.00 75.85  ? 436  LYS A CG    1 
ATOM   3532  C CD    . LYS B 2 439  ? 159.867 116.796 107.223 1.00 77.22  ? 436  LYS A CD    1 
ATOM   3533  C CE    . LYS B 2 439  ? 159.180 115.466 106.976 1.00 77.04  ? 436  LYS A CE    1 
ATOM   3534  N NZ    . LYS B 2 439  ? 159.562 114.456 107.998 1.00 78.26  ? 436  LYS A NZ    1 
ATOM   3535  N N     . GLN B 2 440  ? 160.155 121.814 109.451 1.00 74.16  ? 437  GLN A N     1 
ATOM   3536  C CA    . GLN B 2 440  ? 160.938 123.046 109.489 1.00 73.05  ? 437  GLN A CA    1 
ATOM   3537  C C     . GLN B 2 440  ? 160.850 123.721 110.851 1.00 71.98  ? 437  GLN A C     1 
ATOM   3538  O O     . GLN B 2 440  ? 161.858 124.211 111.372 1.00 71.92  ? 437  GLN A O     1 
ATOM   3539  C CB    . GLN B 2 440  ? 160.473 123.997 108.386 1.00 70.87  ? 437  GLN A CB    1 
ATOM   3540  N N     . LYS B 2 441  ? 159.655 123.755 111.448 1.00 71.57  ? 438  LYS A N     1 
ATOM   3541  C CA    . LYS B 2 441  ? 159.504 124.394 112.752 1.00 73.43  ? 438  LYS A CA    1 
ATOM   3542  C C     . LYS B 2 441  ? 160.206 123.596 113.842 1.00 76.29  ? 438  LYS A C     1 
ATOM   3543  O O     . LYS B 2 441  ? 160.760 124.176 114.783 1.00 78.76  ? 438  LYS A O     1 
ATOM   3544  C CB    . LYS B 2 441  ? 158.022 124.560 113.089 1.00 72.83  ? 438  LYS A CB    1 
ATOM   3545  C CG    . LYS B 2 441  ? 157.742 125.513 114.243 1.00 72.88  ? 438  LYS A CG    1 
ATOM   3546  C CD    . LYS B 2 441  ? 157.684 126.957 113.763 1.00 73.60  ? 438  LYS A CD    1 
ATOM   3547  C CE    . LYS B 2 441  ? 157.483 127.927 114.917 1.00 75.06  ? 438  LYS A CE    1 
ATOM   3548  N NZ    . LYS B 2 441  ? 158.682 128.002 115.799 1.00 78.59  ? 438  LYS A NZ    1 
ATOM   3549  N N     . THR B 2 442  ? 160.194 122.265 113.733 1.00 78.54  ? 439  THR A N     1 
ATOM   3550  C CA    . THR B 2 442  ? 160.833 121.433 114.746 1.00 81.90  ? 439  THR A CA    1 
ATOM   3551  C C     . THR B 2 442  ? 162.348 121.608 114.727 1.00 85.48  ? 439  THR A C     1 
ATOM   3552  O O     . THR B 2 442  ? 162.972 121.803 115.774 1.00 86.85  ? 439  THR A O     1 
ATOM   3553  C CB    . THR B 2 442  ? 160.455 119.966 114.538 1.00 83.01  ? 439  THR A CB    1 
ATOM   3554  O OG1   . THR B 2 442  ? 159.035 119.818 114.654 1.00 82.75  ? 439  THR A OG1   1 
ATOM   3555  C CG2   . THR B 2 442  ? 161.136 119.092 115.573 1.00 84.91  ? 439  THR A CG2   1 
ATOM   3556  N N     . SER B 2 443  ? 162.956 121.540 113.540 1.00 86.01  ? 440  SER A N     1 
ATOM   3557  C CA    . SER B 2 443  ? 164.398 121.734 113.446 1.00 87.83  ? 440  SER A CA    1 
ATOM   3558  C C     . SER B 2 443  ? 164.792 123.164 113.790 1.00 85.40  ? 440  SER A C     1 
ATOM   3559  O O     . SER B 2 443  ? 165.878 123.390 114.335 1.00 87.95  ? 440  SER A O     1 
ATOM   3560  C CB    . SER B 2 443  ? 164.892 121.374 112.044 1.00 89.67  ? 440  SER A CB    1 
ATOM   3561  O OG    . SER B 2 443  ? 164.432 122.310 111.085 1.00 89.22  ? 440  SER A OG    1 
ATOM   3562  N N     . GLU B 2 444  ? 163.931 124.136 113.482 1.00 81.24  ? 441  GLU A N     1 
ATOM   3563  C CA    . GLU B 2 444  ? 164.222 125.526 113.817 1.00 80.45  ? 441  GLU A CA    1 
ATOM   3564  C C     . GLU B 2 444  ? 164.300 125.715 115.328 1.00 77.42  ? 441  GLU A C     1 
ATOM   3565  O O     . GLU B 2 444  ? 165.211 126.376 115.838 1.00 74.97  ? 441  GLU A O     1 
ATOM   3566  C CB    . GLU B 2 444  ? 163.155 126.442 113.213 1.00 83.37  ? 441  GLU A CB    1 
ATOM   3567  C CG    . GLU B 2 444  ? 163.471 127.926 113.292 1.00 89.14  ? 441  GLU A CG    1 
ATOM   3568  C CD    . GLU B 2 444  ? 162.298 128.788 112.864 1.00 91.57  ? 441  GLU A CD    1 
ATOM   3569  O OE1   . GLU B 2 444  ? 161.300 128.854 113.613 1.00 90.05  ? 441  GLU A OE1   1 
ATOM   3570  O OE2   . GLU B 2 444  ? 162.369 129.392 111.773 1.00 93.69  ? 441  GLU A OE2   1 
ATOM   3571  N N     . ILE B 2 445  ? 163.345 125.137 116.060 1.00 77.37  ? 442  ILE A N     1 
ATOM   3572  C CA    . ILE B 2 445  ? 163.359 125.237 117.515 1.00 77.48  ? 442  ILE A CA    1 
ATOM   3573  C C     . ILE B 2 445  ? 164.506 124.423 118.099 1.00 81.29  ? 442  ILE A C     1 
ATOM   3574  O O     . ILE B 2 445  ? 165.204 124.875 119.015 1.00 83.89  ? 442  ILE A O     1 
ATOM   3575  C CB    . ILE B 2 445  ? 161.999 124.798 118.090 1.00 71.65  ? 442  ILE A CB    1 
ATOM   3576  C CG1   . ILE B 2 445  ? 160.896 125.756 117.641 1.00 68.15  ? 442  ILE A CG1   1 
ATOM   3577  C CG2   . ILE B 2 445  ? 162.057 124.721 119.607 1.00 70.36  ? 442  ILE A CG2   1 
ATOM   3578  C CD1   . ILE B 2 445  ? 159.515 125.363 118.120 1.00 65.90  ? 442  ILE A CD1   1 
ATOM   3579  N N     . LEU B 2 446  ? 164.725 123.212 117.575 1.00 83.47  ? 443  LEU A N     1 
ATOM   3580  C CA    . LEU B 2 446  ? 165.787 122.357 118.098 1.00 85.31  ? 443  LEU A CA    1 
ATOM   3581  C C     . LEU B 2 446  ? 167.165 122.955 117.840 1.00 86.32  ? 443  LEU A C     1 
ATOM   3582  O O     . LEU B 2 446  ? 168.063 122.835 118.681 1.00 86.56  ? 443  LEU A O     1 
ATOM   3583  C CB    . LEU B 2 446  ? 165.684 120.960 117.486 1.00 86.70  ? 443  LEU A CB    1 
ATOM   3584  C CG    . LEU B 2 446  ? 164.552 120.072 118.009 1.00 87.22  ? 443  LEU A CG    1 
ATOM   3585  C CD1   . LEU B 2 446  ? 164.470 118.776 117.218 1.00 88.01  ? 443  LEU A CD1   1 
ATOM   3586  C CD2   . LEU B 2 446  ? 164.742 119.788 119.491 1.00 88.52  ? 443  LEU A CD2   1 
ATOM   3587  N N     . SER B 2 447  ? 167.353 123.602 116.688 1.00 88.14  ? 444  SER A N     1 
ATOM   3588  C CA    . SER B 2 447  ? 168.643 124.218 116.398 1.00 91.13  ? 444  SER A CA    1 
ATOM   3589  C C     . SER B 2 447  ? 168.906 125.407 117.313 1.00 90.72  ? 444  SER A C     1 
ATOM   3590  O O     . SER B 2 447  ? 170.036 125.606 117.772 1.00 92.77  ? 444  SER A O     1 
ATOM   3591  C CB    . SER B 2 447  ? 168.710 124.646 114.931 1.00 93.47  ? 444  SER A CB    1 
ATOM   3592  O OG    . SER B 2 447  ? 167.712 125.607 114.633 1.00 94.40  ? 444  SER A OG    1 
ATOM   3593  N N     . HIS B 2 448  ? 167.874 126.208 117.594 1.00 87.50  ? 445  HIS A N     1 
ATOM   3594  C CA    . HIS B 2 448  ? 168.048 127.349 118.489 1.00 87.46  ? 445  HIS A CA    1 
ATOM   3595  C C     . HIS B 2 448  ? 168.362 126.896 119.910 1.00 89.75  ? 445  HIS A C     1 
ATOM   3596  O O     . HIS B 2 448  ? 169.199 127.501 120.589 1.00 85.95  ? 445  HIS A O     1 
ATOM   3597  C CB    . HIS B 2 448  ? 166.801 128.230 118.469 1.00 85.74  ? 445  HIS A CB    1 
ATOM   3598  C CG    . HIS B 2 448  ? 166.715 129.125 117.271 1.00 85.36  ? 445  HIS A CG    1 
ATOM   3599  N ND1   . HIS B 2 448  ? 165.536 129.351 116.594 1.00 83.08  ? 445  HIS A ND1   1 
ATOM   3600  C CD2   . HIS B 2 448  ? 167.660 129.855 116.634 1.00 86.80  ? 445  HIS A CD2   1 
ATOM   3601  C CE1   . HIS B 2 448  ? 165.761 130.179 115.589 1.00 82.91  ? 445  HIS A CE1   1 
ATOM   3602  N NE2   . HIS B 2 448  ? 167.041 130.499 115.592 1.00 85.21  ? 445  HIS A NE2   1 
ATOM   3603  N N     . ALA B 2 449  ? 167.701 125.834 120.378 1.00 100.67 ? 446  ALA A N     1 
ATOM   3604  C CA    . ALA B 2 449  ? 168.022 125.295 121.695 1.00 107.66 ? 446  ALA A CA    1 
ATOM   3605  C C     . ALA B 2 449  ? 169.393 124.634 121.695 1.00 112.85 ? 446  ALA A C     1 
ATOM   3606  O O     . ALA B 2 449  ? 170.126 124.708 122.690 1.00 115.14 ? 446  ALA A O     1 
ATOM   3607  C CB    . ALA B 2 449  ? 166.944 124.306 122.137 1.00 102.88 ? 446  ALA A CB    1 
ATOM   3608  N N     . HIS B 2 450  ? 169.759 123.982 120.590 1.00 115.10 ? 447  HIS A N     1 
ATOM   3609  C CA    . HIS B 2 450  ? 171.092 123.398 120.481 1.00 118.19 ? 447  HIS A CA    1 
ATOM   3610  C C     . HIS B 2 450  ? 172.159 124.480 120.381 1.00 118.55 ? 447  HIS A C     1 
ATOM   3611  O O     . HIS B 2 450  ? 173.247 124.341 120.950 1.00 121.24 ? 447  HIS A O     1 
ATOM   3612  C CB    . HIS B 2 450  ? 171.155 122.459 119.277 1.00 121.14 ? 447  HIS A CB    1 
ATOM   3613  C CG    . HIS B 2 450  ? 172.538 122.235 118.753 1.00 128.20 ? 447  HIS A CG    1 
ATOM   3614  N ND1   . HIS B 2 450  ? 173.565 121.757 119.537 1.00 133.27 ? 447  HIS A ND1   1 
ATOM   3615  C CD2   . HIS B 2 450  ? 173.064 122.424 117.519 1.00 130.97 ? 447  HIS A CD2   1 
ATOM   3616  C CE1   . HIS B 2 450  ? 174.664 121.662 118.810 1.00 136.11 ? 447  HIS A CE1   1 
ATOM   3617  N NE2   . HIS B 2 450  ? 174.387 122.061 117.581 1.00 135.00 ? 447  HIS A NE2   1 
ATOM   3618  N N     . ALA B 2 451  ? 171.866 125.568 119.666 1.00 114.33 ? 448  ALA A N     1 
ATOM   3619  C CA    . ALA B 2 451  ? 172.808 126.675 119.547 1.00 111.04 ? 448  ALA A CA    1 
ATOM   3620  C C     . ALA B 2 451  ? 172.876 127.536 120.800 1.00 106.42 ? 448  ALA A C     1 
ATOM   3621  O O     . ALA B 2 451  ? 173.774 128.378 120.906 1.00 109.27 ? 448  ALA A O     1 
ATOM   3622  C CB    . ALA B 2 451  ? 172.446 127.553 118.347 1.00 106.97 ? 448  ALA A CB    1 
ATOM   3623  N N     . ALA B 2 452  ? 171.956 127.348 121.745 1.00 100.07 ? 449  ALA A N     1 
ATOM   3624  C CA    . ALA B 2 452  ? 171.961 128.110 122.987 1.00 97.80  ? 449  ALA A CA    1 
ATOM   3625  C C     . ALA B 2 452  ? 172.608 127.367 124.147 1.00 99.67  ? 449  ALA A C     1 
ATOM   3626  O O     . ALA B 2 452  ? 173.142 128.012 125.053 1.00 99.07  ? 449  ALA A O     1 
ATOM   3627  C CB    . ALA B 2 452  ? 170.531 128.501 123.380 1.00 95.05  ? 449  ALA A CB    1 
ATOM   3628  N N     . LEU B 2 453  ? 172.577 126.032 124.140 1.00 102.48 ? 450  LEU A N     1 
ATOM   3629  C CA    . LEU B 2 453  ? 173.179 125.278 125.234 1.00 105.44 ? 450  LEU A CA    1 
ATOM   3630  C C     . LEU B 2 453  ? 174.698 125.360 125.216 1.00 113.03 ? 450  LEU A C     1 
ATOM   3631  O O     . LEU B 2 453  ? 175.332 125.306 126.274 1.00 115.75 ? 450  LEU A O     1 
ATOM   3632  C CB    . LEU B 2 453  ? 172.731 123.817 125.185 1.00 102.11 ? 450  LEU A CB    1 
ATOM   3633  C CG    . LEU B 2 453  ? 171.359 123.506 125.782 1.00 96.49  ? 450  LEU A CG    1 
ATOM   3634  C CD1   . LEU B 2 453  ? 171.119 122.007 125.810 1.00 95.71  ? 450  LEU A CD1   1 
ATOM   3635  C CD2   . LEU B 2 453  ? 171.244 124.090 127.178 1.00 95.06  ? 450  LEU A CD2   1 
ATOM   3636  N N     . ASP B 2 454  ? 175.300 125.480 124.033 1.00 121.03 ? 451  ASP A N     1 
ATOM   3637  C CA    . ASP B 2 454  ? 176.748 125.604 123.936 1.00 126.47 ? 451  ASP A CA    1 
ATOM   3638  C C     . ASP B 2 454  ? 177.223 127.051 123.982 1.00 127.80 ? 451  ASP A C     1 
ATOM   3639  O O     . ASP B 2 454  ? 178.410 127.289 124.227 1.00 131.43 ? 451  ASP A O     1 
ATOM   3640  C CB    . ASP B 2 454  ? 177.252 124.935 122.653 1.00 128.65 ? 451  ASP A CB    1 
ATOM   3641  C CG    . ASP B 2 454  ? 176.540 125.433 121.414 1.00 129.79 ? 451  ASP A CG    1 
ATOM   3642  O OD1   . ASP B 2 454  ? 175.465 126.053 121.554 1.00 130.11 ? 451  ASP A OD1   1 
ATOM   3643  O OD2   . ASP B 2 454  ? 177.050 125.201 120.296 1.00 131.16 ? 451  ASP A OD2   1 
ATOM   3644  N N     . GLN B 2 455  ? 176.333 128.009 123.759 1.00 119.27 ? 452  GLN A N     1 
ATOM   3645  C CA    . GLN B 2 455  ? 176.696 129.418 123.862 1.00 117.23 ? 452  GLN A CA    1 
ATOM   3646  C C     . GLN B 2 455  ? 176.858 129.795 125.328 1.00 117.40 ? 452  GLN A C     1 
ATOM   3647  O O     . GLN B 2 455  ? 175.903 129.651 126.104 1.00 115.47 ? 452  GLN A O     1 
ATOM   3648  C CB    . GLN B 2 455  ? 175.633 130.290 123.201 1.00 113.66 ? 452  GLN A CB    1 
ATOM   3649  C CG    . GLN B 2 455  ? 175.977 131.771 123.160 1.00 114.16 ? 452  GLN A CG    1 
ATOM   3650  C CD    . GLN B 2 455  ? 174.799 132.631 122.740 1.00 111.69 ? 452  GLN A CD    1 
ATOM   3651  O OE1   . GLN B 2 455  ? 173.661 132.390 123.149 1.00 109.11 ? 452  GLN A OE1   1 
ATOM   3652  N NE2   . GLN B 2 455  ? 175.064 133.640 121.919 1.00 112.62 ? 452  GLN A NE2   1 
ATOM   3653  N N     . PRO B 2 456  ? 178.023 130.274 125.755 1.00 119.43 ? 453  PRO A N     1 
ATOM   3654  C CA    . PRO B 2 456  ? 178.226 130.572 127.174 1.00 120.27 ? 453  PRO A CA    1 
ATOM   3655  C C     . PRO B 2 456  ? 177.553 131.867 127.599 1.00 117.33 ? 453  PRO A C     1 
ATOM   3656  O O     . PRO B 2 456  ? 177.433 132.823 126.829 1.00 117.36 ? 453  PRO A O     1 
ATOM   3657  C CB    . PRO B 2 456  ? 179.750 130.680 127.291 1.00 123.73 ? 453  PRO A CB    1 
ATOM   3658  C CG    . PRO B 2 456  ? 180.180 131.154 125.944 1.00 123.50 ? 453  PRO A CG    1 
ATOM   3659  C CD    . PRO B 2 456  ? 179.241 130.507 124.958 1.00 120.99 ? 453  PRO A CD    1 
ATOM   3660  N N     . LEU B 2 457  ? 177.112 131.885 128.856 1.00 114.91 ? 454  LEU A N     1 
ATOM   3661  C CA    . LEU B 2 457  ? 176.522 133.079 129.432 1.00 113.11 ? 454  LEU A CA    1 
ATOM   3662  C C     . LEU B 2 457  ? 177.596 134.135 129.680 1.00 115.46 ? 454  LEU A C     1 
ATOM   3663  O O     . LEU B 2 457  ? 178.781 133.815 129.796 1.00 118.75 ? 454  LEU A O     1 
ATOM   3664  C CB    . LEU B 2 457  ? 175.805 132.742 130.740 1.00 114.30 ? 454  LEU A CB    1 
ATOM   3665  C CG    . LEU B 2 457  ? 174.366 132.229 130.654 1.00 113.38 ? 454  LEU A CG    1 
ATOM   3666  C CD1   . LEU B 2 457  ? 173.552 133.059 129.669 1.00 110.47 ? 454  LEU A CD1   1 
ATOM   3667  C CD2   . LEU B 2 457  ? 174.328 130.757 130.292 1.00 115.64 ? 454  LEU A CD2   1 
ATOM   3668  N N     . PRO B 2 458  ? 177.205 135.415 129.764 1.00 114.32 ? 455  PRO A N     1 
ATOM   3669  C CA    . PRO B 2 458  ? 178.193 136.463 130.054 1.00 116.61 ? 455  PRO A CA    1 
ATOM   3670  C C     . PRO B 2 458  ? 178.659 136.428 131.501 1.00 118.12 ? 455  PRO A C     1 
ATOM   3671  O O     . PRO B 2 458  ? 178.205 135.594 132.288 1.00 119.72 ? 455  PRO A O     1 
ATOM   3672  C CB    . PRO B 2 458  ? 177.432 137.754 129.738 1.00 112.98 ? 455  PRO A CB    1 
ATOM   3673  C CG    . PRO B 2 458  ? 176.008 137.407 129.986 1.00 108.76 ? 455  PRO A CG    1 
ATOM   3674  C CD    . PRO B 2 458  ? 175.861 135.977 129.542 1.00 109.94 ? 455  PRO A CD    1 
ATOM   3675  N N     . THR B 2 459  ? 179.565 137.337 131.860 1.00 118.19 ? 456  THR A N     1 
ATOM   3676  C CA    . THR B 2 459  ? 180.087 137.362 133.223 1.00 119.56 ? 456  THR A CA    1 
ATOM   3677  C C     . THR B 2 459  ? 179.148 138.099 134.172 1.00 117.71 ? 456  THR A C     1 
ATOM   3678  O O     . THR B 2 459  ? 178.973 137.679 135.322 1.00 117.84 ? 456  THR A O     1 
ATOM   3679  C CB    . THR B 2 459  ? 181.475 138.001 133.243 1.00 123.08 ? 456  THR A CB    1 
ATOM   3680  O OG1   . THR B 2 459  ? 181.408 139.315 132.673 1.00 122.90 ? 456  THR A OG1   1 
ATOM   3681  C CG2   . THR B 2 459  ? 182.461 137.156 132.446 1.00 125.17 ? 456  THR A CG2   1 
ATOM   3682  N N     . THR B 2 460  ? 178.538 139.192 133.717 1.00 116.18 ? 457  THR A N     1 
ATOM   3683  C CA    . THR B 2 460  ? 177.632 139.979 134.539 1.00 114.36 ? 457  THR A CA    1 
ATOM   3684  C C     . THR B 2 460  ? 176.431 140.407 133.706 1.00 111.03 ? 457  THR A C     1 
ATOM   3685  O O     . THR B 2 460  ? 176.400 140.242 132.484 1.00 108.59 ? 457  THR A O     1 
ATOM   3686  C CB    . THR B 2 460  ? 178.325 141.216 135.130 1.00 115.73 ? 457  THR A CB    1 
ATOM   3687  O OG1   . THR B 2 460  ? 179.031 141.914 134.096 1.00 117.12 ? 457  THR A OG1   1 
ATOM   3688  C CG2   . THR B 2 460  ? 179.297 140.820 136.233 1.00 119.14 ? 457  THR A CG2   1 
ATOM   3689  N N     . LEU B 2 461  ? 175.430 140.961 134.392 1.00 109.57 ? 458  LEU A N     1 
ATOM   3690  C CA    . LEU B 2 461  ? 174.251 141.538 133.760 1.00 104.67 ? 458  LEU A CA    1 
ATOM   3691  C C     . LEU B 2 461  ? 174.295 143.063 133.753 1.00 104.08 ? 458  LEU A C     1 
ATOM   3692  O O     . LEU B 2 461  ? 173.246 143.717 133.747 1.00 102.62 ? 458  LEU A O     1 
ATOM   3693  C CB    . LEU B 2 461  ? 172.981 141.049 134.457 1.00 100.50 ? 458  LEU A CB    1 
ATOM   3694  C CG    . LEU B 2 461  ? 172.220 139.869 133.851 1.00 97.36  ? 458  LEU A CG    1 
ATOM   3695  C CD1   . LEU B 2 461  ? 173.137 138.681 133.615 1.00 99.18  ? 458  LEU A CD1   1 
ATOM   3696  C CD2   . LEU B 2 461  ? 171.059 139.480 134.751 1.00 94.91  ? 458  LEU A CD2   1 
ATOM   3697  N N     . LYS B 2 462  ? 175.498 143.644 133.759 1.00 107.06 ? 459  LYS A N     1 
ATOM   3698  C CA    . LYS B 2 462  ? 175.625 145.094 133.839 1.00 106.37 ? 459  LYS A CA    1 
ATOM   3699  C C     . LYS B 2 462  ? 175.161 145.761 132.549 1.00 104.15 ? 459  LYS A C     1 
ATOM   3700  O O     . LYS B 2 462  ? 174.408 146.742 132.582 1.00 100.03 ? 459  LYS A O     1 
ATOM   3701  C CB    . LYS B 2 462  ? 177.071 145.475 134.156 1.00 110.59 ? 459  LYS A CB    1 
ATOM   3702  N N     . LYS B 2 463  ? 175.601 145.247 131.406 1.00 106.81 ? 460  LYS A N     1 
ATOM   3703  C CA    . LYS B 2 463  ? 175.243 145.824 130.119 1.00 106.37 ? 460  LYS A CA    1 
ATOM   3704  C C     . LYS B 2 463  ? 173.959 145.198 129.586 1.00 103.79 ? 460  LYS A C     1 
ATOM   3705  O O     . LYS B 2 463  ? 173.630 144.048 129.892 1.00 105.94 ? 460  LYS A O     1 
ATOM   3706  C CB    . LYS B 2 463  ? 176.373 145.631 129.107 1.00 107.92 ? 460  LYS A CB    1 
ATOM   3707  N N     . GLN B 2 464  ? 173.228 145.976 128.783 1.00 99.44  ? 461  GLN A N     1 
ATOM   3708  C CA    . GLN B 2 464  ? 172.008 145.464 128.168 1.00 94.74  ? 461  GLN A CA    1 
ATOM   3709  C C     . GLN B 2 464  ? 172.315 144.396 127.125 1.00 94.89  ? 461  GLN A C     1 
ATOM   3710  O O     . GLN B 2 464  ? 171.510 143.480 126.924 1.00 91.32  ? 461  GLN A O     1 
ATOM   3711  C CB    . GLN B 2 464  ? 171.214 146.608 127.537 1.00 94.02  ? 461  GLN A CB    1 
ATOM   3712  C CG    . GLN B 2 464  ? 169.864 146.197 126.968 1.00 93.35  ? 461  GLN A CG    1 
ATOM   3713  C CD    . GLN B 2 464  ? 168.871 145.793 128.044 1.00 93.30  ? 461  GLN A CD    1 
ATOM   3714  O OE1   . GLN B 2 464  ? 168.114 144.837 127.878 1.00 93.98  ? 461  GLN A OE1   1 
ATOM   3715  N NE2   . GLN B 2 464  ? 168.871 146.524 129.154 1.00 91.14  ? 461  GLN A NE2   1 
ATOM   3716  N N     . GLU B 2 465  ? 173.469 144.495 126.459 1.00 100.41 ? 462  GLU A N     1 
ATOM   3717  C CA    . GLU B 2 465  ? 173.862 143.464 125.505 1.00 99.85  ? 462  GLU A CA    1 
ATOM   3718  C C     . GLU B 2 465  ? 174.071 142.121 126.192 1.00 98.56  ? 462  GLU A C     1 
ATOM   3719  O O     . GLU B 2 465  ? 173.903 141.070 125.565 1.00 99.86  ? 462  GLU A O     1 
ATOM   3720  C CB    . GLU B 2 465  ? 175.133 143.887 124.767 1.00 99.10  ? 462  GLU A CB    1 
ATOM   3721  N N     . GLU B 2 466  ? 174.431 142.136 127.476 1.00 95.50  ? 463  GLU A N     1 
ATOM   3722  C CA    . GLU B 2 466  ? 174.558 140.900 128.238 1.00 98.40  ? 463  GLU A CA    1 
ATOM   3723  C C     . GLU B 2 466  ? 173.212 140.419 128.766 1.00 97.71  ? 463  GLU A C     1 
ATOM   3724  O O     . GLU B 2 466  ? 173.031 139.215 128.983 1.00 94.71  ? 463  GLU A O     1 
ATOM   3725  C CB    . GLU B 2 466  ? 175.548 141.093 129.388 1.00 103.30 ? 463  GLU A CB    1 
ATOM   3726  C CG    . GLU B 2 466  ? 176.984 141.315 128.930 1.00 108.98 ? 463  GLU A CG    1 
ATOM   3727  C CD    . GLU B 2 466  ? 177.914 141.693 130.069 1.00 112.74 ? 463  GLU A CD    1 
ATOM   3728  O OE1   . GLU B 2 466  ? 177.475 142.426 130.978 1.00 111.64 ? 463  GLU A OE1   1 
ATOM   3729  O OE2   . GLU B 2 466  ? 179.085 141.257 130.050 1.00 115.84 ? 463  GLU A OE2   1 
ATOM   3730  N N     . LYS B 2 467  ? 172.263 141.334 128.984 1.00 100.66 ? 464  LYS A N     1 
ATOM   3731  C CA    . LYS B 2 467  ? 170.908 140.920 129.332 1.00 99.79  ? 464  LYS A CA    1 
ATOM   3732  C C     . LYS B 2 467  ? 170.202 140.281 128.145 1.00 99.19  ? 464  LYS A C     1 
ATOM   3733  O O     . LYS B 2 467  ? 169.374 139.382 128.327 1.00 96.31  ? 464  LYS A O     1 
ATOM   3734  C CB    . LYS B 2 467  ? 170.096 142.114 129.836 1.00 96.47  ? 464  LYS A CB    1 
ATOM   3735  C CG    . LYS B 2 467  ? 170.575 142.709 131.150 1.00 96.26  ? 464  LYS A CG    1 
ATOM   3736  C CD    . LYS B 2 467  ? 169.632 143.810 131.619 1.00 92.50  ? 464  LYS A CD    1 
ATOM   3737  C CE    . LYS B 2 467  ? 170.092 144.424 132.930 1.00 93.21  ? 464  LYS A CE    1 
ATOM   3738  N NZ    . LYS B 2 467  ? 169.146 145.469 133.412 1.00 91.33  ? 464  LYS A NZ    1 
ATOM   3739  N N     . GLU B 2 468  ? 170.518 140.728 126.927 1.00 104.32 ? 465  GLU A N     1 
ATOM   3740  C CA    . GLU B 2 468  ? 169.820 140.230 125.746 1.00 104.58 ? 465  GLU A CA    1 
ATOM   3741  C C     . GLU B 2 468  ? 170.150 138.768 125.477 1.00 102.27 ? 465  GLU A C     1 
ATOM   3742  O O     . GLU B 2 468  ? 169.258 137.980 125.138 1.00 100.21 ? 465  GLU A O     1 
ATOM   3743  C CB    . GLU B 2 468  ? 170.173 141.090 124.534 1.00 109.72 ? 465  GLU A CB    1 
ATOM   3744  C CG    . GLU B 2 468  ? 169.430 140.712 123.267 1.00 112.31 ? 465  GLU A CG    1 
ATOM   3745  C CD    . GLU B 2 468  ? 169.877 141.529 122.071 1.00 116.62 ? 465  GLU A CD    1 
ATOM   3746  O OE1   . GLU B 2 468  ? 170.957 142.152 122.147 1.00 119.43 ? 465  GLU A OE1   1 
ATOM   3747  O OE2   . GLU B 2 468  ? 169.146 141.550 121.059 1.00 116.64 ? 465  GLU A OE2   1 
ATOM   3748  N N     . ILE B 2 469  ? 171.421 138.384 125.621 1.00 100.52 ? 466  ILE A N     1 
ATOM   3749  C CA    . ILE B 2 469  ? 171.802 137.005 125.335 1.00 98.57  ? 466  ILE A CA    1 
ATOM   3750  C C     . ILE B 2 469  ? 171.248 136.056 126.391 1.00 93.64  ? 466  ILE A C     1 
ATOM   3751  O O     . ILE B 2 469  ? 170.984 134.883 126.099 1.00 92.53  ? 466  ILE A O     1 
ATOM   3752  C CB    . ILE B 2 469  ? 173.332 136.882 125.208 1.00 103.21 ? 466  ILE A CB    1 
ATOM   3753  C CG1   . ILE B 2 469  ? 174.030 137.499 126.422 1.00 105.63 ? 466  ILE A CG1   1 
ATOM   3754  C CG2   . ILE B 2 469  ? 173.813 137.540 123.922 1.00 104.37 ? 466  ILE A CG2   1 
ATOM   3755  C CD1   . ILE B 2 469  ? 175.538 137.531 126.301 1.00 109.15 ? 466  ILE A CD1   1 
ATOM   3756  N N     . LEU B 2 470  ? 171.056 136.535 127.622 1.00 89.71  ? 467  LEU A N     1 
ATOM   3757  C CA    . LEU B 2 470  ? 170.395 135.707 128.627 1.00 86.53  ? 467  LEU A CA    1 
ATOM   3758  C C     . LEU B 2 470  ? 168.935 135.468 128.262 1.00 79.99  ? 467  LEU A C     1 
ATOM   3759  O O     . LEU B 2 470  ? 168.429 134.348 128.403 1.00 78.87  ? 467  LEU A O     1 
ATOM   3760  C CB    . LEU B 2 470  ? 170.506 136.356 130.007 1.00 87.22  ? 467  LEU A CB    1 
ATOM   3761  C CG    . LEU B 2 470  ? 169.744 135.650 131.134 1.00 86.75  ? 467  LEU A CG    1 
ATOM   3762  C CD1   . LEU B 2 470  ? 170.243 134.224 131.315 1.00 65.94  ? 467  LEU A CD1   1 
ATOM   3763  C CD2   . LEU B 2 470  ? 169.844 136.428 132.438 1.00 64.76  ? 467  LEU A CD2   1 
ATOM   3764  N N     . LYS B 2 471  ? 168.245 136.508 127.787 1.00 74.89  ? 468  LYS A N     1 
ATOM   3765  C CA    . LYS B 2 471  ? 166.866 136.335 127.342 1.00 70.96  ? 468  LYS A CA    1 
ATOM   3766  C C     . LYS B 2 471  ? 166.800 135.477 126.085 1.00 67.59  ? 468  LYS A C     1 
ATOM   3767  O O     . LYS B 2 471  ? 165.883 134.660 125.931 1.00 65.01  ? 468  LYS A O     1 
ATOM   3768  C CB    . LYS B 2 471  ? 166.217 137.696 127.091 1.00 73.91  ? 468  LYS A CB    1 
ATOM   3769  C CG    . LYS B 2 471  ? 164.774 137.610 126.617 1.00 75.39  ? 468  LYS A CG    1 
ATOM   3770  C CD    . LYS B 2 471  ? 164.368 138.845 125.828 1.00 75.19  ? 468  LYS A CD    1 
ATOM   3771  C CE    . LYS B 2 471  ? 163.036 138.629 125.126 1.00 72.68  ? 468  LYS A CE    1 
ATOM   3772  N NZ    . LYS B 2 471  ? 162.745 139.700 124.133 1.00 71.46  ? 468  LYS A NZ    1 
ATOM   3773  N N     . SER B 2 472  ? 167.766 135.642 125.177 1.00 68.41  ? 469  SER A N     1 
ATOM   3774  C CA    . SER B 2 472  ? 167.755 134.883 123.929 1.00 67.77  ? 469  SER A CA    1 
ATOM   3775  C C     . SER B 2 472  ? 167.875 133.389 124.187 1.00 66.87  ? 469  SER A C     1 
ATOM   3776  O O     . SER B 2 472  ? 167.186 132.583 123.549 1.00 66.10  ? 469  SER A O     1 
ATOM   3777  C CB    . SER B 2 472  ? 168.882 135.363 123.017 1.00 69.74  ? 469  SER A CB    1 
ATOM   3778  O OG    . SER B 2 472  ? 168.913 134.624 121.808 1.00 69.95  ? 469  SER A OG    1 
ATOM   3779  N N     . GLN B 2 473  ? 168.746 132.995 125.120 1.00 68.20  ? 470  GLN A N     1 
ATOM   3780  C CA    . GLN B 2 473  ? 168.887 131.578 125.440 1.00 70.57  ? 470  GLN A CA    1 
ATOM   3781  C C     . GLN B 2 473  ? 167.668 131.048 126.184 1.00 72.83  ? 470  GLN A C     1 
ATOM   3782  O O     . GLN B 2 473  ? 167.295 129.882 126.006 1.00 72.14  ? 470  GLN A O     1 
ATOM   3783  C CB    . GLN B 2 473  ? 170.155 131.349 126.261 1.00 74.11  ? 470  GLN A CB    1 
ATOM   3784  C CG    . GLN B 2 473  ? 171.433 131.737 125.536 1.00 76.56  ? 470  GLN A CG    1 
ATOM   3785  C CD    . GLN B 2 473  ? 172.666 131.568 126.400 1.00 77.40  ? 470  GLN A CD    1 
ATOM   3786  O OE1   . GLN B 2 473  ? 172.646 130.845 127.394 1.00 75.67  ? 470  GLN A OE1   1 
ATOM   3787  N NE2   . GLN B 2 473  ? 173.747 132.241 126.024 1.00 79.94  ? 470  GLN A NE2   1 
ATOM   3788  N N     . LEU B 2 474  ? 167.038 131.880 127.017 1.00 75.55  ? 471  LEU A N     1 
ATOM   3789  C CA    . LEU B 2 474  ? 165.816 131.460 127.692 1.00 77.12  ? 471  LEU A CA    1 
ATOM   3790  C C     . LEU B 2 474  ? 164.655 131.319 126.717 1.00 71.75  ? 471  LEU A C     1 
ATOM   3791  O O     . LEU B 2 474  ? 163.795 130.451 126.901 1.00 71.07  ? 471  LEU A O     1 
ATOM   3792  C CB    . LEU B 2 474  ? 165.461 132.447 128.805 1.00 80.44  ? 471  LEU A CB    1 
ATOM   3793  C CG    . LEU B 2 474  ? 166.326 132.382 130.064 1.00 58.88  ? 471  LEU A CG    1 
ATOM   3794  C CD1   . LEU B 2 474  ? 165.996 133.534 130.994 1.00 60.52  ? 471  LEU A CD1   1 
ATOM   3795  C CD2   . LEU B 2 474  ? 166.127 131.053 130.771 1.00 59.54  ? 471  LEU A CD2   1 
ATOM   3796  N N     . ASP B 2 475  ? 164.609 132.162 125.681 1.00 68.64  ? 472  ASP A N     1 
ATOM   3797  C CA    . ASP B 2 475  ? 163.572 132.021 124.662 1.00 66.28  ? 472  ASP A CA    1 
ATOM   3798  C C     . ASP B 2 475  ? 163.720 130.705 123.911 1.00 66.04  ? 472  ASP A C     1 
ATOM   3799  O O     . ASP B 2 475  ? 162.723 130.052 123.580 1.00 64.97  ? 472  ASP A O     1 
ATOM   3800  C CB    . ASP B 2 475  ? 163.622 133.201 123.689 1.00 68.60  ? 472  ASP A CB    1 
ATOM   3801  C CG    . ASP B 2 475  ? 163.296 134.524 124.357 1.00 73.49  ? 472  ASP A CG    1 
ATOM   3802  O OD1   . ASP B 2 475  ? 162.551 134.525 125.360 1.00 74.30  ? 472  ASP A OD1   1 
ATOM   3803  O OD2   . ASP B 2 475  ? 163.788 135.569 123.877 1.00 76.76  ? 472  ASP A OD2   1 
ATOM   3804  N N     . SER B 2 476  ? 164.962 130.297 123.634 1.00 67.57  ? 473  SER A N     1 
ATOM   3805  C CA    . SER B 2 476  ? 165.189 129.017 122.973 1.00 67.93  ? 473  SER A CA    1 
ATOM   3806  C C     . SER B 2 476  ? 164.807 127.854 123.879 1.00 66.79  ? 473  SER A C     1 
ATOM   3807  O O     . SER B 2 476  ? 164.262 126.847 123.414 1.00 65.37  ? 473  SER A O     1 
ATOM   3808  C CB    . SER B 2 476  ? 166.648 128.906 122.536 1.00 68.89  ? 473  SER A CB    1 
ATOM   3809  O OG    . SER B 2 476  ? 167.023 130.013 121.735 1.00 68.08  ? 473  SER A OG    1 
ATOM   3810  N N     . LEU B 2 477  ? 165.086 127.975 125.180 1.00 67.29  ? 474  LEU A N     1 
ATOM   3811  C CA    . LEU B 2 477  ? 164.697 126.932 126.121 1.00 68.69  ? 474  LEU A CA    1 
ATOM   3812  C C     . LEU B 2 477  ? 163.183 126.875 126.288 1.00 65.97  ? 474  LEU A C     1 
ATOM   3813  O O     . LEU B 2 477  ? 162.601 125.787 126.357 1.00 66.56  ? 474  LEU A O     1 
ATOM   3814  C CB    . LEU B 2 477  ? 165.376 127.156 127.471 1.00 73.32  ? 474  LEU A CB    1 
ATOM   3815  C CG    . LEU B 2 477  ? 166.674 126.386 127.722 1.00 77.31  ? 474  LEU A CG    1 
ATOM   3816  C CD1   . LEU B 2 477  ? 166.399 124.892 127.738 1.00 79.38  ? 474  LEU A CD1   1 
ATOM   3817  C CD2   . LEU B 2 477  ? 167.724 126.724 126.677 1.00 77.75  ? 474  LEU A CD2   1 
ATOM   3818  N N     . LEU B 2 478  ? 162.528 128.038 126.360 1.00 64.71  ? 475  LEU A N     1 
ATOM   3819  C CA    . LEU B 2 478  ? 161.073 128.053 126.455 1.00 62.41  ? 475  LEU A CA    1 
ATOM   3820  C C     . LEU B 2 478  ? 160.427 127.624 125.144 1.00 62.51  ? 475  LEU A C     1 
ATOM   3821  O O     . LEU B 2 478  ? 159.317 127.078 125.151 1.00 62.11  ? 475  LEU A O     1 
ATOM   3822  C CB    . LEU B 2 478  ? 160.585 129.444 126.864 1.00 59.61  ? 475  LEU A CB    1 
ATOM   3823  C CG    . LEU B 2 478  ? 159.120 129.543 127.302 1.00 56.12  ? 475  LEU A CG    1 
ATOM   3824  C CD1   . LEU B 2 478  ? 158.882 128.712 128.551 1.00 57.41  ? 475  LEU A CD1   1 
ATOM   3825  C CD2   . LEU B 2 478  ? 158.713 130.990 127.529 1.00 53.35  ? 475  LEU A CD2   1 
ATOM   3826  N N     . GLY B 2 479  ? 161.099 127.863 124.015 1.00 62.12  ? 476  GLY A N     1 
ATOM   3827  C CA    . GLY B 2 479  ? 160.567 127.412 122.741 1.00 61.59  ? 476  GLY A CA    1 
ATOM   3828  C C     . GLY B 2 479  ? 160.508 125.901 122.641 1.00 64.11  ? 476  GLY A C     1 
ATOM   3829  O O     . GLY B 2 479  ? 159.526 125.337 122.153 1.00 64.88  ? 476  GLY A O     1 
ATOM   3830  N N     . LEU B 2 480  ? 161.560 125.223 123.105 1.00 66.05  ? 477  LEU A N     1 
ATOM   3831  C CA    . LEU B 2 480  ? 161.534 123.764 123.147 1.00 65.05  ? 477  LEU A CA    1 
ATOM   3832  C C     . LEU B 2 480  ? 160.528 123.263 124.173 1.00 64.78  ? 477  LEU A C     1 
ATOM   3833  O O     . LEU B 2 480  ? 159.847 122.256 123.944 1.00 64.93  ? 477  LEU A O     1 
ATOM   3834  C CB    . LEU B 2 480  ? 162.932 123.224 123.450 1.00 64.07  ? 477  LEU A CB    1 
ATOM   3835  C CG    . LEU B 2 480  ? 163.053 121.708 123.590 1.00 63.64  ? 477  LEU A CG    1 
ATOM   3836  C CD1   . LEU B 2 480  ? 162.579 121.012 122.323 1.00 63.27  ? 477  LEU A CD1   1 
ATOM   3837  C CD2   . LEU B 2 480  ? 164.484 121.323 123.915 1.00 66.18  ? 477  LEU A CD2   1 
ATOM   3838  N N     . TYR B 2 481  ? 160.419 123.954 125.312 1.00 65.27  ? 478  TYR A N     1 
ATOM   3839  C CA    . TYR B 2 481  ? 159.418 123.589 126.309 1.00 66.19  ? 478  TYR A CA    1 
ATOM   3840  C C     . TYR B 2 481  ? 158.008 123.777 125.764 1.00 62.10  ? 478  TYR A C     1 
ATOM   3841  O O     . TYR B 2 481  ? 157.106 122.987 126.067 1.00 60.52  ? 478  TYR A O     1 
ATOM   3842  C CB    . TYR B 2 481  ? 159.621 124.414 127.581 1.00 72.60  ? 478  TYR A CB    1 
ATOM   3843  C CG    . TYR B 2 481  ? 158.523 124.249 128.611 1.00 79.32  ? 478  TYR A CG    1 
ATOM   3844  C CD1   . TYR B 2 481  ? 158.501 123.153 129.461 1.00 83.61  ? 478  TYR A CD1   1 
ATOM   3845  C CD2   . TYR B 2 481  ? 157.514 125.197 128.736 1.00 81.64  ? 478  TYR A CD2   1 
ATOM   3846  C CE1   . TYR B 2 481  ? 157.501 123.000 130.404 1.00 85.19  ? 478  TYR A CE1   1 
ATOM   3847  C CE2   . TYR B 2 481  ? 156.510 125.052 129.674 1.00 82.85  ? 478  TYR A CE2   1 
ATOM   3848  C CZ    . TYR B 2 481  ? 156.508 123.953 130.506 1.00 84.32  ? 478  TYR A CZ    1 
ATOM   3849  O OH    . TYR B 2 481  ? 155.511 123.807 131.444 1.00 84.24  ? 478  TYR A OH    1 
ATOM   3850  N N     . HIS B 2 482  ? 157.801 124.822 124.958 1.00 59.93  ? 479  HIS A N     1 
ATOM   3851  C CA    . HIS B 2 482  ? 156.504 125.016 124.316 1.00 57.10  ? 479  HIS A CA    1 
ATOM   3852  C C     . HIS B 2 482  ? 156.214 123.912 123.310 1.00 57.22  ? 479  HIS A C     1 
ATOM   3853  O O     . HIS B 2 482  ? 155.071 123.458 123.189 1.00 57.45  ? 479  HIS A O     1 
ATOM   3854  C CB    . HIS B 2 482  ? 156.455 126.381 123.634 1.00 54.21  ? 479  HIS A CB    1 
ATOM   3855  C CG    . HIS B 2 482  ? 156.201 127.518 124.572 1.00 54.70  ? 479  HIS A CG    1 
ATOM   3856  N ND1   . HIS B 2 482  ? 155.536 127.364 125.768 1.00 55.09  ? 479  HIS A ND1   1 
ATOM   3857  C CD2   . HIS B 2 482  ? 156.531 128.828 124.490 1.00 54.58  ? 479  HIS A CD2   1 
ATOM   3858  C CE1   . HIS B 2 482  ? 155.464 128.530 126.382 1.00 55.29  ? 479  HIS A CE1   1 
ATOM   3859  N NE2   . HIS B 2 482  ? 156.061 129.436 125.628 1.00 54.99  ? 479  HIS A NE2   1 
ATOM   3860  N N     . LEU B 2 483  ? 157.239 123.471 122.579 1.00 58.11  ? 480  LEU A N     1 
ATOM   3861  C CA    . LEU B 2 483  ? 157.034 122.459 121.548 1.00 57.89  ? 480  LEU A CA    1 
ATOM   3862  C C     . LEU B 2 483  ? 156.601 121.129 122.150 1.00 59.17  ? 480  LEU A C     1 
ATOM   3863  O O     . LEU B 2 483  ? 155.741 120.437 121.592 1.00 59.88  ? 480  LEU A O     1 
ATOM   3864  C CB    . LEU B 2 483  ? 158.312 122.290 120.726 1.00 57.68  ? 480  LEU A CB    1 
ATOM   3865  C CG    . LEU B 2 483  ? 158.304 121.216 119.638 1.00 55.56  ? 480  LEU A CG    1 
ATOM   3866  C CD1   . LEU B 2 483  ? 157.197 121.479 118.632 1.00 54.20  ? 480  LEU A CD1   1 
ATOM   3867  C CD2   . LEU B 2 483  ? 159.653 121.147 118.945 1.00 55.50  ? 480  LEU A CD2   1 
ATOM   3868  N N     . LEU B 2 484  ? 157.175 120.758 123.297 1.00 60.00  ? 481  LEU A N     1 
ATOM   3869  C CA    . LEU B 2 484  ? 156.866 119.459 123.889 1.00 60.84  ? 481  LEU A CA    1 
ATOM   3870  C C     . LEU B 2 484  ? 155.438 119.399 124.415 1.00 61.91  ? 481  LEU A C     1 
ATOM   3871  O O     . LEU B 2 484  ? 154.842 118.316 124.457 1.00 65.30  ? 481  LEU A O     1 
ATOM   3872  C CB    . LEU B 2 484  ? 157.859 119.140 125.006 1.00 61.05  ? 481  LEU A CB    1 
ATOM   3873  C CG    . LEU B 2 484  ? 159.321 118.994 124.578 1.00 62.36  ? 481  LEU A CG    1 
ATOM   3874  C CD1   . LEU B 2 484  ? 160.193 118.605 125.763 1.00 65.84  ? 481  LEU A CD1   1 
ATOM   3875  C CD2   . LEU B 2 484  ? 159.459 117.983 123.449 1.00 59.89  ? 481  LEU A CD2   1 
ATOM   3876  N N     . ASP B 2 485  ? 154.872 120.537 124.812 1.00 59.93  ? 482  ASP A N     1 
ATOM   3877  C CA    . ASP B 2 485  ? 153.499 120.582 125.305 1.00 59.54  ? 482  ASP A CA    1 
ATOM   3878  C C     . ASP B 2 485  ? 152.464 120.478 124.191 1.00 59.21  ? 482  ASP A C     1 
ATOM   3879  O O     . ASP B 2 485  ? 151.265 120.602 124.467 1.00 56.86  ? 482  ASP A O     1 
ATOM   3880  C CB    . ASP B 2 485  ? 153.271 121.860 126.113 1.00 60.17  ? 482  ASP A CB    1 
ATOM   3881  C CG    . ASP B 2 485  ? 153.661 121.705 127.570 1.00 64.91  ? 482  ASP A CG    1 
ATOM   3882  O OD1   . ASP B 2 485  ? 154.586 120.918 127.859 1.00 68.43  ? 482  ASP A OD1   1 
ATOM   3883  O OD2   . ASP B 2 485  ? 153.038 122.364 128.429 1.00 66.76  ? 482  ASP A OD2   1 
ATOM   3884  N N     . TRP B 2 486  ? 152.894 120.255 122.948 1.00 59.22  ? 483  TRP A N     1 
ATOM   3885  C CA    . TRP B 2 486  ? 151.944 120.043 121.860 1.00 56.64  ? 483  TRP A CA    1 
ATOM   3886  C C     . TRP B 2 486  ? 151.247 118.694 121.974 1.00 58.54  ? 483  TRP A C     1 
ATOM   3887  O O     . TRP B 2 486  ? 150.112 118.543 121.509 1.00 58.97  ? 483  TRP A O     1 
ATOM   3888  C CB    . TRP B 2 486  ? 152.653 120.147 120.511 1.00 55.98  ? 483  TRP A CB    1 
ATOM   3889  C CG    . TRP B 2 486  ? 153.021 121.540 120.106 1.00 56.90  ? 483  TRP A CG    1 
ATOM   3890  C CD1   . TRP B 2 486  ? 152.943 122.667 120.872 1.00 56.59  ? 483  TRP A CD1   1 
ATOM   3891  C CD2   . TRP B 2 486  ? 153.517 121.955 118.829 1.00 55.97  ? 483  TRP A CD2   1 
ATOM   3892  N NE1   . TRP B 2 486  ? 153.363 123.760 120.151 1.00 54.32  ? 483  TRP A NE1   1 
ATOM   3893  C CE2   . TRP B 2 486  ? 153.721 123.349 118.891 1.00 54.76  ? 483  TRP A CE2   1 
ATOM   3894  C CE3   . TRP B 2 486  ? 153.807 121.284 117.636 1.00 55.78  ? 483  TRP A CE3   1 
ATOM   3895  C CZ2   . TRP B 2 486  ? 154.202 124.083 117.810 1.00 55.30  ? 483  TRP A CZ2   1 
ATOM   3896  C CZ3   . TRP B 2 486  ? 154.286 122.015 116.563 1.00 56.83  ? 483  TRP A CZ3   1 
ATOM   3897  C CH2   . TRP B 2 486  ? 154.479 123.399 116.658 1.00 56.14  ? 483  TRP A CH2   1 
ATOM   3898  N N     . PHE B 2 487  ? 151.902 117.710 122.584 1.00 61.90  ? 484  PHE A N     1 
ATOM   3899  C CA    . PHE B 2 487  ? 151.393 116.348 122.615 1.00 66.86  ? 484  PHE A CA    1 
ATOM   3900  C C     . PHE B 2 487  ? 150.511 116.122 123.835 1.00 74.18  ? 484  PHE A C     1 
ATOM   3901  O O     . PHE B 2 487  ? 150.783 116.646 124.920 1.00 71.55  ? 484  PHE A O     1 
ATOM   3902  C CB    . PHE B 2 487  ? 152.551 115.349 122.610 1.00 67.09  ? 484  PHE A CB    1 
ATOM   3903  C CG    . PHE B 2 487  ? 153.490 115.522 121.450 1.00 65.91  ? 484  PHE A CG    1 
ATOM   3904  C CD1   . PHE B 2 487  ? 153.161 115.034 120.196 1.00 62.18  ? 484  PHE A CD1   1 
ATOM   3905  C CD2   . PHE B 2 487  ? 154.703 116.173 121.615 1.00 67.70  ? 484  PHE A CD2   1 
ATOM   3906  C CE1   . PHE B 2 487  ? 154.023 115.193 119.127 1.00 61.39  ? 484  PHE A CE1   1 
ATOM   3907  C CE2   . PHE B 2 487  ? 155.569 116.333 120.548 1.00 67.20  ? 484  PHE A CE2   1 
ATOM   3908  C CZ    . PHE B 2 487  ? 155.228 115.843 119.303 1.00 63.97  ? 484  PHE A CZ    1 
ATOM   3909  N N     . ALA B 2 488  ? 149.456 115.333 123.648 1.00 83.31  ? 485  ALA A N     1 
ATOM   3910  C CA    . ALA B 2 488  ? 148.530 115.040 124.732 1.00 90.72  ? 485  ALA A CA    1 
ATOM   3911  C C     . ALA B 2 488  ? 149.209 114.208 125.812 1.00 96.80  ? 485  ALA A C     1 
ATOM   3912  O O     . ALA B 2 488  ? 149.963 113.275 125.522 1.00 95.35  ? 485  ALA A O     1 
ATOM   3913  C CB    . ALA B 2 488  ? 147.302 114.304 124.196 1.00 89.57  ? 485  ALA A CB    1 
ATOM   3914  N N     . VAL B 2 489  ? 148.926 114.548 127.068 1.00 105.19 ? 486  VAL A N     1 
ATOM   3915  C CA    . VAL B 2 489  ? 149.577 113.910 128.208 1.00 109.76 ? 486  VAL A CA    1 
ATOM   3916  C C     . VAL B 2 489  ? 148.621 112.916 128.857 1.00 109.59 ? 486  VAL A C     1 
ATOM   3917  O O     . VAL B 2 489  ? 149.055 111.927 129.462 1.00 111.37 ? 486  VAL A O     1 
ATOM   3918  C CB    . VAL B 2 489  ? 150.054 114.962 129.226 1.00 112.13 ? 486  VAL A CB    1 
ATOM   3919  C CG1   . VAL B 2 489  ? 150.982 114.334 130.257 1.00 115.35 ? 486  VAL A CG1   1 
ATOM   3920  C CG2   . VAL B 2 489  ? 150.741 116.115 128.510 1.00 111.13 ? 486  VAL A CG2   1 
ATOM   3921  N N     . ASP B 2 490  ? 147.320 113.166 128.733 1.00 105.19 ? 487  ASP A N     1 
ATOM   3922  C CA    . ASP B 2 490  ? 146.328 112.316 129.377 1.00 105.27 ? 487  ASP A CA    1 
ATOM   3923  C C     . ASP B 2 490  ? 146.394 110.896 128.829 1.00 105.98 ? 487  ASP A C     1 
ATOM   3924  O O     . ASP B 2 490  ? 146.607 110.681 127.633 1.00 106.07 ? 487  ASP A O     1 
ATOM   3925  C CB    . ASP B 2 490  ? 144.925 112.893 129.177 1.00 103.54 ? 487  ASP A CB    1 
ATOM   3926  N N     . GLU B 2 491  ? 146.212 109.923 129.720 1.00 105.09 ? 488  GLU A N     1 
ATOM   3927  C CA    . GLU B 2 491  ? 146.228 108.513 129.353 1.00 101.99 ? 488  GLU A CA    1 
ATOM   3928  C C     . GLU B 2 491  ? 144.920 108.048 128.723 1.00 97.73  ? 488  GLU A C     1 
ATOM   3929  O O     . GLU B 2 491  ? 144.739 106.842 128.523 1.00 97.66  ? 488  GLU A O     1 
ATOM   3930  C CB    . GLU B 2 491  ? 146.547 107.653 130.579 1.00 102.24 ? 488  GLU A CB    1 
ATOM   3931  N N     . SER B 2 492  ? 144.009 108.972 128.417 1.00 93.83  ? 489  SER A N     1 
ATOM   3932  C CA    . SER B 2 492  ? 142.755 108.595 127.772 1.00 90.65  ? 489  SER A CA    1 
ATOM   3933  C C     . SER B 2 492  ? 142.980 108.124 126.340 1.00 89.67  ? 489  SER A C     1 
ATOM   3934  O O     . SER B 2 492  ? 142.174 107.347 125.813 1.00 90.05  ? 489  SER A O     1 
ATOM   3935  C CB    . SER B 2 492  ? 141.778 109.768 127.803 1.00 87.23  ? 489  SER A CB    1 
ATOM   3936  O OG    . SER B 2 492  ? 142.372 110.943 127.279 1.00 83.94  ? 489  SER A OG    1 
ATOM   3937  N N     . ASN B 2 493  ? 144.056 108.568 125.701 1.00 88.83  ? 490  ASN A N     1 
ATOM   3938  C CA    . ASN B 2 493  ? 144.376 108.170 124.340 1.00 87.07  ? 490  ASN A CA    1 
ATOM   3939  C C     . ASN B 2 493  ? 145.332 106.980 124.341 1.00 89.27  ? 490  ASN A C     1 
ATOM   3940  O O     . ASN B 2 493  ? 146.033 106.714 125.321 1.00 88.67  ? 490  ASN A O     1 
ATOM   3941  C CB    . ASN B 2 493  ? 144.998 109.335 123.568 1.00 84.17  ? 490  ASN A CB    1 
ATOM   3942  C CG    . ASN B 2 493  ? 144.295 110.654 123.832 1.00 81.82  ? 490  ASN A CG    1 
ATOM   3943  O OD1   . ASN B 2 493  ? 143.264 110.954 123.230 1.00 80.56  ? 490  ASN A OD1   1 
ATOM   3944  N ND2   . ASN B 2 493  ? 144.858 111.456 124.731 1.00 81.05  ? 490  ASN A ND2   1 
ATOM   3945  N N     . GLU B 2 494  ? 145.353 106.262 123.217 1.00 91.56  ? 491  GLU A N     1 
ATOM   3946  C CA    . GLU B 2 494  ? 146.253 105.123 123.038 1.00 92.54  ? 491  GLU A CA    1 
ATOM   3947  C C     . GLU B 2 494  ? 147.633 105.655 122.665 1.00 94.62  ? 491  GLU A C     1 
ATOM   3948  O O     . GLU B 2 494  ? 148.012 105.747 121.495 1.00 92.87  ? 491  GLU A O     1 
ATOM   3949  C CB    . GLU B 2 494  ? 145.717 104.168 121.981 1.00 88.15  ? 491  GLU A CB    1 
ATOM   3950  C CG    . GLU B 2 494  ? 144.545 103.323 122.446 1.00 85.16  ? 491  GLU A CG    1 
ATOM   3951  C CD    . GLU B 2 494  ? 144.151 102.268 121.431 1.00 83.10  ? 491  GLU A CD    1 
ATOM   3952  O OE1   . GLU B 2 494  ? 144.055 102.606 120.233 1.00 81.29  ? 491  GLU A OE1   1 
ATOM   3953  O OE2   . GLU B 2 494  ? 143.943 101.102 121.829 1.00 84.13  ? 491  GLU A OE2   1 
ATOM   3954  N N     . VAL B 2 495  ? 148.401 106.011 123.694 1.00 100.90 ? 492  VAL A N     1 
ATOM   3955  C CA    . VAL B 2 495  ? 149.730 106.576 123.502 1.00 99.65  ? 492  VAL A CA    1 
ATOM   3956  C C     . VAL B 2 495  ? 150.728 105.463 123.218 1.00 98.55  ? 492  VAL A C     1 
ATOM   3957  O O     . VAL B 2 495  ? 150.563 104.316 123.651 1.00 98.98  ? 492  VAL A O     1 
ATOM   3958  C CB    . VAL B 2 495  ? 150.149 107.408 124.732 1.00 101.24 ? 492  VAL A CB    1 
ATOM   3959  C CG1   . VAL B 2 495  ? 149.265 108.640 124.860 1.00 99.94  ? 492  VAL A CG1   1 
ATOM   3960  C CG2   . VAL B 2 495  ? 150.076 106.559 125.994 1.00 104.30 ? 492  VAL A CG2   1 
ATOM   3961  N N     . ASP B 2 496  ? 151.774 105.806 122.475 1.00 97.18  ? 493  ASP A N     1 
ATOM   3962  C CA    . ASP B 2 496  ? 152.815 104.845 122.153 1.00 96.99  ? 493  ASP A CA    1 
ATOM   3963  C C     . ASP B 2 496  ? 153.567 104.447 123.421 1.00 98.87  ? 493  ASP A C     1 
ATOM   3964  O O     . ASP B 2 496  ? 153.786 105.285 124.301 1.00 100.36 ? 493  ASP A O     1 
ATOM   3965  C CB    . ASP B 2 496  ? 153.782 105.439 121.129 1.00 94.48  ? 493  ASP A CB    1 
ATOM   3966  C CG    . ASP B 2 496  ? 154.773 104.425 120.598 1.00 95.54  ? 493  ASP A CG    1 
ATOM   3967  O OD1   . ASP B 2 496  ? 154.461 103.764 119.586 1.00 94.90  ? 493  ASP A OD1   1 
ATOM   3968  O OD2   . ASP B 2 496  ? 155.866 104.292 121.187 1.00 97.72  ? 493  ASP A OD2   1 
ATOM   3969  N N     . PRO B 2 497  ? 153.953 103.173 123.559 1.00 99.80  ? 494  PRO A N     1 
ATOM   3970  C CA    . PRO B 2 497  ? 154.695 102.751 124.756 1.00 100.18 ? 494  PRO A CA    1 
ATOM   3971  C C     . PRO B 2 497  ? 156.002 103.505 124.940 1.00 97.70  ? 494  PRO A C     1 
ATOM   3972  O O     . PRO B 2 497  ? 156.192 104.194 125.946 1.00 96.91  ? 494  PRO A O     1 
ATOM   3973  C CB    . PRO B 2 497  ? 154.943 101.258 124.503 1.00 103.34 ? 494  PRO A CB    1 
ATOM   3974  C CG    . PRO B 2 497  ? 153.858 100.846 123.568 1.00 101.94 ? 494  PRO A CG    1 
ATOM   3975  C CD    . PRO B 2 497  ? 153.613 102.035 122.687 1.00 99.88  ? 494  PRO A CD    1 
ATOM   3976  N N     . GLU B 2 498  ? 156.906 103.388 123.965 1.00 96.41  ? 495  GLU A N     1 
ATOM   3977  C CA    . GLU B 2 498  ? 158.226 103.994 124.104 1.00 95.14  ? 495  GLU A CA    1 
ATOM   3978  C C     . GLU B 2 498  ? 158.165 105.511 123.972 1.00 92.29  ? 495  GLU A C     1 
ATOM   3979  O O     . GLU B 2 498  ? 158.836 106.230 124.721 1.00 93.51  ? 495  GLU A O     1 
ATOM   3980  C CB    . GLU B 2 498  ? 159.185 103.402 123.070 1.00 95.44  ? 495  GLU A CB    1 
ATOM   3981  N N     . PHE B 2 499  ? 157.364 106.019 123.030 1.00 86.17  ? 496  PHE A N     1 
ATOM   3982  C CA    . PHE B 2 499  ? 157.355 107.454 122.764 1.00 79.92  ? 496  PHE A CA    1 
ATOM   3983  C C     . PHE B 2 499  ? 156.822 108.242 123.953 1.00 76.77  ? 496  PHE A C     1 
ATOM   3984  O O     . PHE B 2 499  ? 157.404 109.265 124.333 1.00 77.69  ? 496  PHE A O     1 
ATOM   3985  C CB    . PHE B 2 499  ? 156.530 107.754 121.513 1.00 75.12  ? 496  PHE A CB    1 
ATOM   3986  C CG    . PHE B 2 499  ? 156.659 109.173 121.026 1.00 72.57  ? 496  PHE A CG    1 
ATOM   3987  C CD1   . PHE B 2 499  ? 155.822 110.168 121.506 1.00 70.92  ? 496  PHE A CD1   1 
ATOM   3988  C CD2   . PHE B 2 499  ? 157.623 109.511 120.089 1.00 73.09  ? 496  PHE A CD2   1 
ATOM   3989  C CE1   . PHE B 2 499  ? 155.941 111.471 121.060 1.00 69.17  ? 496  PHE A CE1   1 
ATOM   3990  C CE2   . PHE B 2 499  ? 157.746 110.814 119.640 1.00 71.51  ? 496  PHE A CE2   1 
ATOM   3991  C CZ    . PHE B 2 499  ? 156.905 111.795 120.127 1.00 69.31  ? 496  PHE A CZ    1 
ATOM   3992  N N     . SER B 2 500  ? 155.719 107.789 124.550 1.00 74.04  ? 497  SER A N     1 
ATOM   3993  C CA    . SER B 2 500  ? 155.147 108.513 125.681 1.00 73.44  ? 497  SER A CA    1 
ATOM   3994  C C     . SER B 2 500  ? 156.075 108.495 126.889 1.00 78.22  ? 497  SER A C     1 
ATOM   3995  O O     . SER B 2 500  ? 156.070 109.441 127.684 1.00 75.81  ? 497  SER A O     1 
ATOM   3996  C CB    . SER B 2 500  ? 153.786 107.927 126.053 1.00 72.94  ? 497  SER A CB    1 
ATOM   3997  O OG    . SER B 2 500  ? 153.205 108.630 127.136 1.00 74.00  ? 497  SER A OG    1 
ATOM   3998  N N     . ALA B 2 501  ? 156.875 107.438 127.043 1.00 83.05  ? 498  ALA A N     1 
ATOM   3999  C CA    . ALA B 2 501  ? 157.797 107.378 128.173 1.00 85.02  ? 498  ALA A CA    1 
ATOM   4000  C C     . ALA B 2 501  ? 158.993 108.298 127.957 1.00 84.98  ? 498  ALA A C     1 
ATOM   4001  O O     . ALA B 2 501  ? 159.407 109.010 128.878 1.00 85.84  ? 498  ALA A O     1 
ATOM   4002  C CB    . ALA B 2 501  ? 158.257 105.938 128.402 1.00 86.72  ? 498  ALA A CB    1 
ATOM   4003  N N     . ARG B 2 502  ? 159.561 108.295 126.748 1.00 85.52  ? 499  ARG A N     1 
ATOM   4004  C CA    . ARG B 2 502  ? 160.703 109.159 126.466 1.00 88.02  ? 499  ARG A CA    1 
ATOM   4005  C C     . ARG B 2 502  ? 160.299 110.627 126.410 1.00 87.53  ? 499  ARG A C     1 
ATOM   4006  O O     . ARG B 2 502  ? 161.089 111.499 126.791 1.00 89.00  ? 499  ARG A O     1 
ATOM   4007  C CB    . ARG B 2 502  ? 161.368 108.744 125.153 1.00 91.14  ? 499  ARG A CB    1 
ATOM   4008  C CG    . ARG B 2 502  ? 161.813 107.293 125.105 1.00 98.39  ? 499  ARG A CG    1 
ATOM   4009  C CD    . ARG B 2 502  ? 162.657 107.025 123.871 1.00 103.76 ? 499  ARG A CD    1 
ATOM   4010  N NE    . ARG B 2 502  ? 163.956 107.683 123.957 1.00 109.77 ? 499  ARG A NE    1 
ATOM   4011  C CZ    . ARG B 2 502  ? 164.817 107.777 122.947 1.00 113.65 ? 499  ARG A CZ    1 
ATOM   4012  N NH1   . ARG B 2 502  ? 164.515 107.260 121.765 1.00 113.83 ? 499  ARG A NH1   1 
ATOM   4013  N NH2   . ARG B 2 502  ? 165.979 108.393 123.121 1.00 115.95 ? 499  ARG A NH2   1 
ATOM   4014  N N     . LEU B 2 503  ? 159.086 110.919 125.937 1.00 86.59  ? 500  LEU A N     1 
ATOM   4015  C CA    . LEU B 2 503  ? 158.626 112.303 125.885 1.00 83.48  ? 500  LEU A CA    1 
ATOM   4016  C C     . LEU B 2 503  ? 158.356 112.842 127.284 1.00 82.48  ? 500  LEU A C     1 
ATOM   4017  O O     . LEU B 2 503  ? 158.775 113.956 127.622 1.00 82.34  ? 500  LEU A O     1 
ATOM   4018  C CB    . LEU B 2 503  ? 157.372 112.408 125.018 1.00 78.20  ? 500  LEU A CB    1 
ATOM   4019  C CG    . LEU B 2 503  ? 156.712 113.785 124.956 1.00 74.84  ? 500  LEU A CG    1 
ATOM   4020  C CD1   . LEU B 2 503  ? 157.671 114.815 124.377 1.00 75.31  ? 500  LEU A CD1   1 
ATOM   4021  C CD2   . LEU B 2 503  ? 155.430 113.729 124.145 1.00 72.65  ? 500  LEU A CD2   1 
ATOM   4022  N N     . THR B 2 504  ? 157.661 112.061 128.115 1.00 82.46  ? 501  THR A N     1 
ATOM   4023  C CA    . THR B 2 504  ? 157.364 112.503 129.474 1.00 83.03  ? 501  THR A CA    1 
ATOM   4024  C C     . THR B 2 504  ? 158.636 112.685 130.293 1.00 83.95  ? 501  THR A C     1 
ATOM   4025  O O     . THR B 2 504  ? 158.665 113.500 131.221 1.00 84.42  ? 501  THR A O     1 
ATOM   4026  C CB    . THR B 2 504  ? 156.431 111.503 130.160 1.00 85.10  ? 501  THR A CB    1 
ATOM   4027  O OG1   . THR B 2 504  ? 155.420 111.079 129.237 1.00 84.13  ? 501  THR A OG1   1 
ATOM   4028  C CG2   . THR B 2 504  ? 155.762 112.139 131.371 1.00 87.44  ? 501  THR A CG2   1 
ATOM   4029  N N     . GLY B 2 505  ? 159.694 111.943 129.961 1.00 85.49  ? 502  GLY A N     1 
ATOM   4030  C CA    . GLY B 2 505  ? 160.947 112.106 130.681 1.00 87.05  ? 502  GLY A CA    1 
ATOM   4031  C C     . GLY B 2 505  ? 161.608 113.441 130.397 1.00 83.65  ? 502  GLY A C     1 
ATOM   4032  O O     . GLY B 2 505  ? 161.968 114.179 131.319 1.00 84.50  ? 502  GLY A O     1 
ATOM   4033  N N     . ILE B 2 506  ? 161.774 113.775 129.115 1.00 80.70  ? 503  ILE A N     1 
ATOM   4034  C CA    . ILE B 2 506  ? 162.397 115.044 128.759 1.00 80.89  ? 503  ILE A CA    1 
ATOM   4035  C C     . ILE B 2 506  ? 161.452 116.217 128.979 1.00 83.11  ? 503  ILE A C     1 
ATOM   4036  O O     . ILE B 2 506  ? 161.911 117.358 129.103 1.00 83.07  ? 503  ILE A O     1 
ATOM   4037  C CB    . ILE B 2 506  ? 162.896 115.013 127.303 1.00 78.19  ? 503  ILE A CB    1 
ATOM   4038  C CG1   . ILE B 2 506  ? 161.725 114.845 126.335 1.00 75.43  ? 503  ILE A CG1   1 
ATOM   4039  C CG2   . ILE B 2 506  ? 163.906 113.895 127.111 1.00 80.82  ? 503  ILE A CG2   1 
ATOM   4040  C CD1   . ILE B 2 506  ? 162.141 114.804 124.881 1.00 74.34  ? 503  ILE A CD1   1 
ATOM   4041  N N     . LYS B 2 507  ? 160.141 115.974 129.029 1.00 85.24  ? 504  LYS A N     1 
ATOM   4042  C CA    . LYS B 2 507  ? 159.206 117.053 129.327 1.00 85.52  ? 504  LYS A CA    1 
ATOM   4043  C C     . LYS B 2 507  ? 159.319 117.492 130.781 1.00 90.70  ? 504  LYS A C     1 
ATOM   4044  O O     . LYS B 2 507  ? 159.248 118.691 131.083 1.00 87.62  ? 504  LYS A O     1 
ATOM   4045  C CB    . LYS B 2 507  ? 157.775 116.619 129.004 1.00 82.62  ? 504  LYS A CB    1 
ATOM   4046  C CG    . LYS B 2 507  ? 156.715 117.655 129.351 1.00 81.76  ? 504  LYS A CG    1 
ATOM   4047  C CD    . LYS B 2 507  ? 155.317 117.183 128.975 1.00 81.05  ? 504  LYS A CD    1 
ATOM   4048  C CE    . LYS B 2 507  ? 155.163 117.043 127.470 1.00 80.65  ? 504  LYS A CE    1 
ATOM   4049  N NZ    . LYS B 2 507  ? 153.765 116.711 127.077 1.00 78.56  ? 504  LYS A NZ    1 
ATOM   4050  N N     . LEU B 2 508  ? 159.502 116.538 131.696 1.00 102.75 ? 505  LEU A N     1 
ATOM   4051  C CA    . LEU B 2 508  ? 159.692 116.869 133.103 1.00 105.40 ? 505  LEU A CA    1 
ATOM   4052  C C     . LEU B 2 508  ? 161.091 117.392 133.397 1.00 107.48 ? 505  LEU A C     1 
ATOM   4053  O O     . LEU B 2 508  ? 161.276 118.105 134.389 1.00 108.38 ? 505  LEU A O     1 
ATOM   4054  C CB    . LEU B 2 508  ? 159.404 115.647 133.981 1.00 107.96 ? 505  LEU A CB    1 
ATOM   4055  C CG    . LEU B 2 508  ? 157.983 115.504 134.538 1.00 110.35 ? 505  LEU A CG    1 
ATOM   4056  C CD1   . LEU B 2 508  ? 156.945 115.447 133.426 1.00 109.49 ? 505  LEU A CD1   1 
ATOM   4057  C CD2   . LEU B 2 508  ? 157.882 114.278 135.435 1.00 113.18 ? 505  LEU A CD2   1 
ATOM   4058  N N     . GLU B 2 509  ? 162.077 117.055 132.564 1.00 102.75 ? 506  GLU A N     1 
ATOM   4059  C CA    . GLU B 2 509  ? 163.422 117.589 132.733 1.00 103.00 ? 506  GLU A CA    1 
ATOM   4060  C C     . GLU B 2 509  ? 163.576 118.978 132.126 1.00 102.90 ? 506  GLU A C     1 
ATOM   4061  O O     . GLU B 2 509  ? 164.543 119.677 132.447 1.00 104.27 ? 506  GLU A O     1 
ATOM   4062  C CB    . GLU B 2 509  ? 164.444 116.626 132.127 1.00 104.08 ? 506  GLU A CB    1 
ATOM   4063  C CG    . GLU B 2 509  ? 164.593 115.333 132.916 1.00 107.41 ? 506  GLU A CG    1 
ATOM   4064  C CD    . GLU B 2 509  ? 165.348 114.259 132.157 1.00 110.86 ? 506  GLU A CD    1 
ATOM   4065  O OE1   . GLU B 2 509  ? 166.322 114.598 131.452 1.00 111.82 ? 506  GLU A OE1   1 
ATOM   4066  O OE2   . GLU B 2 509  ? 164.965 113.074 132.262 1.00 112.85 ? 506  GLU A OE2   1 
ATOM   4067  N N     . MET B 2 510  ? 162.652 119.385 131.258 1.00 101.52 ? 507  MET A N     1 
ATOM   4068  C CA    . MET B 2 510  ? 162.572 120.753 130.767 1.00 100.24 ? 507  MET A CA    1 
ATOM   4069  C C     . MET B 2 510  ? 161.596 121.603 131.570 1.00 102.99 ? 507  MET A C     1 
ATOM   4070  O O     . MET B 2 510  ? 161.477 122.803 131.307 1.00 101.13 ? 507  MET A O     1 
ATOM   4071  C CB    . MET B 2 510  ? 162.163 120.760 129.289 1.00 95.44  ? 507  MET A CB    1 
ATOM   4072  C CG    . MET B 2 510  ? 163.218 120.221 128.337 1.00 94.68  ? 507  MET A CG    1 
ATOM   4073  S SD    . MET B 2 510  ? 164.482 121.440 127.931 1.00 94.39  ? 507  MET A SD    1 
ATOM   4074  C CE    . MET B 2 510  ? 163.476 122.722 127.191 1.00 91.88  ? 507  MET A CE    1 
ATOM   4075  N N     . GLU B 2 511  ? 160.901 121.004 132.535 1.00 112.46 ? 508  GLU A N     1 
ATOM   4076  C CA    . GLU B 2 511  ? 159.924 121.747 133.327 1.00 113.12 ? 508  GLU A CA    1 
ATOM   4077  C C     . GLU B 2 511  ? 160.527 122.880 134.152 1.00 112.73 ? 508  GLU A C     1 
ATOM   4078  O O     . GLU B 2 511  ? 159.911 123.961 134.196 1.00 111.84 ? 508  GLU A O     1 
ATOM   4079  C CB    . GLU B 2 511  ? 159.150 120.765 134.222 1.00 117.39 ? 508  GLU A CB    1 
ATOM   4080  C CG    . GLU B 2 511  ? 158.219 121.416 135.230 1.00 119.48 ? 508  GLU A CG    1 
ATOM   4081  C CD    . GLU B 2 511  ? 157.441 120.396 136.037 1.00 123.38 ? 508  GLU A CD    1 
ATOM   4082  O OE1   . GLU B 2 511  ? 157.013 119.377 135.454 1.00 123.82 ? 508  GLU A OE1   1 
ATOM   4083  O OE2   . GLU B 2 511  ? 157.267 120.605 137.257 1.00 125.81 ? 508  GLU A OE2   1 
ATOM   4084  N N     . PRO B 2 512  ? 161.678 122.729 134.822 1.00 104.02 ? 509  PRO A N     1 
ATOM   4085  C CA    . PRO B 2 512  ? 162.228 123.864 135.585 1.00 99.69  ? 509  PRO A CA    1 
ATOM   4086  C C     . PRO B 2 512  ? 162.606 125.066 134.730 1.00 97.05  ? 509  PRO A C     1 
ATOM   4087  O O     . PRO B 2 512  ? 162.860 126.139 135.293 1.00 98.09  ? 509  PRO A O     1 
ATOM   4088  C CB    . PRO B 2 512  ? 163.464 123.263 136.268 1.00 100.65 ? 509  PRO A CB    1 
ATOM   4089  C CG    . PRO B 2 512  ? 163.181 121.811 136.342 1.00 102.25 ? 509  PRO A CG    1 
ATOM   4090  C CD    . PRO B 2 512  ? 162.443 121.494 135.079 1.00 102.74 ? 509  PRO A CD    1 
ATOM   4091  N N     . SER B 2 513  ? 162.652 124.930 133.402 1.00 91.01  ? 510  SER A N     1 
ATOM   4092  C CA    . SER B 2 513  ? 163.011 126.063 132.555 1.00 83.19  ? 510  SER A CA    1 
ATOM   4093  C C     . SER B 2 513  ? 161.916 127.119 132.500 1.00 75.65  ? 510  SER A C     1 
ATOM   4094  O O     . SER B 2 513  ? 162.212 128.284 132.209 1.00 74.11  ? 510  SER A O     1 
ATOM   4095  C CB    . SER B 2 513  ? 163.345 125.579 131.142 1.00 80.27  ? 510  SER A CB    1 
ATOM   4096  O OG    . SER B 2 513  ? 162.233 124.938 130.544 1.00 77.09  ? 510  SER A OG    1 
ATOM   4097  N N     . LEU B 2 514  ? 160.664 126.745 132.770 1.00 72.35  ? 511  LEU A N     1 
ATOM   4098  C CA    . LEU B 2 514  ? 159.584 127.729 132.768 1.00 69.78  ? 511  LEU A CA    1 
ATOM   4099  C C     . LEU B 2 514  ? 159.720 128.692 133.939 1.00 72.78  ? 511  LEU A C     1 
ATOM   4100  O O     . LEU B 2 514  ? 159.608 129.913 133.768 1.00 73.23  ? 511  LEU A O     1 
ATOM   4101  C CB    . LEU B 2 514  ? 158.228 127.022 132.802 1.00 66.82  ? 511  LEU A CB    1 
ATOM   4102  C CG    . LEU B 2 514  ? 157.001 127.926 132.939 1.00 64.21  ? 511  LEU A CG    1 
ATOM   4103  C CD1   . LEU B 2 514  ? 156.902 128.896 131.768 1.00 62.52  ? 511  LEU A CD1   1 
ATOM   4104  C CD2   . LEU B 2 514  ? 155.734 127.095 133.058 1.00 63.30  ? 511  LEU A CD2   1 
ATOM   4105  N N     . SER B 2 515  ? 159.957 128.163 135.143 1.00 76.44  ? 512  SER A N     1 
ATOM   4106  C CA    . SER B 2 515  ? 160.145 129.031 136.300 1.00 76.70  ? 512  SER A CA    1 
ATOM   4107  C C     . SER B 2 515  ? 161.431 129.836 136.189 1.00 76.20  ? 512  SER A C     1 
ATOM   4108  O O     . SER B 2 515  ? 161.503 130.959 136.703 1.00 76.35  ? 512  SER A O     1 
ATOM   4109  C CB    . SER B 2 515  ? 160.146 128.206 137.587 1.00 79.55  ? 512  SER A CB    1 
ATOM   4110  O OG    . SER B 2 515  ? 161.295 127.382 137.665 1.00 84.44  ? 512  SER A OG    1 
ATOM   4111  N N     . PHE B 2 516  ? 162.452 129.287 135.528 1.00 75.39  ? 513  PHE A N     1 
ATOM   4112  C CA    . PHE B 2 516  ? 163.686 130.040 135.331 1.00 77.38  ? 513  PHE A CA    1 
ATOM   4113  C C     . PHE B 2 516  ? 163.475 131.234 134.412 1.00 75.58  ? 513  PHE A C     1 
ATOM   4114  O O     . PHE B 2 516  ? 164.151 132.259 134.568 1.00 76.28  ? 513  PHE A O     1 
ATOM   4115  C CB    . PHE B 2 516  ? 164.782 129.133 134.776 1.00 80.06  ? 513  PHE A CB    1 
ATOM   4116  C CG    . PHE B 2 516  ? 165.672 128.548 135.833 1.00 84.69  ? 513  PHE A CG    1 
ATOM   4117  C CD1   . PHE B 2 516  ? 165.387 128.735 137.176 1.00 86.32  ? 513  PHE A CD1   1 
ATOM   4118  C CD2   . PHE B 2 516  ? 166.801 127.830 135.486 1.00 86.89  ? 513  PHE A CD2   1 
ATOM   4119  C CE1   . PHE B 2 516  ? 166.206 128.204 138.154 1.00 88.99  ? 513  PHE A CE1   1 
ATOM   4120  C CE2   . PHE B 2 516  ? 167.625 127.298 136.458 1.00 90.26  ? 513  PHE A CE2   1 
ATOM   4121  C CZ    . PHE B 2 516  ? 167.328 127.485 137.793 1.00 91.57  ? 513  PHE A CZ    1 
ATOM   4122  N N     . TYR B 2 517  ? 162.553 131.128 133.454 1.00 74.45  ? 514  TYR A N     1 
ATOM   4123  C CA    . TYR B 2 517  ? 162.226 132.280 132.620 1.00 71.64  ? 514  TYR A CA    1 
ATOM   4124  C C     . TYR B 2 517  ? 161.573 133.379 133.450 1.00 71.61  ? 514  TYR A C     1 
ATOM   4125  O O     . TYR B 2 517  ? 161.948 134.553 133.351 1.00 72.45  ? 514  TYR A O     1 
ATOM   4126  C CB    . TYR B 2 517  ? 161.310 131.856 131.470 1.00 68.42  ? 514  TYR A CB    1 
ATOM   4127  C CG    . TYR B 2 517  ? 161.108 132.930 130.423 1.00 66.16  ? 514  TYR A CG    1 
ATOM   4128  C CD1   . TYR B 2 517  ? 160.137 133.911 130.580 1.00 63.57  ? 514  TYR A CD1   1 
ATOM   4129  C CD2   . TYR B 2 517  ? 161.887 132.961 129.273 1.00 66.60  ? 514  TYR A CD2   1 
ATOM   4130  C CE1   . TYR B 2 517  ? 159.953 134.895 129.628 1.00 62.72  ? 514  TYR A CE1   1 
ATOM   4131  C CE2   . TYR B 2 517  ? 161.709 133.937 128.313 1.00 64.16  ? 514  TYR A CE2   1 
ATOM   4132  C CZ    . TYR B 2 517  ? 160.741 134.902 128.495 1.00 63.61  ? 514  TYR A CZ    1 
ATOM   4133  O OH    . TYR B 2 517  ? 160.562 135.876 127.540 1.00 65.35  ? 514  TYR A OH    1 
ATOM   4134  N N     . ASN B 2 518  ? 160.594 133.014 134.281 1.00 72.31  ? 515  ASN A N     1 
ATOM   4135  C CA    . ASN B 2 518  ? 159.909 134.010 135.094 1.00 73.99  ? 515  ASN A CA    1 
ATOM   4136  C C     . ASN B 2 518  ? 160.816 134.552 136.194 1.00 77.54  ? 515  ASN A C     1 
ATOM   4137  O O     . ASN B 2 518  ? 160.803 135.753 136.478 1.00 79.60  ? 515  ASN A O     1 
ATOM   4138  C CB    . ASN B 2 518  ? 158.631 133.419 135.687 1.00 74.88  ? 515  ASN A CB    1 
ATOM   4139  C CG    . ASN B 2 518  ? 157.534 133.248 134.654 1.00 73.59  ? 515  ASN A CG    1 
ATOM   4140  O OD1   . ASN B 2 518  ? 157.407 134.053 133.730 1.00 72.82  ? 515  ASN A OD1   1 
ATOM   4141  N ND2   . ASN B 2 518  ? 156.734 132.198 134.803 1.00 73.12  ? 515  ASN A ND2   1 
ATOM   4142  N N     . LYS B 2 519  ? 161.687 133.722 136.760 1.00 78.53  ? 516  LYS A N     1 
ATOM   4143  C CA    . LYS B 2 519  ? 162.509 134.282 137.863 1.00 78.99  ? 516  LYS A CA    1 
ATOM   4144  C C     . LYS B 2 519  ? 163.440 135.321 137.264 1.00 77.73  ? 516  LYS A C     1 
ATOM   4145  O O     . LYS B 2 519  ? 163.502 136.465 137.785 1.00 76.91  ? 516  LYS A O     1 
ATOM   4146  C CB    . LYS B 2 519  ? 163.351 133.218 138.563 1.00 83.53  ? 516  LYS A CB    1 
ATOM   4147  C CG    . LYS B 2 519  ? 162.568 132.178 139.351 1.00 86.21  ? 516  LYS A CG    1 
ATOM   4148  C CD    . LYS B 2 519  ? 163.342 130.895 139.563 1.00 92.12  ? 516  LYS A CD    1 
ATOM   4149  C CE    . LYS B 2 519  ? 162.495 129.779 140.136 1.00 93.79  ? 516  LYS A CE    1 
ATOM   4150  N NZ    . LYS B 2 519  ? 163.234 128.495 140.174 1.00 96.57  ? 516  LYS A NZ    1 
ATOM   4151  N N     . ALA B 2 520  ? 164.084 134.965 136.170 1.00 76.46  ? 517  ALA A N     1 
ATOM   4152  C CA    . ALA B 2 520  ? 165.071 135.903 135.611 1.00 74.11  ? 517  ALA A CA    1 
ATOM   4153  C C     . ALA B 2 520  ? 164.371 137.200 135.207 1.00 71.48  ? 517  ALA A C     1 
ATOM   4154  O O     . ALA B 2 520  ? 164.954 138.277 135.452 1.00 73.72  ? 517  ALA A O     1 
ATOM   4155  C CB    . ALA B 2 520  ? 165.770 135.273 134.438 1.00 71.01  ? 517  ALA A CB    1 
ATOM   4156  N N     . ARG B 2 521  ? 163.172 137.116 134.629 1.00 74.05  ? 518  ARG A N     1 
ATOM   4157  C CA    . ARG B 2 521  ? 162.551 138.369 134.141 1.00 74.05  ? 518  ARG A CA    1 
ATOM   4158  C C     . ARG B 2 521  ? 162.254 139.288 135.331 1.00 74.05  ? 518  ARG A C     1 
ATOM   4159  O O     . ARG B 2 521  ? 162.538 140.493 135.214 1.00 74.05  ? 518  ARG A O     1 
ATOM   4160  C CB    . ARG B 2 521  ? 161.293 138.074 133.335 1.00 74.05  ? 518  ARG A CB    1 
ATOM   4161  C CG    . ARG B 2 521  ? 160.561 139.315 132.847 1.00 74.05  ? 518  ARG A CG    1 
ATOM   4162  C CD    . ARG B 2 521  ? 159.244 139.527 133.567 1.00 74.05  ? 518  ARG A CD    1 
ATOM   4163  N NE    . ARG B 2 521  ? 158.450 138.307 133.592 1.00 74.05  ? 518  ARG A NE    1 
ATOM   4164  C CZ    . ARG B 2 521  ? 157.659 137.904 132.608 1.00 74.05  ? 518  ARG A CZ    1 
ATOM   4165  N NH1   . ARG B 2 521  ? 157.553 138.621 131.504 1.00 74.05  ? 518  ARG A NH1   1 
ATOM   4166  N NH2   . ARG B 2 521  ? 156.981 136.777 132.727 1.00 74.05  ? 518  ARG A NH2   1 
ATOM   4167  N N     . ASN B 2 522  ? 161.733 138.746 136.432 1.00 66.70  ? 519  ASN A N     1 
ATOM   4168  C CA    . ASN B 2 522  ? 161.402 139.567 137.618 1.00 66.70  ? 519  ASN A CA    1 
ATOM   4169  C C     . ASN B 2 522  ? 162.675 140.129 138.192 1.00 66.70  ? 519  ASN A C     1 
ATOM   4170  O O     . ASN B 2 522  ? 162.648 141.264 138.635 1.00 66.70  ? 519  ASN A O     1 
ATOM   4171  C CB    . ASN B 2 522  ? 160.725 138.774 138.719 1.00 66.70  ? 519  ASN A CB    1 
ATOM   4172  C CG    . ASN B 2 522  ? 159.414 138.159 138.275 1.00 66.70  ? 519  ASN A CG    1 
ATOM   4173  O OD1   . ASN B 2 522  ? 158.755 138.674 137.375 1.00 66.70  ? 519  ASN A OD1   1 
ATOM   4174  N ND2   . ASN B 2 522  ? 159.024 137.063 138.906 1.00 66.70  ? 519  ASN A ND2   1 
ATOM   4175  N N     . TYR B 2 523  ? 163.744 139.360 138.186 1.00 73.24  ? 520  TYR A N     1 
ATOM   4176  C CA    . TYR B 2 523  ? 165.012 139.971 138.651 1.00 73.24  ? 520  TYR A CA    1 
ATOM   4177  C C     . TYR B 2 523  ? 165.389 141.204 137.829 1.00 73.24  ? 520  TYR A C     1 
ATOM   4178  O O     . TYR B 2 523  ? 165.935 142.137 138.433 1.00 73.24  ? 520  TYR A O     1 
ATOM   4179  C CB    . TYR B 2 523  ? 166.205 139.028 138.554 1.00 73.24  ? 520  TYR A CB    1 
ATOM   4180  C CG    . TYR B 2 523  ? 167.519 139.737 138.762 1.00 73.24  ? 520  TYR A CG    1 
ATOM   4181  C CD1   . TYR B 2 523  ? 167.965 140.036 140.035 1.00 73.24  ? 520  TYR A CD1   1 
ATOM   4182  C CD2   . TYR B 2 523  ? 168.293 140.148 137.691 1.00 73.24  ? 520  TYR A CD2   1 
ATOM   4183  C CE1   . TYR B 2 523  ? 169.159 140.701 140.244 1.00 73.24  ? 520  TYR A CE1   1 
ATOM   4184  C CE2   . TYR B 2 523  ? 169.489 140.813 137.882 1.00 73.24  ? 520  TYR A CE2   1 
ATOM   4185  C CZ    . TYR B 2 523  ? 169.921 141.092 139.163 1.00 73.24  ? 520  TYR A CZ    1 
ATOM   4186  O OH    . TYR B 2 523  ? 171.094 141.755 139.367 1.00 73.24  ? 520  TYR A OH    1 
ATOM   4187  N N     . ALA B 2 524  ? 165.111 141.250 136.521 1.00 61.85  ? 521  ALA A N     1 
ATOM   4188  C CA    . ALA B 2 524  ? 165.590 142.381 135.736 1.00 61.85  ? 521  ALA A CA    1 
ATOM   4189  C C     . ALA B 2 524  ? 164.587 143.527 135.725 1.00 61.85  ? 521  ALA A C     1 
ATOM   4190  O O     . ALA B 2 524  ? 164.978 144.689 135.573 1.00 61.85  ? 521  ALA A O     1 
ATOM   4191  C CB    . ALA B 2 524  ? 165.904 141.934 134.309 1.00 61.85  ? 521  ALA A CB    1 
ATOM   4192  N N     . THR B 2 525  ? 163.298 143.226 135.886 1.00 60.62  ? 522  THR A N     1 
ATOM   4193  C CA    . THR B 2 525  ? 162.269 144.256 135.858 1.00 60.62  ? 522  THR A CA    1 
ATOM   4194  C C     . THR B 2 525  ? 161.972 144.849 137.229 1.00 60.62  ? 522  THR A C     1 
ATOM   4195  O O     . THR B 2 525  ? 161.180 145.794 137.313 1.00 60.62  ? 522  THR A O     1 
ATOM   4196  C CB    . THR B 2 525  ? 160.975 143.697 135.262 1.00 60.62  ? 522  THR A CB    1 
ATOM   4197  O OG1   . THR B 2 525  ? 160.483 142.637 136.091 1.00 60.62  ? 522  THR A OG1   1 
ATOM   4198  C CG2   . THR B 2 525  ? 161.220 143.166 133.859 1.00 60.62  ? 522  THR A CG2   1 
ATOM   4199  N N     . LYS B 2 526  ? 162.574 144.330 138.296 1.00 55.13  ? 523  LYS A N     1 
ATOM   4200  C CA    . LYS B 2 526  ? 162.297 144.857 139.623 1.00 55.13  ? 523  LYS A CA    1 
ATOM   4201  C C     . LYS B 2 526  ? 162.941 146.227 139.798 1.00 55.13  ? 523  LYS A C     1 
ATOM   4202  O O     . LYS B 2 526  ? 163.970 146.541 139.193 1.00 55.13  ? 523  LYS A O     1 
ATOM   4203  C CB    . LYS B 2 526  ? 162.801 143.902 140.706 1.00 55.13  ? 523  LYS A CB    1 
ATOM   4204  C CG    . LYS B 2 526  ? 164.308 143.900 140.895 1.00 55.13  ? 523  LYS A CG    1 
ATOM   4205  C CD    . LYS B 2 526  ? 164.691 143.449 142.295 1.00 55.13  ? 523  LYS A CD    1 
ATOM   4206  C CE    . LYS B 2 526  ? 166.201 143.414 142.470 1.00 55.13  ? 523  LYS A CE    1 
ATOM   4207  N NZ    . LYS B 2 526  ? 166.861 144.588 141.835 1.00 55.13  ? 523  LYS A NZ    1 
ATOM   4208  N N     . LYS B 2 527  ? 162.314 147.051 140.629 1.00 48.55  ? 524  LYS A N     1 
ATOM   4209  C CA    . LYS B 2 527  ? 162.840 148.367 140.936 1.00 48.55  ? 524  LYS A CA    1 
ATOM   4210  C C     . LYS B 2 527  ? 164.041 148.258 141.870 1.00 48.55  ? 524  LYS A C     1 
ATOM   4211  O O     . LYS B 2 527  ? 164.170 147.288 142.621 1.00 48.55  ? 524  LYS A O     1 
ATOM   4212  C CB    . LYS B 2 527  ? 161.751 149.230 141.563 1.00 42.47  ? 524  LYS A CB    1 
ATOM   4213  C CG    . LYS B 2 527  ? 160.521 149.403 140.689 1.00 42.47  ? 524  LYS A CG    1 
ATOM   4214  C CD    . LYS B 2 527  ? 159.285 149.697 141.522 1.00 42.47  ? 524  LYS A CD    1 
ATOM   4215  C CE    . LYS B 2 527  ? 158.032 149.701 140.662 1.00 42.47  ? 524  LYS A CE    1 
ATOM   4216  N NZ    . LYS B 2 527  ? 157.474 148.332 140.484 1.00 42.47  ? 524  LYS A NZ    1 
ATOM   4217  N N     . PRO B 2 528  ? 164.939 149.247 141.847 1.00 48.55  ? 525  PRO A N     1 
ATOM   4218  C CA    . PRO B 2 528  ? 166.154 149.155 142.669 1.00 48.55  ? 525  PRO A CA    1 
ATOM   4219  C C     . PRO B 2 528  ? 165.912 149.397 144.151 1.00 48.55  ? 525  PRO A C     1 
ATOM   4220  O O     . PRO B 2 528  ? 166.871 149.532 144.917 1.00 48.55  ? 525  PRO A O     1 
ATOM   4221  C CB    . PRO B 2 528  ? 167.063 150.243 142.080 1.00 48.55  ? 525  PRO A CB    1 
ATOM   4222  C CG    . PRO B 2 528  ? 166.462 150.599 140.758 1.00 48.55  ? 525  PRO A CG    1 
ATOM   4223  C CD    . PRO B 2 528  ? 164.998 150.378 140.907 1.00 48.55  ? 525  PRO A CD    1 
ATOM   4224  N N     . TYR B 2 529  ? 164.653 149.454 144.576 1.00 48.55  ? 526  TYR A N     1 
ATOM   4225  C CA    . TYR B 2 529  ? 164.351 149.738 145.971 1.00 48.55  ? 526  TYR A CA    1 
ATOM   4226  C C     . TYR B 2 529  ? 164.310 148.434 146.762 1.00 48.55  ? 526  TYR A C     1 
ATOM   4227  O O     . TYR B 2 529  ? 164.696 147.364 146.282 1.00 48.55  ? 526  TYR A O     1 
ATOM   4228  C CB    . TYR B 2 529  ? 163.021 150.472 146.108 1.00 48.55  ? 526  TYR A CB    1 
ATOM   4229  C CG    . TYR B 2 529  ? 162.744 151.498 145.044 1.00 48.55  ? 526  TYR A CG    1 
ATOM   4230  C CD1   . TYR B 2 529  ? 163.562 152.602 144.879 1.00 48.55  ? 526  TYR A CD1   1 
ATOM   4231  C CD2   . TYR B 2 529  ? 161.625 151.383 144.233 1.00 48.55  ? 526  TYR A CD2   1 
ATOM   4232  C CE1   . TYR B 2 529  ? 163.293 153.542 143.909 1.00 48.55  ? 526  TYR A CE1   1 
ATOM   4233  C CE2   . TYR B 2 529  ? 161.345 152.316 143.265 1.00 48.55  ? 526  TYR A CE2   1 
ATOM   4234  C CZ    . TYR B 2 529  ? 162.181 153.396 143.106 1.00 48.55  ? 526  TYR A CZ    1 
ATOM   4235  O OH    . TYR B 2 529  ? 161.903 154.333 142.138 1.00 48.55  ? 526  TYR A OH    1 
ATOM   4236  N N     . SER B 2 530  ? 163.831 148.523 148.001 1.00 48.55  ? 527  SER A N     1 
ATOM   4237  C CA    . SER B 2 530  ? 163.430 147.353 148.781 1.00 48.55  ? 527  SER A CA    1 
ATOM   4238  C C     . SER B 2 530  ? 162.262 147.810 149.657 1.00 48.55  ? 527  SER A C     1 
ATOM   4239  O O     . SER B 2 530  ? 162.460 148.333 150.756 1.00 48.55  ? 527  SER A O     1 
ATOM   4240  C CB    . SER B 2 530  ? 164.577 146.794 149.606 1.00 48.55  ? 527  SER A CB    1 
ATOM   4241  O OG    . SER B 2 530  ? 165.677 146.454 148.780 1.00 48.55  ? 527  SER A OG    1 
ATOM   4242  N N     . VAL B 2 531  ? 161.045 147.605 149.148 1.00 48.55  ? 528  VAL A N     1 
ATOM   4243  C CA    . VAL B 2 531  ? 159.837 148.044 149.844 1.00 48.55  ? 528  VAL A CA    1 
ATOM   4244  C C     . VAL B 2 531  ? 159.492 147.134 151.012 1.00 48.55  ? 528  VAL A C     1 
ATOM   4245  O O     . VAL B 2 531  ? 158.583 147.450 151.791 1.00 48.55  ? 528  VAL A O     1 
ATOM   4246  C CB    . VAL B 2 531  ? 158.698 148.142 148.809 1.00 48.55  ? 528  VAL A CB    1 
ATOM   4247  C CG1   . VAL B 2 531  ? 157.426 148.731 149.411 1.00 48.55  ? 528  VAL A CG1   1 
ATOM   4248  C CG2   . VAL B 2 531  ? 159.148 148.963 147.611 1.00 48.55  ? 528  VAL A CG2   1 
ATOM   4249  N N     . GLU B 2 532  ? 160.217 146.029 151.177 1.00 48.55  ? 529  GLU A N     1 
ATOM   4250  C CA    . GLU B 2 532  ? 159.959 145.115 152.281 1.00 48.55  ? 529  GLU A CA    1 
ATOM   4251  C C     . GLU B 2 532  ? 160.096 145.833 153.618 1.00 48.55  ? 529  GLU A C     1 
ATOM   4252  O O     . GLU B 2 532  ? 160.957 146.698 153.796 1.00 48.55  ? 529  GLU A O     1 
ATOM   4253  C CB    . GLU B 2 532  ? 160.909 143.916 152.204 1.00 48.55  ? 529  GLU A CB    1 
ATOM   4254  C CG    . GLU B 2 532  ? 162.386 144.262 152.018 1.00 48.55  ? 529  GLU A CG    1 
ATOM   4255  C CD    . GLU B 2 532  ? 163.075 144.683 153.303 1.00 48.55  ? 529  GLU A CD    1 
ATOM   4256  O OE1   . GLU B 2 532  ? 162.575 144.336 154.393 1.00 48.55  ? 529  GLU A OE1   1 
ATOM   4257  O OE2   . GLU B 2 532  ? 164.127 145.352 153.221 1.00 48.55  ? 529  GLU A OE2   1 
ATOM   4258  N N     . LYS B 2 533  ? 159.219 145.481 154.554 1.00 48.55  ? 530  LYS A N     1 
ATOM   4259  C CA    . LYS B 2 533  ? 159.146 146.165 155.834 1.00 48.55  ? 530  LYS A CA    1 
ATOM   4260  C C     . LYS B 2 533  ? 158.521 145.234 156.861 1.00 48.55  ? 530  LYS A C     1 
ATOM   4261  O O     . LYS B 2 533  ? 157.811 144.286 156.517 1.00 48.55  ? 530  LYS A O     1 
ATOM   4262  C CB    . LYS B 2 533  ? 158.343 147.464 155.719 1.00 48.55  ? 530  LYS A CB    1 
ATOM   4263  C CG    . LYS B 2 533  ? 156.890 147.246 155.340 1.00 48.55  ? 530  LYS A CG    1 
ATOM   4264  C CD    . LYS B 2 533  ? 156.157 148.562 155.169 1.00 48.55  ? 530  LYS A CD    1 
ATOM   4265  C CE    . LYS B 2 533  ? 154.699 148.331 154.818 1.00 48.55  ? 530  LYS A CE    1 
ATOM   4266  N NZ    . LYS B 2 533  ? 154.547 147.717 153.472 1.00 48.55  ? 530  LYS A NZ    1 
ATOM   4267  N N     . PHE B 2 534  ? 158.793 145.517 158.132 1.00 48.55  ? 531  PHE A N     1 
ATOM   4268  C CA    . PHE B 2 534  ? 158.273 144.725 159.235 1.00 48.55  ? 531  PHE A CA    1 
ATOM   4269  C C     . PHE B 2 534  ? 157.542 145.632 160.211 1.00 48.55  ? 531  PHE A C     1 
ATOM   4270  O O     . PHE B 2 534  ? 157.959 146.769 160.448 1.00 48.55  ? 531  PHE A O     1 
ATOM   4271  C CB    . PHE B 2 534  ? 159.390 143.958 159.957 1.00 48.55  ? 531  PHE A CB    1 
ATOM   4272  C CG    . PHE B 2 534  ? 160.562 144.808 160.357 1.00 48.55  ? 531  PHE A CG    1 
ATOM   4273  C CD1   . PHE B 2 534  ? 160.579 145.457 161.579 1.00 48.55  ? 531  PHE A CD1   1 
ATOM   4274  C CD2   . PHE B 2 534  ? 161.655 144.940 159.519 1.00 48.55  ? 531  PHE A CD2   1 
ATOM   4275  C CE1   . PHE B 2 534  ? 161.658 146.232 161.952 1.00 48.55  ? 531  PHE A CE1   1 
ATOM   4276  C CE2   . PHE B 2 534  ? 162.736 145.712 159.887 1.00 48.55  ? 531  PHE A CE2   1 
ATOM   4277  C CZ    . PHE B 2 534  ? 162.737 146.359 161.105 1.00 48.55  ? 531  PHE A CZ    1 
ATOM   4278  N N     . LYS B 2 535  ? 156.450 145.124 160.772 1.00 48.55  ? 532  LYS A N     1 
ATOM   4279  C CA    . LYS B 2 535  ? 155.610 145.928 161.643 1.00 48.55  ? 532  LYS A CA    1 
ATOM   4280  C C     . LYS B 2 535  ? 156.258 146.104 163.010 1.00 48.55  ? 532  LYS A C     1 
ATOM   4281  O O     . LYS B 2 535  ? 157.003 145.244 163.488 1.00 48.55  ? 532  LYS A O     1 
ATOM   4282  C CB    . LYS B 2 535  ? 154.225 145.296 161.791 1.00 48.55  ? 532  LYS A CB    1 
ATOM   4283  C CG    . LYS B 2 535  ? 154.119 144.236 162.871 1.00 48.55  ? 532  LYS A CG    1 
ATOM   4284  C CD    . LYS B 2 535  ? 152.772 143.535 162.820 1.00 48.55  ? 532  LYS A CD    1 
ATOM   4285  C CE    . LYS B 2 535  ? 151.633 144.510 163.059 1.00 48.55  ? 532  LYS A CE    1 
ATOM   4286  N NZ    . LYS B 2 535  ? 151.637 145.038 164.450 1.00 48.55  ? 532  LYS A NZ    1 
ATOM   4287  N N     . LEU B 2 536  ? 155.979 147.247 163.628 1.00 48.55  ? 533  LEU A N     1 
ATOM   4288  C CA    . LEU B 2 536  ? 156.474 147.565 164.958 1.00 48.55  ? 533  LEU A CA    1 
ATOM   4289  C C     . LEU B 2 536  ? 155.362 147.368 165.978 1.00 48.55  ? 533  LEU A C     1 
ATOM   4290  O O     . LEU B 2 536  ? 154.238 147.842 165.786 1.00 48.55  ? 533  LEU A O     1 
ATOM   4291  C CB    . LEU B 2 536  ? 156.993 149.001 165.022 1.00 48.55  ? 533  LEU A CB    1 
ATOM   4292  C CG    . LEU B 2 536  ? 158.089 149.377 164.027 1.00 48.55  ? 533  LEU A CG    1 
ATOM   4293  C CD1   . LEU B 2 536  ? 158.458 150.839 164.180 1.00 48.55  ? 533  LEU A CD1   1 
ATOM   4294  C CD2   . LEU B 2 536  ? 159.309 148.492 164.213 1.00 48.55  ? 533  LEU A CD2   1 
ATOM   4295  N N     . ASN B 2 537  ? 155.682 146.666 167.064 1.00 48.55  ? 534  ASN A N     1 
ATOM   4296  C CA    . ASN B 2 537  ? 154.710 146.366 168.101 1.00 48.55  ? 534  ASN A CA    1 
ATOM   4297  C C     . ASN B 2 537  ? 155.002 147.029 169.436 1.00 48.55  ? 534  ASN A C     1 
ATOM   4298  O O     . ASN B 2 537  ? 154.076 147.176 170.241 1.00 48.55  ? 534  ASN A O     1 
ATOM   4299  C CB    . ASN B 2 537  ? 154.612 144.848 168.320 1.00 48.55  ? 534  ASN A CB    1 
ATOM   4300  C CG    . ASN B 2 537  ? 153.852 144.152 167.213 1.00 48.55  ? 534  ASN A CG    1 
ATOM   4301  O OD1   . ASN B 2 537  ? 153.121 144.786 166.453 1.00 48.55  ? 534  ASN A OD1   1 
ATOM   4302  N ND2   . ASN B 2 537  ? 154.025 142.840 167.111 1.00 48.55  ? 534  ASN A ND2   1 
ATOM   4303  N N     . PHE B 2 538  ? 156.249 147.427 169.695 1.00 48.55  ? 535  PHE A N     1 
ATOM   4304  C CA    . PHE B 2 538  ? 156.640 148.047 170.960 1.00 48.55  ? 535  PHE A CA    1 
ATOM   4305  C C     . PHE B 2 538  ? 156.262 147.178 172.156 1.00 48.55  ? 535  PHE A C     1 
ATOM   4306  O O     . PHE B 2 538  ? 155.872 147.688 173.210 1.00 48.55  ? 535  PHE A O     1 
ATOM   4307  C CB    . PHE B 2 538  ? 156.043 149.450 171.102 1.00 48.55  ? 535  PHE A CB    1 
ATOM   4308  C CG    . PHE B 2 538  ? 156.503 150.414 170.047 1.00 48.55  ? 535  PHE A CG    1 
ATOM   4309  C CD1   . PHE B 2 538  ? 157.652 151.162 170.229 1.00 48.55  ? 535  PHE A CD1   1 
ATOM   4310  C CD2   . PHE B 2 538  ? 155.785 150.577 168.876 1.00 48.55  ? 535  PHE A CD2   1 
ATOM   4311  C CE1   . PHE B 2 538  ? 158.078 152.051 169.263 1.00 48.55  ? 535  PHE A CE1   1 
ATOM   4312  C CE2   . PHE B 2 538  ? 156.206 151.466 167.906 1.00 48.55  ? 535  PHE A CE2   1 
ATOM   4313  C CZ    . PHE B 2 538  ? 157.354 152.204 168.101 1.00 48.55  ? 535  PHE A CZ    1 
ATOM   4314  N N     . GLN B 2 539  ? 156.373 145.858 171.989 1.00 48.55  ? 536  GLN A N     1 
ATOM   4315  C CA    . GLN B 2 539  ? 156.089 144.880 173.040 1.00 48.55  ? 536  GLN A CA    1 
ATOM   4316  C C     . GLN B 2 539  ? 154.645 144.962 173.529 1.00 48.55  ? 536  GLN A C     1 
ATOM   4317  O O     . GLN B 2 539  ? 154.340 144.576 174.660 1.00 48.55  ? 536  GLN A O     1 
ATOM   4318  C CB    . GLN B 2 539  ? 157.061 145.027 174.215 1.00 48.55  ? 536  GLN A CB    1 
ATOM   4319  C CG    . GLN B 2 539  ? 158.523 145.090 173.806 1.00 48.55  ? 536  GLN A CG    1 
ATOM   4320  C CD    . GLN B 2 539  ? 159.225 143.754 173.939 1.00 48.55  ? 536  GLN A CD    1 
ATOM   4321  O OE1   . GLN B 2 539  ? 158.582 142.709 174.041 1.00 48.55  ? 536  GLN A OE1   1 
ATOM   4322  N NE2   . GLN B 2 539  ? 160.552 143.782 173.939 1.00 48.55  ? 536  GLN A NE2   1 
ATOM   4323  N N     . MET B 2 540  ? 153.743 145.466 172.688 1.00 48.55  ? 537  MET A N     1 
ATOM   4324  C CA    . MET B 2 540  ? 152.322 145.525 173.017 1.00 48.55  ? 537  MET A CA    1 
ATOM   4325  C C     . MET B 2 540  ? 151.507 144.794 171.961 1.00 48.55  ? 537  MET A C     1 
ATOM   4326  O O     . MET B 2 540  ? 151.391 145.276 170.824 1.00 48.55  ? 537  MET A O     1 
ATOM   4327  C CB    . MET B 2 540  ? 151.856 146.977 173.148 1.00 48.55  ? 537  MET A CB    1 
ATOM   4328  C CG    . MET B 2 540  ? 152.436 147.673 174.360 1.00 48.55  ? 537  MET A CG    1 
ATOM   4329  S SD    . MET B 2 540  ? 152.792 149.419 174.140 1.00 48.55  ? 537  MET A SD    1 
ATOM   4330  C CE    . MET B 2 540  ? 153.073 149.881 175.846 1.00 48.55  ? 537  MET A CE    1 
ATOM   4331  N N     . PRO B 2 541  ? 150.943 143.625 172.276 1.00 48.55  ? 538  PRO A N     1 
ATOM   4332  C CA    . PRO B 2 541  ? 150.142 142.902 171.274 1.00 48.55  ? 538  PRO A CA    1 
ATOM   4333  C C     . PRO B 2 541  ? 148.997 143.716 170.698 1.00 48.55  ? 538  PRO A C     1 
ATOM   4334  O O     . PRO B 2 541  ? 148.699 143.586 169.504 1.00 48.55  ? 538  PRO A O     1 
ATOM   4335  C CB    . PRO B 2 541  ? 149.615 141.686 172.049 1.00 48.55  ? 538  PRO A CB    1 
ATOM   4336  C CG    . PRO B 2 541  ? 150.374 141.634 173.341 1.00 48.55  ? 538  PRO A CG    1 
ATOM   4337  C CD    . PRO B 2 541  ? 151.344 142.768 173.401 1.00 48.55  ? 538  PRO A CD    1 
ATOM   4338  N N     . THR B 2 542  ? 148.347 144.551 171.502 1.00 48.55  ? 539  THR A N     1 
ATOM   4339  C CA    . THR B 2 542  ? 147.146 145.268 171.092 1.00 48.55  ? 539  THR A CA    1 
ATOM   4340  C C     . THR B 2 542  ? 147.427 146.752 170.892 1.00 48.55  ? 539  THR A C     1 
ATOM   4341  O O     . THR B 2 542  ? 146.609 147.609 171.231 1.00 48.55  ? 539  THR A O     1 
ATOM   4342  C CB    . THR B 2 542  ? 146.021 145.072 172.105 1.00 48.55  ? 539  THR A CB    1 
ATOM   4343  O OG1   . THR B 2 542  ? 146.438 145.562 173.386 1.00 48.55  ? 539  THR A OG1   1 
ATOM   4344  C CG2   . THR B 2 542  ? 145.662 143.598 172.225 1.00 48.55  ? 539  THR A CG2   1 
ATOM   4345  N N     . LEU B 2 543  ? 148.594 147.074 170.340 1.00 48.55  ? 540  LEU A N     1 
ATOM   4346  C CA    . LEU B 2 543  ? 148.926 148.465 170.065 1.00 48.55  ? 540  LEU A CA    1 
ATOM   4347  C C     . LEU B 2 543  ? 148.053 149.001 168.938 1.00 48.55  ? 540  LEU A C     1 
ATOM   4348  O O     . LEU B 2 543  ? 147.842 148.328 167.925 1.00 48.55  ? 540  LEU A O     1 
ATOM   4349  C CB    . LEU B 2 543  ? 150.409 148.595 169.711 1.00 48.55  ? 540  LEU A CB    1 
ATOM   4350  C CG    . LEU B 2 543  ? 151.012 149.995 169.559 1.00 48.55  ? 540  LEU A CG    1 
ATOM   4351  C CD1   . LEU B 2 543  ? 152.486 149.955 169.900 1.00 48.55  ? 540  LEU A CD1   1 
ATOM   4352  C CD2   . LEU B 2 543  ? 150.835 150.537 168.149 1.00 48.55  ? 540  LEU A CD2   1 
ATOM   4353  N N     . ALA B 2 544  ? 147.543 150.218 169.127 1.00 48.55  ? 541  ALA A N     1 
ATOM   4354  C CA    . ALA B 2 544  ? 146.687 150.908 168.163 1.00 48.55  ? 541  ALA A CA    1 
ATOM   4355  C C     . ALA B 2 544  ? 145.429 150.116 167.823 1.00 48.55  ? 541  ALA A C     1 
ATOM   4356  O O     . ALA B 2 544  ? 144.780 150.384 166.807 1.00 48.55  ? 541  ALA A O     1 
ATOM   4357  C CB    . ALA B 2 544  ? 147.456 151.251 166.881 1.00 48.55  ? 541  ALA A CB    1 
ATOM   4358  N N     . SER B 2 545  ? 145.072 149.136 168.655 1.00 48.55  ? 542  SER A N     1 
ATOM   4359  C CA    . SER B 2 545  ? 143.844 148.381 168.427 1.00 48.55  ? 542  SER A CA    1 
ATOM   4360  C C     . SER B 2 545  ? 142.617 149.268 168.585 1.00 48.55  ? 542  SER A C     1 
ATOM   4361  O O     . SER B 2 545  ? 141.661 149.164 167.808 1.00 48.55  ? 542  SER A O     1 
ATOM   4362  C CB    . SER B 2 545  ? 143.774 147.193 169.384 1.00 48.55  ? 542  SER A CB    1 
ATOM   4363  O OG    . SER B 2 545  ? 142.459 146.673 169.455 1.00 48.55  ? 542  SER A OG    1 
ATOM   4364  N N     . GLY B 2 546  ? 142.622 150.137 169.585 1.00 48.55  ? 543  GLY A N     1 
ATOM   4365  C CA    . GLY B 2 546  ? 141.512 151.042 169.810 1.00 48.55  ? 543  GLY A CA    1 
ATOM   4366  C C     . GLY B 2 546  ? 142.008 152.358 170.367 1.00 48.55  ? 543  GLY A C     1 
ATOM   4367  O O     . GLY B 2 546  ? 142.998 152.413 171.099 1.00 48.55  ? 543  GLY A O     1 
ATOM   4368  N N     . TRP B 2 547  ? 141.304 153.426 170.008 1.00 48.55  ? 544  TRP A N     1 
ATOM   4369  C CA    . TRP B 2 547  ? 141.702 154.773 170.388 1.00 48.55  ? 544  TRP A CA    1 
ATOM   4370  C C     . TRP B 2 547  ? 141.010 155.268 171.651 1.00 48.55  ? 544  TRP A C     1 
ATOM   4371  O O     . TRP B 2 547  ? 141.275 156.396 172.079 1.00 48.55  ? 544  TRP A O     1 
ATOM   4372  C CB    . TRP B 2 547  ? 141.416 155.748 169.243 1.00 48.55  ? 544  TRP A CB    1 
ATOM   4373  C CG    . TRP B 2 547  ? 142.014 155.338 167.936 1.00 48.55  ? 544  TRP A CG    1 
ATOM   4374  C CD1   . TRP B 2 547  ? 141.354 154.811 166.867 1.00 48.55  ? 544  TRP A CD1   1 
ATOM   4375  C CD2   . TRP B 2 547  ? 143.394 155.405 167.562 1.00 48.55  ? 544  TRP A CD2   1 
ATOM   4376  N NE1   . TRP B 2 547  ? 142.235 154.555 165.846 1.00 48.55  ? 544  TRP A NE1   1 
ATOM   4377  C CE2   . TRP B 2 547  ? 143.494 154.910 166.249 1.00 48.55  ? 544  TRP A CE2   1 
ATOM   4378  C CE3   . TRP B 2 547  ? 144.553 155.839 168.209 1.00 48.55  ? 544  TRP A CE3   1 
ATOM   4379  C CZ2   . TRP B 2 547  ? 144.707 154.836 165.571 1.00 48.55  ? 544  TRP A CZ2   1 
ATOM   4380  C CZ3   . TRP B 2 547  ? 145.755 155.761 167.535 1.00 48.55  ? 544  TRP A CZ3   1 
ATOM   4381  C CH2   . TRP B 2 547  ? 145.823 155.267 166.230 1.00 48.55  ? 544  TRP A CH2   1 
ATOM   4382  N N     . ASP B 2 548  ? 140.150 154.456 172.261 1.00 48.55  ? 545  ASP A N     1 
ATOM   4383  C CA    . ASP B 2 548  ? 139.312 154.931 173.354 1.00 48.55  ? 545  ASP A CA    1 
ATOM   4384  C C     . ASP B 2 548  ? 140.151 155.337 174.559 1.00 48.55  ? 545  ASP A C     1 
ATOM   4385  O O     . ASP B 2 548  ? 141.221 154.777 174.813 1.00 48.55  ? 545  ASP A O     1 
ATOM   4386  C CB    . ASP B 2 548  ? 138.309 153.853 173.757 1.00 48.55  ? 545  ASP A CB    1 
ATOM   4387  C CG    . ASP B 2 548  ? 137.060 154.427 174.393 1.00 48.55  ? 545  ASP A CG    1 
ATOM   4388  O OD1   . ASP B 2 548  ? 137.186 155.307 175.271 1.00 48.55  ? 545  ASP A OD1   1 
ATOM   4389  O OD2   . ASP B 2 548  ? 135.949 153.999 174.015 1.00 48.55  ? 545  ASP A OD2   1 
ATOM   4390  N N     . VAL B 2 549  ? 139.652 156.328 175.301 1.00 48.55  ? 546  VAL A N     1 
ATOM   4391  C CA    . VAL B 2 549  ? 140.379 156.835 176.460 1.00 48.55  ? 546  VAL A CA    1 
ATOM   4392  C C     . VAL B 2 549  ? 140.443 155.780 177.560 1.00 48.55  ? 546  VAL A C     1 
ATOM   4393  O O     . VAL B 2 549  ? 141.437 155.688 178.290 1.00 48.55  ? 546  VAL A O     1 
ATOM   4394  C CB    . VAL B 2 549  ? 139.747 158.151 176.953 1.00 48.55  ? 546  VAL A CB    1 
ATOM   4395  C CG1   . VAL B 2 549  ? 138.321 157.928 177.438 1.00 48.55  ? 546  VAL A CG1   1 
ATOM   4396  C CG2   . VAL B 2 549  ? 140.600 158.778 178.045 1.00 48.55  ? 546  VAL A CG2   1 
ATOM   4397  N N     . ASN B 2 550  ? 139.389 154.974 177.704 1.00 48.55  ? 547  ASN A N     1 
ATOM   4398  C CA    . ASN B 2 550  ? 139.403 153.922 178.715 1.00 48.55  ? 547  ASN A CA    1 
ATOM   4399  C C     . ASN B 2 550  ? 140.413 152.835 178.369 1.00 48.55  ? 547  ASN A C     1 
ATOM   4400  O O     . ASN B 2 550  ? 141.080 152.294 179.258 1.00 48.55  ? 547  ASN A O     1 
ATOM   4401  C CB    . ASN B 2 550  ? 138.005 153.331 178.877 1.00 48.55  ? 547  ASN A CB    1 
ATOM   4402  C CG    . ASN B 2 550  ? 137.006 154.340 179.402 1.00 48.55  ? 547  ASN A CG    1 
ATOM   4403  O OD1   . ASN B 2 550  ? 137.380 155.344 180.007 1.00 48.55  ? 547  ASN A OD1   1 
ATOM   4404  N ND2   . ASN B 2 550  ? 135.725 154.079 179.171 1.00 48.55  ? 547  ASN A ND2   1 
ATOM   4405  N N     . LYS B 2 551  ? 140.543 152.503 177.087 1.00 48.55  ? 548  LYS A N     1 
ATOM   4406  C CA    . LYS B 2 551  ? 141.536 151.545 176.625 1.00 48.55  ? 548  LYS A CA    1 
ATOM   4407  C C     . LYS B 2 551  ? 142.819 152.217 176.157 1.00 48.55  ? 548  LYS A C     1 
ATOM   4408  O O     . LYS B 2 551  ? 143.656 151.561 175.528 1.00 48.55  ? 548  LYS A O     1 
ATOM   4409  C CB    . LYS B 2 551  ? 140.962 150.678 175.503 1.00 48.55  ? 548  LYS A CB    1 
ATOM   4410  C CG    . LYS B 2 551  ? 139.910 149.687 175.965 1.00 48.55  ? 548  LYS A CG    1 
ATOM   4411  C CD    . LYS B 2 551  ? 140.541 148.545 176.743 1.00 48.55  ? 548  LYS A CD    1 
ATOM   4412  C CE    . LYS B 2 551  ? 141.521 147.759 175.887 1.00 48.55  ? 548  LYS A CE    1 
ATOM   4413  N NZ    . LYS B 2 551  ? 140.918 147.329 174.597 1.00 48.55  ? 548  LYS A NZ    1 
ATOM   4414  N N     . GLU B 2 552  ? 142.979 153.512 176.437 1.00 48.55  ? 549  GLU A N     1 
ATOM   4415  C CA    . GLU B 2 552  ? 144.236 154.194 176.152 1.00 48.55  ? 549  GLU A CA    1 
ATOM   4416  C C     . GLU B 2 552  ? 145.403 153.514 176.853 1.00 48.55  ? 549  GLU A C     1 
ATOM   4417  O O     . GLU B 2 552  ? 146.493 153.387 176.285 1.00 48.55  ? 549  GLU A O     1 
ATOM   4418  C CB    . GLU B 2 552  ? 144.139 155.654 176.590 1.00 48.55  ? 549  GLU A CB    1 
ATOM   4419  C CG    . GLU B 2 552  ? 144.954 156.624 175.771 1.00 48.55  ? 549  GLU A CG    1 
ATOM   4420  C CD    . GLU B 2 552  ? 144.726 158.060 176.196 1.00 48.55  ? 549  GLU A CD    1 
ATOM   4421  O OE1   . GLU B 2 552  ? 143.552 158.473 176.299 1.00 48.55  ? 549  GLU A OE1   1 
ATOM   4422  O OE2   . GLU B 2 552  ? 145.721 158.774 176.440 1.00 48.55  ? 549  GLU A OE2   1 
ATOM   4423  N N     . LYS B 2 553  ? 145.189 153.077 178.095 1.00 48.57  ? 550  LYS A N     1 
ATOM   4424  C CA    . LYS B 2 553  ? 146.257 152.460 178.872 1.00 48.57  ? 550  LYS A CA    1 
ATOM   4425  C C     . LYS B 2 553  ? 146.770 151.191 178.206 1.00 48.57  ? 550  LYS A C     1 
ATOM   4426  O O     . LYS B 2 553  ? 147.983 150.964 178.136 1.00 48.57  ? 550  LYS A O     1 
ATOM   4427  C CB    . LYS B 2 553  ? 145.752 152.147 180.279 1.00 48.57  ? 550  LYS A CB    1 
ATOM   4428  C CG    . LYS B 2 553  ? 146.808 151.630 181.234 1.00 48.57  ? 550  LYS A CG    1 
ATOM   4429  C CD    . LYS B 2 553  ? 146.201 151.354 182.601 1.00 48.57  ? 550  LYS A CD    1 
ATOM   4430  C CE    . LYS B 2 553  ? 145.840 152.641 183.319 1.00 48.57  ? 550  LYS A CE    1 
ATOM   4431  N NZ    . LYS B 2 553  ? 147.049 153.422 183.678 1.00 48.57  ? 550  LYS A NZ    1 
ATOM   4432  N N     . CYS B 2 554  ? 145.861 150.355 177.708 1.00 48.55  ? 551  CYS A N     1 
ATOM   4433  C CA    . CYS B 2 554  ? 146.244 149.013 177.290 1.00 48.55  ? 551  CYS A CA    1 
ATOM   4434  C C     . CYS B 2 554  ? 146.605 148.950 175.811 1.00 48.55  ? 551  CYS A C     1 
ATOM   4435  O O     . CYS B 2 554  ? 147.073 147.908 175.338 1.00 48.55  ? 551  CYS A O     1 
ATOM   4436  C CB    . CYS B 2 554  ? 145.113 148.039 177.615 1.00 47.36  ? 551  CYS A CB    1 
ATOM   4437  S SG    . CYS B 2 554  ? 144.835 147.885 179.397 1.00 47.36  ? 551  CYS A SG    1 
ATOM   4438  N N     . ASN B 2 555  ? 146.399 150.039 175.072 1.00 48.55  ? 552  ASN A N     1 
ATOM   4439  C CA    . ASN B 2 555  ? 146.758 150.109 173.660 1.00 48.55  ? 552  ASN A CA    1 
ATOM   4440  C C     . ASN B 2 555  ? 147.951 151.016 173.395 1.00 48.55  ? 552  ASN A C     1 
ATOM   4441  O O     . ASN B 2 555  ? 148.741 150.741 172.488 1.00 48.55  ? 552  ASN A O     1 
ATOM   4442  C CB    . ASN B 2 555  ? 145.561 150.588 172.833 1.00 48.55  ? 552  ASN A CB    1 
ATOM   4443  C CG    . ASN B 2 555  ? 144.309 149.778 173.098 1.00 48.55  ? 552  ASN A CG    1 
ATOM   4444  O OD1   . ASN B 2 555  ? 144.350 148.757 173.782 1.00 48.55  ? 552  ASN A OD1   1 
ATOM   4445  N ND2   . ASN B 2 555  ? 143.184 150.237 172.563 1.00 48.55  ? 552  ASN A ND2   1 
ATOM   4446  N N     . GLY B 2 556  ? 148.102 152.087 174.166 1.00 48.55  ? 553  GLY A N     1 
ATOM   4447  C CA    . GLY B 2 556  ? 149.264 152.951 174.048 1.00 48.55  ? 553  GLY A CA    1 
ATOM   4448  C C     . GLY B 2 556  ? 149.388 153.699 172.738 1.00 48.55  ? 553  GLY A C     1 
ATOM   4449  O O     . GLY B 2 556  ? 150.487 153.766 172.172 1.00 48.55  ? 553  GLY A O     1 
ATOM   4450  N N     . ALA B 2 557  ? 148.292 154.264 172.238 1.00 48.55  ? 554  ALA A N     1 
ATOM   4451  C CA    . ALA B 2 557  ? 148.316 155.029 170.999 1.00 48.55  ? 554  ALA A CA    1 
ATOM   4452  C C     . ALA B 2 557  ? 147.364 156.207 171.117 1.00 48.55  ? 554  ALA A C     1 
ATOM   4453  O O     . ALA B 2 557  ? 146.197 156.030 171.479 1.00 48.55  ? 554  ALA A O     1 
ATOM   4454  C CB    . ALA B 2 557  ? 147.935 154.154 169.800 1.00 48.55  ? 554  ALA A CB    1 
ATOM   4455  N N     . ILE B 2 558  ? 147.863 157.406 170.811 1.00 48.55  ? 555  ILE A N     1 
ATOM   4456  C CA    . ILE B 2 558  ? 147.086 158.638 170.887 1.00 48.55  ? 555  ILE A CA    1 
ATOM   4457  C C     . ILE B 2 558  ? 147.461 159.536 169.716 1.00 48.55  ? 555  ILE A C     1 
ATOM   4458  O O     . ILE B 2 558  ? 148.407 159.270 168.973 1.00 48.55  ? 555  ILE A O     1 
ATOM   4459  C CB    . ILE B 2 558  ? 147.299 159.384 172.221 1.00 48.55  ? 555  ILE A CB    1 
ATOM   4460  C CG1   . ILE B 2 558  ? 148.791 159.538 172.515 1.00 48.55  ? 555  ILE A CG1   1 
ATOM   4461  C CG2   . ILE B 2 558  ? 146.599 158.667 173.353 1.00 48.55  ? 555  ILE A CG2   1 
ATOM   4462  C CD1   . ILE B 2 558  ? 149.082 160.260 173.809 1.00 48.55  ? 555  ILE A CD1   1 
ATOM   4463  N N     . LEU B 2 559  ? 146.695 160.614 169.557 1.00 48.55  ? 556  LEU A N     1 
ATOM   4464  C CA    . LEU B 2 559  ? 146.925 161.597 168.509 1.00 48.55  ? 556  LEU A CA    1 
ATOM   4465  C C     . LEU B 2 559  ? 146.928 162.997 169.102 1.00 48.55  ? 556  LEU A C     1 
ATOM   4466  O O     . LEU B 2 559  ? 146.416 163.227 170.201 1.00 48.55  ? 556  LEU A O     1 
ATOM   4467  C CB    . LEU B 2 559  ? 145.864 161.526 167.402 1.00 48.55  ? 556  LEU A CB    1 
ATOM   4468  C CG    . LEU B 2 559  ? 145.951 160.428 166.343 1.00 48.55  ? 556  LEU A CG    1 
ATOM   4469  C CD1   . LEU B 2 559  ? 145.589 159.080 166.917 1.00 48.55  ? 556  LEU A CD1   1 
ATOM   4470  C CD2   . LEU B 2 559  ? 145.044 160.763 165.180 1.00 48.55  ? 556  LEU A CD2   1 
ATOM   4471  N N     . PHE B 2 560  ? 147.511 163.931 168.358 1.00 48.55  ? 557  PHE A N     1 
ATOM   4472  C CA    . PHE B 2 560  ? 147.552 165.337 168.726 1.00 48.55  ? 557  PHE A CA    1 
ATOM   4473  C C     . PHE B 2 560  ? 147.346 166.186 167.479 1.00 48.55  ? 557  PHE A C     1 
ATOM   4474  O O     . PHE B 2 560  ? 147.194 165.674 166.366 1.00 48.55  ? 557  PHE A O     1 
ATOM   4475  C CB    . PHE B 2 560  ? 148.879 165.698 169.404 1.00 48.55  ? 557  PHE A CB    1 
ATOM   4476  C CG    . PHE B 2 560  ? 149.122 164.974 170.694 1.00 48.55  ? 557  PHE A CG    1 
ATOM   4477  C CD1   . PHE B 2 560  ? 148.583 165.444 171.878 1.00 48.55  ? 557  PHE A CD1   1 
ATOM   4478  C CD2   . PHE B 2 560  ? 149.901 163.834 170.726 1.00 48.55  ? 557  PHE A CD2   1 
ATOM   4479  C CE1   . PHE B 2 560  ? 148.809 164.785 173.067 1.00 48.55  ? 557  PHE A CE1   1 
ATOM   4480  C CE2   . PHE B 2 560  ? 150.130 163.172 171.912 1.00 48.55  ? 557  PHE A CE2   1 
ATOM   4481  C CZ    . PHE B 2 560  ? 149.584 163.649 173.083 1.00 48.55  ? 557  PHE A CZ    1 
ATOM   4482  N N     . VAL B 2 561  ? 147.346 167.501 167.675 1.00 48.55  ? 558  VAL A N     1 
ATOM   4483  C CA    . VAL B 2 561  ? 147.324 168.455 166.572 1.00 48.55  ? 558  VAL A CA    1 
ATOM   4484  C C     . VAL B 2 561  ? 147.898 169.769 167.082 1.00 48.55  ? 558  VAL A C     1 
ATOM   4485  O O     . VAL B 2 561  ? 147.593 170.208 168.194 1.00 48.55  ? 558  VAL A O     1 
ATOM   4486  C CB    . VAL B 2 561  ? 145.899 168.617 165.988 1.00 48.55  ? 558  VAL A CB    1 
ATOM   4487  C CG1   . VAL B 2 561  ? 144.948 169.227 167.005 1.00 48.55  ? 558  VAL A CG1   1 
ATOM   4488  C CG2   . VAL B 2 561  ? 145.937 169.456 164.718 1.00 48.55  ? 558  VAL A CG2   1 
ATOM   4489  N N     . LYS B 2 562  ? 148.759 170.379 166.271 1.00 48.55  ? 559  LYS A N     1 
ATOM   4490  C CA    . LYS B 2 562  ? 149.414 171.628 166.646 1.00 48.55  ? 559  LYS A CA    1 
ATOM   4491  C C     . LYS B 2 562  ? 149.871 172.332 165.381 1.00 48.55  ? 559  LYS A C     1 
ATOM   4492  O O     . LYS B 2 562  ? 150.639 171.761 164.600 1.00 48.55  ? 559  LYS A O     1 
ATOM   4493  C CB    . LYS B 2 562  ? 150.600 171.370 167.576 1.00 48.55  ? 559  LYS A CB    1 
ATOM   4494  C CG    . LYS B 2 562  ? 151.240 172.633 168.126 1.00 48.55  ? 559  LYS A CG    1 
ATOM   4495  C CD    . LYS B 2 562  ? 152.393 172.308 169.061 1.00 48.55  ? 559  LYS A CD    1 
ATOM   4496  C CE    . LYS B 2 562  ? 153.553 171.678 168.309 1.00 48.55  ? 559  LYS A CE    1 
ATOM   4497  N NZ    . LYS B 2 562  ? 153.811 172.363 167.013 1.00 48.55  ? 559  LYS A NZ    1 
ATOM   4498  N N     . ASN B 2 563  ? 149.399 173.565 165.184 1.00 48.55  ? 560  ASN A N     1 
ATOM   4499  C CA    . ASN B 2 563  ? 149.744 174.370 164.011 1.00 48.55  ? 560  ASN A CA    1 
ATOM   4500  C C     . ASN B 2 563  ? 149.378 173.648 162.716 1.00 48.55  ? 560  ASN A C     1 
ATOM   4501  O O     . ASN B 2 563  ? 150.049 173.792 161.692 1.00 48.55  ? 560  ASN A O     1 
ATOM   4502  C CB    . ASN B 2 563  ? 151.225 174.754 164.018 1.00 48.55  ? 560  ASN A CB    1 
ATOM   4503  C CG    . ASN B 2 563  ? 151.621 175.524 165.260 1.00 48.55  ? 560  ASN A CG    1 
ATOM   4504  O OD1   . ASN B 2 563  ? 150.769 176.038 165.984 1.00 48.55  ? 560  ASN A OD1   1 
ATOM   4505  N ND2   . ASN B 2 563  ? 152.922 175.606 165.515 1.00 48.55  ? 560  ASN A ND2   1 
ATOM   4506  N N     . GLY B 2 564  ? 148.305 172.864 162.761 1.00 48.55  ? 561  GLY A N     1 
ATOM   4507  C CA    . GLY B 2 564  ? 147.870 172.115 161.602 1.00 48.55  ? 561  GLY A CA    1 
ATOM   4508  C C     . GLY B 2 564  ? 148.675 170.873 161.298 1.00 48.55  ? 561  GLY A C     1 
ATOM   4509  O O     . GLY B 2 564  ? 148.436 170.240 160.264 1.00 48.55  ? 561  GLY A O     1 
ATOM   4510  N N     . LEU B 2 565  ? 149.617 170.504 162.159 1.00 48.55  ? 562  LEU A N     1 
ATOM   4511  C CA    . LEU B 2 565  ? 150.425 169.304 161.986 1.00 48.55  ? 562  LEU A CA    1 
ATOM   4512  C C     . LEU B 2 565  ? 149.943 168.237 162.957 1.00 48.55  ? 562  LEU A C     1 
ATOM   4513  O O     . LEU B 2 565  ? 149.860 168.484 164.164 1.00 48.55  ? 562  LEU A O     1 
ATOM   4514  C CB    . LEU B 2 565  ? 151.909 169.598 162.214 1.00 48.55  ? 562  LEU A CB    1 
ATOM   4515  C CG    . LEU B 2 565  ? 152.520 170.806 161.500 1.00 48.55  ? 562  LEU A CG    1 
ATOM   4516  C CD1   . LEU B 2 565  ? 154.036 170.755 161.583 1.00 48.55  ? 562  LEU A CD1   1 
ATOM   4517  C CD2   . LEU B 2 565  ? 152.072 170.864 160.047 1.00 48.55  ? 562  LEU A CD2   1 
ATOM   4518  N N     . TYR B 2 566  ? 149.626 167.059 162.430 1.00 48.55  ? 563  TYR A N     1 
ATOM   4519  C CA    . TYR B 2 566  ? 149.082 165.976 163.235 1.00 48.55  ? 563  TYR A CA    1 
ATOM   4520  C C     . TYR B 2 566  ? 150.211 165.087 163.738 1.00 48.55  ? 563  TYR A C     1 
ATOM   4521  O O     . TYR B 2 566  ? 151.084 164.681 162.965 1.00 48.55  ? 563  TYR A O     1 
ATOM   4522  C CB    . TYR B 2 566  ? 148.075 165.158 162.426 1.00 48.55  ? 563  TYR A CB    1 
ATOM   4523  C CG    . TYR B 2 566  ? 146.871 165.960 161.995 1.00 48.55  ? 563  TYR A CG    1 
ATOM   4524  C CD1   . TYR B 2 566  ? 145.782 166.121 162.839 1.00 48.55  ? 563  TYR A CD1   1 
ATOM   4525  C CD2   . TYR B 2 566  ? 146.827 166.566 160.748 1.00 48.55  ? 563  TYR A CD2   1 
ATOM   4526  C CE1   . TYR B 2 566  ? 144.683 166.858 162.451 1.00 48.55  ? 563  TYR A CE1   1 
ATOM   4527  C CE2   . TYR B 2 566  ? 145.731 167.304 160.351 1.00 48.55  ? 563  TYR A CE2   1 
ATOM   4528  C CZ    . TYR B 2 566  ? 144.662 167.447 161.206 1.00 48.55  ? 563  TYR A CZ    1 
ATOM   4529  O OH    . TYR B 2 566  ? 143.567 168.182 160.815 1.00 48.55  ? 563  TYR A OH    1 
ATOM   4530  N N     . TYR B 2 567  ? 150.190 164.793 165.033 1.00 48.55  ? 564  TYR A N     1 
ATOM   4531  C CA    . TYR B 2 567  ? 151.205 163.977 165.676 1.00 48.55  ? 564  TYR A CA    1 
ATOM   4532  C C     . TYR B 2 567  ? 150.580 162.708 166.238 1.00 48.55  ? 564  TYR A C     1 
ATOM   4533  O O     . TYR B 2 567  ? 149.425 162.703 166.671 1.00 48.55  ? 564  TYR A O     1 
ATOM   4534  C CB    . TYR B 2 567  ? 151.903 164.744 166.804 1.00 48.55  ? 564  TYR A CB    1 
ATOM   4535  C CG    . TYR B 2 567  ? 152.718 165.935 166.353 1.00 48.55  ? 564  TYR A CG    1 
ATOM   4536  C CD1   . TYR B 2 567  ? 152.104 167.086 165.886 1.00 48.55  ? 564  TYR A CD1   1 
ATOM   4537  C CD2   . TYR B 2 567  ? 154.103 165.910 166.410 1.00 48.55  ? 564  TYR A CD2   1 
ATOM   4538  C CE1   . TYR B 2 567  ? 152.846 168.175 165.478 1.00 48.55  ? 564  TYR A CE1   1 
ATOM   4539  C CE2   . TYR B 2 567  ? 154.852 166.994 166.006 1.00 48.55  ? 564  TYR A CE2   1 
ATOM   4540  C CZ    . TYR B 2 567  ? 154.220 168.124 165.541 1.00 48.55  ? 564  TYR A CZ    1 
ATOM   4541  O OH    . TYR B 2 567  ? 154.965 169.207 165.137 1.00 48.55  ? 564  TYR A OH    1 
ATOM   4542  N N     . LEU B 2 568  ? 151.357 161.630 166.227 1.00 48.55  ? 565  LEU A N     1 
ATOM   4543  C CA    . LEU B 2 568  ? 150.958 160.360 166.817 1.00 48.55  ? 565  LEU A CA    1 
ATOM   4544  C C     . LEU B 2 568  ? 151.809 160.097 168.049 1.00 48.55  ? 565  LEU A C     1 
ATOM   4545  O O     . LEU B 2 568  ? 153.040 160.179 167.988 1.00 48.55  ? 565  LEU A O     1 
ATOM   4546  C CB    . LEU B 2 568  ? 151.103 159.214 165.813 1.00 48.55  ? 565  LEU A CB    1 
ATOM   4547  C CG    . LEU B 2 568  ? 150.759 157.812 166.318 1.00 48.55  ? 565  LEU A CG    1 
ATOM   4548  C CD1   . LEU B 2 568  ? 149.914 157.076 165.301 1.00 48.55  ? 565  LEU A CD1   1 
ATOM   4549  C CD2   . LEU B 2 568  ? 152.024 157.025 166.615 1.00 48.55  ? 565  LEU A CD2   1 
ATOM   4550  N N     . GLY B 2 569  ? 151.153 159.781 169.162 1.00 48.55  ? 566  GLY A N     1 
ATOM   4551  C CA    . GLY B 2 569  ? 151.826 159.535 170.424 1.00 48.55  ? 566  GLY A CA    1 
ATOM   4552  C C     . GLY B 2 569  ? 151.733 158.066 170.803 1.00 48.55  ? 566  GLY A C     1 
ATOM   4553  O O     . GLY B 2 569  ? 150.669 157.455 170.699 1.00 48.55  ? 566  GLY A O     1 
ATOM   4554  N N     . ILE B 2 570  ? 152.862 157.518 171.240 1.00 48.55  ? 567  ILE A N     1 
ATOM   4555  C CA    . ILE B 2 570  ? 152.957 156.129 171.670 1.00 48.55  ? 567  ILE A CA    1 
ATOM   4556  C C     . ILE B 2 570  ? 153.567 156.102 173.063 1.00 48.55  ? 567  ILE A C     1 
ATOM   4557  O O     . ILE B 2 570  ? 154.621 156.705 173.297 1.00 48.55  ? 567  ILE A O     1 
ATOM   4558  C CB    . ILE B 2 570  ? 153.791 155.285 170.691 1.00 48.55  ? 567  ILE A CB    1 
ATOM   4559  C CG1   . ILE B 2 570  ? 152.928 154.831 169.518 1.00 48.55  ? 567  ILE A CG1   1 
ATOM   4560  C CG2   . ILE B 2 570  ? 154.393 154.079 171.393 1.00 48.55  ? 567  ILE A CG2   1 
ATOM   4561  C CD1   . ILE B 2 570  ? 153.720 154.187 168.419 1.00 48.55  ? 567  ILE A CD1   1 
ATOM   4562  N N     . MET B 2 571  ? 152.902 155.408 173.984 1.00 48.55  ? 568  MET A N     1 
ATOM   4563  C CA    . MET B 2 571  ? 153.426 155.228 175.327 1.00 48.55  ? 568  MET A CA    1 
ATOM   4564  C C     . MET B 2 571  ? 154.154 153.897 175.383 1.00 48.55  ? 568  MET A C     1 
ATOM   4565  O O     . MET B 2 571  ? 153.517 152.851 175.196 1.00 48.55  ? 568  MET A O     1 
ATOM   4566  C CB    . MET B 2 571  ? 152.301 155.265 176.358 1.00 48.55  ? 568  MET A CB    1 
ATOM   4567  C CG    . MET B 2 571  ? 151.777 156.655 176.664 1.00 48.55  ? 568  MET A CG    1 
ATOM   4568  S SD    . MET B 2 571  ? 150.776 157.338 175.332 1.00 48.55  ? 568  MET A SD    1 
ATOM   4569  C CE    . MET B 2 571  ? 149.272 156.387 175.521 1.00 48.55  ? 568  MET A CE    1 
ATOM   4570  N N     . PRO B 2 572  ? 155.461 153.873 175.615 1.00 48.83  ? 569  PRO A N     1 
ATOM   4571  C CA    . PRO B 2 572  ? 156.184 152.602 175.667 1.00 48.83  ? 569  PRO A CA    1 
ATOM   4572  C C     . PRO B 2 572  ? 156.126 151.980 177.056 1.00 48.83  ? 569  PRO A C     1 
ATOM   4573  O O     . PRO B 2 572  ? 155.712 152.601 178.035 1.00 48.83  ? 569  PRO A O     1 
ATOM   4574  C CB    . PRO B 2 572  ? 157.612 153.007 175.303 1.00 48.83  ? 569  PRO A CB    1 
ATOM   4575  C CG    . PRO B 2 572  ? 157.737 154.384 175.864 1.00 48.83  ? 569  PRO A CG    1 
ATOM   4576  C CD    . PRO B 2 572  ? 156.368 155.025 175.750 1.00 48.83  ? 569  PRO A CD    1 
ATOM   4577  N N     . LYS B 2 573  ? 156.549 150.720 177.120 1.00 81.33  ? 570  LYS A N     1 
ATOM   4578  C CA    . LYS B 2 573  ? 156.668 150.034 178.398 1.00 81.33  ? 570  LYS A CA    1 
ATOM   4579  C C     . LYS B 2 573  ? 157.748 150.696 179.243 1.00 81.33  ? 570  LYS A C     1 
ATOM   4580  O O     . LYS B 2 573  ? 158.845 150.982 178.754 1.00 81.33  ? 570  LYS A O     1 
ATOM   4581  C CB    . LYS B 2 573  ? 156.999 148.558 178.183 1.00 81.33  ? 570  LYS A CB    1 
ATOM   4582  C CG    . LYS B 2 573  ? 155.793 147.635 178.166 1.00 81.33  ? 570  LYS A CG    1 
ATOM   4583  C CD    . LYS B 2 573  ? 156.225 146.178 178.217 1.00 81.33  ? 570  LYS A CD    1 
ATOM   4584  C CE    . LYS B 2 573  ? 155.041 145.238 178.065 1.00 81.33  ? 570  LYS A CE    1 
ATOM   4585  N NZ    . LYS B 2 573  ? 154.289 145.494 176.807 1.00 81.33  ? 570  LYS A NZ    1 
ATOM   4586  N N     . ALA B 2 580  ? 151.449 154.673 183.715 1.00 81.11  ? 577  ALA A N     1 
ATOM   4587  C CA    . ALA B 2 580  ? 150.462 155.604 183.193 1.00 81.11  ? 577  ALA A CA    1 
ATOM   4588  C C     . ALA B 2 580  ? 151.056 156.989 182.984 1.00 81.11  ? 577  ALA A C     1 
ATOM   4589  O O     . ALA B 2 580  ? 151.813 157.492 183.820 1.00 81.11  ? 577  ALA A O     1 
ATOM   4590  C CB    . ALA B 2 580  ? 149.267 155.698 184.141 1.00 81.11  ? 577  ALA A CB    1 
ATOM   4591  N N     . LEU B 2 581  ? 150.711 157.602 181.856 1.00 58.08  ? 578  LEU A N     1 
ATOM   4592  C CA    . LEU B 2 581  ? 150.934 159.027 181.644 1.00 58.08  ? 578  LEU A CA    1 
ATOM   4593  C C     . LEU B 2 581  ? 149.625 159.751 181.931 1.00 58.08  ? 578  LEU A C     1 
ATOM   4594  O O     . LEU B 2 581  ? 148.736 159.805 181.075 1.00 58.08  ? 578  LEU A O     1 
ATOM   4595  C CB    . LEU B 2 581  ? 151.417 159.310 180.225 1.00 58.08  ? 578  LEU A CB    1 
ATOM   4596  C CG    . LEU B 2 581  ? 152.927 159.304 179.994 1.00 58.08  ? 578  LEU A CG    1 
ATOM   4597  C CD1   . LEU B 2 581  ? 153.225 159.409 178.513 1.00 58.08  ? 578  LEU A CD1   1 
ATOM   4598  C CD2   . LEU B 2 581  ? 153.584 160.443 180.754 1.00 58.08  ? 578  LEU A CD2   1 
ATOM   4599  N N     . SER B 2 582  ? 149.506 160.304 183.134 1.00 56.04  ? 579  SER A N     1 
ATOM   4600  C CA    . SER B 2 582  ? 148.300 161.024 183.535 1.00 56.04  ? 579  SER A CA    1 
ATOM   4601  C C     . SER B 2 582  ? 148.379 162.418 182.931 1.00 56.04  ? 579  SER A C     1 
ATOM   4602  O O     . SER B 2 582  ? 148.858 163.365 183.555 1.00 56.04  ? 579  SER A O     1 
ATOM   4603  C CB    . SER B 2 582  ? 148.171 161.065 185.052 1.00 56.04  ? 579  SER A CB    1 
ATOM   4604  O OG    . SER B 2 582  ? 147.951 159.769 185.580 1.00 56.04  ? 579  SER A OG    1 
ATOM   4605  N N     . PHE B 2 583  ? 147.914 162.539 181.690 1.00 48.55  ? 580  PHE A N     1 
ATOM   4606  C CA    . PHE B 2 583  ? 147.921 163.827 181.013 1.00 48.55  ? 580  PHE A CA    1 
ATOM   4607  C C     . PHE B 2 583  ? 146.980 164.795 181.715 1.00 48.55  ? 580  PHE A C     1 
ATOM   4608  O O     . PHE B 2 583  ? 145.783 164.528 181.852 1.00 48.55  ? 580  PHE A O     1 
ATOM   4609  C CB    . PHE B 2 583  ? 147.506 163.653 179.553 1.00 48.55  ? 580  PHE A CB    1 
ATOM   4610  C CG    . PHE B 2 583  ? 148.522 162.937 178.712 1.00 48.55  ? 580  PHE A CG    1 
ATOM   4611  C CD1   . PHE B 2 583  ? 149.643 163.598 178.242 1.00 48.55  ? 580  PHE A CD1   1 
ATOM   4612  C CD2   . PHE B 2 583  ? 148.354 161.602 178.388 1.00 48.55  ? 580  PHE A CD2   1 
ATOM   4613  C CE1   . PHE B 2 583  ? 150.578 162.940 177.466 1.00 48.55  ? 580  PHE A CE1   1 
ATOM   4614  C CE2   . PHE B 2 583  ? 149.285 160.940 177.612 1.00 48.55  ? 580  PHE A CE2   1 
ATOM   4615  C CZ    . PHE B 2 583  ? 150.398 161.611 177.152 1.00 48.55  ? 580  PHE A CZ    1 
ATOM   4616  N N     . GLU B 2 584  ? 147.524 165.927 182.161 1.00 49.91  ? 581  GLU A N     1 
ATOM   4617  C CA    . GLU B 2 584  ? 146.718 166.944 182.815 1.00 49.91  ? 581  GLU A CA    1 
ATOM   4618  C C     . GLU B 2 584  ? 146.327 167.995 181.792 1.00 49.91  ? 581  GLU A C     1 
ATOM   4619  O O     . GLU B 2 584  ? 147.203 168.725 181.303 1.00 49.91  ? 581  GLU A O     1 
ATOM   4620  C CB    . GLU B 2 584  ? 147.480 167.586 183.973 1.00 49.90  ? 581  GLU A CB    1 
ATOM   4621  C CG    . GLU B 2 584  ? 147.460 166.780 185.262 1.00 49.90  ? 581  GLU A CG    1 
ATOM   4622  C CD    . GLU B 2 584  ? 148.590 165.775 185.340 1.00 49.90  ? 581  GLU A CD    1 
ATOM   4623  O OE1   . GLU B 2 584  ? 149.591 165.947 184.614 1.00 49.90  ? 581  GLU A OE1   1 
ATOM   4624  O OE2   . GLU B 2 584  ? 148.478 164.811 186.127 1.00 49.90  ? 581  GLU A OE2   1 
ATOM   4625  N N     . PRO B 2 585  ? 145.051 168.110 181.430 1.00 48.55  ? 582  PRO A N     1 
ATOM   4626  C CA    . PRO B 2 585  ? 144.654 169.127 180.454 1.00 48.55  ? 582  PRO A CA    1 
ATOM   4627  C C     . PRO B 2 585  ? 144.836 170.531 181.007 1.00 48.55  ? 582  PRO A C     1 
ATOM   4628  O O     . PRO B 2 585  ? 144.802 170.757 182.219 1.00 48.55  ? 582  PRO A O     1 
ATOM   4629  C CB    . PRO B 2 585  ? 143.175 168.818 180.197 1.00 48.55  ? 582  PRO A CB    1 
ATOM   4630  C CG    . PRO B 2 585  ? 142.986 167.407 180.646 1.00 48.55  ? 582  PRO A CG    1 
ATOM   4631  C CD    . PRO B 2 585  ? 143.939 167.213 181.782 1.00 48.55  ? 582  PRO A CD    1 
ATOM   4632  N N     . THR B 2 586  ? 145.035 171.480 180.098 1.00 48.55  ? 583  THR A N     1 
ATOM   4633  C CA    . THR B 2 586  ? 145.157 172.889 180.436 1.00 48.55  ? 583  THR A CA    1 
ATOM   4634  C C     . THR B 2 586  ? 144.122 173.678 179.644 1.00 48.55  ? 583  THR A C     1 
ATOM   4635  O O     . THR B 2 586  ? 143.338 173.118 178.871 1.00 48.55  ? 583  THR A O     1 
ATOM   4636  C CB    . THR B 2 586  ? 146.571 173.415 180.154 1.00 48.55  ? 583  THR A CB    1 
ATOM   4637  O OG1   . THR B 2 586  ? 146.862 173.285 178.757 1.00 48.55  ? 583  THR A OG1   1 
ATOM   4638  C CG2   . THR B 2 586  ? 147.602 172.637 180.959 1.00 48.55  ? 583  THR A CG2   1 
ATOM   4639  N N     . GLU B 2 587  ? 144.119 174.991 179.844 1.00 50.34  ? 584  GLU A N     1 
ATOM   4640  C CA    . GLU B 2 587  ? 143.184 175.850 179.138 1.00 50.34  ? 584  GLU A CA    1 
ATOM   4641  C C     . GLU B 2 587  ? 143.635 176.063 177.696 1.00 50.34  ? 584  GLU A C     1 
ATOM   4642  O O     . GLU B 2 587  ? 144.793 175.832 177.334 1.00 50.34  ? 584  GLU A O     1 
ATOM   4643  C CB    . GLU B 2 587  ? 143.045 177.195 179.852 1.00 50.34  ? 584  GLU A CB    1 
ATOM   4644  C CG    . GLU B 2 587  ? 142.486 177.094 181.264 1.00 50.34  ? 584  GLU A CG    1 
ATOM   4645  C CD    . GLU B 2 587  ? 141.011 176.741 181.289 1.00 50.34  ? 584  GLU A CD    1 
ATOM   4646  O OE1   . GLU B 2 587  ? 140.325 176.963 180.268 1.00 50.34  ? 584  GLU A OE1   1 
ATOM   4647  O OE2   . GLU B 2 587  ? 140.536 176.240 182.330 1.00 50.34  ? 584  GLU A OE2   1 
ATOM   4648  N N     . LYS B 2 588  ? 142.691 176.507 176.863 1.00 48.55  ? 585  LYS A N     1 
ATOM   4649  C CA    . LYS B 2 588  ? 142.983 176.761 175.458 1.00 48.55  ? 585  LYS A CA    1 
ATOM   4650  C C     . LYS B 2 588  ? 144.014 177.867 175.272 1.00 48.55  ? 585  LYS A C     1 
ATOM   4651  O O     . LYS B 2 588  ? 144.729 177.869 174.264 1.00 48.55  ? 585  LYS A O     1 
ATOM   4652  C CB    . LYS B 2 588  ? 141.689 177.115 174.720 1.00 47.36  ? 585  LYS A CB    1 
ATOM   4653  C CG    . LYS B 2 588  ? 141.846 177.378 173.230 1.00 47.36  ? 585  LYS A CG    1 
ATOM   4654  C CD    . LYS B 2 588  ? 142.188 176.107 172.471 1.00 47.36  ? 585  LYS A CD    1 
ATOM   4655  C CE    . LYS B 2 588  ? 142.235 176.359 170.972 1.00 47.36  ? 585  LYS A CE    1 
ATOM   4656  N NZ    . LYS B 2 588  ? 142.633 175.144 170.210 1.00 47.36  ? 585  LYS A NZ    1 
ATOM   4657  N N     . THR B 2 589  ? 144.117 178.795 176.226 1.00 51.69  ? 586  THR A N     1 
ATOM   4658  C CA    . THR B 2 589  ? 145.063 179.898 176.090 1.00 51.69  ? 586  THR A CA    1 
ATOM   4659  C C     . THR B 2 589  ? 146.510 179.420 176.150 1.00 51.69  ? 586  THR A C     1 
ATOM   4660  O O     . THR B 2 589  ? 147.385 180.027 175.523 1.00 51.69  ? 586  THR A O     1 
ATOM   4661  C CB    . THR B 2 589  ? 144.798 180.958 177.164 1.00 51.69  ? 586  THR A CB    1 
ATOM   4662  O OG1   . THR B 2 589  ? 145.628 182.103 176.927 1.00 51.69  ? 586  THR A OG1   1 
ATOM   4663  C CG2   . THR B 2 589  ? 145.067 180.410 178.562 1.00 51.69  ? 586  THR A CG2   1 
ATOM   4664  N N     . SER B 2 590  ? 146.783 178.346 176.886 1.00 48.55  ? 587  SER A N     1 
ATOM   4665  C CA    . SER B 2 590  ? 148.144 177.840 176.987 1.00 48.55  ? 587  SER A CA    1 
ATOM   4666  C C     . SER B 2 590  ? 148.555 177.151 175.692 1.00 48.55  ? 587  SER A C     1 
ATOM   4667  O O     . SER B 2 590  ? 147.764 176.440 175.068 1.00 48.55  ? 587  SER A O     1 
ATOM   4668  C CB    . SER B 2 590  ? 148.265 176.868 178.160 1.00 48.55  ? 587  SER A CB    1 
ATOM   4669  O OG    . SER B 2 590  ? 147.482 175.708 177.942 1.00 48.55  ? 587  SER A OG    1 
ATOM   4670  N N     . GLU B 2 591  ? 149.803 177.369 175.288 1.00 48.55  ? 588  GLU A N     1 
ATOM   4671  C CA    . GLU B 2 591  ? 150.330 176.740 174.088 1.00 48.55  ? 588  GLU A CA    1 
ATOM   4672  C C     . GLU B 2 591  ? 150.621 175.266 174.343 1.00 48.55  ? 588  GLU A C     1 
ATOM   4673  O O     . GLU B 2 591  ? 150.957 174.859 175.459 1.00 48.55  ? 588  GLU A O     1 
ATOM   4674  C CB    . GLU B 2 591  ? 151.599 177.453 173.618 1.00 48.55  ? 588  GLU A CB    1 
ATOM   4675  C CG    . GLU B 2 591  ? 152.803 177.274 174.532 1.00 48.55  ? 588  GLU A CG    1 
ATOM   4676  C CD    . GLU B 2 591  ? 152.828 178.267 175.679 1.00 48.55  ? 588  GLU A CD    1 
ATOM   4677  O OE1   . GLU B 2 591  ? 151.785 178.897 175.952 1.00 48.55  ? 588  GLU A OE1   1 
ATOM   4678  O OE2   . GLU B 2 591  ? 153.895 178.417 176.311 1.00 48.55  ? 588  GLU A OE2   1 
ATOM   4679  N N     . GLY B 2 592  ? 150.478 174.466 173.300 1.00 48.55  ? 589  GLY A N     1 
ATOM   4680  C CA    . GLY B 2 592  ? 150.757 173.050 173.391 1.00 48.55  ? 589  GLY A CA    1 
ATOM   4681  C C     . GLY B 2 592  ? 149.939 172.271 172.382 1.00 48.55  ? 589  GLY A C     1 
ATOM   4682  O O     . GLY B 2 592  ? 149.368 172.828 171.449 1.00 48.55  ? 589  GLY A O     1 
ATOM   4683  N N     . PHE B 2 593  ? 149.899 170.961 172.598 1.00 48.55  ? 590  PHE A N     1 
ATOM   4684  C CA    . PHE B 2 593  ? 149.188 170.052 171.716 1.00 48.55  ? 590  PHE A CA    1 
ATOM   4685  C C     . PHE B 2 593  ? 147.734 169.906 172.154 1.00 48.55  ? 590  PHE A C     1 
ATOM   4686  O O     . PHE B 2 593  ? 147.367 170.192 173.296 1.00 48.55  ? 590  PHE A O     1 
ATOM   4687  C CB    . PHE B 2 593  ? 149.865 168.680 171.698 1.00 48.55  ? 590  PHE A CB    1 
ATOM   4688  C CG    . PHE B 2 593  ? 151.310 168.715 171.288 1.00 48.55  ? 590  PHE A CG    1 
ATOM   4689  C CD1   . PHE B 2 593  ? 152.295 169.083 172.188 1.00 48.55  ? 590  PHE A CD1   1 
ATOM   4690  C CD2   . PHE B 2 593  ? 151.684 168.365 170.004 1.00 48.55  ? 590  PHE A CD2   1 
ATOM   4691  C CE1   . PHE B 2 593  ? 153.623 169.113 171.811 1.00 48.55  ? 590  PHE A CE1   1 
ATOM   4692  C CE2   . PHE B 2 593  ? 153.009 168.391 169.621 1.00 48.55  ? 590  PHE A CE2   1 
ATOM   4693  C CZ    . PHE B 2 593  ? 153.980 168.765 170.526 1.00 48.55  ? 590  PHE A CZ    1 
ATOM   4694  N N     . ASP B 2 594  ? 146.903 169.448 171.223 1.00 48.55  ? 591  ASP A N     1 
ATOM   4695  C CA    . ASP B 2 594  ? 145.490 169.190 171.477 1.00 48.55  ? 591  ASP A CA    1 
ATOM   4696  C C     . ASP B 2 594  ? 145.256 167.691 171.355 1.00 48.55  ? 591  ASP A C     1 
ATOM   4697  O O     . ASP B 2 594  ? 145.177 167.157 170.243 1.00 48.55  ? 591  ASP A O     1 
ATOM   4698  C CB    . ASP B 2 594  ? 144.606 169.966 170.504 1.00 48.55  ? 591  ASP A CB    1 
ATOM   4699  C CG    . ASP B 2 594  ? 144.646 171.460 170.745 1.00 48.55  ? 591  ASP A CG    1 
ATOM   4700  O OD1   . ASP B 2 594  ? 144.862 171.870 171.904 1.00 48.55  ? 591  ASP A OD1   1 
ATOM   4701  O OD2   . ASP B 2 594  ? 144.461 172.225 169.775 1.00 48.55  ? 591  ASP A OD2   1 
ATOM   4702  N N     . LYS B 2 595  ? 145.142 167.016 172.494 1.00 48.55  ? 592  LYS A N     1 
ATOM   4703  C CA    . LYS B 2 595  ? 144.988 165.570 172.505 1.00 48.55  ? 592  LYS A CA    1 
ATOM   4704  C C     . LYS B 2 595  ? 143.588 165.172 172.059 1.00 48.55  ? 592  LYS A C     1 
ATOM   4705  O O     . LYS B 2 595  ? 142.596 165.797 172.442 1.00 48.55  ? 592  LYS A O     1 
ATOM   4706  C CB    . LYS B 2 595  ? 145.268 165.017 173.901 1.00 48.55  ? 592  LYS A CB    1 
ATOM   4707  C CG    . LYS B 2 595  ? 144.931 163.548 174.067 1.00 48.55  ? 592  LYS A CG    1 
ATOM   4708  C CD    . LYS B 2 595  ? 145.732 162.918 175.188 1.00 48.55  ? 592  LYS A CD    1 
ATOM   4709  C CE    . LYS B 2 595  ? 144.917 161.860 175.904 1.00 48.55  ? 592  LYS A CE    1 
ATOM   4710  N NZ    . LYS B 2 595  ? 144.325 160.892 174.941 1.00 48.55  ? 592  LYS A NZ    1 
ATOM   4711  N N     . MET B 2 596  ? 143.516 164.124 171.245 1.00 48.55  ? 593  MET A N     1 
ATOM   4712  C CA    . MET B 2 596  ? 142.239 163.586 170.800 1.00 48.55  ? 593  MET A CA    1 
ATOM   4713  C C     . MET B 2 596  ? 141.696 162.634 171.857 1.00 48.55  ? 593  MET A C     1 
ATOM   4714  O O     . MET B 2 596  ? 142.359 161.656 172.218 1.00 48.55  ? 593  MET A O     1 
ATOM   4715  C CB    . MET B 2 596  ? 142.399 162.867 169.463 1.00 48.55  ? 593  MET A CB    1 
ATOM   4716  C CG    . MET B 2 596  ? 141.178 162.074 169.038 1.00 48.55  ? 593  MET A CG    1 
ATOM   4717  S SD    . MET B 2 596  ? 141.606 160.538 168.204 1.00 48.55  ? 593  MET A SD    1 
ATOM   4718  C CE    . MET B 2 596  ? 142.304 159.600 169.559 1.00 48.55  ? 593  MET A CE    1 
ATOM   4719  N N     . TYR B 2 597  ? 140.496 162.918 172.354 1.00 48.55  ? 594  TYR A N     1 
ATOM   4720  C CA    . TYR B 2 597  ? 139.814 162.043 173.299 1.00 48.55  ? 594  TYR A CA    1 
ATOM   4721  C C     . TYR B 2 597  ? 138.753 161.259 172.538 1.00 48.55  ? 594  TYR A C     1 
ATOM   4722  O O     . TYR B 2 597  ? 137.771 161.831 172.054 1.00 48.55  ? 594  TYR A O     1 
ATOM   4723  C CB    . TYR B 2 597  ? 139.205 162.840 174.450 1.00 48.55  ? 594  TYR A CB    1 
ATOM   4724  C CG    . TYR B 2 597  ? 140.219 163.255 175.488 1.00 48.55  ? 594  TYR A CG    1 
ATOM   4725  C CD1   . TYR B 2 597  ? 140.949 164.426 175.345 1.00 48.55  ? 594  TYR A CD1   1 
ATOM   4726  C CD2   . TYR B 2 597  ? 140.459 162.466 176.603 1.00 48.55  ? 594  TYR A CD2   1 
ATOM   4727  C CE1   . TYR B 2 597  ? 141.880 164.804 176.289 1.00 48.55  ? 594  TYR A CE1   1 
ATOM   4728  C CE2   . TYR B 2 597  ? 141.389 162.836 177.552 1.00 48.55  ? 594  TYR A CE2   1 
ATOM   4729  C CZ    . TYR B 2 597  ? 142.097 164.006 177.390 1.00 48.55  ? 594  TYR A CZ    1 
ATOM   4730  O OH    . TYR B 2 597  ? 143.025 164.379 178.334 1.00 48.55  ? 594  TYR A OH    1 
ATOM   4731  N N     . TYR B 2 598  ? 138.959 159.953 172.435 1.00 48.55  ? 595  TYR A N     1 
ATOM   4732  C CA    . TYR B 2 598  ? 138.110 159.067 171.650 1.00 48.55  ? 595  TYR A CA    1 
ATOM   4733  C C     . TYR B 2 598  ? 137.189 158.321 172.607 1.00 48.55  ? 595  TYR A C     1 
ATOM   4734  O O     . TYR B 2 598  ? 137.655 157.581 173.477 1.00 48.55  ? 595  TYR A O     1 
ATOM   4735  C CB    . TYR B 2 598  ? 138.977 158.104 170.842 1.00 48.55  ? 595  TYR A CB    1 
ATOM   4736  C CG    . TYR B 2 598  ? 138.265 157.295 169.783 1.00 48.55  ? 595  TYR A CG    1 
ATOM   4737  C CD1   . TYR B 2 598  ? 137.677 156.078 170.091 1.00 48.55  ? 595  TYR A CD1   1 
ATOM   4738  C CD2   . TYR B 2 598  ? 138.221 157.728 168.467 1.00 48.55  ? 595  TYR A CD2   1 
ATOM   4739  C CE1   . TYR B 2 598  ? 137.043 155.329 169.124 1.00 48.55  ? 595  TYR A CE1   1 
ATOM   4740  C CE2   . TYR B 2 598  ? 137.590 156.985 167.494 1.00 48.55  ? 595  TYR A CE2   1 
ATOM   4741  C CZ    . TYR B 2 598  ? 137.002 155.787 167.827 1.00 48.55  ? 595  TYR A CZ    1 
ATOM   4742  O OH    . TYR B 2 598  ? 136.369 155.042 166.860 1.00 48.55  ? 595  TYR A OH    1 
ATOM   4743  N N     . ASP B 2 599  ? 135.886 158.533 172.462 1.00 48.55  ? 596  ASP A N     1 
ATOM   4744  C CA    . ASP B 2 599  ? 134.882 157.830 173.250 1.00 48.55  ? 596  ASP A CA    1 
ATOM   4745  C C     . ASP B 2 599  ? 134.042 156.983 172.307 1.00 48.55  ? 596  ASP A C     1 
ATOM   4746  O O     . ASP B 2 599  ? 133.473 157.503 171.341 1.00 48.55  ? 596  ASP A O     1 
ATOM   4747  C CB    . ASP B 2 599  ? 134.006 158.810 174.029 1.00 48.55  ? 596  ASP A CB    1 
ATOM   4748  C CG    . ASP B 2 599  ? 134.653 159.270 175.319 1.00 48.55  ? 596  ASP A CG    1 
ATOM   4749  O OD1   . ASP B 2 599  ? 135.304 158.440 175.986 1.00 48.55  ? 596  ASP A OD1   1 
ATOM   4750  O OD2   . ASP B 2 599  ? 134.512 160.461 175.666 1.00 48.55  ? 596  ASP A OD2   1 
ATOM   4751  N N     . TYR B 2 600  ? 133.965 155.685 172.587 1.00 48.55  ? 597  TYR A N     1 
ATOM   4752  C CA    . TYR B 2 600  ? 133.262 154.756 171.719 1.00 48.55  ? 597  TYR A CA    1 
ATOM   4753  C C     . TYR B 2 600  ? 132.505 153.742 172.561 1.00 48.55  ? 597  TYR A C     1 
ATOM   4754  O O     . TYR B 2 600  ? 132.893 153.428 173.689 1.00 48.55  ? 597  TYR A O     1 
ATOM   4755  C CB    . TYR B 2 600  ? 134.228 154.035 170.770 1.00 48.55  ? 597  TYR A CB    1 
ATOM   4756  C CG    . TYR B 2 600  ? 133.547 153.285 169.649 1.00 48.55  ? 597  TYR A CG    1 
ATOM   4757  C CD1   . TYR B 2 600  ? 132.399 153.782 169.052 1.00 48.55  ? 597  TYR A CD1   1 
ATOM   4758  C CD2   . TYR B 2 600  ? 134.056 152.079 169.189 1.00 48.55  ? 597  TYR A CD2   1 
ATOM   4759  C CE1   . TYR B 2 600  ? 131.774 153.099 168.030 1.00 48.55  ? 597  TYR A CE1   1 
ATOM   4760  C CE2   . TYR B 2 600  ? 133.438 151.389 168.166 1.00 48.55  ? 597  TYR A CE2   1 
ATOM   4761  C CZ    . TYR B 2 600  ? 132.298 151.903 167.590 1.00 48.55  ? 597  TYR A CZ    1 
ATOM   4762  O OH    . TYR B 2 600  ? 131.678 151.219 166.570 1.00 48.55  ? 597  TYR A OH    1 
ATOM   4763  N N     . PHE B 2 601  ? 131.418 153.238 171.995 1.00 58.84  ? 598  PHE A N     1 
ATOM   4764  C CA    . PHE B 2 601  ? 130.583 152.228 172.644 1.00 58.84  ? 598  PHE A CA    1 
ATOM   4765  C C     . PHE B 2 601  ? 130.014 151.391 171.510 1.00 58.84  ? 598  PHE A C     1 
ATOM   4766  O O     . PHE B 2 601  ? 129.073 151.818 170.823 1.00 58.84  ? 598  PHE A O     1 
ATOM   4767  C CB    . PHE B 2 601  ? 129.480 152.864 173.486 1.00 58.84  ? 598  PHE A CB    1 
ATOM   4768  C CG    . PHE B 2 601  ? 129.043 152.029 174.654 1.00 58.84  ? 598  PHE A CG    1 
ATOM   4769  C CD1   . PHE B 2 601  ? 129.970 151.537 175.555 1.00 58.84  ? 598  PHE A CD1   1 
ATOM   4770  C CD2   . PHE B 2 601  ? 127.702 151.770 174.874 1.00 58.84  ? 598  PHE A CD2   1 
ATOM   4771  C CE1   . PHE B 2 601  ? 129.571 150.780 176.637 1.00 58.84  ? 598  PHE A CE1   1 
ATOM   4772  C CE2   . PHE B 2 601  ? 127.296 151.019 175.956 1.00 58.84  ? 598  PHE A CE2   1 
ATOM   4773  C CZ    . PHE B 2 601  ? 128.232 150.522 176.838 1.00 58.84  ? 598  PHE A CZ    1 
ATOM   4774  N N     . PRO B 2 602  ? 130.565 150.190 171.273 1.00 64.37  ? 599  PRO A N     1 
ATOM   4775  C CA    . PRO B 2 602  ? 130.373 149.501 169.985 1.00 64.37  ? 599  PRO A CA    1 
ATOM   4776  C C     . PRO B 2 602  ? 128.940 149.427 169.476 1.00 64.37  ? 599  PRO A C     1 
ATOM   4777  O O     . PRO B 2 602  ? 128.652 149.912 168.377 1.00 64.37  ? 599  PRO A O     1 
ATOM   4778  C CB    . PRO B 2 602  ? 130.923 148.098 170.267 1.00 64.37  ? 599  PRO A CB    1 
ATOM   4779  C CG    . PRO B 2 602  ? 131.967 148.317 171.305 1.00 64.37  ? 599  PRO A CG    1 
ATOM   4780  C CD    . PRO B 2 602  ? 131.484 149.458 172.163 1.00 64.37  ? 599  PRO A CD    1 
ATOM   4781  N N     . ASP B 2 603  ? 128.035 148.837 170.254 1.00 68.32  ? 600  ASP A N     1 
ATOM   4782  C CA    . ASP B 2 603  ? 126.652 148.697 169.818 1.00 68.32  ? 600  ASP A CA    1 
ATOM   4783  C C     . ASP B 2 603  ? 125.780 148.416 171.030 1.00 68.32  ? 600  ASP A C     1 
ATOM   4784  O O     . ASP B 2 603  ? 126.155 147.617 171.893 1.00 68.32  ? 600  ASP A O     1 
ATOM   4785  C CB    . ASP B 2 603  ? 126.515 147.578 168.781 1.00 68.32  ? 600  ASP A CB    1 
ATOM   4786  C CG    . ASP B 2 603  ? 125.112 147.473 168.211 1.00 68.32  ? 600  ASP A CG    1 
ATOM   4787  O OD1   . ASP B 2 603  ? 124.300 148.394 168.433 1.00 68.32  ? 600  ASP A OD1   1 
ATOM   4788  O OD2   . ASP B 2 603  ? 124.822 146.462 167.537 1.00 68.32  ? 600  ASP A OD2   1 
ATOM   4789  N N     . ALA B 2 604  ? 124.619 149.070 171.088 1.00 68.83  ? 601  ALA A N     1 
ATOM   4790  C CA    . ALA B 2 604  ? 123.747 148.924 172.247 1.00 68.83  ? 601  ALA A CA    1 
ATOM   4791  C C     . ALA B 2 604  ? 123.089 147.550 172.281 1.00 68.83  ? 601  ALA A C     1 
ATOM   4792  O O     . ALA B 2 604  ? 122.710 147.062 173.352 1.00 68.83  ? 601  ALA A O     1 
ATOM   4793  C CB    . ALA B 2 604  ? 122.691 150.027 172.249 1.00 68.83  ? 601  ALA A CB    1 
ATOM   4794  N N     . ALA B 2 605  ? 122.939 146.911 171.118 1.00 72.37  ? 602  ALA A N     1 
ATOM   4795  C CA    . ALA B 2 605  ? 122.331 145.585 171.079 1.00 72.37  ? 602  ALA A CA    1 
ATOM   4796  C C     . ALA B 2 605  ? 123.195 144.549 171.785 1.00 72.37  ? 602  ALA A C     1 
ATOM   4797  O O     . ALA B 2 605  ? 122.709 143.469 172.137 1.00 72.37  ? 602  ALA A O     1 
ATOM   4798  C CB    . ALA B 2 605  ? 122.075 145.164 169.632 1.00 72.37  ? 602  ALA A CB    1 
ATOM   4799  N N     . LYS B 2 606  ? 124.472 144.859 171.999 1.00 72.45  ? 603  LYS A N     1 
ATOM   4800  C CA    . LYS B 2 606  ? 125.416 143.945 172.627 1.00 72.45  ? 603  LYS A CA    1 
ATOM   4801  C C     . LYS B 2 606  ? 126.069 144.506 173.880 1.00 72.45  ? 603  LYS A C     1 
ATOM   4802  O O     . LYS B 2 606  ? 126.300 143.753 174.827 1.00 72.45  ? 603  LYS A O     1 
ATOM   4803  C CB    . LYS B 2 606  ? 126.504 143.552 171.619 1.00 72.45  ? 603  LYS A CB    1 
ATOM   4804  C CG    . LYS B 2 606  ? 127.112 144.741 170.888 1.00 72.45  ? 603  LYS A CG    1 
ATOM   4805  C CD    . LYS B 2 606  ? 128.032 144.319 169.754 1.00 72.45  ? 603  LYS A CD    1 
ATOM   4806  C CE    . LYS B 2 606  ? 127.266 143.651 168.625 1.00 72.45  ? 603  LYS A CE    1 
ATOM   4807  N NZ    . LYS B 2 606  ? 126.285 144.536 167.948 1.00 72.45  ? 603  LYS A NZ    1 
ATOM   4808  N N     . MET B 2 607  ? 126.369 145.805 173.908 1.00 72.02  ? 604  MET A N     1 
ATOM   4809  C CA    . MET B 2 607  ? 126.993 146.407 175.084 1.00 72.02  ? 604  MET A CA    1 
ATOM   4810  C C     . MET B 2 607  ? 126.053 146.409 176.283 1.00 72.02  ? 604  MET A C     1 
ATOM   4811  O O     . MET B 2 607  ? 126.433 145.984 177.380 1.00 72.02  ? 604  MET A O     1 
ATOM   4812  C CB    . MET B 2 607  ? 127.443 147.832 174.762 1.00 72.02  ? 604  MET A CB    1 
ATOM   4813  C CG    . MET B 2 607  ? 128.846 147.960 174.202 1.00 72.02  ? 604  MET A CG    1 
ATOM   4814  S SD    . MET B 2 607  ? 130.078 147.197 175.273 1.00 72.02  ? 604  MET A SD    1 
ATOM   4815  C CE    . MET B 2 607  ? 130.922 146.138 174.113 1.00 72.02  ? 604  MET A CE    1 
ATOM   4816  N N     . ILE B 2 608  ? 124.824 146.899 176.098 1.00 71.98  ? 605  ILE A N     1 
ATOM   4817  C CA    . ILE B 2 608  ? 123.932 147.113 177.239 1.00 71.98  ? 605  ILE A CA    1 
ATOM   4818  C C     . ILE B 2 608  ? 123.609 145.818 177.976 1.00 71.98  ? 605  ILE A C     1 
ATOM   4819  O O     . ILE B 2 608  ? 123.715 145.797 179.214 1.00 71.98  ? 605  ILE A O     1 
ATOM   4820  C CB    . ILE B 2 608  ? 122.672 147.875 176.792 1.00 71.98  ? 605  ILE A CB    1 
ATOM   4821  C CG1   . ILE B 2 608  ? 123.048 149.024 175.856 1.00 71.98  ? 605  ILE A CG1   1 
ATOM   4822  C CG2   . ILE B 2 608  ? 121.912 148.396 177.999 1.00 71.98  ? 605  ILE A CG2   1 
ATOM   4823  C CD1   . ILE B 2 608  ? 123.815 150.137 176.530 1.00 71.98  ? 605  ILE A CD1   1 
ATOM   4824  N N     . PRO B 2 609  ? 123.206 144.725 177.313 1.00 74.61  ? 606  PRO A N     1 
ATOM   4825  C CA    . PRO B 2 609  ? 123.011 143.476 178.068 1.00 74.61  ? 606  PRO A CA    1 
ATOM   4826  C C     . PRO B 2 609  ? 124.280 142.981 178.737 1.00 74.61  ? 606  PRO A C     1 
ATOM   4827  O O     . PRO B 2 609  ? 124.218 142.399 179.827 1.00 74.61  ? 606  PRO A O     1 
ATOM   4828  C CB    . PRO B 2 609  ? 122.509 142.496 176.998 1.00 74.61  ? 606  PRO A CB    1 
ATOM   4829  C CG    . PRO B 2 609  ? 121.921 143.358 175.945 1.00 74.61  ? 606  PRO A CG    1 
ATOM   4830  C CD    . PRO B 2 609  ? 122.803 144.565 175.904 1.00 74.61  ? 606  PRO A CD    1 
ATOM   4831  N N     . LYS B 2 610  ? 125.438 143.206 178.112 1.00 71.11  ? 607  LYS A N     1 
ATOM   4832  C CA    . LYS B 2 610  ? 126.694 142.723 178.675 1.00 71.11  ? 607  LYS A CA    1 
ATOM   4833  C C     . LYS B 2 610  ? 127.060 143.471 179.951 1.00 71.11  ? 607  LYS A C     1 
ATOM   4834  O O     . LYS B 2 610  ? 127.580 142.873 180.899 1.00 71.11  ? 607  LYS A O     1 
ATOM   4835  C CB    . LYS B 2 610  ? 127.810 142.852 177.639 1.00 71.11  ? 607  LYS A CB    1 
ATOM   4836  C CG    . LYS B 2 610  ? 129.210 142.682 178.198 1.00 71.11  ? 607  LYS A CG    1 
ATOM   4837  C CD    . LYS B 2 610  ? 130.255 143.067 177.169 1.00 71.11  ? 607  LYS A CD    1 
ATOM   4838  C CE    . LYS B 2 610  ? 131.655 142.829 177.694 1.00 71.11  ? 607  LYS A CE    1 
ATOM   4839  N NZ    . LYS B 2 610  ? 131.865 141.409 178.083 1.00 71.11  ? 607  LYS A NZ    1 
ATOM   4840  N N     . CYS B 2 611  ? 126.791 144.774 179.997 1.00 78.21  ? 608  CYS A N     1 
ATOM   4841  C CA    . CYS B 2 611  ? 127.219 145.599 181.119 1.00 78.21  ? 608  CYS A CA    1 
ATOM   4842  C C     . CYS B 2 611  ? 126.154 145.770 182.193 1.00 78.21  ? 608  CYS A C     1 
ATOM   4843  O O     . CYS B 2 611  ? 126.485 146.187 183.308 1.00 78.21  ? 608  CYS A O     1 
ATOM   4844  C CB    . CYS B 2 611  ? 127.651 146.981 180.620 1.00 78.21  ? 608  CYS A CB    1 
ATOM   4845  S SG    . CYS B 2 611  ? 129.088 146.968 179.524 1.00 78.21  ? 608  CYS A SG    1 
ATOM   4846  N N     . SER B 2 612  ? 124.891 145.464 181.895 1.00 83.09  ? 609  SER A N     1 
ATOM   4847  C CA    . SER B 2 612  ? 123.800 145.705 182.830 1.00 83.09  ? 609  SER A CA    1 
ATOM   4848  C C     . SER B 2 612  ? 123.144 144.418 183.314 1.00 83.09  ? 609  SER A C     1 
ATOM   4849  O O     . SER B 2 612  ? 123.054 144.188 184.523 1.00 83.09  ? 609  SER A O     1 
ATOM   4850  C CB    . SER B 2 612  ? 122.753 146.622 182.183 1.00 83.09  ? 609  SER A CB    1 
ATOM   4851  O OG    . SER B 2 612  ? 121.976 145.915 181.232 1.00 83.09  ? 609  SER A OG    1 
ATOM   4852  N N     . THR B 2 613  ? 122.680 143.567 182.401 1.00 88.30  ? 610  THR A N     1 
ATOM   4853  C CA    . THR B 2 613  ? 121.872 142.416 182.785 1.00 88.30  ? 610  THR A CA    1 
ATOM   4854  C C     . THR B 2 613  ? 122.685 141.127 182.856 1.00 88.30  ? 610  THR A C     1 
ATOM   4855  O O     . THR B 2 613  ? 122.565 140.369 183.824 1.00 88.30  ? 610  THR A O     1 
ATOM   4856  C CB    . THR B 2 613  ? 120.706 142.245 181.807 1.00 88.30  ? 610  THR A CB    1 
ATOM   4857  O OG1   . THR B 2 613  ? 119.896 143.428 181.815 1.00 88.30  ? 610  THR A OG1   1 
ATOM   4858  C CG2   . THR B 2 613  ? 119.850 141.051 182.200 1.00 88.30  ? 610  THR A CG2   1 
ATOM   4859  N N     . GLN B 2 614  ? 123.519 140.864 181.849 1.00 87.46  ? 611  GLN A N     1 
ATOM   4860  C CA    . GLN B 2 614  ? 124.245 139.603 181.750 1.00 87.46  ? 611  GLN A CA    1 
ATOM   4861  C C     . GLN B 2 614  ? 125.577 139.622 182.492 1.00 87.46  ? 611  GLN A C     1 
ATOM   4862  O O     . GLN B 2 614  ? 126.487 138.860 182.139 1.00 87.46  ? 611  GLN A O     1 
ATOM   4863  C CB    . GLN B 2 614  ? 124.455 139.229 180.283 1.00 87.46  ? 611  GLN A CB    1 
ATOM   4864  C CG    . GLN B 2 614  ? 123.337 138.381 179.699 1.00 87.46  ? 611  GLN A CG    1 
ATOM   4865  C CD    . GLN B 2 614  ? 122.073 139.173 179.442 1.00 87.46  ? 611  GLN A CD    1 
ATOM   4866  O OE1   . GLN B 2 614  ? 122.089 140.403 179.430 1.00 87.46  ? 611  GLN A OE1   1 
ATOM   4867  N NE2   . GLN B 2 614  ? 120.966 138.469 179.237 1.00 87.46  ? 611  GLN A NE2   1 
ATOM   4868  N N     . LEU B 2 615  ? 125.721 140.474 183.504 1.00 94.44  ? 612  LEU A N     1 
ATOM   4869  C CA    . LEU B 2 615  ? 126.864 140.363 184.399 1.00 94.44  ? 612  LEU A CA    1 
ATOM   4870  C C     . LEU B 2 615  ? 126.805 139.032 185.136 1.00 94.44  ? 612  LEU A C     1 
ATOM   4871  O O     . LEU B 2 615  ? 125.724 138.528 185.453 1.00 94.44  ? 612  LEU A O     1 
ATOM   4872  C CB    . LEU B 2 615  ? 126.881 141.519 185.400 1.00 94.44  ? 612  LEU A CB    1 
ATOM   4873  C CG    . LEU B 2 615  ? 126.788 142.940 184.846 1.00 94.44  ? 612  LEU A CG    1 
ATOM   4874  C CD1   . LEU B 2 615  ? 126.628 143.942 185.975 1.00 94.44  ? 612  LEU A CD1   1 
ATOM   4875  C CD2   . LEU B 2 615  ? 128.014 143.265 184.024 1.00 94.44  ? 612  LEU A CD2   1 
ATOM   4876  N N     . LYS B 2 616  ? 127.979 138.454 185.398 1.00 105.98 ? 613  LYS A N     1 
ATOM   4877  C CA    . LYS B 2 616  ? 128.030 137.145 186.041 1.00 105.98 ? 613  LYS A CA    1 
ATOM   4878  C C     . LYS B 2 616  ? 127.392 137.186 187.425 1.00 105.98 ? 613  LYS A C     1 
ATOM   4879  O O     . LYS B 2 616  ? 126.644 136.278 187.805 1.00 105.98 ? 613  LYS A O     1 
ATOM   4880  C CB    . LYS B 2 616  ? 129.476 136.658 186.126 1.00 105.98 ? 613  LYS A CB    1 
ATOM   4881  C CG    . LYS B 2 616  ? 129.611 135.162 186.356 1.00 105.98 ? 613  LYS A CG    1 
ATOM   4882  C CD    . LYS B 2 616  ? 130.959 134.651 185.879 1.00 105.98 ? 613  LYS A CD    1 
ATOM   4883  C CE    . LYS B 2 616  ? 131.045 134.657 184.361 1.00 105.98 ? 613  LYS A CE    1 
ATOM   4884  N NZ    . LYS B 2 616  ? 129.956 133.854 183.740 1.00 105.98 ? 613  LYS A NZ    1 
ATOM   4885  N N     . ALA B 2 617  ? 127.680 138.237 188.196 1.00 108.85 ? 614  ALA A N     1 
ATOM   4886  C CA    . ALA B 2 617  ? 127.081 138.366 189.520 1.00 108.85 ? 614  ALA A CA    1 
ATOM   4887  C C     . ALA B 2 617  ? 125.573 138.567 189.431 1.00 108.85 ? 614  ALA A C     1 
ATOM   4888  O O     . ALA B 2 617  ? 124.814 137.976 190.207 1.00 108.85 ? 614  ALA A O     1 
ATOM   4889  C CB    . ALA B 2 617  ? 127.733 139.521 190.280 1.00 108.85 ? 614  ALA A CB    1 
ATOM   4890  N N     . VAL B 2 618  ? 125.121 139.400 188.491 1.00 106.20 ? 615  VAL A N     1 
ATOM   4891  C CA    . VAL B 2 618  ? 123.696 139.705 188.389 1.00 106.20 ? 615  VAL A CA    1 
ATOM   4892  C C     . VAL B 2 618  ? 122.920 138.497 187.879 1.00 106.20 ? 615  VAL A C     1 
ATOM   4893  O O     . VAL B 2 618  ? 121.841 138.174 188.390 1.00 106.20 ? 615  VAL A O     1 
ATOM   4894  C CB    . VAL B 2 618  ? 123.478 140.939 187.494 1.00 106.20 ? 615  VAL A CB    1 
ATOM   4895  C CG1   . VAL B 2 618  ? 121.995 141.246 187.362 1.00 106.20 ? 615  VAL A CG1   1 
ATOM   4896  C CG2   . VAL B 2 618  ? 124.222 142.137 188.060 1.00 106.20 ? 615  VAL A CG2   1 
ATOM   4897  N N     . THR B 2 619  ? 123.451 137.815 186.861 1.00 107.74 ? 616  THR A N     1 
ATOM   4898  C CA    . THR B 2 619  ? 122.736 136.685 186.275 1.00 107.74 ? 616  THR A CA    1 
ATOM   4899  C C     . THR B 2 619  ? 122.562 135.552 187.280 1.00 107.74 ? 616  THR A C     1 
ATOM   4900  O O     . THR B 2 619  ? 121.486 134.950 187.369 1.00 107.74 ? 616  THR A O     1 
ATOM   4901  C CB    . THR B 2 619  ? 123.470 136.184 185.031 1.00 107.74 ? 616  THR A CB    1 
ATOM   4902  O OG1   . THR B 2 619  ? 123.738 137.287 184.156 1.00 107.74 ? 616  THR A OG1   1 
ATOM   4903  C CG2   . THR B 2 619  ? 122.628 135.153 184.293 1.00 107.74 ? 616  THR A CG2   1 
ATOM   4904  N N     . ALA B 2 620  ? 123.613 135.245 188.044 1.00 112.36 ? 617  ALA A N     1 
ATOM   4905  C CA    . ALA B 2 620  ? 123.528 134.164 189.020 1.00 112.36 ? 617  ALA A CA    1 
ATOM   4906  C C     . ALA B 2 620  ? 122.533 134.491 190.126 1.00 112.36 ? 617  ALA A C     1 
ATOM   4907  O O     . ALA B 2 620  ? 121.773 133.620 190.565 1.00 112.36 ? 617  ALA A O     1 
ATOM   4908  C CB    . ALA B 2 620  ? 124.909 133.877 189.607 1.00 112.36 ? 617  ALA A CB    1 
ATOM   4909  N N     . HIS B 2 621  ? 122.530 135.741 190.595 1.00 113.47 ? 618  HIS A N     1 
ATOM   4910  C CA    . HIS B 2 621  ? 121.635 136.125 191.683 1.00 113.47 ? 618  HIS A CA    1 
ATOM   4911  C C     . HIS B 2 621  ? 120.173 136.009 191.270 1.00 113.47 ? 618  HIS A C     1 
ATOM   4912  O O     . HIS B 2 621  ? 119.341 135.510 192.037 1.00 113.47 ? 618  HIS A O     1 
ATOM   4913  C CB    . HIS B 2 621  ? 121.955 137.550 192.139 1.00 113.47 ? 618  HIS A CB    1 
ATOM   4914  C CG    . HIS B 2 621  ? 120.944 138.130 193.079 1.00 113.47 ? 618  HIS A CG    1 
ATOM   4915  N ND1   . HIS B 2 621  ? 119.780 138.729 192.645 1.00 113.47 ? 618  HIS A ND1   1 
ATOM   4916  C CD2   . HIS B 2 621  ? 120.927 138.212 194.430 1.00 113.47 ? 618  HIS A CD2   1 
ATOM   4917  C CE1   . HIS B 2 621  ? 119.088 139.149 193.689 1.00 113.47 ? 618  HIS A CE1   1 
ATOM   4918  N NE2   . HIS B 2 621  ? 119.762 138.848 194.784 1.00 113.47 ? 618  HIS A NE2   1 
ATOM   4919  N N     . PHE B 2 622  ? 119.839 136.461 190.059 1.00 116.75 ? 619  PHE A N     1 
ATOM   4920  C CA    . PHE B 2 622  ? 118.443 136.465 189.635 1.00 116.75 ? 619  PHE A CA    1 
ATOM   4921  C C     . PHE B 2 622  ? 117.961 135.071 189.261 1.00 116.75 ? 619  PHE A C     1 
ATOM   4922  O O     . PHE B 2 622  ? 116.777 134.761 189.435 1.00 116.75 ? 619  PHE A O     1 
ATOM   4923  C CB    . PHE B 2 622  ? 118.254 137.425 188.463 1.00 116.75 ? 619  PHE A CB    1 
ATOM   4924  C CG    . PHE B 2 622  ? 117.979 138.835 188.885 1.00 116.75 ? 619  PHE A CG    1 
ATOM   4925  C CD1   . PHE B 2 622  ? 116.796 139.166 189.525 1.00 116.75 ? 619  PHE A CD1   1 
ATOM   4926  C CD2   . PHE B 2 622  ? 118.912 139.829 188.653 1.00 116.75 ? 619  PHE A CD2   1 
ATOM   4927  C CE1   . PHE B 2 622  ? 116.547 140.466 189.918 1.00 116.75 ? 619  PHE A CE1   1 
ATOM   4928  C CE2   . PHE B 2 622  ? 118.670 141.126 189.044 1.00 116.75 ? 619  PHE A CE2   1 
ATOM   4929  C CZ    . PHE B 2 622  ? 117.486 141.448 189.676 1.00 116.75 ? 619  PHE A CZ    1 
ATOM   4930  N N     . GLN B 2 623  ? 118.851 134.227 188.738 1.00 115.20 ? 620  GLN A N     1 
ATOM   4931  C CA    . GLN B 2 623  ? 118.458 132.862 188.409 1.00 115.20 ? 620  GLN A CA    1 
ATOM   4932  C C     . GLN B 2 623  ? 118.044 132.102 189.663 1.00 115.20 ? 620  GLN A C     1 
ATOM   4933  O O     . GLN B 2 623  ? 117.086 131.320 189.636 1.00 115.20 ? 620  GLN A O     1 
ATOM   4934  C CB    . GLN B 2 623  ? 119.603 132.145 187.691 1.00 115.20 ? 620  GLN A CB    1 
ATOM   4935  C CG    . GLN B 2 623  ? 119.351 130.671 187.402 1.00 115.20 ? 620  GLN A CG    1 
ATOM   4936  C CD    . GLN B 2 623  ? 118.047 130.431 186.663 1.00 115.20 ? 620  GLN A CD    1 
ATOM   4937  O OE1   . GLN B 2 623  ? 117.720 131.143 185.714 1.00 115.20 ? 620  GLN A OE1   1 
ATOM   4938  N NE2   . GLN B 2 623  ? 117.298 129.421 187.093 1.00 115.20 ? 620  GLN A NE2   1 
ATOM   4939  N N     . THR B 2 624  ? 118.741 132.334 190.778 1.00 117.48 ? 621  THR A N     1 
ATOM   4940  C CA    . THR B 2 624  ? 118.444 131.598 192.003 1.00 117.48 ? 621  THR A CA    1 
ATOM   4941  C C     . THR B 2 624  ? 117.400 132.307 192.862 1.00 117.48 ? 621  THR A C     1 
ATOM   4942  O O     . THR B 2 624  ? 116.417 131.688 193.284 1.00 117.48 ? 621  THR A O     1 
ATOM   4943  C CB    . THR B 2 624  ? 119.728 131.368 192.804 1.00 117.48 ? 621  THR A CB    1 
ATOM   4944  O OG1   . THR B 2 624  ? 120.740 130.820 191.949 1.00 117.48 ? 621  THR A OG1   1 
ATOM   4945  C CG2   . THR B 2 624  ? 119.473 130.416 193.963 1.00 117.48 ? 621  THR A CG2   1 
ATOM   4946  N N     . HIS B 2 625  ? 117.581 133.599 193.132 1.00 116.50 ? 622  HIS A N     1 
ATOM   4947  C CA    . HIS B 2 625  ? 116.710 134.302 194.065 1.00 116.50 ? 622  HIS A CA    1 
ATOM   4948  C C     . HIS B 2 625  ? 116.053 135.471 193.339 1.00 116.50 ? 622  HIS A C     1 
ATOM   4949  O O     . HIS B 2 625  ? 116.653 136.079 192.450 1.00 116.50 ? 622  HIS A O     1 
ATOM   4950  C CB    . HIS B 2 625  ? 117.494 134.780 195.298 1.00 116.50 ? 622  HIS A CB    1 
ATOM   4951  C CG    . HIS B 2 625  ? 116.634 135.351 196.382 1.00 116.50 ? 622  HIS A CG    1 
ATOM   4952  N ND1   . HIS B 2 625  ? 116.249 136.674 196.424 1.00 116.50 ? 622  HIS A ND1   1 
ATOM   4953  C CD2   . HIS B 2 625  ? 116.089 134.765 197.474 1.00 116.50 ? 622  HIS A CD2   1 
ATOM   4954  C CE1   . HIS B 2 625  ? 115.502 136.875 197.495 1.00 116.50 ? 622  HIS A CE1   1 
ATOM   4955  N NE2   . HIS B 2 625  ? 115.389 135.734 198.149 1.00 116.50 ? 622  HIS A NE2   1 
ATOM   4956  N N     . THR B 2 626  ? 114.814 135.788 193.725 1.00 119.50 ? 623  THR A N     1 
ATOM   4957  C CA    . THR B 2 626  ? 113.939 136.605 192.888 1.00 119.50 ? 623  THR A CA    1 
ATOM   4958  C C     . THR B 2 626  ? 113.880 138.084 193.263 1.00 119.50 ? 623  THR A C     1 
ATOM   4959  O O     . THR B 2 626  ? 113.190 138.843 192.573 1.00 119.50 ? 623  THR A O     1 
ATOM   4960  C CB    . THR B 2 626  ? 112.509 136.047 192.912 1.00 119.50 ? 623  THR A CB    1 
ATOM   4961  O OG1   . THR B 2 626  ? 112.021 136.032 194.258 1.00 119.50 ? 623  THR A OG1   1 
ATOM   4962  C CG2   . THR B 2 626  ? 112.464 134.638 192.342 1.00 119.50 ? 623  THR A CG2   1 
ATOM   4963  N N     . THR B 2 627  ? 114.555 138.521 194.320 1.00 116.93 ? 624  THR A N     1 
ATOM   4964  C CA    . THR B 2 627  ? 114.433 139.917 194.717 1.00 116.93 ? 624  THR A CA    1 
ATOM   4965  C C     . THR B 2 627  ? 115.239 140.827 193.792 1.00 116.93 ? 624  THR A C     1 
ATOM   4966  O O     . THR B 2 627  ? 116.265 140.420 193.241 1.00 116.93 ? 624  THR A O     1 
ATOM   4967  C CB    . THR B 2 627  ? 114.889 140.122 196.159 1.00 116.93 ? 624  THR A CB    1 
ATOM   4968  O OG1   . THR B 2 627  ? 116.141 139.457 196.374 1.00 116.93 ? 624  THR A OG1   1 
ATOM   4969  C CG2   . THR B 2 627  ? 113.831 139.632 197.136 1.00 116.93 ? 624  THR A CG2   1 
ATOM   4970  N N     . PRO B 2 628  ? 114.913 142.147 193.696 1.00 114.08 ? 625  PRO A N     1 
ATOM   4971  C CA    . PRO B 2 628  ? 115.622 143.069 192.791 1.00 114.08 ? 625  PRO A CA    1 
ATOM   4972  C C     . PRO B 2 628  ? 116.986 143.526 193.319 1.00 114.08 ? 625  PRO A C     1 
ATOM   4973  O O     . PRO B 2 628  ? 117.383 143.033 194.352 1.00 114.08 ? 625  PRO A O     1 
ATOM   4974  C CB    . PRO B 2 628  ? 114.703 144.291 192.746 1.00 114.08 ? 625  PRO A CB    1 
ATOM   4975  C CG    . PRO B 2 628  ? 114.110 144.329 194.126 1.00 114.08 ? 625  PRO A CG    1 
ATOM   4976  C CD    . PRO B 2 628  ? 113.862 142.871 194.440 1.00 114.08 ? 625  PRO A CD    1 
ATOM   4977  N N     . ILE B 2 629  ? 117.660 144.449 192.618 1.00 108.99 ? 626  ILE A N     1 
ATOM   4978  C CA    . ILE B 2 629  ? 119.047 144.826 193.047 1.00 108.99 ? 626  ILE A CA    1 
ATOM   4979  C C     . ILE B 2 629  ? 119.460 146.189 192.483 1.00 108.99 ? 626  ILE A C     1 
ATOM   4980  O O     . ILE B 2 629  ? 119.142 146.465 191.317 1.00 108.99 ? 626  ILE A O     1 
ATOM   4981  C CB    . ILE B 2 629  ? 120.078 143.736 192.666 1.00 108.99 ? 626  ILE A CB    1 
ATOM   4982  C CG1   . ILE B 2 629  ? 121.488 144.084 193.146 1.00 108.99 ? 626  ILE A CG1   1 
ATOM   4983  C CG2   . ILE B 2 629  ? 120.051 143.459 191.172 1.00 108.99 ? 626  ILE A CG2   1 
ATOM   4984  C CD1   . ILE B 2 629  ? 122.536 143.088 192.714 1.00 108.99 ? 626  ILE A CD1   1 
ATOM   4985  N N     . LEU B 2 630  ? 120.177 146.984 193.284 1.00 104.04 ? 627  LEU A N     1 
ATOM   4986  C CA    . LEU B 2 630  ? 120.684 148.307 192.834 1.00 104.04 ? 627  LEU A CA    1 
ATOM   4987  C C     . LEU B 2 630  ? 122.148 148.143 192.420 1.00 104.04 ? 627  LEU A C     1 
ATOM   4988  O O     . LEU B 2 630  ? 122.982 147.928 193.318 1.00 104.04 ? 627  LEU A O     1 
ATOM   4989  C CB    . LEU B 2 630  ? 120.579 149.312 193.983 1.00 104.04 ? 627  LEU A CB    1 
ATOM   4990  C CG    . LEU B 2 630  ? 119.216 149.973 194.186 1.00 104.04 ? 627  LEU A CG    1 
ATOM   4991  C CD1   . LEU B 2 630  ? 118.711 150.586 192.891 1.00 104.04 ? 627  LEU A CD1   1 
ATOM   4992  C CD2   . LEU B 2 630  ? 118.203 148.991 194.751 1.00 104.04 ? 627  LEU A CD2   1 
ATOM   4993  N N     . LEU B 2 631  ? 122.452 148.240 191.125 1.00 96.75  ? 628  LEU A N     1 
ATOM   4994  C CA    . LEU B 2 631  ? 123.840 147.999 190.666 1.00 96.75  ? 628  LEU A CA    1 
ATOM   4995  C C     . LEU B 2 631  ? 124.675 149.251 190.933 1.00 96.75  ? 628  LEU A C     1 
ATOM   4996  O O     . LEU B 2 631  ? 124.494 150.236 190.203 1.00 96.75  ? 628  LEU A O     1 
ATOM   4997  C CB    . LEU B 2 631  ? 123.809 147.648 189.178 1.00 96.75  ? 628  LEU A CB    1 
ATOM   4998  C CG    . LEU B 2 631  ? 123.767 146.159 188.842 1.00 96.75  ? 628  LEU A CG    1 
ATOM   4999  C CD1   . LEU B 2 631  ? 122.605 145.473 189.541 1.00 96.75  ? 628  LEU A CD1   1 
ATOM   5000  C CD2   . LEU B 2 631  ? 123.682 145.951 187.339 1.00 96.75  ? 628  LEU A CD2   1 
ATOM   5001  N N     . SER B 2 632  ? 125.544 149.214 191.948 1.00 95.44  ? 629  SER A N     1 
ATOM   5002  C CA    . SER B 2 632  ? 126.313 150.405 192.288 1.00 95.44  ? 629  SER A CA    1 
ATOM   5003  C C     . SER B 2 632  ? 127.802 150.210 192.027 1.00 95.44  ? 629  SER A C     1 
ATOM   5004  O O     . SER B 2 632  ? 128.629 150.926 192.601 1.00 95.44  ? 629  SER A O     1 
ATOM   5005  C CB    . SER B 2 632  ? 126.075 150.800 193.746 1.00 95.44  ? 629  SER A CB    1 
ATOM   5006  O OG    . SER B 2 632  ? 126.439 149.749 194.624 1.00 95.44  ? 629  SER A OG    1 
ATOM   5007  N N     . ASN B 2 633  ? 128.160 149.255 191.174 1.00 89.51  ? 630  ASN A N     1 
ATOM   5008  C CA    . ASN B 2 633  ? 129.546 148.987 190.818 1.00 89.51  ? 630  ASN A CA    1 
ATOM   5009  C C     . ASN B 2 633  ? 129.800 149.539 189.423 1.00 89.51  ? 630  ASN A C     1 
ATOM   5010  O O     . ASN B 2 633  ? 129.199 149.071 188.450 1.00 89.51  ? 630  ASN A O     1 
ATOM   5011  C CB    . ASN B 2 633  ? 129.846 147.489 190.872 1.00 89.51  ? 630  ASN A CB    1 
ATOM   5012  C CG    . ASN B 2 633  ? 131.324 147.184 190.730 1.00 89.51  ? 630  ASN A CG    1 
ATOM   5013  O OD1   . ASN B 2 633  ? 132.167 148.076 190.834 1.00 89.51  ? 630  ASN A OD1   1 
ATOM   5014  N ND2   . ASN B 2 633  ? 131.647 145.918 190.492 1.00 89.51  ? 630  ASN A ND2   1 
ATOM   5015  N N     . ASN B 2 634  ? 130.696 150.524 189.333 1.00 83.14  ? 631  ASN A N     1 
ATOM   5016  C CA    . ASN B 2 634  ? 130.977 151.236 188.085 1.00 83.14  ? 631  ASN A CA    1 
ATOM   5017  C C     . ASN B 2 634  ? 129.685 151.883 187.571 1.00 83.14  ? 631  ASN A C     1 
ATOM   5018  O O     . ASN B 2 634  ? 129.179 151.575 186.490 1.00 83.14  ? 631  ASN A O     1 
ATOM   5019  C CB    . ASN B 2 634  ? 131.642 150.295 187.062 1.00 83.14  ? 631  ASN A CB    1 
ATOM   5020  C CG    . ASN B 2 634  ? 131.575 150.795 185.624 1.00 83.14  ? 631  ASN A CG    1 
ATOM   5021  O OD1   . ASN B 2 634  ? 131.574 151.999 185.366 1.00 83.14  ? 631  ASN A OD1   1 
ATOM   5022  N ND2   . ASN B 2 634  ? 131.521 149.862 184.680 1.00 83.14  ? 631  ASN A ND2   1 
ATOM   5023  N N     . PHE B 2 635  ? 129.094 152.733 188.410 1.00 87.81  ? 632  PHE A N     1 
ATOM   5024  C CA    . PHE B 2 635  ? 127.918 153.520 188.068 1.00 87.81  ? 632  PHE A CA    1 
ATOM   5025  C C     . PHE B 2 635  ? 127.955 154.824 188.850 1.00 87.81  ? 632  PHE A C     1 
ATOM   5026  O O     . PHE B 2 635  ? 128.362 154.842 190.016 1.00 87.81  ? 632  PHE A O     1 
ATOM   5027  C CB    . PHE B 2 635  ? 126.611 152.770 188.379 1.00 87.81  ? 632  PHE A CB    1 
ATOM   5028  C CG    . PHE B 2 635  ? 126.269 151.695 187.384 1.00 87.81  ? 632  PHE A CG    1 
ATOM   5029  C CD1   . PHE B 2 635  ? 125.628 152.006 186.198 1.00 87.81  ? 632  PHE A CD1   1 
ATOM   5030  C CD2   . PHE B 2 635  ? 126.559 150.369 187.652 1.00 87.81  ? 632  PHE A CD2   1 
ATOM   5031  C CE1   . PHE B 2 635  ? 125.308 151.018 185.288 1.00 87.81  ? 632  PHE A CE1   1 
ATOM   5032  C CE2   . PHE B 2 635  ? 126.239 149.377 186.746 1.00 87.81  ? 632  PHE A CE2   1 
ATOM   5033  C CZ    . PHE B 2 635  ? 125.613 149.702 185.564 1.00 87.81  ? 632  PHE A CZ    1 
ATOM   5034  N N     . ILE B 2 636  ? 127.530 155.915 188.209 1.00 84.48  ? 633  ILE A N     1 
ATOM   5035  C CA    . ILE B 2 636  ? 127.482 157.199 188.902 1.00 84.48  ? 633  ILE A CA    1 
ATOM   5036  C C     . ILE B 2 636  ? 126.453 157.165 190.029 1.00 84.48  ? 633  ILE A C     1 
ATOM   5037  O O     . ILE B 2 636  ? 126.709 157.657 191.134 1.00 84.48  ? 633  ILE A O     1 
ATOM   5038  C CB    . ILE B 2 636  ? 127.222 158.343 187.902 1.00 84.48  ? 633  ILE A CB    1 
ATOM   5039  C CG1   . ILE B 2 636  ? 127.071 159.680 188.634 1.00 84.48  ? 633  ILE A CG1   1 
ATOM   5040  C CG2   . ILE B 2 636  ? 126.034 158.037 187.007 1.00 84.48  ? 633  ILE A CG2   1 
ATOM   5041  C CD1   . ILE B 2 636  ? 127.152 160.887 187.723 1.00 84.48  ? 633  ILE A CD1   1 
ATOM   5042  N N     . GLU B 2 637  ? 125.283 156.584 189.776 1.00 87.41  ? 634  GLU A N     1 
ATOM   5043  C CA    . GLU B 2 637  ? 124.312 156.296 190.819 1.00 87.41  ? 634  GLU A CA    1 
ATOM   5044  C C     . GLU B 2 637  ? 123.837 154.857 190.687 1.00 87.41  ? 634  GLU A C     1 
ATOM   5045  O O     . GLU B 2 637  ? 123.878 154.285 189.594 1.00 87.41  ? 634  GLU A O     1 
ATOM   5046  C CB    . GLU B 2 637  ? 123.105 157.248 190.768 1.00 87.41  ? 634  GLU A CB    1 
ATOM   5047  C CG    . GLU B 2 637  ? 122.239 157.136 189.525 1.00 87.41  ? 634  GLU A CG    1 
ATOM   5048  C CD    . GLU B 2 637  ? 122.550 158.213 188.507 1.00 87.41  ? 634  GLU A CD    1 
ATOM   5049  O OE1   . GLU B 2 637  ? 123.568 158.914 188.679 1.00 87.41  ? 634  GLU A OE1   1 
ATOM   5050  O OE2   . GLU B 2 637  ? 121.775 158.366 187.540 1.00 87.41  ? 634  GLU A OE2   1 
ATOM   5051  N N     . PRO B 2 638  ? 123.436 154.140 191.750 1.00 91.89  ? 635  PRO A N     1 
ATOM   5052  C CA    . PRO B 2 638  ? 123.007 152.768 191.543 1.00 91.89  ? 635  PRO A CA    1 
ATOM   5053  C C     . PRO B 2 638  ? 121.869 152.660 190.515 1.00 91.89  ? 635  PRO A C     1 
ATOM   5054  O O     . PRO B 2 638  ? 120.942 153.431 190.603 1.00 91.89  ? 635  PRO A O     1 
ATOM   5055  C CB    . PRO B 2 638  ? 122.509 152.322 192.926 1.00 91.89  ? 635  PRO A CB    1 
ATOM   5056  C CG    . PRO B 2 638  ? 122.314 153.607 193.704 1.00 91.89  ? 635  PRO A CG    1 
ATOM   5057  C CD    . PRO B 2 638  ? 123.360 154.553 193.156 1.00 91.89  ? 635  PRO A CD    1 
ATOM   5058  N N     . LEU B 2 639  ? 121.976 151.733 189.560 1.00 96.93  ? 636  LEU A N     1 
ATOM   5059  C CA    . LEU B 2 639  ? 120.892 151.465 188.582 1.00 96.93  ? 636  LEU A CA    1 
ATOM   5060  C C     . LEU B 2 639  ? 120.150 150.263 189.135 1.00 96.93  ? 636  LEU A C     1 
ATOM   5061  O O     . LEU B 2 639  ? 120.744 149.553 189.955 1.00 96.93  ? 636  LEU A O     1 
ATOM   5062  C CB    . LEU B 2 639  ? 121.534 151.126 187.235 1.00 96.93  ? 636  LEU A CB    1 
ATOM   5063  C CG    . LEU B 2 639  ? 120.699 150.291 186.266 1.00 96.93  ? 636  LEU A CG    1 
ATOM   5064  C CD1   . LEU B 2 639  ? 119.711 151.161 185.506 1.00 96.93  ? 636  LEU A CD1   1 
ATOM   5065  C CD2   . LEU B 2 639  ? 121.595 149.540 185.295 1.00 96.93  ? 636  LEU A CD2   1 
ATOM   5066  N N     . GLU B 2 640  ? 118.918 150.027 188.696 1.00 107.73 ? 637  GLU A N     1 
ATOM   5067  C CA    . GLU B 2 640  ? 118.115 148.932 189.299 1.00 107.73 ? 637  GLU A CA    1 
ATOM   5068  C C     . GLU B 2 640  ? 117.745 147.898 188.241 1.00 107.73 ? 637  GLU A C     1 
ATOM   5069  O O     . GLU B 2 640  ? 117.580 148.282 187.076 1.00 107.73 ? 637  GLU A O     1 
ATOM   5070  C CB    . GLU B 2 640  ? 116.855 149.513 189.948 1.00 107.73 ? 637  GLU A CB    1 
ATOM   5071  C CG    . GLU B 2 640  ? 115.811 148.474 190.324 1.00 107.73 ? 637  GLU A CG    1 
ATOM   5072  C CD    . GLU B 2 640  ? 116.173 147.563 191.485 1.00 107.73 ? 637  GLU A CD    1 
ATOM   5073  O OE1   . GLU B 2 640  ? 116.146 148.034 192.635 1.00 107.73 ? 637  GLU A OE1   1 
ATOM   5074  O OE2   . GLU B 2 640  ? 116.461 146.381 191.237 1.00 107.73 ? 637  GLU A OE2   1 
ATOM   5075  N N     . ILE B 2 641  ? 117.647 146.635 188.639 1.00 111.01 ? 638  ILE A N     1 
ATOM   5076  C CA    . ILE B 2 641  ? 117.184 145.581 187.697 1.00 111.01 ? 638  ILE A CA    1 
ATOM   5077  C C     . ILE B 2 641  ? 116.130 144.747 188.429 1.00 111.01 ? 638  ILE A C     1 
ATOM   5078  O O     . ILE B 2 641  ? 116.447 144.221 189.510 1.00 111.01 ? 638  ILE A O     1 
ATOM   5079  C CB    . ILE B 2 641  ? 118.362 144.726 187.208 1.00 111.01 ? 638  ILE A CB    1 
ATOM   5080  C CG1   . ILE B 2 641  ? 119.294 145.525 186.295 1.00 111.01 ? 638  ILE A CG1   1 
ATOM   5081  C CG2   . ILE B 2 641  ? 117.872 143.457 186.529 1.00 111.01 ? 638  ILE A CG2   1 
ATOM   5082  C CD1   . ILE B 2 641  ? 120.185 144.662 185.441 1.00 111.01 ? 638  ILE A CD1   1 
ATOM   5083  N N     . THR B 2 642  ? 114.920 144.656 187.872 1.00 114.98 ? 639  THR A N     1 
ATOM   5084  C CA    . THR B 2 642  ? 113.835 143.869 188.503 1.00 114.98 ? 639  THR A CA    1 
ATOM   5085  C C     . THR B 2 642  ? 113.845 142.464 187.917 1.00 114.98 ? 639  THR A C     1 
ATOM   5086  O O     . THR B 2 642  ? 114.500 142.268 186.885 1.00 114.98 ? 639  THR A O     1 
ATOM   5087  C CB    . THR B 2 642  ? 112.487 144.552 188.286 1.00 114.98 ? 639  THR A CB    1 
ATOM   5088  O OG1   . THR B 2 642  ? 112.292 144.632 186.875 1.00 114.98 ? 639  THR A OG1   1 
ATOM   5089  C CG2   . THR B 2 642  ? 112.426 145.936 188.890 1.00 114.98 ? 639  THR A CG2   1 
ATOM   5090  N N     . LYS B 2 643  ? 113.148 141.525 188.542 1.00 115.77 ? 640  LYS A N     1 
ATOM   5091  C CA    . LYS B 2 643  ? 113.152 140.132 188.110 1.00 115.77 ? 640  LYS A CA    1 
ATOM   5092  C C     . LYS B 2 643  ? 112.612 139.988 186.691 1.00 115.77 ? 640  LYS A C     1 
ATOM   5093  O O     . LYS B 2 643  ? 113.148 139.209 185.894 1.00 115.77 ? 640  LYS A O     1 
ATOM   5094  C CB    . LYS B 2 643  ? 112.341 139.276 189.083 1.00 115.77 ? 640  LYS A CB    1 
ATOM   5095  C CG    . LYS B 2 643  ? 112.194 137.823 188.657 1.00 115.77 ? 640  LYS A CG    1 
ATOM   5096  C CD    . LYS B 2 643  ? 113.552 137.149 188.514 1.00 115.77 ? 640  LYS A CD    1 
ATOM   5097  C CE    . LYS B 2 643  ? 113.410 135.703 188.067 1.00 115.77 ? 640  LYS A CE    1 
ATOM   5098  N NZ    . LYS B 2 643  ? 114.730 135.078 187.775 1.00 115.77 ? 640  LYS A NZ    1 
ATOM   5099  N N     . GLU B 2 644  ? 111.553 140.729 186.359 1.00 114.12 ? 641  GLU A N     1 
ATOM   5100  C CA    . GLU B 2 644  ? 110.916 140.561 185.056 1.00 114.12 ? 641  GLU A CA    1 
ATOM   5101  C C     . GLU B 2 644  ? 111.834 140.994 183.917 1.00 114.12 ? 641  GLU A C     1 
ATOM   5102  O O     . GLU B 2 644  ? 111.906 140.318 182.884 1.00 114.12 ? 641  GLU A O     1 
ATOM   5103  C CB    . GLU B 2 644  ? 109.588 141.323 185.012 1.00 114.12 ? 641  GLU A CB    1 
ATOM   5104  C CG    . GLU B 2 644  ? 109.689 142.824 185.239 1.00 114.12 ? 641  GLU A CG    1 
ATOM   5105  C CD    . GLU B 2 644  ? 109.670 143.196 186.709 1.00 114.12 ? 641  GLU A CD    1 
ATOM   5106  O OE1   . GLU B 2 644  ? 109.906 142.308 187.555 1.00 114.12 ? 641  GLU A OE1   1 
ATOM   5107  O OE2   . GLU B 2 644  ? 109.419 144.379 187.020 1.00 114.12 ? 641  GLU A OE2   1 
ATOM   5108  N N     . ILE B 2 645  ? 112.549 142.111 184.082 1.00 111.64 ? 642  ILE A N     1 
ATOM   5109  C CA    . ILE B 2 645  ? 113.389 142.598 182.990 1.00 111.64 ? 642  ILE A CA    1 
ATOM   5110  C C     . ILE B 2 645  ? 114.517 141.618 182.702 1.00 111.64 ? 642  ILE A C     1 
ATOM   5111  O O     . ILE B 2 645  ? 114.979 141.513 181.559 1.00 111.64 ? 642  ILE A O     1 
ATOM   5112  C CB    . ILE B 2 645  ? 113.923 144.011 183.292 1.00 111.64 ? 642  ILE A CB    1 
ATOM   5113  C CG1   . ILE B 2 645  ? 114.807 144.012 184.539 1.00 111.64 ? 642  ILE A CG1   1 
ATOM   5114  C CG2   . ILE B 2 645  ? 112.771 144.993 183.448 1.00 111.64 ? 642  ILE A CG2   1 
ATOM   5115  C CD1   . ILE B 2 645  ? 115.543 145.316 184.751 1.00 111.64 ? 642  ILE A CD1   1 
ATOM   5116  N N     . TYR B 2 646  ? 114.983 140.889 183.718 1.00 112.17 ? 643  TYR A N     1 
ATOM   5117  C CA    . TYR B 2 646  ? 115.912 139.794 183.464 1.00 112.17 ? 643  TYR A CA    1 
ATOM   5118  C C     . TYR B 2 646  ? 115.227 138.664 182.708 1.00 112.17 ? 643  TYR A C     1 
ATOM   5119  O O     . TYR B 2 646  ? 115.829 138.047 181.820 1.00 112.17 ? 643  TYR A O     1 
ATOM   5120  C CB    . TYR B 2 646  ? 116.501 139.283 184.777 1.00 112.17 ? 643  TYR A CB    1 
ATOM   5121  C CG    . TYR B 2 646  ? 117.247 137.977 184.633 1.00 112.17 ? 643  TYR A CG    1 
ATOM   5122  C CD1   . TYR B 2 646  ? 118.417 137.903 183.891 1.00 112.17 ? 643  TYR A CD1   1 
ATOM   5123  C CD2   . TYR B 2 646  ? 116.778 136.818 185.235 1.00 112.17 ? 643  TYR A CD2   1 
ATOM   5124  C CE1   . TYR B 2 646  ? 119.101 136.712 183.754 1.00 112.17 ? 643  TYR A CE1   1 
ATOM   5125  C CE2   . TYR B 2 646  ? 117.455 135.622 185.104 1.00 112.17 ? 643  TYR A CE2   1 
ATOM   5126  C CZ    . TYR B 2 646  ? 118.616 135.574 184.362 1.00 112.17 ? 643  TYR A CZ    1 
ATOM   5127  O OH    . TYR B 2 646  ? 119.295 134.385 184.229 1.00 112.17 ? 643  TYR A OH    1 
ATOM   5128  N N     . ASP B 2 647  ? 113.968 138.375 183.048 1.00 112.70 ? 644  ASP A N     1 
ATOM   5129  C CA    . ASP B 2 647  ? 113.218 137.364 182.311 1.00 112.70 ? 644  ASP A CA    1 
ATOM   5130  C C     . ASP B 2 647  ? 112.942 137.819 180.884 1.00 112.70 ? 644  ASP A C     1 
ATOM   5131  O O     . ASP B 2 647  ? 112.847 136.992 179.971 1.00 112.70 ? 644  ASP A O     1 
ATOM   5132  C CB    . ASP B 2 647  ? 111.914 137.040 183.038 1.00 112.70 ? 644  ASP A CB    1 
ATOM   5133  C CG    . ASP B 2 647  ? 112.142 136.306 184.344 1.00 112.70 ? 644  ASP A CG    1 
ATOM   5134  O OD1   . ASP B 2 647  ? 113.150 135.575 184.448 1.00 112.70 ? 644  ASP A OD1   1 
ATOM   5135  O OD2   . ASP B 2 647  ? 111.314 136.457 185.266 1.00 112.70 ? 644  ASP A OD2   1 
ATOM   5136  N N     . LEU B 2 648  ? 112.798 139.130 180.675 1.00 111.81 ? 645  LEU A N     1 
ATOM   5137  C CA    . LEU B 2 648  ? 112.690 139.648 179.315 1.00 111.81 ? 645  LEU A CA    1 
ATOM   5138  C C     . LEU B 2 648  ? 113.963 139.373 178.526 1.00 111.81 ? 645  LEU A C     1 
ATOM   5139  O O     . LEU B 2 648  ? 113.907 139.060 177.331 1.00 111.81 ? 645  LEU A O     1 
ATOM   5140  C CB    . LEU B 2 648  ? 112.385 141.146 179.341 1.00 111.81 ? 645  LEU A CB    1 
ATOM   5141  C CG    . LEU B 2 648  ? 110.921 141.568 179.188 1.00 111.81 ? 645  LEU A CG    1 
ATOM   5142  C CD1   . LEU B 2 648  ? 110.104 141.204 180.418 1.00 111.81 ? 645  LEU A CD1   1 
ATOM   5143  C CD2   . LEU B 2 648  ? 110.823 143.060 178.901 1.00 111.81 ? 645  LEU A CD2   1 
ATOM   5144  N N     . ASN B 2 649  ? 115.121 139.491 179.178 1.00 109.84 ? 646  ASN A N     1 
ATOM   5145  C CA    . ASN B 2 649  ? 116.379 139.159 178.518 1.00 109.84 ? 646  ASN A CA    1 
ATOM   5146  C C     . ASN B 2 649  ? 116.448 137.676 178.173 1.00 109.84 ? 646  ASN A C     1 
ATOM   5147  O O     . ASN B 2 649  ? 116.875 137.308 177.072 1.00 109.84 ? 646  ASN A O     1 
ATOM   5148  C CB    . ASN B 2 649  ? 117.558 139.552 179.406 1.00 109.84 ? 646  ASN A CB    1 
ATOM   5149  C CG    . ASN B 2 649  ? 117.929 141.014 179.271 1.00 109.84 ? 646  ASN A CG    1 
ATOM   5150  O OD1   . ASN B 2 649  ? 118.843 141.369 178.528 1.00 109.84 ? 646  ASN A OD1   1 
ATOM   5151  N ND2   . ASN B 2 649  ? 117.226 141.871 180.003 1.00 109.84 ? 646  ASN A ND2   1 
ATOM   5152  N N     . ASN B 2 650  ? 116.035 136.810 179.099 1.00 109.82 ? 647  ASN A N     1 
ATOM   5153  C CA    . ASN B 2 650  ? 116.119 135.359 178.935 1.00 109.82 ? 647  ASN A CA    1 
ATOM   5154  C C     . ASN B 2 650  ? 114.764 134.737 179.243 1.00 109.82 ? 647  ASN A C     1 
ATOM   5155  O O     . ASN B 2 650  ? 114.518 134.277 180.366 1.00 109.82 ? 647  ASN A O     1 
ATOM   5156  C CB    . ASN B 2 650  ? 117.208 134.763 179.829 1.00 109.82 ? 647  ASN A CB    1 
ATOM   5157  C CG    . ASN B 2 650  ? 118.508 135.541 179.766 1.00 109.82 ? 647  ASN A CG    1 
ATOM   5158  O OD1   . ASN B 2 650  ? 118.955 135.935 178.690 1.00 109.82 ? 647  ASN A OD1   1 
ATOM   5159  N ND2   . ASN B 2 650  ? 119.110 135.784 180.924 1.00 109.82 ? 647  ASN A ND2   1 
ATOM   5160  N N     . PRO B 2 651  ? 113.860 134.707 178.270 1.00 116.21 ? 648  PRO A N     1 
ATOM   5161  C CA    . PRO B 2 651  ? 112.561 134.063 178.480 1.00 116.21 ? 648  PRO A CA    1 
ATOM   5162  C C     . PRO B 2 651  ? 112.680 132.545 178.415 1.00 116.21 ? 648  PRO A C     1 
ATOM   5163  O O     . PRO B 2 651  ? 113.721 131.984 178.072 1.00 116.21 ? 648  PRO A O     1 
ATOM   5164  C CB    . PRO B 2 651  ? 111.712 134.603 177.327 1.00 116.21 ? 648  PRO A CB    1 
ATOM   5165  C CG    . PRO B 2 651  ? 112.699 134.866 176.241 1.00 116.21 ? 648  PRO A CG    1 
ATOM   5166  C CD    . PRO B 2 651  ? 113.985 135.278 176.917 1.00 116.21 ? 648  PRO A CD    1 
ATOM   5167  N N     . GLU B 2 652  ? 111.579 131.884 178.759 1.00 123.39 ? 649  GLU A N     1 
ATOM   5168  C CA    . GLU B 2 652  ? 111.521 130.426 178.727 1.00 123.39 ? 649  GLU A CA    1 
ATOM   5169  C C     . GLU B 2 652  ? 111.557 129.907 177.293 1.00 123.39 ? 649  GLU A C     1 
ATOM   5170  O O     . GLU B 2 652  ? 111.587 128.699 177.061 1.00 123.39 ? 649  GLU A O     1 
ATOM   5171  C CB    . GLU B 2 652  ? 110.263 129.921 179.437 1.00 123.39 ? 649  GLU A CB    1 
ATOM   5172  C CG    . GLU B 2 652  ? 110.094 130.440 180.857 1.00 123.39 ? 649  GLU A CG    1 
ATOM   5173  C CD    . GLU B 2 652  ? 111.006 129.743 181.849 1.00 123.39 ? 649  GLU A CD    1 
ATOM   5174  O OE1   . GLU B 2 652  ? 111.605 128.708 181.487 1.00 123.39 ? 649  GLU A OE1   1 
ATOM   5175  O OE2   . GLU B 2 652  ? 111.123 130.230 182.993 1.00 123.39 ? 649  GLU A OE2   1 
ATOM   5176  N N     . PRO B 2 655  ? 112.709 132.474 171.600 1.00 124.60 ? 652  PRO A N     1 
ATOM   5177  C CA    . PRO B 2 655  ? 112.973 133.831 171.112 1.00 124.60 ? 652  PRO A CA    1 
ATOM   5178  C C     . PRO B 2 655  ? 112.561 134.906 172.116 1.00 124.60 ? 652  PRO A C     1 
ATOM   5179  O O     . PRO B 2 655  ? 111.579 134.735 172.839 1.00 124.60 ? 652  PRO A O     1 
ATOM   5180  C CB    . PRO B 2 655  ? 112.129 133.912 169.840 1.00 124.60 ? 652  PRO A CB    1 
ATOM   5181  C CG    . PRO B 2 655  ? 110.997 132.977 170.086 1.00 124.60 ? 652  PRO A CG    1 
ATOM   5182  C CD    . PRO B 2 655  ? 111.530 131.870 170.956 1.00 124.60 ? 652  PRO A CD    1 
ATOM   5183  N N     . LYS B 2 656  ? 113.314 136.003 172.150 1.00 115.74 ? 653  LYS A N     1 
ATOM   5184  C CA    . LYS B 2 656  ? 113.092 137.054 173.130 1.00 115.74 ? 653  LYS A CA    1 
ATOM   5185  C C     . LYS B 2 656  ? 111.780 137.788 172.860 1.00 115.74 ? 653  LYS A C     1 
ATOM   5186  O O     . LYS B 2 656  ? 111.393 138.030 171.713 1.00 115.74 ? 653  LYS A O     1 
ATOM   5187  C CB    . LYS B 2 656  ? 114.260 138.040 173.122 1.00 115.74 ? 653  LYS A CB    1 
ATOM   5188  C CG    . LYS B 2 656  ? 115.506 137.518 173.821 1.00 115.74 ? 653  LYS A CG    1 
ATOM   5189  C CD    . LYS B 2 656  ? 116.762 138.188 173.290 1.00 115.74 ? 653  LYS A CD    1 
ATOM   5190  C CE    . LYS B 2 656  ? 117.303 137.459 172.071 1.00 115.74 ? 653  LYS A CE    1 
ATOM   5191  N NZ    . LYS B 2 656  ? 118.067 136.237 172.446 1.00 115.74 ? 653  LYS A NZ    1 
ATOM   5192  N N     . LYS B 2 657  ? 111.093 138.144 173.946 1.00 115.18 ? 654  LYS A N     1 
ATOM   5193  C CA    . LYS B 2 657  ? 109.810 138.833 173.861 1.00 115.18 ? 654  LYS A CA    1 
ATOM   5194  C C     . LYS B 2 657  ? 109.928 140.216 173.233 1.00 115.18 ? 654  LYS A C     1 
ATOM   5195  O O     . LYS B 2 657  ? 109.116 140.575 172.373 1.00 115.18 ? 654  LYS A O     1 
ATOM   5196  C CB    . LYS B 2 657  ? 109.182 138.948 175.253 1.00 115.18 ? 654  LYS A CB    1 
ATOM   5197  C CG    . LYS B 2 657  ? 108.892 137.610 175.914 1.00 115.18 ? 654  LYS A CG    1 
ATOM   5198  C CD    . LYS B 2 657  ? 108.163 137.794 177.235 1.00 115.18 ? 654  LYS A CD    1 
ATOM   5199  C CE    . LYS B 2 657  ? 109.098 138.315 178.313 1.00 115.18 ? 654  LYS A CE    1 
ATOM   5200  N NZ    . LYS B 2 657  ? 110.243 137.393 178.545 1.00 115.18 ? 654  LYS A NZ    1 
ATOM   5201  N N     . PHE B 2 658  ? 110.923 141.005 173.647 1.00 108.79 ? 655  PHE A N     1 
ATOM   5202  C CA    . PHE B 2 658  ? 111.129 142.314 173.037 1.00 108.79 ? 655  PHE A CA    1 
ATOM   5203  C C     . PHE B 2 658  ? 111.630 142.205 171.604 1.00 108.79 ? 655  PHE A C     1 
ATOM   5204  O O     . PHE B 2 658  ? 111.496 143.163 170.836 1.00 108.79 ? 655  PHE A O     1 
ATOM   5205  C CB    . PHE B 2 658  ? 112.095 143.142 173.888 1.00 108.79 ? 655  PHE A CB    1 
ATOM   5206  C CG    . PHE B 2 658  ? 113.471 142.552 174.001 1.00 108.79 ? 655  PHE A CG    1 
ATOM   5207  C CD1   . PHE B 2 658  ? 113.770 141.654 175.013 1.00 108.79 ? 655  PHE A CD1   1 
ATOM   5208  C CD2   . PHE B 2 658  ? 114.468 142.903 173.110 1.00 108.79 ? 655  PHE A CD2   1 
ATOM   5209  C CE1   . PHE B 2 658  ? 115.035 141.111 175.126 1.00 108.79 ? 655  PHE A CE1   1 
ATOM   5210  C CE2   . PHE B 2 658  ? 115.736 142.363 173.217 1.00 108.79 ? 655  PHE A CE2   1 
ATOM   5211  C CZ    . PHE B 2 658  ? 116.019 141.467 174.227 1.00 108.79 ? 655  PHE A CZ    1 
ATOM   5212  N N     . GLN B 2 659  ? 112.199 141.064 171.230 1.00 112.15 ? 656  GLN A N     1 
ATOM   5213  C CA    . GLN B 2 659  ? 112.574 140.790 169.852 1.00 112.15 ? 656  GLN A CA    1 
ATOM   5214  C C     . GLN B 2 659  ? 111.315 140.510 169.036 1.00 112.15 ? 656  GLN A C     1 
ATOM   5215  O O     . GLN B 2 659  ? 110.215 140.394 169.582 1.00 112.15 ? 656  GLN A O     1 
ATOM   5216  C CB    . GLN B 2 659  ? 113.539 139.602 169.789 1.00 112.15 ? 656  GLN A CB    1 
ATOM   5217  C CG    . GLN B 2 659  ? 114.316 139.460 168.486 1.00 112.15 ? 656  GLN A CG    1 
ATOM   5218  C CD    . GLN B 2 659  ? 115.222 138.245 168.477 1.00 112.15 ? 656  GLN A CD    1 
ATOM   5219  O OE1   . GLN B 2 659  ? 115.214 137.443 169.411 1.00 112.15 ? 656  GLN A OE1   1 
ATOM   5220  N NE2   . GLN B 2 659  ? 116.012 138.103 167.419 1.00 112.15 ? 656  GLN A NE2   1 
ATOM   5221  N N     . THR B 2 660  ? 111.482 140.397 167.719 1.00 117.09 ? 657  THR A N     1 
ATOM   5222  C CA    . THR B 2 660  ? 110.345 140.153 166.840 1.00 117.09 ? 657  THR A CA    1 
ATOM   5223  C C     . THR B 2 660  ? 109.923 138.690 166.897 1.00 117.09 ? 657  THR A C     1 
ATOM   5224  O O     . THR B 2 660  ? 109.861 138.011 165.867 1.00 117.09 ? 657  THR A O     1 
ATOM   5225  C CB    . THR B 2 660  ? 110.677 140.549 165.400 1.00 117.09 ? 657  THR A CB    1 
ATOM   5226  O OG1   . THR B 2 660  ? 111.753 139.736 164.914 1.00 117.09 ? 657  THR A OG1   1 
ATOM   5227  C CG2   . THR B 2 660  ? 111.084 142.013 165.329 1.00 117.09 ? 657  THR A CG2   1 
ATOM   5228  N N     . ALA B 2 661  ? 109.633 138.199 168.104 1.00 118.17 ? 658  ALA A N     1 
ATOM   5229  C CA    . ALA B 2 661  ? 109.145 136.833 168.254 1.00 118.17 ? 658  ALA A CA    1 
ATOM   5230  C C     . ALA B 2 661  ? 107.646 136.762 168.005 1.00 118.17 ? 658  ALA A C     1 
ATOM   5231  O O     . ALA B 2 661  ? 107.167 135.901 167.259 1.00 118.17 ? 658  ALA A O     1 
ATOM   5232  C CB    . ALA B 2 661  ? 109.484 136.307 169.648 1.00 118.17 ? 658  ALA A CB    1 
ATOM   5233  N N     . TYR B 2 662  ? 106.887 137.666 168.628 1.00 114.82 ? 659  TYR A N     1 
ATOM   5234  C CA    . TYR B 2 662  ? 105.439 137.675 168.451 1.00 114.82 ? 659  TYR A CA    1 
ATOM   5235  C C     . TYR B 2 662  ? 105.068 138.027 167.016 1.00 114.82 ? 659  TYR A C     1 
ATOM   5236  O O     . TYR B 2 662  ? 104.127 137.462 166.449 1.00 114.82 ? 659  TYR A O     1 
ATOM   5237  C CB    . TYR B 2 662  ? 104.802 138.655 169.436 1.00 114.82 ? 659  TYR A CB    1 
ATOM   5238  C CG    . TYR B 2 662  ? 104.933 138.234 170.884 1.00 114.82 ? 659  TYR A CG    1 
ATOM   5239  C CD1   . TYR B 2 662  ? 104.075 137.293 171.435 1.00 114.82 ? 659  TYR A CD1   1 
ATOM   5240  C CD2   . TYR B 2 662  ? 105.921 138.774 171.697 1.00 114.82 ? 659  TYR A CD2   1 
ATOM   5241  C CE1   . TYR B 2 662  ? 104.193 136.905 172.757 1.00 114.82 ? 659  TYR A CE1   1 
ATOM   5242  C CE2   . TYR B 2 662  ? 106.047 138.392 173.019 1.00 114.82 ? 659  TYR A CE2   1 
ATOM   5243  C CZ    . TYR B 2 662  ? 105.180 137.457 173.543 1.00 114.82 ? 659  TYR A CZ    1 
ATOM   5244  O OH    . TYR B 2 662  ? 105.302 137.074 174.859 1.00 114.82 ? 659  TYR A OH    1 
ATOM   5245  N N     . ALA B 2 663  ? 105.804 138.963 166.412 1.00 117.39 ? 660  ALA A N     1 
ATOM   5246  C CA    . ALA B 2 663  ? 105.534 139.343 165.029 1.00 117.39 ? 660  ALA A CA    1 
ATOM   5247  C C     . ALA B 2 663  ? 105.757 138.174 164.078 1.00 117.39 ? 660  ALA A C     1 
ATOM   5248  O O     . ALA B 2 663  ? 104.985 137.975 163.132 1.00 117.39 ? 660  ALA A O     1 
ATOM   5249  C CB    . ALA B 2 663  ? 106.407 140.533 164.631 1.00 117.39 ? 660  ALA A CB    1 
ATOM   5250  N N     . LYS B 2 664  ? 106.813 137.392 164.309 1.00 119.18 ? 661  LYS A N     1 
ATOM   5251  C CA    . LYS B 2 664  ? 107.086 136.236 163.461 1.00 119.18 ? 661  LYS A CA    1 
ATOM   5252  C C     . LYS B 2 664  ? 106.023 135.155 163.633 1.00 119.18 ? 661  LYS A C     1 
ATOM   5253  O O     . LYS B 2 664  ? 105.545 134.583 162.647 1.00 119.18 ? 661  LYS A O     1 
ATOM   5254  C CB    . LYS B 2 664  ? 108.475 135.676 163.770 1.00 119.18 ? 661  LYS A CB    1 
ATOM   5255  C CG    . LYS B 2 664  ? 108.896 134.529 162.867 1.00 119.18 ? 661  LYS A CG    1 
ATOM   5256  C CD    . LYS B 2 664  ? 110.314 134.076 163.173 1.00 119.18 ? 661  LYS A CD    1 
ATOM   5257  C CE    . LYS B 2 664  ? 110.702 132.871 162.332 1.00 119.18 ? 661  LYS A CE    1 
ATOM   5258  N NZ    . LYS B 2 664  ? 110.612 133.160 160.874 1.00 119.18 ? 661  LYS A NZ    1 
ATOM   5259  N N     . LYS B 2 665  ? 105.643 134.865 164.875 1.00 117.10 ? 662  LYS A N     1 
ATOM   5260  C CA    . LYS B 2 665  ? 104.638 133.849 165.151 1.00 117.10 ? 662  LYS A CA    1 
ATOM   5261  C C     . LYS B 2 665  ? 104.008 134.134 166.506 1.00 117.10 ? 662  LYS A C     1 
ATOM   5262  O O     . LYS B 2 665  ? 104.637 134.736 167.380 1.00 117.10 ? 662  LYS A O     1 
ATOM   5263  C CB    . LYS B 2 665  ? 105.242 132.440 165.121 1.00 117.10 ? 662  LYS A CB    1 
ATOM   5264  C CG    . LYS B 2 665  ? 106.347 132.215 166.141 1.00 117.10 ? 662  LYS A CG    1 
ATOM   5265  C CD    . LYS B 2 665  ? 106.955 130.829 166.002 1.00 117.10 ? 662  LYS A CD    1 
ATOM   5266  C CE    . LYS B 2 665  ? 108.081 130.618 167.001 1.00 117.10 ? 662  LYS A CE    1 
ATOM   5267  N NZ    . LYS B 2 665  ? 109.251 131.491 166.708 1.00 117.10 ? 662  LYS A NZ    1 
ATOM   5268  N N     . THR B 2 666  ? 102.761 133.685 166.668 1.00 115.85 ? 663  THR A N     1 
ATOM   5269  C CA    . THR B 2 666  ? 101.986 133.907 167.892 1.00 115.85 ? 663  THR A CA    1 
ATOM   5270  C C     . THR B 2 666  ? 101.908 135.389 168.250 1.00 115.85 ? 663  THR A C     1 
ATOM   5271  O O     . THR B 2 666  ? 102.422 135.816 169.286 1.00 115.85 ? 663  THR A O     1 
ATOM   5272  C CB    . THR B 2 666  ? 102.548 133.103 169.070 1.00 115.85 ? 663  THR A CB    1 
ATOM   5273  O OG1   . THR B 2 666  ? 103.790 133.676 169.497 1.00 115.85 ? 663  THR A OG1   1 
ATOM   5274  C CG2   . THR B 2 666  ? 102.773 131.652 168.668 1.00 115.85 ? 663  THR A CG2   1 
ATOM   5275  N N     . GLY B 2 667  ? 101.272 136.182 167.391 1.00 116.03 ? 664  GLY A N     1 
ATOM   5276  C CA    . GLY B 2 667  ? 101.181 137.617 167.584 1.00 116.03 ? 664  GLY A CA    1 
ATOM   5277  C C     . GLY B 2 667  ? 100.451 138.057 168.836 1.00 116.03 ? 664  GLY A C     1 
ATOM   5278  O O     . GLY B 2 667  ? 99.418  137.487 169.199 1.00 116.03 ? 664  GLY A O     1 
ATOM   5279  N N     . ASP B 2 668  ? 100.988 139.080 169.506 1.00 111.42 ? 665  ASP A N     1 
ATOM   5280  C CA    . ASP B 2 668  ? 100.330 139.664 170.675 1.00 111.42 ? 665  ASP A CA    1 
ATOM   5281  C C     . ASP B 2 668  ? 100.810 141.112 170.777 1.00 111.42 ? 665  ASP A C     1 
ATOM   5282  O O     . ASP B 2 668  ? 101.921 141.363 171.251 1.00 111.42 ? 665  ASP A O     1 
ATOM   5283  C CB    . ASP B 2 668  ? 100.642 138.877 171.938 1.00 111.42 ? 665  ASP A CB    1 
ATOM   5284  C CG    . ASP B 2 668  ? 100.136 139.563 173.194 1.00 111.42 ? 665  ASP A CG    1 
ATOM   5285  O OD1   . ASP B 2 668  ? 99.117  140.282 173.115 1.00 111.42 ? 665  ASP A OD1   1 
ATOM   5286  O OD2   . ASP B 2 668  ? 100.757 139.381 174.262 1.00 111.42 ? 665  ASP A OD2   1 
ATOM   5287  N N     . GLN B 2 669  ? 99.969  142.046 170.328 1.00 110.02 ? 666  GLN A N     1 
ATOM   5288  C CA    . GLN B 2 669  ? 100.365 143.450 170.300 1.00 110.02 ? 666  GLN A CA    1 
ATOM   5289  C C     . GLN B 2 669  ? 100.525 144.020 171.704 1.00 110.02 ? 666  GLN A C     1 
ATOM   5290  O O     . GLN B 2 669  ? 101.467 144.774 171.972 1.00 110.02 ? 666  GLN A O     1 
ATOM   5291  C CB    . GLN B 2 669  ? 99.345  144.267 169.506 1.00 110.02 ? 666  GLN A CB    1 
ATOM   5292  C CG    . GLN B 2 669  ? 99.837  145.647 169.103 1.00 110.02 ? 666  GLN A CG    1 
ATOM   5293  C CD    . GLN B 2 669  ? 100.987 145.591 168.117 1.00 110.02 ? 666  GLN A CD    1 
ATOM   5294  O OE1   . GLN B 2 669  ? 101.066 144.682 167.290 1.00 110.02 ? 666  GLN A OE1   1 
ATOM   5295  N NE2   . GLN B 2 669  ? 101.887 146.564 168.200 1.00 110.02 ? 666  GLN A NE2   1 
ATOM   5296  N N     . LYS B 2 670  ? 99.609  143.677 172.613 1.00 111.69 ? 667  LYS A N     1 
ATOM   5297  C CA    . LYS B 2 670  ? 99.651  144.243 173.959 1.00 111.69 ? 667  LYS A CA    1 
ATOM   5298  C C     . LYS B 2 670  ? 100.908 143.804 174.700 1.00 111.69 ? 667  LYS A C     1 
ATOM   5299  O O     . LYS B 2 670  ? 101.573 144.615 175.355 1.00 111.69 ? 667  LYS A O     1 
ATOM   5300  C CB    . LYS B 2 670  ? 98.394  143.841 174.733 1.00 111.69 ? 667  LYS A CB    1 
ATOM   5301  C CG    . LYS B 2 670  ? 98.471  144.093 176.232 1.00 111.69 ? 667  LYS A CG    1 
ATOM   5302  C CD    . LYS B 2 670  ? 98.622  145.577 176.536 1.00 111.69 ? 667  LYS A CD    1 
ATOM   5303  C CE    . LYS B 2 670  ? 98.811  145.822 178.024 1.00 111.69 ? 667  LYS A CE    1 
ATOM   5304  N NZ    . LYS B 2 670  ? 99.689  144.796 178.649 1.00 111.69 ? 667  LYS A NZ    1 
ATOM   5305  N N     . GLY B 2 671  ? 101.249 142.518 174.609 1.00 108.46 ? 668  GLY A N     1 
ATOM   5306  C CA    . GLY B 2 671  ? 102.472 142.042 175.234 1.00 108.46 ? 668  GLY A CA    1 
ATOM   5307  C C     . GLY B 2 671  ? 103.720 142.600 174.577 1.00 108.46 ? 668  GLY A C     1 
ATOM   5308  O O     . GLY B 2 671  ? 104.720 142.868 175.248 1.00 108.46 ? 668  GLY A O     1 
ATOM   5309  N N     . TYR B 2 672  ? 103.681 142.772 173.254 1.00 106.84 ? 669  TYR A N     1 
ATOM   5310  C CA    . TYR B 2 672  ? 104.832 143.297 172.527 1.00 106.84 ? 669  TYR A CA    1 
ATOM   5311  C C     . TYR B 2 672  ? 105.213 144.691 173.009 1.00 106.84 ? 669  TYR A C     1 
ATOM   5312  O O     . TYR B 2 672  ? 106.374 144.946 173.350 1.00 106.84 ? 669  TYR A O     1 
ATOM   5313  C CB    . TYR B 2 672  ? 104.533 143.316 171.028 1.00 106.84 ? 669  TYR A CB    1 
ATOM   5314  C CG    . TYR B 2 672  ? 105.756 143.197 170.154 1.00 106.84 ? 669  TYR A CG    1 
ATOM   5315  C CD1   . TYR B 2 672  ? 106.330 141.963 169.886 1.00 106.84 ? 669  TYR A CD1   1 
ATOM   5316  C CD2   . TYR B 2 672  ? 106.336 144.326 169.594 1.00 106.84 ? 669  TYR A CD2   1 
ATOM   5317  C CE1   . TYR B 2 672  ? 107.449 141.859 169.084 1.00 106.84 ? 669  TYR A CE1   1 
ATOM   5318  C CE2   . TYR B 2 672  ? 107.451 144.233 168.794 1.00 106.84 ? 669  TYR A CE2   1 
ATOM   5319  C CZ    . TYR B 2 672  ? 108.005 143.000 168.542 1.00 106.84 ? 669  TYR A CZ    1 
ATOM   5320  O OH    . TYR B 2 672  ? 109.119 142.915 167.743 1.00 106.84 ? 669  TYR A OH    1 
ATOM   5321  N N     . ARG B 2 673  ? 104.246 145.610 173.045 1.00 103.34 ? 670  ARG A N     1 
ATOM   5322  C CA    . ARG B 2 673  ? 104.569 147.001 173.345 1.00 103.34 ? 670  ARG A CA    1 
ATOM   5323  C C     . ARG B 2 673  ? 105.003 147.170 174.795 1.00 103.34 ? 670  ARG A C     1 
ATOM   5324  O O     . ARG B 2 673  ? 105.873 147.996 175.095 1.00 103.34 ? 670  ARG A O     1 
ATOM   5325  C CB    . ARG B 2 673  ? 103.374 147.898 173.027 1.00 103.34 ? 670  ARG A CB    1 
ATOM   5326  C CG    . ARG B 2 673  ? 102.840 147.724 171.614 1.00 103.34 ? 670  ARG A CG    1 
ATOM   5327  C CD    . ARG B 2 673  ? 103.854 148.150 170.564 1.00 103.34 ? 670  ARG A CD    1 
ATOM   5328  N NE    . ARG B 2 673  ? 104.130 149.581 170.593 1.00 103.34 ? 670  ARG A NE    1 
ATOM   5329  C CZ    . ARG B 2 673  ? 105.056 150.177 169.854 1.00 103.34 ? 670  ARG A CZ    1 
ATOM   5330  N NH1   . ARG B 2 673  ? 105.806 149.495 169.004 1.00 103.34 ? 670  ARG A NH1   1 
ATOM   5331  N NH2   . ARG B 2 673  ? 105.231 151.490 169.968 1.00 103.34 ? 670  ARG A NH2   1 
ATOM   5332  N N     . GLU B 2 674  ? 104.404 146.405 175.711 1.00 101.33 ? 671  GLU A N     1 
ATOM   5333  C CA    . GLU B 2 674  ? 104.839 146.442 177.103 1.00 101.33 ? 671  GLU A CA    1 
ATOM   5334  C C     . GLU B 2 674  ? 106.275 145.954 177.237 1.00 101.33 ? 671  GLU A C     1 
ATOM   5335  O O     . GLU B 2 674  ? 107.083 146.550 177.958 1.00 101.33 ? 671  GLU A O     1 
ATOM   5336  C CB    . GLU B 2 674  ? 103.901 145.602 177.970 1.00 101.33 ? 671  GLU A CB    1 
ATOM   5337  C CG    . GLU B 2 674  ? 104.268 145.592 179.444 1.00 101.33 ? 671  GLU A CG    1 
ATOM   5338  C CD    . GLU B 2 674  ? 103.098 145.226 180.335 1.00 101.33 ? 671  GLU A CD    1 
ATOM   5339  O OE1   . GLU B 2 674  ? 102.235 144.440 179.891 1.00 101.33 ? 671  GLU A OE1   1 
ATOM   5340  O OE2   . GLU B 2 674  ? 103.041 145.725 181.479 1.00 101.33 ? 671  GLU A OE2   1 
ATOM   5341  N N     . ALA B 2 675  ? 106.611 144.861 176.549 1.00 100.04 ? 672  ALA A N     1 
ATOM   5342  C CA    . ALA B 2 675  ? 107.986 144.375 176.564 1.00 100.04 ? 672  ALA A CA    1 
ATOM   5343  C C     . ALA B 2 675  ? 108.926 145.368 175.895 1.00 100.04 ? 672  ALA A C     1 
ATOM   5344  O O     . ALA B 2 675  ? 110.040 145.603 176.377 1.00 100.04 ? 672  ALA A O     1 
ATOM   5345  C CB    . ALA B 2 675  ? 108.068 143.011 175.881 1.00 100.04 ? 672  ALA A CB    1 
ATOM   5346  N N     . LEU B 2 676  ? 108.494 145.956 174.778 1.00 95.81  ? 673  LEU A N     1 
ATOM   5347  C CA    . LEU B 2 676  ? 109.338 146.903 174.058 1.00 95.81  ? 673  LEU A CA    1 
ATOM   5348  C C     . LEU B 2 676  ? 109.609 148.153 174.885 1.00 95.81  ? 673  LEU A C     1 
ATOM   5349  O O     . LEU B 2 676  ? 110.745 148.639 174.933 1.00 95.81  ? 673  LEU A O     1 
ATOM   5350  C CB    . LEU B 2 676  ? 108.681 147.271 172.730 1.00 95.81  ? 673  LEU A CB    1 
ATOM   5351  C CG    . LEU B 2 676  ? 109.456 148.210 171.809 1.00 95.81  ? 673  LEU A CG    1 
ATOM   5352  C CD1   . LEU B 2 676  ? 110.757 147.572 171.381 1.00 95.81  ? 673  LEU A CD1   1 
ATOM   5353  C CD2   . LEU B 2 676  ? 108.613 148.561 170.601 1.00 95.81  ? 673  LEU A CD2   1 
ATOM   5354  N N     . CYS B 2 677  ? 108.580 148.690 175.545 1.00 97.07  ? 674  CYS A N     1 
ATOM   5355  C CA    . CYS B 2 677  ? 108.756 149.927 176.300 1.00 97.07  ? 674  CYS A CA    1 
ATOM   5356  C C     . CYS B 2 677  ? 109.594 149.698 177.552 1.00 97.07  ? 674  CYS A C     1 
ATOM   5357  O O     . CYS B 2 677  ? 110.347 150.584 177.971 1.00 97.07  ? 674  CYS A O     1 
ATOM   5358  C CB    . CYS B 2 677  ? 107.396 150.523 176.663 1.00 97.07  ? 674  CYS A CB    1 
ATOM   5359  S SG    . CYS B 2 677  ? 106.521 149.660 177.988 1.00 97.07  ? 674  CYS A SG    1 
ATOM   5360  N N     . LYS B 2 678  ? 109.470 148.520 178.167 1.00 95.40  ? 675  LYS A N     1 
ATOM   5361  C CA    . LYS B 2 678  ? 110.287 148.208 179.336 1.00 95.40  ? 675  LYS A CA    1 
ATOM   5362  C C     . LYS B 2 678  ? 111.764 148.143 178.970 1.00 95.40  ? 675  LYS A C     1 
ATOM   5363  O O     . LYS B 2 678  ? 112.621 148.619 179.724 1.00 95.40  ? 675  LYS A O     1 
ATOM   5364  C CB    . LYS B 2 678  ? 109.828 146.890 179.959 1.00 95.40  ? 675  LYS A CB    1 
ATOM   5365  C CG    . LYS B 2 678  ? 108.559 146.999 180.788 1.00 95.40  ? 675  LYS A CG    1 
ATOM   5366  C CD    . LYS B 2 678  ? 108.161 145.650 181.366 1.00 95.40  ? 675  LYS A CD    1 
ATOM   5367  C CE    . LYS B 2 678  ? 106.926 145.766 182.245 1.00 95.40  ? 675  LYS A CE    1 
ATOM   5368  N NZ    . LYS B 2 678  ? 107.188 146.562 183.476 1.00 95.40  ? 675  LYS A NZ    1 
ATOM   5369  N N     . TRP B 2 679  ? 112.080 147.549 177.817 1.00 92.81  ? 676  TRP A N     1 
ATOM   5370  C CA    . TRP B 2 679  ? 113.469 147.449 177.383 1.00 92.81  ? 676  TRP A CA    1 
ATOM   5371  C C     . TRP B 2 679  ? 114.072 148.821 177.106 1.00 92.81  ? 676  TRP A C     1 
ATOM   5372  O O     . TRP B 2 679  ? 115.208 149.100 177.508 1.00 92.81  ? 676  TRP A O     1 
ATOM   5373  C CB    . TRP B 2 679  ? 113.558 146.564 176.140 1.00 92.81  ? 676  TRP A CB    1 
ATOM   5374  C CG    . TRP B 2 679  ? 114.952 146.341 175.645 1.00 92.81  ? 676  TRP A CG    1 
ATOM   5375  C CD1   . TRP B 2 679  ? 115.546 146.947 174.576 1.00 92.81  ? 676  TRP A CD1   1 
ATOM   5376  C CD2   . TRP B 2 679  ? 115.930 145.454 176.197 1.00 92.81  ? 676  TRP A CD2   1 
ATOM   5377  N NE1   . TRP B 2 679  ? 116.831 146.489 174.426 1.00 92.81  ? 676  TRP A NE1   1 
ATOM   5378  C CE2   . TRP B 2 679  ? 117.093 145.572 175.410 1.00 92.81  ? 676  TRP A CE2   1 
ATOM   5379  C CE3   . TRP B 2 679  ? 115.936 144.571 177.279 1.00 92.81  ? 676  TRP A CE3   1 
ATOM   5380  C CZ2   . TRP B 2 679  ? 118.248 144.841 175.671 1.00 92.81  ? 676  TRP A CZ2   1 
ATOM   5381  C CZ3   . TRP B 2 679  ? 117.084 143.846 177.536 1.00 92.81  ? 676  TRP A CZ3   1 
ATOM   5382  C CH2   . TRP B 2 679  ? 118.224 143.985 176.736 1.00 92.81  ? 676  TRP A CH2   1 
ATOM   5383  N N     . ILE B 2 680  ? 113.330 149.690 176.419 1.00 89.53  ? 677  ILE A N     1 
ATOM   5384  C CA    . ILE B 2 680  ? 113.892 150.971 175.999 1.00 89.53  ? 677  ILE A CA    1 
ATOM   5385  C C     . ILE B 2 680  ? 114.092 151.891 177.196 1.00 89.53  ? 677  ILE A C     1 
ATOM   5386  O O     . ILE B 2 680  ? 115.129 152.555 177.320 1.00 89.53  ? 677  ILE A O     1 
ATOM   5387  C CB    . ILE B 2 680  ? 113.000 151.620 174.926 1.00 89.53  ? 677  ILE A CB    1 
ATOM   5388  C CG1   . ILE B 2 680  ? 112.952 150.744 173.675 1.00 89.53  ? 677  ILE A CG1   1 
ATOM   5389  C CG2   . ILE B 2 680  ? 113.533 152.985 174.565 1.00 89.53  ? 677  ILE A CG2   1 
ATOM   5390  C CD1   . ILE B 2 680  ? 111.902 151.171 172.674 1.00 89.53  ? 677  ILE A CD1   1 
ATOM   5391  N N     . ASP B 2 681  ? 113.105 151.951 178.094 1.00 90.79  ? 678  ASP A N     1 
ATOM   5392  C CA    . ASP B 2 681  ? 113.247 152.774 179.292 1.00 90.79  ? 678  ASP A CA    1 
ATOM   5393  C C     . ASP B 2 681  ? 114.422 152.306 180.140 1.00 90.79  ? 678  ASP A C     1 
ATOM   5394  O O     . ASP B 2 681  ? 115.095 153.117 180.786 1.00 90.79  ? 678  ASP A O     1 
ATOM   5395  C CB    . ASP B 2 681  ? 111.952 152.752 180.105 1.00 90.79  ? 678  ASP A CB    1 
ATOM   5396  C CG    . ASP B 2 681  ? 110.793 153.402 179.374 1.00 90.79  ? 678  ASP A CG    1 
ATOM   5397  O OD1   . ASP B 2 681  ? 111.024 154.400 178.661 1.00 90.79  ? 678  ASP A OD1   1 
ATOM   5398  O OD2   . ASP B 2 681  ? 109.651 152.916 179.514 1.00 90.79  ? 678  ASP A OD2   1 
ATOM   5399  N N     . PHE B 2 682  ? 114.677 150.996 180.152 1.00 89.80  ? 679  PHE A N     1 
ATOM   5400  C CA    . PHE B 2 682  ? 115.860 150.471 180.825 1.00 89.80  ? 679  PHE A CA    1 
ATOM   5401  C C     . PHE B 2 682  ? 117.133 151.036 180.207 1.00 89.80  ? 679  PHE A C     1 
ATOM   5402  O O     . PHE B 2 682  ? 118.050 151.452 180.924 1.00 89.80  ? 679  PHE A O     1 
ATOM   5403  C CB    . PHE B 2 682  ? 115.851 148.943 180.745 1.00 89.80  ? 679  PHE A CB    1 
ATOM   5404  C CG    . PHE B 2 682  ? 116.966 148.274 181.500 1.00 89.80  ? 679  PHE A CG    1 
ATOM   5405  C CD1   . PHE B 2 682  ? 117.658 148.936 182.501 1.00 89.80  ? 679  PHE A CD1   1 
ATOM   5406  C CD2   . PHE B 2 682  ? 117.336 146.978 181.185 1.00 89.80  ? 679  PHE A CD2   1 
ATOM   5407  C CE1   . PHE B 2 682  ? 118.685 148.313 183.179 1.00 89.80  ? 679  PHE A CE1   1 
ATOM   5408  C CE2   . PHE B 2 682  ? 118.361 146.350 181.859 1.00 89.80  ? 679  PHE A CE2   1 
ATOM   5409  C CZ    . PHE B 2 682  ? 119.037 147.019 182.854 1.00 89.80  ? 679  PHE A CZ    1 
ATOM   5410  N N     . THR B 2 683  ? 117.199 151.073 178.874 1.00 85.61  ? 680  THR A N     1 
ATOM   5411  C CA    . THR B 2 683  ? 118.409 151.538 178.204 1.00 85.61  ? 680  THR A CA    1 
ATOM   5412  C C     . THR B 2 683  ? 118.695 153.000 178.524 1.00 85.61  ? 680  THR A C     1 
ATOM   5413  O O     . THR B 2 683  ? 119.845 153.372 178.785 1.00 85.61  ? 680  THR A O     1 
ATOM   5414  C CB    . THR B 2 683  ? 118.282 151.332 176.694 1.00 85.61  ? 680  THR A CB    1 
ATOM   5415  O OG1   . THR B 2 683  ? 118.180 149.931 176.410 1.00 85.61  ? 680  THR A OG1   1 
ATOM   5416  C CG2   . THR B 2 683  ? 119.497 151.895 175.974 1.00 85.61  ? 680  THR A CG2   1 
ATOM   5417  N N     . ARG B 2 684  ? 117.659 153.843 178.516 1.00 89.45  ? 681  ARG A N     1 
ATOM   5418  C CA    . ARG B 2 684  ? 117.853 155.257 178.821 1.00 89.45  ? 681  ARG A CA    1 
ATOM   5419  C C     . ARG B 2 684  ? 118.371 155.448 180.240 1.00 89.45  ? 681  ARG A C     1 
ATOM   5420  O O     . ARG B 2 684  ? 119.262 156.272 180.478 1.00 89.45  ? 681  ARG A O     1 
ATOM   5421  C CB    . ARG B 2 684  ? 116.544 156.022 178.624 1.00 89.45  ? 681  ARG A CB    1 
ATOM   5422  C CG    . ARG B 2 684  ? 116.123 156.190 177.174 1.00 89.45  ? 681  ARG A CG    1 
ATOM   5423  C CD    . ARG B 2 684  ? 117.076 157.105 176.419 1.00 89.45  ? 681  ARG A CD    1 
ATOM   5424  N NE    . ARG B 2 684  ? 116.936 158.503 176.810 1.00 89.45  ? 681  ARG A NE    1 
ATOM   5425  C CZ    . ARG B 2 684  ? 115.899 159.273 176.510 1.00 89.45  ? 681  ARG A CZ    1 
ATOM   5426  N NH1   . ARG B 2 684  ? 114.876 158.815 175.806 1.00 89.45  ? 681  ARG A NH1   1 
ATOM   5427  N NH2   . ARG B 2 684  ? 115.888 160.537 176.925 1.00 89.45  ? 681  ARG A NH2   1 
ATOM   5428  N N     . ASP B 2 685  ? 117.820 154.700 181.198 1.00 88.40  ? 682  ASP A N     1 
ATOM   5429  C CA    . ASP B 2 685  ? 118.306 154.784 182.571 1.00 88.40  ? 682  ASP A CA    1 
ATOM   5430  C C     . ASP B 2 685  ? 119.745 154.297 182.679 1.00 88.40  ? 682  ASP A C     1 
ATOM   5431  O O     . ASP B 2 685  ? 120.567 154.917 183.363 1.00 88.40  ? 682  ASP A O     1 
ATOM   5432  C CB    . ASP B 2 685  ? 117.396 153.980 183.500 1.00 88.40  ? 682  ASP A CB    1 
ATOM   5433  C CG    . ASP B 2 685  ? 117.465 154.458 184.937 1.00 88.40  ? 682  ASP A CG    1 
ATOM   5434  O OD1   . ASP B 2 685  ? 117.804 155.640 185.157 1.00 88.40  ? 682  ASP A OD1   1 
ATOM   5435  O OD2   . ASP B 2 685  ? 117.181 153.652 185.848 1.00 88.40  ? 682  ASP A OD2   1 
ATOM   5436  N N     . PHE B 2 686  ? 120.069 153.187 182.009 1.00 83.24  ? 683  PHE A N     1 
ATOM   5437  C CA    . PHE B 2 686  ? 121.419 152.638 182.102 1.00 83.24  ? 683  PHE A CA    1 
ATOM   5438  C C     . PHE B 2 686  ? 122.449 153.601 181.532 1.00 83.24  ? 683  PHE A C     1 
ATOM   5439  O O     . PHE B 2 686  ? 123.532 153.772 182.104 1.00 83.24  ? 683  PHE A O     1 
ATOM   5440  C CB    . PHE B 2 686  ? 121.498 151.289 181.387 1.00 83.24  ? 683  PHE A CB    1 
ATOM   5441  C CG    . PHE B 2 686  ? 122.903 150.772 181.225 1.00 83.24  ? 683  PHE A CG    1 
ATOM   5442  C CD1   . PHE B 2 686  ? 123.523 150.084 182.253 1.00 83.24  ? 683  PHE A CD1   1 
ATOM   5443  C CD2   . PHE B 2 686  ? 123.599 150.968 180.044 1.00 83.24  ? 683  PHE A CD2   1 
ATOM   5444  C CE1   . PHE B 2 686  ? 124.812 149.608 182.109 1.00 83.24  ? 683  PHE A CE1   1 
ATOM   5445  C CE2   . PHE B 2 686  ? 124.887 150.495 179.896 1.00 83.24  ? 683  PHE A CE2   1 
ATOM   5446  C CZ    . PHE B 2 686  ? 125.493 149.813 180.928 1.00 83.24  ? 683  PHE A CZ    1 
ATOM   5447  N N     . LEU B 2 687  ? 122.135 154.233 180.400 1.00 81.56  ? 684  LEU A N     1 
ATOM   5448  C CA    . LEU B 2 687  ? 123.071 155.179 179.804 1.00 81.56  ? 684  LEU A CA    1 
ATOM   5449  C C     . LEU B 2 687  ? 123.292 156.377 180.716 1.00 81.56  ? 684  LEU A C     1 
ATOM   5450  O O     . LEU B 2 687  ? 124.407 156.903 180.804 1.00 81.56  ? 684  LEU A O     1 
ATOM   5451  C CB    . LEU B 2 687  ? 122.561 155.628 178.437 1.00 81.56  ? 684  LEU A CB    1 
ATOM   5452  C CG    . LEU B 2 687  ? 122.667 154.585 177.324 1.00 81.56  ? 684  LEU A CG    1 
ATOM   5453  C CD1   . LEU B 2 687  ? 122.270 155.192 175.994 1.00 81.56  ? 684  LEU A CD1   1 
ATOM   5454  C CD2   . LEU B 2 687  ? 124.072 154.011 177.257 1.00 81.56  ? 684  LEU A CD2   1 
ATOM   5455  N N     . SER B 2 688  ? 122.243 156.817 181.411 1.00 85.30  ? 685  SER A N     1 
ATOM   5456  C CA    . SER B 2 688  ? 122.387 157.931 182.341 1.00 85.30  ? 685  SER A CA    1 
ATOM   5457  C C     . SER B 2 688  ? 123.229 157.538 183.549 1.00 85.30  ? 685  SER A C     1 
ATOM   5458  O O     . SER B 2 688  ? 123.962 158.367 184.100 1.00 85.30  ? 685  SER A O     1 
ATOM   5459  C CB    . SER B 2 688  ? 121.011 158.424 182.784 1.00 85.30  ? 685  SER A CB    1 
ATOM   5460  O OG    . SER B 2 688  ? 120.445 157.553 183.748 1.00 85.30  ? 685  SER A OG    1 
ATOM   5461  N N     . LYS B 2 689  ? 123.136 156.280 183.977 1.00 88.83  ? 686  LYS A N     1 
ATOM   5462  C CA    . LYS B 2 689  ? 123.821 155.825 185.179 1.00 88.83  ? 686  LYS A CA    1 
ATOM   5463  C C     . LYS B 2 689  ? 125.180 155.190 184.905 1.00 88.83  ? 686  LYS A C     1 
ATOM   5464  O O     . LYS B 2 689  ? 125.978 155.057 185.838 1.00 88.83  ? 686  LYS A O     1 
ATOM   5465  C CB    . LYS B 2 689  ? 122.939 154.832 185.944 1.00 88.83  ? 686  LYS A CB    1 
ATOM   5466  C CG    . LYS B 2 689  ? 121.588 155.402 186.348 1.00 88.83  ? 686  LYS A CG    1 
ATOM   5467  C CD    . LYS B 2 689  ? 120.634 154.314 186.804 1.00 88.83  ? 686  LYS A CD    1 
ATOM   5468  C CE    . LYS B 2 689  ? 119.684 154.825 187.874 1.00 88.83  ? 686  LYS A CE    1 
ATOM   5469  N NZ    . LYS B 2 689  ? 118.786 153.750 188.379 1.00 88.83  ? 686  LYS A NZ    1 
ATOM   5470  N N     . TYR B 2 690  ? 125.465 154.795 183.668 1.00 76.52  ? 687  TYR A N     1 
ATOM   5471  C CA    . TYR B 2 690  ? 126.764 154.217 183.368 1.00 76.52  ? 687  TYR A CA    1 
ATOM   5472  C C     . TYR B 2 690  ? 127.833 155.307 183.420 1.00 76.52  ? 687  TYR A C     1 
ATOM   5473  O O     . TYR B 2 690  ? 127.551 156.497 183.254 1.00 76.52  ? 687  TYR A O     1 
ATOM   5474  C CB    . TYR B 2 690  ? 126.739 153.530 182.003 1.00 76.52  ? 687  TYR A CB    1 
ATOM   5475  C CG    . TYR B 2 690  ? 128.031 152.848 181.618 1.00 76.52  ? 687  TYR A CG    1 
ATOM   5476  C CD1   . TYR B 2 690  ? 128.387 151.634 182.189 1.00 76.52  ? 687  TYR A CD1   1 
ATOM   5477  C CD2   . TYR B 2 690  ? 128.886 153.405 180.680 1.00 76.52  ? 687  TYR A CD2   1 
ATOM   5478  C CE1   . TYR B 2 690  ? 129.560 150.998 181.842 1.00 76.52  ? 687  TYR A CE1   1 
ATOM   5479  C CE2   . TYR B 2 690  ? 130.063 152.774 180.326 1.00 76.52  ? 687  TYR A CE2   1 
ATOM   5480  C CZ    . TYR B 2 690  ? 130.395 151.572 180.911 1.00 76.52  ? 687  TYR A CZ    1 
ATOM   5481  O OH    . TYR B 2 690  ? 131.567 150.941 180.563 1.00 76.52  ? 687  TYR A OH    1 
ATOM   5482  N N     . THR B 2 691  ? 129.077 154.888 183.663 1.00 79.03  ? 688  THR A N     1 
ATOM   5483  C CA    . THR B 2 691  ? 130.126 155.835 184.037 1.00 79.03  ? 688  THR A CA    1 
ATOM   5484  C C     . THR B 2 691  ? 130.423 156.831 182.920 1.00 79.03  ? 688  THR A C     1 
ATOM   5485  O O     . THR B 2 691  ? 130.406 158.048 183.137 1.00 79.03  ? 688  THR A O     1 
ATOM   5486  C CB    . THR B 2 691  ? 131.397 155.080 184.429 1.00 79.03  ? 688  THR A CB    1 
ATOM   5487  O OG1   . THR B 2 691  ? 131.123 154.231 185.551 1.00 79.03  ? 688  THR A OG1   1 
ATOM   5488  C CG2   . THR B 2 691  ? 132.501 156.059 184.799 1.00 79.03  ? 688  THR A CG2   1 
ATOM   5489  N N     . LYS B 2 692  ? 130.696 156.336 181.711 1.00 76.30  ? 689  LYS A N     1 
ATOM   5490  C CA    . LYS B 2 692  ? 131.177 157.208 180.646 1.00 76.30  ? 689  LYS A CA    1 
ATOM   5491  C C     . LYS B 2 692  ? 130.096 157.630 179.661 1.00 76.30  ? 689  LYS A C     1 
ATOM   5492  O O     . LYS B 2 692  ? 130.311 158.583 178.905 1.00 76.30  ? 689  LYS A O     1 
ATOM   5493  C CB    . LYS B 2 692  ? 132.332 156.535 179.888 1.00 76.30  ? 689  LYS A CB    1 
ATOM   5494  C CG    . LYS B 2 692  ? 131.948 155.333 179.042 1.00 76.30  ? 689  LYS A CG    1 
ATOM   5495  C CD    . LYS B 2 692  ? 131.792 155.706 177.576 1.00 76.30  ? 689  LYS A CD    1 
ATOM   5496  C CE    . LYS B 2 692  ? 131.600 154.475 176.711 1.00 76.30  ? 689  LYS A CE    1 
ATOM   5497  N NZ    . LYS B 2 692  ? 131.443 154.839 175.278 1.00 76.30  ? 689  LYS A NZ    1 
ATOM   5498  N N     . THR B 2 693  ? 128.950 156.955 179.647 1.00 83.84  ? 690  THR A N     1 
ATOM   5499  C CA    . THR B 2 693  ? 127.837 157.335 178.788 1.00 83.84  ? 690  THR A CA    1 
ATOM   5500  C C     . THR B 2 693  ? 126.832 158.238 179.493 1.00 83.84  ? 690  THR A C     1 
ATOM   5501  O O     . THR B 2 693  ? 125.753 158.489 178.946 1.00 83.84  ? 690  THR A O     1 
ATOM   5502  C CB    . THR B 2 693  ? 127.126 156.087 178.256 1.00 83.84  ? 690  THR A CB    1 
ATOM   5503  O OG1   . THR B 2 693  ? 126.413 155.448 179.322 1.00 83.84  ? 690  THR A OG1   1 
ATOM   5504  C CG2   . THR B 2 693  ? 128.130 155.112 177.667 1.00 83.84  ? 690  THR A CG2   1 
ATOM   5505  N N     . THR B 2 694  ? 127.164 158.731 180.689 1.00 89.72  ? 691  THR A N     1 
ATOM   5506  C CA    . THR B 2 694  ? 126.194 159.466 181.494 1.00 89.72  ? 691  THR A CA    1 
ATOM   5507  C C     . THR B 2 694  ? 125.811 160.804 180.870 1.00 89.72  ? 691  THR A C     1 
ATOM   5508  O O     . THR B 2 694  ? 124.719 161.316 181.141 1.00 89.72  ? 691  THR A O     1 
ATOM   5509  C CB    . THR B 2 694  ? 126.740 159.685 182.906 1.00 89.72  ? 691  THR A CB    1 
ATOM   5510  O OG1   . THR B 2 694  ? 125.786 160.423 183.681 1.00 89.72  ? 691  THR A OG1   1 
ATOM   5511  C CG2   . THR B 2 694  ? 128.054 160.451 182.863 1.00 89.72  ? 691  THR A CG2   1 
ATOM   5512  N N     . SER B 2 695  ? 126.680 161.387 180.045 1.00 92.45  ? 692  SER A N     1 
ATOM   5513  C CA    . SER B 2 695  ? 126.452 162.732 179.529 1.00 92.45  ? 692  SER A CA    1 
ATOM   5514  C C     . SER B 2 695  ? 126.544 162.827 178.011 1.00 92.45  ? 692  SER A C     1 
ATOM   5515  O O     . SER B 2 695  ? 126.733 163.930 177.486 1.00 92.45  ? 692  SER A O     1 
ATOM   5516  C CB    . SER B 2 695  ? 127.440 163.713 180.167 1.00 92.45  ? 692  SER A CB    1 
ATOM   5517  O OG    . SER B 2 695  ? 127.280 163.755 181.575 1.00 92.45  ? 692  SER A OG    1 
ATOM   5518  N N     . ILE B 2 696  ? 126.419 161.718 177.289 1.00 93.00  ? 693  ILE A N     1 
ATOM   5519  C CA    . ILE B 2 696  ? 126.547 161.745 175.821 1.00 93.00  ? 693  ILE A CA    1 
ATOM   5520  C C     . ILE B 2 696  ? 125.142 161.967 175.267 1.00 93.00  ? 693  ILE A C     1 
ATOM   5521  O O     . ILE B 2 696  ? 124.432 161.044 174.858 1.00 93.00  ? 693  ILE A O     1 
ATOM   5522  C CB    . ILE B 2 696  ? 127.232 160.483 175.275 1.00 93.00  ? 693  ILE A CB    1 
ATOM   5523  C CG1   . ILE B 2 696  ? 127.223 160.473 173.742 1.00 93.00  ? 693  ILE A CG1   1 
ATOM   5524  C CG2   . ILE B 2 696  ? 126.620 159.213 175.867 1.00 93.00  ? 693  ILE A CG2   1 
ATOM   5525  C CD1   . ILE B 2 696  ? 128.039 161.585 173.120 1.00 93.00  ? 693  ILE A CD1   1 
ATOM   5526  N N     . ASP B 2 697  ? 124.732 163.238 175.261 1.00 101.07 ? 694  ASP A N     1 
ATOM   5527  C CA    . ASP B 2 697  ? 123.547 163.742 174.552 1.00 101.07 ? 694  ASP A CA    1 
ATOM   5528  C C     . ASP B 2 697  ? 122.370 162.768 174.592 1.00 101.07 ? 694  ASP A C     1 
ATOM   5529  O O     . ASP B 2 697  ? 121.803 162.391 173.564 1.00 101.07 ? 694  ASP A O     1 
ATOM   5530  C CB    . ASP B 2 697  ? 123.901 164.103 173.110 1.00 101.07 ? 694  ASP A CB    1 
ATOM   5531  C CG    . ASP B 2 697  ? 124.824 165.303 173.021 1.00 101.07 ? 694  ASP A CG    1 
ATOM   5532  O OD1   . ASP B 2 697  ? 125.169 165.869 174.080 1.00 101.07 ? 694  ASP A OD1   1 
ATOM   5533  O OD2   . ASP B 2 697  ? 125.203 165.681 171.892 1.00 101.07 ? 694  ASP A OD2   1 
ATOM   5534  N N     . LEU B 2 698  ? 121.997 162.355 175.802 1.00 102.11 ? 695  LEU A N     1 
ATOM   5535  C CA    . LEU B 2 698  ? 120.886 161.424 175.953 1.00 102.11 ? 695  LEU A CA    1 
ATOM   5536  C C     . LEU B 2 698  ? 119.526 162.106 175.884 1.00 102.11 ? 695  LEU A C     1 
ATOM   5537  O O     . LEU B 2 698  ? 118.509 161.412 175.781 1.00 102.11 ? 695  LEU A O     1 
ATOM   5538  C CB    . LEU B 2 698  ? 121.019 160.650 177.271 1.00 102.11 ? 695  LEU A CB    1 
ATOM   5539  C CG    . LEU B 2 698  ? 121.047 161.410 178.602 1.00 102.11 ? 695  LEU A CG    1 
ATOM   5540  C CD1   . LEU B 2 698  ? 119.646 161.636 179.162 1.00 102.11 ? 695  LEU A CD1   1 
ATOM   5541  C CD2   . LEU B 2 698  ? 121.913 160.675 179.610 1.00 102.11 ? 695  LEU A CD2   1 
ATOM   5542  N N     . SER B 2 699  ? 119.481 163.438 175.938 1.00 106.09 ? 696  SER A N     1 
ATOM   5543  C CA    . SER B 2 699  ? 118.214 164.156 175.887 1.00 106.09 ? 696  SER A CA    1 
ATOM   5544  C C     . SER B 2 699  ? 117.645 164.254 174.478 1.00 106.09 ? 696  SER A C     1 
ATOM   5545  O O     . SER B 2 699  ? 116.461 164.574 174.325 1.00 106.09 ? 696  SER A O     1 
ATOM   5546  C CB    . SER B 2 699  ? 118.380 165.559 176.474 1.00 106.09 ? 696  SER A CB    1 
ATOM   5547  O OG    . SER B 2 699  ? 119.274 166.335 175.696 1.00 106.09 ? 696  SER A OG    1 
ATOM   5548  N N     . SER B 2 700  ? 118.451 163.985 173.450 1.00 101.52 ? 697  SER A N     1 
ATOM   5549  C CA    . SER B 2 700  ? 117.975 164.081 172.076 1.00 101.52 ? 697  SER A CA    1 
ATOM   5550  C C     . SER B 2 700  ? 117.149 162.875 171.650 1.00 101.52 ? 697  SER A C     1 
ATOM   5551  O O     . SER B 2 700  ? 116.596 162.887 170.545 1.00 101.52 ? 697  SER A O     1 
ATOM   5552  C CB    . SER B 2 700  ? 119.157 164.258 171.122 1.00 101.52 ? 697  SER A CB    1 
ATOM   5553  O OG    . SER B 2 700  ? 118.729 164.244 169.772 1.00 101.52 ? 697  SER A OG    1 
ATOM   5554  N N     . LEU B 2 701  ? 117.057 161.844 172.484 1.00 93.87  ? 698  LEU A N     1 
ATOM   5555  C CA    . LEU B 2 701  ? 116.247 160.682 172.145 1.00 93.87  ? 698  LEU A CA    1 
ATOM   5556  C C     . LEU B 2 701  ? 114.765 161.025 172.224 1.00 93.87  ? 698  LEU A C     1 
ATOM   5557  O O     . LEU B 2 701  ? 114.335 161.811 173.073 1.00 93.87  ? 698  LEU A O     1 
ATOM   5558  C CB    . LEU B 2 701  ? 116.561 159.514 173.081 1.00 93.87  ? 698  LEU A CB    1 
ATOM   5559  C CG    . LEU B 2 701  ? 117.770 158.622 172.782 1.00 93.87  ? 698  LEU A CG    1 
ATOM   5560  C CD1   . LEU B 2 701  ? 117.585 157.903 171.454 1.00 93.87  ? 698  LEU A CD1   1 
ATOM   5561  C CD2   . LEU B 2 701  ? 119.083 159.392 172.813 1.00 93.87  ? 698  LEU A CD2   1 
ATOM   5562  N N     . ARG B 2 702  ? 113.981 160.429 171.331 1.00 90.57  ? 699  ARG A N     1 
ATOM   5563  C CA    . ARG B 2 702  ? 112.555 160.696 171.312 1.00 90.57  ? 699  ARG A CA    1 
ATOM   5564  C C     . ARG B 2 702  ? 111.802 159.567 172.017 1.00 90.57  ? 699  ARG A C     1 
ATOM   5565  O O     . ARG B 2 702  ? 112.210 158.405 171.946 1.00 90.57  ? 699  ARG A O     1 
ATOM   5566  C CB    . ARG B 2 702  ? 112.074 160.877 169.873 1.00 90.57  ? 699  ARG A CB    1 
ATOM   5567  C CG    . ARG B 2 702  ? 110.638 161.349 169.717 1.00 90.57  ? 699  ARG A CG    1 
ATOM   5568  C CD    . ARG B 2 702  ? 109.710 160.230 169.288 1.00 90.57  ? 699  ARG A CD    1 
ATOM   5569  N NE    . ARG B 2 702  ? 110.030 159.784 167.936 1.00 90.57  ? 699  ARG A NE    1 
ATOM   5570  C CZ    . ARG B 2 702  ? 109.555 158.682 167.370 1.00 90.57  ? 699  ARG A CZ    1 
ATOM   5571  N NH1   . ARG B 2 702  ? 108.710 157.887 168.005 1.00 90.57  ? 699  ARG A NH1   1 
ATOM   5572  N NH2   . ARG B 2 702  ? 109.934 158.373 166.133 1.00 90.57  ? 699  ARG A NH2   1 
ATOM   5573  N N     . PRO B 2 703  ? 110.710 159.907 172.732 1.00 89.13  ? 700  PRO A N     1 
ATOM   5574  C CA    . PRO B 2 703  ? 110.090 158.998 173.686 1.00 89.13  ? 700  PRO A CA    1 
ATOM   5575  C C     . PRO B 2 703  ? 109.944 157.537 173.274 1.00 89.13  ? 700  PRO A C     1 
ATOM   5576  O O     . PRO B 2 703  ? 109.820 157.203 172.091 1.00 89.13  ? 700  PRO A O     1 
ATOM   5577  C CB    . PRO B 2 703  ? 108.710 159.656 173.840 1.00 89.13  ? 700  PRO A CB    1 
ATOM   5578  C CG    . PRO B 2 703  ? 109.086 161.229 173.553 1.00 89.13  ? 700  PRO A CG    1 
ATOM   5579  C CD    . PRO B 2 703  ? 110.587 161.170 173.489 1.00 89.13  ? 700  PRO A CD    1 
ATOM   5580  N N     . SER B 2 704  ? 109.918 156.660 174.282 1.00 92.52  ? 701  SER A N     1 
ATOM   5581  C CA    . SER B 2 704  ? 110.120 155.224 174.121 1.00 92.52  ? 701  SER A CA    1 
ATOM   5582  C C     . SER B 2 704  ? 108.878 154.467 173.668 1.00 92.52  ? 701  SER A C     1 
ATOM   5583  O O     . SER B 2 704  ? 108.980 153.577 172.817 1.00 92.52  ? 701  SER A O     1 
ATOM   5584  C CB    . SER B 2 704  ? 110.610 154.627 175.441 1.00 92.52  ? 701  SER A CB    1 
ATOM   5585  O OG    . SER B 2 704  ? 111.623 155.426 176.026 1.00 92.52  ? 701  SER A OG    1 
ATOM   5586  N N     . SER B 2 705  ? 107.709 154.791 174.226 1.00 94.19  ? 702  SER A N     1 
ATOM   5587  C CA    . SER B 2 705  ? 106.554 153.906 174.099 1.00 94.19  ? 702  SER A CA    1 
ATOM   5588  C C     . SER B 2 705  ? 106.095 153.746 172.655 1.00 94.19  ? 702  SER A C     1 
ATOM   5589  O O     . SER B 2 705  ? 105.493 152.723 172.311 1.00 94.19  ? 702  SER A O     1 
ATOM   5590  C CB    . SER B 2 705  ? 105.402 154.419 174.964 1.00 94.19  ? 702  SER A CB    1 
ATOM   5591  O OG    . SER B 2 705  ? 105.838 154.679 176.287 1.00 94.19  ? 702  SER A OG    1 
ATOM   5592  N N     . GLN B 2 706  ? 106.362 154.728 171.799 1.00 93.77  ? 703  GLN A N     1 
ATOM   5593  C CA    . GLN B 2 706  ? 105.854 154.691 170.435 1.00 93.77  ? 703  GLN A CA    1 
ATOM   5594  C C     . GLN B 2 706  ? 106.908 154.305 169.403 1.00 93.77  ? 703  GLN A C     1 
ATOM   5595  O O     . GLN B 2 706  ? 106.619 154.354 168.202 1.00 93.77  ? 703  GLN A O     1 
ATOM   5596  C CB    . GLN B 2 706  ? 105.232 156.041 170.067 1.00 93.77  ? 703  GLN A CB    1 
ATOM   5597  C CG    . GLN B 2 706  ? 106.229 157.157 169.868 1.00 93.77  ? 703  GLN A CG    1 
ATOM   5598  C CD    . GLN B 2 706  ? 106.730 157.734 171.173 1.00 93.77  ? 703  GLN A CD    1 
ATOM   5599  O OE1   . GLN B 2 706  ? 106.321 157.314 172.255 1.00 93.77  ? 703  GLN A OE1   1 
ATOM   5600  N NE2   . GLN B 2 706  ? 107.619 158.708 171.076 1.00 93.77  ? 703  GLN A NE2   1 
ATOM   5601  N N     . TYR B 2 707  ? 108.112 153.926 169.826 1.00 90.94  ? 704  TYR A N     1 
ATOM   5602  C CA    . TYR B 2 707  ? 109.074 153.362 168.889 1.00 90.94  ? 704  TYR A CA    1 
ATOM   5603  C C     . TYR B 2 707  ? 108.569 152.018 168.382 1.00 90.94  ? 704  TYR A C     1 
ATOM   5604  O O     . TYR B 2 707  ? 107.910 151.276 169.115 1.00 90.94  ? 704  TYR A O     1 
ATOM   5605  C CB    . TYR B 2 707  ? 110.446 153.201 169.543 1.00 90.94  ? 704  TYR A CB    1 
ATOM   5606  C CG    . TYR B 2 707  ? 111.323 154.430 169.449 1.00 90.94  ? 704  TYR A CG    1 
ATOM   5607  C CD1   . TYR B 2 707  ? 110.779 155.678 169.180 1.00 90.94  ? 704  TYR A CD1   1 
ATOM   5608  C CD2   . TYR B 2 707  ? 112.700 154.336 169.597 1.00 90.94  ? 704  TYR A CD2   1 
ATOM   5609  C CE1   . TYR B 2 707  ? 111.580 156.800 169.086 1.00 90.94  ? 704  TYR A CE1   1 
ATOM   5610  C CE2   . TYR B 2 707  ? 113.508 155.455 169.499 1.00 90.94  ? 704  TYR A CE2   1 
ATOM   5611  C CZ    . TYR B 2 707  ? 112.942 156.683 169.245 1.00 90.94  ? 704  TYR A CZ    1 
ATOM   5612  O OH    . TYR B 2 707  ? 113.740 157.800 169.149 1.00 90.94  ? 704  TYR A OH    1 
ATOM   5613  N N     . LYS B 2 708  ? 108.864 151.711 167.118 1.00 92.90  ? 705  LYS A N     1 
ATOM   5614  C CA    . LYS B 2 708  ? 108.329 150.491 166.522 1.00 92.90  ? 705  LYS A CA    1 
ATOM   5615  C C     . LYS B 2 708  ? 109.041 149.251 167.049 1.00 92.90  ? 705  LYS A C     1 
ATOM   5616  O O     . LYS B 2 708  ? 108.393 148.247 167.366 1.00 92.90  ? 705  LYS A O     1 
ATOM   5617  C CB    . LYS B 2 708  ? 108.429 150.561 164.998 1.00 92.90  ? 705  LYS A CB    1 
ATOM   5618  C CG    . LYS B 2 708  ? 107.955 149.300 164.295 1.00 92.90  ? 705  LYS A CG    1 
ATOM   5619  C CD    . LYS B 2 708  ? 106.479 149.050 164.564 1.00 92.90  ? 705  LYS A CD    1 
ATOM   5620  C CE    . LYS B 2 708  ? 106.016 147.737 163.955 1.00 92.90  ? 705  LYS A CE    1 
ATOM   5621  N NZ    . LYS B 2 708  ? 106.177 147.724 162.475 1.00 92.90  ? 705  LYS A NZ    1 
ATOM   5622  N N     . ASP B 2 709  ? 110.366 149.301 167.153 1.00 93.57  ? 706  ASP A N     1 
ATOM   5623  C CA    . ASP B 2 709  ? 111.142 148.150 167.597 1.00 93.57  ? 706  ASP A CA    1 
ATOM   5624  C C     . ASP B 2 709  ? 112.531 148.622 167.999 1.00 93.57  ? 706  ASP A C     1 
ATOM   5625  O O     . ASP B 2 709  ? 112.854 149.810 167.924 1.00 93.57  ? 706  ASP A O     1 
ATOM   5626  C CB    . ASP B 2 709  ? 111.225 147.077 166.506 1.00 93.57  ? 706  ASP A CB    1 
ATOM   5627  C CG    . ASP B 2 709  ? 111.562 147.655 165.145 1.00 93.57  ? 706  ASP A CG    1 
ATOM   5628  O OD1   . ASP B 2 709  ? 111.553 148.897 165.006 1.00 93.57  ? 706  ASP A OD1   1 
ATOM   5629  O OD2   . ASP B 2 709  ? 111.837 146.869 164.215 1.00 93.57  ? 706  ASP A OD2   1 
ATOM   5630  N N     . LEU B 2 710  ? 113.353 147.665 168.438 1.00 88.24  ? 707  LEU A N     1 
ATOM   5631  C CA    . LEU B 2 710  ? 114.751 147.942 168.744 1.00 88.24  ? 707  LEU A CA    1 
ATOM   5632  C C     . LEU B 2 710  ? 115.526 148.467 167.545 1.00 88.24  ? 707  LEU A C     1 
ATOM   5633  O O     . LEU B 2 710  ? 116.525 149.168 167.738 1.00 88.24  ? 707  LEU A O     1 
ATOM   5634  C CB    . LEU B 2 710  ? 115.448 146.683 169.265 1.00 88.24  ? 707  LEU A CB    1 
ATOM   5635  C CG    . LEU B 2 710  ? 115.420 146.336 170.755 1.00 88.24  ? 707  LEU A CG    1 
ATOM   5636  C CD1   . LEU B 2 710  ? 114.006 146.185 171.276 1.00 88.24  ? 707  LEU A CD1   1 
ATOM   5637  C CD2   . LEU B 2 710  ? 116.220 145.068 171.001 1.00 88.24  ? 707  LEU A CD2   1 
ATOM   5638  N N     . GLY B 2 711  ? 115.099 148.139 166.324 1.00 87.59  ? 708  GLY A N     1 
ATOM   5639  C CA    . GLY B 2 711  ? 115.883 148.500 165.154 1.00 87.59  ? 708  GLY A CA    1 
ATOM   5640  C C     . GLY B 2 711  ? 116.047 149.998 164.993 1.00 87.59  ? 708  GLY A C     1 
ATOM   5641  O O     . GLY B 2 711  ? 117.151 150.492 164.756 1.00 87.59  ? 708  GLY A O     1 
ATOM   5642  N N     . GLU B 2 712  ? 114.949 150.746 165.124 1.00 88.46  ? 709  GLU A N     1 
ATOM   5643  C CA    . GLU B 2 712  ? 115.036 152.190 164.938 1.00 88.46  ? 709  GLU A CA    1 
ATOM   5644  C C     . GLU B 2 712  ? 115.597 152.877 166.177 1.00 88.46  ? 709  GLU A C     1 
ATOM   5645  O O     . GLU B 2 712  ? 116.114 153.996 166.090 1.00 88.46  ? 709  GLU A O     1 
ATOM   5646  C CB    . GLU B 2 712  ? 113.668 152.760 164.563 1.00 88.46  ? 709  GLU A CB    1 
ATOM   5647  C CG    . GLU B 2 712  ? 112.609 152.652 165.640 1.00 88.46  ? 709  GLU A CG    1 
ATOM   5648  C CD    . GLU B 2 712  ? 111.248 153.097 165.144 1.00 88.46  ? 709  GLU A CD    1 
ATOM   5649  O OE1   . GLU B 2 712  ? 111.134 153.443 163.950 1.00 88.46  ? 709  GLU A OE1   1 
ATOM   5650  O OE2   . GLU B 2 712  ? 110.293 153.103 165.946 1.00 88.46  ? 709  GLU A OE2   1 
ATOM   5651  N N     . TYR B 2 713  ? 115.504 152.228 167.340 1.00 79.70  ? 710  TYR A N     1 
ATOM   5652  C CA    . TYR B 2 713  ? 116.172 152.756 168.525 1.00 79.70  ? 710  TYR A CA    1 
ATOM   5653  C C     . TYR B 2 713  ? 117.683 152.614 168.417 1.00 79.70  ? 710  TYR A C     1 
ATOM   5654  O O     . TYR B 2 713  ? 118.428 153.567 168.671 1.00 79.70  ? 710  TYR A O     1 
ATOM   5655  C CB    . TYR B 2 713  ? 115.656 152.063 169.785 1.00 79.70  ? 710  TYR A CB    1 
ATOM   5656  C CG    . TYR B 2 713  ? 116.147 152.712 171.059 1.00 79.70  ? 710  TYR A CG    1 
ATOM   5657  C CD1   . TYR B 2 713  ? 115.530 153.842 171.573 1.00 79.70  ? 710  TYR A CD1   1 
ATOM   5658  C CD2   . TYR B 2 713  ? 117.225 152.183 171.753 1.00 79.70  ? 710  TYR A CD2   1 
ATOM   5659  C CE1   . TYR B 2 713  ? 115.983 154.438 172.733 1.00 79.70  ? 710  TYR A CE1   1 
ATOM   5660  C CE2   . TYR B 2 713  ? 117.680 152.766 172.917 1.00 79.70  ? 710  TYR A CE2   1 
ATOM   5661  C CZ    . TYR B 2 713  ? 117.055 153.892 173.404 1.00 79.70  ? 710  TYR A CZ    1 
ATOM   5662  O OH    . TYR B 2 713  ? 117.508 154.476 174.564 1.00 79.70  ? 710  TYR A OH    1 
ATOM   5663  N N     . TYR B 2 714  ? 118.157 151.426 168.041 1.00 78.30  ? 711  TYR A N     1 
ATOM   5664  C CA    . TYR B 2 714  ? 119.596 151.210 167.954 1.00 78.30  ? 711  TYR A CA    1 
ATOM   5665  C C     . TYR B 2 714  ? 120.192 151.949 166.762 1.00 78.30  ? 711  TYR A C     1 
ATOM   5666  O O     . TYR B 2 714  ? 121.346 152.388 166.812 1.00 78.30  ? 711  TYR A O     1 
ATOM   5667  C CB    . TYR B 2 714  ? 119.900 149.715 167.885 1.00 78.30  ? 711  TYR A CB    1 
ATOM   5668  C CG    . TYR B 2 714  ? 119.612 148.996 169.182 1.00 78.30  ? 711  TYR A CG    1 
ATOM   5669  C CD1   . TYR B 2 714  ? 119.636 149.676 170.393 1.00 78.30  ? 711  TYR A CD1   1 
ATOM   5670  C CD2   . TYR B 2 714  ? 119.323 147.640 169.200 1.00 78.30  ? 711  TYR A CD2   1 
ATOM   5671  C CE1   . TYR B 2 714  ? 119.373 149.028 171.582 1.00 78.30  ? 711  TYR A CE1   1 
ATOM   5672  C CE2   . TYR B 2 714  ? 119.063 146.982 170.386 1.00 78.30  ? 711  TYR A CE2   1 
ATOM   5673  C CZ    . TYR B 2 714  ? 119.089 147.681 171.574 1.00 78.30  ? 711  TYR A CZ    1 
ATOM   5674  O OH    . TYR B 2 714  ? 118.829 147.031 172.758 1.00 78.30  ? 711  TYR A OH    1 
ATOM   5675  N N     . ALA B 2 715  ? 119.421 152.097 165.682 1.00 76.79  ? 712  ALA A N     1 
ATOM   5676  C CA    . ALA B 2 715  ? 119.871 152.930 164.573 1.00 76.79  ? 712  ALA A CA    1 
ATOM   5677  C C     . ALA B 2 715  ? 119.969 154.392 164.985 1.00 76.79  ? 712  ALA A C     1 
ATOM   5678  O O     . ALA B 2 715  ? 120.666 155.177 164.332 1.00 76.79  ? 712  ALA A O     1 
ATOM   5679  C CB    . ALA B 2 715  ? 118.932 152.775 163.377 1.00 76.79  ? 712  ALA A CB    1 
ATOM   5680  N N     . GLU B 2 716  ? 119.275 154.776 166.057 1.00 74.28  ? 713  GLU A N     1 
ATOM   5681  C CA    . GLU B 2 716  ? 119.365 156.140 166.560 1.00 74.28  ? 713  GLU A CA    1 
ATOM   5682  C C     . GLU B 2 716  ? 120.347 156.254 167.719 1.00 74.28  ? 713  GLU A C     1 
ATOM   5683  O O     . GLU B 2 716  ? 120.887 157.338 167.961 1.00 74.28  ? 713  GLU A O     1 
ATOM   5684  C CB    . GLU B 2 716  ? 117.983 156.631 166.993 1.00 74.28  ? 713  GLU A CB    1 
ATOM   5685  C CG    . GLU B 2 716  ? 117.907 158.123 167.277 1.00 74.28  ? 713  GLU A CG    1 
ATOM   5686  C CD    . GLU B 2 716  ? 116.499 158.584 167.600 1.00 74.28  ? 713  GLU A CD    1 
ATOM   5687  O OE1   . GLU B 2 716  ? 115.554 157.789 167.415 1.00 74.28  ? 713  GLU A OE1   1 
ATOM   5688  O OE2   . GLU B 2 716  ? 116.339 159.741 168.043 1.00 74.28  ? 713  GLU A OE2   1 
ATOM   5689  N N     . LEU B 2 717  ? 120.598 155.157 168.434 1.00 69.78  ? 714  LEU A N     1 
ATOM   5690  C CA    . LEU B 2 717  ? 121.469 155.192 169.602 1.00 69.78  ? 714  LEU A CA    1 
ATOM   5691  C C     . LEU B 2 717  ? 122.937 154.999 169.238 1.00 69.78  ? 714  LEU A C     1 
ATOM   5692  O O     . LEU B 2 717  ? 123.804 155.703 169.765 1.00 69.78  ? 714  LEU A O     1 
ATOM   5693  C CB    . LEU B 2 717  ? 121.038 154.127 170.614 1.00 69.78  ? 714  LEU A CB    1 
ATOM   5694  C CG    . LEU B 2 717  ? 121.741 154.238 171.966 1.00 69.78  ? 714  LEU A CG    1 
ATOM   5695  C CD1   . LEU B 2 717  ? 121.642 155.663 172.485 1.00 69.78  ? 714  LEU A CD1   1 
ATOM   5696  C CD2   . LEU B 2 717  ? 121.158 153.259 172.967 1.00 69.78  ? 714  LEU A CD2   1 
ATOM   5697  N N     . ASN B 2 718  ? 123.229 154.049 168.353 1.00 61.56  ? 715  ASN A N     1 
ATOM   5698  C CA    . ASN B 2 718  ? 124.613 153.778 167.973 1.00 61.56  ? 715  ASN A CA    1 
ATOM   5699  C C     . ASN B 2 718  ? 125.353 154.987 167.408 1.00 61.56  ? 715  ASN A C     1 
ATOM   5700  O O     . ASN B 2 718  ? 126.515 155.193 167.796 1.00 61.56  ? 715  ASN A O     1 
ATOM   5701  C CB    . ASN B 2 718  ? 124.654 152.610 166.977 1.00 61.56  ? 715  ASN A CB    1 
ATOM   5702  C CG    . ASN B 2 718  ? 124.133 151.322 167.572 1.00 61.56  ? 715  ASN A CG    1 
ATOM   5703  O OD1   . ASN B 2 718  ? 124.027 151.188 168.791 1.00 61.56  ? 715  ASN A OD1   1 
ATOM   5704  N ND2   . ASN B 2 718  ? 123.803 150.363 166.715 1.00 61.56  ? 715  ASN A ND2   1 
ATOM   5705  N N     . PRO B 2 719  ? 124.785 155.799 166.507 1.00 55.85  ? 716  PRO A N     1 
ATOM   5706  C CA    . PRO B 2 719  ? 125.534 156.974 166.029 1.00 55.85  ? 716  PRO A CA    1 
ATOM   5707  C C     . PRO B 2 719  ? 125.901 157.954 167.129 1.00 55.85  ? 716  PRO A C     1 
ATOM   5708  O O     . PRO B 2 719  ? 126.954 158.597 167.044 1.00 55.85  ? 716  PRO A O     1 
ATOM   5709  C CB    . PRO B 2 719  ? 124.580 157.607 165.007 1.00 55.85  ? 716  PRO A CB    1 
ATOM   5710  C CG    . PRO B 2 719  ? 123.702 156.497 164.570 1.00 55.85  ? 716  PRO A CG    1 
ATOM   5711  C CD    . PRO B 2 719  ? 123.511 155.642 165.781 1.00 55.85  ? 716  PRO A CD    1 
ATOM   5712  N N     . LEU B 2 720  ? 125.064 158.095 168.158 1.00 54.61  ? 717  LEU A N     1 
ATOM   5713  C CA    . LEU B 2 720  ? 125.348 159.068 169.207 1.00 54.61  ? 717  LEU A CA    1 
ATOM   5714  C C     . LEU B 2 720  ? 126.501 158.627 170.099 1.00 54.61  ? 717  LEU A C     1 
ATOM   5715  O O     . LEU B 2 720  ? 127.181 159.474 170.689 1.00 54.61  ? 717  LEU A O     1 
ATOM   5716  C CB    . LEU B 2 720  ? 124.098 159.314 170.049 1.00 54.61  ? 717  LEU A CB    1 
ATOM   5717  C CG    . LEU B 2 720  ? 122.802 159.557 169.278 1.00 54.61  ? 717  LEU A CG    1 
ATOM   5718  C CD1   . LEU B 2 720  ? 121.622 159.607 170.228 1.00 54.61  ? 717  LEU A CD1   1 
ATOM   5719  C CD2   . LEU B 2 720  ? 122.892 160.837 168.463 1.00 54.61  ? 717  LEU A CD2   1 
ATOM   5720  N N     . LEU B 2 721  ? 126.736 157.318 170.211 1.00 48.55  ? 718  LEU A N     1 
ATOM   5721  C CA    . LEU B 2 721  ? 127.748 156.827 171.142 1.00 48.55  ? 718  LEU A CA    1 
ATOM   5722  C C     . LEU B 2 721  ? 129.152 157.236 170.711 1.00 48.55  ? 718  LEU A C     1 
ATOM   5723  O O     . LEU B 2 721  ? 129.992 157.572 171.555 1.00 48.55  ? 718  LEU A O     1 
ATOM   5724  C CB    . LEU B 2 721  ? 127.642 155.309 171.272 1.00 48.55  ? 718  LEU A CB    1 
ATOM   5725  C CG    . LEU B 2 721  ? 126.271 154.790 171.707 1.00 48.55  ? 718  LEU A CG    1 
ATOM   5726  C CD1   . LEU B 2 721  ? 126.157 153.295 171.462 1.00 48.55  ? 718  LEU A CD1   1 
ATOM   5727  C CD2   . LEU B 2 721  ? 126.007 155.121 173.165 1.00 48.55  ? 718  LEU A CD2   1 
ATOM   5728  N N     . TYR B 2 722  ? 129.426 157.215 169.410 1.00 48.55  ? 719  TYR A N     1 
ATOM   5729  C CA    . TYR B 2 722  ? 130.743 157.588 168.913 1.00 48.55  ? 719  TYR A CA    1 
ATOM   5730  C C     . TYR B 2 722  ? 130.942 159.096 169.016 1.00 48.55  ? 719  TYR A C     1 
ATOM   5731  O O     . TYR B 2 722  ? 130.075 159.877 168.611 1.00 48.55  ? 719  TYR A O     1 
ATOM   5732  C CB    . TYR B 2 722  ? 130.902 157.118 167.468 1.00 48.55  ? 719  TYR A CB    1 
ATOM   5733  C CG    . TYR B 2 722  ? 132.123 157.647 166.756 1.00 48.55  ? 719  TYR A CG    1 
ATOM   5734  C CD1   . TYR B 2 722  ? 133.352 157.023 166.890 1.00 48.55  ? 719  TYR A CD1   1 
ATOM   5735  C CD2   . TYR B 2 722  ? 132.039 158.755 165.924 1.00 48.55  ? 719  TYR A CD2   1 
ATOM   5736  C CE1   . TYR B 2 722  ? 134.465 157.498 166.235 1.00 48.55  ? 719  TYR A CE1   1 
ATOM   5737  C CE2   . TYR B 2 722  ? 133.149 159.236 165.264 1.00 48.55  ? 719  TYR A CE2   1 
ATOM   5738  C CZ    . TYR B 2 722  ? 134.359 158.603 165.422 1.00 48.55  ? 719  TYR A CZ    1 
ATOM   5739  O OH    . TYR B 2 722  ? 135.468 159.078 164.764 1.00 48.55  ? 719  TYR A OH    1 
ATOM   5740  N N     . HIS B 2 723  ? 132.087 159.506 169.558 1.00 48.55  ? 720  HIS A N     1 
ATOM   5741  C CA    . HIS B 2 723  ? 132.374 160.920 169.753 1.00 48.55  ? 720  HIS A CA    1 
ATOM   5742  C C     . HIS B 2 723  ? 133.879 161.121 169.849 1.00 48.55  ? 720  HIS A C     1 
ATOM   5743  O O     . HIS B 2 723  ? 134.609 160.235 170.301 1.00 48.55  ? 720  HIS A O     1 
ATOM   5744  C CB    . HIS B 2 723  ? 131.682 161.459 171.009 1.00 48.55  ? 720  HIS A CB    1 
ATOM   5745  C CG    . HIS B 2 723  ? 131.811 162.939 171.183 1.00 48.55  ? 720  HIS A CG    1 
ATOM   5746  N ND1   . HIS B 2 723  ? 132.885 163.523 171.819 1.00 48.55  ? 720  HIS A ND1   1 
ATOM   5747  C CD2   . HIS B 2 723  ? 131.002 163.956 170.802 1.00 48.55  ? 720  HIS A CD2   1 
ATOM   5748  C CE1   . HIS B 2 723  ? 132.732 164.835 171.824 1.00 48.55  ? 720  HIS A CE1   1 
ATOM   5749  N NE2   . HIS B 2 723  ? 131.597 165.124 171.213 1.00 48.55  ? 720  HIS A NE2   1 
ATOM   5750  N N     . ILE B 2 724  ? 134.331 162.297 169.418 1.00 48.55  ? 721  ILE A N     1 
ATOM   5751  C CA    . ILE B 2 724  ? 135.732 162.692 169.495 1.00 48.55  ? 721  ILE A CA    1 
ATOM   5752  C C     . ILE B 2 724  ? 135.800 164.115 170.029 1.00 48.55  ? 721  ILE A C     1 
ATOM   5753  O O     . ILE B 2 724  ? 135.091 165.001 169.538 1.00 48.55  ? 721  ILE A O     1 
ATOM   5754  C CB    . ILE B 2 724  ? 136.435 162.594 168.128 1.00 48.55  ? 721  ILE A CB    1 
ATOM   5755  C CG1   . ILE B 2 724  ? 136.797 161.143 167.815 1.00 48.55  ? 721  ILE A CG1   1 
ATOM   5756  C CG2   . ILE B 2 724  ? 137.681 163.464 168.095 1.00 48.55  ? 721  ILE A CG2   1 
ATOM   5757  C CD1   . ILE B 2 724  ? 137.422 160.958 166.454 1.00 48.55  ? 721  ILE A CD1   1 
ATOM   5758  N N     . SER B 2 725  ? 136.648 164.334 171.031 1.00 48.55  ? 722  SER A N     1 
ATOM   5759  C CA    . SER B 2 725  ? 136.836 165.647 171.624 1.00 48.55  ? 722  SER A CA    1 
ATOM   5760  C C     . SER B 2 725  ? 138.323 165.955 171.714 1.00 48.55  ? 722  SER A C     1 
ATOM   5761  O O     . SER B 2 725  ? 139.161 165.056 171.816 1.00 48.55  ? 722  SER A O     1 
ATOM   5762  C CB    . SER B 2 725  ? 136.196 165.736 173.016 1.00 48.55  ? 722  SER A CB    1 
ATOM   5763  O OG    . SER B 2 725  ? 136.286 167.051 173.535 1.00 48.55  ? 722  SER A OG    1 
ATOM   5764  N N     . PHE B 2 726  ? 138.643 167.246 171.673 1.00 48.55  ? 723  PHE A N     1 
ATOM   5765  C CA    . PHE B 2 726  ? 140.020 167.715 171.747 1.00 48.55  ? 723  PHE A CA    1 
ATOM   5766  C C     . PHE B 2 726  ? 140.177 168.611 172.964 1.00 48.55  ? 723  PHE A C     1 
ATOM   5767  O O     . PHE B 2 726  ? 139.403 169.555 173.148 1.00 48.55  ? 723  PHE A O     1 
ATOM   5768  C CB    . PHE B 2 726  ? 140.417 168.472 170.476 1.00 48.55  ? 723  PHE A CB    1 
ATOM   5769  C CG    . PHE B 2 726  ? 140.831 167.579 169.344 1.00 48.55  ? 723  PHE A CG    1 
ATOM   5770  C CD1   . PHE B 2 726  ? 142.099 167.027 169.311 1.00 48.55  ? 723  PHE A CD1   1 
ATOM   5771  C CD2   . PHE B 2 726  ? 139.954 167.290 168.314 1.00 48.55  ? 723  PHE A CD2   1 
ATOM   5772  C CE1   . PHE B 2 726  ? 142.486 166.206 168.271 1.00 48.55  ? 723  PHE A CE1   1 
ATOM   5773  C CE2   . PHE B 2 726  ? 140.336 166.468 167.272 1.00 48.55  ? 723  PHE A CE2   1 
ATOM   5774  C CZ    . PHE B 2 726  ? 141.603 165.926 167.251 1.00 48.55  ? 723  PHE A CZ    1 
ATOM   5775  N N     . GLN B 2 727  ? 141.176 168.313 173.790 1.00 48.55  ? 724  GLN A N     1 
ATOM   5776  C CA    . GLN B 2 727  ? 141.469 169.087 174.987 1.00 48.55  ? 724  GLN A CA    1 
ATOM   5777  C C     . GLN B 2 727  ? 142.938 169.479 174.977 1.00 48.55  ? 724  GLN A C     1 
ATOM   5778  O O     . GLN B 2 727  ? 143.809 168.634 174.747 1.00 48.55  ? 724  GLN A O     1 
ATOM   5779  C CB    . GLN B 2 727  ? 141.127 168.291 176.248 1.00 48.55  ? 724  GLN A CB    1 
ATOM   5780  C CG    . GLN B 2 727  ? 139.649 168.326 176.603 1.00 48.55  ? 724  GLN A CG    1 
ATOM   5781  C CD    . GLN B 2 727  ? 139.401 168.328 178.096 1.00 48.55  ? 724  GLN A CD    1 
ATOM   5782  O OE1   . GLN B 2 727  ? 140.337 168.356 178.893 1.00 48.55  ? 724  GLN A OE1   1 
ATOM   5783  N NE2   . GLN B 2 727  ? 138.131 168.299 178.485 1.00 48.55  ? 724  GLN A NE2   1 
ATOM   5784  N N     . ARG B 2 728  ? 143.207 170.759 175.221 1.00 48.55  ? 725  ARG A N     1 
ATOM   5785  C CA    . ARG B 2 728  ? 144.568 171.272 175.156 1.00 48.55  ? 725  ARG A CA    1 
ATOM   5786  C C     . ARG B 2 728  ? 145.439 170.661 176.246 1.00 48.55  ? 725  ARG A C     1 
ATOM   5787  O O     . ARG B 2 728  ? 145.017 170.514 177.396 1.00 48.55  ? 725  ARG A O     1 
ATOM   5788  C CB    . ARG B 2 728  ? 144.562 172.795 175.279 1.00 48.55  ? 725  ARG A CB    1 
ATOM   5789  C CG    . ARG B 2 728  ? 145.939 173.426 175.419 1.00 48.55  ? 725  ARG A CG    1 
ATOM   5790  C CD    . ARG B 2 728  ? 146.763 173.263 174.156 1.00 48.55  ? 725  ARG A CD    1 
ATOM   5791  N NE    . ARG B 2 728  ? 146.032 173.671 172.963 1.00 48.55  ? 725  ARG A NE    1 
ATOM   5792  C CZ    . ARG B 2 728  ? 146.140 174.860 172.389 1.00 48.55  ? 725  ARG A CZ    1 
ATOM   5793  N NH1   . ARG B 2 728  ? 146.944 175.791 172.875 1.00 48.55  ? 725  ARG A NH1   1 
ATOM   5794  N NH2   . ARG B 2 728  ? 145.428 175.120 171.297 1.00 48.55  ? 725  ARG A NH2   1 
ATOM   5795  N N     . ILE B 2 729  ? 146.665 170.303 175.873 1.00 48.55  ? 726  ILE A N     1 
ATOM   5796  C CA    . ILE B 2 729  ? 147.673 169.800 176.797 1.00 48.55  ? 726  ILE A CA    1 
ATOM   5797  C C     . ILE B 2 729  ? 148.910 170.676 176.662 1.00 48.55  ? 726  ILE A C     1 
ATOM   5798  O O     . ILE B 2 729  ? 149.311 171.021 175.545 1.00 48.55  ? 726  ILE A O     1 
ATOM   5799  C CB    . ILE B 2 729  ? 148.006 168.322 176.529 1.00 48.55  ? 726  ILE A CB    1 
ATOM   5800  C CG1   . ILE B 2 729  ? 146.835 167.434 176.944 1.00 48.55  ? 726  ILE A CG1   1 
ATOM   5801  C CG2   . ILE B 2 729  ? 149.256 167.908 177.277 1.00 48.55  ? 726  ILE A CG2   1 
ATOM   5802  C CD1   . ILE B 2 729  ? 147.117 165.961 176.804 1.00 48.55  ? 726  ILE A CD1   1 
ATOM   5803  N N     . ALA B 2 730  ? 149.502 171.042 177.799 1.00 48.55  ? 727  ALA A N     1 
ATOM   5804  C CA    . ALA B 2 730  ? 150.614 171.983 177.806 1.00 48.55  ? 727  ALA A CA    1 
ATOM   5805  C C     . ALA B 2 730  ? 151.786 171.460 176.986 1.00 48.55  ? 727  ALA A C     1 
ATOM   5806  O O     . ALA B 2 730  ? 152.072 170.260 176.971 1.00 48.55  ? 727  ALA A O     1 
ATOM   5807  C CB    . ALA B 2 730  ? 151.060 172.259 179.242 1.00 48.55  ? 727  ALA A CB    1 
ATOM   5808  N N     . GLU B 2 731  ? 152.462 172.380 176.291 1.00 48.55  ? 728  GLU A N     1 
ATOM   5809  C CA    . GLU B 2 731  ? 153.604 172.003 175.464 1.00 48.55  ? 728  GLU A CA    1 
ATOM   5810  C C     . GLU B 2 731  ? 154.743 171.438 176.300 1.00 48.55  ? 728  GLU A C     1 
ATOM   5811  O O     . GLU B 2 731  ? 155.408 170.486 175.876 1.00 48.55  ? 728  GLU A O     1 
ATOM   5812  C CB    . GLU B 2 731  ? 154.083 173.212 174.656 1.00 48.55  ? 728  GLU A CB    1 
ATOM   5813  C CG    . GLU B 2 731  ? 155.093 172.890 173.561 1.00 48.55  ? 728  GLU A CG    1 
ATOM   5814  C CD    . GLU B 2 731  ? 156.521 172.841 174.068 1.00 48.55  ? 728  GLU A CD    1 
ATOM   5815  O OE1   . GLU B 2 731  ? 156.829 173.548 175.051 1.00 48.55  ? 728  GLU A OE1   1 
ATOM   5816  O OE2   . GLU B 2 731  ? 157.336 172.096 173.484 1.00 48.55  ? 728  GLU A OE2   1 
ATOM   5817  N N     . LYS B 2 732  ? 154.987 172.012 177.479 1.00 48.55  ? 729  LYS A N     1 
ATOM   5818  C CA    . LYS B 2 732  ? 156.089 171.547 178.315 1.00 48.55  ? 729  LYS A CA    1 
ATOM   5819  C C     . LYS B 2 732  ? 155.884 170.103 178.751 1.00 48.55  ? 729  LYS A C     1 
ATOM   5820  O O     . LYS B 2 732  ? 156.837 169.317 178.786 1.00 48.55  ? 729  LYS A O     1 
ATOM   5821  C CB    . LYS B 2 732  ? 156.243 172.457 179.533 1.00 43.16  ? 729  LYS A CB    1 
ATOM   5822  C CG    . LYS B 2 732  ? 157.455 172.143 180.392 1.00 43.16  ? 729  LYS A CG    1 
ATOM   5823  C CD    . LYS B 2 732  ? 157.550 173.087 181.580 1.00 43.16  ? 729  LYS A CD    1 
ATOM   5824  C CE    . LYS B 2 732  ? 157.938 174.489 181.141 1.00 43.16  ? 729  LYS A CE    1 
ATOM   5825  N NZ    . LYS B 2 732  ? 159.327 174.537 180.606 1.00 43.16  ? 729  LYS A NZ    1 
ATOM   5826  N N     . GLU B 2 733  ? 154.646 169.735 179.089 1.00 48.55  ? 730  GLU A N     1 
ATOM   5827  C CA    . GLU B 2 733  ? 154.377 168.379 179.556 1.00 48.55  ? 730  GLU A CA    1 
ATOM   5828  C C     . GLU B 2 733  ? 154.675 167.351 178.471 1.00 48.55  ? 730  GLU A C     1 
ATOM   5829  O O     . GLU B 2 733  ? 155.278 166.306 178.739 1.00 48.55  ? 730  GLU A O     1 
ATOM   5830  C CB    . GLU B 2 733  ? 152.928 168.265 180.026 1.00 48.55  ? 730  GLU A CB    1 
ATOM   5831  C CG    . GLU B 2 733  ? 152.617 166.969 180.757 1.00 48.55  ? 730  GLU A CG    1 
ATOM   5832  C CD    . GLU B 2 733  ? 151.137 166.792 181.029 1.00 48.55  ? 730  GLU A CD    1 
ATOM   5833  O OE1   . GLU B 2 733  ? 150.320 167.349 180.267 1.00 48.55  ? 730  GLU A OE1   1 
ATOM   5834  O OE2   . GLU B 2 733  ? 150.790 166.095 182.004 1.00 48.55  ? 730  GLU A OE2   1 
ATOM   5835  N N     . ILE B 2 734  ? 154.258 167.630 177.235 1.00 48.55  ? 731  ILE A N     1 
ATOM   5836  C CA    . ILE B 2 734  ? 154.514 166.701 176.138 1.00 48.55  ? 731  ILE A CA    1 
ATOM   5837  C C     . ILE B 2 734  ? 156.003 166.647 175.819 1.00 48.55  ? 731  ILE A C     1 
ATOM   5838  O O     . ILE B 2 734  ? 156.581 165.566 175.658 1.00 48.55  ? 731  ILE A O     1 
ATOM   5839  C CB    . ILE B 2 734  ? 153.689 167.089 174.899 1.00 48.55  ? 731  ILE A CB    1 
ATOM   5840  C CG1   . ILE B 2 734  ? 152.198 167.103 175.231 1.00 48.55  ? 731  ILE A CG1   1 
ATOM   5841  C CG2   . ILE B 2 734  ? 153.962 166.126 173.757 1.00 48.55  ? 731  ILE A CG2   1 
ATOM   5842  C CD1   . ILE B 2 734  ? 151.644 165.741 175.568 1.00 48.55  ? 731  ILE A CD1   1 
ATOM   5843  N N     . MET B 2 735  ? 156.644 167.813 175.719 1.00 48.55  ? 732  MET A N     1 
ATOM   5844  C CA    . MET B 2 735  ? 158.056 167.852 175.351 1.00 48.55  ? 732  MET A CA    1 
ATOM   5845  C C     . MET B 2 735  ? 158.926 167.194 176.414 1.00 48.55  ? 732  MET A C     1 
ATOM   5846  O O     . MET B 2 735  ? 159.867 166.461 176.090 1.00 48.55  ? 732  MET A O     1 
ATOM   5847  C CB    . MET B 2 735  ? 158.497 169.296 175.113 1.00 48.55  ? 732  MET A CB    1 
ATOM   5848  C CG    . MET B 2 735  ? 159.901 169.432 174.546 1.00 48.55  ? 732  MET A CG    1 
ATOM   5849  S SD    . MET B 2 735  ? 160.249 168.215 173.262 1.00 48.55  ? 732  MET A SD    1 
ATOM   5850  C CE    . MET B 2 735  ? 161.948 168.617 172.865 1.00 48.55  ? 732  MET A CE    1 
ATOM   5851  N N     . ASP B 2 736  ? 158.631 167.446 177.691 1.00 48.55  ? 733  ASP A N     1 
ATOM   5852  C CA    . ASP B 2 736  ? 159.399 166.817 178.761 1.00 48.55  ? 733  ASP A CA    1 
ATOM   5853  C C     . ASP B 2 736  ? 159.121 165.321 178.833 1.00 48.55  ? 733  ASP A C     1 
ATOM   5854  O O     . ASP B 2 736  ? 159.996 164.541 179.227 1.00 48.55  ? 733  ASP A O     1 
ATOM   5855  C CB    . ASP B 2 736  ? 159.089 167.488 180.098 1.00 48.55  ? 733  ASP A CB    1 
ATOM   5856  C CG    . ASP B 2 736  ? 160.011 167.028 181.208 1.00 48.55  ? 733  ASP A CG    1 
ATOM   5857  O OD1   . ASP B 2 736  ? 161.164 167.504 181.259 1.00 48.55  ? 733  ASP A OD1   1 
ATOM   5858  O OD2   . ASP B 2 736  ? 159.583 166.190 182.030 1.00 48.55  ? 733  ASP A OD2   1 
ATOM   5859  N N     . ALA B 2 737  ? 157.907 164.903 178.465 1.00 48.55  ? 734  ALA A N     1 
ATOM   5860  C CA    . ALA B 2 737  ? 157.590 163.479 178.444 1.00 48.55  ? 734  ALA A CA    1 
ATOM   5861  C C     . ALA B 2 737  ? 158.446 162.740 177.425 1.00 48.55  ? 734  ALA A C     1 
ATOM   5862  O O     . ALA B 2 737  ? 158.884 161.611 177.671 1.00 48.55  ? 734  ALA A O     1 
ATOM   5863  C CB    . ALA B 2 737  ? 156.105 163.273 178.149 1.00 48.55  ? 734  ALA A CB    1 
ATOM   5864  N N     . VAL B 2 738  ? 158.684 163.358 176.267 1.00 48.55  ? 735  VAL A N     1 
ATOM   5865  C CA    . VAL B 2 738  ? 159.561 162.752 175.270 1.00 48.55  ? 735  VAL A CA    1 
ATOM   5866  C C     . VAL B 2 738  ? 160.993 162.700 175.785 1.00 48.55  ? 735  VAL A C     1 
ATOM   5867  O O     . VAL B 2 738  ? 161.716 161.721 175.559 1.00 48.55  ? 735  VAL A O     1 
ATOM   5868  C CB    . VAL B 2 738  ? 159.461 163.519 173.938 1.00 48.55  ? 735  VAL A CB    1 
ATOM   5869  C CG1   . VAL B 2 738  ? 160.421 162.937 172.912 1.00 48.55  ? 735  VAL A CG1   1 
ATOM   5870  C CG2   . VAL B 2 738  ? 158.034 163.490 173.418 1.00 48.55  ? 735  VAL A CG2   1 
ATOM   5871  N N     . GLU B 2 739  ? 161.425 163.750 176.489 1.00 48.55  ? 736  GLU A N     1 
ATOM   5872  C CA    . GLU B 2 739  ? 162.786 163.783 177.017 1.00 48.55  ? 736  GLU A CA    1 
ATOM   5873  C C     . GLU B 2 739  ? 163.019 162.668 178.028 1.00 48.55  ? 736  GLU A C     1 
ATOM   5874  O O     . GLU B 2 739  ? 164.073 162.021 178.016 1.00 48.55  ? 736  GLU A O     1 
ATOM   5875  C CB    . GLU B 2 739  ? 163.070 165.145 177.650 1.00 48.55  ? 736  GLU A CB    1 
ATOM   5876  C CG    . GLU B 2 739  ? 163.089 166.301 176.664 1.00 48.55  ? 736  GLU A CG    1 
ATOM   5877  C CD    . GLU B 2 739  ? 164.244 166.213 175.687 1.00 48.55  ? 736  GLU A CD    1 
ATOM   5878  O OE1   . GLU B 2 739  ? 165.311 165.691 176.073 1.00 48.55  ? 736  GLU A OE1   1 
ATOM   5879  O OE2   . GLU B 2 739  ? 164.086 166.666 174.534 1.00 48.55  ? 736  GLU A OE2   1 
ATOM   5880  N N     . THR B 2 740  ? 162.049 162.426 178.913 1.00 48.55  ? 737  THR A N     1 
ATOM   5881  C CA    . THR B 2 740  ? 162.223 161.380 179.915 1.00 48.55  ? 737  THR A CA    1 
ATOM   5882  C C     . THR B 2 740  ? 161.949 159.995 179.341 1.00 48.55  ? 737  THR A C     1 
ATOM   5883  O O     . THR B 2 740  ? 162.221 158.988 180.005 1.00 48.55  ? 737  THR A O     1 
ATOM   5884  C CB    . THR B 2 740  ? 161.326 161.648 181.123 1.00 48.55  ? 737  THR A CB    1 
ATOM   5885  O OG1   . THR B 2 740  ? 161.573 160.661 182.132 1.00 48.55  ? 737  THR A OG1   1 
ATOM   5886  C CG2   . THR B 2 740  ? 159.863 161.606 180.725 1.00 48.55  ? 737  THR A CG2   1 
ATOM   5887  N N     . GLY B 2 741  ? 161.416 159.920 178.126 1.00 48.55  ? 738  GLY A N     1 
ATOM   5888  C CA    . GLY B 2 741  ? 161.243 158.657 177.440 1.00 48.55  ? 738  GLY A CA    1 
ATOM   5889  C C     . GLY B 2 741  ? 159.893 157.994 177.590 1.00 48.55  ? 738  GLY A C     1 
ATOM   5890  O O     . GLY B 2 741  ? 159.748 156.836 177.182 1.00 48.55  ? 738  GLY A O     1 
ATOM   5891  N N     . LYS B 2 742  ? 158.903 158.678 178.159 1.00 48.72  ? 739  LYS A N     1 
ATOM   5892  C CA    . LYS B 2 742  ? 157.594 158.079 178.379 1.00 48.72  ? 739  LYS A CA    1 
ATOM   5893  C C     . LYS B 2 742  ? 156.626 158.290 177.223 1.00 48.72  ? 739  LYS A C     1 
ATOM   5894  O O     . LYS B 2 742  ? 155.548 157.688 177.226 1.00 48.72  ? 739  LYS A O     1 
ATOM   5895  C CB    . LYS B 2 742  ? 156.970 158.628 179.667 1.00 48.72  ? 739  LYS A CB    1 
ATOM   5896  C CG    . LYS B 2 742  ? 157.906 158.619 180.863 1.00 48.72  ? 739  LYS A CG    1 
ATOM   5897  C CD    . LYS B 2 742  ? 157.220 159.154 182.110 1.00 48.72  ? 739  LYS A CD    1 
ATOM   5898  C CE    . LYS B 2 742  ? 156.007 158.318 182.480 1.00 48.72  ? 739  LYS A CE    1 
ATOM   5899  N NZ    . LYS B 2 742  ? 156.302 156.860 182.438 1.00 48.72  ? 739  LYS A NZ    1 
ATOM   5900  N N     . LEU B 2 743  ? 156.971 159.119 176.241 1.00 48.55  ? 740  LEU A N     1 
ATOM   5901  C CA    . LEU B 2 743  ? 156.110 159.339 175.089 1.00 48.55  ? 740  LEU A CA    1 
ATOM   5902  C C     . LEU B 2 743  ? 156.953 159.368 173.825 1.00 48.55  ? 740  LEU A C     1 
ATOM   5903  O O     . LEU B 2 743  ? 158.015 159.996 173.792 1.00 48.55  ? 740  LEU A O     1 
ATOM   5904  C CB    . LEU B 2 743  ? 155.314 160.643 175.216 1.00 48.55  ? 740  LEU A CB    1 
ATOM   5905  C CG    . LEU B 2 743  ? 154.339 160.937 174.074 1.00 48.55  ? 740  LEU A CG    1 
ATOM   5906  C CD1   . LEU B 2 743  ? 153.151 159.993 174.127 1.00 48.55  ? 740  LEU A CD1   1 
ATOM   5907  C CD2   . LEU B 2 743  ? 153.877 162.383 174.119 1.00 48.55  ? 740  LEU A CD2   1 
ATOM   5908  N N     . TYR B 2 744  ? 156.475 158.686 172.790 1.00 48.55  ? 741  TYR A N     1 
ATOM   5909  C CA    . TYR B 2 744  ? 157.147 158.626 171.495 1.00 48.55  ? 741  TYR A CA    1 
ATOM   5910  C C     . TYR B 2 744  ? 156.329 159.445 170.501 1.00 48.55  ? 741  TYR A C     1 
ATOM   5911  O O     . TYR B 2 744  ? 155.383 158.945 169.891 1.00 48.55  ? 741  TYR A O     1 
ATOM   5912  C CB    . TYR B 2 744  ? 157.313 157.184 171.026 1.00 48.55  ? 741  TYR A CB    1 
ATOM   5913  C CG    . TYR B 2 744  ? 158.329 156.394 171.816 1.00 48.55  ? 741  TYR A CG    1 
ATOM   5914  C CD1   . TYR B 2 744  ? 159.252 157.033 172.630 1.00 48.55  ? 741  TYR A CD1   1 
ATOM   5915  C CD2   . TYR B 2 744  ? 158.371 155.011 171.739 1.00 48.55  ? 741  TYR A CD2   1 
ATOM   5916  C CE1   . TYR B 2 744  ? 160.184 156.316 173.351 1.00 48.55  ? 741  TYR A CE1   1 
ATOM   5917  C CE2   . TYR B 2 744  ? 159.299 154.286 172.456 1.00 48.55  ? 741  TYR A CE2   1 
ATOM   5918  C CZ    . TYR B 2 744  ? 160.202 154.943 173.260 1.00 48.55  ? 741  TYR A CZ    1 
ATOM   5919  O OH    . TYR B 2 744  ? 161.129 154.224 173.976 1.00 48.55  ? 741  TYR A OH    1 
ATOM   5920  N N     . LEU B 2 745  ? 156.699 160.712 170.344 1.00 48.55  ? 742  LEU A N     1 
ATOM   5921  C CA    . LEU B 2 745  ? 156.020 161.571 169.388 1.00 48.55  ? 742  LEU A CA    1 
ATOM   5922  C C     . LEU B 2 745  ? 156.369 161.164 167.962 1.00 48.55  ? 742  LEU A C     1 
ATOM   5923  O O     . LEU B 2 745  ? 157.472 160.693 167.676 1.00 48.55  ? 742  LEU A O     1 
ATOM   5924  C CB    . LEU B 2 745  ? 156.391 163.034 169.620 1.00 48.55  ? 742  LEU A CB    1 
ATOM   5925  C CG    . LEU B 2 745  ? 155.382 163.856 170.420 1.00 48.55  ? 742  LEU A CG    1 
ATOM   5926  C CD1   . LEU B 2 745  ? 155.937 165.239 170.722 1.00 48.55  ? 742  LEU A CD1   1 
ATOM   5927  C CD2   . LEU B 2 745  ? 154.065 163.953 169.674 1.00 48.55  ? 742  LEU A CD2   1 
ATOM   5928  N N     . PHE B 2 746  ? 155.409 161.356 167.060 1.00 48.55  ? 743  PHE A N     1 
ATOM   5929  C CA    . PHE B 2 746  ? 155.582 160.975 165.661 1.00 48.55  ? 743  PHE A CA    1 
ATOM   5930  C C     . PHE B 2 746  ? 154.718 161.895 164.814 1.00 48.55  ? 743  PHE A C     1 
ATOM   5931  O O     . PHE B 2 746  ? 153.487 161.810 164.868 1.00 48.55  ? 743  PHE A O     1 
ATOM   5932  C CB    . PHE B 2 746  ? 155.203 159.513 165.440 1.00 48.55  ? 743  PHE A CB    1 
ATOM   5933  C CG    . PHE B 2 746  ? 156.273 158.541 165.839 1.00 48.55  ? 743  PHE A CG    1 
ATOM   5934  C CD1   . PHE B 2 746  ? 157.483 158.511 165.171 1.00 48.55  ? 743  PHE A CD1   1 
ATOM   5935  C CD2   . PHE B 2 746  ? 156.067 157.653 166.879 1.00 48.55  ? 743  PHE A CD2   1 
ATOM   5936  C CE1   . PHE B 2 746  ? 158.467 157.617 165.534 1.00 48.55  ? 743  PHE A CE1   1 
ATOM   5937  C CE2   . PHE B 2 746  ? 157.048 156.758 167.245 1.00 48.55  ? 743  PHE A CE2   1 
ATOM   5938  C CZ    . PHE B 2 746  ? 158.248 156.740 166.572 1.00 48.55  ? 743  PHE A CZ    1 
ATOM   5939  N N     . GLN B 2 747  ? 155.353 162.766 164.035 1.00 48.55  ? 744  GLN A N     1 
ATOM   5940  C CA    . GLN B 2 747  ? 154.609 163.688 163.188 1.00 48.55  ? 744  GLN A CA    1 
ATOM   5941  C C     . GLN B 2 747  ? 154.086 162.960 161.957 1.00 48.55  ? 744  GLN A C     1 
ATOM   5942  O O     . GLN B 2 747  ? 154.856 162.343 161.214 1.00 48.55  ? 744  GLN A O     1 
ATOM   5943  C CB    . GLN B 2 747  ? 155.487 164.865 162.775 1.00 48.55  ? 744  GLN A CB    1 
ATOM   5944  C CG    . GLN B 2 747  ? 154.739 165.922 161.980 1.00 48.55  ? 744  GLN A CG    1 
ATOM   5945  C CD    . GLN B 2 747  ? 155.654 166.778 161.131 1.00 48.55  ? 744  GLN A CD    1 
ATOM   5946  O OE1   . GLN B 2 747  ? 156.851 166.881 161.397 1.00 48.55  ? 744  GLN A OE1   1 
ATOM   5947  N NE2   . GLN B 2 747  ? 155.092 167.401 160.102 1.00 48.55  ? 744  GLN A NE2   1 
ATOM   5948  N N     . ILE B 2 748  ? 152.775 163.033 161.745 1.00 48.55  ? 745  ILE A N     1 
ATOM   5949  C CA    . ILE B 2 748  ? 152.148 162.465 160.557 1.00 48.55  ? 745  ILE A CA    1 
ATOM   5950  C C     . ILE B 2 748  ? 152.485 163.363 159.370 1.00 48.55  ? 745  ILE A C     1 
ATOM   5951  O O     . ILE B 2 748  ? 152.143 164.548 159.362 1.00 48.55  ? 745  ILE A O     1 
ATOM   5952  C CB    . ILE B 2 748  ? 150.635 162.322 160.745 1.00 48.55  ? 745  ILE A CB    1 
ATOM   5953  C CG1   . ILE B 2 748  ? 150.339 161.325 161.868 1.00 48.55  ? 745  ILE A CG1   1 
ATOM   5954  C CG2   . ILE B 2 748  ? 149.963 161.932 159.453 1.00 48.55  ? 745  ILE A CG2   1 
ATOM   5955  C CD1   . ILE B 2 748  ? 148.871 161.038 162.060 1.00 48.55  ? 745  ILE A CD1   1 
ATOM   5956  N N     . TYR B 2 749  ? 153.161 162.803 158.367 1.00 48.55  ? 746  TYR A N     1 
ATOM   5957  C CA    . TYR B 2 749  ? 153.695 163.575 157.252 1.00 48.55  ? 746  TYR A CA    1 
ATOM   5958  C C     . TYR B 2 749  ? 153.453 162.821 155.953 1.00 48.55  ? 746  TYR A C     1 
ATOM   5959  O O     . TYR B 2 749  ? 153.887 161.673 155.809 1.00 48.55  ? 746  TYR A O     1 
ATOM   5960  C CB    . TYR B 2 749  ? 155.191 163.844 157.460 1.00 48.55  ? 746  TYR A CB    1 
ATOM   5961  C CG    . TYR B 2 749  ? 155.923 164.418 156.269 1.00 48.55  ? 746  TYR A CG    1 
ATOM   5962  C CD1   . TYR B 2 749  ? 156.010 165.789 156.081 1.00 48.55  ? 746  TYR A CD1   1 
ATOM   5963  C CD2   . TYR B 2 749  ? 156.549 163.591 155.345 1.00 48.55  ? 746  TYR A CD2   1 
ATOM   5964  C CE1   . TYR B 2 749  ? 156.684 166.322 155.001 1.00 48.55  ? 746  TYR A CE1   1 
ATOM   5965  C CE2   . TYR B 2 749  ? 157.225 164.113 154.262 1.00 48.55  ? 746  TYR A CE2   1 
ATOM   5966  C CZ    . TYR B 2 749  ? 157.290 165.479 154.095 1.00 48.55  ? 746  TYR A CZ    1 
ATOM   5967  O OH    . TYR B 2 749  ? 157.964 166.005 153.016 1.00 48.55  ? 746  TYR A OH    1 
ATOM   5968  N N     . ASN B 2 750  ? 152.763 163.464 155.010 1.00 48.55  ? 747  ASN A N     1 
ATOM   5969  C CA    . ASN B 2 750  ? 152.446 162.852 153.722 1.00 48.55  ? 747  ASN A CA    1 
ATOM   5970  C C     . ASN B 2 750  ? 152.632 163.848 152.582 1.00 48.55  ? 747  ASN A C     1 
ATOM   5971  O O     . ASN B 2 750  ? 151.800 163.939 151.673 1.00 48.55  ? 747  ASN A O     1 
ATOM   5972  C CB    . ASN B 2 750  ? 151.027 162.283 153.717 1.00 48.55  ? 747  ASN A CB    1 
ATOM   5973  C CG    . ASN B 2 750  ? 149.966 163.351 153.897 1.00 48.55  ? 747  ASN A CG    1 
ATOM   5974  O OD1   . ASN B 2 750  ? 150.257 164.471 154.316 1.00 48.55  ? 747  ASN A OD1   1 
ATOM   5975  N ND2   . ASN B 2 750  ? 148.725 163.009 153.572 1.00 48.55  ? 747  ASN A ND2   1 
ATOM   5976  N N     . LYS B 2 751  ? 153.719 164.623 152.631 1.00 48.55  ? 748  LYS A N     1 
ATOM   5977  C CA    . LYS B 2 751  ? 154.136 165.533 151.562 1.00 48.55  ? 748  LYS A CA    1 
ATOM   5978  C C     . LYS B 2 751  ? 153.177 166.710 151.403 1.00 48.55  ? 748  LYS A C     1 
ATOM   5979  O O     . LYS B 2 751  ? 153.464 167.657 150.663 1.00 48.55  ? 748  LYS A O     1 
ATOM   5980  C CB    . LYS B 2 751  ? 154.274 164.777 150.232 1.00 31.31  ? 748  LYS A CB    1 
ATOM   5981  C CG    . LYS B 2 751  ? 154.934 165.568 149.108 1.00 31.31  ? 748  LYS A CG    1 
ATOM   5982  C CD    . LYS B 2 751  ? 154.559 165.020 147.740 1.00 31.31  ? 748  LYS A CD    1 
ATOM   5983  C CE    . LYS B 2 751  ? 153.083 165.202 147.450 1.00 31.31  ? 748  LYS A CE    1 
ATOM   5984  N NZ    . LYS B 2 751  ? 152.624 164.288 146.370 1.00 31.31  ? 748  LYS A NZ    1 
ATOM   5985  N N     . ASP B 2 752  ? 152.056 166.685 152.114 1.00 48.55  ? 749  ASP A N     1 
ATOM   5986  C CA    . ASP B 2 752  ? 151.120 167.798 152.113 1.00 48.55  ? 749  ASP A CA    1 
ATOM   5987  C C     . ASP B 2 752  ? 151.294 168.698 153.326 1.00 48.55  ? 749  ASP A C     1 
ATOM   5988  O O     . ASP B 2 752  ? 150.624 169.730 153.420 1.00 48.55  ? 749  ASP A O     1 
ATOM   5989  C CB    . ASP B 2 752  ? 149.682 167.279 152.038 1.00 48.55  ? 749  ASP A CB    1 
ATOM   5990  C CG    . ASP B 2 752  ? 149.321 166.779 150.654 1.00 48.55  ? 749  ASP A CG    1 
ATOM   5991  O OD1   . ASP B 2 752  ? 149.997 167.180 149.684 1.00 48.55  ? 749  ASP A OD1   1 
ATOM   5992  O OD2   . ASP B 2 752  ? 148.368 165.982 150.533 1.00 48.55  ? 749  ASP A OD2   1 
ATOM   5993  N N     . PHE B 2 753  ? 152.176 168.327 154.251 1.00 48.55  ? 750  PHE A N     1 
ATOM   5994  C CA    . PHE B 2 753  ? 152.521 169.152 155.398 1.00 48.55  ? 750  PHE A CA    1 
ATOM   5995  C C     . PHE B 2 753  ? 153.914 169.753 155.273 1.00 48.55  ? 750  PHE A C     1 
ATOM   5996  O O     . PHE B 2 753  ? 154.434 170.300 156.251 1.00 48.55  ? 750  PHE A O     1 
ATOM   5997  C CB    . PHE B 2 753  ? 152.406 168.334 156.684 1.00 48.55  ? 750  PHE A CB    1 
ATOM   5998  C CG    . PHE B 2 753  ? 151.063 167.690 156.871 1.00 48.55  ? 750  PHE A CG    1 
ATOM   5999  C CD1   . PHE B 2 753  ? 149.907 168.447 156.837 1.00 48.55  ? 750  PHE A CD1   1 
ATOM   6000  C CD2   . PHE B 2 753  ? 150.957 166.327 157.077 1.00 48.55  ? 750  PHE A CD2   1 
ATOM   6001  C CE1   . PHE B 2 753  ? 148.671 167.856 157.009 1.00 48.55  ? 750  PHE A CE1   1 
ATOM   6002  C CE2   . PHE B 2 753  ? 149.724 165.732 157.248 1.00 48.55  ? 750  PHE A CE2   1 
ATOM   6003  C CZ    . PHE B 2 753  ? 148.580 166.497 157.214 1.00 48.55  ? 750  PHE A CZ    1 
ATOM   6004  N N     . ALA B 2 754  ? 154.530 169.661 154.097 1.00 48.55  ? 751  ALA A N     1 
ATOM   6005  C CA    . ALA B 2 754  ? 155.866 170.194 153.896 1.00 48.55  ? 751  ALA A CA    1 
ATOM   6006  C C     . ALA B 2 754  ? 155.844 171.720 153.894 1.00 48.55  ? 751  ALA A C     1 
ATOM   6007  O O     . ALA B 2 754  ? 154.802 172.357 153.717 1.00 48.55  ? 751  ALA A O     1 
ATOM   6008  C CB    . ALA B 2 754  ? 156.458 169.674 152.587 1.00 48.55  ? 751  ALA A CB    1 
ATOM   6009  N N     . LYS B 2 755  ? 157.025 172.307 154.099 1.00 48.55  ? 752  LYS A N     1 
ATOM   6010  C CA    . LYS B 2 755  ? 157.122 173.761 154.176 1.00 48.55  ? 752  LYS A CA    1 
ATOM   6011  C C     . LYS B 2 755  ? 156.926 174.416 152.815 1.00 48.55  ? 752  LYS A C     1 
ATOM   6012  O O     . LYS B 2 755  ? 156.429 175.545 152.740 1.00 48.55  ? 752  LYS A O     1 
ATOM   6013  C CB    . LYS B 2 755  ? 158.466 174.165 154.786 1.00 41.88  ? 752  LYS A CB    1 
ATOM   6014  C CG    . LYS B 2 755  ? 159.654 174.055 153.844 1.00 41.88  ? 752  LYS A CG    1 
ATOM   6015  C CD    . LYS B 2 755  ? 160.763 175.016 154.238 1.00 41.88  ? 752  LYS A CD    1 
ATOM   6016  C CE    . LYS B 2 755  ? 161.967 174.873 153.322 1.00 41.88  ? 752  LYS A CE    1 
ATOM   6017  N NZ    . LYS B 2 755  ? 162.791 173.683 153.670 1.00 41.88  ? 752  LYS A NZ    1 
ATOM   6018  N N     . GLY B 2 756  ? 157.304 173.735 151.738 1.00 48.55  ? 753  GLY A N     1 
ATOM   6019  C CA    . GLY B 2 756  ? 157.133 174.246 150.396 1.00 48.55  ? 753  GLY A CA    1 
ATOM   6020  C C     . GLY B 2 756  ? 155.829 173.884 149.731 1.00 48.55  ? 753  GLY A C     1 
ATOM   6021  O O     . GLY B 2 756  ? 155.658 174.146 148.537 1.00 48.55  ? 753  GLY A O     1 
ATOM   6022  N N     . HIS B 2 757  ? 154.899 173.283 150.467 1.00 48.55  ? 754  HIS A N     1 
ATOM   6023  C CA    . HIS B 2 757  ? 153.649 172.818 149.883 1.00 48.55  ? 754  HIS A CA    1 
ATOM   6024  C C     . HIS B 2 757  ? 152.776 174.003 149.491 1.00 48.55  ? 754  HIS A C     1 
ATOM   6025  O O     . HIS B 2 757  ? 152.404 174.819 150.340 1.00 48.55  ? 754  HIS A O     1 
ATOM   6026  C CB    . HIS B 2 757  ? 152.912 171.918 150.871 1.00 48.55  ? 754  HIS A CB    1 
ATOM   6027  C CG    . HIS B 2 757  ? 151.476 171.682 150.520 1.00 48.55  ? 754  HIS A CG    1 
ATOM   6028  N ND1   . HIS B 2 757  ? 150.472 171.673 151.464 1.00 48.55  ? 754  HIS A ND1   1 
ATOM   6029  C CD2   . HIS B 2 757  ? 150.877 171.433 149.331 1.00 48.55  ? 754  HIS A CD2   1 
ATOM   6030  C CE1   . HIS B 2 757  ? 149.315 171.437 150.871 1.00 48.55  ? 754  HIS A CE1   1 
ATOM   6031  N NE2   . HIS B 2 757  ? 149.534 171.288 149.577 1.00 48.55  ? 754  HIS A NE2   1 
ATOM   6032  N N     . HIS B 2 758  ? 152.451 174.093 148.203 1.00 48.55  ? 755  HIS A N     1 
ATOM   6033  C CA    . HIS B 2 758  ? 151.489 175.082 147.724 1.00 48.55  ? 755  HIS A CA    1 
ATOM   6034  C C     . HIS B 2 758  ? 150.740 174.458 146.554 1.00 48.55  ? 755  HIS A C     1 
ATOM   6035  O O     . HIS B 2 758  ? 151.318 174.252 145.483 1.00 48.55  ? 755  HIS A O     1 
ATOM   6036  C CB    . HIS B 2 758  ? 152.183 176.383 147.327 1.00 48.55  ? 755  HIS A CB    1 
ATOM   6037  C CG    . HIS B 2 758  ? 153.184 176.229 146.225 1.00 48.55  ? 755  HIS A CG    1 
ATOM   6038  N ND1   . HIS B 2 758  ? 152.822 176.166 144.897 1.00 48.55  ? 755  HIS A ND1   1 
ATOM   6039  C CD2   . HIS B 2 758  ? 154.533 176.126 146.252 1.00 48.55  ? 755  HIS A CD2   1 
ATOM   6040  C CE1   . HIS B 2 758  ? 153.905 176.030 144.153 1.00 48.55  ? 755  HIS A CE1   1 
ATOM   6041  N NE2   . HIS B 2 758  ? 154.957 176.003 144.952 1.00 48.55  ? 755  HIS A NE2   1 
ATOM   6042  N N     . GLY B 2 759  ? 149.471 174.138 146.768 1.00 48.55  ? 756  GLY A N     1 
ATOM   6043  C CA    . GLY B 2 759  ? 148.665 173.460 145.776 1.00 48.55  ? 756  GLY A CA    1 
ATOM   6044  C C     . GLY B 2 759  ? 147.669 172.515 146.416 1.00 48.55  ? 756  GLY A C     1 
ATOM   6045  O O     . GLY B 2 759  ? 147.705 172.235 147.613 1.00 48.55  ? 756  GLY A O     1 
ATOM   6046  N N     . LYS B 2 760  ? 146.764 172.027 145.577 1.00 48.55  ? 757  LYS A N     1 
ATOM   6047  C CA    . LYS B 2 760  ? 145.710 171.150 146.058 1.00 48.55  ? 757  LYS A CA    1 
ATOM   6048  C C     . LYS B 2 760  ? 146.300 169.827 146.547 1.00 48.55  ? 757  LYS A C     1 
ATOM   6049  O O     . LYS B 2 760  ? 147.191 169.264 145.903 1.00 48.55  ? 757  LYS A O     1 
ATOM   6050  C CB    . LYS B 2 760  ? 144.673 170.919 144.959 1.00 48.55  ? 757  LYS A CB    1 
ATOM   6051  C CG    . LYS B 2 760  ? 145.210 170.275 143.699 1.00 48.55  ? 757  LYS A CG    1 
ATOM   6052  C CD    . LYS B 2 760  ? 144.118 170.163 142.653 1.00 48.55  ? 757  LYS A CD    1 
ATOM   6053  C CE    . LYS B 2 760  ? 143.786 171.520 142.059 1.00 48.55  ? 757  LYS A CE    1 
ATOM   6054  N NZ    . LYS B 2 760  ? 142.810 171.413 140.940 1.00 48.55  ? 757  LYS A NZ    1 
ATOM   6055  N N     . PRO B 2 761  ? 145.840 169.319 147.691 1.00 48.55  ? 758  PRO A N     1 
ATOM   6056  C CA    . PRO B 2 761  ? 146.495 168.159 148.305 1.00 48.55  ? 758  PRO A CA    1 
ATOM   6057  C C     . PRO B 2 761  ? 145.950 166.824 147.828 1.00 48.55  ? 758  PRO A C     1 
ATOM   6058  O O     . PRO B 2 761  ? 145.069 166.767 146.964 1.00 48.55  ? 758  PRO A O     1 
ATOM   6059  C CB    . PRO B 2 761  ? 146.220 168.365 149.797 1.00 48.55  ? 758  PRO A CB    1 
ATOM   6060  C CG    . PRO B 2 761  ? 144.910 169.092 149.832 1.00 48.55  ? 758  PRO A CG    1 
ATOM   6061  C CD    . PRO B 2 761  ? 144.751 169.846 148.531 1.00 48.55  ? 758  PRO A CD    1 
ATOM   6062  N N     . ASN B 2 762  ? 146.479 165.744 148.394 1.00 48.55  ? 759  ASN A N     1 
ATOM   6063  C CA    . ASN B 2 762  ? 146.027 164.405 148.059 1.00 48.55  ? 759  ASN A CA    1 
ATOM   6064  C C     . ASN B 2 762  ? 144.638 164.148 148.635 1.00 48.55  ? 759  ASN A C     1 
ATOM   6065  O O     . ASN B 2 762  ? 144.182 164.825 149.561 1.00 48.55  ? 759  ASN A O     1 
ATOM   6066  C CB    . ASN B 2 762  ? 147.010 163.362 148.587 1.00 48.55  ? 759  ASN A CB    1 
ATOM   6067  C CG    . ASN B 2 762  ? 148.364 163.446 147.917 1.00 48.55  ? 759  ASN A CG    1 
ATOM   6068  O OD1   . ASN B 2 762  ? 148.460 163.650 146.708 1.00 48.55  ? 759  ASN A OD1   1 
ATOM   6069  N ND2   . ASN B 2 762  ? 149.422 163.289 148.702 1.00 48.55  ? 759  ASN A ND2   1 
ATOM   6070  N N     . LEU B 2 763  ? 143.958 163.152 148.064 1.00 48.55  ? 760  LEU A N     1 
ATOM   6071  C CA    . LEU B 2 763  ? 142.630 162.794 148.550 1.00 48.55  ? 760  LEU A CA    1 
ATOM   6072  C C     . LEU B 2 763  ? 142.689 162.249 149.972 1.00 48.55  ? 760  LEU A C     1 
ATOM   6073  O O     . LEU B 2 763  ? 141.812 162.542 150.793 1.00 48.55  ? 760  LEU A O     1 
ATOM   6074  C CB    . LEU B 2 763  ? 141.983 161.777 147.613 1.00 48.55  ? 760  LEU A CB    1 
ATOM   6075  C CG    . LEU B 2 763  ? 141.286 162.355 146.382 1.00 48.55  ? 760  LEU A CG    1 
ATOM   6076  C CD1   . LEU B 2 763  ? 140.410 161.303 145.728 1.00 48.55  ? 760  LEU A CD1   1 
ATOM   6077  C CD2   . LEU B 2 763  ? 140.471 163.583 146.753 1.00 48.55  ? 760  LEU A CD2   1 
ATOM   6078  N N     . HIS B 2 764  ? 143.712 161.449 150.281 1.00 48.55  ? 761  HIS A N     1 
ATOM   6079  C CA    . HIS B 2 764  ? 143.835 160.895 151.625 1.00 48.55  ? 761  HIS A CA    1 
ATOM   6080  C C     . HIS B 2 764  ? 144.112 161.985 152.652 1.00 48.55  ? 761  HIS A C     1 
ATOM   6081  O O     . HIS B 2 764  ? 143.657 161.893 153.799 1.00 48.55  ? 761  HIS A O     1 
ATOM   6082  C CB    . HIS B 2 764  ? 144.925 159.827 151.656 1.00 48.55  ? 761  HIS A CB    1 
ATOM   6083  C CG    . HIS B 2 764  ? 144.540 158.558 150.964 1.00 48.55  ? 761  HIS A CG    1 
ATOM   6084  N ND1   . HIS B 2 764  ? 144.777 158.338 149.625 1.00 48.55  ? 761  HIS A ND1   1 
ATOM   6085  C CD2   . HIS B 2 764  ? 143.927 157.442 151.426 1.00 48.55  ? 761  HIS A CD2   1 
ATOM   6086  C CE1   . HIS B 2 764  ? 144.330 157.141 149.292 1.00 48.55  ? 761  HIS A CE1   1 
ATOM   6087  N NE2   . HIS B 2 764  ? 143.811 156.576 150.367 1.00 48.55  ? 761  HIS A NE2   1 
ATOM   6088  N N     . THR B 2 765  ? 144.863 163.019 152.267 1.00 48.55  ? 762  THR A N     1 
ATOM   6089  C CA    . THR B 2 765  ? 145.058 164.155 153.160 1.00 48.55  ? 762  THR A CA    1 
ATOM   6090  C C     . THR B 2 765  ? 143.733 164.838 153.470 1.00 48.55  ? 762  THR A C     1 
ATOM   6091  O O     . THR B 2 765  ? 143.461 165.193 154.623 1.00 48.55  ? 762  THR A O     1 
ATOM   6092  C CB    . THR B 2 765  ? 146.044 165.147 152.544 1.00 48.55  ? 762  THR A CB    1 
ATOM   6093  O OG1   . THR B 2 765  ? 147.363 164.588 152.567 1.00 48.55  ? 762  THR A OG1   1 
ATOM   6094  C CG2   . THR B 2 765  ? 146.045 166.458 153.316 1.00 48.55  ? 762  THR A CG2   1 
ATOM   6095  N N     . LEU B 2 766  ? 142.887 165.019 152.452 1.00 48.55  ? 763  LEU A N     1 
ATOM   6096  C CA    . LEU B 2 766  ? 141.568 165.596 152.683 1.00 48.55  ? 763  LEU A CA    1 
ATOM   6097  C C     . LEU B 2 766  ? 140.710 164.679 153.543 1.00 48.55  ? 763  LEU A C     1 
ATOM   6098  O O     . LEU B 2 766  ? 139.899 165.150 154.349 1.00 48.55  ? 763  LEU A O     1 
ATOM   6099  C CB    . LEU B 2 766  ? 140.879 165.886 151.351 1.00 48.55  ? 763  LEU A CB    1 
ATOM   6100  C CG    . LEU B 2 766  ? 141.370 167.133 150.616 1.00 48.55  ? 763  LEU A CG    1 
ATOM   6101  C CD1   . LEU B 2 766  ? 140.535 167.374 149.374 1.00 48.55  ? 763  LEU A CD1   1 
ATOM   6102  C CD2   . LEU B 2 766  ? 141.338 168.344 151.533 1.00 48.55  ? 763  LEU A CD2   1 
ATOM   6103  N N     . TYR B 2 767  ? 140.864 163.363 153.378 1.00 48.55  ? 764  TYR A N     1 
ATOM   6104  C CA    . TYR B 2 767  ? 140.209 162.425 154.282 1.00 48.55  ? 764  TYR A CA    1 
ATOM   6105  C C     . TYR B 2 767  ? 140.686 162.631 155.712 1.00 48.55  ? 764  TYR A C     1 
ATOM   6106  O O     . TYR B 2 767  ? 139.885 162.646 156.654 1.00 48.55  ? 764  TYR A O     1 
ATOM   6107  C CB    . TYR B 2 767  ? 140.479 160.987 153.839 1.00 48.55  ? 764  TYR A CB    1 
ATOM   6108  C CG    . TYR B 2 767  ? 139.778 160.564 152.569 1.00 48.55  ? 764  TYR A CG    1 
ATOM   6109  C CD1   . TYR B 2 767  ? 138.651 161.231 152.114 1.00 48.55  ? 764  TYR A CD1   1 
ATOM   6110  C CD2   . TYR B 2 767  ? 140.244 159.485 151.831 1.00 48.55  ? 764  TYR A CD2   1 
ATOM   6111  C CE1   . TYR B 2 767  ? 138.011 160.836 150.955 1.00 48.55  ? 764  TYR A CE1   1 
ATOM   6112  C CE2   . TYR B 2 767  ? 139.612 159.085 150.674 1.00 48.55  ? 764  TYR A CE2   1 
ATOM   6113  C CZ    . TYR B 2 767  ? 138.497 159.762 150.240 1.00 48.55  ? 764  TYR A CZ    1 
ATOM   6114  O OH    . TYR B 2 767  ? 137.870 159.357 149.086 1.00 48.55  ? 764  TYR A OH    1 
ATOM   6115  N N     . TRP B 2 768  ? 141.998 162.792 155.892 1.00 48.55  ? 765  TRP A N     1 
ATOM   6116  C CA    . TRP B 2 768  ? 142.544 162.990 157.230 1.00 48.55  ? 765  TRP A CA    1 
ATOM   6117  C C     . TRP B 2 768  ? 142.193 164.369 157.771 1.00 48.55  ? 765  TRP A C     1 
ATOM   6118  O O     . TRP B 2 768  ? 141.801 164.507 158.935 1.00 48.55  ? 765  TRP A O     1 
ATOM   6119  C CB    . TRP B 2 768  ? 144.056 162.790 157.209 1.00 48.55  ? 765  TRP A CB    1 
ATOM   6120  C CG    . TRP B 2 768  ? 144.660 162.698 158.565 1.00 48.55  ? 765  TRP A CG    1 
ATOM   6121  C CD1   . TRP B 2 768  ? 145.461 163.618 159.170 1.00 48.55  ? 765  TRP A CD1   1 
ATOM   6122  C CD2   . TRP B 2 768  ? 144.515 161.619 159.492 1.00 48.55  ? 765  TRP A CD2   1 
ATOM   6123  N NE1   . TRP B 2 768  ? 145.825 163.178 160.419 1.00 48.55  ? 765  TRP A NE1   1 
ATOM   6124  C CE2   . TRP B 2 768  ? 145.255 161.952 160.639 1.00 48.55  ? 765  TRP A CE2   1 
ATOM   6125  C CE3   . TRP B 2 768  ? 143.829 160.401 159.462 1.00 48.55  ? 765  TRP A CE3   1 
ATOM   6126  C CZ2   . TRP B 2 768  ? 145.330 161.115 161.746 1.00 48.55  ? 765  TRP A CZ2   1 
ATOM   6127  C CZ3   . TRP B 2 768  ? 143.904 159.572 160.562 1.00 48.55  ? 765  TRP A CZ3   1 
ATOM   6128  C CH2   . TRP B 2 768  ? 144.649 159.932 161.689 1.00 48.55  ? 765  TRP A CH2   1 
ATOM   6129  N N     . THR B 2 769  ? 142.337 165.406 156.941 1.00 48.55  ? 766  THR A N     1 
ATOM   6130  C CA    . THR B 2 769  ? 141.967 166.752 157.366 1.00 48.55  ? 766  THR A CA    1 
ATOM   6131  C C     . THR B 2 769  ? 140.471 166.851 157.636 1.00 48.55  ? 766  THR A C     1 
ATOM   6132  O O     . THR B 2 769  ? 140.050 167.492 158.606 1.00 48.55  ? 766  THR A O     1 
ATOM   6133  C CB    . THR B 2 769  ? 142.391 167.773 156.311 1.00 48.55  ? 766  THR A CB    1 
ATOM   6134  O OG1   . THR B 2 769  ? 143.806 167.684 156.100 1.00 48.55  ? 766  THR A OG1   1 
ATOM   6135  C CG2   . THR B 2 769  ? 142.042 169.184 156.760 1.00 48.55  ? 766  THR A CG2   1 
ATOM   6136  N N     . GLY B 2 770  ? 139.654 166.214 156.796 1.00 48.55  ? 767  GLY A N     1 
ATOM   6137  C CA    . GLY B 2 770  ? 138.216 166.250 156.988 1.00 48.55  ? 767  GLY A CA    1 
ATOM   6138  C C     . GLY B 2 770  ? 137.732 165.430 158.163 1.00 48.55  ? 767  GLY A C     1 
ATOM   6139  O O     . GLY B 2 770  ? 136.628 165.674 158.661 1.00 48.55  ? 767  GLY A O     1 
ATOM   6140  N N     . LEU B 2 771  ? 138.527 164.457 158.612 1.00 48.55  ? 768  LEU A N     1 
ATOM   6141  C CA    . LEU B 2 771  ? 138.146 163.676 159.783 1.00 48.55  ? 768  LEU A CA    1 
ATOM   6142  C C     . LEU B 2 771  ? 138.137 164.542 161.035 1.00 48.55  ? 768  LEU A C     1 
ATOM   6143  O O     . LEU B 2 771  ? 137.266 164.390 161.900 1.00 48.55  ? 768  LEU A O     1 
ATOM   6144  C CB    . LEU B 2 771  ? 139.094 162.488 159.951 1.00 48.55  ? 768  LEU A CB    1 
ATOM   6145  C CG    . LEU B 2 771  ? 138.724 161.381 160.941 1.00 48.55  ? 768  LEU A CG    1 
ATOM   6146  C CD1   . LEU B 2 771  ? 139.343 160.075 160.493 1.00 48.55  ? 768  LEU A CD1   1 
ATOM   6147  C CD2   . LEU B 2 771  ? 139.170 161.703 162.356 1.00 48.55  ? 768  LEU A CD2   1 
ATOM   6148  N N     . PHE B 2 772  ? 139.097 165.456 161.150 1.00 48.55  ? 769  PHE A N     1 
ATOM   6149  C CA    . PHE B 2 772  ? 139.224 166.322 162.312 1.00 48.55  ? 769  PHE A CA    1 
ATOM   6150  C C     . PHE B 2 772  ? 138.655 167.714 162.075 1.00 48.55  ? 769  PHE A C     1 
ATOM   6151  O O     . PHE B 2 772  ? 138.905 168.618 162.879 1.00 48.55  ? 769  PHE A O     1 
ATOM   6152  C CB    . PHE B 2 772  ? 140.689 166.415 162.737 1.00 48.55  ? 769  PHE A CB    1 
ATOM   6153  C CG    . PHE B 2 772  ? 141.295 165.092 163.099 1.00 48.55  ? 769  PHE A CG    1 
ATOM   6154  C CD1   . PHE B 2 772  ? 140.891 164.423 164.239 1.00 48.55  ? 769  PHE A CD1   1 
ATOM   6155  C CD2   . PHE B 2 772  ? 142.258 164.513 162.295 1.00 48.55  ? 769  PHE A CD2   1 
ATOM   6156  C CE1   . PHE B 2 772  ? 141.444 163.207 164.577 1.00 48.55  ? 769  PHE A CE1   1 
ATOM   6157  C CE2   . PHE B 2 772  ? 142.814 163.296 162.627 1.00 48.55  ? 769  PHE A CE2   1 
ATOM   6158  C CZ    . PHE B 2 772  ? 142.405 162.642 163.769 1.00 48.55  ? 769  PHE A CZ    1 
ATOM   6159  N N     . SER B 2 773  ? 137.905 167.908 160.994 1.00 48.55  ? 770  SER A N     1 
ATOM   6160  C CA    . SER B 2 773  ? 137.240 169.181 160.775 1.00 48.55  ? 770  SER A CA    1 
ATOM   6161  C C     . SER B 2 773  ? 136.168 169.391 161.843 1.00 48.55  ? 770  SER A C     1 
ATOM   6162  O O     . SER B 2 773  ? 135.574 168.427 162.333 1.00 48.55  ? 770  SER A O     1 
ATOM   6163  C CB    . SER B 2 773  ? 136.615 169.225 159.383 1.00 48.55  ? 770  SER A CB    1 
ATOM   6164  O OG    . SER B 2 773  ? 135.489 168.368 159.302 1.00 48.55  ? 770  SER A OG    1 
ATOM   6165  N N     . PRO B 2 774  ? 135.907 170.643 162.230 1.00 48.55  ? 771  PRO A N     1 
ATOM   6166  C CA    . PRO B 2 774  ? 134.933 170.882 163.310 1.00 48.55  ? 771  PRO A CA    1 
ATOM   6167  C C     . PRO B 2 774  ? 133.553 170.316 163.026 1.00 48.55  ? 771  PRO A C     1 
ATOM   6168  O O     . PRO B 2 774  ? 132.872 169.865 163.956 1.00 48.55  ? 771  PRO A O     1 
ATOM   6169  C CB    . PRO B 2 774  ? 134.907 172.413 163.419 1.00 48.55  ? 771  PRO A CB    1 
ATOM   6170  C CG    . PRO B 2 774  ? 136.216 172.857 162.869 1.00 48.55  ? 771  PRO A CG    1 
ATOM   6171  C CD    . PRO B 2 774  ? 136.562 171.885 161.785 1.00 48.55  ? 771  PRO A CD    1 
ATOM   6172  N N     . GLU B 2 775  ? 133.116 170.325 161.765 1.00 48.55  ? 772  GLU A N     1 
ATOM   6173  C CA    . GLU B 2 775  ? 131.793 169.798 161.443 1.00 48.55  ? 772  GLU A CA    1 
ATOM   6174  C C     . GLU B 2 775  ? 131.746 168.282 161.594 1.00 48.55  ? 772  GLU A C     1 
ATOM   6175  O O     . GLU B 2 775  ? 130.721 167.727 162.006 1.00 48.55  ? 772  GLU A O     1 
ATOM   6176  C CB    . GLU B 2 775  ? 131.391 170.211 160.028 1.00 48.55  ? 772  GLU A CB    1 
ATOM   6177  C CG    . GLU B 2 775  ? 132.516 170.146 159.011 1.00 48.55  ? 772  GLU A CG    1 
ATOM   6178  C CD    . GLU B 2 775  ? 133.203 171.483 158.813 1.00 48.55  ? 772  GLU A CD    1 
ATOM   6179  O OE1   . GLU B 2 775  ? 133.241 172.282 159.773 1.00 48.55  ? 772  GLU A OE1   1 
ATOM   6180  O OE2   . GLU B 2 775  ? 133.705 171.736 157.698 1.00 48.55  ? 772  GLU A OE2   1 
ATOM   6181  N N     . ASN B 2 776  ? 132.842 167.596 161.261 1.00 48.55  ? 773  ASN A N     1 
ATOM   6182  C CA    . ASN B 2 776  ? 132.862 166.140 161.369 1.00 48.55  ? 773  ASN A CA    1 
ATOM   6183  C C     . ASN B 2 776  ? 132.739 165.688 162.818 1.00 48.55  ? 773  ASN A C     1 
ATOM   6184  O O     . ASN B 2 776  ? 132.054 164.701 163.110 1.00 48.55  ? 773  ASN A O     1 
ATOM   6185  C CB    . ASN B 2 776  ? 134.137 165.583 160.740 1.00 48.55  ? 773  ASN A CB    1 
ATOM   6186  C CG    . ASN B 2 776  ? 134.177 164.070 160.752 1.00 48.55  ? 773  ASN A CG    1 
ATOM   6187  O OD1   . ASN B 2 776  ? 133.412 163.412 160.048 1.00 48.55  ? 773  ASN A OD1   1 
ATOM   6188  N ND2   . ASN B 2 776  ? 135.072 163.508 161.556 1.00 48.55  ? 773  ASN A ND2   1 
ATOM   6189  N N     . LEU B 2 777  ? 133.408 166.384 163.738 1.00 48.55  ? 774  LEU A N     1 
ATOM   6190  C CA    . LEU B 2 777  ? 133.248 166.069 165.154 1.00 48.55  ? 774  LEU A CA    1 
ATOM   6191  C C     . LEU B 2 777  ? 131.844 166.411 165.639 1.00 48.55  ? 774  LEU A C     1 
ATOM   6192  O O     . LEU B 2 777  ? 131.309 165.739 166.529 1.00 48.55  ? 774  LEU A O     1 
ATOM   6193  C CB    . LEU B 2 777  ? 134.300 166.802 165.987 1.00 48.55  ? 774  LEU A CB    1 
ATOM   6194  C CG    . LEU B 2 777  ? 135.730 166.252 166.013 1.00 48.55  ? 774  LEU A CG    1 
ATOM   6195  C CD1   . LEU B 2 777  ? 136.455 166.468 164.697 1.00 48.55  ? 774  LEU A CD1   1 
ATOM   6196  C CD2   . LEU B 2 777  ? 136.512 166.878 167.156 1.00 48.55  ? 774  LEU A CD2   1 
ATOM   6197  N N     . ALA B 2 778  ? 131.235 167.456 165.073 1.00 48.55  ? 775  ALA A N     1 
ATOM   6198  C CA    . ALA B 2 778  ? 129.876 167.816 165.463 1.00 48.55  ? 775  ALA A CA    1 
ATOM   6199  C C     . ALA B 2 778  ? 128.879 166.742 165.048 1.00 48.55  ? 775  ALA A C     1 
ATOM   6200  O O     . ALA B 2 778  ? 128.061 166.295 165.860 1.00 48.55  ? 775  ALA A O     1 
ATOM   6201  C CB    . ALA B 2 778  ? 129.496 169.167 164.857 1.00 48.55  ? 775  ALA A CB    1 
ATOM   6202  N N     . LYS B 2 779  ? 128.931 166.315 163.788 1.00 48.55  ? 776  LYS A N     1 
ATOM   6203  C CA    . LYS B 2 779  ? 128.115 165.206 163.302 1.00 48.55  ? 776  LYS A CA    1 
ATOM   6204  C C     . LYS B 2 779  ? 129.034 164.263 162.538 1.00 48.55  ? 776  LYS A C     1 
ATOM   6205  O O     . LYS B 2 779  ? 129.731 164.684 161.610 1.00 48.55  ? 776  LYS A O     1 
ATOM   6206  C CB    . LYS B 2 779  ? 126.947 165.699 162.440 1.00 48.55  ? 776  LYS A CB    1 
ATOM   6207  C CG    . LYS B 2 779  ? 127.316 166.518 161.205 1.00 48.55  ? 776  LYS A CG    1 
ATOM   6208  C CD    . LYS B 2 779  ? 127.301 165.672 159.939 1.00 48.55  ? 776  LYS A CD    1 
ATOM   6209  C CE    . LYS B 2 779  ? 127.575 166.518 158.706 1.00 48.55  ? 776  LYS A CE    1 
ATOM   6210  N NZ    . LYS B 2 779  ? 127.587 165.700 157.462 1.00 48.55  ? 776  LYS A NZ    1 
ATOM   6211  N N     . THR B 2 780  ? 129.061 162.999 162.947 1.00 48.55  ? 777  THR A N     1 
ATOM   6212  C CA    . THR B 2 780  ? 130.039 162.069 162.403 1.00 48.55  ? 777  THR A CA    1 
ATOM   6213  C C     . THR B 2 780  ? 129.673 161.640 160.987 1.00 48.55  ? 777  THR A C     1 
ATOM   6214  O O     . THR B 2 780  ? 128.522 161.307 160.690 1.00 48.55  ? 777  THR A O     1 
ATOM   6215  C CB    . THR B 2 780  ? 130.186 160.849 163.317 1.00 48.55  ? 777  THR A CB    1 
ATOM   6216  O OG1   . THR B 2 780  ? 131.219 159.991 162.815 1.00 48.55  ? 777  THR A OG1   1 
ATOM   6217  C CG2   . THR B 2 780  ? 128.878 160.072 163.436 1.00 48.55  ? 777  THR A CG2   1 
ATOM   6218  N N     . SER B 2 781  ? 130.664 161.692 160.101 1.00 48.55  ? 778  SER A N     1 
ATOM   6219  C CA    . SER B 2 781  ? 130.552 161.111 158.767 1.00 48.55  ? 778  SER A CA    1 
ATOM   6220  C C     . SER B 2 781  ? 131.755 160.274 158.371 1.00 48.55  ? 778  SER A C     1 
ATOM   6221  O O     . SER B 2 781  ? 131.615 159.405 157.504 1.00 48.55  ? 778  SER A O     1 
ATOM   6222  C CB    . SER B 2 781  ? 130.342 162.207 157.716 1.00 48.55  ? 778  SER A CB    1 
ATOM   6223  O OG    . SER B 2 781  ? 130.257 161.655 156.414 1.00 48.55  ? 778  SER A OG    1 
ATOM   6224  N N     . ILE B 2 782  ? 132.925 160.493 158.967 1.00 48.55  ? 779  ILE A N     1 
ATOM   6225  C CA    . ILE B 2 782  ? 134.100 159.653 158.774 1.00 48.55  ? 779  ILE A CA    1 
ATOM   6226  C C     . ILE B 2 782  ? 134.555 159.190 160.150 1.00 48.55  ? 779  ILE A C     1 
ATOM   6227  O O     . ILE B 2 782  ? 135.030 160.000 160.955 1.00 48.55  ? 779  ILE A O     1 
ATOM   6228  C CB    . ILE B 2 782  ? 135.229 160.403 158.051 1.00 48.55  ? 779  ILE A CB    1 
ATOM   6229  C CG1   . ILE B 2 782  ? 134.671 161.241 156.900 1.00 48.55  ? 779  ILE A CG1   1 
ATOM   6230  C CG2   . ILE B 2 782  ? 136.273 159.425 157.539 1.00 48.55  ? 779  ILE A CG2   1 
ATOM   6231  C CD1   . ILE B 2 782  ? 135.708 162.107 156.223 1.00 48.55  ? 779  ILE A CD1   1 
ATOM   6232  N N     . LYS B 2 783  ? 134.414 157.896 160.421 1.00 48.55  ? 780  LYS A N     1 
ATOM   6233  C CA    . LYS B 2 783  ? 134.783 157.333 161.712 1.00 48.55  ? 780  LYS A CA    1 
ATOM   6234  C C     . LYS B 2 783  ? 136.235 156.882 161.699 1.00 48.55  ? 780  LYS A C     1 
ATOM   6235  O O     . LYS B 2 783  ? 136.702 156.274 160.731 1.00 48.55  ? 780  LYS A O     1 
ATOM   6236  C CB    . LYS B 2 783  ? 133.887 156.152 162.090 1.00 48.55  ? 780  LYS A CB    1 
ATOM   6237  C CG    . LYS B 2 783  ? 134.281 155.515 163.419 1.00 48.55  ? 780  LYS A CG    1 
ATOM   6238  C CD    . LYS B 2 783  ? 133.258 154.518 163.928 1.00 48.55  ? 780  LYS A CD    1 
ATOM   6239  C CE    . LYS B 2 783  ? 133.389 153.178 163.228 1.00 48.55  ? 780  LYS A CE    1 
ATOM   6240  N NZ    . LYS B 2 783  ? 134.624 152.456 163.639 1.00 48.55  ? 780  LYS A NZ    1 
ATOM   6241  N N     . LEU B 2 784  ? 136.944 157.179 162.784 1.00 48.55  ? 781  LEU A N     1 
ATOM   6242  C CA    . LEU B 2 784  ? 138.328 156.752 162.959 1.00 48.55  ? 781  LEU A CA    1 
ATOM   6243  C C     . LEU B 2 784  ? 138.311 155.346 163.544 1.00 48.55  ? 781  LEU A C     1 
ATOM   6244  O O     . LEU B 2 784  ? 138.207 155.167 164.759 1.00 48.55  ? 781  LEU A O     1 
ATOM   6245  C CB    . LEU B 2 784  ? 139.078 157.723 163.862 1.00 48.55  ? 781  LEU A CB    1 
ATOM   6246  C CG    . LEU B 2 784  ? 140.573 157.474 164.030 1.00 48.55  ? 781  LEU A CG    1 
ATOM   6247  C CD1   . LEU B 2 784  ? 141.244 157.469 162.675 1.00 48.55  ? 781  LEU A CD1   1 
ATOM   6248  C CD2   . LEU B 2 784  ? 141.190 158.526 164.933 1.00 48.55  ? 781  LEU A CD2   1 
ATOM   6249  N N     . ASN B 2 785  ? 138.408 154.341 162.677 1.00 48.55  ? 782  ASN A N     1 
ATOM   6250  C CA    . ASN B 2 785  ? 138.374 152.959 163.128 1.00 48.55  ? 782  ASN A CA    1 
ATOM   6251  C C     . ASN B 2 785  ? 139.639 152.609 163.905 1.00 48.55  ? 782  ASN A C     1 
ATOM   6252  O O     . ASN B 2 785  ? 140.657 153.303 163.843 1.00 48.55  ? 782  ASN A O     1 
ATOM   6253  C CB    . ASN B 2 785  ? 138.226 152.004 161.945 1.00 48.55  ? 782  ASN A CB    1 
ATOM   6254  C CG    . ASN B 2 785  ? 136.949 152.227 161.172 1.00 48.55  ? 782  ASN A CG    1 
ATOM   6255  O OD1   . ASN B 2 785  ? 135.856 151.963 161.669 1.00 48.55  ? 782  ASN A OD1   1 
ATOM   6256  N ND2   . ASN B 2 785  ? 137.078 152.708 159.944 1.00 48.55  ? 782  ASN A ND2   1 
ATOM   6257  N N     . GLY B 2 786  ? 139.559 151.509 164.646 1.00 48.55  ? 783  GLY A N     1 
ATOM   6258  C CA    . GLY B 2 786  ? 140.700 150.977 165.365 1.00 48.55  ? 783  GLY A CA    1 
ATOM   6259  C C     . GLY B 2 786  ? 141.530 150.060 164.495 1.00 48.55  ? 783  GLY A C     1 
ATOM   6260  O O     . GLY B 2 786  ? 141.505 150.143 163.262 1.00 48.55  ? 783  GLY A O     1 
ATOM   6261  N N     . GLN B 2 787  ? 142.276 149.169 165.146 1.00 48.55  ? 784  GLN A N     1 
ATOM   6262  C CA    . GLN B 2 787  ? 143.112 148.184 164.458 1.00 48.55  ? 784  GLN A CA    1 
ATOM   6263  C C     . GLN B 2 787  ? 144.106 148.856 163.514 1.00 48.55  ? 784  GLN A C     1 
ATOM   6264  O O     . GLN B 2 787  ? 144.347 148.394 162.397 1.00 48.55  ? 784  GLN A O     1 
ATOM   6265  C CB    . GLN B 2 787  ? 142.256 147.162 163.707 1.00 48.55  ? 784  GLN A CB    1 
ATOM   6266  C CG    . GLN B 2 787  ? 141.829 145.968 164.545 1.00 48.55  ? 784  GLN A CG    1 
ATOM   6267  C CD    . GLN B 2 787  ? 140.462 146.156 165.173 1.00 48.55  ? 784  GLN A CD    1 
ATOM   6268  O OE1   . GLN B 2 787  ? 139.465 146.337 164.475 1.00 48.55  ? 784  GLN A OE1   1 
ATOM   6269  N NE2   . GLN B 2 787  ? 140.409 146.112 166.499 1.00 48.55  ? 784  GLN A NE2   1 
ATOM   6270  N N     . ALA B 2 788  ? 144.686 149.963 163.966 1.00 48.55  ? 785  ALA A N     1 
ATOM   6271  C CA    . ALA B 2 788  ? 145.742 150.613 163.209 1.00 48.55  ? 785  ALA A CA    1 
ATOM   6272  C C     . ALA B 2 788  ? 147.051 149.843 163.362 1.00 48.55  ? 785  ALA A C     1 
ATOM   6273  O O     . ALA B 2 788  ? 147.247 149.083 164.314 1.00 48.55  ? 785  ALA A O     1 
ATOM   6274  C CB    . ALA B 2 788  ? 145.921 152.060 163.664 1.00 48.55  ? 785  ALA A CB    1 
ATOM   6275  N N     . GLU B 2 789  ? 147.953 150.047 162.406 1.00 48.55  ? 786  GLU A N     1 
ATOM   6276  C CA    . GLU B 2 789  ? 149.219 149.331 162.383 1.00 48.55  ? 786  GLU A CA    1 
ATOM   6277  C C     . GLU B 2 789  ? 150.354 150.295 162.075 1.00 48.55  ? 786  GLU A C     1 
ATOM   6278  O O     . GLU B 2 789  ? 150.166 151.305 161.393 1.00 48.55  ? 786  GLU A O     1 
ATOM   6279  C CB    . GLU B 2 789  ? 149.206 148.198 161.349 1.00 48.55  ? 786  GLU A CB    1 
ATOM   6280  C CG    . GLU B 2 789  ? 148.248 147.066 161.677 1.00 48.55  ? 786  GLU A CG    1 
ATOM   6281  C CD    . GLU B 2 789  ? 147.868 146.253 160.455 1.00 48.55  ? 786  GLU A CD    1 
ATOM   6282  O OE1   . GLU B 2 789  ? 148.644 145.350 160.076 1.00 48.55  ? 786  GLU A OE1   1 
ATOM   6283  O OE2   . GLU B 2 789  ? 146.794 146.516 159.874 1.00 48.55  ? 786  GLU A OE2   1 
ATOM   6284  N N     . LEU B 2 790  ? 151.538 149.968 162.586 1.00 48.55  ? 787  LEU A N     1 
ATOM   6285  C CA    . LEU B 2 790  ? 152.753 150.717 162.315 1.00 48.55  ? 787  LEU A CA    1 
ATOM   6286  C C     . LEU B 2 790  ? 153.762 149.823 161.608 1.00 48.55  ? 787  LEU A C     1 
ATOM   6287  O O     . LEU B 2 790  ? 153.665 148.593 161.643 1.00 48.55  ? 787  LEU A O     1 
ATOM   6288  C CB    . LEU B 2 790  ? 153.369 151.282 163.598 1.00 48.55  ? 787  LEU A CB    1 
ATOM   6289  C CG    . LEU B 2 790  ? 152.770 152.585 164.127 1.00 48.55  ? 787  LEU A CG    1 
ATOM   6290  C CD1   . LEU B 2 790  ? 151.462 152.339 164.863 1.00 48.55  ? 787  LEU A CD1   1 
ATOM   6291  C CD2   . LEU B 2 790  ? 153.774 153.288 165.014 1.00 48.55  ? 787  LEU A CD2   1 
ATOM   6292  N N     . PHE B 2 791  ? 154.740 150.456 160.963 1.00 48.55  ? 788  PHE A N     1 
ATOM   6293  C CA    . PHE B 2 791  ? 155.725 149.726 160.180 1.00 48.55  ? 788  PHE A CA    1 
ATOM   6294  C C     . PHE B 2 791  ? 157.058 150.456 160.233 1.00 48.55  ? 788  PHE A C     1 
ATOM   6295  O O     . PHE B 2 791  ? 157.150 151.594 160.700 1.00 48.55  ? 788  PHE A O     1 
ATOM   6296  C CB    . PHE B 2 791  ? 155.269 149.554 158.727 1.00 48.55  ? 788  PHE A CB    1 
ATOM   6297  C CG    . PHE B 2 791  ? 154.107 148.621 158.565 1.00 48.55  ? 788  PHE A CG    1 
ATOM   6298  C CD1   . PHE B 2 791  ? 154.289 147.252 158.619 1.00 48.55  ? 788  PHE A CD1   1 
ATOM   6299  C CD2   . PHE B 2 791  ? 152.831 149.114 158.364 1.00 48.55  ? 788  PHE A CD2   1 
ATOM   6300  C CE1   . PHE B 2 791  ? 153.222 146.392 158.474 1.00 48.55  ? 788  PHE A CE1   1 
ATOM   6301  C CE2   . PHE B 2 791  ? 151.760 148.259 158.219 1.00 48.55  ? 788  PHE A CE2   1 
ATOM   6302  C CZ    . PHE B 2 791  ? 151.957 146.896 158.275 1.00 48.55  ? 788  PHE A CZ    1 
ATOM   6303  N N     . TYR B 2 792  ? 158.095 149.777 159.748 1.00 48.55  ? 789  TYR A N     1 
ATOM   6304  C CA    . TYR B 2 792  ? 159.445 150.325 159.693 1.00 48.55  ? 789  TYR A CA    1 
ATOM   6305  C C     . TYR B 2 792  ? 160.137 149.738 158.476 1.00 48.55  ? 789  TYR A C     1 
ATOM   6306  O O     . TYR B 2 792  ? 160.247 148.514 158.355 1.00 48.55  ? 789  TYR A O     1 
ATOM   6307  C CB    . TYR B 2 792  ? 160.222 150.004 160.973 1.00 48.55  ? 789  TYR A CB    1 
ATOM   6308  C CG    . TYR B 2 792  ? 161.648 150.508 161.002 1.00 48.55  ? 789  TYR A CG    1 
ATOM   6309  C CD1   . TYR B 2 792  ? 162.691 149.726 160.528 1.00 48.55  ? 789  TYR A CD1   1 
ATOM   6310  C CD2   . TYR B 2 792  ? 161.954 151.757 161.522 1.00 48.55  ? 789  TYR A CD2   1 
ATOM   6311  C CE1   . TYR B 2 792  ? 163.994 150.176 160.560 1.00 48.55  ? 789  TYR A CE1   1 
ATOM   6312  C CE2   . TYR B 2 792  ? 163.256 152.216 161.559 1.00 48.55  ? 789  TYR A CE2   1 
ATOM   6313  C CZ    . TYR B 2 792  ? 164.271 151.421 161.075 1.00 48.55  ? 789  TYR A CZ    1 
ATOM   6314  O OH    . TYR B 2 792  ? 165.570 151.869 161.109 1.00 48.55  ? 789  TYR A OH    1 
ATOM   6315  N N     . ARG B 2 793  ? 160.601 150.605 157.579 1.00 48.55  ? 790  ARG A N     1 
ATOM   6316  C CA    . ARG B 2 793  ? 161.172 150.177 156.306 1.00 48.55  ? 790  ARG A CA    1 
ATOM   6317  C C     . ARG B 2 793  ? 162.679 150.384 156.309 1.00 48.55  ? 790  ARG A C     1 
ATOM   6318  O O     . ARG B 2 793  ? 163.148 151.530 156.230 1.00 48.55  ? 790  ARG A O     1 
ATOM   6319  C CB    . ARG B 2 793  ? 160.528 150.950 155.152 1.00 48.55  ? 790  ARG A CB    1 
ATOM   6320  C CG    . ARG B 2 793  ? 161.002 150.536 153.774 1.00 48.55  ? 790  ARG A CG    1 
ATOM   6321  C CD    . ARG B 2 793  ? 160.291 151.342 152.706 1.00 48.55  ? 790  ARG A CD    1 
ATOM   6322  N NE    . ARG B 2 793  ? 160.658 152.751 152.755 1.00 48.55  ? 790  ARG A NE    1 
ATOM   6323  C CZ    . ARG B 2 793  ? 160.043 153.709 152.076 1.00 48.55  ? 790  ARG A CZ    1 
ATOM   6324  N NH1   . ARG B 2 793  ? 159.007 153.447 151.297 1.00 48.55  ? 790  ARG A NH1   1 
ATOM   6325  N NH2   . ARG B 2 793  ? 160.473 154.962 152.187 1.00 48.55  ? 790  ARG A NH2   1 
ATOM   6326  N N     . PRO B 2 794  ? 163.478 149.323 156.411 1.00 48.55  ? 791  PRO A N     1 
ATOM   6327  C CA    . PRO B 2 794  ? 164.933 149.488 156.342 1.00 48.55  ? 791  PRO A CA    1 
ATOM   6328  C C     . PRO B 2 794  ? 165.358 150.068 155.002 1.00 48.55  ? 791  PRO A C     1 
ATOM   6329  O O     . PRO B 2 794  ? 164.777 149.763 153.959 1.00 48.55  ? 791  PRO A O     1 
ATOM   6330  C CB    . PRO B 2 794  ? 165.462 148.063 156.533 1.00 48.55  ? 791  PRO A CB    1 
ATOM   6331  C CG    . PRO B 2 794  ? 164.363 147.339 157.225 1.00 48.55  ? 791  PRO A CG    1 
ATOM   6332  C CD    . PRO B 2 794  ? 163.092 147.934 156.708 1.00 48.55  ? 791  PRO A CD    1 
ATOM   6333  N N     . LYS B 2 795  ? 166.382 150.914 155.042 1.00 48.55  ? 792  LYS A N     1 
ATOM   6334  C CA    . LYS B 2 795  ? 166.868 151.554 153.832 1.00 48.55  ? 792  LYS A CA    1 
ATOM   6335  C C     . LYS B 2 795  ? 167.548 150.536 152.922 1.00 48.55  ? 792  LYS A C     1 
ATOM   6336  O O     . LYS B 2 795  ? 168.048 149.498 153.364 1.00 48.55  ? 792  LYS A O     1 
ATOM   6337  C CB    . LYS B 2 795  ? 167.838 152.685 154.173 1.00 33.45  ? 792  LYS A CB    1 
ATOM   6338  C CG    . LYS B 2 795  ? 169.280 152.239 154.357 1.00 33.45  ? 792  LYS A CG    1 
ATOM   6339  C CD    . LYS B 2 795  ? 170.138 153.358 154.923 1.00 33.45  ? 792  LYS A CD    1 
ATOM   6340  C CE    . LYS B 2 795  ? 171.616 153.072 154.726 1.00 33.45  ? 792  LYS A CE    1 
ATOM   6341  N NZ    . LYS B 2 795  ? 172.009 153.155 153.293 1.00 33.45  ? 792  LYS A NZ    1 
ATOM   6342  N N     . SER B 2 796  ? 167.551 150.845 151.626 1.00 48.55  ? 793  SER A N     1 
ATOM   6343  C CA    . SER B 2 796  ? 168.230 150.005 150.642 1.00 48.55  ? 793  SER A CA    1 
ATOM   6344  C C     . SER B 2 796  ? 168.704 150.915 149.514 1.00 48.55  ? 793  SER A C     1 
ATOM   6345  O O     . SER B 2 796  ? 167.937 151.219 148.596 1.00 48.55  ? 793  SER A O     1 
ATOM   6346  C CB    . SER B 2 796  ? 167.312 148.909 150.125 1.00 48.55  ? 793  SER A CB    1 
ATOM   6347  O OG    . SER B 2 796  ? 166.384 149.428 149.188 1.00 48.55  ? 793  SER A OG    1 
ATOM   6348  N N     . ARG B 2 797  ? 169.959 151.341 149.590 1.00 48.55  ? 794  ARG A N     1 
ATOM   6349  C CA    . ARG B 2 797  ? 170.564 152.199 148.576 1.00 48.55  ? 794  ARG A CA    1 
ATOM   6350  C C     . ARG B 2 797  ? 171.711 151.421 147.940 1.00 48.55  ? 794  ARG A C     1 
ATOM   6351  O O     . ARG B 2 797  ? 172.649 151.007 148.627 1.00 48.55  ? 794  ARG A O     1 
ATOM   6352  C CB    . ARG B 2 797  ? 171.046 153.513 149.185 1.00 48.55  ? 794  ARG A CB    1 
ATOM   6353  C CG    . ARG B 2 797  ? 171.248 154.640 148.178 1.00 48.55  ? 794  ARG A CG    1 
ATOM   6354  C CD    . ARG B 2 797  ? 169.943 155.031 147.491 1.00 48.55  ? 794  ARG A CD    1 
ATOM   6355  N NE    . ARG B 2 797  ? 169.688 154.254 146.283 1.00 48.55  ? 794  ARG A NE    1 
ATOM   6356  C CZ    . ARG B 2 797  ? 168.481 154.002 145.797 1.00 48.55  ? 794  ARG A CZ    1 
ATOM   6357  N NH1   . ARG B 2 797  ? 167.389 154.453 146.391 1.00 48.55  ? 794  ARG A NH1   1 
ATOM   6358  N NH2   . ARG B 2 797  ? 168.367 153.279 144.687 1.00 48.55  ? 794  ARG A NH2   1 
ATOM   6359  N N     . MET B 2 798  ? 171.632 151.225 146.625 1.00 51.21  ? 795  MET A N     1 
ATOM   6360  C CA    . MET B 2 798  ? 172.660 150.486 145.904 1.00 51.21  ? 795  MET A CA    1 
ATOM   6361  C C     . MET B 2 798  ? 173.615 151.420 145.169 1.00 51.21  ? 795  MET A C     1 
ATOM   6362  O O     . MET B 2 798  ? 174.836 151.305 145.315 1.00 51.21  ? 795  MET A O     1 
ATOM   6363  C CB    . MET B 2 798  ? 172.012 149.507 144.920 1.00 51.21  ? 795  MET A CB    1 
ATOM   6364  C CG    . MET B 2 798  ? 171.202 148.391 145.572 1.00 51.21  ? 795  MET A CG    1 
ATOM   6365  S SD    . MET B 2 798  ? 172.171 147.306 146.641 1.00 51.21  ? 795  MET A SD    1 
ATOM   6366  C CE    . MET B 2 798  ? 171.719 147.915 148.265 1.00 51.21  ? 795  MET A CE    1 
ATOM   6367  N N     . LYS B 2 799  ? 173.075 152.348 144.379 1.00 55.63  ? 796  LYS A N     1 
ATOM   6368  C CA    . LYS B 2 799  ? 173.878 153.319 143.631 1.00 55.63  ? 796  LYS A CA    1 
ATOM   6369  C C     . LYS B 2 799  ? 173.178 154.671 143.752 1.00 55.63  ? 796  LYS A C     1 
ATOM   6370  O O     . LYS B 2 799  ? 172.291 154.996 142.959 1.00 55.63  ? 796  LYS A O     1 
ATOM   6371  C CB    . LYS B 2 799  ? 174.054 152.898 142.178 1.00 55.63  ? 796  LYS A CB    1 
ATOM   6372  N N     . ARG B 2 800  ? 173.583 155.452 144.749 1.00 54.35  ? 797  ARG A N     1 
ATOM   6373  C CA    . ARG B 2 800  ? 172.967 156.750 144.985 1.00 54.35  ? 797  ARG A CA    1 
ATOM   6374  C C     . ARG B 2 800  ? 173.378 157.724 143.889 1.00 54.35  ? 797  ARG A C     1 
ATOM   6375  O O     . ARG B 2 800  ? 174.560 158.057 143.754 1.00 54.35  ? 797  ARG A O     1 
ATOM   6376  C CB    . ARG B 2 800  ? 173.370 157.284 146.358 1.00 54.35  ? 797  ARG A CB    1 
ATOM   6377  C CG    . ARG B 2 800  ? 172.565 158.487 146.826 1.00 54.35  ? 797  ARG A CG    1 
ATOM   6378  C CD    . ARG B 2 800  ? 173.301 159.793 146.563 1.00 54.35  ? 797  ARG A CD    1 
ATOM   6379  N NE    . ARG B 2 800  ? 174.652 159.782 147.111 1.00 54.35  ? 797  ARG A NE    1 
ATOM   6380  C CZ    . ARG B 2 800  ? 174.951 160.058 148.374 1.00 54.35  ? 797  ARG A CZ    1 
ATOM   6381  N NH1   . ARG B 2 800  ? 174.014 160.372 149.253 1.00 54.35  ? 797  ARG A NH1   1 
ATOM   6382  N NH2   . ARG B 2 800  ? 176.222 160.018 148.763 1.00 54.35  ? 797  ARG A NH2   1 
ATOM   6383  N N     . MET B 2 801  ? 172.404 158.183 143.110 1.00 53.36  ? 798  MET A N     1 
ATOM   6384  C CA    . MET B 2 801  ? 172.628 159.184 142.079 1.00 53.36  ? 798  MET A CA    1 
ATOM   6385  C C     . MET B 2 801  ? 171.777 160.404 142.396 1.00 53.36  ? 798  MET A C     1 
ATOM   6386  O O     . MET B 2 801  ? 170.589 160.280 142.708 1.00 53.36  ? 798  MET A O     1 
ATOM   6387  C CB    . MET B 2 801  ? 172.291 158.637 140.684 1.00 53.36  ? 798  MET A CB    1 
ATOM   6388  C CG    . MET B 2 801  ? 172.668 159.562 139.529 1.00 53.36  ? 798  MET A CG    1 
ATOM   6389  S SD    . MET B 2 801  ? 171.430 160.811 139.126 1.00 53.36  ? 798  MET A SD    1 
ATOM   6390  C CE    . MET B 2 801  ? 170.743 160.129 137.619 1.00 53.36  ? 798  MET A CE    1 
ATOM   6391  N N     . ALA B 2 802  ? 172.390 161.582 142.317 1.00 54.83  ? 799  ALA A N     1 
ATOM   6392  C CA    . ALA B 2 802  ? 171.717 162.810 142.704 1.00 54.83  ? 799  ALA A CA    1 
ATOM   6393  C C     . ALA B 2 802  ? 172.237 163.957 141.854 1.00 54.83  ? 799  ALA A C     1 
ATOM   6394  O O     . ALA B 2 802  ? 173.328 163.890 141.282 1.00 54.83  ? 799  ALA A O     1 
ATOM   6395  C CB    . ALA B 2 802  ? 171.916 163.113 144.194 1.00 54.83  ? 799  ALA A CB    1 
ATOM   6396  N N     . HIS B 2 803  ? 171.437 165.018 141.781 1.00 55.11  ? 800  HIS A N     1 
ATOM   6397  C CA    . HIS B 2 803  ? 171.792 166.217 141.026 1.00 55.11  ? 800  HIS A CA    1 
ATOM   6398  C C     . HIS B 2 803  ? 172.464 167.193 141.982 1.00 55.11  ? 800  HIS A C     1 
ATOM   6399  O O     . HIS B 2 803  ? 171.808 167.960 142.687 1.00 55.11  ? 800  HIS A O     1 
ATOM   6400  C CB    . HIS B 2 803  ? 170.562 166.826 140.366 1.00 55.11  ? 800  HIS A CB    1 
ATOM   6401  C CG    . HIS B 2 803  ? 169.869 165.904 139.411 1.00 55.11  ? 800  HIS A CG    1 
ATOM   6402  N ND1   . HIS B 2 803  ? 168.701 166.246 138.764 1.00 55.11  ? 800  HIS A ND1   1 
ATOM   6403  C CD2   . HIS B 2 803  ? 170.184 164.658 138.985 1.00 55.11  ? 800  HIS A CD2   1 
ATOM   6404  C CE1   . HIS B 2 803  ? 168.323 165.247 137.986 1.00 55.11  ? 800  HIS A CE1   1 
ATOM   6405  N NE2   . HIS B 2 803  ? 169.205 164.272 138.102 1.00 55.11  ? 800  HIS A NE2   1 
ATOM   6406  N N     . ARG B 2 804  ? 173.792 167.153 142.015 1.00 68.06  ? 801  ARG A N     1 
ATOM   6407  C CA    . ARG B 2 804  ? 174.545 168.046 142.878 1.00 68.06  ? 801  ARG A CA    1 
ATOM   6408  C C     . ARG B 2 804  ? 174.572 169.457 142.297 1.00 68.06  ? 801  ARG A C     1 
ATOM   6409  O O     . ARG B 2 804  ? 174.274 169.683 141.121 1.00 68.06  ? 801  ARG A O     1 
ATOM   6410  C CB    . ARG B 2 804  ? 175.970 167.528 143.073 1.00 68.06  ? 801  ARG A CB    1 
ATOM   6411  C CG    . ARG B 2 804  ? 176.679 167.159 141.782 1.00 68.06  ? 801  ARG A CG    1 
ATOM   6412  C CD    . ARG B 2 804  ? 178.131 166.788 142.038 1.00 68.06  ? 801  ARG A CD    1 
ATOM   6413  N NE    . ARG B 2 804  ? 178.299 165.356 142.255 1.00 68.06  ? 801  ARG A NE    1 
ATOM   6414  C CZ    . ARG B 2 804  ? 178.458 164.464 141.287 1.00 68.06  ? 801  ARG A CZ    1 
ATOM   6415  N NH1   . ARG B 2 804  ? 178.475 164.822 140.013 1.00 68.06  ? 801  ARG A NH1   1 
ATOM   6416  N NH2   . ARG B 2 804  ? 178.603 163.180 141.604 1.00 68.06  ? 801  ARG A NH2   1 
ATOM   6417  N N     . LEU B 2 805  ? 174.931 170.415 143.149 1.00 71.83  ? 802  LEU A N     1 
ATOM   6418  C CA    . LEU B 2 805  ? 174.999 171.806 142.722 1.00 71.83  ? 802  LEU A CA    1 
ATOM   6419  C C     . LEU B 2 805  ? 176.098 171.994 141.684 1.00 71.83  ? 802  LEU A C     1 
ATOM   6420  O O     . LEU B 2 805  ? 177.146 171.344 141.737 1.00 71.83  ? 802  LEU A O     1 
ATOM   6421  C CB    . LEU B 2 805  ? 175.246 172.717 143.926 1.00 71.83  ? 802  LEU A CB    1 
ATOM   6422  C CG    . LEU B 2 805  ? 174.191 172.664 145.033 1.00 71.83  ? 802  LEU A CG    1 
ATOM   6423  C CD1   . LEU B 2 805  ? 174.815 172.968 146.386 1.00 71.83  ? 802  LEU A CD1   1 
ATOM   6424  C CD2   . LEU B 2 805  ? 173.049 173.625 144.736 1.00 71.83  ? 802  LEU A CD2   1 
ATOM   6425  N N     . GLY B 2 806  ? 175.850 172.890 140.731 1.00 71.32  ? 803  GLY A N     1 
ATOM   6426  C CA    . GLY B 2 806  ? 176.776 173.146 139.651 1.00 71.32  ? 803  GLY A CA    1 
ATOM   6427  C C     . GLY B 2 806  ? 176.505 172.375 138.378 1.00 71.32  ? 803  GLY A C     1 
ATOM   6428  O O     . GLY B 2 806  ? 177.086 172.708 137.337 1.00 71.32  ? 803  GLY A O     1 
ATOM   6429  N N     . GLU B 2 807  ? 175.646 171.361 138.424 1.00 71.95  ? 804  GLU A N     1 
ATOM   6430  C CA    . GLU B 2 807  ? 175.287 170.606 137.235 1.00 71.95  ? 804  GLU A CA    1 
ATOM   6431  C C     . GLU B 2 807  ? 174.109 171.273 136.528 1.00 71.95  ? 804  GLU A C     1 
ATOM   6432  O O     . GLU B 2 807  ? 173.686 172.381 136.870 1.00 71.95  ? 804  GLU A O     1 
ATOM   6433  C CB    . GLU B 2 807  ? 174.964 169.160 137.602 1.00 71.94  ? 804  GLU A CB    1 
ATOM   6434  C CG    . GLU B 2 807  ? 176.086 168.437 138.326 1.00 71.94  ? 804  GLU A CG    1 
ATOM   6435  C CD    . GLU B 2 807  ? 175.918 166.930 138.300 1.00 71.94  ? 804  GLU A CD    1 
ATOM   6436  O OE1   . GLU B 2 807  ? 174.809 166.459 137.972 1.00 71.94  ? 804  GLU A OE1   1 
ATOM   6437  O OE2   . GLU B 2 807  ? 176.896 166.216 138.608 1.00 71.94  ? 804  GLU A OE2   1 
ATOM   6438  N N     . LYS B 2 808  ? 173.575 170.591 135.520 1.00 63.69  ? 805  LYS A N     1 
ATOM   6439  C CA    . LYS B 2 808  ? 172.417 171.061 134.773 1.00 63.69  ? 805  LYS A CA    1 
ATOM   6440  C C     . LYS B 2 808  ? 171.341 169.985 134.783 1.00 63.69  ? 805  LYS A C     1 
ATOM   6441  O O     . LYS B 2 808  ? 171.626 168.816 134.502 1.00 63.69  ? 805  LYS A O     1 
ATOM   6442  C CB    . LYS B 2 808  ? 172.800 171.416 133.335 1.00 63.69  ? 805  LYS A CB    1 
ATOM   6443  C CG    . LYS B 2 808  ? 174.071 172.243 133.215 1.00 63.69  ? 805  LYS A CG    1 
ATOM   6444  C CD    . LYS B 2 808  ? 173.915 173.356 132.192 1.00 63.69  ? 805  LYS A CD    1 
ATOM   6445  C CE    . LYS B 2 808  ? 175.196 174.163 132.056 1.00 63.69  ? 805  LYS A CE    1 
ATOM   6446  N NZ    . LYS B 2 808  ? 176.326 173.334 131.552 1.00 63.69  ? 805  LYS A NZ    1 
ATOM   6447  N N     . MET B 2 809  ? 170.110 170.378 135.102 1.00 60.43  ? 806  MET A N     1 
ATOM   6448  C CA    . MET B 2 809  ? 168.965 169.469 135.107 1.00 60.43  ? 806  MET A CA    1 
ATOM   6449  C C     . MET B 2 809  ? 168.204 169.670 133.803 1.00 60.43  ? 806  MET A C     1 
ATOM   6450  O O     . MET B 2 809  ? 167.535 170.691 133.617 1.00 60.43  ? 806  MET A O     1 
ATOM   6451  C CB    . MET B 2 809  ? 168.055 169.706 136.308 1.00 60.43  ? 806  MET A CB    1 
ATOM   6452  C CG    . MET B 2 809  ? 168.669 169.377 137.651 1.00 60.43  ? 806  MET A CG    1 
ATOM   6453  S SD    . MET B 2 809  ? 167.488 169.628 138.989 1.00 60.43  ? 806  MET A SD    1 
ATOM   6454  C CE    . MET B 2 809  ? 167.441 171.415 139.078 1.00 60.43  ? 806  MET A CE    1 
ATOM   6455  N N     . LEU B 2 810  ? 168.303 168.699 132.903 1.00 56.89  ? 807  LEU A N     1 
ATOM   6456  C CA    . LEU B 2 810  ? 167.571 168.763 131.651 1.00 56.89  ? 807  LEU A CA    1 
ATOM   6457  C C     . LEU B 2 810  ? 166.140 168.281 131.844 1.00 56.89  ? 807  LEU A C     1 
ATOM   6458  O O     . LEU B 2 810  ? 165.878 167.308 132.557 1.00 56.89  ? 807  LEU A O     1 
ATOM   6459  C CB    . LEU B 2 810  ? 168.263 167.922 130.580 1.00 56.89  ? 807  LEU A CB    1 
ATOM   6460  C CG    . LEU B 2 810  ? 167.991 168.340 129.137 1.00 56.89  ? 807  LEU A CG    1 
ATOM   6461  C CD1   . LEU B 2 810  ? 168.762 169.604 128.788 1.00 56.89  ? 807  LEU A CD1   1 
ATOM   6462  C CD2   . LEU B 2 810  ? 168.337 167.213 128.185 1.00 56.89  ? 807  LEU A CD2   1 
ATOM   6463  N N     . ASN B 2 811  ? 165.209 168.976 131.201 1.00 53.19  ? 808  ASN A N     1 
ATOM   6464  C CA    . ASN B 2 811  ? 163.812 168.583 131.251 1.00 53.19  ? 808  ASN A CA    1 
ATOM   6465  C C     . ASN B 2 811  ? 163.556 167.402 130.321 1.00 53.19  ? 808  ASN A C     1 
ATOM   6466  O O     . ASN B 2 811  ? 164.297 167.154 129.366 1.00 53.19  ? 808  ASN A O     1 
ATOM   6467  C CB    . ASN B 2 811  ? 162.908 169.753 130.866 1.00 53.19  ? 808  ASN A CB    1 
ATOM   6468  C CG    . ASN B 2 811  ? 162.538 170.617 132.050 1.00 53.19  ? 808  ASN A CG    1 
ATOM   6469  O OD1   . ASN B 2 811  ? 163.024 170.409 133.162 1.00 53.19  ? 808  ASN A OD1   1 
ATOM   6470  N ND2   . ASN B 2 811  ? 161.671 171.595 131.820 1.00 53.19  ? 808  ASN A ND2   1 
ATOM   6471  N N     . LYS B 2 812  ? 162.487 166.668 130.612 1.00 49.88  ? 809  LYS A N     1 
ATOM   6472  C CA    . LYS B 2 812  ? 162.061 165.555 129.778 1.00 49.88  ? 809  LYS A CA    1 
ATOM   6473  C C     . LYS B 2 812  ? 161.012 165.961 128.754 1.00 49.88  ? 809  LYS A C     1 
ATOM   6474  O O     . LYS B 2 812  ? 160.488 165.096 128.046 1.00 49.88  ? 809  LYS A O     1 
ATOM   6475  C CB    . LYS B 2 812  ? 161.527 164.412 130.645 1.00 49.88  ? 809  LYS A CB    1 
ATOM   6476  C CG    . LYS B 2 812  ? 162.603 163.477 131.166 1.00 49.88  ? 809  LYS A CG    1 
ATOM   6477  C CD    . LYS B 2 812  ? 162.002 162.190 131.705 1.00 49.88  ? 809  LYS A CD    1 
ATOM   6478  C CE    . LYS B 2 812  ? 162.894 161.561 132.762 1.00 49.88  ? 809  LYS A CE    1 
ATOM   6479  N NZ    . LYS B 2 812  ? 162.545 162.021 134.134 1.00 49.88  ? 809  LYS A NZ    1 
ATOM   6480  N N     . LYS B 2 813  ? 160.697 167.250 128.659 1.00 51.57  ? 810  LYS A N     1 
ATOM   6481  C CA    . LYS B 2 813  ? 159.736 167.746 127.687 1.00 51.57  ? 810  LYS A CA    1 
ATOM   6482  C C     . LYS B 2 813  ? 160.354 168.909 126.927 1.00 51.57  ? 810  LYS A C     1 
ATOM   6483  O O     . LYS B 2 813  ? 161.267 169.581 127.413 1.00 51.57  ? 810  LYS A O     1 
ATOM   6484  C CB    . LYS B 2 813  ? 158.424 168.180 128.352 1.00 51.58  ? 810  LYS A CB    1 
ATOM   6485  C CG    . LYS B 2 813  ? 157.671 167.050 129.031 1.00 51.58  ? 810  LYS A CG    1 
ATOM   6486  C CD    . LYS B 2 813  ? 156.250 167.462 129.371 1.00 51.58  ? 810  LYS A CD    1 
ATOM   6487  C CE    . LYS B 2 813  ? 156.220 168.456 130.516 1.00 51.58  ? 810  LYS A CE    1 
ATOM   6488  N NZ    . LYS B 2 813  ? 154.827 168.780 130.924 1.00 51.58  ? 810  LYS A NZ    1 
ATOM   6489  N N     . LEU B 2 814  ? 159.843 169.140 125.722 1.00 54.85  ? 811  LEU A N     1 
ATOM   6490  C CA    . LEU B 2 814  ? 160.374 170.174 124.846 1.00 54.85  ? 811  LEU A CA    1 
ATOM   6491  C C     . LEU B 2 814  ? 159.812 171.532 125.271 1.00 54.85  ? 811  LEU A C     1 
ATOM   6492  O O     . LEU B 2 814  ? 159.216 171.678 126.342 1.00 54.85  ? 811  LEU A O     1 
ATOM   6493  C CB    . LEU B 2 814  ? 160.053 169.853 123.388 1.00 54.85  ? 811  LEU A CB    1 
ATOM   6494  C CG    . LEU B 2 814  ? 160.949 168.879 122.612 1.00 54.85  ? 811  LEU A CG    1 
ATOM   6495  C CD1   . LEU B 2 814  ? 162.356 169.423 122.471 1.00 54.85  ? 811  LEU A CD1   1 
ATOM   6496  C CD2   . LEU B 2 814  ? 160.964 167.485 123.214 1.00 54.85  ? 811  LEU A CD2   1 
ATOM   6497  N N     . LYS B 2 815  ? 160.002 172.552 124.429 1.00 58.06  ? 812  LYS A N     1 
ATOM   6498  C CA    . LYS B 2 815  ? 159.495 173.883 124.750 1.00 58.06  ? 812  LYS A CA    1 
ATOM   6499  C C     . LYS B 2 815  ? 157.972 173.922 124.792 1.00 58.06  ? 812  LYS A C     1 
ATOM   6500  O O     . LYS B 2 815  ? 157.397 174.645 125.613 1.00 58.06  ? 812  LYS A O     1 
ATOM   6501  C CB    . LYS B 2 815  ? 160.019 174.908 123.744 1.00 58.06  ? 812  LYS A CB    1 
ATOM   6502  C CG    . LYS B 2 815  ? 161.530 174.935 123.610 1.00 58.06  ? 812  LYS A CG    1 
ATOM   6503  C CD    . LYS B 2 815  ? 162.013 176.261 123.045 1.00 58.06  ? 812  LYS A CD    1 
ATOM   6504  C CE    . LYS B 2 815  ? 162.068 177.333 124.122 1.00 58.06  ? 812  LYS A CE    1 
ATOM   6505  N NZ    . LYS B 2 815  ? 163.213 177.128 125.053 1.00 58.06  ? 812  LYS A NZ    1 
ATOM   6506  N N     . ASP B 2 816  ? 157.303 173.159 123.925 1.00 55.29  ? 813  ASP A N     1 
ATOM   6507  C CA    . ASP B 2 816  ? 155.844 173.159 123.904 1.00 55.29  ? 813  ASP A CA    1 
ATOM   6508  C C     . ASP B 2 816  ? 155.238 172.484 125.127 1.00 55.29  ? 813  ASP A C     1 
ATOM   6509  O O     . ASP B 2 816  ? 154.015 172.541 125.299 1.00 55.29  ? 813  ASP A O     1 
ATOM   6510  C CB    . ASP B 2 816  ? 155.332 172.485 122.629 1.00 55.29  ? 813  ASP A CB    1 
ATOM   6511  C CG    . ASP B 2 816  ? 156.046 171.187 122.328 1.00 55.29  ? 813  ASP A CG    1 
ATOM   6512  O OD1   . ASP B 2 816  ? 157.248 171.083 122.646 1.00 55.29  ? 813  ASP A OD1   1 
ATOM   6513  O OD2   . ASP B 2 816  ? 155.407 170.271 121.770 1.00 55.29  ? 813  ASP A OD2   1 
ATOM   6514  N N     . GLN B 2 817  ? 156.054 171.836 125.958 1.00 57.12  ? 814  GLN A N     1 
ATOM   6515  C CA    . GLN B 2 817  ? 155.669 171.264 127.245 1.00 57.12  ? 814  GLN A CA    1 
ATOM   6516  C C     . GLN B 2 817  ? 154.688 170.107 127.119 1.00 57.12  ? 814  GLN A C     1 
ATOM   6517  O O     . GLN B 2 817  ? 153.984 169.801 128.087 1.00 57.12  ? 814  GLN A O     1 
ATOM   6518  C CB    . GLN B 2 817  ? 155.077 172.324 128.183 1.00 57.12  ? 814  GLN A CB    1 
ATOM   6519  C CG    . GLN B 2 817  ? 155.978 173.528 128.413 1.00 57.12  ? 814  GLN A CG    1 
ATOM   6520  C CD    . GLN B 2 817  ? 157.083 173.252 129.412 1.00 57.12  ? 814  GLN A CD    1 
ATOM   6521  O OE1   . GLN B 2 817  ? 157.075 172.231 130.099 1.00 57.12  ? 814  GLN A OE1   1 
ATOM   6522  N NE2   . GLN B 2 817  ? 158.044 174.165 129.498 1.00 57.12  ? 814  GLN A NE2   1 
ATOM   6523  N N     . LYS B 2 818  ? 154.618 169.450 125.961 1.00 51.95  ? 815  LYS A N     1 
ATOM   6524  C CA    . LYS B 2 818  ? 153.723 168.316 125.788 1.00 51.95  ? 815  LYS A CA    1 
ATOM   6525  C C     . LYS B 2 818  ? 154.357 167.113 125.107 1.00 51.95  ? 815  LYS A C     1 
ATOM   6526  O O     . LYS B 2 818  ? 153.779 166.023 125.174 1.00 51.95  ? 815  LYS A O     1 
ATOM   6527  C CB    . LYS B 2 818  ? 152.475 168.730 124.991 1.00 51.94  ? 815  LYS A CB    1 
ATOM   6528  C CG    . LYS B 2 818  ? 152.760 169.148 123.557 1.00 51.94  ? 815  LYS A CG    1 
ATOM   6529  C CD    . LYS B 2 818  ? 151.478 169.515 122.822 1.00 51.94  ? 815  LYS A CD    1 
ATOM   6530  C CE    . LYS B 2 818  ? 150.652 170.521 123.607 1.00 51.94  ? 815  LYS A CE    1 
ATOM   6531  N NZ    . LYS B 2 818  ? 149.793 171.350 122.716 1.00 51.94  ? 815  LYS A NZ    1 
ATOM   6532  N N     . THR B 2 819  ? 155.515 167.261 124.468 1.00 53.34  ? 816  THR A N     1 
ATOM   6533  C CA    . THR B 2 819  ? 156.150 166.155 123.757 1.00 53.34  ? 816  THR A CA    1 
ATOM   6534  C C     . THR B 2 819  ? 157.364 165.663 124.531 1.00 53.34  ? 816  THR A C     1 
ATOM   6535  O O     . THR B 2 819  ? 158.381 166.369 124.603 1.00 53.34  ? 816  THR A O     1 
ATOM   6536  C CB    . THR B 2 819  ? 156.556 166.584 122.344 1.00 53.34  ? 816  THR A CB    1 
ATOM   6537  O OG1   . THR B 2 819  ? 157.505 167.655 122.420 1.00 53.34  ? 816  THR A OG1   1 
ATOM   6538  C CG2   . THR B 2 819  ? 155.338 167.039 121.554 1.00 53.34  ? 816  THR A CG2   1 
ATOM   6539  N N     . PRO B 2 820  ? 157.310 164.480 125.139 1.00 48.55  ? 817  PRO A N     1 
ATOM   6540  C CA    . PRO B 2 820  ? 158.489 163.961 125.841 1.00 48.55  ? 817  PRO A CA    1 
ATOM   6541  C C     . PRO B 2 820  ? 159.611 163.598 124.881 1.00 48.55  ? 817  PRO A C     1 
ATOM   6542  O O     . PRO B 2 820  ? 159.376 163.165 123.751 1.00 48.55  ? 817  PRO A O     1 
ATOM   6543  C CB    . PRO B 2 820  ? 157.955 162.721 126.568 1.00 48.55  ? 817  PRO A CB    1 
ATOM   6544  C CG    . PRO B 2 820  ? 156.706 162.356 125.840 1.00 48.55  ? 817  PRO A CG    1 
ATOM   6545  C CD    . PRO B 2 820  ? 156.120 163.648 125.371 1.00 48.55  ? 817  PRO A CD    1 
ATOM   6546  N N     . ILE B 2 821  ? 160.839 163.786 125.348 1.00 48.55  ? 818  ILE A N     1 
ATOM   6547  C CA    . ILE B 2 821  ? 162.023 163.335 124.608 1.00 48.55  ? 818  ILE A CA    1 
ATOM   6548  C C     . ILE B 2 821  ? 162.081 161.812 124.647 1.00 48.55  ? 818  ILE A C     1 
ATOM   6549  O O     . ILE B 2 821  ? 161.662 161.211 125.653 1.00 48.55  ? 818  ILE A O     1 
ATOM   6550  C CB    . ILE B 2 821  ? 163.286 163.954 125.216 1.00 48.55  ? 818  ILE A CB    1 
ATOM   6551  C CG1   . ILE B 2 821  ? 163.273 165.471 125.046 1.00 48.55  ? 818  ILE A CG1   1 
ATOM   6552  C CG2   . ILE B 2 821  ? 164.548 163.384 124.591 1.00 48.55  ? 818  ILE A CG2   1 
ATOM   6553  C CD1   . ILE B 2 821  ? 164.556 166.139 125.475 1.00 48.55  ? 818  ILE A CD1   1 
ATOM   6554  N N     . PRO B 2 822  ? 162.559 161.143 123.596 1.00 50.97  ? 819  PRO A N     1 
ATOM   6555  C CA    . PRO B 2 822  ? 162.795 159.698 123.697 1.00 50.97  ? 819  PRO A CA    1 
ATOM   6556  C C     . PRO B 2 822  ? 163.781 159.385 124.813 1.00 50.97  ? 819  PRO A C     1 
ATOM   6557  O O     . PRO B 2 822  ? 164.684 160.170 125.108 1.00 50.97  ? 819  PRO A O     1 
ATOM   6558  C CB    . PRO B 2 822  ? 163.362 159.334 122.322 1.00 50.97  ? 819  PRO A CB    1 
ATOM   6559  C CG    . PRO B 2 822  ? 162.815 160.371 121.409 1.00 50.97  ? 819  PRO A CG    1 
ATOM   6560  C CD    . PRO B 2 822  ? 162.708 161.633 122.214 1.00 50.97  ? 819  PRO A CD    1 
ATOM   6561  N N     . ASP B 2 823  ? 163.593 158.221 125.438 1.00 58.27  ? 820  ASP A N     1 
ATOM   6562  C CA    . ASP B 2 823  ? 164.367 157.875 126.627 1.00 58.27  ? 820  ASP A CA    1 
ATOM   6563  C C     . ASP B 2 823  ? 165.859 157.809 126.323 1.00 58.27  ? 820  ASP A C     1 
ATOM   6564  O O     . ASP B 2 823  ? 166.686 158.289 127.108 1.00 58.27  ? 820  ASP A O     1 
ATOM   6565  C CB    . ASP B 2 823  ? 163.875 156.546 127.201 1.00 58.27  ? 820  ASP A CB    1 
ATOM   6566  C CG    . ASP B 2 823  ? 162.390 156.555 127.501 1.00 58.27  ? 820  ASP A CG    1 
ATOM   6567  O OD1   . ASP B 2 823  ? 161.591 156.692 126.551 1.00 58.27  ? 820  ASP A OD1   1 
ATOM   6568  O OD2   . ASP B 2 823  ? 162.020 156.424 128.687 1.00 58.27  ? 820  ASP A OD2   1 
ATOM   6569  N N     . THR B 2 824  ? 166.226 157.212 125.187 1.00 56.45  ? 821  THR A N     1 
ATOM   6570  C CA    . THR B 2 824  ? 167.641 157.082 124.853 1.00 56.45  ? 821  THR A CA    1 
ATOM   6571  C C     . THR B 2 824  ? 168.262 158.433 124.518 1.00 56.45  ? 821  THR A C     1 
ATOM   6572  O O     . THR B 2 824  ? 169.434 158.675 124.828 1.00 56.45  ? 821  THR A O     1 
ATOM   6573  C CB    . THR B 2 824  ? 167.824 156.098 123.696 1.00 56.45  ? 821  THR A CB    1 
ATOM   6574  O OG1   . THR B 2 824  ? 169.201 156.075 123.298 1.00 56.45  ? 821  THR A OG1   1 
ATOM   6575  C CG2   . THR B 2 824  ? 166.956 156.484 122.506 1.00 56.45  ? 821  THR A CG2   1 
ATOM   6576  N N     . LEU B 2 825  ? 167.497 159.325 123.887 1.00 57.93  ? 822  LEU A N     1 
ATOM   6577  C CA    . LEU B 2 825  ? 168.045 160.625 123.514 1.00 57.93  ? 822  LEU A CA    1 
ATOM   6578  C C     . LEU B 2 825  ? 168.179 161.543 124.722 1.00 57.93  ? 822  LEU A C     1 
ATOM   6579  O O     . LEU B 2 825  ? 169.130 162.328 124.806 1.00 57.93  ? 822  LEU A O     1 
ATOM   6580  C CB    . LEU B 2 825  ? 167.177 161.272 122.437 1.00 57.93  ? 822  LEU A CB    1 
ATOM   6581  C CG    . LEU B 2 825  ? 167.163 160.543 121.093 1.00 57.93  ? 822  LEU A CG    1 
ATOM   6582  C CD1   . LEU B 2 825  ? 166.169 161.183 120.135 1.00 57.93  ? 822  LEU A CD1   1 
ATOM   6583  C CD2   . LEU B 2 825  ? 168.558 160.511 120.489 1.00 57.93  ? 822  LEU A CD2   1 
ATOM   6584  N N     . TYR B 2 826  ? 167.236 161.466 125.665 1.00 60.75  ? 823  TYR A N     1 
ATOM   6585  C CA    . TYR B 2 826  ? 167.288 162.341 126.832 1.00 60.75  ? 823  TYR A CA    1 
ATOM   6586  C C     . TYR B 2 826  ? 168.523 162.061 127.678 1.00 60.75  ? 823  TYR A C     1 
ATOM   6587  O O     . TYR B 2 826  ? 169.170 162.991 128.173 1.00 60.75  ? 823  TYR A O     1 
ATOM   6588  C CB    . TYR B 2 826  ? 166.020 162.184 127.670 1.00 60.75  ? 823  TYR A CB    1 
ATOM   6589  C CG    . TYR B 2 826  ? 166.146 162.726 129.076 1.00 60.75  ? 823  TYR A CG    1 
ATOM   6590  C CD1   . TYR B 2 826  ? 166.261 164.090 129.307 1.00 60.75  ? 823  TYR A CD1   1 
ATOM   6591  C CD2   . TYR B 2 826  ? 166.147 161.875 130.173 1.00 60.75  ? 823  TYR A CD2   1 
ATOM   6592  C CE1   . TYR B 2 826  ? 166.376 164.591 130.589 1.00 60.75  ? 823  TYR A CE1   1 
ATOM   6593  C CE2   . TYR B 2 826  ? 166.261 162.367 131.459 1.00 60.75  ? 823  TYR A CE2   1 
ATOM   6594  C CZ    . TYR B 2 826  ? 166.375 163.725 131.661 1.00 60.75  ? 823  TYR A CZ    1 
ATOM   6595  O OH    . TYR B 2 826  ? 166.489 164.220 132.940 1.00 60.75  ? 823  TYR A OH    1 
ATOM   6596  N N     . GLN B 2 827  ? 168.860 160.782 127.862 1.00 63.77  ? 824  GLN A N     1 
ATOM   6597  C CA    . GLN B 2 827  ? 170.052 160.436 128.628 1.00 63.77  ? 824  GLN A CA    1 
ATOM   6598  C C     . GLN B 2 827  ? 171.313 160.944 127.941 1.00 63.77  ? 824  GLN A C     1 
ATOM   6599  O O     . GLN B 2 827  ? 172.230 161.444 128.603 1.00 63.77  ? 824  GLN A O     1 
ATOM   6600  C CB    . GLN B 2 827  ? 170.120 158.923 128.832 1.00 63.77  ? 824  GLN A CB    1 
ATOM   6601  C CG    . GLN B 2 827  ? 171.257 158.466 129.728 1.00 63.77  ? 824  GLN A CG    1 
ATOM   6602  C CD    . GLN B 2 827  ? 171.266 156.964 129.933 1.00 63.77  ? 824  GLN A CD    1 
ATOM   6603  O OE1   . GLN B 2 827  ? 170.436 156.244 129.377 1.00 63.77  ? 824  GLN A OE1   1 
ATOM   6604  N NE2   . GLN B 2 827  ? 172.207 156.482 130.737 1.00 63.77  ? 824  GLN A NE2   1 
ATOM   6605  N N     . GLU B 2 828  ? 171.379 160.819 126.614 1.00 67.44  ? 825  GLU A N     1 
ATOM   6606  C CA    . GLU B 2 828  ? 172.536 161.323 125.880 1.00 67.44  ? 825  GLU A CA    1 
ATOM   6607  C C     . GLU B 2 828  ? 172.636 162.839 125.980 1.00 67.44  ? 825  GLU A C     1 
ATOM   6608  O O     . GLU B 2 828  ? 173.730 163.385 126.168 1.00 67.44  ? 825  GLU A O     1 
ATOM   6609  C CB    . GLU B 2 828  ? 172.458 160.885 124.418 1.00 67.44  ? 825  GLU A CB    1 
ATOM   6610  C CG    . GLU B 2 828  ? 172.811 159.425 124.188 1.00 67.44  ? 825  GLU A CG    1 
ATOM   6611  C CD    . GLU B 2 828  ? 174.305 159.176 124.202 1.00 67.44  ? 825  GLU A CD    1 
ATOM   6612  O OE1   . GLU B 2 828  ? 174.985 159.585 123.237 1.00 67.44  ? 825  GLU A OE1   1 
ATOM   6613  O OE2   . GLU B 2 828  ? 174.800 158.570 125.175 1.00 67.44  ? 825  GLU A OE2   1 
ATOM   6614  N N     . LEU B 2 829  ? 171.507 163.539 125.850 1.00 66.66  ? 826  LEU A N     1 
ATOM   6615  C CA    . LEU B 2 829  ? 171.521 164.993 125.980 1.00 66.66  ? 826  LEU A CA    1 
ATOM   6616  C C     . LEU B 2 829  ? 171.886 165.419 127.396 1.00 66.66  ? 826  LEU A C     1 
ATOM   6617  O O     . LEU B 2 829  ? 172.602 166.409 127.585 1.00 66.66  ? 826  LEU A O     1 
ATOM   6618  C CB    . LEU B 2 829  ? 170.167 165.575 125.577 1.00 66.66  ? 826  LEU A CB    1 
ATOM   6619  C CG    . LEU B 2 829  ? 169.765 165.449 124.109 1.00 66.66  ? 826  LEU A CG    1 
ATOM   6620  C CD1   . LEU B 2 829  ? 168.344 165.943 123.902 1.00 66.66  ? 826  LEU A CD1   1 
ATOM   6621  C CD2   . LEU B 2 829  ? 170.733 166.220 123.229 1.00 66.66  ? 826  LEU A CD2   1 
ATOM   6622  N N     . TYR B 2 830  ? 171.396 164.690 128.403 1.00 66.62  ? 827  TYR A N     1 
ATOM   6623  C CA    . TYR B 2 830  ? 171.736 165.015 129.785 1.00 66.62  ? 827  TYR A CA    1 
ATOM   6624  C C     . TYR B 2 830  ? 173.235 164.899 130.023 1.00 66.62  ? 827  TYR A C     1 
ATOM   6625  O O     . TYR B 2 830  ? 173.830 165.741 130.706 1.00 66.62  ? 827  TYR A O     1 
ATOM   6626  C CB    . TYR B 2 830  ? 170.972 164.103 130.743 1.00 66.62  ? 827  TYR A CB    1 
ATOM   6627  C CG    . TYR B 2 830  ? 171.213 164.412 132.204 1.00 66.62  ? 827  TYR A CG    1 
ATOM   6628  C CD1   . TYR B 2 830  ? 170.539 165.447 132.834 1.00 66.62  ? 827  TYR A CD1   1 
ATOM   6629  C CD2   . TYR B 2 830  ? 172.114 163.666 132.951 1.00 66.62  ? 827  TYR A CD2   1 
ATOM   6630  C CE1   . TYR B 2 830  ? 170.755 165.733 134.168 1.00 66.62  ? 827  TYR A CE1   1 
ATOM   6631  C CE2   . TYR B 2 830  ? 172.338 163.944 134.285 1.00 66.62  ? 827  TYR A CE2   1 
ATOM   6632  C CZ    . TYR B 2 830  ? 171.656 164.979 134.888 1.00 66.62  ? 827  TYR A CZ    1 
ATOM   6633  O OH    . TYR B 2 830  ? 171.875 165.259 136.217 1.00 66.62  ? 827  TYR A OH    1 
ATOM   6634  N N     . ASP B 2 831  ? 173.862 163.860 129.470 1.00 70.79  ? 828  ASP A N     1 
ATOM   6635  C CA    . ASP B 2 831  ? 175.306 163.712 129.609 1.00 70.79  ? 828  ASP A CA    1 
ATOM   6636  C C     . ASP B 2 831  ? 176.056 164.788 128.834 1.00 70.79  ? 828  ASP A C     1 
ATOM   6637  O O     . ASP B 2 831  ? 177.128 165.226 129.267 1.00 70.79  ? 828  ASP A O     1 
ATOM   6638  C CB    . ASP B 2 831  ? 175.737 162.322 129.142 1.00 70.79  ? 828  ASP A CB    1 
ATOM   6639  C CG    . ASP B 2 831  ? 175.232 161.219 130.052 1.00 70.79  ? 828  ASP A CG    1 
ATOM   6640  O OD1   . ASP B 2 831  ? 175.051 161.478 131.260 1.00 70.79  ? 828  ASP A OD1   1 
ATOM   6641  O OD2   . ASP B 2 831  ? 175.016 160.092 129.558 1.00 70.79  ? 828  ASP A OD2   1 
ATOM   6642  N N     . TYR B 2 832  ? 175.516 165.221 127.695 1.00 75.11  ? 829  TYR A N     1 
ATOM   6643  C CA    . TYR B 2 832  ? 176.192 166.223 126.878 1.00 75.11  ? 829  TYR A CA    1 
ATOM   6644  C C     . TYR B 2 832  ? 176.096 167.612 127.501 1.00 75.11  ? 829  TYR A C     1 
ATOM   6645  O O     . TYR B 2 832  ? 177.101 168.320 127.622 1.00 75.11  ? 829  TYR A O     1 
ATOM   6646  C CB    . TYR B 2 832  ? 175.605 166.232 125.465 1.00 75.11  ? 829  TYR A CB    1 
ATOM   6647  C CG    . TYR B 2 832  ? 176.217 167.275 124.562 1.00 75.11  ? 829  TYR A CG    1 
ATOM   6648  C CD1   . TYR B 2 832  ? 177.465 167.076 123.987 1.00 75.11  ? 829  TYR A CD1   1 
ATOM   6649  C CD2   . TYR B 2 832  ? 175.553 168.463 124.290 1.00 75.11  ? 829  TYR A CD2   1 
ATOM   6650  C CE1   . TYR B 2 832  ? 178.032 168.027 123.161 1.00 75.11  ? 829  TYR A CE1   1 
ATOM   6651  C CE2   . TYR B 2 832  ? 176.113 169.421 123.466 1.00 75.11  ? 829  TYR A CE2   1 
ATOM   6652  C CZ    . TYR B 2 832  ? 177.352 169.198 122.904 1.00 75.11  ? 829  TYR A CZ    1 
ATOM   6653  O OH    . TYR B 2 832  ? 177.912 170.149 122.083 1.00 75.11  ? 829  TYR A OH    1 
ATOM   6654  N N     . VAL B 2 833  ? 174.886 168.020 127.896 1.00 69.66  ? 830  VAL A N     1 
ATOM   6655  C CA    . VAL B 2 833  ? 174.701 169.353 128.462 1.00 69.66  ? 830  VAL A CA    1 
ATOM   6656  C C     . VAL B 2 833  ? 175.434 169.480 129.790 1.00 69.66  ? 830  VAL A C     1 
ATOM   6657  O O     . VAL B 2 833  ? 175.858 170.578 130.173 1.00 69.66  ? 830  VAL A O     1 
ATOM   6658  C CB    . VAL B 2 833  ? 173.198 169.676 128.600 1.00 69.66  ? 830  VAL A CB    1 
ATOM   6659  C CG1   . VAL B 2 833  ? 172.558 168.840 129.700 1.00 69.66  ? 830  VAL A CG1   1 
ATOM   6660  C CG2   . VAL B 2 833  ? 172.991 171.162 128.856 1.00 69.66  ? 830  VAL A CG2   1 
ATOM   6661  N N     . ASN B 2 834  ? 175.606 168.371 130.506 1.00 74.33  ? 831  ASN A N     1 
ATOM   6662  C CA    . ASN B 2 834  ? 176.364 168.365 131.749 1.00 74.33  ? 831  ASN A CA    1 
ATOM   6663  C C     . ASN B 2 834  ? 177.853 168.136 131.521 1.00 74.33  ? 831  ASN A C     1 
ATOM   6664  O O     . ASN B 2 834  ? 178.607 168.055 132.498 1.00 74.33  ? 831  ASN A O     1 
ATOM   6665  C CB    . ASN B 2 834  ? 175.808 167.298 132.695 1.00 74.33  ? 831  ASN A CB    1 
ATOM   6666  C CG    . ASN B 2 834  ? 176.093 167.602 134.151 1.00 74.33  ? 831  ASN A CG    1 
ATOM   6667  O OD1   . ASN B 2 834  ? 176.669 168.639 134.480 1.00 74.33  ? 831  ASN A OD1   1 
ATOM   6668  N ND2   . ASN B 2 834  ? 175.680 166.701 135.034 1.00 74.33  ? 831  ASN A ND2   1 
ATOM   6669  N N     . HIS B 2 835  ? 178.280 168.016 130.262 1.00 75.15  ? 832  HIS A N     1 
ATOM   6670  C CA    . HIS B 2 835  ? 179.691 167.869 129.900 1.00 75.15  ? 832  HIS A CA    1 
ATOM   6671  C C     . HIS B 2 835  ? 180.279 166.579 130.469 1.00 75.15  ? 832  HIS A C     1 
ATOM   6672  O O     . HIS B 2 835  ? 181.312 166.580 131.142 1.00 75.15  ? 832  HIS A O     1 
ATOM   6673  C CB    . HIS B 2 835  ? 180.500 169.090 130.343 1.00 75.15  ? 832  HIS A CB    1 
ATOM   6674  C CG    . HIS B 2 835  ? 180.125 170.352 129.631 1.00 75.15  ? 832  HIS A CG    1 
ATOM   6675  N ND1   . HIS B 2 835  ? 179.127 171.190 130.081 1.00 75.15  ? 832  HIS A ND1   1 
ATOM   6676  C CD2   . HIS B 2 835  ? 180.611 170.918 128.502 1.00 75.15  ? 832  HIS A CD2   1 
ATOM   6677  C CE1   . HIS B 2 835  ? 179.015 172.218 129.259 1.00 75.15  ? 832  HIS A CE1   1 
ATOM   6678  N NE2   . HIS B 2 835  ? 179.904 172.078 128.293 1.00 75.15  ? 832  HIS A NE2   1 
ATOM   6679  N N     . ARG B 2 836  ? 179.604 165.463 130.190 1.00 80.40  ? 833  ARG A N     1 
ATOM   6680  C CA    . ARG B 2 836  ? 180.064 164.154 130.629 1.00 80.40  ? 833  ARG A CA    1 
ATOM   6681  C C     . ARG B 2 836  ? 180.075 163.105 129.524 1.00 80.40  ? 833  ARG A C     1 
ATOM   6682  O O     . ARG B 2 836  ? 180.637 162.025 129.734 1.00 80.40  ? 833  ARG A O     1 
ATOM   6683  C CB    . ARG B 2 836  ? 179.201 163.647 131.796 1.00 80.40  ? 833  ARG A CB    1 
ATOM   6684  C CG    . ARG B 2 836  ? 179.860 162.573 132.651 1.00 80.40  ? 833  ARG A CG    1 
ATOM   6685  C CD    . ARG B 2 836  ? 178.993 162.188 133.838 1.00 80.40  ? 833  ARG A CD    1 
ATOM   6686  N NE    . ARG B 2 836  ? 178.901 163.262 134.820 1.00 80.40  ? 833  ARG A NE    1 
ATOM   6687  C CZ    . ARG B 2 836  ? 177.792 163.935 135.094 1.00 80.40  ? 833  ARG A CZ    1 
ATOM   6688  N NH1   . ARG B 2 836  ? 176.654 163.676 134.471 1.00 80.40  ? 833  ARG A NH1   1 
ATOM   6689  N NH2   . ARG B 2 836  ? 177.826 164.891 136.018 1.00 80.40  ? 833  ARG A NH2   1 
ATOM   6690  N N     . LEU B 2 837  ? 179.497 163.387 128.360 1.00 92.33  ? 834  LEU A N     1 
ATOM   6691  C CA    . LEU B 2 837  ? 179.448 162.427 127.264 1.00 92.33  ? 834  LEU A CA    1 
ATOM   6692  C C     . LEU B 2 837  ? 180.707 162.562 126.417 1.00 92.33  ? 834  LEU A C     1 
ATOM   6693  O O     . LEU B 2 837  ? 180.949 163.616 125.817 1.00 92.33  ? 834  LEU A O     1 
ATOM   6694  C CB    . LEU B 2 837  ? 178.200 162.643 126.410 1.00 92.33  ? 834  LEU A CB    1 
ATOM   6695  C CG    . LEU B 2 837  ? 177.979 161.639 125.278 1.00 92.33  ? 834  LEU A CG    1 
ATOM   6696  C CD1   . LEU B 2 837  ? 177.725 160.247 125.836 1.00 92.33  ? 834  LEU A CD1   1 
ATOM   6697  C CD2   . LEU B 2 837  ? 176.831 162.080 124.387 1.00 92.33  ? 834  LEU A CD2   1 
ATOM   6698  N N     . SER B 2 838  ? 181.504 161.495 126.366 1.00 107.97 ? 835  SER A N     1 
ATOM   6699  C CA    . SER B 2 838  ? 182.738 161.499 125.591 1.00 107.97 ? 835  SER A CA    1 
ATOM   6700  C C     . SER B 2 838  ? 182.504 161.307 124.099 1.00 107.97 ? 835  SER A C     1 
ATOM   6701  O O     . SER B 2 838  ? 183.418 161.565 123.309 1.00 107.97 ? 835  SER A O     1 
ATOM   6702  C CB    . SER B 2 838  ? 183.683 160.409 126.104 1.00 107.97 ? 835  SER A CB    1 
ATOM   6703  O OG    . SER B 2 838  ? 183.079 159.130 126.023 1.00 107.97 ? 835  SER A OG    1 
ATOM   6704  N N     . HIS B 2 839  ? 181.316 160.866 123.697 1.00 110.71 ? 836  HIS A N     1 
ATOM   6705  C CA    . HIS B 2 839  ? 180.987 160.667 122.296 1.00 110.71 ? 836  HIS A CA    1 
ATOM   6706  C C     . HIS B 2 839  ? 180.389 161.946 121.715 1.00 110.71 ? 836  HIS A C     1 
ATOM   6707  O O     . HIS B 2 839  ? 180.395 163.011 122.338 1.00 110.71 ? 836  HIS A O     1 
ATOM   6708  C CB    . HIS B 2 839  ? 180.025 159.488 122.134 1.00 110.71 ? 836  HIS A CB    1 
ATOM   6709  C CG    . HIS B 2 839  ? 180.619 158.167 122.511 1.00 110.71 ? 836  HIS A CG    1 
ATOM   6710  N ND1   . HIS B 2 839  ? 180.577 157.673 123.797 1.00 110.71 ? 836  HIS A ND1   1 
ATOM   6711  C CD2   . HIS B 2 839  ? 181.266 157.236 121.771 1.00 110.71 ? 836  HIS A CD2   1 
ATOM   6712  C CE1   . HIS B 2 839  ? 181.174 156.495 123.833 1.00 110.71 ? 836  HIS A CE1   1 
ATOM   6713  N NE2   . HIS B 2 839  ? 181.601 156.207 122.617 1.00 110.71 ? 836  HIS A NE2   1 
ATOM   6714  N N     . ASP B 2 840  ? 179.866 161.835 120.499 1.00 106.88 ? 837  ASP A N     1 
ATOM   6715  C CA    . ASP B 2 840  ? 179.218 162.941 119.815 1.00 106.88 ? 837  ASP A CA    1 
ATOM   6716  C C     . ASP B 2 840  ? 177.732 162.650 119.652 1.00 106.88 ? 837  ASP A C     1 
ATOM   6717  O O     . ASP B 2 840  ? 177.327 161.506 119.426 1.00 106.88 ? 837  ASP A O     1 
ATOM   6718  C CB    . ASP B 2 840  ? 179.854 163.193 118.445 1.00 106.88 ? 837  ASP A CB    1 
ATOM   6719  C CG    . ASP B 2 840  ? 179.280 164.414 117.751 1.00 106.88 ? 837  ASP A CG    1 
ATOM   6720  O OD1   . ASP B 2 840  ? 179.163 165.471 118.406 1.00 106.88 ? 837  ASP A OD1   1 
ATOM   6721  O OD2   . ASP B 2 840  ? 178.946 164.316 116.552 1.00 106.88 ? 837  ASP A OD2   1 
ATOM   6722  N N     . LEU B 2 841  ? 176.921 163.699 119.781 1.00 90.34  ? 838  LEU A N     1 
ATOM   6723  C CA    . LEU B 2 841  ? 175.482 163.554 119.613 1.00 90.34  ? 838  LEU A CA    1 
ATOM   6724  C C     . LEU B 2 841  ? 175.153 163.083 118.203 1.00 90.34  ? 838  LEU A C     1 
ATOM   6725  O O     . LEU B 2 841  ? 175.760 163.524 117.224 1.00 90.34  ? 838  LEU A O     1 
ATOM   6726  C CB    . LEU B 2 841  ? 174.778 164.880 119.903 1.00 90.34  ? 838  LEU A CB    1 
ATOM   6727  C CG    . LEU B 2 841  ? 175.045 165.515 121.266 1.00 90.34  ? 838  LEU A CG    1 
ATOM   6728  C CD1   . LEU B 2 841  ? 174.113 166.694 121.496 1.00 90.34  ? 838  LEU A CD1   1 
ATOM   6729  C CD2   . LEU B 2 841  ? 174.884 164.483 122.368 1.00 90.34  ? 838  LEU A CD2   1 
ATOM   6730  N N     . SER B 2 842  ? 174.183 162.179 118.106 1.00 85.01  ? 839  SER A N     1 
ATOM   6731  C CA    . SER B 2 842  ? 173.772 161.647 116.817 1.00 85.01  ? 839  SER A CA    1 
ATOM   6732  C C     . SER B 2 842  ? 173.068 162.730 116.001 1.00 85.01  ? 839  SER A C     1 
ATOM   6733  O O     . SER B 2 842  ? 172.830 163.848 116.467 1.00 85.01  ? 839  SER A O     1 
ATOM   6734  C CB    . SER B 2 842  ? 172.871 160.430 117.010 1.00 85.01  ? 839  SER A CB    1 
ATOM   6735  O OG    . SER B 2 842  ? 173.493 159.461 117.835 1.00 85.01  ? 839  SER A OG    1 
ATOM   6736  N N     . ASP B 2 843  ? 172.734 162.387 114.755 1.00 82.98  ? 840  ASP A N     1 
ATOM   6737  C CA    . ASP B 2 843  ? 172.061 163.340 113.878 1.00 82.98  ? 840  ASP A CA    1 
ATOM   6738  C C     . ASP B 2 843  ? 170.712 163.754 114.453 1.00 82.98  ? 840  ASP A C     1 
ATOM   6739  O O     . ASP B 2 843  ? 170.345 164.934 114.422 1.00 82.98  ? 840  ASP A O     1 
ATOM   6740  C CB    . ASP B 2 843  ? 171.893 162.739 112.482 1.00 82.98  ? 840  ASP A CB    1 
ATOM   6741  C CG    . ASP B 2 843  ? 173.191 162.716 111.699 1.00 82.98  ? 840  ASP A CG    1 
ATOM   6742  O OD1   . ASP B 2 843  ? 174.264 162.609 112.328 1.00 82.98  ? 840  ASP A OD1   1 
ATOM   6743  O OD2   . ASP B 2 843  ? 173.137 162.804 110.454 1.00 82.98  ? 840  ASP A OD2   1 
ATOM   6744  N N     . GLU B 2 844  ? 169.956 162.791 114.983 1.00 78.85  ? 841  GLU A N     1 
ATOM   6745  C CA    . GLU B 2 844  ? 168.680 163.121 115.607 1.00 78.85  ? 841  GLU A CA    1 
ATOM   6746  C C     . GLU B 2 844  ? 168.883 163.849 116.931 1.00 78.85  ? 841  GLU A C     1 
ATOM   6747  O O     . GLU B 2 844  ? 168.080 164.714 117.299 1.00 78.85  ? 841  GLU A O     1 
ATOM   6748  C CB    . GLU B 2 844  ? 167.843 161.853 115.797 1.00 78.85  ? 841  GLU A CB    1 
ATOM   6749  C CG    . GLU B 2 844  ? 168.376 160.877 116.836 1.00 78.85  ? 841  GLU A CG    1 
ATOM   6750  C CD    . GLU B 2 844  ? 169.427 159.935 116.278 1.00 78.85  ? 841  GLU A CD    1 
ATOM   6751  O OE1   . GLU B 2 844  ? 169.965 160.214 115.186 1.00 78.85  ? 841  GLU A OE1   1 
ATOM   6752  O OE2   . GLU B 2 844  ? 169.717 158.913 116.935 1.00 78.85  ? 841  GLU A OE2   1 
ATOM   6753  N N     . ALA B 2 845  ? 169.949 163.512 117.661 1.00 76.23  ? 842  ALA A N     1 
ATOM   6754  C CA    . ALA B 2 845  ? 170.227 164.191 118.922 1.00 76.23  ? 842  ALA A CA    1 
ATOM   6755  C C     . ALA B 2 845  ? 170.586 165.655 118.698 1.00 76.23  ? 842  ALA A C     1 
ATOM   6756  O O     . ALA B 2 845  ? 170.158 166.528 119.461 1.00 76.23  ? 842  ALA A O     1 
ATOM   6757  C CB    . ALA B 2 845  ? 171.348 163.472 119.671 1.00 76.23  ? 842  ALA A CB    1 
ATOM   6758  N N     . ARG B 2 846  ? 171.377 165.940 117.661 1.00 81.12  ? 843  ARG A N     1 
ATOM   6759  C CA    . ARG B 2 846  ? 171.765 167.319 117.380 1.00 81.12  ? 843  ARG A CA    1 
ATOM   6760  C C     . ARG B 2 846  ? 170.557 168.174 117.019 1.00 81.12  ? 843  ARG A C     1 
ATOM   6761  O O     . ARG B 2 846  ? 170.449 169.325 117.458 1.00 81.12  ? 843  ARG A O     1 
ATOM   6762  C CB    . ARG B 2 846  ? 172.803 167.356 116.258 1.00 81.12  ? 843  ARG A CB    1 
ATOM   6763  C CG    . ARG B 2 846  ? 174.175 166.844 116.664 1.00 81.12  ? 843  ARG A CG    1 
ATOM   6764  C CD    . ARG B 2 846  ? 175.280 167.707 116.076 1.00 81.12  ? 843  ARG A CD    1 
ATOM   6765  N NE    . ARG B 2 846  ? 175.397 168.988 116.763 1.00 81.12  ? 843  ARG A NE    1 
ATOM   6766  C CZ    . ARG B 2 846  ? 176.094 169.182 117.874 1.00 81.12  ? 843  ARG A CZ    1 
ATOM   6767  N NH1   . ARG B 2 846  ? 176.754 168.195 118.457 1.00 81.12  ? 843  ARG A NH1   1 
ATOM   6768  N NH2   . ARG B 2 846  ? 176.129 170.397 118.414 1.00 81.12  ? 843  ARG A NH2   1 
ATOM   6769  N N     . ALA B 2 847  ? 169.642 167.632 116.213 1.00 69.58  ? 844  ALA A N     1 
ATOM   6770  C CA    . ALA B 2 847  ? 168.462 168.394 115.817 1.00 69.58  ? 844  ALA A CA    1 
ATOM   6771  C C     . ALA B 2 847  ? 167.573 168.696 117.015 1.00 69.58  ? 844  ALA A C     1 
ATOM   6772  O O     . ALA B 2 847  ? 166.839 169.691 117.020 1.00 69.58  ? 844  ALA A O     1 
ATOM   6773  C CB    . ALA B 2 847  ? 167.681 167.635 114.745 1.00 69.58  ? 844  ALA A CB    1 
ATOM   6774  N N     . LEU B 2 848  ? 167.624 167.846 118.040 1.00 64.68  ? 845  LEU A N     1 
ATOM   6775  C CA    . LEU B 2 848  ? 166.816 168.043 119.235 1.00 64.68  ? 845  LEU A CA    1 
ATOM   6776  C C     . LEU B 2 848  ? 167.454 169.017 120.217 1.00 64.68  ? 845  LEU A C     1 
ATOM   6777  O O     . LEU B 2 848  ? 166.775 169.485 121.137 1.00 64.68  ? 845  LEU A O     1 
ATOM   6778  C CB    . LEU B 2 848  ? 166.572 166.693 119.913 1.00 64.68  ? 845  LEU A CB    1 
ATOM   6779  C CG    . LEU B 2 848  ? 165.513 166.588 121.007 1.00 64.68  ? 845  LEU A CG    1 
ATOM   6780  C CD1   . LEU B 2 848  ? 164.146 166.951 120.455 1.00 64.68  ? 845  LEU A CD1   1 
ATOM   6781  C CD2   . LEU B 2 848  ? 165.502 165.185 121.583 1.00 64.68  ? 845  LEU A CD2   1 
ATOM   6782  N N     . LEU B 2 849  ? 168.737 169.334 120.037 1.00 65.69  ? 846  LEU A N     1 
ATOM   6783  C CA    . LEU B 2 849  ? 169.429 170.221 120.972 1.00 65.69  ? 846  LEU A CA    1 
ATOM   6784  C C     . LEU B 2 849  ? 168.843 171.628 121.033 1.00 65.69  ? 846  LEU A C     1 
ATOM   6785  O O     . LEU B 2 849  ? 168.610 172.121 122.150 1.00 65.69  ? 846  LEU A O     1 
ATOM   6786  C CB    . LEU B 2 849  ? 170.922 170.258 120.630 1.00 65.69  ? 846  LEU A CB    1 
ATOM   6787  C CG    . LEU B 2 849  ? 171.808 171.084 121.564 1.00 65.69  ? 846  LEU A CG    1 
ATOM   6788  C CD1   . LEU B 2 849  ? 173.057 170.306 121.932 1.00 65.69  ? 846  LEU A CD1   1 
ATOM   6789  C CD2   . LEU B 2 849  ? 172.177 172.415 120.926 1.00 65.69  ? 846  LEU A CD2   1 
ATOM   6790  N N     . PRO B 2 850  ? 168.595 172.333 119.922 1.00 62.26  ? 847  PRO A N     1 
ATOM   6791  C CA    . PRO B 2 850  ? 168.084 173.710 120.051 1.00 62.26  ? 847  PRO A CA    1 
ATOM   6792  C C     . PRO B 2 850  ? 166.681 173.789 120.622 1.00 62.26  ? 847  PRO A C     1 
ATOM   6793  O O     . PRO B 2 850  ? 166.253 174.879 121.019 1.00 62.26  ? 847  PRO A O     1 
ATOM   6794  C CB    . PRO B 2 850  ? 168.134 174.263 118.618 1.00 62.26  ? 847  PRO A CB    1 
ATOM   6795  C CG    . PRO B 2 850  ? 168.493 173.151 117.733 1.00 62.26  ? 847  PRO A CG    1 
ATOM   6796  C CD    . PRO B 2 850  ? 168.748 171.916 118.516 1.00 62.26  ? 847  PRO A CD    1 
ATOM   6797  N N     . ASN B 2 851  ? 165.950 172.678 120.675 1.00 60.18  ? 848  ASN A N     1 
ATOM   6798  C CA    . ASN B 2 851  ? 164.573 172.689 121.144 1.00 60.18  ? 848  ASN A CA    1 
ATOM   6799  C C     . ASN B 2 851  ? 164.420 172.251 122.596 1.00 60.18  ? 848  ASN A C     1 
ATOM   6800  O O     . ASN B 2 851  ? 163.326 172.389 123.152 1.00 60.18  ? 848  ASN A O     1 
ATOM   6801  C CB    . ASN B 2 851  ? 163.710 171.796 120.247 1.00 60.18  ? 848  ASN A CB    1 
ATOM   6802  C CG    . ASN B 2 851  ? 162.328 172.368 120.012 1.00 60.18  ? 848  ASN A CG    1 
ATOM   6803  O OD1   . ASN B 2 851  ? 161.967 173.401 120.576 1.00 60.18  ? 848  ASN A OD1   1 
ATOM   6804  N ND2   . ASN B 2 851  ? 161.545 171.698 119.174 1.00 60.18  ? 848  ASN A ND2   1 
ATOM   6805  N N     . VAL B 2 852  ? 165.473 171.734 123.223 1.00 56.56  ? 849  VAL A N     1 
ATOM   6806  C CA    . VAL B 2 852  ? 165.387 171.265 124.599 1.00 56.56  ? 849  VAL A CA    1 
ATOM   6807  C C     . VAL B 2 852  ? 165.751 172.407 125.542 1.00 56.56  ? 849  VAL A C     1 
ATOM   6808  O O     . VAL B 2 852  ? 166.506 173.319 125.196 1.00 56.56  ? 849  VAL A O     1 
ATOM   6809  C CB    . VAL B 2 852  ? 166.289 170.031 124.830 1.00 56.56  ? 849  VAL A CB    1 
ATOM   6810  C CG1   . VAL B 2 852  ? 167.756 170.401 124.685 1.00 56.56  ? 849  VAL A CG1   1 
ATOM   6811  C CG2   . VAL B 2 852  ? 166.013 169.393 126.185 1.00 56.56  ? 849  VAL A CG2   1 
ATOM   6812  N N     . ILE B 2 853  ? 165.198 172.360 126.752 1.00 56.03  ? 850  ILE A N     1 
ATOM   6813  C CA    . ILE B 2 853  ? 165.422 173.377 127.773 1.00 56.03  ? 850  ILE A CA    1 
ATOM   6814  C C     . ILE B 2 853  ? 166.242 172.769 128.904 1.00 56.03  ? 850  ILE A C     1 
ATOM   6815  O O     . ILE B 2 853  ? 166.037 171.610 129.284 1.00 56.03  ? 850  ILE A O     1 
ATOM   6816  C CB    . ILE B 2 853  ? 164.091 173.962 128.292 1.00 56.03  ? 850  ILE A CB    1 
ATOM   6817  C CG1   . ILE B 2 853  ? 164.347 175.192 129.166 1.00 56.03  ? 850  ILE A CG1   1 
ATOM   6818  C CG2   . ILE B 2 853  ? 163.272 172.912 129.032 1.00 56.03  ? 850  ILE A CG2   1 
ATOM   6819  C CD1   . ILE B 2 853  ? 163.105 176.008 129.450 1.00 56.03  ? 850  ILE A CD1   1 
ATOM   6820  N N     . THR B 2 854  ? 167.192 173.545 129.417 1.00 57.07  ? 851  THR A N     1 
ATOM   6821  C CA    . THR B 2 854  ? 168.077 173.110 130.486 1.00 57.07  ? 851  THR A CA    1 
ATOM   6822  C C     . THR B 2 854  ? 167.922 174.023 131.696 1.00 57.07  ? 851  THR A C     1 
ATOM   6823  O O     . THR B 2 854  ? 167.553 175.195 131.577 1.00 57.07  ? 851  THR A O     1 
ATOM   6824  C CB    . THR B 2 854  ? 169.542 173.094 130.029 1.00 57.07  ? 851  THR A CB    1 
ATOM   6825  O OG1   . THR B 2 854  ? 170.383 172.713 131.124 1.00 57.07  ? 851  THR A OG1   1 
ATOM   6826  C CG2   . THR B 2 854  ? 169.961 174.466 129.525 1.00 57.07  ? 851  THR A CG2   1 
ATOM   6827  N N     . LYS B 2 855  ? 168.204 173.466 132.873 1.00 56.72  ? 852  LYS A N     1 
ATOM   6828  C CA    . LYS B 2 855  ? 168.065 174.187 134.129 1.00 56.72  ? 852  LYS A CA    1 
ATOM   6829  C C     . LYS B 2 855  ? 169.261 173.898 135.022 1.00 56.72  ? 852  LYS A C     1 
ATOM   6830  O O     . LYS B 2 855  ? 169.719 172.756 135.108 1.00 56.72  ? 852  LYS A O     1 
ATOM   6831  C CB    . LYS B 2 855  ? 166.778 173.790 134.859 1.00 56.72  ? 852  LYS A CB    1 
ATOM   6832  C CG    . LYS B 2 855  ? 165.505 174.162 134.129 1.00 56.72  ? 852  LYS A CG    1 
ATOM   6833  C CD    . LYS B 2 855  ? 164.285 173.733 134.919 1.00 56.72  ? 852  LYS A CD    1 
ATOM   6834  C CE    . LYS B 2 855  ? 163.015 173.976 134.129 1.00 56.72  ? 852  LYS A CE    1 
ATOM   6835  N NZ    . LYS B 2 855  ? 162.748 175.426 133.927 1.00 56.72  ? 852  LYS A NZ    1 
ATOM   6836  N N     . GLU B 2 856  ? 169.759 174.936 135.689 1.00 61.03  ? 853  GLU A N     1 
ATOM   6837  C CA    . GLU B 2 856  ? 170.799 174.750 136.686 1.00 61.03  ? 853  GLU A CA    1 
ATOM   6838  C C     . GLU B 2 856  ? 170.212 174.125 137.948 1.00 61.03  ? 853  GLU A C     1 
ATOM   6839  O O     . GLU B 2 856  ? 169.013 174.228 138.226 1.00 61.03  ? 853  GLU A O     1 
ATOM   6840  C CB    . GLU B 2 856  ? 171.469 176.082 137.023 1.00 61.02  ? 853  GLU A CB    1 
ATOM   6841  C CG    . GLU B 2 856  ? 171.834 176.920 135.810 1.00 61.02  ? 853  GLU A CG    1 
ATOM   6842  C CD    . GLU B 2 856  ? 172.639 176.146 134.786 1.00 61.02  ? 853  GLU A CD    1 
ATOM   6843  O OE1   . GLU B 2 856  ? 173.819 175.841 135.062 1.00 61.02  ? 853  GLU A OE1   1 
ATOM   6844  O OE2   . GLU B 2 856  ? 172.092 175.839 133.706 1.00 61.02  ? 853  GLU A OE2   1 
ATOM   6845  N N     . VAL B 2 857  ? 171.075 173.469 138.720 1.00 61.72  ? 854  VAL A N     1 
ATOM   6846  C CA    . VAL B 2 857  ? 170.663 172.805 139.953 1.00 61.72  ? 854  VAL A CA    1 
ATOM   6847  C C     . VAL B 2 857  ? 170.624 173.860 141.053 1.00 61.72  ? 854  VAL A C     1 
ATOM   6848  O O     . VAL B 2 857  ? 171.620 174.107 141.734 1.00 61.72  ? 854  VAL A O     1 
ATOM   6849  C CB    . VAL B 2 857  ? 171.588 171.643 140.312 1.00 61.72  ? 854  VAL A CB    1 
ATOM   6850  C CG1   . VAL B 2 857  ? 170.956 170.792 141.398 1.00 61.72  ? 854  VAL A CG1   1 
ATOM   6851  C CG2   . VAL B 2 857  ? 171.870 170.799 139.082 1.00 61.72  ? 854  VAL A CG2   1 
ATOM   6852  N N     . SER B 2 858  ? 169.457 174.483 141.228 1.00 58.07  ? 855  SER A N     1 
ATOM   6853  C CA    . SER B 2 858  ? 169.288 175.451 142.306 1.00 58.07  ? 855  SER A CA    1 
ATOM   6854  C C     . SER B 2 858  ? 169.398 174.783 143.672 1.00 58.07  ? 855  SER A C     1 
ATOM   6855  O O     . SER B 2 858  ? 170.013 175.339 144.590 1.00 58.07  ? 855  SER A O     1 
ATOM   6856  C CB    . SER B 2 858  ? 167.947 176.171 142.159 1.00 58.07  ? 855  SER A CB    1 
ATOM   6857  O OG    . SER B 2 858  ? 167.750 176.617 140.827 1.00 58.07  ? 855  SER A OG    1 
ATOM   6858  N N     . HIS B 2 859  ? 168.813 173.596 143.829 1.00 55.63  ? 856  HIS A N     1 
ATOM   6859  C CA    . HIS B 2 859  ? 168.867 172.875 145.092 1.00 55.63  ? 856  HIS A CA    1 
ATOM   6860  C C     . HIS B 2 859  ? 169.088 171.392 144.824 1.00 55.63  ? 856  HIS A C     1 
ATOM   6861  O O     . HIS B 2 859  ? 168.740 170.871 143.762 1.00 55.63  ? 856  HIS A O     1 
ATOM   6862  C CB    . HIS B 2 859  ? 167.593 173.095 145.925 1.00 55.63  ? 856  HIS A CB    1 
ATOM   6863  C CG    . HIS B 2 859  ? 166.325 172.769 145.200 1.00 55.63  ? 856  HIS A CG    1 
ATOM   6864  N ND1   . HIS B 2 859  ? 165.370 173.719 144.908 1.00 55.63  ? 856  HIS A ND1   1 
ATOM   6865  C CD2   . HIS B 2 859  ? 165.846 171.596 144.720 1.00 55.63  ? 856  HIS A CD2   1 
ATOM   6866  C CE1   . HIS B 2 859  ? 164.362 173.148 144.273 1.00 55.63  ? 856  HIS A CE1   1 
ATOM   6867  N NE2   . HIS B 2 859  ? 164.626 171.860 144.146 1.00 55.63  ? 856  HIS A NE2   1 
ATOM   6868  N N     . GLU B 2 860  ? 169.663 170.717 145.817 1.00 52.73  ? 857  GLU A N     1 
ATOM   6869  C CA    . GLU B 2 860  ? 170.083 169.330 145.662 1.00 52.73  ? 857  GLU A CA    1 
ATOM   6870  C C     . GLU B 2 860  ? 168.876 168.398 145.645 1.00 52.73  ? 857  GLU A C     1 
ATOM   6871  O O     . GLU B 2 860  ? 167.990 168.495 146.499 1.00 52.73  ? 857  GLU A O     1 
ATOM   6872  C CB    . GLU B 2 860  ? 171.042 168.952 146.792 1.00 52.73  ? 857  GLU A CB    1 
ATOM   6873  C CG    . GLU B 2 860  ? 171.739 167.609 146.626 1.00 52.73  ? 857  GLU A CG    1 
ATOM   6874  C CD    . GLU B 2 860  ? 170.898 166.441 147.100 1.00 52.73  ? 857  GLU A CD    1 
ATOM   6875  O OE1   . GLU B 2 860  ? 170.064 166.636 148.013 1.00 52.73  ? 857  GLU A OE1   1 
ATOM   6876  O OE2   . GLU B 2 860  ? 171.081 165.329 146.561 1.00 52.73  ? 857  GLU A OE2   1 
ATOM   6877  N N     . ILE B 2 861  ? 168.852 167.486 144.676 1.00 48.91  ? 858  ILE A N     1 
ATOM   6878  C CA    . ILE B 2 861  ? 167.739 166.564 144.463 1.00 48.91  ? 858  ILE A CA    1 
ATOM   6879  C C     . ILE B 2 861  ? 168.300 165.148 144.444 1.00 48.91  ? 858  ILE A C     1 
ATOM   6880  O O     . ILE B 2 861  ? 169.284 164.878 143.745 1.00 48.91  ? 858  ILE A O     1 
ATOM   6881  C CB    . ILE B 2 861  ? 166.983 166.873 143.160 1.00 48.91  ? 858  ILE A CB    1 
ATOM   6882  C CG1   . ILE B 2 861  ? 166.101 168.106 143.337 1.00 48.91  ? 858  ILE A CG1   1 
ATOM   6883  C CG2   . ILE B 2 861  ? 166.124 165.693 142.744 1.00 48.91  ? 858  ILE A CG2   1 
ATOM   6884  C CD1   . ILE B 2 861  ? 165.620 168.695 142.033 1.00 48.91  ? 858  ILE A CD1   1 
ATOM   6885  N N     . ILE B 2 862  ? 167.688 164.255 145.218 1.00 48.55  ? 859  ILE A N     1 
ATOM   6886  C CA    . ILE B 2 862  ? 168.084 162.851 145.284 1.00 48.55  ? 859  ILE A CA    1 
ATOM   6887  C C     . ILE B 2 862  ? 167.081 162.017 144.500 1.00 48.55  ? 859  ILE A C     1 
ATOM   6888  O O     . ILE B 2 862  ? 165.867 162.130 144.712 1.00 48.55  ? 859  ILE A O     1 
ATOM   6889  C CB    . ILE B 2 862  ? 168.170 162.359 146.739 1.00 48.55  ? 859  ILE A CB    1 
ATOM   6890  C CG1   . ILE B 2 862  ? 169.287 163.079 147.488 1.00 48.55  ? 859  ILE A CG1   1 
ATOM   6891  C CG2   . ILE B 2 862  ? 168.362 160.847 146.778 1.00 48.55  ? 859  ILE A CG2   1 
ATOM   6892  C CD1   . ILE B 2 862  ? 169.267 162.853 148.987 1.00 48.55  ? 859  ILE A CD1   1 
ATOM   6893  N N     . LYS B 2 863  ? 167.586 161.169 143.604 1.00 48.55  ? 860  LYS A N     1 
ATOM   6894  C CA    . LYS B 2 863  ? 166.738 160.249 142.859 1.00 48.55  ? 860  LYS A CA    1 
ATOM   6895  C C     . LYS B 2 863  ? 166.228 159.155 143.791 1.00 48.55  ? 860  LYS A C     1 
ATOM   6896  O O     . LYS B 2 863  ? 166.999 158.301 144.240 1.00 48.55  ? 860  LYS A O     1 
ATOM   6897  C CB    . LYS B 2 863  ? 167.524 159.672 141.677 1.00 48.55  ? 860  LYS A CB    1 
ATOM   6898  C CG    . LYS B 2 863  ? 166.798 158.695 140.764 1.00 48.55  ? 860  LYS A CG    1 
ATOM   6899  C CD    . LYS B 2 863  ? 167.040 157.254 141.177 1.00 48.55  ? 860  LYS A CD    1 
ATOM   6900  C CE    . LYS B 2 863  ? 168.479 156.829 140.885 1.00 48.55  ? 860  LYS A CE    1 
ATOM   6901  N NZ    . LYS B 2 863  ? 168.755 155.414 141.264 1.00 48.55  ? 860  LYS A NZ    1 
ATOM   6902  N N     . ASP B 2 864  ? 164.917 159.177 144.058 1.00 48.55  ? 861  ASP A N     1 
ATOM   6903  C CA    . ASP B 2 864  ? 164.278 158.288 145.034 1.00 48.55  ? 861  ASP A CA    1 
ATOM   6904  C C     . ASP B 2 864  ? 164.931 158.400 146.411 1.00 48.55  ? 861  ASP A C     1 
ATOM   6905  O O     . ASP B 2 864  ? 165.595 157.481 146.894 1.00 48.55  ? 861  ASP A O     1 
ATOM   6906  C CB    . ASP B 2 864  ? 164.245 156.840 144.542 1.00 43.05  ? 861  ASP A CB    1 
ATOM   6907  C CG    . ASP B 2 864  ? 163.633 156.715 143.164 1.00 43.05  ? 861  ASP A CG    1 
ATOM   6908  O OD1   . ASP B 2 864  ? 162.396 156.859 143.058 1.00 43.05  ? 861  ASP A OD1   1 
ATOM   6909  O OD2   . ASP B 2 864  ? 164.373 156.457 142.198 1.00 43.05  ? 861  ASP A OD2   1 
ATOM   6910  N N     . ARG B 2 865  ? 164.733 159.558 147.043 1.00 48.55  ? 862  ARG A N     1 
ATOM   6911  C CA    . ARG B 2 865  ? 165.208 159.781 148.403 1.00 48.55  ? 862  ARG A CA    1 
ATOM   6912  C C     . ARG B 2 865  ? 164.458 158.946 149.435 1.00 48.55  ? 862  ARG A C     1 
ATOM   6913  O O     . ARG B 2 865  ? 164.936 158.812 150.567 1.00 48.55  ? 862  ARG A O     1 
ATOM   6914  C CB    . ARG B 2 865  ? 165.088 161.267 148.747 1.00 34.73  ? 862  ARG A CB    1 
ATOM   6915  C CG    . ARG B 2 865  ? 165.892 161.716 149.953 1.00 34.73  ? 862  ARG A CG    1 
ATOM   6916  C CD    . ARG B 2 865  ? 165.183 162.840 150.690 1.00 34.73  ? 862  ARG A CD    1 
ATOM   6917  N NE    . ARG B 2 865  ? 164.802 163.912 149.780 1.00 34.73  ? 862  ARG A NE    1 
ATOM   6918  C CZ    . ARG B 2 865  ? 164.020 164.933 150.105 1.00 34.73  ? 862  ARG A CZ    1 
ATOM   6919  N NH1   . ARG B 2 865  ? 163.517 165.058 151.322 1.00 34.73  ? 862  ARG A NH1   1 
ATOM   6920  N NH2   . ARG B 2 865  ? 163.739 165.852 149.187 1.00 34.73  ? 862  ARG A NH2   1 
ATOM   6921  N N     . ARG B 2 866  ? 163.299 158.385 149.078 1.00 48.55  ? 863  ARG A N     1 
ATOM   6922  C CA    . ARG B 2 866  ? 162.485 157.682 150.066 1.00 48.55  ? 863  ARG A CA    1 
ATOM   6923  C C     . ARG B 2 866  ? 163.228 156.495 150.660 1.00 48.55  ? 863  ARG A C     1 
ATOM   6924  O O     . ARG B 2 866  ? 163.159 156.251 151.870 1.00 48.55  ? 863  ARG A O     1 
ATOM   6925  C CB    . ARG B 2 866  ? 161.170 157.213 149.442 1.00 48.55  ? 863  ARG A CB    1 
ATOM   6926  C CG    . ARG B 2 866  ? 160.454 158.250 148.607 1.00 48.55  ? 863  ARG A CG    1 
ATOM   6927  C CD    . ARG B 2 866  ? 159.314 157.629 147.827 1.00 48.55  ? 863  ARG A CD    1 
ATOM   6928  N NE    . ARG B 2 866  ? 159.771 156.923 146.638 1.00 48.55  ? 863  ARG A NE    1 
ATOM   6929  C CZ    . ARG B 2 866  ? 160.066 157.510 145.487 1.00 48.55  ? 863  ARG A CZ    1 
ATOM   6930  N NH1   . ARG B 2 866  ? 159.970 158.820 145.335 1.00 48.55  ? 863  ARG A NH1   1 
ATOM   6931  N NH2   . ARG B 2 866  ? 160.464 156.763 144.462 1.00 48.55  ? 863  ARG A NH2   1 
ATOM   6932  N N     . PHE B 2 867  ? 163.947 155.748 149.828 1.00 48.55  ? 864  PHE A N     1 
ATOM   6933  C CA    . PHE B 2 867  ? 164.604 154.517 150.240 1.00 48.55  ? 864  PHE A CA    1 
ATOM   6934  C C     . PHE B 2 867  ? 166.069 154.718 150.595 1.00 48.55  ? 864  PHE A C     1 
ATOM   6935  O O     . PHE B 2 867  ? 166.772 153.738 150.864 1.00 48.55  ? 864  PHE A O     1 
ATOM   6936  C CB    . PHE B 2 867  ? 164.460 153.470 149.139 1.00 48.55  ? 864  PHE A CB    1 
ATOM   6937  C CG    . PHE B 2 867  ? 163.036 153.185 148.772 1.00 48.55  ? 864  PHE A CG    1 
ATOM   6938  C CD1   . PHE B 2 867  ? 162.273 152.324 149.539 1.00 48.55  ? 864  PHE A CD1   1 
ATOM   6939  C CD2   . PHE B 2 867  ? 162.445 153.813 147.693 1.00 48.55  ? 864  PHE A CD2   1 
ATOM   6940  C CE1   . PHE B 2 867  ? 160.959 152.063 149.212 1.00 48.55  ? 864  PHE A CE1   1 
ATOM   6941  C CE2   . PHE B 2 867  ? 161.130 153.559 147.361 1.00 48.55  ? 864  PHE A CE2   1 
ATOM   6942  C CZ    . PHE B 2 867  ? 160.385 152.684 148.125 1.00 48.55  ? 864  PHE A CZ    1 
ATOM   6943  N N     . THR B 2 868  ? 166.546 155.962 150.603 1.00 48.55  ? 865  THR A N     1 
ATOM   6944  C CA    . THR B 2 868  ? 167.924 156.225 150.997 1.00 48.55  ? 865  THR A CA    1 
ATOM   6945  C C     . THR B 2 868  ? 168.118 156.100 152.503 1.00 48.55  ? 865  THR A C     1 
ATOM   6946  O O     . THR B 2 868  ? 169.225 155.793 152.957 1.00 48.55  ? 865  THR A O     1 
ATOM   6947  C CB    . THR B 2 868  ? 168.343 157.619 150.523 1.00 48.55  ? 865  THR A CB    1 
ATOM   6948  O OG1   . THR B 2 868  ? 167.979 157.785 149.147 1.00 48.55  ? 865  THR A OG1   1 
ATOM   6949  C CG2   . THR B 2 868  ? 169.847 157.806 150.661 1.00 48.55  ? 865  THR A CG2   1 
ATOM   6950  N N     . SER B 2 869  ? 167.063 156.317 153.286 1.00 48.55  ? 866  SER A N     1 
ATOM   6951  C CA    . SER B 2 869  ? 167.140 156.276 154.738 1.00 48.55  ? 866  SER A CA    1 
ATOM   6952  C C     . SER B 2 869  ? 165.964 155.487 155.297 1.00 48.55  ? 866  SER A C     1 
ATOM   6953  O O     . SER B 2 869  ? 164.931 155.322 154.645 1.00 48.55  ? 866  SER A O     1 
ATOM   6954  C CB    . SER B 2 869  ? 167.156 157.687 155.340 1.00 48.55  ? 866  SER A CB    1 
ATOM   6955  O OG    . SER B 2 869  ? 167.185 157.636 156.755 1.00 48.55  ? 866  SER A OG    1 
ATOM   6956  N N     . ASP B 2 870  ? 166.141 154.997 156.521 1.00 48.55  ? 867  ASP A N     1 
ATOM   6957  C CA    . ASP B 2 870  ? 165.094 154.237 157.189 1.00 48.55  ? 867  ASP A CA    1 
ATOM   6958  C C     . ASP B 2 870  ? 163.883 155.121 157.462 1.00 48.55  ? 867  ASP A C     1 
ATOM   6959  O O     . ASP B 2 870  ? 164.018 156.296 157.813 1.00 48.55  ? 867  ASP A O     1 
ATOM   6960  C CB    . ASP B 2 870  ? 165.621 153.653 158.497 1.00 48.55  ? 867  ASP A CB    1 
ATOM   6961  C CG    . ASP B 2 870  ? 166.764 152.682 158.282 1.00 48.55  ? 867  ASP A CG    1 
ATOM   6962  O OD1   . ASP B 2 870  ? 166.807 152.039 157.213 1.00 48.55  ? 867  ASP A OD1   1 
ATOM   6963  O OD2   . ASP B 2 870  ? 167.623 152.564 159.182 1.00 48.55  ? 867  ASP A OD2   1 
ATOM   6964  N N     . LYS B 2 871  ? 162.693 154.549 157.299 1.00 48.55  ? 868  LYS A N     1 
ATOM   6965  C CA    . LYS B 2 871  ? 161.450 155.290 157.445 1.00 48.55  ? 868  LYS A CA    1 
ATOM   6966  C C     . LYS B 2 871  ? 160.466 154.513 158.305 1.00 48.55  ? 868  LYS A C     1 
ATOM   6967  O O     . LYS B 2 871  ? 160.426 153.280 158.260 1.00 48.55  ? 868  LYS A O     1 
ATOM   6968  C CB    . LYS B 2 871  ? 160.816 155.582 156.079 1.00 48.55  ? 868  LYS A CB    1 
ATOM   6969  C CG    . LYS B 2 871  ? 161.636 156.503 155.192 1.00 48.55  ? 868  LYS A CG    1 
ATOM   6970  C CD    . LYS B 2 871  ? 161.576 157.939 155.679 1.00 48.55  ? 868  LYS A CD    1 
ATOM   6971  C CE    . LYS B 2 871  ? 161.915 158.909 154.562 1.00 48.55  ? 868  LYS A CE    1 
ATOM   6972  N NZ    . LYS B 2 871  ? 160.810 159.016 153.571 1.00 48.55  ? 868  LYS A NZ    1 
ATOM   6973  N N     . PHE B 2 872  ? 159.677 155.242 159.088 1.00 48.55  ? 869  PHE A N     1 
ATOM   6974  C CA    . PHE B 2 872  ? 158.547 154.675 159.805 1.00 48.55  ? 869  PHE A CA    1 
ATOM   6975  C C     . PHE B 2 872  ? 157.265 154.923 159.019 1.00 48.55  ? 869  PHE A C     1 
ATOM   6976  O O     . PHE B 2 872  ? 157.169 155.857 158.219 1.00 48.55  ? 869  PHE A O     1 
ATOM   6977  C CB    . PHE B 2 872  ? 158.420 155.276 161.205 1.00 48.55  ? 869  PHE A CB    1 
ATOM   6978  C CG    . PHE B 2 872  ? 159.586 154.986 162.105 1.00 48.55  ? 869  PHE A CG    1 
ATOM   6979  C CD1   . PHE B 2 872  ? 160.782 155.667 161.959 1.00 48.55  ? 869  PHE A CD1   1 
ATOM   6980  C CD2   . PHE B 2 872  ? 159.480 154.042 163.109 1.00 48.55  ? 869  PHE A CD2   1 
ATOM   6981  C CE1   . PHE B 2 872  ? 161.851 155.403 162.790 1.00 48.55  ? 869  PHE A CE1   1 
ATOM   6982  C CE2   . PHE B 2 872  ? 160.546 153.777 163.944 1.00 48.55  ? 869  PHE A CE2   1 
ATOM   6983  C CZ    . PHE B 2 872  ? 161.731 154.458 163.784 1.00 48.55  ? 869  PHE A CZ    1 
ATOM   6984  N N     . PHE B 2 873  ? 156.270 154.073 159.255 1.00 48.55  ? 870  PHE A N     1 
ATOM   6985  C CA    . PHE B 2 873  ? 155.012 154.192 158.536 1.00 48.55  ? 870  PHE A CA    1 
ATOM   6986  C C     . PHE B 2 873  ? 153.860 153.870 159.472 1.00 48.55  ? 870  PHE A C     1 
ATOM   6987  O O     . PHE B 2 873  ? 153.980 153.025 160.363 1.00 48.55  ? 870  PHE A O     1 
ATOM   6988  C CB    . PHE B 2 873  ? 154.989 153.280 157.307 1.00 48.55  ? 870  PHE A CB    1 
ATOM   6989  C CG    . PHE B 2 873  ? 155.868 153.758 156.192 1.00 48.55  ? 870  PHE A CG    1 
ATOM   6990  C CD1   . PHE B 2 873  ? 155.491 154.834 155.410 1.00 48.55  ? 870  PHE A CD1   1 
ATOM   6991  C CD2   . PHE B 2 873  ? 157.079 153.143 155.936 1.00 48.55  ? 870  PHE A CD2   1 
ATOM   6992  C CE1   . PHE B 2 873  ? 156.301 155.282 154.389 1.00 48.55  ? 870  PHE A CE1   1 
ATOM   6993  C CE2   . PHE B 2 873  ? 157.894 153.587 154.915 1.00 48.55  ? 870  PHE A CE2   1 
ATOM   6994  C CZ    . PHE B 2 873  ? 157.504 154.658 154.140 1.00 48.55  ? 870  PHE A CZ    1 
ATOM   6995  N N     . PHE B 2 874  ? 152.740 154.556 159.258 1.00 48.55  ? 871  PHE A N     1 
ATOM   6996  C CA    . PHE B 2 874  ? 151.556 154.409 160.096 1.00 48.55  ? 871  PHE A CA    1 
ATOM   6997  C C     . PHE B 2 874  ? 150.355 154.176 159.196 1.00 48.55  ? 871  PHE A C     1 
ATOM   6998  O O     . PHE B 2 874  ? 150.098 154.969 158.285 1.00 48.55  ? 871  PHE A O     1 
ATOM   6999  C CB    . PHE B 2 874  ? 151.349 155.651 160.968 1.00 48.55  ? 871  PHE A CB    1 
ATOM   7000  C CG    . PHE B 2 874  ? 150.028 155.684 161.678 1.00 48.55  ? 871  PHE A CG    1 
ATOM   7001  C CD1   . PHE B 2 874  ? 149.618 154.616 162.458 1.00 48.55  ? 871  PHE A CD1   1 
ATOM   7002  C CD2   . PHE B 2 874  ? 149.200 156.787 161.574 1.00 48.55  ? 871  PHE A CD2   1 
ATOM   7003  C CE1   . PHE B 2 874  ? 148.404 154.647 163.114 1.00 48.55  ? 871  PHE A CE1   1 
ATOM   7004  C CE2   . PHE B 2 874  ? 147.987 156.824 162.228 1.00 48.55  ? 871  PHE A CE2   1 
ATOM   7005  C CZ    . PHE B 2 874  ? 147.588 155.753 163.000 1.00 48.55  ? 871  PHE A CZ    1 
ATOM   7006  N N     . HIS B 2 875  ? 149.624 153.095 159.448 1.00 48.55  ? 872  HIS A N     1 
ATOM   7007  C CA    . HIS B 2 875  ? 148.441 152.737 158.676 1.00 48.55  ? 872  HIS A CA    1 
ATOM   7008  C C     . HIS B 2 875  ? 147.218 152.876 159.570 1.00 48.55  ? 872  HIS A C     1 
ATOM   7009  O O     . HIS B 2 875  ? 147.176 152.298 160.661 1.00 48.55  ? 872  HIS A O     1 
ATOM   7010  C CB    . HIS B 2 875  ? 148.545 151.313 158.132 1.00 48.55  ? 872  HIS A CB    1 
ATOM   7011  C CG    . HIS B 2 875  ? 149.682 151.106 157.180 1.00 48.55  ? 872  HIS A CG    1 
ATOM   7012  N ND1   . HIS B 2 875  ? 149.599 150.255 156.100 1.00 48.55  ? 872  HIS A ND1   1 
ATOM   7013  C CD2   . HIS B 2 875  ? 150.927 151.637 157.145 1.00 48.55  ? 872  HIS A CD2   1 
ATOM   7014  C CE1   . HIS B 2 875  ? 150.743 150.271 155.441 1.00 48.55  ? 872  HIS A CE1   1 
ATOM   7015  N NE2   . HIS B 2 875  ? 151.566 151.101 156.054 1.00 48.55  ? 872  HIS A NE2   1 
ATOM   7016  N N     . VAL B 2 876  ? 146.230 153.636 159.110 1.00 48.55  ? 873  VAL A N     1 
ATOM   7017  C CA    . VAL B 2 876  ? 145.024 153.874 159.897 1.00 48.55  ? 873  VAL A CA    1 
ATOM   7018  C C     . VAL B 2 876  ? 143.791 153.733 159.011 1.00 48.55  ? 873  VAL A C     1 
ATOM   7019  O O     . VAL B 2 876  ? 143.754 154.282 157.900 1.00 48.55  ? 873  VAL A O     1 
ATOM   7020  C CB    . VAL B 2 876  ? 145.078 155.248 160.586 1.00 48.55  ? 873  VAL A CB    1 
ATOM   7021  C CG1   . VAL B 2 876  ? 145.180 156.374 159.567 1.00 48.55  ? 873  VAL A CG1   1 
ATOM   7022  C CG2   . VAL B 2 876  ? 143.871 155.435 161.479 1.00 48.55  ? 873  VAL A CG2   1 
ATOM   7023  N N     . PRO B 2 877  ? 142.781 152.982 159.439 1.00 48.55  ? 874  PRO A N     1 
ATOM   7024  C CA    . PRO B 2 877  ? 141.556 152.861 158.650 1.00 48.55  ? 874  PRO A CA    1 
ATOM   7025  C C     . PRO B 2 877  ? 140.490 153.860 159.067 1.00 48.55  ? 874  PRO A C     1 
ATOM   7026  O O     . PRO B 2 877  ? 140.346 154.217 160.238 1.00 48.55  ? 874  PRO A O     1 
ATOM   7027  C CB    . PRO B 2 877  ? 141.106 151.425 158.947 1.00 48.55  ? 874  PRO A CB    1 
ATOM   7028  C CG    . PRO B 2 877  ? 141.580 151.179 160.335 1.00 48.55  ? 874  PRO A CG    1 
ATOM   7029  C CD    . PRO B 2 877  ? 142.786 152.061 160.587 1.00 48.55  ? 874  PRO A CD    1 
ATOM   7030  N N     . ILE B 2 878  ? 139.731 154.314 158.071 1.00 48.55  ? 875  ILE A N     1 
ATOM   7031  C CA    . ILE B 2 878  ? 138.617 155.225 158.284 1.00 48.55  ? 875  ILE A CA    1 
ATOM   7032  C C     . ILE B 2 878  ? 137.394 154.665 157.572 1.00 48.55  ? 875  ILE A C     1 
ATOM   7033  O O     . ILE B 2 878  ? 137.499 153.928 156.589 1.00 48.55  ? 875  ILE A O     1 
ATOM   7034  C CB    . ILE B 2 878  ? 138.920 156.656 157.791 1.00 48.55  ? 875  ILE A CB    1 
ATOM   7035  C CG1   . ILE B 2 878  ? 139.092 156.676 156.274 1.00 48.55  ? 875  ILE A CG1   1 
ATOM   7036  C CG2   . ILE B 2 878  ? 140.167 157.199 158.464 1.00 48.55  ? 875  ILE A CG2   1 
ATOM   7037  C CD1   . ILE B 2 878  ? 139.150 158.068 155.690 1.00 48.55  ? 875  ILE A CD1   1 
ATOM   7038  N N     . THR B 2 879  ? 136.221 155.018 158.089 1.00 48.55  ? 876  THR A N     1 
ATOM   7039  C CA    . THR B 2 879  ? 134.945 154.548 157.552 1.00 48.55  ? 876  THR A CA    1 
ATOM   7040  C C     . THR B 2 879  ? 134.159 155.755 157.053 1.00 48.55  ? 876  THR A C     1 
ATOM   7041  O O     . THR B 2 879  ? 133.564 156.491 157.846 1.00 48.55  ? 876  THR A O     1 
ATOM   7042  C CB    . THR B 2 879  ? 134.157 153.769 158.601 1.00 48.55  ? 876  THR A CB    1 
ATOM   7043  O OG1   . THR B 2 879  ? 134.872 152.578 158.948 1.00 48.55  ? 876  THR A OG1   1 
ATOM   7044  C CG2   . THR B 2 879  ? 132.790 153.385 158.059 1.00 48.55  ? 876  THR A CG2   1 
ATOM   7045  N N     . LEU B 2 880  ? 134.164 155.957 155.741 1.00 48.55  ? 877  LEU A N     1 
ATOM   7046  C CA    . LEU B 2 880  ? 133.395 157.027 155.131 1.00 48.55  ? 877  LEU A CA    1 
ATOM   7047  C C     . LEU B 2 880  ? 131.922 156.645 155.057 1.00 48.55  ? 877  LEU A C     1 
ATOM   7048  O O     . LEU B 2 880  ? 131.569 155.465 154.979 1.00 48.55  ? 877  LEU A O     1 
ATOM   7049  C CB    . LEU B 2 880  ? 133.938 157.337 153.737 1.00 48.55  ? 877  LEU A CB    1 
ATOM   7050  C CG    . LEU B 2 880  ? 135.372 157.868 153.725 1.00 48.55  ? 877  LEU A CG    1 
ATOM   7051  C CD1   . LEU B 2 880  ? 136.118 157.413 152.484 1.00 48.55  ? 877  LEU A CD1   1 
ATOM   7052  C CD2   . LEU B 2 880  ? 135.371 159.381 153.815 1.00 48.55  ? 877  LEU A CD2   1 
ATOM   7053  N N     . ASN B 2 881  ? 131.061 157.664 155.084 1.00 48.55  ? 878  ASN A N     1 
ATOM   7054  C CA    . ASN B 2 881  ? 129.609 157.478 155.077 1.00 48.55  ? 878  ASN A CA    1 
ATOM   7055  C C     . ASN B 2 881  ? 129.165 156.581 156.233 1.00 48.55  ? 878  ASN A C     1 
ATOM   7056  O O     . ASN B 2 881  ? 128.461 155.587 156.046 1.00 48.55  ? 878  ASN A O     1 
ATOM   7057  C CB    . ASN B 2 881  ? 129.132 156.921 153.734 1.00 48.55  ? 878  ASN A CB    1 
ATOM   7058  C CG    . ASN B 2 881  ? 129.320 157.902 152.599 1.00 48.55  ? 878  ASN A CG    1 
ATOM   7059  O OD1   . ASN B 2 881  ? 129.944 157.585 151.587 1.00 48.55  ? 878  ASN A OD1   1 
ATOM   7060  N ND2   . ASN B 2 881  ? 128.778 159.102 152.759 1.00 48.55  ? 878  ASN A ND2   1 
ATOM   7061  N N     . TYR B 2 882  ? 129.590 156.945 157.445 1.00 48.55  ? 879  TYR A N     1 
ATOM   7062  C CA    . TYR B 2 882  ? 129.299 156.121 158.614 1.00 48.55  ? 879  TYR A CA    1 
ATOM   7063  C C     . TYR B 2 882  ? 127.815 156.106 158.948 1.00 48.55  ? 879  TYR A C     1 
ATOM   7064  O O     . TYR B 2 882  ? 127.315 155.117 159.496 1.00 48.55  ? 879  TYR A O     1 
ATOM   7065  C CB    . TYR B 2 882  ? 130.115 156.610 159.813 1.00 48.55  ? 879  TYR A CB    1 
ATOM   7066  C CG    . TYR B 2 882  ? 129.774 155.927 161.118 1.00 48.55  ? 879  TYR A CG    1 
ATOM   7067  C CD1   . TYR B 2 882  ? 130.435 154.774 161.512 1.00 48.55  ? 879  TYR A CD1   1 
ATOM   7068  C CD2   . TYR B 2 882  ? 128.818 156.457 161.974 1.00 48.55  ? 879  TYR A CD2   1 
ATOM   7069  C CE1   . TYR B 2 882  ? 130.126 154.148 162.703 1.00 48.55  ? 879  TYR A CE1   1 
ATOM   7070  C CE2   . TYR B 2 882  ? 128.508 155.841 163.170 1.00 48.55  ? 879  TYR A CE2   1 
ATOM   7071  C CZ    . TYR B 2 882  ? 129.168 154.688 163.531 1.00 48.55  ? 879  TYR A CZ    1 
ATOM   7072  O OH    . TYR B 2 882  ? 128.867 154.069 164.722 1.00 48.55  ? 879  TYR A OH    1 
ATOM   7073  N N     . GLN B 2 883  ? 127.092 157.178 158.627 1.00 48.55  ? 880  GLN A N     1 
ATOM   7074  C CA    . GLN B 2 883  ? 125.676 157.243 158.964 1.00 48.55  ? 880  GLN A CA    1 
ATOM   7075  C C     . GLN B 2 883  ? 124.812 156.372 158.063 1.00 48.55  ? 880  GLN A C     1 
ATOM   7076  O O     . GLN B 2 883  ? 123.617 156.224 158.337 1.00 48.55  ? 880  GLN A O     1 
ATOM   7077  C CB    . GLN B 2 883  ? 125.189 158.691 158.902 1.00 48.55  ? 880  GLN A CB    1 
ATOM   7078  C CG    . GLN B 2 883  ? 125.770 159.589 159.983 1.00 48.55  ? 880  GLN A CG    1 
ATOM   7079  C CD    . GLN B 2 883  ? 125.169 159.330 161.351 1.00 48.55  ? 880  GLN A CD    1 
ATOM   7080  O OE1   . GLN B 2 883  ? 124.240 158.537 161.496 1.00 48.55  ? 880  GLN A OE1   1 
ATOM   7081  N NE2   . GLN B 2 883  ? 125.699 160.003 162.365 1.00 48.55  ? 880  GLN A NE2   1 
ATOM   7082  N N     . ALA B 2 884  ? 125.379 155.797 157.008 1.00 48.55  ? 881  ALA A N     1 
ATOM   7083  C CA    . ALA B 2 884  ? 124.621 155.000 156.058 1.00 48.55  ? 881  ALA A CA    1 
ATOM   7084  C C     . ALA B 2 884  ? 124.609 153.535 156.491 1.00 48.55  ? 881  ALA A C     1 
ATOM   7085  O O     . ALA B 2 884  ? 125.158 153.164 157.531 1.00 48.55  ? 881  ALA A O     1 
ATOM   7086  C CB    . ALA B 2 884  ? 125.199 155.172 154.656 1.00 48.55  ? 881  ALA A CB    1 
ATOM   7087  N N     . ALA B 2 885  ? 123.974 152.687 155.687 1.00 48.55  ? 882  ALA A N     1 
ATOM   7088  C CA    . ALA B 2 885  ? 123.873 151.269 155.985 1.00 48.55  ? 882  ALA A CA    1 
ATOM   7089  C C     . ALA B 2 885  ? 125.211 150.571 155.761 1.00 48.55  ? 882  ALA A C     1 
ATOM   7090  O O     . ALA B 2 885  ? 126.130 151.111 155.140 1.00 48.55  ? 882  ALA A O     1 
ATOM   7091  C CB    . ALA B 2 885  ? 122.790 150.613 155.128 1.00 48.55  ? 882  ALA A CB    1 
ATOM   7092  N N     . ASN B 2 886  ? 125.314 149.352 156.292 1.00 48.55  ? 883  ASN A N     1 
ATOM   7093  C CA    . ASN B 2 886  ? 126.549 148.588 156.153 1.00 48.55  ? 883  ASN A CA    1 
ATOM   7094  C C     . ASN B 2 886  ? 126.783 148.163 154.708 1.00 48.55  ? 883  ASN A C     1 
ATOM   7095  O O     . ASN B 2 886  ? 127.904 148.269 154.199 1.00 48.55  ? 883  ASN A O     1 
ATOM   7096  C CB    . ASN B 2 886  ? 126.517 147.368 157.072 1.00 48.55  ? 883  ASN A CB    1 
ATOM   7097  C CG    . ASN B 2 886  ? 127.130 147.645 158.429 1.00 48.55  ? 883  ASN A CG    1 
ATOM   7098  O OD1   . ASN B 2 886  ? 127.143 148.784 158.896 1.00 48.55  ? 883  ASN A OD1   1 
ATOM   7099  N ND2   . ASN B 2 886  ? 127.641 146.602 159.072 1.00 48.55  ? 883  ASN A ND2   1 
ATOM   7100  N N     . SER B 2 887  ? 125.743 147.684 154.035 1.00 48.55  ? 884  SER A N     1 
ATOM   7101  C CA    . SER B 2 887  ? 125.852 147.192 152.673 1.00 48.55  ? 884  SER A CA    1 
ATOM   7102  C C     . SER B 2 887  ? 124.764 147.808 151.806 1.00 48.55  ? 884  SER A C     1 
ATOM   7103  O O     . SER B 2 887  ? 123.657 148.072 152.286 1.00 48.55  ? 884  SER A O     1 
ATOM   7104  C CB    . SER B 2 887  ? 125.739 145.661 152.629 1.00 48.55  ? 884  SER A CB    1 
ATOM   7105  O OG    . SER B 2 887  ? 125.431 145.203 151.324 1.00 48.55  ? 884  SER A OG    1 
ATOM   7106  N N     . PRO B 2 888  ? 125.057 148.057 150.530 1.00 48.55  ? 885  PRO A N     1 
ATOM   7107  C CA    . PRO B 2 888  ? 124.036 148.617 149.637 1.00 48.55  ? 885  PRO A CA    1 
ATOM   7108  C C     . PRO B 2 888  ? 122.847 147.680 149.491 1.00 48.55  ? 885  PRO A C     1 
ATOM   7109  O O     . PRO B 2 888  ? 122.994 146.456 149.465 1.00 48.55  ? 885  PRO A O     1 
ATOM   7110  C CB    . PRO B 2 888  ? 124.782 148.791 148.308 1.00 48.55  ? 885  PRO A CB    1 
ATOM   7111  C CG    . PRO B 2 888  ? 125.980 147.902 148.415 1.00 48.55  ? 885  PRO A CG    1 
ATOM   7112  C CD    . PRO B 2 888  ? 126.356 147.903 149.858 1.00 48.55  ? 885  PRO A CD    1 
ATOM   7113  N N     . SER B 2 889  ? 121.658 148.270 149.394 1.00 48.55  ? 886  SER A N     1 
ATOM   7114  C CA    . SER B 2 889  ? 120.412 147.522 149.255 1.00 48.55  ? 886  SER A CA    1 
ATOM   7115  C C     . SER B 2 889  ? 119.756 147.917 147.940 1.00 48.55  ? 886  SER A C     1 
ATOM   7116  O O     . SER B 2 889  ? 119.135 148.981 147.850 1.00 48.55  ? 886  SER A O     1 
ATOM   7117  C CB    . SER B 2 889  ? 119.475 147.785 150.433 1.00 48.55  ? 886  SER A CB    1 
ATOM   7118  O OG    . SER B 2 889  ? 119.037 149.133 150.445 1.00 48.55  ? 886  SER A OG    1 
ATOM   7119  N N     . LYS B 2 890  ? 119.894 147.059 146.927 1.00 48.55  ? 887  LYS A N     1 
ATOM   7120  C CA    . LYS B 2 890  ? 119.303 147.282 145.607 1.00 48.55  ? 887  LYS A CA    1 
ATOM   7121  C C     . LYS B 2 890  ? 119.774 148.605 145.006 1.00 48.55  ? 887  LYS A C     1 
ATOM   7122  O O     . LYS B 2 890  ? 118.977 149.489 144.683 1.00 48.55  ? 887  LYS A O     1 
ATOM   7123  C CB    . LYS B 2 890  ? 117.775 147.216 145.671 1.00 48.55  ? 887  LYS A CB    1 
ATOM   7124  C CG    . LYS B 2 890  ? 117.216 145.806 145.786 1.00 48.55  ? 887  LYS A CG    1 
ATOM   7125  C CD    . LYS B 2 890  ? 118.018 144.820 144.951 1.00 48.55  ? 887  LYS A CD    1 
ATOM   7126  C CE    . LYS B 2 890  ? 117.599 143.387 145.233 1.00 48.55  ? 887  LYS A CE    1 
ATOM   7127  N NZ    . LYS B 2 890  ? 116.179 143.139 144.861 1.00 48.55  ? 887  LYS A NZ    1 
ATOM   7128  N N     . PHE B 2 891  ? 121.094 148.738 144.865 1.00 48.55  ? 888  PHE A N     1 
ATOM   7129  C CA    . PHE B 2 891  ? 121.660 149.944 144.268 1.00 48.55  ? 888  PHE A CA    1 
ATOM   7130  C C     . PHE B 2 891  ? 121.236 150.094 142.814 1.00 48.55  ? 888  PHE A C     1 
ATOM   7131  O O     . PHE B 2 891  ? 120.898 151.197 142.369 1.00 48.55  ? 888  PHE A O     1 
ATOM   7132  C CB    . PHE B 2 891  ? 123.183 149.916 144.380 1.00 48.55  ? 888  PHE A CB    1 
ATOM   7133  C CG    . PHE B 2 891  ? 123.833 151.245 144.132 1.00 48.55  ? 888  PHE A CG    1 
ATOM   7134  C CD1   . PHE B 2 891  ? 124.166 151.637 142.848 1.00 48.55  ? 888  PHE A CD1   1 
ATOM   7135  C CD2   . PHE B 2 891  ? 124.117 152.099 145.181 1.00 48.55  ? 888  PHE A CD2   1 
ATOM   7136  C CE1   . PHE B 2 891  ? 124.766 152.856 142.617 1.00 48.55  ? 888  PHE A CE1   1 
ATOM   7137  C CE2   . PHE B 2 891  ? 124.718 153.318 144.953 1.00 48.55  ? 888  PHE A CE2   1 
ATOM   7138  C CZ    . PHE B 2 891  ? 125.041 153.697 143.670 1.00 48.55  ? 888  PHE A CZ    1 
ATOM   7139  N N     . ASN B 2 892  ? 121.255 148.996 142.055 1.00 48.55  ? 889  ASN A N     1 
ATOM   7140  C CA    . ASN B 2 892  ? 120.884 149.064 140.646 1.00 48.55  ? 889  ASN A CA    1 
ATOM   7141  C C     . ASN B 2 892  ? 119.422 149.455 140.477 1.00 48.55  ? 889  ASN A C     1 
ATOM   7142  O O     . ASN B 2 892  ? 119.071 150.187 139.545 1.00 48.55  ? 889  ASN A O     1 
ATOM   7143  C CB    . ASN B 2 892  ? 121.165 147.726 139.965 1.00 48.55  ? 889  ASN A CB    1 
ATOM   7144  C CG    . ASN B 2 892  ? 122.622 147.561 139.588 1.00 48.55  ? 889  ASN A CG    1 
ATOM   7145  O OD1   . ASN B 2 892  ? 123.418 148.490 139.723 1.00 48.55  ? 889  ASN A OD1   1 
ATOM   7146  N ND2   . ASN B 2 892  ? 122.980 146.375 139.112 1.00 48.55  ? 889  ASN A ND2   1 
ATOM   7147  N N     . GLN B 2 893  ? 118.552 148.970 141.366 1.00 48.55  ? 890  GLN A N     1 
ATOM   7148  C CA    . GLN B 2 893  ? 117.139 149.324 141.285 1.00 48.55  ? 890  GLN A CA    1 
ATOM   7149  C C     . GLN B 2 893  ? 116.931 150.819 141.491 1.00 48.55  ? 890  GLN A C     1 
ATOM   7150  O O     . GLN B 2 893  ? 116.111 151.440 140.805 1.00 48.55  ? 890  GLN A O     1 
ATOM   7151  C CB    . GLN B 2 893  ? 116.340 148.523 142.312 1.00 48.55  ? 890  GLN A CB    1 
ATOM   7152  C CG    . GLN B 2 893  ? 114.836 148.576 142.109 1.00 48.55  ? 890  GLN A CG    1 
ATOM   7153  C CD    . GLN B 2 893  ? 114.141 149.447 143.137 1.00 48.55  ? 890  GLN A CD    1 
ATOM   7154  O OE1   . GLN B 2 893  ? 114.685 149.720 144.206 1.00 48.55  ? 890  GLN A OE1   1 
ATOM   7155  N NE2   . GLN B 2 893  ? 112.930 149.889 142.816 1.00 48.55  ? 890  GLN A NE2   1 
ATOM   7156  N N     . ARG B 2 894  ? 117.662 151.414 142.436 1.00 48.55  ? 891  ARG A N     1 
ATOM   7157  C CA    . ARG B 2 894  ? 117.543 152.850 142.667 1.00 48.55  ? 891  ARG A CA    1 
ATOM   7158  C C     . ARG B 2 894  ? 118.075 153.649 141.483 1.00 48.55  ? 891  ARG A C     1 
ATOM   7159  O O     . ARG B 2 894  ? 117.485 154.664 141.096 1.00 48.55  ? 891  ARG A O     1 
ATOM   7160  C CB    . ARG B 2 894  ? 118.277 153.234 143.951 1.00 48.55  ? 891  ARG A CB    1 
ATOM   7161  C CG    . ARG B 2 894  ? 118.135 154.694 144.338 1.00 48.55  ? 891  ARG A CG    1 
ATOM   7162  C CD    . ARG B 2 894  ? 119.083 155.050 145.468 1.00 48.55  ? 891  ARG A CD    1 
ATOM   7163  N NE    . ARG B 2 894  ? 119.350 153.903 146.327 1.00 48.55  ? 891  ARG A NE    1 
ATOM   7164  C CZ    . ARG B 2 894  ? 118.904 153.778 147.570 1.00 48.55  ? 891  ARG A CZ    1 
ATOM   7165  N NH1   . ARG B 2 894  ? 118.162 154.715 148.136 1.00 48.55  ? 891  ARG A NH1   1 
ATOM   7166  N NH2   . ARG B 2 894  ? 119.211 152.684 148.262 1.00 48.55  ? 891  ARG A NH2   1 
ATOM   7167  N N     . VAL B 2 895  ? 119.193 153.209 140.900 1.00 48.55  ? 892  VAL A N     1 
ATOM   7168  C CA    . VAL B 2 895  ? 119.755 153.904 139.744 1.00 48.55  ? 892  VAL A CA    1 
ATOM   7169  C C     . VAL B 2 895  ? 118.807 153.817 138.557 1.00 48.55  ? 892  VAL A C     1 
ATOM   7170  O O     . VAL B 2 895  ? 118.563 154.812 137.862 1.00 48.55  ? 892  VAL A O     1 
ATOM   7171  C CB    . VAL B 2 895  ? 121.143 153.332 139.404 1.00 48.55  ? 892  VAL A CB    1 
ATOM   7172  C CG1   . VAL B 2 895  ? 121.537 153.690 137.980 1.00 48.55  ? 892  VAL A CG1   1 
ATOM   7173  C CG2   . VAL B 2 895  ? 122.178 153.836 140.392 1.00 48.55  ? 892  VAL A CG2   1 
ATOM   7174  N N     . ASN B 2 896  ? 118.254 152.629 138.308 1.00 48.55  ? 893  ASN A N     1 
ATOM   7175  C CA    . ASN B 2 896  ? 117.335 152.453 137.189 1.00 48.55  ? 893  ASN A CA    1 
ATOM   7176  C C     . ASN B 2 896  ? 116.078 153.295 137.368 1.00 48.55  ? 893  ASN A C     1 
ATOM   7177  O O     . ASN B 2 896  ? 115.547 153.842 136.394 1.00 48.55  ? 893  ASN A O     1 
ATOM   7178  C CB    . ASN B 2 896  ? 116.975 150.976 137.039 1.00 48.55  ? 893  ASN A CB    1 
ATOM   7179  C CG    . ASN B 2 896  ? 118.133 150.144 136.530 1.00 48.55  ? 893  ASN A CG    1 
ATOM   7180  O OD1   . ASN B 2 896  ? 119.152 150.677 136.095 1.00 48.55  ? 893  ASN A OD1   1 
ATOM   7181  N ND2   . ASN B 2 896  ? 117.985 148.827 136.588 1.00 48.55  ? 893  ASN A ND2   1 
ATOM   7182  N N     . ALA B 2 897  ? 115.584 153.403 138.604 1.00 48.55  ? 894  ALA A N     1 
ATOM   7183  C CA    . ALA B 2 897  ? 114.401 154.218 138.860 1.00 48.55  ? 894  ALA A CA    1 
ATOM   7184  C C     . ALA B 2 897  ? 114.662 155.687 138.551 1.00 48.55  ? 894  ALA A C     1 
ATOM   7185  O O     . ALA B 2 897  ? 113.813 156.364 137.960 1.00 48.55  ? 894  ALA A O     1 
ATOM   7186  C CB    . ALA B 2 897  ? 113.947 154.045 140.308 1.00 48.55  ? 894  ALA A CB    1 
ATOM   7187  N N     . TYR B 2 898  ? 115.829 156.202 138.949 1.00 48.55  ? 895  TYR A N     1 
ATOM   7188  C CA    . TYR B 2 898  ? 116.173 157.581 138.619 1.00 48.55  ? 895  TYR A CA    1 
ATOM   7189  C C     . TYR B 2 898  ? 116.309 157.771 137.115 1.00 48.55  ? 895  TYR A C     1 
ATOM   7190  O O     . TYR B 2 898  ? 115.845 158.777 136.564 1.00 48.55  ? 895  TYR A O     1 
ATOM   7191  C CB    . TYR B 2 898  ? 117.467 157.993 139.319 1.00 48.55  ? 895  TYR A CB    1 
ATOM   7192  C CG    . TYR B 2 898  ? 118.130 159.187 138.670 1.00 48.55  ? 895  TYR A CG    1 
ATOM   7193  C CD1   . TYR B 2 898  ? 117.589 160.458 138.793 1.00 48.55  ? 895  TYR A CD1   1 
ATOM   7194  C CD2   . TYR B 2 898  ? 119.284 159.039 137.916 1.00 48.55  ? 895  TYR A CD2   1 
ATOM   7195  C CE1   . TYR B 2 898  ? 118.185 161.547 138.195 1.00 48.55  ? 895  TYR A CE1   1 
ATOM   7196  C CE2   . TYR B 2 898  ? 119.885 160.124 137.312 1.00 48.55  ? 895  TYR A CE2   1 
ATOM   7197  C CZ    . TYR B 2 898  ? 119.330 161.375 137.455 1.00 48.55  ? 895  TYR A CZ    1 
ATOM   7198  O OH    . TYR B 2 898  ? 119.926 162.458 136.854 1.00 48.55  ? 895  TYR A OH    1 
ATOM   7199  N N     . LEU B 2 899  ? 116.954 156.821 136.435 1.00 48.55  ? 896  LEU A N     1 
ATOM   7200  C CA    . LEU B 2 899  ? 117.127 156.930 134.992 1.00 48.55  ? 896  LEU A CA    1 
ATOM   7201  C C     . LEU B 2 899  ? 115.790 156.900 134.265 1.00 48.55  ? 896  LEU A C     1 
ATOM   7202  O O     . LEU B 2 899  ? 115.649 157.509 133.199 1.00 48.55  ? 896  LEU A O     1 
ATOM   7203  C CB    . LEU B 2 899  ? 118.032 155.807 134.489 1.00 48.55  ? 896  LEU A CB    1 
ATOM   7204  C CG    . LEU B 2 899  ? 119.534 155.985 134.711 1.00 48.55  ? 896  LEU A CG    1 
ATOM   7205  C CD1   . LEU B 2 899  ? 120.265 154.672 134.490 1.00 48.55  ? 896  LEU A CD1   1 
ATOM   7206  C CD2   . LEU B 2 899  ? 120.090 157.062 133.800 1.00 48.55  ? 896  LEU A CD2   1 
ATOM   7207  N N     . LYS B 2 900  ? 114.804 156.194 134.820 1.00 48.55  ? 897  LYS A N     1 
ATOM   7208  C CA    . LYS B 2 900  ? 113.494 156.121 134.185 1.00 48.55  ? 897  LYS A CA    1 
ATOM   7209  C C     . LYS B 2 900  ? 112.803 157.479 134.171 1.00 48.55  ? 897  LYS A C     1 
ATOM   7210  O O     . LYS B 2 900  ? 112.180 157.857 133.173 1.00 48.55  ? 897  LYS A O     1 
ATOM   7211  C CB    . LYS B 2 900  ? 112.627 155.086 134.901 1.00 48.55  ? 897  LYS A CB    1 
ATOM   7212  C CG    . LYS B 2 900  ? 111.467 154.563 134.075 1.00 48.55  ? 897  LYS A CG    1 
ATOM   7213  C CD    . LYS B 2 900  ? 110.532 153.712 134.919 1.00 48.55  ? 897  LYS A CD    1 
ATOM   7214  C CE    . LYS B 2 900  ? 111.302 152.680 135.728 1.00 48.55  ? 897  LYS A CE    1 
ATOM   7215  N NZ    . LYS B 2 900  ? 112.103 151.775 134.860 1.00 48.55  ? 897  LYS A NZ    1 
ATOM   7216  N N     . GLU B 2 901  ? 112.903 158.228 135.267 1.00 48.55  ? 898  GLU A N     1 
ATOM   7217  C CA    . GLU B 2 901  ? 112.196 159.495 135.400 1.00 48.55  ? 898  GLU A CA    1 
ATOM   7218  C C     . GLU B 2 901  ? 112.973 160.680 134.841 1.00 48.55  ? 898  GLU A C     1 
ATOM   7219  O O     . GLU B 2 901  ? 112.467 161.806 134.888 1.00 48.55  ? 898  GLU A O     1 
ATOM   7220  C CB    . GLU B 2 901  ? 111.854 159.755 136.870 1.00 48.55  ? 898  GLU A CB    1 
ATOM   7221  C CG    . GLU B 2 901  ? 113.066 159.961 137.763 1.00 48.55  ? 898  GLU A CG    1 
ATOM   7222  C CD    . GLU B 2 901  ? 112.691 160.150 139.220 1.00 48.55  ? 898  GLU A CD    1 
ATOM   7223  O OE1   . GLU B 2 901  ? 111.484 160.098 139.537 1.00 48.55  ? 898  GLU A OE1   1 
ATOM   7224  O OE2   . GLU B 2 901  ? 113.604 160.352 140.048 1.00 48.55  ? 898  GLU A OE2   1 
ATOM   7225  N N     . HIS B 2 902  ? 114.177 160.461 134.319 1.00 48.55  ? 899  HIS A N     1 
ATOM   7226  C CA    . HIS B 2 902  ? 115.009 161.524 133.754 1.00 48.55  ? 899  HIS A CA    1 
ATOM   7227  C C     . HIS B 2 902  ? 115.425 161.108 132.351 1.00 48.55  ? 899  HIS A C     1 
ATOM   7228  O O     . HIS B 2 902  ? 116.558 160.660 132.131 1.00 48.55  ? 899  HIS A O     1 
ATOM   7229  C CB    . HIS B 2 902  ? 116.225 161.804 134.638 1.00 48.55  ? 899  HIS A CB    1 
ATOM   7230  C CG    . HIS B 2 902  ? 115.960 162.785 135.737 1.00 48.55  ? 899  HIS A CG    1 
ATOM   7231  N ND1   . HIS B 2 902  ? 115.416 162.417 136.948 1.00 48.55  ? 899  HIS A ND1   1 
ATOM   7232  C CD2   . HIS B 2 902  ? 116.168 164.121 135.808 1.00 48.55  ? 899  HIS A CD2   1 
ATOM   7233  C CE1   . HIS B 2 902  ? 115.298 163.484 137.718 1.00 48.55  ? 899  HIS A CE1   1 
ATOM   7234  N NE2   . HIS B 2 902  ? 115.748 164.531 137.050 1.00 48.55  ? 899  HIS A NE2   1 
ATOM   7235  N N     . PRO B 2 903  ? 114.526 161.239 131.371 1.00 48.55  ? 900  PRO A N     1 
ATOM   7236  C CA    . PRO B 2 903  ? 114.848 160.792 130.006 1.00 48.55  ? 900  PRO A CA    1 
ATOM   7237  C C     . PRO B 2 903  ? 115.916 161.625 129.318 1.00 48.55  ? 900  PRO A C     1 
ATOM   7238  O O     . PRO B 2 903  ? 116.447 161.182 128.292 1.00 48.55  ? 900  PRO A O     1 
ATOM   7239  C CB    . PRO B 2 903  ? 113.503 160.905 129.269 1.00 48.55  ? 900  PRO A CB    1 
ATOM   7240  C CG    . PRO B 2 903  ? 112.465 161.104 130.342 1.00 48.55  ? 900  PRO A CG    1 
ATOM   7241  C CD    . PRO B 2 903  ? 113.166 161.791 131.463 1.00 48.55  ? 900  PRO A CD    1 
ATOM   7242  N N     . GLU B 2 904  ? 116.250 162.802 129.840 1.00 48.55  ? 901  GLU A N     1 
ATOM   7243  C CA    . GLU B 2 904  ? 117.220 163.689 129.211 1.00 48.55  ? 901  GLU A CA    1 
ATOM   7244  C C     . GLU B 2 904  ? 118.650 163.431 129.667 1.00 48.55  ? 901  GLU A C     1 
ATOM   7245  O O     . GLU B 2 904  ? 119.542 164.210 129.316 1.00 48.55  ? 901  GLU A O     1 
ATOM   7246  C CB    . GLU B 2 904  ? 116.859 165.157 129.476 1.00 48.55  ? 901  GLU A CB    1 
ATOM   7247  C CG    . GLU B 2 904  ? 115.630 165.683 128.730 1.00 48.55  ? 901  GLU A CG    1 
ATOM   7248  C CD    . GLU B 2 904  ? 114.364 164.895 129.011 1.00 48.55  ? 901  GLU A CD    1 
ATOM   7249  O OE1   . GLU B 2 904  ? 113.954 164.826 130.188 1.00 48.55  ? 901  GLU A OE1   1 
ATOM   7250  O OE2   . GLU B 2 904  ? 113.780 164.346 128.053 1.00 48.55  ? 901  GLU A OE2   1 
ATOM   7251  N N     . THR B 2 905  ? 118.888 162.377 130.438 1.00 48.55  ? 902  THR A N     1 
ATOM   7252  C CA    . THR B 2 905  ? 120.238 162.090 130.912 1.00 48.55  ? 902  THR A CA    1 
ATOM   7253  C C     . THR B 2 905  ? 121.150 161.753 129.736 1.00 48.55  ? 902  THR A C     1 
ATOM   7254  O O     . THR B 2 905  ? 120.754 160.991 128.845 1.00 48.55  ? 902  THR A O     1 
ATOM   7255  C CB    . THR B 2 905  ? 120.220 160.944 131.924 1.00 48.55  ? 902  THR A CB    1 
ATOM   7256  O OG1   . THR B 2 905  ? 121.562 160.621 132.312 1.00 48.55  ? 902  THR A OG1   1 
ATOM   7257  C CG2   . THR B 2 905  ? 119.543 159.709 131.346 1.00 48.55  ? 902  THR A CG2   1 
ATOM   7258  N N     . PRO B 2 906  ? 122.350 162.313 129.677 1.00 48.55  ? 903  PRO A N     1 
ATOM   7259  C CA    . PRO B 2 906  ? 123.275 162.005 128.585 1.00 48.55  ? 903  PRO A CA    1 
ATOM   7260  C C     . PRO B 2 906  ? 124.013 160.696 128.851 1.00 48.55  ? 903  PRO A C     1 
ATOM   7261  O O     . PRO B 2 906  ? 123.903 160.092 129.915 1.00 48.55  ? 903  PRO A O     1 
ATOM   7262  C CB    . PRO B 2 906  ? 124.225 163.203 128.582 1.00 48.55  ? 903  PRO A CB    1 
ATOM   7263  C CG    . PRO B 2 906  ? 124.203 163.704 129.974 1.00 48.55  ? 903  PRO A CG    1 
ATOM   7264  C CD    . PRO B 2 906  ? 122.852 163.386 130.551 1.00 48.55  ? 903  PRO A CD    1 
ATOM   7265  N N     . ILE B 2 907  ? 124.772 160.263 127.847 1.00 48.55  ? 904  ILE A N     1 
ATOM   7266  C CA    . ILE B 2 907  ? 125.495 158.999 127.881 1.00 48.55  ? 904  ILE A CA    1 
ATOM   7267  C C     . ILE B 2 907  ? 126.955 159.270 127.551 1.00 48.55  ? 904  ILE A C     1 
ATOM   7268  O O     . ILE B 2 907  ? 127.268 160.053 126.649 1.00 48.55  ? 904  ILE A O     1 
ATOM   7269  C CB    . ILE B 2 907  ? 124.904 157.974 126.889 1.00 48.55  ? 904  ILE A CB    1 
ATOM   7270  C CG1   . ILE B 2 907  ? 123.384 157.885 127.025 1.00 48.55  ? 904  ILE A CG1   1 
ATOM   7271  C CG2   . ILE B 2 907  ? 125.528 156.612 127.099 1.00 48.55  ? 904  ILE A CG2   1 
ATOM   7272  C CD1   . ILE B 2 907  ? 122.913 157.383 128.358 1.00 48.55  ? 904  ILE A CD1   1 
ATOM   7273  N N     . ILE B 2 908  ? 127.853 158.615 128.283 1.00 48.55  ? 905  ILE A N     1 
ATOM   7274  C CA    . ILE B 2 908  ? 129.290 158.733 128.064 1.00 48.55  ? 905  ILE A CA    1 
ATOM   7275  C C     . ILE B 2 908  ? 129.822 157.375 127.633 1.00 48.55  ? 905  ILE A C     1 
ATOM   7276  O O     . ILE B 2 908  ? 129.591 156.368 128.312 1.00 48.55  ? 905  ILE A O     1 
ATOM   7277  C CB    . ILE B 2 908  ? 130.024 159.230 129.322 1.00 48.55  ? 905  ILE A CB    1 
ATOM   7278  C CG1   . ILE B 2 908  ? 129.402 160.531 129.830 1.00 48.55  ? 905  ILE A CG1   1 
ATOM   7279  C CG2   . ILE B 2 908  ? 131.502 159.423 129.032 1.00 48.55  ? 905  ILE A CG2   1 
ATOM   7280  C CD1   . ILE B 2 908  ? 130.223 161.227 130.891 1.00 48.55  ? 905  ILE A CD1   1 
ATOM   7281  N N     . GLY B 2 909  ? 130.526 157.348 126.511 1.00 48.55  ? 906  GLY A N     1 
ATOM   7282  C CA    . GLY B 2 909  ? 131.108 156.121 125.986 1.00 48.55  ? 906  GLY A CA    1 
ATOM   7283  C C     . GLY B 2 909  ? 132.614 156.241 125.879 1.00 48.55  ? 906  GLY A C     1 
ATOM   7284  O O     . GLY B 2 909  ? 133.136 157.311 125.560 1.00 48.55  ? 906  GLY A O     1 
ATOM   7285  N N     . ILE B 2 910  ? 133.308 155.137 126.147 1.00 48.55  ? 907  ILE A N     1 
ATOM   7286  C CA    . ILE B 2 910  ? 134.764 155.094 126.123 1.00 48.55  ? 907  ILE A CA    1 
ATOM   7287  C C     . ILE B 2 910  ? 135.204 153.933 125.244 1.00 48.55  ? 907  ILE A C     1 
ATOM   7288  O O     . ILE B 2 910  ? 134.740 152.802 125.423 1.00 48.55  ? 907  ILE A O     1 
ATOM   7289  C CB    . ILE B 2 910  ? 135.355 154.952 127.537 1.00 48.55  ? 907  ILE A CB    1 
ATOM   7290  C CG1   . ILE B 2 910  ? 134.925 156.124 128.414 1.00 48.55  ? 907  ILE A CG1   1 
ATOM   7291  C CG2   . ILE B 2 910  ? 136.869 154.862 127.477 1.00 48.55  ? 907  ILE A CG2   1 
ATOM   7292  C CD1   . ILE B 2 910  ? 134.992 155.826 129.882 1.00 48.55  ? 907  ILE A CD1   1 
ATOM   7293  N N     . ASP B 2 911  ? 136.095 154.215 124.297 1.00 48.55  ? 908  ASP A N     1 
ATOM   7294  C CA    . ASP B 2 911  ? 136.664 153.196 123.430 1.00 48.55  ? 908  ASP A CA    1 
ATOM   7295  C C     . ASP B 2 911  ? 138.145 153.476 123.241 1.00 48.55  ? 908  ASP A C     1 
ATOM   7296  O O     . ASP B 2 911  ? 138.549 154.627 123.061 1.00 48.55  ? 908  ASP A O     1 
ATOM   7297  C CB    . ASP B 2 911  ? 135.962 153.152 122.067 1.00 48.55  ? 908  ASP A CB    1 
ATOM   7298  C CG    . ASP B 2 911  ? 136.116 151.810 121.374 1.00 48.55  ? 908  ASP A CG    1 
ATOM   7299  O OD1   . ASP B 2 911  ? 137.068 151.072 121.704 1.00 48.55  ? 908  ASP A OD1   1 
ATOM   7300  O OD2   . ASP B 2 911  ? 135.283 151.493 120.500 1.00 48.55  ? 908  ASP A OD2   1 
ATOM   7301  N N     . ARG B 2 912  ? 138.949 152.417 123.283 1.00 48.55  ? 909  ARG A N     1 
ATOM   7302  C CA    . ARG B 2 912  ? 140.387 152.532 123.072 1.00 48.55  ? 909  ARG A CA    1 
ATOM   7303  C C     . ARG B 2 912  ? 140.650 152.667 121.578 1.00 48.55  ? 909  ARG A C     1 
ATOM   7304  O O     . ARG B 2 912  ? 140.305 151.776 120.797 1.00 48.55  ? 909  ARG A O     1 
ATOM   7305  C CB    . ARG B 2 912  ? 141.110 151.320 123.648 1.00 48.55  ? 909  ARG A CB    1 
ATOM   7306  C CG    . ARG B 2 912  ? 140.813 151.051 125.109 1.00 48.55  ? 909  ARG A CG    1 
ATOM   7307  C CD    . ARG B 2 912  ? 141.211 149.637 125.487 1.00 48.55  ? 909  ARG A CD    1 
ATOM   7308  N NE    . ARG B 2 912  ? 140.174 148.671 125.145 1.00 48.55  ? 909  ARG A NE    1 
ATOM   7309  C CZ    . ARG B 2 912  ? 140.352 147.357 125.128 1.00 48.55  ? 909  ARG A CZ    1 
ATOM   7310  N NH1   . ARG B 2 912  ? 141.521 146.814 125.425 1.00 48.55  ? 909  ARG A NH1   1 
ATOM   7311  N NH2   . ARG B 2 912  ? 139.331 146.569 124.806 1.00 48.55  ? 909  ARG A NH2   1 
ATOM   7312  N N     . GLY B 2 913  ? 141.249 153.780 121.175 1.00 48.55  ? 910  GLY A N     1 
ATOM   7313  C CA    . GLY B 2 913  ? 141.573 153.973 119.781 1.00 48.55  ? 910  GLY A CA    1 
ATOM   7314  C C     . GLY B 2 913  ? 142.907 153.363 119.402 1.00 48.55  ? 910  GLY A C     1 
ATOM   7315  O O     . GLY B 2 913  ? 143.664 152.868 120.238 1.00 48.55  ? 910  GLY A O     1 
ATOM   7316  N N     . GLU B 2 914  ? 143.194 153.403 118.103 1.00 48.55  ? 911  GLU A N     1 
ATOM   7317  C CA    . GLU B 2 914  ? 144.477 152.956 117.577 1.00 48.55  ? 911  GLU A CA    1 
ATOM   7318  C C     . GLU B 2 914  ? 145.515 154.067 117.544 1.00 48.55  ? 911  GLU A C     1 
ATOM   7319  O O     . GLU B 2 914  ? 146.680 153.830 117.875 1.00 48.55  ? 911  GLU A O     1 
ATOM   7320  C CB    . GLU B 2 914  ? 144.303 152.379 116.168 1.00 48.55  ? 911  GLU A CB    1 
ATOM   7321  C CG    . GLU B 2 914  ? 143.502 151.088 116.122 1.00 48.55  ? 911  GLU A CG    1 
ATOM   7322  C CD    . GLU B 2 914  ? 143.334 150.555 114.712 1.00 48.55  ? 911  GLU A CD    1 
ATOM   7323  O OE1   . GLU B 2 914  ? 143.732 151.257 113.758 1.00 48.55  ? 911  GLU A OE1   1 
ATOM   7324  O OE2   . GLU B 2 914  ? 142.801 149.436 114.557 1.00 48.55  ? 911  GLU A OE2   1 
ATOM   7325  N N     . ARG B 2 915  ? 145.118 155.277 117.155 1.00 48.55  ? 912  ARG A N     1 
ATOM   7326  C CA    . ARG B 2 915  ? 146.017 156.421 117.139 1.00 48.55  ? 912  ARG A CA    1 
ATOM   7327  C C     . ARG B 2 915  ? 145.968 157.231 118.427 1.00 48.55  ? 912  ARG A C     1 
ATOM   7328  O O     . ARG B 2 915  ? 146.676 158.237 118.533 1.00 48.55  ? 912  ARG A O     1 
ATOM   7329  C CB    . ARG B 2 915  ? 145.693 157.331 115.950 1.00 48.55  ? 912  ARG A CB    1 
ATOM   7330  C CG    . ARG B 2 915  ? 145.884 156.665 114.595 1.00 48.55  ? 912  ARG A CG    1 
ATOM   7331  C CD    . ARG B 2 915  ? 147.357 156.496 114.238 1.00 48.55  ? 912  ARG A CD    1 
ATOM   7332  N NE    . ARG B 2 915  ? 148.210 157.511 114.845 1.00 48.55  ? 912  ARG A NE    1 
ATOM   7333  C CZ    . ARG B 2 915  ? 148.333 158.753 114.398 1.00 48.55  ? 912  ARG A CZ    1 
ATOM   7334  N NH1   . ARG B 2 915  ? 147.672 159.173 113.331 1.00 48.55  ? 912  ARG A NH1   1 
ATOM   7335  N NH2   . ARG B 2 915  ? 149.141 159.596 115.036 1.00 48.55  ? 912  ARG A NH2   1 
ATOM   7336  N N     . ASN B 2 916  ? 145.142 156.832 119.392 1.00 48.55  ? 913  ASN A N     1 
ATOM   7337  C CA    . ASN B 2 916  ? 145.120 157.467 120.701 1.00 48.55  ? 913  ASN A CA    1 
ATOM   7338  C C     . ASN B 2 916  ? 144.630 156.451 121.724 1.00 48.55  ? 913  ASN A C     1 
ATOM   7339  O O     . ASN B 2 916  ? 143.843 155.558 121.402 1.00 48.55  ? 913  ASN A O     1 
ATOM   7340  C CB    . ASN B 2 916  ? 144.248 158.728 120.705 1.00 48.55  ? 913  ASN A CB    1 
ATOM   7341  C CG    . ASN B 2 916  ? 142.902 158.516 120.043 1.00 48.55  ? 913  ASN A CG    1 
ATOM   7342  O OD1   . ASN B 2 916  ? 142.376 157.405 120.012 1.00 48.55  ? 913  ASN A OD1   1 
ATOM   7343  N ND2   . ASN B 2 916  ? 142.339 159.589 119.501 1.00 48.55  ? 913  ASN A ND2   1 
ATOM   7344  N N     . LEU B 2 917  ? 145.119 156.591 122.959 1.00 48.55  ? 914  LEU A N     1 
ATOM   7345  C CA    . LEU B 2 917  ? 144.852 155.583 123.981 1.00 48.55  ? 914  LEU A CA    1 
ATOM   7346  C C     . LEU B 2 917  ? 143.368 155.498 124.316 1.00 48.55  ? 914  LEU A C     1 
ATOM   7347  O O     . LEU B 2 917  ? 142.778 154.412 124.287 1.00 48.55  ? 914  LEU A O     1 
ATOM   7348  C CB    . LEU B 2 917  ? 145.672 155.880 125.236 1.00 48.55  ? 914  LEU A CB    1 
ATOM   7349  C CG    . LEU B 2 917  ? 147.190 155.799 125.085 1.00 48.55  ? 914  LEU A CG    1 
ATOM   7350  C CD1   . LEU B 2 917  ? 147.891 156.062 126.404 1.00 48.55  ? 914  LEU A CD1   1 
ATOM   7351  C CD2   . LEU B 2 917  ? 147.587 154.440 124.539 1.00 48.55  ? 914  LEU A CD2   1 
ATOM   7352  N N     . ILE B 2 918  ? 142.746 156.629 124.638 1.00 48.55  ? 915  ILE A N     1 
ATOM   7353  C CA    . ILE B 2 918  ? 141.350 156.662 125.055 1.00 48.55  ? 915  ILE A CA    1 
ATOM   7354  C C     . ILE B 2 918  ? 140.654 157.816 124.349 1.00 48.55  ? 915  ILE A C     1 
ATOM   7355  O O     . ILE B 2 918  ? 141.166 158.940 124.337 1.00 48.55  ? 915  ILE A O     1 
ATOM   7356  C CB    . ILE B 2 918  ? 141.215 156.800 126.584 1.00 48.55  ? 915  ILE A CB    1 
ATOM   7357  C CG1   . ILE B 2 918  ? 141.559 155.478 127.270 1.00 48.55  ? 915  ILE A CG1   1 
ATOM   7358  C CG2   . ILE B 2 918  ? 139.815 157.252 126.967 1.00 48.55  ? 915  ILE A CG2   1 
ATOM   7359  C CD1   . ILE B 2 918  ? 140.496 154.417 127.117 1.00 48.55  ? 915  ILE A CD1   1 
ATOM   7360  N N     . TYR B 2 919  ? 139.491 157.537 123.765 1.00 48.55  ? 916  TYR A N     1 
ATOM   7361  C CA    . TYR B 2 919  ? 138.651 158.559 123.158 1.00 48.55  ? 916  TYR A CA    1 
ATOM   7362  C C     . TYR B 2 919  ? 137.262 158.456 123.765 1.00 48.55  ? 916  TYR A C     1 
ATOM   7363  O O     . TYR B 2 919  ? 136.735 157.352 123.927 1.00 48.55  ? 916  TYR A O     1 
ATOM   7364  C CB    . TYR B 2 919  ? 138.578 158.398 121.638 1.00 48.55  ? 916  TYR A CB    1 
ATOM   7365  C CG    . TYR B 2 919  ? 138.277 159.684 120.904 1.00 48.55  ? 916  TYR A CG    1 
ATOM   7366  C CD1   . TYR B 2 919  ? 136.970 160.091 120.681 1.00 48.55  ? 916  TYR A CD1   1 
ATOM   7367  C CD2   . TYR B 2 919  ? 139.302 160.484 120.422 1.00 48.55  ? 916  TYR A CD2   1 
ATOM   7368  C CE1   . TYR B 2 919  ? 136.693 161.266 120.011 1.00 48.55  ? 916  TYR A CE1   1 
ATOM   7369  C CE2   . TYR B 2 919  ? 139.036 161.658 119.747 1.00 48.55  ? 916  TYR A CE2   1 
ATOM   7370  C CZ    . TYR B 2 919  ? 137.730 162.044 119.544 1.00 48.55  ? 916  TYR A CZ    1 
ATOM   7371  O OH    . TYR B 2 919  ? 137.460 163.214 118.873 1.00 48.55  ? 916  TYR A OH    1 
ATOM   7372  N N     . ILE B 2 920  ? 136.673 159.601 124.100 1.00 48.55  ? 917  ILE A N     1 
ATOM   7373  C CA    . ILE B 2 920  ? 135.370 159.640 124.747 1.00 48.55  ? 917  ILE A CA    1 
ATOM   7374  C C     . ILE B 2 920  ? 134.427 160.512 123.931 1.00 48.55  ? 917  ILE A C     1 
ATOM   7375  O O     . ILE B 2 920  ? 134.823 161.537 123.366 1.00 48.55  ? 917  ILE A O     1 
ATOM   7376  C CB    . ILE B 2 920  ? 135.459 160.149 126.204 1.00 48.55  ? 917  ILE A CB    1 
ATOM   7377  C CG1   . ILE B 2 920  ? 135.846 161.626 126.242 1.00 48.55  ? 917  ILE A CG1   1 
ATOM   7378  C CG2   . ILE B 2 920  ? 136.444 159.312 127.005 1.00 48.55  ? 917  ILE A CG2   1 
ATOM   7379  C CD1   . ILE B 2 920  ? 135.899 162.204 127.631 1.00 48.55  ? 917  ILE A CD1   1 
ATOM   7380  N N     . THR B 2 921  ? 133.174 160.074 123.845 1.00 48.55  ? 918  THR A N     1 
ATOM   7381  C CA    . THR B 2 921  ? 132.114 160.833 123.199 1.00 48.55  ? 918  THR A CA    1 
ATOM   7382  C C     . THR B 2 921  ? 130.887 160.815 124.093 1.00 48.55  ? 918  THR A C     1 
ATOM   7383  O O     . THR B 2 921  ? 130.497 159.759 124.599 1.00 48.55  ? 918  THR A O     1 
ATOM   7384  C CB    . THR B 2 921  ? 131.749 160.261 121.823 1.00 48.55  ? 918  THR A CB    1 
ATOM   7385  O OG1   . THR B 2 921  ? 131.191 158.952 121.986 1.00 48.55  ? 918  THR A OG1   1 
ATOM   7386  C CG2   . THR B 2 921  ? 132.972 160.182 120.920 1.00 48.55  ? 918  THR A CG2   1 
ATOM   7387  N N     . VAL B 2 922  ? 130.280 161.982 124.284 1.00 48.55  ? 919  VAL A N     1 
ATOM   7388  C CA    . VAL B 2 922  ? 129.065 162.117 125.077 1.00 48.55  ? 919  VAL A CA    1 
ATOM   7389  C C     . VAL B 2 922  ? 127.907 162.399 124.130 1.00 48.55  ? 919  VAL A C     1 
ATOM   7390  O O     . VAL B 2 922  ? 128.004 163.269 123.256 1.00 48.55  ? 919  VAL A O     1 
ATOM   7391  C CB    . VAL B 2 922  ? 129.201 163.209 126.153 1.00 48.55  ? 919  VAL A CB    1 
ATOM   7392  C CG1   . VAL B 2 922  ? 130.254 162.810 127.167 1.00 48.55  ? 919  VAL A CG1   1 
ATOM   7393  C CG2   . VAL B 2 922  ? 129.560 164.545 125.537 1.00 48.55  ? 919  VAL A CG2   1 
ATOM   7394  N N     . ILE B 2 923  ? 126.827 161.639 124.283 1.00 48.55  ? 920  ILE A N     1 
ATOM   7395  C CA    . ILE B 2 923  ? 125.663 161.736 123.414 1.00 48.55  ? 920  ILE A CA    1 
ATOM   7396  C C     . ILE B 2 923  ? 124.448 162.080 124.262 1.00 48.55  ? 920  ILE A C     1 
ATOM   7397  O O     . ILE B 2 923  ? 124.312 161.607 125.396 1.00 48.55  ? 920  ILE A O     1 
ATOM   7398  C CB    . ILE B 2 923  ? 125.432 160.436 122.615 1.00 48.55  ? 920  ILE A CB    1 
ATOM   7399  C CG1   . ILE B 2 923  ? 125.080 159.277 123.547 1.00 48.55  ? 920  ILE A CG1   1 
ATOM   7400  C CG2   . ILE B 2 923  ? 126.661 160.093 121.796 1.00 48.55  ? 920  ILE A CG2   1 
ATOM   7401  C CD1   . ILE B 2 923  ? 124.710 158.004 122.825 1.00 48.55  ? 920  ILE A CD1   1 
ATOM   7402  N N     . ASP B 2 924  ? 123.581 162.925 123.719 1.00 48.55  ? 921  ASP A N     1 
ATOM   7403  C CA    . ASP B 2 924  ? 122.366 163.332 124.408 1.00 48.55  ? 921  ASP A CA    1 
ATOM   7404  C C     . ASP B 2 924  ? 121.315 162.227 124.304 1.00 48.55  ? 921  ASP A C     1 
ATOM   7405  O O     . ASP B 2 924  ? 121.581 161.120 123.827 1.00 48.55  ? 921  ASP A O     1 
ATOM   7406  C CB    . ASP B 2 924  ? 121.904 164.692 123.877 1.00 48.55  ? 921  ASP A CB    1 
ATOM   7407  C CG    . ASP B 2 924  ? 121.319 164.632 122.464 1.00 48.55  ? 921  ASP A CG    1 
ATOM   7408  O OD1   . ASP B 2 924  ? 120.775 163.593 122.042 1.00 48.55  ? 921  ASP A OD1   1 
ATOM   7409  O OD2   . ASP B 2 924  ? 121.409 165.660 121.760 1.00 48.55  ? 921  ASP A OD2   1 
ATOM   7410  N N     . SER B 2 925  ? 120.097 162.521 124.765 1.00 48.55  ? 922  SER A N     1 
ATOM   7411  C CA    . SER B 2 925  ? 119.035 161.522 124.743 1.00 48.55  ? 922  SER A CA    1 
ATOM   7412  C C     . SER B 2 925  ? 118.648 161.148 123.318 1.00 48.55  ? 922  SER A C     1 
ATOM   7413  O O     . SER B 2 925  ? 118.417 159.971 123.018 1.00 48.55  ? 922  SER A O     1 
ATOM   7414  C CB    . SER B 2 925  ? 117.816 162.038 125.506 1.00 48.55  ? 922  SER A CB    1 
ATOM   7415  O OG    . SER B 2 925  ? 117.482 163.353 125.101 1.00 48.55  ? 922  SER A OG    1 
ATOM   7416  N N     . THR B 2 926  ? 118.570 162.134 122.428 1.00 48.55  ? 923  THR A N     1 
ATOM   7417  C CA    . THR B 2 926  ? 118.091 161.897 121.072 1.00 48.55  ? 923  THR A CA    1 
ATOM   7418  C C     . THR B 2 926  ? 119.202 161.552 120.086 1.00 48.55  ? 923  THR A C     1 
ATOM   7419  O O     . THR B 2 926  ? 118.907 161.325 118.908 1.00 48.55  ? 923  THR A O     1 
ATOM   7420  C CB    . THR B 2 926  ? 117.296 163.111 120.579 1.00 48.55  ? 923  THR A CB    1 
ATOM   7421  O OG1   . THR B 2 926  ? 116.868 162.894 119.228 1.00 48.55  ? 923  THR A OG1   1 
ATOM   7422  C CG2   . THR B 2 926  ? 118.122 164.380 120.669 1.00 48.55  ? 923  THR A CG2   1 
ATOM   7423  N N     . GLY B 2 927  ? 120.461 161.504 120.524 1.00 48.55  ? 924  GLY A N     1 
ATOM   7424  C CA    . GLY B 2 927  ? 121.518 160.888 119.750 1.00 48.55  ? 924  GLY A CA    1 
ATOM   7425  C C     . GLY B 2 927  ? 122.648 161.794 119.302 1.00 48.55  ? 924  GLY A C     1 
ATOM   7426  O O     . GLY B 2 927  ? 123.734 161.285 119.002 1.00 48.55  ? 924  GLY A O     1 
ATOM   7427  N N     . LYS B 2 928  ? 122.439 163.107 119.241 1.00 48.55  ? 925  LYS A N     1 
ATOM   7428  C CA    . LYS B 2 928  ? 123.500 163.991 118.778 1.00 48.55  ? 925  LYS A CA    1 
ATOM   7429  C C     . LYS B 2 928  ? 124.650 164.062 119.779 1.00 48.55  ? 925  LYS A C     1 
ATOM   7430  O O     . LYS B 2 928  ? 124.457 163.980 120.995 1.00 48.55  ? 925  LYS A O     1 
ATOM   7431  C CB    . LYS B 2 928  ? 122.962 165.395 118.490 1.00 29.03  ? 925  LYS A CB    1 
ATOM   7432  C CG    . LYS B 2 928  ? 122.327 165.556 117.107 1.00 29.03  ? 925  LYS A CG    1 
ATOM   7433  C CD    . LYS B 2 928  ? 120.966 164.898 116.961 1.00 29.03  ? 925  LYS A CD    1 
ATOM   7434  C CE    . LYS B 2 928  ? 119.906 165.614 117.773 1.00 29.03  ? 925  LYS A CE    1 
ATOM   7435  N NZ    . LYS B 2 928  ? 118.570 164.993 117.563 1.00 29.03  ? 925  LYS A NZ    1 
ATOM   7436  N N     . ILE B 2 929  ? 125.859 164.215 119.243 1.00 48.55  ? 926  ILE A N     1 
ATOM   7437  C CA    . ILE B 2 929  ? 127.080 164.244 120.043 1.00 48.55  ? 926  ILE A CA    1 
ATOM   7438  C C     . ILE B 2 929  ? 127.212 165.627 120.669 1.00 48.55  ? 926  ILE A C     1 
ATOM   7439  O O     . ILE B 2 929  ? 127.111 166.644 119.979 1.00 48.55  ? 926  ILE A O     1 
ATOM   7440  C CB    . ILE B 2 929  ? 128.313 163.905 119.199 1.00 48.55  ? 926  ILE A CB    1 
ATOM   7441  C CG1   . ILE B 2 929  ? 128.212 162.485 118.647 1.00 48.55  ? 926  ILE A CG1   1 
ATOM   7442  C CG2   . ILE B 2 929  ? 129.581 164.061 120.018 1.00 48.55  ? 926  ILE A CG2   1 
ATOM   7443  C CD1   . ILE B 2 929  ? 129.284 162.151 117.636 1.00 48.55  ? 926  ILE A CD1   1 
ATOM   7444  N N     . LEU B 2 930  ? 127.436 165.667 121.982 1.00 48.55  ? 927  LEU A N     1 
ATOM   7445  C CA    . LEU B 2 930  ? 127.673 166.941 122.650 1.00 48.55  ? 927  LEU A CA    1 
ATOM   7446  C C     . LEU B 2 930  ? 129.156 167.290 122.678 1.00 48.55  ? 927  LEU A C     1 
ATOM   7447  O O     . LEU B 2 930  ? 129.519 168.468 122.575 1.00 48.55  ? 927  LEU A O     1 
ATOM   7448  C CB    . LEU B 2 930  ? 127.107 166.904 124.068 1.00 48.55  ? 927  LEU A CB    1 
ATOM   7449  C CG    . LEU B 2 930  ? 125.585 166.997 124.177 1.00 48.55  ? 927  LEU A CG    1 
ATOM   7450  C CD1   . LEU B 2 930  ? 125.143 166.914 125.629 1.00 48.55  ? 927  LEU A CD1   1 
ATOM   7451  C CD2   . LEU B 2 930  ? 125.081 168.277 123.532 1.00 48.55  ? 927  LEU A CD2   1 
ATOM   7452  N N     . GLU B 2 931  ? 130.023 166.288 122.809 1.00 48.55  ? 928  GLU A N     1 
ATOM   7453  C CA    . GLU B 2 931  ? 131.457 166.526 122.900 1.00 48.55  ? 928  GLU A CA    1 
ATOM   7454  C C     . GLU B 2 931  ? 132.200 165.225 122.640 1.00 48.55  ? 928  GLU A C     1 
ATOM   7455  O O     . GLU B 2 931  ? 131.892 164.198 123.249 1.00 48.55  ? 928  GLU A O     1 
ATOM   7456  C CB    . GLU B 2 931  ? 131.839 167.085 124.276 1.00 48.55  ? 928  GLU A CB    1 
ATOM   7457  C CG    . GLU B 2 931  ? 133.263 166.772 124.701 1.00 48.55  ? 928  GLU A CG    1 
ATOM   7458  C CD    . GLU B 2 931  ? 133.580 167.283 126.091 1.00 48.55  ? 928  GLU A CD    1 
ATOM   7459  O OE1   . GLU B 2 931  ? 132.663 167.810 126.755 1.00 48.55  ? 928  GLU A OE1   1 
ATOM   7460  O OE2   . GLU B 2 931  ? 134.746 167.158 126.520 1.00 48.55  ? 928  GLU A OE2   1 
ATOM   7461  N N     . GLN B 2 932  ? 133.173 165.280 121.734 1.00 48.55  ? 929  GLN A N     1 
ATOM   7462  C CA    . GLN B 2 932  ? 134.086 164.174 121.482 1.00 48.55  ? 929  GLN A CA    1 
ATOM   7463  C C     . GLN B 2 932  ? 135.501 164.656 121.756 1.00 48.55  ? 929  GLN A C     1 
ATOM   7464  O O     . GLN B 2 932  ? 135.916 165.695 121.234 1.00 48.55  ? 929  GLN A O     1 
ATOM   7465  C CB    . GLN B 2 932  ? 133.957 163.659 120.046 1.00 48.55  ? 929  GLN A CB    1 
ATOM   7466  C CG    . GLN B 2 932  ? 133.800 164.751 119.003 1.00 48.55  ? 929  GLN A CG    1 
ATOM   7467  C CD    . GLN B 2 932  ? 133.486 164.198 117.630 1.00 48.55  ? 929  GLN A CD    1 
ATOM   7468  O OE1   . GLN B 2 932  ? 133.925 163.106 117.274 1.00 48.55  ? 929  GLN A OE1   1 
ATOM   7469  N NE2   . GLN B 2 932  ? 132.719 164.951 116.849 1.00 48.55  ? 929  GLN A NE2   1 
ATOM   7470  N N     . ARG B 2 933  ? 136.236 163.908 122.575 1.00 48.55  ? 930  ARG A N     1 
ATOM   7471  C CA    . ARG B 2 933  ? 137.531 164.356 123.060 1.00 48.55  ? 930  ARG A CA    1 
ATOM   7472  C C     . ARG B 2 933  ? 138.536 163.217 122.989 1.00 48.55  ? 930  ARG A C     1 
ATOM   7473  O O     . ARG B 2 933  ? 138.177 162.038 123.042 1.00 48.55  ? 930  ARG A O     1 
ATOM   7474  C CB    . ARG B 2 933  ? 137.432 164.880 124.499 1.00 48.55  ? 930  ARG A CB    1 
ATOM   7475  C CG    . ARG B 2 933  ? 138.560 165.805 124.917 1.00 48.55  ? 930  ARG A CG    1 
ATOM   7476  C CD    . ARG B 2 933  ? 138.032 166.975 125.723 1.00 48.55  ? 930  ARG A CD    1 
ATOM   7477  N NE    . ARG B 2 933  ? 137.268 166.531 126.883 1.00 48.55  ? 930  ARG A NE    1 
ATOM   7478  C CZ    . ARG B 2 933  ? 137.806 166.148 128.032 1.00 48.55  ? 930  ARG A CZ    1 
ATOM   7479  N NH1   . ARG B 2 933  ? 139.116 166.137 128.213 1.00 48.55  ? 930  ARG A NH1   1 
ATOM   7480  N NH2   . ARG B 2 933  ? 137.009 165.765 129.026 1.00 48.55  ? 930  ARG A NH2   1 
ATOM   7481  N N     . SER B 2 934  ? 139.806 163.589 122.869 1.00 48.55  ? 931  SER A N     1 
ATOM   7482  C CA    . SER B 2 934  ? 140.920 162.652 122.914 1.00 48.55  ? 931  SER A CA    1 
ATOM   7483  C C     . SER B 2 934  ? 141.619 162.790 124.258 1.00 48.55  ? 931  SER A C     1 
ATOM   7484  O O     . SER B 2 934  ? 141.930 163.905 124.689 1.00 48.55  ? 931  SER A O     1 
ATOM   7485  C CB    . SER B 2 934  ? 141.904 162.907 121.771 1.00 48.55  ? 931  SER A CB    1 
ATOM   7486  O OG    . SER B 2 934  ? 142.777 161.806 121.597 1.00 48.55  ? 931  SER A OG    1 
ATOM   7487  N N     . LEU B 2 935  ? 141.864 161.659 124.917 1.00 48.55  ? 932  LEU A N     1 
ATOM   7488  C CA    . LEU B 2 935  ? 142.403 161.641 126.270 1.00 48.55  ? 932  LEU A CA    1 
ATOM   7489  C C     . LEU B 2 935  ? 143.896 161.344 126.310 1.00 48.55  ? 932  LEU A C     1 
ATOM   7490  O O     . LEU B 2 935  ? 144.421 160.993 127.372 1.00 48.55  ? 932  LEU A O     1 
ATOM   7491  C CB    . LEU B 2 935  ? 141.648 160.626 127.129 1.00 48.55  ? 932  LEU A CB    1 
ATOM   7492  C CG    . LEU B 2 935  ? 140.408 161.129 127.868 1.00 48.55  ? 932  LEU A CG    1 
ATOM   7493  C CD1   . LEU B 2 935  ? 140.810 162.185 128.876 1.00 48.55  ? 932  LEU A CD1   1 
ATOM   7494  C CD2   . LEU B 2 935  ? 139.377 161.676 126.903 1.00 48.55  ? 932  LEU A CD2   1 
ATOM   7495  N N     . ASN B 2 936  ? 144.592 161.473 125.185 1.00 48.55  ? 933  ASN A N     1 
ATOM   7496  C CA    . ASN B 2 936  ? 146.016 161.173 125.151 1.00 48.55  ? 933  ASN A CA    1 
ATOM   7497  C C     . ASN B 2 936  ? 146.884 162.345 125.586 1.00 48.55  ? 933  ASN A C     1 
ATOM   7498  O O     . ASN B 2 936  ? 148.112 162.214 125.596 1.00 48.55  ? 933  ASN A O     1 
ATOM   7499  C CB    . ASN B 2 936  ? 146.427 160.713 123.748 1.00 48.55  ? 933  ASN A CB    1 
ATOM   7500  C CG    . ASN B 2 936  ? 146.006 161.683 122.668 1.00 48.55  ? 933  ASN A CG    1 
ATOM   7501  O OD1   . ASN B 2 936  ? 145.277 162.641 122.927 1.00 48.55  ? 933  ASN A OD1   1 
ATOM   7502  N ND2   . ASN B 2 936  ? 146.457 161.437 121.445 1.00 48.55  ? 933  ASN A ND2   1 
ATOM   7503  N N     . THR B 2 937  ? 146.284 163.477 125.946 1.00 48.55  ? 934  THR A N     1 
ATOM   7504  C CA    . THR B 2 937  ? 147.011 164.639 126.451 1.00 48.55  ? 934  THR A CA    1 
ATOM   7505  C C     . THR B 2 937  ? 146.379 165.044 127.779 1.00 48.55  ? 934  THR A C     1 
ATOM   7506  O O     . THR B 2 937  ? 145.391 165.785 127.804 1.00 48.55  ? 934  THR A O     1 
ATOM   7507  C CB    . THR B 2 937  ? 146.986 165.789 125.449 1.00 48.55  ? 934  THR A CB    1 
ATOM   7508  O OG1   . THR B 2 937  ? 147.398 165.311 124.162 1.00 48.55  ? 934  THR A OG1   1 
ATOM   7509  C CG2   . THR B 2 937  ? 147.925 166.899 125.892 1.00 48.55  ? 934  THR A CG2   1 
ATOM   7510  N N     . ILE B 2 938  ? 146.951 164.563 128.880 1.00 48.55  ? 935  ILE A N     1 
ATOM   7511  C CA    . ILE B 2 938  ? 146.432 164.807 130.220 1.00 48.55  ? 935  ILE A CA    1 
ATOM   7512  C C     . ILE B 2 938  ? 147.472 165.591 131.007 1.00 48.55  ? 935  ILE A C     1 
ATOM   7513  O O     . ILE B 2 938  ? 148.640 165.189 131.073 1.00 48.55  ? 935  ILE A O     1 
ATOM   7514  C CB    . ILE B 2 938  ? 146.082 163.494 130.944 1.00 48.55  ? 935  ILE A CB    1 
ATOM   7515  C CG1   . ILE B 2 938  ? 144.910 162.797 130.253 1.00 48.55  ? 935  ILE A CG1   1 
ATOM   7516  C CG2   . ILE B 2 938  ? 145.755 163.761 132.403 1.00 48.55  ? 935  ILE A CG2   1 
ATOM   7517  C CD1   . ILE B 2 938  ? 144.786 161.330 130.599 1.00 48.55  ? 935  ILE A CD1   1 
ATOM   7518  N N     . GLN B 2 939  ? 147.043 166.704 131.602 1.00 48.55  ? 936  GLN A N     1 
ATOM   7519  C CA    . GLN B 2 939  ? 147.902 167.559 132.422 1.00 48.55  ? 936  GLN A CA    1 
ATOM   7520  C C     . GLN B 2 939  ? 149.136 168.010 131.644 1.00 48.55  ? 936  GLN A C     1 
ATOM   7521  O O     . GLN B 2 939  ? 150.271 167.920 132.117 1.00 48.55  ? 936  GLN A O     1 
ATOM   7522  C CB    . GLN B 2 939  ? 148.294 166.856 133.722 1.00 48.55  ? 936  GLN A CB    1 
ATOM   7523  C CG    . GLN B 2 939  ? 148.706 167.801 134.842 1.00 48.55  ? 936  GLN A CG    1 
ATOM   7524  C CD    . GLN B 2 939  ? 147.667 168.870 135.118 1.00 48.55  ? 936  GLN A CD    1 
ATOM   7525  O OE1   . GLN B 2 939  ? 146.466 168.598 135.134 1.00 48.55  ? 936  GLN A OE1   1 
ATOM   7526  N NE2   . GLN B 2 939  ? 148.125 170.097 135.337 1.00 48.55  ? 936  GLN A NE2   1 
ATOM   7527  N N     . GLN B 2 940  ? 148.896 168.502 130.428 1.00 48.55  ? 937  GLN A N     1 
ATOM   7528  C CA    . GLN B 2 940  ? 149.950 169.037 129.567 1.00 48.55  ? 937  GLN A CA    1 
ATOM   7529  C C     . GLN B 2 940  ? 151.044 167.997 129.331 1.00 48.55  ? 937  GLN A C     1 
ATOM   7530  O O     . GLN B 2 940  ? 152.230 168.242 129.562 1.00 48.55  ? 937  GLN A O     1 
ATOM   7531  C CB    . GLN B 2 940  ? 150.529 170.328 130.152 1.00 45.50  ? 937  GLN A CB    1 
ATOM   7532  C CG    . GLN B 2 940  ? 151.296 171.186 129.157 1.00 45.50  ? 937  GLN A CG    1 
ATOM   7533  C CD    . GLN B 2 940  ? 150.426 171.678 128.017 1.00 45.50  ? 937  GLN A CD    1 
ATOM   7534  O OE1   . GLN B 2 940  ? 150.500 171.168 126.899 1.00 45.50  ? 937  GLN A OE1   1 
ATOM   7535  N NE2   . GLN B 2 940  ? 149.595 172.675 128.296 1.00 45.50  ? 937  GLN A NE2   1 
ATOM   7536  N N     . PHE B 2 941  ? 150.635 166.812 128.885 1.00 48.55  ? 938  PHE A N     1 
ATOM   7537  C CA    . PHE B 2 941  ? 151.575 165.739 128.589 1.00 48.55  ? 938  PHE A CA    1 
ATOM   7538  C C     . PHE B 2 941  ? 150.924 164.762 127.625 1.00 48.55  ? 938  PHE A C     1 
ATOM   7539  O O     . PHE B 2 941  ? 149.834 164.253 127.899 1.00 48.55  ? 938  PHE A O     1 
ATOM   7540  C CB    . PHE B 2 941  ? 152.007 165.016 129.867 1.00 48.55  ? 938  PHE A CB    1 
ATOM   7541  C CG    . PHE B 2 941  ? 153.126 164.042 129.659 1.00 48.55  ? 938  PHE A CG    1 
ATOM   7542  C CD1   . PHE B 2 941  ? 154.443 164.463 129.698 1.00 48.55  ? 938  PHE A CD1   1 
ATOM   7543  C CD2   . PHE B 2 941  ? 152.863 162.706 129.428 1.00 48.55  ? 938  PHE A CD2   1 
ATOM   7544  C CE1   . PHE B 2 941  ? 155.475 163.570 129.507 1.00 48.55  ? 938  PHE A CE1   1 
ATOM   7545  C CE2   . PHE B 2 941  ? 153.889 161.811 129.237 1.00 48.55  ? 938  PHE A CE2   1 
ATOM   7546  C CZ    . PHE B 2 941  ? 155.198 162.242 129.277 1.00 48.55  ? 938  PHE A CZ    1 
ATOM   7547  N N     . ASP B 2 942  ? 151.596 164.496 126.508 1.00 48.55  ? 939  ASP A N     1 
ATOM   7548  C CA    . ASP B 2 942  ? 151.091 163.574 125.499 1.00 48.55  ? 939  ASP A CA    1 
ATOM   7549  C C     . ASP B 2 942  ? 151.589 162.170 125.815 1.00 48.55  ? 939  ASP A C     1 
ATOM   7550  O O     . ASP B 2 942  ? 152.800 161.928 125.846 1.00 48.55  ? 939  ASP A O     1 
ATOM   7551  C CB    . ASP B 2 942  ? 151.533 164.001 124.101 1.00 48.55  ? 939  ASP A CB    1 
ATOM   7552  C CG    . ASP B 2 942  ? 150.630 163.457 123.015 1.00 48.55  ? 939  ASP A CG    1 
ATOM   7553  O OD1   . ASP B 2 942  ? 150.260 162.266 123.087 1.00 48.55  ? 939  ASP A OD1   1 
ATOM   7554  O OD2   . ASP B 2 942  ? 150.290 164.220 122.087 1.00 48.55  ? 939  ASP A OD2   1 
ATOM   7555  N N     . TYR B 2 943  ? 150.656 161.248 126.050 1.00 48.55  ? 940  TYR A N     1 
ATOM   7556  C CA    . TYR B 2 943  ? 151.020 159.891 126.434 1.00 48.55  ? 940  TYR A CA    1 
ATOM   7557  C C     . TYR B 2 943  ? 151.147 158.956 125.239 1.00 48.55  ? 940  TYR A C     1 
ATOM   7558  O O     . TYR B 2 943  ? 152.107 158.181 125.162 1.00 48.55  ? 940  TYR A O     1 
ATOM   7559  C CB    . TYR B 2 943  ? 149.991 159.328 127.415 1.00 48.55  ? 940  TYR A CB    1 
ATOM   7560  C CG    . TYR B 2 943  ? 150.193 159.773 128.844 1.00 48.55  ? 940  TYR A CG    1 
ATOM   7561  C CD1   . TYR B 2 943  ? 149.665 160.972 129.298 1.00 48.55  ? 940  TYR A CD1   1 
ATOM   7562  C CD2   . TYR B 2 943  ? 150.903 158.990 129.742 1.00 48.55  ? 940  TYR A CD2   1 
ATOM   7563  C CE1   . TYR B 2 943  ? 149.843 161.382 130.603 1.00 48.55  ? 940  TYR A CE1   1 
ATOM   7564  C CE2   . TYR B 2 943  ? 151.087 159.392 131.049 1.00 48.55  ? 940  TYR A CE2   1 
ATOM   7565  C CZ    . TYR B 2 943  ? 150.553 160.589 131.474 1.00 48.55  ? 940  TYR A CZ    1 
ATOM   7566  O OH    . TYR B 2 943  ? 150.732 160.998 132.775 1.00 48.55  ? 940  TYR A OH    1 
ATOM   7567  N N     . GLN B 2 944  ? 150.201 159.010 124.302 1.00 48.55  ? 941  GLN A N     1 
ATOM   7568  C CA    . GLN B 2 944  ? 150.179 158.091 123.171 1.00 48.55  ? 941  GLN A CA    1 
ATOM   7569  C C     . GLN B 2 944  ? 151.024 158.580 122.004 1.00 48.55  ? 941  GLN A C     1 
ATOM   7570  O O     . GLN B 2 944  ? 151.882 157.842 121.511 1.00 48.55  ? 941  GLN A O     1 
ATOM   7571  C CB    . GLN B 2 944  ? 148.741 157.863 122.693 1.00 48.55  ? 941  GLN A CB    1 
ATOM   7572  C CG    . GLN B 2 944  ? 148.566 156.624 121.817 1.00 48.55  ? 941  GLN A CG    1 
ATOM   7573  C CD    . GLN B 2 944  ? 148.981 156.845 120.374 1.00 48.55  ? 941  GLN A CD    1 
ATOM   7574  O OE1   . GLN B 2 944  ? 149.021 157.976 119.891 1.00 48.55  ? 941  GLN A OE1   1 
ATOM   7575  N NE2   . GLN B 2 944  ? 149.295 155.758 119.678 1.00 48.55  ? 941  GLN A NE2   1 
ATOM   7576  N N     . LYS B 2 945  ? 150.782 159.808 121.542 1.00 48.55  ? 942  LYS A N     1 
ATOM   7577  C CA    . LYS B 2 945  ? 151.452 160.291 120.340 1.00 48.55  ? 942  LYS A CA    1 
ATOM   7578  C C     . LYS B 2 945  ? 152.966 160.264 120.487 1.00 48.55  ? 942  LYS A C     1 
ATOM   7579  O O     . LYS B 2 945  ? 153.674 159.946 119.524 1.00 48.55  ? 942  LYS A O     1 
ATOM   7580  C CB    . LYS B 2 945  ? 150.971 161.702 120.003 1.00 47.82  ? 942  LYS A CB    1 
ATOM   7581  C CG    . LYS B 2 945  ? 149.478 161.798 119.742 1.00 47.82  ? 942  LYS A CG    1 
ATOM   7582  C CD    . LYS B 2 945  ? 149.092 163.169 119.216 1.00 47.82  ? 942  LYS A CD    1 
ATOM   7583  C CE    . LYS B 2 945  ? 147.611 163.229 118.897 1.00 47.82  ? 942  LYS A CE    1 
ATOM   7584  N NZ    . LYS B 2 945  ? 147.257 164.461 118.143 1.00 47.82  ? 942  LYS A NZ    1 
ATOM   7585  N N     . LYS B 2 946  ? 153.484 160.584 121.673 1.00 48.55  ? 943  LYS A N     1 
ATOM   7586  C CA    . LYS B 2 946  ? 154.928 160.579 121.876 1.00 48.55  ? 943  LYS A CA    1 
ATOM   7587  C C     . LYS B 2 946  ? 155.378 159.525 122.879 1.00 48.55  ? 943  LYS A C     1 
ATOM   7588  O O     . LYS B 2 946  ? 156.135 158.625 122.505 1.00 48.55  ? 943  LYS A O     1 
ATOM   7589  C CB    . LYS B 2 946  ? 155.407 161.969 122.316 1.00 48.55  ? 943  LYS A CB    1 
ATOM   7590  C CG    . LYS B 2 946  ? 154.733 163.135 121.591 1.00 48.55  ? 943  LYS A CG    1 
ATOM   7591  C CD    . LYS B 2 946  ? 154.918 163.054 120.074 1.00 48.55  ? 943  LYS A CD    1 
ATOM   7592  C CE    . LYS B 2 946  ? 156.386 163.062 119.665 1.00 48.55  ? 943  LYS A CE    1 
ATOM   7593  N NZ    . LYS B 2 946  ? 157.066 164.351 119.990 1.00 48.55  ? 943  LYS A NZ    1 
ATOM   7594  N N     . LEU B 2 947  ? 154.915 159.579 124.130 1.00 48.55  ? 944  LEU A N     1 
ATOM   7595  C CA    . LEU B 2 947  ? 155.567 158.797 125.180 1.00 48.55  ? 944  LEU A CA    1 
ATOM   7596  C C     . LEU B 2 947  ? 155.424 157.301 124.936 1.00 48.55  ? 944  LEU A C     1 
ATOM   7597  O O     . LEU B 2 947  ? 156.410 156.558 124.996 1.00 48.55  ? 944  LEU A O     1 
ATOM   7598  C CB    . LEU B 2 947  ? 155.014 159.163 126.555 1.00 48.55  ? 944  LEU A CB    1 
ATOM   7599  C CG    . LEU B 2 947  ? 155.807 158.465 127.667 1.00 48.55  ? 944  LEU A CG    1 
ATOM   7600  C CD1   . LEU B 2 947  ? 157.254 158.940 127.684 1.00 48.55  ? 944  LEU A CD1   1 
ATOM   7601  C CD2   . LEU B 2 947  ? 155.164 158.657 129.027 1.00 48.55  ? 944  LEU A CD2   1 
ATOM   7602  N N     . ASP B 2 948  ? 154.207 156.837 124.663 1.00 48.55  ? 945  ASP A N     1 
ATOM   7603  C CA    . ASP B 2 948  ? 154.025 155.413 124.414 1.00 48.55  ? 945  ASP A CA    1 
ATOM   7604  C C     . ASP B 2 948  ? 154.656 155.003 123.089 1.00 48.55  ? 945  ASP A C     1 
ATOM   7605  O O     . ASP B 2 948  ? 155.101 153.860 122.937 1.00 48.55  ? 945  ASP A O     1 
ATOM   7606  C CB    . ASP B 2 948  ? 152.539 155.062 124.444 1.00 48.55  ? 945  ASP A CB    1 
ATOM   7607  C CG    . ASP B 2 948  ? 152.296 153.571 124.444 1.00 48.55  ? 945  ASP A CG    1 
ATOM   7608  O OD1   . ASP B 2 948  ? 152.525 152.932 125.491 1.00 48.55  ? 945  ASP A OD1   1 
ATOM   7609  O OD2   . ASP B 2 948  ? 151.874 153.036 123.398 1.00 48.55  ? 945  ASP A OD2   1 
ATOM   7610  N N     . ASN B 2 949  ? 154.715 155.924 122.123 1.00 48.55  ? 946  ASN A N     1 
ATOM   7611  C CA    . ASN B 2 949  ? 155.264 155.583 120.813 1.00 48.55  ? 946  ASN A CA    1 
ATOM   7612  C C     . ASN B 2 949  ? 156.778 155.410 120.861 1.00 48.55  ? 946  ASN A C     1 
ATOM   7613  O O     . ASN B 2 949  ? 157.312 154.437 120.316 1.00 48.55  ? 946  ASN A O     1 
ATOM   7614  C CB    . ASN B 2 949  ? 154.879 156.646 119.785 1.00 48.55  ? 946  ASN A CB    1 
ATOM   7615  C CG    . ASN B 2 949  ? 153.468 156.466 119.265 1.00 48.55  ? 946  ASN A CG    1 
ATOM   7616  O OD1   . ASN B 2 949  ? 152.747 155.565 119.692 1.00 48.55  ? 946  ASN A OD1   1 
ATOM   7617  N ND2   . ASN B 2 949  ? 153.068 157.322 118.331 1.00 48.55  ? 946  ASN A ND2   1 
ATOM   7618  N N     . ARG B 2 950  ? 157.492 156.346 121.494 1.00 48.55  ? 947  ARG A N     1 
ATOM   7619  C CA    . ARG B 2 950  ? 158.936 156.175 121.643 1.00 48.55  ? 947  ARG A CA    1 
ATOM   7620  C C     . ARG B 2 950  ? 159.269 155.000 122.552 1.00 48.55  ? 947  ARG A C     1 
ATOM   7621  O O     . ARG B 2 950  ? 160.276 154.314 122.339 1.00 48.55  ? 947  ARG A O     1 
ATOM   7622  C CB    . ARG B 2 950  ? 159.594 157.460 122.149 1.00 48.55  ? 947  ARG A CB    1 
ATOM   7623  C CG    . ARG B 2 950  ? 159.769 158.549 121.090 1.00 48.55  ? 947  ARG A CG    1 
ATOM   7624  C CD    . ARG B 2 950  ? 158.557 159.432 120.885 1.00 48.55  ? 947  ARG A CD    1 
ATOM   7625  N NE    . ARG B 2 950  ? 158.877 160.575 120.038 1.00 48.55  ? 947  ARG A NE    1 
ATOM   7626  C CZ    . ARG B 2 950  ? 158.708 160.605 118.723 1.00 48.55  ? 947  ARG A CZ    1 
ATOM   7627  N NH1   . ARG B 2 950  ? 158.199 159.575 118.068 1.00 48.55  ? 947  ARG A NH1   1 
ATOM   7628  N NH2   . ARG B 2 950  ? 159.060 161.695 118.048 1.00 48.55  ? 947  ARG A NH2   1 
ATOM   7629  N N     . GLU B 2 951  ? 158.447 154.751 123.573 1.00 48.55  ? 948  GLU A N     1 
ATOM   7630  C CA    . GLU B 2 951  ? 158.616 153.531 124.354 1.00 48.55  ? 948  GLU A CA    1 
ATOM   7631  C C     . GLU B 2 951  ? 158.348 152.299 123.498 1.00 48.55  ? 948  GLU A C     1 
ATOM   7632  O O     . GLU B 2 951  ? 159.023 151.273 123.643 1.00 48.55  ? 948  GLU A O     1 
ATOM   7633  C CB    . GLU B 2 951  ? 157.703 153.552 125.580 1.00 48.55  ? 948  GLU A CB    1 
ATOM   7634  C CG    . GLU B 2 951  ? 158.163 154.494 126.680 1.00 48.55  ? 948  GLU A CG    1 
ATOM   7635  C CD    . GLU B 2 951  ? 159.124 153.835 127.649 1.00 48.55  ? 948  GLU A CD    1 
ATOM   7636  O OE1   . GLU B 2 951  ? 159.779 152.845 127.263 1.00 48.55  ? 948  GLU A OE1   1 
ATOM   7637  O OE2   . GLU B 2 951  ? 159.225 154.306 128.800 1.00 48.55  ? 948  GLU A OE2   1 
ATOM   7638  N N     . LYS B 2 952  ? 157.362 152.382 122.601 1.00 48.55  ? 949  LYS A N     1 
ATOM   7639  C CA    . LYS B 2 952  ? 157.143 151.304 121.642 1.00 48.55  ? 949  LYS A CA    1 
ATOM   7640  C C     . LYS B 2 952  ? 158.328 151.164 120.695 1.00 48.55  ? 949  LYS A C     1 
ATOM   7641  O O     . LYS B 2 952  ? 158.714 150.047 120.332 1.00 48.55  ? 949  LYS A O     1 
ATOM   7642  C CB    . LYS B 2 952  ? 155.854 151.549 120.859 1.00 48.55  ? 949  LYS A CB    1 
ATOM   7643  C CG    . LYS B 2 952  ? 155.535 150.475 119.831 1.00 48.55  ? 949  LYS A CG    1 
ATOM   7644  C CD    . LYS B 2 952  ? 155.197 149.152 120.499 1.00 48.55  ? 949  LYS A CD    1 
ATOM   7645  C CE    . LYS B 2 952  ? 154.728 148.125 119.481 1.00 48.55  ? 949  LYS A CE    1 
ATOM   7646  N NZ    . LYS B 2 952  ? 155.816 147.738 118.540 1.00 48.55  ? 949  LYS A NZ    1 
ATOM   7647  N N     . GLU B 2 953  ? 158.915 152.290 120.282 1.00 50.18  ? 950  GLU A N     1 
ATOM   7648  C CA    . GLU B 2 953  ? 160.096 152.244 119.425 1.00 50.18  ? 950  GLU A CA    1 
ATOM   7649  C C     . GLU B 2 953  ? 161.266 151.572 120.135 1.00 50.18  ? 950  GLU A C     1 
ATOM   7650  O O     . GLU B 2 953  ? 162.069 150.876 119.503 1.00 50.18  ? 950  GLU A O     1 
ATOM   7651  C CB    . GLU B 2 953  ? 160.468 153.658 118.979 1.00 50.18  ? 950  GLU A CB    1 
ATOM   7652  C CG    . GLU B 2 953  ? 161.768 153.756 118.201 1.00 50.18  ? 950  GLU A CG    1 
ATOM   7653  C CD    . GLU B 2 953  ? 162.448 155.099 118.375 1.00 50.18  ? 950  GLU A CD    1 
ATOM   7654  O OE1   . GLU B 2 953  ? 163.082 155.314 119.430 1.00 50.18  ? 950  GLU A OE1   1 
ATOM   7655  O OE2   . GLU B 2 953  ? 162.349 155.940 117.457 1.00 50.18  ? 950  GLU A OE2   1 
ATOM   7656  N N     . ARG B 2 954  ? 161.376 151.768 121.452 1.00 55.08  ? 951  ARG A N     1 
ATOM   7657  C CA    . ARG B 2 954  ? 162.415 151.092 122.221 1.00 55.08  ? 951  ARG A CA    1 
ATOM   7658  C C     . ARG B 2 954  ? 162.239 149.580 122.183 1.00 55.08  ? 951  ARG A C     1 
ATOM   7659  O O     . ARG B 2 954  ? 163.222 148.836 122.083 1.00 55.08  ? 951  ARG A O     1 
ATOM   7660  C CB    . ARG B 2 954  ? 162.406 151.589 123.666 1.00 55.08  ? 951  ARG A CB    1 
ATOM   7661  C CG    . ARG B 2 954  ? 163.712 151.373 124.408 1.00 55.08  ? 951  ARG A CG    1 
ATOM   7662  C CD    . ARG B 2 954  ? 163.776 152.216 125.670 1.00 55.08  ? 951  ARG A CD    1 
ATOM   7663  N NE    . ARG B 2 954  ? 165.106 152.205 126.267 1.00 55.08  ? 951  ARG A NE    1 
ATOM   7664  C CZ    . ARG B 2 954  ? 165.982 153.194 126.160 1.00 55.08  ? 951  ARG A CZ    1 
ATOM   7665  N NH1   . ARG B 2 954  ? 165.701 154.294 125.482 1.00 55.08  ? 951  ARG A NH1   1 
ATOM   7666  N NH2   . ARG B 2 954  ? 167.169 153.077 126.748 1.00 55.08  ? 951  ARG A NH2   1 
ATOM   7667  N N     . VAL B 2 955  ? 160.994 149.106 122.277 1.00 53.67  ? 952  VAL A N     1 
ATOM   7668  C CA    . VAL B 2 955  ? 160.736 147.667 122.275 1.00 53.67  ? 952  VAL A CA    1 
ATOM   7669  C C     . VAL B 2 955  ? 161.198 147.045 120.963 1.00 53.67  ? 952  VAL A C     1 
ATOM   7670  O O     . VAL B 2 955  ? 161.840 145.988 120.948 1.00 53.67  ? 952  VAL A O     1 
ATOM   7671  C CB    . VAL B 2 955  ? 159.245 147.390 122.538 1.00 53.67  ? 952  VAL A CB    1 
ATOM   7672  C CG1   . VAL B 2 955  ? 158.922 145.927 122.298 1.00 53.67  ? 952  VAL A CG1   1 
ATOM   7673  C CG2   . VAL B 2 955  ? 158.884 147.781 123.954 1.00 53.67  ? 952  VAL A CG2   1 
ATOM   7674  N N     . ALA B 2 956  ? 160.880 147.693 119.841 1.00 52.77  ? 953  ALA A N     1 
ATOM   7675  C CA    . ALA B 2 956  ? 161.327 147.183 118.550 1.00 52.77  ? 953  ALA A CA    1 
ATOM   7676  C C     . ALA B 2 956  ? 162.845 147.197 118.438 1.00 52.77  ? 953  ALA A C     1 
ATOM   7677  O O     . ALA B 2 956  ? 163.427 146.330 117.778 1.00 52.77  ? 953  ALA A O     1 
ATOM   7678  C CB    . ALA B 2 956  ? 160.701 147.997 117.418 1.00 52.77  ? 953  ALA A CB    1 
ATOM   7679  N N     . ALA B 2 957  ? 163.500 148.171 119.070 1.00 55.10  ? 954  ALA A N     1 
ATOM   7680  C CA    . ALA B 2 957  ? 164.955 148.249 119.013 1.00 55.10  ? 954  ALA A CA    1 
ATOM   7681  C C     . ALA B 2 957  ? 165.618 147.239 119.943 1.00 55.10  ? 954  ALA A C     1 
ATOM   7682  O O     . ALA B 2 957  ? 166.681 146.699 119.616 1.00 55.10  ? 954  ALA A O     1 
ATOM   7683  C CB    . ALA B 2 957  ? 165.417 149.666 119.350 1.00 55.10  ? 954  ALA A CB    1 
ATOM   7684  N N     . ARG B 2 958  ? 165.014 146.968 121.100 1.00 60.77  ? 955  ARG A N     1 
ATOM   7685  C CA    . ARG B 2 958  ? 165.623 146.116 122.114 1.00 60.77  ? 955  ARG A CA    1 
ATOM   7686  C C     . ARG B 2 958  ? 164.871 144.805 122.312 1.00 60.77  ? 955  ARG A C     1 
ATOM   7687  O O     . ARG B 2 958  ? 165.466 143.731 122.188 1.00 60.77  ? 955  ARG A O     1 
ATOM   7688  C CB    . ARG B 2 958  ? 165.725 146.871 123.448 1.00 60.77  ? 955  ARG A CB    1 
ATOM   7689  C CG    . ARG B 2 958  ? 166.959 147.755 123.601 1.00 60.77  ? 955  ARG A CG    1 
ATOM   7690  C CD    . ARG B 2 958  ? 166.934 148.972 122.691 1.00 60.77  ? 955  ARG A CD    1 
ATOM   7691  N NE    . ARG B 2 958  ? 168.050 149.870 122.969 1.00 60.77  ? 955  ARG A NE    1 
ATOM   7692  C CZ    . ARG B 2 958  ? 168.339 150.953 122.261 1.00 60.77  ? 955  ARG A CZ    1 
ATOM   7693  N NH1   . ARG B 2 958  ? 167.610 151.311 121.217 1.00 60.77  ? 955  ARG A NH1   1 
ATOM   7694  N NH2   . ARG B 2 958  ? 169.385 151.696 122.610 1.00 60.77  ? 955  ARG A NH2   1 
ATOM   7695  N N     . GLN B 2 959  ? 163.571 144.868 122.613 1.00 60.20  ? 956  GLN A N     1 
ATOM   7696  C CA    . GLN B 2 959  ? 162.771 143.691 122.965 1.00 60.20  ? 956  GLN A CA    1 
ATOM   7697  C C     . GLN B 2 959  ? 163.355 142.971 124.181 1.00 60.20  ? 956  GLN A C     1 
ATOM   7698  O O     . GLN B 2 959  ? 163.432 141.742 124.231 1.00 60.20  ? 956  GLN A O     1 
ATOM   7699  C CB    . GLN B 2 959  ? 162.628 142.738 121.775 1.00 60.20  ? 956  GLN A CB    1 
ATOM   7700  C CG    . GLN B 2 959  ? 161.378 141.878 121.822 1.00 60.20  ? 956  GLN A CG    1 
ATOM   7701  C CD    . GLN B 2 959  ? 160.120 142.666 121.529 1.00 60.20  ? 956  GLN A CD    1 
ATOM   7702  O OE1   . GLN B 2 959  ? 160.073 143.451 120.583 1.00 60.20  ? 956  GLN A OE1   1 
ATOM   7703  N NE2   . GLN B 2 959  ? 159.091 142.464 122.343 1.00 60.20  ? 956  GLN A NE2   1 
ATOM   7704  N N     . ALA B 2 960  ? 163.771 143.755 125.171 1.00 63.41  ? 957  ALA A N     1 
ATOM   7705  C CA    . ALA B 2 960  ? 164.322 143.222 126.406 1.00 63.41  ? 957  ALA A CA    1 
ATOM   7706  C C     . ALA B 2 960  ? 163.205 143.055 127.434 1.00 63.41  ? 957  ALA A C     1 
ATOM   7707  O O     . ALA B 2 960  ? 162.017 143.147 127.113 1.00 63.41  ? 957  ALA A O     1 
ATOM   7708  C CB    . ALA B 2 960  ? 165.441 144.126 126.918 1.00 63.41  ? 957  ALA A CB    1 
ATOM   7709  N N     . TRP B 2 961  ? 163.575 142.802 128.689 1.00 70.97  ? 958  TRP A N     1 
ATOM   7710  C CA    . TRP B 2 961  ? 162.588 142.666 129.753 1.00 70.97  ? 958  TRP A CA    1 
ATOM   7711  C C     . TRP B 2 961  ? 162.253 143.997 130.413 1.00 70.97  ? 958  TRP A C     1 
ATOM   7712  O O     . TRP B 2 961  ? 161.084 144.257 130.720 1.00 70.97  ? 958  TRP A O     1 
ATOM   7713  C CB    . TRP B 2 961  ? 163.082 141.688 130.821 1.00 70.97  ? 958  TRP A CB    1 
ATOM   7714  C CG    . TRP B 2 961  ? 163.139 140.263 130.378 1.00 70.97  ? 958  TRP A CG    1 
ATOM   7715  C CD1   . TRP B 2 961  ? 162.121 139.528 129.846 1.00 70.97  ? 958  TRP A CD1   1 
ATOM   7716  C CD2   . TRP B 2 961  ? 164.266 139.386 130.463 1.00 70.97  ? 958  TRP A CD2   1 
ATOM   7717  N NE1   . TRP B 2 961  ? 162.549 138.251 129.578 1.00 70.97  ? 958  TRP A NE1   1 
ATOM   7718  C CE2   . TRP B 2 961  ? 163.863 138.138 129.949 1.00 70.97  ? 958  TRP A CE2   1 
ATOM   7719  C CE3   . TRP B 2 961  ? 165.579 139.537 130.917 1.00 70.97  ? 958  TRP A CE3   1 
ATOM   7720  C CZ2   . TRP B 2 961  ? 164.726 137.050 129.877 1.00 70.97  ? 958  TRP A CZ2   1 
ATOM   7721  C CZ3   . TRP B 2 961  ? 166.433 138.456 130.844 1.00 70.97  ? 958  TRP A CZ3   1 
ATOM   7722  C CH2   . TRP B 2 961  ? 166.003 137.228 130.328 1.00 70.97  ? 958  TRP A CH2   1 
ATOM   7723  N N     . SER B 2 962  ? 163.260 144.842 130.642 1.00 59.99  ? 959  SER A N     1 
ATOM   7724  C CA    . SER B 2 962  ? 163.035 146.086 131.372 1.00 59.99  ? 959  SER A CA    1 
ATOM   7725  C C     . SER B 2 962  ? 162.076 147.004 130.627 1.00 59.99  ? 959  SER A C     1 
ATOM   7726  O O     . SER B 2 962  ? 161.215 147.644 131.241 1.00 59.99  ? 959  SER A O     1 
ATOM   7727  C CB    . SER B 2 962  ? 164.366 146.794 131.624 1.00 59.99  ? 959  SER A CB    1 
ATOM   7728  O OG    . SER B 2 962  ? 165.132 146.877 130.435 1.00 59.99  ? 959  SER A OG    1 
ATOM   7729  N N     . VAL B 2 963  ? 162.209 147.084 129.302 1.00 53.56  ? 960  VAL A N     1 
ATOM   7730  C CA    . VAL B 2 963  ? 161.350 147.970 128.522 1.00 53.56  ? 960  VAL A CA    1 
ATOM   7731  C C     . VAL B 2 963  ? 159.902 147.501 128.583 1.00 53.56  ? 960  VAL A C     1 
ATOM   7732  O O     . VAL B 2 963  ? 158.971 148.315 128.565 1.00 53.56  ? 960  VAL A O     1 
ATOM   7733  C CB    . VAL B 2 963  ? 161.857 148.066 127.073 1.00 53.56  ? 960  VAL A CB    1 
ATOM   7734  C CG1   . VAL B 2 963  ? 161.194 149.229 126.358 1.00 53.56  ? 960  VAL A CG1   1 
ATOM   7735  C CG2   . VAL B 2 963  ? 163.369 148.216 127.054 1.00 53.56  ? 960  VAL A CG2   1 
ATOM   7736  N N     . VAL B 2 964  ? 159.686 146.186 128.650 1.00 51.87  ? 961  VAL A N     1 
ATOM   7737  C CA    . VAL B 2 964  ? 158.329 145.663 128.779 1.00 51.87  ? 961  VAL A CA    1 
ATOM   7738  C C     . VAL B 2 964  ? 157.719 146.090 130.107 1.00 51.87  ? 961  VAL A C     1 
ATOM   7739  O O     . VAL B 2 964  ? 156.537 146.450 130.180 1.00 51.87  ? 961  VAL A O     1 
ATOM   7740  C CB    . VAL B 2 964  ? 158.328 144.132 128.618 1.00 51.87  ? 961  VAL A CB    1 
ATOM   7741  C CG1   . VAL B 2 964  ? 156.940 143.567 128.882 1.00 51.87  ? 961  VAL A CG1   1 
ATOM   7742  C CG2   . VAL B 2 964  ? 158.806 143.746 127.228 1.00 51.87  ? 961  VAL A CG2   1 
ATOM   7743  N N     . GLY B 2 965  ? 158.515 146.062 131.178 1.00 49.10  ? 962  GLY A N     1 
ATOM   7744  C CA    . GLY B 2 965  ? 158.002 146.457 132.480 1.00 49.10  ? 962  GLY A CA    1 
ATOM   7745  C C     . GLY B 2 965  ? 157.623 147.925 132.546 1.00 49.10  ? 962  GLY A C     1 
ATOM   7746  O O     . GLY B 2 965  ? 156.663 148.297 133.226 1.00 49.10  ? 962  GLY A O     1 
ATOM   7747  N N     . THR B 2 966  ? 158.375 148.779 131.849 1.00 48.55  ? 963  THR A N     1 
ATOM   7748  C CA    . THR B 2 966  ? 158.088 150.209 131.878 1.00 48.55  ? 963  THR A CA    1 
ATOM   7749  C C     . THR B 2 966  ? 156.751 150.523 131.219 1.00 48.55  ? 963  THR A C     1 
ATOM   7750  O O     . THR B 2 966  ? 156.005 151.389 131.692 1.00 48.55  ? 963  THR A O     1 
ATOM   7751  C CB    . THR B 2 966  ? 159.213 150.989 131.198 1.00 48.55  ? 963  THR A CB    1 
ATOM   7752  O OG1   . THR B 2 966  ? 159.315 150.587 129.826 1.00 48.55  ? 963  THR A OG1   1 
ATOM   7753  C CG2   . THR B 2 966  ? 160.538 150.737 131.900 1.00 48.55  ? 963  THR A CG2   1 
ATOM   7754  N N     . ILE B 2 967  ? 156.431 149.835 130.121 1.00 48.55  ? 964  ILE A N     1 
ATOM   7755  C CA    . ILE B 2 967  ? 155.185 150.110 129.410 1.00 48.55  ? 964  ILE A CA    1 
ATOM   7756  C C     . ILE B 2 967  ? 153.983 149.720 130.259 1.00 48.55  ? 964  ILE A C     1 
ATOM   7757  O O     . ILE B 2 967  ? 152.994 150.460 130.335 1.00 48.55  ? 964  ILE A O     1 
ATOM   7758  C CB    . ILE B 2 967  ? 155.177 149.393 128.048 1.00 48.55  ? 964  ILE A CB    1 
ATOM   7759  C CG1   . ILE B 2 967  ? 156.173 150.053 127.097 1.00 48.55  ? 964  ILE A CG1   1 
ATOM   7760  C CG2   . ILE B 2 967  ? 153.789 149.407 127.441 1.00 48.55  ? 964  ILE A CG2   1 
ATOM   7761  C CD1   . ILE B 2 967  ? 156.266 149.373 125.759 1.00 48.55  ? 964  ILE A CD1   1 
ATOM   7762  N N     . LYS B 2 968  ? 154.045 148.557 130.912 1.00 48.55  ? 965  LYS A N     1 
ATOM   7763  C CA    . LYS B 2 968  ? 152.933 148.129 131.755 1.00 48.55  ? 965  LYS A CA    1 
ATOM   7764  C C     . LYS B 2 968  ? 152.720 149.092 132.915 1.00 48.55  ? 965  LYS A C     1 
ATOM   7765  O O     . LYS B 2 968  ? 151.578 149.407 133.269 1.00 48.55  ? 965  LYS A O     1 
ATOM   7766  C CB    . LYS B 2 968  ? 153.176 146.712 132.271 1.00 48.55  ? 965  LYS A CB    1 
ATOM   7767  C CG    . LYS B 2 968  ? 151.906 145.978 132.672 1.00 48.55  ? 965  LYS A CG    1 
ATOM   7768  C CD    . LYS B 2 968  ? 152.220 144.644 133.329 1.00 48.55  ? 965  LYS A CD    1 
ATOM   7769  C CE    . LYS B 2 968  ? 151.860 144.659 134.806 1.00 48.55  ? 965  LYS A CE    1 
ATOM   7770  N NZ    . LYS B 2 968  ? 152.221 143.380 135.479 1.00 48.55  ? 965  LYS A NZ    1 
ATOM   7771  N N     . ASP B 2 969  ? 153.810 149.563 133.525 1.00 48.55  ? 966  ASP A N     1 
ATOM   7772  C CA    . ASP B 2 969  ? 153.690 150.556 134.588 1.00 48.55  ? 966  ASP A CA    1 
ATOM   7773  C C     . ASP B 2 969  ? 153.126 151.866 134.055 1.00 48.55  ? 966  ASP A C     1 
ATOM   7774  O O     . ASP B 2 969  ? 152.309 152.515 134.719 1.00 48.55  ? 966  ASP A O     1 
ATOM   7775  C CB    . ASP B 2 969  ? 155.050 150.785 135.247 1.00 48.55  ? 966  ASP A CB    1 
ATOM   7776  C CG    . ASP B 2 969  ? 155.544 149.568 136.003 1.00 48.55  ? 966  ASP A CG    1 
ATOM   7777  O OD1   . ASP B 2 969  ? 154.700 148.785 136.488 1.00 48.55  ? 966  ASP A OD1   1 
ATOM   7778  O OD2   . ASP B 2 969  ? 156.776 149.394 136.112 1.00 48.55  ? 966  ASP A OD2   1 
ATOM   7779  N N     . LEU B 2 970  ? 153.558 152.276 132.859 1.00 48.55  ? 967  LEU A N     1 
ATOM   7780  C CA    . LEU B 2 970  ? 153.086 153.534 132.291 1.00 48.55  ? 967  LEU A CA    1 
ATOM   7781  C C     . LEU B 2 970  ? 151.593 153.489 131.994 1.00 48.55  ? 967  LEU A C     1 
ATOM   7782  O O     . LEU B 2 970  ? 150.874 154.463 132.247 1.00 48.55  ? 967  LEU A O     1 
ATOM   7783  C CB    . LEU B 2 970  ? 153.873 153.866 131.025 1.00 48.55  ? 967  LEU A CB    1 
ATOM   7784  C CG    . LEU B 2 970  ? 153.285 154.983 130.165 1.00 48.55  ? 967  LEU A CG    1 
ATOM   7785  C CD1   . LEU B 2 970  ? 153.297 156.294 130.926 1.00 48.55  ? 967  LEU A CD1   1 
ATOM   7786  C CD2   . LEU B 2 970  ? 154.051 155.109 128.861 1.00 48.55  ? 967  LEU A CD2   1 
ATOM   7787  N N     . LYS B 2 971  ? 151.107 152.369 131.454 1.00 48.55  ? 968  LYS A N     1 
ATOM   7788  C CA    . LYS B 2 971  ? 149.688 152.268 131.128 1.00 48.55  ? 968  LYS A CA    1 
ATOM   7789  C C     . LYS B 2 971  ? 148.827 152.369 132.379 1.00 48.55  ? 968  LYS A C     1 
ATOM   7790  O O     . LYS B 2 971  ? 147.786 153.035 132.371 1.00 48.55  ? 968  LYS A O     1 
ATOM   7791  C CB    . LYS B 2 971  ? 149.407 150.965 130.384 1.00 48.55  ? 968  LYS A CB    1 
ATOM   7792  C CG    . LYS B 2 971  ? 149.988 150.917 128.984 1.00 48.55  ? 968  LYS A CG    1 
ATOM   7793  C CD    . LYS B 2 971  ? 149.547 149.667 128.248 1.00 48.55  ? 968  LYS A CD    1 
ATOM   7794  C CE    . LYS B 2 971  ? 150.261 149.539 126.916 1.00 48.55  ? 968  LYS A CE    1 
ATOM   7795  N NZ    . LYS B 2 971  ? 149.903 150.646 125.989 1.00 48.55  ? 968  LYS A NZ    1 
ATOM   7796  N N     . GLN B 2 972  ? 149.247 151.718 133.466 1.00 48.55  ? 969  GLN A N     1 
ATOM   7797  C CA    . GLN B 2 972  ? 148.515 151.837 134.722 1.00 48.55  ? 969  GLN A CA    1 
ATOM   7798  C C     . GLN B 2 972  ? 148.535 153.272 135.232 1.00 48.55  ? 969  GLN A C     1 
ATOM   7799  O O     . GLN B 2 972  ? 147.532 153.765 135.761 1.00 48.55  ? 969  GLN A O     1 
ATOM   7800  C CB    . GLN B 2 972  ? 149.099 150.884 135.764 1.00 39.00  ? 969  GLN A CB    1 
ATOM   7801  C CG    . GLN B 2 972  ? 148.368 149.557 135.865 1.00 39.00  ? 969  GLN A CG    1 
ATOM   7802  C CD    . GLN B 2 972  ? 149.285 148.415 136.258 1.00 39.00  ? 969  GLN A CD    1 
ATOM   7803  O OE1   . GLN B 2 972  ? 150.308 148.621 136.910 1.00 39.00  ? 969  GLN A OE1   1 
ATOM   7804  N NE2   . GLN B 2 972  ? 148.921 147.200 135.863 1.00 39.00  ? 969  GLN A NE2   1 
ATOM   7805  N N     . GLY B 2 973  ? 149.672 153.954 135.088 1.00 48.55  ? 970  GLY A N     1 
ATOM   7806  C CA    . GLY B 2 973  ? 149.729 155.359 135.458 1.00 48.55  ? 970  GLY A CA    1 
ATOM   7807  C C     . GLY B 2 973  ? 148.832 156.218 134.589 1.00 48.55  ? 970  GLY A C     1 
ATOM   7808  O O     . GLY B 2 973  ? 148.194 157.158 135.067 1.00 48.55  ? 970  GLY A O     1 
ATOM   7809  N N     . TYR B 2 974  ? 148.779 155.907 133.292 1.00 48.55  ? 971  TYR A N     1 
ATOM   7810  C CA    . TYR B 2 974  ? 147.852 156.591 132.398 1.00 48.55  ? 971  TYR A CA    1 
ATOM   7811  C C     . TYR B 2 974  ? 146.405 156.369 132.807 1.00 48.55  ? 971  TYR A C     1 
ATOM   7812  O O     . TYR B 2 974  ? 145.601 157.309 132.811 1.00 48.55  ? 971  TYR A O     1 
ATOM   7813  C CB    . TYR B 2 974  ? 148.065 156.119 130.962 1.00 48.55  ? 971  TYR A CB    1 
ATOM   7814  C CG    . TYR B 2 974  ? 147.175 156.821 129.969 1.00 48.55  ? 971  TYR A CG    1 
ATOM   7815  C CD1   . TYR B 2 974  ? 147.444 158.111 129.548 1.00 48.55  ? 971  TYR A CD1   1 
ATOM   7816  C CD2   . TYR B 2 974  ? 146.052 156.186 129.461 1.00 48.55  ? 971  TYR A CD2   1 
ATOM   7817  C CE1   . TYR B 2 974  ? 146.621 158.748 128.641 1.00 48.55  ? 971  TYR A CE1   1 
ATOM   7818  C CE2   . TYR B 2 974  ? 145.227 156.810 128.561 1.00 48.55  ? 971  TYR A CE2   1 
ATOM   7819  C CZ    . TYR B 2 974  ? 145.514 158.089 128.152 1.00 48.55  ? 971  TYR A CZ    1 
ATOM   7820  O OH    . TYR B 2 974  ? 144.683 158.704 127.249 1.00 48.55  ? 971  TYR A OH    1 
ATOM   7821  N N     . LEU B 2 975  ? 146.050 155.130 133.145 1.00 48.55  ? 972  LEU A N     1 
ATOM   7822  C CA    . LEU B 2 975  ? 144.661 154.827 133.471 1.00 48.55  ? 972  LEU A CA    1 
ATOM   7823  C C     . LEU B 2 975  ? 144.236 155.517 134.760 1.00 48.55  ? 972  LEU A C     1 
ATOM   7824  O O     . LEU B 2 975  ? 143.048 155.791 134.963 1.00 48.55  ? 972  LEU A O     1 
ATOM   7825  C CB    . LEU B 2 975  ? 144.471 153.315 133.562 1.00 48.55  ? 972  LEU A CB    1 
ATOM   7826  C CG    . LEU B 2 975  ? 144.638 152.606 132.216 1.00 48.55  ? 972  LEU A CG    1 
ATOM   7827  C CD1   . LEU B 2 975  ? 144.478 151.104 132.352 1.00 48.55  ? 972  LEU A CD1   1 
ATOM   7828  C CD2   . LEU B 2 975  ? 143.658 153.161 131.198 1.00 48.55  ? 972  LEU A CD2   1 
ATOM   7829  N N     . SER B 2 976  ? 145.194 155.810 135.642 1.00 48.55  ? 973  SER A N     1 
ATOM   7830  C CA    . SER B 2 976  ? 144.889 156.594 136.834 1.00 48.55  ? 973  SER A CA    1 
ATOM   7831  C C     . SER B 2 976  ? 144.473 158.012 136.462 1.00 48.55  ? 973  SER A C     1 
ATOM   7832  O O     . SER B 2 976  ? 143.527 158.566 137.034 1.00 48.55  ? 973  SER A O     1 
ATOM   7833  C CB    . SER B 2 976  ? 146.096 156.614 137.771 1.00 48.55  ? 973  SER A CB    1 
ATOM   7834  O OG    . SER B 2 976  ? 147.130 157.428 137.248 1.00 48.55  ? 973  SER A OG    1 
ATOM   7835  N N     . GLN B 2 977  ? 145.176 158.618 135.502 1.00 48.55  ? 974  GLN A N     1 
ATOM   7836  C CA    . GLN B 2 977  ? 144.815 159.957 135.049 1.00 48.55  ? 974  GLN A CA    1 
ATOM   7837  C C     . GLN B 2 977  ? 143.453 159.960 134.368 1.00 48.55  ? 974  GLN A C     1 
ATOM   7838  O O     . GLN B 2 977  ? 142.672 160.905 134.526 1.00 48.55  ? 974  GLN A O     1 
ATOM   7839  C CB    . GLN B 2 977  ? 145.886 160.498 134.102 1.00 48.55  ? 974  GLN A CB    1 
ATOM   7840  C CG    . GLN B 2 977  ? 147.312 160.287 134.576 1.00 48.55  ? 974  GLN A CG    1 
ATOM   7841  C CD    . GLN B 2 977  ? 147.652 161.119 135.792 1.00 48.55  ? 974  GLN A CD    1 
ATOM   7842  O OE1   . GLN B 2 977  ? 147.167 162.239 135.947 1.00 48.55  ? 974  GLN A OE1   1 
ATOM   7843  N NE2   . GLN B 2 977  ? 148.494 160.577 136.663 1.00 48.55  ? 974  GLN A NE2   1 
ATOM   7844  N N     . VAL B 2 978  ? 143.155 158.911 133.599 1.00 48.55  ? 975  VAL A N     1 
ATOM   7845  C CA    . VAL B 2 978  ? 141.885 158.831 132.885 1.00 48.55  ? 975  VAL A CA    1 
ATOM   7846  C C     . VAL B 2 978  ? 140.719 158.720 133.861 1.00 48.55  ? 975  VAL A C     1 
ATOM   7847  O O     . VAL B 2 978  ? 139.610 159.186 133.571 1.00 48.55  ? 975  VAL A O     1 
ATOM   7848  C CB    . VAL B 2 978  ? 141.932 157.656 131.889 1.00 48.55  ? 975  VAL A CB    1 
ATOM   7849  C CG1   . VAL B 2 978  ? 140.545 157.270 131.416 1.00 48.55  ? 975  VAL A CG1   1 
ATOM   7850  C CG2   . VAL B 2 978  ? 142.811 158.015 130.707 1.00 48.55  ? 975  VAL A CG2   1 
ATOM   7851  N N     . ILE B 2 979  ? 140.951 158.131 135.037 1.00 48.55  ? 976  ILE A N     1 
ATOM   7852  C CA    . ILE B 2 979  ? 139.895 158.013 136.041 1.00 48.55  ? 976  ILE A CA    1 
ATOM   7853  C C     . ILE B 2 979  ? 139.382 159.391 136.440 1.00 48.55  ? 976  ILE A C     1 
ATOM   7854  O O     . ILE B 2 979  ? 138.173 159.609 136.577 1.00 48.55  ? 976  ILE A O     1 
ATOM   7855  C CB    . ILE B 2 979  ? 140.402 157.227 137.263 1.00 48.55  ? 976  ILE A CB    1 
ATOM   7856  C CG1   . ILE B 2 979  ? 140.591 155.753 136.911 1.00 48.55  ? 976  ILE A CG1   1 
ATOM   7857  C CG2   . ILE B 2 979  ? 139.444 157.371 138.432 1.00 48.55  ? 976  ILE A CG2   1 
ATOM   7858  C CD1   . ILE B 2 979  ? 141.364 154.979 137.951 1.00 48.55  ? 976  ILE A CD1   1 
ATOM   7859  N N     . HIS B 2 980  ? 140.297 160.344 136.628 1.00 48.55  ? 977  HIS A N     1 
ATOM   7860  C CA    . HIS B 2 980  ? 139.899 161.679 137.064 1.00 48.55  ? 977  HIS A CA    1 
ATOM   7861  C C     . HIS B 2 980  ? 139.030 162.367 136.020 1.00 48.55  ? 977  HIS A C     1 
ATOM   7862  O O     . HIS B 2 980  ? 138.066 163.061 136.360 1.00 48.55  ? 977  HIS A O     1 
ATOM   7863  C CB    . HIS B 2 980  ? 141.134 162.524 137.369 1.00 48.55  ? 977  HIS A CB    1 
ATOM   7864  C CG    . HIS B 2 980  ? 140.839 163.982 137.531 1.00 48.55  ? 977  HIS A CG    1 
ATOM   7865  N ND1   . HIS B 2 980  ? 141.176 164.921 136.581 1.00 48.55  ? 977  HIS A ND1   1 
ATOM   7866  C CD2   . HIS B 2 980  ? 140.235 164.663 138.534 1.00 48.55  ? 977  HIS A CD2   1 
ATOM   7867  C CE1   . HIS B 2 980  ? 140.795 166.117 136.991 1.00 48.55  ? 977  HIS A CE1   1 
ATOM   7868  N NE2   . HIS B 2 980  ? 140.221 165.988 138.173 1.00 48.55  ? 977  HIS A NE2   1 
ATOM   7869  N N     . GLU B 2 981  ? 139.360 162.195 134.739 1.00 48.55  ? 978  GLU A N     1 
ATOM   7870  C CA    . GLU B 2 981  ? 138.604 162.883 133.698 1.00 48.55  ? 978  GLU A CA    1 
ATOM   7871  C C     . GLU B 2 981  ? 137.212 162.287 133.535 1.00 48.55  ? 978  GLU A C     1 
ATOM   7872  O O     . GLU B 2 981  ? 136.255 163.007 133.228 1.00 48.55  ? 978  GLU A O     1 
ATOM   7873  C CB    . GLU B 2 981  ? 139.365 162.842 132.373 1.00 48.55  ? 978  GLU A CB    1 
ATOM   7874  C CG    . GLU B 2 981  ? 138.958 163.924 131.369 1.00 48.55  ? 978  GLU A CG    1 
ATOM   7875  C CD    . GLU B 2 981  ? 138.835 165.320 131.969 1.00 48.55  ? 978  GLU A CD    1 
ATOM   7876  O OE1   . GLU B 2 981  ? 139.548 165.637 132.945 1.00 48.55  ? 978  GLU A OE1   1 
ATOM   7877  O OE2   . GLU B 2 981  ? 138.012 166.107 131.456 1.00 48.55  ? 978  GLU A OE2   1 
ATOM   7878  N N     . ILE B 2 982  ? 137.079 160.974 133.728 1.00 48.55  ? 979  ILE A N     1 
ATOM   7879  C CA    . ILE B 2 982  ? 135.768 160.339 133.616 1.00 48.55  ? 979  ILE A CA    1 
ATOM   7880  C C     . ILE B 2 982  ? 134.847 160.827 134.726 1.00 48.55  ? 979  ILE A C     1 
ATOM   7881  O O     . ILE B 2 982  ? 133.696 161.210 134.481 1.00 48.55  ? 979  ILE A O     1 
ATOM   7882  C CB    . ILE B 2 982  ? 135.907 158.807 133.640 1.00 48.55  ? 979  ILE A CB    1 
ATOM   7883  C CG1   . ILE B 2 982  ? 136.521 158.304 132.337 1.00 48.55  ? 979  ILE A CG1   1 
ATOM   7884  C CG2   . ILE B 2 982  ? 134.557 158.151 133.874 1.00 48.55  ? 979  ILE A CG2   1 
ATOM   7885  C CD1   . ILE B 2 982  ? 137.170 156.958 132.478 1.00 48.55  ? 979  ILE A CD1   1 
ATOM   7886  N N     . VAL B 2 983  ? 135.340 160.821 135.965 1.00 48.55  ? 980  VAL A N     1 
ATOM   7887  C CA    . VAL B 2 983  ? 134.512 161.245 137.089 1.00 48.55  ? 980  VAL A CA    1 
ATOM   7888  C C     . VAL B 2 983  ? 134.234 162.741 137.016 1.00 48.55  ? 980  VAL A C     1 
ATOM   7889  O O     . VAL B 2 983  ? 133.168 163.207 137.435 1.00 48.55  ? 980  VAL A O     1 
ATOM   7890  C CB    . VAL B 2 983  ? 135.166 160.839 138.424 1.00 48.55  ? 980  VAL A CB    1 
ATOM   7891  C CG1   . VAL B 2 983  ? 135.455 159.347 138.435 1.00 48.55  ? 980  VAL A CG1   1 
ATOM   7892  C CG2   . VAL B 2 983  ? 136.441 161.628 138.676 1.00 48.55  ? 980  VAL A CG2   1 
ATOM   7893  N N     . ASP B 2 984  ? 135.179 163.519 136.484 1.00 48.55  ? 981  ASP A N     1 
ATOM   7894  C CA    . ASP B 2 984  ? 134.955 164.953 136.332 1.00 48.55  ? 981  ASP A CA    1 
ATOM   7895  C C     . ASP B 2 984  ? 133.908 165.231 135.261 1.00 48.55  ? 981  ASP A C     1 
ATOM   7896  O O     . ASP B 2 984  ? 133.013 166.064 135.450 1.00 48.55  ? 981  ASP A O     1 
ATOM   7897  C CB    . ASP B 2 984  ? 136.269 165.657 135.998 1.00 48.55  ? 981  ASP A CB    1 
ATOM   7898  C CG    . ASP B 2 984  ? 136.238 167.136 136.325 1.00 48.55  ? 981  ASP A CG    1 
ATOM   7899  O OD1   . ASP B 2 984  ? 135.147 167.658 136.635 1.00 48.55  ? 981  ASP A OD1   1 
ATOM   7900  O OD2   . ASP B 2 984  ? 137.308 167.779 136.273 1.00 48.55  ? 981  ASP A OD2   1 
ATOM   7901  N N     . LEU B 2 985  ? 134.007 164.541 134.123 1.00 48.55  ? 982  LEU A N     1 
ATOM   7902  C CA    . LEU B 2 985  ? 133.044 164.751 133.046 1.00 48.55  ? 982  LEU A CA    1 
ATOM   7903  C C     . LEU B 2 985  ? 131.660 164.253 133.439 1.00 48.55  ? 982  LEU A C     1 
ATOM   7904  O O     . LEU B 2 985  ? 130.648 164.857 133.067 1.00 48.55  ? 982  LEU A O     1 
ATOM   7905  C CB    . LEU B 2 985  ? 133.519 164.055 131.773 1.00 48.55  ? 982  LEU A CB    1 
ATOM   7906  C CG    . LEU B 2 985  ? 132.699 164.371 130.523 1.00 48.55  ? 982  LEU A CG    1 
ATOM   7907  C CD1   . LEU B 2 985  ? 132.855 165.835 130.147 1.00 48.55  ? 982  LEU A CD1   1 
ATOM   7908  C CD2   . LEU B 2 985  ? 133.096 163.470 129.373 1.00 48.55  ? 982  LEU A CD2   1 
ATOM   7909  N N     . MET B 2 986  ? 131.598 163.148 134.184 1.00 48.55  ? 983  MET A N     1 
ATOM   7910  C CA    . MET B 2 986  ? 130.312 162.591 134.589 1.00 48.55  ? 983  MET A CA    1 
ATOM   7911  C C     . MET B 2 986  ? 129.524 163.576 135.440 1.00 48.55  ? 983  MET A C     1 
ATOM   7912  O O     . MET B 2 986  ? 128.331 163.798 135.209 1.00 48.55  ? 983  MET A O     1 
ATOM   7913  C CB    . MET B 2 986  ? 130.525 161.287 135.353 1.00 48.55  ? 983  MET A CB    1 
ATOM   7914  C CG    . MET B 2 986  ? 129.543 160.195 135.002 1.00 48.55  ? 983  MET A CG    1 
ATOM   7915  S SD    . MET B 2 986  ? 129.572 158.882 136.229 1.00 48.55  ? 983  MET A SD    1 
ATOM   7916  C CE    . MET B 2 986  ? 131.261 158.330 136.046 1.00 48.55  ? 983  MET A CE    1 
ATOM   7917  N N     . ILE B 2 987  ? 130.179 164.181 136.433 1.00 48.55  ? 984  ILE A N     1 
ATOM   7918  C CA    . ILE B 2 987  ? 129.474 165.073 137.348 1.00 48.55  ? 984  ILE A CA    1 
ATOM   7919  C C     . ILE B 2 987  ? 128.996 166.321 136.621 1.00 48.55  ? 984  ILE A C     1 
ATOM   7920  O O     . ILE B 2 987  ? 127.919 166.851 136.921 1.00 48.55  ? 984  ILE A O     1 
ATOM   7921  C CB    . ILE B 2 987  ? 130.369 165.416 138.556 1.00 48.55  ? 984  ILE A CB    1 
ATOM   7922  C CG1   . ILE B 2 987  ? 130.787 164.140 139.291 1.00 48.55  ? 984  ILE A CG1   1 
ATOM   7923  C CG2   . ILE B 2 987  ? 129.653 166.359 139.510 1.00 48.55  ? 984  ILE A CG2   1 
ATOM   7924  C CD1   . ILE B 2 987  ? 129.699 163.086 139.386 1.00 48.55  ? 984  ILE A CD1   1 
ATOM   7925  N N     . HIS B 2 988  ? 129.774 166.804 135.651 1.00 48.55  ? 985  HIS A N     1 
ATOM   7926  C CA    . HIS B 2 988  ? 129.358 167.973 134.884 1.00 48.55  ? 985  HIS A CA    1 
ATOM   7927  C C     . HIS B 2 988  ? 128.117 167.678 134.050 1.00 48.55  ? 985  HIS A C     1 
ATOM   7928  O O     . HIS B 2 988  ? 127.247 168.543 133.895 1.00 48.55  ? 985  HIS A O     1 
ATOM   7929  C CB    . HIS B 2 988  ? 130.506 168.452 133.996 1.00 48.55  ? 985  HIS A CB    1 
ATOM   7930  C CG    . HIS B 2 988  ? 130.099 169.471 132.979 1.00 48.55  ? 985  HIS A CG    1 
ATOM   7931  N ND1   . HIS B 2 988  ? 130.356 169.322 131.633 1.00 48.55  ? 985  HIS A ND1   1 
ATOM   7932  C CD2   . HIS B 2 988  ? 129.452 170.653 133.109 1.00 48.55  ? 985  HIS A CD2   1 
ATOM   7933  C CE1   . HIS B 2 988  ? 129.887 170.368 130.979 1.00 48.55  ? 985  HIS A CE1   1 
ATOM   7934  N NE2   . HIS B 2 988  ? 129.333 171.191 131.851 1.00 48.55  ? 985  HIS A NE2   1 
ATOM   7935  N N     . TYR B 2 989  ? 128.015 166.465 133.506 1.00 48.55  ? 986  TYR A N     1 
ATOM   7936  C CA    . TYR B 2 989  ? 126.886 166.088 132.668 1.00 48.55  ? 986  TYR A CA    1 
ATOM   7937  C C     . TYR B 2 989  ? 125.832 165.264 133.395 1.00 48.55  ? 986  TYR A C     1 
ATOM   7938  O O     . TYR B 2 989  ? 124.745 165.064 132.843 1.00 48.55  ? 986  TYR A O     1 
ATOM   7939  C CB    . TYR B 2 989  ? 127.371 165.305 131.441 1.00 48.55  ? 986  TYR A CB    1 
ATOM   7940  C CG    . TYR B 2 989  ? 127.916 166.172 130.331 1.00 48.55  ? 986  TYR A CG    1 
ATOM   7941  C CD1   . TYR B 2 989  ? 127.102 167.085 129.675 1.00 48.55  ? 986  TYR A CD1   1 
ATOM   7942  C CD2   . TYR B 2 989  ? 129.240 166.071 129.930 1.00 48.55  ? 986  TYR A CD2   1 
ATOM   7943  C CE1   . TYR B 2 989  ? 127.594 167.878 128.658 1.00 48.55  ? 986  TYR A CE1   1 
ATOM   7944  C CE2   . TYR B 2 989  ? 129.739 166.859 128.913 1.00 48.55  ? 986  TYR A CE2   1 
ATOM   7945  C CZ    . TYR B 2 989  ? 128.913 167.761 128.281 1.00 48.55  ? 986  TYR A CZ    1 
ATOM   7946  O OH    . TYR B 2 989  ? 129.409 168.547 127.268 1.00 48.55  ? 986  TYR A OH    1 
ATOM   7947  N N     . GLN B 2 990  ? 126.117 164.791 134.611 1.00 48.55  ? 987  GLN A N     1 
ATOM   7948  C CA    . GLN B 2 990  ? 125.200 163.931 135.362 1.00 48.55  ? 987  GLN A CA    1 
ATOM   7949  C C     . GLN B 2 990  ? 124.810 162.695 134.557 1.00 48.55  ? 987  GLN A C     1 
ATOM   7950  O O     . GLN B 2 990  ? 123.648 162.281 134.556 1.00 48.55  ? 987  GLN A O     1 
ATOM   7951  C CB    . GLN B 2 990  ? 123.950 164.701 135.801 1.00 48.55  ? 987  GLN A CB    1 
ATOM   7952  C CG    . GLN B 2 990  ? 124.226 165.802 136.811 1.00 48.55  ? 987  GLN A CG    1 
ATOM   7953  C CD    . GLN B 2 990  ? 122.976 166.257 137.533 1.00 48.55  ? 987  GLN A CD    1 
ATOM   7954  O OE1   . GLN B 2 990  ? 121.861 166.064 137.049 1.00 48.55  ? 987  GLN A OE1   1 
ATOM   7955  N NE2   . GLN B 2 990  ? 123.154 166.863 138.700 1.00 48.55  ? 987  GLN A NE2   1 
ATOM   7956  N N     . ALA B 2 991  ? 125.780 162.099 133.871 1.00 48.55  ? 988  ALA A N     1 
ATOM   7957  C CA    . ALA B 2 991  ? 125.527 161.058 132.891 1.00 48.55  ? 988  ALA A CA    1 
ATOM   7958  C C     . ALA B 2 991  ? 125.875 159.681 133.447 1.00 48.55  ? 988  ALA A C     1 
ATOM   7959  O O     . ALA B 2 991  ? 126.392 159.533 134.556 1.00 48.55  ? 988  ALA A O     1 
ATOM   7960  C CB    . ALA B 2 991  ? 126.317 161.336 131.611 1.00 48.55  ? 988  ALA A CB    1 
ATOM   7961  N N     . VAL B 2 992  ? 125.575 158.658 132.652 1.00 48.55  ? 989  VAL A N     1 
ATOM   7962  C CA    . VAL B 2 992  ? 125.946 157.278 132.936 1.00 48.55  ? 989  VAL A CA    1 
ATOM   7963  C C     . VAL B 2 992  ? 127.004 156.869 131.920 1.00 48.55  ? 989  VAL A C     1 
ATOM   7964  O O     . VAL B 2 992  ? 126.798 156.998 130.707 1.00 48.55  ? 989  VAL A O     1 
ATOM   7965  C CB    . VAL B 2 992  ? 124.725 156.343 132.907 1.00 48.55  ? 989  VAL A CB    1 
ATOM   7966  C CG1   . VAL B 2 992  ? 123.976 156.459 131.595 1.00 48.55  ? 989  VAL A CG1   1 
ATOM   7967  C CG2   . VAL B 2 992  ? 125.149 154.903 133.134 1.00 48.55  ? 989  VAL A CG2   1 
ATOM   7968  N N     . VAL B 2 993  ? 128.147 156.412 132.412 1.00 48.55  ? 990  VAL A N     1 
ATOM   7969  C CA    . VAL B 2 993  ? 129.283 156.098 131.556 1.00 48.55  ? 990  VAL A CA    1 
ATOM   7970  C C     . VAL B 2 993  ? 129.174 154.655 131.093 1.00 48.55  ? 990  VAL A C     1 
ATOM   7971  O O     . VAL B 2 993  ? 129.008 153.739 131.907 1.00 48.55  ? 990  VAL A O     1 
ATOM   7972  C CB    . VAL B 2 993  ? 130.611 156.347 132.288 1.00 48.55  ? 990  VAL A CB    1 
ATOM   7973  C CG1   . VAL B 2 993  ? 131.767 155.903 131.426 1.00 48.55  ? 990  VAL A CG1   1 
ATOM   7974  C CG2   . VAL B 2 993  ? 130.750 157.816 132.611 1.00 48.55  ? 990  VAL A CG2   1 
ATOM   7975  N N     . VAL B 2 994  ? 129.266 154.451 129.783 1.00 48.55  ? 991  VAL A N     1 
ATOM   7976  C CA    . VAL B 2 994  ? 129.131 153.137 129.172 1.00 48.55  ? 991  VAL A CA    1 
ATOM   7977  C C     . VAL B 2 994  ? 130.514 152.684 128.729 1.00 48.55  ? 991  VAL A C     1 
ATOM   7978  O O     . VAL B 2 994  ? 131.050 153.176 127.729 1.00 48.55  ? 991  VAL A O     1 
ATOM   7979  C CB    . VAL B 2 994  ? 128.148 153.155 127.996 1.00 48.55  ? 991  VAL A CB    1 
ATOM   7980  C CG1   . VAL B 2 994  ? 128.091 151.793 127.336 1.00 48.55  ? 991  VAL A CG1   1 
ATOM   7981  C CG2   . VAL B 2 994  ? 126.773 153.571 128.473 1.00 48.55  ? 991  VAL A CG2   1 
ATOM   7982  N N     . LEU B 2 995  ? 131.093 151.746 129.471 1.00 48.55  ? 992  LEU A N     1 
ATOM   7983  C CA    . LEU B 2 995  ? 132.358 151.135 129.099 1.00 48.55  ? 992  LEU A CA    1 
ATOM   7984  C C     . LEU B 2 995  ? 132.085 150.016 128.096 1.00 48.55  ? 992  LEU A C     1 
ATOM   7985  O O     . LEU B 2 995  ? 130.978 149.880 127.569 1.00 48.55  ? 992  LEU A O     1 
ATOM   7986  C CB    . LEU B 2 995  ? 133.092 150.613 130.333 1.00 48.55  ? 992  LEU A CB    1 
ATOM   7987  C CG    . LEU B 2 995  ? 133.922 151.560 131.207 1.00 48.55  ? 992  LEU A CG    1 
ATOM   7988  C CD1   . LEU B 2 995  ? 135.057 152.184 130.409 1.00 48.55  ? 992  LEU A CD1   1 
ATOM   7989  C CD2   . LEU B 2 995  ? 133.069 152.622 131.876 1.00 48.55  ? 992  LEU A CD2   1 
ATOM   7990  N N     . GLU B 2 996  ? 133.096 149.197 127.820 1.00 48.55  ? 993  GLU A N     1 
ATOM   7991  C CA    . GLU B 2 996  ? 132.934 148.011 126.988 1.00 48.55  ? 993  GLU A CA    1 
ATOM   7992  C C     . GLU B 2 996  ? 133.295 146.790 127.817 1.00 48.55  ? 993  GLU A C     1 
ATOM   7993  O O     . GLU B 2 996  ? 134.393 146.722 128.380 1.00 48.55  ? 993  GLU A O     1 
ATOM   7994  C CB    . GLU B 2 996  ? 133.800 148.092 125.726 1.00 48.55  ? 993  GLU A CB    1 
ATOM   7995  C CG    . GLU B 2 996  ? 135.245 148.491 125.971 1.00 48.55  ? 993  GLU A CG    1 
ATOM   7996  C CD    . GLU B 2 996  ? 136.069 148.500 124.699 1.00 48.55  ? 993  GLU A CD    1 
ATOM   7997  O OE1   . GLU B 2 996  ? 135.482 148.334 123.609 1.00 48.55  ? 993  GLU A OE1   1 
ATOM   7998  O OE2   . GLU B 2 996  ? 137.302 148.672 124.789 1.00 48.55  ? 993  GLU A OE2   1 
ATOM   7999  N N     . ASN B 2 997  ? 132.373 145.835 127.907 1.00 48.55  ? 994  ASN A N     1 
ATOM   8000  C CA    . ASN B 2 997  ? 132.650 144.619 128.655 1.00 48.55  ? 994  ASN A CA    1 
ATOM   8001  C C     . ASN B 2 997  ? 133.698 143.775 127.938 1.00 48.55  ? 994  ASN A C     1 
ATOM   8002  O O     . ASN B 2 997  ? 133.784 143.768 126.707 1.00 48.55  ? 994  ASN A O     1 
ATOM   8003  C CB    . ASN B 2 997  ? 131.357 143.832 128.912 1.00 48.55  ? 994  ASN A CB    1 
ATOM   8004  C CG    . ASN B 2 997  ? 130.808 143.134 127.674 1.00 48.55  ? 994  ASN A CG    1 
ATOM   8005  O OD1   . ASN B 2 997  ? 131.215 143.401 126.545 1.00 48.55  ? 994  ASN A OD1   1 
ATOM   8006  N ND2   . ASN B 2 997  ? 129.863 142.228 127.894 1.00 48.55  ? 994  ASN A ND2   1 
ATOM   8007  N N     . LEU B 2 998  ? 134.531 143.101 128.721 1.00 48.55  ? 995  LEU A N     1 
ATOM   8008  C CA    . LEU B 2 998  ? 135.673 142.378 128.183 1.00 48.55  ? 995  LEU A CA    1 
ATOM   8009  C C     . LEU B 2 998  ? 135.391 140.900 127.957 1.00 48.55  ? 995  LEU A C     1 
ATOM   8010  O O     . LEU B 2 998  ? 136.250 140.197 127.416 1.00 48.55  ? 995  LEU A O     1 
ATOM   8011  C CB    . LEU B 2 998  ? 136.878 142.548 129.111 1.00 48.55  ? 995  LEU A CB    1 
ATOM   8012  C CG    . LEU B 2 998  ? 137.277 144.000 129.392 1.00 48.55  ? 995  LEU A CG    1 
ATOM   8013  C CD1   . LEU B 2 998  ? 138.673 144.068 129.975 1.00 48.55  ? 995  LEU A CD1   1 
ATOM   8014  C CD2   . LEU B 2 998  ? 137.191 144.848 128.131 1.00 48.55  ? 995  LEU A CD2   1 
ATOM   8015  N N     . ASN B 2 999  ? 134.215 140.413 128.355 1.00 33.79  ? 996  ASN A N     1 
ATOM   8016  C CA    . ASN B 2 999  ? 133.862 139.026 128.078 1.00 33.79  ? 996  ASN A CA    1 
ATOM   8017  C C     . ASN B 2 999  ? 133.649 138.801 126.587 1.00 33.79  ? 996  ASN A C     1 
ATOM   8018  O O     . ASN B 2 999  ? 133.943 137.717 126.068 1.00 33.79  ? 996  ASN A O     1 
ATOM   8019  C CB    . ASN B 2 999  ? 132.610 138.634 128.861 1.00 33.79  ? 996  ASN A CB    1 
ATOM   8020  C CG    . ASN B 2 999  ? 132.810 138.718 130.359 1.00 33.79  ? 996  ASN A CG    1 
ATOM   8021  O OD1   . ASN B 2 999  ? 133.870 138.367 130.876 1.00 33.79  ? 996  ASN A OD1   1 
ATOM   8022  N ND2   . ASN B 2 999  ? 131.788 139.186 131.067 1.00 33.79  ? 996  ASN A ND2   1 
ATOM   8023  N N     . PHE B 2 1000 ? 133.140 139.808 125.886 1.00 33.41  ? 997  PHE A N     1 
ATOM   8024  C CA    . PHE B 2 1000 ? 132.775 139.693 124.483 1.00 33.41  ? 997  PHE A CA    1 
ATOM   8025  C C     . PHE B 2 1000 ? 133.749 140.477 123.614 1.00 33.41  ? 997  PHE A C     1 
ATOM   8026  O O     . PHE B 2 1000 ? 134.051 141.640 123.896 1.00 33.41  ? 997  PHE A O     1 
ATOM   8027  C CB    . PHE B 2 1000 ? 131.350 140.200 124.248 1.00 33.41  ? 997  PHE A CB    1 
ATOM   8028  C CG    . PHE B 2 1000 ? 130.288 139.338 124.868 1.00 33.41  ? 997  PHE A CG    1 
ATOM   8029  C CD1   . PHE B 2 1000 ? 130.582 138.058 125.309 1.00 33.41  ? 997  PHE A CD1   1 
ATOM   8030  C CD2   . PHE B 2 1000 ? 128.994 139.807 125.010 1.00 33.41  ? 997  PHE A CD2   1 
ATOM   8031  C CE1   . PHE B 2 1000 ? 129.607 137.265 125.880 1.00 33.41  ? 997  PHE A CE1   1 
ATOM   8032  C CE2   . PHE B 2 1000 ? 128.013 139.018 125.580 1.00 33.41  ? 997  PHE A CE2   1 
ATOM   8033  C CZ    . PHE B 2 1000 ? 128.321 137.745 126.015 1.00 33.41  ? 997  PHE A CZ    1 
ATOM   8034  N N     . GLY B 2 1001 ? 134.234 139.832 122.556 1.00 42.84  ? 998  GLY A N     1 
ATOM   8035  C CA    . GLY B 2 1001 ? 135.081 140.491 121.584 1.00 42.84  ? 998  GLY A CA    1 
ATOM   8036  C C     . GLY B 2 1001 ? 136.554 140.443 121.931 1.00 42.84  ? 998  GLY A C     1 
ATOM   8037  O O     . GLY B 2 1001 ? 136.979 139.983 122.995 1.00 42.84  ? 998  GLY A O     1 
ATOM   8038  N N     . PHE B 2 1002 ? 137.353 140.943 120.990 1.00 46.47  ? 999  PHE A N     1 
ATOM   8039  C CA    . PHE B 2 1002 ? 138.800 141.009 121.150 1.00 46.47  ? 999  PHE A CA    1 
ATOM   8040  C C     . PHE B 2 1002 ? 139.296 142.250 120.426 1.00 46.47  ? 999  PHE A C     1 
ATOM   8041  O O     . PHE B 2 1002 ? 138.751 142.617 119.380 1.00 46.47  ? 999  PHE A O     1 
ATOM   8042  C CB    . PHE B 2 1002 ? 139.481 139.751 120.600 1.00 46.47  ? 999  PHE A CB    1 
ATOM   8043  C CG    . PHE B 2 1002 ? 140.980 139.848 120.542 1.00 46.47  ? 999  PHE A CG    1 
ATOM   8044  C CD1   . PHE B 2 1002 ? 141.736 139.796 121.702 1.00 46.47  ? 999  PHE A CD1   1 
ATOM   8045  C CD2   . PHE B 2 1002 ? 141.632 139.990 119.329 1.00 46.47  ? 999  PHE A CD2   1 
ATOM   8046  C CE1   . PHE B 2 1002 ? 143.115 139.885 121.652 1.00 46.47  ? 999  PHE A CE1   1 
ATOM   8047  C CE2   . PHE B 2 1002 ? 143.011 140.079 119.272 1.00 46.47  ? 999  PHE A CE2   1 
ATOM   8048  C CZ    . PHE B 2 1002 ? 143.753 140.027 120.436 1.00 46.47  ? 999  PHE A CZ    1 
ATOM   8049  N N     . LYS B 2 1003 ? 140.321 142.890 120.979 1.00 41.06  ? 1000 LYS A N     1 
ATOM   8050  C CA    . LYS B 2 1003 ? 140.787 144.171 120.474 1.00 41.06  ? 1000 LYS A CA    1 
ATOM   8051  C C     . LYS B 2 1003 ? 142.063 143.986 119.662 1.00 41.06  ? 1000 LYS A C     1 
ATOM   8052  O O     . LYS B 2 1003 ? 142.929 143.182 120.020 1.00 41.06  ? 1000 LYS A O     1 
ATOM   8053  C CB    . LYS B 2 1003 ? 141.022 145.139 121.634 1.00 41.06  ? 1000 LYS A CB    1 
ATOM   8054  C CG    . LYS B 2 1003 ? 141.552 146.493 121.227 1.00 41.06  ? 1000 LYS A CG    1 
ATOM   8055  C CD    . LYS B 2 1003 ? 140.440 147.296 120.574 1.00 41.06  ? 1000 LYS A CD    1 
ATOM   8056  C CE    . LYS B 2 1003 ? 140.340 148.688 121.164 1.00 41.06  ? 1000 LYS A CE    1 
ATOM   8057  N NZ    . LYS B 2 1003 ? 139.238 149.473 120.542 1.00 41.06  ? 1000 LYS A NZ    1 
ATOM   8058  N N     . SER B 2 1004 ? 142.170 144.734 118.566 1.00 42.75  ? 1001 SER A N     1 
ATOM   8059  C CA    . SER B 2 1004 ? 143.292 144.592 117.651 1.00 42.75  ? 1001 SER A CA    1 
ATOM   8060  C C     . SER B 2 1004 ? 144.604 144.990 118.323 1.00 42.75  ? 1001 SER A C     1 
ATOM   8061  O O     . SER B 2 1004 ? 144.646 145.831 119.226 1.00 42.75  ? 1001 SER A O     1 
ATOM   8062  C CB    . SER B 2 1004 ? 143.070 145.438 116.397 1.00 42.75  ? 1001 SER A CB    1 
ATOM   8063  O OG    . SER B 2 1004 ? 144.251 145.514 115.618 1.00 42.75  ? 1001 SER A OG    1 
ATOM   8064  N N     . LYS B 2 1005 ? 145.691 144.364 117.864 1.00 40.58  ? 1002 LYS A N     1 
ATOM   8065  C CA    . LYS B 2 1005 ? 147.006 144.603 118.448 1.00 40.58  ? 1002 LYS A CA    1 
ATOM   8066  C C     . LYS B 2 1005 ? 147.525 146.009 118.178 1.00 40.58  ? 1002 LYS A C     1 
ATOM   8067  O O     . LYS B 2 1005 ? 148.429 146.465 118.886 1.00 40.58  ? 1002 LYS A O     1 
ATOM   8068  C CB    . LYS B 2 1005 ? 148.012 143.579 117.918 1.00 40.58  ? 1002 LYS A CB    1 
ATOM   8069  C CG    . LYS B 2 1005 ? 147.722 142.143 118.323 1.00 40.58  ? 1002 LYS A CG    1 
ATOM   8070  C CD    . LYS B 2 1005 ? 147.854 141.202 117.135 1.00 40.58  ? 1002 LYS A CD    1 
ATOM   8071  C CE    . LYS B 2 1005 ? 149.188 141.388 116.427 1.00 40.58  ? 1002 LYS A CE    1 
ATOM   8072  N NZ    . LYS B 2 1005 ? 149.190 140.780 115.068 1.00 40.58  ? 1002 LYS A NZ    1 
ATOM   8073  N N     . ARG B 2 1006 ? 146.985 146.702 117.173 1.00 42.20  ? 1003 ARG A N     1 
ATOM   8074  C CA    . ARG B 2 1006 ? 147.471 148.038 116.849 1.00 42.20  ? 1003 ARG A CA    1 
ATOM   8075  C C     . ARG B 2 1006 ? 147.066 149.076 117.887 1.00 42.20  ? 1003 ARG A C     1 
ATOM   8076  O O     . ARG B 2 1006 ? 147.622 150.179 117.890 1.00 42.20  ? 1003 ARG A O     1 
ATOM   8077  C CB    . ARG B 2 1006 ? 146.966 148.468 115.471 1.00 42.20  ? 1003 ARG A CB    1 
ATOM   8078  C CG    . ARG B 2 1006 ? 147.642 147.763 114.308 1.00 42.20  ? 1003 ARG A CG    1 
ATOM   8079  C CD    . ARG B 2 1006 ? 147.123 148.283 112.977 1.00 42.20  ? 1003 ARG A CD    1 
ATOM   8080  N NE    . ARG B 2 1006 ? 145.675 148.156 112.868 1.00 42.20  ? 1003 ARG A NE    1 
ATOM   8081  C CZ    . ARG B 2 1006 ? 145.040 147.026 112.589 1.00 42.20  ? 1003 ARG A CZ    1 
ATOM   8082  N NH1   . ARG B 2 1006 ? 145.698 145.897 112.378 1.00 42.20  ? 1003 ARG A NH1   1 
ATOM   8083  N NH2   . ARG B 2 1006 ? 143.712 147.028 112.518 1.00 42.20  ? 1003 ARG A NH2   1 
ATOM   8084  N N     . THR B 2 1007 ? 146.116 148.754 118.759 1.00 37.58  ? 1004 THR A N     1 
ATOM   8085  C CA    . THR B 2 1007 ? 145.658 149.713 119.752 1.00 37.58  ? 1004 THR A CA    1 
ATOM   8086  C C     . THR B 2 1007 ? 146.692 149.885 120.858 1.00 37.58  ? 1004 THR A C     1 
ATOM   8087  O O     . THR B 2 1007 ? 147.473 148.978 121.158 1.00 37.58  ? 1004 THR A O     1 
ATOM   8088  C CB    . THR B 2 1007 ? 144.325 149.268 120.345 1.00 37.58  ? 1004 THR A CB    1 
ATOM   8089  O OG1   . THR B 2 1007 ? 144.492 148.004 120.999 1.00 37.58  ? 1004 THR A OG1   1 
ATOM   8090  C CG2   . THR B 2 1007 ? 143.295 149.124 119.242 1.00 37.58  ? 1004 THR A CG2   1 
ATOM   8091  N N     . GLY B 2 1008 ? 146.693 151.073 121.463 1.00 34.84  ? 1005 GLY A N     1 
ATOM   8092  C CA    . GLY B 2 1008 ? 147.687 151.373 122.479 1.00 34.84  ? 1005 GLY A CA    1 
ATOM   8093  C C     . GLY B 2 1008 ? 147.541 150.525 123.728 1.00 34.84  ? 1005 GLY A C     1 
ATOM   8094  O O     . GLY B 2 1008 ? 148.528 149.999 124.249 1.00 34.84  ? 1005 GLY A O     1 
ATOM   8095  N N     . ILE B 2 1009 ? 146.316 150.365 124.214 1.00 33.36  ? 1006 ILE A N     1 
ATOM   8096  C CA    . ILE B 2 1009 ? 146.047 149.674 125.470 1.00 33.36  ? 1006 ILE A CA    1 
ATOM   8097  C C     . ILE B 2 1009 ? 145.886 148.186 125.197 1.00 33.36  ? 1006 ILE A C     1 
ATOM   8098  O O     . ILE B 2 1009 ? 145.222 147.785 124.234 1.00 33.36  ? 1006 ILE A O     1 
ATOM   8099  C CB    . ILE B 2 1009 ? 144.796 150.253 126.158 1.00 33.36  ? 1006 ILE A CB    1 
ATOM   8100  C CG1   . ILE B 2 1009 ? 145.020 151.723 126.512 1.00 33.36  ? 1006 ILE A CG1   1 
ATOM   8101  C CG2   . ILE B 2 1009 ? 144.446 149.457 127.404 1.00 33.36  ? 1006 ILE A CG2   1 
ATOM   8102  C CD1   . ILE B 2 1009 ? 146.185 151.954 127.445 1.00 33.36  ? 1006 ILE A CD1   1 
ATOM   8103  N N     . ALA B 2 1010 ? 146.495 147.362 126.052 1.00 37.19  ? 1007 ALA A N     1 
ATOM   8104  C CA    . ALA B 2 1010 ? 146.431 145.912 125.912 1.00 37.19  ? 1007 ALA A CA    1 
ATOM   8105  C C     . ALA B 2 1010 ? 145.010 145.399 126.108 1.00 37.19  ? 1007 ALA A C     1 
ATOM   8106  O O     . ALA B 2 1010 ? 144.104 146.170 126.440 1.00 37.19  ? 1007 ALA A O     1 
ATOM   8107  C CB    . ALA B 2 1010 ? 147.378 145.236 126.906 1.00 37.19  ? 1007 ALA A CB    1 
ATOM   8108  N N     . GLU B 2 1011 ? 144.808 144.100 125.912 1.00 42.29  ? 1008 GLU A N     1 
ATOM   8109  C CA    . GLU B 2 1011 ? 143.484 143.495 125.964 1.00 42.29  ? 1008 GLU A CA    1 
ATOM   8110  C C     . GLU B 2 1011 ? 143.304 142.753 127.283 1.00 42.29  ? 1008 GLU A C     1 
ATOM   8111  O O     . GLU B 2 1011 ? 144.039 141.802 127.570 1.00 42.29  ? 1008 GLU A O     1 
ATOM   8112  C CB    . GLU B 2 1011 ? 143.278 142.544 124.784 1.00 42.29  ? 1008 GLU A CB    1 
ATOM   8113  C CG    . GLU B 2 1011 ? 141.822 142.213 124.501 1.00 42.29  ? 1008 GLU A CG    1 
ATOM   8114  C CD    . GLU B 2 1011 ? 141.404 140.882 125.094 1.00 42.29  ? 1008 GLU A CD    1 
ATOM   8115  O OE1   . GLU B 2 1011 ? 142.210 139.929 125.049 1.00 42.29  ? 1008 GLU A OE1   1 
ATOM   8116  O OE2   . GLU B 2 1011 ? 140.268 140.788 125.605 1.00 42.29  ? 1008 GLU A OE2   1 
ATOM   8117  N N     . LYS B 2 1012 ? 142.348 143.214 128.091 1.00 38.26  ? 1009 LYS A N     1 
ATOM   8118  C CA    . LYS B 2 1012 ? 141.857 142.493 129.262 1.00 38.26  ? 1009 LYS A CA    1 
ATOM   8119  C C     . LYS B 2 1012 ? 142.911 142.380 130.359 1.00 38.26  ? 1009 LYS A C     1 
ATOM   8120  O O     . LYS B 2 1012 ? 142.639 141.832 131.432 1.00 38.26  ? 1009 LYS A O     1 
ATOM   8121  C CB    . LYS B 2 1012 ? 141.355 141.103 128.853 1.00 38.26  ? 1009 LYS A CB    1 
ATOM   8122  C CG    . LYS B 2 1012 ? 140.338 140.494 129.805 1.00 38.26  ? 1009 LYS A CG    1 
ATOM   8123  C CD    . LYS B 2 1012 ? 140.155 139.011 129.538 1.00 38.26  ? 1009 LYS A CD    1 
ATOM   8124  C CE    . LYS B 2 1012 ? 139.202 138.777 128.379 1.00 38.26  ? 1009 LYS A CE    1 
ATOM   8125  N NZ    . LYS B 2 1012 ? 137.780 138.919 128.796 1.00 38.26  ? 1009 LYS A NZ    1 
ATOM   8126  N N     . ALA B 2 1013 ? 144.112 142.899 130.109 1.00 36.48  ? 1010 ALA A N     1 
ATOM   8127  C CA    . ALA B 2 1013 ? 145.168 142.834 131.113 1.00 36.48  ? 1010 ALA A CA    1 
ATOM   8128  C C     . ALA B 2 1013 ? 145.146 144.062 132.015 1.00 36.48  ? 1010 ALA A C     1 
ATOM   8129  O O     . ALA B 2 1013 ? 145.008 143.947 133.238 1.00 36.48  ? 1010 ALA A O     1 
ATOM   8130  C CB    . ALA B 2 1013 ? 146.532 142.688 130.432 1.00 36.48  ? 1010 ALA A CB    1 
ATOM   8131  N N     . VAL B 2 1014 ? 145.274 145.249 131.425 1.00 48.55  ? 1011 VAL A N     1 
ATOM   8132  C CA    . VAL B 2 1014 ? 145.335 146.489 132.189 1.00 48.55  ? 1011 VAL A CA    1 
ATOM   8133  C C     . VAL B 2 1014 ? 143.977 147.175 132.171 1.00 48.55  ? 1011 VAL A C     1 
ATOM   8134  O O     . VAL B 2 1014 ? 143.639 147.930 133.090 1.00 48.55  ? 1011 VAL A O     1 
ATOM   8135  C CB    . VAL B 2 1014 ? 146.434 147.419 131.645 1.00 48.55  ? 1011 VAL A CB    1 
ATOM   8136  C CG1   . VAL B 2 1014 ? 147.799 146.776 131.818 1.00 48.55  ? 1011 VAL A CG1   1 
ATOM   8137  C CG2   . VAL B 2 1014 ? 146.184 147.740 130.183 1.00 48.55  ? 1011 VAL A CG2   1 
ATOM   8138  N N     . TYR B 2 1015 ? 143.186 146.919 131.127 1.00 48.55  ? 1012 TYR A N     1 
ATOM   8139  C CA    . TYR B 2 1015 ? 141.874 147.549 131.032 1.00 48.55  ? 1012 TYR A CA    1 
ATOM   8140  C C     . TYR B 2 1015 ? 140.870 146.908 131.979 1.00 48.55  ? 1012 TYR A C     1 
ATOM   8141  O O     . TYR B 2 1015 ? 139.963 147.590 132.470 1.00 48.55  ? 1012 TYR A O     1 
ATOM   8142  C CB    . TYR B 2 1015 ? 141.363 147.491 129.595 1.00 48.55  ? 1012 TYR A CB    1 
ATOM   8143  C CG    . TYR B 2 1015 ? 140.335 148.549 129.277 1.00 48.55  ? 1012 TYR A CG    1 
ATOM   8144  C CD1   . TYR B 2 1015 ? 140.720 149.844 128.961 1.00 48.55  ? 1012 TYR A CD1   1 
ATOM   8145  C CD2   . TYR B 2 1015 ? 138.979 148.258 129.305 1.00 48.55  ? 1012 TYR A CD2   1 
ATOM   8146  C CE1   . TYR B 2 1015 ? 139.785 150.816 128.671 1.00 48.55  ? 1012 TYR A CE1   1 
ATOM   8147  C CE2   . TYR B 2 1015 ? 138.035 149.224 129.016 1.00 48.55  ? 1012 TYR A CE2   1 
ATOM   8148  C CZ    . TYR B 2 1015 ? 138.444 150.501 128.700 1.00 48.55  ? 1012 TYR A CZ    1 
ATOM   8149  O OH    . TYR B 2 1015 ? 137.509 151.467 128.412 1.00 48.55  ? 1012 TYR A OH    1 
ATOM   8150  N N     . GLN B 2 1016 ? 141.007 145.607 132.241 1.00 48.55  ? 1013 GLN A N     1 
ATOM   8151  C CA    . GLN B 2 1016 ? 140.125 144.954 133.203 1.00 48.55  ? 1013 GLN A CA    1 
ATOM   8152  C C     . GLN B 2 1016 ? 140.330 145.520 134.601 1.00 48.55  ? 1013 GLN A C     1 
ATOM   8153  O O     . GLN B 2 1016 ? 139.367 145.707 135.353 1.00 48.55  ? 1013 GLN A O     1 
ATOM   8154  C CB    . GLN B 2 1016 ? 140.359 143.444 133.188 1.00 48.55  ? 1013 GLN A CB    1 
ATOM   8155  C CG    . GLN B 2 1016 ? 139.381 142.658 134.038 1.00 48.55  ? 1013 GLN A CG    1 
ATOM   8156  C CD    . GLN B 2 1016 ? 137.952 142.781 133.549 1.00 48.55  ? 1013 GLN A CD    1 
ATOM   8157  O OE1   . GLN B 2 1016 ? 137.144 143.499 134.136 1.00 48.55  ? 1013 GLN A OE1   1 
ATOM   8158  N NE2   . GLN B 2 1016 ? 137.632 142.075 132.471 1.00 48.55  ? 1013 GLN A NE2   1 
ATOM   8159  N N     . GLN B 2 1017 ? 141.584 145.796 134.968 1.00 48.55  ? 1014 GLN A N     1 
ATOM   8160  C CA    . GLN B 2 1017 ? 141.858 146.460 136.236 1.00 48.55  ? 1014 GLN A CA    1 
ATOM   8161  C C     . GLN B 2 1017 ? 141.356 147.898 136.231 1.00 48.55  ? 1014 GLN A C     1 
ATOM   8162  O O     . GLN B 2 1017 ? 140.934 148.410 137.274 1.00 48.55  ? 1014 GLN A O     1 
ATOM   8163  C CB    . GLN B 2 1017 ? 143.358 146.417 136.531 1.00 48.55  ? 1014 GLN A CB    1 
ATOM   8164  C CG    . GLN B 2 1017 ? 143.784 147.174 137.779 1.00 48.55  ? 1014 GLN A CG    1 
ATOM   8165  C CD    . GLN B 2 1017 ? 143.190 146.592 139.046 1.00 48.55  ? 1014 GLN A CD    1 
ATOM   8166  O OE1   . GLN B 2 1017 ? 142.806 147.324 139.958 1.00 48.55  ? 1014 GLN A OE1   1 
ATOM   8167  N NE2   . GLN B 2 1017 ? 143.116 145.267 139.112 1.00 48.55  ? 1014 GLN A NE2   1 
ATOM   8168  N N     . PHE B 2 1018 ? 141.387 148.556 135.070 1.00 48.55  ? 1015 PHE A N     1 
ATOM   8169  C CA    . PHE B 2 1018 ? 140.942 149.943 134.985 1.00 48.55  ? 1015 PHE A CA    1 
ATOM   8170  C C     . PHE B 2 1018 ? 139.462 150.075 135.320 1.00 48.55  ? 1015 PHE A C     1 
ATOM   8171  O O     . PHE B 2 1018 ? 139.054 151.025 135.998 1.00 48.55  ? 1015 PHE A O     1 
ATOM   8172  C CB    . PHE B 2 1018 ? 141.227 150.496 133.591 1.00 48.55  ? 1015 PHE A CB    1 
ATOM   8173  C CG    . PHE B 2 1018 ? 140.485 151.759 133.276 1.00 48.55  ? 1015 PHE A CG    1 
ATOM   8174  C CD1   . PHE B 2 1018 ? 140.803 152.941 133.918 1.00 48.55  ? 1015 PHE A CD1   1 
ATOM   8175  C CD2   . PHE B 2 1018 ? 139.476 151.767 132.331 1.00 48.55  ? 1015 PHE A CD2   1 
ATOM   8176  C CE1   . PHE B 2 1018 ? 140.124 154.103 133.627 1.00 48.55  ? 1015 PHE A CE1   1 
ATOM   8177  C CE2   . PHE B 2 1018 ? 138.796 152.926 132.037 1.00 48.55  ? 1015 PHE A CE2   1 
ATOM   8178  C CZ    . PHE B 2 1018 ? 139.122 154.094 132.685 1.00 48.55  ? 1015 PHE A CZ    1 
ATOM   8179  N N     . GLU B 2 1019 ? 138.640 149.138 134.843 1.00 48.55  ? 1016 GLU A N     1 
ATOM   8180  C CA    . GLU B 2 1019 ? 137.215 149.177 135.153 1.00 48.55  ? 1016 GLU A CA    1 
ATOM   8181  C C     . GLU B 2 1019 ? 136.972 149.014 136.647 1.00 48.55  ? 1016 GLU A C     1 
ATOM   8182  O O     . GLU B 2 1019 ? 136.098 149.678 137.217 1.00 48.55  ? 1016 GLU A O     1 
ATOM   8183  C CB    . GLU B 2 1019 ? 136.475 148.096 134.367 1.00 48.55  ? 1016 GLU A CB    1 
ATOM   8184  C CG    . GLU B 2 1019 ? 136.746 148.119 132.875 1.00 48.55  ? 1016 GLU A CG    1 
ATOM   8185  C CD    . GLU B 2 1019 ? 135.674 147.405 132.080 1.00 48.55  ? 1016 GLU A CD    1 
ATOM   8186  O OE1   . GLU B 2 1019 ? 134.904 146.630 132.683 1.00 48.55  ? 1016 GLU A OE1   1 
ATOM   8187  O OE2   . GLU B 2 1019 ? 135.602 147.617 130.852 1.00 48.55  ? 1016 GLU A OE2   1 
ATOM   8188  N N     . LYS B 2 1020 ? 137.730 148.128 137.296 1.00 48.55  ? 1017 LYS A N     1 
ATOM   8189  C CA    . LYS B 2 1020 ? 137.597 147.958 138.739 1.00 48.55  ? 1017 LYS A CA    1 
ATOM   8190  C C     . LYS B 2 1020 ? 137.973 149.234 139.480 1.00 48.55  ? 1017 LYS A C     1 
ATOM   8191  O O     . LYS B 2 1020 ? 137.326 149.601 140.468 1.00 48.55  ? 1017 LYS A O     1 
ATOM   8192  C CB    . LYS B 2 1020 ? 138.462 146.790 139.211 1.00 48.55  ? 1017 LYS A CB    1 
ATOM   8193  C CG    . LYS B 2 1020 ? 138.202 146.365 140.645 1.00 48.55  ? 1017 LYS A CG    1 
ATOM   8194  C CD    . LYS B 2 1020 ? 139.101 145.208 141.049 1.00 48.55  ? 1017 LYS A CD    1 
ATOM   8195  C CE    . LYS B 2 1020 ? 140.412 145.705 141.634 1.00 48.55  ? 1017 LYS A CE    1 
ATOM   8196  N NZ    . LYS B 2 1020 ? 140.356 145.805 143.118 1.00 48.55  ? 1017 LYS A NZ    1 
ATOM   8197  N N     . MET B 2 1021 ? 139.020 149.923 139.020 1.00 48.55  ? 1018 MET A N     1 
ATOM   8198  C CA    . MET B 2 1021 ? 139.428 151.164 139.669 1.00 48.55  ? 1018 MET A CA    1 
ATOM   8199  C C     . MET B 2 1021 ? 138.384 152.257 139.481 1.00 48.55  ? 1018 MET A C     1 
ATOM   8200  O O     . MET B 2 1021 ? 138.281 153.174 140.303 1.00 48.55  ? 1018 MET A O     1 
ATOM   8201  C CB    . MET B 2 1021 ? 140.784 151.617 139.129 1.00 48.55  ? 1018 MET A CB    1 
ATOM   8202  C CG    . MET B 2 1021 ? 141.934 150.695 139.487 1.00 48.55  ? 1018 MET A CG    1 
ATOM   8203  S SD    . MET B 2 1021 ? 143.497 151.223 138.760 1.00 48.55  ? 1018 MET A SD    1 
ATOM   8204  C CE    . MET B 2 1021 ? 143.835 152.697 139.719 1.00 48.55  ? 1018 MET A CE    1 
ATOM   8205  N N     . LEU B 2 1022 ? 137.601 152.180 138.403 1.00 48.55  ? 1019 LEU A N     1 
ATOM   8206  C CA    . LEU B 2 1022 ? 136.536 153.156 138.202 1.00 48.55  ? 1019 LEU A CA    1 
ATOM   8207  C C     . LEU B 2 1022 ? 135.366 152.893 139.141 1.00 48.55  ? 1019 LEU A C     1 
ATOM   8208  O O     . LEU B 2 1022 ? 134.762 153.833 139.670 1.00 48.55  ? 1019 LEU A O     1 
ATOM   8209  C CB    . LEU B 2 1022 ? 136.073 153.138 136.746 1.00 48.55  ? 1019 LEU A CB    1 
ATOM   8210  C CG    . LEU B 2 1022 ? 135.445 154.428 136.218 1.00 48.55  ? 1019 LEU A CG    1 
ATOM   8211  C CD1   . LEU B 2 1022 ? 136.408 155.590 136.367 1.00 48.55  ? 1019 LEU A CD1   1 
ATOM   8212  C CD2   . LEU B 2 1022 ? 135.020 154.265 134.769 1.00 48.55  ? 1019 LEU A CD2   1 
ATOM   8213  N N     . ILE B 2 1023 ? 135.028 151.619 139.355 1.00 48.55  ? 1020 ILE A N     1 
ATOM   8214  C CA    . ILE B 2 1023 ? 133.959 151.280 140.291 1.00 48.55  ? 1020 ILE A CA    1 
ATOM   8215  C C     . ILE B 2 1023 ? 134.353 151.662 141.711 1.00 48.55  ? 1020 ILE A C     1 
ATOM   8216  O O     . ILE B 2 1023 ? 133.556 152.241 142.459 1.00 48.55  ? 1020 ILE A O     1 
ATOM   8217  C CB    . ILE B 2 1023 ? 133.607 149.785 140.182 1.00 48.55  ? 1020 ILE A CB    1 
ATOM   8218  C CG1   . ILE B 2 1023 ? 132.918 149.496 138.848 1.00 48.55  ? 1020 ILE A CG1   1 
ATOM   8219  C CG2   . ILE B 2 1023 ? 132.720 149.357 141.338 1.00 48.55  ? 1020 ILE A CG2   1 
ATOM   8220  C CD1   . ILE B 2 1023 ? 132.696 148.024 138.587 1.00 48.55  ? 1020 ILE A CD1   1 
ATOM   8221  N N     . ASP B 2 1024 ? 135.588 151.344 142.105 1.00 48.55  ? 1021 ASP A N     1 
ATOM   8222  C CA    . ASP B 2 1024 ? 136.053 151.689 143.445 1.00 48.55  ? 1021 ASP A CA    1 
ATOM   8223  C C     . ASP B 2 1024 ? 136.106 153.198 143.642 1.00 48.55  ? 1021 ASP A C     1 
ATOM   8224  O O     . ASP B 2 1024 ? 135.758 153.704 144.715 1.00 48.55  ? 1021 ASP A O     1 
ATOM   8225  C CB    . ASP B 2 1024 ? 137.424 151.064 143.700 1.00 48.55  ? 1021 ASP A CB    1 
ATOM   8226  C CG    . ASP B 2 1024 ? 137.364 149.554 143.808 1.00 48.55  ? 1021 ASP A CG    1 
ATOM   8227  O OD1   . ASP B 2 1024 ? 136.315 149.028 144.233 1.00 48.55  ? 1021 ASP A OD1   1 
ATOM   8228  O OD2   . ASP B 2 1024 ? 138.368 148.893 143.467 1.00 48.55  ? 1021 ASP A OD2   1 
ATOM   8229  N N     . LYS B 2 1025 ? 136.554 153.933 142.621 1.00 48.55  ? 1022 LYS A N     1 
ATOM   8230  C CA    . LYS B 2 1025 ? 136.591 155.388 142.720 1.00 48.55  ? 1022 LYS A CA    1 
ATOM   8231  C C     . LYS B 2 1025 ? 135.192 155.962 142.893 1.00 48.55  ? 1022 LYS A C     1 
ATOM   8232  O O     . LYS B 2 1025 ? 134.976 156.858 143.717 1.00 48.55  ? 1022 LYS A O     1 
ATOM   8233  C CB    . LYS B 2 1025 ? 137.266 155.979 141.482 1.00 48.55  ? 1022 LYS A CB    1 
ATOM   8234  C CG    . LYS B 2 1025 ? 137.035 157.465 141.286 1.00 48.55  ? 1022 LYS A CG    1 
ATOM   8235  C CD    . LYS B 2 1025 ? 137.670 158.281 142.393 1.00 48.55  ? 1022 LYS A CD    1 
ATOM   8236  C CE    . LYS B 2 1025 ? 138.299 159.545 141.837 1.00 48.55  ? 1022 LYS A CE    1 
ATOM   8237  N NZ    . LYS B 2 1025 ? 138.952 160.356 142.899 1.00 48.55  ? 1022 LYS A NZ    1 
ATOM   8238  N N     . LEU B 2 1026 ? 134.227 155.455 142.128 1.00 48.55  ? 1023 LEU A N     1 
ATOM   8239  C CA    . LEU B 2 1026 ? 132.846 155.896 142.255 1.00 48.55  ? 1023 LEU A CA    1 
ATOM   8240  C C     . LEU B 2 1026 ? 132.134 155.276 143.446 1.00 48.55  ? 1023 LEU A C     1 
ATOM   8241  O O     . LEU B 2 1026 ? 131.041 155.732 143.799 1.00 48.55  ? 1023 LEU A O     1 
ATOM   8242  C CB    . LEU B 2 1026 ? 132.073 155.573 140.980 1.00 48.55  ? 1023 LEU A CB    1 
ATOM   8243  C CG    . LEU B 2 1026 ? 132.527 156.311 139.729 1.00 48.55  ? 1023 LEU A CG    1 
ATOM   8244  C CD1   . LEU B 2 1026 ? 131.566 156.002 138.619 1.00 48.55  ? 1023 LEU A CD1   1 
ATOM   8245  C CD2   . LEU B 2 1026 ? 132.582 157.800 139.987 1.00 48.55  ? 1023 LEU A CD2   1 
ATOM   8246  N N     . ASN B 2 1027 ? 132.716 154.245 144.059 1.00 48.55  ? 1024 ASN A N     1 
ATOM   8247  C CA    . ASN B 2 1027 ? 132.137 153.687 145.274 1.00 48.55  ? 1024 ASN A CA    1 
ATOM   8248  C C     . ASN B 2 1027 ? 132.088 154.739 146.374 1.00 48.55  ? 1024 ASN A C     1 
ATOM   8249  O O     . ASN B 2 1027 ? 131.093 154.849 147.099 1.00 48.55  ? 1024 ASN A O     1 
ATOM   8250  C CB    . ASN B 2 1027 ? 132.946 152.466 145.714 1.00 48.55  ? 1024 ASN A CB    1 
ATOM   8251  C CG    . ASN B 2 1027 ? 132.292 151.704 146.846 1.00 48.55  ? 1024 ASN A CG    1 
ATOM   8252  O OD1   . ASN B 2 1027 ? 131.237 152.088 147.341 1.00 48.55  ? 1024 ASN A OD1   1 
ATOM   8253  N ND2   . ASN B 2 1027 ? 132.922 150.611 147.262 1.00 48.55  ? 1024 ASN A ND2   1 
ATOM   8254  N N     . CYS B 2 1028 ? 133.151 155.532 146.502 1.00 48.55  ? 1025 CYS A N     1 
ATOM   8255  C CA    . CYS B 2 1028 ? 133.192 156.679 147.411 1.00 48.55  ? 1025 CYS A CA    1 
ATOM   8256  C C     . CYS B 2 1028 ? 133.959 157.779 146.679 1.00 48.55  ? 1025 CYS A C     1 
ATOM   8257  O O     . CYS B 2 1028 ? 135.190 157.843 146.747 1.00 48.55  ? 1025 CYS A O     1 
ATOM   8258  C CB    . CYS B 2 1028 ? 133.840 156.315 148.739 1.00 48.55  ? 1025 CYS A CB    1 
ATOM   8259  S SG    . CYS B 2 1028 ? 133.581 157.527 150.044 1.00 48.55  ? 1025 CYS A SG    1 
ATOM   8260  N N     . LEU B 2 1029 ? 133.225 158.642 145.984 1.00 48.55  ? 1026 LEU A N     1 
ATOM   8261  C CA    . LEU B 2 1029 ? 133.812 159.634 145.094 1.00 48.55  ? 1026 LEU A CA    1 
ATOM   8262  C C     . LEU B 2 1029 ? 133.860 160.993 145.776 1.00 48.55  ? 1026 LEU A C     1 
ATOM   8263  O O     . LEU B 2 1029 ? 132.835 161.492 146.253 1.00 48.55  ? 1026 LEU A O     1 
ATOM   8264  C CB    . LEU B 2 1029 ? 133.016 159.733 143.792 1.00 48.55  ? 1026 LEU A CB    1 
ATOM   8265  C CG    . LEU B 2 1029 ? 133.385 160.902 142.875 1.00 48.55  ? 1026 LEU A CG    1 
ATOM   8266  C CD1   . LEU B 2 1029 ? 134.807 160.755 142.361 1.00 48.55  ? 1026 LEU A CD1   1 
ATOM   8267  C CD2   . LEU B 2 1029 ? 132.402 161.020 141.723 1.00 48.55  ? 1026 LEU A CD2   1 
ATOM   8268  N N     . VAL B 2 1030 ? 135.048 161.588 145.814 1.00 48.55  ? 1027 VAL A N     1 
ATOM   8269  C CA    . VAL B 2 1030 ? 135.247 162.928 146.348 1.00 48.55  ? 1027 VAL A CA    1 
ATOM   8270  C C     . VAL B 2 1030 ? 136.069 163.728 145.349 1.00 48.55  ? 1027 VAL A C     1 
ATOM   8271  O O     . VAL B 2 1030 ? 137.072 163.238 144.817 1.00 48.55  ? 1027 VAL A O     1 
ATOM   8272  C CB    . VAL B 2 1030 ? 135.932 162.899 147.731 1.00 48.55  ? 1027 VAL A CB    1 
ATOM   8273  C CG1   . VAL B 2 1030 ? 137.223 162.104 147.678 1.00 48.55  ? 1027 VAL A CG1   1 
ATOM   8274  C CG2   . VAL B 2 1030 ? 136.195 164.312 148.225 1.00 48.55  ? 1027 VAL A CG2   1 
ATOM   8275  N N     . LEU B 2 1031 ? 135.630 164.951 145.074 1.00 48.55  ? 1028 LEU A N     1 
ATOM   8276  C CA    . LEU B 2 1031 ? 136.362 165.872 144.218 1.00 48.55  ? 1028 LEU A CA    1 
ATOM   8277  C C     . LEU B 2 1031 ? 137.040 166.915 145.094 1.00 48.55  ? 1028 LEU A C     1 
ATOM   8278  O O     . LEU B 2 1031 ? 136.376 167.601 145.878 1.00 48.55  ? 1028 LEU A O     1 
ATOM   8279  C CB    . LEU B 2 1031 ? 135.429 166.529 143.201 1.00 48.55  ? 1028 LEU A CB    1 
ATOM   8280  C CG    . LEU B 2 1031 ? 134.598 165.529 142.395 1.00 48.55  ? 1028 LEU A CG    1 
ATOM   8281  C CD1   . LEU B 2 1031 ? 133.386 166.194 141.768 1.00 48.55  ? 1028 LEU A CD1   1 
ATOM   8282  C CD2   . LEU B 2 1031 ? 135.453 164.860 141.331 1.00 48.55  ? 1028 LEU A CD2   1 
ATOM   8283  N N     . LYS B 2 1032 ? 138.362 167.028 144.958 1.00 48.55  ? 1029 LYS A N     1 
ATOM   8284  C CA    . LYS B 2 1032 ? 139.144 167.774 145.938 1.00 48.55  ? 1029 LYS A CA    1 
ATOM   8285  C C     . LYS B 2 1032 ? 138.901 169.275 145.850 1.00 48.55  ? 1029 LYS A C     1 
ATOM   8286  O O     . LYS B 2 1032 ? 139.292 170.019 146.757 1.00 48.55  ? 1029 LYS A O     1 
ATOM   8287  C CB    . LYS B 2 1032 ? 140.628 167.448 145.772 1.00 48.55  ? 1029 LYS A CB    1 
ATOM   8288  C CG    . LYS B 2 1032 ? 141.192 167.744 144.402 1.00 48.55  ? 1029 LYS A CG    1 
ATOM   8289  C CD    . LYS B 2 1032 ? 142.656 167.353 144.338 1.00 48.55  ? 1029 LYS A CD    1 
ATOM   8290  C CE    . LYS B 2 1032 ? 142.819 165.845 144.385 1.00 48.55  ? 1029 LYS A CE    1 
ATOM   8291  N NZ    . LYS B 2 1032 ? 144.235 165.432 144.189 1.00 48.55  ? 1029 LYS A NZ    1 
ATOM   8292  N N     . ASP B 2 1033 ? 138.264 169.743 144.776 1.00 48.55  ? 1030 ASP A N     1 
ATOM   8293  C CA    . ASP B 2 1033 ? 137.877 171.147 144.710 1.00 48.55  ? 1030 ASP A CA    1 
ATOM   8294  C C     . ASP B 2 1033 ? 136.557 171.415 145.421 1.00 48.55  ? 1030 ASP A C     1 
ATOM   8295  O O     . ASP B 2 1033 ? 136.332 172.539 145.881 1.00 48.55  ? 1030 ASP A O     1 
ATOM   8296  C CB    . ASP B 2 1033 ? 137.788 171.600 143.252 1.00 48.55  ? 1030 ASP A CB    1 
ATOM   8297  C CG    . ASP B 2 1033 ? 139.146 171.918 142.658 1.00 48.55  ? 1030 ASP A CG    1 
ATOM   8298  O OD1   . ASP B 2 1033 ? 140.165 171.695 143.346 1.00 48.55  ? 1030 ASP A OD1   1 
ATOM   8299  O OD2   . ASP B 2 1033 ? 139.196 172.392 141.503 1.00 48.55  ? 1030 ASP A OD2   1 
ATOM   8300  N N     . TYR B 2 1034 ? 135.687 170.414 145.519 1.00 48.55  ? 1031 TYR A N     1 
ATOM   8301  C CA    . TYR B 2 1034 ? 134.385 170.602 146.134 1.00 48.55  ? 1031 TYR A CA    1 
ATOM   8302  C C     . TYR B 2 1034 ? 134.524 170.840 147.637 1.00 48.55  ? 1031 TYR A C     1 
ATOM   8303  O O     . TYR B 2 1034 ? 135.388 170.250 148.291 1.00 48.55  ? 1031 TYR A O     1 
ATOM   8304  C CB    . TYR B 2 1034 ? 133.501 169.386 145.877 1.00 48.55  ? 1031 TYR A CB    1 
ATOM   8305  C CG    . TYR B 2 1034 ? 132.747 169.448 144.569 1.00 48.55  ? 1031 TYR A CG    1 
ATOM   8306  C CD1   . TYR B 2 1034 ? 133.423 169.534 143.360 1.00 48.55  ? 1031 TYR A CD1   1 
ATOM   8307  C CD2   . TYR B 2 1034 ? 131.362 169.406 144.541 1.00 48.55  ? 1031 TYR A CD2   1 
ATOM   8308  C CE1   . TYR B 2 1034 ? 132.740 169.591 142.162 1.00 48.55  ? 1031 TYR A CE1   1 
ATOM   8309  C CE2   . TYR B 2 1034 ? 130.669 169.459 143.349 1.00 48.55  ? 1031 TYR A CE2   1 
ATOM   8310  C CZ    . TYR B 2 1034 ? 131.363 169.550 142.162 1.00 48.55  ? 1031 TYR A CZ    1 
ATOM   8311  O OH    . TYR B 2 1034 ? 130.677 169.603 140.971 1.00 48.55  ? 1031 TYR A OH    1 
ATOM   8312  N N     . PRO B 2 1035 ? 133.686 171.703 148.207 1.00 48.55  ? 1032 PRO A N     1 
ATOM   8313  C CA    . PRO B 2 1035 ? 133.741 171.944 149.651 1.00 48.55  ? 1032 PRO A CA    1 
ATOM   8314  C C     . PRO B 2 1035 ? 133.257 170.738 150.440 1.00 48.55  ? 1032 PRO A C     1 
ATOM   8315  O O     . PRO B 2 1035 ? 132.523 169.881 149.943 1.00 48.55  ? 1032 PRO A O     1 
ATOM   8316  C CB    . PRO B 2 1035 ? 132.813 173.146 149.849 1.00 48.55  ? 1032 PRO A CB    1 
ATOM   8317  C CG    . PRO B 2 1035 ? 131.874 173.083 148.702 1.00 48.55  ? 1032 PRO A CG    1 
ATOM   8318  C CD    . PRO B 2 1035 ? 132.650 172.516 147.548 1.00 48.55  ? 1032 PRO A CD    1 
ATOM   8319  N N     . ALA B 2 1036 ? 133.696 170.681 151.700 1.00 48.55  ? 1033 ALA A N     1 
ATOM   8320  C CA    . ALA B 2 1036 ? 133.348 169.556 152.561 1.00 48.55  ? 1033 ALA A CA    1 
ATOM   8321  C C     . ALA B 2 1036 ? 131.848 169.489 152.822 1.00 48.55  ? 1033 ALA A C     1 
ATOM   8322  O O     . ALA B 2 1036 ? 131.255 168.404 152.784 1.00 48.55  ? 1033 ALA A O     1 
ATOM   8323  C CB    . ALA B 2 1036 ? 134.115 169.653 153.879 1.00 48.55  ? 1033 ALA A CB    1 
ATOM   8324  N N     . GLU B 2 1037 ? 131.217 170.635 153.091 1.00 48.55  ? 1034 GLU A N     1 
ATOM   8325  C CA    . GLU B 2 1037 ? 129.802 170.634 153.450 1.00 48.55  ? 1034 GLU A CA    1 
ATOM   8326  C C     . GLU B 2 1037 ? 128.935 170.200 152.276 1.00 48.55  ? 1034 GLU A C     1 
ATOM   8327  O O     . GLU B 2 1037 ? 128.024 169.381 152.442 1.00 48.55  ? 1034 GLU A O     1 
ATOM   8328  C CB    . GLU B 2 1037 ? 129.397 172.022 153.963 1.00 25.40  ? 1034 GLU A CB    1 
ATOM   8329  C CG    . GLU B 2 1037 ? 127.935 172.191 154.421 1.00 25.40  ? 1034 GLU A CG    1 
ATOM   8330  C CD    . GLU B 2 1037 ? 126.923 172.273 153.286 1.00 25.40  ? 1034 GLU A CD    1 
ATOM   8331  O OE1   . GLU B 2 1037 ? 127.318 172.589 152.144 1.00 25.40  ? 1034 GLU A OE1   1 
ATOM   8332  O OE2   . GLU B 2 1037 ? 125.726 172.023 153.542 1.00 25.40  ? 1034 GLU A OE2   1 
ATOM   8333  N N     . LYS B 2 1038 ? 129.196 170.738 151.090 1.00 48.55  ? 1035 LYS A N     1 
ATOM   8334  C CA    . LYS B 2 1038 ? 128.379 170.413 149.932 1.00 48.55  ? 1035 LYS A CA    1 
ATOM   8335  C C     . LYS B 2 1038 ? 128.580 168.960 149.525 1.00 48.55  ? 1035 LYS A C     1 
ATOM   8336  O O     . LYS B 2 1038 ? 129.693 168.429 149.550 1.00 48.55  ? 1035 LYS A O     1 
ATOM   8337  C CB    . LYS B 2 1038 ? 128.712 171.335 148.761 1.00 25.25  ? 1035 LYS A CB    1 
ATOM   8338  C CG    . LYS B 2 1038 ? 127.829 171.126 147.542 1.00 25.25  ? 1035 LYS A CG    1 
ATOM   8339  C CD    . LYS B 2 1038 ? 128.064 172.200 146.496 1.00 25.25  ? 1035 LYS A CD    1 
ATOM   8340  C CE    . LYS B 2 1038 ? 129.397 172.008 145.797 1.00 25.25  ? 1035 LYS A CE    1 
ATOM   8341  N NZ    . LYS B 2 1038 ? 129.596 172.999 144.705 1.00 25.25  ? 1035 LYS A NZ    1 
ATOM   8342  N N     . VAL B 2 1039 ? 127.471 168.311 149.164 1.00 48.55  ? 1036 VAL A N     1 
ATOM   8343  C CA    . VAL B 2 1039 ? 127.531 166.936 148.691 1.00 48.55  ? 1036 VAL A CA    1 
ATOM   8344  C C     . VAL B 2 1039 ? 128.434 166.847 147.468 1.00 48.55  ? 1036 VAL A C     1 
ATOM   8345  O O     . VAL B 2 1039 ? 128.436 167.728 146.598 1.00 48.55  ? 1036 VAL A O     1 
ATOM   8346  C CB    . VAL B 2 1039 ? 126.111 166.414 148.414 1.00 48.55  ? 1036 VAL A CB    1 
ATOM   8347  C CG1   . VAL B 2 1039 ? 125.451 167.220 147.324 1.00 48.55  ? 1036 VAL A CG1   1 
ATOM   8348  C CG2   . VAL B 2 1039 ? 126.158 164.954 148.019 1.00 48.55  ? 1036 VAL A CG2   1 
ATOM   8349  N N     . GLY B 2 1040 ? 129.229 165.781 147.413 1.00 48.55  ? 1037 GLY A N     1 
ATOM   8350  C CA    . GLY B 2 1040 ? 130.336 165.683 146.493 1.00 48.55  ? 1037 GLY A CA    1 
ATOM   8351  C C     . GLY B 2 1040 ? 131.684 165.968 147.115 1.00 48.55  ? 1037 GLY A C     1 
ATOM   8352  O O     . GLY B 2 1040 ? 132.707 165.834 146.431 1.00 48.55  ? 1037 GLY A O     1 
ATOM   8353  N N     . GLY B 2 1041 ? 131.717 166.355 148.391 1.00 48.55  ? 1038 GLY A N     1 
ATOM   8354  C CA    . GLY B 2 1041 ? 132.958 166.622 149.082 1.00 48.55  ? 1038 GLY A CA    1 
ATOM   8355  C C     . GLY B 2 1041 ? 133.392 165.463 149.959 1.00 48.55  ? 1038 GLY A C     1 
ATOM   8356  O O     . GLY B 2 1041 ? 132.914 164.336 149.844 1.00 48.55  ? 1038 GLY A O     1 
ATOM   8357  N N     . VAL B 2 1042 ? 134.332 165.764 150.858 1.00 48.55  ? 1039 VAL A N     1 
ATOM   8358  C CA    . VAL B 2 1042 ? 134.886 164.729 151.725 1.00 48.55  ? 1039 VAL A CA    1 
ATOM   8359  C C     . VAL B 2 1042 ? 133.853 164.240 152.737 1.00 48.55  ? 1039 VAL A C     1 
ATOM   8360  O O     . VAL B 2 1042 ? 133.800 163.044 153.047 1.00 48.55  ? 1039 VAL A O     1 
ATOM   8361  C CB    . VAL B 2 1042 ? 136.169 165.244 152.407 1.00 48.55  ? 1039 VAL A CB    1 
ATOM   8362  C CG1   . VAL B 2 1042 ? 135.906 166.542 153.146 1.00 48.55  ? 1039 VAL A CG1   1 
ATOM   8363  C CG2   . VAL B 2 1042 ? 136.738 164.193 153.345 1.00 48.55  ? 1039 VAL A CG2   1 
ATOM   8364  N N     . LEU B 2 1043 ? 133.010 165.135 153.257 1.00 48.55  ? 1040 LEU A N     1 
ATOM   8365  C CA    . LEU B 2 1043 ? 132.029 164.727 154.259 1.00 48.55  ? 1040 LEU A CA    1 
ATOM   8366  C C     . LEU B 2 1043 ? 130.858 163.971 153.641 1.00 48.55  ? 1040 LEU A C     1 
ATOM   8367  O O     . LEU B 2 1043 ? 130.308 163.060 154.271 1.00 48.55  ? 1040 LEU A O     1 
ATOM   8368  C CB    . LEU B 2 1043 ? 131.521 165.945 155.033 1.00 48.55  ? 1040 LEU A CB    1 
ATOM   8369  C CG    . LEU B 2 1043 ? 132.273 166.376 156.296 1.00 48.55  ? 1040 LEU A CG    1 
ATOM   8370  C CD1   . LEU B 2 1043 ? 132.182 165.301 157.364 1.00 48.55  ? 1040 LEU A CD1   1 
ATOM   8371  C CD2   . LEU B 2 1043 ? 133.723 166.713 156.009 1.00 48.55  ? 1040 LEU A CD2   1 
ATOM   8372  N N     . ASN B 2 1044 ? 130.459 164.326 152.420 1.00 48.55  ? 1041 ASN A N     1 
ATOM   8373  C CA    . ASN B 2 1044 ? 129.310 163.715 151.750 1.00 48.55  ? 1041 ASN A CA    1 
ATOM   8374  C C     . ASN B 2 1044 ? 129.722 163.257 150.358 1.00 48.55  ? 1041 ASN A C     1 
ATOM   8375  O O     . ASN B 2 1044 ? 129.377 163.893 149.353 1.00 48.55  ? 1041 ASN A O     1 
ATOM   8376  C CB    . ASN B 2 1044 ? 128.133 164.687 151.679 1.00 48.55  ? 1041 ASN A CB    1 
ATOM   8377  C CG    . ASN B 2 1044 ? 127.783 165.275 153.029 1.00 48.55  ? 1041 ASN A CG    1 
ATOM   8378  O OD1   . ASN B 2 1044 ? 127.722 164.564 154.032 1.00 48.55  ? 1041 ASN A OD1   1 
ATOM   8379  N ND2   . ASN B 2 1044 ? 127.550 166.582 153.063 1.00 48.55  ? 1041 ASN A ND2   1 
ATOM   8380  N N     . PRO B 2 1045 ? 130.461 162.156 150.260 1.00 48.55  ? 1042 PRO A N     1 
ATOM   8381  C CA    . PRO B 2 1045 ? 130.914 161.685 148.949 1.00 48.55  ? 1042 PRO A CA    1 
ATOM   8382  C C     . PRO B 2 1045 ? 129.773 161.105 148.128 1.00 48.55  ? 1042 PRO A C     1 
ATOM   8383  O O     . PRO B 2 1045 ? 128.752 160.653 148.651 1.00 48.55  ? 1042 PRO A O     1 
ATOM   8384  C CB    . PRO B 2 1045 ? 131.949 160.606 149.289 1.00 48.55  ? 1042 PRO A CB    1 
ATOM   8385  C CG    . PRO B 2 1045 ? 132.198 160.728 150.766 1.00 48.55  ? 1042 PRO A CG    1 
ATOM   8386  C CD    . PRO B 2 1045 ? 130.954 161.299 151.348 1.00 48.55  ? 1042 PRO A CD    1 
ATOM   8387  N N     . TYR B 2 1046 ? 129.966 161.128 146.811 1.00 48.55  ? 1043 TYR A N     1 
ATOM   8388  C CA    . TYR B 2 1046 ? 129.026 160.486 145.903 1.00 48.55  ? 1043 TYR A CA    1 
ATOM   8389  C C     . TYR B 2 1046 ? 129.068 158.971 146.050 1.00 48.55  ? 1043 TYR A C     1 
ATOM   8390  O O     . TYR B 2 1046 ? 130.110 158.384 146.351 1.00 48.55  ? 1043 TYR A O     1 
ATOM   8391  C CB    . TYR B 2 1046 ? 129.328 160.868 144.455 1.00 48.55  ? 1043 TYR A CB    1 
ATOM   8392  C CG    . TYR B 2 1046 ? 128.970 162.288 144.090 1.00 48.55  ? 1043 TYR A CG    1 
ATOM   8393  C CD1   . TYR B 2 1046 ? 128.126 163.040 144.891 1.00 48.55  ? 1043 TYR A CD1   1 
ATOM   8394  C CD2   . TYR B 2 1046 ? 129.475 162.874 142.941 1.00 48.55  ? 1043 TYR A CD2   1 
ATOM   8395  C CE1   . TYR B 2 1046 ? 127.792 164.336 144.554 1.00 48.55  ? 1043 TYR A CE1   1 
ATOM   8396  C CE2   . TYR B 2 1046 ? 129.150 164.169 142.600 1.00 48.55  ? 1043 TYR A CE2   1 
ATOM   8397  C CZ    . TYR B 2 1046 ? 128.309 164.895 143.407 1.00 48.55  ? 1043 TYR A CZ    1 
ATOM   8398  O OH    . TYR B 2 1046 ? 127.989 166.186 143.062 1.00 48.55  ? 1043 TYR A OH    1 
ATOM   8399  N N     . GLN B 2 1047 ? 127.916 158.344 145.835 1.00 48.55  ? 1044 GLN A N     1 
ATOM   8400  C CA    . GLN B 2 1047 ? 127.776 156.893 145.768 1.00 48.55  ? 1044 GLN A CA    1 
ATOM   8401  C C     . GLN B 2 1047 ? 127.126 156.600 144.419 1.00 48.55  ? 1044 GLN A C     1 
ATOM   8402  O O     . GLN B 2 1047 ? 125.898 156.573 144.305 1.00 48.55  ? 1044 GLN A O     1 
ATOM   8403  C CB    . GLN B 2 1047 ? 126.943 156.358 146.929 1.00 48.55  ? 1044 GLN A CB    1 
ATOM   8404  C CG    . GLN B 2 1047 ? 127.497 156.689 148.304 1.00 48.55  ? 1044 GLN A CG    1 
ATOM   8405  C CD    . GLN B 2 1047 ? 128.617 155.763 148.720 1.00 48.55  ? 1044 GLN A CD    1 
ATOM   8406  O OE1   . GLN B 2 1047 ? 128.590 154.569 148.427 1.00 48.55  ? 1044 GLN A OE1   1 
ATOM   8407  N NE2   . GLN B 2 1047 ? 129.611 156.307 149.411 1.00 48.55  ? 1044 GLN A NE2   1 
ATOM   8408  N N     . LEU B 2 1048 ? 127.951 156.392 143.393 1.00 48.55  ? 1045 LEU A N     1 
ATOM   8409  C CA    . LEU B 2 1048 ? 127.461 156.244 142.031 1.00 48.55  ? 1045 LEU A CA    1 
ATOM   8410  C C     . LEU B 2 1048 ? 127.553 154.825 141.492 1.00 48.55  ? 1045 LEU A C     1 
ATOM   8411  O O     . LEU B 2 1048 ? 126.950 154.540 140.452 1.00 48.55  ? 1045 LEU A O     1 
ATOM   8412  C CB    . LEU B 2 1048 ? 128.223 157.186 141.089 1.00 48.55  ? 1045 LEU A CB    1 
ATOM   8413  C CG    . LEU B 2 1048 ? 127.853 158.664 141.195 1.00 48.55  ? 1045 LEU A CG    1 
ATOM   8414  C CD1   . LEU B 2 1048 ? 128.847 159.526 140.438 1.00 48.55  ? 1045 LEU A CD1   1 
ATOM   8415  C CD2   . LEU B 2 1048 ? 126.446 158.886 140.679 1.00 48.55  ? 1045 LEU A CD2   1 
ATOM   8416  N N     . THR B 2 1049 ? 128.282 153.934 142.158 1.00 48.55  ? 1046 THR A N     1 
ATOM   8417  C CA    . THR B 2 1049 ? 128.392 152.552 141.720 1.00 48.55  ? 1046 THR A CA    1 
ATOM   8418  C C     . THR B 2 1049 ? 128.224 151.630 142.917 1.00 48.55  ? 1046 THR A C     1 
ATOM   8419  O O     . THR B 2 1049 ? 128.520 151.995 144.057 1.00 48.55  ? 1046 THR A O     1 
ATOM   8420  C CB    . THR B 2 1049 ? 129.737 152.269 141.039 1.00 48.55  ? 1046 THR A CB    1 
ATOM   8421  O OG1   . THR B 2 1049 ? 130.801 152.779 141.850 1.00 48.55  ? 1046 THR A OG1   1 
ATOM   8422  C CG2   . THR B 2 1049 ? 129.790 152.922 139.669 1.00 48.55  ? 1046 THR A CG2   1 
ATOM   8423  N N     . ASP B 2 1050 ? 127.738 150.424 142.641 1.00 48.55  ? 1047 ASP A N     1 
ATOM   8424  C CA    . ASP B 2 1050 ? 127.632 149.410 143.674 1.00 48.55  ? 1047 ASP A CA    1 
ATOM   8425  C C     . ASP B 2 1050 ? 129.020 148.891 144.039 1.00 48.55  ? 1047 ASP A C     1 
ATOM   8426  O O     . ASP B 2 1050 ? 129.981 149.016 143.276 1.00 48.55  ? 1047 ASP A O     1 
ATOM   8427  C CB    . ASP B 2 1050 ? 126.737 148.261 143.204 1.00 48.55  ? 1047 ASP A CB    1 
ATOM   8428  C CG    . ASP B 2 1050 ? 126.246 147.392 144.348 1.00 48.55  ? 1047 ASP A CG    1 
ATOM   8429  O OD1   . ASP B 2 1050 ? 126.934 147.313 145.386 1.00 48.55  ? 1047 ASP A OD1   1 
ATOM   8430  O OD2   . ASP B 2 1050 ? 125.164 146.784 144.206 1.00 48.55  ? 1047 ASP A OD2   1 
ATOM   8431  N N     . GLN B 2 1051 ? 129.116 148.309 145.231 1.00 48.55  ? 1048 GLN A N     1 
ATOM   8432  C CA    . GLN B 2 1051 ? 130.390 147.781 145.698 1.00 48.55  ? 1048 GLN A CA    1 
ATOM   8433  C C     . GLN B 2 1051 ? 130.850 146.638 144.803 1.00 48.55  ? 1048 GLN A C     1 
ATOM   8434  O O     . GLN B 2 1051 ? 130.064 145.766 144.425 1.00 48.55  ? 1048 GLN A O     1 
ATOM   8435  C CB    . GLN B 2 1051 ? 130.265 147.303 147.144 1.00 48.55  ? 1048 GLN A CB    1 
ATOM   8436  C CG    . GLN B 2 1051 ? 131.528 147.480 147.968 1.00 48.55  ? 1048 GLN A CG    1 
ATOM   8437  C CD    . GLN B 2 1051 ? 131.320 147.135 149.428 1.00 48.55  ? 1048 GLN A CD    1 
ATOM   8438  O OE1   . GLN B 2 1051 ? 130.225 147.294 149.965 1.00 48.55  ? 1048 GLN A OE1   1 
ATOM   8439  N NE2   . GLN B 2 1051 ? 132.375 146.661 150.080 1.00 48.55  ? 1048 GLN A NE2   1 
ATOM   8440  N N     . PHE B 2 1052 ? 132.135 146.651 144.462 1.00 48.55  ? 1049 PHE A N     1 
ATOM   8441  C CA    . PHE B 2 1052 ? 132.688 145.629 143.586 1.00 48.55  ? 1049 PHE A CA    1 
ATOM   8442  C C     . PHE B 2 1052 ? 132.708 144.281 144.294 1.00 48.55  ? 1049 PHE A C     1 
ATOM   8443  O O     . PHE B 2 1052 ? 133.071 144.190 145.471 1.00 48.55  ? 1049 PHE A O     1 
ATOM   8444  C CB    . PHE B 2 1052 ? 134.098 146.020 143.147 1.00 48.55  ? 1049 PHE A CB    1 
ATOM   8445  C CG    . PHE B 2 1052 ? 134.774 144.993 142.287 1.00 48.55  ? 1049 PHE A CG    1 
ATOM   8446  C CD1   . PHE B 2 1052 ? 134.482 144.903 140.938 1.00 48.55  ? 1049 PHE A CD1   1 
ATOM   8447  C CD2   . PHE B 2 1052 ? 135.708 144.125 142.825 1.00 48.55  ? 1049 PHE A CD2   1 
ATOM   8448  C CE1   . PHE B 2 1052 ? 135.104 143.962 140.143 1.00 48.55  ? 1049 PHE A CE1   1 
ATOM   8449  C CE2   . PHE B 2 1052 ? 136.332 143.182 142.034 1.00 48.55  ? 1049 PHE A CE2   1 
ATOM   8450  C CZ    . PHE B 2 1052 ? 136.030 143.102 140.691 1.00 48.55  ? 1049 PHE A CZ    1 
ATOM   8451  N N     . THR B 2 1053 ? 132.313 143.231 143.575 1.00 48.55  ? 1050 THR A N     1 
ATOM   8452  C CA    . THR B 2 1053 ? 132.304 141.876 144.110 1.00 48.55  ? 1050 THR A CA    1 
ATOM   8453  C C     . THR B 2 1053 ? 133.311 140.980 143.401 1.00 48.55  ? 1050 THR A C     1 
ATOM   8454  O O     . THR B 2 1053 ? 134.190 140.402 144.046 1.00 48.55  ? 1050 THR A O     1 
ATOM   8455  C CB    . THR B 2 1053 ? 130.895 141.278 144.007 1.00 48.55  ? 1050 THR A CB    1 
ATOM   8456  O OG1   . THR B 2 1053 ? 130.339 141.582 142.722 1.00 48.55  ? 1050 THR A OG1   1 
ATOM   8457  C CG2   . THR B 2 1053 ? 129.994 141.851 145.090 1.00 48.55  ? 1050 THR A CG2   1 
ATOM   8458  N N     . SER B 2 1054 ? 133.209 140.857 142.080 1.00 48.55  ? 1051 SER A N     1 
ATOM   8459  C CA    . SER B 2 1054 ? 134.139 140.048 141.307 1.00 48.55  ? 1051 SER A CA    1 
ATOM   8460  C C     . SER B 2 1054 ? 134.010 140.425 139.840 1.00 48.55  ? 1051 SER A C     1 
ATOM   8461  O O     . SER B 2 1054 ? 133.007 141.003 139.414 1.00 48.55  ? 1051 SER A O     1 
ATOM   8462  C CB    . SER B 2 1054 ? 133.884 138.549 141.501 1.00 48.55  ? 1051 SER A CB    1 
ATOM   8463  O OG    . SER B 2 1054 ? 134.790 137.775 140.735 1.00 48.55  ? 1051 SER A OG    1 
ATOM   8464  N N     . PHE B 2 1055 ? 135.049 140.091 139.073 1.00 48.55  ? 1052 PHE A N     1 
ATOM   8465  C CA    . PHE B 2 1055 ? 135.038 140.375 137.643 1.00 48.55  ? 1052 PHE A CA    1 
ATOM   8466  C C     . PHE B 2 1055 ? 133.960 139.566 136.932 1.00 48.55  ? 1052 PHE A C     1 
ATOM   8467  O O     . PHE B 2 1055 ? 133.265 140.075 136.046 1.00 48.55  ? 1052 PHE A O     1 
ATOM   8468  C CB    . PHE B 2 1055 ? 136.415 140.088 137.046 1.00 48.55  ? 1052 PHE A CB    1 
ATOM   8469  C CG    . PHE B 2 1055 ? 137.398 141.207 137.228 1.00 48.55  ? 1052 PHE A CG    1 
ATOM   8470  C CD1   . PHE B 2 1055 ? 136.964 142.515 137.353 1.00 48.55  ? 1052 PHE A CD1   1 
ATOM   8471  C CD2   . PHE B 2 1055 ? 138.758 140.951 137.271 1.00 48.55  ? 1052 PHE A CD2   1 
ATOM   8472  C CE1   . PHE B 2 1055 ? 137.867 143.548 137.521 1.00 48.55  ? 1052 PHE A CE1   1 
ATOM   8473  C CE2   . PHE B 2 1055 ? 139.666 141.978 137.441 1.00 48.55  ? 1052 PHE A CE2   1 
ATOM   8474  C CZ    . PHE B 2 1055 ? 139.221 143.278 137.565 1.00 48.55  ? 1052 PHE A CZ    1 
ATOM   8475  N N     . ALA B 2 1056 ? 133.814 138.293 137.303 1.00 48.55  ? 1053 ALA A N     1 
ATOM   8476  C CA    . ALA B 2 1056 ? 132.798 137.450 136.686 1.00 48.55  ? 1053 ALA A CA    1 
ATOM   8477  C C     . ALA B 2 1056 ? 131.393 137.806 137.151 1.00 48.55  ? 1053 ALA A C     1 
ATOM   8478  O O     . ALA B 2 1056 ? 130.443 137.710 136.366 1.00 48.55  ? 1053 ALA A O     1 
ATOM   8479  C CB    . ALA B 2 1056 ? 133.088 135.978 136.980 1.00 48.55  ? 1053 ALA A CB    1 
ATOM   8480  N N     . LYS B 2 1057 ? 131.240 138.214 138.413 1.00 48.55  ? 1054 LYS A N     1 
ATOM   8481  C CA    . LYS B 2 1057 ? 129.907 138.454 138.956 1.00 48.55  ? 1054 LYS A CA    1 
ATOM   8482  C C     . LYS B 2 1057 ? 129.263 139.695 138.350 1.00 48.55  ? 1054 LYS A C     1 
ATOM   8483  O O     . LYS B 2 1057 ? 128.038 139.744 138.189 1.00 48.55  ? 1054 LYS A O     1 
ATOM   8484  C CB    . LYS B 2 1057 ? 129.972 138.573 140.479 1.00 48.55  ? 1054 LYS A CB    1 
ATOM   8485  C CG    . LYS B 2 1057 ? 130.506 137.338 141.203 1.00 48.55  ? 1054 LYS A CG    1 
ATOM   8486  C CD    . LYS B 2 1057 ? 129.509 136.182 141.194 1.00 48.55  ? 1054 LYS A CD    1 
ATOM   8487  C CE    . LYS B 2 1057 ? 129.829 135.153 140.118 1.00 48.55  ? 1054 LYS A CE    1 
ATOM   8488  N NZ    . LYS B 2 1057 ? 128.916 133.979 140.183 1.00 48.55  ? 1054 LYS A NZ    1 
ATOM   8489  N N     . MET B 2 1058 ? 130.060 140.709 138.018 1.00 48.55  ? 1055 MET A N     1 
ATOM   8490  C CA    . MET B 2 1058 ? 129.490 141.948 137.505 1.00 48.55  ? 1055 MET A CA    1 
ATOM   8491  C C     . MET B 2 1058 ? 128.830 141.713 136.152 1.00 48.55  ? 1055 MET A C     1 
ATOM   8492  O O     . MET B 2 1058 ? 129.357 140.995 135.297 1.00 48.55  ? 1055 MET A O     1 
ATOM   8493  C CB    . MET B 2 1058 ? 130.561 143.037 137.394 1.00 48.55  ? 1055 MET A CB    1 
ATOM   8494  C CG    . MET B 2 1058 ? 131.656 142.767 136.379 1.00 48.55  ? 1055 MET A CG    1 
ATOM   8495  S SD    . MET B 2 1058 ? 132.902 144.070 136.347 1.00 48.55  ? 1055 MET A SD    1 
ATOM   8496  C CE    . MET B 2 1058 ? 134.016 143.443 135.094 1.00 48.55  ? 1055 MET A CE    1 
ATOM   8497  N N     . GLY B 2 1059 ? 127.661 142.307 135.971 1.00 48.55  ? 1056 GLY A N     1 
ATOM   8498  C CA    . GLY B 2 1059 ? 126.887 142.159 134.757 1.00 48.55  ? 1056 GLY A CA    1 
ATOM   8499  C C     . GLY B 2 1059 ? 127.066 143.321 133.810 1.00 48.55  ? 1056 GLY A C     1 
ATOM   8500  O O     . GLY B 2 1059 ? 128.139 143.926 133.721 1.00 48.55  ? 1056 GLY A O     1 
ATOM   8501  N N     . THR B 2 1060 ? 125.995 143.638 133.085 1.00 48.55  ? 1057 THR A N     1 
ATOM   8502  C CA    . THR B 2 1060 ? 126.017 144.752 132.149 1.00 48.55  ? 1057 THR A CA    1 
ATOM   8503  C C     . THR B 2 1060 ? 125.825 146.099 132.829 1.00 48.55  ? 1057 THR A C     1 
ATOM   8504  O O     . THR B 2 1060 ? 125.944 147.132 132.161 1.00 48.55  ? 1057 THR A O     1 
ATOM   8505  C CB    . THR B 2 1060 ? 124.939 144.565 131.079 1.00 48.55  ? 1057 THR A CB    1 
ATOM   8506  O OG1   . THR B 2 1060 ? 125.217 145.425 129.966 1.00 48.55  ? 1057 THR A OG1   1 
ATOM   8507  C CG2   . THR B 2 1060 ? 123.566 144.900 131.639 1.00 48.55  ? 1057 THR A CG2   1 
ATOM   8508  N N     . GLN B 2 1061 ? 125.535 146.118 134.128 1.00 48.55  ? 1058 GLN A N     1 
ATOM   8509  C CA    . GLN B 2 1061 ? 125.288 147.359 134.848 1.00 48.55  ? 1058 GLN A CA    1 
ATOM   8510  C C     . GLN B 2 1061 ? 125.857 147.261 136.253 1.00 48.55  ? 1058 GLN A C     1 
ATOM   8511  O O     . GLN B 2 1061 ? 125.629 146.269 136.951 1.00 48.55  ? 1058 GLN A O     1 
ATOM   8512  C CB    . GLN B 2 1061 ? 123.788 147.670 134.911 1.00 48.55  ? 1058 GLN A CB    1 
ATOM   8513  C CG    . GLN B 2 1061 ? 123.397 148.619 136.030 1.00 48.55  ? 1058 GLN A CG    1 
ATOM   8514  C CD    . GLN B 2 1061 ? 121.916 148.933 136.035 1.00 48.55  ? 1058 GLN A CD    1 
ATOM   8515  O OE1   . GLN B 2 1061 ? 121.084 148.060 135.789 1.00 48.55  ? 1058 GLN A OE1   1 
ATOM   8516  N NE2   . GLN B 2 1061 ? 121.578 150.185 136.316 1.00 48.55  ? 1058 GLN A NE2   1 
ATOM   8517  N N     . SER B 2 1062 ? 126.596 148.294 136.661 1.00 48.55  ? 1059 SER A N     1 
ATOM   8518  C CA    . SER B 2 1062 ? 127.100 148.427 138.031 1.00 48.55  ? 1059 SER A CA    1 
ATOM   8519  C C     . SER B 2 1062 ? 126.915 149.892 138.419 1.00 48.55  ? 1059 SER A C     1 
ATOM   8520  O O     . SER B 2 1062 ? 127.792 150.725 138.175 1.00 48.55  ? 1059 SER A O     1 
ATOM   8521  C CB    . SER B 2 1062 ? 128.552 147.987 138.143 1.00 48.55  ? 1059 SER A CB    1 
ATOM   8522  O OG    . SER B 2 1062 ? 129.077 148.294 139.423 1.00 48.55  ? 1059 SER A OG    1 
ATOM   8523  N N     . GLY B 2 1063 ? 125.771 150.198 139.024 1.00 48.55  ? 1060 GLY A N     1 
ATOM   8524  C CA    . GLY B 2 1063 ? 125.442 151.569 139.357 1.00 48.55  ? 1060 GLY A CA    1 
ATOM   8525  C C     . GLY B 2 1063 ? 125.266 152.430 138.125 1.00 48.55  ? 1060 GLY A C     1 
ATOM   8526  O O     . GLY B 2 1063 ? 124.431 152.132 137.267 1.00 48.55  ? 1060 GLY A O     1 
ATOM   8527  N N     . PHE B 2 1064 ? 126.049 153.506 138.024 1.00 48.55  ? 1061 PHE A N     1 
ATOM   8528  C CA    . PHE B 2 1064 ? 126.038 154.373 136.853 1.00 48.55  ? 1061 PHE A CA    1 
ATOM   8529  C C     . PHE B 2 1064 ? 127.092 153.982 135.826 1.00 48.55  ? 1061 PHE A C     1 
ATOM   8530  O O     . PHE B 2 1064 ? 127.608 154.850 135.110 1.00 48.55  ? 1061 PHE A O     1 
ATOM   8531  C CB    . PHE B 2 1064 ? 126.222 155.833 137.267 1.00 48.55  ? 1061 PHE A CB    1 
ATOM   8532  C CG    . PHE B 2 1064 ? 124.934 156.568 137.485 1.00 48.55  ? 1061 PHE A CG    1 
ATOM   8533  C CD1   . PHE B 2 1064 ? 124.093 156.228 138.529 1.00 48.55  ? 1061 PHE A CD1   1 
ATOM   8534  C CD2   . PHE B 2 1064 ? 124.556 157.590 136.636 1.00 48.55  ? 1061 PHE A CD2   1 
ATOM   8535  C CE1   . PHE B 2 1064 ? 122.907 156.904 138.727 1.00 48.55  ? 1061 PHE A CE1   1 
ATOM   8536  C CE2   . PHE B 2 1064 ? 123.370 158.264 136.827 1.00 48.55  ? 1061 PHE A CE2   1 
ATOM   8537  C CZ    . PHE B 2 1064 ? 122.546 157.922 137.874 1.00 48.55  ? 1061 PHE A CZ    1 
ATOM   8538  N N     . LEU B 2 1065 ? 127.442 152.702 135.747 1.00 48.55  ? 1062 LEU A N     1 
ATOM   8539  C CA    . LEU B 2 1065 ? 128.340 152.188 134.722 1.00 48.55  ? 1062 LEU A CA    1 
ATOM   8540  C C     . LEU B 2 1065 ? 127.643 151.076 133.957 1.00 48.55  ? 1062 LEU A C     1 
ATOM   8541  O O     . LEU B 2 1065 ? 127.164 150.108 134.558 1.00 48.55  ? 1062 LEU A O     1 
ATOM   8542  C CB    . LEU B 2 1065 ? 129.646 151.672 135.329 1.00 48.55  ? 1062 LEU A CB    1 
ATOM   8543  C CG    . LEU B 2 1065 ? 130.848 152.606 135.201 1.00 48.55  ? 1062 LEU A CG    1 
ATOM   8544  C CD1   . LEU B 2 1065 ? 130.626 153.857 136.016 1.00 48.55  ? 1062 LEU A CD1   1 
ATOM   8545  C CD2   . LEU B 2 1065 ? 132.122 151.902 135.634 1.00 48.55  ? 1062 LEU A CD2   1 
ATOM   8546  N N     . PHE B 2 1066 ? 127.590 151.216 132.638 1.00 48.55  ? 1063 PHE A N     1 
ATOM   8547  C CA    . PHE B 2 1066 ? 127.021 150.208 131.758 1.00 48.55  ? 1063 PHE A CA    1 
ATOM   8548  C C     . PHE B 2 1066 ? 128.126 149.599 130.907 1.00 48.55  ? 1063 PHE A C     1 
ATOM   8549  O O     . PHE B 2 1066 ? 129.047 150.298 130.476 1.00 48.55  ? 1063 PHE A O     1 
ATOM   8550  C CB    . PHE B 2 1066 ? 125.935 150.802 130.857 1.00 48.55  ? 1063 PHE A CB    1 
ATOM   8551  C CG    . PHE B 2 1066 ? 124.687 151.206 131.590 1.00 48.55  ? 1063 PHE A CG    1 
ATOM   8552  C CD1   . PHE B 2 1066 ? 124.446 150.765 132.878 1.00 48.55  ? 1063 PHE A CD1   1 
ATOM   8553  C CD2   . PHE B 2 1066 ? 123.750 152.024 130.984 1.00 48.55  ? 1063 PHE A CD2   1 
ATOM   8554  C CE1   . PHE B 2 1066 ? 123.298 151.135 133.549 1.00 48.55  ? 1063 PHE A CE1   1 
ATOM   8555  C CE2   . PHE B 2 1066 ? 122.601 152.396 131.651 1.00 48.55  ? 1063 PHE A CE2   1 
ATOM   8556  C CZ    . PHE B 2 1066 ? 122.376 151.951 132.935 1.00 48.55  ? 1063 PHE A CZ    1 
ATOM   8557  N N     . TYR B 2 1067 ? 128.040 148.295 130.681 1.00 48.55  ? 1064 TYR A N     1 
ATOM   8558  C CA    . TYR B 2 1067 ? 129.004 147.575 129.864 1.00 48.55  ? 1064 TYR A CA    1 
ATOM   8559  C C     . TYR B 2 1067 ? 128.291 146.965 128.666 1.00 48.55  ? 1064 TYR A C     1 
ATOM   8560  O O     . TYR B 2 1067 ? 127.254 146.311 128.822 1.00 48.55  ? 1064 TYR A O     1 
ATOM   8561  C CB    . TYR B 2 1067 ? 129.713 146.497 130.684 1.00 48.55  ? 1064 TYR A CB    1 
ATOM   8562  C CG    . TYR B 2 1067 ? 130.366 147.034 131.937 1.00 48.55  ? 1064 TYR A CG    1 
ATOM   8563  C CD1   . TYR B 2 1067 ? 131.570 147.720 131.875 1.00 48.55  ? 1064 TYR A CD1   1 
ATOM   8564  C CD2   . TYR B 2 1067 ? 129.776 146.860 133.181 1.00 48.55  ? 1064 TYR A CD2   1 
ATOM   8565  C CE1   . TYR B 2 1067 ? 132.169 148.216 133.014 1.00 48.55  ? 1064 TYR A CE1   1 
ATOM   8566  C CE2   . TYR B 2 1067 ? 130.369 147.352 134.327 1.00 48.55  ? 1064 TYR A CE2   1 
ATOM   8567  C CZ    . TYR B 2 1067 ? 131.566 148.028 134.237 1.00 48.55  ? 1064 TYR A CZ    1 
ATOM   8568  O OH    . TYR B 2 1067 ? 132.162 148.521 135.374 1.00 48.55  ? 1064 TYR A OH    1 
ATOM   8569  N N     . VAL B 2 1068 ? 128.847 147.181 127.479 1.00 48.55  ? 1065 VAL A N     1 
ATOM   8570  C CA    . VAL B 2 1068 ? 128.225 146.739 126.234 1.00 48.55  ? 1065 VAL A CA    1 
ATOM   8571  C C     . VAL B 2 1068 ? 129.244 145.947 125.424 1.00 48.55  ? 1065 VAL A C     1 
ATOM   8572  O O     . VAL B 2 1068 ? 130.456 146.147 125.593 1.00 48.55  ? 1065 VAL A O     1 
ATOM   8573  C CB    . VAL B 2 1068 ? 127.686 147.932 125.429 1.00 48.55  ? 1065 VAL A CB    1 
ATOM   8574  C CG1   . VAL B 2 1068 ? 126.494 148.555 126.137 1.00 48.55  ? 1065 VAL A CG1   1 
ATOM   8575  C CG2   . VAL B 2 1068 ? 128.782 148.957 125.205 1.00 48.55  ? 1065 VAL A CG2   1 
ATOM   8576  N N     . PRO B 2 1069 ? 128.809 145.033 124.556 1.00 48.55  ? 1066 PRO A N     1 
ATOM   8577  C CA    . PRO B 2 1069 ? 129.768 144.274 123.746 1.00 48.55  ? 1066 PRO A CA    1 
ATOM   8578  C C     . PRO B 2 1069 ? 130.605 145.183 122.857 1.00 48.55  ? 1066 PRO A C     1 
ATOM   8579  O O     . PRO B 2 1069 ? 130.088 146.065 122.170 1.00 48.55  ? 1066 PRO A O     1 
ATOM   8580  C CB    . PRO B 2 1069 ? 128.873 143.346 122.917 1.00 48.55  ? 1066 PRO A CB    1 
ATOM   8581  C CG    . PRO B 2 1069 ? 127.634 143.202 123.724 1.00 48.55  ? 1066 PRO A CG    1 
ATOM   8582  C CD    . PRO B 2 1069 ? 127.436 144.518 124.417 1.00 48.55  ? 1066 PRO A CD    1 
ATOM   8583  N N     . ALA B 2 1070 ? 131.916 144.954 122.888 1.00 48.55  ? 1067 ALA A N     1 
ATOM   8584  C CA    . ALA B 2 1070 ? 132.836 145.722 122.050 1.00 48.55  ? 1067 ALA A CA    1 
ATOM   8585  C C     . ALA B 2 1070 ? 132.611 145.531 120.554 1.00 48.55  ? 1067 ALA A C     1 
ATOM   8586  O O     . ALA B 2 1070 ? 132.635 146.537 119.823 1.00 48.55  ? 1067 ALA A O     1 
ATOM   8587  C CB    . ALA B 2 1070 ? 134.279 145.383 122.437 1.00 48.55  ? 1067 ALA A CB    1 
ATOM   8588  N N     . PRO B 2 1071 ? 132.413 144.315 120.026 1.00 48.55  ? 1068 PRO A N     1 
ATOM   8589  C CA    . PRO B 2 1071 ? 132.370 144.155 118.566 1.00 48.55  ? 1068 PRO A CA    1 
ATOM   8590  C C     . PRO B 2 1071 ? 131.241 144.943 117.920 1.00 48.55  ? 1068 PRO A C     1 
ATOM   8591  O O     . PRO B 2 1071 ? 130.199 145.197 118.528 1.00 48.55  ? 1068 PRO A O     1 
ATOM   8592  C CB    . PRO B 2 1071 ? 132.171 142.645 118.378 1.00 48.55  ? 1068 PRO A CB    1 
ATOM   8593  C CG    . PRO B 2 1071 ? 131.650 142.158 119.677 1.00 48.55  ? 1068 PRO A CG    1 
ATOM   8594  C CD    . PRO B 2 1071 ? 132.323 143.007 120.698 1.00 48.55  ? 1068 PRO A CD    1 
ATOM   8595  N N     . TYR B 2 1072 ? 131.477 145.334 116.667 1.00 48.55  ? 1069 TYR A N     1 
ATOM   8596  C CA    . TYR B 2 1072 ? 130.542 146.123 115.866 1.00 48.55  ? 1069 TYR A CA    1 
ATOM   8597  C C     . TYR B 2 1072 ? 130.264 147.475 116.525 1.00 48.55  ? 1069 TYR A C     1 
ATOM   8598  O O     . TYR B 2 1072 ? 129.132 147.816 116.873 1.00 48.55  ? 1069 TYR A O     1 
ATOM   8599  C CB    . TYR B 2 1072 ? 129.247 145.349 115.597 1.00 48.55  ? 1069 TYR A CB    1 
ATOM   8600  C CG    . TYR B 2 1072 ? 129.468 144.024 114.903 1.00 48.55  ? 1069 TYR A CG    1 
ATOM   8601  C CD1   . TYR B 2 1072 ? 129.827 142.891 115.620 1.00 48.55  ? 1069 TYR A CD1   1 
ATOM   8602  C CD2   . TYR B 2 1072 ? 129.337 143.912 113.527 1.00 48.55  ? 1069 TYR A CD2   1 
ATOM   8603  C CE1   . TYR B 2 1072 ? 130.037 141.682 114.988 1.00 48.55  ? 1069 TYR A CE1   1 
ATOM   8604  C CE2   . TYR B 2 1072 ? 129.545 142.708 112.885 1.00 48.55  ? 1069 TYR A CE2   1 
ATOM   8605  C CZ    . TYR B 2 1072 ? 129.895 141.596 113.620 1.00 48.55  ? 1069 TYR A CZ    1 
ATOM   8606  O OH    . TYR B 2 1072 ? 130.103 140.394 112.985 1.00 48.55  ? 1069 TYR A OH    1 
ATOM   8607  N N     . THR B 2 1073 ? 131.343 148.236 116.708 1.00 48.55  ? 1070 THR A N     1 
ATOM   8608  C CA    . THR B 2 1073 ? 131.264 149.624 117.144 1.00 48.55  ? 1070 THR A CA    1 
ATOM   8609  C C     . THR B 2 1073 ? 132.149 150.569 116.347 1.00 48.55  ? 1070 THR A C     1 
ATOM   8610  O O     . THR B 2 1073 ? 131.870 151.774 116.334 1.00 48.55  ? 1070 THR A O     1 
ATOM   8611  C CB    . THR B 2 1073 ? 131.630 149.751 118.631 1.00 48.55  ? 1070 THR A CB    1 
ATOM   8612  O OG1   . THR B 2 1073 ? 132.893 149.118 118.871 1.00 48.55  ? 1070 THR A OG1   1 
ATOM   8613  C CG2   . THR B 2 1073 ? 130.564 149.111 119.508 1.00 48.55  ? 1070 THR A CG2   1 
ATOM   8614  N N     . SER B 2 1074 ? 133.196 150.077 115.687 1.00 48.55  ? 1071 SER A N     1 
ATOM   8615  C CA    . SER B 2 1074 ? 134.102 150.907 114.903 1.00 48.55  ? 1071 SER A CA    1 
ATOM   8616  C C     . SER B 2 1074 ? 133.891 150.744 113.404 1.00 48.55  ? 1071 SER A C     1 
ATOM   8617  O O     . SER B 2 1074 ? 133.877 151.735 112.668 1.00 48.55  ? 1071 SER A O     1 
ATOM   8618  C CB    . SER B 2 1074 ? 135.556 150.581 115.265 1.00 48.55  ? 1071 SER A CB    1 
ATOM   8619  O OG    . SER B 2 1074 ? 136.456 151.413 114.555 1.00 48.55  ? 1071 SER A OG    1 
ATOM   8620  N N     . LYS B 2 1075 ? 133.725 149.509 112.934 1.00 48.55  ? 1072 LYS A N     1 
ATOM   8621  C CA    . LYS B 2 1075 ? 133.509 149.249 111.516 1.00 48.55  ? 1072 LYS A CA    1 
ATOM   8622  C C     . LYS B 2 1075 ? 132.047 149.461 111.146 1.00 48.55  ? 1072 LYS A C     1 
ATOM   8623  O O     . LYS B 2 1075 ? 131.427 148.592 110.525 1.00 48.55  ? 1072 LYS A O     1 
ATOM   8624  C CB    . LYS B 2 1075 ? 133.933 147.821 111.159 1.00 48.55  ? 1072 LYS A CB    1 
ATOM   8625  C CG    . LYS B 2 1075 ? 135.277 147.383 111.723 1.00 48.55  ? 1072 LYS A CG    1 
ATOM   8626  C CD    . LYS B 2 1075 ? 136.354 148.423 111.482 1.00 48.55  ? 1072 LYS A CD    1 
ATOM   8627  C CE    . LYS B 2 1075 ? 136.864 148.342 110.055 1.00 48.55  ? 1072 LYS A CE    1 
ATOM   8628  N NZ    . LYS B 2 1075 ? 137.387 146.986 109.727 1.00 48.55  ? 1072 LYS A NZ    1 
ATOM   8629  N N     . ILE B 2 1076 ? 131.488 150.609 111.518 1.00 48.55  ? 1073 ILE A N     1 
ATOM   8630  C CA    . ILE B 2 1076 ? 130.093 150.932 111.251 1.00 48.55  ? 1073 ILE A CA    1 
ATOM   8631  C C     . ILE B 2 1076 ? 130.019 152.360 110.734 1.00 48.55  ? 1073 ILE A C     1 
ATOM   8632  O O     . ILE B 2 1076 ? 130.634 153.265 111.308 1.00 48.55  ? 1073 ILE A O     1 
ATOM   8633  C CB    . ILE B 2 1076 ? 129.212 150.771 112.505 1.00 48.55  ? 1073 ILE A CB    1 
ATOM   8634  C CG1   . ILE B 2 1076 ? 129.132 149.306 112.926 1.00 48.55  ? 1073 ILE A CG1   1 
ATOM   8635  C CG2   . ILE B 2 1076 ? 127.816 151.318 112.259 1.00 48.55  ? 1073 ILE A CG2   1 
ATOM   8636  C CD1   . ILE B 2 1076 ? 128.255 149.074 114.128 1.00 48.55  ? 1073 ILE A CD1   1 
ATOM   8637  N N     . ASP B 2 1077 ? 129.276 152.557 109.658 1.00 48.55  ? 1074 ASP A N     1 
ATOM   8638  C CA    . ASP B 2 1077 ? 128.980 153.898 109.179 1.00 48.55  ? 1074 ASP A CA    1 
ATOM   8639  C C     . ASP B 2 1077 ? 128.036 154.580 110.158 1.00 48.55  ? 1074 ASP A C     1 
ATOM   8640  O O     . ASP B 2 1077 ? 126.919 154.087 110.362 1.00 48.55  ? 1074 ASP A O     1 
ATOM   8641  C CB    . ASP B 2 1077 ? 128.346 153.830 107.794 1.00 48.55  ? 1074 ASP A CB    1 
ATOM   8642  C CG    . ASP B 2 1077 ? 128.213 155.189 107.143 1.00 48.55  ? 1074 ASP A CG    1 
ATOM   8643  O OD1   . ASP B 2 1077 ? 128.742 156.176 107.695 1.00 48.55  ? 1074 ASP A OD1   1 
ATOM   8644  O OD2   . ASP B 2 1077 ? 127.561 155.273 106.083 1.00 48.55  ? 1074 ASP A OD2   1 
ATOM   8645  N N     . PRO B 2 1078 ? 128.423 155.693 110.783 1.00 48.55  ? 1075 PRO A N     1 
ATOM   8646  C CA    . PRO B 2 1078 ? 127.484 156.389 111.675 1.00 48.55  ? 1075 PRO A CA    1 
ATOM   8647  C C     . PRO B 2 1078 ? 126.251 156.915 110.964 1.00 48.55  ? 1075 PRO A C     1 
ATOM   8648  O O     . PRO B 2 1078 ? 125.187 157.005 111.586 1.00 48.55  ? 1075 PRO A O     1 
ATOM   8649  C CB    . PRO B 2 1078 ? 128.328 157.529 112.259 1.00 48.55  ? 1075 PRO A CB    1 
ATOM   8650  C CG    . PRO B 2 1078 ? 129.450 157.708 111.301 1.00 48.55  ? 1075 PRO A CG    1 
ATOM   8651  C CD    . PRO B 2 1078 ? 129.735 156.356 110.729 1.00 48.55  ? 1075 PRO A CD    1 
ATOM   8652  N N     . LEU B 2 1079 ? 126.359 157.263 109.681 1.00 48.55  ? 1076 LEU A N     1 
ATOM   8653  C CA    . LEU B 2 1079 ? 125.225 157.834 108.963 1.00 48.55  ? 1076 LEU A CA    1 
ATOM   8654  C C     . LEU B 2 1079 ? 124.201 156.774 108.572 1.00 48.55  ? 1076 LEU A C     1 
ATOM   8655  O O     . LEU B 2 1079 ? 122.995 157.043 108.587 1.00 48.55  ? 1076 LEU A O     1 
ATOM   8656  C CB    . LEU B 2 1079 ? 125.720 158.580 107.726 1.00 48.55  ? 1076 LEU A CB    1 
ATOM   8657  C CG    . LEU B 2 1079 ? 126.001 160.069 107.922 1.00 48.55  ? 1076 LEU A CG    1 
ATOM   8658  C CD1   . LEU B 2 1079 ? 126.383 160.723 106.607 1.00 48.55  ? 1076 LEU A CD1   1 
ATOM   8659  C CD2   . LEU B 2 1079 ? 124.789 160.755 108.523 1.00 48.55  ? 1076 LEU A CD2   1 
ATOM   8660  N N     . THR B 2 1080 ? 124.654 155.569 108.218 1.00 48.55  ? 1077 THR A N     1 
ATOM   8661  C CA    . THR B 2 1080 ? 123.765 154.530 107.718 1.00 48.55  ? 1077 THR A CA    1 
ATOM   8662  C C     . THR B 2 1080 ? 123.734 153.263 108.558 1.00 48.55  ? 1077 THR A C     1 
ATOM   8663  O O     . THR B 2 1080 ? 122.806 152.465 108.393 1.00 48.55  ? 1077 THR A O     1 
ATOM   8664  C CB    . THR B 2 1080 ? 124.149 154.135 106.283 1.00 48.55  ? 1077 THR A CB    1 
ATOM   8665  O OG1   . THR B 2 1080 ? 125.336 153.333 106.310 1.00 48.55  ? 1077 THR A OG1   1 
ATOM   8666  C CG2   . THR B 2 1080 ? 124.400 155.367 105.436 1.00 48.55  ? 1077 THR A CG2   1 
ATOM   8667  N N     . GLY B 2 1081 ? 124.706 153.047 109.439 1.00 48.55  ? 1078 GLY A N     1 
ATOM   8668  C CA    . GLY B 2 1081 ? 124.772 151.798 110.166 1.00 48.55  ? 1078 GLY A CA    1 
ATOM   8669  C C     . GLY B 2 1081 ? 125.290 150.631 109.361 1.00 48.55  ? 1078 GLY A C     1 
ATOM   8670  O O     . GLY B 2 1081 ? 125.116 149.481 109.780 1.00 48.55  ? 1078 GLY A O     1 
ATOM   8671  N N     . PHE B 2 1082 ? 125.918 150.891 108.220 1.00 48.55  ? 1079 PHE A N     1 
ATOM   8672  C CA    . PHE B 2 1082 ? 126.391 149.825 107.352 1.00 48.55  ? 1079 PHE A CA    1 
ATOM   8673  C C     . PHE B 2 1082 ? 127.663 149.193 107.904 1.00 48.55  ? 1079 PHE A C     1 
ATOM   8674  O O     . PHE B 2 1082 ? 128.491 149.862 108.527 1.00 48.55  ? 1079 PHE A O     1 
ATOM   8675  C CB    . PHE B 2 1082 ? 126.644 150.373 105.950 1.00 48.55  ? 1079 PHE A CB    1 
ATOM   8676  C CG    . PHE B 2 1082 ? 127.084 149.337 104.963 1.00 48.55  ? 1079 PHE A CG    1 
ATOM   8677  C CD1   . PHE B 2 1082 ? 126.177 148.440 104.430 1.00 48.55  ? 1079 PHE A CD1   1 
ATOM   8678  C CD2   . PHE B 2 1082 ? 128.402 149.265 104.563 1.00 48.55  ? 1079 PHE A CD2   1 
ATOM   8679  C CE1   . PHE B 2 1082 ? 126.579 147.489 103.518 1.00 48.55  ? 1079 PHE A CE1   1 
ATOM   8680  C CE2   . PHE B 2 1082 ? 128.807 148.318 103.654 1.00 48.55  ? 1079 PHE A CE2   1 
ATOM   8681  C CZ    . PHE B 2 1082 ? 127.897 147.428 103.129 1.00 48.55  ? 1079 PHE A CZ    1 
ATOM   8682  N N     . VAL B 2 1083 ? 127.807 147.888 107.674 1.00 48.55  ? 1080 VAL A N     1 
ATOM   8683  C CA    . VAL B 2 1083 ? 129.012 147.146 108.015 1.00 48.55  ? 1080 VAL A CA    1 
ATOM   8684  C C     . VAL B 2 1083 ? 129.436 146.351 106.790 1.00 48.55  ? 1080 VAL A C     1 
ATOM   8685  O O     . VAL B 2 1083 ? 128.645 146.106 105.878 1.00 48.55  ? 1080 VAL A O     1 
ATOM   8686  C CB    . VAL B 2 1083 ? 128.812 146.202 109.220 1.00 48.55  ? 1080 VAL A CB    1 
ATOM   8687  C CG1   . VAL B 2 1083 ? 128.301 146.970 110.417 1.00 48.55  ? 1080 VAL A CG1   1 
ATOM   8688  C CG2   . VAL B 2 1083 ? 127.858 145.077 108.859 1.00 48.55  ? 1080 VAL A CG2   1 
ATOM   8689  N N     . ASP B 2 1084 ? 130.708 145.958 106.775 1.00 48.55  ? 1081 ASP A N     1 
ATOM   8690  C CA    . ASP B 2 1084 ? 131.222 145.109 105.709 1.00 48.55  ? 1081 ASP A CA    1 
ATOM   8691  C C     . ASP B 2 1084 ? 130.470 143.788 105.809 1.00 48.55  ? 1081 ASP A C     1 
ATOM   8692  O O     . ASP B 2 1084 ? 130.690 143.018 106.753 1.00 48.55  ? 1081 ASP A O     1 
ATOM   8693  C CB    . ASP B 2 1084 ? 132.739 144.929 105.848 1.00 48.55  ? 1081 ASP A CB    1 
ATOM   8694  C CG    . ASP B 2 1084 ? 133.330 143.921 104.859 1.00 48.55  ? 1081 ASP A CG    1 
ATOM   8695  O OD1   . ASP B 2 1084 ? 132.588 143.169 104.192 1.00 48.55  ? 1081 ASP A OD1   1 
ATOM   8696  O OD2   . ASP B 2 1084 ? 134.573 143.884 104.749 1.00 48.55  ? 1081 ASP A OD2   1 
ATOM   8697  N N     . PRO B 2 1085 ? 129.578 143.487 104.861 1.00 48.55  ? 1082 PRO A N     1 
ATOM   8698  C CA    . PRO B 2 1085 ? 128.700 142.323 105.020 1.00 48.55  ? 1082 PRO A CA    1 
ATOM   8699  C C     . PRO B 2 1085 ? 129.357 140.998 104.690 1.00 48.55  ? 1082 PRO A C     1 
ATOM   8700  O O     . PRO B 2 1085 ? 128.754 139.950 104.957 1.00 48.55  ? 1082 PRO A O     1 
ATOM   8701  C CB    . PRO B 2 1085 ? 127.558 142.623 104.045 1.00 48.55  ? 1082 PRO A CB    1 
ATOM   8702  C CG    . PRO B 2 1085 ? 128.206 143.417 102.959 1.00 48.55  ? 1082 PRO A CG    1 
ATOM   8703  C CD    . PRO B 2 1085 ? 129.394 144.141 103.554 1.00 48.55  ? 1082 PRO A CD    1 
ATOM   8704  N N     . PHE B 2 1086 ? 130.562 141.002 104.131 1.00 48.55  ? 1083 PHE A N     1 
ATOM   8705  C CA    . PHE B 2 1086 ? 131.222 139.786 103.684 1.00 48.55  ? 1083 PHE A CA    1 
ATOM   8706  C C     . PHE B 2 1086 ? 132.448 139.503 104.538 1.00 48.55  ? 1083 PHE A C     1 
ATOM   8707  O O     . PHE B 2 1086 ? 133.168 140.424 104.936 1.00 48.55  ? 1083 PHE A O     1 
ATOM   8708  C CB    . PHE B 2 1086 ? 131.640 139.895 102.217 1.00 48.55  ? 1083 PHE A CB    1 
ATOM   8709  C CG    . PHE B 2 1086 ? 130.611 140.537 101.341 1.00 48.55  ? 1083 PHE A CG    1 
ATOM   8710  C CD1   . PHE B 2 1086 ? 129.422 139.891 101.063 1.00 48.55  ? 1083 PHE A CD1   1 
ATOM   8711  C CD2   . PHE B 2 1086 ? 130.833 141.786 100.792 1.00 48.55  ? 1083 PHE A CD2   1 
ATOM   8712  C CE1   . PHE B 2 1086 ? 128.475 140.478 100.256 1.00 48.55  ? 1083 PHE A CE1   1 
ATOM   8713  C CE2   . PHE B 2 1086 ? 129.888 142.379 99.984  1.00 48.55  ? 1083 PHE A CE2   1 
ATOM   8714  C CZ    . PHE B 2 1086 ? 128.706 141.725 99.716  1.00 48.55  ? 1083 PHE A CZ    1 
ATOM   8715  N N     . VAL B 2 1087 ? 132.679 138.225 104.817 1.00 48.55  ? 1084 VAL A N     1 
ATOM   8716  C CA    . VAL B 2 1087 ? 133.921 137.780 105.433 1.00 48.55  ? 1084 VAL A CA    1 
ATOM   8717  C C     . VAL B 2 1087 ? 134.880 137.368 104.322 1.00 48.55  ? 1084 VAL A C     1 
ATOM   8718  O O     . VAL B 2 1087 ? 134.576 136.490 103.507 1.00 48.55  ? 1084 VAL A O     1 
ATOM   8719  C CB    . VAL B 2 1087 ? 133.676 136.645 106.442 1.00 48.55  ? 1084 VAL A CB    1 
ATOM   8720  C CG1   . VAL B 2 1087 ? 132.792 137.142 107.570 1.00 48.55  ? 1084 VAL A CG1   1 
ATOM   8721  C CG2   . VAL B 2 1087 ? 132.999 135.457 105.784 1.00 48.55  ? 1084 VAL A CG2   1 
ATOM   8722  N N     . TRP B 2 1088 ? 136.025 138.043 104.258 1.00 48.55  ? 1085 TRP A N     1 
ATOM   8723  C CA    . TRP B 2 1088 ? 136.962 137.857 103.160 1.00 48.55  ? 1085 TRP A CA    1 
ATOM   8724  C C     . TRP B 2 1088 ? 137.801 136.596 103.303 1.00 48.55  ? 1085 TRP A C     1 
ATOM   8725  O O     . TRP B 2 1088 ? 138.515 136.237 102.361 1.00 48.55  ? 1085 TRP A O     1 
ATOM   8726  C CB    . TRP B 2 1088 ? 137.864 139.086 103.051 1.00 48.55  ? 1085 TRP A CB    1 
ATOM   8727  C CG    . TRP B 2 1088 ? 137.104 140.318 102.673 1.00 48.55  ? 1085 TRP A CG    1 
ATOM   8728  C CD1   . TRP B 2 1088 ? 136.929 141.437 103.432 1.00 48.55  ? 1085 TRP A CD1   1 
ATOM   8729  C CD2   . TRP B 2 1088 ? 136.410 140.555 101.443 1.00 48.55  ? 1085 TRP A CD2   1 
ATOM   8730  N NE1   . TRP B 2 1088 ? 136.170 142.357 102.751 1.00 48.55  ? 1085 TRP A NE1   1 
ATOM   8731  C CE2   . TRP B 2 1088 ? 135.839 141.839 101.527 1.00 48.55  ? 1085 TRP A CE2   1 
ATOM   8732  C CE3   . TRP B 2 1088 ? 136.217 139.807 100.278 1.00 48.55  ? 1085 TRP A CE3   1 
ATOM   8733  C CZ2   . TRP B 2 1088 ? 135.088 142.391 100.494 1.00 48.55  ? 1085 TRP A CZ2   1 
ATOM   8734  C CZ3   . TRP B 2 1088 ? 135.471 140.357 99.253  1.00 48.55  ? 1085 TRP A CZ3   1 
ATOM   8735  C CH2   . TRP B 2 1088 ? 134.917 141.636 99.367  1.00 48.55  ? 1085 TRP A CH2   1 
ATOM   8736  N N     . LYS B 2 1089 ? 137.732 135.922 104.451 1.00 58.24  ? 1086 LYS A N     1 
ATOM   8737  C CA    . LYS B 2 1089 ? 138.481 134.685 104.631 1.00 58.24  ? 1086 LYS A CA    1 
ATOM   8738  C C     . LYS B 2 1089 ? 137.906 133.552 103.790 1.00 58.24  ? 1086 LYS A C     1 
ATOM   8739  O O     . LYS B 2 1089 ? 138.635 132.625 103.423 1.00 58.24  ? 1086 LYS A O     1 
ATOM   8740  C CB    . LYS B 2 1089 ? 138.494 134.298 106.111 1.00 58.24  ? 1086 LYS A CB    1 
ATOM   8741  C CG    . LYS B 2 1089 ? 139.457 133.176 106.465 1.00 58.24  ? 1086 LYS A CG    1 
ATOM   8742  C CD    . LYS B 2 1089 ? 140.865 133.482 105.981 1.00 58.24  ? 1086 LYS A CD    1 
ATOM   8743  C CE    . LYS B 2 1089 ? 141.487 134.621 106.772 1.00 58.24  ? 1086 LYS A CE    1 
ATOM   8744  N NZ    . LYS B 2 1089 ? 142.962 134.690 106.579 1.00 58.24  ? 1086 LYS A NZ    1 
ATOM   8745  N N     . THR B 2 1090 ? 136.609 133.605 103.477 1.00 48.72  ? 1087 THR A N     1 
ATOM   8746  C CA    . THR B 2 1090 ? 135.967 132.490 102.787 1.00 48.72  ? 1087 THR A CA    1 
ATOM   8747  C C     . THR B 2 1090 ? 136.524 132.292 101.383 1.00 48.72  ? 1087 THR A C     1 
ATOM   8748  O O     . THR B 2 1090 ? 136.776 131.156 100.964 1.00 48.72  ? 1087 THR A O     1 
ATOM   8749  C CB    . THR B 2 1090 ? 134.456 132.705 102.728 1.00 48.72  ? 1087 THR A CB    1 
ATOM   8750  O OG1   . THR B 2 1090 ? 134.180 134.067 102.379 1.00 48.72  ? 1087 THR A OG1   1 
ATOM   8751  C CG2   . THR B 2 1090 ? 133.820 132.384 104.069 1.00 48.72  ? 1087 THR A CG2   1 
ATOM   8752  N N     . ILE B 2 1091 ? 136.723 133.376 100.641 1.00 49.71  ? 1088 ILE A N     1 
ATOM   8753  C CA    . ILE B 2 1091 ? 137.034 133.272 99.219  1.00 49.71  ? 1088 ILE A CA    1 
ATOM   8754  C C     . ILE B 2 1091 ? 138.545 133.245 99.014  1.00 49.71  ? 1088 ILE A C     1 
ATOM   8755  O O     . ILE B 2 1091 ? 139.267 134.135 99.474  1.00 49.71  ? 1088 ILE A O     1 
ATOM   8756  C CB    . ILE B 2 1091 ? 136.382 134.415 98.426  1.00 49.71  ? 1088 ILE A CB    1 
ATOM   8757  C CG1   . ILE B 2 1091 ? 136.743 135.777 99.021  1.00 49.71  ? 1088 ILE A CG1   1 
ATOM   8758  C CG2   . ILE B 2 1091 ? 134.871 134.242 98.395  1.00 49.71  ? 1088 ILE A CG2   1 
ATOM   8759  C CD1   . ILE B 2 1091 ? 136.296 136.942 98.171  1.00 49.71  ? 1088 ILE A CD1   1 
ATOM   8760  N N     . LYS B 2 1092 ? 139.028 132.202 98.336  1.00 54.96  ? 1089 LYS A N     1 
ATOM   8761  C CA    . LYS B 2 1092 ? 140.402 132.153 97.851  1.00 54.96  ? 1089 LYS A CA    1 
ATOM   8762  C C     . LYS B 2 1092 ? 140.426 131.862 96.357  1.00 54.96  ? 1089 LYS A C     1 
ATOM   8763  O O     . LYS B 2 1092 ? 141.242 132.421 95.617  1.00 54.96  ? 1089 LYS A O     1 
ATOM   8764  C CB    . LYS B 2 1092 ? 141.225 131.079 98.570  1.00 54.96  ? 1089 LYS A CB    1 
ATOM   8765  C CG    . LYS B 2 1092 ? 141.776 131.434 99.941  1.00 54.96  ? 1089 LYS A CG    1 
ATOM   8766  C CD    . LYS B 2 1092 ? 140.744 131.298 101.040 1.00 54.96  ? 1089 LYS A CD    1 
ATOM   8767  C CE    . LYS B 2 1092 ? 141.407 131.463 102.399 1.00 54.96  ? 1089 LYS A CE    1 
ATOM   8768  N NZ    . LYS B 2 1092 ? 140.434 131.378 103.517 1.00 54.96  ? 1089 LYS A NZ    1 
ATOM   8769  N N     . ASN B 2 1093 ? 139.530 130.990 95.910  1.00 54.12  ? 1090 ASN A N     1 
ATOM   8770  C CA    . ASN B 2 1093 ? 139.598 130.395 94.585  1.00 54.12  ? 1090 ASN A CA    1 
ATOM   8771  C C     . ASN B 2 1093 ? 138.998 131.315 93.528  1.00 54.12  ? 1090 ASN A C     1 
ATOM   8772  O O     . ASN B 2 1093 ? 138.287 132.278 93.824  1.00 54.12  ? 1090 ASN A O     1 
ATOM   8773  C CB    . ASN B 2 1093 ? 138.883 129.040 94.576  1.00 54.12  ? 1090 ASN A CB    1 
ATOM   8774  C CG    . ASN B 2 1093 ? 139.650 127.972 95.329  1.00 54.12  ? 1090 ASN A CG    1 
ATOM   8775  O OD1   . ASN B 2 1093 ? 140.874 127.881 95.227  1.00 54.12  ? 1090 ASN A OD1   1 
ATOM   8776  N ND2   . ASN B 2 1093 ? 138.933 127.156 96.093  1.00 54.12  ? 1090 ASN A ND2   1 
ATOM   8777  N N     . HIS B 2 1094 ? 139.310 130.998 92.270  1.00 53.45  ? 1091 HIS A N     1 
ATOM   8778  C CA    . HIS B 2 1094 ? 138.739 131.731 91.146  1.00 53.45  ? 1091 HIS A CA    1 
ATOM   8779  C C     . HIS B 2 1094 ? 137.241 131.484 91.031  1.00 53.45  ? 1091 HIS A C     1 
ATOM   8780  O O     . HIS B 2 1094 ? 136.480 132.391 90.673  1.00 53.45  ? 1091 HIS A O     1 
ATOM   8781  C CB    . HIS B 2 1094 ? 139.452 131.327 89.856  1.00 53.45  ? 1091 HIS A CB    1 
ATOM   8782  C CG    . HIS B 2 1094 ? 139.050 132.132 88.661  1.00 53.45  ? 1091 HIS A CG    1 
ATOM   8783  N ND1   . HIS B 2 1094 ? 137.965 131.808 87.876  1.00 53.45  ? 1091 HIS A ND1   1 
ATOM   8784  C CD2   . HIS B 2 1094 ? 139.600 133.237 88.105  1.00 53.45  ? 1091 HIS A CD2   1 
ATOM   8785  C CE1   . HIS B 2 1094 ? 137.859 132.685 86.893  1.00 53.45  ? 1091 HIS A CE1   1 
ATOM   8786  N NE2   . HIS B 2 1094 ? 138.841 133.560 87.008  1.00 53.45  ? 1091 HIS A NE2   1 
ATOM   8787  N N     . GLU B 2 1095 ? 136.801 130.256 91.319  1.00 56.31  ? 1092 GLU A N     1 
ATOM   8788  C CA    . GLU B 2 1095 ? 135.381 129.930 91.222  1.00 56.31  ? 1092 GLU A CA    1 
ATOM   8789  C C     . GLU B 2 1095 ? 134.559 130.722 92.230  1.00 56.31  ? 1092 GLU A C     1 
ATOM   8790  O O     . GLU B 2 1095 ? 133.459 131.190 91.915  1.00 56.31  ? 1092 GLU A O     1 
ATOM   8791  C CB    . GLU B 2 1095 ? 135.172 128.429 91.421  1.00 56.31  ? 1092 GLU A CB    1 
ATOM   8792  C CG    . GLU B 2 1095 ? 135.367 127.601 90.161  1.00 56.31  ? 1092 GLU A CG    1 
ATOM   8793  C CD    . GLU B 2 1095 ? 134.417 127.999 89.048  1.00 56.31  ? 1092 GLU A CD    1 
ATOM   8794  O OE1   . GLU B 2 1095 ? 133.262 127.525 89.053  1.00 56.31  ? 1092 GLU A OE1   1 
ATOM   8795  O OE2   . GLU B 2 1095 ? 134.827 128.784 88.167  1.00 56.31  ? 1092 GLU A OE2   1 
ATOM   8796  N N     . SER B 2 1096 ? 135.072 130.874 93.454  1.00 52.17  ? 1093 SER A N     1 
ATOM   8797  C CA    . SER B 2 1096 ? 134.368 131.669 94.454  1.00 52.17  ? 1093 SER A CA    1 
ATOM   8798  C C     . SER B 2 1096 ? 134.263 133.125 94.022  1.00 52.17  ? 1093 SER A C     1 
ATOM   8799  O O     . SER B 2 1096 ? 133.281 133.806 94.340  1.00 52.17  ? 1093 SER A O     1 
ATOM   8800  C CB    . SER B 2 1096 ? 135.074 131.559 95.805  1.00 52.17  ? 1093 SER A CB    1 
ATOM   8801  O OG    . SER B 2 1096 ? 136.236 132.368 95.837  1.00 52.17  ? 1093 SER A OG    1 
ATOM   8802  N N     . ARG B 2 1097 ? 135.268 133.621 93.299  1.00 51.15  ? 1094 ARG A N     1 
ATOM   8803  C CA    . ARG B 2 1097 ? 135.209 134.987 92.792  1.00 51.15  ? 1094 ARG A CA    1 
ATOM   8804  C C     . ARG B 2 1097 ? 134.115 135.137 91.743  1.00 51.15  ? 1094 ARG A C     1 
ATOM   8805  O O     . ARG B 2 1097 ? 133.479 136.193 91.647  1.00 51.15  ? 1094 ARG A O     1 
ATOM   8806  C CB    . ARG B 2 1097 ? 136.569 135.394 92.228  1.00 51.15  ? 1094 ARG A CB    1 
ATOM   8807  C CG    . ARG B 2 1097 ? 137.642 135.546 93.293  1.00 51.15  ? 1094 ARG A CG    1 
ATOM   8808  C CD    . ARG B 2 1097 ? 138.906 136.170 92.734  1.00 51.15  ? 1094 ARG A CD    1 
ATOM   8809  N NE    . ARG B 2 1097 ? 140.026 136.034 93.658  1.00 51.15  ? 1094 ARG A NE    1 
ATOM   8810  C CZ    . ARG B 2 1097 ? 140.803 134.963 93.741  1.00 51.15  ? 1094 ARG A CZ    1 
ATOM   8811  N NH1   . ARG B 2 1097 ? 140.620 133.915 92.956  1.00 51.15  ? 1094 ARG A NH1   1 
ATOM   8812  N NH2   . ARG B 2 1097 ? 141.792 134.947 94.630  1.00 51.15  ? 1094 ARG A NH2   1 
ATOM   8813  N N     . LYS B 2 1098 ? 133.887 134.095 90.938  1.00 52.41  ? 1095 LYS A N     1 
ATOM   8814  C CA    . LYS B 2 1098 ? 132.742 134.106 90.034  1.00 52.41  ? 1095 LYS A CA    1 
ATOM   8815  C C     . LYS B 2 1098 ? 131.436 134.189 90.810  1.00 52.41  ? 1095 LYS A C     1 
ATOM   8816  O O     . LYS B 2 1098 ? 130.545 134.974 90.463  1.00 52.41  ? 1095 LYS A O     1 
ATOM   8817  C CB    . LYS B 2 1098 ? 132.742 132.856 89.153  1.00 52.41  ? 1095 LYS A CB    1 
ATOM   8818  C CG    . LYS B 2 1098 ? 133.712 132.873 87.985  1.00 52.41  ? 1095 LYS A CG    1 
ATOM   8819  C CD    . LYS B 2 1098 ? 133.291 131.835 86.951  1.00 52.41  ? 1095 LYS A CD    1 
ATOM   8820  C CE    . LYS B 2 1098 ? 134.267 131.750 85.791  1.00 52.41  ? 1095 LYS A CE    1 
ATOM   8821  N NZ    . LYS B 2 1098 ? 135.474 130.960 86.150  1.00 52.41  ? 1095 LYS A NZ    1 
ATOM   8822  N N     . HIS B 2 1099 ? 131.304 133.382 91.865  1.00 48.94  ? 1096 HIS A N     1 
ATOM   8823  C CA    . HIS B 2 1099 ? 130.077 133.382 92.654  1.00 48.94  ? 1096 HIS A CA    1 
ATOM   8824  C C     . HIS B 2 1099 ? 129.883 134.708 93.378  1.00 48.94  ? 1096 HIS A C     1 
ATOM   8825  O O     . HIS B 2 1099 ? 128.763 135.227 93.451  1.00 48.94  ? 1096 HIS A O     1 
ATOM   8826  C CB    . HIS B 2 1099 ? 130.096 132.226 93.655  1.00 48.94  ? 1096 HIS A CB    1 
ATOM   8827  C CG    . HIS B 2 1099 ? 130.344 130.887 93.032  1.00 48.94  ? 1096 HIS A CG    1 
ATOM   8828  N ND1   . HIS B 2 1099 ? 130.686 129.776 93.773  1.00 48.94  ? 1096 HIS A ND1   1 
ATOM   8829  C CD2   . HIS B 2 1099 ? 130.290 130.477 91.743  1.00 48.94  ? 1096 HIS A CD2   1 
ATOM   8830  C CE1   . HIS B 2 1099 ? 130.839 128.741 92.966  1.00 48.94  ? 1096 HIS A CE1   1 
ATOM   8831  N NE2   . HIS B 2 1099 ? 130.604 129.140 91.728  1.00 48.94  ? 1096 HIS A NE2   1 
ATOM   8832  N N     . PHE B 2 1100 ? 130.964 135.267 93.927  1.00 48.55  ? 1097 PHE A N     1 
ATOM   8833  C CA    . PHE B 2 1100 ? 130.852 136.498 94.703  1.00 48.55  ? 1097 PHE A CA    1 
ATOM   8834  C C     . PHE B 2 1100 ? 130.374 137.656 93.842  1.00 48.55  ? 1097 PHE A C     1 
ATOM   8835  O O     . PHE B 2 1100 ? 129.539 138.459 94.275  1.00 48.55  ? 1097 PHE A O     1 
ATOM   8836  C CB    . PHE B 2 1100 ? 132.194 136.833 95.353  1.00 48.55  ? 1097 PHE A CB    1 
ATOM   8837  C CG    . PHE B 2 1100 ? 132.201 138.140 96.091  1.00 48.55  ? 1097 PHE A CG    1 
ATOM   8838  C CD1   . PHE B 2 1100 ? 131.193 138.452 96.988  1.00 48.55  ? 1097 PHE A CD1   1 
ATOM   8839  C CD2   . PHE B 2 1100 ? 133.215 139.059 95.887  1.00 48.55  ? 1097 PHE A CD2   1 
ATOM   8840  C CE1   . PHE B 2 1100 ? 131.199 139.654 97.667  1.00 48.55  ? 1097 PHE A CE1   1 
ATOM   8841  C CE2   . PHE B 2 1100 ? 133.225 140.263 96.563  1.00 48.55  ? 1097 PHE A CE2   1 
ATOM   8842  C CZ    . PHE B 2 1100 ? 132.216 140.560 97.454  1.00 48.55  ? 1097 PHE A CZ    1 
ATOM   8843  N N     . LEU B 2 1101 ? 130.895 137.766 92.620  1.00 48.55  ? 1098 LEU A N     1 
ATOM   8844  C CA    . LEU B 2 1101 ? 130.517 138.891 91.776  1.00 48.55  ? 1098 LEU A CA    1 
ATOM   8845  C C     . LEU B 2 1101 ? 129.221 138.619 91.026  1.00 48.55  ? 1098 LEU A C     1 
ATOM   8846  O O     . LEU B 2 1101 ? 128.634 139.542 90.451  1.00 48.55  ? 1098 LEU A O     1 
ATOM   8847  C CB    . LEU B 2 1101 ? 131.651 139.216 90.807  1.00 48.55  ? 1098 LEU A CB    1 
ATOM   8848  C CG    . LEU B 2 1101 ? 132.643 140.260 91.329  1.00 48.55  ? 1098 LEU A CG    1 
ATOM   8849  C CD1   . LEU B 2 1101 ? 133.535 140.764 90.213  1.00 48.55  ? 1098 LEU A CD1   1 
ATOM   8850  C CD2   . LEU B 2 1101 ? 131.928 141.415 92.019  1.00 48.55  ? 1098 LEU A CD2   1 
ATOM   8851  N N     . GLU B 2 1102 ? 128.759 137.367 91.019  1.00 48.55  ? 1099 GLU A N     1 
ATOM   8852  C CA    . GLU B 2 1102 ? 127.447 137.063 90.463  1.00 48.55  ? 1099 GLU A CA    1 
ATOM   8853  C C     . GLU B 2 1102 ? 126.318 137.461 91.403  1.00 48.55  ? 1099 GLU A C     1 
ATOM   8854  O O     . GLU B 2 1102 ? 125.220 137.777 90.933  1.00 48.55  ? 1099 GLU A O     1 
ATOM   8855  C CB    . GLU B 2 1102 ? 127.343 135.574 90.132  1.00 48.55  ? 1099 GLU A CB    1 
ATOM   8856  C CG    . GLU B 2 1102 ? 126.294 135.247 89.084  1.00 48.55  ? 1099 GLU A CG    1 
ATOM   8857  C CD    . GLU B 2 1102 ? 126.527 135.983 87.780  1.00 48.55  ? 1099 GLU A CD    1 
ATOM   8858  O OE1   . GLU B 2 1102 ? 127.530 135.684 87.100  1.00 48.55  ? 1099 GLU A OE1   1 
ATOM   8859  O OE2   . GLU B 2 1102 ? 125.706 136.859 87.434  1.00 48.55  ? 1099 GLU A OE2   1 
ATOM   8860  N N     . GLY B 2 1103 ? 126.563 137.451 92.715  1.00 48.55  ? 1100 GLY A N     1 
ATOM   8861  C CA    . GLY B 2 1103 ? 125.511 137.787 93.659  1.00 48.55  ? 1100 GLY A CA    1 
ATOM   8862  C C     . GLY B 2 1103 ? 125.062 139.231 93.552  1.00 48.55  ? 1100 GLY A C     1 
ATOM   8863  O O     . GLY B 2 1103 ? 123.881 139.538 93.728  1.00 48.55  ? 1100 GLY A O     1 
ATOM   8864  N N     . PHE B 2 1104 ? 125.996 140.136 93.271  1.00 48.55  ? 1101 PHE A N     1 
ATOM   8865  C CA    . PHE B 2 1104 ? 125.654 141.543 93.124  1.00 48.55  ? 1101 PHE A CA    1 
ATOM   8866  C C     . PHE B 2 1104 ? 124.717 141.740 91.938  1.00 48.55  ? 1101 PHE A C     1 
ATOM   8867  O O     . PHE B 2 1104 ? 124.819 141.058 90.915  1.00 48.55  ? 1101 PHE A O     1 
ATOM   8868  C CB    . PHE B 2 1104 ? 126.918 142.380 92.943  1.00 48.55  ? 1101 PHE A CB    1 
ATOM   8869  C CG    . PHE B 2 1104 ? 127.803 142.405 94.153  1.00 48.55  ? 1101 PHE A CG    1 
ATOM   8870  C CD1   . PHE B 2 1104 ? 127.430 143.108 95.284  1.00 48.55  ? 1101 PHE A CD1   1 
ATOM   8871  C CD2   . PHE B 2 1104 ? 129.006 141.724 94.160  1.00 48.55  ? 1101 PHE A CD2   1 
ATOM   8872  C CE1   . PHE B 2 1104 ? 128.242 143.132 96.400  1.00 48.55  ? 1101 PHE A CE1   1 
ATOM   8873  C CE2   . PHE B 2 1104 ? 129.822 141.744 95.271  1.00 48.55  ? 1101 PHE A CE2   1 
ATOM   8874  C CZ    . PHE B 2 1104 ? 129.440 142.449 96.393  1.00 48.55  ? 1101 PHE A CZ    1 
ATOM   8875  N N     . ASP B 2 1105 ? 123.790 142.687 92.085  1.00 48.55  ? 1102 ASP A N     1 
ATOM   8876  C CA    . ASP B 2 1105 ? 122.773 142.890 91.060  1.00 48.55  ? 1102 ASP A CA    1 
ATOM   8877  C C     . ASP B 2 1105 ? 123.345 143.614 89.846  1.00 48.55  ? 1102 ASP A C     1 
ATOM   8878  O O     . ASP B 2 1105 ? 123.367 143.068 88.737  1.00 48.55  ? 1102 ASP A O     1 
ATOM   8879  C CB    . ASP B 2 1105 ? 121.585 143.657 91.643  1.00 48.55  ? 1102 ASP A CB    1 
ATOM   8880  C CG    . ASP B 2 1105 ? 120.643 142.762 92.423  1.00 48.55  ? 1102 ASP A CG    1 
ATOM   8881  O OD1   . ASP B 2 1105 ? 121.102 141.723 92.942  1.00 48.55  ? 1102 ASP A OD1   1 
ATOM   8882  O OD2   . ASP B 2 1105 ? 119.443 143.095 92.515  1.00 48.55  ? 1102 ASP A OD2   1 
ATOM   8883  N N     . PHE B 2 1106 ? 123.817 144.845 90.033  1.00 48.55  ? 1103 PHE A N     1 
ATOM   8884  C CA    . PHE B 2 1106 ? 124.292 145.611 88.889  1.00 48.55  ? 1103 PHE A CA    1 
ATOM   8885  C C     . PHE B 2 1106 ? 125.280 146.677 89.338  1.00 48.55  ? 1103 PHE A C     1 
ATOM   8886  O O     . PHE B 2 1106 ? 125.154 147.245 90.427  1.00 48.55  ? 1103 PHE A O     1 
ATOM   8887  C CB    . PHE B 2 1106 ? 123.127 146.254 88.122  1.00 48.55  ? 1103 PHE A CB    1 
ATOM   8888  C CG    . PHE B 2 1106 ? 122.349 147.263 88.919  1.00 48.55  ? 1103 PHE A CG    1 
ATOM   8889  C CD1   . PHE B 2 1106 ? 121.259 146.869 89.677  1.00 48.55  ? 1103 PHE A CD1   1 
ATOM   8890  C CD2   . PHE B 2 1106 ? 122.696 148.603 88.902  1.00 48.55  ? 1103 PHE A CD2   1 
ATOM   8891  C CE1   . PHE B 2 1106 ? 120.533 147.791 90.406  1.00 48.55  ? 1103 PHE A CE1   1 
ATOM   8892  C CE2   . PHE B 2 1106 ? 121.977 149.529 89.633  1.00 48.55  ? 1103 PHE A CE2   1 
ATOM   8893  C CZ    . PHE B 2 1106 ? 120.894 149.122 90.386  1.00 48.55  ? 1103 PHE A CZ    1 
ATOM   8894  N N     . LEU B 2 1107 ? 126.259 146.937 88.474  1.00 48.55  ? 1104 LEU A N     1 
ATOM   8895  C CA    . LEU B 2 1107 ? 127.225 148.016 88.634  1.00 48.55  ? 1104 LEU A CA    1 
ATOM   8896  C C     . LEU B 2 1107 ? 127.223 148.857 87.369  1.00 48.55  ? 1104 LEU A C     1 
ATOM   8897  O O     . LEU B 2 1107 ? 127.364 148.321 86.265  1.00 48.55  ? 1104 LEU A O     1 
ATOM   8898  C CB    . LEU B 2 1107 ? 128.631 147.475 88.907  1.00 48.55  ? 1104 LEU A CB    1 
ATOM   8899  C CG    . LEU B 2 1107 ? 129.764 148.470 89.166  1.00 48.55  ? 1104 LEU A CG    1 
ATOM   8900  C CD1   . LEU B 2 1107 ? 129.564 149.233 90.460  1.00 48.55  ? 1104 LEU A CD1   1 
ATOM   8901  C CD2   . LEU B 2 1107 ? 131.098 147.741 89.181  1.00 48.55  ? 1104 LEU A CD2   1 
ATOM   8902  N N     . HIS B 2 1108 ? 127.067 150.167 87.529  1.00 48.55  ? 1105 HIS A N     1 
ATOM   8903  C CA    . HIS B 2 1108 ? 126.982 151.072 86.395  1.00 48.55  ? 1105 HIS A CA    1 
ATOM   8904  C C     . HIS B 2 1108 ? 127.645 152.395 86.742  1.00 48.55  ? 1105 HIS A C     1 
ATOM   8905  O O     . HIS B 2 1108 ? 127.741 152.775 87.911  1.00 48.55  ? 1105 HIS A O     1 
ATOM   8906  C CB    . HIS B 2 1108 ? 125.525 151.303 85.971  1.00 48.55  ? 1105 HIS A CB    1 
ATOM   8907  C CG    . HIS B 2 1108 ? 124.721 152.081 86.964  1.00 48.55  ? 1105 HIS A CG    1 
ATOM   8908  N ND1   . HIS B 2 1108 ? 124.350 153.392 86.756  1.00 48.55  ? 1105 HIS A ND1   1 
ATOM   8909  C CD2   . HIS B 2 1108 ? 124.215 151.735 88.171  1.00 48.55  ? 1105 HIS A CD2   1 
ATOM   8910  C CE1   . HIS B 2 1108 ? 123.653 153.820 87.792  1.00 48.55  ? 1105 HIS A CE1   1 
ATOM   8911  N NE2   . HIS B 2 1108 ? 123.555 152.834 88.665  1.00 48.55  ? 1105 HIS A NE2   1 
ATOM   8912  N N     . TYR B 2 1109 ? 128.098 153.094 85.705  1.00 51.13  ? 1106 TYR A N     1 
ATOM   8913  C CA    . TYR B 2 1109 ? 128.776 154.377 85.854  1.00 51.13  ? 1106 TYR A CA    1 
ATOM   8914  C C     . TYR B 2 1109 ? 127.755 155.495 85.697  1.00 51.13  ? 1106 TYR A C     1 
ATOM   8915  O O     . TYR B 2 1109 ? 127.308 155.786 84.583  1.00 51.13  ? 1106 TYR A O     1 
ATOM   8916  C CB    . TYR B 2 1109 ? 129.895 154.509 84.825  1.00 51.13  ? 1106 TYR A CB    1 
ATOM   8917  C CG    . TYR B 2 1109 ? 130.592 155.850 84.832  1.00 51.13  ? 1106 TYR A CG    1 
ATOM   8918  C CD1   . TYR B 2 1109 ? 131.536 156.159 85.799  1.00 51.13  ? 1106 TYR A CD1   1 
ATOM   8919  C CD2   . TYR B 2 1109 ? 130.308 156.804 83.865  1.00 51.13  ? 1106 TYR A CD2   1 
ATOM   8920  C CE1   . TYR B 2 1109 ? 132.177 157.381 85.806  1.00 51.13  ? 1106 TYR A CE1   1 
ATOM   8921  C CE2   . TYR B 2 1109 ? 130.943 158.029 83.864  1.00 51.13  ? 1106 TYR A CE2   1 
ATOM   8922  C CZ    . TYR B 2 1109 ? 131.877 158.313 84.836  1.00 51.13  ? 1106 TYR A CZ    1 
ATOM   8923  O OH    . TYR B 2 1109 ? 132.513 159.533 84.839  1.00 51.13  ? 1106 TYR A OH    1 
ATOM   8924  N N     . ASP B 2 1110 ? 127.387 156.123 86.810  1.00 58.35  ? 1107 ASP A N     1 
ATOM   8925  C CA    . ASP B 2 1110 ? 126.472 157.259 86.782  1.00 58.35  ? 1107 ASP A CA    1 
ATOM   8926  C C     . ASP B 2 1110 ? 127.205 158.448 86.172  1.00 58.35  ? 1107 ASP A C     1 
ATOM   8927  O O     . ASP B 2 1110 ? 128.072 159.048 86.815  1.00 58.35  ? 1107 ASP A O     1 
ATOM   8928  C CB    . ASP B 2 1110 ? 125.968 157.574 88.186  1.00 58.35  ? 1107 ASP A CB    1 
ATOM   8929  C CG    . ASP B 2 1110 ? 124.718 158.429 88.177  1.00 58.35  ? 1107 ASP A CG    1 
ATOM   8930  O OD1   . ASP B 2 1110 ? 123.991 158.408 87.161  1.00 58.35  ? 1107 ASP A OD1   1 
ATOM   8931  O OD2   . ASP B 2 1110 ? 124.460 159.119 89.185  1.00 58.35  ? 1107 ASP A OD2   1 
ATOM   8932  N N     . VAL B 2 1111 ? 126.860 158.787 84.929  1.00 58.98  ? 1108 VAL A N     1 
ATOM   8933  C CA    . VAL B 2 1111 ? 127.586 159.831 84.211  1.00 58.98  ? 1108 VAL A CA    1 
ATOM   8934  C C     . VAL B 2 1111 ? 127.366 161.191 84.861  1.00 58.98  ? 1108 VAL A C     1 
ATOM   8935  O O     . VAL B 2 1111 ? 128.277 162.027 84.900  1.00 58.98  ? 1108 VAL A O     1 
ATOM   8936  C CB    . VAL B 2 1111 ? 127.180 159.838 82.726  1.00 58.98  ? 1108 VAL A CB    1 
ATOM   8937  C CG1   . VAL B 2 1111 ? 127.809 158.660 82.003  1.00 58.98  ? 1108 VAL A CG1   1 
ATOM   8938  C CG2   . VAL B 2 1111 ? 125.665 159.800 82.587  1.00 58.98  ? 1108 VAL A CG2   1 
ATOM   8939  N N     . LYS B 2 1112 ? 126.158 161.440 85.373  1.00 61.79  ? 1109 LYS A N     1 
ATOM   8940  C CA    . LYS B 2 1112 ? 125.857 162.743 85.956  1.00 61.79  ? 1109 LYS A CA    1 
ATOM   8941  C C     . LYS B 2 1112 ? 126.677 162.998 87.216  1.00 61.79  ? 1109 LYS A C     1 
ATOM   8942  O O     . LYS B 2 1112 ? 127.141 164.122 87.442  1.00 61.79  ? 1109 LYS A O     1 
ATOM   8943  C CB    . LYS B 2 1112 ? 124.361 162.852 86.253  1.00 61.79  ? 1109 LYS A CB    1 
ATOM   8944  C CG    . LYS B 2 1112 ? 123.781 161.661 86.999  1.00 61.79  ? 1109 LYS A CG    1 
ATOM   8945  C CD    . LYS B 2 1112 ? 122.262 161.718 87.032  1.00 61.79  ? 1109 LYS A CD    1 
ATOM   8946  C CE    . LYS B 2 1112 ? 121.698 160.781 88.087  1.00 61.79  ? 1109 LYS A CE    1 
ATOM   8947  N NZ    . LYS B 2 1112 ? 121.530 161.464 89.400  1.00 61.79  ? 1109 LYS A NZ    1 
ATOM   8948  N N     . THR B 2 1113 ? 126.869 161.972 88.047  1.00 57.35  ? 1110 THR A N     1 
ATOM   8949  C CA    . THR B 2 1113 ? 127.601 162.120 89.297  1.00 57.35  ? 1110 THR A CA    1 
ATOM   8950  C C     . THR B 2 1113 ? 129.022 161.580 89.242  1.00 57.35  ? 1110 THR A C     1 
ATOM   8951  O O     . THR B 2 1113 ? 129.823 161.911 90.123  1.00 57.35  ? 1110 THR A O     1 
ATOM   8952  C CB    . THR B 2 1113 ? 126.847 161.427 90.443  1.00 57.35  ? 1110 THR A CB    1 
ATOM   8953  O OG1   . THR B 2 1113 ? 126.741 160.025 90.169  1.00 57.35  ? 1110 THR A OG1   1 
ATOM   8954  C CG2   . THR B 2 1113 ? 125.453 162.017 90.597  1.00 57.35  ? 1110 THR A CG2   1 
ATOM   8955  N N     . GLY B 2 1114 ? 129.359 160.766 88.244  1.00 50.21  ? 1111 GLY A N     1 
ATOM   8956  C CA    . GLY B 2 1114 ? 130.704 160.236 88.150  1.00 50.21  ? 1111 GLY A CA    1 
ATOM   8957  C C     . GLY B 2 1114 ? 131.052 159.195 89.187  1.00 50.21  ? 1111 GLY A C     1 
ATOM   8958  O O     . GLY B 2 1114 ? 132.234 158.998 89.478  1.00 50.21  ? 1111 GLY A O     1 
ATOM   8959  N N     . ASP B 2 1115 ? 130.057 158.521 89.757  1.00 48.87  ? 1112 ASP A N     1 
ATOM   8960  C CA    . ASP B 2 1115 ? 130.272 157.492 90.763  1.00 48.87  ? 1112 ASP A CA    1 
ATOM   8961  C C     . ASP B 2 1115 ? 129.649 156.184 90.302  1.00 48.87  ? 1112 ASP A C     1 
ATOM   8962  O O     . ASP B 2 1115 ? 128.486 156.153 89.889  1.00 48.87  ? 1112 ASP A O     1 
ATOM   8963  C CB    . ASP B 2 1115 ? 129.665 157.896 92.113  1.00 48.87  ? 1112 ASP A CB    1 
ATOM   8964  C CG    . ASP B 2 1115 ? 130.189 159.224 92.617  1.00 48.87  ? 1112 ASP A CG    1 
ATOM   8965  O OD1   . ASP B 2 1115 ? 131.304 159.613 92.219  1.00 48.87  ? 1112 ASP A OD1   1 
ATOM   8966  O OD2   . ASP B 2 1115 ? 129.484 159.879 93.413  1.00 48.87  ? 1112 ASP A OD2   1 
ATOM   8967  N N     . PHE B 2 1116 ? 130.423 155.105 90.374  1.00 48.55  ? 1113 PHE A N     1 
ATOM   8968  C CA    . PHE B 2 1116 ? 129.875 153.777 90.143  1.00 48.55  ? 1113 PHE A CA    1 
ATOM   8969  C C     . PHE B 2 1116 ? 128.970 153.395 91.305  1.00 48.55  ? 1113 PHE A C     1 
ATOM   8970  O O     . PHE B 2 1116 ? 129.232 153.756 92.454  1.00 48.55  ? 1113 PHE A O     1 
ATOM   8971  C CB    . PHE B 2 1116 ? 130.990 152.743 89.989  1.00 48.55  ? 1113 PHE A CB    1 
ATOM   8972  C CG    . PHE B 2 1116 ? 131.832 152.929 88.761  1.00 48.55  ? 1113 PHE A CG    1 
ATOM   8973  C CD1   . PHE B 2 1116 ? 132.805 153.912 88.714  1.00 48.55  ? 1113 PHE A CD1   1 
ATOM   8974  C CD2   . PHE B 2 1116 ? 131.653 152.118 87.655  1.00 48.55  ? 1113 PHE A CD2   1 
ATOM   8975  C CE1   . PHE B 2 1116 ? 133.583 154.081 87.588  1.00 48.55  ? 1113 PHE A CE1   1 
ATOM   8976  C CE2   . PHE B 2 1116 ? 132.428 152.284 86.525  1.00 48.55  ? 1113 PHE A CE2   1 
ATOM   8977  C CZ    . PHE B 2 1116 ? 133.394 153.267 86.492  1.00 48.55  ? 1113 PHE A CZ    1 
ATOM   8978  N N     . ILE B 2 1117 ? 127.897 152.671 91.002  1.00 48.55  ? 1114 ILE A N     1 
ATOM   8979  C CA    . ILE B 2 1117 ? 126.933 152.231 92.005  1.00 48.55  ? 1114 ILE A CA    1 
ATOM   8980  C C     . ILE B 2 1117 ? 126.800 150.720 91.900  1.00 48.55  ? 1114 ILE A C     1 
ATOM   8981  O O     . ILE B 2 1117 ? 126.457 150.196 90.834  1.00 48.55  ? 1114 ILE A O     1 
ATOM   8982  C CB    . ILE B 2 1117 ? 125.570 152.915 91.825  1.00 48.55  ? 1114 ILE A CB    1 
ATOM   8983  C CG1   . ILE B 2 1117 ? 125.701 154.426 92.023  1.00 48.55  ? 1114 ILE A CG1   1 
ATOM   8984  C CG2   . ILE B 2 1117 ? 124.552 152.336 92.794  1.00 48.55  ? 1114 ILE A CG2   1 
ATOM   8985  C CD1   . ILE B 2 1117 ? 124.470 155.204 91.613  1.00 48.55  ? 1114 ILE A CD1   1 
ATOM   8986  N N     . LEU B 2 1118 ? 127.054 150.025 93.005  1.00 48.55  ? 1115 LEU A N     1 
ATOM   8987  C CA    . LEU B 2 1118 ? 126.988 148.567 93.070  1.00 48.55  ? 1115 LEU A CA    1 
ATOM   8988  C C     . LEU B 2 1118 ? 125.833 148.192 93.993  1.00 48.55  ? 1115 LEU A C     1 
ATOM   8989  O O     . LEU B 2 1118 ? 125.946 148.284 95.218  1.00 48.55  ? 1115 LEU A O     1 
ATOM   8990  C CB    . LEU B 2 1118 ? 128.305 147.978 93.561  1.00 48.55  ? 1115 LEU A CB    1 
ATOM   8991  C CG    . LEU B 2 1118 ? 128.345 146.459 93.718  1.00 48.55  ? 1115 LEU A CG    1 
ATOM   8992  C CD1   . LEU B 2 1118 ? 128.438 145.780 92.361  1.00 48.55  ? 1115 LEU A CD1   1 
ATOM   8993  C CD2   . LEU B 2 1118 ? 129.498 146.046 94.614  1.00 48.55  ? 1115 LEU A CD2   1 
ATOM   8994  N N     . HIS B 2 1119 ? 124.721 147.769 93.400  1.00 48.55  ? 1116 HIS A N     1 
ATOM   8995  C CA    . HIS B 2 1119 ? 123.571 147.342 94.184  1.00 48.55  ? 1116 HIS A CA    1 
ATOM   8996  C C     . HIS B 2 1119 ? 123.799 145.940 94.732  1.00 48.55  ? 1116 HIS A C     1 
ATOM   8997  O O     . HIS B 2 1119 ? 124.214 145.036 94.002  1.00 48.55  ? 1116 HIS A O     1 
ATOM   8998  C CB    . HIS B 2 1119 ? 122.308 147.375 93.329  1.00 48.55  ? 1116 HIS A CB    1 
ATOM   8999  C CG    . HIS B 2 1119 ? 121.040 147.267 94.117  1.00 48.55  ? 1116 HIS A CG    1 
ATOM   9000  N ND1   . HIS B 2 1119 ? 120.174 148.326 94.280  1.00 48.55  ? 1116 HIS A ND1   1 
ATOM   9001  C CD2   . HIS B 2 1119 ? 120.490 146.225 94.782  1.00 48.55  ? 1116 HIS A CD2   1 
ATOM   9002  C CE1   . HIS B 2 1119 ? 119.146 147.941 95.015  1.00 48.55  ? 1116 HIS A CE1   1 
ATOM   9003  N NE2   . HIS B 2 1119 ? 119.313 146.670 95.333  1.00 48.55  ? 1116 HIS A NE2   1 
ATOM   9004  N N     . PHE B 2 1120 ? 123.528 145.761 96.021  1.00 48.55  ? 1117 PHE A N     1 
ATOM   9005  C CA    . PHE B 2 1120 ? 123.656 144.462 96.661  1.00 48.55  ? 1117 PHE A CA    1 
ATOM   9006  C C     . PHE B 2 1120 ? 122.424 144.200 97.511  1.00 48.55  ? 1117 PHE A C     1 
ATOM   9007  O O     . PHE B 2 1120 ? 121.876 145.112 98.135  1.00 48.55  ? 1117 PHE A O     1 
ATOM   9008  C CB    . PHE B 2 1120 ? 124.917 144.374 97.527  1.00 48.55  ? 1117 PHE A CB    1 
ATOM   9009  C CG    . PHE B 2 1120 ? 125.011 143.110 98.326  1.00 48.55  ? 1117 PHE A CG    1 
ATOM   9010  C CD1   . PHE B 2 1120 ? 125.065 141.881 97.693  1.00 48.55  ? 1117 PHE A CD1   1 
ATOM   9011  C CD2   . PHE B 2 1120 ? 125.037 143.147 99.708  1.00 48.55  ? 1117 PHE A CD2   1 
ATOM   9012  C CE1   . PHE B 2 1120 ? 125.150 140.714 98.422  1.00 48.55  ? 1117 PHE A CE1   1 
ATOM   9013  C CE2   . PHE B 2 1120 ? 125.121 141.982 100.444 1.00 48.55  ? 1117 PHE A CE2   1 
ATOM   9014  C CZ    . PHE B 2 1120 ? 125.176 140.764 99.799  1.00 48.55  ? 1117 PHE A CZ    1 
ATOM   9015  N N     . LYS B 2 1121 ? 121.996 142.942 97.530  1.00 48.55  ? 1118 LYS A N     1 
ATOM   9016  C CA    . LYS B 2 1121 ? 120.840 142.514 98.302  1.00 48.55  ? 1118 LYS A CA    1 
ATOM   9017  C C     . LYS B 2 1121 ? 121.290 141.559 99.397  1.00 48.55  ? 1118 LYS A C     1 
ATOM   9018  O O     . LYS B 2 1121 ? 122.072 140.637 99.146  1.00 48.55  ? 1118 LYS A O     1 
ATOM   9019  C CB    . LYS B 2 1121 ? 119.800 141.838 97.407  1.00 48.55  ? 1118 LYS A CB    1 
ATOM   9020  C CG    . LYS B 2 1121 ? 119.477 142.610 96.141  1.00 48.55  ? 1118 LYS A CG    1 
ATOM   9021  C CD    . LYS B 2 1121 ? 118.099 142.249 95.615  1.00 48.55  ? 1118 LYS A CD    1 
ATOM   9022  C CE    . LYS B 2 1121 ? 118.027 140.781 95.230  1.00 48.55  ? 1118 LYS A CE    1 
ATOM   9023  N NZ    . LYS B 2 1121 ? 118.934 140.460 94.093  1.00 48.55  ? 1118 LYS A NZ    1 
ATOM   9024  N N     . MET B 2 1122 ? 120.791 141.783 100.614 1.00 48.55  ? 1119 MET A N     1 
ATOM   9025  C CA    . MET B 2 1122 ? 121.217 140.972 101.748 1.00 48.55  ? 1119 MET A CA    1 
ATOM   9026  C C     . MET B 2 1122 ? 120.679 139.549 101.690 1.00 48.55  ? 1119 MET A C     1 
ATOM   9027  O O     . MET B 2 1122 ? 121.173 138.686 102.423 1.00 48.55  ? 1119 MET A O     1 
ATOM   9028  C CB    . MET B 2 1122 ? 120.797 141.636 103.059 1.00 48.55  ? 1119 MET A CB    1 
ATOM   9029  C CG    . MET B 2 1122 ? 121.580 142.894 103.389 1.00 48.55  ? 1119 MET A CG    1 
ATOM   9030  S SD    . MET B 2 1122 ? 123.317 142.538 103.713 1.00 48.55  ? 1119 MET A SD    1 
ATOM   9031  C CE    . MET B 2 1122 ? 123.695 143.770 104.954 1.00 48.55  ? 1119 MET A CE    1 
ATOM   9032  N N     . ASN B 2 1123 ? 119.686 139.280 100.843 1.00 48.55  ? 1120 ASN A N     1 
ATOM   9033  C CA    . ASN B 2 1123 ? 119.182 137.926 100.666 1.00 48.55  ? 1120 ASN A CA    1 
ATOM   9034  C C     . ASN B 2 1123 ? 119.955 137.145 99.609  1.00 48.55  ? 1120 ASN A C     1 
ATOM   9035  O O     . ASN B 2 1123 ? 119.422 136.180 99.048  1.00 48.55  ? 1120 ASN A O     1 
ATOM   9036  C CB    . ASN B 2 1123 ? 117.690 137.954 100.321 1.00 48.55  ? 1120 ASN A CB    1 
ATOM   9037  C CG    . ASN B 2 1123 ? 117.395 138.719 99.046  1.00 48.55  ? 1120 ASN A CG    1 
ATOM   9038  O OD1   . ASN B 2 1123 ? 118.297 139.245 98.397  1.00 48.55  ? 1120 ASN A OD1   1 
ATOM   9039  N ND2   . ASN B 2 1123 ? 116.121 138.784 98.680  1.00 48.55  ? 1120 ASN A ND2   1 
ATOM   9040  N N     . ARG B 2 1124 ? 121.192 137.547 99.329  1.00 48.55  ? 1121 ARG A N     1 
ATOM   9041  C CA    . ARG B 2 1124 ? 122.043 136.869 98.365  1.00 48.55  ? 1121 ARG A CA    1 
ATOM   9042  C C     . ARG B 2 1124 ? 123.443 136.746 98.946  1.00 48.55  ? 1121 ARG A C     1 
ATOM   9043  O O     . ARG B 2 1124 ? 123.810 137.454 99.886  1.00 48.55  ? 1121 ARG A O     1 
ATOM   9044  C CB    . ARG B 2 1124 ? 122.084 137.612 97.024  1.00 48.55  ? 1121 ARG A CB    1 
ATOM   9045  C CG    . ARG B 2 1124 ? 120.844 137.420 96.172  1.00 48.55  ? 1121 ARG A CG    1 
ATOM   9046  C CD    . ARG B 2 1124 ? 120.763 136.000 95.632  1.00 48.55  ? 1121 ARG A CD    1 
ATOM   9047  N NE    . ARG B 2 1124 ? 121.605 135.797 94.458  1.00 48.55  ? 1121 ARG A NE    1 
ATOM   9048  C CZ    . ARG B 2 1124 ? 121.428 136.390 93.284  1.00 48.55  ? 1121 ARG A CZ    1 
ATOM   9049  N NH1   . ARG B 2 1124 ? 120.415 137.214 93.068  1.00 48.55  ? 1121 ARG A NH1   1 
ATOM   9050  N NH2   . ARG B 2 1124 ? 122.283 136.140 92.297  1.00 48.55  ? 1121 ARG A NH2   1 
ATOM   9051  N N     . ASN B 2 1125 ? 124.224 135.831 98.368  1.00 48.55  ? 1122 ASN A N     1 
ATOM   9052  C CA    . ASN B 2 1125 ? 125.591 135.560 98.815  1.00 48.55  ? 1122 ASN A CA    1 
ATOM   9053  C C     . ASN B 2 1125 ? 125.627 135.188 100.295 1.00 48.55  ? 1122 ASN A C     1 
ATOM   9054  O O     . ASN B 2 1125 ? 126.505 135.625 101.042 1.00 48.55  ? 1122 ASN A O     1 
ATOM   9055  C CB    . ASN B 2 1125 ? 126.513 136.748 98.531  1.00 48.55  ? 1122 ASN A CB    1 
ATOM   9056  C CG    . ASN B 2 1125 ? 126.894 136.854 97.071  1.00 48.55  ? 1122 ASN A CG    1 
ATOM   9057  O OD1   . ASN B 2 1125 ? 126.891 135.861 96.343  1.00 48.55  ? 1122 ASN A OD1   1 
ATOM   9058  N ND2   . ASN B 2 1125 ? 127.226 138.062 96.632  1.00 48.55  ? 1122 ASN A ND2   1 
ATOM   9059  N N     . LEU B 2 1126 ? 124.663 134.367 100.722 1.00 48.55  ? 1123 LEU A N     1 
ATOM   9060  C CA    . LEU B 2 1126 ? 124.557 134.013 102.134 1.00 48.55  ? 1123 LEU A CA    1 
ATOM   9061  C C     . LEU B 2 1126 ? 125.781 133.251 102.624 1.00 48.55  ? 1123 LEU A C     1 
ATOM   9062  O O     . LEU B 2 1126 ? 126.143 133.352 103.801 1.00 48.55  ? 1123 LEU A O     1 
ATOM   9063  C CB    . LEU B 2 1126 ? 123.294 133.185 102.382 1.00 48.55  ? 1123 LEU A CB    1 
ATOM   9064  C CG    . LEU B 2 1126 ? 121.936 133.893 102.444 1.00 48.55  ? 1123 LEU A CG    1 
ATOM   9065  C CD1   . LEU B 2 1126 ? 121.486 134.378 101.074 1.00 48.55  ? 1123 LEU A CD1   1 
ATOM   9066  C CD2   . LEU B 2 1126 ? 120.887 132.981 103.063 1.00 48.55  ? 1123 LEU A CD2   1 
ATOM   9067  N N     . SER B 2 1127 ? 126.427 132.484 101.745 1.00 48.55  ? 1124 SER A N     1 
ATOM   9068  C CA    . SER B 2 1127 ? 127.600 131.720 102.158 1.00 48.55  ? 1124 SER A CA    1 
ATOM   9069  C C     . SER B 2 1127 ? 128.797 132.630 102.406 1.00 48.55  ? 1124 SER A C     1 
ATOM   9070  O O     . SER B 2 1127 ? 129.715 132.268 103.151 1.00 48.55  ? 1124 SER A O     1 
ATOM   9071  C CB    . SER B 2 1127 ? 127.934 130.664 101.104 1.00 48.55  ? 1124 SER A CB    1 
ATOM   9072  O OG    . SER B 2 1127 ? 128.128 131.257 99.833  1.00 48.55  ? 1124 SER A OG    1 
ATOM   9073  N N     . PHE B 2 1128 ? 128.807 133.813 101.790 1.00 48.55  ? 1125 PHE A N     1 
ATOM   9074  C CA    . PHE B 2 1128 ? 129.922 134.739 101.944 1.00 48.55  ? 1125 PHE A CA    1 
ATOM   9075  C C     . PHE B 2 1128 ? 129.667 135.803 103.004 1.00 48.55  ? 1125 PHE A C     1 
ATOM   9076  O O     . PHE B 2 1128 ? 130.599 136.526 103.370 1.00 48.55  ? 1125 PHE A O     1 
ATOM   9077  C CB    . PHE B 2 1128 ? 130.249 135.411 100.605 1.00 48.55  ? 1125 PHE A CB    1 
ATOM   9078  C CG    . PHE B 2 1128 ? 130.492 134.446 99.467  1.00 48.55  ? 1125 PHE A CG    1 
ATOM   9079  C CD1   . PHE B 2 1128 ? 130.694 133.094 99.697  1.00 48.55  ? 1125 PHE A CD1   1 
ATOM   9080  C CD2   . PHE B 2 1128 ? 130.504 134.899 98.160  1.00 48.55  ? 1125 PHE A CD2   1 
ATOM   9081  C CE1   . PHE B 2 1128 ? 130.913 132.219 98.651  1.00 48.55  ? 1125 PHE A CE1   1 
ATOM   9082  C CE2   . PHE B 2 1128 ? 130.720 134.026 97.110  1.00 48.55  ? 1125 PHE A CE2   1 
ATOM   9083  C CZ    . PHE B 2 1128 ? 130.925 132.686 97.356  1.00 48.55  ? 1125 PHE A CZ    1 
ATOM   9084  N N     . GLN B 2 1129 ? 128.440 135.915 103.506 1.00 48.55  ? 1126 GLN A N     1 
ATOM   9085  C CA    . GLN B 2 1129 ? 128.147 136.867 104.564 1.00 48.55  ? 1126 GLN A CA    1 
ATOM   9086  C C     . GLN B 2 1129 ? 128.672 136.359 105.905 1.00 48.55  ? 1126 GLN A C     1 
ATOM   9087  O O     . GLN B 2 1129 ? 129.313 135.308 106.002 1.00 48.55  ? 1126 GLN A O     1 
ATOM   9088  C CB    . GLN B 2 1129 ? 126.645 137.128 104.658 1.00 48.55  ? 1126 GLN A CB    1 
ATOM   9089  C CG    . GLN B 2 1129 ? 126.016 137.668 103.392 1.00 48.55  ? 1126 GLN A CG    1 
ATOM   9090  C CD    . GLN B 2 1129 ? 124.991 138.745 103.674 1.00 48.55  ? 1126 GLN A CD    1 
ATOM   9091  O OE1   . GLN B 2 1129 ? 124.222 138.650 104.630 1.00 48.55  ? 1126 GLN A OE1   1 
ATOM   9092  N NE2   . GLN B 2 1129 ? 124.973 139.777 102.841 1.00 48.55  ? 1126 GLN A NE2   1 
ATOM   9093  N N     . ARG B 2 1130 ? 128.389 137.127 106.955 1.00 48.55  ? 1127 ARG A N     1 
ATOM   9094  C CA    . ARG B 2 1130 ? 128.784 136.773 108.310 1.00 48.55  ? 1127 ARG A CA    1 
ATOM   9095  C C     . ARG B 2 1130 ? 127.614 136.305 109.165 1.00 48.55  ? 1127 ARG A C     1 
ATOM   9096  O O     . ARG B 2 1130 ? 127.775 136.146 110.379 1.00 48.55  ? 1127 ARG A O     1 
ATOM   9097  C CB    . ARG B 2 1130 ? 129.478 137.959 108.984 1.00 48.55  ? 1127 ARG A CB    1 
ATOM   9098  C CG    . ARG B 2 1130 ? 128.679 139.249 108.951 1.00 48.55  ? 1127 ARG A CG    1 
ATOM   9099  C CD    . ARG B 2 1130 ? 129.364 140.357 109.741 1.00 48.55  ? 1127 ARG A CD    1 
ATOM   9100  N NE    . ARG B 2 1130 ? 130.535 140.890 109.055 1.00 48.55  ? 1127 ARG A NE    1 
ATOM   9101  C CZ    . ARG B 2 1130 ? 131.781 140.490 109.270 1.00 48.55  ? 1127 ARG A CZ    1 
ATOM   9102  N NH1   . ARG B 2 1130 ? 132.064 139.556 110.163 1.00 48.55  ? 1127 ARG A NH1   1 
ATOM   9103  N NH2   . ARG B 2 1130 ? 132.770 141.045 108.575 1.00 48.55  ? 1127 ARG A NH2   1 
ATOM   9104  N N     . GLY B 2 1131 ? 126.447 136.081 108.566 1.00 48.55  ? 1128 GLY A N     1 
ATOM   9105  C CA    . GLY B 2 1131 ? 125.299 135.617 109.317 1.00 48.55  ? 1128 GLY A CA    1 
ATOM   9106  C C     . GLY B 2 1131 ? 124.570 136.679 110.105 1.00 48.55  ? 1128 GLY A C     1 
ATOM   9107  O O     . GLY B 2 1131 ? 123.792 136.342 111.002 1.00 48.55  ? 1128 GLY A O     1 
ATOM   9108  N N     . LEU B 2 1132 ? 124.794 137.956 109.801 1.00 48.55  ? 1129 LEU A N     1 
ATOM   9109  C CA    . LEU B 2 1132 ? 124.137 139.068 110.487 1.00 48.55  ? 1129 LEU A CA    1 
ATOM   9110  C C     . LEU B 2 1132 ? 123.451 139.937 109.444 1.00 48.55  ? 1129 LEU A C     1 
ATOM   9111  O O     . LEU B 2 1132 ? 124.039 140.900 108.934 1.00 48.55  ? 1129 LEU A O     1 
ATOM   9112  C CB    . LEU B 2 1132 ? 125.136 139.875 111.317 1.00 48.55  ? 1129 LEU A CB    1 
ATOM   9113  C CG    . LEU B 2 1132 ? 125.764 139.140 112.501 1.00 48.55  ? 1129 LEU A CG    1 
ATOM   9114  C CD1   . LEU B 2 1132 ? 126.834 139.995 113.157 1.00 48.55  ? 1129 LEU A CD1   1 
ATOM   9115  C CD2   . LEU B 2 1132 ? 124.699 138.739 113.511 1.00 48.55  ? 1129 LEU A CD2   1 
ATOM   9116  N N     . PRO B 2 1133 ? 122.202 139.622 109.097 1.00 48.55  ? 1130 PRO A N     1 
ATOM   9117  C CA    . PRO B 2 1133 ? 121.504 140.396 108.062 1.00 48.55  ? 1130 PRO A CA    1 
ATOM   9118  C C     . PRO B 2 1133 ? 121.181 141.819 108.492 1.00 48.55  ? 1130 PRO A C     1 
ATOM   9119  O O     . PRO B 2 1133 ? 121.505 142.776 107.782 1.00 48.55  ? 1130 PRO A O     1 
ATOM   9120  C CB    . PRO B 2 1133 ? 120.227 139.581 107.821 1.00 48.55  ? 1130 PRO A CB    1 
ATOM   9121  C CG    . PRO B 2 1133 ? 119.999 138.858 109.106 1.00 48.55  ? 1130 PRO A CG    1 
ATOM   9122  C CD    . PRO B 2 1133 ? 121.364 138.542 109.646 1.00 48.55  ? 1130 PRO A CD    1 
ATOM   9123  N N     . GLY B 2 1134 ? 120.549 141.969 109.653 1.00 48.55  ? 1131 GLY A N     1 
ATOM   9124  C CA    . GLY B 2 1134 ? 120.149 143.287 110.098 1.00 48.55  ? 1131 GLY A CA    1 
ATOM   9125  C C     . GLY B 2 1134 ? 118.975 143.825 109.295 1.00 48.55  ? 1131 GLY A C     1 
ATOM   9126  O O     . GLY B 2 1134 ? 118.265 143.094 108.600 1.00 48.55  ? 1131 GLY A O     1 
ATOM   9127  N N     . PHE B 2 1135 ? 118.773 145.133 109.401 1.00 48.55  ? 1132 PHE A N     1 
ATOM   9128  C CA    . PHE B 2 1135 ? 117.733 145.837 108.668 1.00 48.55  ? 1132 PHE A CA    1 
ATOM   9129  C C     . PHE B 2 1135 ? 118.296 146.180 107.285 1.00 48.55  ? 1132 PHE A C     1 
ATOM   9130  O O     . PHE B 2 1135 ? 119.358 145.685 106.897 1.00 48.55  ? 1132 PHE A O     1 
ATOM   9131  C CB    . PHE B 2 1135 ? 117.272 147.035 109.506 1.00 48.55  ? 1132 PHE A CB    1 
ATOM   9132  C CG    . PHE B 2 1135 ? 116.157 147.838 108.896 1.00 48.55  ? 1132 PHE A CG    1 
ATOM   9133  C CD1   . PHE B 2 1135 ? 114.858 147.360 108.909 1.00 48.55  ? 1132 PHE A CD1   1 
ATOM   9134  C CD2   . PHE B 2 1135 ? 116.398 149.093 108.362 1.00 48.55  ? 1132 PHE A CD2   1 
ATOM   9135  C CE1   . PHE B 2 1135 ? 113.828 148.099 108.362 1.00 48.55  ? 1132 PHE A CE1   1 
ATOM   9136  C CE2   . PHE B 2 1135 ? 115.371 149.837 107.814 1.00 48.55  ? 1132 PHE A CE2   1 
ATOM   9137  C CZ    . PHE B 2 1135 ? 114.084 149.340 107.816 1.00 48.55  ? 1132 PHE A CZ    1 
ATOM   9138  N N     . MET B 2 1136 ? 117.592 147.018 106.515 1.00 48.55  ? 1133 MET A N     1 
ATOM   9139  C CA    . MET B 2 1136 ? 118.053 147.461 105.202 1.00 48.55  ? 1133 MET A CA    1 
ATOM   9140  C C     . MET B 2 1136 ? 118.255 146.281 104.259 1.00 48.55  ? 1133 MET A C     1 
ATOM   9141  O O     . MET B 2 1136 ? 119.398 145.882 104.000 1.00 48.55  ? 1133 MET A O     1 
ATOM   9142  C CB    . MET B 2 1136 ? 119.345 148.270 105.321 1.00 48.55  ? 1133 MET A CB    1 
ATOM   9143  C CG    . MET B 2 1136 ? 119.167 149.641 105.943 1.00 48.55  ? 1133 MET A CG    1 
ATOM   9144  S SD    . MET B 2 1136 ? 118.146 150.723 104.929 1.00 48.55  ? 1133 MET A SD    1 
ATOM   9145  C CE    . MET B 2 1136 ? 118.121 152.200 105.939 1.00 48.55  ? 1133 MET A CE    1 
ATOM   9146  N N     . PRO B 2 1137 ? 117.173 145.687 103.747 1.00 48.55  ? 1134 PRO A N     1 
ATOM   9147  C CA    . PRO B 2 1137 ? 117.319 144.483 102.910 1.00 48.55  ? 1134 PRO A CA    1 
ATOM   9148  C C     . PRO B 2 1137 ? 118.195 144.680 101.685 1.00 48.55  ? 1134 PRO A C     1 
ATOM   9149  O O     . PRO B 2 1137 ? 118.767 143.703 101.186 1.00 48.55  ? 1134 PRO A O     1 
ATOM   9150  C CB    . PRO B 2 1137 ? 115.871 144.159 102.515 1.00 48.55  ? 1134 PRO A CB    1 
ATOM   9151  C CG    . PRO B 2 1137 ? 115.136 145.452 102.665 1.00 48.55  ? 1134 PRO A CG    1 
ATOM   9152  C CD    . PRO B 2 1137 ? 115.776 146.141 103.827 1.00 48.55  ? 1134 PRO A CD    1 
ATOM   9153  N N     . ALA B 2 1138 ? 118.320 145.905 101.179 1.00 48.55  ? 1135 ALA A N     1 
ATOM   9154  C CA    . ALA B 2 1138 ? 119.141 146.180 100.009 1.00 48.55  ? 1135 ALA A CA    1 
ATOM   9155  C C     . ALA B 2 1138 ? 120.071 147.350 100.290 1.00 48.55  ? 1135 ALA A C     1 
ATOM   9156  O O     . ALA B 2 1138 ? 119.708 148.285 101.011 1.00 48.55  ? 1135 ALA A O     1 
ATOM   9157  C CB    . ALA B 2 1138 ? 118.277 146.484 98.780  1.00 48.55  ? 1135 ALA A CB    1 
ATOM   9158  N N     . TRP B 2 1139 ? 121.267 147.294 99.712  1.00 48.55  ? 1136 TRP A N     1 
ATOM   9159  C CA    . TRP B 2 1139 ? 122.276 148.330 99.859  1.00 48.55  ? 1136 TRP A CA    1 
ATOM   9160  C C     . TRP B 2 1139 ? 122.725 148.816 98.488  1.00 48.55  ? 1136 TRP A C     1 
ATOM   9161  O O     . TRP B 2 1139 ? 122.511 148.154 97.469  1.00 48.55  ? 1136 TRP A O     1 
ATOM   9162  C CB    . TRP B 2 1139 ? 123.489 147.821 100.648 1.00 48.55  ? 1136 TRP A CB    1 
ATOM   9163  C CG    . TRP B 2 1139 ? 123.268 147.731 102.124 1.00 48.55  ? 1136 TRP A CG    1 
ATOM   9164  C CD1   . TRP B 2 1139 ? 123.245 146.599 102.879 1.00 48.55  ? 1136 TRP A CD1   1 
ATOM   9165  C CD2   . TRP B 2 1139 ? 123.055 148.822 103.027 1.00 48.55  ? 1136 TRP A CD2   1 
ATOM   9166  N NE1   . TRP B 2 1139 ? 123.022 146.915 104.197 1.00 48.55  ? 1136 TRP A NE1   1 
ATOM   9167  C CE2   . TRP B 2 1139 ? 122.901 148.274 104.313 1.00 48.55  ? 1136 TRP A CE2   1 
ATOM   9168  C CE3   . TRP B 2 1139 ? 122.973 150.207 102.872 1.00 48.55  ? 1136 TRP A CE3   1 
ATOM   9169  C CZ2   . TRP B 2 1139 ? 122.677 149.062 105.437 1.00 48.55  ? 1136 TRP A CZ2   1 
ATOM   9170  C CZ3   . TRP B 2 1139 ? 122.747 150.988 103.988 1.00 48.55  ? 1136 TRP A CZ3   1 
ATOM   9171  C CH2   . TRP B 2 1139 ? 122.601 150.414 105.253 1.00 48.55  ? 1136 TRP A CH2   1 
ATOM   9172  N N     . ASP B 2 1140 ? 123.360 149.988 98.474  1.00 48.55  ? 1137 ASP A N     1 
ATOM   9173  C CA    . ASP B 2 1140 ? 123.898 150.591 97.254  1.00 48.55  ? 1137 ASP A CA    1 
ATOM   9174  C C     . ASP B 2 1140 ? 125.343 151.001 97.522  1.00 48.55  ? 1137 ASP A C     1 
ATOM   9175  O O     . ASP B 2 1140 ? 125.613 152.149 97.882  1.00 48.55  ? 1137 ASP A O     1 
ATOM   9176  C CB    . ASP B 2 1140 ? 123.052 151.779 96.809  1.00 48.55  ? 1137 ASP A CB    1 
ATOM   9177  C CG    . ASP B 2 1140 ? 121.680 151.366 96.314  1.00 48.55  ? 1137 ASP A CG    1 
ATOM   9178  O OD1   . ASP B 2 1140 ? 121.548 150.239 95.793  1.00 48.55  ? 1137 ASP A OD1   1 
ATOM   9179  O OD2   . ASP B 2 1140 ? 120.733 152.170 96.445  1.00 48.55  ? 1137 ASP A OD2   1 
ATOM   9180  N N     . ILE B 2 1141 ? 126.273 150.064 97.334  1.00 48.55  ? 1138 ILE A N     1 
ATOM   9181  C CA    . ILE B 2 1141 ? 127.688 150.377 97.485  1.00 48.55  ? 1138 ILE A CA    1 
ATOM   9182  C C     . ILE B 2 1141 ? 128.142 151.195 96.286  1.00 48.55  ? 1138 ILE A C     1 
ATOM   9183  O O     . ILE B 2 1141 ? 127.919 150.810 95.132  1.00 48.55  ? 1138 ILE A O     1 
ATOM   9184  C CB    . ILE B 2 1141 ? 128.513 149.091 97.633  1.00 48.55  ? 1138 ILE A CB    1 
ATOM   9185  C CG1   . ILE B 2 1141 ? 127.846 148.147 98.633  1.00 48.55  ? 1138 ILE A CG1   1 
ATOM   9186  C CG2   . ILE B 2 1141 ? 129.928 149.417 98.071  1.00 48.55  ? 1138 ILE A CG2   1 
ATOM   9187  C CD1   . ILE B 2 1141 ? 128.622 146.876 98.885  1.00 48.55  ? 1138 ILE A CD1   1 
ATOM   9188  N N     . VAL B 2 1142 ? 128.780 152.331 96.550  1.00 48.55  ? 1139 VAL A N     1 
ATOM   9189  C CA    . VAL B 2 1142 ? 129.086 153.313 95.518  1.00 48.55  ? 1139 VAL A CA    1 
ATOM   9190  C C     . VAL B 2 1142 ? 130.590 153.537 95.459  1.00 48.55  ? 1139 VAL A C     1 
ATOM   9191  O O     . VAL B 2 1142 ? 131.266 153.557 96.495  1.00 48.55  ? 1139 VAL A O     1 
ATOM   9192  C CB    . VAL B 2 1142 ? 128.339 154.638 95.758  1.00 48.55  ? 1139 VAL A CB    1 
ATOM   9193  C CG1   . VAL B 2 1142 ? 126.837 154.413 95.704  1.00 48.55  ? 1139 VAL A CG1   1 
ATOM   9194  C CG2   . VAL B 2 1142 ? 128.729 155.227 97.091  1.00 48.55  ? 1139 VAL A CG2   1 
ATOM   9195  N N     . PHE B 2 1143 ? 131.113 153.681 94.240  1.00 48.55  ? 1140 PHE A N     1 
ATOM   9196  C CA    . PHE B 2 1143 ? 132.519 154.017 94.015  1.00 48.55  ? 1140 PHE A CA    1 
ATOM   9197  C C     . PHE B 2 1143 ? 132.602 155.523 93.785  1.00 48.55  ? 1140 PHE A C     1 
ATOM   9198  O O     . PHE B 2 1143 ? 132.653 156.015 92.656  1.00 48.55  ? 1140 PHE A O     1 
ATOM   9199  C CB    . PHE B 2 1143 ? 133.086 153.236 92.835  1.00 48.55  ? 1140 PHE A CB    1 
ATOM   9200  C CG    . PHE B 2 1143 ? 133.379 151.790 93.130  1.00 48.55  ? 1140 PHE A CG    1 
ATOM   9201  C CD1   . PHE B 2 1143 ? 132.537 151.038 93.929  1.00 48.55  ? 1140 PHE A CD1   1 
ATOM   9202  C CD2   . PHE B 2 1143 ? 134.499 151.181 92.594  1.00 48.55  ? 1140 PHE A CD2   1 
ATOM   9203  C CE1   . PHE B 2 1143 ? 132.810 149.711 94.191  1.00 48.55  ? 1140 PHE A CE1   1 
ATOM   9204  C CE2   . PHE B 2 1143 ? 134.776 149.856 92.854  1.00 48.55  ? 1140 PHE A CE2   1 
ATOM   9205  C CZ    . PHE B 2 1143 ? 133.931 149.122 93.652  1.00 48.55  ? 1140 PHE A CZ    1 
ATOM   9206  N N     . GLU B 2 1144 ? 132.607 156.263 94.889  1.00 48.55  ? 1141 GLU A N     1 
ATOM   9207  C CA    . GLU B 2 1144 ? 132.555 157.716 94.830  1.00 48.55  ? 1141 GLU A CA    1 
ATOM   9208  C C     . GLU B 2 1144 ? 133.800 158.288 94.155  1.00 48.55  ? 1141 GLU A C     1 
ATOM   9209  O O     . GLU B 2 1144 ? 134.914 157.780 94.313  1.00 48.55  ? 1141 GLU A O     1 
ATOM   9210  C CB    . GLU B 2 1144 ? 132.368 158.283 96.239  1.00 48.55  ? 1141 GLU A CB    1 
ATOM   9211  C CG    . GLU B 2 1144 ? 133.574 158.159 97.153  1.00 48.55  ? 1141 GLU A CG    1 
ATOM   9212  C CD    . GLU B 2 1144 ? 133.572 159.194 98.259  1.00 48.55  ? 1141 GLU A CD    1 
ATOM   9213  O OE1   . GLU B 2 1144 ? 132.531 159.338 98.936  1.00 48.55  ? 1141 GLU A OE1   1 
ATOM   9214  O OE2   . GLU B 2 1144 ? 134.612 159.847 98.469  1.00 48.55  ? 1141 GLU A OE2   1 
ATOM   9215  N N     . LYS B 2 1145 ? 133.590 159.350 93.379  1.00 48.55  ? 1142 LYS A N     1 
ATOM   9216  C CA    . LYS B 2 1145 ? 134.635 159.897 92.525  1.00 48.55  ? 1142 LYS A CA    1 
ATOM   9217  C C     . LYS B 2 1145 ? 135.758 160.512 93.351  1.00 48.55  ? 1142 LYS A C     1 
ATOM   9218  O O     . LYS B 2 1145 ? 135.534 161.103 94.410  1.00 48.55  ? 1142 LYS A O     1 
ATOM   9219  C CB    . LYS B 2 1145 ? 134.051 160.945 91.574  1.00 48.55  ? 1142 LYS A CB    1 
ATOM   9220  C CG    . LYS B 2 1145 ? 135.063 161.585 90.634  1.00 48.55  ? 1142 LYS A CG    1 
ATOM   9221  C CD    . LYS B 2 1145 ? 134.525 161.676 89.215  1.00 48.55  ? 1142 LYS A CD    1 
ATOM   9222  C CE    . LYS B 2 1145 ? 133.312 162.588 89.139  1.00 48.55  ? 1142 LYS A CE    1 
ATOM   9223  N NZ    . LYS B 2 1145 ? 133.629 163.975 89.575  1.00 48.55  ? 1142 LYS A NZ    1 
ATOM   9224  N N     . ASN B 2 1146 ? 136.985 160.369 92.846  1.00 48.55  ? 1143 ASN A N     1 
ATOM   9225  C CA    . ASN B 2 1146 ? 138.177 160.887 93.514  1.00 48.55  ? 1143 ASN A CA    1 
ATOM   9226  C C     . ASN B 2 1146 ? 138.308 162.388 93.245  1.00 48.55  ? 1143 ASN A C     1 
ATOM   9227  O O     . ASN B 2 1146 ? 139.219 162.864 92.565  1.00 48.55  ? 1143 ASN A O     1 
ATOM   9228  C CB    . ASN B 2 1146 ? 139.412 160.124 93.056  1.00 48.55  ? 1143 ASN A CB    1 
ATOM   9229  C CG    . ASN B 2 1146 ? 139.280 158.630 93.263  1.00 48.55  ? 1143 ASN A CG    1 
ATOM   9230  O OD1   . ASN B 2 1146 ? 139.548 157.840 92.358  1.00 48.55  ? 1143 ASN A OD1   1 
ATOM   9231  N ND2   . ASN B 2 1146 ? 138.862 158.233 94.458  1.00 48.55  ? 1143 ASN A ND2   1 
ATOM   9232  N N     . GLU B 2 1147 ? 137.363 163.139 93.803  1.00 48.55  ? 1144 GLU A N     1 
ATOM   9233  C CA    . GLU B 2 1147 ? 137.372 164.591 93.706  1.00 48.55  ? 1144 GLU A CA    1 
ATOM   9234  C C     . GLU B 2 1147 ? 138.150 165.189 94.869  1.00 48.55  ? 1144 GLU A C     1 
ATOM   9235  O O     . GLU B 2 1147 ? 138.287 164.567 95.926  1.00 48.55  ? 1144 GLU A O     1 
ATOM   9236  C CB    . GLU B 2 1147 ? 135.946 165.145 93.695  1.00 48.55  ? 1144 GLU A CB    1 
ATOM   9237  C CG    . GLU B 2 1147 ? 135.123 164.735 92.487  1.00 48.55  ? 1144 GLU A CG    1 
ATOM   9238  C CD    . GLU B 2 1147 ? 133.698 165.249 92.552  1.00 48.55  ? 1144 GLU A CD    1 
ATOM   9239  O OE1   . GLU B 2 1147 ? 133.338 165.879 93.569  1.00 48.55  ? 1144 GLU A OE1   1 
ATOM   9240  O OE2   . GLU B 2 1147 ? 132.937 165.023 91.588  1.00 48.55  ? 1144 GLU A OE2   1 
ATOM   9241  N N     . THR B 2 1148 ? 138.661 166.404 94.666  1.00 48.55  ? 1145 THR A N     1 
ATOM   9242  C CA    . THR B 2 1148 ? 139.406 167.116 95.704  1.00 48.55  ? 1145 THR A CA    1 
ATOM   9243  C C     . THR B 2 1148 ? 138.413 167.903 96.555  1.00 48.55  ? 1145 THR A C     1 
ATOM   9244  O O     . THR B 2 1148 ? 138.116 169.075 96.312  1.00 48.55  ? 1145 THR A O     1 
ATOM   9245  C CB    . THR B 2 1148 ? 140.464 168.021 95.087  1.00 48.55  ? 1145 THR A CB    1 
ATOM   9246  O OG1   . THR B 2 1148 ? 141.304 167.252 94.219  1.00 48.55  ? 1145 THR A OG1   1 
ATOM   9247  C CG2   . THR B 2 1148 ? 141.320 168.656 96.173  1.00 48.55  ? 1145 THR A CG2   1 
ATOM   9248  N N     . GLN B 2 1149 ? 137.885 167.231 97.574  1.00 48.55  ? 1146 GLN A N     1 
ATOM   9249  C CA    . GLN B 2 1149 ? 136.928 167.858 98.470  1.00 48.55  ? 1146 GLN A CA    1 
ATOM   9250  C C     . GLN B 2 1149 ? 137.646 168.705 99.518  1.00 48.55  ? 1146 GLN A C     1 
ATOM   9251  O O     . GLN B 2 1149 ? 138.852 168.578 99.744  1.00 48.55  ? 1146 GLN A O     1 
ATOM   9252  C CB    . GLN B 2 1149 ? 136.059 166.801 99.150  1.00 48.55  ? 1146 GLN A CB    1 
ATOM   9253  C CG    . GLN B 2 1149 ? 135.267 165.937 98.185  1.00 48.55  ? 1146 GLN A CG    1 
ATOM   9254  C CD    . GLN B 2 1149 ? 134.266 166.737 97.375  1.00 48.55  ? 1146 GLN A CD    1 
ATOM   9255  O OE1   . GLN B 2 1149 ? 134.358 166.808 96.150  1.00 48.55  ? 1146 GLN A OE1   1 
ATOM   9256  N NE2   . GLN B 2 1149 ? 133.303 167.344 98.058  1.00 48.55  ? 1146 GLN A NE2   1 
ATOM   9257  N N     . PHE B 2 1150 ? 136.880 169.581 100.164 1.00 48.55  ? 1147 PHE A N     1 
ATOM   9258  C CA    . PHE B 2 1150 ? 137.398 170.492 101.174 1.00 48.55  ? 1147 PHE A CA    1 
ATOM   9259  C C     . PHE B 2 1150 ? 136.626 170.307 102.473 1.00 48.55  ? 1147 PHE A C     1 
ATOM   9260  O O     . PHE B 2 1150 ? 135.401 170.158 102.462 1.00 48.55  ? 1147 PHE A O     1 
ATOM   9261  C CB    . PHE B 2 1150 ? 137.302 171.949 100.708 1.00 48.55  ? 1147 PHE A CB    1 
ATOM   9262  C CG    . PHE B 2 1150 ? 138.303 172.314 99.649  1.00 48.55  ? 1147 PHE A CG    1 
ATOM   9263  C CD1   . PHE B 2 1150 ? 138.165 171.846 98.354  1.00 48.55  ? 1147 PHE A CD1   1 
ATOM   9264  C CD2   . PHE B 2 1150 ? 139.382 173.127 99.950  1.00 48.55  ? 1147 PHE A CD2   1 
ATOM   9265  C CE1   . PHE B 2 1150 ? 139.085 172.180 97.379  1.00 48.55  ? 1147 PHE A CE1   1 
ATOM   9266  C CE2   . PHE B 2 1150 ? 140.305 173.465 98.979  1.00 48.55  ? 1147 PHE A CE2   1 
ATOM   9267  C CZ    . PHE B 2 1150 ? 140.156 172.990 97.692  1.00 48.55  ? 1147 PHE A CZ    1 
ATOM   9268  N N     . ASP B 2 1151 ? 137.349 170.320 103.590 1.00 48.55  ? 1148 ASP A N     1 
ATOM   9269  C CA    . ASP B 2 1151 ? 136.757 170.086 104.897 1.00 48.55  ? 1148 ASP A CA    1 
ATOM   9270  C C     . ASP B 2 1151 ? 136.358 171.414 105.540 1.00 48.55  ? 1148 ASP A C     1 
ATOM   9271  O O     . ASP B 2 1151 ? 136.352 172.467 104.897 1.00 48.55  ? 1148 ASP A O     1 
ATOM   9272  C CB    . ASP B 2 1151 ? 137.722 169.300 105.780 1.00 48.55  ? 1148 ASP A CB    1 
ATOM   9273  C CG    . ASP B 2 1151 ? 139.018 170.041 106.033 1.00 48.55  ? 1148 ASP A CG    1 
ATOM   9274  O OD1   . ASP B 2 1151 ? 139.318 170.994 105.284 1.00 48.55  ? 1148 ASP A OD1   1 
ATOM   9275  O OD2   . ASP B 2 1151 ? 139.739 169.670 106.982 1.00 48.55  ? 1148 ASP A OD2   1 
ATOM   9276  N N     . ALA B 2 1152 ? 136.011 171.368 106.829 1.00 48.55  ? 1149 ALA A N     1 
ATOM   9277  C CA    . ALA B 2 1152 ? 135.642 172.585 107.545 1.00 48.55  ? 1149 ALA A CA    1 
ATOM   9278  C C     . ALA B 2 1152 ? 136.820 173.546 107.651 1.00 48.55  ? 1149 ALA A C     1 
ATOM   9279  O O     . ALA B 2 1152 ? 136.657 174.759 107.475 1.00 48.55  ? 1149 ALA A O     1 
ATOM   9280  C CB    . ALA B 2 1152 ? 135.106 172.235 108.933 1.00 48.55  ? 1149 ALA A CB    1 
ATOM   9281  N N     . LYS B 2 1153 ? 138.015 173.024 107.939 1.00 48.55  ? 1150 LYS A N     1 
ATOM   9282  C CA    . LYS B 2 1153 ? 139.202 173.865 108.027 1.00 48.55  ? 1150 LYS A CA    1 
ATOM   9283  C C     . LYS B 2 1153 ? 139.716 174.303 106.662 1.00 48.55  ? 1150 LYS A C     1 
ATOM   9284  O O     . LYS B 2 1153 ? 140.614 175.149 106.602 1.00 48.55  ? 1150 LYS A O     1 
ATOM   9285  C CB    . LYS B 2 1153 ? 140.312 173.132 108.782 1.00 46.69  ? 1150 LYS A CB    1 
ATOM   9286  C CG    . LYS B 2 1153 ? 140.010 172.893 110.252 1.00 46.69  ? 1150 LYS A CG    1 
ATOM   9287  C CD    . LYS B 2 1153 ? 141.176 172.212 110.951 1.00 46.69  ? 1150 LYS A CD    1 
ATOM   9288  C CE    . LYS B 2 1153 ? 140.844 171.898 112.401 1.00 46.69  ? 1150 LYS A CE    1 
ATOM   9289  N NZ    . LYS B 2 1153 ? 140.695 173.132 113.220 1.00 46.69  ? 1150 LYS A NZ    1 
ATOM   9290  N N     . GLY B 2 1154 ? 139.176 173.755 105.577 1.00 48.55  ? 1151 GLY A N     1 
ATOM   9291  C CA    . GLY B 2 1154 ? 139.601 174.112 104.243 1.00 48.55  ? 1151 GLY A CA    1 
ATOM   9292  C C     . GLY B 2 1154 ? 140.748 173.298 103.688 1.00 48.55  ? 1151 GLY A C     1 
ATOM   9293  O O     . GLY B 2 1154 ? 141.174 173.555 102.553 1.00 48.55  ? 1151 GLY A O     1 
ATOM   9294  N N     . THR B 2 1155 ? 141.264 172.336 104.441 1.00 48.55  ? 1152 THR A N     1 
ATOM   9295  C CA    . THR B 2 1155 ? 142.349 171.502 103.937 1.00 48.55  ? 1152 THR A CA    1 
ATOM   9296  C C     . THR B 2 1155 ? 141.823 170.583 102.840 1.00 48.55  ? 1152 THR A C     1 
ATOM   9297  O O     . THR B 2 1155 ? 140.710 170.058 102.958 1.00 48.55  ? 1152 THR A O     1 
ATOM   9298  C CB    . THR B 2 1155 ? 142.970 170.680 105.064 1.00 48.55  ? 1152 THR A CB    1 
ATOM   9299  O OG1   . THR B 2 1155 ? 141.980 169.810 105.628 1.00 48.55  ? 1152 THR A OG1   1 
ATOM   9300  C CG2   . THR B 2 1155 ? 143.513 171.595 106.152 1.00 48.55  ? 1152 THR A CG2   1 
ATOM   9301  N N     . PRO B 2 1156 ? 142.581 170.364 101.769 1.00 48.55  ? 1153 PRO A N     1 
ATOM   9302  C CA    . PRO B 2 1156 ? 142.087 169.524 100.681 1.00 48.55  ? 1153 PRO A CA    1 
ATOM   9303  C C     . PRO B 2 1156 ? 142.456 168.057 100.849 1.00 48.55  ? 1153 PRO A C     1 
ATOM   9304  O O     . PRO B 2 1156 ? 143.484 167.703 101.429 1.00 48.55  ? 1153 PRO A O     1 
ATOM   9305  C CB    . PRO B 2 1156 ? 142.763 170.140 99.452  1.00 48.55  ? 1153 PRO A CB    1 
ATOM   9306  C CG    . PRO B 2 1156 ? 144.072 170.776 100.021 1.00 48.55  ? 1153 PRO A CG    1 
ATOM   9307  C CD    . PRO B 2 1156 ? 144.003 170.673 101.546 1.00 48.55  ? 1153 PRO A CD    1 
ATOM   9308  N N     . PHE B 2 1157 ? 141.583 167.197 100.331 1.00 48.55  ? 1154 PHE A N     1 
ATOM   9309  C CA    . PHE B 2 1157 ? 141.806 165.759 100.354 1.00 48.55  ? 1154 PHE A CA    1 
ATOM   9310  C C     . PHE B 2 1157 ? 141.089 165.142 99.164  1.00 48.55  ? 1154 PHE A C     1 
ATOM   9311  O O     . PHE B 2 1157 ? 140.171 165.742 98.599  1.00 48.55  ? 1154 PHE A O     1 
ATOM   9312  C CB    . PHE B 2 1157 ? 141.348 165.142 101.687 1.00 48.55  ? 1154 PHE A CB    1 
ATOM   9313  C CG    . PHE B 2 1157 ? 139.866 165.265 101.961 1.00 48.55  ? 1154 PHE A CG    1 
ATOM   9314  C CD1   . PHE B 2 1157 ? 138.933 164.537 101.240 1.00 48.55  ? 1154 PHE A CD1   1 
ATOM   9315  C CD2   . PHE B 2 1157 ? 139.412 166.124 102.948 1.00 48.55  ? 1154 PHE A CD2   1 
ATOM   9316  C CE1   . PHE B 2 1157 ? 137.582 164.658 101.503 1.00 48.55  ? 1154 PHE A CE1   1 
ATOM   9317  C CE2   . PHE B 2 1157 ? 138.063 166.250 103.213 1.00 48.55  ? 1154 PHE A CE2   1 
ATOM   9318  C CZ    . PHE B 2 1157 ? 137.147 165.517 102.489 1.00 48.55  ? 1154 PHE A CZ    1 
ATOM   9319  N N     . ILE B 2 1158 ? 141.516 163.942 98.789  1.00 48.55  ? 1155 ILE A N     1 
ATOM   9320  C CA    . ILE B 2 1158 ? 140.942 163.243 97.645  1.00 48.55  ? 1155 ILE A CA    1 
ATOM   9321  C C     . ILE B 2 1158 ? 139.843 162.319 98.149  1.00 48.55  ? 1155 ILE A C     1 
ATOM   9322  O O     . ILE B 2 1158 ? 140.098 161.414 98.951  1.00 48.55  ? 1155 ILE A O     1 
ATOM   9323  C CB    . ILE B 2 1158 ? 142.008 162.458 96.867  1.00 48.55  ? 1155 ILE A CB    1 
ATOM   9324  C CG1   . ILE B 2 1158 ? 143.065 163.399 96.277  1.00 48.55  ? 1155 ILE A CG1   1 
ATOM   9325  C CG2   . ILE B 2 1158 ? 141.354 161.647 95.762  1.00 48.55  ? 1155 ILE A CG2   1 
ATOM   9326  C CD1   . ILE B 2 1158 ? 144.239 163.686 97.196  1.00 48.55  ? 1155 ILE A CD1   1 
ATOM   9327  N N     . ALA B 2 1159 ? 138.622 162.548 97.677  1.00 48.55  ? 1156 ALA A N     1 
ATOM   9328  C CA    . ALA B 2 1159 ? 137.485 161.747 98.101  1.00 48.55  ? 1156 ALA A CA    1 
ATOM   9329  C C     . ALA B 2 1159 ? 137.639 160.303 97.638  1.00 48.55  ? 1156 ALA A C     1 
ATOM   9330  O O     . ALA B 2 1159 ? 138.170 160.023 96.561  1.00 48.55  ? 1156 ALA A O     1 
ATOM   9331  C CB    . ALA B 2 1159 ? 136.188 162.343 97.553  1.00 48.55  ? 1156 ALA A CB    1 
ATOM   9332  N N     . GLY B 2 1160 ? 137.176 159.378 98.475  1.00 48.55  ? 1157 GLY A N     1 
ATOM   9333  C CA    . GLY B 2 1160 ? 137.239 157.969 98.154  1.00 48.55  ? 1157 GLY A CA    1 
ATOM   9334  C C     . GLY B 2 1160 ? 138.595 157.325 98.327  1.00 48.55  ? 1157 GLY A C     1 
ATOM   9335  O O     . GLY B 2 1160 ? 138.775 156.179 97.897  1.00 48.55  ? 1157 GLY A O     1 
ATOM   9336  N N     . LYS B 2 1161 ? 139.553 158.017 98.936  1.00 48.55  ? 1158 LYS A N     1 
ATOM   9337  C CA    . LYS B 2 1161 ? 140.890 157.464 99.104  1.00 48.55  ? 1158 LYS A CA    1 
ATOM   9338  C C     . LYS B 2 1161 ? 140.860 156.273 100.053 1.00 48.55  ? 1158 LYS A C     1 
ATOM   9339  O O     . LYS B 2 1161 ? 140.165 156.293 101.072 1.00 48.55  ? 1158 LYS A O     1 
ATOM   9340  C CB    . LYS B 2 1161 ? 141.835 158.543 99.631  1.00 48.55  ? 1158 LYS A CB    1 
ATOM   9341  C CG    . LYS B 2 1161 ? 143.286 158.116 99.746  1.00 48.55  ? 1158 LYS A CG    1 
ATOM   9342  C CD    . LYS B 2 1161 ? 144.111 159.196 100.424 1.00 48.55  ? 1158 LYS A CD    1 
ATOM   9343  C CE    . LYS B 2 1161 ? 145.597 158.952 100.249 1.00 48.55  ? 1158 LYS A CE    1 
ATOM   9344  N NZ    . LYS B 2 1161 ? 146.081 157.849 101.120 1.00 48.55  ? 1158 LYS A NZ    1 
ATOM   9345  N N     . ARG B 2 1162 ? 141.615 155.233 99.713  1.00 48.55  ? 1159 ARG A N     1 
ATOM   9346  C CA    . ARG B 2 1162 ? 141.706 154.033 100.527 1.00 48.55  ? 1159 ARG A CA    1 
ATOM   9347  C C     . ARG B 2 1162 ? 143.162 153.674 100.791 1.00 48.55  ? 1159 ARG A C     1 
ATOM   9348  O O     . ARG B 2 1162 ? 144.008 153.734 99.894  1.00 48.55  ? 1159 ARG A O     1 
ATOM   9349  C CB    . ARG B 2 1162 ? 141.001 152.847 99.860  1.00 48.55  ? 1159 ARG A CB    1 
ATOM   9350  C CG    . ARG B 2 1162 ? 139.500 153.006 99.726  1.00 48.55  ? 1159 ARG A CG    1 
ATOM   9351  C CD    . ARG B 2 1162 ? 138.820 152.912 101.079 1.00 48.55  ? 1159 ARG A CD    1 
ATOM   9352  N NE    . ARG B 2 1162 ? 137.370 152.842 100.954 1.00 48.55  ? 1159 ARG A NE    1 
ATOM   9353  C CZ    . ARG B 2 1162 ? 136.577 153.898 100.831 1.00 48.55  ? 1159 ARG A CZ    1 
ATOM   9354  N NH1   . ARG B 2 1162 ? 137.064 155.127 100.801 1.00 48.55  ? 1159 ARG A NH1   1 
ATOM   9355  N NH2   . ARG B 2 1162 ? 135.264 153.715 100.731 1.00 48.55  ? 1159 ARG A NH2   1 
ATOM   9356  N N     . ILE B 2 1163 ? 143.441 153.301 102.036 1.00 48.55  ? 1160 ILE A N     1 
ATOM   9357  C CA    . ILE B 2 1163 ? 144.731 152.758 102.441 1.00 48.55  ? 1160 ILE A CA    1 
ATOM   9358  C C     . ILE B 2 1163 ? 144.544 151.257 102.603 1.00 48.55  ? 1160 ILE A C     1 
ATOM   9359  O O     . ILE B 2 1163 ? 143.950 150.799 103.588 1.00 48.55  ? 1160 ILE A O     1 
ATOM   9360  C CB    . ILE B 2 1163 ? 145.244 153.399 103.736 1.00 48.55  ? 1160 ILE A CB    1 
ATOM   9361  C CG1   . ILE B 2 1163 ? 145.631 154.856 103.496 1.00 48.55  ? 1160 ILE A CG1   1 
ATOM   9362  C CG2   . ILE B 2 1163 ? 146.436 152.628 104.277 1.00 48.55  ? 1160 ILE A CG2   1 
ATOM   9363  C CD1   . ILE B 2 1163 ? 146.874 155.015 102.663 1.00 48.55  ? 1160 ILE A CD1   1 
ATOM   9364  N N     . VAL B 2 1164 ? 145.033 150.486 101.638 1.00 57.65  ? 1161 VAL A N     1 
ATOM   9365  C CA    . VAL B 2 1164 ? 144.879 149.038 101.621 1.00 57.65  ? 1161 VAL A CA    1 
ATOM   9366  C C     . VAL B 2 1164 ? 146.248 148.412 101.840 1.00 57.65  ? 1161 VAL A C     1 
ATOM   9367  O O     . VAL B 2 1164 ? 147.229 148.871 101.253 1.00 57.65  ? 1161 VAL A O     1 
ATOM   9368  C CB    . VAL B 2 1164 ? 144.250 148.525 100.312 1.00 57.65  ? 1161 VAL A CB    1 
ATOM   9369  C CG1   . VAL B 2 1164 ? 142.817 149.006 100.212 1.00 57.65  ? 1161 VAL A CG1   1 
ATOM   9370  C CG2   . VAL B 2 1164 ? 145.043 148.999 99.105  1.00 57.65  ? 1161 VAL A CG2   1 
ATOM   9371  N N     . PRO B 2 1165 ? 146.369 147.394 102.692 1.00 80.58  ? 1162 PRO A N     1 
ATOM   9372  C CA    . PRO B 2 1165 ? 147.677 146.774 102.961 1.00 80.58  ? 1162 PRO A CA    1 
ATOM   9373  C C     . PRO B 2 1165 ? 147.985 145.528 102.139 1.00 80.58  ? 1162 PRO A C     1 
ATOM   9374  O O     . PRO B 2 1165 ? 148.994 144.873 102.424 1.00 80.58  ? 1162 PRO A O     1 
ATOM   9375  C CB    . PRO B 2 1165 ? 147.547 146.413 104.443 1.00 80.58  ? 1162 PRO A CB    1 
ATOM   9376  C CG    . PRO B 2 1165 ? 146.095 146.050 104.595 1.00 80.58  ? 1162 PRO A CG    1 
ATOM   9377  C CD    . PRO B 2 1165 ? 145.317 146.843 103.563 1.00 80.58  ? 1162 PRO A CD    1 
ATOM   9378  N N     . VAL B 2 1166 ? 147.160 145.186 101.151 1.00 98.83  ? 1163 VAL A N     1 
ATOM   9379  C CA    . VAL B 2 1166 ? 147.367 143.961 100.386 1.00 98.83  ? 1163 VAL A CA    1 
ATOM   9380  C C     . VAL B 2 1166 ? 148.600 144.123 99.507  1.00 98.83  ? 1163 VAL A C     1 
ATOM   9381  O O     . VAL B 2 1166 ? 148.593 144.887 98.534  1.00 98.83  ? 1163 VAL A O     1 
ATOM   9382  C CB    . VAL B 2 1166 ? 146.128 143.620 99.549  1.00 98.83  ? 1163 VAL A CB    1 
ATOM   9383  C CG1   . VAL B 2 1166 ? 146.395 142.399 98.680  1.00 98.83  ? 1163 VAL A CG1   1 
ATOM   9384  C CG2   . VAL B 2 1166 ? 144.927 143.386 100.452 1.00 98.83  ? 1163 VAL A CG2   1 
ATOM   9385  N N     . ILE B 2 1167 ? 149.669 143.401 99.847  1.00 112.37 ? 1164 ILE A N     1 
ATOM   9386  C CA    . ILE B 2 1167 ? 150.920 143.422 99.100  1.00 112.37 ? 1164 ILE A CA    1 
ATOM   9387  C C     . ILE B 2 1167 ? 151.277 142.037 98.573  1.00 112.37 ? 1164 ILE A C     1 
ATOM   9388  O O     . ILE B 2 1167 ? 151.628 141.876 97.400  1.00 112.37 ? 1164 ILE A O     1 
ATOM   9389  C CB    . ILE B 2 1167 ? 152.076 143.994 99.952  1.00 112.37 ? 1164 ILE A CB    1 
ATOM   9390  C CG1   . ILE B 2 1167 ? 151.651 145.293 100.641 1.00 112.37 ? 1164 ILE A CG1   1 
ATOM   9391  C CG2   . ILE B 2 1167 ? 153.311 144.217 99.093  1.00 112.37 ? 1164 ILE A CG2   1 
ATOM   9392  C CD1   . ILE B 2 1167 ? 151.265 146.396 99.683  1.00 112.37 ? 1164 ILE A CD1   1 
ATOM   9393  N N     . GLU B 2 1168 ? 151.193 141.021 99.430  1.00 133.30 ? 1165 GLU A N     1 
ATOM   9394  C CA    . GLU B 2 1168 ? 151.525 139.654 99.062  1.00 133.30 ? 1165 GLU A CA    1 
ATOM   9395  C C     . GLU B 2 1168 ? 150.526 138.714 99.724  1.00 133.30 ? 1165 GLU A C     1 
ATOM   9396  O O     . GLU B 2 1168 ? 149.775 139.105 100.622 1.00 133.30 ? 1165 GLU A O     1 
ATOM   9397  C CB    . GLU B 2 1168 ? 152.964 139.301 99.464  1.00 133.30 ? 1165 GLU A CB    1 
ATOM   9398  C CG    . GLU B 2 1168 ? 153.588 138.147 98.685  1.00 133.30 ? 1165 GLU A CG    1 
ATOM   9399  C CD    . GLU B 2 1168 ? 153.516 138.341 97.182  1.00 133.30 ? 1165 GLU A CD    1 
ATOM   9400  O OE1   . GLU B 2 1168 ? 152.517 137.911 96.568  1.00 133.30 ? 1165 GLU A OE1   1 
ATOM   9401  O OE2   . GLU B 2 1168 ? 154.463 138.925 96.613  1.00 133.30 ? 1165 GLU A OE2   1 
ATOM   9402  N N     . ASN B 2 1169 ? 150.515 137.461 99.261  1.00 141.56 ? 1166 ASN A N     1 
ATOM   9403  C CA    . ASN B 2 1169 ? 149.614 136.466 99.834  1.00 141.56 ? 1166 ASN A CA    1 
ATOM   9404  C C     . ASN B 2 1169 ? 149.913 136.243 101.312 1.00 141.56 ? 1166 ASN A C     1 
ATOM   9405  O O     . ASN B 2 1169 ? 148.996 136.149 102.137 1.00 141.56 ? 1166 ASN A O     1 
ATOM   9406  C CB    . ASN B 2 1169 ? 149.719 135.154 99.055  1.00 141.56 ? 1166 ASN A CB    1 
ATOM   9407  C CG    . ASN B 2 1169 ? 151.152 134.784 98.725  1.00 141.56 ? 1166 ASN A CG    1 
ATOM   9408  O OD1   . ASN B 2 1169 ? 152.089 135.220 99.393  1.00 141.56 ? 1166 ASN A OD1   1 
ATOM   9409  N ND2   . ASN B 2 1169 ? 151.330 133.974 97.687  1.00 141.56 ? 1166 ASN A ND2   1 
ATOM   9410  N N     . HIS B 2 1170 ? 151.196 136.155 101.666 1.00 144.68 ? 1167 HIS A N     1 
ATOM   9411  C CA    . HIS B 2 1170 ? 151.572 136.022 103.068 1.00 144.68 ? 1167 HIS A CA    1 
ATOM   9412  C C     . HIS B 2 1170 ? 151.830 137.374 103.719 1.00 144.68 ? 1167 HIS A C     1 
ATOM   9413  O O     . HIS B 2 1170 ? 151.618 137.526 104.927 1.00 144.68 ? 1167 HIS A O     1 
ATOM   9414  C CB    . HIS B 2 1170 ? 152.808 135.131 103.201 1.00 144.68 ? 1167 HIS A CB    1 
ATOM   9415  C CG    . HIS B 2 1170 ? 153.177 134.817 104.618 1.00 144.68 ? 1167 HIS A CG    1 
ATOM   9416  N ND1   . HIS B 2 1170 ? 153.994 135.631 105.372 1.00 144.68 ? 1167 HIS A ND1   1 
ATOM   9417  C CD2   . HIS B 2 1170 ? 152.839 133.779 105.418 1.00 144.68 ? 1167 HIS A CD2   1 
ATOM   9418  C CE1   . HIS B 2 1170 ? 154.144 135.108 106.576 1.00 144.68 ? 1167 HIS A CE1   1 
ATOM   9419  N NE2   . HIS B 2 1170 ? 153.453 133.983 106.629 1.00 144.68 ? 1167 HIS A NE2   1 
ATOM   9420  N N     . ARG B 2 1171 ? 152.284 138.361 102.945 1.00 131.91 ? 1168 ARG A N     1 
ATOM   9421  C CA    . ARG B 2 1171 ? 152.565 139.699 103.465 1.00 131.91 ? 1168 ARG A CA    1 
ATOM   9422  C C     . ARG B 2 1171 ? 151.414 140.622 103.073 1.00 131.91 ? 1168 ARG A C     1 
ATOM   9423  O O     . ARG B 2 1171 ? 151.458 141.334 102.070 1.00 131.91 ? 1168 ARG A O     1 
ATOM   9424  C CB    . ARG B 2 1171 ? 153.907 140.207 102.946 1.00 131.91 ? 1168 ARG A CB    1 
ATOM   9425  C CG    . ARG B 2 1171 ? 154.359 141.523 103.563 1.00 131.91 ? 1168 ARG A CG    1 
ATOM   9426  C CD    . ARG B 2 1171 ? 154.849 141.335 104.992 1.00 131.91 ? 1168 ARG A CD    1 
ATOM   9427  N NE    . ARG B 2 1171 ? 153.768 141.451 105.963 1.00 131.91 ? 1168 ARG A NE    1 
ATOM   9428  C CZ    . ARG B 2 1171 ? 153.903 141.235 107.265 1.00 131.91 ? 1168 ARG A CZ    1 
ATOM   9429  N NH1   . ARG B 2 1171 ? 155.066 140.888 107.791 1.00 131.91 ? 1168 ARG A NH1   1 
ATOM   9430  N NH2   . ARG B 2 1171 ? 152.845 141.370 108.058 1.00 131.91 ? 1168 ARG A NH2   1 
ATOM   9431  N N     . PHE B 2 1172 ? 150.364 140.597 103.890 1.00 124.82 ? 1169 PHE A N     1 
ATOM   9432  C CA    . PHE B 2 1172 ? 149.193 141.440 103.694 1.00 124.82 ? 1169 PHE A CA    1 
ATOM   9433  C C     . PHE B 2 1172 ? 149.162 142.629 104.646 1.00 124.82 ? 1169 PHE A C     1 
ATOM   9434  O O     . PHE B 2 1172 ? 148.158 143.345 104.693 1.00 124.82 ? 1169 PHE A O     1 
ATOM   9435  C CB    . PHE B 2 1172 ? 147.916 140.608 103.845 1.00 124.82 ? 1169 PHE A CB    1 
ATOM   9436  C CG    . PHE B 2 1172 ? 147.486 140.403 105.272 1.00 124.82 ? 1169 PHE A CG    1 
ATOM   9437  C CD1   . PHE B 2 1172 ? 148.191 139.551 106.105 1.00 124.82 ? 1169 PHE A CD1   1 
ATOM   9438  C CD2   . PHE B 2 1172 ? 146.371 141.054 105.775 1.00 124.82 ? 1169 PHE A CD2   1 
ATOM   9439  C CE1   . PHE B 2 1172 ? 147.797 139.358 107.417 1.00 124.82 ? 1169 PHE A CE1   1 
ATOM   9440  C CE2   . PHE B 2 1172 ? 145.973 140.865 107.085 1.00 124.82 ? 1169 PHE A CE2   1 
ATOM   9441  C CZ    . PHE B 2 1172 ? 146.686 140.016 107.907 1.00 124.82 ? 1169 PHE A CZ    1 
ATOM   9442  N N     . THR B 2 1173 ? 150.236 142.854 105.405 1.00 122.22 ? 1170 THR A N     1 
ATOM   9443  C CA    . THR B 2 1173 ? 150.266 143.930 106.385 1.00 122.22 ? 1170 THR A CA    1 
ATOM   9444  C C     . THR B 2 1173 ? 151.593 144.685 106.381 1.00 122.22 ? 1170 THR A C     1 
ATOM   9445  O O     . THR B 2 1173 ? 151.714 145.696 107.081 1.00 122.22 ? 1170 THR A O     1 
ATOM   9446  C CB    . THR B 2 1173 ? 149.973 143.352 107.789 1.00 122.22 ? 1170 THR A CB    1 
ATOM   9447  O OG1   . THR B 2 1173 ? 148.759 142.593 107.738 1.00 122.22 ? 1170 THR A OG1   1 
ATOM   9448  C CG2   . THR B 2 1173 ? 149.773 144.448 108.831 1.00 122.22 ? 1170 THR A CG2   1 
ATOM   9449  N N     . GLY B 2 1174 ? 152.571 144.262 105.576 1.00 114.69 ? 1171 GLY A N     1 
ATOM   9450  C CA    . GLY B 2 1174 ? 153.907 144.830 105.678 1.00 114.69 ? 1171 GLY A CA    1 
ATOM   9451  C C     . GLY B 2 1174 ? 153.951 146.321 105.397 1.00 114.69 ? 1171 GLY A C     1 
ATOM   9452  O O     . GLY B 2 1174 ? 154.545 147.091 106.156 1.00 114.69 ? 1171 GLY A O     1 
ATOM   9453  N N     . ARG B 2 1175 ? 153.322 146.750 104.305 1.00 95.82  ? 1172 ARG A N     1 
ATOM   9454  C CA    . ARG B 2 1175 ? 153.343 148.153 103.917 1.00 95.82  ? 1172 ARG A CA    1 
ATOM   9455  C C     . ARG B 2 1175 ? 151.971 148.565 103.404 1.00 95.82  ? 1172 ARG A C     1 
ATOM   9456  O O     . ARG B 2 1175 ? 151.174 147.738 102.956 1.00 95.82  ? 1172 ARG A O     1 
ATOM   9457  C CB    . ARG B 2 1175 ? 154.411 148.439 102.850 1.00 95.82  ? 1172 ARG A CB    1 
ATOM   9458  C CG    . ARG B 2 1175 ? 155.843 148.256 103.332 1.00 95.82  ? 1172 ARG A CG    1 
ATOM   9459  C CD    . ARG B 2 1175 ? 156.851 148.477 102.211 1.00 95.82  ? 1172 ARG A CD    1 
ATOM   9460  N NE    . ARG B 2 1175 ? 156.374 148.000 100.918 1.00 95.82  ? 1172 ARG A NE    1 
ATOM   9461  C CZ    . ARG B 2 1175 ? 156.305 146.723 100.565 1.00 95.82  ? 1172 ARG A CZ    1 
ATOM   9462  N NH1   . ARG B 2 1175 ? 156.681 145.756 101.387 1.00 95.82  ? 1172 ARG A NH1   1 
ATOM   9463  N NH2   . ARG B 2 1175 ? 155.851 146.409 99.355  1.00 95.82  ? 1172 ARG A NH2   1 
ATOM   9464  N N     . TYR B 2 1176 ? 151.711 149.865 103.476 1.00 70.96  ? 1173 TYR A N     1 
ATOM   9465  C CA    . TYR B 2 1176 ? 150.447 150.451 103.060 1.00 70.96  ? 1173 TYR A CA    1 
ATOM   9466  C C     . TYR B 2 1176 ? 150.621 151.187 101.737 1.00 70.96  ? 1173 TYR A C     1 
ATOM   9467  O O     . TYR B 2 1176 ? 151.686 151.732 101.438 1.00 70.96  ? 1173 TYR A O     1 
ATOM   9468  C CB    . TYR B 2 1176 ? 149.920 151.410 104.132 1.00 70.96  ? 1173 TYR A CB    1 
ATOM   9469  C CG    . TYR B 2 1176 ? 149.446 150.728 105.398 1.00 70.96  ? 1173 TYR A CG    1 
ATOM   9470  C CD1   . TYR B 2 1176 ? 149.410 149.343 105.497 1.00 70.96  ? 1173 TYR A CD1   1 
ATOM   9471  C CD2   . TYR B 2 1176 ? 149.048 151.471 106.500 1.00 70.96  ? 1173 TYR A CD2   1 
ATOM   9472  C CE1   . TYR B 2 1176 ? 148.984 148.720 106.652 1.00 70.96  ? 1173 TYR A CE1   1 
ATOM   9473  C CE2   . TYR B 2 1176 ? 148.620 150.855 107.661 1.00 70.96  ? 1173 TYR A CE2   1 
ATOM   9474  C CZ    . TYR B 2 1176 ? 148.590 149.480 107.731 1.00 70.96  ? 1173 TYR A CZ    1 
ATOM   9475  O OH    . TYR B 2 1176 ? 148.164 148.862 108.884 1.00 70.96  ? 1173 TYR A OH    1 
ATOM   9476  N N     . ARG B 2 1177 ? 149.555 151.197 100.941 1.00 57.92  ? 1174 ARG A N     1 
ATOM   9477  C CA    . ARG B 2 1177 ? 149.596 151.804 99.617  1.00 57.92  ? 1174 ARG A CA    1 
ATOM   9478  C C     . ARG B 2 1177 ? 148.352 152.648 99.391  1.00 57.92  ? 1174 ARG A C     1 
ATOM   9479  O O     . ARG B 2 1177 ? 147.247 152.248 99.768  1.00 57.92  ? 1174 ARG A O     1 
ATOM   9480  C CB    . ARG B 2 1177 ? 149.722 150.734 98.524  1.00 57.92  ? 1174 ARG A CB    1 
ATOM   9481  C CG    . ARG B 2 1177 ? 148.537 149.786 98.427  1.00 57.92  ? 1174 ARG A CG    1 
ATOM   9482  C CD    . ARG B 2 1177 ? 148.741 148.742 97.344  1.00 57.92  ? 1174 ARG A CD    1 
ATOM   9483  N NE    . ARG B 2 1177 ? 148.461 149.272 96.015  1.00 57.92  ? 1174 ARG A NE    1 
ATOM   9484  C CZ    . ARG B 2 1177 ? 147.411 148.933 95.280  1.00 57.92  ? 1174 ARG A CZ    1 
ATOM   9485  N NH1   . ARG B 2 1177 ? 146.515 148.062 95.715  1.00 57.92  ? 1174 ARG A NH1   1 
ATOM   9486  N NH2   . ARG B 2 1177 ? 147.256 149.481 94.078  1.00 57.92  ? 1174 ARG A NH2   1 
ATOM   9487  N N     . ASP B 2 1178 ? 148.542 153.824 98.800  1.00 49.50  ? 1175 ASP A N     1 
ATOM   9488  C CA    . ASP B 2 1178 ? 147.413 154.633 98.367  1.00 49.50  ? 1175 ASP A CA    1 
ATOM   9489  C C     . ASP B 2 1178 ? 146.685 153.934 97.228  1.00 49.50  ? 1175 ASP A C     1 
ATOM   9490  O O     . ASP B 2 1178 ? 147.305 153.452 96.276  1.00 49.50  ? 1175 ASP A O     1 
ATOM   9491  C CB    . ASP B 2 1178 ? 147.887 156.012 97.911  1.00 49.50  ? 1175 ASP A CB    1 
ATOM   9492  C CG    . ASP B 2 1178 ? 148.431 156.851 99.050  1.00 49.50  ? 1175 ASP A CG    1 
ATOM   9493  O OD1   . ASP B 2 1178 ? 147.973 156.670 100.196 1.00 49.50  ? 1175 ASP A OD1   1 
ATOM   9494  O OD2   . ASP B 2 1178 ? 149.318 157.694 98.797  1.00 49.50  ? 1175 ASP A OD2   1 
ATOM   9495  N N     . LEU B 2 1179 ? 145.360 153.879 97.324  1.00 48.55  ? 1176 LEU A N     1 
ATOM   9496  C CA    . LEU B 2 1179 ? 144.553 153.254 96.290  1.00 48.55  ? 1176 LEU A CA    1 
ATOM   9497  C C     . LEU B 2 1179 ? 143.306 154.091 96.056  1.00 48.55  ? 1176 LEU A C     1 
ATOM   9498  O O     . LEU B 2 1179 ? 142.674 154.557 97.007  1.00 48.55  ? 1176 LEU A O     1 
ATOM   9499  C CB    . LEU B 2 1179 ? 144.166 151.822 96.671  1.00 48.55  ? 1176 LEU A CB    1 
ATOM   9500  C CG    . LEU B 2 1179 ? 143.373 151.063 95.610  1.00 48.55  ? 1176 LEU A CG    1 
ATOM   9501  C CD1   . LEU B 2 1179 ? 144.219 150.911 94.364  1.00 48.55  ? 1176 LEU A CD1   1 
ATOM   9502  C CD2   . LEU B 2 1179 ? 142.953 149.708 96.123  1.00 48.55  ? 1176 LEU A CD2   1 
ATOM   9503  N N     . TYR B 2 1180 ? 142.960 154.278 94.786  1.00 48.55  ? 1177 TYR A N     1 
ATOM   9504  C CA    . TYR B 2 1180 ? 141.799 155.076 94.395  1.00 48.55  ? 1177 TYR A CA    1 
ATOM   9505  C C     . TYR B 2 1180 ? 140.826 154.177 93.649  1.00 48.55  ? 1177 TYR A C     1 
ATOM   9506  O O     . TYR B 2 1180 ? 141.032 153.890 92.456  1.00 48.55  ? 1177 TYR A O     1 
ATOM   9507  C CB    . TYR B 2 1180 ? 142.217 156.263 93.529  1.00 48.55  ? 1177 TYR A CB    1 
ATOM   9508  C CG    . TYR B 2 1180 ? 143.235 157.173 94.185  1.00 48.55  ? 1177 TYR A CG    1 
ATOM   9509  C CD1   . TYR B 2 1180 ? 144.576 156.816 94.248  1.00 48.55  ? 1177 TYR A CD1   1 
ATOM   9510  C CD2   . TYR B 2 1180 ? 142.854 158.381 94.749  1.00 48.55  ? 1177 TYR A CD2   1 
ATOM   9511  C CE1   . TYR B 2 1180 ? 145.508 157.639 94.847  1.00 48.55  ? 1177 TYR A CE1   1 
ATOM   9512  C CE2   . TYR B 2 1180 ? 143.780 159.210 95.350  1.00 48.55  ? 1177 TYR A CE2   1 
ATOM   9513  C CZ    . TYR B 2 1180 ? 145.104 158.835 95.397  1.00 48.55  ? 1177 TYR A CZ    1 
ATOM   9514  O OH    . TYR B 2 1180 ? 146.028 159.660 95.995  1.00 48.55  ? 1177 TYR A OH    1 
ATOM   9515  N N     . PRO B 2 1181 ? 139.766 153.693 94.306  1.00 48.55  ? 1178 PRO A N     1 
ATOM   9516  C CA    . PRO B 2 1181 ? 138.884 152.711 93.653  1.00 48.55  ? 1178 PRO A CA    1 
ATOM   9517  C C     . PRO B 2 1181 ? 138.261 153.202 92.360  1.00 48.55  ? 1178 PRO A C     1 
ATOM   9518  O O     . PRO B 2 1181 ? 138.134 152.423 91.407  1.00 48.55  ? 1178 PRO A O     1 
ATOM   9519  C CB    . PRO B 2 1181 ? 137.821 152.437 94.725  1.00 48.55  ? 1178 PRO A CB    1 
ATOM   9520  C CG    . PRO B 2 1181 ? 138.476 152.796 96.012  1.00 48.55  ? 1178 PRO A CG    1 
ATOM   9521  C CD    . PRO B 2 1181 ? 139.370 153.953 95.699  1.00 48.55  ? 1178 PRO A CD    1 
ATOM   9522  N N     . ALA B 2 1182 ? 137.864 154.473 92.296  1.00 48.55  ? 1179 ALA A N     1 
ATOM   9523  C CA    . ALA B 2 1182 ? 137.261 154.989 91.073  1.00 48.55  ? 1179 ALA A CA    1 
ATOM   9524  C C     . ALA B 2 1182 ? 138.274 155.051 89.938  1.00 48.55  ? 1179 ALA A C     1 
ATOM   9525  O O     . ALA B 2 1182 ? 137.953 154.714 88.792  1.00 48.55  ? 1179 ALA A O     1 
ATOM   9526  C CB    . ALA B 2 1182 ? 136.653 156.367 91.328  1.00 48.55  ? 1179 ALA A CB    1 
ATOM   9527  N N     . ASN B 2 1183 ? 139.503 155.476 90.235  1.00 48.55  ? 1180 ASN A N     1 
ATOM   9528  C CA    . ASN B 2 1183 ? 140.500 155.656 89.185  1.00 48.55  ? 1180 ASN A CA    1 
ATOM   9529  C C     . ASN B 2 1183 ? 141.051 154.318 88.707  1.00 48.55  ? 1180 ASN A C     1 
ATOM   9530  O O     . ASN B 2 1183 ? 141.369 154.154 87.524  1.00 48.55  ? 1180 ASN A O     1 
ATOM   9531  C CB    . ASN B 2 1183 ? 141.628 156.558 89.685  1.00 48.55  ? 1180 ASN A CB    1 
ATOM   9532  C CG    . ASN B 2 1183 ? 141.232 158.019 89.714  1.00 48.55  ? 1180 ASN A CG    1 
ATOM   9533  O OD1   . ASN B 2 1183 ? 140.179 158.399 89.203  1.00 48.55  ? 1180 ASN A OD1   1 
ATOM   9534  N ND2   . ASN B 2 1183 ? 142.077 158.850 90.314  1.00 48.55  ? 1180 ASN A ND2   1 
ATOM   9535  N N     . GLU B 2 1184 ? 141.189 153.352 89.616  1.00 48.55  ? 1181 GLU A N     1 
ATOM   9536  C CA    . GLU B 2 1184 ? 141.714 152.049 89.219  1.00 48.55  ? 1181 GLU A CA    1 
ATOM   9537  C C     . GLU B 2 1184 ? 140.660 151.225 88.492  1.00 48.55  ? 1181 GLU A C     1 
ATOM   9538  O O     . GLU B 2 1184 ? 140.993 150.386 87.648  1.00 48.55  ? 1181 GLU A O     1 
ATOM   9539  C CB    . GLU B 2 1184 ? 142.242 151.301 90.441  1.00 48.55  ? 1181 GLU A CB    1 
ATOM   9540  C CG    . GLU B 2 1184 ? 143.398 152.000 91.137  1.00 48.55  ? 1181 GLU A CG    1 
ATOM   9541  C CD    . GLU B 2 1184 ? 144.607 152.202 90.237  1.00 48.55  ? 1181 GLU A CD    1 
ATOM   9542  O OE1   . GLU B 2 1184 ? 144.773 151.433 89.266  1.00 48.55  ? 1181 GLU A OE1   1 
ATOM   9543  O OE2   . GLU B 2 1184 ? 145.394 153.134 90.505  1.00 48.55  ? 1181 GLU A OE2   1 
ATOM   9544  N N     . LEU B 2 1185 ? 139.384 151.442 88.810  1.00 48.55  ? 1182 LEU A N     1 
ATOM   9545  C CA    . LEU B 2 1185 ? 138.324 150.737 88.098  1.00 48.55  ? 1182 LEU A CA    1 
ATOM   9546  C C     . LEU B 2 1185 ? 138.220 151.218 86.656  1.00 48.55  ? 1182 LEU A C     1 
ATOM   9547  O O     . LEU B 2 1185 ? 138.129 150.410 85.726  1.00 48.55  ? 1182 LEU A O     1 
ATOM   9548  C CB    . LEU B 2 1185 ? 136.991 150.911 88.825  1.00 48.55  ? 1182 LEU A CB    1 
ATOM   9549  C CG    . LEU B 2 1185 ? 135.798 150.217 88.167  1.00 48.55  ? 1182 LEU A CG    1 
ATOM   9550  C CD1   . LEU B 2 1185 ? 136.039 148.724 88.077  1.00 48.55  ? 1182 LEU A CD1   1 
ATOM   9551  C CD2   . LEU B 2 1185 ? 134.524 150.505 88.939  1.00 48.55  ? 1182 LEU A CD2   1 
ATOM   9552  N N     . ILE B 2 1186 ? 138.237 152.537 86.449  1.00 48.55  ? 1183 ILE A N     1 
ATOM   9553  C CA    . ILE B 2 1186 ? 138.160 153.063 85.090  1.00 48.55  ? 1183 ILE A CA    1 
ATOM   9554  C C     . ILE B 2 1186 ? 139.421 152.710 84.312  1.00 48.55  ? 1183 ILE A C     1 
ATOM   9555  O O     . ILE B 2 1186 ? 139.380 152.519 83.092  1.00 48.55  ? 1183 ILE A O     1 
ATOM   9556  C CB    . ILE B 2 1186 ? 137.899 154.580 85.105  1.00 48.55  ? 1183 ILE A CB    1 
ATOM   9557  C CG1   . ILE B 2 1186 ? 139.042 155.330 85.790  1.00 48.55  ? 1183 ILE A CG1   1 
ATOM   9558  C CG2   . ILE B 2 1186 ? 136.579 154.884 85.791  1.00 48.55  ? 1183 ILE A CG2   1 
ATOM   9559  C CD1   . ILE B 2 1186 ? 138.965 156.833 85.636  1.00 48.55  ? 1183 ILE A CD1   1 
ATOM   9560  N N     . ALA B 2 1187 ? 140.561 152.622 85.002  1.00 48.55  ? 1184 ALA A N     1 
ATOM   9561  C CA    . ALA B 2 1187 ? 141.784 152.166 84.349  1.00 48.55  ? 1184 ALA A CA    1 
ATOM   9562  C C     . ALA B 2 1187 ? 141.669 150.707 83.930  1.00 48.55  ? 1184 ALA A C     1 
ATOM   9563  O O     . ALA B 2 1187 ? 142.153 150.319 82.860  1.00 48.55  ? 1184 ALA A O     1 
ATOM   9564  C CB    . ALA B 2 1187 ? 142.982 152.367 85.276  1.00 48.55  ? 1184 ALA A CB    1 
ATOM   9565  N N     . LEU B 2 1188 ? 141.038 149.881 84.767  1.00 48.55  ? 1185 LEU A N     1 
ATOM   9566  C CA    . LEU B 2 1188 ? 140.865 148.473 84.427  1.00 48.55  ? 1185 LEU A CA    1 
ATOM   9567  C C     . LEU B 2 1188 ? 139.891 148.303 83.268  1.00 48.55  ? 1185 LEU A C     1 
ATOM   9568  O O     . LEU B 2 1188 ? 140.188 147.606 82.293  1.00 48.55  ? 1185 LEU A O     1 
ATOM   9569  C CB    . LEU B 2 1188 ? 140.385 147.696 85.653  1.00 48.55  ? 1185 LEU A CB    1 
ATOM   9570  C CG    . LEU B 2 1188 ? 140.260 146.178 85.506  1.00 48.55  ? 1185 LEU A CG    1 
ATOM   9571  C CD1   . LEU B 2 1188 ? 140.805 145.488 86.740  1.00 48.55  ? 1185 LEU A CD1   1 
ATOM   9572  C CD2   . LEU B 2 1188 ? 138.814 145.768 85.263  1.00 48.55  ? 1185 LEU A CD2   1 
ATOM   9573  N N     . LEU B 2 1189 ? 138.726 148.951 83.350  1.00 52.06  ? 1186 LEU A N     1 
ATOM   9574  C CA    . LEU B 2 1189 ? 137.715 148.790 82.309  1.00 52.06  ? 1186 LEU A CA    1 
ATOM   9575  C C     . LEU B 2 1189 ? 138.212 149.306 80.965  1.00 52.06  ? 1186 LEU A C     1 
ATOM   9576  O O     . LEU B 2 1189 ? 137.940 148.698 79.923  1.00 52.06  ? 1186 LEU A O     1 
ATOM   9577  C CB    . LEU B 2 1189 ? 136.422 149.501 82.712  1.00 52.06  ? 1186 LEU A CB    1 
ATOM   9578  C CG    . LEU B 2 1189 ? 135.777 149.079 84.033  1.00 52.06  ? 1186 LEU A CG    1 
ATOM   9579  C CD1   . LEU B 2 1189 ? 134.371 149.644 84.145  1.00 52.06  ? 1186 LEU A CD1   1 
ATOM   9580  C CD2   . LEU B 2 1189 ? 135.754 147.564 84.156  1.00 52.06  ? 1186 LEU A CD2   1 
ATOM   9581  N N     . GLU B 2 1190 ? 138.935 150.427 80.968  1.00 49.31  ? 1187 GLU A N     1 
ATOM   9582  C CA    . GLU B 2 1190 ? 139.466 150.965 79.720  1.00 49.31  ? 1187 GLU A CA    1 
ATOM   9583  C C     . GLU B 2 1190 ? 140.441 149.992 79.070  1.00 49.31  ? 1187 GLU A C     1 
ATOM   9584  O O     . GLU B 2 1190 ? 140.417 149.801 77.848  1.00 49.31  ? 1187 GLU A O     1 
ATOM   9585  C CB    . GLU B 2 1190 ? 140.143 152.311 79.978  1.00 49.31  ? 1187 GLU A CB    1 
ATOM   9586  C CG    . GLU B 2 1190 ? 139.220 153.511 79.839  1.00 49.31  ? 1187 GLU A CG    1 
ATOM   9587  C CD    . GLU B 2 1190 ? 139.879 154.808 80.268  1.00 49.31  ? 1187 GLU A CD    1 
ATOM   9588  O OE1   . GLU B 2 1190 ? 141.126 154.853 80.325  1.00 49.31  ? 1187 GLU A OE1   1 
ATOM   9589  O OE2   . GLU B 2 1190 ? 139.150 155.783 80.548  1.00 49.31  ? 1187 GLU A OE2   1 
ATOM   9590  N N     . GLU B 2 1191 ? 141.309 149.368 79.870  1.00 51.86  ? 1188 GLU A N     1 
ATOM   9591  C CA    . GLU B 2 1191 ? 142.284 148.434 79.316  1.00 51.86  ? 1188 GLU A CA    1 
ATOM   9592  C C     . GLU B 2 1191 ? 141.592 147.188 78.771  1.00 51.86  ? 1188 GLU A C     1 
ATOM   9593  O O     . GLU B 2 1191 ? 141.954 146.689 77.699  1.00 51.86  ? 1188 GLU A O     1 
ATOM   9594  C CB    . GLU B 2 1191 ? 143.327 148.084 80.385  1.00 51.86  ? 1188 GLU A CB    1 
ATOM   9595  C CG    . GLU B 2 1191 ? 144.591 147.338 79.915  1.00 51.86  ? 1188 GLU A CG    1 
ATOM   9596  C CD    . GLU B 2 1191 ? 144.343 145.946 79.366  1.00 51.86  ? 1188 GLU A CD    1 
ATOM   9597  O OE1   . GLU B 2 1191 ? 143.511 145.217 79.941  1.00 51.86  ? 1188 GLU A OE1   1 
ATOM   9598  O OE2   . GLU B 2 1191 ? 144.992 145.578 78.364  1.00 51.86  ? 1188 GLU A OE2   1 
ATOM   9599  N N     . LYS B 2 1192 ? 140.580 146.683 79.482  1.00 53.05  ? 1189 LYS A N     1 
ATOM   9600  C CA    . LYS B 2 1192 ? 139.822 145.534 78.999  1.00 53.05  ? 1189 LYS A CA    1 
ATOM   9601  C C     . LYS B 2 1192 ? 138.919 145.873 77.823  1.00 53.05  ? 1189 LYS A C     1 
ATOM   9602  O O     . LYS B 2 1192 ? 138.414 144.955 77.169  1.00 53.05  ? 1189 LYS A O     1 
ATOM   9603  C CB    . LYS B 2 1192 ? 138.961 144.933 80.118  1.00 53.05  ? 1189 LYS A CB    1 
ATOM   9604  C CG    . LYS B 2 1192 ? 139.650 144.737 81.458  1.00 53.05  ? 1189 LYS A CG    1 
ATOM   9605  C CD    . LYS B 2 1192 ? 140.996 144.061 81.306  1.00 53.05  ? 1189 LYS A CD    1 
ATOM   9606  C CE    . LYS B 2 1192 ? 140.859 142.554 81.358  1.00 53.05  ? 1189 LYS A CE    1 
ATOM   9607  N NZ    . LYS B 2 1192 ? 142.135 141.900 81.756  1.00 53.05  ? 1189 LYS A NZ    1 
ATOM   9608  N N     . GLY B 2 1193 ? 138.713 147.152 77.532  1.00 52.88  ? 1190 GLY A N     1 
ATOM   9609  C CA    . GLY B 2 1193 ? 137.780 147.529 76.488  1.00 52.88  ? 1190 GLY A CA    1 
ATOM   9610  C C     . GLY B 2 1193 ? 136.342 147.197 76.820  1.00 52.88  ? 1190 GLY A C     1 
ATOM   9611  O O     . GLY B 2 1193 ? 135.577 146.809 75.928  1.00 52.88  ? 1190 GLY A O     1 
ATOM   9612  N N     . ILE B 2 1194 ? 135.959 147.330 78.086  1.00 53.30  ? 1191 ILE A N     1 
ATOM   9613  C CA    . ILE B 2 1194 ? 134.587 147.110 78.528  1.00 53.30  ? 1191 ILE A CA    1 
ATOM   9614  C C     . ILE B 2 1194 ? 133.897 148.464 78.585  1.00 53.30  ? 1191 ILE A C     1 
ATOM   9615  O O     . ILE B 2 1194 ? 134.314 149.350 79.340  1.00 53.30  ? 1191 ILE A O     1 
ATOM   9616  C CB    . ILE B 2 1194 ? 134.541 146.408 79.893  1.00 53.30  ? 1191 ILE A CB    1 
ATOM   9617  C CG1   . ILE B 2 1194 ? 135.255 145.056 79.824  1.00 53.30  ? 1191 ILE A CG1   1 
ATOM   9618  C CG2   . ILE B 2 1194 ? 133.103 146.238 80.357  1.00 53.30  ? 1191 ILE A CG2   1 
ATOM   9619  C CD1   . ILE B 2 1194 ? 134.636 144.086 78.841  1.00 53.30  ? 1191 ILE A CD1   1 
ATOM   9620  N N     . VAL B 2 1195 ? 132.845 148.629 77.789  1.00 52.97  ? 1192 VAL A N     1 
ATOM   9621  C CA    . VAL B 2 1195 ? 132.158 149.912 77.696  1.00 52.97  ? 1192 VAL A CA    1 
ATOM   9622  C C     . VAL B 2 1195 ? 131.422 150.187 79.002  1.00 52.97  ? 1192 VAL A C     1 
ATOM   9623  O O     . VAL B 2 1195 ? 130.732 149.314 79.543  1.00 52.97  ? 1192 VAL A O     1 
ATOM   9624  C CB    . VAL B 2 1195 ? 131.209 149.939 76.485  1.00 52.97  ? 1192 VAL A CB    1 
ATOM   9625  C CG1   . VAL B 2 1195 ? 130.088 148.915 76.629  1.00 52.97  ? 1192 VAL A CG1   1 
ATOM   9626  C CG2   . VAL B 2 1195 ? 130.638 151.337 76.292  1.00 52.97  ? 1192 VAL A CG2   1 
ATOM   9627  N N     . PHE B 2 1196 ? 131.604 151.395 79.534  1.00 51.05  ? 1193 PHE A N     1 
ATOM   9628  C CA    . PHE B 2 1196 ? 130.939 151.795 80.767  1.00 51.05  ? 1193 PHE A CA    1 
ATOM   9629  C C     . PHE B 2 1196 ? 130.371 153.205 80.741  1.00 51.05  ? 1193 PHE A C     1 
ATOM   9630  O O     . PHE B 2 1196 ? 129.671 153.574 81.689  1.00 51.05  ? 1193 PHE A O     1 
ATOM   9631  C CB    . PHE B 2 1196 ? 131.899 151.658 81.959  1.00 51.05  ? 1193 PHE A CB    1 
ATOM   9632  C CG    . PHE B 2 1196 ? 132.922 152.753 82.051  1.00 51.05  ? 1193 PHE A CG    1 
ATOM   9633  C CD1   . PHE B 2 1196 ? 134.044 152.738 81.240  1.00 51.05  ? 1193 PHE A CD1   1 
ATOM   9634  C CD2   . PHE B 2 1196 ? 132.775 153.786 82.960  1.00 51.05  ? 1193 PHE A CD2   1 
ATOM   9635  C CE1   . PHE B 2 1196 ? 134.992 153.738 81.324  1.00 51.05  ? 1193 PHE A CE1   1 
ATOM   9636  C CE2   . PHE B 2 1196 ? 133.719 154.790 83.049  1.00 51.05  ? 1193 PHE A CE2   1 
ATOM   9637  C CZ    . PHE B 2 1196 ? 134.829 154.766 82.229  1.00 51.05  ? 1193 PHE A CZ    1 
ATOM   9638  N N     . ARG B 2 1197 ? 130.638 154.006 79.706  1.00 53.82  ? 1194 ARG A N     1 
ATOM   9639  C CA    . ARG B 2 1197 ? 130.065 155.347 79.643  1.00 53.82  ? 1194 ARG A CA    1 
ATOM   9640  C C     . ARG B 2 1197 ? 128.559 155.307 79.421  1.00 53.82  ? 1194 ARG A C     1 
ATOM   9641  O O     . ARG B 2 1197 ? 127.847 156.223 79.849  1.00 53.82  ? 1194 ARG A O     1 
ATOM   9642  C CB    . ARG B 2 1197 ? 130.739 156.158 78.537  1.00 53.82  ? 1194 ARG A CB    1 
ATOM   9643  C CG    . ARG B 2 1197 ? 131.762 157.161 79.042  1.00 53.82  ? 1194 ARG A CG    1 
ATOM   9644  C CD    . ARG B 2 1197 ? 133.107 156.503 79.290  1.00 53.82  ? 1194 ARG A CD    1 
ATOM   9645  N NE    . ARG B 2 1197 ? 134.064 157.431 79.879  1.00 53.82  ? 1194 ARG A NE    1 
ATOM   9646  C CZ    . ARG B 2 1197 ? 135.376 157.238 79.907  1.00 53.82  ? 1194 ARG A CZ    1 
ATOM   9647  N NH1   . ARG B 2 1197 ? 135.927 156.159 79.376  1.00 53.82  ? 1194 ARG A NH1   1 
ATOM   9648  N NH2   . ARG B 2 1197 ? 136.154 158.150 80.483  1.00 53.82  ? 1194 ARG A NH2   1 
ATOM   9649  N N     . ASP B 2 1198 ? 128.056 154.265 78.758  1.00 53.44  ? 1195 ASP A N     1 
ATOM   9650  C CA    . ASP B 2 1198 ? 126.627 154.155 78.492  1.00 53.44  ? 1195 ASP A CA    1 
ATOM   9651  C C     . ASP B 2 1198 ? 125.810 153.868 79.744  1.00 53.44  ? 1195 ASP A C     1 
ATOM   9652  O O     . ASP B 2 1198 ? 124.578 153.937 79.685  1.00 53.44  ? 1195 ASP A O     1 
ATOM   9653  C CB    . ASP B 2 1198 ? 126.371 153.068 77.446  1.00 53.44  ? 1195 ASP A CB    1 
ATOM   9654  C CG    . ASP B 2 1198 ? 126.920 151.714 77.861  1.00 53.44  ? 1195 ASP A CG    1 
ATOM   9655  O OD1   . ASP B 2 1198 ? 127.580 151.631 78.918  1.00 53.44  ? 1195 ASP A OD1   1 
ATOM   9656  O OD2   . ASP B 2 1198 ? 126.689 150.731 77.127  1.00 53.44  ? 1195 ASP A OD2   1 
ATOM   9657  N N     . GLY B 2 1199 ? 126.455 153.549 80.863  1.00 54.09  ? 1196 GLY A N     1 
ATOM   9658  C CA    . GLY B 2 1199 ? 125.737 153.191 82.067  1.00 54.09  ? 1196 GLY A CA    1 
ATOM   9659  C C     . GLY B 2 1199 ? 125.251 151.762 82.113  1.00 54.09  ? 1196 GLY A C     1 
ATOM   9660  O O     . GLY B 2 1199 ? 124.410 151.437 82.958  1.00 54.09  ? 1196 GLY A O     1 
ATOM   9661  N N     . SER B 2 1200 ? 125.745 150.901 81.229  1.00 51.09  ? 1197 SER A N     1 
ATOM   9662  C CA    . SER B 2 1200 ? 125.307 149.517 81.199  1.00 51.09  ? 1197 SER A CA    1 
ATOM   9663  C C     . SER B 2 1200 ? 125.919 148.728 82.352  1.00 51.09  ? 1197 SER A C     1 
ATOM   9664  O O     . SER B 2 1200 ? 126.873 149.160 83.005  1.00 51.09  ? 1197 SER A O     1 
ATOM   9665  C CB    . SER B 2 1200 ? 125.677 148.867 79.866  1.00 51.09  ? 1197 SER A CB    1 
ATOM   9666  O OG    . SER B 2 1200 ? 125.283 147.507 79.836  1.00 51.09  ? 1197 SER A OG    1 
ATOM   9667  N N     . ASN B 2 1201 ? 125.344 147.555 82.601  1.00 49.10  ? 1198 ASN A N     1 
ATOM   9668  C CA    . ASN B 2 1201 ? 125.855 146.668 83.636  1.00 49.10  ? 1198 ASN A CA    1 
ATOM   9669  C C     . ASN B 2 1201 ? 127.268 146.212 83.296  1.00 49.10  ? 1198 ASN A C     1 
ATOM   9670  O O     . ASN B 2 1201 ? 127.587 145.932 82.138  1.00 49.10  ? 1198 ASN A O     1 
ATOM   9671  C CB    . ASN B 2 1201 ? 124.931 145.462 83.789  1.00 49.10  ? 1198 ASN A CB    1 
ATOM   9672  C CG    . ASN B 2 1201 ? 123.694 145.774 84.602  1.00 49.10  ? 1198 ASN A CG    1 
ATOM   9673  O OD1   . ASN B 2 1201 ? 123.232 146.915 84.639  1.00 49.10  ? 1198 ASN A OD1   1 
ATOM   9674  N ND2   . ASN B 2 1201 ? 123.139 144.756 85.248  1.00 49.10  ? 1198 ASN A ND2   1 
ATOM   9675  N N     . ILE B 2 1202 ? 128.118 146.138 84.318  1.00 52.96  ? 1199 ILE A N     1 
ATOM   9676  C CA    . ILE B 2 1202 ? 129.527 145.813 84.122  1.00 52.96  ? 1199 ILE A CA    1 
ATOM   9677  C C     . ILE B 2 1202 ? 129.784 144.362 84.509  1.00 52.96  ? 1199 ILE A C     1 
ATOM   9678  O O     . ILE B 2 1202 ? 130.608 143.680 83.888  1.00 52.96  ? 1199 ILE A O     1 
ATOM   9679  C CB    . ILE B 2 1202 ? 130.425 146.774 84.923  1.00 52.96  ? 1199 ILE A CB    1 
ATOM   9680  C CG1   . ILE B 2 1202 ? 130.172 148.217 84.487  1.00 52.96  ? 1199 ILE A CG1   1 
ATOM   9681  C CG2   . ILE B 2 1202 ? 131.891 146.430 84.730  1.00 52.96  ? 1199 ILE A CG2   1 
ATOM   9682  C CD1   . ILE B 2 1202 ? 130.478 148.474 83.029  1.00 52.96  ? 1199 ILE A CD1   1 
ATOM   9683  N N     . LEU B 2 1203 ? 129.078 143.878 85.532  1.00 53.97  ? 1200 LEU A N     1 
ATOM   9684  C CA    . LEU B 2 1203 ? 129.258 142.493 85.966  1.00 53.97  ? 1200 LEU A CA    1 
ATOM   9685  C C     . LEU B 2 1203 ? 128.932 141.472 84.883  1.00 53.97  ? 1200 LEU A C     1 
ATOM   9686  O O     . LEU B 2 1203 ? 129.724 140.530 84.704  1.00 53.97  ? 1200 LEU A O     1 
ATOM   9687  C CB    . LEU B 2 1203 ? 128.444 142.229 87.239  1.00 53.97  ? 1200 LEU A CB    1 
ATOM   9688  C CG    . LEU B 2 1203 ? 129.059 142.624 88.583  1.00 53.97  ? 1200 LEU A CG    1 
ATOM   9689  C CD1   . LEU B 2 1203 ? 130.300 141.793 88.807  1.00 53.97  ? 1200 LEU A CD1   1 
ATOM   9690  C CD2   . LEU B 2 1203 ? 129.392 144.096 88.673  1.00 53.97  ? 1200 LEU A CD2   1 
ATOM   9691  N N     . PRO B 2 1204 ? 127.813 141.563 84.152  1.00 53.26  ? 1201 PRO A N     1 
ATOM   9692  C CA    . PRO B 2 1204 ? 127.603 140.599 83.058  1.00 53.26  ? 1201 PRO A CA    1 
ATOM   9693  C C     . PRO B 2 1204 ? 128.694 140.642 82.004  1.00 53.26  ? 1201 PRO A C     1 
ATOM   9694  O O     . PRO B 2 1204 ? 129.015 139.606 81.409  1.00 53.26  ? 1201 PRO A O     1 
ATOM   9695  C CB    . PRO B 2 1204 ? 126.236 141.006 82.489  1.00 53.26  ? 1201 PRO A CB    1 
ATOM   9696  C CG    . PRO B 2 1204 ? 125.561 141.715 83.600  1.00 53.26  ? 1201 PRO A CG    1 
ATOM   9697  C CD    . PRO B 2 1204 ? 126.643 142.440 84.331  1.00 53.26  ? 1201 PRO A CD    1 
ATOM   9698  N N     . LYS B 2 1205 ? 129.276 141.817 81.753  1.00 53.90  ? 1202 LYS A N     1 
ATOM   9699  C CA    . LYS B 2 1205 ? 130.357 141.906 80.777  1.00 53.90  ? 1202 LYS A CA    1 
ATOM   9700  C C     . LYS B 2 1205 ? 131.630 141.247 81.293  1.00 53.90  ? 1202 LYS A C     1 
ATOM   9701  O O     . LYS B 2 1205 ? 132.305 140.528 80.549  1.00 53.90  ? 1202 LYS A O     1 
ATOM   9702  C CB    . LYS B 2 1205 ? 130.614 143.366 80.409  1.00 53.90  ? 1202 LYS A CB    1 
ATOM   9703  C CG    . LYS B 2 1205 ? 129.355 144.148 80.085  1.00 53.90  ? 1202 LYS A CG    1 
ATOM   9704  C CD    . LYS B 2 1205 ? 129.605 145.158 78.979  1.00 53.90  ? 1202 LYS A CD    1 
ATOM   9705  C CE    . LYS B 2 1205 ? 128.683 146.356 79.110  1.00 53.90  ? 1202 LYS A CE    1 
ATOM   9706  N NZ    . LYS B 2 1205 ? 127.251 145.949 79.099  1.00 53.90  ? 1202 LYS A NZ    1 
ATOM   9707  N N     . LEU B 2 1206 ? 131.979 141.483 82.560  1.00 55.48  ? 1203 LEU A N     1 
ATOM   9708  C CA    . LEU B 2 1206 ? 133.168 140.851 83.123  1.00 55.48  ? 1203 LEU A CA    1 
ATOM   9709  C C     . LEU B 2 1206 ? 133.016 139.337 83.173  1.00 55.48  ? 1203 LEU A C     1 
ATOM   9710  O O     . LEU B 2 1206 ? 133.959 138.600 82.864  1.00 55.48  ? 1203 LEU A O     1 
ATOM   9711  C CB    . LEU B 2 1206 ? 133.454 141.402 84.520  1.00 55.48  ? 1203 LEU A CB    1 
ATOM   9712  C CG    . LEU B 2 1206 ? 133.911 142.856 84.629  1.00 55.48  ? 1203 LEU A CG    1 
ATOM   9713  C CD1   . LEU B 2 1206 ? 133.523 143.428 85.982  1.00 55.48  ? 1203 LEU A CD1   1 
ATOM   9714  C CD2   . LEU B 2 1206 ? 135.409 142.966 84.406  1.00 55.48  ? 1203 LEU A CD2   1 
ATOM   9715  N N     . LEU B 2 1207 ? 131.835 138.856 83.568  1.00 57.19  ? 1204 LEU A N     1 
ATOM   9716  C CA    . LEU B 2 1207 ? 131.614 137.416 83.655  1.00 57.19  ? 1204 LEU A CA    1 
ATOM   9717  C C     . LEU B 2 1207 ? 131.686 136.759 82.283  1.00 57.19  ? 1204 LEU A C     1 
ATOM   9718  O O     . LEU B 2 1207 ? 132.264 135.676 82.139  1.00 57.19  ? 1204 LEU A O     1 
ATOM   9719  C CB    . LEU B 2 1207 ? 130.271 137.128 84.325  1.00 57.19  ? 1204 LEU A CB    1 
ATOM   9720  C CG    . LEU B 2 1207 ? 130.294 136.904 85.840  1.00 57.19  ? 1204 LEU A CG    1 
ATOM   9721  C CD1   . LEU B 2 1207 ? 131.102 135.661 86.183  1.00 57.19  ? 1204 LEU A CD1   1 
ATOM   9722  C CD2   . LEU B 2 1207 ? 130.834 138.118 86.583  1.00 57.19  ? 1204 LEU A CD2   1 
ATOM   9723  N N     . GLU B 2 1208 ? 131.103 137.390 81.262  1.00 61.56  ? 1205 GLU A N     1 
ATOM   9724  C CA    . GLU B 2 1208 ? 131.180 136.836 79.917  1.00 61.56  ? 1205 GLU A CA    1 
ATOM   9725  C C     . GLU B 2 1208 ? 132.545 137.047 79.276  1.00 61.56  ? 1205 GLU A C     1 
ATOM   9726  O O     . GLU B 2 1208 ? 132.907 136.296 78.364  1.00 61.56  ? 1205 GLU A O     1 
ATOM   9727  C CB    . GLU B 2 1208 ? 130.084 137.431 79.027  1.00 61.56  ? 1205 GLU A CB    1 
ATOM   9728  C CG    . GLU B 2 1208 ? 130.333 138.857 78.564  1.00 61.56  ? 1205 GLU A CG    1 
ATOM   9729  C CD    . GLU B 2 1208 ? 129.056 139.554 78.133  1.00 61.56  ? 1205 GLU A CD    1 
ATOM   9730  O OE1   . GLU B 2 1208 ? 128.056 138.854 77.871  1.00 61.56  ? 1205 GLU A OE1   1 
ATOM   9731  O OE2   . GLU B 2 1208 ? 129.054 140.800 78.048  1.00 61.56  ? 1205 GLU A OE2   1 
ATOM   9732  N N     . ASN B 2 1209 ? 133.304 138.051 79.724  1.00 60.44  ? 1206 ASN A N     1 
ATOM   9733  C CA    . ASN B 2 1209 ? 134.659 138.233 79.214  1.00 60.44  ? 1206 ASN A CA    1 
ATOM   9734  C C     . ASN B 2 1209 ? 135.568 137.090 79.652  1.00 60.44  ? 1206 ASN A C     1 
ATOM   9735  O O     . ASN B 2 1209 ? 136.417 136.634 78.877  1.00 60.44  ? 1206 ASN A O     1 
ATOM   9736  C CB    . ASN B 2 1209 ? 135.220 139.576 79.679  1.00 60.44  ? 1206 ASN A CB    1 
ATOM   9737  C CG    . ASN B 2 1209 ? 136.409 140.027 78.857  1.00 60.44  ? 1206 ASN A CG    1 
ATOM   9738  O OD1   . ASN B 2 1209 ? 136.806 139.362 77.900  1.00 60.44  ? 1206 ASN A OD1   1 
ATOM   9739  N ND2   . ASN B 2 1209 ? 136.987 141.164 79.227  1.00 60.44  ? 1206 ASN A ND2   1 
ATOM   9740  N N     . ASP B 2 1210 ? 135.401 136.620 80.890  1.00 62.52  ? 1207 ASP A N     1 
ATOM   9741  C CA    . ASP B 2 1210 ? 136.135 135.473 81.426  1.00 62.52  ? 1207 ASP A CA    1 
ATOM   9742  C C     . ASP B 2 1210 ? 137.648 135.701 81.383  1.00 62.52  ? 1207 ASP A C     1 
ATOM   9743  O O     . ASP B 2 1210 ? 138.392 135.014 80.680  1.00 62.52  ? 1207 ASP A O     1 
ATOM   9744  C CB    . ASP B 2 1210 ? 135.748 134.184 80.692  1.00 62.52  ? 1207 ASP A CB    1 
ATOM   9745  C CG    . ASP B 2 1210 ? 134.536 133.510 81.302  1.00 62.52  ? 1207 ASP A CG    1 
ATOM   9746  O OD1   . ASP B 2 1210 ? 134.251 133.766 82.491  1.00 62.52  ? 1207 ASP A OD1   1 
ATOM   9747  O OD2   . ASP B 2 1210 ? 133.868 132.727 80.594  1.00 62.52  ? 1207 ASP A OD2   1 
ATOM   9748  N N     . ASP B 2 1211 ? 138.094 136.692 82.152  1.00 59.14  ? 1208 ASP A N     1 
ATOM   9749  C CA    . ASP B 2 1211 ? 139.513 136.945 82.365  1.00 59.14  ? 1208 ASP A CA    1 
ATOM   9750  C C     . ASP B 2 1211 ? 139.814 136.788 83.848  1.00 59.14  ? 1208 ASP A C     1 
ATOM   9751  O O     . ASP B 2 1211 ? 139.138 137.390 84.688  1.00 59.14  ? 1208 ASP A O     1 
ATOM   9752  C CB    . ASP B 2 1211 ? 139.916 138.336 81.874  1.00 59.14  ? 1208 ASP A CB    1 
ATOM   9753  C CG    . ASP B 2 1211 ? 141.420 138.496 81.753  1.00 59.14  ? 1208 ASP A CG    1 
ATOM   9754  O OD1   . ASP B 2 1211 ? 142.151 137.541 82.092  1.00 59.14  ? 1208 ASP A OD1   1 
ATOM   9755  O OD2   . ASP B 2 1211 ? 141.874 139.571 81.312  1.00 59.14  ? 1208 ASP A OD2   1 
ATOM   9756  N N     . SER B 2 1212 ? 140.825 135.976 84.163  1.00 55.96  ? 1209 SER A N     1 
ATOM   9757  C CA    . SER B 2 1212 ? 141.175 135.727 85.557  1.00 55.96  ? 1209 SER A CA    1 
ATOM   9758  C C     . SER B 2 1212 ? 141.686 136.988 86.241  1.00 55.96  ? 1209 SER A C     1 
ATOM   9759  O O     . SER B 2 1212 ? 141.387 137.230 87.415  1.00 55.96  ? 1209 SER A O     1 
ATOM   9760  C CB    . SER B 2 1212 ? 142.218 134.612 85.644  1.00 55.96  ? 1209 SER A CB    1 
ATOM   9761  O OG    . SER B 2 1212 ? 142.280 134.072 86.952  1.00 55.96  ? 1209 SER A OG    1 
ATOM   9762  N N     . HIS B 2 1213 ? 142.474 137.798 85.530  1.00 55.63  ? 1210 HIS A N     1 
ATOM   9763  C CA    . HIS B 2 1213 ? 143.057 138.983 86.151  1.00 55.63  ? 1210 HIS A CA    1 
ATOM   9764  C C     . HIS B 2 1213 ? 141.993 140.023 86.479  1.00 55.63  ? 1210 HIS A C     1 
ATOM   9765  O O     . HIS B 2 1213 ? 142.001 140.606 87.569  1.00 55.63  ? 1210 HIS A O     1 
ATOM   9766  C CB    . HIS B 2 1213 ? 144.130 139.581 85.242  1.00 55.63  ? 1210 HIS A CB    1 
ATOM   9767  C CG    . HIS B 2 1213 ? 144.983 140.610 85.915  1.00 55.63  ? 1210 HIS A CG    1 
ATOM   9768  N ND1   . HIS B 2 1213 ? 145.682 140.353 87.075  1.00 55.63  ? 1210 HIS A ND1   1 
ATOM   9769  C CD2   . HIS B 2 1213 ? 145.249 141.898 85.593  1.00 55.63  ? 1210 HIS A CD2   1 
ATOM   9770  C CE1   . HIS B 2 1213 ? 146.342 141.438 87.438  1.00 55.63  ? 1210 HIS A CE1   1 
ATOM   9771  N NE2   . HIS B 2 1213 ? 146.097 142.390 86.555  1.00 55.63  ? 1210 HIS A NE2   1 
ATOM   9772  N N     . ALA B 2 1214 ? 141.071 140.274 85.546  1.00 49.26  ? 1211 ALA A N     1 
ATOM   9773  C CA    . ALA B 2 1214 ? 140.034 141.273 85.784  1.00 49.26  ? 1211 ALA A CA    1 
ATOM   9774  C C     . ALA B 2 1214 ? 139.091 140.841 86.899  1.00 49.26  ? 1211 ALA A C     1 
ATOM   9775  O O     . ALA B 2 1214 ? 138.708 141.656 87.747  1.00 49.26  ? 1211 ALA A O     1 
ATOM   9776  C CB    . ALA B 2 1214 ? 139.255 141.539 84.497  1.00 49.26  ? 1211 ALA A CB    1 
ATOM   9777  N N     . ILE B 2 1215 ? 138.701 139.565 86.915  1.00 51.62  ? 1212 ILE A N     1 
ATOM   9778  C CA    . ILE B 2 1215 ? 137.804 139.081 87.960  1.00 51.62  ? 1212 ILE A CA    1 
ATOM   9779  C C     . ILE B 2 1215 ? 138.507 139.094 89.313  1.00 51.62  ? 1212 ILE A C     1 
ATOM   9780  O O     . ILE B 2 1215 ? 137.880 139.332 90.351  1.00 51.62  ? 1212 ILE A O     1 
ATOM   9781  C CB    . ILE B 2 1215 ? 137.261 137.684 87.600  1.00 51.62  ? 1212 ILE A CB    1 
ATOM   9782  C CG1   . ILE B 2 1215 ? 136.028 137.349 88.440  1.00 51.62  ? 1212 ILE A CG1   1 
ATOM   9783  C CG2   . ILE B 2 1215 ? 138.316 136.613 87.782  1.00 51.62  ? 1212 ILE A CG2   1 
ATOM   9784  C CD1   . ILE B 2 1215 ? 134.832 138.208 88.123  1.00 51.62  ? 1212 ILE A CD1   1 
ATOM   9785  N N     . ASP B 2 1216 ? 139.818 138.837 89.325  1.00 50.91  ? 1213 ASP A N     1 
ATOM   9786  C CA    . ASP B 2 1216 ? 140.568 138.869 90.577  1.00 50.91  ? 1213 ASP A CA    1 
ATOM   9787  C C     . ASP B 2 1216 ? 140.750 140.295 91.078  1.00 50.91  ? 1213 ASP A C     1 
ATOM   9788  O O     . ASP B 2 1216 ? 140.563 140.571 92.268  1.00 50.91  ? 1213 ASP A O     1 
ATOM   9789  C CB    . ASP B 2 1216 ? 141.925 138.190 90.392  1.00 50.91  ? 1213 ASP A CB    1 
ATOM   9790  C CG    . ASP B 2 1216 ? 142.702 138.076 91.688  1.00 50.91  ? 1213 ASP A CG    1 
ATOM   9791  O OD1   . ASP B 2 1216 ? 142.385 137.182 92.498  1.00 50.91  ? 1213 ASP A OD1   1 
ATOM   9792  O OD2   . ASP B 2 1216 ? 143.635 138.881 91.895  1.00 50.91  ? 1213 ASP A OD2   1 
ATOM   9793  N N     . THR B 2 1217 ? 141.120 141.214 90.184  1.00 48.55  ? 1214 THR A N     1 
ATOM   9794  C CA    . THR B 2 1217 ? 141.373 142.588 90.602  1.00 48.55  ? 1214 THR A CA    1 
ATOM   9795  C C     . THR B 2 1217 ? 140.094 143.270 91.071  1.00 48.55  ? 1214 THR A C     1 
ATOM   9796  O O     . THR B 2 1217 ? 140.120 144.061 92.020  1.00 48.55  ? 1214 THR A O     1 
ATOM   9797  C CB    . THR B 2 1217 ? 142.013 143.377 89.462  1.00 48.55  ? 1214 THR A CB    1 
ATOM   9798  O OG1   . THR B 2 1217 ? 143.007 142.568 88.819  1.00 48.55  ? 1214 THR A OG1   1 
ATOM   9799  C CG2   . THR B 2 1217 ? 142.668 144.641 89.995  1.00 48.55  ? 1214 THR A CG2   1 
ATOM   9800  N N     . MET B 2 1218 ? 138.964 142.971 90.424  1.00 48.55  ? 1215 MET A N     1 
ATOM   9801  C CA    . MET B 2 1218 ? 137.707 143.613 90.797  1.00 48.55  ? 1215 MET A CA    1 
ATOM   9802  C C     . MET B 2 1218 ? 137.304 143.258 92.223  1.00 48.55  ? 1215 MET A C     1 
ATOM   9803  O O     . MET B 2 1218 ? 136.791 144.109 92.959  1.00 48.55  ? 1215 MET A O     1 
ATOM   9804  C CB    . MET B 2 1218 ? 136.605 143.223 89.814  1.00 48.55  ? 1215 MET A CB    1 
ATOM   9805  C CG    . MET B 2 1218 ? 135.263 143.872 90.101  1.00 48.55  ? 1215 MET A CG    1 
ATOM   9806  S SD    . MET B 2 1218 ? 135.094 145.509 89.373  1.00 48.55  ? 1215 MET A SD    1 
ATOM   9807  C CE    . MET B 2 1218 ? 135.038 146.525 90.847  1.00 48.55  ? 1215 MET A CE    1 
ATOM   9808  N N     . VAL B 2 1219 ? 137.525 142.007 92.631  1.00 48.55  ? 1216 VAL A N     1 
ATOM   9809  C CA    . VAL B 2 1219 ? 137.198 141.604 93.996  1.00 48.55  ? 1216 VAL A CA    1 
ATOM   9810  C C     . VAL B 2 1219 ? 138.042 142.383 94.996  1.00 48.55  ? 1216 VAL A C     1 
ATOM   9811  O O     . VAL B 2 1219 ? 137.550 142.806 96.050  1.00 48.55  ? 1216 VAL A O     1 
ATOM   9812  C CB    . VAL B 2 1219 ? 137.374 140.083 94.164  1.00 48.55  ? 1216 VAL A CB    1 
ATOM   9813  C CG1   . VAL B 2 1219 ? 137.138 139.676 95.609  1.00 48.55  ? 1216 VAL A CG1   1 
ATOM   9814  C CG2   . VAL B 2 1219 ? 136.426 139.337 93.241  1.00 48.55  ? 1216 VAL A CG2   1 
ATOM   9815  N N     . ALA B 2 1220 ? 139.323 142.587 94.683  1.00 48.55  ? 1217 ALA A N     1 
ATOM   9816  C CA    . ALA B 2 1220 ? 140.177 143.387 95.555  1.00 48.55  ? 1217 ALA A CA    1 
ATOM   9817  C C     . ALA B 2 1220 ? 139.689 144.828 95.635  1.00 48.55  ? 1217 ALA A C     1 
ATOM   9818  O O     . ALA B 2 1220 ? 139.816 145.478 96.679  1.00 48.55  ? 1217 ALA A O     1 
ATOM   9819  C CB    . ALA B 2 1220 ? 141.624 143.335 95.065  1.00 48.55  ? 1217 ALA A CB    1 
ATOM   9820  N N     . LEU B 2 1221 ? 139.140 145.352 94.536  1.00 48.55  ? 1218 LEU A N     1 
ATOM   9821  C CA    . LEU B 2 1221 ? 138.559 146.690 94.573  1.00 48.55  ? 1218 LEU A CA    1 
ATOM   9822  C C     . LEU B 2 1221 ? 137.318 146.730 95.456  1.00 48.55  ? 1218 LEU A C     1 
ATOM   9823  O O     . LEU B 2 1221 ? 137.107 147.700 96.194  1.00 48.55  ? 1218 LEU A O     1 
ATOM   9824  C CB    . LEU B 2 1221 ? 138.235 147.167 93.158  1.00 48.55  ? 1218 LEU A CB    1 
ATOM   9825  C CG    . LEU B 2 1221 ? 139.329 147.950 92.424  1.00 48.55  ? 1218 LEU A CG    1 
ATOM   9826  C CD1   . LEU B 2 1221 ? 139.624 149.241 93.160  1.00 48.55  ? 1218 LEU A CD1   1 
ATOM   9827  C CD2   . LEU B 2 1221 ? 140.601 147.140 92.251  1.00 48.55  ? 1218 LEU A CD2   1 
ATOM   9828  N N     . ILE B 2 1222 ? 136.479 145.693 95.389  1.00 48.55  ? 1219 ILE A N     1 
ATOM   9829  C CA    . ILE B 2 1222 ? 135.348 145.596 96.308  1.00 48.55  ? 1219 ILE A CA    1 
ATOM   9830  C C     . ILE B 2 1222 ? 135.846 145.459 97.739  1.00 48.55  ? 1219 ILE A C     1 
ATOM   9831  O O     . ILE B 2 1222 ? 135.255 146.008 98.676  1.00 48.55  ? 1219 ILE A O     1 
ATOM   9832  C CB    . ILE B 2 1222 ? 134.431 144.424 95.912  1.00 48.55  ? 1219 ILE A CB    1 
ATOM   9833  C CG1   . ILE B 2 1222 ? 133.992 144.557 94.454  1.00 48.55  ? 1219 ILE A CG1   1 
ATOM   9834  C CG2   . ILE B 2 1222 ? 133.216 144.367 96.823  1.00 48.55  ? 1219 ILE A CG2   1 
ATOM   9835  C CD1   . ILE B 2 1222 ? 133.110 145.747 94.191  1.00 48.55  ? 1219 ILE A CD1   1 
ATOM   9836  N N     . ARG B 2 1223 ? 136.942 144.723 97.928  1.00 48.55  ? 1220 ARG A N     1 
ATOM   9837  C CA    . ARG B 2 1223 ? 137.597 144.669 99.231  1.00 48.55  ? 1220 ARG A CA    1 
ATOM   9838  C C     . ARG B 2 1223 ? 137.990 146.062 99.701  1.00 48.55  ? 1220 ARG A C     1 
ATOM   9839  O O     . ARG B 2 1223 ? 137.866 146.392 100.886 1.00 48.55  ? 1220 ARG A O     1 
ATOM   9840  C CB    . ARG B 2 1223 ? 138.828 143.764 99.149  1.00 48.55  ? 1220 ARG A CB    1 
ATOM   9841  C CG    . ARG B 2 1223 ? 139.651 143.686 100.422 1.00 48.55  ? 1220 ARG A CG    1 
ATOM   9842  C CD    . ARG B 2 1223 ? 139.266 142.486 101.256 1.00 48.55  ? 1220 ARG A CD    1 
ATOM   9843  N NE    . ARG B 2 1223 ? 140.003 142.433 102.513 1.00 48.55  ? 1220 ARG A NE    1 
ATOM   9844  C CZ    . ARG B 2 1223 ? 141.088 141.699 102.715 1.00 48.55  ? 1220 ARG A CZ    1 
ATOM   9845  N NH1   . ARG B 2 1223 ? 141.595 140.938 101.759 1.00 48.55  ? 1220 ARG A NH1   1 
ATOM   9846  N NH2   . ARG B 2 1223 ? 141.679 141.728 103.906 1.00 48.55  ? 1220 ARG A NH2   1 
ATOM   9847  N N     . SER B 2 1224 ? 138.467 146.896 98.778  1.00 48.55  ? 1221 SER A N     1 
ATOM   9848  C CA    . SER B 2 1224 ? 138.971 148.212 99.151  1.00 48.55  ? 1221 SER A CA    1 
ATOM   9849  C C     . SER B 2 1224 ? 137.838 149.158 99.527  1.00 48.55  ? 1221 SER A C     1 
ATOM   9850  O O     . SER B 2 1224 ? 137.924 149.872 100.533 1.00 48.55  ? 1221 SER A O     1 
ATOM   9851  C CB    . SER B 2 1224 ? 139.793 148.787 98.001  1.00 48.55  ? 1221 SER A CB    1 
ATOM   9852  O OG    . SER B 2 1224 ? 140.999 148.064 97.850  1.00 48.55  ? 1221 SER A OG    1 
ATOM   9853  N N     . VAL B 2 1225 ? 136.769 149.180 98.728  1.00 48.55  ? 1222 VAL A N     1 
ATOM   9854  C CA    . VAL B 2 1225 ? 135.659 150.092 98.989  1.00 48.55  ? 1222 VAL A CA    1 
ATOM   9855  C C     . VAL B 2 1225 ? 134.987 149.755 100.312 1.00 48.55  ? 1222 VAL A C     1 
ATOM   9856  O O     . VAL B 2 1225 ? 134.659 150.647 101.104 1.00 48.55  ? 1222 VAL A O     1 
ATOM   9857  C CB    . VAL B 2 1225 ? 134.661 150.060 97.819  1.00 48.55  ? 1222 VAL A CB    1 
ATOM   9858  C CG1   . VAL B 2 1225 ? 133.412 150.852 98.162  1.00 48.55  ? 1222 VAL A CG1   1 
ATOM   9859  C CG2   . VAL B 2 1225 ? 135.310 150.604 96.565  1.00 48.55  ? 1222 VAL A CG2   1 
ATOM   9860  N N     . LEU B 2 1226 ? 134.777 148.466 100.578 1.00 48.55  ? 1223 LEU A N     1 
ATOM   9861  C CA    . LEU B 2 1226 ? 134.145 148.042 101.820 1.00 48.55  ? 1223 LEU A CA    1 
ATOM   9862  C C     . LEU B 2 1226 ? 135.019 148.287 103.043 1.00 48.55  ? 1223 LEU A C     1 
ATOM   9863  O O     . LEU B 2 1226 ? 134.510 148.218 104.166 1.00 48.55  ? 1223 LEU A O     1 
ATOM   9864  C CB    . LEU B 2 1226 ? 133.776 146.559 101.737 1.00 48.55  ? 1223 LEU A CB    1 
ATOM   9865  C CG    . LEU B 2 1226 ? 132.423 146.188 101.125 1.00 48.55  ? 1223 LEU A CG    1 
ATOM   9866  C CD1   . LEU B 2 1226 ? 131.307 146.785 101.946 1.00 48.55  ? 1223 LEU A CD1   1 
ATOM   9867  C CD2   . LEU B 2 1226 ? 132.302 146.625 99.674  1.00 48.55  ? 1223 LEU A CD2   1 
ATOM   9868  N N     . GLN B 2 1227 ? 136.307 148.570 102.858 1.00 48.55  ? 1224 GLN A N     1 
ATOM   9869  C CA    . GLN B 2 1227 ? 137.214 148.843 103.972 1.00 48.55  ? 1224 GLN A CA    1 
ATOM   9870  C C     . GLN B 2 1227 ? 137.000 150.280 104.426 1.00 48.55  ? 1224 GLN A C     1 
ATOM   9871  O O     . GLN B 2 1227 ? 137.567 151.225 103.875 1.00 48.55  ? 1224 GLN A O     1 
ATOM   9872  C CB    . GLN B 2 1227 ? 138.661 148.597 103.566 1.00 48.55  ? 1224 GLN A CB    1 
ATOM   9873  C CG    . GLN B 2 1227 ? 139.669 148.925 104.656 1.00 48.55  ? 1224 GLN A CG    1 
ATOM   9874  C CD    . GLN B 2 1227 ? 141.082 148.530 104.284 1.00 48.55  ? 1224 GLN A CD    1 
ATOM   9875  O OE1   . GLN B 2 1227 ? 141.403 148.365 103.108 1.00 48.55  ? 1224 GLN A OE1   1 
ATOM   9876  N NE2   . GLN B 2 1227 ? 141.938 148.379 105.287 1.00 48.55  ? 1224 GLN A NE2   1 
ATOM   9877  N N     . MET B 2 1228 ? 136.157 150.447 105.446 1.00 48.55  ? 1225 MET A N     1 
ATOM   9878  C CA    . MET B 2 1228 ? 135.897 151.780 105.977 1.00 48.55  ? 1225 MET A CA    1 
ATOM   9879  C C     . MET B 2 1228 ? 137.105 152.328 106.726 1.00 48.55  ? 1225 MET A C     1 
ATOM   9880  O O     . MET B 2 1228 ? 137.417 153.519 106.625 1.00 48.55  ? 1225 MET A O     1 
ATOM   9881  C CB    . MET B 2 1228 ? 134.668 151.746 106.885 1.00 48.55  ? 1225 MET A CB    1 
ATOM   9882  C CG    . MET B 2 1228 ? 133.357 151.635 106.131 1.00 48.55  ? 1225 MET A CG    1 
ATOM   9883  S SD    . MET B 2 1228 ? 131.923 151.651 107.216 1.00 48.55  ? 1225 MET A SD    1 
ATOM   9884  C CE    . MET B 2 1228 ? 131.368 149.958 107.047 1.00 48.55  ? 1225 MET A CE    1 
ATOM   9885  N N     . ARG B 2 1229 ? 137.801 151.476 107.475 1.00 48.55  ? 1226 ARG A N     1 
ATOM   9886  C CA    . ARG B 2 1229 ? 138.926 151.915 108.291 1.00 48.55  ? 1226 ARG A CA    1 
ATOM   9887  C C     . ARG B 2 1229 ? 140.133 152.193 107.405 1.00 48.55  ? 1226 ARG A C     1 
ATOM   9888  O O     . ARG B 2 1229 ? 140.666 151.280 106.766 1.00 48.55  ? 1226 ARG A O     1 
ATOM   9889  C CB    . ARG B 2 1229 ? 139.263 150.856 109.338 1.00 48.55  ? 1226 ARG A CB    1 
ATOM   9890  C CG    . ARG B 2 1229 ? 140.183 151.338 110.441 1.00 48.55  ? 1226 ARG A CG    1 
ATOM   9891  C CD    . ARG B 2 1229 ? 139.552 152.484 111.207 1.00 48.55  ? 1226 ARG A CD    1 
ATOM   9892  N NE    . ARG B 2 1229 ? 140.411 152.971 112.279 1.00 48.55  ? 1226 ARG A NE    1 
ATOM   9893  C CZ    . ARG B 2 1229 ? 140.535 152.391 113.464 1.00 48.55  ? 1226 ARG A CZ    1 
ATOM   9894  N NH1   . ARG B 2 1229 ? 139.877 151.284 113.766 1.00 48.55  ? 1226 ARG A NH1   1 
ATOM   9895  N NH2   . ARG B 2 1229 ? 141.336 152.940 114.373 1.00 48.55  ? 1226 ARG A NH2   1 
ATOM   9896  N N     . ASN B 2 1230 ? 140.562 153.453 107.368 1.00 48.55  ? 1227 ASN A N     1 
ATOM   9897  C CA    . ASN B 2 1230 ? 141.739 153.868 106.613 1.00 48.55  ? 1227 ASN A CA    1 
ATOM   9898  C C     . ASN B 2 1230 ? 142.726 154.499 107.580 1.00 48.55  ? 1227 ASN A C     1 
ATOM   9899  O O     . ASN B 2 1230 ? 142.460 155.575 108.124 1.00 48.55  ? 1227 ASN A O     1 
ATOM   9900  C CB    . ASN B 2 1230 ? 141.369 154.859 105.506 1.00 48.55  ? 1227 ASN A CB    1 
ATOM   9901  C CG    . ASN B 2 1230 ? 140.420 154.269 104.481 1.00 48.55  ? 1227 ASN A CG    1 
ATOM   9902  O OD1   . ASN B 2 1230 ? 139.769 153.255 104.725 1.00 48.55  ? 1227 ASN A OD1   1 
ATOM   9903  N ND2   . ASN B 2 1230 ? 140.329 154.914 103.326 1.00 48.55  ? 1227 ASN A ND2   1 
ATOM   9904  N N     . SER B 2 1231 ? 143.862 153.839 107.790 1.00 48.55  ? 1228 SER A N     1 
ATOM   9905  C CA    . SER B 2 1231 ? 144.852 154.302 108.749 1.00 48.55  ? 1228 SER A CA    1 
ATOM   9906  C C     . SER B 2 1231 ? 146.240 154.248 108.132 1.00 48.55  ? 1228 SER A C     1 
ATOM   9907  O O     . SER B 2 1231 ? 146.617 153.246 107.520 1.00 48.55  ? 1228 SER A O     1 
ATOM   9908  C CB    . SER B 2 1231 ? 144.820 153.462 110.032 1.00 48.55  ? 1228 SER A CB    1 
ATOM   9909  O OG    . SER B 2 1231 ? 144.805 152.077 109.734 1.00 48.55  ? 1228 SER A OG    1 
ATOM   9910  N N     . ASN B 2 1232 ? 146.995 155.332 108.301 1.00 53.97  ? 1229 ASN A N     1 
ATOM   9911  C CA    . ASN B 2 1232 ? 148.380 155.409 107.841 1.00 53.97  ? 1229 ASN A CA    1 
ATOM   9912  C C     . ASN B 2 1232 ? 149.180 156.133 108.914 1.00 53.97  ? 1229 ASN A C     1 
ATOM   9913  O O     . ASN B 2 1232 ? 149.030 157.346 109.089 1.00 53.97  ? 1229 ASN A O     1 
ATOM   9914  C CB    . ASN B 2 1232 ? 148.485 156.129 106.497 1.00 53.97  ? 1229 ASN A CB    1 
ATOM   9915  C CG    . ASN B 2 1232 ? 149.868 156.024 105.885 1.00 53.97  ? 1229 ASN A CG    1 
ATOM   9916  O OD1   . ASN B 2 1232 ? 150.142 156.604 104.834 1.00 53.97  ? 1229 ASN A OD1   1 
ATOM   9917  N ND2   . ASN B 2 1232 ? 150.750 155.281 106.543 1.00 53.97  ? 1229 ASN A ND2   1 
ATOM   9918  N N     . ALA B 2 1233 ? 150.024 155.389 109.631 1.00 53.88  ? 1230 ALA A N     1 
ATOM   9919  C CA    . ALA B 2 1233 ? 150.759 155.969 110.751 1.00 53.88  ? 1230 ALA A CA    1 
ATOM   9920  C C     . ALA B 2 1233 ? 151.745 157.033 110.285 1.00 53.88  ? 1230 ALA A C     1 
ATOM   9921  O O     . ALA B 2 1233 ? 151.896 158.075 110.935 1.00 53.88  ? 1230 ALA A O     1 
ATOM   9922  C CB    . ALA B 2 1233 ? 151.484 154.870 111.527 1.00 53.88  ? 1230 ALA A CB    1 
ATOM   9923  N N     . ALA B 2 1234 ? 152.430 156.787 109.166 1.00 52.08  ? 1231 ALA A N     1 
ATOM   9924  C CA    . ALA B 2 1234 ? 153.484 157.697 108.727 1.00 52.08  ? 1231 ALA A CA    1 
ATOM   9925  C C     . ALA B 2 1234 ? 152.933 159.077 108.390 1.00 52.08  ? 1231 ALA A C     1 
ATOM   9926  O O     . ALA B 2 1234 ? 153.469 160.095 108.842 1.00 52.08  ? 1231 ALA A O     1 
ATOM   9927  C CB    . ALA B 2 1234 ? 154.219 157.105 107.525 1.00 52.08  ? 1231 ALA A CB    1 
ATOM   9928  N N     . THR B 2 1235 ? 151.864 159.134 107.602 1.00 54.35  ? 1232 THR A N     1 
ATOM   9929  C CA    . THR B 2 1235 ? 151.292 160.402 107.174 1.00 54.35  ? 1232 THR A CA    1 
ATOM   9930  C C     . THR B 2 1235 ? 150.162 160.883 108.077 1.00 54.35  ? 1232 THR A C     1 
ATOM   9931  O O     . THR B 2 1235 ? 149.596 161.951 107.822 1.00 54.35  ? 1232 THR A O     1 
ATOM   9932  C CB    . THR B 2 1235 ? 150.798 160.294 105.729 1.00 54.35  ? 1232 THR A CB    1 
ATOM   9933  O OG1   . THR B 2 1235 ? 149.982 159.125 105.587 1.00 54.35  ? 1232 THR A OG1   1 
ATOM   9934  C CG2   . THR B 2 1235 ? 151.976 160.204 104.769 1.00 54.35  ? 1232 THR A CG2   1 
ATOM   9935  N N     . GLY B 2 1236 ? 149.829 160.132 109.122 1.00 53.78  ? 1233 GLY A N     1 
ATOM   9936  C CA    . GLY B 2 1236 ? 148.873 160.598 110.116 1.00 53.78  ? 1233 GLY A CA    1 
ATOM   9937  C C     . GLY B 2 1236 ? 147.447 160.760 109.635 1.00 53.78  ? 1233 GLY A C     1 
ATOM   9938  O O     . GLY B 2 1236 ? 146.803 161.768 109.951 1.00 53.78  ? 1233 GLY A O     1 
ATOM   9939  N N     . GLU B 2 1237 ? 146.936 159.794 108.878 1.00 49.72  ? 1234 GLU A N     1 
ATOM   9940  C CA    . GLU B 2 1237 ? 145.524 159.743 108.523 1.00 49.72  ? 1234 GLU A CA    1 
ATOM   9941  C C     . GLU B 2 1237 ? 144.852 158.589 109.252 1.00 49.72  ? 1234 GLU A C     1 
ATOM   9942  O O     . GLU B 2 1237 ? 145.380 157.473 109.281 1.00 49.72  ? 1234 GLU A O     1 
ATOM   9943  C CB    . GLU B 2 1237 ? 145.316 159.592 107.013 1.00 49.72  ? 1234 GLU A CB    1 
ATOM   9944  C CG    . GLU B 2 1237 ? 145.821 160.751 106.174 1.00 49.72  ? 1234 GLU A CG    1 
ATOM   9945  C CD    . GLU B 2 1237 ? 147.268 160.601 105.780 1.00 49.72  ? 1234 GLU A CD    1 
ATOM   9946  O OE1   . GLU B 2 1237 ? 147.735 159.449 105.668 1.00 49.72  ? 1234 GLU A OE1   1 
ATOM   9947  O OE2   . GLU B 2 1237 ? 147.936 161.637 105.576 1.00 49.72  ? 1234 GLU A OE2   1 
ATOM   9948  N N     . ASP B 2 1238 ? 143.691 158.867 109.841 1.00 48.55  ? 1235 ASP A N     1 
ATOM   9949  C CA    . ASP B 2 1238 ? 142.867 157.829 110.454 1.00 48.55  ? 1235 ASP A CA    1 
ATOM   9950  C C     . ASP B 2 1238 ? 141.418 158.272 110.318 1.00 48.55  ? 1235 ASP A C     1 
ATOM   9951  O O     . ASP B 2 1238 ? 140.939 159.074 111.126 1.00 48.55  ? 1235 ASP A O     1 
ATOM   9952  C CB    . ASP B 2 1238 ? 143.248 157.612 111.912 1.00 48.55  ? 1235 ASP A CB    1 
ATOM   9953  C CG    . ASP B 2 1238 ? 142.815 156.255 112.429 1.00 48.55  ? 1235 ASP A CG    1 
ATOM   9954  O OD1   . ASP B 2 1238 ? 142.495 155.377 111.600 1.00 48.55  ? 1235 ASP A OD1   1 
ATOM   9955  O OD2   . ASP B 2 1238 ? 142.792 156.066 113.663 1.00 48.55  ? 1235 ASP A OD2   1 
ATOM   9956  N N     . TYR B 2 1239 ? 140.730 157.754 109.305 1.00 48.55  ? 1236 TYR A N     1 
ATOM   9957  C CA    . TYR B 2 1239 ? 139.386 158.205 108.984 1.00 48.55  ? 1236 TYR A CA    1 
ATOM   9958  C C     . TYR B 2 1239 ? 138.552 157.014 108.541 1.00 48.55  ? 1236 TYR A C     1 
ATOM   9959  O O     . TYR B 2 1239 ? 139.076 155.943 108.225 1.00 48.55  ? 1236 TYR A O     1 
ATOM   9960  C CB    . TYR B 2 1239 ? 139.406 159.283 107.896 1.00 48.55  ? 1236 TYR A CB    1 
ATOM   9961  C CG    . TYR B 2 1239 ? 139.907 158.796 106.554 1.00 48.55  ? 1236 TYR A CG    1 
ATOM   9962  C CD1   . TYR B 2 1239 ? 141.258 158.844 106.239 1.00 48.55  ? 1236 TYR A CD1   1 
ATOM   9963  C CD2   . TYR B 2 1239 ? 139.031 158.291 105.603 1.00 48.55  ? 1236 TYR A CD2   1 
ATOM   9964  C CE1   . TYR B 2 1239 ? 141.721 158.403 105.016 1.00 48.55  ? 1236 TYR A CE1   1 
ATOM   9965  C CE2   . TYR B 2 1239 ? 139.485 157.849 104.379 1.00 48.55  ? 1236 TYR A CE2   1 
ATOM   9966  C CZ    . TYR B 2 1239 ? 140.830 157.908 104.090 1.00 48.55  ? 1236 TYR A CZ    1 
ATOM   9967  O OH    . TYR B 2 1239 ? 141.287 157.466 102.872 1.00 48.55  ? 1236 TYR A OH    1 
ATOM   9968  N N     . ILE B 2 1240 ? 137.238 157.215 108.519 1.00 48.55  ? 1237 ILE A N     1 
ATOM   9969  C CA    . ILE B 2 1240 ? 136.299 156.226 108.007 1.00 48.55  ? 1237 ILE A CA    1 
ATOM   9970  C C     . ILE B 2 1240 ? 135.532 156.849 106.850 1.00 48.55  ? 1237 ILE A C     1 
ATOM   9971  O O     . ILE B 2 1240 ? 134.884 157.888 107.014 1.00 48.55  ? 1237 ILE A O     1 
ATOM   9972  C CB    . ILE B 2 1240 ? 135.333 155.724 109.098 1.00 48.55  ? 1237 ILE A CB    1 
ATOM   9973  C CG1   . ILE B 2 1240 ? 134.794 156.889 109.926 1.00 48.55  ? 1237 ILE A CG1   1 
ATOM   9974  C CG2   . ILE B 2 1240 ? 136.021 154.705 109.992 1.00 48.55  ? 1237 ILE A CG2   1 
ATOM   9975  C CD1   . ILE B 2 1240 ? 133.710 156.489 110.891 1.00 48.55  ? 1237 ILE A CD1   1 
ATOM   9976  N N     . ASN B 2 1241 ? 135.617 156.222 105.681 1.00 48.55  ? 1238 ASN A N     1 
ATOM   9977  C CA    . ASN B 2 1241 ? 134.876 156.647 104.503 1.00 48.55  ? 1238 ASN A CA    1 
ATOM   9978  C C     . ASN B 2 1241 ? 133.828 155.592 104.189 1.00 48.55  ? 1238 ASN A C     1 
ATOM   9979  O O     . ASN B 2 1241 ? 134.164 154.426 103.956 1.00 48.55  ? 1238 ASN A O     1 
ATOM   9980  C CB    . ASN B 2 1241 ? 135.807 156.859 103.307 1.00 48.55  ? 1238 ASN A CB    1 
ATOM   9981  C CG    . ASN B 2 1241 ? 135.131 157.591 102.164 1.00 48.55  ? 1238 ASN A CG    1 
ATOM   9982  O OD1   . ASN B 2 1241 ? 134.114 157.142 101.636 1.00 48.55  ? 1238 ASN A OD1   1 
ATOM   9983  N ND2   . ASN B 2 1241 ? 135.696 158.728 101.776 1.00 48.55  ? 1238 ASN A ND2   1 
ATOM   9984  N N     . SER B 2 1242 ? 132.573 156.000 104.186 1.00 48.55  ? 1239 SER A N     1 
ATOM   9985  C CA    . SER B 2 1242 ? 131.479 155.059 104.012 1.00 48.55  ? 1239 SER A CA    1 
ATOM   9986  C C     . SER B 2 1242 ? 131.390 154.600 102.560 1.00 48.55  ? 1239 SER A C     1 
ATOM   9987  O O     . SER B 2 1242 ? 131.669 155.378 101.643 1.00 48.55  ? 1239 SER A O     1 
ATOM   9988  C CB    . SER B 2 1242 ? 130.160 155.697 104.427 1.00 48.55  ? 1239 SER A CB    1 
ATOM   9989  O OG    . SER B 2 1242 ? 129.064 154.862 104.099 1.00 48.55  ? 1239 SER A OG    1 
ATOM   9990  N N     . PRO B 2 1243 ? 131.006 153.344 102.323 1.00 48.55  ? 1240 PRO A N     1 
ATOM   9991  C CA    . PRO B 2 1243 ? 130.760 152.884 100.955 1.00 48.55  ? 1240 PRO A CA    1 
ATOM   9992  C C     . PRO B 2 1243 ? 129.325 153.054 100.486 1.00 48.55  ? 1240 PRO A C     1 
ATOM   9993  O O     . PRO B 2 1243 ? 129.039 152.750 99.320  1.00 48.55  ? 1240 PRO A O     1 
ATOM   9994  C CB    . PRO B 2 1243 ? 131.129 151.399 101.036 1.00 48.55  ? 1240 PRO A CB    1 
ATOM   9995  C CG    . PRO B 2 1243 ? 130.751 151.015 102.426 1.00 48.55  ? 1240 PRO A CG    1 
ATOM   9996  C CD    . PRO B 2 1243 ? 130.937 152.239 103.295 1.00 48.55  ? 1240 PRO A CD    1 
ATOM   9997  N N     . VAL B 2 1244 ? 128.422 153.526 101.345 1.00 48.55  ? 1241 VAL A N     1 
ATOM   9998  C CA    . VAL B 2 1244 ? 127.016 153.671 100.998 1.00 48.55  ? 1241 VAL A CA    1 
ATOM   9999  C C     . VAL B 2 1244 ? 126.536 155.050 101.428 1.00 48.55  ? 1241 VAL A C     1 
ATOM   10000 O O     . VAL B 2 1244 ? 127.083 155.662 102.352 1.00 48.55  ? 1241 VAL A O     1 
ATOM   10001 C CB    . VAL B 2 1244 ? 126.153 152.559 101.638 1.00 48.55  ? 1241 VAL A CB    1 
ATOM   10002 C CG1   . VAL B 2 1244 ? 126.019 152.776 103.135 1.00 48.55  ? 1241 VAL A CG1   1 
ATOM   10003 C CG2   . VAL B 2 1244 ? 124.788 152.479 100.971 1.00 48.55  ? 1241 VAL A CG2   1 
ATOM   10004 N N     . ARG B 2 1245 ? 125.513 155.544 100.738 1.00 48.55  ? 1242 ARG A N     1 
ATOM   10005 C CA    . ARG B 2 1245 ? 124.930 156.847 101.014 1.00 48.55  ? 1242 ARG A CA    1 
ATOM   10006 C C     . ARG B 2 1245 ? 123.714 156.706 101.922 1.00 48.55  ? 1242 ARG A C     1 
ATOM   10007 O O     . ARG B 2 1245 ? 123.013 155.691 101.902 1.00 48.55  ? 1242 ARG A O     1 
ATOM   10008 C CB    . ARG B 2 1245 ? 124.538 157.539 99.708  1.00 48.55  ? 1242 ARG A CB    1 
ATOM   10009 C CG    . ARG B 2 1245 ? 123.389 156.866 98.972  1.00 48.55  ? 1242 ARG A CG    1 
ATOM   10010 C CD    . ARG B 2 1245 ? 123.051 157.589 97.679  1.00 48.55  ? 1242 ARG A CD    1 
ATOM   10011 N NE    . ARG B 2 1245 ? 124.147 157.523 96.720  1.00 48.55  ? 1242 ARG A NE    1 
ATOM   10012 C CZ    . ARG B 2 1245 ? 124.920 158.549 96.389  1.00 48.55  ? 1242 ARG A CZ    1 
ATOM   10013 N NH1   . ARG B 2 1245 ? 124.742 159.748 96.920  1.00 48.55  ? 1242 ARG A NH1   1 
ATOM   10014 N NH2   . ARG B 2 1245 ? 125.895 158.368 95.503  1.00 48.55  ? 1242 ARG A NH2   1 
ATOM   10015 N N     . ASP B 2 1246 ? 123.475 157.735 102.729 1.00 48.55  ? 1243 ASP A N     1 
ATOM   10016 C CA    . ASP B 2 1246 ? 122.343 157.742 103.642 1.00 48.55  ? 1243 ASP A CA    1 
ATOM   10017 C C     . ASP B 2 1246 ? 121.114 158.300 102.926 1.00 48.55  ? 1243 ASP A C     1 
ATOM   10018 O O     . ASP B 2 1246 ? 121.088 158.435 101.700 1.00 48.55  ? 1243 ASP A O     1 
ATOM   10019 C CB    . ASP B 2 1246 ? 122.675 158.533 104.905 1.00 48.55  ? 1243 ASP A CB    1 
ATOM   10020 C CG    . ASP B 2 1246 ? 122.910 160.002 104.630 1.00 48.55  ? 1243 ASP A CG    1 
ATOM   10021 O OD1   . ASP B 2 1246 ? 121.931 160.775 104.676 1.00 48.55  ? 1243 ASP A OD1   1 
ATOM   10022 O OD2   . ASP B 2 1246 ? 124.069 160.387 104.377 1.00 48.55  ? 1243 ASP A OD2   1 
ATOM   10023 N N     . LEU B 2 1247 ? 120.070 158.621 103.695 1.00 51.01  ? 1244 LEU A N     1 
ATOM   10024 C CA    . LEU B 2 1247 ? 118.839 159.135 103.102 1.00 51.01  ? 1244 LEU A CA    1 
ATOM   10025 C C     . LEU B 2 1247 ? 119.059 160.473 102.408 1.00 51.01  ? 1244 LEU A C     1 
ATOM   10026 O O     . LEU B 2 1247 ? 118.334 160.806 101.464 1.00 51.01  ? 1244 LEU A O     1 
ATOM   10027 C CB    . LEU B 2 1247 ? 117.755 159.266 104.173 1.00 51.01  ? 1244 LEU A CB    1 
ATOM   10028 C CG    . LEU B 2 1247 ? 116.809 158.077 104.369 1.00 51.01  ? 1244 LEU A CG    1 
ATOM   10029 C CD1   . LEU B 2 1247 ? 115.968 157.849 103.121 1.00 51.01  ? 1244 LEU A CD1   1 
ATOM   10030 C CD2   . LEU B 2 1247 ? 117.569 156.812 104.748 1.00 51.01  ? 1244 LEU A CD2   1 
ATOM   10031 N N     . ASN B 2 1248 ? 120.046 161.252 102.855 1.00 52.77  ? 1245 ASN A N     1 
ATOM   10032 C CA    . ASN B 2 1248 ? 120.311 162.542 102.231 1.00 52.77  ? 1245 ASN A CA    1 
ATOM   10033 C C     . ASN B 2 1248 ? 121.045 162.402 100.904 1.00 52.77  ? 1245 ASN A C     1 
ATOM   10034 O O     . ASN B 2 1248 ? 121.118 163.373 100.144 1.00 52.77  ? 1245 ASN A O     1 
ATOM   10035 C CB    . ASN B 2 1248 ? 121.112 163.433 103.183 1.00 52.77  ? 1245 ASN A CB    1 
ATOM   10036 C CG    . ASN B 2 1248 ? 121.066 164.898 102.794 1.00 52.77  ? 1245 ASN A CG    1 
ATOM   10037 O OD1   . ASN B 2 1248 ? 121.856 165.360 101.970 1.00 52.77  ? 1245 ASN A OD1   1 
ATOM   10038 N ND2   . ASN B 2 1248 ? 120.136 165.638 103.387 1.00 52.77  ? 1245 ASN A ND2   1 
ATOM   10039 N N     . GLY B 2 1249 ? 121.578 161.222 100.603 1.00 49.96  ? 1246 GLY A N     1 
ATOM   10040 C CA    . GLY B 2 1249 ? 122.292 161.017 99.361  1.00 49.96  ? 1246 GLY A CA    1 
ATOM   10041 C C     . GLY B 2 1249 ? 123.745 161.429 99.381  1.00 49.96  ? 1246 GLY A C     1 
ATOM   10042 O O     . GLY B 2 1249 ? 124.317 161.693 98.317  1.00 49.96  ? 1246 GLY A O     1 
ATOM   10043 N N     . VAL B 2 1250 ? 124.364 161.495 100.557 1.00 48.55  ? 1247 VAL A N     1 
ATOM   10044 C CA    . VAL B 2 1250 ? 125.761 161.881 100.698 1.00 48.55  ? 1247 VAL A CA    1 
ATOM   10045 C C     . VAL B 2 1250 ? 126.496 160.778 101.448 1.00 48.55  ? 1247 VAL A C     1 
ATOM   10046 O O     . VAL B 2 1250 ? 125.961 160.195 102.397 1.00 48.55  ? 1247 VAL A O     1 
ATOM   10047 C CB    . VAL B 2 1250 ? 125.907 163.240 101.419 1.00 48.55  ? 1247 VAL A CB    1 
ATOM   10048 C CG1   . VAL B 2 1250 ? 125.263 163.197 102.799 1.00 48.55  ? 1247 VAL A CG1   1 
ATOM   10049 C CG2   . VAL B 2 1250 ? 127.371 163.648 101.515 1.00 48.55  ? 1247 VAL A CG2   1 
ATOM   10050 N N     . CYS B 2 1251 ? 127.713 160.474 101.005 1.00 48.55  ? 1248 CYS A N     1 
ATOM   10051 C CA    . CYS B 2 1251 ? 128.515 159.443 101.647 1.00 48.55  ? 1248 CYS A CA    1 
ATOM   10052 C C     . CYS B 2 1251 ? 129.324 160.045 102.786 1.00 48.55  ? 1248 CYS A C     1 
ATOM   10053 O O     . CYS B 2 1251 ? 129.954 161.095 102.626 1.00 48.55  ? 1248 CYS A O     1 
ATOM   10054 C CB    . CYS B 2 1251 ? 129.440 158.776 100.634 1.00 48.55  ? 1248 CYS A CB    1 
ATOM   10055 S SG    . CYS B 2 1251 ? 128.604 157.585 99.583  1.00 48.55  ? 1248 CYS A SG    1 
ATOM   10056 N N     . PHE B 2 1252 ? 129.300 159.379 103.938 1.00 48.55  ? 1249 PHE A N     1 
ATOM   10057 C CA    . PHE B 2 1252 ? 130.011 159.885 105.101 1.00 48.55  ? 1249 PHE A CA    1 
ATOM   10058 C C     . PHE B 2 1252 ? 131.514 159.871 104.860 1.00 48.55  ? 1249 PHE A C     1 
ATOM   10059 O O     . PHE B 2 1252 ? 132.073 158.892 104.359 1.00 48.55  ? 1249 PHE A O     1 
ATOM   10060 C CB    . PHE B 2 1252 ? 129.672 159.054 106.337 1.00 48.55  ? 1249 PHE A CB    1 
ATOM   10061 C CG    . PHE B 2 1252 ? 130.378 159.508 107.580 1.00 48.55  ? 1249 PHE A CG    1 
ATOM   10062 C CD1   . PHE B 2 1252 ? 130.102 160.745 108.133 1.00 48.55  ? 1249 PHE A CD1   1 
ATOM   10063 C CD2   . PHE B 2 1252 ? 131.322 158.704 108.190 1.00 48.55  ? 1249 PHE A CD2   1 
ATOM   10064 C CE1   . PHE B 2 1252 ? 130.750 161.168 109.274 1.00 48.55  ? 1249 PHE A CE1   1 
ATOM   10065 C CE2   . PHE B 2 1252 ? 131.973 159.123 109.329 1.00 48.55  ? 1249 PHE A CE2   1 
ATOM   10066 C CZ    . PHE B 2 1252 ? 131.686 160.355 109.872 1.00 48.55  ? 1249 PHE A CZ    1 
ATOM   10067 N N     . ASP B 2 1253 ? 132.166 160.970 105.222 1.00 48.55  ? 1250 ASP A N     1 
ATOM   10068 C CA    . ASP B 2 1253 ? 133.618 161.076 105.119 1.00 48.55  ? 1250 ASP A CA    1 
ATOM   10069 C C     . ASP B 2 1253 ? 134.095 161.890 106.312 1.00 48.55  ? 1250 ASP A C     1 
ATOM   10070 O O     . ASP B 2 1253 ? 133.906 163.110 106.344 1.00 48.55  ? 1250 ASP A O     1 
ATOM   10071 C CB    . ASP B 2 1253 ? 134.033 161.722 103.802 1.00 48.55  ? 1250 ASP A CB    1 
ATOM   10072 C CG    . ASP B 2 1253 ? 135.530 161.684 103.581 1.00 48.55  ? 1250 ASP A CG    1 
ATOM   10073 O OD1   . ASP B 2 1253 ? 136.062 160.594 103.281 1.00 48.55  ? 1250 ASP A OD1   1 
ATOM   10074 O OD2   . ASP B 2 1253 ? 136.175 162.746 103.701 1.00 48.55  ? 1250 ASP A OD2   1 
ATOM   10075 N N     . SER B 2 1254 ? 134.705 161.217 107.290 1.00 48.55  ? 1251 SER A N     1 
ATOM   10076 C CA    . SER B 2 1254 ? 135.081 161.881 108.532 1.00 48.55  ? 1251 SER A CA    1 
ATOM   10077 C C     . SER B 2 1254 ? 136.174 162.921 108.331 1.00 48.55  ? 1251 SER A C     1 
ATOM   10078 O O     . SER B 2 1254 ? 136.420 163.722 109.239 1.00 48.55  ? 1251 SER A O     1 
ATOM   10079 C CB    . SER B 2 1254 ? 135.531 160.852 109.568 1.00 48.55  ? 1251 SER A CB    1 
ATOM   10080 O OG    . SER B 2 1254 ? 136.825 160.366 109.271 1.00 48.55  ? 1251 SER A OG    1 
ATOM   10081 N N     . ARG B 2 1255 ? 136.836 162.927 107.173 1.00 48.55  ? 1252 ARG A N     1 
ATOM   10082 C CA    . ARG B 2 1255 ? 137.827 163.957 106.894 1.00 48.55  ? 1252 ARG A CA    1 
ATOM   10083 C C     . ARG B 2 1255 ? 137.203 165.341 106.779 1.00 48.55  ? 1252 ARG A C     1 
ATOM   10084 O O     . ARG B 2 1255 ? 137.923 166.339 106.867 1.00 48.55  ? 1252 ARG A O     1 
ATOM   10085 C CB    . ARG B 2 1255 ? 138.592 163.622 105.613 1.00 48.55  ? 1252 ARG A CB    1 
ATOM   10086 C CG    . ARG B 2 1255 ? 139.347 162.306 105.672 1.00 48.55  ? 1252 ARG A CG    1 
ATOM   10087 C CD    . ARG B 2 1255 ? 139.140 161.495 104.405 1.00 48.55  ? 1252 ARG A CD    1 
ATOM   10088 N NE    . ARG B 2 1255 ? 140.102 161.834 103.365 1.00 48.55  ? 1252 ARG A NE    1 
ATOM   10089 C CZ    . ARG B 2 1255 ? 140.036 161.394 102.117 1.00 48.55  ? 1252 ARG A CZ    1 
ATOM   10090 N NH1   . ARG B 2 1255 ? 139.062 160.594 101.717 1.00 48.55  ? 1252 ARG A NH1   1 
ATOM   10091 N NH2   . ARG B 2 1255 ? 140.971 161.766 101.247 1.00 48.55  ? 1252 ARG A NH2   1 
ATOM   10092 N N     . PHE B 2 1256 ? 135.883 165.423 106.589 1.00 48.55  ? 1253 PHE A N     1 
ATOM   10093 C CA    . PHE B 2 1256 ? 135.212 166.715 106.528 1.00 48.55  ? 1253 PHE A CA    1 
ATOM   10094 C C     . PHE B 2 1256 ? 135.162 167.405 107.884 1.00 48.55  ? 1253 PHE A C     1 
ATOM   10095 O O     . PHE B 2 1256 ? 134.875 168.606 107.942 1.00 48.55  ? 1253 PHE A O     1 
ATOM   10096 C CB    . PHE B 2 1256 ? 133.795 166.547 105.980 1.00 48.55  ? 1253 PHE A CB    1 
ATOM   10097 C CG    . PHE B 2 1256 ? 133.738 166.378 104.490 1.00 48.55  ? 1253 PHE A CG    1 
ATOM   10098 C CD1   . PHE B 2 1256 ? 134.133 167.402 103.648 1.00 48.55  ? 1253 PHE A CD1   1 
ATOM   10099 C CD2   . PHE B 2 1256 ? 133.288 165.195 103.932 1.00 48.55  ? 1253 PHE A CD2   1 
ATOM   10100 C CE1   . PHE B 2 1256 ? 134.081 167.247 102.277 1.00 48.55  ? 1253 PHE A CE1   1 
ATOM   10101 C CE2   . PHE B 2 1256 ? 133.235 165.035 102.563 1.00 48.55  ? 1253 PHE A CE2   1 
ATOM   10102 C CZ    . PHE B 2 1256 ? 133.631 166.062 101.735 1.00 48.55  ? 1253 PHE A CZ    1 
ATOM   10103 N N     . GLN B 2 1257 ? 135.435 166.674 108.967 1.00 48.55  ? 1254 GLN A N     1 
ATOM   10104 C CA    . GLN B 2 1257 ? 135.474 167.229 110.321 1.00 48.55  ? 1254 GLN A CA    1 
ATOM   10105 C C     . GLN B 2 1257 ? 134.154 167.899 110.699 1.00 48.55  ? 1254 GLN A C     1 
ATOM   10106 O O     . GLN B 2 1257 ? 134.131 168.972 111.304 1.00 48.55  ? 1254 GLN A O     1 
ATOM   10107 C CB    . GLN B 2 1257 ? 136.645 168.200 110.487 1.00 48.55  ? 1254 GLN A CB    1 
ATOM   10108 C CG    . GLN B 2 1257 ? 137.957 167.688 109.913 1.00 48.55  ? 1254 GLN A CG    1 
ATOM   10109 C CD    . GLN B 2 1257 ? 138.747 166.860 110.907 1.00 48.55  ? 1254 GLN A CD    1 
ATOM   10110 O OE1   . GLN B 2 1257 ? 139.336 167.392 111.847 1.00 48.55  ? 1254 GLN A OE1   1 
ATOM   10111 N NE2   . GLN B 2 1257 ? 138.763 165.549 110.702 1.00 48.55  ? 1254 GLN A NE2   1 
ATOM   10112 N N     . ASN B 2 1258 ? 133.048 167.263 110.340 1.00 48.55  ? 1255 ASN A N     1 
ATOM   10113 C CA    . ASN B 2 1258 ? 131.742 167.732 110.783 1.00 48.55  ? 1255 ASN A CA    1 
ATOM   10114 C C     . ASN B 2 1258 ? 131.609 167.474 112.280 1.00 48.55  ? 1255 ASN A C     1 
ATOM   10115 O O     . ASN B 2 1258 ? 131.828 166.343 112.727 1.00 48.55  ? 1255 ASN A O     1 
ATOM   10116 C CB    . ASN B 2 1258 ? 130.635 167.012 110.015 1.00 48.55  ? 1255 ASN A CB    1 
ATOM   10117 C CG    . ASN B 2 1258 ? 129.390 167.860 109.840 1.00 48.55  ? 1255 ASN A CG    1 
ATOM   10118 O OD1   . ASN B 2 1258 ? 129.434 169.083 109.955 1.00 48.55  ? 1255 ASN A OD1   1 
ATOM   10119 N ND2   . ASN B 2 1258 ? 128.269 167.209 109.558 1.00 48.55  ? 1255 ASN A ND2   1 
ATOM   10120 N N     . PRO B 2 1259 ? 131.260 168.479 113.087 1.00 48.55  ? 1256 PRO A N     1 
ATOM   10121 C CA    . PRO B 2 1259 ? 131.297 168.278 114.542 1.00 48.55  ? 1256 PRO A CA    1 
ATOM   10122 C C     . PRO B 2 1259 ? 130.126 167.481 115.092 1.00 48.55  ? 1256 PRO A C     1 
ATOM   10123 O O     . PRO B 2 1259 ? 130.229 166.947 116.204 1.00 48.55  ? 1256 PRO A O     1 
ATOM   10124 C CB    . PRO B 2 1259 ? 131.324 169.713 115.084 1.00 48.55  ? 1256 PRO A CB    1 
ATOM   10125 C CG    . PRO B 2 1259 ? 130.709 170.566 113.989 1.00 48.55  ? 1256 PRO A CG    1 
ATOM   10126 C CD    . PRO B 2 1259 ? 130.564 169.728 112.739 1.00 48.55  ? 1256 PRO A CD    1 
ATOM   10127 N N     . GLU B 2 1260 ? 129.018 167.377 114.360 1.00 48.55  ? 1257 GLU A N     1 
ATOM   10128 C CA    . GLU B 2 1260 ? 127.880 166.595 114.828 1.00 48.55  ? 1257 GLU A CA    1 
ATOM   10129 C C     . GLU B 2 1260 ? 128.035 165.104 114.559 1.00 48.55  ? 1257 GLU A C     1 
ATOM   10130 O O     . GLU B 2 1260 ? 127.196 164.319 115.011 1.00 48.55  ? 1257 GLU A O     1 
ATOM   10131 C CB    . GLU B 2 1260 ? 126.587 167.108 114.187 1.00 48.55  ? 1257 GLU A CB    1 
ATOM   10132 C CG    . GLU B 2 1260 ? 126.385 166.672 112.748 1.00 48.55  ? 1257 GLU A CG    1 
ATOM   10133 C CD    . GLU B 2 1260 ? 125.302 167.468 112.047 1.00 48.55  ? 1257 GLU A CD    1 
ATOM   10134 O OE1   . GLU B 2 1260 ? 124.122 167.066 112.126 1.00 48.55  ? 1257 GLU A OE1   1 
ATOM   10135 O OE2   . GLU B 2 1260 ? 125.629 168.497 111.419 1.00 48.55  ? 1257 GLU A OE2   1 
ATOM   10136 N N     . TRP B 2 1261 ? 129.076 164.701 113.846 1.00 48.55  ? 1258 TRP A N     1 
ATOM   10137 C CA    . TRP B 2 1261 ? 129.392 163.314 113.554 1.00 48.55  ? 1258 TRP A CA    1 
ATOM   10138 C C     . TRP B 2 1261 ? 130.826 163.048 113.983 1.00 48.55  ? 1258 TRP A C     1 
ATOM   10139 O O     . TRP B 2 1261 ? 131.604 163.989 114.170 1.00 48.55  ? 1258 TRP A O     1 
ATOM   10140 C CB    . TRP B 2 1261 ? 129.210 163.009 112.059 1.00 48.55  ? 1258 TRP A CB    1 
ATOM   10141 C CG    . TRP B 2 1261 ? 127.802 163.208 111.588 1.00 48.55  ? 1258 TRP A CG    1 
ATOM   10142 C CD1   . TRP B 2 1261 ? 127.366 164.120 110.674 1.00 48.55  ? 1258 TRP A CD1   1 
ATOM   10143 C CD2   . TRP B 2 1261 ? 126.642 162.487 112.021 1.00 48.55  ? 1258 TRP A CD2   1 
ATOM   10144 N NE1   . TRP B 2 1261 ? 126.008 164.008 110.505 1.00 48.55  ? 1258 TRP A NE1   1 
ATOM   10145 C CE2   . TRP B 2 1261 ? 125.540 163.012 111.322 1.00 48.55  ? 1258 TRP A CE2   1 
ATOM   10146 C CE3   . TRP B 2 1261 ? 126.430 161.446 112.930 1.00 48.55  ? 1258 TRP A CE3   1 
ATOM   10147 C CZ2   . TRP B 2 1261 ? 124.244 162.534 111.502 1.00 48.55  ? 1258 TRP A CZ2   1 
ATOM   10148 C CZ3   . TRP B 2 1261 ? 125.144 160.971 113.107 1.00 48.55  ? 1258 TRP A CZ3   1 
ATOM   10149 C CH2   . TRP B 2 1261 ? 124.068 161.515 112.397 1.00 48.55  ? 1258 TRP A CH2   1 
ATOM   10150 N N     . PRO B 2 1262 ? 131.197 161.783 114.188 1.00 48.55  ? 1259 PRO A N     1 
ATOM   10151 C CA    . PRO B 2 1262 ? 132.543 161.488 114.698 1.00 48.55  ? 1259 PRO A CA    1 
ATOM   10152 C C     . PRO B 2 1262 ? 133.637 162.103 113.836 1.00 48.55  ? 1259 PRO A C     1 
ATOM   10153 O O     . PRO B 2 1262 ? 133.625 161.999 112.608 1.00 48.55  ? 1259 PRO A O     1 
ATOM   10154 C CB    . PRO B 2 1262 ? 132.599 159.958 114.669 1.00 48.55  ? 1259 PRO A CB    1 
ATOM   10155 C CG    . PRO B 2 1262 ? 131.191 159.542 114.846 1.00 48.55  ? 1259 PRO A CG    1 
ATOM   10156 C CD    . PRO B 2 1262 ? 130.361 160.571 114.130 1.00 48.55  ? 1259 PRO A CD    1 
ATOM   10157 N N     . MET B 2 1263 ? 134.593 162.753 114.505 1.00 48.55  ? 1260 MET A N     1 
ATOM   10158 C CA    . MET B 2 1263 ? 135.689 163.419 113.811 1.00 48.55  ? 1260 MET A CA    1 
ATOM   10159 C C     . MET B 2 1263 ? 136.663 162.423 113.197 1.00 48.55  ? 1260 MET A C     1 
ATOM   10160 O O     . MET B 2 1263 ? 137.046 162.564 112.031 1.00 48.55  ? 1260 MET A O     1 
ATOM   10161 C CB    . MET B 2 1263 ? 136.432 164.346 114.773 1.00 48.55  ? 1260 MET A CB    1 
ATOM   10162 C CG    . MET B 2 1263 ? 135.655 165.576 115.202 1.00 48.55  ? 1260 MET A CG    1 
ATOM   10163 S SD    . MET B 2 1263 ? 134.903 166.447 113.819 1.00 48.55  ? 1260 MET A SD    1 
ATOM   10164 C CE    . MET B 2 1263 ? 134.939 168.129 114.433 1.00 48.55  ? 1260 MET A CE    1 
ATOM   10165 N N     . ASP B 2 1264 ? 137.074 161.415 113.961 1.00 48.55  ? 1261 ASP A N     1 
ATOM   10166 C CA    . ASP B 2 1264 ? 138.098 160.478 113.523 1.00 48.55  ? 1261 ASP A CA    1 
ATOM   10167 C C     . ASP B 2 1264 ? 137.556 159.063 113.683 1.00 48.55  ? 1261 ASP A C     1 
ATOM   10168 O O     . ASP B 2 1264 ? 136.428 158.854 114.139 1.00 48.55  ? 1261 ASP A O     1 
ATOM   10169 C CB    . ASP B 2 1264 ? 139.400 160.696 114.304 1.00 48.55  ? 1261 ASP A CB    1 
ATOM   10170 C CG    . ASP B 2 1264 ? 140.072 162.010 113.960 1.00 48.55  ? 1261 ASP A CG    1 
ATOM   10171 O OD1   . ASP B 2 1264 ? 139.907 162.481 112.815 1.00 48.55  ? 1261 ASP A OD1   1 
ATOM   10172 O OD2   . ASP B 2 1264 ? 140.766 162.573 114.833 1.00 48.55  ? 1261 ASP A OD2   1 
ATOM   10173 N N     . ALA B 2 1265 ? 138.371 158.082 113.292 1.00 48.55  ? 1262 ALA A N     1 
ATOM   10174 C CA    . ALA B 2 1265 ? 137.949 156.688 113.374 1.00 48.55  ? 1262 ALA A CA    1 
ATOM   10175 C C     . ALA B 2 1265 ? 137.768 156.246 114.819 1.00 48.55  ? 1262 ALA A C     1 
ATOM   10176 O O     . ALA B 2 1265 ? 136.826 155.510 115.136 1.00 48.55  ? 1262 ALA A O     1 
ATOM   10177 C CB    . ALA B 2 1265 ? 138.959 155.795 112.660 1.00 48.55  ? 1262 ALA A CB    1 
ATOM   10178 N N     . ASP B 2 1266 ? 138.662 156.680 115.709 1.00 48.55  ? 1263 ASP A N     1 
ATOM   10179 C CA    . ASP B 2 1266 ? 138.531 156.329 117.119 1.00 48.55  ? 1263 ASP A CA    1 
ATOM   10180 C C     . ASP B 2 1266 ? 137.295 156.976 117.733 1.00 48.55  ? 1263 ASP A C     1 
ATOM   10181 O O     . ASP B 2 1266 ? 136.744 156.470 118.718 1.00 48.55  ? 1263 ASP A O     1 
ATOM   10182 C CB    . ASP B 2 1266 ? 139.792 156.742 117.876 1.00 48.55  ? 1263 ASP A CB    1 
ATOM   10183 C CG    . ASP B 2 1266 ? 141.054 156.208 117.231 1.00 48.55  ? 1263 ASP A CG    1 
ATOM   10184 O OD1   . ASP B 2 1266 ? 141.006 155.097 116.663 1.00 48.55  ? 1263 ASP A OD1   1 
ATOM   10185 O OD2   . ASP B 2 1266 ? 142.092 156.900 117.283 1.00 48.55  ? 1263 ASP A OD2   1 
ATOM   10186 N N     . ALA B 2 1267 ? 136.849 158.098 117.166 1.00 48.55  ? 1264 ALA A N     1 
ATOM   10187 C CA    . ALA B 2 1267 ? 135.618 158.726 117.635 1.00 48.55  ? 1264 ALA A CA    1 
ATOM   10188 C C     . ALA B 2 1267 ? 134.408 157.851 117.343 1.00 48.55  ? 1264 ALA A C     1 
ATOM   10189 O O     . ALA B 2 1267 ? 133.461 157.802 118.136 1.00 48.55  ? 1264 ALA A O     1 
ATOM   10190 C CB    . ALA B 2 1267 ? 135.452 160.101 116.990 1.00 48.55  ? 1264 ALA A CB    1 
ATOM   10191 N N     . ASN B 2 1268 ? 134.418 157.158 116.202 1.00 48.55  ? 1265 ASN A N     1 
ATOM   10192 C CA    . ASN B 2 1268 ? 133.280 156.328 115.825 1.00 48.55  ? 1265 ASN A CA    1 
ATOM   10193 C C     . ASN B 2 1268 ? 133.086 155.176 116.802 1.00 48.55  ? 1265 ASN A C     1 
ATOM   10194 O O     . ASN B 2 1268 ? 131.950 154.821 117.136 1.00 48.55  ? 1265 ASN A O     1 
ATOM   10195 C CB    . ASN B 2 1268 ? 133.467 155.800 114.405 1.00 48.55  ? 1265 ASN A CB    1 
ATOM   10196 C CG    . ASN B 2 1268 ? 132.167 155.347 113.778 1.00 48.55  ? 1265 ASN A CG    1 
ATOM   10197 O OD1   . ASN B 2 1268 ? 131.192 156.096 113.735 1.00 48.55  ? 1265 ASN A OD1   1 
ATOM   10198 N ND2   . ASN B 2 1268 ? 132.146 154.116 113.284 1.00 48.55  ? 1265 ASN A ND2   1 
ATOM   10199 N N     . GLY B 2 1269 ? 134.183 154.573 117.263 1.00 48.55  ? 1266 GLY A N     1 
ATOM   10200 C CA    . GLY B 2 1269 ? 134.065 153.481 118.215 1.00 48.55  ? 1266 GLY A CA    1 
ATOM   10201 C C     . GLY B 2 1269 ? 133.456 153.923 119.532 1.00 48.55  ? 1266 GLY A C     1 
ATOM   10202 O O     . GLY B 2 1269 ? 132.590 153.246 120.091 1.00 48.55  ? 1266 GLY A O     1 
ATOM   10203 N N     . ALA B 2 1270 ? 133.903 155.070 120.045 1.00 48.55  ? 1267 ALA A N     1 
ATOM   10204 C CA    . ALA B 2 1270 ? 133.334 155.596 121.281 1.00 48.55  ? 1267 ALA A CA    1 
ATOM   10205 C C     . ALA B 2 1270 ? 131.903 156.069 121.069 1.00 48.55  ? 1267 ALA A C     1 
ATOM   10206 O O     . ALA B 2 1270 ? 131.070 155.981 121.979 1.00 48.55  ? 1267 ALA A O     1 
ATOM   10207 C CB    . ALA B 2 1270 ? 134.203 156.733 121.818 1.00 48.55  ? 1267 ALA A CB    1 
ATOM   10208 N N     . TYR B 2 1271 ? 131.599 156.582 119.875 1.00 48.55  ? 1268 TYR A N     1 
ATOM   10209 C CA    . TYR B 2 1271 ? 130.248 157.055 119.595 1.00 48.55  ? 1268 TYR A CA    1 
ATOM   10210 C C     . TYR B 2 1271 ? 129.252 155.904 119.565 1.00 48.55  ? 1268 TYR A C     1 
ATOM   10211 O O     . TYR B 2 1271 ? 128.109 156.051 120.013 1.00 48.55  ? 1268 TYR A O     1 
ATOM   10212 C CB    . TYR B 2 1271 ? 130.223 157.822 118.274 1.00 48.55  ? 1268 TYR A CB    1 
ATOM   10213 C CG    . TYR B 2 1271 ? 128.841 158.244 117.836 1.00 48.55  ? 1268 TYR A CG    1 
ATOM   10214 C CD1   . TYR B 2 1271 ? 128.015 158.966 118.682 1.00 48.55  ? 1268 TYR A CD1   1 
ATOM   10215 C CD2   . TYR B 2 1271 ? 128.367 157.929 116.572 1.00 48.55  ? 1268 TYR A CD2   1 
ATOM   10216 C CE1   . TYR B 2 1271 ? 126.752 159.355 118.286 1.00 48.55  ? 1268 TYR A CE1   1 
ATOM   10217 C CE2   . TYR B 2 1271 ? 127.107 158.314 116.166 1.00 48.55  ? 1268 TYR A CE2   1 
ATOM   10218 C CZ    . TYR B 2 1271 ? 126.305 159.028 117.027 1.00 48.55  ? 1268 TYR A CZ    1 
ATOM   10219 O OH    . TYR B 2 1271 ? 125.047 159.415 116.627 1.00 48.55  ? 1268 TYR A OH    1 
ATOM   10220 N N     . HIS B 2 1272 ? 129.665 154.748 119.046 1.00 48.55  ? 1269 HIS A N     1 
ATOM   10221 C CA    . HIS B 2 1272 ? 128.742 153.627 118.929 1.00 48.55  ? 1269 HIS A CA    1 
ATOM   10222 C C     . HIS B 2 1272 ? 128.669 152.803 120.207 1.00 48.55  ? 1269 HIS A C     1 
ATOM   10223 O O     . HIS B 2 1272 ? 127.653 152.145 120.454 1.00 48.55  ? 1269 HIS A O     1 
ATOM   10224 C CB    . HIS B 2 1272 ? 129.137 152.747 117.745 1.00 48.55  ? 1269 HIS A CB    1 
ATOM   10225 C CG    . HIS B 2 1272 ? 128.647 153.262 116.428 1.00 48.55  ? 1269 HIS A CG    1 
ATOM   10226 N ND1   . HIS B 2 1272 ? 129.406 154.083 115.622 1.00 48.55  ? 1269 HIS A ND1   1 
ATOM   10227 C CD2   . HIS B 2 1272 ? 127.471 153.085 115.783 1.00 48.55  ? 1269 HIS A CD2   1 
ATOM   10228 C CE1   . HIS B 2 1272 ? 128.721 154.384 114.534 1.00 48.55  ? 1269 HIS A CE1   1 
ATOM   10229 N NE2   . HIS B 2 1272 ? 127.543 153.791 114.607 1.00 48.55  ? 1269 HIS A NE2   1 
ATOM   10230 N N     . ILE B 2 1273 ? 129.725 152.818 121.023 1.00 48.55  ? 1270 ILE A N     1 
ATOM   10231 C CA    . ILE B 2 1273 ? 129.643 152.198 122.343 1.00 48.55  ? 1270 ILE A CA    1 
ATOM   10232 C C     . ILE B 2 1273 ? 128.638 152.944 123.209 1.00 48.55  ? 1270 ILE A C     1 
ATOM   10233 O O     . ILE B 2 1273 ? 127.833 152.332 123.923 1.00 48.55  ? 1270 ILE A O     1 
ATOM   10234 C CB    . ILE B 2 1273 ? 131.034 152.143 122.999 1.00 48.55  ? 1270 ILE A CB    1 
ATOM   10235 C CG1   . ILE B 2 1273 ? 131.856 151.002 122.404 1.00 48.55  ? 1270 ILE A CG1   1 
ATOM   10236 C CG2   . ILE B 2 1273 ? 130.914 151.978 124.503 1.00 48.55  ? 1270 ILE A CG2   1 
ATOM   10237 C CD1   . ILE B 2 1273 ? 133.220 150.843 123.031 1.00 48.55  ? 1270 ILE A CD1   1 
ATOM   10238 N N     . ALA B 2 1274 ? 128.661 154.277 123.153 1.00 48.55  ? 1271 ALA A N     1 
ATOM   10239 C CA    . ALA B 2 1274 ? 127.668 155.065 123.874 1.00 48.55  ? 1271 ALA A CA    1 
ATOM   10240 C C     . ALA B 2 1274 ? 126.272 154.831 123.315 1.00 48.55  ? 1271 ALA A C     1 
ATOM   10241 O O     . ALA B 2 1274 ? 125.283 154.864 124.056 1.00 48.55  ? 1271 ALA A O     1 
ATOM   10242 C CB    . ALA B 2 1274 ? 128.030 156.548 123.816 1.00 48.55  ? 1271 ALA A CB    1 
ATOM   10243 N N     . LEU B 2 1275 ? 126.170 154.596 122.005 1.00 48.55  ? 1272 LEU A N     1 
ATOM   10244 C CA    . LEU B 2 1275 ? 124.875 154.290 121.409 1.00 48.55  ? 1272 LEU A CA    1 
ATOM   10245 C C     . LEU B 2 1275 ? 124.371 152.926 121.861 1.00 48.55  ? 1272 LEU A C     1 
ATOM   10246 O O     . LEU B 2 1275 ? 123.160 152.723 122.009 1.00 48.55  ? 1272 LEU A O     1 
ATOM   10247 C CB    . LEU B 2 1275 ? 124.969 154.353 119.886 1.00 48.55  ? 1272 LEU A CB    1 
ATOM   10248 C CG    . LEU B 2 1275 ? 124.865 155.742 119.254 1.00 48.55  ? 1272 LEU A CG    1 
ATOM   10249 C CD1   . LEU B 2 1275 ? 124.946 155.647 117.740 1.00 48.55  ? 1272 LEU A CD1   1 
ATOM   10250 C CD2   . LEU B 2 1275 ? 123.577 156.423 119.677 1.00 48.55  ? 1272 LEU A CD2   1 
ATOM   10251 N N     . LYS B 2 1276 ? 125.283 151.976 122.077 1.00 48.55  ? 1273 LYS A N     1 
ATOM   10252 C CA    . LYS B 2 1276 ? 124.888 150.682 122.623 1.00 48.55  ? 1273 LYS A CA    1 
ATOM   10253 C C     . LYS B 2 1276 ? 124.344 150.829 124.037 1.00 48.55  ? 1273 LYS A C     1 
ATOM   10254 O O     . LYS B 2 1276 ? 123.367 150.168 124.408 1.00 48.55  ? 1273 LYS A O     1 
ATOM   10255 C CB    . LYS B 2 1276 ? 126.071 149.717 122.601 1.00 48.55  ? 1273 LYS A CB    1 
ATOM   10256 C CG    . LYS B 2 1276 ? 126.031 148.714 121.465 1.00 48.55  ? 1273 LYS A CG    1 
ATOM   10257 C CD    . LYS B 2 1276 ? 127.202 147.752 121.543 1.00 48.55  ? 1273 LYS A CD    1 
ATOM   10258 C CE    . LYS B 2 1276 ? 127.211 146.798 120.364 1.00 48.55  ? 1273 LYS A CE    1 
ATOM   10259 N NZ    . LYS B 2 1276 ? 128.366 145.861 120.422 1.00 48.55  ? 1273 LYS A NZ    1 
ATOM   10260 N N     . GLY B 2 1277 ? 124.974 151.681 124.848 1.00 48.55  ? 1274 GLY A N     1 
ATOM   10261 C CA    . GLY B 2 1277 ? 124.432 151.967 126.165 1.00 48.55  ? 1274 GLY A CA    1 
ATOM   10262 C C     . GLY B 2 1277 ? 123.077 152.641 126.096 1.00 48.55  ? 1274 GLY A C     1 
ATOM   10263 O O     . GLY B 2 1277 ? 122.214 152.412 126.947 1.00 48.55  ? 1274 GLY A O     1 
ATOM   10264 N N     . GLN B 2 1278 ? 122.874 153.487 125.084 1.00 48.55  ? 1275 GLN A N     1 
ATOM   10265 C CA    . GLN B 2 1278 ? 121.564 154.093 124.879 1.00 48.55  ? 1275 GLN A CA    1 
ATOM   10266 C C     . GLN B 2 1278 ? 120.520 153.032 124.562 1.00 48.55  ? 1275 GLN A C     1 
ATOM   10267 O O     . GLN B 2 1278 ? 119.356 153.152 124.963 1.00 48.55  ? 1275 GLN A O     1 
ATOM   10268 C CB    . GLN B 2 1278 ? 121.641 155.132 123.761 1.00 48.55  ? 1275 GLN A CB    1 
ATOM   10269 C CG    . GLN B 2 1278 ? 120.301 155.700 123.337 1.00 48.55  ? 1275 GLN A CG    1 
ATOM   10270 C CD    . GLN B 2 1278 ? 120.414 157.117 122.817 1.00 48.55  ? 1275 GLN A CD    1 
ATOM   10271 O OE1   . GLN B 2 1278 ? 120.695 158.046 123.573 1.00 48.55  ? 1275 GLN A OE1   1 
ATOM   10272 N NE2   . GLN B 2 1278 ? 120.193 157.291 121.520 1.00 48.55  ? 1275 GLN A NE2   1 
ATOM   10273 N N     . LEU B 2 1279 ? 120.922 151.981 123.844 1.00 48.55  ? 1276 LEU A N     1 
ATOM   10274 C CA    . LEU B 2 1279 ? 120.013 150.876 123.561 1.00 48.55  ? 1276 LEU A CA    1 
ATOM   10275 C C     . LEU B 2 1279 ? 119.550 150.205 124.848 1.00 48.55  ? 1276 LEU A C     1 
ATOM   10276 O O     . LEU B 2 1279 ? 118.361 149.913 125.017 1.00 48.55  ? 1276 LEU A O     1 
ATOM   10277 C CB    . LEU B 2 1279 ? 120.701 149.872 122.633 1.00 48.55  ? 1276 LEU A CB    1 
ATOM   10278 C CG    . LEU B 2 1279 ? 119.916 148.708 122.026 1.00 48.55  ? 1276 LEU A CG    1 
ATOM   10279 C CD1   . LEU B 2 1279 ? 120.540 148.312 120.704 1.00 48.55  ? 1276 LEU A CD1   1 
ATOM   10280 C CD2   . LEU B 2 1279 ? 119.906 147.513 122.959 1.00 48.55  ? 1276 LEU A CD2   1 
ATOM   10281 N N     . LEU B 2 1280 ? 120.481 149.951 125.771 1.00 48.55  ? 1277 LEU A N     1 
ATOM   10282 C CA    . LEU B 2 1280 ? 120.108 149.342 127.044 1.00 48.55  ? 1277 LEU A CA    1 
ATOM   10283 C C     . LEU B 2 1280 ? 119.223 150.270 127.865 1.00 48.55  ? 1277 LEU A C     1 
ATOM   10284 O O     . LEU B 2 1280 ? 118.232 149.830 128.459 1.00 48.55  ? 1277 LEU A O     1 
ATOM   10285 C CB    . LEU B 2 1280 ? 121.360 148.961 127.831 1.00 48.55  ? 1277 LEU A CB    1 
ATOM   10286 C CG    . LEU B 2 1280 ? 121.965 147.600 127.490 1.00 48.55  ? 1277 LEU A CG    1 
ATOM   10287 C CD1   . LEU B 2 1280 ? 123.153 147.313 128.384 1.00 48.55  ? 1277 LEU A CD1   1 
ATOM   10288 C CD2   . LEU B 2 1280 ? 120.917 146.508 127.624 1.00 48.55  ? 1277 LEU A CD2   1 
ATOM   10289 N N     . LEU B 2 1281 ? 119.564 151.559 127.911 1.00 48.55  ? 1278 LEU A N     1 
ATOM   10290 C CA    . LEU B 2 1281 ? 118.763 152.508 128.677 1.00 48.55  ? 1278 LEU A CA    1 
ATOM   10291 C C     . LEU B 2 1281 ? 117.368 152.658 128.083 1.00 48.55  ? 1278 LEU A C     1 
ATOM   10292 O O     . LEU B 2 1281 ? 116.388 152.817 128.820 1.00 48.55  ? 1278 LEU A O     1 
ATOM   10293 C CB    . LEU B 2 1281 ? 119.472 153.860 128.743 1.00 48.55  ? 1278 LEU A CB    1 
ATOM   10294 C CG    . LEU B 2 1281 ? 118.793 154.954 129.568 1.00 48.55  ? 1278 LEU A CG    1 
ATOM   10295 C CD1   . LEU B 2 1281 ? 118.698 154.545 131.030 1.00 48.55  ? 1278 LEU A CD1   1 
ATOM   10296 C CD2   . LEU B 2 1281 ? 119.534 156.275 129.426 1.00 48.55  ? 1278 LEU A CD2   1 
ATOM   10297 N N     . ASN B 2 1282 ? 117.259 152.619 126.753 1.00 48.55  ? 1279 ASN A N     1 
ATOM   10298 C CA    . ASN B 2 1282 ? 115.948 152.705 126.119 1.00 48.55  ? 1279 ASN A CA    1 
ATOM   10299 C C     . ASN B 2 1282 ? 115.080 151.505 126.475 1.00 48.55  ? 1279 ASN A C     1 
ATOM   10300 O O     . ASN B 2 1282 ? 113.879 151.655 126.728 1.00 48.55  ? 1279 ASN A O     1 
ATOM   10301 C CB    . ASN B 2 1282 ? 116.103 152.830 124.604 1.00 48.55  ? 1279 ASN A CB    1 
ATOM   10302 C CG    . ASN B 2 1282 ? 116.308 154.263 124.158 1.00 48.55  ? 1279 ASN A CG    1 
ATOM   10303 O OD1   . ASN B 2 1282 ? 117.113 154.996 124.734 1.00 48.55  ? 1279 ASN A OD1   1 
ATOM   10304 N ND2   . ASN B 2 1282 ? 115.578 154.673 123.128 1.00 48.55  ? 1279 ASN A ND2   1 
ATOM   10305 N N     . HIS B 2 1283 ? 115.666 150.305 126.496 1.00 48.55  ? 1280 HIS A N     1 
ATOM   10306 C CA    . HIS B 2 1283 ? 114.913 149.131 126.925 1.00 48.55  ? 1280 HIS A CA    1 
ATOM   10307 C C     . HIS B 2 1283 ? 114.542 149.221 128.399 1.00 48.55  ? 1280 HIS A C     1 
ATOM   10308 O O     . HIS B 2 1283 ? 113.516 148.675 128.820 1.00 48.55  ? 1280 HIS A O     1 
ATOM   10309 C CB    . HIS B 2 1283 ? 115.704 147.855 126.641 1.00 48.55  ? 1280 HIS A CB    1 
ATOM   10310 C CG    . HIS B 2 1283 ? 115.768 147.496 125.190 1.00 48.55  ? 1280 HIS A CG    1 
ATOM   10311 N ND1   . HIS B 2 1283 ? 116.952 147.459 124.486 1.00 48.55  ? 1280 HIS A ND1   1 
ATOM   10312 C CD2   . HIS B 2 1283 ? 114.796 147.167 124.308 1.00 48.55  ? 1280 HIS A CD2   1 
ATOM   10313 C CE1   . HIS B 2 1283 ? 116.708 147.116 123.234 1.00 48.55  ? 1280 HIS A CE1   1 
ATOM   10314 N NE2   . HIS B 2 1283 ? 115.407 146.934 123.099 1.00 48.55  ? 1280 HIS A NE2   1 
ATOM   10315 N N     . LEU B 2 1284 ? 115.368 149.898 129.198 1.00 48.55  ? 1281 LEU A N     1 
ATOM   10316 C CA    . LEU B 2 1284 ? 115.020 150.135 130.595 1.00 48.55  ? 1281 LEU A CA    1 
ATOM   10317 C C     . LEU B 2 1284 ? 113.751 150.972 130.701 1.00 48.55  ? 1281 LEU A C     1 
ATOM   10318 O O     . LEU B 2 1284 ? 112.868 150.685 131.517 1.00 48.55  ? 1281 LEU A O     1 
ATOM   10319 C CB    . LEU B 2 1284 ? 116.192 150.816 131.309 1.00 48.55  ? 1281 LEU A CB    1 
ATOM   10320 C CG    . LEU B 2 1284 ? 116.075 151.333 132.746 1.00 48.55  ? 1281 LEU A CG    1 
ATOM   10321 C CD1   . LEU B 2 1284 ? 117.448 151.324 133.385 1.00 48.55  ? 1281 LEU A CD1   1 
ATOM   10322 C CD2   . LEU B 2 1284 ? 115.498 152.741 132.806 1.00 48.55  ? 1281 LEU A CD2   1 
ATOM   10323 N N     . LYS B 2 1285 ? 113.648 152.019 129.880 1.00 48.55  ? 1282 LYS A N     1 
ATOM   10324 C CA    . LYS B 2 1285 ? 112.491 152.904 129.945 1.00 48.55  ? 1282 LYS A CA    1 
ATOM   10325 C C     . LYS B 2 1285 ? 111.233 152.217 129.428 1.00 48.55  ? 1282 LYS A C     1 
ATOM   10326 O O     . LYS B 2 1285 ? 110.151 152.371 130.008 1.00 48.55  ? 1282 LYS A O     1 
ATOM   10327 C CB    . LYS B 2 1285 ? 112.772 154.183 129.158 1.00 48.55  ? 1282 LYS A CB    1 
ATOM   10328 C CG    . LYS B 2 1285 ? 111.648 155.202 129.193 1.00 48.55  ? 1282 LYS A CG    1 
ATOM   10329 C CD    . LYS B 2 1285 ? 112.060 156.492 128.504 1.00 48.55  ? 1282 LYS A CD    1 
ATOM   10330 C CE    . LYS B 2 1285 ? 112.113 156.322 126.994 1.00 48.55  ? 1282 LYS A CE    1 
ATOM   10331 N NZ    . LYS B 2 1285 ? 112.402 157.608 126.301 1.00 48.55  ? 1282 LYS A NZ    1 
ATOM   10332 N N     . GLU B 2 1286 ? 111.350 151.456 128.337 1.00 52.35  ? 1283 GLU A N     1 
ATOM   10333 C CA    . GLU B 2 1286 ? 110.167 150.830 127.754 1.00 52.35  ? 1283 GLU A CA    1 
ATOM   10334 C C     . GLU B 2 1286 ? 109.680 149.659 128.600 1.00 52.35  ? 1283 GLU A C     1 
ATOM   10335 O O     . GLU B 2 1286 ? 108.472 149.407 128.680 1.00 52.35  ? 1283 GLU A O     1 
ATOM   10336 C CB    . GLU B 2 1286 ? 110.455 150.390 126.315 1.00 52.35  ? 1283 GLU A CB    1 
ATOM   10337 C CG    . GLU B 2 1286 ? 111.427 149.228 126.169 1.00 52.35  ? 1283 GLU A CG    1 
ATOM   10338 C CD    . GLU B 2 1286 ? 110.731 147.880 126.121 1.00 52.35  ? 1283 GLU A CD    1 
ATOM   10339 O OE1   . GLU B 2 1286 ? 109.517 147.846 125.833 1.00 52.35  ? 1283 GLU A OE1   1 
ATOM   10340 O OE2   . GLU B 2 1286 ? 111.400 146.855 126.372 1.00 52.35  ? 1283 GLU A OE2   1 
ATOM   10341 N N     . SER B 2 1287 ? 110.595 148.935 129.238 1.00 55.50  ? 1284 SER A N     1 
ATOM   10342 C CA    . SER B 2 1287 ? 110.200 147.804 130.065 1.00 55.50  ? 1284 SER A CA    1 
ATOM   10343 C C     . SER B 2 1287 ? 109.660 148.285 131.405 1.00 55.50  ? 1284 SER A C     1 
ATOM   10344 O O     . SER B 2 1287 ? 110.205 149.207 132.020 1.00 55.50  ? 1284 SER A O     1 
ATOM   10345 C CB    . SER B 2 1287 ? 111.383 146.861 130.283 1.00 55.50  ? 1284 SER A CB    1 
ATOM   10346 O OG    . SER B 2 1287 ? 111.124 145.955 131.342 1.00 55.50  ? 1284 SER A OG    1 
ATOM   10347 N N     . LYS B 2 1288 ? 108.574 147.654 131.856 1.00 64.08  ? 1285 LYS A N     1 
ATOM   10348 C CA    . LYS B 2 1288 ? 107.987 148.020 133.140 1.00 64.08  ? 1285 LYS A CA    1 
ATOM   10349 C C     . LYS B 2 1288 ? 108.895 147.625 134.298 1.00 64.08  ? 1285 LYS A C     1 
ATOM   10350 O O     . LYS B 2 1288 ? 109.042 148.382 135.265 1.00 64.08  ? 1285 LYS A O     1 
ATOM   10351 C CB    . LYS B 2 1288 ? 106.611 147.370 133.290 1.00 64.08  ? 1285 LYS A CB    1 
ATOM   10352 C CG    . LYS B 2 1288 ? 105.536 147.989 132.411 1.00 64.08  ? 1285 LYS A CG    1 
ATOM   10353 C CD    . LYS B 2 1288 ? 104.190 147.318 132.631 1.00 64.08  ? 1285 LYS A CD    1 
ATOM   10354 C CE    . LYS B 2 1288 ? 103.103 147.977 131.797 1.00 64.08  ? 1285 LYS A CE    1 
ATOM   10355 N NZ    . LYS B 2 1288 ? 101.795 147.282 131.941 1.00 64.08  ? 1285 LYS A NZ    1 
ATOM   10356 N N     . ASP B 2 1289 ? 109.511 146.449 134.220 1.00 61.49  ? 1286 ASP A N     1 
ATOM   10357 C CA    . ASP B 2 1289 ? 110.371 145.977 135.294 1.00 61.49  ? 1286 ASP A CA    1 
ATOM   10358 C C     . ASP B 2 1289 ? 111.685 146.752 135.317 1.00 61.49  ? 1286 ASP A C     1 
ATOM   10359 O O     . ASP B 2 1289 ? 112.151 147.264 134.296 1.00 61.49  ? 1286 ASP A O     1 
ATOM   10360 C CB    . ASP B 2 1289 ? 110.648 144.482 135.139 1.00 61.49  ? 1286 ASP A CB    1 
ATOM   10361 C CG    . ASP B 2 1289 ? 111.025 143.820 136.450 1.00 61.49  ? 1286 ASP A CG    1 
ATOM   10362 O OD1   . ASP B 2 1289 ? 111.148 144.535 137.466 1.00 61.49  ? 1286 ASP A OD1   1 
ATOM   10363 O OD2   . ASP B 2 1289 ? 111.198 142.583 136.464 1.00 61.49  ? 1286 ASP A OD2   1 
ATOM   10364 N N     . LEU B 2 1290 ? 112.282 146.833 136.505 1.00 55.08  ? 1287 LEU A N     1 
ATOM   10365 C CA    . LEU B 2 1290 ? 113.551 147.537 136.690 1.00 55.08  ? 1287 LEU A CA    1 
ATOM   10366 C C     . LEU B 2 1290 ? 114.725 146.562 136.573 1.00 55.08  ? 1287 LEU A C     1 
ATOM   10367 O O     . LEU B 2 1290 ? 115.545 146.406 137.477 1.00 55.08  ? 1287 LEU A O     1 
ATOM   10368 C CB    . LEU B 2 1290 ? 113.564 148.265 138.030 1.00 55.08  ? 1287 LEU A CB    1 
ATOM   10369 C CG    . LEU B 2 1290 ? 112.749 149.557 138.151 1.00 55.08  ? 1287 LEU A CG    1 
ATOM   10370 C CD1   . LEU B 2 1290 ? 111.268 149.269 138.367 1.00 55.08  ? 1287 LEU A CD1   1 
ATOM   10371 C CD2   . LEU B 2 1290 ? 113.296 150.433 139.268 1.00 55.08  ? 1287 LEU A CD2   1 
ATOM   10372 N N     . LYS B 2 1291 ? 114.789 145.899 135.421 1.00 61.97  ? 1288 LYS A N     1 
ATOM   10373 C CA    . LYS B 2 1291 ? 115.856 144.956 135.125 1.00 61.97  ? 1288 LYS A CA    1 
ATOM   10374 C C     . LYS B 2 1291 ? 116.333 145.176 133.698 1.00 61.97  ? 1288 LYS A C     1 
ATOM   10375 O O     . LYS B 2 1291 ? 115.592 145.677 132.849 1.00 61.97  ? 1288 LYS A O     1 
ATOM   10376 C CB    . LYS B 2 1291 ? 115.399 143.502 135.312 1.00 61.97  ? 1288 LYS A CB    1 
ATOM   10377 C CG    . LYS B 2 1291 ? 114.126 143.146 134.564 1.00 61.97  ? 1288 LYS A CG    1 
ATOM   10378 C CD    . LYS B 2 1291 ? 113.986 141.641 134.402 1.00 61.97  ? 1288 LYS A CD    1 
ATOM   10379 C CE    . LYS B 2 1291 ? 113.986 140.938 135.750 1.00 61.97  ? 1288 LYS A CE    1 
ATOM   10380 N NZ    . LYS B 2 1291 ? 113.549 139.519 135.638 1.00 61.97  ? 1288 LYS A NZ    1 
ATOM   10381 N N     . LEU B 2 1292 ? 117.581 144.797 133.443 1.00 54.01  ? 1289 LEU A N     1 
ATOM   10382 C CA    . LEU B 2 1292 ? 118.214 144.990 132.148 1.00 54.01  ? 1289 LEU A CA    1 
ATOM   10383 C C     . LEU B 2 1292 ? 118.517 143.647 131.499 1.00 54.01  ? 1289 LEU A C     1 
ATOM   10384 O O     . LEU B 2 1292 ? 118.730 142.640 132.181 1.00 54.01  ? 1289 LEU A O     1 
ATOM   10385 C CB    . LEU B 2 1292 ? 119.507 145.803 132.274 1.00 54.01  ? 1289 LEU A CB    1 
ATOM   10386 C CG    . LEU B 2 1292 ? 119.405 147.331 132.307 1.00 54.01  ? 1289 LEU A CG    1 
ATOM   10387 C CD1   . LEU B 2 1292 ? 118.837 147.848 130.997 1.00 54.01  ? 1289 LEU A CD1   1 
ATOM   10388 C CD2   . LEU B 2 1292 ? 118.583 147.826 133.484 1.00 54.01  ? 1289 LEU A CD2   1 
ATOM   10389 N N     . GLN B 2 1293 ? 118.526 143.644 130.168 1.00 60.99  ? 1290 GLN A N     1 
ATOM   10390 C CA    . GLN B 2 1293 ? 118.852 142.435 129.426 1.00 60.99  ? 1290 GLN A CA    1 
ATOM   10391 C C     . GLN B 2 1293 ? 120.301 142.035 129.674 1.00 60.99  ? 1290 GLN A C     1 
ATOM   10392 O O     . GLN B 2 1293 ? 121.200 142.879 129.707 1.00 60.99  ? 1290 GLN A O     1 
ATOM   10393 C CB    . GLN B 2 1293 ? 118.611 142.651 127.932 1.00 60.99  ? 1290 GLN A CB    1 
ATOM   10394 C CG    . GLN B 2 1293 ? 117.197 142.328 127.476 1.00 60.99  ? 1290 GLN A CG    1 
ATOM   10395 C CD    . GLN B 2 1293 ? 116.681 141.025 128.053 1.00 60.99  ? 1290 GLN A CD    1 
ATOM   10396 O OE1   . GLN B 2 1293 ? 115.904 141.020 129.008 1.00 60.99  ? 1290 GLN A OE1   1 
ATOM   10397 N NE2   . GLN B 2 1293 ? 117.111 139.910 127.474 1.00 60.99  ? 1290 GLN A NE2   1 
ATOM   10398 N N     . ASN B 2 1294 ? 120.524 140.733 129.849 1.00 63.74  ? 1291 ASN A N     1 
ATOM   10399 C CA    . ASN B 2 1294 ? 121.861 140.196 130.102 1.00 63.74  ? 1291 ASN A CA    1 
ATOM   10400 C C     . ASN B 2 1294 ? 122.643 140.199 128.791 1.00 63.74  ? 1291 ASN A C     1 
ATOM   10401 O O     . ASN B 2 1294 ? 122.889 139.165 128.167 1.00 63.74  ? 1291 ASN A O     1 
ATOM   10402 C CB    . ASN B 2 1294 ? 121.775 138.797 130.700 1.00 63.74  ? 1291 ASN A CB    1 
ATOM   10403 C CG    . ASN B 2 1294 ? 120.785 138.712 131.844 1.00 63.74  ? 1291 ASN A CG    1 
ATOM   10404 O OD1   . ASN B 2 1294 ? 120.742 139.586 132.710 1.00 63.74  ? 1291 ASN A OD1   1 
ATOM   10405 N ND2   . ASN B 2 1294 ? 119.980 137.656 131.853 1.00 63.74  ? 1291 ASN A ND2   1 
ATOM   10406 N N     . GLY B 2 1295 ? 123.039 141.396 128.370 1.00 55.32  ? 1292 GLY A N     1 
ATOM   10407 C CA    . GLY B 2 1295 ? 123.750 141.575 127.124 1.00 55.32  ? 1292 GLY A CA    1 
ATOM   10408 C C     . GLY B 2 1295 ? 122.815 141.775 125.945 1.00 55.32  ? 1292 GLY A C     1 
ATOM   10409 O O     . GLY B 2 1295 ? 121.617 141.486 125.992 1.00 55.32  ? 1292 GLY A O     1 
ATOM   10410 N N     . ILE B 2 1296 ? 123.388 142.286 124.860 1.00 48.55  ? 1293 ILE A N     1 
ATOM   10411 C CA    . ILE B 2 1296 ? 122.654 142.547 123.629 1.00 48.55  ? 1293 ILE A CA    1 
ATOM   10412 C C     . ILE B 2 1296 ? 123.365 141.847 122.478 1.00 48.55  ? 1293 ILE A C     1 
ATOM   10413 O O     . ILE B 2 1296 ? 124.595 141.895 122.369 1.00 48.55  ? 1293 ILE A O     1 
ATOM   10414 C CB    . ILE B 2 1296 ? 122.504 144.061 123.361 1.00 48.55  ? 1293 ILE A CB    1 
ATOM   10415 C CG1   . ILE B 2 1296 ? 123.867 144.730 123.183 1.00 48.55  ? 1293 ILE A CG1   1 
ATOM   10416 C CG2   . ILE B 2 1296 ? 121.733 144.725 124.488 1.00 48.55  ? 1293 ILE A CG2   1 
ATOM   10417 C CD1   . ILE B 2 1296 ? 123.780 146.154 122.692 1.00 48.55  ? 1293 ILE A CD1   1 
ATOM   10418 N N     . SER B 2 1297 ? 122.588 141.170 121.638 1.00 48.55  ? 1294 SER A N     1 
ATOM   10419 C CA    . SER B 2 1297 ? 123.147 140.417 120.527 1.00 48.55  ? 1294 SER A CA    1 
ATOM   10420 C C     . SER B 2 1297 ? 123.633 141.352 119.428 1.00 48.55  ? 1294 SER A C     1 
ATOM   10421 O O     . SER B 2 1297 ? 123.179 142.493 119.306 1.00 48.55  ? 1294 SER A O     1 
ATOM   10422 C CB    . SER B 2 1297 ? 122.111 139.443 119.964 1.00 48.55  ? 1294 SER A CB    1 
ATOM   10423 O OG    . SER B 2 1297 ? 120.927 140.120 119.585 1.00 48.55  ? 1294 SER A OG    1 
ATOM   10424 N N     . ASN B 2 1298 ? 124.577 140.853 118.627 1.00 48.55  ? 1295 ASN A N     1 
ATOM   10425 C CA    . ASN B 2 1298 ? 125.115 141.650 117.529 1.00 48.55  ? 1295 ASN A CA    1 
ATOM   10426 C C     . ASN B 2 1298 ? 124.037 141.980 116.507 1.00 48.55  ? 1295 ASN A C     1 
ATOM   10427 O O     . ASN B 2 1298 ? 123.985 143.101 115.987 1.00 48.55  ? 1295 ASN A O     1 
ATOM   10428 C CB    . ASN B 2 1298 ? 126.274 140.909 116.864 1.00 48.55  ? 1295 ASN A CB    1 
ATOM   10429 C CG    . ASN B 2 1298 ? 127.354 140.514 117.848 1.00 48.55  ? 1295 ASN A CG    1 
ATOM   10430 O OD1   . ASN B 2 1298 ? 128.175 141.337 118.251 1.00 48.55  ? 1295 ASN A OD1   1 
ATOM   10431 N ND2   . ASN B 2 1298 ? 127.358 139.246 118.243 1.00 48.55  ? 1295 ASN A ND2   1 
ATOM   10432 N N     . GLN B 2 1299 ? 123.170 141.013 116.200 1.00 48.55  ? 1296 GLN A N     1 
ATOM   10433 C CA    . GLN B 2 1299 ? 122.113 141.247 115.223 1.00 48.55  ? 1296 GLN A CA    1 
ATOM   10434 C C     . GLN B 2 1299 ? 121.134 142.308 115.709 1.00 48.55  ? 1296 GLN A C     1 
ATOM   10435 O O     . GLN B 2 1299 ? 120.687 143.155 114.927 1.00 48.55  ? 1296 GLN A O     1 
ATOM   10436 C CB    . GLN B 2 1299 ? 121.386 139.937 114.919 1.00 48.55  ? 1296 GLN A CB    1 
ATOM   10437 C CG    . GLN B 2 1299 ? 120.007 140.109 114.308 1.00 48.55  ? 1296 GLN A CG    1 
ATOM   10438 C CD    . GLN B 2 1299 ? 120.051 140.729 112.926 1.00 48.55  ? 1296 GLN A CD    1 
ATOM   10439 O OE1   . GLN B 2 1299 ? 121.068 140.668 112.236 1.00 48.55  ? 1296 GLN A OE1   1 
ATOM   10440 N NE2   . GLN B 2 1299 ? 118.942 141.331 112.514 1.00 48.55  ? 1296 GLN A NE2   1 
ATOM   10441 N N     . ASP B 2 1300 ? 120.789 142.280 116.999 1.00 48.55  ? 1297 ASP A N     1 
ATOM   10442 C CA    . ASP B 2 1300 ? 119.869 143.276 117.537 1.00 48.55  ? 1297 ASP A CA    1 
ATOM   10443 C C     . ASP B 2 1300 ? 120.467 144.674 117.467 1.00 48.55  ? 1297 ASP A C     1 
ATOM   10444 O O     . ASP B 2 1300 ? 119.769 145.641 117.139 1.00 48.55  ? 1297 ASP A O     1 
ATOM   10445 C CB    . ASP B 2 1300 ? 119.493 142.924 118.975 1.00 48.55  ? 1297 ASP A CB    1 
ATOM   10446 C CG    . ASP B 2 1300 ? 118.290 143.703 119.470 1.00 48.55  ? 1297 ASP A CG    1 
ATOM   10447 O OD1   . ASP B 2 1300 ? 117.607 144.338 118.639 1.00 48.55  ? 1297 ASP A OD1   1 
ATOM   10448 O OD2   . ASP B 2 1300 ? 118.026 143.680 120.691 1.00 48.55  ? 1297 ASP A OD2   1 
ATOM   10449 N N     . TRP B 2 1301 ? 121.758 144.803 117.779 1.00 48.55  ? 1298 TRP A N     1 
ATOM   10450 C CA    . TRP B 2 1301 ? 122.419 146.100 117.678 1.00 48.55  ? 1298 TRP A CA    1 
ATOM   10451 C C     . TRP B 2 1301 ? 122.434 146.595 116.238 1.00 48.55  ? 1298 TRP A C     1 
ATOM   10452 O O     . TRP B 2 1301 ? 122.187 147.777 115.973 1.00 48.55  ? 1298 TRP A O     1 
ATOM   10453 C CB    . TRP B 2 1301 ? 123.842 146.009 118.230 1.00 48.55  ? 1298 TRP A CB    1 
ATOM   10454 C CG    . TRP B 2 1301 ? 124.731 147.134 117.791 1.00 48.55  ? 1298 TRP A CG    1 
ATOM   10455 C CD1   . TRP B 2 1301 ? 125.896 147.028 117.092 1.00 48.55  ? 1298 TRP A CD1   1 
ATOM   10456 C CD2   . TRP B 2 1301 ? 124.531 148.533 118.026 1.00 48.55  ? 1298 TRP A CD2   1 
ATOM   10457 N NE1   . TRP B 2 1301 ? 126.433 148.271 116.875 1.00 48.55  ? 1298 TRP A NE1   1 
ATOM   10458 C CE2   . TRP B 2 1301 ? 125.614 149.213 117.437 1.00 48.55  ? 1298 TRP A CE2   1 
ATOM   10459 C CE3   . TRP B 2 1301 ? 123.541 149.276 118.675 1.00 48.55  ? 1298 TRP A CE3   1 
ATOM   10460 C CZ2   . TRP B 2 1301 ? 125.735 150.598 117.477 1.00 48.55  ? 1298 TRP A CZ2   1 
ATOM   10461 C CZ3   . TRP B 2 1301 ? 123.663 150.652 118.713 1.00 48.55  ? 1298 TRP A CZ3   1 
ATOM   10462 C CH2   . TRP B 2 1301 ? 124.752 151.298 118.118 1.00 48.55  ? 1298 TRP A CH2   1 
ATOM   10463 N N     . LEU B 2 1302 ? 122.726 145.701 115.292 1.00 48.55  ? 1299 LEU A N     1 
ATOM   10464 C CA    . LEU B 2 1302 ? 122.733 146.090 113.886 1.00 48.55  ? 1299 LEU A CA    1 
ATOM   10465 C C     . LEU B 2 1302 ? 121.342 146.497 113.421 1.00 48.55  ? 1299 LEU A C     1 
ATOM   10466 O O     . LEU B 2 1302 ? 121.189 147.469 112.672 1.00 48.55  ? 1299 LEU A O     1 
ATOM   10467 C CB    . LEU B 2 1302 ? 123.276 144.949 113.028 1.00 48.55  ? 1299 LEU A CB    1 
ATOM   10468 C CG    . LEU B 2 1302 ? 124.798 144.822 113.007 1.00 48.55  ? 1299 LEU A CG    1 
ATOM   10469 C CD1   . LEU B 2 1302 ? 125.225 143.566 112.265 1.00 48.55  ? 1299 LEU A CD1   1 
ATOM   10470 C CD2   . LEU B 2 1302 ? 125.419 146.056 112.385 1.00 48.55  ? 1299 LEU A CD2   1 
ATOM   10471 N N     . ALA B 2 1303 ? 120.314 145.763 113.851 1.00 48.55  ? 1300 ALA A N     1 
ATOM   10472 C CA    . ALA B 2 1303 ? 118.948 146.124 113.492 1.00 48.55  ? 1300 ALA A CA    1 
ATOM   10473 C C     . ALA B 2 1303 ? 118.557 147.465 114.096 1.00 48.55  ? 1300 ALA A C     1 
ATOM   10474 O O     . ALA B 2 1303 ? 117.855 148.260 113.461 1.00 48.55  ? 1300 ALA A O     1 
ATOM   10475 C CB    . ALA B 2 1303 ? 117.981 145.029 113.937 1.00 48.55  ? 1300 ALA A CB    1 
ATOM   10476 N N     . TYR B 2 1304 ? 118.996 147.731 115.328 1.00 48.55  ? 1301 TYR A N     1 
ATOM   10477 C CA    . TYR B 2 1304 ? 118.641 148.980 115.994 1.00 48.55  ? 1301 TYR A CA    1 
ATOM   10478 C C     . TYR B 2 1304 ? 119.269 150.181 115.297 1.00 48.55  ? 1301 TYR A C     1 
ATOM   10479 O O     . TYR B 2 1304 ? 118.584 151.163 114.991 1.00 48.55  ? 1301 TYR A O     1 
ATOM   10480 C CB    . TYR B 2 1304 ? 119.070 148.927 117.459 1.00 48.55  ? 1301 TYR A CB    1 
ATOM   10481 C CG    . TYR B 2 1304 ? 118.712 150.162 118.251 1.00 48.55  ? 1301 TYR A CG    1 
ATOM   10482 C CD1   . TYR B 2 1304 ? 117.409 150.390 118.667 1.00 48.55  ? 1301 TYR A CD1   1 
ATOM   10483 C CD2   . TYR B 2 1304 ? 119.679 151.100 118.583 1.00 48.55  ? 1301 TYR A CD2   1 
ATOM   10484 C CE1   . TYR B 2 1304 ? 117.078 151.519 119.392 1.00 48.55  ? 1301 TYR A CE1   1 
ATOM   10485 C CE2   . TYR B 2 1304 ? 119.359 152.230 119.306 1.00 48.55  ? 1301 TYR A CE2   1 
ATOM   10486 C CZ    . TYR B 2 1304 ? 118.058 152.435 119.708 1.00 48.55  ? 1301 TYR A CZ    1 
ATOM   10487 O OH    . TYR B 2 1304 ? 117.735 153.561 120.429 1.00 48.55  ? 1301 TYR A OH    1 
ATOM   10488 N N     . ILE B 2 1305 ? 120.577 150.122 115.040 1.00 48.55  ? 1302 ILE A N     1 
ATOM   10489 C CA    . ILE B 2 1305 ? 121.272 151.279 114.484 1.00 48.55  ? 1302 ILE A CA    1 
ATOM   10490 C C     . ILE B 2 1305 ? 120.843 151.527 113.042 1.00 48.55  ? 1302 ILE A C     1 
ATOM   10491 O O     . ILE B 2 1305 ? 120.709 152.679 112.612 1.00 48.55  ? 1302 ILE A O     1 
ATOM   10492 C CB    . ILE B 2 1305 ? 122.798 151.104 114.613 1.00 48.55  ? 1302 ILE A CB    1 
ATOM   10493 C CG1   . ILE B 2 1305 ? 123.521 152.385 114.193 1.00 48.55  ? 1302 ILE A CG1   1 
ATOM   10494 C CG2   . ILE B 2 1305 ? 123.292 149.910 113.807 1.00 48.55  ? 1302 ILE A CG2   1 
ATOM   10495 C CD1   . ILE B 2 1305 ? 123.165 153.587 115.036 1.00 48.55  ? 1302 ILE A CD1   1 
ATOM   10496 N N     . GLN B 2 1306 ? 120.619 150.460 112.273 1.00 48.55  ? 1303 GLN A N     1 
ATOM   10497 C CA    . GLN B 2 1306 ? 120.227 150.631 110.879 1.00 48.55  ? 1303 GLN A CA    1 
ATOM   10498 C C     . GLN B 2 1306 ? 118.811 151.182 110.767 1.00 48.55  ? 1303 GLN A C     1 
ATOM   10499 O O     . GLN B 2 1306 ? 118.540 152.046 109.924 1.00 48.55  ? 1303 GLN A O     1 
ATOM   10500 C CB    . GLN B 2 1306 ? 120.355 149.305 110.133 1.00 48.55  ? 1303 GLN A CB    1 
ATOM   10501 C CG    . GLN B 2 1306 ? 121.785 148.943 109.778 1.00 48.55  ? 1303 GLN A CG    1 
ATOM   10502 C CD    . GLN B 2 1306 ? 121.920 147.527 109.268 1.00 48.55  ? 1303 GLN A CD    1 
ATOM   10503 O OE1   . GLN B 2 1306 ? 120.959 146.759 109.272 1.00 48.55  ? 1303 GLN A OE1   1 
ATOM   10504 N NE2   . GLN B 2 1306 ? 123.118 147.170 108.824 1.00 48.55  ? 1303 GLN A NE2   1 
ATOM   10505 N N     . GLU B 2 1307 ? 117.894 150.692 111.603 1.00 48.55  ? 1304 GLU A N     1 
ATOM   10506 C CA    . GLU B 2 1307 ? 116.528 151.207 111.588 1.00 48.55  ? 1304 GLU A CA    1 
ATOM   10507 C C     . GLU B 2 1307 ? 116.475 152.649 112.076 1.00 48.55  ? 1304 GLU A C     1 
ATOM   10508 O O     . GLU B 2 1307 ? 115.699 153.458 111.554 1.00 48.55  ? 1304 GLU A O     1 
ATOM   10509 C CB    . GLU B 2 1307 ? 115.623 150.318 112.440 1.00 48.55  ? 1304 GLU A CB    1 
ATOM   10510 C CG    . GLU B 2 1307 ? 114.157 150.715 112.417 1.00 48.55  ? 1304 GLU A CG    1 
ATOM   10511 C CD    . GLU B 2 1307 ? 113.288 149.779 113.234 1.00 48.55  ? 1304 GLU A CD    1 
ATOM   10512 O OE1   . GLU B 2 1307 ? 113.764 149.279 114.275 1.00 48.55  ? 1304 GLU A OE1   1 
ATOM   10513 O OE2   . GLU B 2 1307 ? 112.128 149.543 112.835 1.00 48.55  ? 1304 GLU A OE2   1 
ATOM   10514 N N     . LEU B 2 1308 ? 117.287 152.986 113.080 1.00 48.55  ? 1305 LEU A N     1 
ATOM   10515 C CA    . LEU B 2 1308 ? 117.269 154.337 113.632 1.00 48.55  ? 1305 LEU A CA    1 
ATOM   10516 C C     . LEU B 2 1308 ? 117.689 155.368 112.592 1.00 48.55  ? 1305 LEU A C     1 
ATOM   10517 O O     . LEU B 2 1308 ? 117.080 156.440 112.493 1.00 48.55  ? 1305 LEU A O     1 
ATOM   10518 C CB    . LEU B 2 1308 ? 118.175 154.409 114.862 1.00 48.55  ? 1305 LEU A CB    1 
ATOM   10519 C CG    . LEU B 2 1308 ? 117.996 155.595 115.813 1.00 48.55  ? 1305 LEU A CG    1 
ATOM   10520 C CD1   . LEU B 2 1308 ? 118.263 155.163 117.246 1.00 48.55  ? 1305 LEU A CD1   1 
ATOM   10521 C CD2   . LEU B 2 1308 ? 118.902 156.753 115.432 1.00 48.55  ? 1305 LEU A CD2   1 
ATOM   10522 N N     . ARG B 2 1309 ? 118.725 155.065 111.809 1.00 48.55  ? 1306 ARG A N     1 
ATOM   10523 C CA    . ARG B 2 1309 ? 119.198 156.000 110.797 1.00 48.55  ? 1306 ARG A CA    1 
ATOM   10524 C C     . ARG B 2 1309 ? 118.269 156.092 109.594 1.00 48.55  ? 1306 ARG A C     1 
ATOM   10525 O O     . ARG B 2 1309 ? 118.406 157.028 108.800 1.00 48.55  ? 1306 ARG A O     1 
ATOM   10526 C CB    . ARG B 2 1309 ? 120.601 155.609 110.335 1.00 48.55  ? 1306 ARG A CB    1 
ATOM   10527 C CG    . ARG B 2 1309 ? 121.648 155.660 111.432 1.00 48.55  ? 1306 ARG A CG    1 
ATOM   10528 C CD    . ARG B 2 1309 ? 121.908 157.087 111.879 1.00 48.55  ? 1306 ARG A CD    1 
ATOM   10529 N NE    . ARG B 2 1309 ? 123.137 157.197 112.655 1.00 48.55  ? 1306 ARG A NE    1 
ATOM   10530 C CZ    . ARG B 2 1309 ? 123.210 157.054 113.971 1.00 48.55  ? 1306 ARG A CZ    1 
ATOM   10531 N NH1   . ARG B 2 1309 ? 122.136 156.797 114.698 1.00 48.55  ? 1306 ARG A NH1   1 
ATOM   10532 N NH2   . ARG B 2 1309 ? 124.390 157.173 114.572 1.00 48.55  ? 1306 ARG A NH2   1 
ATOM   10533 N N     . ASN B 2 1310 ? 117.340 155.155 109.437 1.00 48.55  ? 1307 ASN A N     1 
ATOM   10534 C CA    . ASN B 2 1310 ? 116.384 155.212 108.339 1.00 48.55  ? 1307 ASN A CA    1 
ATOM   10535 C C     . ASN B 2 1310 ? 115.310 156.255 108.633 1.00 48.55  ? 1307 ASN A C     1 
ATOM   10536 O O     . ASN B 2 1310 ? 114.839 156.374 109.764 1.00 48.55  ? 1307 ASN A O     1 
ATOM   10537 C CB    . ASN B 2 1310 ? 115.745 153.841 108.106 1.00 48.55  ? 1307 ASN A CB    1 
ATOM   10538 C CG    . ASN B 2 1310 ? 114.960 153.773 106.808 1.00 48.55  ? 1307 ASN A CG    1 
ATOM   10539 O OD1   . ASN B 2 1310 ? 114.877 154.751 106.064 1.00 48.55  ? 1307 ASN A OD1   1 
ATOM   10540 N ND2   . ASN B 2 1310 ? 114.379 152.613 106.529 1.00 48.55  ? 1307 ASN A ND2   1 
ATOM   10541 O OXT   . ASN B 2 1310 ? 114.886 157.002 107.752 1.00 35.58  ? 1307 ASN A OXT   1 
ATOM   10542 P P     . DG  C 3 1    ? 143.734 138.847 201.672 1.00 285.35 ? 1    DG  C P     1 
ATOM   10543 O OP1   . DG  C 3 1    ? 143.982 138.407 203.063 1.00 285.35 ? 1    DG  C OP1   1 
ATOM   10544 O OP2   . DG  C 3 1    ? 142.912 140.050 201.411 1.00 285.35 ? 1    DG  C OP2   1 
ATOM   10545 O "O5'" . DG  C 3 1    ? 145.136 139.032 200.922 1.00 285.35 ? 1    DG  C "O5'" 1 
ATOM   10546 C "C5'" . DG  C 3 1    ? 146.353 139.007 201.663 1.00 285.35 ? 1    DG  C "C5'" 1 
ATOM   10547 C "C4'" . DG  C 3 1    ? 146.590 140.335 202.360 1.00 285.35 ? 1    DG  C "C4'" 1 
ATOM   10548 O "O4'" . DG  C 3 1    ? 147.962 140.390 202.835 1.00 285.35 ? 1    DG  C "O4'" 1 
ATOM   10549 C "C3'" . DG  C 3 1    ? 146.409 141.563 201.476 1.00 285.35 ? 1    DG  C "C3'" 1 
ATOM   10550 O "O3'" . DG  C 3 1    ? 145.917 142.660 202.245 1.00 285.35 ? 1    DG  C "O3'" 1 
ATOM   10551 C "C2'" . DG  C 3 1    ? 147.823 141.822 200.974 1.00 285.35 ? 1    DG  C "C2'" 1 
ATOM   10552 C "C1'" . DG  C 3 1    ? 148.659 141.436 202.185 1.00 285.35 ? 1    DG  C "C1'" 1 
ATOM   10553 N N9    . DG  C 3 1    ? 149.996 140.960 201.838 1.00 285.35 ? 1    DG  C N9    1 
ATOM   10554 C C8    . DG  C 3 1    ? 150.511 139.706 202.058 1.00 285.35 ? 1    DG  C C8    1 
ATOM   10555 N N7    . DG  C 3 1    ? 151.738 139.567 201.638 1.00 285.35 ? 1    DG  C N7    1 
ATOM   10556 C C5    . DG  C 3 1    ? 152.057 140.808 201.101 1.00 285.35 ? 1    DG  C C5    1 
ATOM   10557 C C6    . DG  C 3 1    ? 153.254 141.259 200.495 1.00 285.35 ? 1    DG  C C6    1 
ATOM   10558 O O6    . DG  C 3 1    ? 154.304 140.629 200.306 1.00 285.35 ? 1    DG  C O6    1 
ATOM   10559 N N1    . DG  C 3 1    ? 153.157 142.588 200.087 1.00 285.35 ? 1    DG  C N1    1 
ATOM   10560 C C2    . DG  C 3 1    ? 152.044 143.380 200.245 1.00 285.35 ? 1    DG  C C2    1 
ATOM   10561 N N2    . DG  C 3 1    ? 152.139 144.639 199.790 1.00 285.35 ? 1    DG  C N2    1 
ATOM   10562 N N3    . DG  C 3 1    ? 150.917 142.970 200.813 1.00 285.35 ? 1    DG  C N3    1 
ATOM   10563 C C4    . DG  C 3 1    ? 150.995 141.677 201.215 1.00 285.35 ? 1    DG  C C4    1 
ATOM   10564 P P     . DT  C 3 2    ? 144.566 143.415 201.806 1.00 262.05 ? 2    DT  C P     1 
ATOM   10565 O OP1   . DT  C 3 2    ? 143.755 143.616 203.027 1.00 262.05 ? 2    DT  C OP1   1 
ATOM   10566 O OP2   . DT  C 3 2    ? 143.993 142.672 200.662 1.00 262.05 ? 2    DT  C OP2   1 
ATOM   10567 O "O5'" . DT  C 3 2    ? 145.062 144.845 201.279 1.00 262.05 ? 2    DT  C "O5'" 1 
ATOM   10568 C "C5'" . DT  C 3 2    ? 146.174 144.937 200.391 1.00 262.05 ? 2    DT  C "C5'" 1 
ATOM   10569 C "C4'" . DT  C 3 2    ? 145.782 145.609 199.088 1.00 262.05 ? 2    DT  C "C4'" 1 
ATOM   10570 O "O4'" . DT  C 3 2    ? 146.773 145.296 198.080 1.00 262.05 ? 2    DT  C "O4'" 1 
ATOM   10571 C "C3'" . DT  C 3 2    ? 144.478 145.123 198.485 1.00 262.05 ? 2    DT  C "C3'" 1 
ATOM   10572 O "O3'" . DT  C 3 2    ? 144.023 146.060 197.519 1.00 262.05 ? 2    DT  C "O3'" 1 
ATOM   10573 C "C2'" . DT  C 3 2    ? 144.934 143.836 197.818 1.00 262.05 ? 2    DT  C "C2'" 1 
ATOM   10574 C "C1'" . DT  C 3 2    ? 146.273 144.277 197.228 1.00 262.05 ? 2    DT  C "C1'" 1 
ATOM   10575 N N1    . DT  C 3 2    ? 147.286 143.188 197.155 1.00 262.05 ? 2    DT  C N1    1 
ATOM   10576 C C2    . DT  C 3 2    ? 148.516 143.457 196.607 1.00 262.05 ? 2    DT  C C2    1 
ATOM   10577 O O2    . DT  C 3 2    ? 148.827 144.550 196.167 1.00 262.05 ? 2    DT  C O2    1 
ATOM   10578 N N3    . DT  C 3 2    ? 149.378 142.396 196.587 1.00 262.05 ? 2    DT  C N3    1 
ATOM   10579 C C4    . DT  C 3 2    ? 149.139 141.117 197.053 1.00 262.05 ? 2    DT  C C4    1 
ATOM   10580 O O4    . DT  C 3 2    ? 149.984 140.229 196.990 1.00 262.05 ? 2    DT  C O4    1 
ATOM   10581 C C5    . DT  C 3 2    ? 147.828 140.900 197.617 1.00 262.05 ? 2    DT  C C5    1 
ATOM   10582 C C7    . DT  C 3 2    ? 147.452 139.551 198.155 1.00 262.05 ? 2    DT  C C7    1 
ATOM   10583 C C6    . DT  C 3 2    ? 146.973 141.935 197.639 1.00 262.05 ? 2    DT  C C6    1 
ATOM   10584 P P     . DA  C 3 3    ? 142.937 147.177 197.912 1.00 234.35 ? 3    DA  C P     1 
ATOM   10585 O OP1   . DA  C 3 3    ? 143.301 147.721 199.239 1.00 234.35 ? 3    DA  C OP1   1 
ATOM   10586 O OP2   . DA  C 3 3    ? 141.595 146.591 197.701 1.00 234.35 ? 3    DA  C OP2   1 
ATOM   10587 O "O5'" . DA  C 3 3    ? 143.150 148.318 196.811 1.00 234.35 ? 3    DA  C "O5'" 1 
ATOM   10588 C "C5'" . DA  C 3 3    ? 142.912 148.036 195.435 1.00 234.35 ? 3    DA  C "C5'" 1 
ATOM   10589 C "C4'" . DA  C 3 3    ? 144.199 148.108 194.632 1.00 234.35 ? 3    DA  C "C4'" 1 
ATOM   10590 O "O4'" . DA  C 3 3    ? 144.996 146.915 194.881 1.00 234.35 ? 3    DA  C "O4'" 1 
ATOM   10591 C "C3'" . DA  C 3 3    ? 144.007 148.137 193.121 1.00 234.35 ? 3    DA  C "C3'" 1 
ATOM   10592 O "O3'" . DA  C 3 3    ? 145.137 148.753 192.514 1.00 234.35 ? 3    DA  C "O3'" 1 
ATOM   10593 C "C2'" . DA  C 3 3    ? 143.969 146.651 192.806 1.00 234.35 ? 3    DA  C "C2'" 1 
ATOM   10594 C "C1'" . DA  C 3 3    ? 145.126 146.186 193.673 1.00 234.35 ? 3    DA  C "C1'" 1 
ATOM   10595 N N9    . DA  C 3 3    ? 145.125 144.758 193.982 1.00 234.35 ? 3    DA  C N9    1 
ATOM   10596 C C8    . DA  C 3 3    ? 144.108 144.031 194.535 1.00 234.35 ? 3    DA  C C8    1 
ATOM   10597 N N7    . DA  C 3 3    ? 144.401 142.763 194.713 1.00 234.35 ? 3    DA  C N7    1 
ATOM   10598 C C5    . DA  C 3 3    ? 145.701 142.651 194.245 1.00 234.35 ? 3    DA  C C5    1 
ATOM   10599 C C6    . DA  C 3 3    ? 146.590 141.560 194.156 1.00 234.35 ? 3    DA  C C6    1 
ATOM   10600 N N6    . DA  C 3 3    ? 146.278 140.323 194.555 1.00 234.35 ? 3    DA  C N6    1 
ATOM   10601 N N1    . DA  C 3 3    ? 147.816 141.791 193.638 1.00 234.35 ? 3    DA  C N1    1 
ATOM   10602 C C2    . DA  C 3 3    ? 148.124 143.032 193.245 1.00 234.35 ? 3    DA  C C2    1 
ATOM   10603 N N3    . DA  C 3 3    ? 147.374 144.133 193.278 1.00 234.35 ? 3    DA  C N3    1 
ATOM   10604 C C4    . DA  C 3 3    ? 146.163 143.872 193.794 1.00 234.35 ? 3    DA  C C4    1 
ATOM   10605 P P     . DG  C 3 4    ? 144.952 149.943 191.451 1.00 192.82 ? 4    DG  C P     1 
ATOM   10606 O OP1   . DG  C 3 4    ? 145.001 151.220 192.196 1.00 192.82 ? 4    DG  C OP1   1 
ATOM   10607 O OP2   . DG  C 3 4    ? 143.773 149.622 190.615 1.00 192.82 ? 4    DG  C OP2   1 
ATOM   10608 O "O5'" . DG  C 3 4    ? 146.255 149.834 190.526 1.00 192.82 ? 4    DG  C "O5'" 1 
ATOM   10609 C "C5'" . DG  C 3 4    ? 147.555 149.847 191.116 1.00 192.82 ? 4    DG  C "C5'" 1 
ATOM   10610 C "C4'" . DG  C 3 4    ? 148.623 149.407 190.121 1.00 192.82 ? 4    DG  C "C4'" 1 
ATOM   10611 O "O4'" . DG  C 3 4    ? 148.853 147.982 190.239 1.00 192.82 ? 4    DG  C "O4'" 1 
ATOM   10612 C "C3'" . DG  C 3 4    ? 148.297 149.648 188.657 1.00 192.82 ? 4    DG  C "C3'" 1 
ATOM   10613 O "O3'" . DG  C 3 4    ? 149.492 149.880 187.929 1.00 192.82 ? 4    DG  C "O3'" 1 
ATOM   10614 C "C2'" . DG  C 3 4    ? 147.631 148.341 188.235 1.00 192.82 ? 4    DG  C "C2'" 1 
ATOM   10615 C "C1'" . DG  C 3 4    ? 148.327 147.301 189.113 1.00 192.82 ? 4    DG  C "C1'" 1 
ATOM   10616 N N9    . DG  C 3 4    ? 147.424 146.268 189.605 1.00 192.82 ? 4    DG  C N9    1 
ATOM   10617 C C8    . DG  C 3 4    ? 146.158 146.454 190.098 1.00 192.82 ? 4    DG  C C8    1 
ATOM   10618 N N7    . DG  C 3 4    ? 145.581 145.351 190.475 1.00 192.82 ? 4    DG  C N7    1 
ATOM   10619 C C5    . DG  C 3 4    ? 146.527 144.369 190.236 1.00 192.82 ? 4    DG  C C5    1 
ATOM   10620 C C6    . DG  C 3 4    ? 146.461 142.976 190.454 1.00 192.82 ? 4    DG  C C6    1 
ATOM   10621 O O6    . DG  C 3 4    ? 145.523 142.317 190.924 1.00 192.82 ? 4    DG  C O6    1 
ATOM   10622 N N1    . DG  C 3 4    ? 147.637 142.339 190.071 1.00 192.82 ? 4    DG  C N1    1 
ATOM   10623 C C2    . DG  C 3 4    ? 148.741 142.973 189.542 1.00 192.82 ? 4    DG  C C2    1 
ATOM   10624 N N2    . DG  C 3 4    ? 149.784 142.188 189.227 1.00 192.82 ? 4    DG  C N2    1 
ATOM   10625 N N3    . DG  C 3 4    ? 148.813 144.282 189.329 1.00 192.82 ? 4    DG  C N3    1 
ATOM   10626 C C4    . DG  C 3 4    ? 147.673 144.915 189.700 1.00 192.82 ? 4    DG  C C4    1 
ATOM   10627 P P     . DT  C 3 5    ? 149.436 150.194 186.355 1.00 154.60 ? 5    DT  C P     1 
ATOM   10628 O OP1   . DT  C 3 5    ? 150.517 151.165 186.082 1.00 154.60 ? 5    DT  C OP1   1 
ATOM   10629 O OP2   . DT  C 3 5    ? 148.041 150.535 185.994 1.00 154.60 ? 5    DT  C OP2   1 
ATOM   10630 O "O5'" . DT  C 3 5    ? 149.801 148.792 185.671 1.00 154.60 ? 5    DT  C "O5'" 1 
ATOM   10631 C "C5'" . DT  C 3 5    ? 151.085 148.220 185.886 1.00 154.60 ? 5    DT  C "C5'" 1 
ATOM   10632 C "C4'" . DT  C 3 5    ? 151.136 146.770 185.429 1.00 154.60 ? 5    DT  C "C4'" 1 
ATOM   10633 O "O4'" . DT  C 3 5    ? 150.171 145.973 186.166 1.00 154.60 ? 5    DT  C "O4'" 1 
ATOM   10634 C "C3'" . DT  C 3 5    ? 150.842 146.525 183.943 1.00 154.60 ? 5    DT  C "C3'" 1 
ATOM   10635 O "O3'" . DT  C 3 5    ? 151.853 145.671 183.409 1.00 154.60 ? 5    DT  C "O3'" 1 
ATOM   10636 C "C2'" . DT  C 3 5    ? 149.472 145.834 183.969 1.00 154.60 ? 5    DT  C "C2'" 1 
ATOM   10637 C "C1'" . DT  C 3 5    ? 149.569 145.070 185.272 1.00 154.60 ? 5    DT  C "C1'" 1 
ATOM   10638 N N1    . DT  C 3 5    ? 148.259 144.636 185.839 1.00 154.60 ? 5    DT  C N1    1 
ATOM   10639 C C2    . DT  C 3 5    ? 148.044 143.298 186.070 1.00 154.60 ? 5    DT  C C2    1 
ATOM   10640 O O2    . DT  C 3 5    ? 148.867 142.437 185.818 1.00 154.60 ? 5    DT  C O2    1 
ATOM   10641 N N3    . DT  C 3 5    ? 146.818 142.996 186.600 1.00 154.60 ? 5    DT  C N3    1 
ATOM   10642 C C4    . DT  C 3 5    ? 145.812 143.887 186.927 1.00 154.60 ? 5    DT  C C4    1 
ATOM   10643 O O4    . DT  C 3 5    ? 144.744 143.523 187.403 1.00 154.60 ? 5    DT  C O4    1 
ATOM   10644 C C5    . DT  C 3 5    ? 146.103 145.274 186.664 1.00 154.60 ? 5    DT  C C5    1 
ATOM   10645 C C7    . DT  C 3 5    ? 145.079 146.326 186.971 1.00 154.60 ? 5    DT  C C7    1 
ATOM   10646 C C6    . DT  C 3 5    ? 147.300 145.579 186.140 1.00 154.60 ? 5    DT  C C6    1 
ATOM   10647 P P     . DG  C 3 6    ? 151.943 145.357 181.835 1.00 120.98 ? 6    DG  C P     1 
ATOM   10648 O OP1   . DG  C 3 6    ? 153.196 145.960 181.333 1.00 120.98 ? 6    DG  C OP1   1 
ATOM   10649 O OP2   . DG  C 3 6    ? 150.658 145.690 181.185 1.00 120.98 ? 6    DG  C OP2   1 
ATOM   10650 O "O5'" . DG  C 3 6    ? 152.090 143.769 181.788 1.00 120.98 ? 6    DG  C "O5'" 1 
ATOM   10651 C "C5'" . DG  C 3 6    ? 151.218 142.962 182.563 1.00 120.98 ? 6    DG  C "C5'" 1 
ATOM   10652 C "C4'" . DG  C 3 6    ? 150.462 141.993 181.679 1.00 120.98 ? 6    DG  C "C4'" 1 
ATOM   10653 O "O4'" . DG  C 3 6    ? 149.140 141.761 182.235 1.00 120.98 ? 6    DG  C "O4'" 1 
ATOM   10654 C "C3'" . DG  C 3 6    ? 150.235 142.473 180.246 1.00 120.98 ? 6    DG  C "C3'" 1 
ATOM   10655 O "O3'" . DG  C 3 6    ? 150.370 141.379 179.350 1.00 120.98 ? 6    DG  C "O3'" 1 
ATOM   10656 C "C2'" . DG  C 3 6    ? 148.802 142.993 180.286 1.00 120.98 ? 6    DG  C "C2'" 1 
ATOM   10657 C "C1'" . DG  C 3 6    ? 148.167 142.006 181.246 1.00 120.98 ? 6    DG  C "C1'" 1 
ATOM   10658 N N9    . DG  C 3 6    ? 146.959 142.505 181.895 1.00 120.98 ? 6    DG  C N9    1 
ATOM   10659 C C8    . DG  C 3 6    ? 146.592 143.816 182.075 1.00 120.98 ? 6    DG  C C8    1 
ATOM   10660 N N7    . DG  C 3 6    ? 145.452 143.955 182.695 1.00 120.98 ? 6    DG  C N7    1 
ATOM   10661 C C5    . DG  C 3 6    ? 145.039 142.651 182.940 1.00 120.98 ? 6    DG  C C5    1 
ATOM   10662 C C6    . DG  C 3 6    ? 143.875 142.168 183.583 1.00 120.98 ? 6    DG  C C6    1 
ATOM   10663 O O6    . DG  C 3 6    ? 142.945 142.818 184.080 1.00 120.98 ? 6    DG  C O6    1 
ATOM   10664 N N1    . DG  C 3 6    ? 143.846 140.777 183.617 1.00 120.98 ? 6    DG  C N1    1 
ATOM   10665 C C2    . DG  C 3 6    ? 144.818 139.957 183.094 1.00 120.98 ? 6    DG  C C2    1 
ATOM   10666 N N2    . DG  C 3 6    ? 144.626 138.637 183.223 1.00 120.98 ? 6    DG  C N2    1 
ATOM   10667 N N3    . DG  C 3 6    ? 145.913 140.399 182.495 1.00 120.98 ? 6    DG  C N3    1 
ATOM   10668 C C4    . DG  C 3 6    ? 145.955 141.750 182.453 1.00 120.98 ? 6    DG  C C4    1 
HETATM 10669 P P     . 2YR C 3 7    ? 150.355 141.624 177.763 1.00 102.66 ? 7    2YR C P     1 
HETATM 10670 O OP1   . 2YR C 3 7    ? 151.344 140.703 177.161 1.00 102.66 ? 7    2YR C OP1   1 
HETATM 10671 O OP2   . 2YR C 3 7    ? 150.470 143.080 177.525 1.00 102.66 ? 7    2YR C OP2   1 
HETATM 10672 O "O5'" . 2YR C 3 7    ? 148.889 141.163 177.322 1.00 102.66 ? 7    2YR C "O5'" 1 
HETATM 10673 C "C5'" . 2YR C 3 7    ? 148.719 139.980 176.550 1.00 102.66 ? 7    2YR C "C5'" 1 
HETATM 10674 C "C4'" . 2YR C 3 7    ? 148.020 138.901 177.358 1.00 102.66 ? 7    2YR C "C4'" 1 
HETATM 10675 O "O4'" . 2YR C 3 7    ? 147.352 139.506 178.498 1.00 102.66 ? 7    2YR C "O4'" 1 
HETATM 10676 C "C3'" . 2YR C 3 7    ? 146.936 138.139 176.600 1.00 102.66 ? 7    2YR C "C3'" 1 
HETATM 10677 O "O3'" . 2YR C 3 7    ? 146.870 136.789 177.053 1.00 102.66 ? 7    2YR C "O3'" 1 
HETATM 10678 C "C2'" . 2YR C 3 7    ? 145.683 138.909 176.978 1.00 102.66 ? 7    2YR C "C2'" 1 
HETATM 10679 C "C1'" . 2YR C 3 7    ? 145.970 139.226 178.436 1.00 102.66 ? 7    2YR C "C1'" 1 
HETATM 10680 N N1    . 2YR C 3 7    ? 145.222 140.405 178.939 1.00 102.66 ? 7    2YR C N1    1 
HETATM 10681 C C2    . 2YR C 3 7    ? 144.093 140.218 179.743 1.00 102.66 ? 7    2YR C C2    1 
HETATM 10682 O O2    . 2YR C 3 7    ? 143.741 139.068 180.030 1.00 102.66 ? 7    2YR C O2    1 
HETATM 10683 N N3    . 2YR C 3 7    ? 143.420 141.305 180.190 1.00 102.66 ? 7    2YR C N3    1 
HETATM 10684 C C4    . 2YR C 3 7    ? 143.832 142.528 179.857 1.00 102.66 ? 7    2YR C C4    1 
HETATM 10685 N N4    . 2YR C 3 7    ? 143.137 143.572 180.322 1.00 102.66 ? 7    2YR C N4    1 
HETATM 10686 C C5    . 2YR C 3 7    ? 144.980 142.734 179.035 1.00 102.66 ? 7    2YR C C5    1 
HETATM 10687 C C6    . 2YR C 3 7    ? 145.636 141.657 178.603 1.00 102.66 ? 7    2YR C C6    1 
HETATM 10688 S S     . 2YR C 3 7    ? 144.462 145.917 179.707 1.00 97.95  ? 7    2YR C S     1 
HETATM 10689 C C8    . 2YR C 3 7    ? 142.698 145.724 179.386 1.00 97.95  ? 7    2YR C C8    1 
HETATM 10690 C C9    . 2YR C 3 7    ? 142.213 144.273 179.436 1.00 97.95  ? 7    2YR C C9    1 
ATOM   10691 P P     . DT  C 3 8    ? 146.141 135.671 176.155 1.00 85.82  ? 8    DT  C P     1 
ATOM   10692 O OP1   . DT  C 3 8    ? 147.150 134.639 175.832 1.00 85.82  ? 8    DT  C OP1   1 
ATOM   10693 O OP2   . DT  C 3 8    ? 145.429 136.366 175.060 1.00 85.82  ? 8    DT  C OP2   1 
ATOM   10694 O "O5'" . DT  C 3 8    ? 145.042 135.034 177.133 1.00 85.82  ? 8    DT  C "O5'" 1 
ATOM   10695 C "C5'" . DT  C 3 8    ? 144.229 135.880 177.938 1.00 85.82  ? 8    DT  C "C5'" 1 
ATOM   10696 C "C4'" . DT  C 3 8    ? 142.885 135.240 178.236 1.00 85.82  ? 8    DT  C "C4'" 1 
ATOM   10697 O "O4'" . DT  C 3 8    ? 142.015 136.238 178.834 1.00 85.82  ? 8    DT  C "O4'" 1 
ATOM   10698 C "C3'" . DT  C 3 8    ? 142.119 134.759 177.016 1.00 85.82  ? 8    DT  C "C3'" 1 
ATOM   10699 O "O3'" . DT  C 3 8    ? 141.124 133.813 177.415 1.00 85.82  ? 8    DT  C "O3'" 1 
ATOM   10700 C "C2'" . DT  C 3 8    ? 141.488 136.057 176.553 1.00 85.82  ? 8    DT  C "C2'" 1 
ATOM   10701 C "C1'" . DT  C 3 8    ? 141.042 136.642 177.884 1.00 85.82  ? 8    DT  C "C1'" 1 
ATOM   10702 N N1    . DT  C 3 8    ? 140.952 138.131 177.887 1.00 85.82  ? 8    DT  C N1    1 
ATOM   10703 C C2    . DT  C 3 8    ? 139.930 138.735 178.572 1.00 85.82  ? 8    DT  C C2    1 
ATOM   10704 O O2    . DT  C 3 8    ? 139.082 138.116 179.188 1.00 85.82  ? 8    DT  C O2    1 
ATOM   10705 N N3    . DT  C 3 8    ? 139.933 140.100 178.515 1.00 85.82  ? 8    DT  C N3    1 
ATOM   10706 C C4    . DT  C 3 8    ? 140.835 140.908 177.853 1.00 85.82  ? 8    DT  C C4    1 
ATOM   10707 O O4    . DT  C 3 8    ? 140.751 142.131 177.863 1.00 85.82  ? 8    DT  C O4    1 
ATOM   10708 C C5    . DT  C 3 8    ? 141.882 140.215 177.151 1.00 85.82  ? 8    DT  C C5    1 
ATOM   10709 C C7    . DT  C 3 8    ? 142.917 140.991 176.396 1.00 85.82  ? 8    DT  C C7    1 
ATOM   10710 C C6    . DT  C 3 8    ? 141.892 138.873 177.199 1.00 85.82  ? 8    DT  C C6    1 
ATOM   10711 P P     . DT  C 3 9    ? 140.082 133.198 176.351 1.00 70.79  ? 9    DT  C P     1 
ATOM   10712 O OP1   . DT  C 3 9    ? 140.055 131.738 176.583 1.00 70.79  ? 9    DT  C OP1   1 
ATOM   10713 O OP2   . DT  C 3 9    ? 140.391 133.703 174.996 1.00 70.79  ? 9    DT  C OP2   1 
ATOM   10714 O "O5'" . DT  C 3 9    ? 138.669 133.800 176.802 1.00 70.79  ? 9    DT  C "O5'" 1 
ATOM   10715 C "C5'" . DT  C 3 9    ? 138.100 133.413 178.053 1.00 70.79  ? 9    DT  C "C5'" 1 
ATOM   10716 C "C4'" . DT  C 3 9    ? 136.716 134.018 178.255 1.00 70.79  ? 9    DT  C "C4'" 1 
ATOM   10717 O "O4'" . DT  C 3 9    ? 136.785 135.466 178.163 1.00 70.79  ? 9    DT  C "O4'" 1 
ATOM   10718 C "C3'" . DT  C 3 9    ? 135.654 133.598 177.246 1.00 70.79  ? 9    DT  C "C3'" 1 
ATOM   10719 O "O3'" . DT  C 3 9    ? 134.380 133.588 177.885 1.00 70.79  ? 9    DT  C "O3'" 1 
ATOM   10720 C "C2'" . DT  C 3 9    ? 135.748 134.708 176.208 1.00 70.79  ? 9    DT  C "C2'" 1 
ATOM   10721 C "C1'" . DT  C 3 9    ? 135.965 135.918 177.101 1.00 70.79  ? 9    DT  C "C1'" 1 
ATOM   10722 N N1    . DT  C 3 9    ? 136.662 137.068 176.444 1.00 70.79  ? 9    DT  C N1    1 
ATOM   10723 C C2    . DT  C 3 9    ? 136.226 138.346 176.702 1.00 70.79  ? 9    DT  C C2    1 
ATOM   10724 O O2    . DT  C 3 9    ? 135.275 138.595 177.419 1.00 70.79  ? 9    DT  C O2    1 
ATOM   10725 N N3    . DT  C 3 9    ? 136.944 139.332 176.079 1.00 70.79  ? 9    DT  C N3    1 
ATOM   10726 C C4    . DT  C 3 9    ? 138.034 139.176 175.250 1.00 70.79  ? 9    DT  C C4    1 
ATOM   10727 O O4    . DT  C 3 9    ? 138.611 140.129 174.740 1.00 70.79  ? 9    DT  C O4    1 
ATOM   10728 C C5    . DT  C 3 9    ? 138.450 137.815 175.027 1.00 70.79  ? 9    DT  C C5    1 
ATOM   10729 C C7    . DT  C 3 9    ? 139.621 137.528 174.136 1.00 70.79  ? 9    DT  C C7    1 
ATOM   10730 C C6    . DT  C 3 9    ? 137.758 136.835 175.634 1.00 70.79  ? 9    DT  C C6    1 
ATOM   10731 P P     . DT  C 3 10   ? 133.073 133.050 177.121 1.00 67.39  ? 10   DT  C P     1 
ATOM   10732 O OP1   . DT  C 3 10   ? 132.419 132.068 178.013 1.00 67.39  ? 10   DT  C OP1   1 
ATOM   10733 O OP2   . DT  C 3 10   ? 133.457 132.646 175.751 1.00 67.39  ? 10   DT  C OP2   1 
ATOM   10734 O "O5'" . DT  C 3 10   ? 132.136 134.342 177.017 1.00 67.39  ? 10   DT  C "O5'" 1 
ATOM   10735 C "C5'" . DT  C 3 10   ? 131.755 135.043 178.200 1.00 67.39  ? 10   DT  C "C5'" 1 
ATOM   10736 C "C4'" . DT  C 3 10   ? 130.869 136.235 177.874 1.00 67.39  ? 10   DT  C "C4'" 1 
ATOM   10737 O "O4'" . DT  C 3 10   ? 131.678 137.326 177.354 1.00 67.39  ? 10   DT  C "O4'" 1 
ATOM   10738 C "C3'" . DT  C 3 10   ? 129.794 135.977 176.821 1.00 67.39  ? 10   DT  C "C3'" 1 
ATOM   10739 O "O3'" . DT  C 3 10   ? 128.619 136.719 177.141 1.00 67.39  ? 10   DT  C "O3'" 1 
ATOM   10740 C "C2'" . DT  C 3 10   ? 130.453 136.500 175.549 1.00 67.39  ? 10   DT  C "C2'" 1 
ATOM   10741 C "C1'" . DT  C 3 10   ? 131.185 137.717 176.090 1.00 67.39  ? 10   DT  C "C1'" 1 
ATOM   10742 N N1    . DT  C 3 10   ? 132.340 138.165 175.247 1.00 67.39  ? 10   DT  C N1    1 
ATOM   10743 C C2    . DT  C 3 10   ? 132.525 139.511 175.015 1.00 67.39  ? 10   DT  C C2    1 
ATOM   10744 O O2    . DT  C 3 10   ? 131.782 140.373 175.449 1.00 67.39  ? 10   DT  C O2    1 
ATOM   10745 N N3    . DT  C 3 10   ? 133.613 139.811 174.237 1.00 67.39  ? 10   DT  C N3    1 
ATOM   10746 C C4    . DT  C 3 10   ? 134.518 138.924 173.692 1.00 67.39  ? 10   DT  C C4    1 
ATOM   10747 O O4    . DT  C 3 10   ? 135.466 139.286 173.007 1.00 67.39  ? 10   DT  C O4    1 
ATOM   10748 C C5    . DT  C 3 10   ? 134.271 137.537 173.975 1.00 67.39  ? 10   DT  C C5    1 
ATOM   10749 C C7    . DT  C 3 10   ? 135.188 136.491 173.419 1.00 67.39  ? 10   DT  C C7    1 
ATOM   10750 C C6    . DT  C 3 10   ? 133.207 137.224 174.732 1.00 67.39  ? 10   DT  C C6    1 
ATOM   10751 P P     . DG  C 3 11   ? 127.165 136.050 176.988 1.00 71.33  ? 11   DG  C P     1 
ATOM   10752 O OP1   . DG  C 3 11   ? 126.599 135.897 178.346 1.00 71.33  ? 11   DG  C OP1   1 
ATOM   10753 O OP2   . DG  C 3 11   ? 127.300 134.867 176.111 1.00 71.33  ? 11   DG  C OP2   1 
ATOM   10754 O "O5'" . DG  C 3 11   ? 126.315 137.153 176.200 1.00 71.33  ? 11   DG  C "O5'" 1 
ATOM   10755 C "C5'" . DG  C 3 11   ? 125.810 138.294 176.888 1.00 71.33  ? 11   DG  C "C5'" 1 
ATOM   10756 C "C4'" . DG  C 3 11   ? 125.737 139.493 175.960 1.00 71.33  ? 11   DG  C "C4'" 1 
ATOM   10757 O "O4'" . DG  C 3 11   ? 127.069 139.982 175.720 1.00 71.33  ? 11   DG  C "O4'" 1 
ATOM   10758 C "C3'" . DG  C 3 11   ? 125.156 139.199 174.586 1.00 71.33  ? 11   DG  C "C3'" 1 
ATOM   10759 O "O3'" . DG  C 3 11   ? 123.746 139.443 174.596 1.00 71.33  ? 11   DG  C "O3'" 1 
ATOM   10760 C "C2'" . DG  C 3 11   ? 125.884 140.185 173.662 1.00 71.33  ? 11   DG  C "C2'" 1 
ATOM   10761 C "C1'" . DG  C 3 11   ? 127.152 140.565 174.438 1.00 71.33  ? 11   DG  C "C1'" 1 
ATOM   10762 N N9    . DG  C 3 11   ? 128.390 140.105 173.818 1.00 71.33  ? 11   DG  C N9    1 
ATOM   10763 C C8    . DG  C 3 11   ? 128.876 138.826 173.816 1.00 71.33  ? 11   DG  C C8    1 
ATOM   10764 N N7    . DG  C 3 11   ? 130.017 138.703 173.199 1.00 71.33  ? 11   DG  C N7    1 
ATOM   10765 C C5    . DG  C 3 11   ? 130.310 139.986 172.765 1.00 71.33  ? 11   DG  C C5    1 
ATOM   10766 C C6    . DG  C 3 11   ? 131.422 140.466 172.037 1.00 71.33  ? 11   DG  C C6    1 
ATOM   10767 O O6    . DG  C 3 11   ? 132.399 139.830 171.621 1.00 71.33  ? 11   DG  C O6    1 
ATOM   10768 N N1    . DG  C 3 11   ? 131.331 141.833 171.801 1.00 71.33  ? 11   DG  C N1    1 
ATOM   10769 C C2    . DG  C 3 11   ? 130.295 142.632 172.216 1.00 71.33  ? 11   DG  C C2    1 
ATOM   10770 N N2    . DG  C 3 11   ? 130.380 143.929 171.894 1.00 71.33  ? 11   DG  C N2    1 
ATOM   10771 N N3    . DG  C 3 11   ? 129.245 142.194 172.902 1.00 71.33  ? 11   DG  C N3    1 
ATOM   10772 C C4    . DG  C 3 11   ? 129.320 140.864 173.140 1.00 71.33  ? 11   DG  C C4    1 
ATOM   10773 P P     . DT  C 3 12   ? 122.700 138.221 174.602 1.00 82.83  ? 12   DT  C P     1 
ATOM   10774 O OP1   . DT  C 3 12   ? 122.569 137.752 175.998 1.00 82.83  ? 12   DT  C OP1   1 
ATOM   10775 O OP2   . DT  C 3 12   ? 123.106 137.273 173.542 1.00 82.83  ? 12   DT  C OP2   1 
ATOM   10776 O "O5'" . DT  C 3 12   ? 121.316 138.892 174.153 1.00 82.83  ? 12   DT  C "O5'" 1 
ATOM   10777 C "C5'" . DT  C 3 12   ? 120.848 138.756 172.806 1.00 82.83  ? 12   DT  C "C5'" 1 
ATOM   10778 C "C4'" . DT  C 3 12   ? 121.414 139.852 171.918 1.00 82.83  ? 12   DT  C "C4'" 1 
ATOM   10779 O "O4'" . DT  C 3 12   ? 122.845 139.878 172.060 1.00 82.83  ? 12   DT  C "O4'" 1 
ATOM   10780 C "C3'" . DT  C 3 12   ? 121.169 139.666 170.429 1.00 82.83  ? 12   DT  C "C3'" 1 
ATOM   10781 O "O3'" . DT  C 3 12   ? 119.940 140.291 170.053 1.00 82.83  ? 12   DT  C "O3'" 1 
ATOM   10782 C "C2'" . DT  C 3 12   ? 122.366 140.367 169.782 1.00 82.83  ? 12   DT  C "C2'" 1 
ATOM   10783 C "C1'" . DT  C 3 12   ? 123.435 140.367 170.880 1.00 82.83  ? 12   DT  C "C1'" 1 
ATOM   10784 N N1    . DT  C 3 12   ? 124.629 139.529 170.562 1.00 82.83  ? 12   DT  C N1    1 
ATOM   10785 C C2    . DT  C 3 12   ? 125.665 140.088 169.860 1.00 82.83  ? 12   DT  C C2    1 
ATOM   10786 O O2    . DT  C 3 12   ? 125.655 141.237 169.471 1.00 82.83  ? 12   DT  C O2    1 
ATOM   10787 N N3    . DT  C 3 12   ? 126.716 139.248 169.618 1.00 82.83  ? 12   DT  C N3    1 
ATOM   10788 C C4    . DT  C 3 12   ? 126.835 137.928 170.008 1.00 82.83  ? 12   DT  C C4    1 
ATOM   10789 O O4    . DT  C 3 12   ? 127.824 137.253 169.743 1.00 82.83  ? 12   DT  C O4    1 
ATOM   10790 C C5    . DT  C 3 12   ? 125.713 137.401 170.747 1.00 82.83  ? 12   DT  C C5    1 
ATOM   10791 C C7    . DT  C 3 12   ? 125.726 135.979 171.224 1.00 82.83  ? 12   DT  C C7    1 
ATOM   10792 C C6    . DT  C 3 12   ? 124.675 138.218 170.987 1.00 82.83  ? 12   DT  C C6    1 
ATOM   10793 P P     . DC  C 3 13   ? 119.461 140.287 168.517 1.00 94.07  ? 13   DC  C P     1 
ATOM   10794 O OP1   . DC  C 3 13   ? 118.011 140.582 168.503 1.00 94.07  ? 13   DC  C OP1   1 
ATOM   10795 O OP2   . DC  C 3 13   ? 119.963 139.042 167.896 1.00 94.07  ? 13   DC  C OP2   1 
ATOM   10796 O "O5'" . DC  C 3 13   ? 120.243 141.519 167.856 1.00 94.07  ? 13   DC  C "O5'" 1 
ATOM   10797 C "C5'" . DC  C 3 13   ? 120.321 141.642 166.436 1.00 94.07  ? 13   DC  C "C5'" 1 
ATOM   10798 C "C4'" . DC  C 3 13   ? 121.570 142.407 166.027 1.00 94.07  ? 13   DC  C "C4'" 1 
ATOM   10799 O "O4'" . DC  C 3 13   ? 122.691 141.931 166.799 1.00 94.07  ? 13   DC  C "O4'" 1 
ATOM   10800 C "C3'" . DC  C 3 13   ? 121.984 142.226 164.575 1.00 94.07  ? 13   DC  C "C3'" 1 
ATOM   10801 O "O3'" . DC  C 3 13   ? 121.354 143.217 163.759 1.00 94.07  ? 13   DC  C "O3'" 1 
ATOM   10802 C "C2'" . DC  C 3 13   ? 123.500 142.427 164.614 1.00 94.07  ? 13   DC  C "C2'" 1 
ATOM   10803 C "C1'" . DC  C 3 13   ? 123.884 142.056 166.049 1.00 94.07  ? 13   DC  C "C1'" 1 
ATOM   10804 N N1    . DC  C 3 13   ? 124.669 140.778 166.186 1.00 94.07  ? 13   DC  C N1    1 
ATOM   10805 C C2    . DC  C 3 13   ? 125.944 140.656 165.606 1.00 94.07  ? 13   DC  C C2    1 
ATOM   10806 O O2    . DC  C 3 13   ? 126.415 141.598 164.956 1.00 94.07  ? 13   DC  C O2    1 
ATOM   10807 N N3    . DC  C 3 13   ? 126.625 139.494 165.769 1.00 94.07  ? 13   DC  C N3    1 
ATOM   10808 C C4    . DC  C 3 13   ? 126.094 138.498 166.476 1.00 94.07  ? 13   DC  C C4    1 
ATOM   10809 N N4    . DC  C 3 13   ? 126.808 137.375 166.607 1.00 94.07  ? 13   DC  C N4    1 
ATOM   10810 C C5    . DC  C 3 13   ? 124.810 138.605 167.078 1.00 94.07  ? 13   DC  C C5    1 
ATOM   10811 C C6    . DC  C 3 13   ? 124.143 139.750 166.912 1.00 94.07  ? 13   DC  C C6    1 
ATOM   10812 P P     . DG  C 3 14   ? 120.897 142.864 162.258 1.00 108.20 ? 14   DG  C P     1 
ATOM   10813 O OP1   . DG  C 3 14   ? 119.460 143.197 162.148 1.00 108.20 ? 14   DG  C OP1   1 
ATOM   10814 O OP2   . DG  C 3 14   ? 121.353 141.491 161.954 1.00 108.20 ? 14   DG  C OP2   1 
ATOM   10815 O "O5'" . DG  C 3 14   ? 121.727 143.881 161.336 1.00 108.20 ? 14   DG  C "O5'" 1 
ATOM   10816 C "C5'" . DG  C 3 14   ? 122.952 144.448 161.801 1.00 108.20 ? 14   DG  C "C5'" 1 
ATOM   10817 C "C4'" . DG  C 3 14   ? 124.123 144.008 160.936 1.00 108.20 ? 14   DG  C "C4'" 1 
ATOM   10818 O "O4'" . DG  C 3 14   ? 124.871 142.966 161.620 1.00 108.20 ? 14   DG  C "O4'" 1 
ATOM   10819 C "C3'" . DG  C 3 14   ? 123.741 143.432 159.571 1.00 108.20 ? 14   DG  C "C3'" 1 
ATOM   10820 O "O3'" . DG  C 3 14   ? 124.647 143.886 158.571 1.00 108.20 ? 14   DG  C "O3'" 1 
ATOM   10821 C "C2'" . DG  C 3 14   ? 123.865 141.929 159.789 1.00 108.20 ? 14   DG  C "C2'" 1 
ATOM   10822 C "C1'" . DG  C 3 14   ? 125.029 141.860 160.762 1.00 108.20 ? 14   DG  C "C1'" 1 
ATOM   10823 N N9    . DG  C 3 14   ? 125.034 140.640 161.564 1.00 108.20 ? 14   DG  C N9    1 
ATOM   10824 C C8    . DG  C 3 14   ? 124.020 140.174 162.361 1.00 108.20 ? 14   DG  C C8    1 
ATOM   10825 N N7    . DG  C 3 14   ? 124.299 139.052 162.959 1.00 108.20 ? 14   DG  C N7    1 
ATOM   10826 C C5    . DG  C 3 14   ? 125.578 138.746 162.523 1.00 108.20 ? 14   DG  C C5    1 
ATOM   10827 C C6    . DG  C 3 14   ? 126.401 137.644 162.834 1.00 108.20 ? 14   DG  C C6    1 
ATOM   10828 O O6    . DG  C 3 14   ? 126.154 136.688 163.582 1.00 108.20 ? 14   DG  C O6    1 
ATOM   10829 N N1    . DG  C 3 14   ? 127.624 137.715 162.178 1.00 108.20 ? 14   DG  C N1    1 
ATOM   10830 C C2    . DG  C 3 14   ? 128.008 138.725 161.329 1.00 108.20 ? 14   DG  C C2    1 
ATOM   10831 N N2    . DG  C 3 14   ? 129.232 138.619 160.789 1.00 108.20 ? 14   DG  C N2    1 
ATOM   10832 N N3    . DG  C 3 14   ? 127.244 139.768 161.027 1.00 108.20 ? 14   DG  C N3    1 
ATOM   10833 C C4    . DG  C 3 14   ? 126.046 139.711 161.660 1.00 108.20 ? 14   DG  C C4    1 
ATOM   10834 P P     . DT  C 3 15   ? 124.442 143.447 157.038 1.00 115.77 ? 15   DT  C P     1 
ATOM   10835 O OP1   . DT  C 3 15   ? 125.104 144.459 156.186 1.00 115.77 ? 15   DT  C OP1   1 
ATOM   10836 O OP2   . DT  C 3 15   ? 123.005 143.152 156.845 1.00 115.77 ? 15   DT  C OP2   1 
ATOM   10837 O "O5'" . DT  C 3 15   ? 125.243 142.066 156.916 1.00 115.77 ? 15   DT  C "O5'" 1 
ATOM   10838 C "C5'" . DT  C 3 15   ? 126.650 142.035 157.136 1.00 115.77 ? 15   DT  C "C5'" 1 
ATOM   10839 C "C4'" . DT  C 3 15   ? 127.212 140.642 156.893 1.00 115.77 ? 15   DT  C "C4'" 1 
ATOM   10840 O "O4'" . DT  C 3 15   ? 126.806 139.752 157.968 1.00 115.77 ? 15   DT  C "O4'" 1 
ATOM   10841 C "C3'" . DT  C 3 15   ? 126.753 139.972 155.598 1.00 115.77 ? 15   DT  C "C3'" 1 
ATOM   10842 O "O3'" . DT  C 3 15   ? 127.831 139.242 155.023 1.00 115.77 ? 15   DT  C "O3'" 1 
ATOM   10843 C "C2'" . DT  C 3 15   ? 125.648 139.039 156.081 1.00 115.77 ? 15   DT  C "C2'" 1 
ATOM   10844 C "C1'" . DT  C 3 15   ? 126.219 138.596 157.416 1.00 115.77 ? 15   DT  C "C1'" 1 
ATOM   10845 N N1    . DT  C 3 15   ? 125.198 138.077 158.370 1.00 115.77 ? 15   DT  C N1    1 
ATOM   10846 C C2    . DT  C 3 15   ? 125.486 136.959 159.117 1.00 115.77 ? 15   DT  C C2    1 
ATOM   10847 O O2    . DT  C 3 15   ? 126.543 136.360 159.041 1.00 115.77 ? 15   DT  C O2    1 
ATOM   10848 N N3    . DT  C 3 15   ? 124.488 136.565 159.966 1.00 115.77 ? 15   DT  C N3    1 
ATOM   10849 C C4    . DT  C 3 15   ? 123.254 137.163 160.140 1.00 115.77 ? 15   DT  C C4    1 
ATOM   10850 O O4    . DT  C 3 15   ? 122.421 136.732 160.930 1.00 115.77 ? 15   DT  C O4    1 
ATOM   10851 C C5    . DT  C 3 15   ? 123.015 138.330 159.326 1.00 115.77 ? 15   DT  C C5    1 
ATOM   10852 C C7    . DT  C 3 15   ? 121.710 139.064 159.426 1.00 115.77 ? 15   DT  C C7    1 
ATOM   10853 C C6    . DT  C 3 15   ? 123.987 138.726 158.489 1.00 115.77 ? 15   DT  C C6    1 
ATOM   10854 P P     . DC  C 3 16   ? 128.180 139.403 153.463 1.00 126.59 ? 16   DC  C P     1 
ATOM   10855 O OP1   . DC  C 3 16   ? 129.581 139.868 153.366 1.00 126.59 ? 16   DC  C OP1   1 
ATOM   10856 O OP2   . DC  C 3 16   ? 127.097 140.194 152.838 1.00 126.59 ? 16   DC  C OP2   1 
ATOM   10857 O "O5'" . DC  C 3 16   ? 128.094 137.911 152.890 1.00 126.59 ? 16   DC  C "O5'" 1 
ATOM   10858 C "C5'" . DC  C 3 16   ? 126.913 137.140 153.082 1.00 126.59 ? 16   DC  C "C5'" 1 
ATOM   10859 C "C4'" . DC  C 3 16   ? 127.173 135.985 154.032 1.00 126.59 ? 16   DC  C "C4'" 1 
ATOM   10860 O "O4'" . DC  C 3 16   ? 126.306 136.107 155.189 1.00 126.59 ? 16   DC  C "O4'" 1 
ATOM   10861 C "C3'" . DC  C 3 16   ? 126.897 134.602 153.456 1.00 126.59 ? 16   DC  C "C3'" 1 
ATOM   10862 O "O3'" . DC  C 3 16   ? 127.770 133.647 154.044 1.00 126.59 ? 16   DC  C "O3'" 1 
ATOM   10863 C "C2'" . DC  C 3 16   ? 125.450 134.361 153.864 1.00 126.59 ? 16   DC  C "C2'" 1 
ATOM   10864 C "C1'" . DC  C 3 16   ? 125.411 135.015 155.240 1.00 126.59 ? 16   DC  C "C1'" 1 
ATOM   10865 N N1    . DC  C 3 16   ? 124.061 135.525 155.616 1.00 126.59 ? 16   DC  C N1    1 
ATOM   10866 C C2    . DC  C 3 16   ? 123.343 134.894 156.635 1.00 126.59 ? 16   DC  C C2    1 
ATOM   10867 O O2    . DC  C 3 16   ? 123.846 133.924 157.211 1.00 126.59 ? 16   DC  C O2    1 
ATOM   10868 N N3    . DC  C 3 16   ? 122.116 135.366 156.964 1.00 126.59 ? 16   DC  C N3    1 
ATOM   10869 C C4    . DC  C 3 16   ? 121.609 136.417 156.317 1.00 126.59 ? 16   DC  C C4    1 
ATOM   10870 N N4    . DC  C 3 16   ? 120.395 136.846 156.676 1.00 126.59 ? 16   DC  C N4    1 
ATOM   10871 C C5    . DC  C 3 16   ? 122.325 137.073 155.273 1.00 126.59 ? 16   DC  C C5    1 
ATOM   10872 C C6    . DC  C 3 16   ? 123.534 136.596 154.957 1.00 126.59 ? 16   DC  C C6    1 
ATOM   10873 P P     . DG  D 4 16   ? 121.502 126.869 160.576 1.00 122.92 ? 16   DG  D P     1 
ATOM   10874 O OP1   . DG  D 4 16   ? 122.378 126.781 159.386 1.00 122.92 ? 16   DG  D OP1   1 
ATOM   10875 O OP2   . DG  D 4 16   ? 120.209 126.150 160.600 1.00 122.92 ? 16   DG  D OP2   1 
ATOM   10876 O "O5'" . DG  D 4 16   ? 122.332 126.444 161.878 1.00 122.92 ? 16   DG  D "O5'" 1 
ATOM   10877 C "C5'" . DG  D 4 16   ? 123.325 125.423 161.792 1.00 122.92 ? 16   DG  D "C5'" 1 
ATOM   10878 C "C4'" . DG  D 4 16   ? 124.722 126.021 161.735 1.00 122.92 ? 16   DG  D "C4'" 1 
ATOM   10879 O "O4'" . DG  D 4 16   ? 124.697 127.234 160.941 1.00 122.92 ? 16   DG  D "O4'" 1 
ATOM   10880 C "C3'" . DG  D 4 16   ? 125.310 126.432 163.078 1.00 122.92 ? 16   DG  D "C3'" 1 
ATOM   10881 O "O3'" . DG  D 4 16   ? 126.729 126.358 163.021 1.00 122.92 ? 16   DG  D "O3'" 1 
ATOM   10882 C "C2'" . DG  D 4 16   ? 124.837 127.872 163.204 1.00 122.92 ? 16   DG  D "C2'" 1 
ATOM   10883 C "C1'" . DG  D 4 16   ? 124.969 128.353 161.764 1.00 122.92 ? 16   DG  D "C1'" 1 
ATOM   10884 N N9    . DG  D 4 16   ? 124.033 129.414 161.415 1.00 122.92 ? 16   DG  D N9    1 
ATOM   10885 C C8    . DG  D 4 16   ? 122.788 129.629 161.951 1.00 122.92 ? 16   DG  D C8    1 
ATOM   10886 N N7    . DG  D 4 16   ? 122.172 130.657 161.437 1.00 122.92 ? 16   DG  D N7    1 
ATOM   10887 C C5    . DG  D 4 16   ? 123.067 131.155 160.501 1.00 122.92 ? 16   DG  D C5    1 
ATOM   10888 C C6    . DG  D 4 16   ? 122.953 132.263 159.632 1.00 122.92 ? 16   DG  D C6    1 
ATOM   10889 O O6    . DG  D 4 16   ? 122.005 133.052 159.514 1.00 122.92 ? 16   DG  D O6    1 
ATOM   10890 N N1    . DG  D 4 16   ? 124.090 132.419 158.845 1.00 122.92 ? 16   DG  D N1    1 
ATOM   10891 C C2    . DG  D 4 16   ? 125.197 131.606 158.891 1.00 122.92 ? 16   DG  D C2    1 
ATOM   10892 N N2    . DG  D 4 16   ? 126.197 131.916 158.054 1.00 122.92 ? 16   DG  D N2    1 
ATOM   10893 N N3    . DG  D 4 16   ? 125.317 130.564 159.701 1.00 122.92 ? 16   DG  D N3    1 
ATOM   10894 C C4    . DG  D 4 16   ? 124.217 130.400 160.475 1.00 122.92 ? 16   DG  D C4    1 
ATOM   10895 P P     . DA  D 4 17   ? 127.596 126.270 164.372 1.00 125.27 ? 17   DA  D P     1 
ATOM   10896 O OP1   . DA  D 4 17   ? 127.139 125.078 165.120 1.00 125.27 ? 17   DA  D OP1   1 
ATOM   10897 O OP2   . DA  D 4 17   ? 127.565 127.600 165.020 1.00 125.27 ? 17   DA  D OP2   1 
ATOM   10898 O "O5'" . DA  D 4 17   ? 129.088 126.012 163.852 1.00 125.27 ? 17   DA  D "O5'" 1 
ATOM   10899 C "C5'" . DA  D 4 17   ? 130.152 126.850 164.291 1.00 125.27 ? 17   DA  D "C5'" 1 
ATOM   10900 C "C4'" . DA  D 4 17   ? 130.628 127.758 163.170 1.00 125.27 ? 17   DA  D "C4'" 1 
ATOM   10901 O "O4'" . DA  D 4 17   ? 129.484 128.405 162.551 1.00 125.27 ? 17   DA  D "O4'" 1 
ATOM   10902 C "C3'" . DA  D 4 17   ? 131.572 128.881 163.613 1.00 125.27 ? 17   DA  D "C3'" 1 
ATOM   10903 O "O3'" . DA  D 4 17   ? 132.691 128.980 162.736 1.00 125.27 ? 17   DA  D "O3'" 1 
ATOM   10904 C "C2'" . DA  D 4 17   ? 130.699 130.127 163.543 1.00 125.27 ? 17   DA  D "C2'" 1 
ATOM   10905 C "C1'" . DA  D 4 17   ? 129.743 129.780 162.413 1.00 125.27 ? 17   DA  D "C1'" 1 
ATOM   10906 N N9    . DA  D 4 17   ? 128.483 130.510 162.501 1.00 125.27 ? 17   DA  D N9    1 
ATOM   10907 C C8    . DA  D 4 17   ? 127.399 130.192 163.269 1.00 125.27 ? 17   DA  D C8    1 
ATOM   10908 N N7    . DA  D 4 17   ? 126.407 131.044 163.164 1.00 125.27 ? 17   DA  D N7    1 
ATOM   10909 C C5    . DA  D 4 17   ? 126.878 131.994 162.273 1.00 125.27 ? 17   DA  D C5    1 
ATOM   10910 C C6    . DA  D 4 17   ? 126.303 133.166 161.743 1.00 125.27 ? 17   DA  D C6    1 
ATOM   10911 N N6    . DA  D 4 17   ? 125.073 133.588 162.054 1.00 125.27 ? 17   DA  D N6    1 
ATOM   10912 N N1    . DA  D 4 17   ? 127.043 133.888 160.877 1.00 125.27 ? 17   DA  D N1    1 
ATOM   10913 C C2    . DA  D 4 17   ? 128.273 133.462 160.567 1.00 125.27 ? 17   DA  D C2    1 
ATOM   10914 N N3    . DA  D 4 17   ? 128.917 132.379 160.998 1.00 125.27 ? 17   DA  D N3    1 
ATOM   10915 C C4    . DA  D 4 17   ? 128.156 131.680 161.855 1.00 125.27 ? 17   DA  D C4    1 
ATOM   10916 P P     . DC  D 4 18   ? 134.004 129.784 163.202 1.00 114.28 ? 18   DC  D P     1 
ATOM   10917 O OP1   . DC  D 4 18   ? 135.178 129.105 162.612 1.00 114.28 ? 18   DC  D OP1   1 
ATOM   10918 O OP2   . DC  D 4 18   ? 133.919 129.965 164.668 1.00 114.28 ? 18   DC  D OP2   1 
ATOM   10919 O "O5'" . DC  D 4 18   ? 133.848 131.228 162.525 1.00 114.28 ? 18   DC  D "O5'" 1 
ATOM   10920 C "C5'" . DC  D 4 18   ? 134.296 131.437 161.188 1.00 114.28 ? 18   DC  D "C5'" 1 
ATOM   10921 C "C4'" . DC  D 4 18   ? 134.264 132.913 160.817 1.00 114.28 ? 18   DC  D "C4'" 1 
ATOM   10922 O "O4'" . DC  D 4 18   ? 132.897 133.401 160.863 1.00 114.28 ? 18   DC  D "O4'" 1 
ATOM   10923 C "C3'" . DC  D 4 18   ? 135.076 133.838 161.725 1.00 114.28 ? 18   DC  D "C3'" 1 
ATOM   10924 O "O3'" . DC  D 4 18   ? 135.728 134.833 160.942 1.00 114.28 ? 18   DC  D "O3'" 1 
ATOM   10925 C "C2'" . DC  D 4 18   ? 134.011 134.453 162.627 1.00 114.28 ? 18   DC  D "C2'" 1 
ATOM   10926 C "C1'" . DC  D 4 18   ? 132.833 134.555 161.671 1.00 114.28 ? 18   DC  D "C1'" 1 
ATOM   10927 N N1    . DC  D 4 18   ? 131.514 134.570 162.358 1.00 114.28 ? 18   DC  D N1    1 
ATOM   10928 C C2    . DC  D 4 18   ? 130.678 135.684 162.237 1.00 114.28 ? 18   DC  D C2    1 
ATOM   10929 O O2    . DC  D 4 18   ? 131.052 136.653 161.566 1.00 114.28 ? 18   DC  D O2    1 
ATOM   10930 N N3    . DC  D 4 18   ? 129.485 135.678 162.880 1.00 114.28 ? 18   DC  D N3    1 
ATOM   10931 C C4    . DC  D 4 18   ? 129.118 134.619 163.599 1.00 114.28 ? 18   DC  D C4    1 
ATOM   10932 N N4    . DC  D 4 18   ? 127.928 134.658 164.207 1.00 114.28 ? 18   DC  D N4    1 
ATOM   10933 C C5    . DC  D 4 18   ? 129.956 133.478 163.733 1.00 114.28 ? 18   DC  D C5    1 
ATOM   10934 C C6    . DC  D 4 18   ? 131.130 133.494 163.097 1.00 114.28 ? 18   DC  D C6    1 
ATOM   10935 P P     . DG  D 4 19   ? 137.119 135.473 161.430 1.00 98.00  ? 19   DG  D P     1 
ATOM   10936 O OP1   . DG  D 4 19   ? 138.194 134.926 160.574 1.00 98.00  ? 19   DG  D OP1   1 
ATOM   10937 O OP2   . DG  D 4 19   ? 137.196 135.313 162.899 1.00 98.00  ? 19   DG  D OP2   1 
ATOM   10938 O "O5'" . DG  D 4 19   ? 136.951 137.035 161.120 1.00 98.00  ? 19   DG  D "O5'" 1 
ATOM   10939 C "C5'" . DG  D 4 19   ? 136.267 137.868 162.046 1.00 98.00  ? 19   DG  D "C5'" 1 
ATOM   10940 C "C4'" . DG  D 4 19   ? 135.790 139.149 161.387 1.00 98.00  ? 19   DG  D "C4'" 1 
ATOM   10941 O "O4'" . DG  D 4 19   ? 134.343 139.145 161.350 1.00 98.00  ? 19   DG  D "O4'" 1 
ATOM   10942 C "C3'" . DG  D 4 19   ? 136.120 140.406 162.159 1.00 98.00  ? 19   DG  D "C3'" 1 
ATOM   10943 O "O3'" . DG  D 4 19   ? 135.926 141.550 161.332 1.00 98.00  ? 19   DG  D "O3'" 1 
ATOM   10944 C "C2'" . DG  D 4 19   ? 135.070 140.340 163.251 1.00 98.00  ? 19   DG  D "C2'" 1 
ATOM   10945 C "C1'" . DG  D 4 19   ? 133.846 139.878 162.460 1.00 98.00  ? 19   DG  D "C1'" 1 
ATOM   10946 N N9    . DG  D 4 19   ? 132.948 139.009 163.216 1.00 98.00  ? 19   DG  D N9    1 
ATOM   10947 C C8    . DG  D 4 19   ? 133.159 137.691 163.534 1.00 98.00  ? 19   DG  D C8    1 
ATOM   10948 N N7    . DG  D 4 19   ? 132.183 137.156 164.210 1.00 98.00  ? 19   DG  D N7    1 
ATOM   10949 C C5    . DG  D 4 19   ? 131.256 138.179 164.342 1.00 98.00  ? 19   DG  D C5    1 
ATOM   10950 C C6    . DG  D 4 19   ? 129.995 138.184 164.981 1.00 98.00  ? 19   DG  D C6    1 
ATOM   10951 O O6    . DG  D 4 19   ? 129.432 137.255 165.573 1.00 98.00  ? 19   DG  D O6    1 
ATOM   10952 N N1    . DG  D 4 19   ? 129.380 139.427 164.896 1.00 98.00  ? 19   DG  D N1    1 
ATOM   10953 C C2    . DG  D 4 19   ? 129.910 140.528 164.267 1.00 98.00  ? 19   DG  D C2    1 
ATOM   10954 N N2    . DG  D 4 19   ? 129.161 141.642 164.289 1.00 98.00  ? 19   DG  D N2    1 
ATOM   10955 N N3    . DG  D 4 19   ? 131.094 140.538 163.661 1.00 98.00  ? 19   DG  D N3    1 
ATOM   10956 C C4    . DG  D 4 19   ? 131.710 139.331 163.738 1.00 98.00  ? 19   DG  D C4    1 
ATOM   10957 P P     . DA  D 4 20   ? 136.563 142.968 161.742 1.00 82.08  ? 20   DA  D P     1 
ATOM   10958 O OP1   . DA  D 4 20   ? 136.482 143.852 160.558 1.00 82.08  ? 20   DA  D OP1   1 
ATOM   10959 O OP2   . DA  D 4 20   ? 137.874 142.704 162.374 1.00 82.08  ? 20   DA  D OP2   1 
ATOM   10960 O "O5'" . DA  D 4 20   ? 135.578 143.533 162.874 1.00 82.08  ? 20   DA  D "O5'" 1 
ATOM   10961 C "C5'" . DA  D 4 20   ? 134.212 143.817 162.563 1.00 82.08  ? 20   DA  D "C5'" 1 
ATOM   10962 C "C4'" . DA  D 4 20   ? 133.682 144.974 163.402 1.00 82.08  ? 20   DA  D "C4'" 1 
ATOM   10963 O "O4'" . DA  D 4 20   ? 132.654 144.497 164.300 1.00 82.08  ? 20   DA  D "O4'" 1 
ATOM   10964 C "C3'" . DA  D 4 20   ? 134.700 145.648 164.301 1.00 82.08  ? 20   DA  D "C3'" 1 
ATOM   10965 O "O3'" . DA  D 4 20   ? 134.296 146.984 164.569 1.00 82.08  ? 20   DA  D "O3'" 1 
ATOM   10966 C "C2'" . DA  D 4 20   ? 134.648 144.785 165.561 1.00 82.08  ? 20   DA  D "C2'" 1 
ATOM   10967 C "C1'" . DA  D 4 20   ? 133.185 144.331 165.604 1.00 82.08  ? 20   DA  D "C1'" 1 
ATOM   10968 N N9    . DA  D 4 20   ? 133.032 142.929 165.967 1.00 82.08  ? 20   DA  D N9    1 
ATOM   10969 C C8    . DA  D 4 20   ? 133.922 141.927 165.737 1.00 82.08  ? 20   DA  D C8    1 
ATOM   10970 N N7    . DA  D 4 20   ? 133.521 140.751 166.151 1.00 82.08  ? 20   DA  D N7    1 
ATOM   10971 C C5    . DA  D 4 20   ? 132.277 141.001 166.696 1.00 82.08  ? 20   DA  D C5    1 
ATOM   10972 C C6    . DA  D 4 20   ? 131.328 140.164 167.311 1.00 82.08  ? 20   DA  D C6    1 
ATOM   10973 N N6    . DA  D 4 20   ? 131.506 138.851 167.483 1.00 82.08  ? 20   DA  D N6    1 
ATOM   10974 N N1    . DA  D 4 20   ? 130.187 140.731 167.746 1.00 82.08  ? 20   DA  D N1    1 
ATOM   10975 C C2    . DA  D 4 20   ? 130.016 142.045 167.573 1.00 82.08  ? 20   DA  D C2    1 
ATOM   10976 N N3    . DA  D 4 20   ? 130.833 142.933 167.011 1.00 82.08  ? 20   DA  D N3    1 
ATOM   10977 C C4    . DA  D 4 20   ? 131.957 142.340 166.589 1.00 82.08  ? 20   DA  D C4    1 
ATOM   10978 P P     . DC  D 4 21   ? 135.398 148.134 164.778 1.00 65.33  ? 21   DC  D P     1 
ATOM   10979 O OP1   . DC  D 4 21   ? 134.713 149.318 165.343 1.00 65.33  ? 21   DC  D OP1   1 
ATOM   10980 O OP2   . DC  D 4 21   ? 136.150 148.265 163.511 1.00 65.33  ? 21   DC  D OP2   1 
ATOM   10981 O "O5'" . DC  D 4 21   ? 136.392 147.514 165.868 1.00 65.33  ? 21   DC  D "O5'" 1 
ATOM   10982 C "C5'" . DC  D 4 21   ? 136.741 148.259 167.030 1.00 65.33  ? 21   DC  D "C5'" 1 
ATOM   10983 C "C4'" . DC  D 4 21   ? 135.699 148.082 168.122 1.00 65.33  ? 21   DC  D "C4'" 1 
ATOM   10984 O "O4'" . DC  D 4 21   ? 135.086 146.791 167.997 1.00 65.33  ? 21   DC  D "O4'" 1 
ATOM   10985 C "C3'" . DC  D 4 21   ? 136.249 148.113 169.537 1.00 65.33  ? 21   DC  D "C3'" 1 
ATOM   10986 O "O3'" . DC  D 4 21   ? 136.159 149.425 170.058 1.00 65.33  ? 21   DC  D "O3'" 1 
ATOM   10987 C "C2'" . DC  D 4 21   ? 135.346 147.139 170.315 1.00 65.33  ? 21   DC  D "C2'" 1 
ATOM   10988 C "C1'" . DC  D 4 21   ? 134.513 146.451 169.234 1.00 65.33  ? 21   DC  D "C1'" 1 
ATOM   10989 N N1    . DC  D 4 21   ? 134.486 144.965 169.347 1.00 65.33  ? 21   DC  D N1    1 
ATOM   10990 C C2    . DC  D 4 21   ? 133.371 144.333 169.908 1.00 65.33  ? 21   DC  D C2    1 
ATOM   10991 O O2    . DC  D 4 21   ? 132.428 145.025 170.312 1.00 65.33  ? 21   DC  D O2    1 
ATOM   10992 N N3    . DC  D 4 21   ? 133.357 142.981 169.993 1.00 65.33  ? 21   DC  D N3    1 
ATOM   10993 C C4    . DC  D 4 21   ? 134.394 142.273 169.543 1.00 65.33  ? 21   DC  D C4    1 
ATOM   10994 N N4    . DC  D 4 21   ? 134.335 140.942 169.648 1.00 65.33  ? 21   DC  D N4    1 
ATOM   10995 C C5    . DC  D 4 21   ? 135.537 142.899 168.966 1.00 65.33  ? 21   DC  D C5    1 
ATOM   10996 C C6    . DC  D 4 21   ? 135.540 144.233 168.889 1.00 65.33  ? 21   DC  D C6    1 
ATOM   10997 P P     . DA  D 4 22   ? 137.399 150.062 170.852 1.00 60.03  ? 22   DA  D P     1 
ATOM   10998 O OP1   . DA  D 4 22   ? 138.178 150.877 169.894 1.00 60.03  ? 22   DA  D OP1   1 
ATOM   10999 O OP2   . DA  D 4 22   ? 138.060 148.970 171.598 1.00 60.03  ? 22   DA  D OP2   1 
ATOM   11000 O "O5'" . DA  D 4 22   ? 136.711 151.036 171.916 1.00 60.03  ? 22   DA  D "O5'" 1 
ATOM   11001 C "C5'" . DA  D 4 22   ? 136.800 150.748 173.303 1.00 60.03  ? 22   DA  D "C5'" 1 
ATOM   11002 C "C4'" . DA  D 4 22   ? 135.618 149.920 173.766 1.00 60.03  ? 22   DA  D "C4'" 1 
ATOM   11003 O "O4'" . DA  D 4 22   ? 135.654 148.645 173.115 1.00 60.03  ? 22   DA  D "O4'" 1 
ATOM   11004 C "C3'" . DA  D 4 22   ? 135.609 149.617 175.256 1.00 60.03  ? 22   DA  D "C3'" 1 
ATOM   11005 O "O3'" . DA  D 4 22   ? 134.724 150.504 175.919 1.00 60.03  ? 22   DA  D "O3'" 1 
ATOM   11006 C "C2'" . DA  D 4 22   ? 135.132 148.158 175.362 1.00 60.03  ? 22   DA  D "C2'" 1 
ATOM   11007 C "C1'" . DA  D 4 22   ? 135.000 147.695 173.915 1.00 60.03  ? 22   DA  D "C1'" 1 
ATOM   11008 N N9    . DA  D 4 22   ? 135.609 146.396 173.642 1.00 60.03  ? 22   DA  D N9    1 
ATOM   11009 C C8    . DA  D 4 22   ? 136.828 146.175 173.067 1.00 60.03  ? 22   DA  D C8    1 
ATOM   11010 N N7    . DA  D 4 22   ? 137.119 144.909 172.910 1.00 60.03  ? 22   DA  D N7    1 
ATOM   11011 C C5    . DA  D 4 22   ? 136.014 144.250 173.418 1.00 60.03  ? 22   DA  D C5    1 
ATOM   11012 C C6    . DA  D 4 22   ? 135.709 142.885 173.544 1.00 60.03  ? 22   DA  D C6    1 
ATOM   11013 N N6    . DA  D 4 22   ? 136.536 141.916 173.147 1.00 60.03  ? 22   DA  D N6    1 
ATOM   11014 N N1    . DA  D 4 22   ? 134.523 142.555 174.095 1.00 60.03  ? 22   DA  D N1    1 
ATOM   11015 C C2    . DA  D 4 22   ? 133.702 143.535 174.489 1.00 60.03  ? 22   DA  D C2    1 
ATOM   11016 N N3    . DA  D 4 22   ? 133.882 144.856 174.422 1.00 60.03  ? 22   DA  D N3    1 
ATOM   11017 C C4    . DA  D 4 22   ? 135.070 145.149 173.870 1.00 60.03  ? 22   DA  D C4    1 
ATOM   11018 P P     . DA  D 4 23   ? 135.060 151.011 177.404 1.00 65.99  ? 23   DA  D P     1 
ATOM   11019 O OP1   . DA  D 4 23   ? 134.358 152.293 177.627 1.00 65.99  ? 23   DA  D OP1   1 
ATOM   11020 O OP2   . DA  D 4 23   ? 136.527 150.929 177.561 1.00 65.99  ? 23   DA  D OP2   1 
ATOM   11021 O "O5'" . DA  D 4 23   ? 134.421 149.890 178.342 1.00 65.99  ? 23   DA  D "O5'" 1 
ATOM   11022 C "C5'" . DA  D 4 23   ? 133.102 149.427 178.098 1.00 65.99  ? 23   DA  D "C5'" 1 
ATOM   11023 C "C4'" . DA  D 4 23   ? 132.888 148.063 178.725 1.00 65.99  ? 23   DA  D "C4'" 1 
ATOM   11024 O "O4'" . DA  D 4 23   ? 133.578 147.051 177.941 1.00 65.99  ? 23   DA  D "O4'" 1 
ATOM   11025 C "C3'" . DA  D 4 23   ? 133.420 147.920 180.154 1.00 65.99  ? 23   DA  D "C3'" 1 
ATOM   11026 O "O3'" . DA  D 4 23   ? 132.513 147.150 180.935 1.00 65.99  ? 23   DA  D "O3'" 1 
ATOM   11027 C "C2'" . DA  D 4 23   ? 134.732 147.179 179.942 1.00 65.99  ? 23   DA  D "C2'" 1 
ATOM   11028 C "C1'" . DA  D 4 23   ? 134.338 146.252 178.811 1.00 65.99  ? 23   DA  D "C1'" 1 
ATOM   11029 N N9    . DA  D 4 23   ? 135.474 145.680 178.089 1.00 65.99  ? 23   DA  D N9    1 
ATOM   11030 C C8    . DA  D 4 23   ? 136.570 146.340 177.611 1.00 65.99  ? 23   DA  D C8    1 
ATOM   11031 N N7    . DA  D 4 23   ? 137.436 145.561 177.007 1.00 65.99  ? 23   DA  D N7    1 
ATOM   11032 C C5    . DA  D 4 23   ? 136.874 144.301 177.107 1.00 65.99  ? 23   DA  D C5    1 
ATOM   11033 C C6    . DA  D 4 23   ? 137.301 143.033 176.668 1.00 65.99  ? 23   DA  D C6    1 
ATOM   11034 N N6    . DA  D 4 23   ? 138.447 142.829 176.012 1.00 65.99  ? 23   DA  D N6    1 
ATOM   11035 N N1    . DA  D 4 23   ? 136.502 141.978 176.933 1.00 65.99  ? 23   DA  D N1    1 
ATOM   11036 C C2    . DA  D 4 23   ? 135.356 142.187 177.589 1.00 65.99  ? 23   DA  D C2    1 
ATOM   11037 N N3    . DA  D 4 23   ? 134.852 143.328 178.050 1.00 65.99  ? 23   DA  D N3    1 
ATOM   11038 C C4    . DA  D 4 23   ? 135.666 144.356 177.772 1.00 65.99  ? 23   DA  D C4    1 
ATOM   11039 P P     . DA  D 4 24   ? 132.590 147.180 182.541 1.00 79.15  ? 24   DA  D P     1 
ATOM   11040 O OP1   . DA  D 4 24   ? 131.394 147.902 183.025 1.00 79.15  ? 24   DA  D OP1   1 
ATOM   11041 O OP2   . DA  D 4 24   ? 133.936 147.647 182.938 1.00 79.15  ? 24   DA  D OP2   1 
ATOM   11042 O "O5'" . DA  D 4 24   ? 132.460 145.641 182.960 1.00 79.15  ? 24   DA  D "O5'" 1 
ATOM   11043 C "C5'" . DA  D 4 24   ? 131.200 144.981 182.867 1.00 79.15  ? 24   DA  D "C5'" 1 
ATOM   11044 C "C4'" . DA  D 4 24   ? 131.381 143.475 182.783 1.00 79.15  ? 24   DA  D "C4'" 1 
ATOM   11045 O "O4'" . DA  D 4 24   ? 132.310 143.166 181.716 1.00 79.15  ? 24   DA  D "O4'" 1 
ATOM   11046 C "C3'" . DA  D 4 24   ? 131.932 142.817 184.047 1.00 79.15  ? 24   DA  D "C3'" 1 
ATOM   11047 O "O3'" . DA  D 4 24   ? 131.169 141.620 184.431 1.00 79.15  ? 24   DA  D "O3'" 1 
ATOM   11048 C "C2'" . DA  D 4 24   ? 133.397 142.531 183.723 1.00 79.15  ? 24   DA  D "C2'" 1 
ATOM   11049 C "C1'" . DA  D 4 24   ? 133.403 142.417 182.202 1.00 79.15  ? 24   DA  D "C1'" 1 
ATOM   11050 N N9    . DA  D 4 24   ? 134.615 142.945 181.596 1.00 79.15  ? 24   DA  D N9    1 
ATOM   11051 C C8    . DA  D 4 24   ? 134.978 144.254 181.504 1.00 79.15  ? 24   DA  D C8    1 
ATOM   11052 N N7    . DA  D 4 24   ? 136.128 144.443 180.907 1.00 79.15  ? 24   DA  D N7    1 
ATOM   11053 C C5    . DA  D 4 24   ? 136.550 143.167 180.590 1.00 79.15  ? 24   DA  D C5    1 
ATOM   11054 C C6    . DA  D 4 24   ? 137.698 142.688 179.939 1.00 79.15  ? 24   DA  D C6    1 
ATOM   11055 N N6    . DA  D 4 24   ? 138.671 143.483 179.485 1.00 79.15  ? 24   DA  D N6    1 
ATOM   11056 N N1    . DA  D 4 24   ? 137.813 141.355 179.782 1.00 79.15  ? 24   DA  D N1    1 
ATOM   11057 C C2    . DA  D 4 24   ? 136.837 140.564 180.237 1.00 79.15  ? 24   DA  D C2    1 
ATOM   11058 N N3    . DA  D 4 24   ? 135.712 140.900 180.863 1.00 79.15  ? 24   DA  D N3    1 
ATOM   11059 C C4    . DA  D 4 24   ? 135.626 142.230 181.001 1.00 79.15  ? 24   DA  D C4    1 
ATOM   11060 P P     . DG  D 4 25   ? 131.035 140.305 183.500 1.00 95.28  ? 25   DG  D P     1 
ATOM   11061 O OP1   . DG  D 4 25   ? 130.640 140.660 182.121 1.00 95.28  ? 25   DG  D OP1   1 
ATOM   11062 O OP2   . DG  D 4 25   ? 130.178 139.370 184.258 1.00 95.28  ? 25   DG  D OP2   1 
ATOM   11063 O "O5'" . DG  D 4 25   ? 132.499 139.662 183.478 1.00 95.28  ? 25   DG  D "O5'" 1 
ATOM   11064 C "C5'" . DG  D 4 25   ? 133.035 139.059 184.648 1.00 95.28  ? 25   DG  D "C5'" 1 
ATOM   11065 C "C4'" . DG  D 4 25   ? 134.156 138.098 184.291 1.00 95.28  ? 25   DG  D "C4'" 1 
ATOM   11066 O "O4'" . DG  D 4 25   ? 135.109 138.764 183.417 1.00 95.28  ? 25   DG  D "O4'" 1 
ATOM   11067 C "C3'" . DG  D 4 25   ? 134.978 137.598 185.473 1.00 95.28  ? 25   DG  D "C3'" 1 
ATOM   11068 O "O3'" . DG  D 4 25   ? 135.496 136.308 185.180 1.00 95.28  ? 25   DG  D "O3'" 1 
ATOM   11069 C "C2'" . DG  D 4 25   ? 136.092 138.633 185.531 1.00 95.28  ? 25   DG  D "C2'" 1 
ATOM   11070 C "C1'" . DG  D 4 25   ? 136.374 138.805 184.048 1.00 95.28  ? 25   DG  D "C1'" 1 
ATOM   11071 N N9    . DG  D 4 25   ? 137.025 140.064 183.703 1.00 95.28  ? 25   DG  D N9    1 
ATOM   11072 C C8    . DG  D 4 25   ? 136.537 141.330 183.906 1.00 95.28  ? 25   DG  D C8    1 
ATOM   11073 N N7    . DG  D 4 25   ? 137.336 142.269 183.482 1.00 95.28  ? 25   DG  D N7    1 
ATOM   11074 C C5    . DG  D 4 25   ? 138.422 141.581 182.960 1.00 95.28  ? 25   DG  D C5    1 
ATOM   11075 C C6    . DG  D 4 25   ? 139.606 142.069 182.359 1.00 95.28  ? 25   DG  D C6    1 
ATOM   11076 O O6    . DG  D 4 25   ? 139.936 143.246 182.160 1.00 95.28  ? 25   DG  D O6    1 
ATOM   11077 N N1    . DG  D 4 25   ? 140.450 141.034 181.970 1.00 95.28  ? 25   DG  D N1    1 
ATOM   11078 C C2    . DG  D 4 25   ? 140.185 139.697 182.141 1.00 95.28  ? 25   DG  D C2    1 
ATOM   11079 N N2    . DG  D 4 25   ? 141.122 138.845 181.702 1.00 95.28  ? 25   DG  D N2    1 
ATOM   11080 N N3    . DG  D 4 25   ? 139.080 139.227 182.703 1.00 95.28  ? 25   DG  D N3    1 
ATOM   11081 C C4    . DG  D 4 25   ? 138.246 140.223 183.087 1.00 95.28  ? 25   DG  D C4    1 
ATOM   11082 P P     . DC  D 4 26   ? 135.210 135.069 186.162 1.00 122.44 ? 26   DC  D P     1 
ATOM   11083 O OP1   . DC  D 4 26   ? 134.159 134.236 185.538 1.00 122.44 ? 26   DC  D OP1   1 
ATOM   11084 O OP2   . DC  D 4 26   ? 135.012 135.611 187.525 1.00 122.44 ? 26   DC  D OP2   1 
ATOM   11085 O "O5'" . DC  D 4 26   ? 136.584 134.250 186.152 1.00 122.44 ? 26   DC  D "O5'" 1 
ATOM   11086 C "C5'" . DC  D 4 26   ? 137.703 134.728 186.888 1.00 122.44 ? 26   DC  D "C5'" 1 
ATOM   11087 C "C4'" . DC  D 4 26   ? 139.003 134.394 186.179 1.00 122.44 ? 26   DC  D "C4'" 1 
ATOM   11088 O "O4'" . DC  D 4 26   ? 139.397 135.518 185.344 1.00 122.44 ? 26   DC  D "O4'" 1 
ATOM   11089 C "C3'" . DC  D 4 26   ? 140.191 134.158 187.104 1.00 122.44 ? 26   DC  D "C3'" 1 
ATOM   11090 O "O3'" . DC  D 4 26   ? 141.151 133.325 186.451 1.00 122.44 ? 26   DC  D "O3'" 1 
ATOM   11091 C "C2'" . DC  D 4 26   ? 140.724 135.571 187.267 1.00 122.44 ? 26   DC  D "C2'" 1 
ATOM   11092 C "C1'" . DC  D 4 26   ? 140.611 136.056 185.832 1.00 122.44 ? 26   DC  D "C1'" 1 
ATOM   11093 N N1    . DC  D 4 26   ? 140.575 137.537 185.687 1.00 122.44 ? 26   DC  D N1    1 
ATOM   11094 C C2    . DC  D 4 26   ? 141.650 138.193 185.085 1.00 122.44 ? 26   DC  D C2    1 
ATOM   11095 O O2    . DC  D 4 26   ? 142.615 137.525 184.698 1.00 122.44 ? 26   DC  D O2    1 
ATOM   11096 N N3    . DC  D 4 26   ? 141.609 139.541 184.955 1.00 122.44 ? 26   DC  D N3    1 
ATOM   11097 C C4    . DC  D 4 26   ? 140.548 140.219 185.393 1.00 122.44 ? 26   DC  D C4    1 
ATOM   11098 N N4    . DC  D 4 26   ? 140.547 141.548 185.242 1.00 122.44 ? 26   DC  D N4    1 
ATOM   11099 C C5    . DC  D 4 26   ? 139.440 139.565 186.008 1.00 122.44 ? 26   DC  D C5    1 
ATOM   11100 C C6    . DC  D 4 26   ? 139.494 138.236 186.130 1.00 122.44 ? 26   DC  D C6    1 
ATOM   11101 P P     . DA  D 4 27   ? 141.552 131.893 187.062 1.00 149.96 ? 27   DA  D P     1 
ATOM   11102 O OP1   . DA  D 4 27   ? 141.915 131.015 185.927 1.00 149.96 ? 27   DA  D OP1   1 
ATOM   11103 O OP2   . DA  D 4 27   ? 140.476 131.485 187.992 1.00 149.96 ? 27   DA  D OP2   1 
ATOM   11104 O "O5'" . DA  D 4 27   ? 142.870 132.184 187.926 1.00 149.96 ? 27   DA  D "O5'" 1 
ATOM   11105 C "C5'" . DA  D 4 27   ? 143.554 133.425 187.795 1.00 149.96 ? 27   DA  D "C5'" 1 
ATOM   11106 C "C4'" . DA  D 4 27   ? 144.886 133.252 187.090 1.00 149.96 ? 27   DA  D "C4'" 1 
ATOM   11107 O "O4'" . DA  D 4 27   ? 145.116 134.388 186.229 1.00 149.96 ? 27   DA  D "O4'" 1 
ATOM   11108 C "C3'" . DA  D 4 27   ? 146.089 133.242 188.006 1.00 149.96 ? 27   DA  D "C3'" 1 
ATOM   11109 O "O3'" . DA  D 4 27   ? 147.207 132.691 187.325 1.00 149.96 ? 27   DA  D "O3'" 1 
ATOM   11110 C "C2'" . DA  D 4 27   ? 146.278 134.732 188.268 1.00 149.96 ? 27   DA  D "C2'" 1 
ATOM   11111 C "C1'" . DA  D 4 27   ? 145.920 135.340 186.908 1.00 149.96 ? 27   DA  D "C1'" 1 
ATOM   11112 N N9    . DA  D 4 27   ? 145.162 136.584 186.999 1.00 149.96 ? 27   DA  D N9    1 
ATOM   11113 C C8    . DA  D 4 27   ? 143.912 136.746 187.522 1.00 149.96 ? 27   DA  D C8    1 
ATOM   11114 N N7    . DA  D 4 27   ? 143.467 137.976 187.459 1.00 149.96 ? 27   DA  D N7    1 
ATOM   11115 C C5    . DA  D 4 27   ? 144.493 138.669 186.845 1.00 149.96 ? 27   DA  D C5    1 
ATOM   11116 C C6    . DA  D 4 27   ? 144.638 140.021 186.489 1.00 149.96 ? 27   DA  D C6    1 
ATOM   11117 N N6    . DA  D 4 27   ? 143.695 140.940 186.711 1.00 149.96 ? 27   DA  D N6    1 
ATOM   11118 N N1    . DA  D 4 27   ? 145.793 140.394 185.895 1.00 149.96 ? 27   DA  D N1    1 
ATOM   11119 C C2    . DA  D 4 27   ? 146.729 139.461 185.670 1.00 149.96 ? 27   DA  D C2    1 
ATOM   11120 N N3    . DA  D 4 27   ? 146.704 138.161 185.961 1.00 149.96 ? 27   DA  D N3    1 
ATOM   11121 C C4    . DA  D 4 27   ? 145.547 137.827 186.552 1.00 149.96 ? 27   DA  D C4    1 
ATOM   11122 P P     . DC  D 4 28   ? 148.440 132.081 188.155 1.00 192.06 ? 28   DC  D P     1 
ATOM   11123 O OP1   . DC  D 4 28   ? 149.206 131.208 187.237 1.00 192.06 ? 28   DC  D OP1   1 
ATOM   11124 O OP2   . DC  D 4 28   ? 147.903 131.529 189.418 1.00 192.06 ? 28   DC  D OP2   1 
ATOM   11125 O "O5'" . DC  D 4 28   ? 149.332 133.359 188.515 1.00 192.06 ? 28   DC  D "O5'" 1 
ATOM   11126 C "C5'" . DC  D 4 28   ? 149.976 134.093 187.479 1.00 192.06 ? 28   DC  D "C5'" 1 
ATOM   11127 C "C4'" . DC  D 4 28   ? 150.803 135.234 188.048 1.00 192.06 ? 28   DC  D "C4'" 1 
ATOM   11128 O "O4'" . DC  D 4 28   ? 150.000 136.445 188.110 1.00 192.06 ? 28   DC  D "O4'" 1 
ATOM   11129 C "C3'" . DC  D 4 28   ? 151.335 135.015 189.464 1.00 192.06 ? 28   DC  D "C3'" 1 
ATOM   11130 O "O3'" . DC  D 4 28   ? 152.617 135.610 189.580 1.00 192.06 ? 28   DC  D "O3'" 1 
ATOM   11131 C "C2'" . DC  D 4 28   ? 150.307 135.755 190.313 1.00 192.06 ? 28   DC  D "C2'" 1 
ATOM   11132 C "C1'" . DC  D 4 28   ? 150.028 136.955 189.426 1.00 192.06 ? 28   DC  D "C1'" 1 
ATOM   11133 N N1    . DC  D 4 28   ? 148.728 137.619 189.701 1.00 192.06 ? 28   DC  D N1    1 
ATOM   11134 C C2    . DC  D 4 28   ? 148.503 138.913 189.229 1.00 192.06 ? 28   DC  D C2    1 
ATOM   11135 O O2    . DC  D 4 28   ? 149.397 139.506 188.622 1.00 192.06 ? 28   DC  D O2    1 
ATOM   11136 N N3    . DC  D 4 28   ? 147.325 139.515 189.495 1.00 192.06 ? 28   DC  D N3    1 
ATOM   11137 C C4    . DC  D 4 28   ? 146.379 138.860 190.166 1.00 192.06 ? 28   DC  D C4    1 
ATOM   11138 N N4    . DC  D 4 28   ? 145.229 139.498 190.392 1.00 192.06 ? 28   DC  D N4    1 
ATOM   11139 C C5    . DC  D 4 28   ? 146.581 137.535 190.652 1.00 192.06 ? 28   DC  D C5    1 
ATOM   11140 C C6    . DC  D 4 28   ? 147.761 136.958 190.399 1.00 192.06 ? 28   DC  D C6    1 
ATOM   11141 P P     . DT  D 4 29   ? 153.627 135.172 190.751 1.00 225.94 ? 29   DT  D P     1 
ATOM   11142 O OP1   . DT  D 4 29   ? 154.469 134.075 190.227 1.00 225.94 ? 29   DT  D OP1   1 
ATOM   11143 O OP2   . DT  D 4 29   ? 152.850 134.971 191.994 1.00 225.94 ? 29   DT  D OP2   1 
ATOM   11144 O "O5'" . DT  D 4 29   ? 154.538 136.470 190.953 1.00 225.94 ? 29   DT  D "O5'" 1 
ATOM   11145 C "C5'" . DT  D 4 29   ? 154.981 137.201 189.816 1.00 225.94 ? 29   DT  D "C5'" 1 
ATOM   11146 C "C4'" . DT  D 4 29   ? 154.579 138.662 189.919 1.00 225.94 ? 29   DT  D "C4'" 1 
ATOM   11147 O "O4'" . DT  D 4 29   ? 153.148 138.760 190.160 1.00 225.94 ? 29   DT  D "O4'" 1 
ATOM   11148 C "C3'" . DT  D 4 29   ? 155.253 139.439 191.053 1.00 225.94 ? 29   DT  D "C3'" 1 
ATOM   11149 O "O3'" . DT  D 4 29   ? 155.654 140.729 190.591 1.00 225.94 ? 29   DT  D "O3'" 1 
ATOM   11150 C "C2'" . DT  D 4 29   ? 154.150 139.538 192.104 1.00 225.94 ? 29   DT  D "C2'" 1 
ATOM   11151 C "C1'" . DT  D 4 29   ? 152.922 139.657 191.222 1.00 225.94 ? 29   DT  D "C1'" 1 
ATOM   11152 N N1    . DT  D 4 29   ? 151.649 139.286 191.909 1.00 225.94 ? 29   DT  D N1    1 
ATOM   11153 C C2    . DT  D 4 29   ? 150.590 140.164 191.881 1.00 225.94 ? 29   DT  D C2    1 
ATOM   11154 O O2    . DT  D 4 29   ? 150.632 141.242 191.316 1.00 225.94 ? 29   DT  D O2    1 
ATOM   11155 N N3    . DT  D 4 29   ? 149.469 139.733 192.542 1.00 225.94 ? 29   DT  D N3    1 
ATOM   11156 C C4    . DT  D 4 29   ? 149.306 138.535 193.213 1.00 225.94 ? 29   DT  D C4    1 
ATOM   11157 O O4    . DT  D 4 29   ? 148.258 138.235 193.776 1.00 225.94 ? 29   DT  D O4    1 
ATOM   11158 C C5    . DT  D 4 29   ? 150.456 137.661 193.207 1.00 225.94 ? 29   DT  D C5    1 
ATOM   11159 C C7    . DT  D 4 29   ? 150.399 136.335 193.905 1.00 225.94 ? 29   DT  D C7    1 
ATOM   11160 C C6    . DT  D 4 29   ? 151.560 138.075 192.565 1.00 225.94 ? 29   DT  D C6    1 
ATOM   11161 P P     . DA  D 4 30   ? 157.207 141.144 190.594 1.00 263.37 ? 30   DA  D P     1 
ATOM   11162 O OP1   . DA  D 4 30   ? 157.750 140.849 189.250 1.00 263.37 ? 30   DA  D OP1   1 
ATOM   11163 O OP2   . DA  D 4 30   ? 157.831 140.535 191.789 1.00 263.37 ? 30   DA  D OP2   1 
ATOM   11164 O "O5'" . DA  D 4 30   ? 157.187 142.731 190.807 1.00 263.37 ? 30   DA  D "O5'" 1 
ATOM   11165 C "C5'" . DA  D 4 30   ? 156.841 143.598 189.729 1.00 263.37 ? 30   DA  D "C5'" 1 
ATOM   11166 C "C4'" . DA  D 4 30   ? 156.339 144.948 190.234 1.00 263.37 ? 30   DA  D "C4'" 1 
ATOM   11167 O "O4'" . DA  D 4 30   ? 155.155 144.762 191.045 1.00 263.37 ? 30   DA  D "O4'" 1 
ATOM   11168 C "C3'" . DA  D 4 30   ? 157.306 145.732 191.108 1.00 263.37 ? 30   DA  D "C3'" 1 
ATOM   11169 O "O3'" . DA  D 4 30   ? 157.061 147.128 190.956 1.00 263.37 ? 30   DA  D "O3'" 1 
ATOM   11170 C "C2'" . DA  D 4 30   ? 156.957 145.249 192.515 1.00 263.37 ? 30   DA  D "C2'" 1 
ATOM   11171 C "C1'" . DA  D 4 30   ? 155.453 144.990 192.413 1.00 263.37 ? 30   DA  D "C1'" 1 
ATOM   11172 N N9    . DA  D 4 30   ? 155.012 143.817 193.160 1.00 263.37 ? 30   DA  D N9    1 
ATOM   11173 C C8    . DA  D 4 30   ? 155.737 142.691 193.429 1.00 263.37 ? 30   DA  D C8    1 
ATOM   11174 N N7    . DA  D 4 30   ? 155.077 141.787 194.112 1.00 263.37 ? 30   DA  D N7    1 
ATOM   11175 C C5    . DA  D 4 30   ? 153.828 142.355 194.293 1.00 263.37 ? 30   DA  D C5    1 
ATOM   11176 C C6    . DA  D 4 30   ? 152.663 141.901 194.941 1.00 263.37 ? 30   DA  D C6    1 
ATOM   11177 N N6    . DA  D 4 30   ? 152.573 140.712 195.548 1.00 263.37 ? 30   DA  D N6    1 
ATOM   11178 N N1    . DA  D 4 30   ? 151.590 142.718 194.942 1.00 263.37 ? 30   DA  D N1    1 
ATOM   11179 C C2    . DA  D 4 30   ? 151.683 143.906 194.334 1.00 263.37 ? 30   DA  D C2    1 
ATOM   11180 N N3    . DA  D 4 30   ? 152.720 144.441 193.694 1.00 263.37 ? 30   DA  D N3    1 
ATOM   11181 C C4    . DA  D 4 30   ? 153.770 143.606 193.710 1.00 263.37 ? 30   DA  D C4    1 
ATOM   11182 P P     . DC  D 4 31   ? 157.866 148.203 191.839 1.00 279.87 ? 31   DC  D P     1 
ATOM   11183 O OP1   . DC  D 4 31   ? 157.912 149.462 191.063 1.00 279.87 ? 31   DC  D OP1   1 
ATOM   11184 O OP2   . DC  D 4 31   ? 159.127 147.576 192.292 1.00 279.87 ? 31   DC  D OP2   1 
ATOM   11185 O "O5'" . DC  D 4 31   ? 156.929 148.425 193.118 1.00 279.87 ? 31   DC  D "O5'" 1 
ATOM   11186 C "C5'" . DC  D 4 31   ? 155.587 148.872 192.944 1.00 279.87 ? 31   DC  D "C5'" 1 
ATOM   11187 C "C4'" . DC  D 4 31   ? 154.788 148.715 194.227 1.00 279.87 ? 31   DC  D "C4'" 1 
ATOM   11188 O "O4'" . DC  D 4 31   ? 154.718 147.317 194.589 1.00 279.87 ? 31   DC  D "O4'" 1 
ATOM   11189 C "C3'" . DC  D 4 31   ? 155.360 149.449 195.445 1.00 279.87 ? 31   DC  D "C3'" 1 
ATOM   11190 O "O3'" . DC  D 4 31   ? 154.409 150.382 195.944 1.00 279.87 ? 31   DC  D "O3'" 1 
ATOM   11191 C "C2'" . DC  D 4 31   ? 155.648 148.336 196.463 1.00 279.87 ? 31   DC  D "C2'" 1 
ATOM   11192 C "C1'" . DC  D 4 31   ? 154.745 147.208 195.987 1.00 279.87 ? 31   DC  D "C1'" 1 
ATOM   11193 N N1    . DC  D 4 31   ? 155.252 145.852 196.345 1.00 279.87 ? 31   DC  D N1    1 
ATOM   11194 C C2    . DC  D 4 31   ? 154.416 144.950 197.015 1.00 279.87 ? 31   DC  D C2    1 
ATOM   11195 O O2    . DC  D 4 31   ? 153.260 145.291 197.298 1.00 279.87 ? 31   DC  D O2    1 
ATOM   11196 N N3    . DC  D 4 31   ? 154.896 143.722 197.332 1.00 279.87 ? 31   DC  D N3    1 
ATOM   11197 C C4    . DC  D 4 31   ? 156.147 143.390 197.009 1.00 279.87 ? 31   DC  D C4    1 
ATOM   11198 N N4    . DC  D 4 31   ? 156.577 142.168 197.343 1.00 279.87 ? 31   DC  D N4    1 
ATOM   11199 C C5    . DC  D 4 31   ? 157.014 144.296 196.330 1.00 279.87 ? 31   DC  D C5    1 
ATOM   11200 C C6    . DC  D 4 31   ? 156.530 145.503 196.022 1.00 279.87 ? 31   DC  D C6    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   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  26   LYS A N   
729   C CA  . LYS B 29   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  26   LYS A CA  
730   C C   . LYS B 29   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  26   LYS A C   
731   O O   . LYS B 29   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  26   LYS A O   
737   N N   . THR B 30   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  27   THR A N   
738   C CA  . THR B 30   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  27   THR A CA  
739   C C   . THR B 30   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  27   THR A C   
740   O O   . THR B 30   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  27   THR A O   
741   C CB  . THR B 30   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  27   THR A CB  
742   O OG1 . THR B 30   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  27   THR A OG1 
743   C CG2 . THR B 30   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  27   THR A CG2 
744   N N   . LEU B 31   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  28   LEU A N   
745   C CA  . LEU B 31   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  28   LEU A CA  
746   C C   . LEU B 31   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  28   LEU A C   
747   O O   . LEU B 31   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  28   LEU A O   
748   C CB  . LEU B 31   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  28   LEU A CB  
749   C CG  . LEU B 31   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  28   LEU A CG  
750   C CD1 . LEU B 31   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  28   LEU A CD1 
751   C CD2 . LEU B 31   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  28   LEU A CD2 
752   N N   . LYS B 32   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  29   LYS A N   
753   C CA  . LYS B 32   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  29   LYS A CA  
754   C C   . LYS B 32   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  29   LYS A C   
755   O O   . LYS B 32   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  29   LYS A O   
756   C CB  . LYS B 32   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  29   LYS A CB  
757   C CG  . LYS B 32   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  29   LYS A CG  
758   C CD  . LYS B 32   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  29   LYS A CD  
759   C CE  . LYS B 32   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  29   LYS A CE  
760   N NZ  . LYS B 32   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  29   LYS A NZ  
761   N N   . HIS B 33   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  30   HIS A N   
762   C CA  . HIS B 33   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  30   HIS A CA  
763   C C   . HIS B 33   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  30   HIS A C   
764   O O   . HIS B 33   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  30   HIS A O   
765   C CB  . HIS B 33   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  30   HIS A CB  
766   C CG  . HIS B 33   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  30   HIS A CG  
767   N ND1 . HIS B 33   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  30   HIS A ND1 
768   C CD2 . HIS B 33   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  30   HIS A CD2 
769   C CE1 . HIS B 33   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  30   HIS A CE1 
770   N NE2 . HIS B 33   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  30   HIS A NE2 
771   N N   . ILE B 34   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  31   ILE A N   
772   C CA  . ILE B 34   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  31   ILE A CA  
773   C C   . ILE B 34   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  31   ILE A C   
774   O O   . ILE B 34   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  31   ILE A O   
775   C CB  . ILE B 34   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  31   ILE A CB  
776   C CG1 . ILE B 34   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  31   ILE A CG1 
777   C CG2 . ILE B 34   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  31   ILE A CG2 
778   C CD1 . ILE B 34   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  31   ILE A CD1 
779   N N   . GLN B 35   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  32   GLN A N   
780   C CA  . GLN B 35   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  32   GLN A CA  
781   C C   . GLN B 35   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  32   GLN A C   
782   O O   . GLN B 35   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  32   GLN A O   
783   C CB  . GLN B 35   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  32   GLN A CB  
784   C CG  . GLN B 35   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  32   GLN A CG  
785   C CD  . GLN B 35   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  32   GLN A CD  
786   O OE1 . GLN B 35   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  32   GLN A OE1 
787   N NE2 . GLN B 35   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  32   GLN A NE2 
788   N N   . GLU B 36   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  33   GLU A N   
789   C CA  . GLU B 36   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  33   GLU A CA  
790   C C   . GLU B 36   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  33   GLU A C   
791   O O   . GLU B 36   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  33   GLU A O   
792   C CB  . GLU B 36   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  33   GLU A CB  
793   C CG  . GLU B 36   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  33   GLU A CG  
794   C CD  . GLU B 36   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  33   GLU A CD  
795   O OE1 . GLU B 36   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  33   GLU A OE1 
796   O OE2 . GLU B 36   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  33   GLU A OE2 
797   N N   . GLN B 37   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  34   GLN A N   
798   C CA  . GLN B 37   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  34   GLN A CA  
799   C C   . GLN B 37   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  34   GLN A C   
800   O O   . GLN B 37   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  34   GLN A O   
801   C CB  . GLN B 37   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  34   GLN A CB  
802   C CG  . GLN B 37   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  34   GLN A CG  
803   C CD  . GLN B 37   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  34   GLN A CD  
804   O OE1 . GLN B 37   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  34   GLN A OE1 
805   N NE2 . GLN B 37   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  34   GLN A NE2 
806   N N   . GLY B 38   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  35   GLY A N   
807   C CA  . GLY B 38   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  35   GLY A CA  
808   C C   . GLY B 38   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  35   GLY A C   
809   O O   . GLY B 38   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  35   GLY A O   
810   N N   . PHE B 39   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  36   PHE A N   
811   C CA  . PHE B 39   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  36   PHE A CA  
812   C C   . PHE B 39   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  36   PHE A C   
813   O O   . PHE B 39   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  36   PHE A O   
814   C CB  . PHE B 39   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  36   PHE A CB  
815   C CG  . PHE B 39   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  36   PHE A CG  
816   C CD1 . PHE B 39   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  36   PHE A CD1 
817   C CD2 . PHE B 39   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  36   PHE A CD2 
818   C CE1 . PHE B 39   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  36   PHE A CE1 
819   C CE2 . PHE B 39   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  36   PHE A CE2 
820   C CZ  . PHE B 39   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  36   PHE A CZ  
821   N N   . ILE B 40   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  37   ILE A N   
822   C CA  . ILE B 40   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  37   ILE A CA  
823   C C   . ILE B 40   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  37   ILE A C   
824   O O   . ILE B 40   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  37   ILE A O   
825   C CB  . ILE B 40   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  37   ILE A CB  
826   C CG1 . ILE B 40   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  37   ILE A CG1 
827   C CG2 . ILE B 40   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  37   ILE A CG2 
828   C CD1 . ILE B 40   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  37   ILE A CD1 
829   N N   . GLU B 41   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  38   GLU A N   
830   C CA  . GLU B 41   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  38   GLU A CA  
831   C C   . GLU B 41   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  38   GLU A C   
832   O O   . GLU B 41   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  38   GLU A O   
833   C CB  . GLU B 41   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  38   GLU A CB  
834   C CG  . GLU B 41   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  38   GLU A CG  
835   C CD  . GLU B 41   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  38   GLU A CD  
836   O OE1 . GLU B 41   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  38   GLU A OE1 
837   O OE2 . GLU B 41   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  38   GLU A OE2 
838   N N   . GLU B 42   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  39   GLU A N   
839   C CA  . GLU B 42   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  39   GLU A CA  
840   C C   . GLU B 42   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  39   GLU A C   
841   O O   . GLU B 42   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  39   GLU A O   
842   C CB  . GLU B 42   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  39   GLU A CB  
843   C CG  . GLU B 42   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  39   GLU A CG  
844   C CD  . GLU B 42   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  39   GLU A CD  
845   O OE1 . GLU B 42   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  39   GLU A OE1 
846   O OE2 . GLU B 42   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  39   GLU A OE2 
847   N N   . ASP B 43   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  40   ASP A N   
848   C CA  . ASP B 43   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  40   ASP A CA  
849   C C   . ASP B 43   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  40   ASP A C   
850   O O   . ASP B 43   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  40   ASP A O   
851   C CB  . ASP B 43   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  40   ASP A CB  
852   C CG  . ASP B 43   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  40   ASP A CG  
853   O OD1 . ASP B 43   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  40   ASP A OD1 
854   O OD2 . ASP B 43   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  40   ASP A OD2 
855   N N   . LYS B 44   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  41   LYS A N   
856   C CA  . LYS B 44   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  41   LYS A CA  
857   C C   . LYS B 44   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  41   LYS A C   
858   O O   . LYS B 44   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  41   LYS A O   
859   C CB  . LYS B 44   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  41   LYS A CB  
860   C CG  . LYS B 44   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  41   LYS A CG  
861   C CD  . LYS B 44   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  41   LYS A CD  
862   C CE  . LYS B 44   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  41   LYS A CE  
863   N NZ  . LYS B 44   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  41   LYS A NZ  
864   N N   . ALA B 45   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  42   ALA A N   
865   C CA  . ALA B 45   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  42   ALA A CA  
866   C C   . ALA B 45   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  42   ALA A C   
867   O O   . ALA B 45   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  42   ALA A O   
868   C CB  . ALA B 45   ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  42   ALA A CB  
869   N N   . ARG B 46   ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  43   ARG A N   
870   C CA  . ARG B 46   ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  43   ARG A CA  
871   C C   . ARG B 46   ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  43   ARG A C   
872   O O   . ARG B 46   ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  43   ARG A O   
873   C CB  . ARG B 46   ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  43   ARG A CB  
874   C CG  . ARG B 46   ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  43   ARG A CG  
875   C CD  . ARG B 46   ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  43   ARG A CD  
876   N NE  . ARG B 46   ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  43   ARG A NE  
877   C CZ  . ARG B 46   ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  43   ARG A CZ  
878   N NH1 . ARG B 46   ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  43   ARG A NH1 
879   N NH2 . ARG B 46   ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  43   ARG A NH2 
880   N N   . ASN B 47   ? 0.6614 0.6614 0.6614 0.0000  0.0000  0.0000  44   ASN A N   
881   C CA  . ASN B 47   ? 0.6614 0.6614 0.6614 0.0000  0.0000  0.0000  44   ASN A CA  
882   C C   . ASN B 47   ? 0.6614 0.6614 0.6614 0.0000  0.0000  0.0000  44   ASN A C   
883   O O   . ASN B 47   ? 0.6614 0.6614 0.6614 0.0000  0.0000  0.0000  44   ASN A O   
884   C CB  . ASN B 47   ? 0.6614 0.6614 0.6614 0.0000  0.0000  0.0000  44   ASN A CB  
885   C CG  . ASN B 47   ? 0.6614 0.6614 0.6614 0.0000  0.0000  0.0000  44   ASN A CG  
886   O OD1 . ASN B 47   ? 0.6614 0.6614 0.6614 0.0000  0.0000  0.0000  44   ASN A OD1 
887   N ND2 . ASN B 47   ? 0.6614 0.6614 0.6614 0.0000  0.0000  0.0000  44   ASN A ND2 
888   N N   . ASP B 48   ? 0.6899 0.6899 0.6899 0.0000  0.0000  0.0000  45   ASP A N   
889   C CA  . ASP B 48   ? 0.6899 0.6899 0.6899 0.0000  0.0000  0.0000  45   ASP A CA  
890   C C   . ASP B 48   ? 0.6899 0.6899 0.6899 0.0000  0.0000  0.0000  45   ASP A C   
891   O O   . ASP B 48   ? 0.6899 0.6899 0.6899 0.0000  0.0000  0.0000  45   ASP A O   
892   C CB  . ASP B 48   ? 0.6899 0.6899 0.6899 0.0000  0.0000  0.0000  45   ASP A CB  
893   C CG  . ASP B 48   ? 0.6899 0.6899 0.6899 0.0000  0.0000  0.0000  45   ASP A CG  
894   O OD1 . ASP B 48   ? 0.6899 0.6899 0.6899 0.0000  0.0000  0.0000  45   ASP A OD1 
895   O OD2 . ASP B 48   ? 0.6899 0.6899 0.6899 0.0000  0.0000  0.0000  45   ASP A OD2 
896   N N   . HIS B 49   ? 0.6990 0.6990 0.6990 0.0000  0.0000  0.0000  46   HIS A N   
897   C CA  . HIS B 49   ? 0.6990 0.6990 0.6990 0.0000  0.0000  0.0000  46   HIS A CA  
898   C C   . HIS B 49   ? 0.6990 0.6990 0.6990 0.0000  0.0000  0.0000  46   HIS A C   
899   O O   . HIS B 49   ? 0.6990 0.6990 0.6990 0.0000  0.0000  0.0000  46   HIS A O   
900   C CB  . HIS B 49   ? 0.6990 0.6990 0.6990 0.0000  0.0000  0.0000  46   HIS A CB  
901   C CG  . HIS B 49   ? 0.6990 0.6990 0.6990 0.0000  0.0000  0.0000  46   HIS A CG  
902   N ND1 . HIS B 49   ? 0.6990 0.6990 0.6990 0.0000  0.0000  0.0000  46   HIS A ND1 
903   C CD2 . HIS B 49   ? 0.6990 0.6990 0.6990 0.0000  0.0000  0.0000  46   HIS A CD2 
904   C CE1 . HIS B 49   ? 0.6990 0.6990 0.6990 0.0000  0.0000  0.0000  46   HIS A CE1 
905   N NE2 . HIS B 49   ? 0.6990 0.6990 0.6990 0.0000  0.0000  0.0000  46   HIS A NE2 
906   N N   . TYR B 50   ? 1.3546 0.7167 0.9007 -0.3343 -0.2415 0.2361  47   TYR A N   
907   C CA  . TYR B 50   ? 1.2889 0.6603 0.8585 -0.3042 -0.2271 0.2296  47   TYR A CA  
908   C C   . TYR B 50   ? 1.2695 0.6436 0.8498 -0.2941 -0.2219 0.2205  47   TYR A C   
909   O O   . TYR B 50   ? 1.2735 0.6189 0.8470 -0.2652 -0.2184 0.2106  47   TYR A O   
910   C CB  . TYR B 50   ? 1.2189 0.6547 0.8314 -0.3077 -0.2133 0.2386  47   TYR A CB  
911   C CG  . TYR B 50   ? 1.1554 0.6174 0.7999 -0.2840 -0.1980 0.2333  47   TYR A CG  
912   C CD1 . TYR B 50   ? 1.1334 0.5781 0.7764 -0.2499 -0.1923 0.2230  47   TYR A CD1 
913   C CD2 . TYR B 50   ? 1.1067 0.6302 0.7909 -0.2871 -0.1861 0.2303  47   TYR A CD2 
914   C CE1 . TYR B 50   ? 1.0891 0.5768 0.7693 -0.2226 -0.1757 0.2108  47   TYR A CE1 
915   C CE2 . TYR B 50   ? 1.0616 0.6237 0.7810 -0.2587 -0.1698 0.2175  47   TYR A CE2 
916   C CZ  . TYR B 50   ? 1.0611 0.6052 0.7785 -0.2279 -0.1649 0.2081  47   TYR A CZ  
917   O OH  . TYR B 50   ? 0.9889 0.5718 0.7399 -0.2025 -0.1497 0.1967  47   TYR A OH  
918   N N   . LYS B 51   ? 1.2457 0.6560 0.8423 -0.3165 -0.2216 0.2239  48   LYS A N   
919   C CA  . LYS B 51   ? 1.2040 0.6205 0.8127 -0.3084 -0.2162 0.2158  48   LYS A CA  
920   C C   . LYS B 51   ? 1.2563 0.6071 0.8232 -0.2981 -0.2282 0.2052  48   LYS A C   
921   O O   . LYS B 51   ? 1.2446 0.5834 0.8144 -0.2786 -0.2235 0.1954  48   LYS A O   
922   C CB  . LYS B 51   ? 1.1629 0.6380 0.7991 -0.3346 -0.2129 0.2226  48   LYS A CB  
923   C CG  . LYS B 51   ? 1.1223 0.6678 0.8015 -0.3402 -0.1994 0.2315  48   LYS A CG  
924   C CD  . LYS B 51   ? 1.1123 0.7181 0.8194 -0.3589 -0.1943 0.2359  48   LYS A CD  
925   C CE  . LYS B 51   ? 1.0719 0.7478 0.8206 -0.3588 -0.1798 0.2429  48   LYS A CE  
926   N NZ  . LYS B 51   ? 1.0450 0.7818 0.8210 -0.3713 -0.1736 0.2457  48   LYS A NZ  
927   N N   . GLU B 52   ? 1.3000 0.6081 0.8267 -0.3105 -0.2442 0.2068  49   GLU A N   
928   C CA  . GLU B 52   ? 1.3737 0.6156 0.8557 -0.2980 -0.2565 0.1962  49   GLU A CA  
929   C C   . GLU B 52   ? 1.4109 0.6089 0.8735 -0.2616 -0.2548 0.1869  49   GLU A C   
930   O O   . GLU B 52   ? 1.4586 0.6196 0.9011 -0.2379 -0.2567 0.1751  49   GLU A O   
931   C CB  . GLU B 52   ? 1.4509 0.6600 0.8928 -0.3237 -0.2753 0.2014  49   GLU A CB  
932   C CG  . GLU B 52   ? 1.4519 0.6951 0.9030 -0.3569 -0.2802 0.2088  49   GLU A CG  
933   C CD  . GLU B 52   ? 1.5070 0.7246 0.9204 -0.3850 -0.2992 0.2169  49   GLU A CD  
934   O OE1 . GLU B 52   ? 1.4826 0.7301 0.9065 -0.4034 -0.2998 0.2285  49   GLU A OE1 
935   O OE2 . GLU B 52   ? 1.5795 0.7464 0.9510 -0.3884 -0.3141 0.2120  49   GLU A OE2 
936   N N   . LEU B 53   ? 1.3904 0.5948 0.8587 -0.2553 -0.2512 0.1921  50   LEU A N   
937   C CA  . LEU B 53   ? 1.3974 0.5618 0.8443 -0.2209 -0.2508 0.1844  50   LEU A CA  
938   C C   . LEU B 53   ? 1.3875 0.5772 0.8655 -0.1914 -0.2352 0.1790  50   LEU A C   
939   O O   . LEU B 53   ? 1.4252 0.5821 0.8840 -0.1579 -0.2349 0.1691  50   LEU A O   
940   C CB  . LEU B 53   ? 1.3831 0.5431 0.8216 -0.2265 -0.2541 0.1926  50   LEU A CB  
941   C CG  . LEU B 53   ? 1.4183 0.5410 0.8341 -0.1923 -0.2542 0.1862  50   LEU A CG  
942   C CD1 . LEU B 53   ? 1.4953 0.5527 0.8608 -0.1728 -0.2664 0.1740  50   LEU A CD1 
943   C CD2 . LEU B 53   ? 1.4539 0.5763 0.8634 -0.2035 -0.2578 0.1957  50   LEU A CD2 
944   N N   . LYS B 54   ? 1.3221 0.5712 0.8464 -0.2026 -0.2226 0.1853  51   LYS A N   
945   C CA  . LYS B 54   ? 1.2362 0.5343 0.8015 -0.1727 -0.2042 0.1748  51   LYS A CA  
946   C C   . LYS B 54   ? 1.1966 0.4744 0.7520 -0.1455 -0.2025 0.1601  51   LYS A C   
947   O O   . LYS B 54   ? 1.1565 0.4373 0.7161 -0.1119 -0.1951 0.1511  51   LYS A O   
948   C CB  . LYS B 54   ? 1.2110 0.5878 0.8300 -0.1889 -0.1901 0.1786  51   LYS A CB  
949   C CG  . LYS B 54   ? 1.1834 0.6109 0.8436 -0.1628 -0.1723 0.1665  51   LYS A CG  
950   C CD  . LYS B 54   ? 1.1498 0.6408 0.8518 -0.1798 -0.1620 0.1688  51   LYS A CD  
951   C CE  . LYS B 54   ? 1.1280 0.6587 0.8633 -0.1557 -0.1470 0.1565  51   LYS A CE  
952   N NZ  . LYS B 54   ? 1.0867 0.6701 0.8554 -0.1706 -0.1389 0.1575  51   LYS A NZ  
953   N N   . PRO B 55   ? 1.2026 0.4624 0.7453 -0.1572 -0.2090 0.1574  52   PRO A N   
954   C CA  . PRO B 55   ? 1.1997 0.4390 0.7308 -0.1287 -0.2076 0.1432  52   PRO A CA  
955   C C   . PRO B 55   ? 1.3083 0.4750 0.7859 -0.1041 -0.2199 0.1382  52   PRO A C   
956   O O   . PRO B 55   ? 1.2966 0.4601 0.7715 -0.0697 -0.2145 0.1265  52   PRO A O   
957   C CB  . PRO B 55   ? 1.2031 0.4350 0.7281 -0.1523 -0.2142 0.1437  52   PRO A CB  
958   C CG  . PRO B 55   ? 1.1917 0.4681 0.7444 -0.1885 -0.2122 0.1565  52   PRO A CG  
959   C CD  . PRO B 55   ? 1.2180 0.4827 0.7596 -0.1958 -0.2167 0.1668  52   PRO A CD  
960   N N   . ILE B 56   ? 1.3999 0.5190 0.8382 -0.1192 -0.2349 0.1449  53   ILE A N   
961   C CA  . ILE B 56   ? 1.3477 0.4122 0.7395 -0.0931 -0.2443 0.1365  53   ILE A CA  
962   C C   . ILE B 56   ? 1.5505 0.6250 0.9511 -0.0610 -0.2355 0.1353  53   ILE A C   
963   O O   . ILE B 56   ? 1.3506 0.4037 0.7315 -0.0243 -0.2348 0.1249  53   ILE A O   
964   C CB  . ILE B 56   ? 1.6272 0.6551 0.9823 -0.1181 -0.2602 0.1416  53   ILE A CB  
965   C CG1 . ILE B 56   ? 1.6393 0.6626 0.9864 -0.1505 -0.2694 0.1437  53   ILE A CG1 
966   C CG2 . ILE B 56   ? 1.4723 0.4410 0.7757 -0.0906 -0.2707 0.1324  53   ILE A CG2 
967   C CD1 . ILE B 56   ? 1.4720 0.4700 0.7888 -0.1813 -0.2851 0.1516  53   ILE A CD1 
968   N N   . ILE B 57   ? 1.4244 0.5350 0.8547 -0.0736 -0.2285 0.1463  54   ILE A N   
969   C CA  . ILE B 57   ? 1.4045 0.5400 0.8511 -0.0448 -0.2182 0.1441  54   ILE A CA  
970   C C   . ILE B 57   ? 1.3669 0.5562 0.8521 -0.0166 -0.2012 0.1323  54   ILE A C   
971   O O   . ILE B 57   ? 1.3679 0.5606 0.8498 0.0178  -0.1961 0.1256  54   ILE A O   
972   C CB  . ILE B 57   ? 1.3754 0.5539 0.8540 -0.0666 -0.2119 0.1557  54   ILE A CB  
973   C CG1 . ILE B 57   ? 1.4415 0.5737 0.8829 -0.0927 -0.2278 0.1662  54   ILE A CG1 
974   C CG2 . ILE B 57   ? 1.3475 0.5615 0.8491 -0.0378 -0.1996 0.1525  54   ILE A CG2 
975   C CD1 . ILE B 57   ? 1.4224 0.5895 0.8885 -0.1124 -0.2235 0.1793  54   ILE A CD1 
976   N N   . ASP B 58   ? 1.3305 0.5635 0.8516 -0.0310 -0.1926 0.1302  55   ASP A N   
977   C CA  . ASP B 58   ? 1.3129 0.5970 0.8703 -0.0080 -0.1771 0.1200  55   ASP A CA  
978   C C   . ASP B 58   ? 1.3680 0.6158 0.8934 0.0253  -0.1812 0.1088  55   ASP A C   
979   O O   . ASP B 58   ? 1.3323 0.6188 0.8808 0.0517  -0.1692 0.1011  55   ASP A O   
980   C CB  . ASP B 58   ? 1.3024 0.6311 0.8971 -0.0308 -0.1694 0.1201  55   ASP A CB  
981   C CG  . ASP B 58   ? 1.2744 0.6602 0.9124 -0.0525 -0.1597 0.1285  55   ASP A CG  
982   O OD1 . ASP B 58   ? 1.2668 0.6762 0.9201 -0.0417 -0.1530 0.1306  55   ASP A OD1 
983   O OD2 . ASP B 58   ? 1.2565 0.6643 0.9120 -0.0793 -0.1589 0.1330  55   ASP A OD2 
984   N N   . ARG B 59   ? 1.4721 0.6469 0.9431 0.0245  -0.1983 0.1079  56   ARG A N   
985   C CA  . ARG B 59   ? 1.5424 0.6788 0.9773 0.0597  -0.2032 0.0970  56   ARG A CA  
986   C C   . ARG B 59   ? 1.5579 0.7009 0.9867 0.0968  -0.1984 0.0936  56   ARG A C   
987   O O   . ARG B 59   ? 1.5641 0.7186 0.9910 0.1306  -0.1929 0.0842  56   ARG A O   
988   C CB  . ARG B 59   ? 1.6364 0.6854 1.0071 0.0520  -0.2247 0.0974  56   ARG A CB  
989   C CG  . ARG B 59   ? 1.6466 0.6901 1.0202 0.0141  -0.2307 0.1007  56   ARG A CG  
990   C CD  . ARG B 59   ? 1.7183 0.7093 1.0437 0.0176  -0.2444 0.0912  56   ARG A CD  
991   N NE  . ARG B 59   ? 1.7357 0.7160 1.0557 -0.0229 -0.2538 0.0964  56   ARG A NE  
992   C CZ  . ARG B 59   ? 1.7696 0.7163 1.0583 -0.0472 -0.2680 0.1014  56   ARG A CZ  
993   N NH1 . ARG B 59   ? 1.7898 0.7061 1.0484 -0.0350 -0.2744 0.1011  56   ARG A NH1 
994   N NH2 . ARG B 59   ? 1.7791 0.7241 1.0657 -0.0837 -0.2760 0.1068  56   ARG A NH2 
995   N N   . ILE B 60   ? 1.5824 0.7217 1.0087 0.0912  -0.2003 0.1017  57   ILE A N   
996   C CA  . ILE B 60   ? 1.5822 0.7322 1.0046 0.1254  -0.1955 0.0994  57   ILE A CA  
997   C C   . ILE B 60   ? 1.5106 0.7455 0.9911 0.1381  -0.1753 0.0959  57   ILE A C   
998   O O   . ILE B 60   ? 1.5302 0.7831 1.0098 0.1733  -0.1695 0.0891  57   ILE A O   
999   C CB  . ILE B 60   ? 1.6060 0.7337 1.0140 0.1133  -0.2021 0.1095  57   ILE A CB  
1000  C CG1 . ILE B 60   ? 1.6932 0.7454 1.0467 0.0963  -0.2212 0.1115  57   ILE A CG1 
1001  C CG2 . ILE B 60   ? 1.6175 0.7573 1.0207 0.1495  -0.1973 0.1072  57   ILE A CG2 
1002  C CD1 . ILE B 60   ? 1.7286 0.7664 1.0710 0.0804  -0.2268 0.1201  57   ILE A CD1 
1003  N N   . TYR B 61   ? 1.3658 0.6545 0.8959 0.1096  -0.1651 0.1011  58   TYR A N   
1004  C CA  . TYR B 61   ? 1.2400 0.6052 0.8228 0.1179  -0.1474 0.0983  58   TYR A CA  
1005  C C   . TYR B 61   ? 1.1975 0.5790 0.7873 0.1340  -0.1421 0.0888  58   TYR A C   
1006  O O   . TYR B 61   ? 1.1482 0.5667 0.7525 0.1608  -0.1330 0.0838  58   TYR A O   
1007  C CB  . TYR B 61   ? 1.1697 0.5809 0.7974 0.0842  -0.1393 0.1054  58   TYR A CB  
1008  C CG  . TYR B 61   ? 1.1859 0.5949 0.8145 0.0698  -0.1418 0.1151  58   TYR A CG  
1009  C CD1 . TYR B 61   ? 1.1949 0.6342 0.8385 0.0866  -0.1347 0.1165  58   TYR A CD1 
1010  C CD2 . TYR B 61   ? 1.2101 0.5899 0.8254 0.0384  -0.1512 0.1235  58   TYR A CD2 
1011  C CE1 . TYR B 61   ? 1.2019 0.6397 0.8464 0.0738  -0.1368 0.1254  58   TYR A CE1 
1012  C CE2 . TYR B 61   ? 1.2319 0.6119 0.8482 0.0250  -0.1534 0.1331  58   TYR A CE2 
1013  C CZ  . TYR B 61   ? 1.2265 0.6345 0.8573 0.0434  -0.1460 0.1336  58   TYR A CZ  
1014  O OH  . TYR B 61   ? 1.2421 0.6507 0.8739 0.0306  -0.1480 0.1430  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  ? 1.6755 1.0350 1.1937 -0.2180 -0.2428 -0.0310 505  LEU A N   
4051  C CA  . LEU B 508  ? 1.7407 1.0410 1.2232 -0.2170 -0.2545 -0.0296 505  LEU A CA  
4052  C C   . LEU B 508  ? 1.7788 1.0632 1.2419 -0.2587 -0.2714 -0.0158 505  LEU A C   
4053  O O   . LEU B 508  ? 1.8052 1.0602 1.2525 -0.2623 -0.2772 -0.0109 505  LEU A O   
4054  C CB  . LEU B 508  ? 1.8151 1.0406 1.2464 -0.1949 -0.2669 -0.0415 505  LEU A CB  
4055  C CG  . LEU B 508  ? 1.8461 1.0651 1.2815 -0.1494 -0.2539 -0.0530 505  LEU A CG  
4056  C CD1 . LEU B 508  ? 1.7963 1.0827 1.2810 -0.1298 -0.2320 -0.0579 505  LEU A CD1 
4057  C CD2 . LEU B 508  ? 1.9265 1.0690 1.3049 -0.1289 -0.2688 -0.0639 505  LEU A CD2 
4058  N N   . GLU B 509  ? 1.7118 1.0167 1.1755 -0.2908 -0.2797 -0.0087 506  GLU A N   
4059  C CA  . GLU B 509  ? 1.7207 1.0223 1.1705 -0.3333 -0.2948 0.0066  506  GLU A CA  
4060  C C   . GLU B 509  ? 1.6780 1.0550 1.1766 -0.3469 -0.2812 0.0183  506  GLU A C   
4061  O O   . GLU B 509  ? 1.6965 1.0769 1.1884 -0.3763 -0.2901 0.0323  506  GLU A O   
4062  C CB  . GLU B 509  ? 1.7380 1.0439 1.1726 -0.3563 -0.3054 0.0126  506  GLU A CB  
4063  C CG  . GLU B 509  ? 1.8218 1.0550 1.2044 -0.3436 -0.3191 0.0066  506  GLU A CG  
4064  C CD  . GLU B 509  ? 1.8673 1.1064 1.2386 -0.3614 -0.3274 0.0092  506  GLU A CD  
4065  O OE1 . GLU B 509  ? 1.9012 1.1006 1.2470 -0.3417 -0.3317 -0.0022 506  GLU A OE1 
4066  O OE2 . GLU B 509  ? 1.8714 1.1570 1.2593 -0.3940 -0.3293 0.0231  506  GLU A OE2 
4067  N N   . MET B 510  ? 1.6233 1.0633 1.1706 -0.3235 -0.2588 0.0139  507  MET A N   
4068  C CA  . MET B 510  ? 1.5698 1.0770 1.1619 -0.3272 -0.2439 0.0227  507  MET A CA  
4069  C C   . MET B 510  ? 1.6041 1.1022 1.2070 -0.3002 -0.2327 0.0188  507  MET A C   
4070  O O   . MET B 510  ? 1.5531 1.0998 1.1896 -0.3014 -0.2211 0.0256  507  MET A O   
4071  C CB  . MET B 510  ? 1.4699 1.0502 1.1060 -0.3183 -0.2269 0.0207  507  MET A CB  
4072  C CG  . MET B 510  ? 1.4509 1.0604 1.0860 -0.3479 -0.2355 0.0277  507  MET A CG  
4073  S SD  . MET B 510  ? 1.4212 1.0901 1.0751 -0.3867 -0.2388 0.0479  507  MET A SD  
4074  C CE  . MET B 510  ? 1.3473 1.0878 1.0561 -0.3587 -0.2123 0.0466  507  MET A CE  
4075  N N   . GLU B 511  ? 1.7534 1.1919 1.3276 -0.2752 -0.2362 0.0080  508  GLU A N   
4076  C CA  . GLU B 511  ? 1.7611 1.1925 1.3446 -0.2481 -0.2257 0.0041  508  GLU A CA  
4077  C C   . GLU B 511  ? 1.7617 1.1829 1.3386 -0.2660 -0.2319 0.0152  508  GLU A C   
4078  O O   . GLU B 511  ? 1.7285 1.1846 1.3365 -0.2537 -0.2178 0.0172  508  GLU A O   
4079  C CB  . GLU B 511  ? 1.8471 1.2169 1.3963 -0.2176 -0.2301 -0.0091 508  GLU A CB  
4080  C CG  . GLU B 511  ? 1.8781 1.2330 1.4285 -0.1901 -0.2225 -0.0128 508  GLU A CG  
4081  C CD  . GLU B 511  ? 1.9565 1.2580 1.4734 -0.1574 -0.2261 -0.0257 508  GLU A CD  
4082  O OE1 . GLU B 511  ? 1.9606 1.2662 1.4778 -0.1437 -0.2230 -0.0343 508  GLU A OE1 
4083  O OE2 . GLU B 511  ? 2.0115 1.2679 1.5009 -0.1444 -0.2323 -0.0272 508  GLU A OE2 
4084  N N   . PRO B 512  ? 1.6802 1.0546 1.2174 -0.2950 -0.2525 0.0231  509  PRO A N   
4085  C CA  . PRO B 512  ? 1.6292 0.9970 1.1616 -0.3124 -0.2577 0.0345  509  PRO A CA  
4086  C C   . PRO B 512  ? 1.5548 1.0001 1.1325 -0.3311 -0.2467 0.0467  509  PRO A C   
4087  O O   . PRO B 512  ? 1.5651 1.0150 1.1468 -0.3401 -0.2469 0.0554  509  PRO A O   
4088  C CB  . PRO B 512  ? 1.6799 0.9854 1.1590 -0.3423 -0.2830 0.0413  509  PRO A CB  
4089  C CG  . PRO B 512  ? 1.7256 0.9857 1.1738 -0.3248 -0.2896 0.0291  509  PRO A CG  
4090  C CD  . PRO B 512  ? 1.6999 1.0154 1.1885 -0.3108 -0.2734 0.0212  509  PRO A CD  
4091  N N   . SER B 513  ? 1.4472 0.9533 1.0574 -0.3358 -0.2373 0.0475  510  SER A N   
4092  C CA  . SER B 513  ? 1.3097 0.8909 0.9604 -0.3504 -0.2268 0.0586  510  SER A CA  
4093  C C   . SER B 513  ? 1.1901 0.8068 0.8774 -0.3223 -0.2069 0.0549  510  SER A C   
4094  O O   . SER B 513  ? 1.1464 0.8106 0.8590 -0.3325 -0.2005 0.0647  510  SER A O   
4095  C CB  . SER B 513  ? 1.2476 0.8826 0.9196 -0.3602 -0.2227 0.0599  510  SER A CB  
4096  O OG  . SER B 513  ? 1.1990 0.8429 0.8870 -0.3285 -0.2096 0.0460  510  SER A OG  
4097  N N   . LEU B 514  ? 1.1545 0.7506 0.8440 -0.2875 -0.1975 0.0415  511  LEU A N   
4098  C CA  . LEU B 514  ? 1.1010 0.7277 0.8225 -0.2624 -0.1800 0.0384  511  LEU A CA  
4099  C C   . LEU B 514  ? 1.1507 0.7531 0.8615 -0.2658 -0.1840 0.0445  511  LEU A C   
4100  O O   . LEU B 514  ? 1.1336 0.7770 0.8719 -0.2664 -0.1744 0.0507  511  LEU A O   
4101  C CB  . LEU B 514  ? 1.0676 0.6793 0.7919 -0.2268 -0.1703 0.0239  511  LEU A CB  
4102  C CG  . LEU B 514  ? 1.0173 0.6529 0.7694 -0.2005 -0.1537 0.0202  511  LEU A CG  
4103  C CD1 . LEU B 514  ? 0.9593 0.6637 0.7524 -0.2037 -0.1401 0.0253  511  LEU A CD1 
4104  C CD2 . LEU B 514  ? 1.0121 0.6309 0.7621 -0.1685 -0.1466 0.0072  511  LEU A CD2 
4105  N N   . SER B 515  ? 1.2339 0.7678 0.9027 -0.2670 -0.1987 0.0426  512  SER A N   
4106  C CA  . SER B 515  ? 1.2512 0.7574 0.9058 -0.2708 -0.2040 0.0486  512  SER A CA  
4107  C C   . SER B 515  ? 1.2373 0.7650 0.8930 -0.3081 -0.2124 0.0646  512  SER A C   
4108  O O   . SER B 515  ? 1.2332 0.7705 0.8972 -0.3115 -0.2099 0.0717  512  SER A O   
4109  C CB  . SER B 515  ? 1.3316 0.7555 0.9355 -0.2623 -0.2193 0.0425  512  SER A CB  
4110  O OG  . SER B 515  ? 1.4191 0.8038 0.9856 -0.2903 -0.2389 0.0470  512  SER A OG  
4111  N N   . PHE B 516  ? 1.2263 0.7645 0.8738 -0.3365 -0.2223 0.0711  513  PHE A N   
4112  C CA  . PHE B 516  ? 1.2402 0.8087 0.8911 -0.3734 -0.2298 0.0878  513  PHE A CA  
4113  C C   . PHE B 516  ? 1.1738 0.8238 0.8740 -0.3699 -0.2121 0.0933  513  PHE A C   
4114  O O   . PHE B 516  ? 1.1719 0.8472 0.8793 -0.3897 -0.2140 0.1062  513  PHE A O   
4115  C CB  . PHE B 516  ? 1.2812 0.8478 0.9131 -0.4047 -0.2444 0.0938  513  PHE A CB  
4116  C CG  . PHE B 516  ? 1.3794 0.8787 0.9596 -0.4222 -0.2652 0.0987  513  PHE A CG  
4117  C CD1 . PHE B 516  ? 1.4295 0.8691 0.9810 -0.4083 -0.2708 0.0957  513  PHE A CD1 
4118  C CD2 . PHE B 516  ? 1.4123 0.9156 0.9734 -0.4454 -0.2764 0.1069  513  PHE A CD2 
4119  C CE1 . PHE B 516  ? 1.4980 0.8818 1.0015 -0.4169 -0.2878 0.1002  513  PHE A CE1 
4120  C CE2 . PHE B 516  ? 1.4901 0.9363 1.0032 -0.4558 -0.2936 0.1120  513  PHE A CE2 
4121  C CZ  . PHE B 516  ? 1.5367 0.9225 1.0202 -0.4414 -0.2996 0.1084  513  PHE A CZ  
4122  N N   . TYR B 517  ? 1.1354 0.8259 0.8676 -0.3448 -0.1954 0.0840  514  TYR A N   
4123  C CA  . TYR B 517  ? 1.0622 0.8229 0.8368 -0.3367 -0.1787 0.0876  514  TYR A CA  
4124  C C   . TYR B 517  ? 1.0617 0.8146 0.8444 -0.3209 -0.1715 0.0874  514  TYR A C   
4125  O O   . TYR B 517  ? 1.0537 0.8451 0.8538 -0.3307 -0.1676 0.0973  514  TYR A O   
4126  C CB  . TYR B 517  ? 1.0011 0.7966 0.8021 -0.3121 -0.1640 0.0768  514  TYR A CB  
4127  C CG  . TYR B 517  ? 0.9356 0.8029 0.7752 -0.3055 -0.1488 0.0807  514  TYR A CG  
4128  C CD1 . TYR B 517  ? 0.8918 0.7717 0.7517 -0.2826 -0.1357 0.0771  514  TYR A CD1 
4129  C CD2 . TYR B 517  ? 0.9181 0.8405 0.7720 -0.3213 -0.1482 0.0881  514  TYR A CD2 
4130  C CE1 . TYR B 517  ? 0.8508 0.7910 0.7413 -0.2753 -0.1231 0.0802  514  TYR A CE1 
4131  C CE2 . TYR B 517  ? 0.8555 0.8414 0.7407 -0.3122 -0.1349 0.0911  514  TYR A CE2 
4132  C CZ  . TYR B 517  ? 0.8408 0.8330 0.7430 -0.2890 -0.1227 0.0869  514  TYR A CZ  
4133  O OH  . TYR B 517  ? 0.8345 0.8850 0.7635 -0.2788 -0.1107 0.0894  514  TYR A OH  
4134  N N   . ASN B 518  ? 1.0907 0.7961 0.8605 -0.2958 -0.1698 0.0763  515  ASN A N   
4135  C CA  . ASN B 518  ? 1.1120 0.8103 0.8891 -0.2796 -0.1630 0.0757  515  ASN A CA  
4136  C C   . ASN B 518  ? 1.1761 0.8420 0.9280 -0.3017 -0.1766 0.0865  515  ASN A C   
4137  O O   . ASN B 518  ? 1.1901 0.8776 0.9567 -0.3026 -0.1714 0.0930  515  ASN A O   
4138  C CB  . ASN B 518  ? 1.1385 0.7990 0.9076 -0.2469 -0.1580 0.0618  515  ASN A CB  
4139  C CG  . ASN B 518  ? 1.0988 0.7985 0.8986 -0.2232 -0.1417 0.0526  515  ASN A CG  
4140  O OD1 . ASN B 518  ? 1.0604 0.8148 0.8917 -0.2232 -0.1306 0.0559  515  ASN A OD1 
4141  N ND2 . ASN B 518  ? 1.1062 0.7772 0.8949 -0.2025 -0.1407 0.0411  515  ASN A ND2 
4142  N N   . LYS B 519  ? 1.2200 0.8320 0.9319 -0.3200 -0.1947 0.0887  516  LYS A N   
4143  C CA  . LYS B 519  ? 1.2473 0.8236 0.9305 -0.3435 -0.2095 0.0998  516  LYS A CA  
4144  C C   . LYS B 519  ? 1.2065 0.8383 0.9086 -0.3742 -0.2101 0.1160  516  LYS A C   
4145  O O   . LYS B 519  ? 1.1970 0.8284 0.8968 -0.3847 -0.2127 0.1255  516  LYS A O   
4146  C CB  . LYS B 519  ? 1.3453 0.8506 0.9779 -0.3590 -0.2304 0.0992  516  LYS A CB  
4147  C CG  . LYS B 519  ? 1.4126 0.8490 1.0141 -0.3297 -0.2341 0.0859  516  LYS A CG  
4148  C CD  . LYS B 519  ? 1.5312 0.8924 1.0764 -0.3473 -0.2573 0.0866  516  LYS A CD  
4149  C CE  . LYS B 519  ? 1.5875 0.8788 1.0974 -0.3152 -0.2617 0.0734  516  LYS A CE  
4150  N NZ  . LYS B 519  ? 1.6601 0.8923 1.1170 -0.3218 -0.2806 0.0737  516  LYS A NZ  
4151  N N   . ALA B 520  ? 1.1674 0.8497 0.8879 -0.3881 -0.2076 0.1198  517  ALA A N   
4152  C CA  . ALA B 520  ? 1.1122 0.8537 0.8501 -0.4166 -0.2083 0.1359  517  ALA A CA  
4153  C C   . ALA B 520  ? 1.0455 0.8466 0.8238 -0.3989 -0.1900 0.1369  517  ALA A C   
4154  O O   . ALA B 520  ? 1.0620 0.8916 0.8474 -0.4154 -0.1911 0.1497  517  ALA A O   
4155  C CB  . ALA B 520  ? 1.0579 0.8381 0.8021 -0.4348 -0.2112 0.1396  517  ALA A CB  
4156  N N   . ARG B 521  ? 0.9378 0.9378 0.9378 0.0000  0.0000  0.0000  518  ARG A N   
4157  C CA  . ARG B 521  ? 0.9378 0.9378 0.9378 0.0000  0.0000  0.0000  518  ARG A CA  
4158  C C   . ARG B 521  ? 0.9378 0.9378 0.9378 0.0000  0.0000  0.0000  518  ARG A C   
4159  O O   . ARG B 521  ? 0.9378 0.9378 0.9378 0.0000  0.0000  0.0000  518  ARG A O   
4160  C CB  . ARG B 521  ? 0.9378 0.9378 0.9378 0.0000  0.0000  0.0000  518  ARG A CB  
4161  C CG  . ARG B 521  ? 0.9378 0.9378 0.9378 0.0000  0.0000  0.0000  518  ARG A CG  
4162  C CD  . ARG B 521  ? 0.9378 0.9378 0.9378 0.0000  0.0000  0.0000  518  ARG A CD  
4163  N NE  . ARG B 521  ? 0.9378 0.9378 0.9378 0.0000  0.0000  0.0000  518  ARG A NE  
4164  C CZ  . ARG B 521  ? 0.9378 0.9378 0.9378 0.0000  0.0000  0.0000  518  ARG A CZ  
4165  N NH1 . ARG B 521  ? 0.9378 0.9378 0.9378 0.0000  0.0000  0.0000  518  ARG A NH1 
4166  N NH2 . ARG B 521  ? 0.9378 0.9378 0.9378 0.0000  0.0000  0.0000  518  ARG A NH2 
4167  N N   . ASN B 522  ? 0.8448 0.8448 0.8448 0.0000  0.0000  0.0000  519  ASN A N   
4168  C CA  . ASN B 522  ? 0.8448 0.8448 0.8448 0.0000  0.0000  0.0000  519  ASN A CA  
4169  C C   . ASN B 522  ? 0.8448 0.8448 0.8448 0.0000  0.0000  0.0000  519  ASN A C   
4170  O O   . ASN B 522  ? 0.8448 0.8448 0.8448 0.0000  0.0000  0.0000  519  ASN A O   
4171  C CB  . ASN B 522  ? 0.8448 0.8448 0.8448 0.0000  0.0000  0.0000  519  ASN A CB  
4172  C CG  . ASN B 522  ? 0.8448 0.8448 0.8448 0.0000  0.0000  0.0000  519  ASN A CG  
4173  O OD1 . ASN B 522  ? 0.8448 0.8448 0.8448 0.0000  0.0000  0.0000  519  ASN A OD1 
4174  N ND2 . ASN B 522  ? 0.8448 0.8448 0.8448 0.0000  0.0000  0.0000  519  ASN A ND2 
4175  N N   . TYR B 523  ? 0.9276 0.9276 0.9276 0.0000  0.0000  0.0000  520  TYR A N   
4176  C CA  . TYR B 523  ? 0.9276 0.9276 0.9276 0.0000  0.0000  0.0000  520  TYR A CA  
4177  C C   . TYR B 523  ? 0.9276 0.9276 0.9276 0.0000  0.0000  0.0000  520  TYR A C   
4178  O O   . TYR B 523  ? 0.9276 0.9276 0.9276 0.0000  0.0000  0.0000  520  TYR A O   
4179  C CB  . TYR B 523  ? 0.9276 0.9276 0.9276 0.0000  0.0000  0.0000  520  TYR A CB  
4180  C CG  . TYR B 523  ? 0.9276 0.9276 0.9276 0.0000  0.0000  0.0000  520  TYR A CG  
4181  C CD1 . TYR B 523  ? 0.9276 0.9276 0.9276 0.0000  0.0000  0.0000  520  TYR A CD1 
4182  C CD2 . TYR B 523  ? 0.9276 0.9276 0.9276 0.0000  0.0000  0.0000  520  TYR A CD2 
4183  C CE1 . TYR B 523  ? 0.9276 0.9276 0.9276 0.0000  0.0000  0.0000  520  TYR A CE1 
4184  C CE2 . TYR B 523  ? 0.9276 0.9276 0.9276 0.0000  0.0000  0.0000  520  TYR A CE2 
4185  C CZ  . TYR B 523  ? 0.9276 0.9276 0.9276 0.0000  0.0000  0.0000  520  TYR A CZ  
4186  O OH  . TYR B 523  ? 0.9276 0.9276 0.9276 0.0000  0.0000  0.0000  520  TYR A OH  
4187  N N   . ALA B 524  ? 0.7833 0.7833 0.7833 0.0000  0.0000  0.0000  521  ALA A N   
4188  C CA  . ALA B 524  ? 0.7833 0.7833 0.7833 0.0000  0.0000  0.0000  521  ALA A CA  
4189  C C   . ALA B 524  ? 0.7833 0.7833 0.7833 0.0000  0.0000  0.0000  521  ALA A C   
4190  O O   . ALA B 524  ? 0.7833 0.7833 0.7833 0.0000  0.0000  0.0000  521  ALA A O   
4191  C CB  . ALA B 524  ? 0.7833 0.7833 0.7833 0.0000  0.0000  0.0000  521  ALA A CB  
4192  N N   . THR B 525  ? 0.7678 0.7678 0.7678 0.0000  0.0000  0.0000  522  THR A N   
4193  C CA  . THR B 525  ? 0.7678 0.7678 0.7678 0.0000  0.0000  0.0000  522  THR A CA  
4194  C C   . THR B 525  ? 0.7678 0.7678 0.7678 0.0000  0.0000  0.0000  522  THR A C   
4195  O O   . THR B 525  ? 0.7678 0.7678 0.7678 0.0000  0.0000  0.0000  522  THR A O   
4196  C CB  . THR B 525  ? 0.7678 0.7678 0.7678 0.0000  0.0000  0.0000  522  THR A CB  
4197  O OG1 . THR B 525  ? 0.7678 0.7678 0.7678 0.0000  0.0000  0.0000  522  THR A OG1 
4198  C CG2 . THR B 525  ? 0.7678 0.7678 0.7678 0.0000  0.0000  0.0000  522  THR A CG2 
4199  N N   . LYS B 526  ? 0.6982 0.6982 0.6982 0.0000  0.0000  0.0000  523  LYS A N   
4200  C CA  . LYS B 526  ? 0.6982 0.6982 0.6982 0.0000  0.0000  0.0000  523  LYS A CA  
4201  C C   . LYS B 526  ? 0.6982 0.6982 0.6982 0.0000  0.0000  0.0000  523  LYS A C   
4202  O O   . LYS B 526  ? 0.6982 0.6982 0.6982 0.0000  0.0000  0.0000  523  LYS A O   
4203  C CB  . LYS B 526  ? 0.6982 0.6982 0.6982 0.0000  0.0000  0.0000  523  LYS A CB  
4204  C CG  . LYS B 526  ? 0.6982 0.6982 0.6982 0.0000  0.0000  0.0000  523  LYS A CG  
4205  C CD  . LYS B 526  ? 0.6982 0.6982 0.6982 0.0000  0.0000  0.0000  523  LYS A CD  
4206  C CE  . LYS B 526  ? 0.6982 0.6982 0.6982 0.0000  0.0000  0.0000  523  LYS A CE  
4207  N NZ  . LYS B 526  ? 0.6982 0.6982 0.6982 0.0000  0.0000  0.0000  523  LYS A NZ  
4208  N N   . LYS B 527  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  524  LYS A N   
4209  C CA  . LYS B 527  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  524  LYS A CA  
4210  C C   . LYS B 527  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  524  LYS A C   
4211  O O   . LYS B 527  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  524  LYS A O   
4217  N N   . PRO B 528  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  525  PRO A N   
4218  C CA  . PRO B 528  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  525  PRO A CA  
4219  C C   . PRO B 528  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  525  PRO A C   
4220  O O   . PRO B 528  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  525  PRO A O   
4221  C CB  . PRO B 528  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  525  PRO A CB  
4222  C CG  . PRO B 528  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  525  PRO A CG  
4223  C CD  . PRO B 528  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  525  PRO A CD  
4224  N N   . TYR B 529  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  526  TYR A N   
4225  C CA  . TYR B 529  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  526  TYR A CA  
4226  C C   . TYR B 529  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  526  TYR A C   
4227  O O   . TYR B 529  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  526  TYR A O   
4228  C CB  . TYR B 529  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  526  TYR A CB  
4229  C CG  . TYR B 529  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  526  TYR A CG  
4230  C CD1 . TYR B 529  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  526  TYR A CD1 
4231  C CD2 . TYR B 529  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  526  TYR A CD2 
4232  C CE1 . TYR B 529  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  526  TYR A CE1 
4233  C CE2 . TYR B 529  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  526  TYR A CE2 
4234  C CZ  . TYR B 529  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  526  TYR A CZ  
4235  O OH  . TYR B 529  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  526  TYR A OH  
4236  N N   . SER B 530  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  527  SER A N   
4237  C CA  . SER B 530  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  527  SER A CA  
4238  C C   . SER B 530  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  527  SER A C   
4239  O O   . SER B 530  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  527  SER A O   
4240  C CB  . SER B 530  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  527  SER A CB  
4241  O OG  . SER B 530  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  527  SER A OG  
4242  N N   . VAL B 531  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  528  VAL A N   
4243  C CA  . VAL B 531  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  528  VAL A CA  
4244  C C   . VAL B 531  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  528  VAL A C   
4245  O O   . VAL B 531  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  528  VAL A O   
4246  C CB  . VAL B 531  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  528  VAL A CB  
4247  C CG1 . VAL B 531  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  528  VAL A CG1 
4248  C CG2 . VAL B 531  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  528  VAL A CG2 
4249  N N   . GLU B 532  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  529  GLU A N   
4250  C CA  . GLU B 532  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  529  GLU A CA  
4251  C C   . GLU B 532  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  529  GLU A C   
4252  O O   . GLU B 532  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  529  GLU A O   
4253  C CB  . GLU B 532  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  529  GLU A CB  
4254  C CG  . GLU B 532  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  529  GLU A CG  
4255  C CD  . GLU B 532  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  529  GLU A CD  
4256  O OE1 . GLU B 532  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  529  GLU A OE1 
4257  O OE2 . GLU B 532  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  529  GLU A OE2 
4258  N N   . LYS B 533  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  530  LYS A N   
4259  C CA  . LYS B 533  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  530  LYS A CA  
4260  C C   . LYS B 533  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  530  LYS A C   
4261  O O   . LYS B 533  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  530  LYS A O   
4262  C CB  . LYS B 533  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  530  LYS A CB  
4263  C CG  . LYS B 533  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  530  LYS A CG  
4264  C CD  . LYS B 533  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  530  LYS A CD  
4265  C CE  . LYS B 533  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  530  LYS A CE  
4266  N NZ  . LYS B 533  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  530  LYS A NZ  
4267  N N   . PHE B 534  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  531  PHE A N   
4268  C CA  . PHE B 534  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  531  PHE A CA  
4269  C C   . PHE B 534  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  531  PHE A C   
4270  O O   . PHE B 534  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  531  PHE A O   
4271  C CB  . PHE B 534  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  531  PHE A CB  
4272  C CG  . PHE B 534  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  531  PHE A CG  
4273  C CD1 . PHE B 534  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  531  PHE A CD1 
4274  C CD2 . PHE B 534  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  531  PHE A CD2 
4275  C CE1 . PHE B 534  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  531  PHE A CE1 
4276  C CE2 . PHE B 534  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  531  PHE A CE2 
4277  C CZ  . PHE B 534  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  531  PHE A CZ  
4278  N N   . LYS B 535  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  532  LYS A N   
4279  C CA  . LYS B 535  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  532  LYS A CA  
4280  C C   . LYS B 535  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  532  LYS A C   
4281  O O   . LYS B 535  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  532  LYS A O   
4282  C CB  . LYS B 535  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  532  LYS A CB  
4283  C CG  . LYS B 535  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  532  LYS A CG  
4284  C CD  . LYS B 535  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  532  LYS A CD  
4285  C CE  . LYS B 535  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  532  LYS A CE  
4286  N NZ  . LYS B 535  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  532  LYS A NZ  
4287  N N   . LEU B 536  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  533  LEU A N   
4288  C CA  . LEU B 536  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  533  LEU A CA  
4289  C C   . LEU B 536  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  533  LEU A C   
4290  O O   . LEU B 536  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  533  LEU A O   
4291  C CB  . LEU B 536  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  533  LEU A CB  
4292  C CG  . LEU B 536  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  533  LEU A CG  
4293  C CD1 . LEU B 536  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  533  LEU A CD1 
4294  C CD2 . LEU B 536  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  533  LEU A CD2 
4295  N N   . ASN B 537  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  534  ASN A N   
4296  C CA  . ASN B 537  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  534  ASN A CA  
4297  C C   . ASN B 537  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  534  ASN A C   
4298  O O   . ASN B 537  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  534  ASN A O   
4299  C CB  . ASN B 537  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  534  ASN A CB  
4300  C CG  . ASN B 537  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  534  ASN A CG  
4301  O OD1 . ASN B 537  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  534  ASN A OD1 
4302  N ND2 . ASN B 537  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  534  ASN A ND2 
4303  N N   . PHE B 538  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  535  PHE A N   
4304  C CA  . PHE B 538  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  535  PHE A CA  
4305  C C   . PHE B 538  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  535  PHE A C   
4306  O O   . PHE B 538  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  535  PHE A O   
4307  C CB  . PHE B 538  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  535  PHE A CB  
4308  C CG  . PHE B 538  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  535  PHE A CG  
4309  C CD1 . PHE B 538  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  535  PHE A CD1 
4310  C CD2 . PHE B 538  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  535  PHE A CD2 
4311  C CE1 . PHE B 538  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  535  PHE A CE1 
4312  C CE2 . PHE B 538  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  535  PHE A CE2 
4313  C CZ  . PHE B 538  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  535  PHE A CZ  
4314  N N   . GLN B 539  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  536  GLN A N   
4315  C CA  . GLN B 539  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  536  GLN A CA  
4316  C C   . GLN B 539  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  536  GLN A C   
4317  O O   . GLN B 539  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  536  GLN A O   
4318  C CB  . GLN B 539  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  536  GLN A CB  
4319  C CG  . GLN B 539  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  536  GLN A CG  
4320  C CD  . GLN B 539  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  536  GLN A CD  
4321  O OE1 . GLN B 539  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  536  GLN A OE1 
4322  N NE2 . GLN B 539  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  536  GLN A NE2 
4323  N N   . MET B 540  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  537  MET A N   
4324  C CA  . MET B 540  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  537  MET A CA  
4325  C C   . MET B 540  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  537  MET A C   
4326  O O   . MET B 540  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  537  MET A O   
4327  C CB  . MET B 540  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  537  MET A CB  
4328  C CG  . MET B 540  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  537  MET A CG  
4329  S SD  . MET B 540  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  537  MET A SD  
4330  C CE  . MET B 540  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  537  MET A CE  
4331  N N   . PRO B 541  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  538  PRO A N   
4332  C CA  . PRO B 541  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  538  PRO A CA  
4333  C C   . PRO B 541  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  538  PRO A C   
4334  O O   . PRO B 541  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  538  PRO A O   
4335  C CB  . PRO B 541  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  538  PRO A CB  
4336  C CG  . PRO B 541  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  538  PRO A CG  
4337  C CD  . PRO B 541  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  538  PRO A CD  
4338  N N   . THR B 542  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  539  THR A N   
4339  C CA  . THR B 542  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  539  THR A CA  
4340  C C   . THR B 542  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  539  THR A C   
4341  O O   . THR B 542  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  539  THR A O   
4342  C CB  . THR B 542  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  539  THR A CB  
4343  O OG1 . THR B 542  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  539  THR A OG1 
4344  C CG2 . THR B 542  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  539  THR A CG2 
4345  N N   . LEU B 543  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  540  LEU A N   
4346  C CA  . LEU B 543  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  540  LEU A CA  
4347  C C   . LEU B 543  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  540  LEU A C   
4348  O O   . LEU B 543  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  540  LEU A O   
4349  C CB  . LEU B 543  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  540  LEU A CB  
4350  C CG  . LEU B 543  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  540  LEU A CG  
4351  C CD1 . LEU B 543  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  540  LEU A CD1 
4352  C CD2 . LEU B 543  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  540  LEU A CD2 
4353  N N   . ALA B 544  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  541  ALA A N   
4354  C CA  . ALA B 544  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  541  ALA A CA  
4355  C C   . ALA B 544  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  541  ALA A C   
4356  O O   . ALA B 544  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  541  ALA A O   
4357  C CB  . ALA B 544  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  541  ALA A CB  
4358  N N   . SER B 545  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  542  SER A N   
4359  C CA  . SER B 545  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  542  SER A CA  
4360  C C   . SER B 545  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  542  SER A C   
4361  O O   . SER B 545  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  542  SER A O   
4362  C CB  . SER B 545  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  542  SER A CB  
4363  O OG  . SER B 545  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  542  SER A OG  
4364  N N   . GLY B 546  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  543  GLY A N   
4365  C CA  . GLY B 546  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  543  GLY A CA  
4366  C C   . GLY B 546  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  543  GLY A C   
4367  O O   . GLY B 546  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  543  GLY A O   
4368  N N   . TRP B 547  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  544  TRP A N   
4369  C CA  . TRP B 547  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  544  TRP A CA  
4370  C C   . TRP B 547  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  544  TRP A C   
4371  O O   . TRP B 547  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  544  TRP A O   
4372  C CB  . TRP B 547  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  544  TRP A CB  
4373  C CG  . TRP B 547  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  544  TRP A CG  
4374  C CD1 . TRP B 547  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  544  TRP A CD1 
4375  C CD2 . TRP B 547  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  544  TRP A CD2 
4376  N NE1 . TRP B 547  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  544  TRP A NE1 
4377  C CE2 . TRP B 547  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  544  TRP A CE2 
4378  C CE3 . TRP B 547  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  544  TRP A CE3 
4379  C CZ2 . TRP B 547  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  544  TRP A CZ2 
4380  C CZ3 . TRP B 547  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  544  TRP A CZ3 
4381  C CH2 . TRP B 547  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  544  TRP A CH2 
4382  N N   . ASP B 548  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  545  ASP A N   
4383  C CA  . ASP B 548  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  545  ASP A CA  
4384  C C   . ASP B 548  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  545  ASP A C   
4385  O O   . ASP B 548  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  545  ASP A O   
4386  C CB  . ASP B 548  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  545  ASP A CB  
4387  C CG  . ASP B 548  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  545  ASP A CG  
4388  O OD1 . ASP B 548  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  545  ASP A OD1 
4389  O OD2 . ASP B 548  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  545  ASP A OD2 
4390  N N   . VAL B 549  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  546  VAL A N   
4391  C CA  . VAL B 549  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  546  VAL A CA  
4392  C C   . VAL B 549  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  546  VAL A C   
4393  O O   . VAL B 549  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  546  VAL A O   
4394  C CB  . VAL B 549  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  546  VAL A CB  
4395  C CG1 . VAL B 549  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  546  VAL A CG1 
4396  C CG2 . VAL B 549  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  546  VAL A CG2 
4397  N N   . ASN B 550  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  547  ASN A N   
4398  C CA  . ASN B 550  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  547  ASN A CA  
4399  C C   . ASN B 550  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  547  ASN A C   
4400  O O   . ASN B 550  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  547  ASN A O   
4401  C CB  . ASN B 550  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  547  ASN A CB  
4402  C CG  . ASN B 550  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  547  ASN A CG  
4403  O OD1 . ASN B 550  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  547  ASN A OD1 
4404  N ND2 . ASN B 550  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  547  ASN A ND2 
4405  N N   . LYS B 551  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  548  LYS A N   
4406  C CA  . LYS B 551  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  548  LYS A CA  
4407  C C   . LYS B 551  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  548  LYS A C   
4408  O O   . LYS B 551  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  548  LYS A O   
4409  C CB  . LYS B 551  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  548  LYS A CB  
4410  C CG  . LYS B 551  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  548  LYS A CG  
4411  C CD  . LYS B 551  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  548  LYS A CD  
4412  C CE  . LYS B 551  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  548  LYS A CE  
4413  N NZ  . LYS B 551  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  548  LYS A NZ  
4414  N N   . GLU B 552  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  549  GLU A N   
4415  C CA  . GLU B 552  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  549  GLU A CA  
4416  C C   . GLU B 552  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  549  GLU A C   
4417  O O   . GLU B 552  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  549  GLU A O   
4418  C CB  . GLU B 552  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  549  GLU A CB  
4419  C CG  . GLU B 552  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  549  GLU A CG  
4420  C CD  . GLU B 552  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  549  GLU A CD  
4421  O OE1 . GLU B 552  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  549  GLU A OE1 
4422  O OE2 . GLU B 552  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  549  GLU A OE2 
4423  N N   . LYS B 553  ? 0.6151 0.6151 0.6151 0.0000  0.0000  0.0000  550  LYS A N   
4424  C CA  . LYS B 553  ? 0.6151 0.6151 0.6151 0.0000  0.0000  0.0000  550  LYS A CA  
4425  C C   . LYS B 553  ? 0.6151 0.6151 0.6151 0.0000  0.0000  0.0000  550  LYS A C   
4426  O O   . LYS B 553  ? 0.6151 0.6151 0.6151 0.0000  0.0000  0.0000  550  LYS A O   
4427  C CB  . LYS B 553  ? 0.6151 0.6151 0.6151 0.0000  0.0000  0.0000  550  LYS A CB  
4428  C CG  . LYS B 553  ? 0.6151 0.6151 0.6151 0.0000  0.0000  0.0000  550  LYS A CG  
4429  C CD  . LYS B 553  ? 0.6151 0.6151 0.6151 0.0000  0.0000  0.0000  550  LYS A CD  
4430  C CE  . LYS B 553  ? 0.6151 0.6151 0.6151 0.0000  0.0000  0.0000  550  LYS A CE  
4431  N NZ  . LYS B 553  ? 0.6151 0.6151 0.6151 0.0000  0.0000  0.0000  550  LYS A NZ  
4432  N N   . CYS B 554  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  551  CYS A N   
4433  C CA  . CYS B 554  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  551  CYS A CA  
4434  C C   . CYS B 554  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  551  CYS A C   
4435  O O   . CYS B 554  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  551  CYS A O   
4438  N N   . ASN B 555  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  552  ASN A N   
4439  C CA  . ASN B 555  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  552  ASN A CA  
4440  C C   . ASN B 555  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  552  ASN A C   
4441  O O   . ASN B 555  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  552  ASN A O   
4442  C CB  . ASN B 555  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  552  ASN A CB  
4443  C CG  . ASN B 555  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  552  ASN A CG  
4444  O OD1 . ASN B 555  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  552  ASN A OD1 
4445  N ND2 . ASN B 555  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  552  ASN A ND2 
4446  N N   . GLY B 556  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  553  GLY A N   
4447  C CA  . GLY B 556  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  553  GLY A CA  
4448  C C   . GLY B 556  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  553  GLY A C   
4449  O O   . GLY B 556  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  553  GLY A O   
4450  N N   . ALA B 557  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  554  ALA A N   
4451  C CA  . ALA B 557  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  554  ALA A CA  
4452  C C   . ALA B 557  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  554  ALA A C   
4453  O O   . ALA B 557  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  554  ALA A O   
4454  C CB  . ALA B 557  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  554  ALA A CB  
4455  N N   . ILE B 558  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  555  ILE A N   
4456  C CA  . ILE B 558  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  555  ILE A CA  
4457  C C   . ILE B 558  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  555  ILE A C   
4458  O O   . ILE B 558  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  555  ILE A O   
4459  C CB  . ILE B 558  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  555  ILE A CB  
4460  C CG1 . ILE B 558  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  555  ILE A CG1 
4461  C CG2 . ILE B 558  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  555  ILE A CG2 
4462  C CD1 . ILE B 558  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  555  ILE A CD1 
4463  N N   . LEU B 559  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  556  LEU A N   
4464  C CA  . LEU B 559  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  556  LEU A CA  
4465  C C   . LEU B 559  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  556  LEU A C   
4466  O O   . LEU B 559  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  556  LEU A O   
4467  C CB  . LEU B 559  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  556  LEU A CB  
4468  C CG  . LEU B 559  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  556  LEU A CG  
4469  C CD1 . LEU B 559  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  556  LEU A CD1 
4470  C CD2 . LEU B 559  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  556  LEU A CD2 
4471  N N   . PHE B 560  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  557  PHE A N   
4472  C CA  . PHE B 560  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  557  PHE A CA  
4473  C C   . PHE B 560  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  557  PHE A C   
4474  O O   . PHE B 560  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  557  PHE A O   
4475  C CB  . PHE B 560  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  557  PHE A CB  
4476  C CG  . PHE B 560  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  557  PHE A CG  
4477  C CD1 . PHE B 560  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  557  PHE A CD1 
4478  C CD2 . PHE B 560  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  557  PHE A CD2 
4479  C CE1 . PHE B 560  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  557  PHE A CE1 
4480  C CE2 . PHE B 560  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  557  PHE A CE2 
4481  C CZ  . PHE B 560  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  557  PHE A CZ  
4482  N N   . VAL B 561  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  558  VAL A N   
4483  C CA  . VAL B 561  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  558  VAL A CA  
4484  C C   . VAL B 561  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  558  VAL A C   
4485  O O   . VAL B 561  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  558  VAL A O   
4486  C CB  . VAL B 561  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  558  VAL A CB  
4487  C CG1 . VAL B 561  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  558  VAL A CG1 
4488  C CG2 . VAL B 561  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  558  VAL A CG2 
4489  N N   . LYS B 562  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  559  LYS A N   
4490  C CA  . LYS B 562  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  559  LYS A CA  
4491  C C   . LYS B 562  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  559  LYS A C   
4492  O O   . LYS B 562  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  559  LYS A O   
4493  C CB  . LYS B 562  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  559  LYS A CB  
4494  C CG  . LYS B 562  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  559  LYS A CG  
4495  C CD  . LYS B 562  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  559  LYS A CD  
4496  C CE  . LYS B 562  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  559  LYS A CE  
4497  N NZ  . LYS B 562  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  559  LYS A NZ  
4498  N N   . ASN B 563  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  560  ASN A N   
4499  C CA  . ASN B 563  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  560  ASN A CA  
4500  C C   . ASN B 563  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  560  ASN A C   
4501  O O   . ASN B 563  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  560  ASN A O   
4502  C CB  . ASN B 563  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  560  ASN A CB  
4503  C CG  . ASN B 563  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  560  ASN A CG  
4504  O OD1 . ASN B 563  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  560  ASN A OD1 
4505  N ND2 . ASN B 563  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  560  ASN A ND2 
4506  N N   . GLY B 564  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  561  GLY A N   
4507  C CA  . GLY B 564  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  561  GLY A CA  
4508  C C   . GLY B 564  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  561  GLY A C   
4509  O O   . GLY B 564  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  561  GLY A O   
4510  N N   . LEU B 565  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  562  LEU A N   
4511  C CA  . LEU B 565  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  562  LEU A CA  
4512  C C   . LEU B 565  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  562  LEU A C   
4513  O O   . LEU B 565  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  562  LEU A O   
4514  C CB  . LEU B 565  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  562  LEU A CB  
4515  C CG  . LEU B 565  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  562  LEU A CG  
4516  C CD1 . LEU B 565  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  562  LEU A CD1 
4517  C CD2 . LEU B 565  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  562  LEU A CD2 
4518  N N   . TYR B 566  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  563  TYR A N   
4519  C CA  . TYR B 566  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  563  TYR A CA  
4520  C C   . TYR B 566  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  563  TYR A C   
4521  O O   . TYR B 566  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  563  TYR A O   
4522  C CB  . TYR B 566  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  563  TYR A CB  
4523  C CG  . TYR B 566  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  563  TYR A CG  
4524  C CD1 . TYR B 566  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  563  TYR A CD1 
4525  C CD2 . TYR B 566  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  563  TYR A CD2 
4526  C CE1 . TYR B 566  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  563  TYR A CE1 
4527  C CE2 . TYR B 566  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  563  TYR A CE2 
4528  C CZ  . TYR B 566  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  563  TYR A CZ  
4529  O OH  . TYR B 566  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  563  TYR A OH  
4530  N N   . TYR B 567  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  564  TYR A N   
4531  C CA  . TYR B 567  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  564  TYR A CA  
4532  C C   . TYR B 567  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  564  TYR A C   
4533  O O   . TYR B 567  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  564  TYR A O   
4534  C CB  . TYR B 567  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  564  TYR A CB  
4535  C CG  . TYR B 567  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  564  TYR A CG  
4536  C CD1 . TYR B 567  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  564  TYR A CD1 
4537  C CD2 . TYR B 567  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  564  TYR A CD2 
4538  C CE1 . TYR B 567  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  564  TYR A CE1 
4539  C CE2 . TYR B 567  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  564  TYR A CE2 
4540  C CZ  . TYR B 567  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  564  TYR A CZ  
4541  O OH  . TYR B 567  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  564  TYR A OH  
4542  N N   . LEU B 568  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  565  LEU A N   
4543  C CA  . LEU B 568  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  565  LEU A CA  
4544  C C   . LEU B 568  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  565  LEU A C   
4545  O O   . LEU B 568  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  565  LEU A O   
4546  C CB  . LEU B 568  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  565  LEU A CB  
4547  C CG  . LEU B 568  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  565  LEU A CG  
4548  C CD1 . LEU B 568  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  565  LEU A CD1 
4549  C CD2 . LEU B 568  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  565  LEU A CD2 
4550  N N   . GLY B 569  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  566  GLY A N   
4551  C CA  . GLY B 569  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  566  GLY A CA  
4552  C C   . GLY B 569  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  566  GLY A C   
4553  O O   . GLY B 569  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  566  GLY A O   
4554  N N   . ILE B 570  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  567  ILE A N   
4555  C CA  . ILE B 570  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  567  ILE A CA  
4556  C C   . ILE B 570  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  567  ILE A C   
4557  O O   . ILE B 570  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  567  ILE A O   
4558  C CB  . ILE B 570  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  567  ILE A CB  
4559  C CG1 . ILE B 570  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  567  ILE A CG1 
4560  C CG2 . ILE B 570  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  567  ILE A CG2 
4561  C CD1 . ILE B 570  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  567  ILE A CD1 
4562  N N   . MET B 571  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  568  MET A N   
4563  C CA  . MET B 571  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  568  MET A CA  
4564  C C   . MET B 571  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  568  MET A C   
4565  O O   . MET B 571  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  568  MET A O   
4566  C CB  . MET B 571  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  568  MET A CB  
4567  C CG  . MET B 571  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  568  MET A CG  
4568  S SD  . MET B 571  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  568  MET A SD  
4569  C CE  . MET B 571  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  568  MET A CE  
4570  N N   . PRO B 572  ? 0.6185 0.6185 0.6185 0.0000  0.0000  0.0000  569  PRO A N   
4571  C CA  . PRO B 572  ? 0.6185 0.6185 0.6185 0.0000  0.0000  0.0000  569  PRO A CA  
4572  C C   . PRO B 572  ? 0.6185 0.6185 0.6185 0.0000  0.0000  0.0000  569  PRO A C   
4573  O O   . PRO B 572  ? 0.6185 0.6185 0.6185 0.0000  0.0000  0.0000  569  PRO A O   
4574  C CB  . PRO B 572  ? 0.6185 0.6185 0.6185 0.0000  0.0000  0.0000  569  PRO A CB  
4575  C CG  . PRO B 572  ? 0.6185 0.6185 0.6185 0.0000  0.0000  0.0000  569  PRO A CG  
4576  C CD  . PRO B 572  ? 0.6185 0.6185 0.6185 0.0000  0.0000  0.0000  569  PRO A CD  
4577  N N   . LYS B 573  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  570  LYS A N   
4578  C CA  . LYS B 573  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  570  LYS A CA  
4579  C C   . LYS B 573  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  570  LYS A C   
4580  O O   . LYS B 573  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  570  LYS A O   
4581  C CB  . LYS B 573  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  570  LYS A CB  
4582  C CG  . LYS B 573  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  570  LYS A CG  
4583  C CD  . LYS B 573  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  570  LYS A CD  
4584  C CE  . LYS B 573  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  570  LYS A CE  
4585  N NZ  . LYS B 573  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  570  LYS A NZ  
4586  N N   . ALA B 580  ? 1.0273 1.0273 1.0273 0.0000  0.0000  0.0000  577  ALA A N   
4587  C CA  . ALA B 580  ? 1.0273 1.0273 1.0273 0.0000  0.0000  0.0000  577  ALA A CA  
4588  C C   . ALA B 580  ? 1.0273 1.0273 1.0273 0.0000  0.0000  0.0000  577  ALA A C   
4589  O O   . ALA B 580  ? 1.0273 1.0273 1.0273 0.0000  0.0000  0.0000  577  ALA A O   
4590  C CB  . ALA B 580  ? 1.0273 1.0273 1.0273 0.0000  0.0000  0.0000  577  ALA A CB  
4591  N N   . LEU B 581  ? 0.7356 0.7356 0.7356 0.0000  0.0000  0.0000  578  LEU A N   
4592  C CA  . LEU B 581  ? 0.7356 0.7356 0.7356 0.0000  0.0000  0.0000  578  LEU A CA  
4593  C C   . LEU B 581  ? 0.7356 0.7356 0.7356 0.0000  0.0000  0.0000  578  LEU A C   
4594  O O   . LEU B 581  ? 0.7356 0.7356 0.7356 0.0000  0.0000  0.0000  578  LEU A O   
4599  N N   . SER B 582  ? 0.7098 0.7098 0.7098 0.0000  0.0000  0.0000  579  SER A N   
4600  C CA  . SER B 582  ? 0.7098 0.7098 0.7098 0.0000  0.0000  0.0000  579  SER A CA  
4601  C C   . SER B 582  ? 0.7098 0.7098 0.7098 0.0000  0.0000  0.0000  579  SER A C   
4602  O O   . SER B 582  ? 0.7098 0.7098 0.7098 0.0000  0.0000  0.0000  579  SER A O   
4603  C CB  . SER B 582  ? 0.7098 0.7098 0.7098 0.0000  0.0000  0.0000  579  SER A CB  
4604  O OG  . SER B 582  ? 0.7098 0.7098 0.7098 0.0000  0.0000  0.0000  579  SER A OG  
4605  N N   . PHE B 583  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  580  PHE A N   
4606  C CA  . PHE B 583  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  580  PHE A CA  
4607  C C   . PHE B 583  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  580  PHE A C   
4608  O O   . PHE B 583  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  580  PHE A O   
4609  C CB  . PHE B 583  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  580  PHE A CB  
4610  C CG  . PHE B 583  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  580  PHE A CG  
4611  C CD1 . PHE B 583  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  580  PHE A CD1 
4612  C CD2 . PHE B 583  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  580  PHE A CD2 
4613  C CE1 . PHE B 583  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  580  PHE A CE1 
4614  C CE2 . PHE B 583  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  580  PHE A CE2 
4615  C CZ  . PHE B 583  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  580  PHE A CZ  
4616  N N   . GLU B 584  ? 0.6321 0.6321 0.6321 0.0000  0.0000  0.0000  581  GLU A N   
4617  C CA  . GLU B 584  ? 0.6321 0.6321 0.6321 0.0000  0.0000  0.0000  581  GLU A CA  
4618  C C   . GLU B 584  ? 0.6321 0.6321 0.6321 0.0000  0.0000  0.0000  581  GLU A C   
4619  O O   . GLU B 584  ? 0.6321 0.6321 0.6321 0.0000  0.0000  0.0000  581  GLU A O   
4625  N N   . PRO B 585  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  582  PRO A N   
4626  C CA  . PRO B 585  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  582  PRO A CA  
4627  C C   . PRO B 585  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  582  PRO A C   
4628  O O   . PRO B 585  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  582  PRO A O   
4629  C CB  . PRO B 585  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  582  PRO A CB  
4630  C CG  . PRO B 585  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  582  PRO A CG  
4631  C CD  . PRO B 585  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  582  PRO A CD  
4632  N N   . THR B 586  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  583  THR A N   
4633  C CA  . THR B 586  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  583  THR A CA  
4634  C C   . THR B 586  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  583  THR A C   
4635  O O   . THR B 586  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  583  THR A O   
4636  C CB  . THR B 586  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  583  THR A CB  
4637  O OG1 . THR B 586  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  583  THR A OG1 
4638  C CG2 . THR B 586  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  583  THR A CG2 
4639  N N   . GLU B 587  ? 0.6376 0.6376 0.6376 0.0000  0.0000  0.0000  584  GLU A N   
4640  C CA  . GLU B 587  ? 0.6376 0.6376 0.6376 0.0000  0.0000  0.0000  584  GLU A CA  
4641  C C   . GLU B 587  ? 0.6376 0.6376 0.6376 0.0000  0.0000  0.0000  584  GLU A C   
4642  O O   . GLU B 587  ? 0.6376 0.6376 0.6376 0.0000  0.0000  0.0000  584  GLU A O   
4643  C CB  . GLU B 587  ? 0.6376 0.6376 0.6376 0.0000  0.0000  0.0000  584  GLU A CB  
4644  C CG  . GLU B 587  ? 0.6376 0.6376 0.6376 0.0000  0.0000  0.0000  584  GLU A CG  
4645  C CD  . GLU B 587  ? 0.6376 0.6376 0.6376 0.0000  0.0000  0.0000  584  GLU A CD  
4646  O OE1 . GLU B 587  ? 0.6376 0.6376 0.6376 0.0000  0.0000  0.0000  584  GLU A OE1 
4647  O OE2 . GLU B 587  ? 0.6376 0.6376 0.6376 0.0000  0.0000  0.0000  584  GLU A OE2 
4648  N N   . LYS B 588  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  585  LYS A N   
4649  C CA  . LYS B 588  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  585  LYS A CA  
4650  C C   . LYS B 588  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  585  LYS A C   
4651  O O   . LYS B 588  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  585  LYS A O   
4657  N N   . THR B 589  ? 0.6546 0.6546 0.6546 0.0000  0.0000  0.0000  586  THR A N   
4658  C CA  . THR B 589  ? 0.6546 0.6546 0.6546 0.0000  0.0000  0.0000  586  THR A CA  
4659  C C   . THR B 589  ? 0.6546 0.6546 0.6546 0.0000  0.0000  0.0000  586  THR A C   
4660  O O   . THR B 589  ? 0.6546 0.6546 0.6546 0.0000  0.0000  0.0000  586  THR A O   
4661  C CB  . THR B 589  ? 0.6546 0.6546 0.6546 0.0000  0.0000  0.0000  586  THR A CB  
4662  O OG1 . THR B 589  ? 0.6546 0.6546 0.6546 0.0000  0.0000  0.0000  586  THR A OG1 
4663  C CG2 . THR B 589  ? 0.6546 0.6546 0.6546 0.0000  0.0000  0.0000  586  THR A CG2 
4664  N N   . SER B 590  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  587  SER A N   
4665  C CA  . SER B 590  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  587  SER A CA  
4666  C C   . SER B 590  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  587  SER A C   
4667  O O   . SER B 590  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  587  SER A O   
4668  C CB  . SER B 590  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  587  SER A CB  
4669  O OG  . SER B 590  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  587  SER A OG  
4670  N N   . GLU B 591  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  588  GLU A N   
4671  C CA  . GLU B 591  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  588  GLU A CA  
4672  C C   . GLU B 591  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  588  GLU A C   
4673  O O   . GLU B 591  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  588  GLU A O   
4674  C CB  . GLU B 591  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  588  GLU A CB  
4675  C CG  . GLU B 591  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  588  GLU A CG  
4676  C CD  . GLU B 591  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  588  GLU A CD  
4677  O OE1 . GLU B 591  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  588  GLU A OE1 
4678  O OE2 . GLU B 591  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  588  GLU A OE2 
4679  N N   . GLY B 592  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  589  GLY A N   
4680  C CA  . GLY B 592  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  589  GLY A CA  
4681  C C   . GLY B 592  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  589  GLY A C   
4682  O O   . GLY B 592  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  589  GLY A O   
4683  N N   . PHE B 593  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  590  PHE A N   
4684  C CA  . PHE B 593  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  590  PHE A CA  
4685  C C   . PHE B 593  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  590  PHE A C   
4686  O O   . PHE B 593  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  590  PHE A O   
4687  C CB  . PHE B 593  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  590  PHE A CB  
4688  C CG  . PHE B 593  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  590  PHE A CG  
4689  C CD1 . PHE B 593  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  590  PHE A CD1 
4690  C CD2 . PHE B 593  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  590  PHE A CD2 
4691  C CE1 . PHE B 593  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  590  PHE A CE1 
4692  C CE2 . PHE B 593  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  590  PHE A CE2 
4693  C CZ  . PHE B 593  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  590  PHE A CZ  
4694  N N   . ASP B 594  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  591  ASP A N   
4695  C CA  . ASP B 594  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  591  ASP A CA  
4696  C C   . ASP B 594  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  591  ASP A C   
4697  O O   . ASP B 594  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  591  ASP A O   
4698  C CB  . ASP B 594  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  591  ASP A CB  
4699  C CG  . ASP B 594  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  591  ASP A CG  
4700  O OD1 . ASP B 594  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  591  ASP A OD1 
4701  O OD2 . ASP B 594  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  591  ASP A OD2 
4702  N N   . LYS B 595  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  592  LYS A N   
4703  C CA  . LYS B 595  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  592  LYS A CA  
4704  C C   . LYS B 595  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  592  LYS A C   
4705  O O   . LYS B 595  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  592  LYS A O   
4706  C CB  . LYS B 595  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  592  LYS A CB  
4707  C CG  . LYS B 595  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  592  LYS A CG  
4708  C CD  . LYS B 595  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  592  LYS A CD  
4709  C CE  . LYS B 595  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  592  LYS A CE  
4710  N NZ  . LYS B 595  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  592  LYS A NZ  
4711  N N   . MET B 596  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  593  MET A N   
4712  C CA  . MET B 596  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  593  MET A CA  
4713  C C   . MET B 596  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  593  MET A C   
4714  O O   . MET B 596  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  593  MET A O   
4715  C CB  . MET B 596  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  593  MET A CB  
4716  C CG  . MET B 596  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  593  MET A CG  
4717  S SD  . MET B 596  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  593  MET A SD  
4718  C CE  . MET B 596  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  593  MET A CE  
4719  N N   . TYR B 597  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  594  TYR A N   
4720  C CA  . TYR B 597  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  594  TYR A CA  
4721  C C   . TYR B 597  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  594  TYR A C   
4722  O O   . TYR B 597  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  594  TYR A O   
4723  C CB  . TYR B 597  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  594  TYR A CB  
4724  C CG  . TYR B 597  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  594  TYR A CG  
4725  C CD1 . TYR B 597  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  594  TYR A CD1 
4726  C CD2 . TYR B 597  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  594  TYR A CD2 
4727  C CE1 . TYR B 597  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  594  TYR A CE1 
4728  C CE2 . TYR B 597  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  594  TYR A CE2 
4729  C CZ  . TYR B 597  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  594  TYR A CZ  
4730  O OH  . TYR B 597  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  594  TYR A OH  
4731  N N   . TYR B 598  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  595  TYR A N   
4732  C CA  . TYR B 598  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  595  TYR A CA  
4733  C C   . TYR B 598  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  595  TYR A C   
4734  O O   . TYR B 598  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  595  TYR A O   
4735  C CB  . TYR B 598  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  595  TYR A CB  
4736  C CG  . TYR B 598  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  595  TYR A CG  
4737  C CD1 . TYR B 598  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  595  TYR A CD1 
4738  C CD2 . TYR B 598  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  595  TYR A CD2 
4739  C CE1 . TYR B 598  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  595  TYR A CE1 
4740  C CE2 . TYR B 598  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  595  TYR A CE2 
4741  C CZ  . TYR B 598  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  595  TYR A CZ  
4742  O OH  . TYR B 598  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  595  TYR A OH  
4743  N N   . ASP B 599  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  596  ASP A N   
4744  C CA  . ASP B 599  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  596  ASP A CA  
4745  C C   . ASP B 599  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  596  ASP A C   
4746  O O   . ASP B 599  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  596  ASP A O   
4747  C CB  . ASP B 599  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  596  ASP A CB  
4748  C CG  . ASP B 599  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  596  ASP A CG  
4749  O OD1 . ASP B 599  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  596  ASP A OD1 
4750  O OD2 . ASP B 599  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  596  ASP A OD2 
4751  N N   . TYR B 600  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  597  TYR A N   
4752  C CA  . TYR B 600  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  597  TYR A CA  
4753  C C   . TYR B 600  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  597  TYR A C   
4754  O O   . TYR B 600  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  597  TYR A O   
4755  C CB  . TYR B 600  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  597  TYR A CB  
4756  C CG  . TYR B 600  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  597  TYR A CG  
4757  C CD1 . TYR B 600  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  597  TYR A CD1 
4758  C CD2 . TYR B 600  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  597  TYR A CD2 
4759  C CE1 . TYR B 600  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  597  TYR A CE1 
4760  C CE2 . TYR B 600  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  597  TYR A CE2 
4761  C CZ  . TYR B 600  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  597  TYR A CZ  
4762  O OH  . TYR B 600  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  597  TYR A OH  
4763  N N   . PHE B 601  ? 0.7452 0.7452 0.7452 0.0000  0.0000  0.0000  598  PHE A N   
4764  C CA  . PHE B 601  ? 0.7452 0.7452 0.7452 0.0000  0.0000  0.0000  598  PHE A CA  
4765  C C   . PHE B 601  ? 0.7452 0.7452 0.7452 0.0000  0.0000  0.0000  598  PHE A C   
4766  O O   . PHE B 601  ? 0.7452 0.7452 0.7452 0.0000  0.0000  0.0000  598  PHE A O   
4767  C CB  . PHE B 601  ? 0.7452 0.7452 0.7452 0.0000  0.0000  0.0000  598  PHE A CB  
4768  C CG  . PHE B 601  ? 0.7452 0.7452 0.7452 0.0000  0.0000  0.0000  598  PHE A CG  
4769  C CD1 . PHE B 601  ? 0.7452 0.7452 0.7452 0.0000  0.0000  0.0000  598  PHE A CD1 
4770  C CD2 . PHE B 601  ? 0.7452 0.7452 0.7452 0.0000  0.0000  0.0000  598  PHE A CD2 
4771  C CE1 . PHE B 601  ? 0.7452 0.7452 0.7452 0.0000  0.0000  0.0000  598  PHE A CE1 
4772  C CE2 . PHE B 601  ? 0.7452 0.7452 0.7452 0.0000  0.0000  0.0000  598  PHE A CE2 
4773  C CZ  . PHE B 601  ? 0.7452 0.7452 0.7452 0.0000  0.0000  0.0000  598  PHE A CZ  
4774  N N   . PRO B 602  ? 0.8152 0.8152 0.8152 0.0000  0.0000  0.0000  599  PRO A N   
4775  C CA  . PRO B 602  ? 0.8152 0.8152 0.8152 0.0000  0.0000  0.0000  599  PRO A CA  
4776  C C   . PRO B 602  ? 0.8152 0.8152 0.8152 0.0000  0.0000  0.0000  599  PRO A C   
4777  O O   . PRO B 602  ? 0.8152 0.8152 0.8152 0.0000  0.0000  0.0000  599  PRO A O   
4778  C CB  . PRO B 602  ? 0.8152 0.8152 0.8152 0.0000  0.0000  0.0000  599  PRO A CB  
4779  C CG  . PRO B 602  ? 0.8152 0.8152 0.8152 0.0000  0.0000  0.0000  599  PRO A CG  
4780  C CD  . PRO B 602  ? 0.8152 0.8152 0.8152 0.0000  0.0000  0.0000  599  PRO A CD  
4781  N N   . ASP B 603  ? 0.8653 0.8653 0.8653 0.0000  0.0000  0.0000  600  ASP A N   
4782  C CA  . ASP B 603  ? 0.8653 0.8653 0.8653 0.0000  0.0000  0.0000  600  ASP A CA  
4783  C C   . ASP B 603  ? 0.8653 0.8653 0.8653 0.0000  0.0000  0.0000  600  ASP A C   
4784  O O   . ASP B 603  ? 0.8653 0.8653 0.8653 0.0000  0.0000  0.0000  600  ASP A O   
4785  C CB  . ASP B 603  ? 0.8653 0.8653 0.8653 0.0000  0.0000  0.0000  600  ASP A CB  
4786  C CG  . ASP B 603  ? 0.8653 0.8653 0.8653 0.0000  0.0000  0.0000  600  ASP A CG  
4787  O OD1 . ASP B 603  ? 0.8653 0.8653 0.8653 0.0000  0.0000  0.0000  600  ASP A OD1 
4788  O OD2 . ASP B 603  ? 0.8653 0.8653 0.8653 0.0000  0.0000  0.0000  600  ASP A OD2 
4789  N N   . ALA B 604  ? 0.8717 0.8717 0.8717 0.0000  0.0000  0.0000  601  ALA A N   
4790  C CA  . ALA B 604  ? 0.8717 0.8717 0.8717 0.0000  0.0000  0.0000  601  ALA A CA  
4791  C C   . ALA B 604  ? 0.8717 0.8717 0.8717 0.0000  0.0000  0.0000  601  ALA A C   
4792  O O   . ALA B 604  ? 0.8717 0.8717 0.8717 0.0000  0.0000  0.0000  601  ALA A O   
4793  C CB  . ALA B 604  ? 0.8717 0.8717 0.8717 0.0000  0.0000  0.0000  601  ALA A CB  
4794  N N   . ALA B 605  ? 0.9166 0.9166 0.9166 0.0000  0.0000  0.0000  602  ALA A N   
4795  C CA  . ALA B 605  ? 0.9166 0.9166 0.9166 0.0000  0.0000  0.0000  602  ALA A CA  
4796  C C   . ALA B 605  ? 0.9166 0.9166 0.9166 0.0000  0.0000  0.0000  602  ALA A C   
4797  O O   . ALA B 605  ? 0.9166 0.9166 0.9166 0.0000  0.0000  0.0000  602  ALA A O   
4798  C CB  . ALA B 605  ? 0.9166 0.9166 0.9166 0.0000  0.0000  0.0000  602  ALA A CB  
4799  N N   . LYS B 606  ? 0.9176 0.9176 0.9176 0.0000  0.0000  0.0000  603  LYS A N   
4800  C CA  . LYS B 606  ? 0.9176 0.9176 0.9176 0.0000  0.0000  0.0000  603  LYS A CA  
4801  C C   . LYS B 606  ? 0.9176 0.9176 0.9176 0.0000  0.0000  0.0000  603  LYS A C   
4802  O O   . LYS B 606  ? 0.9176 0.9176 0.9176 0.0000  0.0000  0.0000  603  LYS A O   
4803  C CB  . LYS B 606  ? 0.9176 0.9176 0.9176 0.0000  0.0000  0.0000  603  LYS A CB  
4804  C CG  . LYS B 606  ? 0.9176 0.9176 0.9176 0.0000  0.0000  0.0000  603  LYS A CG  
4805  C CD  . LYS B 606  ? 0.9176 0.9176 0.9176 0.0000  0.0000  0.0000  603  LYS A CD  
4806  C CE  . LYS B 606  ? 0.9176 0.9176 0.9176 0.0000  0.0000  0.0000  603  LYS A CE  
4807  N NZ  . LYS B 606  ? 0.9176 0.9176 0.9176 0.0000  0.0000  0.0000  603  LYS A NZ  
4808  N N   . MET B 607  ? 0.9121 0.9121 0.9121 0.0000  0.0000  0.0000  604  MET A N   
4809  C CA  . MET B 607  ? 0.9121 0.9121 0.9121 0.0000  0.0000  0.0000  604  MET A CA  
4810  C C   . MET B 607  ? 0.9121 0.9121 0.9121 0.0000  0.0000  0.0000  604  MET A C   
4811  O O   . MET B 607  ? 0.9121 0.9121 0.9121 0.0000  0.0000  0.0000  604  MET A O   
4812  C CB  . MET B 607  ? 0.9121 0.9121 0.9121 0.0000  0.0000  0.0000  604  MET A CB  
4813  C CG  . MET B 607  ? 0.9121 0.9121 0.9121 0.0000  0.0000  0.0000  604  MET A CG  
4814  S SD  . MET B 607  ? 0.9121 0.9121 0.9121 0.0000  0.0000  0.0000  604  MET A SD  
4815  C CE  . MET B 607  ? 0.9121 0.9121 0.9121 0.0000  0.0000  0.0000  604  MET A CE  
4816  N N   . ILE B 608  ? 0.9116 0.9116 0.9116 0.0000  0.0000  0.0000  605  ILE A N   
4817  C CA  . ILE B 608  ? 0.9116 0.9116 0.9116 0.0000  0.0000  0.0000  605  ILE A CA  
4818  C C   . ILE B 608  ? 0.9116 0.9116 0.9116 0.0000  0.0000  0.0000  605  ILE A C   
4819  O O   . ILE B 608  ? 0.9116 0.9116 0.9116 0.0000  0.0000  0.0000  605  ILE A O   
4820  C CB  . ILE B 608  ? 0.9116 0.9116 0.9116 0.0000  0.0000  0.0000  605  ILE A CB  
4821  C CG1 . ILE B 608  ? 0.9116 0.9116 0.9116 0.0000  0.0000  0.0000  605  ILE A CG1 
4822  C CG2 . ILE B 608  ? 0.9116 0.9116 0.9116 0.0000  0.0000  0.0000  605  ILE A CG2 
4823  C CD1 . ILE B 608  ? 0.9116 0.9116 0.9116 0.0000  0.0000  0.0000  605  ILE A CD1 
4824  N N   . PRO B 609  ? 0.9450 0.9450 0.9450 0.0000  0.0000  0.0000  606  PRO A N   
4825  C CA  . PRO B 609  ? 0.9450 0.9450 0.9450 0.0000  0.0000  0.0000  606  PRO A CA  
4826  C C   . PRO B 609  ? 0.9450 0.9450 0.9450 0.0000  0.0000  0.0000  606  PRO A C   
4827  O O   . PRO B 609  ? 0.9450 0.9450 0.9450 0.0000  0.0000  0.0000  606  PRO A O   
4828  C CB  . PRO B 609  ? 0.9450 0.9450 0.9450 0.0000  0.0000  0.0000  606  PRO A CB  
4829  C CG  . PRO B 609  ? 0.9450 0.9450 0.9450 0.0000  0.0000  0.0000  606  PRO A CG  
4830  C CD  . PRO B 609  ? 0.9450 0.9450 0.9450 0.0000  0.0000  0.0000  606  PRO A CD  
4831  N N   . LYS B 610  ? 0.9006 0.9006 0.9006 0.0000  0.0000  0.0000  607  LYS A N   
4832  C CA  . LYS B 610  ? 0.9006 0.9006 0.9006 0.0000  0.0000  0.0000  607  LYS A CA  
4833  C C   . LYS B 610  ? 0.9006 0.9006 0.9006 0.0000  0.0000  0.0000  607  LYS A C   
4834  O O   . LYS B 610  ? 0.9006 0.9006 0.9006 0.0000  0.0000  0.0000  607  LYS A O   
4835  C CB  . LYS B 610  ? 0.9006 0.9006 0.9006 0.0000  0.0000  0.0000  607  LYS A CB  
4836  C CG  . LYS B 610  ? 0.9006 0.9006 0.9006 0.0000  0.0000  0.0000  607  LYS A CG  
4837  C CD  . LYS B 610  ? 0.9006 0.9006 0.9006 0.0000  0.0000  0.0000  607  LYS A CD  
4838  C CE  . LYS B 610  ? 0.9006 0.9006 0.9006 0.0000  0.0000  0.0000  607  LYS A CE  
4839  N NZ  . LYS B 610  ? 0.9006 0.9006 0.9006 0.0000  0.0000  0.0000  607  LYS A NZ  
4840  N N   . CYS B 611  ? 0.9905 0.9905 0.9905 0.0000  0.0000  0.0000  608  CYS A N   
4841  C CA  . CYS B 611  ? 0.9905 0.9905 0.9905 0.0000  0.0000  0.0000  608  CYS A CA  
4842  C C   . CYS B 611  ? 0.9905 0.9905 0.9905 0.0000  0.0000  0.0000  608  CYS A C   
4843  O O   . CYS B 611  ? 0.9905 0.9905 0.9905 0.0000  0.0000  0.0000  608  CYS A O   
4844  C CB  . CYS B 611  ? 0.9905 0.9905 0.9905 0.0000  0.0000  0.0000  608  CYS A CB  
4845  S SG  . CYS B 611  ? 0.9905 0.9905 0.9905 0.0000  0.0000  0.0000  608  CYS A SG  
4846  N N   . SER B 612  ? 1.0523 1.0523 1.0523 0.0000  0.0000  0.0000  609  SER A N   
4847  C CA  . SER B 612  ? 1.0523 1.0523 1.0523 0.0000  0.0000  0.0000  609  SER A CA  
4848  C C   . SER B 612  ? 1.0523 1.0523 1.0523 0.0000  0.0000  0.0000  609  SER A C   
4849  O O   . SER B 612  ? 1.0523 1.0523 1.0523 0.0000  0.0000  0.0000  609  SER A O   
4850  C CB  . SER B 612  ? 1.0523 1.0523 1.0523 0.0000  0.0000  0.0000  609  SER A CB  
4851  O OG  . SER B 612  ? 1.0523 1.0523 1.0523 0.0000  0.0000  0.0000  609  SER A OG  
4852  N N   . THR B 613  ? 1.1183 1.1183 1.1183 0.0000  0.0000  0.0000  610  THR A N   
4853  C CA  . THR B 613  ? 1.1183 1.1183 1.1183 0.0000  0.0000  0.0000  610  THR A CA  
4854  C C   . THR B 613  ? 1.1183 1.1183 1.1183 0.0000  0.0000  0.0000  610  THR A C   
4855  O O   . THR B 613  ? 1.1183 1.1183 1.1183 0.0000  0.0000  0.0000  610  THR A O   
4856  C CB  . THR B 613  ? 1.1183 1.1183 1.1183 0.0000  0.0000  0.0000  610  THR A CB  
4857  O OG1 . THR B 613  ? 1.1183 1.1183 1.1183 0.0000  0.0000  0.0000  610  THR A OG1 
4858  C CG2 . THR B 613  ? 1.1183 1.1183 1.1183 0.0000  0.0000  0.0000  610  THR A CG2 
4859  N N   . GLN B 614  ? 1.1077 1.1077 1.1077 0.0000  0.0000  0.0000  611  GLN A N   
4860  C CA  . GLN B 614  ? 1.1077 1.1077 1.1077 0.0000  0.0000  0.0000  611  GLN A CA  
4861  C C   . GLN B 614  ? 1.1077 1.1077 1.1077 0.0000  0.0000  0.0000  611  GLN A C   
4862  O O   . GLN B 614  ? 1.1077 1.1077 1.1077 0.0000  0.0000  0.0000  611  GLN A O   
4863  C CB  . GLN B 614  ? 1.1077 1.1077 1.1077 0.0000  0.0000  0.0000  611  GLN A CB  
4864  C CG  . GLN B 614  ? 1.1077 1.1077 1.1077 0.0000  0.0000  0.0000  611  GLN A CG  
4865  C CD  . GLN B 614  ? 1.1077 1.1077 1.1077 0.0000  0.0000  0.0000  611  GLN A CD  
4866  O OE1 . GLN B 614  ? 1.1077 1.1077 1.1077 0.0000  0.0000  0.0000  611  GLN A OE1 
4867  N NE2 . GLN B 614  ? 1.1077 1.1077 1.1077 0.0000  0.0000  0.0000  611  GLN A NE2 
4868  N N   . LEU B 615  ? 1.1961 1.1961 1.1961 0.0000  0.0000  0.0000  612  LEU A N   
4869  C CA  . LEU B 615  ? 1.1961 1.1961 1.1961 0.0000  0.0000  0.0000  612  LEU A CA  
4870  C C   . LEU B 615  ? 1.1961 1.1961 1.1961 0.0000  0.0000  0.0000  612  LEU A C   
4871  O O   . LEU B 615  ? 1.1961 1.1961 1.1961 0.0000  0.0000  0.0000  612  LEU A O   
4872  C CB  . LEU B 615  ? 1.1961 1.1961 1.1961 0.0000  0.0000  0.0000  612  LEU A CB  
4873  C CG  . LEU B 615  ? 1.1961 1.1961 1.1961 0.0000  0.0000  0.0000  612  LEU A CG  
4874  C CD1 . LEU B 615  ? 1.1961 1.1961 1.1961 0.0000  0.0000  0.0000  612  LEU A CD1 
4875  C CD2 . LEU B 615  ? 1.1961 1.1961 1.1961 0.0000  0.0000  0.0000  612  LEU A CD2 
4876  N N   . LYS B 616  ? 1.3422 1.3422 1.3422 0.0000  0.0000  0.0000  613  LYS A N   
4877  C CA  . LYS B 616  ? 1.3422 1.3422 1.3422 0.0000  0.0000  0.0000  613  LYS A CA  
4878  C C   . LYS B 616  ? 1.3422 1.3422 1.3422 0.0000  0.0000  0.0000  613  LYS A C   
4879  O O   . LYS B 616  ? 1.3422 1.3422 1.3422 0.0000  0.0000  0.0000  613  LYS A O   
4880  C CB  . LYS B 616  ? 1.3422 1.3422 1.3422 0.0000  0.0000  0.0000  613  LYS A CB  
4881  C CG  . LYS B 616  ? 1.3422 1.3422 1.3422 0.0000  0.0000  0.0000  613  LYS A CG  
4882  C CD  . LYS B 616  ? 1.3422 1.3422 1.3422 0.0000  0.0000  0.0000  613  LYS A CD  
4883  C CE  . LYS B 616  ? 1.3422 1.3422 1.3422 0.0000  0.0000  0.0000  613  LYS A CE  
4884  N NZ  . LYS B 616  ? 1.3422 1.3422 1.3422 0.0000  0.0000  0.0000  613  LYS A NZ  
4885  N N   . ALA B 617  ? 1.3786 1.3786 1.3786 0.0000  0.0000  0.0000  614  ALA A N   
4886  C CA  . ALA B 617  ? 1.3786 1.3786 1.3786 0.0000  0.0000  0.0000  614  ALA A CA  
4887  C C   . ALA B 617  ? 1.3786 1.3786 1.3786 0.0000  0.0000  0.0000  614  ALA A C   
4888  O O   . ALA B 617  ? 1.3786 1.3786 1.3786 0.0000  0.0000  0.0000  614  ALA A O   
4889  C CB  . ALA B 617  ? 1.3786 1.3786 1.3786 0.0000  0.0000  0.0000  614  ALA A CB  
4890  N N   . VAL B 618  ? 1.3450 1.3450 1.3450 0.0000  0.0000  0.0000  615  VAL A N   
4891  C CA  . VAL B 618  ? 1.3450 1.3450 1.3450 0.0000  0.0000  0.0000  615  VAL A CA  
4892  C C   . VAL B 618  ? 1.3450 1.3450 1.3450 0.0000  0.0000  0.0000  615  VAL A C   
4893  O O   . VAL B 618  ? 1.3450 1.3450 1.3450 0.0000  0.0000  0.0000  615  VAL A O   
4894  C CB  . VAL B 618  ? 1.3450 1.3450 1.3450 0.0000  0.0000  0.0000  615  VAL A CB  
4895  C CG1 . VAL B 618  ? 1.3450 1.3450 1.3450 0.0000  0.0000  0.0000  615  VAL A CG1 
4896  C CG2 . VAL B 618  ? 1.3450 1.3450 1.3450 0.0000  0.0000  0.0000  615  VAL A CG2 
4897  N N   . THR B 619  ? 1.3646 1.3646 1.3646 0.0000  0.0000  0.0000  616  THR A N   
4898  C CA  . THR B 619  ? 1.3646 1.3646 1.3646 0.0000  0.0000  0.0000  616  THR A CA  
4899  C C   . THR B 619  ? 1.3646 1.3646 1.3646 0.0000  0.0000  0.0000  616  THR A C   
4900  O O   . THR B 619  ? 1.3646 1.3646 1.3646 0.0000  0.0000  0.0000  616  THR A O   
4901  C CB  . THR B 619  ? 1.3646 1.3646 1.3646 0.0000  0.0000  0.0000  616  THR A CB  
4902  O OG1 . THR B 619  ? 1.3646 1.3646 1.3646 0.0000  0.0000  0.0000  616  THR A OG1 
4903  C CG2 . THR B 619  ? 1.3646 1.3646 1.3646 0.0000  0.0000  0.0000  616  THR A CG2 
4904  N N   . ALA B 620  ? 1.4230 1.4230 1.4230 0.0000  0.0000  0.0000  617  ALA A N   
4905  C CA  . ALA B 620  ? 1.4230 1.4230 1.4230 0.0000  0.0000  0.0000  617  ALA A CA  
4906  C C   . ALA B 620  ? 1.4230 1.4230 1.4230 0.0000  0.0000  0.0000  617  ALA A C   
4907  O O   . ALA B 620  ? 1.4230 1.4230 1.4230 0.0000  0.0000  0.0000  617  ALA A O   
4908  C CB  . ALA B 620  ? 1.4230 1.4230 1.4230 0.0000  0.0000  0.0000  617  ALA A CB  
4909  N N   . HIS B 621  ? 1.4371 1.4371 1.4371 0.0000  0.0000  0.0000  618  HIS A N   
4910  C CA  . HIS B 621  ? 1.4371 1.4371 1.4371 0.0000  0.0000  0.0000  618  HIS A CA  
4911  C C   . HIS B 621  ? 1.4371 1.4371 1.4371 0.0000  0.0000  0.0000  618  HIS A C   
4912  O O   . HIS B 621  ? 1.4371 1.4371 1.4371 0.0000  0.0000  0.0000  618  HIS A O   
4913  C CB  . HIS B 621  ? 1.4371 1.4371 1.4371 0.0000  0.0000  0.0000  618  HIS A CB  
4914  C CG  . HIS B 621  ? 1.4371 1.4371 1.4371 0.0000  0.0000  0.0000  618  HIS A CG  
4915  N ND1 . HIS B 621  ? 1.4371 1.4371 1.4371 0.0000  0.0000  0.0000  618  HIS A ND1 
4916  C CD2 . HIS B 621  ? 1.4371 1.4371 1.4371 0.0000  0.0000  0.0000  618  HIS A CD2 
4917  C CE1 . HIS B 621  ? 1.4371 1.4371 1.4371 0.0000  0.0000  0.0000  618  HIS A CE1 
4918  N NE2 . HIS B 621  ? 1.4371 1.4371 1.4371 0.0000  0.0000  0.0000  618  HIS A NE2 
4919  N N   . PHE B 622  ? 1.4787 1.4787 1.4787 0.0000  0.0000  0.0000  619  PHE A N   
4920  C CA  . PHE B 622  ? 1.4787 1.4787 1.4787 0.0000  0.0000  0.0000  619  PHE A CA  
4921  C C   . PHE B 622  ? 1.4787 1.4787 1.4787 0.0000  0.0000  0.0000  619  PHE A C   
4922  O O   . PHE B 622  ? 1.4787 1.4787 1.4787 0.0000  0.0000  0.0000  619  PHE A O   
4923  C CB  . PHE B 622  ? 1.4787 1.4787 1.4787 0.0000  0.0000  0.0000  619  PHE A CB  
4924  C CG  . PHE B 622  ? 1.4787 1.4787 1.4787 0.0000  0.0000  0.0000  619  PHE A CG  
4925  C CD1 . PHE B 622  ? 1.4787 1.4787 1.4787 0.0000  0.0000  0.0000  619  PHE A CD1 
4926  C CD2 . PHE B 622  ? 1.4787 1.4787 1.4787 0.0000  0.0000  0.0000  619  PHE A CD2 
4927  C CE1 . PHE B 622  ? 1.4787 1.4787 1.4787 0.0000  0.0000  0.0000  619  PHE A CE1 
4928  C CE2 . PHE B 622  ? 1.4787 1.4787 1.4787 0.0000  0.0000  0.0000  619  PHE A CE2 
4929  C CZ  . PHE B 622  ? 1.4787 1.4787 1.4787 0.0000  0.0000  0.0000  619  PHE A CZ  
4930  N N   . GLN B 623  ? 1.4590 1.4590 1.4590 0.0000  0.0000  0.0000  620  GLN A N   
4931  C CA  . GLN B 623  ? 1.4590 1.4590 1.4590 0.0000  0.0000  0.0000  620  GLN A CA  
4932  C C   . GLN B 623  ? 1.4590 1.4590 1.4590 0.0000  0.0000  0.0000  620  GLN A C   
4933  O O   . GLN B 623  ? 1.4590 1.4590 1.4590 0.0000  0.0000  0.0000  620  GLN A O   
4934  C CB  . GLN B 623  ? 1.4590 1.4590 1.4590 0.0000  0.0000  0.0000  620  GLN A CB  
4935  C CG  . GLN B 623  ? 1.4590 1.4590 1.4590 0.0000  0.0000  0.0000  620  GLN A CG  
4936  C CD  . GLN B 623  ? 1.4590 1.4590 1.4590 0.0000  0.0000  0.0000  620  GLN A CD  
4937  O OE1 . GLN B 623  ? 1.4590 1.4590 1.4590 0.0000  0.0000  0.0000  620  GLN A OE1 
4938  N NE2 . GLN B 623  ? 1.4590 1.4590 1.4590 0.0000  0.0000  0.0000  620  GLN A NE2 
4939  N N   . THR B 624  ? 1.4879 1.4879 1.4879 0.0000  0.0000  0.0000  621  THR A N   
4940  C CA  . THR B 624  ? 1.4879 1.4879 1.4879 0.0000  0.0000  0.0000  621  THR A CA  
4941  C C   . THR B 624  ? 1.4879 1.4879 1.4879 0.0000  0.0000  0.0000  621  THR A C   
4942  O O   . THR B 624  ? 1.4879 1.4879 1.4879 0.0000  0.0000  0.0000  621  THR A O   
4943  C CB  . THR B 624  ? 1.4879 1.4879 1.4879 0.0000  0.0000  0.0000  621  THR A CB  
4944  O OG1 . THR B 624  ? 1.4879 1.4879 1.4879 0.0000  0.0000  0.0000  621  THR A OG1 
4945  C CG2 . THR B 624  ? 1.4879 1.4879 1.4879 0.0000  0.0000  0.0000  621  THR A CG2 
4946  N N   . HIS B 625  ? 1.4755 1.4755 1.4755 0.0000  0.0000  0.0000  622  HIS A N   
4947  C CA  . HIS B 625  ? 1.4755 1.4755 1.4755 0.0000  0.0000  0.0000  622  HIS A CA  
4948  C C   . HIS B 625  ? 1.4755 1.4755 1.4755 0.0000  0.0000  0.0000  622  HIS A C   
4949  O O   . HIS B 625  ? 1.4755 1.4755 1.4755 0.0000  0.0000  0.0000  622  HIS A O   
4950  C CB  . HIS B 625  ? 1.4755 1.4755 1.4755 0.0000  0.0000  0.0000  622  HIS A CB  
4951  C CG  . HIS B 625  ? 1.4755 1.4755 1.4755 0.0000  0.0000  0.0000  622  HIS A CG  
4952  N ND1 . HIS B 625  ? 1.4755 1.4755 1.4755 0.0000  0.0000  0.0000  622  HIS A ND1 
4953  C CD2 . HIS B 625  ? 1.4755 1.4755 1.4755 0.0000  0.0000  0.0000  622  HIS A CD2 
4954  C CE1 . HIS B 625  ? 1.4755 1.4755 1.4755 0.0000  0.0000  0.0000  622  HIS A CE1 
4955  N NE2 . HIS B 625  ? 1.4755 1.4755 1.4755 0.0000  0.0000  0.0000  622  HIS A NE2 
4956  N N   . THR B 626  ? 1.5135 1.5135 1.5135 0.0000  0.0000  0.0000  623  THR A N   
4957  C CA  . THR B 626  ? 1.5135 1.5135 1.5135 0.0000  0.0000  0.0000  623  THR A CA  
4958  C C   . THR B 626  ? 1.5135 1.5135 1.5135 0.0000  0.0000  0.0000  623  THR A C   
4959  O O   . THR B 626  ? 1.5135 1.5135 1.5135 0.0000  0.0000  0.0000  623  THR A O   
4960  C CB  . THR B 626  ? 1.5135 1.5135 1.5135 0.0000  0.0000  0.0000  623  THR A CB  
4961  O OG1 . THR B 626  ? 1.5135 1.5135 1.5135 0.0000  0.0000  0.0000  623  THR A OG1 
4962  C CG2 . THR B 626  ? 1.5135 1.5135 1.5135 0.0000  0.0000  0.0000  623  THR A CG2 
4963  N N   . THR B 627  ? 1.4809 1.4809 1.4809 0.0000  0.0000  0.0000  624  THR A N   
4964  C CA  . THR B 627  ? 1.4809 1.4809 1.4809 0.0000  0.0000  0.0000  624  THR A CA  
4965  C C   . THR B 627  ? 1.4809 1.4809 1.4809 0.0000  0.0000  0.0000  624  THR A C   
4966  O O   . THR B 627  ? 1.4809 1.4809 1.4809 0.0000  0.0000  0.0000  624  THR A O   
4967  C CB  . THR B 627  ? 1.4809 1.4809 1.4809 0.0000  0.0000  0.0000  624  THR A CB  
4968  O OG1 . THR B 627  ? 1.4809 1.4809 1.4809 0.0000  0.0000  0.0000  624  THR A OG1 
4969  C CG2 . THR B 627  ? 1.4809 1.4809 1.4809 0.0000  0.0000  0.0000  624  THR A CG2 
4970  N N   . PRO B 628  ? 1.4448 1.4448 1.4448 0.0000  0.0000  0.0000  625  PRO A N   
4971  C CA  . PRO B 628  ? 1.4448 1.4448 1.4448 0.0000  0.0000  0.0000  625  PRO A CA  
4972  C C   . PRO B 628  ? 1.4448 1.4448 1.4448 0.0000  0.0000  0.0000  625  PRO A C   
4973  O O   . PRO B 628  ? 1.4448 1.4448 1.4448 0.0000  0.0000  0.0000  625  PRO A O   
4974  C CB  . PRO B 628  ? 1.4448 1.4448 1.4448 0.0000  0.0000  0.0000  625  PRO A CB  
4975  C CG  . PRO B 628  ? 1.4448 1.4448 1.4448 0.0000  0.0000  0.0000  625  PRO A CG  
4976  C CD  . PRO B 628  ? 1.4448 1.4448 1.4448 0.0000  0.0000  0.0000  625  PRO A CD  
4977  N N   . ILE B 629  ? 1.3804 1.3804 1.3804 0.0000  0.0000  0.0000  626  ILE A N   
4978  C CA  . ILE B 629  ? 1.3804 1.3804 1.3804 0.0000  0.0000  0.0000  626  ILE A CA  
4979  C C   . ILE B 629  ? 1.3804 1.3804 1.3804 0.0000  0.0000  0.0000  626  ILE A C   
4980  O O   . ILE B 629  ? 1.3804 1.3804 1.3804 0.0000  0.0000  0.0000  626  ILE A O   
4981  C CB  . ILE B 629  ? 1.3804 1.3804 1.3804 0.0000  0.0000  0.0000  626  ILE A CB  
4982  C CG1 . ILE B 629  ? 1.3804 1.3804 1.3804 0.0000  0.0000  0.0000  626  ILE A CG1 
4983  C CG2 . ILE B 629  ? 1.3804 1.3804 1.3804 0.0000  0.0000  0.0000  626  ILE A CG2 
4984  C CD1 . ILE B 629  ? 1.3804 1.3804 1.3804 0.0000  0.0000  0.0000  626  ILE A CD1 
4985  N N   . LEU B 630  ? 1.3177 1.3177 1.3177 0.0000  0.0000  0.0000  627  LEU A N   
4986  C CA  . LEU B 630  ? 1.3177 1.3177 1.3177 0.0000  0.0000  0.0000  627  LEU A CA  
4987  C C   . LEU B 630  ? 1.3177 1.3177 1.3177 0.0000  0.0000  0.0000  627  LEU A C   
4988  O O   . LEU B 630  ? 1.3177 1.3177 1.3177 0.0000  0.0000  0.0000  627  LEU A O   
4989  C CB  . LEU B 630  ? 1.3177 1.3177 1.3177 0.0000  0.0000  0.0000  627  LEU A CB  
4990  C CG  . LEU B 630  ? 1.3177 1.3177 1.3177 0.0000  0.0000  0.0000  627  LEU A CG  
4991  C CD1 . LEU B 630  ? 1.3177 1.3177 1.3177 0.0000  0.0000  0.0000  627  LEU A CD1 
4992  C CD2 . LEU B 630  ? 1.3177 1.3177 1.3177 0.0000  0.0000  0.0000  627  LEU A CD2 
4993  N N   . LEU B 631  ? 1.2253 1.2253 1.2253 0.0000  0.0000  0.0000  628  LEU A N   
4994  C CA  . LEU B 631  ? 1.2253 1.2253 1.2253 0.0000  0.0000  0.0000  628  LEU A CA  
4995  C C   . LEU B 631  ? 1.2253 1.2253 1.2253 0.0000  0.0000  0.0000  628  LEU A C   
4996  O O   . LEU B 631  ? 1.2253 1.2253 1.2253 0.0000  0.0000  0.0000  628  LEU A O   
4997  C CB  . LEU B 631  ? 1.2253 1.2253 1.2253 0.0000  0.0000  0.0000  628  LEU A CB  
4998  C CG  . LEU B 631  ? 1.2253 1.2253 1.2253 0.0000  0.0000  0.0000  628  LEU A CG  
4999  C CD1 . LEU B 631  ? 1.2253 1.2253 1.2253 0.0000  0.0000  0.0000  628  LEU A CD1 
5000  C CD2 . LEU B 631  ? 1.2253 1.2253 1.2253 0.0000  0.0000  0.0000  628  LEU A CD2 
5001  N N   . SER B 632  ? 1.2087 1.2087 1.2087 0.0000  0.0000  0.0000  629  SER A N   
5002  C CA  . SER B 632  ? 1.2087 1.2087 1.2087 0.0000  0.0000  0.0000  629  SER A CA  
5003  C C   . SER B 632  ? 1.2087 1.2087 1.2087 0.0000  0.0000  0.0000  629  SER A C   
5004  O O   . SER B 632  ? 1.2087 1.2087 1.2087 0.0000  0.0000  0.0000  629  SER A O   
5005  C CB  . SER B 632  ? 1.2087 1.2087 1.2087 0.0000  0.0000  0.0000  629  SER A CB  
5006  O OG  . SER B 632  ? 1.2087 1.2087 1.2087 0.0000  0.0000  0.0000  629  SER A OG  
5007  N N   . ASN B 633  ? 1.1336 1.1336 1.1336 0.0000  0.0000  0.0000  630  ASN A N   
5008  C CA  . ASN B 633  ? 1.1336 1.1336 1.1336 0.0000  0.0000  0.0000  630  ASN A CA  
5009  C C   . ASN B 633  ? 1.1336 1.1336 1.1336 0.0000  0.0000  0.0000  630  ASN A C   
5010  O O   . ASN B 633  ? 1.1336 1.1336 1.1336 0.0000  0.0000  0.0000  630  ASN A O   
5011  C CB  . ASN B 633  ? 1.1336 1.1336 1.1336 0.0000  0.0000  0.0000  630  ASN A CB  
5012  C CG  . ASN B 633  ? 1.1336 1.1336 1.1336 0.0000  0.0000  0.0000  630  ASN A CG  
5013  O OD1 . ASN B 633  ? 1.1336 1.1336 1.1336 0.0000  0.0000  0.0000  630  ASN A OD1 
5014  N ND2 . ASN B 633  ? 1.1336 1.1336 1.1336 0.0000  0.0000  0.0000  630  ASN A ND2 
5015  N N   . ASN B 634  ? 1.0530 1.0530 1.0530 0.0000  0.0000  0.0000  631  ASN A N   
5016  C CA  . ASN B 634  ? 1.0530 1.0530 1.0530 0.0000  0.0000  0.0000  631  ASN A CA  
5017  C C   . ASN B 634  ? 1.0530 1.0530 1.0530 0.0000  0.0000  0.0000  631  ASN A C   
5018  O O   . ASN B 634  ? 1.0530 1.0530 1.0530 0.0000  0.0000  0.0000  631  ASN A O   
5019  C CB  . ASN B 634  ? 1.0530 1.0530 1.0530 0.0000  0.0000  0.0000  631  ASN A CB  
5020  C CG  . ASN B 634  ? 1.0530 1.0530 1.0530 0.0000  0.0000  0.0000  631  ASN A CG  
5021  O OD1 . ASN B 634  ? 1.0530 1.0530 1.0530 0.0000  0.0000  0.0000  631  ASN A OD1 
5022  N ND2 . ASN B 634  ? 1.0530 1.0530 1.0530 0.0000  0.0000  0.0000  631  ASN A ND2 
5023  N N   . PHE B 635  ? 1.1121 1.1121 1.1121 0.0000  0.0000  0.0000  632  PHE A N   
5024  C CA  . PHE B 635  ? 1.1121 1.1121 1.1121 0.0000  0.0000  0.0000  632  PHE A CA  
5025  C C   . PHE B 635  ? 1.1121 1.1121 1.1121 0.0000  0.0000  0.0000  632  PHE A C   
5026  O O   . PHE B 635  ? 1.1121 1.1121 1.1121 0.0000  0.0000  0.0000  632  PHE A O   
5027  C CB  . PHE B 635  ? 1.1121 1.1121 1.1121 0.0000  0.0000  0.0000  632  PHE A CB  
5028  C CG  . PHE B 635  ? 1.1121 1.1121 1.1121 0.0000  0.0000  0.0000  632  PHE A CG  
5029  C CD1 . PHE B 635  ? 1.1121 1.1121 1.1121 0.0000  0.0000  0.0000  632  PHE A CD1 
5030  C CD2 . PHE B 635  ? 1.1121 1.1121 1.1121 0.0000  0.0000  0.0000  632  PHE A CD2 
5031  C CE1 . PHE B 635  ? 1.1121 1.1121 1.1121 0.0000  0.0000  0.0000  632  PHE A CE1 
5032  C CE2 . PHE B 635  ? 1.1121 1.1121 1.1121 0.0000  0.0000  0.0000  632  PHE A CE2 
5033  C CZ  . PHE B 635  ? 1.1121 1.1121 1.1121 0.0000  0.0000  0.0000  632  PHE A CZ  
5034  N N   . ILE B 636  ? 1.0700 1.0700 1.0700 0.0000  0.0000  0.0000  633  ILE A N   
5035  C CA  . ILE B 636  ? 1.0700 1.0700 1.0700 0.0000  0.0000  0.0000  633  ILE A CA  
5036  C C   . ILE B 636  ? 1.0700 1.0700 1.0700 0.0000  0.0000  0.0000  633  ILE A C   
5037  O O   . ILE B 636  ? 1.0700 1.0700 1.0700 0.0000  0.0000  0.0000  633  ILE A O   
5038  C CB  . ILE B 636  ? 1.0700 1.0700 1.0700 0.0000  0.0000  0.0000  633  ILE A CB  
5039  C CG1 . ILE B 636  ? 1.0700 1.0700 1.0700 0.0000  0.0000  0.0000  633  ILE A CG1 
5040  C CG2 . ILE B 636  ? 1.0700 1.0700 1.0700 0.0000  0.0000  0.0000  633  ILE A CG2 
5041  C CD1 . ILE B 636  ? 1.0700 1.0700 1.0700 0.0000  0.0000  0.0000  633  ILE A CD1 
5042  N N   . GLU B 637  ? 1.1071 1.1071 1.1071 0.0000  0.0000  0.0000  634  GLU A N   
5043  C CA  . GLU B 637  ? 1.1071 1.1071 1.1071 0.0000  0.0000  0.0000  634  GLU A CA  
5044  C C   . GLU B 637  ? 1.1071 1.1071 1.1071 0.0000  0.0000  0.0000  634  GLU A C   
5045  O O   . GLU B 637  ? 1.1071 1.1071 1.1071 0.0000  0.0000  0.0000  634  GLU A O   
5046  C CB  . GLU B 637  ? 1.1071 1.1071 1.1071 0.0000  0.0000  0.0000  634  GLU A CB  
5047  C CG  . GLU B 637  ? 1.1071 1.1071 1.1071 0.0000  0.0000  0.0000  634  GLU A CG  
5048  C CD  . GLU B 637  ? 1.1071 1.1071 1.1071 0.0000  0.0000  0.0000  634  GLU A CD  
5049  O OE1 . GLU B 637  ? 1.1071 1.1071 1.1071 0.0000  0.0000  0.0000  634  GLU A OE1 
5050  O OE2 . GLU B 637  ? 1.1071 1.1071 1.1071 0.0000  0.0000  0.0000  634  GLU A OE2 
5051  N N   . PRO B 638  ? 1.1638 1.1638 1.1638 0.0000  0.0000  0.0000  635  PRO A N   
5052  C CA  . PRO B 638  ? 1.1638 1.1638 1.1638 0.0000  0.0000  0.0000  635  PRO A CA  
5053  C C   . PRO B 638  ? 1.1638 1.1638 1.1638 0.0000  0.0000  0.0000  635  PRO A C   
5054  O O   . PRO B 638  ? 1.1638 1.1638 1.1638 0.0000  0.0000  0.0000  635  PRO A O   
5055  C CB  . PRO B 638  ? 1.1638 1.1638 1.1638 0.0000  0.0000  0.0000  635  PRO A CB  
5056  C CG  . PRO B 638  ? 1.1638 1.1638 1.1638 0.0000  0.0000  0.0000  635  PRO A CG  
5057  C CD  . PRO B 638  ? 1.1638 1.1638 1.1638 0.0000  0.0000  0.0000  635  PRO A CD  
5058  N N   . LEU B 639  ? 1.2276 1.2276 1.2276 0.0000  0.0000  0.0000  636  LEU A N   
5059  C CA  . LEU B 639  ? 1.2276 1.2276 1.2276 0.0000  0.0000  0.0000  636  LEU A CA  
5060  C C   . LEU B 639  ? 1.2276 1.2276 1.2276 0.0000  0.0000  0.0000  636  LEU A C   
5061  O O   . LEU B 639  ? 1.2276 1.2276 1.2276 0.0000  0.0000  0.0000  636  LEU A O   
5062  C CB  . LEU B 639  ? 1.2276 1.2276 1.2276 0.0000  0.0000  0.0000  636  LEU A CB  
5063  C CG  . LEU B 639  ? 1.2276 1.2276 1.2276 0.0000  0.0000  0.0000  636  LEU A CG  
5064  C CD1 . LEU B 639  ? 1.2276 1.2276 1.2276 0.0000  0.0000  0.0000  636  LEU A CD1 
5065  C CD2 . LEU B 639  ? 1.2276 1.2276 1.2276 0.0000  0.0000  0.0000  636  LEU A CD2 
5066  N N   . GLU B 640  ? 1.3644 1.3644 1.3644 0.0000  0.0000  0.0000  637  GLU A N   
5067  C CA  . GLU B 640  ? 1.3644 1.3644 1.3644 0.0000  0.0000  0.0000  637  GLU A CA  
5068  C C   . GLU B 640  ? 1.3644 1.3644 1.3644 0.0000  0.0000  0.0000  637  GLU A C   
5069  O O   . GLU B 640  ? 1.3644 1.3644 1.3644 0.0000  0.0000  0.0000  637  GLU A O   
5070  C CB  . GLU B 640  ? 1.3644 1.3644 1.3644 0.0000  0.0000  0.0000  637  GLU A CB  
5071  C CG  . GLU B 640  ? 1.3644 1.3644 1.3644 0.0000  0.0000  0.0000  637  GLU A CG  
5072  C CD  . GLU B 640  ? 1.3644 1.3644 1.3644 0.0000  0.0000  0.0000  637  GLU A CD  
5073  O OE1 . GLU B 640  ? 1.3644 1.3644 1.3644 0.0000  0.0000  0.0000  637  GLU A OE1 
5074  O OE2 . GLU B 640  ? 1.3644 1.3644 1.3644 0.0000  0.0000  0.0000  637  GLU A OE2 
5075  N N   . ILE B 641  ? 1.4060 1.4060 1.4060 0.0000  0.0000  0.0000  638  ILE A N   
5076  C CA  . ILE B 641  ? 1.4060 1.4060 1.4060 0.0000  0.0000  0.0000  638  ILE A CA  
5077  C C   . ILE B 641  ? 1.4060 1.4060 1.4060 0.0000  0.0000  0.0000  638  ILE A C   
5078  O O   . ILE B 641  ? 1.4060 1.4060 1.4060 0.0000  0.0000  0.0000  638  ILE A O   
5079  C CB  . ILE B 641  ? 1.4060 1.4060 1.4060 0.0000  0.0000  0.0000  638  ILE A CB  
5080  C CG1 . ILE B 641  ? 1.4060 1.4060 1.4060 0.0000  0.0000  0.0000  638  ILE A CG1 
5081  C CG2 . ILE B 641  ? 1.4060 1.4060 1.4060 0.0000  0.0000  0.0000  638  ILE A CG2 
5082  C CD1 . ILE B 641  ? 1.4060 1.4060 1.4060 0.0000  0.0000  0.0000  638  ILE A CD1 
5083  N N   . THR B 642  ? 1.4563 1.4563 1.4563 0.0000  0.0000  0.0000  639  THR A N   
5084  C CA  . THR B 642  ? 1.4563 1.4563 1.4563 0.0000  0.0000  0.0000  639  THR A CA  
5085  C C   . THR B 642  ? 1.4563 1.4563 1.4563 0.0000  0.0000  0.0000  639  THR A C   
5086  O O   . THR B 642  ? 1.4563 1.4563 1.4563 0.0000  0.0000  0.0000  639  THR A O   
5087  C CB  . THR B 642  ? 1.4563 1.4563 1.4563 0.0000  0.0000  0.0000  639  THR A CB  
5088  O OG1 . THR B 642  ? 1.4563 1.4563 1.4563 0.0000  0.0000  0.0000  639  THR A OG1 
5089  C CG2 . THR B 642  ? 1.4563 1.4563 1.4563 0.0000  0.0000  0.0000  639  THR A CG2 
5090  N N   . LYS B 643  ? 1.4662 1.4662 1.4662 0.0000  0.0000  0.0000  640  LYS A N   
5091  C CA  . LYS B 643  ? 1.4662 1.4662 1.4662 0.0000  0.0000  0.0000  640  LYS A CA  
5092  C C   . LYS B 643  ? 1.4662 1.4662 1.4662 0.0000  0.0000  0.0000  640  LYS A C   
5093  O O   . LYS B 643  ? 1.4662 1.4662 1.4662 0.0000  0.0000  0.0000  640  LYS A O   
5094  C CB  . LYS B 643  ? 1.4662 1.4662 1.4662 0.0000  0.0000  0.0000  640  LYS A CB  
5095  C CG  . LYS B 643  ? 1.4662 1.4662 1.4662 0.0000  0.0000  0.0000  640  LYS A CG  
5096  C CD  . LYS B 643  ? 1.4662 1.4662 1.4662 0.0000  0.0000  0.0000  640  LYS A CD  
5097  C CE  . LYS B 643  ? 1.4662 1.4662 1.4662 0.0000  0.0000  0.0000  640  LYS A CE  
5098  N NZ  . LYS B 643  ? 1.4662 1.4662 1.4662 0.0000  0.0000  0.0000  640  LYS A NZ  
5099  N N   . GLU B 644  ? 1.4453 1.4453 1.4453 0.0000  0.0000  0.0000  641  GLU A N   
5100  C CA  . GLU B 644  ? 1.4453 1.4453 1.4453 0.0000  0.0000  0.0000  641  GLU A CA  
5101  C C   . GLU B 644  ? 1.4453 1.4453 1.4453 0.0000  0.0000  0.0000  641  GLU A C   
5102  O O   . GLU B 644  ? 1.4453 1.4453 1.4453 0.0000  0.0000  0.0000  641  GLU A O   
5103  C CB  . GLU B 644  ? 1.4453 1.4453 1.4453 0.0000  0.0000  0.0000  641  GLU A CB  
5104  C CG  . GLU B 644  ? 1.4453 1.4453 1.4453 0.0000  0.0000  0.0000  641  GLU A CG  
5105  C CD  . GLU B 644  ? 1.4453 1.4453 1.4453 0.0000  0.0000  0.0000  641  GLU A CD  
5106  O OE1 . GLU B 644  ? 1.4453 1.4453 1.4453 0.0000  0.0000  0.0000  641  GLU A OE1 
5107  O OE2 . GLU B 644  ? 1.4453 1.4453 1.4453 0.0000  0.0000  0.0000  641  GLU A OE2 
5108  N N   . ILE B 645  ? 1.4140 1.4140 1.4140 0.0000  0.0000  0.0000  642  ILE A N   
5109  C CA  . ILE B 645  ? 1.4140 1.4140 1.4140 0.0000  0.0000  0.0000  642  ILE A CA  
5110  C C   . ILE B 645  ? 1.4140 1.4140 1.4140 0.0000  0.0000  0.0000  642  ILE A C   
5111  O O   . ILE B 645  ? 1.4140 1.4140 1.4140 0.0000  0.0000  0.0000  642  ILE A O   
5112  C CB  . ILE B 645  ? 1.4140 1.4140 1.4140 0.0000  0.0000  0.0000  642  ILE A CB  
5113  C CG1 . ILE B 645  ? 1.4140 1.4140 1.4140 0.0000  0.0000  0.0000  642  ILE A CG1 
5114  C CG2 . ILE B 645  ? 1.4140 1.4140 1.4140 0.0000  0.0000  0.0000  642  ILE A CG2 
5115  C CD1 . ILE B 645  ? 1.4140 1.4140 1.4140 0.0000  0.0000  0.0000  642  ILE A CD1 
5116  N N   . TYR B 646  ? 1.4207 1.4207 1.4207 0.0000  0.0000  0.0000  643  TYR A N   
5117  C CA  . TYR B 646  ? 1.4207 1.4207 1.4207 0.0000  0.0000  0.0000  643  TYR A CA  
5118  C C   . TYR B 646  ? 1.4207 1.4207 1.4207 0.0000  0.0000  0.0000  643  TYR A C   
5119  O O   . TYR B 646  ? 1.4207 1.4207 1.4207 0.0000  0.0000  0.0000  643  TYR A O   
5120  C CB  . TYR B 646  ? 1.4207 1.4207 1.4207 0.0000  0.0000  0.0000  643  TYR A CB  
5121  C CG  . TYR B 646  ? 1.4207 1.4207 1.4207 0.0000  0.0000  0.0000  643  TYR A CG  
5122  C CD1 . TYR B 646  ? 1.4207 1.4207 1.4207 0.0000  0.0000  0.0000  643  TYR A CD1 
5123  C CD2 . TYR B 646  ? 1.4207 1.4207 1.4207 0.0000  0.0000  0.0000  643  TYR A CD2 
5124  C CE1 . TYR B 646  ? 1.4207 1.4207 1.4207 0.0000  0.0000  0.0000  643  TYR A CE1 
5125  C CE2 . TYR B 646  ? 1.4207 1.4207 1.4207 0.0000  0.0000  0.0000  643  TYR A CE2 
5126  C CZ  . TYR B 646  ? 1.4207 1.4207 1.4207 0.0000  0.0000  0.0000  643  TYR A CZ  
5127  O OH  . TYR B 646  ? 1.4207 1.4207 1.4207 0.0000  0.0000  0.0000  643  TYR A OH  
5128  N N   . ASP B 647  ? 1.4273 1.4273 1.4273 0.0000  0.0000  0.0000  644  ASP A N   
5129  C CA  . ASP B 647  ? 1.4273 1.4273 1.4273 0.0000  0.0000  0.0000  644  ASP A CA  
5130  C C   . ASP B 647  ? 1.4273 1.4273 1.4273 0.0000  0.0000  0.0000  644  ASP A C   
5131  O O   . ASP B 647  ? 1.4273 1.4273 1.4273 0.0000  0.0000  0.0000  644  ASP A O   
5132  C CB  . ASP B 647  ? 1.4273 1.4273 1.4273 0.0000  0.0000  0.0000  644  ASP A CB  
5133  C CG  . ASP B 647  ? 1.4273 1.4273 1.4273 0.0000  0.0000  0.0000  644  ASP A CG  
5134  O OD1 . ASP B 647  ? 1.4273 1.4273 1.4273 0.0000  0.0000  0.0000  644  ASP A OD1 
5135  O OD2 . ASP B 647  ? 1.4273 1.4273 1.4273 0.0000  0.0000  0.0000  644  ASP A OD2 
5136  N N   . LEU B 648  ? 1.4161 1.4161 1.4161 0.0000  0.0000  0.0000  645  LEU A N   
5137  C CA  . LEU B 648  ? 1.4161 1.4161 1.4161 0.0000  0.0000  0.0000  645  LEU A CA  
5138  C C   . LEU B 648  ? 1.4161 1.4161 1.4161 0.0000  0.0000  0.0000  645  LEU A C   
5139  O O   . LEU B 648  ? 1.4161 1.4161 1.4161 0.0000  0.0000  0.0000  645  LEU A O   
5140  C CB  . LEU B 648  ? 1.4161 1.4161 1.4161 0.0000  0.0000  0.0000  645  LEU A CB  
5141  C CG  . LEU B 648  ? 1.4161 1.4161 1.4161 0.0000  0.0000  0.0000  645  LEU A CG  
5142  C CD1 . LEU B 648  ? 1.4161 1.4161 1.4161 0.0000  0.0000  0.0000  645  LEU A CD1 
5143  C CD2 . LEU B 648  ? 1.4161 1.4161 1.4161 0.0000  0.0000  0.0000  645  LEU A CD2 
5144  N N   . ASN B 649  ? 1.3912 1.3912 1.3912 0.0000  0.0000  0.0000  646  ASN A N   
5145  C CA  . ASN B 649  ? 1.3912 1.3912 1.3912 0.0000  0.0000  0.0000  646  ASN A CA  
5146  C C   . ASN B 649  ? 1.3912 1.3912 1.3912 0.0000  0.0000  0.0000  646  ASN A C   
5147  O O   . ASN B 649  ? 1.3912 1.3912 1.3912 0.0000  0.0000  0.0000  646  ASN A O   
5148  C CB  . ASN B 649  ? 1.3912 1.3912 1.3912 0.0000  0.0000  0.0000  646  ASN A CB  
5149  C CG  . ASN B 649  ? 1.3912 1.3912 1.3912 0.0000  0.0000  0.0000  646  ASN A CG  
5150  O OD1 . ASN B 649  ? 1.3912 1.3912 1.3912 0.0000  0.0000  0.0000  646  ASN A OD1 
5151  N ND2 . ASN B 649  ? 1.3912 1.3912 1.3912 0.0000  0.0000  0.0000  646  ASN A ND2 
5152  N N   . ASN B 650  ? 1.3909 1.3909 1.3909 0.0000  0.0000  0.0000  647  ASN A N   
5153  C CA  . ASN B 650  ? 1.3909 1.3909 1.3909 0.0000  0.0000  0.0000  647  ASN A CA  
5154  C C   . ASN B 650  ? 1.3909 1.3909 1.3909 0.0000  0.0000  0.0000  647  ASN A C   
5155  O O   . ASN B 650  ? 1.3909 1.3909 1.3909 0.0000  0.0000  0.0000  647  ASN A O   
5156  C CB  . ASN B 650  ? 1.3909 1.3909 1.3909 0.0000  0.0000  0.0000  647  ASN A CB  
5157  C CG  . ASN B 650  ? 1.3909 1.3909 1.3909 0.0000  0.0000  0.0000  647  ASN A CG  
5158  O OD1 . ASN B 650  ? 1.3909 1.3909 1.3909 0.0000  0.0000  0.0000  647  ASN A OD1 
5159  N ND2 . ASN B 650  ? 1.3909 1.3909 1.3909 0.0000  0.0000  0.0000  647  ASN A ND2 
5160  N N   . PRO B 651  ? 1.4718 1.4718 1.4718 0.0000  0.0000  0.0000  648  PRO A N   
5161  C CA  . PRO B 651  ? 1.4718 1.4718 1.4718 0.0000  0.0000  0.0000  648  PRO A CA  
5162  C C   . PRO B 651  ? 1.4718 1.4718 1.4718 0.0000  0.0000  0.0000  648  PRO A C   
5163  O O   . PRO B 651  ? 1.4718 1.4718 1.4718 0.0000  0.0000  0.0000  648  PRO A O   
5164  C CB  . PRO B 651  ? 1.4718 1.4718 1.4718 0.0000  0.0000  0.0000  648  PRO A CB  
5165  C CG  . PRO B 651  ? 1.4718 1.4718 1.4718 0.0000  0.0000  0.0000  648  PRO A CG  
5166  C CD  . PRO B 651  ? 1.4718 1.4718 1.4718 0.0000  0.0000  0.0000  648  PRO A CD  
5167  N N   . GLU B 652  ? 1.5627 1.5627 1.5627 0.0000  0.0000  0.0000  649  GLU A N   
5168  C CA  . GLU B 652  ? 1.5627 1.5627 1.5627 0.0000  0.0000  0.0000  649  GLU A CA  
5169  C C   . GLU B 652  ? 1.5627 1.5627 1.5627 0.0000  0.0000  0.0000  649  GLU A C   
5170  O O   . GLU B 652  ? 1.5627 1.5627 1.5627 0.0000  0.0000  0.0000  649  GLU A O   
5176  N N   . PRO B 655  ? 1.5781 1.5781 1.5781 0.0000  0.0000  0.0000  652  PRO A N   
5177  C CA  . PRO B 655  ? 1.5781 1.5781 1.5781 0.0000  0.0000  0.0000  652  PRO A CA  
5178  C C   . PRO B 655  ? 1.5781 1.5781 1.5781 0.0000  0.0000  0.0000  652  PRO A C   
5179  O O   . PRO B 655  ? 1.5781 1.5781 1.5781 0.0000  0.0000  0.0000  652  PRO A O   
5180  C CB  . PRO B 655  ? 1.5781 1.5781 1.5781 0.0000  0.0000  0.0000  652  PRO A CB  
5181  C CG  . PRO B 655  ? 1.5781 1.5781 1.5781 0.0000  0.0000  0.0000  652  PRO A CG  
5182  C CD  . PRO B 655  ? 1.5781 1.5781 1.5781 0.0000  0.0000  0.0000  652  PRO A CD  
5183  N N   . LYS B 656  ? 1.4659 1.4659 1.4659 0.0000  0.0000  0.0000  653  LYS A N   
5184  C CA  . LYS B 656  ? 1.4659 1.4659 1.4659 0.0000  0.0000  0.0000  653  LYS A CA  
5185  C C   . LYS B 656  ? 1.4659 1.4659 1.4659 0.0000  0.0000  0.0000  653  LYS A C   
5186  O O   . LYS B 656  ? 1.4659 1.4659 1.4659 0.0000  0.0000  0.0000  653  LYS A O   
5187  C CB  . LYS B 656  ? 1.4659 1.4659 1.4659 0.0000  0.0000  0.0000  653  LYS A CB  
5188  C CG  . LYS B 656  ? 1.4659 1.4659 1.4659 0.0000  0.0000  0.0000  653  LYS A CG  
5189  C CD  . LYS B 656  ? 1.4659 1.4659 1.4659 0.0000  0.0000  0.0000  653  LYS A CD  
5190  C CE  . LYS B 656  ? 1.4659 1.4659 1.4659 0.0000  0.0000  0.0000  653  LYS A CE  
5191  N NZ  . LYS B 656  ? 1.4659 1.4659 1.4659 0.0000  0.0000  0.0000  653  LYS A NZ  
5192  N N   . LYS B 657  ? 1.4588 1.4588 1.4588 0.0000  0.0000  0.0000  654  LYS A N   
5193  C CA  . LYS B 657  ? 1.4588 1.4588 1.4588 0.0000  0.0000  0.0000  654  LYS A CA  
5194  C C   . LYS B 657  ? 1.4588 1.4588 1.4588 0.0000  0.0000  0.0000  654  LYS A C   
5195  O O   . LYS B 657  ? 1.4588 1.4588 1.4588 0.0000  0.0000  0.0000  654  LYS A O   
5196  C CB  . LYS B 657  ? 1.4588 1.4588 1.4588 0.0000  0.0000  0.0000  654  LYS A CB  
5197  C CG  . LYS B 657  ? 1.4588 1.4588 1.4588 0.0000  0.0000  0.0000  654  LYS A CG  
5198  C CD  . LYS B 657  ? 1.4588 1.4588 1.4588 0.0000  0.0000  0.0000  654  LYS A CD  
5199  C CE  . LYS B 657  ? 1.4588 1.4588 1.4588 0.0000  0.0000  0.0000  654  LYS A CE  
5200  N NZ  . LYS B 657  ? 1.4588 1.4588 1.4588 0.0000  0.0000  0.0000  654  LYS A NZ  
5201  N N   . PHE B 658  ? 1.3778 1.3778 1.3778 0.0000  0.0000  0.0000  655  PHE A N   
5202  C CA  . PHE B 658  ? 1.3778 1.3778 1.3778 0.0000  0.0000  0.0000  655  PHE A CA  
5203  C C   . PHE B 658  ? 1.3778 1.3778 1.3778 0.0000  0.0000  0.0000  655  PHE A C   
5204  O O   . PHE B 658  ? 1.3778 1.3778 1.3778 0.0000  0.0000  0.0000  655  PHE A O   
5205  C CB  . PHE B 658  ? 1.3778 1.3778 1.3778 0.0000  0.0000  0.0000  655  PHE A CB  
5206  C CG  . PHE B 658  ? 1.3778 1.3778 1.3778 0.0000  0.0000  0.0000  655  PHE A CG  
5207  C CD1 . PHE B 658  ? 1.3778 1.3778 1.3778 0.0000  0.0000  0.0000  655  PHE A CD1 
5208  C CD2 . PHE B 658  ? 1.3778 1.3778 1.3778 0.0000  0.0000  0.0000  655  PHE A CD2 
5209  C CE1 . PHE B 658  ? 1.3778 1.3778 1.3778 0.0000  0.0000  0.0000  655  PHE A CE1 
5210  C CE2 . PHE B 658  ? 1.3778 1.3778 1.3778 0.0000  0.0000  0.0000  655  PHE A CE2 
5211  C CZ  . PHE B 658  ? 1.3778 1.3778 1.3778 0.0000  0.0000  0.0000  655  PHE A CZ  
5212  N N   . GLN B 659  ? 1.4204 1.4204 1.4204 0.0000  0.0000  0.0000  656  GLN A N   
5213  C CA  . GLN B 659  ? 1.4204 1.4204 1.4204 0.0000  0.0000  0.0000  656  GLN A CA  
5214  C C   . GLN B 659  ? 1.4204 1.4204 1.4204 0.0000  0.0000  0.0000  656  GLN A C   
5215  O O   . GLN B 659  ? 1.4204 1.4204 1.4204 0.0000  0.0000  0.0000  656  GLN A O   
5216  C CB  . GLN B 659  ? 1.4204 1.4204 1.4204 0.0000  0.0000  0.0000  656  GLN A CB  
5217  C CG  . GLN B 659  ? 1.4204 1.4204 1.4204 0.0000  0.0000  0.0000  656  GLN A CG  
5218  C CD  . GLN B 659  ? 1.4204 1.4204 1.4204 0.0000  0.0000  0.0000  656  GLN A CD  
5219  O OE1 . GLN B 659  ? 1.4204 1.4204 1.4204 0.0000  0.0000  0.0000  656  GLN A OE1 
5220  N NE2 . GLN B 659  ? 1.4204 1.4204 1.4204 0.0000  0.0000  0.0000  656  GLN A NE2 
5221  N N   . THR B 660  ? 1.4830 1.4830 1.4830 0.0000  0.0000  0.0000  657  THR A N   
5222  C CA  . THR B 660  ? 1.4830 1.4830 1.4830 0.0000  0.0000  0.0000  657  THR A CA  
5223  C C   . THR B 660  ? 1.4830 1.4830 1.4830 0.0000  0.0000  0.0000  657  THR A C   
5224  O O   . THR B 660  ? 1.4830 1.4830 1.4830 0.0000  0.0000  0.0000  657  THR A O   
5225  C CB  . THR B 660  ? 1.4830 1.4830 1.4830 0.0000  0.0000  0.0000  657  THR A CB  
5226  O OG1 . THR B 660  ? 1.4830 1.4830 1.4830 0.0000  0.0000  0.0000  657  THR A OG1 
5227  C CG2 . THR B 660  ? 1.4830 1.4830 1.4830 0.0000  0.0000  0.0000  657  THR A CG2 
5228  N N   . ALA B 661  ? 1.4966 1.4966 1.4966 0.0000  0.0000  0.0000  658  ALA A N   
5229  C CA  . ALA B 661  ? 1.4966 1.4966 1.4966 0.0000  0.0000  0.0000  658  ALA A CA  
5230  C C   . ALA B 661  ? 1.4966 1.4966 1.4966 0.0000  0.0000  0.0000  658  ALA A C   
5231  O O   . ALA B 661  ? 1.4966 1.4966 1.4966 0.0000  0.0000  0.0000  658  ALA A O   
5232  C CB  . ALA B 661  ? 1.4966 1.4966 1.4966 0.0000  0.0000  0.0000  658  ALA A CB  
5233  N N   . TYR B 662  ? 1.4542 1.4542 1.4542 0.0000  0.0000  0.0000  659  TYR A N   
5234  C CA  . TYR B 662  ? 1.4542 1.4542 1.4542 0.0000  0.0000  0.0000  659  TYR A CA  
5235  C C   . TYR B 662  ? 1.4542 1.4542 1.4542 0.0000  0.0000  0.0000  659  TYR A C   
5236  O O   . TYR B 662  ? 1.4542 1.4542 1.4542 0.0000  0.0000  0.0000  659  TYR A O   
5237  C CB  . TYR B 662  ? 1.4542 1.4542 1.4542 0.0000  0.0000  0.0000  659  TYR A CB  
5238  C CG  . TYR B 662  ? 1.4542 1.4542 1.4542 0.0000  0.0000  0.0000  659  TYR A CG  
5239  C CD1 . TYR B 662  ? 1.4542 1.4542 1.4542 0.0000  0.0000  0.0000  659  TYR A CD1 
5240  C CD2 . TYR B 662  ? 1.4542 1.4542 1.4542 0.0000  0.0000  0.0000  659  TYR A CD2 
5241  C CE1 . TYR B 662  ? 1.4542 1.4542 1.4542 0.0000  0.0000  0.0000  659  TYR A CE1 
5242  C CE2 . TYR B 662  ? 1.4542 1.4542 1.4542 0.0000  0.0000  0.0000  659  TYR A CE2 
5243  C CZ  . TYR B 662  ? 1.4542 1.4542 1.4542 0.0000  0.0000  0.0000  659  TYR A CZ  
5244  O OH  . TYR B 662  ? 1.4542 1.4542 1.4542 0.0000  0.0000  0.0000  659  TYR A OH  
5245  N N   . ALA B 663  ? 1.4868 1.4868 1.4868 0.0000  0.0000  0.0000  660  ALA A N   
5246  C CA  . ALA B 663  ? 1.4868 1.4868 1.4868 0.0000  0.0000  0.0000  660  ALA A CA  
5247  C C   . ALA B 663  ? 1.4868 1.4868 1.4868 0.0000  0.0000  0.0000  660  ALA A C   
5248  O O   . ALA B 663  ? 1.4868 1.4868 1.4868 0.0000  0.0000  0.0000  660  ALA A O   
5249  C CB  . ALA B 663  ? 1.4868 1.4868 1.4868 0.0000  0.0000  0.0000  660  ALA A CB  
5250  N N   . LYS B 664  ? 1.5094 1.5094 1.5094 0.0000  0.0000  0.0000  661  LYS A N   
5251  C CA  . LYS B 664  ? 1.5094 1.5094 1.5094 0.0000  0.0000  0.0000  661  LYS A CA  
5252  C C   . LYS B 664  ? 1.5094 1.5094 1.5094 0.0000  0.0000  0.0000  661  LYS A C   
5253  O O   . LYS B 664  ? 1.5094 1.5094 1.5094 0.0000  0.0000  0.0000  661  LYS A O   
5254  C CB  . LYS B 664  ? 1.5094 1.5094 1.5094 0.0000  0.0000  0.0000  661  LYS A CB  
5255  C CG  . LYS B 664  ? 1.5094 1.5094 1.5094 0.0000  0.0000  0.0000  661  LYS A CG  
5256  C CD  . LYS B 664  ? 1.5094 1.5094 1.5094 0.0000  0.0000  0.0000  661  LYS A CD  
5257  C CE  . LYS B 664  ? 1.5094 1.5094 1.5094 0.0000  0.0000  0.0000  661  LYS A CE  
5258  N NZ  . LYS B 664  ? 1.5094 1.5094 1.5094 0.0000  0.0000  0.0000  661  LYS A NZ  
5259  N N   . LYS B 665  ? 1.4831 1.4831 1.4831 0.0000  0.0000  0.0000  662  LYS A N   
5260  C CA  . LYS B 665  ? 1.4831 1.4831 1.4831 0.0000  0.0000  0.0000  662  LYS A CA  
5261  C C   . LYS B 665  ? 1.4831 1.4831 1.4831 0.0000  0.0000  0.0000  662  LYS A C   
5262  O O   . LYS B 665  ? 1.4831 1.4831 1.4831 0.0000  0.0000  0.0000  662  LYS A O   
5263  C CB  . LYS B 665  ? 1.4831 1.4831 1.4831 0.0000  0.0000  0.0000  662  LYS A CB  
5264  C CG  . LYS B 665  ? 1.4831 1.4831 1.4831 0.0000  0.0000  0.0000  662  LYS A CG  
5265  C CD  . LYS B 665  ? 1.4831 1.4831 1.4831 0.0000  0.0000  0.0000  662  LYS A CD  
5266  C CE  . LYS B 665  ? 1.4831 1.4831 1.4831 0.0000  0.0000  0.0000  662  LYS A CE  
5267  N NZ  . LYS B 665  ? 1.4831 1.4831 1.4831 0.0000  0.0000  0.0000  662  LYS A NZ  
5268  N N   . THR B 666  ? 1.4673 1.4673 1.4673 0.0000  0.0000  0.0000  663  THR A N   
5269  C CA  . THR B 666  ? 1.4673 1.4673 1.4673 0.0000  0.0000  0.0000  663  THR A CA  
5270  C C   . THR B 666  ? 1.4673 1.4673 1.4673 0.0000  0.0000  0.0000  663  THR A C   
5271  O O   . THR B 666  ? 1.4673 1.4673 1.4673 0.0000  0.0000  0.0000  663  THR A O   
5272  C CB  . THR B 666  ? 1.4673 1.4673 1.4673 0.0000  0.0000  0.0000  663  THR A CB  
5273  O OG1 . THR B 666  ? 1.4673 1.4673 1.4673 0.0000  0.0000  0.0000  663  THR A OG1 
5274  C CG2 . THR B 666  ? 1.4673 1.4673 1.4673 0.0000  0.0000  0.0000  663  THR A CG2 
5275  N N   . GLY B 667  ? 1.4695 1.4695 1.4695 0.0000  0.0000  0.0000  664  GLY A N   
5276  C CA  . GLY B 667  ? 1.4695 1.4695 1.4695 0.0000  0.0000  0.0000  664  GLY A CA  
5277  C C   . GLY B 667  ? 1.4695 1.4695 1.4695 0.0000  0.0000  0.0000  664  GLY A C   
5278  O O   . GLY B 667  ? 1.4695 1.4695 1.4695 0.0000  0.0000  0.0000  664  GLY A O   
5279  N N   . ASP B 668  ? 1.4111 1.4111 1.4111 0.0000  0.0000  0.0000  665  ASP A N   
5280  C CA  . ASP B 668  ? 1.4111 1.4111 1.4111 0.0000  0.0000  0.0000  665  ASP A CA  
5281  C C   . ASP B 668  ? 1.4111 1.4111 1.4111 0.0000  0.0000  0.0000  665  ASP A C   
5282  O O   . ASP B 668  ? 1.4111 1.4111 1.4111 0.0000  0.0000  0.0000  665  ASP A O   
5283  C CB  . ASP B 668  ? 1.4111 1.4111 1.4111 0.0000  0.0000  0.0000  665  ASP A CB  
5284  C CG  . ASP B 668  ? 1.4111 1.4111 1.4111 0.0000  0.0000  0.0000  665  ASP A CG  
5285  O OD1 . ASP B 668  ? 1.4111 1.4111 1.4111 0.0000  0.0000  0.0000  665  ASP A OD1 
5286  O OD2 . ASP B 668  ? 1.4111 1.4111 1.4111 0.0000  0.0000  0.0000  665  ASP A OD2 
5287  N N   . GLN B 669  ? 1.3934 1.3934 1.3934 0.0000  0.0000  0.0000  666  GLN A N   
5288  C CA  . GLN B 669  ? 1.3934 1.3934 1.3934 0.0000  0.0000  0.0000  666  GLN A CA  
5289  C C   . GLN B 669  ? 1.3934 1.3934 1.3934 0.0000  0.0000  0.0000  666  GLN A C   
5290  O O   . GLN B 669  ? 1.3934 1.3934 1.3934 0.0000  0.0000  0.0000  666  GLN A O   
5291  C CB  . GLN B 669  ? 1.3934 1.3934 1.3934 0.0000  0.0000  0.0000  666  GLN A CB  
5292  C CG  . GLN B 669  ? 1.3934 1.3934 1.3934 0.0000  0.0000  0.0000  666  GLN A CG  
5293  C CD  . GLN B 669  ? 1.3934 1.3934 1.3934 0.0000  0.0000  0.0000  666  GLN A CD  
5294  O OE1 . GLN B 669  ? 1.3934 1.3934 1.3934 0.0000  0.0000  0.0000  666  GLN A OE1 
5295  N NE2 . GLN B 669  ? 1.3934 1.3934 1.3934 0.0000  0.0000  0.0000  666  GLN A NE2 
5296  N N   . LYS B 670  ? 1.4146 1.4146 1.4146 0.0000  0.0000  0.0000  667  LYS A N   
5297  C CA  . LYS B 670  ? 1.4146 1.4146 1.4146 0.0000  0.0000  0.0000  667  LYS A CA  
5298  C C   . LYS B 670  ? 1.4146 1.4146 1.4146 0.0000  0.0000  0.0000  667  LYS A C   
5299  O O   . LYS B 670  ? 1.4146 1.4146 1.4146 0.0000  0.0000  0.0000  667  LYS A O   
5305  N N   . GLY B 671  ? 1.3736 1.3736 1.3736 0.0000  0.0000  0.0000  668  GLY A N   
5306  C CA  . GLY B 671  ? 1.3736 1.3736 1.3736 0.0000  0.0000  0.0000  668  GLY A CA  
5307  C C   . GLY B 671  ? 1.3736 1.3736 1.3736 0.0000  0.0000  0.0000  668  GLY A C   
5308  O O   . GLY B 671  ? 1.3736 1.3736 1.3736 0.0000  0.0000  0.0000  668  GLY A O   
5309  N N   . TYR B 672  ? 1.3531 1.3531 1.3531 0.0000  0.0000  0.0000  669  TYR A N   
5310  C CA  . TYR B 672  ? 1.3531 1.3531 1.3531 0.0000  0.0000  0.0000  669  TYR A CA  
5311  C C   . TYR B 672  ? 1.3531 1.3531 1.3531 0.0000  0.0000  0.0000  669  TYR A C   
5312  O O   . TYR B 672  ? 1.3531 1.3531 1.3531 0.0000  0.0000  0.0000  669  TYR A O   
5313  C CB  . TYR B 672  ? 1.3531 1.3531 1.3531 0.0000  0.0000  0.0000  669  TYR A CB  
5314  C CG  . TYR B 672  ? 1.3531 1.3531 1.3531 0.0000  0.0000  0.0000  669  TYR A CG  
5315  C CD1 . TYR B 672  ? 1.3531 1.3531 1.3531 0.0000  0.0000  0.0000  669  TYR A CD1 
5316  C CD2 . TYR B 672  ? 1.3531 1.3531 1.3531 0.0000  0.0000  0.0000  669  TYR A CD2 
5317  C CE1 . TYR B 672  ? 1.3531 1.3531 1.3531 0.0000  0.0000  0.0000  669  TYR A CE1 
5318  C CE2 . TYR B 672  ? 1.3531 1.3531 1.3531 0.0000  0.0000  0.0000  669  TYR A CE2 
5319  C CZ  . TYR B 672  ? 1.3531 1.3531 1.3531 0.0000  0.0000  0.0000  669  TYR A CZ  
5320  O OH  . TYR B 672  ? 1.3531 1.3531 1.3531 0.0000  0.0000  0.0000  669  TYR A OH  
5321  N N   . ARG B 673  ? 1.3088 1.3088 1.3088 0.0000  0.0000  0.0000  670  ARG A N   
5322  C CA  . ARG B 673  ? 1.3088 1.3088 1.3088 0.0000  0.0000  0.0000  670  ARG A CA  
5323  C C   . ARG B 673  ? 1.3088 1.3088 1.3088 0.0000  0.0000  0.0000  670  ARG A C   
5324  O O   . ARG B 673  ? 1.3088 1.3088 1.3088 0.0000  0.0000  0.0000  670  ARG A O   
5325  C CB  . ARG B 673  ? 1.3088 1.3088 1.3088 0.0000  0.0000  0.0000  670  ARG A CB  
5326  C CG  . ARG B 673  ? 1.3088 1.3088 1.3088 0.0000  0.0000  0.0000  670  ARG A CG  
5327  C CD  . ARG B 673  ? 1.3088 1.3088 1.3088 0.0000  0.0000  0.0000  670  ARG A CD  
5328  N NE  . ARG B 673  ? 1.3088 1.3088 1.3088 0.0000  0.0000  0.0000  670  ARG A NE  
5329  C CZ  . ARG B 673  ? 1.3088 1.3088 1.3088 0.0000  0.0000  0.0000  670  ARG A CZ  
5330  N NH1 . ARG B 673  ? 1.3088 1.3088 1.3088 0.0000  0.0000  0.0000  670  ARG A NH1 
5331  N NH2 . ARG B 673  ? 1.3088 1.3088 1.3088 0.0000  0.0000  0.0000  670  ARG A NH2 
5332  N N   . GLU B 674  ? 1.2833 1.2833 1.2833 0.0000  0.0000  0.0000  671  GLU A N   
5333  C CA  . GLU B 674  ? 1.2833 1.2833 1.2833 0.0000  0.0000  0.0000  671  GLU A CA  
5334  C C   . GLU B 674  ? 1.2833 1.2833 1.2833 0.0000  0.0000  0.0000  671  GLU A C   
5335  O O   . GLU B 674  ? 1.2833 1.2833 1.2833 0.0000  0.0000  0.0000  671  GLU A O   
5336  C CB  . GLU B 674  ? 1.2833 1.2833 1.2833 0.0000  0.0000  0.0000  671  GLU A CB  
5337  C CG  . GLU B 674  ? 1.2833 1.2833 1.2833 0.0000  0.0000  0.0000  671  GLU A CG  
5338  C CD  . GLU B 674  ? 1.2833 1.2833 1.2833 0.0000  0.0000  0.0000  671  GLU A CD  
5339  O OE1 . GLU B 674  ? 1.2833 1.2833 1.2833 0.0000  0.0000  0.0000  671  GLU A OE1 
5340  O OE2 . GLU B 674  ? 1.2833 1.2833 1.2833 0.0000  0.0000  0.0000  671  GLU A OE2 
5341  N N   . ALA B 675  ? 1.2670 1.2670 1.2670 0.0000  0.0000  0.0000  672  ALA A N   
5342  C CA  . ALA B 675  ? 1.2670 1.2670 1.2670 0.0000  0.0000  0.0000  672  ALA A CA  
5343  C C   . ALA B 675  ? 1.2670 1.2670 1.2670 0.0000  0.0000  0.0000  672  ALA A C   
5344  O O   . ALA B 675  ? 1.2670 1.2670 1.2670 0.0000  0.0000  0.0000  672  ALA A O   
5345  C CB  . ALA B 675  ? 1.2670 1.2670 1.2670 0.0000  0.0000  0.0000  672  ALA A CB  
5346  N N   . LEU B 676  ? 1.2134 1.2134 1.2134 0.0000  0.0000  0.0000  673  LEU A N   
5347  C CA  . LEU B 676  ? 1.2134 1.2134 1.2134 0.0000  0.0000  0.0000  673  LEU A CA  
5348  C C   . LEU B 676  ? 1.2134 1.2134 1.2134 0.0000  0.0000  0.0000  673  LEU A C   
5349  O O   . LEU B 676  ? 1.2134 1.2134 1.2134 0.0000  0.0000  0.0000  673  LEU A O   
5350  C CB  . LEU B 676  ? 1.2134 1.2134 1.2134 0.0000  0.0000  0.0000  673  LEU A CB  
5351  C CG  . LEU B 676  ? 1.2134 1.2134 1.2134 0.0000  0.0000  0.0000  673  LEU A CG  
5352  C CD1 . LEU B 676  ? 1.2134 1.2134 1.2134 0.0000  0.0000  0.0000  673  LEU A CD1 
5353  C CD2 . LEU B 676  ? 1.2134 1.2134 1.2134 0.0000  0.0000  0.0000  673  LEU A CD2 
5354  N N   . CYS B 677  ? 1.2294 1.2294 1.2294 0.0000  0.0000  0.0000  674  CYS A N   
5355  C CA  . CYS B 677  ? 1.2294 1.2294 1.2294 0.0000  0.0000  0.0000  674  CYS A CA  
5356  C C   . CYS B 677  ? 1.2294 1.2294 1.2294 0.0000  0.0000  0.0000  674  CYS A C   
5357  O O   . CYS B 677  ? 1.2294 1.2294 1.2294 0.0000  0.0000  0.0000  674  CYS A O   
5358  C CB  . CYS B 677  ? 1.2294 1.2294 1.2294 0.0000  0.0000  0.0000  674  CYS A CB  
5359  S SG  . CYS B 677  ? 1.2294 1.2294 1.2294 0.0000  0.0000  0.0000  674  CYS A SG  
5360  N N   . LYS B 678  ? 1.2082 1.2082 1.2082 0.0000  0.0000  0.0000  675  LYS A N   
5361  C CA  . LYS B 678  ? 1.2082 1.2082 1.2082 0.0000  0.0000  0.0000  675  LYS A CA  
5362  C C   . LYS B 678  ? 1.2082 1.2082 1.2082 0.0000  0.0000  0.0000  675  LYS A C   
5363  O O   . LYS B 678  ? 1.2082 1.2082 1.2082 0.0000  0.0000  0.0000  675  LYS A O   
5364  C CB  . LYS B 678  ? 1.2082 1.2082 1.2082 0.0000  0.0000  0.0000  675  LYS A CB  
5365  C CG  . LYS B 678  ? 1.2082 1.2082 1.2082 0.0000  0.0000  0.0000  675  LYS A CG  
5366  C CD  . LYS B 678  ? 1.2082 1.2082 1.2082 0.0000  0.0000  0.0000  675  LYS A CD  
5367  C CE  . LYS B 678  ? 1.2082 1.2082 1.2082 0.0000  0.0000  0.0000  675  LYS A CE  
5368  N NZ  . LYS B 678  ? 1.2082 1.2082 1.2082 0.0000  0.0000  0.0000  675  LYS A NZ  
5369  N N   . TRP B 679  ? 1.1755 1.1755 1.1755 0.0000  0.0000  0.0000  676  TRP A N   
5370  C CA  . TRP B 679  ? 1.1755 1.1755 1.1755 0.0000  0.0000  0.0000  676  TRP A CA  
5371  C C   . TRP B 679  ? 1.1755 1.1755 1.1755 0.0000  0.0000  0.0000  676  TRP A C   
5372  O O   . TRP B 679  ? 1.1755 1.1755 1.1755 0.0000  0.0000  0.0000  676  TRP A O   
5373  C CB  . TRP B 679  ? 1.1755 1.1755 1.1755 0.0000  0.0000  0.0000  676  TRP A CB  
5374  C CG  . TRP B 679  ? 1.1755 1.1755 1.1755 0.0000  0.0000  0.0000  676  TRP A CG  
5375  C CD1 . TRP B 679  ? 1.1755 1.1755 1.1755 0.0000  0.0000  0.0000  676  TRP A CD1 
5376  C CD2 . TRP B 679  ? 1.1755 1.1755 1.1755 0.0000  0.0000  0.0000  676  TRP A CD2 
5377  N NE1 . TRP B 679  ? 1.1755 1.1755 1.1755 0.0000  0.0000  0.0000  676  TRP A NE1 
5378  C CE2 . TRP B 679  ? 1.1755 1.1755 1.1755 0.0000  0.0000  0.0000  676  TRP A CE2 
5379  C CE3 . TRP B 679  ? 1.1755 1.1755 1.1755 0.0000  0.0000  0.0000  676  TRP A CE3 
5380  C CZ2 . TRP B 679  ? 1.1755 1.1755 1.1755 0.0000  0.0000  0.0000  676  TRP A CZ2 
5381  C CZ3 . TRP B 679  ? 1.1755 1.1755 1.1755 0.0000  0.0000  0.0000  676  TRP A CZ3 
5382  C CH2 . TRP B 679  ? 1.1755 1.1755 1.1755 0.0000  0.0000  0.0000  676  TRP A CH2 
5383  N N   . ILE B 680  ? 1.1339 1.1339 1.1339 0.0000  0.0000  0.0000  677  ILE A N   
5384  C CA  . ILE B 680  ? 1.1339 1.1339 1.1339 0.0000  0.0000  0.0000  677  ILE A CA  
5385  C C   . ILE B 680  ? 1.1339 1.1339 1.1339 0.0000  0.0000  0.0000  677  ILE A C   
5386  O O   . ILE B 680  ? 1.1339 1.1339 1.1339 0.0000  0.0000  0.0000  677  ILE A O   
5387  C CB  . ILE B 680  ? 1.1339 1.1339 1.1339 0.0000  0.0000  0.0000  677  ILE A CB  
5388  C CG1 . ILE B 680  ? 1.1339 1.1339 1.1339 0.0000  0.0000  0.0000  677  ILE A CG1 
5389  C CG2 . ILE B 680  ? 1.1339 1.1339 1.1339 0.0000  0.0000  0.0000  677  ILE A CG2 
5390  C CD1 . ILE B 680  ? 1.1339 1.1339 1.1339 0.0000  0.0000  0.0000  677  ILE A CD1 
5391  N N   . ASP B 681  ? 1.1499 1.1499 1.1499 0.0000  0.0000  0.0000  678  ASP A N   
5392  C CA  . ASP B 681  ? 1.1499 1.1499 1.1499 0.0000  0.0000  0.0000  678  ASP A CA  
5393  C C   . ASP B 681  ? 1.1499 1.1499 1.1499 0.0000  0.0000  0.0000  678  ASP A C   
5394  O O   . ASP B 681  ? 1.1499 1.1499 1.1499 0.0000  0.0000  0.0000  678  ASP A O   
5395  C CB  . ASP B 681  ? 1.1499 1.1499 1.1499 0.0000  0.0000  0.0000  678  ASP A CB  
5396  C CG  . ASP B 681  ? 1.1499 1.1499 1.1499 0.0000  0.0000  0.0000  678  ASP A CG  
5397  O OD1 . ASP B 681  ? 1.1499 1.1499 1.1499 0.0000  0.0000  0.0000  678  ASP A OD1 
5398  O OD2 . ASP B 681  ? 1.1499 1.1499 1.1499 0.0000  0.0000  0.0000  678  ASP A OD2 
5399  N N   . PHE B 682  ? 1.1373 1.1373 1.1373 0.0000  0.0000  0.0000  679  PHE A N   
5400  C CA  . PHE B 682  ? 1.1373 1.1373 1.1373 0.0000  0.0000  0.0000  679  PHE A CA  
5401  C C   . PHE B 682  ? 1.1373 1.1373 1.1373 0.0000  0.0000  0.0000  679  PHE A C   
5402  O O   . PHE B 682  ? 1.1373 1.1373 1.1373 0.0000  0.0000  0.0000  679  PHE A O   
5403  C CB  . PHE B 682  ? 1.1373 1.1373 1.1373 0.0000  0.0000  0.0000  679  PHE A CB  
5404  C CG  . PHE B 682  ? 1.1373 1.1373 1.1373 0.0000  0.0000  0.0000  679  PHE A CG  
5405  C CD1 . PHE B 682  ? 1.1373 1.1373 1.1373 0.0000  0.0000  0.0000  679  PHE A CD1 
5406  C CD2 . PHE B 682  ? 1.1373 1.1373 1.1373 0.0000  0.0000  0.0000  679  PHE A CD2 
5407  C CE1 . PHE B 682  ? 1.1373 1.1373 1.1373 0.0000  0.0000  0.0000  679  PHE A CE1 
5408  C CE2 . PHE B 682  ? 1.1373 1.1373 1.1373 0.0000  0.0000  0.0000  679  PHE A CE2 
5409  C CZ  . PHE B 682  ? 1.1373 1.1373 1.1373 0.0000  0.0000  0.0000  679  PHE A CZ  
5410  N N   . THR B 683  ? 1.0842 1.0842 1.0842 0.0000  0.0000  0.0000  680  THR A N   
5411  C CA  . THR B 683  ? 1.0842 1.0842 1.0842 0.0000  0.0000  0.0000  680  THR A CA  
5412  C C   . THR B 683  ? 1.0842 1.0842 1.0842 0.0000  0.0000  0.0000  680  THR A C   
5413  O O   . THR B 683  ? 1.0842 1.0842 1.0842 0.0000  0.0000  0.0000  680  THR A O   
5414  C CB  . THR B 683  ? 1.0842 1.0842 1.0842 0.0000  0.0000  0.0000  680  THR A CB  
5415  O OG1 . THR B 683  ? 1.0842 1.0842 1.0842 0.0000  0.0000  0.0000  680  THR A OG1 
5416  C CG2 . THR B 683  ? 1.0842 1.0842 1.0842 0.0000  0.0000  0.0000  680  THR A CG2 
5417  N N   . ARG B 684  ? 1.1329 1.1329 1.1329 0.0000  0.0000  0.0000  681  ARG A N   
5418  C CA  . ARG B 684  ? 1.1329 1.1329 1.1329 0.0000  0.0000  0.0000  681  ARG A CA  
5419  C C   . ARG B 684  ? 1.1329 1.1329 1.1329 0.0000  0.0000  0.0000  681  ARG A C   
5420  O O   . ARG B 684  ? 1.1329 1.1329 1.1329 0.0000  0.0000  0.0000  681  ARG A O   
5421  C CB  . ARG B 684  ? 1.1329 1.1329 1.1329 0.0000  0.0000  0.0000  681  ARG A CB  
5422  C CG  . ARG B 684  ? 1.1329 1.1329 1.1329 0.0000  0.0000  0.0000  681  ARG A CG  
5423  C CD  . ARG B 684  ? 1.1329 1.1329 1.1329 0.0000  0.0000  0.0000  681  ARG A CD  
5424  N NE  . ARG B 684  ? 1.1329 1.1329 1.1329 0.0000  0.0000  0.0000  681  ARG A NE  
5425  C CZ  . ARG B 684  ? 1.1329 1.1329 1.1329 0.0000  0.0000  0.0000  681  ARG A CZ  
5426  N NH1 . ARG B 684  ? 1.1329 1.1329 1.1329 0.0000  0.0000  0.0000  681  ARG A NH1 
5427  N NH2 . ARG B 684  ? 1.1329 1.1329 1.1329 0.0000  0.0000  0.0000  681  ARG A NH2 
5428  N N   . ASP B 685  ? 1.1196 1.1196 1.1196 0.0000  0.0000  0.0000  682  ASP A N   
5429  C CA  . ASP B 685  ? 1.1196 1.1196 1.1196 0.0000  0.0000  0.0000  682  ASP A CA  
5430  C C   . ASP B 685  ? 1.1196 1.1196 1.1196 0.0000  0.0000  0.0000  682  ASP A C   
5431  O O   . ASP B 685  ? 1.1196 1.1196 1.1196 0.0000  0.0000  0.0000  682  ASP A O   
5432  C CB  . ASP B 685  ? 1.1196 1.1196 1.1196 0.0000  0.0000  0.0000  682  ASP A CB  
5433  C CG  . ASP B 685  ? 1.1196 1.1196 1.1196 0.0000  0.0000  0.0000  682  ASP A CG  
5434  O OD1 . ASP B 685  ? 1.1196 1.1196 1.1196 0.0000  0.0000  0.0000  682  ASP A OD1 
5435  O OD2 . ASP B 685  ? 1.1196 1.1196 1.1196 0.0000  0.0000  0.0000  682  ASP A OD2 
5436  N N   . PHE B 686  ? 1.0542 1.0542 1.0542 0.0000  0.0000  0.0000  683  PHE A N   
5437  C CA  . PHE B 686  ? 1.0542 1.0542 1.0542 0.0000  0.0000  0.0000  683  PHE A CA  
5438  C C   . PHE B 686  ? 1.0542 1.0542 1.0542 0.0000  0.0000  0.0000  683  PHE A C   
5439  O O   . PHE B 686  ? 1.0542 1.0542 1.0542 0.0000  0.0000  0.0000  683  PHE A O   
5440  C CB  . PHE B 686  ? 1.0542 1.0542 1.0542 0.0000  0.0000  0.0000  683  PHE A CB  
5441  C CG  . PHE B 686  ? 1.0542 1.0542 1.0542 0.0000  0.0000  0.0000  683  PHE A CG  
5442  C CD1 . PHE B 686  ? 1.0542 1.0542 1.0542 0.0000  0.0000  0.0000  683  PHE A CD1 
5443  C CD2 . PHE B 686  ? 1.0542 1.0542 1.0542 0.0000  0.0000  0.0000  683  PHE A CD2 
5444  C CE1 . PHE B 686  ? 1.0542 1.0542 1.0542 0.0000  0.0000  0.0000  683  PHE A CE1 
5445  C CE2 . PHE B 686  ? 1.0542 1.0542 1.0542 0.0000  0.0000  0.0000  683  PHE A CE2 
5446  C CZ  . PHE B 686  ? 1.0542 1.0542 1.0542 0.0000  0.0000  0.0000  683  PHE A CZ  
5447  N N   . LEU B 687  ? 1.0330 1.0330 1.0330 0.0000  0.0000  0.0000  684  LEU A N   
5448  C CA  . LEU B 687  ? 1.0330 1.0330 1.0330 0.0000  0.0000  0.0000  684  LEU A CA  
5449  C C   . LEU B 687  ? 1.0330 1.0330 1.0330 0.0000  0.0000  0.0000  684  LEU A C   
5450  O O   . LEU B 687  ? 1.0330 1.0330 1.0330 0.0000  0.0000  0.0000  684  LEU A O   
5451  C CB  . LEU B 687  ? 1.0330 1.0330 1.0330 0.0000  0.0000  0.0000  684  LEU A CB  
5452  C CG  . LEU B 687  ? 1.0330 1.0330 1.0330 0.0000  0.0000  0.0000  684  LEU A CG  
5453  C CD1 . LEU B 687  ? 1.0330 1.0330 1.0330 0.0000  0.0000  0.0000  684  LEU A CD1 
5454  C CD2 . LEU B 687  ? 1.0330 1.0330 1.0330 0.0000  0.0000  0.0000  684  LEU A CD2 
5455  N N   . SER B 688  ? 1.0803 1.0803 1.0803 0.0000  0.0000  0.0000  685  SER A N   
5456  C CA  . SER B 688  ? 1.0803 1.0803 1.0803 0.0000  0.0000  0.0000  685  SER A CA  
5457  C C   . SER B 688  ? 1.0803 1.0803 1.0803 0.0000  0.0000  0.0000  685  SER A C   
5458  O O   . SER B 688  ? 1.0803 1.0803 1.0803 0.0000  0.0000  0.0000  685  SER A O   
5459  C CB  . SER B 688  ? 1.0803 1.0803 1.0803 0.0000  0.0000  0.0000  685  SER A CB  
5460  O OG  . SER B 688  ? 1.0803 1.0803 1.0803 0.0000  0.0000  0.0000  685  SER A OG  
5461  N N   . LYS B 689  ? 1.1251 1.1251 1.1251 0.0000  0.0000  0.0000  686  LYS A N   
5462  C CA  . LYS B 689  ? 1.1251 1.1251 1.1251 0.0000  0.0000  0.0000  686  LYS A CA  
5463  C C   . LYS B 689  ? 1.1251 1.1251 1.1251 0.0000  0.0000  0.0000  686  LYS A C   
5464  O O   . LYS B 689  ? 1.1251 1.1251 1.1251 0.0000  0.0000  0.0000  686  LYS A O   
5465  C CB  . LYS B 689  ? 1.1251 1.1251 1.1251 0.0000  0.0000  0.0000  686  LYS A CB  
5466  C CG  . LYS B 689  ? 1.1251 1.1251 1.1251 0.0000  0.0000  0.0000  686  LYS A CG  
5467  C CD  . LYS B 689  ? 1.1251 1.1251 1.1251 0.0000  0.0000  0.0000  686  LYS A CD  
5468  C CE  . LYS B 689  ? 1.1251 1.1251 1.1251 0.0000  0.0000  0.0000  686  LYS A CE  
5469  N NZ  . LYS B 689  ? 1.1251 1.1251 1.1251 0.0000  0.0000  0.0000  686  LYS A NZ  
5470  N N   . TYR B 690  ? 0.9692 0.9692 0.9692 0.0000  0.0000  0.0000  687  TYR A N   
5471  C CA  . TYR B 690  ? 0.9692 0.9692 0.9692 0.0000  0.0000  0.0000  687  TYR A CA  
5472  C C   . TYR B 690  ? 0.9692 0.9692 0.9692 0.0000  0.0000  0.0000  687  TYR A C   
5473  O O   . TYR B 690  ? 0.9692 0.9692 0.9692 0.0000  0.0000  0.0000  687  TYR A O   
5474  C CB  . TYR B 690  ? 0.9692 0.9692 0.9692 0.0000  0.0000  0.0000  687  TYR A CB  
5475  C CG  . TYR B 690  ? 0.9692 0.9692 0.9692 0.0000  0.0000  0.0000  687  TYR A CG  
5476  C CD1 . TYR B 690  ? 0.9692 0.9692 0.9692 0.0000  0.0000  0.0000  687  TYR A CD1 
5477  C CD2 . TYR B 690  ? 0.9692 0.9692 0.9692 0.0000  0.0000  0.0000  687  TYR A CD2 
5478  C CE1 . TYR B 690  ? 0.9692 0.9692 0.9692 0.0000  0.0000  0.0000  687  TYR A CE1 
5479  C CE2 . TYR B 690  ? 0.9692 0.9692 0.9692 0.0000  0.0000  0.0000  687  TYR A CE2 
5480  C CZ  . TYR B 690  ? 0.9692 0.9692 0.9692 0.0000  0.0000  0.0000  687  TYR A CZ  
5481  O OH  . TYR B 690  ? 0.9692 0.9692 0.9692 0.0000  0.0000  0.0000  687  TYR A OH  
5482  N N   . THR B 691  ? 1.0009 1.0009 1.0009 0.0000  0.0000  0.0000  688  THR A N   
5483  C CA  . THR B 691  ? 1.0009 1.0009 1.0009 0.0000  0.0000  0.0000  688  THR A CA  
5484  C C   . THR B 691  ? 1.0009 1.0009 1.0009 0.0000  0.0000  0.0000  688  THR A C   
5485  O O   . THR B 691  ? 1.0009 1.0009 1.0009 0.0000  0.0000  0.0000  688  THR A O   
5486  C CB  . THR B 691  ? 1.0009 1.0009 1.0009 0.0000  0.0000  0.0000  688  THR A CB  
5487  O OG1 . THR B 691  ? 1.0009 1.0009 1.0009 0.0000  0.0000  0.0000  688  THR A OG1 
5488  C CG2 . THR B 691  ? 1.0009 1.0009 1.0009 0.0000  0.0000  0.0000  688  THR A CG2 
5489  N N   . LYS B 692  ? 0.9664 0.9664 0.9664 0.0000  0.0000  0.0000  689  LYS A N   
5490  C CA  . LYS B 692  ? 0.9664 0.9664 0.9664 0.0000  0.0000  0.0000  689  LYS A CA  
5491  C C   . LYS B 692  ? 0.9664 0.9664 0.9664 0.0000  0.0000  0.0000  689  LYS A C   
5492  O O   . LYS B 692  ? 0.9664 0.9664 0.9664 0.0000  0.0000  0.0000  689  LYS A O   
5493  C CB  . LYS B 692  ? 0.9664 0.9664 0.9664 0.0000  0.0000  0.0000  689  LYS A CB  
5494  C CG  . LYS B 692  ? 0.9664 0.9664 0.9664 0.0000  0.0000  0.0000  689  LYS A CG  
5495  C CD  . LYS B 692  ? 0.9664 0.9664 0.9664 0.0000  0.0000  0.0000  689  LYS A CD  
5496  C CE  . LYS B 692  ? 0.9664 0.9664 0.9664 0.0000  0.0000  0.0000  689  LYS A CE  
5497  N NZ  . LYS B 692  ? 0.9664 0.9664 0.9664 0.0000  0.0000  0.0000  689  LYS A NZ  
5498  N N   . THR B 693  ? 1.0618 1.0618 1.0618 0.0000  0.0000  0.0000  690  THR A N   
5499  C CA  . THR B 693  ? 1.0618 1.0618 1.0618 0.0000  0.0000  0.0000  690  THR A CA  
5500  C C   . THR B 693  ? 1.0618 1.0618 1.0618 0.0000  0.0000  0.0000  690  THR A C   
5501  O O   . THR B 693  ? 1.0618 1.0618 1.0618 0.0000  0.0000  0.0000  690  THR A O   
5502  C CB  . THR B 693  ? 1.0618 1.0618 1.0618 0.0000  0.0000  0.0000  690  THR A CB  
5503  O OG1 . THR B 693  ? 1.0618 1.0618 1.0618 0.0000  0.0000  0.0000  690  THR A OG1 
5504  C CG2 . THR B 693  ? 1.0618 1.0618 1.0618 0.0000  0.0000  0.0000  690  THR A CG2 
5505  N N   . THR B 694  ? 1.1363 1.1363 1.1363 0.0000  0.0000  0.0000  691  THR A N   
5506  C CA  . THR B 694  ? 1.1363 1.1363 1.1363 0.0000  0.0000  0.0000  691  THR A CA  
5507  C C   . THR B 694  ? 1.1363 1.1363 1.1363 0.0000  0.0000  0.0000  691  THR A C   
5508  O O   . THR B 694  ? 1.1363 1.1363 1.1363 0.0000  0.0000  0.0000  691  THR A O   
5509  C CB  . THR B 694  ? 1.1363 1.1363 1.1363 0.0000  0.0000  0.0000  691  THR A CB  
5510  O OG1 . THR B 694  ? 1.1363 1.1363 1.1363 0.0000  0.0000  0.0000  691  THR A OG1 
5511  C CG2 . THR B 694  ? 1.1363 1.1363 1.1363 0.0000  0.0000  0.0000  691  THR A CG2 
5512  N N   . SER B 695  ? 1.1709 1.1709 1.1709 0.0000  0.0000  0.0000  692  SER A N   
5513  C CA  . SER B 695  ? 1.1709 1.1709 1.1709 0.0000  0.0000  0.0000  692  SER A CA  
5514  C C   . SER B 695  ? 1.1709 1.1709 1.1709 0.0000  0.0000  0.0000  692  SER A C   
5515  O O   . SER B 695  ? 1.1709 1.1709 1.1709 0.0000  0.0000  0.0000  692  SER A O   
5516  C CB  . SER B 695  ? 1.1709 1.1709 1.1709 0.0000  0.0000  0.0000  692  SER A CB  
5517  O OG  . SER B 695  ? 1.1709 1.1709 1.1709 0.0000  0.0000  0.0000  692  SER A OG  
5518  N N   . ILE B 696  ? 1.1778 1.1778 1.1778 0.0000  0.0000  0.0000  693  ILE A N   
5519  C CA  . ILE B 696  ? 1.1778 1.1778 1.1778 0.0000  0.0000  0.0000  693  ILE A CA  
5520  C C   . ILE B 696  ? 1.1778 1.1778 1.1778 0.0000  0.0000  0.0000  693  ILE A C   
5521  O O   . ILE B 696  ? 1.1778 1.1778 1.1778 0.0000  0.0000  0.0000  693  ILE A O   
5522  C CB  . ILE B 696  ? 1.1778 1.1778 1.1778 0.0000  0.0000  0.0000  693  ILE A CB  
5523  C CG1 . ILE B 696  ? 1.1778 1.1778 1.1778 0.0000  0.0000  0.0000  693  ILE A CG1 
5524  C CG2 . ILE B 696  ? 1.1778 1.1778 1.1778 0.0000  0.0000  0.0000  693  ILE A CG2 
5525  C CD1 . ILE B 696  ? 1.1778 1.1778 1.1778 0.0000  0.0000  0.0000  693  ILE A CD1 
5526  N N   . ASP B 697  ? 1.2801 1.2801 1.2801 0.0000  0.0000  0.0000  694  ASP A N   
5527  C CA  . ASP B 697  ? 1.2801 1.2801 1.2801 0.0000  0.0000  0.0000  694  ASP A CA  
5528  C C   . ASP B 697  ? 1.2801 1.2801 1.2801 0.0000  0.0000  0.0000  694  ASP A C   
5529  O O   . ASP B 697  ? 1.2801 1.2801 1.2801 0.0000  0.0000  0.0000  694  ASP A O   
5530  C CB  . ASP B 697  ? 1.2801 1.2801 1.2801 0.0000  0.0000  0.0000  694  ASP A CB  
5531  C CG  . ASP B 697  ? 1.2801 1.2801 1.2801 0.0000  0.0000  0.0000  694  ASP A CG  
5532  O OD1 . ASP B 697  ? 1.2801 1.2801 1.2801 0.0000  0.0000  0.0000  694  ASP A OD1 
5533  O OD2 . ASP B 697  ? 1.2801 1.2801 1.2801 0.0000  0.0000  0.0000  694  ASP A OD2 
5534  N N   . LEU B 698  ? 1.2932 1.2932 1.2932 0.0000  0.0000  0.0000  695  LEU A N   
5535  C CA  . LEU B 698  ? 1.2932 1.2932 1.2932 0.0000  0.0000  0.0000  695  LEU A CA  
5536  C C   . LEU B 698  ? 1.2932 1.2932 1.2932 0.0000  0.0000  0.0000  695  LEU A C   
5537  O O   . LEU B 698  ? 1.2932 1.2932 1.2932 0.0000  0.0000  0.0000  695  LEU A O   
5538  C CB  . LEU B 698  ? 1.2932 1.2932 1.2932 0.0000  0.0000  0.0000  695  LEU A CB  
5539  C CG  . LEU B 698  ? 1.2932 1.2932 1.2932 0.0000  0.0000  0.0000  695  LEU A CG  
5540  C CD1 . LEU B 698  ? 1.2932 1.2932 1.2932 0.0000  0.0000  0.0000  695  LEU A CD1 
5541  C CD2 . LEU B 698  ? 1.2932 1.2932 1.2932 0.0000  0.0000  0.0000  695  LEU A CD2 
5542  N N   . SER B 699  ? 1.3436 1.3436 1.3436 0.0000  0.0000  0.0000  696  SER A N   
5543  C CA  . SER B 699  ? 1.3436 1.3436 1.3436 0.0000  0.0000  0.0000  696  SER A CA  
5544  C C   . SER B 699  ? 1.3436 1.3436 1.3436 0.0000  0.0000  0.0000  696  SER A C   
5545  O O   . SER B 699  ? 1.3436 1.3436 1.3436 0.0000  0.0000  0.0000  696  SER A O   
5546  C CB  . SER B 699  ? 1.3436 1.3436 1.3436 0.0000  0.0000  0.0000  696  SER A CB  
5547  O OG  . SER B 699  ? 1.3436 1.3436 1.3436 0.0000  0.0000  0.0000  696  SER A OG  
5548  N N   . SER B 700  ? 1.2858 1.2858 1.2858 0.0000  0.0000  0.0000  697  SER A N   
5549  C CA  . SER B 700  ? 1.2858 1.2858 1.2858 0.0000  0.0000  0.0000  697  SER A CA  
5550  C C   . SER B 700  ? 1.2858 1.2858 1.2858 0.0000  0.0000  0.0000  697  SER A C   
5551  O O   . SER B 700  ? 1.2858 1.2858 1.2858 0.0000  0.0000  0.0000  697  SER A O   
5552  C CB  . SER B 700  ? 1.2858 1.2858 1.2858 0.0000  0.0000  0.0000  697  SER A CB  
5553  O OG  . SER B 700  ? 1.2858 1.2858 1.2858 0.0000  0.0000  0.0000  697  SER A OG  
5554  N N   . LEU B 701  ? 1.1889 1.1889 1.1889 0.0000  0.0000  0.0000  698  LEU A N   
5555  C CA  . LEU B 701  ? 1.1889 1.1889 1.1889 0.0000  0.0000  0.0000  698  LEU A CA  
5556  C C   . LEU B 701  ? 1.1889 1.1889 1.1889 0.0000  0.0000  0.0000  698  LEU A C   
5557  O O   . LEU B 701  ? 1.1889 1.1889 1.1889 0.0000  0.0000  0.0000  698  LEU A O   
5558  C CB  . LEU B 701  ? 1.1889 1.1889 1.1889 0.0000  0.0000  0.0000  698  LEU A CB  
5559  C CG  . LEU B 701  ? 1.1889 1.1889 1.1889 0.0000  0.0000  0.0000  698  LEU A CG  
5560  C CD1 . LEU B 701  ? 1.1889 1.1889 1.1889 0.0000  0.0000  0.0000  698  LEU A CD1 
5561  C CD2 . LEU B 701  ? 1.1889 1.1889 1.1889 0.0000  0.0000  0.0000  698  LEU A CD2 
5562  N N   . ARG B 702  ? 1.1471 1.1471 1.1471 0.0000  0.0000  0.0000  699  ARG A N   
5563  C CA  . ARG B 702  ? 1.1471 1.1471 1.1471 0.0000  0.0000  0.0000  699  ARG A CA  
5564  C C   . ARG B 702  ? 1.1471 1.1471 1.1471 0.0000  0.0000  0.0000  699  ARG A C   
5565  O O   . ARG B 702  ? 1.1471 1.1471 1.1471 0.0000  0.0000  0.0000  699  ARG A O   
5566  C CB  . ARG B 702  ? 1.1471 1.1471 1.1471 0.0000  0.0000  0.0000  699  ARG A CB  
5567  C CG  . ARG B 702  ? 1.1471 1.1471 1.1471 0.0000  0.0000  0.0000  699  ARG A CG  
5568  C CD  . ARG B 702  ? 1.1471 1.1471 1.1471 0.0000  0.0000  0.0000  699  ARG A CD  
5569  N NE  . ARG B 702  ? 1.1471 1.1471 1.1471 0.0000  0.0000  0.0000  699  ARG A NE  
5570  C CZ  . ARG B 702  ? 1.1471 1.1471 1.1471 0.0000  0.0000  0.0000  699  ARG A CZ  
5571  N NH1 . ARG B 702  ? 1.1471 1.1471 1.1471 0.0000  0.0000  0.0000  699  ARG A NH1 
5572  N NH2 . ARG B 702  ? 1.1471 1.1471 1.1471 0.0000  0.0000  0.0000  699  ARG A NH2 
5573  N N   . PRO B 703  ? 1.1289 1.1289 1.1289 0.0000  0.0000  0.0000  700  PRO A N   
5574  C CA  . PRO B 703  ? 1.1289 1.1289 1.1289 0.0000  0.0000  0.0000  700  PRO A CA  
5575  C C   . PRO B 703  ? 1.1289 1.1289 1.1289 0.0000  0.0000  0.0000  700  PRO A C   
5576  O O   . PRO B 703  ? 1.1289 1.1289 1.1289 0.0000  0.0000  0.0000  700  PRO A O   
5577  C CB  . PRO B 703  ? 1.1289 1.1289 1.1289 0.0000  0.0000  0.0000  700  PRO A CB  
5578  C CG  . PRO B 703  ? 1.1289 1.1289 1.1289 0.0000  0.0000  0.0000  700  PRO A CG  
5579  C CD  . PRO B 703  ? 1.1289 1.1289 1.1289 0.0000  0.0000  0.0000  700  PRO A CD  
5580  N N   . SER B 704  ? 1.1718 1.1718 1.1718 0.0000  0.0000  0.0000  701  SER A N   
5581  C CA  . SER B 704  ? 1.1718 1.1718 1.1718 0.0000  0.0000  0.0000  701  SER A CA  
5582  C C   . SER B 704  ? 1.1718 1.1718 1.1718 0.0000  0.0000  0.0000  701  SER A C   
5583  O O   . SER B 704  ? 1.1718 1.1718 1.1718 0.0000  0.0000  0.0000  701  SER A O   
5584  C CB  . SER B 704  ? 1.1718 1.1718 1.1718 0.0000  0.0000  0.0000  701  SER A CB  
5585  O OG  . SER B 704  ? 1.1718 1.1718 1.1718 0.0000  0.0000  0.0000  701  SER A OG  
5586  N N   . SER B 705  ? 1.1929 1.1929 1.1929 0.0000  0.0000  0.0000  702  SER A N   
5587  C CA  . SER B 705  ? 1.1929 1.1929 1.1929 0.0000  0.0000  0.0000  702  SER A CA  
5588  C C   . SER B 705  ? 1.1929 1.1929 1.1929 0.0000  0.0000  0.0000  702  SER A C   
5589  O O   . SER B 705  ? 1.1929 1.1929 1.1929 0.0000  0.0000  0.0000  702  SER A O   
5590  C CB  . SER B 705  ? 1.1929 1.1929 1.1929 0.0000  0.0000  0.0000  702  SER A CB  
5591  O OG  . SER B 705  ? 1.1929 1.1929 1.1929 0.0000  0.0000  0.0000  702  SER A OG  
5592  N N   . GLN B 706  ? 1.1876 1.1876 1.1876 0.0000  0.0000  0.0000  703  GLN A N   
5593  C CA  . GLN B 706  ? 1.1876 1.1876 1.1876 0.0000  0.0000  0.0000  703  GLN A CA  
5594  C C   . GLN B 706  ? 1.1876 1.1876 1.1876 0.0000  0.0000  0.0000  703  GLN A C   
5595  O O   . GLN B 706  ? 1.1876 1.1876 1.1876 0.0000  0.0000  0.0000  703  GLN A O   
5596  C CB  . GLN B 706  ? 1.1876 1.1876 1.1876 0.0000  0.0000  0.0000  703  GLN A CB  
5597  C CG  . GLN B 706  ? 1.1876 1.1876 1.1876 0.0000  0.0000  0.0000  703  GLN A CG  
5598  C CD  . GLN B 706  ? 1.1876 1.1876 1.1876 0.0000  0.0000  0.0000  703  GLN A CD  
5599  O OE1 . GLN B 706  ? 1.1876 1.1876 1.1876 0.0000  0.0000  0.0000  703  GLN A OE1 
5600  N NE2 . GLN B 706  ? 1.1876 1.1876 1.1876 0.0000  0.0000  0.0000  703  GLN A NE2 
5601  N N   . TYR B 707  ? 1.1518 1.1518 1.1518 0.0000  0.0000  0.0000  704  TYR A N   
5602  C CA  . TYR B 707  ? 1.1518 1.1518 1.1518 0.0000  0.0000  0.0000  704  TYR A CA  
5603  C C   . TYR B 707  ? 1.1518 1.1518 1.1518 0.0000  0.0000  0.0000  704  TYR A C   
5604  O O   . TYR B 707  ? 1.1518 1.1518 1.1518 0.0000  0.0000  0.0000  704  TYR A O   
5605  C CB  . TYR B 707  ? 1.1518 1.1518 1.1518 0.0000  0.0000  0.0000  704  TYR A CB  
5606  C CG  . TYR B 707  ? 1.1518 1.1518 1.1518 0.0000  0.0000  0.0000  704  TYR A CG  
5607  C CD1 . TYR B 707  ? 1.1518 1.1518 1.1518 0.0000  0.0000  0.0000  704  TYR A CD1 
5608  C CD2 . TYR B 707  ? 1.1518 1.1518 1.1518 0.0000  0.0000  0.0000  704  TYR A CD2 
5609  C CE1 . TYR B 707  ? 1.1518 1.1518 1.1518 0.0000  0.0000  0.0000  704  TYR A CE1 
5610  C CE2 . TYR B 707  ? 1.1518 1.1518 1.1518 0.0000  0.0000  0.0000  704  TYR A CE2 
5611  C CZ  . TYR B 707  ? 1.1518 1.1518 1.1518 0.0000  0.0000  0.0000  704  TYR A CZ  
5612  O OH  . TYR B 707  ? 1.1518 1.1518 1.1518 0.0000  0.0000  0.0000  704  TYR A OH  
5613  N N   . LYS B 708  ? 1.1766 1.1766 1.1766 0.0000  0.0000  0.0000  705  LYS A N   
5614  C CA  . LYS B 708  ? 1.1766 1.1766 1.1766 0.0000  0.0000  0.0000  705  LYS A CA  
5615  C C   . LYS B 708  ? 1.1766 1.1766 1.1766 0.0000  0.0000  0.0000  705  LYS A C   
5616  O O   . LYS B 708  ? 1.1766 1.1766 1.1766 0.0000  0.0000  0.0000  705  LYS A O   
5617  C CB  . LYS B 708  ? 1.1766 1.1766 1.1766 0.0000  0.0000  0.0000  705  LYS A CB  
5618  C CG  . LYS B 708  ? 1.1766 1.1766 1.1766 0.0000  0.0000  0.0000  705  LYS A CG  
5619  C CD  . LYS B 708  ? 1.1766 1.1766 1.1766 0.0000  0.0000  0.0000  705  LYS A CD  
5620  C CE  . LYS B 708  ? 1.1766 1.1766 1.1766 0.0000  0.0000  0.0000  705  LYS A CE  
5621  N NZ  . LYS B 708  ? 1.1766 1.1766 1.1766 0.0000  0.0000  0.0000  705  LYS A NZ  
5622  N N   . ASP B 709  ? 1.1851 1.1851 1.1851 0.0000  0.0000  0.0000  706  ASP A N   
5623  C CA  . ASP B 709  ? 1.1851 1.1851 1.1851 0.0000  0.0000  0.0000  706  ASP A CA  
5624  C C   . ASP B 709  ? 1.1851 1.1851 1.1851 0.0000  0.0000  0.0000  706  ASP A C   
5625  O O   . ASP B 709  ? 1.1851 1.1851 1.1851 0.0000  0.0000  0.0000  706  ASP A O   
5626  C CB  . ASP B 709  ? 1.1851 1.1851 1.1851 0.0000  0.0000  0.0000  706  ASP A CB  
5627  C CG  . ASP B 709  ? 1.1851 1.1851 1.1851 0.0000  0.0000  0.0000  706  ASP A CG  
5628  O OD1 . ASP B 709  ? 1.1851 1.1851 1.1851 0.0000  0.0000  0.0000  706  ASP A OD1 
5629  O OD2 . ASP B 709  ? 1.1851 1.1851 1.1851 0.0000  0.0000  0.0000  706  ASP A OD2 
5630  N N   . LEU B 710  ? 1.1176 1.1176 1.1176 0.0000  0.0000  0.0000  707  LEU A N   
5631  C CA  . LEU B 710  ? 1.1176 1.1176 1.1176 0.0000  0.0000  0.0000  707  LEU A CA  
5632  C C   . LEU B 710  ? 1.1176 1.1176 1.1176 0.0000  0.0000  0.0000  707  LEU A C   
5633  O O   . LEU B 710  ? 1.1176 1.1176 1.1176 0.0000  0.0000  0.0000  707  LEU A O   
5634  C CB  . LEU B 710  ? 1.1176 1.1176 1.1176 0.0000  0.0000  0.0000  707  LEU A CB  
5635  C CG  . LEU B 710  ? 1.1176 1.1176 1.1176 0.0000  0.0000  0.0000  707  LEU A CG  
5636  C CD1 . LEU B 710  ? 1.1176 1.1176 1.1176 0.0000  0.0000  0.0000  707  LEU A CD1 
5637  C CD2 . LEU B 710  ? 1.1176 1.1176 1.1176 0.0000  0.0000  0.0000  707  LEU A CD2 
5638  N N   . GLY B 711  ? 1.1093 1.1093 1.1093 0.0000  0.0000  0.0000  708  GLY A N   
5639  C CA  . GLY B 711  ? 1.1093 1.1093 1.1093 0.0000  0.0000  0.0000  708  GLY A CA  
5640  C C   . GLY B 711  ? 1.1093 1.1093 1.1093 0.0000  0.0000  0.0000  708  GLY A C   
5641  O O   . GLY B 711  ? 1.1093 1.1093 1.1093 0.0000  0.0000  0.0000  708  GLY A O   
5642  N N   . GLU B 712  ? 1.1203 1.1203 1.1203 0.0000  0.0000  0.0000  709  GLU A N   
5643  C CA  . GLU B 712  ? 1.1203 1.1203 1.1203 0.0000  0.0000  0.0000  709  GLU A CA  
5644  C C   . GLU B 712  ? 1.1203 1.1203 1.1203 0.0000  0.0000  0.0000  709  GLU A C   
5645  O O   . GLU B 712  ? 1.1203 1.1203 1.1203 0.0000  0.0000  0.0000  709  GLU A O   
5646  C CB  . GLU B 712  ? 1.1203 1.1203 1.1203 0.0000  0.0000  0.0000  709  GLU A CB  
5647  C CG  . GLU B 712  ? 1.1203 1.1203 1.1203 0.0000  0.0000  0.0000  709  GLU A CG  
5648  C CD  . GLU B 712  ? 1.1203 1.1203 1.1203 0.0000  0.0000  0.0000  709  GLU A CD  
5649  O OE1 . GLU B 712  ? 1.1203 1.1203 1.1203 0.0000  0.0000  0.0000  709  GLU A OE1 
5650  O OE2 . GLU B 712  ? 1.1203 1.1203 1.1203 0.0000  0.0000  0.0000  709  GLU A OE2 
5651  N N   . TYR B 713  ? 1.0094 1.0094 1.0094 0.0000  0.0000  0.0000  710  TYR A N   
5652  C CA  . TYR B 713  ? 1.0094 1.0094 1.0094 0.0000  0.0000  0.0000  710  TYR A CA  
5653  C C   . TYR B 713  ? 1.0094 1.0094 1.0094 0.0000  0.0000  0.0000  710  TYR A C   
5654  O O   . TYR B 713  ? 1.0094 1.0094 1.0094 0.0000  0.0000  0.0000  710  TYR A O   
5655  C CB  . TYR B 713  ? 1.0094 1.0094 1.0094 0.0000  0.0000  0.0000  710  TYR A CB  
5656  C CG  . TYR B 713  ? 1.0094 1.0094 1.0094 0.0000  0.0000  0.0000  710  TYR A CG  
5657  C CD1 . TYR B 713  ? 1.0094 1.0094 1.0094 0.0000  0.0000  0.0000  710  TYR A CD1 
5658  C CD2 . TYR B 713  ? 1.0094 1.0094 1.0094 0.0000  0.0000  0.0000  710  TYR A CD2 
5659  C CE1 . TYR B 713  ? 1.0094 1.0094 1.0094 0.0000  0.0000  0.0000  710  TYR A CE1 
5660  C CE2 . TYR B 713  ? 1.0094 1.0094 1.0094 0.0000  0.0000  0.0000  710  TYR A CE2 
5661  C CZ  . TYR B 713  ? 1.0094 1.0094 1.0094 0.0000  0.0000  0.0000  710  TYR A CZ  
5662  O OH  . TYR B 713  ? 1.0094 1.0094 1.0094 0.0000  0.0000  0.0000  710  TYR A OH  
5663  N N   . TYR B 714  ? 0.9917 0.9917 0.9917 0.0000  0.0000  0.0000  711  TYR A N   
5664  C CA  . TYR B 714  ? 0.9917 0.9917 0.9917 0.0000  0.0000  0.0000  711  TYR A CA  
5665  C C   . TYR B 714  ? 0.9917 0.9917 0.9917 0.0000  0.0000  0.0000  711  TYR A C   
5666  O O   . TYR B 714  ? 0.9917 0.9917 0.9917 0.0000  0.0000  0.0000  711  TYR A O   
5667  C CB  . TYR B 714  ? 0.9917 0.9917 0.9917 0.0000  0.0000  0.0000  711  TYR A CB  
5668  C CG  . TYR B 714  ? 0.9917 0.9917 0.9917 0.0000  0.0000  0.0000  711  TYR A CG  
5669  C CD1 . TYR B 714  ? 0.9917 0.9917 0.9917 0.0000  0.0000  0.0000  711  TYR A CD1 
5670  C CD2 . TYR B 714  ? 0.9917 0.9917 0.9917 0.0000  0.0000  0.0000  711  TYR A CD2 
5671  C CE1 . TYR B 714  ? 0.9917 0.9917 0.9917 0.0000  0.0000  0.0000  711  TYR A CE1 
5672  C CE2 . TYR B 714  ? 0.9917 0.9917 0.9917 0.0000  0.0000  0.0000  711  TYR A CE2 
5673  C CZ  . TYR B 714  ? 0.9917 0.9917 0.9917 0.0000  0.0000  0.0000  711  TYR A CZ  
5674  O OH  . TYR B 714  ? 0.9917 0.9917 0.9917 0.0000  0.0000  0.0000  711  TYR A OH  
5675  N N   . ALA B 715  ? 0.9726 0.9726 0.9726 0.0000  0.0000  0.0000  712  ALA A N   
5676  C CA  . ALA B 715  ? 0.9726 0.9726 0.9726 0.0000  0.0000  0.0000  712  ALA A CA  
5677  C C   . ALA B 715  ? 0.9726 0.9726 0.9726 0.0000  0.0000  0.0000  712  ALA A C   
5678  O O   . ALA B 715  ? 0.9726 0.9726 0.9726 0.0000  0.0000  0.0000  712  ALA A O   
5679  C CB  . ALA B 715  ? 0.9726 0.9726 0.9726 0.0000  0.0000  0.0000  712  ALA A CB  
5680  N N   . GLU B 716  ? 0.9408 0.9408 0.9408 0.0000  0.0000  0.0000  713  GLU A N   
5681  C CA  . GLU B 716  ? 0.9408 0.9408 0.9408 0.0000  0.0000  0.0000  713  GLU A CA  
5682  C C   . GLU B 716  ? 0.9408 0.9408 0.9408 0.0000  0.0000  0.0000  713  GLU A C   
5683  O O   . GLU B 716  ? 0.9408 0.9408 0.9408 0.0000  0.0000  0.0000  713  GLU A O   
5684  C CB  . GLU B 716  ? 0.9408 0.9408 0.9408 0.0000  0.0000  0.0000  713  GLU A CB  
5685  C CG  . GLU B 716  ? 0.9408 0.9408 0.9408 0.0000  0.0000  0.0000  713  GLU A CG  
5686  C CD  . GLU B 716  ? 0.9408 0.9408 0.9408 0.0000  0.0000  0.0000  713  GLU A CD  
5687  O OE1 . GLU B 716  ? 0.9408 0.9408 0.9408 0.0000  0.0000  0.0000  713  GLU A OE1 
5688  O OE2 . GLU B 716  ? 0.9408 0.9408 0.9408 0.0000  0.0000  0.0000  713  GLU A OE2 
5689  N N   . LEU B 717  ? 0.8838 0.8838 0.8838 0.0000  0.0000  0.0000  714  LEU A N   
5690  C CA  . LEU B 717  ? 0.8838 0.8838 0.8838 0.0000  0.0000  0.0000  714  LEU A CA  
5691  C C   . LEU B 717  ? 0.8838 0.8838 0.8838 0.0000  0.0000  0.0000  714  LEU A C   
5692  O O   . LEU B 717  ? 0.8838 0.8838 0.8838 0.0000  0.0000  0.0000  714  LEU A O   
5693  C CB  . LEU B 717  ? 0.8838 0.8838 0.8838 0.0000  0.0000  0.0000  714  LEU A CB  
5694  C CG  . LEU B 717  ? 0.8838 0.8838 0.8838 0.0000  0.0000  0.0000  714  LEU A CG  
5695  C CD1 . LEU B 717  ? 0.8838 0.8838 0.8838 0.0000  0.0000  0.0000  714  LEU A CD1 
5696  C CD2 . LEU B 717  ? 0.8838 0.8838 0.8838 0.0000  0.0000  0.0000  714  LEU A CD2 
5697  N N   . ASN B 718  ? 0.7797 0.7797 0.7797 0.0000  0.0000  0.0000  715  ASN A N   
5698  C CA  . ASN B 718  ? 0.7797 0.7797 0.7797 0.0000  0.0000  0.0000  715  ASN A CA  
5699  C C   . ASN B 718  ? 0.7797 0.7797 0.7797 0.0000  0.0000  0.0000  715  ASN A C   
5700  O O   . ASN B 718  ? 0.7797 0.7797 0.7797 0.0000  0.0000  0.0000  715  ASN A O   
5701  C CB  . ASN B 718  ? 0.7797 0.7797 0.7797 0.0000  0.0000  0.0000  715  ASN A CB  
5702  C CG  . ASN B 718  ? 0.7797 0.7797 0.7797 0.0000  0.0000  0.0000  715  ASN A CG  
5703  O OD1 . ASN B 718  ? 0.7797 0.7797 0.7797 0.0000  0.0000  0.0000  715  ASN A OD1 
5704  N ND2 . ASN B 718  ? 0.7797 0.7797 0.7797 0.0000  0.0000  0.0000  715  ASN A ND2 
5705  N N   . PRO B 719  ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  716  PRO A N   
5706  C CA  . PRO B 719  ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  716  PRO A CA  
5707  C C   . PRO B 719  ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  716  PRO A C   
5708  O O   . PRO B 719  ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  716  PRO A O   
5709  C CB  . PRO B 719  ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  716  PRO A CB  
5710  C CG  . PRO B 719  ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  716  PRO A CG  
5711  C CD  . PRO B 719  ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  716  PRO A CD  
5712  N N   . LEU B 720  ? 0.6916 0.6916 0.6916 0.0000  0.0000  0.0000  717  LEU A N   
5713  C CA  . LEU B 720  ? 0.6916 0.6916 0.6916 0.0000  0.0000  0.0000  717  LEU A CA  
5714  C C   . LEU B 720  ? 0.6916 0.6916 0.6916 0.0000  0.0000  0.0000  717  LEU A C   
5715  O O   . LEU B 720  ? 0.6916 0.6916 0.6916 0.0000  0.0000  0.0000  717  LEU A O   
5716  C CB  . LEU B 720  ? 0.6916 0.6916 0.6916 0.0000  0.0000  0.0000  717  LEU A CB  
5717  C CG  . LEU B 720  ? 0.6916 0.6916 0.6916 0.0000  0.0000  0.0000  717  LEU A CG  
5718  C CD1 . LEU B 720  ? 0.6916 0.6916 0.6916 0.0000  0.0000  0.0000  717  LEU A CD1 
5719  C CD2 . LEU B 720  ? 0.6916 0.6916 0.6916 0.0000  0.0000  0.0000  717  LEU A CD2 
5720  N N   . LEU B 721  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  718  LEU A N   
5721  C CA  . LEU B 721  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  718  LEU A CA  
5722  C C   . LEU B 721  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  718  LEU A C   
5723  O O   . LEU B 721  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  718  LEU A O   
5724  C CB  . LEU B 721  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  718  LEU A CB  
5725  C CG  . LEU B 721  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  718  LEU A CG  
5726  C CD1 . LEU B 721  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  718  LEU A CD1 
5727  C CD2 . LEU B 721  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  718  LEU A CD2 
5728  N N   . TYR B 722  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  719  TYR A N   
5729  C CA  . TYR B 722  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  719  TYR A CA  
5730  C C   . TYR B 722  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  719  TYR A C   
5731  O O   . TYR B 722  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  719  TYR A O   
5732  C CB  . TYR B 722  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  719  TYR A CB  
5733  C CG  . TYR B 722  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  719  TYR A CG  
5734  C CD1 . TYR B 722  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  719  TYR A CD1 
5735  C CD2 . TYR B 722  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  719  TYR A CD2 
5736  C CE1 . TYR B 722  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  719  TYR A CE1 
5737  C CE2 . TYR B 722  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  719  TYR A CE2 
5738  C CZ  . TYR B 722  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  719  TYR A CZ  
5739  O OH  . TYR B 722  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  719  TYR A OH  
5740  N N   . HIS B 723  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  720  HIS A N   
5741  C CA  . HIS B 723  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  720  HIS A CA  
5742  C C   . HIS B 723  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  720  HIS A C   
5743  O O   . HIS B 723  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  720  HIS A O   
5744  C CB  . HIS B 723  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  720  HIS A CB  
5745  C CG  . HIS B 723  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  720  HIS A CG  
5746  N ND1 . HIS B 723  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  720  HIS A ND1 
5747  C CD2 . HIS B 723  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  720  HIS A CD2 
5748  C CE1 . HIS B 723  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  720  HIS A CE1 
5749  N NE2 . HIS B 723  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  720  HIS A NE2 
5750  N N   . ILE B 724  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  721  ILE A N   
5751  C CA  . ILE B 724  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  721  ILE A CA  
5752  C C   . ILE B 724  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  721  ILE A C   
5753  O O   . ILE B 724  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  721  ILE A O   
5754  C CB  . ILE B 724  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  721  ILE A CB  
5755  C CG1 . ILE B 724  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  721  ILE A CG1 
5756  C CG2 . ILE B 724  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  721  ILE A CG2 
5757  C CD1 . ILE B 724  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  721  ILE A CD1 
5758  N N   . SER B 725  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  722  SER A N   
5759  C CA  . SER B 725  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  722  SER A CA  
5760  C C   . SER B 725  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  722  SER A C   
5761  O O   . SER B 725  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  722  SER A O   
5762  C CB  . SER B 725  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  722  SER A CB  
5763  O OG  . SER B 725  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  722  SER A OG  
5764  N N   . PHE B 726  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  723  PHE A N   
5765  C CA  . PHE B 726  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  723  PHE A CA  
5766  C C   . PHE B 726  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  723  PHE A C   
5767  O O   . PHE B 726  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  723  PHE A O   
5768  C CB  . PHE B 726  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  723  PHE A CB  
5769  C CG  . PHE B 726  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  723  PHE A CG  
5770  C CD1 . PHE B 726  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  723  PHE A CD1 
5771  C CD2 . PHE B 726  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  723  PHE A CD2 
5772  C CE1 . PHE B 726  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  723  PHE A CE1 
5773  C CE2 . PHE B 726  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  723  PHE A CE2 
5774  C CZ  . PHE B 726  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  723  PHE A CZ  
5775  N N   . GLN B 727  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  724  GLN A N   
5776  C CA  . GLN B 727  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  724  GLN A CA  
5777  C C   . GLN B 727  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  724  GLN A C   
5778  O O   . GLN B 727  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  724  GLN A O   
5779  C CB  . GLN B 727  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  724  GLN A CB  
5780  C CG  . GLN B 727  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  724  GLN A CG  
5781  C CD  . GLN B 727  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  724  GLN A CD  
5782  O OE1 . GLN B 727  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  724  GLN A OE1 
5783  N NE2 . GLN B 727  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  724  GLN A NE2 
5784  N N   . ARG B 728  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  725  ARG A N   
5785  C CA  . ARG B 728  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  725  ARG A CA  
5786  C C   . ARG B 728  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  725  ARG A C   
5787  O O   . ARG B 728  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  725  ARG A O   
5788  C CB  . ARG B 728  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  725  ARG A CB  
5789  C CG  . ARG B 728  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  725  ARG A CG  
5790  C CD  . ARG B 728  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  725  ARG A CD  
5791  N NE  . ARG B 728  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  725  ARG A NE  
5792  C CZ  . ARG B 728  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  725  ARG A CZ  
5793  N NH1 . ARG B 728  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  725  ARG A NH1 
5794  N NH2 . ARG B 728  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  725  ARG A NH2 
5795  N N   . ILE B 729  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  726  ILE A N   
5796  C CA  . ILE B 729  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  726  ILE A CA  
5797  C C   . ILE B 729  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  726  ILE A C   
5798  O O   . ILE B 729  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  726  ILE A O   
5799  C CB  . ILE B 729  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  726  ILE A CB  
5800  C CG1 . ILE B 729  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  726  ILE A CG1 
5801  C CG2 . ILE B 729  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  726  ILE A CG2 
5802  C CD1 . ILE B 729  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  726  ILE A CD1 
5803  N N   . ALA B 730  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  727  ALA A N   
5804  C CA  . ALA B 730  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  727  ALA A CA  
5805  C C   . ALA B 730  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  727  ALA A C   
5806  O O   . ALA B 730  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  727  ALA A O   
5807  C CB  . ALA B 730  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  727  ALA A CB  
5808  N N   . GLU B 731  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  728  GLU A N   
5809  C CA  . GLU B 731  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  728  GLU A CA  
5810  C C   . GLU B 731  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  728  GLU A C   
5811  O O   . GLU B 731  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  728  GLU A O   
5812  C CB  . GLU B 731  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  728  GLU A CB  
5813  C CG  . GLU B 731  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  728  GLU A CG  
5814  C CD  . GLU B 731  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  728  GLU A CD  
5815  O OE1 . GLU B 731  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  728  GLU A OE1 
5816  O OE2 . GLU B 731  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  728  GLU A OE2 
5817  N N   . LYS B 732  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  729  LYS A N   
5818  C CA  . LYS B 732  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  729  LYS A CA  
5819  C C   . LYS B 732  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  729  LYS A C   
5820  O O   . LYS B 732  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  729  LYS A O   
5826  N N   . GLU B 733  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  730  GLU A N   
5827  C CA  . GLU B 733  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  730  GLU A CA  
5828  C C   . GLU B 733  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  730  GLU A C   
5829  O O   . GLU B 733  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  730  GLU A O   
5830  C CB  . GLU B 733  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  730  GLU A CB  
5831  C CG  . GLU B 733  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  730  GLU A CG  
5832  C CD  . GLU B 733  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  730  GLU A CD  
5833  O OE1 . GLU B 733  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  730  GLU A OE1 
5834  O OE2 . GLU B 733  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  730  GLU A OE2 
5835  N N   . ILE B 734  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  731  ILE A N   
5836  C CA  . ILE B 734  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  731  ILE A CA  
5837  C C   . ILE B 734  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  731  ILE A C   
5838  O O   . ILE B 734  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  731  ILE A O   
5839  C CB  . ILE B 734  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  731  ILE A CB  
5840  C CG1 . ILE B 734  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  731  ILE A CG1 
5841  C CG2 . ILE B 734  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  731  ILE A CG2 
5842  C CD1 . ILE B 734  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  731  ILE A CD1 
5843  N N   . MET B 735  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  732  MET A N   
5844  C CA  . MET B 735  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  732  MET A CA  
5845  C C   . MET B 735  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  732  MET A C   
5846  O O   . MET B 735  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  732  MET A O   
5847  C CB  . MET B 735  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  732  MET A CB  
5848  C CG  . MET B 735  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  732  MET A CG  
5849  S SD  . MET B 735  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  732  MET A SD  
5850  C CE  . MET B 735  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  732  MET A CE  
5851  N N   . ASP B 736  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  733  ASP A N   
5852  C CA  . ASP B 736  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  733  ASP A CA  
5853  C C   . ASP B 736  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  733  ASP A C   
5854  O O   . ASP B 736  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  733  ASP A O   
5855  C CB  . ASP B 736  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  733  ASP A CB  
5856  C CG  . ASP B 736  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  733  ASP A CG  
5857  O OD1 . ASP B 736  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  733  ASP A OD1 
5858  O OD2 . ASP B 736  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  733  ASP A OD2 
5859  N N   . ALA B 737  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  734  ALA A N   
5860  C CA  . ALA B 737  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  734  ALA A CA  
5861  C C   . ALA B 737  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  734  ALA A C   
5862  O O   . ALA B 737  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  734  ALA A O   
5863  C CB  . ALA B 737  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  734  ALA A CB  
5864  N N   . VAL B 738  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  735  VAL A N   
5865  C CA  . VAL B 738  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  735  VAL A CA  
5866  C C   . VAL B 738  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  735  VAL A C   
5867  O O   . VAL B 738  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  735  VAL A O   
5868  C CB  . VAL B 738  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  735  VAL A CB  
5869  C CG1 . VAL B 738  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  735  VAL A CG1 
5870  C CG2 . VAL B 738  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  735  VAL A CG2 
5871  N N   . GLU B 739  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  736  GLU A N   
5872  C CA  . GLU B 739  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  736  GLU A CA  
5873  C C   . GLU B 739  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  736  GLU A C   
5874  O O   . GLU B 739  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  736  GLU A O   
5875  C CB  . GLU B 739  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  736  GLU A CB  
5876  C CG  . GLU B 739  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  736  GLU A CG  
5877  C CD  . GLU B 739  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  736  GLU A CD  
5878  O OE1 . GLU B 739  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  736  GLU A OE1 
5879  O OE2 . GLU B 739  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  736  GLU A OE2 
5880  N N   . THR B 740  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  737  THR A N   
5881  C CA  . THR B 740  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  737  THR A CA  
5882  C C   . THR B 740  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  737  THR A C   
5883  O O   . THR B 740  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  737  THR A O   
5884  C CB  . THR B 740  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  737  THR A CB  
5885  O OG1 . THR B 740  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  737  THR A OG1 
5886  C CG2 . THR B 740  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  737  THR A CG2 
5887  N N   . GLY B 741  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  738  GLY A N   
5888  C CA  . GLY B 741  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  738  GLY A CA  
5889  C C   . GLY B 741  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  738  GLY A C   
5890  O O   . GLY B 741  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  738  GLY A O   
5891  N N   . LYS B 742  ? 0.6171 0.6171 0.6171 0.0000  0.0000  0.0000  739  LYS A N   
5892  C CA  . LYS B 742  ? 0.6171 0.6171 0.6171 0.0000  0.0000  0.0000  739  LYS A CA  
5893  C C   . LYS B 742  ? 0.6171 0.6171 0.6171 0.0000  0.0000  0.0000  739  LYS A C   
5894  O O   . LYS B 742  ? 0.6171 0.6171 0.6171 0.0000  0.0000  0.0000  739  LYS A O   
5900  N N   . LEU B 743  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  740  LEU A N   
5901  C CA  . LEU B 743  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  740  LEU A CA  
5902  C C   . LEU B 743  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  740  LEU A C   
5903  O O   . LEU B 743  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  740  LEU A O   
5904  C CB  . LEU B 743  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  740  LEU A CB  
5905  C CG  . LEU B 743  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  740  LEU A CG  
5906  C CD1 . LEU B 743  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  740  LEU A CD1 
5907  C CD2 . LEU B 743  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  740  LEU A CD2 
5908  N N   . TYR B 744  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  741  TYR A N   
5909  C CA  . TYR B 744  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  741  TYR A CA  
5910  C C   . TYR B 744  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  741  TYR A C   
5911  O O   . TYR B 744  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  741  TYR A O   
5912  C CB  . TYR B 744  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  741  TYR A CB  
5913  C CG  . TYR B 744  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  741  TYR A CG  
5914  C CD1 . TYR B 744  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  741  TYR A CD1 
5915  C CD2 . TYR B 744  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  741  TYR A CD2 
5916  C CE1 . TYR B 744  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  741  TYR A CE1 
5917  C CE2 . TYR B 744  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  741  TYR A CE2 
5918  C CZ  . TYR B 744  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  741  TYR A CZ  
5919  O OH  . TYR B 744  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  741  TYR A OH  
5920  N N   . LEU B 745  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  742  LEU A N   
5921  C CA  . LEU B 745  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  742  LEU A CA  
5922  C C   . LEU B 745  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  742  LEU A C   
5923  O O   . LEU B 745  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  742  LEU A O   
5924  C CB  . LEU B 745  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  742  LEU A CB  
5925  C CG  . LEU B 745  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  742  LEU A CG  
5926  C CD1 . LEU B 745  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  742  LEU A CD1 
5927  C CD2 . LEU B 745  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  742  LEU A CD2 
5928  N N   . PHE B 746  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  743  PHE A N   
5929  C CA  . PHE B 746  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  743  PHE A CA  
5930  C C   . PHE B 746  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  743  PHE A C   
5931  O O   . PHE B 746  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  743  PHE A O   
5932  C CB  . PHE B 746  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  743  PHE A CB  
5933  C CG  . PHE B 746  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  743  PHE A CG  
5934  C CD1 . PHE B 746  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  743  PHE A CD1 
5935  C CD2 . PHE B 746  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  743  PHE A CD2 
5936  C CE1 . PHE B 746  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  743  PHE A CE1 
5937  C CE2 . PHE B 746  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  743  PHE A CE2 
5938  C CZ  . PHE B 746  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  743  PHE A CZ  
5939  N N   . GLN B 747  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  744  GLN A N   
5940  C CA  . GLN B 747  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  744  GLN A CA  
5941  C C   . GLN B 747  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  744  GLN A C   
5942  O O   . GLN B 747  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  744  GLN A O   
5943  C CB  . GLN B 747  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  744  GLN A CB  
5944  C CG  . GLN B 747  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  744  GLN A CG  
5945  C CD  . GLN B 747  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  744  GLN A CD  
5946  O OE1 . GLN B 747  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  744  GLN A OE1 
5947  N NE2 . GLN B 747  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  744  GLN A NE2 
5948  N N   . ILE B 748  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  745  ILE A N   
5949  C CA  . ILE B 748  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  745  ILE A CA  
5950  C C   . ILE B 748  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  745  ILE A C   
5951  O O   . ILE B 748  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  745  ILE A O   
5952  C CB  . ILE B 748  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  745  ILE A CB  
5953  C CG1 . ILE B 748  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  745  ILE A CG1 
5954  C CG2 . ILE B 748  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  745  ILE A CG2 
5955  C CD1 . ILE B 748  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  745  ILE A CD1 
5956  N N   . TYR B 749  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  746  TYR A N   
5957  C CA  . TYR B 749  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  746  TYR A CA  
5958  C C   . TYR B 749  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  746  TYR A C   
5959  O O   . TYR B 749  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  746  TYR A O   
5960  C CB  . TYR B 749  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  746  TYR A CB  
5961  C CG  . TYR B 749  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  746  TYR A CG  
5962  C CD1 . TYR B 749  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  746  TYR A CD1 
5963  C CD2 . TYR B 749  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  746  TYR A CD2 
5964  C CE1 . TYR B 749  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  746  TYR A CE1 
5965  C CE2 . TYR B 749  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  746  TYR A CE2 
5966  C CZ  . TYR B 749  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  746  TYR A CZ  
5967  O OH  . TYR B 749  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  746  TYR A OH  
5968  N N   . ASN B 750  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  747  ASN A N   
5969  C CA  . ASN B 750  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  747  ASN A CA  
5970  C C   . ASN B 750  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  747  ASN A C   
5971  O O   . ASN B 750  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  747  ASN A O   
5972  C CB  . ASN B 750  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  747  ASN A CB  
5973  C CG  . ASN B 750  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  747  ASN A CG  
5974  O OD1 . ASN B 750  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  747  ASN A OD1 
5975  N ND2 . ASN B 750  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  747  ASN A ND2 
5976  N N   . LYS B 751  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  748  LYS A N   
5977  C CA  . LYS B 751  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  748  LYS A CA  
5978  C C   . LYS B 751  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  748  LYS A C   
5979  O O   . LYS B 751  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  748  LYS A O   
5985  N N   . ASP B 752  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  749  ASP A N   
5986  C CA  . ASP B 752  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  749  ASP A CA  
5987  C C   . ASP B 752  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  749  ASP A C   
5988  O O   . ASP B 752  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  749  ASP A O   
5989  C CB  . ASP B 752  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  749  ASP A CB  
5990  C CG  . ASP B 752  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  749  ASP A CG  
5991  O OD1 . ASP B 752  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  749  ASP A OD1 
5992  O OD2 . ASP B 752  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  749  ASP A OD2 
5993  N N   . PHE B 753  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  750  PHE A N   
5994  C CA  . PHE B 753  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  750  PHE A CA  
5995  C C   . PHE B 753  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  750  PHE A C   
5996  O O   . PHE B 753  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  750  PHE A O   
5997  C CB  . PHE B 753  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  750  PHE A CB  
5998  C CG  . PHE B 753  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  750  PHE A CG  
5999  C CD1 . PHE B 753  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  750  PHE A CD1 
6000  C CD2 . PHE B 753  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  750  PHE A CD2 
6001  C CE1 . PHE B 753  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  750  PHE A CE1 
6002  C CE2 . PHE B 753  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  750  PHE A CE2 
6003  C CZ  . PHE B 753  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  750  PHE A CZ  
6004  N N   . ALA B 754  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  751  ALA A N   
6005  C CA  . ALA B 754  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  751  ALA A CA  
6006  C C   . ALA B 754  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  751  ALA A C   
6007  O O   . ALA B 754  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  751  ALA A O   
6008  C CB  . ALA B 754  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  751  ALA A CB  
6009  N N   . LYS B 755  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  752  LYS A N   
6010  C CA  . LYS B 755  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  752  LYS A CA  
6011  C C   . LYS B 755  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  752  LYS A C   
6012  O O   . LYS B 755  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  752  LYS A O   
6018  N N   . GLY B 756  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  753  GLY A N   
6019  C CA  . GLY B 756  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  753  GLY A CA  
6020  C C   . GLY B 756  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  753  GLY A C   
6021  O O   . GLY B 756  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  753  GLY A O   
6022  N N   . HIS B 757  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  754  HIS A N   
6023  C CA  . HIS B 757  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  754  HIS A CA  
6024  C C   . HIS B 757  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  754  HIS A C   
6025  O O   . HIS B 757  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  754  HIS A O   
6026  C CB  . HIS B 757  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  754  HIS A CB  
6027  C CG  . HIS B 757  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  754  HIS A CG  
6028  N ND1 . HIS B 757  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  754  HIS A ND1 
6029  C CD2 . HIS B 757  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  754  HIS A CD2 
6030  C CE1 . HIS B 757  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  754  HIS A CE1 
6031  N NE2 . HIS B 757  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  754  HIS A NE2 
6032  N N   . HIS B 758  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  755  HIS A N   
6033  C CA  . HIS B 758  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  755  HIS A CA  
6034  C C   . HIS B 758  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  755  HIS A C   
6035  O O   . HIS B 758  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  755  HIS A O   
6036  C CB  . HIS B 758  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  755  HIS A CB  
6037  C CG  . HIS B 758  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  755  HIS A CG  
6038  N ND1 . HIS B 758  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  755  HIS A ND1 
6039  C CD2 . HIS B 758  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  755  HIS A CD2 
6040  C CE1 . HIS B 758  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  755  HIS A CE1 
6041  N NE2 . HIS B 758  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  755  HIS A NE2 
6042  N N   . GLY B 759  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  756  GLY A N   
6043  C CA  . GLY B 759  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  756  GLY A CA  
6044  C C   . GLY B 759  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  756  GLY A C   
6045  O O   . GLY B 759  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  756  GLY A O   
6046  N N   . LYS B 760  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  757  LYS A N   
6047  C CA  . LYS B 760  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  757  LYS A CA  
6048  C C   . LYS B 760  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  757  LYS A C   
6049  O O   . LYS B 760  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  757  LYS A O   
6050  C CB  . LYS B 760  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  757  LYS A CB  
6051  C CG  . LYS B 760  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  757  LYS A CG  
6052  C CD  . LYS B 760  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  757  LYS A CD  
6053  C CE  . LYS B 760  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  757  LYS A CE  
6054  N NZ  . LYS B 760  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  757  LYS A NZ  
6055  N N   . PRO B 761  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  758  PRO A N   
6056  C CA  . PRO B 761  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  758  PRO A CA  
6057  C C   . PRO B 761  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  758  PRO A C   
6058  O O   . PRO B 761  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  758  PRO A O   
6059  C CB  . PRO B 761  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  758  PRO A CB  
6060  C CG  . PRO B 761  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  758  PRO A CG  
6061  C CD  . PRO B 761  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  758  PRO A CD  
6062  N N   . ASN B 762  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  759  ASN A N   
6063  C CA  . ASN B 762  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  759  ASN A CA  
6064  C C   . ASN B 762  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  759  ASN A C   
6065  O O   . ASN B 762  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  759  ASN A O   
6066  C CB  . ASN B 762  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  759  ASN A CB  
6067  C CG  . ASN B 762  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  759  ASN A CG  
6068  O OD1 . ASN B 762  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  759  ASN A OD1 
6069  N ND2 . ASN B 762  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  759  ASN A ND2 
6070  N N   . LEU B 763  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  760  LEU A N   
6071  C CA  . LEU B 763  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  760  LEU A CA  
6072  C C   . LEU B 763  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  760  LEU A C   
6073  O O   . LEU B 763  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  760  LEU A O   
6074  C CB  . LEU B 763  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  760  LEU A CB  
6075  C CG  . LEU B 763  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  760  LEU A CG  
6076  C CD1 . LEU B 763  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  760  LEU A CD1 
6077  C CD2 . LEU B 763  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  760  LEU A CD2 
6078  N N   . HIS B 764  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  761  HIS A N   
6079  C CA  . HIS B 764  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  761  HIS A CA  
6080  C C   . HIS B 764  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  761  HIS A C   
6081  O O   . HIS B 764  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  761  HIS A O   
6082  C CB  . HIS B 764  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  761  HIS A CB  
6083  C CG  . HIS B 764  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  761  HIS A CG  
6084  N ND1 . HIS B 764  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  761  HIS A ND1 
6085  C CD2 . HIS B 764  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  761  HIS A CD2 
6086  C CE1 . HIS B 764  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  761  HIS A CE1 
6087  N NE2 . HIS B 764  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  761  HIS A NE2 
6088  N N   . THR B 765  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  762  THR A N   
6089  C CA  . THR B 765  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  762  THR A CA  
6090  C C   . THR B 765  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  762  THR A C   
6091  O O   . THR B 765  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  762  THR A O   
6092  C CB  . THR B 765  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  762  THR A CB  
6093  O OG1 . THR B 765  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  762  THR A OG1 
6094  C CG2 . THR B 765  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  762  THR A CG2 
6095  N N   . LEU B 766  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  763  LEU A N   
6096  C CA  . LEU B 766  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  763  LEU A CA  
6097  C C   . LEU B 766  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  763  LEU A C   
6098  O O   . LEU B 766  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  763  LEU A O   
6099  C CB  . LEU B 766  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  763  LEU A CB  
6100  C CG  . LEU B 766  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  763  LEU A CG  
6101  C CD1 . LEU B 766  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  763  LEU A CD1 
6102  C CD2 . LEU B 766  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  763  LEU A CD2 
6103  N N   . TYR B 767  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  764  TYR A N   
6104  C CA  . TYR B 767  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  764  TYR A CA  
6105  C C   . TYR B 767  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  764  TYR A C   
6106  O O   . TYR B 767  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  764  TYR A O   
6107  C CB  . TYR B 767  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  764  TYR A CB  
6108  C CG  . TYR B 767  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  764  TYR A CG  
6109  C CD1 . TYR B 767  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  764  TYR A CD1 
6110  C CD2 . TYR B 767  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  764  TYR A CD2 
6111  C CE1 . TYR B 767  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  764  TYR A CE1 
6112  C CE2 . TYR B 767  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  764  TYR A CE2 
6113  C CZ  . TYR B 767  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  764  TYR A CZ  
6114  O OH  . TYR B 767  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  764  TYR A OH  
6115  N N   . TRP B 768  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  765  TRP A N   
6116  C CA  . TRP B 768  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  765  TRP A CA  
6117  C C   . TRP B 768  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  765  TRP A C   
6118  O O   . TRP B 768  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  765  TRP A O   
6119  C CB  . TRP B 768  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  765  TRP A CB  
6120  C CG  . TRP B 768  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  765  TRP A CG  
6121  C CD1 . TRP B 768  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  765  TRP A CD1 
6122  C CD2 . TRP B 768  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  765  TRP A CD2 
6123  N NE1 . TRP B 768  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  765  TRP A NE1 
6124  C CE2 . TRP B 768  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  765  TRP A CE2 
6125  C CE3 . TRP B 768  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  765  TRP A CE3 
6126  C CZ2 . TRP B 768  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  765  TRP A CZ2 
6127  C CZ3 . TRP B 768  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  765  TRP A CZ3 
6128  C CH2 . TRP B 768  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  765  TRP A CH2 
6129  N N   . THR B 769  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  766  THR A N   
6130  C CA  . THR B 769  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  766  THR A CA  
6131  C C   . THR B 769  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  766  THR A C   
6132  O O   . THR B 769  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  766  THR A O   
6133  C CB  . THR B 769  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  766  THR A CB  
6134  O OG1 . THR B 769  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  766  THR A OG1 
6135  C CG2 . THR B 769  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  766  THR A CG2 
6136  N N   . GLY B 770  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  767  GLY A N   
6137  C CA  . GLY B 770  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  767  GLY A CA  
6138  C C   . GLY B 770  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  767  GLY A C   
6139  O O   . GLY B 770  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  767  GLY A O   
6140  N N   . LEU B 771  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  768  LEU A N   
6141  C CA  . LEU B 771  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  768  LEU A CA  
6142  C C   . LEU B 771  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  768  LEU A C   
6143  O O   . LEU B 771  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  768  LEU A O   
6144  C CB  . LEU B 771  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  768  LEU A CB  
6145  C CG  . LEU B 771  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  768  LEU A CG  
6146  C CD1 . LEU B 771  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  768  LEU A CD1 
6147  C CD2 . LEU B 771  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  768  LEU A CD2 
6148  N N   . PHE B 772  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  769  PHE A N   
6149  C CA  . PHE B 772  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  769  PHE A CA  
6150  C C   . PHE B 772  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  769  PHE A C   
6151  O O   . PHE B 772  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  769  PHE A O   
6152  C CB  . PHE B 772  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  769  PHE A CB  
6153  C CG  . PHE B 772  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  769  PHE A CG  
6154  C CD1 . PHE B 772  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  769  PHE A CD1 
6155  C CD2 . PHE B 772  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  769  PHE A CD2 
6156  C CE1 . PHE B 772  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  769  PHE A CE1 
6157  C CE2 . PHE B 772  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  769  PHE A CE2 
6158  C CZ  . PHE B 772  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  769  PHE A CZ  
6159  N N   . SER B 773  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  770  SER A N   
6160  C CA  . SER B 773  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  770  SER A CA  
6161  C C   . SER B 773  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  770  SER A C   
6162  O O   . SER B 773  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  770  SER A O   
6163  C CB  . SER B 773  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  770  SER A CB  
6164  O OG  . SER B 773  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  770  SER A OG  
6165  N N   . PRO B 774  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  771  PRO A N   
6166  C CA  . PRO B 774  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  771  PRO A CA  
6167  C C   . PRO B 774  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  771  PRO A C   
6168  O O   . PRO B 774  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  771  PRO A O   
6169  C CB  . PRO B 774  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  771  PRO A CB  
6170  C CG  . PRO B 774  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  771  PRO A CG  
6171  C CD  . PRO B 774  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  771  PRO A CD  
6172  N N   . GLU B 775  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  772  GLU A N   
6173  C CA  . GLU B 775  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  772  GLU A CA  
6174  C C   . GLU B 775  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  772  GLU A C   
6175  O O   . GLU B 775  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  772  GLU A O   
6176  C CB  . GLU B 775  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  772  GLU A CB  
6177  C CG  . GLU B 775  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  772  GLU A CG  
6178  C CD  . GLU B 775  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  772  GLU A CD  
6179  O OE1 . GLU B 775  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  772  GLU A OE1 
6180  O OE2 . GLU B 775  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  772  GLU A OE2 
6181  N N   . ASN B 776  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  773  ASN A N   
6182  C CA  . ASN B 776  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  773  ASN A CA  
6183  C C   . ASN B 776  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  773  ASN A C   
6184  O O   . ASN B 776  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  773  ASN A O   
6185  C CB  . ASN B 776  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  773  ASN A CB  
6186  C CG  . ASN B 776  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  773  ASN A CG  
6187  O OD1 . ASN B 776  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  773  ASN A OD1 
6188  N ND2 . ASN B 776  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  773  ASN A ND2 
6189  N N   . LEU B 777  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  774  LEU A N   
6190  C CA  . LEU B 777  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  774  LEU A CA  
6191  C C   . LEU B 777  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  774  LEU A C   
6192  O O   . LEU B 777  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  774  LEU A O   
6193  C CB  . LEU B 777  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  774  LEU A CB  
6194  C CG  . LEU B 777  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  774  LEU A CG  
6195  C CD1 . LEU B 777  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  774  LEU A CD1 
6196  C CD2 . LEU B 777  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  774  LEU A CD2 
6197  N N   . ALA B 778  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  775  ALA A N   
6198  C CA  . ALA B 778  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  775  ALA A CA  
6199  C C   . ALA B 778  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  775  ALA A C   
6200  O O   . ALA B 778  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  775  ALA A O   
6201  C CB  . ALA B 778  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  775  ALA A CB  
6202  N N   . LYS B 779  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  776  LYS A N   
6203  C CA  . LYS B 779  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  776  LYS A CA  
6204  C C   . LYS B 779  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  776  LYS A C   
6205  O O   . LYS B 779  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  776  LYS A O   
6206  C CB  . LYS B 779  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  776  LYS A CB  
6207  C CG  . LYS B 779  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  776  LYS A CG  
6208  C CD  . LYS B 779  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  776  LYS A CD  
6209  C CE  . LYS B 779  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  776  LYS A CE  
6210  N NZ  . LYS B 779  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  776  LYS A NZ  
6211  N N   . THR B 780  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  777  THR A N   
6212  C CA  . THR B 780  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  777  THR A CA  
6213  C C   . THR B 780  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  777  THR A C   
6214  O O   . THR B 780  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  777  THR A O   
6215  C CB  . THR B 780  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  777  THR A CB  
6216  O OG1 . THR B 780  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  777  THR A OG1 
6217  C CG2 . THR B 780  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  777  THR A CG2 
6218  N N   . SER B 781  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  778  SER A N   
6219  C CA  . SER B 781  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  778  SER A CA  
6220  C C   . SER B 781  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  778  SER A C   
6221  O O   . SER B 781  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  778  SER A O   
6222  C CB  . SER B 781  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  778  SER A CB  
6223  O OG  . SER B 781  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  778  SER A OG  
6224  N N   . ILE B 782  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  779  ILE A N   
6225  C CA  . ILE B 782  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  779  ILE A CA  
6226  C C   . ILE B 782  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  779  ILE A C   
6227  O O   . ILE B 782  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  779  ILE A O   
6228  C CB  . ILE B 782  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  779  ILE A CB  
6229  C CG1 . ILE B 782  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  779  ILE A CG1 
6230  C CG2 . ILE B 782  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  779  ILE A CG2 
6231  C CD1 . ILE B 782  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  779  ILE A CD1 
6232  N N   . LYS B 783  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  780  LYS A N   
6233  C CA  . LYS B 783  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  780  LYS A CA  
6234  C C   . LYS B 783  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  780  LYS A C   
6235  O O   . LYS B 783  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  780  LYS A O   
6236  C CB  . LYS B 783  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  780  LYS A CB  
6237  C CG  . LYS B 783  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  780  LYS A CG  
6238  C CD  . LYS B 783  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  780  LYS A CD  
6239  C CE  . LYS B 783  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  780  LYS A CE  
6240  N NZ  . LYS B 783  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  780  LYS A NZ  
6241  N N   . LEU B 784  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  781  LEU A N   
6242  C CA  . LEU B 784  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  781  LEU A CA  
6243  C C   . LEU B 784  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  781  LEU A C   
6244  O O   . LEU B 784  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  781  LEU A O   
6245  C CB  . LEU B 784  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  781  LEU A CB  
6246  C CG  . LEU B 784  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  781  LEU A CG  
6247  C CD1 . LEU B 784  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  781  LEU A CD1 
6248  C CD2 . LEU B 784  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  781  LEU A CD2 
6249  N N   . ASN B 785  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  782  ASN A N   
6250  C CA  . ASN B 785  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  782  ASN A CA  
6251  C C   . ASN B 785  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  782  ASN A C   
6252  O O   . ASN B 785  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  782  ASN A O   
6253  C CB  . ASN B 785  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  782  ASN A CB  
6254  C CG  . ASN B 785  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  782  ASN A CG  
6255  O OD1 . ASN B 785  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  782  ASN A OD1 
6256  N ND2 . ASN B 785  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  782  ASN A ND2 
6257  N N   . GLY B 786  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  783  GLY A N   
6258  C CA  . GLY B 786  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  783  GLY A CA  
6259  C C   . GLY B 786  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  783  GLY A C   
6260  O O   . GLY B 786  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  783  GLY A O   
6261  N N   . GLN B 787  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  784  GLN A N   
6262  C CA  . GLN B 787  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  784  GLN A CA  
6263  C C   . GLN B 787  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  784  GLN A C   
6264  O O   . GLN B 787  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  784  GLN A O   
6265  C CB  . GLN B 787  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  784  GLN A CB  
6266  C CG  . GLN B 787  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  784  GLN A CG  
6267  C CD  . GLN B 787  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  784  GLN A CD  
6268  O OE1 . GLN B 787  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  784  GLN A OE1 
6269  N NE2 . GLN B 787  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  784  GLN A NE2 
6270  N N   . ALA B 788  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  785  ALA A N   
6271  C CA  . ALA B 788  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  785  ALA A CA  
6272  C C   . ALA B 788  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  785  ALA A C   
6273  O O   . ALA B 788  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  785  ALA A O   
6274  C CB  . ALA B 788  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  785  ALA A CB  
6275  N N   . GLU B 789  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  786  GLU A N   
6276  C CA  . GLU B 789  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  786  GLU A CA  
6277  C C   . GLU B 789  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  786  GLU A C   
6278  O O   . GLU B 789  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  786  GLU A O   
6279  C CB  . GLU B 789  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  786  GLU A CB  
6280  C CG  . GLU B 789  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  786  GLU A CG  
6281  C CD  . GLU B 789  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  786  GLU A CD  
6282  O OE1 . GLU B 789  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  786  GLU A OE1 
6283  O OE2 . GLU B 789  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  786  GLU A OE2 
6284  N N   . LEU B 790  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  787  LEU A N   
6285  C CA  . LEU B 790  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  787  LEU A CA  
6286  C C   . LEU B 790  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  787  LEU A C   
6287  O O   . LEU B 790  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  787  LEU A O   
6288  C CB  . LEU B 790  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  787  LEU A CB  
6289  C CG  . LEU B 790  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  787  LEU A CG  
6290  C CD1 . LEU B 790  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  787  LEU A CD1 
6291  C CD2 . LEU B 790  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  787  LEU A CD2 
6292  N N   . PHE B 791  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  788  PHE A N   
6293  C CA  . PHE B 791  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  788  PHE A CA  
6294  C C   . PHE B 791  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  788  PHE A C   
6295  O O   . PHE B 791  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  788  PHE A O   
6296  C CB  . PHE B 791  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  788  PHE A CB  
6297  C CG  . PHE B 791  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  788  PHE A CG  
6298  C CD1 . PHE B 791  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  788  PHE A CD1 
6299  C CD2 . PHE B 791  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  788  PHE A CD2 
6300  C CE1 . PHE B 791  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  788  PHE A CE1 
6301  C CE2 . PHE B 791  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  788  PHE A CE2 
6302  C CZ  . PHE B 791  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  788  PHE A CZ  
6303  N N   . TYR B 792  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  789  TYR A N   
6304  C CA  . TYR B 792  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  789  TYR A CA  
6305  C C   . TYR B 792  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  789  TYR A C   
6306  O O   . TYR B 792  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  789  TYR A O   
6307  C CB  . TYR B 792  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  789  TYR A CB  
6308  C CG  . TYR B 792  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  789  TYR A CG  
6309  C CD1 . TYR B 792  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  789  TYR A CD1 
6310  C CD2 . TYR B 792  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  789  TYR A CD2 
6311  C CE1 . TYR B 792  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  789  TYR A CE1 
6312  C CE2 . TYR B 792  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  789  TYR A CE2 
6313  C CZ  . TYR B 792  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  789  TYR A CZ  
6314  O OH  . TYR B 792  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  789  TYR A OH  
6315  N N   . ARG B 793  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  790  ARG A N   
6316  C CA  . ARG B 793  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  790  ARG A CA  
6317  C C   . ARG B 793  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  790  ARG A C   
6318  O O   . ARG B 793  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  790  ARG A O   
6319  C CB  . ARG B 793  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  790  ARG A CB  
6320  C CG  . ARG B 793  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  790  ARG A CG  
6321  C CD  . ARG B 793  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  790  ARG A CD  
6322  N NE  . ARG B 793  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  790  ARG A NE  
6323  C CZ  . ARG B 793  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  790  ARG A CZ  
6324  N NH1 . ARG B 793  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  790  ARG A NH1 
6325  N NH2 . ARG B 793  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  790  ARG A NH2 
6326  N N   . PRO B 794  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  791  PRO A N   
6327  C CA  . PRO B 794  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  791  PRO A CA  
6328  C C   . PRO B 794  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  791  PRO A C   
6329  O O   . PRO B 794  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  791  PRO A O   
6330  C CB  . PRO B 794  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  791  PRO A CB  
6331  C CG  . PRO B 794  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  791  PRO A CG  
6332  C CD  . PRO B 794  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  791  PRO A CD  
6333  N N   . LYS B 795  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  792  LYS A N   
6334  C CA  . LYS B 795  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  792  LYS A CA  
6335  C C   . LYS B 795  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  792  LYS A C   
6336  O O   . LYS B 795  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  792  LYS A O   
6342  N N   . SER B 796  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  793  SER A N   
6343  C CA  . SER B 796  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  793  SER A CA  
6344  C C   . SER B 796  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  793  SER A C   
6345  O O   . SER B 796  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  793  SER A O   
6346  C CB  . SER B 796  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  793  SER A CB  
6347  O OG  . SER B 796  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  793  SER A OG  
6348  N N   . ARG B 797  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  794  ARG A N   
6349  C CA  . ARG B 797  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  794  ARG A CA  
6350  C C   . ARG B 797  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  794  ARG A C   
6351  O O   . ARG B 797  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  794  ARG A O   
6352  C CB  . ARG B 797  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  794  ARG A CB  
6353  C CG  . ARG B 797  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  794  ARG A CG  
6354  C CD  . ARG B 797  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  794  ARG A CD  
6355  N NE  . ARG B 797  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  794  ARG A NE  
6356  C CZ  . ARG B 797  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  794  ARG A CZ  
6357  N NH1 . ARG B 797  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  794  ARG A NH1 
6358  N NH2 . ARG B 797  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  794  ARG A NH2 
6359  N N   . MET B 798  ? 0.6486 0.6486 0.6486 0.0000  0.0000  0.0000  795  MET A N   
6360  C CA  . MET B 798  ? 0.6486 0.6486 0.6486 0.0000  0.0000  0.0000  795  MET A CA  
6361  C C   . MET B 798  ? 0.6486 0.6486 0.6486 0.0000  0.0000  0.0000  795  MET A C   
6362  O O   . MET B 798  ? 0.6486 0.6486 0.6486 0.0000  0.0000  0.0000  795  MET A O   
6363  C CB  . MET B 798  ? 0.6486 0.6486 0.6486 0.0000  0.0000  0.0000  795  MET A CB  
6364  C CG  . MET B 798  ? 0.6486 0.6486 0.6486 0.0000  0.0000  0.0000  795  MET A CG  
6365  S SD  . MET B 798  ? 0.6486 0.6486 0.6486 0.0000  0.0000  0.0000  795  MET A SD  
6366  C CE  . MET B 798  ? 0.6486 0.6486 0.6486 0.0000  0.0000  0.0000  795  MET A CE  
6429  N N   . GLU B 807  ? 0.9112 0.9112 0.9112 0.0000  0.0000  0.0000  804  GLU A N   
6430  C CA  . GLU B 807  ? 0.9112 0.9112 0.9112 0.0000  0.0000  0.0000  804  GLU A CA  
6431  C C   . GLU B 807  ? 0.9112 0.9112 0.9112 0.0000  0.0000  0.0000  804  GLU A C   
6432  O O   . GLU B 807  ? 0.9112 0.9112 0.9112 0.0000  0.0000  0.0000  804  GLU A O   
6438  N N   . LYS B 808  ? 0.8066 0.8066 0.8066 0.0000  0.0000  0.0000  805  LYS A N   
6439  C CA  . LYS B 808  ? 0.8066 0.8066 0.8066 0.0000  0.0000  0.0000  805  LYS A CA  
6440  C C   . LYS B 808  ? 0.8066 0.8066 0.8066 0.0000  0.0000  0.0000  805  LYS A C   
6441  O O   . LYS B 808  ? 0.8066 0.8066 0.8066 0.0000  0.0000  0.0000  805  LYS A O   
6442  C CB  . LYS B 808  ? 0.8066 0.8066 0.8066 0.0000  0.0000  0.0000  805  LYS A CB  
6443  C CG  . LYS B 808  ? 0.8066 0.8066 0.8066 0.0000  0.0000  0.0000  805  LYS A CG  
6444  C CD  . LYS B 808  ? 0.8066 0.8066 0.8066 0.0000  0.0000  0.0000  805  LYS A CD  
6445  C CE  . LYS B 808  ? 0.8066 0.8066 0.8066 0.0000  0.0000  0.0000  805  LYS A CE  
6446  N NZ  . LYS B 808  ? 0.8066 0.8066 0.8066 0.0000  0.0000  0.0000  805  LYS A NZ  
6447  N N   . MET B 809  ? 0.7653 0.7653 0.7653 0.0000  0.0000  0.0000  806  MET A N   
6448  C CA  . MET B 809  ? 0.7653 0.7653 0.7653 0.0000  0.0000  0.0000  806  MET A CA  
6449  C C   . MET B 809  ? 0.7653 0.7653 0.7653 0.0000  0.0000  0.0000  806  MET A C   
6450  O O   . MET B 809  ? 0.7653 0.7653 0.7653 0.0000  0.0000  0.0000  806  MET A O   
6451  C CB  . MET B 809  ? 0.7653 0.7653 0.7653 0.0000  0.0000  0.0000  806  MET A CB  
6452  C CG  . MET B 809  ? 0.7653 0.7653 0.7653 0.0000  0.0000  0.0000  806  MET A CG  
6453  S SD  . MET B 809  ? 0.7653 0.7653 0.7653 0.0000  0.0000  0.0000  806  MET A SD  
6454  C CE  . MET B 809  ? 0.7653 0.7653 0.7653 0.0000  0.0000  0.0000  806  MET A CE  
6455  N N   . LEU B 810  ? 0.7205 0.7205 0.7205 0.0000  0.0000  0.0000  807  LEU A N   
6456  C CA  . LEU B 810  ? 0.7205 0.7205 0.7205 0.0000  0.0000  0.0000  807  LEU A CA  
6457  C C   . LEU B 810  ? 0.7205 0.7205 0.7205 0.0000  0.0000  0.0000  807  LEU A C   
6458  O O   . LEU B 810  ? 0.7205 0.7205 0.7205 0.0000  0.0000  0.0000  807  LEU A O   
6459  C CB  . LEU B 810  ? 0.7205 0.7205 0.7205 0.0000  0.0000  0.0000  807  LEU A CB  
6460  C CG  . LEU B 810  ? 0.7205 0.7205 0.7205 0.0000  0.0000  0.0000  807  LEU A CG  
6461  C CD1 . LEU B 810  ? 0.7205 0.7205 0.7205 0.0000  0.0000  0.0000  807  LEU A CD1 
6462  C CD2 . LEU B 810  ? 0.7205 0.7205 0.7205 0.0000  0.0000  0.0000  807  LEU A CD2 
6463  N N   . ASN B 811  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  808  ASN A N   
6464  C CA  . ASN B 811  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  808  ASN A CA  
6465  C C   . ASN B 811  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  808  ASN A C   
6466  O O   . ASN B 811  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  808  ASN A O   
6467  C CB  . ASN B 811  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  808  ASN A CB  
6468  C CG  . ASN B 811  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  808  ASN A CG  
6469  O OD1 . ASN B 811  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  808  ASN A OD1 
6470  N ND2 . ASN B 811  ? 0.6737 0.6737 0.6737 0.0000  0.0000  0.0000  808  ASN A ND2 
6471  N N   . LYS B 812  ? 0.6318 0.6318 0.6318 0.0000  0.0000  0.0000  809  LYS A N   
6472  C CA  . LYS B 812  ? 0.6318 0.6318 0.6318 0.0000  0.0000  0.0000  809  LYS A CA  
6473  C C   . LYS B 812  ? 0.6318 0.6318 0.6318 0.0000  0.0000  0.0000  809  LYS A C   
6474  O O   . LYS B 812  ? 0.6318 0.6318 0.6318 0.0000  0.0000  0.0000  809  LYS A O   
6475  C CB  . LYS B 812  ? 0.6318 0.6318 0.6318 0.0000  0.0000  0.0000  809  LYS A CB  
6476  C CG  . LYS B 812  ? 0.6318 0.6318 0.6318 0.0000  0.0000  0.0000  809  LYS A CG  
6477  C CD  . LYS B 812  ? 0.6318 0.6318 0.6318 0.0000  0.0000  0.0000  809  LYS A CD  
6478  C CE  . LYS B 812  ? 0.6318 0.6318 0.6318 0.0000  0.0000  0.0000  809  LYS A CE  
6479  N NZ  . LYS B 812  ? 0.6318 0.6318 0.6318 0.0000  0.0000  0.0000  809  LYS A NZ  
6480  N N   . LYS B 813  ? 0.6532 0.6532 0.6532 0.0000  0.0000  0.0000  810  LYS A N   
6481  C CA  . LYS B 813  ? 0.6532 0.6532 0.6532 0.0000  0.0000  0.0000  810  LYS A CA  
6482  C C   . LYS B 813  ? 0.6532 0.6532 0.6532 0.0000  0.0000  0.0000  810  LYS A C   
6483  O O   . LYS B 813  ? 0.6532 0.6532 0.6532 0.0000  0.0000  0.0000  810  LYS A O   
6489  N N   . LEU B 814  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  811  LEU A N   
6490  C CA  . LEU B 814  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  811  LEU A CA  
6491  C C   . LEU B 814  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  811  LEU A C   
6492  O O   . LEU B 814  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  811  LEU A O   
6493  C CB  . LEU B 814  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  811  LEU A CB  
6494  C CG  . LEU B 814  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  811  LEU A CG  
6495  C CD1 . LEU B 814  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  811  LEU A CD1 
6496  C CD2 . LEU B 814  ? 0.6947 0.6947 0.6947 0.0000  0.0000  0.0000  811  LEU A CD2 
6497  N N   . LYS B 815  ? 0.7353 0.7353 0.7353 0.0000  0.0000  0.0000  812  LYS A N   
6498  C CA  . LYS B 815  ? 0.7353 0.7353 0.7353 0.0000  0.0000  0.0000  812  LYS A CA  
6499  C C   . LYS B 815  ? 0.7353 0.7353 0.7353 0.0000  0.0000  0.0000  812  LYS A C   
6500  O O   . LYS B 815  ? 0.7353 0.7353 0.7353 0.0000  0.0000  0.0000  812  LYS A O   
6501  C CB  . LYS B 815  ? 0.7353 0.7353 0.7353 0.0000  0.0000  0.0000  812  LYS A CB  
6502  C CG  . LYS B 815  ? 0.7353 0.7353 0.7353 0.0000  0.0000  0.0000  812  LYS A CG  
6503  C CD  . LYS B 815  ? 0.7353 0.7353 0.7353 0.0000  0.0000  0.0000  812  LYS A CD  
6504  C CE  . LYS B 815  ? 0.7353 0.7353 0.7353 0.0000  0.0000  0.0000  812  LYS A CE  
6505  N NZ  . LYS B 815  ? 0.7353 0.7353 0.7353 0.0000  0.0000  0.0000  812  LYS A NZ  
6506  N N   . ASP B 816  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  813  ASP A N   
6507  C CA  . ASP B 816  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  813  ASP A CA  
6508  C C   . ASP B 816  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  813  ASP A C   
6509  O O   . ASP B 816  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  813  ASP A O   
6510  C CB  . ASP B 816  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  813  ASP A CB  
6511  C CG  . ASP B 816  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  813  ASP A CG  
6512  O OD1 . ASP B 816  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  813  ASP A OD1 
6513  O OD2 . ASP B 816  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  813  ASP A OD2 
6514  N N   . GLN B 817  ? 0.7234 0.7234 0.7234 0.0000  0.0000  0.0000  814  GLN A N   
6515  C CA  . GLN B 817  ? 0.7234 0.7234 0.7234 0.0000  0.0000  0.0000  814  GLN A CA  
6516  C C   . GLN B 817  ? 0.7234 0.7234 0.7234 0.0000  0.0000  0.0000  814  GLN A C   
6517  O O   . GLN B 817  ? 0.7234 0.7234 0.7234 0.0000  0.0000  0.0000  814  GLN A O   
6518  C CB  . GLN B 817  ? 0.7234 0.7234 0.7234 0.0000  0.0000  0.0000  814  GLN A CB  
6519  C CG  . GLN B 817  ? 0.7234 0.7234 0.7234 0.0000  0.0000  0.0000  814  GLN A CG  
6520  C CD  . GLN B 817  ? 0.7234 0.7234 0.7234 0.0000  0.0000  0.0000  814  GLN A CD  
6521  O OE1 . GLN B 817  ? 0.7234 0.7234 0.7234 0.0000  0.0000  0.0000  814  GLN A OE1 
6522  N NE2 . GLN B 817  ? 0.7234 0.7234 0.7234 0.0000  0.0000  0.0000  814  GLN A NE2 
6523  N N   . LYS B 818  ? 0.6579 0.6579 0.6579 0.0000  0.0000  0.0000  815  LYS A N   
6524  C CA  . LYS B 818  ? 0.6579 0.6579 0.6579 0.0000  0.0000  0.0000  815  LYS A CA  
6525  C C   . LYS B 818  ? 0.6579 0.6579 0.6579 0.0000  0.0000  0.0000  815  LYS A C   
6526  O O   . LYS B 818  ? 0.6579 0.6579 0.6579 0.0000  0.0000  0.0000  815  LYS A O   
6532  N N   . THR B 819  ? 0.6755 0.6755 0.6755 0.0000  0.0000  0.0000  816  THR A N   
6533  C CA  . THR B 819  ? 0.6755 0.6755 0.6755 0.0000  0.0000  0.0000  816  THR A CA  
6534  C C   . THR B 819  ? 0.6755 0.6755 0.6755 0.0000  0.0000  0.0000  816  THR A C   
6535  O O   . THR B 819  ? 0.6755 0.6755 0.6755 0.0000  0.0000  0.0000  816  THR A O   
6536  C CB  . THR B 819  ? 0.6755 0.6755 0.6755 0.0000  0.0000  0.0000  816  THR A CB  
6537  O OG1 . THR B 819  ? 0.6755 0.6755 0.6755 0.0000  0.0000  0.0000  816  THR A OG1 
6538  C CG2 . THR B 819  ? 0.6755 0.6755 0.6755 0.0000  0.0000  0.0000  816  THR A CG2 
6539  N N   . PRO B 820  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  817  PRO A N   
6540  C CA  . PRO B 820  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  817  PRO A CA  
6541  C C   . PRO B 820  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  817  PRO A C   
6542  O O   . PRO B 820  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  817  PRO A O   
6543  C CB  . PRO B 820  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  817  PRO A CB  
6544  C CG  . PRO B 820  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  817  PRO A CG  
6545  C CD  . PRO B 820  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  817  PRO A CD  
6546  N N   . ILE B 821  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  818  ILE A N   
6547  C CA  . ILE B 821  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  818  ILE A CA  
6548  C C   . ILE B 821  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  818  ILE A C   
6549  O O   . ILE B 821  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  818  ILE A O   
6550  C CB  . ILE B 821  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  818  ILE A CB  
6551  C CG1 . ILE B 821  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  818  ILE A CG1 
6552  C CG2 . ILE B 821  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  818  ILE A CG2 
6553  C CD1 . ILE B 821  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  818  ILE A CD1 
6554  N N   . PRO B 822  ? 0.6456 0.6456 0.6456 0.0000  0.0000  0.0000  819  PRO A N   
6555  C CA  . PRO B 822  ? 0.6456 0.6456 0.6456 0.0000  0.0000  0.0000  819  PRO A CA  
6556  C C   . PRO B 822  ? 0.6456 0.6456 0.6456 0.0000  0.0000  0.0000  819  PRO A C   
6557  O O   . PRO B 822  ? 0.6456 0.6456 0.6456 0.0000  0.0000  0.0000  819  PRO A O   
6558  C CB  . PRO B 822  ? 0.6456 0.6456 0.6456 0.0000  0.0000  0.0000  819  PRO A CB  
6559  C CG  . PRO B 822  ? 0.6456 0.6456 0.6456 0.0000  0.0000  0.0000  819  PRO A CG  
6560  C CD  . PRO B 822  ? 0.6456 0.6456 0.6456 0.0000  0.0000  0.0000  819  PRO A CD  
6561  N N   . ASP B 823  ? 0.7380 0.7380 0.7380 0.0000  0.0000  0.0000  820  ASP A N   
6562  C CA  . ASP B 823  ? 0.7380 0.7380 0.7380 0.0000  0.0000  0.0000  820  ASP A CA  
6563  C C   . ASP B 823  ? 0.7380 0.7380 0.7380 0.0000  0.0000  0.0000  820  ASP A C   
6564  O O   . ASP B 823  ? 0.7380 0.7380 0.7380 0.0000  0.0000  0.0000  820  ASP A O   
6565  C CB  . ASP B 823  ? 0.7380 0.7380 0.7380 0.0000  0.0000  0.0000  820  ASP A CB  
6566  C CG  . ASP B 823  ? 0.7380 0.7380 0.7380 0.0000  0.0000  0.0000  820  ASP A CG  
6567  O OD1 . ASP B 823  ? 0.7380 0.7380 0.7380 0.0000  0.0000  0.0000  820  ASP A OD1 
6568  O OD2 . ASP B 823  ? 0.7380 0.7380 0.7380 0.0000  0.0000  0.0000  820  ASP A OD2 
6569  N N   . THR B 824  ? 0.7150 0.7150 0.7150 0.0000  0.0000  0.0000  821  THR A N   
6570  C CA  . THR B 824  ? 0.7150 0.7150 0.7150 0.0000  0.0000  0.0000  821  THR A CA  
6571  C C   . THR B 824  ? 0.7150 0.7150 0.7150 0.0000  0.0000  0.0000  821  THR A C   
6572  O O   . THR B 824  ? 0.7150 0.7150 0.7150 0.0000  0.0000  0.0000  821  THR A O   
6573  C CB  . THR B 824  ? 0.7150 0.7150 0.7150 0.0000  0.0000  0.0000  821  THR A CB  
6574  O OG1 . THR B 824  ? 0.7150 0.7150 0.7150 0.0000  0.0000  0.0000  821  THR A OG1 
6575  C CG2 . THR B 824  ? 0.7150 0.7150 0.7150 0.0000  0.0000  0.0000  821  THR A CG2 
6576  N N   . LEU B 825  ? 0.7337 0.7337 0.7337 0.0000  0.0000  0.0000  822  LEU A N   
6577  C CA  . LEU B 825  ? 0.7337 0.7337 0.7337 0.0000  0.0000  0.0000  822  LEU A CA  
6578  C C   . LEU B 825  ? 0.7337 0.7337 0.7337 0.0000  0.0000  0.0000  822  LEU A C   
6579  O O   . LEU B 825  ? 0.7337 0.7337 0.7337 0.0000  0.0000  0.0000  822  LEU A O   
6580  C CB  . LEU B 825  ? 0.7337 0.7337 0.7337 0.0000  0.0000  0.0000  822  LEU A CB  
6581  C CG  . LEU B 825  ? 0.7337 0.7337 0.7337 0.0000  0.0000  0.0000  822  LEU A CG  
6582  C CD1 . LEU B 825  ? 0.7337 0.7337 0.7337 0.0000  0.0000  0.0000  822  LEU A CD1 
6583  C CD2 . LEU B 825  ? 0.7337 0.7337 0.7337 0.0000  0.0000  0.0000  822  LEU A CD2 
6584  N N   . TYR B 826  ? 0.7694 0.7694 0.7694 0.0000  0.0000  0.0000  823  TYR A N   
6585  C CA  . TYR B 826  ? 0.7694 0.7694 0.7694 0.0000  0.0000  0.0000  823  TYR A CA  
6586  C C   . TYR B 826  ? 0.7694 0.7694 0.7694 0.0000  0.0000  0.0000  823  TYR A C   
6587  O O   . TYR B 826  ? 0.7694 0.7694 0.7694 0.0000  0.0000  0.0000  823  TYR A O   
6588  C CB  . TYR B 826  ? 0.7694 0.7694 0.7694 0.0000  0.0000  0.0000  823  TYR A CB  
6589  C CG  . TYR B 826  ? 0.7694 0.7694 0.7694 0.0000  0.0000  0.0000  823  TYR A CG  
6590  C CD1 . TYR B 826  ? 0.7694 0.7694 0.7694 0.0000  0.0000  0.0000  823  TYR A CD1 
6591  C CD2 . TYR B 826  ? 0.7694 0.7694 0.7694 0.0000  0.0000  0.0000  823  TYR A CD2 
6592  C CE1 . TYR B 826  ? 0.7694 0.7694 0.7694 0.0000  0.0000  0.0000  823  TYR A CE1 
6593  C CE2 . TYR B 826  ? 0.7694 0.7694 0.7694 0.0000  0.0000  0.0000  823  TYR A CE2 
6594  C CZ  . TYR B 826  ? 0.7694 0.7694 0.7694 0.0000  0.0000  0.0000  823  TYR A CZ  
6595  O OH  . TYR B 826  ? 0.7694 0.7694 0.7694 0.0000  0.0000  0.0000  823  TYR A OH  
6596  N N   . GLN B 827  ? 0.8076 0.8076 0.8076 0.0000  0.0000  0.0000  824  GLN A N   
6597  C CA  . GLN B 827  ? 0.8076 0.8076 0.8076 0.0000  0.0000  0.0000  824  GLN A CA  
6598  C C   . GLN B 827  ? 0.8076 0.8076 0.8076 0.0000  0.0000  0.0000  824  GLN A C   
6599  O O   . GLN B 827  ? 0.8076 0.8076 0.8076 0.0000  0.0000  0.0000  824  GLN A O   
6600  C CB  . GLN B 827  ? 0.8076 0.8076 0.8076 0.0000  0.0000  0.0000  824  GLN A CB  
6601  C CG  . GLN B 827  ? 0.8076 0.8076 0.8076 0.0000  0.0000  0.0000  824  GLN A CG  
6602  C CD  . GLN B 827  ? 0.8076 0.8076 0.8076 0.0000  0.0000  0.0000  824  GLN A CD  
6603  O OE1 . GLN B 827  ? 0.8076 0.8076 0.8076 0.0000  0.0000  0.0000  824  GLN A OE1 
6604  N NE2 . GLN B 827  ? 0.8076 0.8076 0.8076 0.0000  0.0000  0.0000  824  GLN A NE2 
6605  N N   . GLU B 828  ? 0.8542 0.8542 0.8542 0.0000  0.0000  0.0000  825  GLU A N   
6606  C CA  . GLU B 828  ? 0.8542 0.8542 0.8542 0.0000  0.0000  0.0000  825  GLU A CA  
6607  C C   . GLU B 828  ? 0.8542 0.8542 0.8542 0.0000  0.0000  0.0000  825  GLU A C   
6608  O O   . GLU B 828  ? 0.8542 0.8542 0.8542 0.0000  0.0000  0.0000  825  GLU A O   
6609  C CB  . GLU B 828  ? 0.8542 0.8542 0.8542 0.0000  0.0000  0.0000  825  GLU A CB  
6610  C CG  . GLU B 828  ? 0.8542 0.8542 0.8542 0.0000  0.0000  0.0000  825  GLU A CG  
6611  C CD  . GLU B 828  ? 0.8542 0.8542 0.8542 0.0000  0.0000  0.0000  825  GLU A CD  
6612  O OE1 . GLU B 828  ? 0.8542 0.8542 0.8542 0.0000  0.0000  0.0000  825  GLU A OE1 
6613  O OE2 . GLU B 828  ? 0.8542 0.8542 0.8542 0.0000  0.0000  0.0000  825  GLU A OE2 
6614  N N   . LEU B 829  ? 0.8443 0.8443 0.8443 0.0000  0.0000  0.0000  826  LEU A N   
6615  C CA  . LEU B 829  ? 0.8443 0.8443 0.8443 0.0000  0.0000  0.0000  826  LEU A CA  
6616  C C   . LEU B 829  ? 0.8443 0.8443 0.8443 0.0000  0.0000  0.0000  826  LEU A C   
6617  O O   . LEU B 829  ? 0.8443 0.8443 0.8443 0.0000  0.0000  0.0000  826  LEU A O   
6618  C CB  . LEU B 829  ? 0.8443 0.8443 0.8443 0.0000  0.0000  0.0000  826  LEU A CB  
6619  C CG  . LEU B 829  ? 0.8443 0.8443 0.8443 0.0000  0.0000  0.0000  826  LEU A CG  
6620  C CD1 . LEU B 829  ? 0.8443 0.8443 0.8443 0.0000  0.0000  0.0000  826  LEU A CD1 
6621  C CD2 . LEU B 829  ? 0.8443 0.8443 0.8443 0.0000  0.0000  0.0000  826  LEU A CD2 
6622  N N   . TYR B 830  ? 0.8437 0.8437 0.8437 0.0000  0.0000  0.0000  827  TYR A N   
6623  C CA  . TYR B 830  ? 0.8437 0.8437 0.8437 0.0000  0.0000  0.0000  827  TYR A CA  
6624  C C   . TYR B 830  ? 0.8437 0.8437 0.8437 0.0000  0.0000  0.0000  827  TYR A C   
6625  O O   . TYR B 830  ? 0.8437 0.8437 0.8437 0.0000  0.0000  0.0000  827  TYR A O   
6626  C CB  . TYR B 830  ? 0.8437 0.8437 0.8437 0.0000  0.0000  0.0000  827  TYR A CB  
6627  C CG  . TYR B 830  ? 0.8437 0.8437 0.8437 0.0000  0.0000  0.0000  827  TYR A CG  
6628  C CD1 . TYR B 830  ? 0.8437 0.8437 0.8437 0.0000  0.0000  0.0000  827  TYR A CD1 
6629  C CD2 . TYR B 830  ? 0.8437 0.8437 0.8437 0.0000  0.0000  0.0000  827  TYR A CD2 
6630  C CE1 . TYR B 830  ? 0.8437 0.8437 0.8437 0.0000  0.0000  0.0000  827  TYR A CE1 
6631  C CE2 . TYR B 830  ? 0.8437 0.8437 0.8437 0.0000  0.0000  0.0000  827  TYR A CE2 
6632  C CZ  . TYR B 830  ? 0.8437 0.8437 0.8437 0.0000  0.0000  0.0000  827  TYR A CZ  
6633  O OH  . TYR B 830  ? 0.8437 0.8437 0.8437 0.0000  0.0000  0.0000  827  TYR A OH  
6634  N N   . ASP B 831  ? 0.8966 0.8966 0.8966 0.0000  0.0000  0.0000  828  ASP A N   
6635  C CA  . ASP B 831  ? 0.8966 0.8966 0.8966 0.0000  0.0000  0.0000  828  ASP A CA  
6636  C C   . ASP B 831  ? 0.8966 0.8966 0.8966 0.0000  0.0000  0.0000  828  ASP A C   
6637  O O   . ASP B 831  ? 0.8966 0.8966 0.8966 0.0000  0.0000  0.0000  828  ASP A O   
6638  C CB  . ASP B 831  ? 0.8966 0.8966 0.8966 0.0000  0.0000  0.0000  828  ASP A CB  
6639  C CG  . ASP B 831  ? 0.8966 0.8966 0.8966 0.0000  0.0000  0.0000  828  ASP A CG  
6640  O OD1 . ASP B 831  ? 0.8966 0.8966 0.8966 0.0000  0.0000  0.0000  828  ASP A OD1 
6641  O OD2 . ASP B 831  ? 0.8966 0.8966 0.8966 0.0000  0.0000  0.0000  828  ASP A OD2 
6642  N N   . TYR B 832  ? 0.9513 0.9513 0.9513 0.0000  0.0000  0.0000  829  TYR A N   
6643  C CA  . TYR B 832  ? 0.9513 0.9513 0.9513 0.0000  0.0000  0.0000  829  TYR A CA  
6644  C C   . TYR B 832  ? 0.9513 0.9513 0.9513 0.0000  0.0000  0.0000  829  TYR A C   
6645  O O   . TYR B 832  ? 0.9513 0.9513 0.9513 0.0000  0.0000  0.0000  829  TYR A O   
6646  C CB  . TYR B 832  ? 0.9513 0.9513 0.9513 0.0000  0.0000  0.0000  829  TYR A CB  
6647  C CG  . TYR B 832  ? 0.9513 0.9513 0.9513 0.0000  0.0000  0.0000  829  TYR A CG  
6648  C CD1 . TYR B 832  ? 0.9513 0.9513 0.9513 0.0000  0.0000  0.0000  829  TYR A CD1 
6649  C CD2 . TYR B 832  ? 0.9513 0.9513 0.9513 0.0000  0.0000  0.0000  829  TYR A CD2 
6650  C CE1 . TYR B 832  ? 0.9513 0.9513 0.9513 0.0000  0.0000  0.0000  829  TYR A CE1 
6651  C CE2 . TYR B 832  ? 0.9513 0.9513 0.9513 0.0000  0.0000  0.0000  829  TYR A CE2 
6652  C CZ  . TYR B 832  ? 0.9513 0.9513 0.9513 0.0000  0.0000  0.0000  829  TYR A CZ  
6653  O OH  . TYR B 832  ? 0.9513 0.9513 0.9513 0.0000  0.0000  0.0000  829  TYR A OH  
6654  N N   . VAL B 833  ? 0.8823 0.8823 0.8823 0.0000  0.0000  0.0000  830  VAL A N   
6655  C CA  . VAL B 833  ? 0.8823 0.8823 0.8823 0.0000  0.0000  0.0000  830  VAL A CA  
6656  C C   . VAL B 833  ? 0.8823 0.8823 0.8823 0.0000  0.0000  0.0000  830  VAL A C   
6657  O O   . VAL B 833  ? 0.8823 0.8823 0.8823 0.0000  0.0000  0.0000  830  VAL A O   
6658  C CB  . VAL B 833  ? 0.8823 0.8823 0.8823 0.0000  0.0000  0.0000  830  VAL A CB  
6659  C CG1 . VAL B 833  ? 0.8823 0.8823 0.8823 0.0000  0.0000  0.0000  830  VAL A CG1 
6660  C CG2 . VAL B 833  ? 0.8823 0.8823 0.8823 0.0000  0.0000  0.0000  830  VAL A CG2 
6661  N N   . ASN B 834  ? 0.9414 0.9414 0.9414 0.0000  0.0000  0.0000  831  ASN A N   
6662  C CA  . ASN B 834  ? 0.9414 0.9414 0.9414 0.0000  0.0000  0.0000  831  ASN A CA  
6663  C C   . ASN B 834  ? 0.9414 0.9414 0.9414 0.0000  0.0000  0.0000  831  ASN A C   
6664  O O   . ASN B 834  ? 0.9414 0.9414 0.9414 0.0000  0.0000  0.0000  831  ASN A O   
6665  C CB  . ASN B 834  ? 0.9414 0.9414 0.9414 0.0000  0.0000  0.0000  831  ASN A CB  
6666  C CG  . ASN B 834  ? 0.9414 0.9414 0.9414 0.0000  0.0000  0.0000  831  ASN A CG  
6667  O OD1 . ASN B 834  ? 0.9414 0.9414 0.9414 0.0000  0.0000  0.0000  831  ASN A OD1 
6668  N ND2 . ASN B 834  ? 0.9414 0.9414 0.9414 0.0000  0.0000  0.0000  831  ASN A ND2 
6669  N N   . HIS B 835  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  832  HIS A N   
6670  C CA  . HIS B 835  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  832  HIS A CA  
6671  C C   . HIS B 835  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  832  HIS A C   
6672  O O   . HIS B 835  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  832  HIS A O   
6673  C CB  . HIS B 835  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  832  HIS A CB  
6674  C CG  . HIS B 835  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  832  HIS A CG  
6675  N ND1 . HIS B 835  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  832  HIS A ND1 
6676  C CD2 . HIS B 835  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  832  HIS A CD2 
6677  C CE1 . HIS B 835  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  832  HIS A CE1 
6678  N NE2 . HIS B 835  ? 0.9518 0.9518 0.9518 0.0000  0.0000  0.0000  832  HIS A NE2 
6679  N N   . ARG B 836  ? 1.0183 1.0183 1.0183 0.0000  0.0000  0.0000  833  ARG A N   
6680  C CA  . ARG B 836  ? 1.0183 1.0183 1.0183 0.0000  0.0000  0.0000  833  ARG A CA  
6681  C C   . ARG B 836  ? 1.0183 1.0183 1.0183 0.0000  0.0000  0.0000  833  ARG A C   
6682  O O   . ARG B 836  ? 1.0183 1.0183 1.0183 0.0000  0.0000  0.0000  833  ARG A O   
6683  C CB  . ARG B 836  ? 1.0183 1.0183 1.0183 0.0000  0.0000  0.0000  833  ARG A CB  
6684  C CG  . ARG B 836  ? 1.0183 1.0183 1.0183 0.0000  0.0000  0.0000  833  ARG A CG  
6685  C CD  . ARG B 836  ? 1.0183 1.0183 1.0183 0.0000  0.0000  0.0000  833  ARG A CD  
6686  N NE  . ARG B 836  ? 1.0183 1.0183 1.0183 0.0000  0.0000  0.0000  833  ARG A NE  
6687  C CZ  . ARG B 836  ? 1.0183 1.0183 1.0183 0.0000  0.0000  0.0000  833  ARG A CZ  
6688  N NH1 . ARG B 836  ? 1.0183 1.0183 1.0183 0.0000  0.0000  0.0000  833  ARG A NH1 
6689  N NH2 . ARG B 836  ? 1.0183 1.0183 1.0183 0.0000  0.0000  0.0000  833  ARG A NH2 
6690  N N   . LEU B 837  ? 1.1694 1.1694 1.1694 0.0000  0.0000  0.0000  834  LEU A N   
6691  C CA  . LEU B 837  ? 1.1694 1.1694 1.1694 0.0000  0.0000  0.0000  834  LEU A CA  
6692  C C   . LEU B 837  ? 1.1694 1.1694 1.1694 0.0000  0.0000  0.0000  834  LEU A C   
6693  O O   . LEU B 837  ? 1.1694 1.1694 1.1694 0.0000  0.0000  0.0000  834  LEU A O   
6694  C CB  . LEU B 837  ? 1.1694 1.1694 1.1694 0.0000  0.0000  0.0000  834  LEU A CB  
6695  C CG  . LEU B 837  ? 1.1694 1.1694 1.1694 0.0000  0.0000  0.0000  834  LEU A CG  
6696  C CD1 . LEU B 837  ? 1.1694 1.1694 1.1694 0.0000  0.0000  0.0000  834  LEU A CD1 
6697  C CD2 . LEU B 837  ? 1.1694 1.1694 1.1694 0.0000  0.0000  0.0000  834  LEU A CD2 
6698  N N   . SER B 838  ? 1.3675 1.3675 1.3675 0.0000  0.0000  0.0000  835  SER A N   
6699  C CA  . SER B 838  ? 1.3675 1.3675 1.3675 0.0000  0.0000  0.0000  835  SER A CA  
6700  C C   . SER B 838  ? 1.3675 1.3675 1.3675 0.0000  0.0000  0.0000  835  SER A C   
6701  O O   . SER B 838  ? 1.3675 1.3675 1.3675 0.0000  0.0000  0.0000  835  SER A O   
6702  C CB  . SER B 838  ? 1.3675 1.3675 1.3675 0.0000  0.0000  0.0000  835  SER A CB  
6703  O OG  . SER B 838  ? 1.3675 1.3675 1.3675 0.0000  0.0000  0.0000  835  SER A OG  
6704  N N   . HIS B 839  ? 1.4021 1.4021 1.4021 0.0000  0.0000  0.0000  836  HIS A N   
6705  C CA  . HIS B 839  ? 1.4021 1.4021 1.4021 0.0000  0.0000  0.0000  836  HIS A CA  
6706  C C   . HIS B 839  ? 1.4021 1.4021 1.4021 0.0000  0.0000  0.0000  836  HIS A C   
6707  O O   . HIS B 839  ? 1.4021 1.4021 1.4021 0.0000  0.0000  0.0000  836  HIS A O   
6708  C CB  . HIS B 839  ? 1.4021 1.4021 1.4021 0.0000  0.0000  0.0000  836  HIS A CB  
6709  C CG  . HIS B 839  ? 1.4021 1.4021 1.4021 0.0000  0.0000  0.0000  836  HIS A CG  
6710  N ND1 . HIS B 839  ? 1.4021 1.4021 1.4021 0.0000  0.0000  0.0000  836  HIS A ND1 
6711  C CD2 . HIS B 839  ? 1.4021 1.4021 1.4021 0.0000  0.0000  0.0000  836  HIS A CD2 
6712  C CE1 . HIS B 839  ? 1.4021 1.4021 1.4021 0.0000  0.0000  0.0000  836  HIS A CE1 
6713  N NE2 . HIS B 839  ? 1.4021 1.4021 1.4021 0.0000  0.0000  0.0000  836  HIS A NE2 
6714  N N   . ASP B 840  ? 1.3536 1.3536 1.3536 0.0000  0.0000  0.0000  837  ASP A N   
6715  C CA  . ASP B 840  ? 1.3536 1.3536 1.3536 0.0000  0.0000  0.0000  837  ASP A CA  
6716  C C   . ASP B 840  ? 1.3536 1.3536 1.3536 0.0000  0.0000  0.0000  837  ASP A C   
6717  O O   . ASP B 840  ? 1.3536 1.3536 1.3536 0.0000  0.0000  0.0000  837  ASP A O   
6718  C CB  . ASP B 840  ? 1.3536 1.3536 1.3536 0.0000  0.0000  0.0000  837  ASP A CB  
6719  C CG  . ASP B 840  ? 1.3536 1.3536 1.3536 0.0000  0.0000  0.0000  837  ASP A CG  
6720  O OD1 . ASP B 840  ? 1.3536 1.3536 1.3536 0.0000  0.0000  0.0000  837  ASP A OD1 
6721  O OD2 . ASP B 840  ? 1.3536 1.3536 1.3536 0.0000  0.0000  0.0000  837  ASP A OD2 
6722  N N   . LEU B 841  ? 1.1442 1.1442 1.1442 0.0000  0.0000  0.0000  838  LEU A N   
6723  C CA  . LEU B 841  ? 1.1442 1.1442 1.1442 0.0000  0.0000  0.0000  838  LEU A CA  
6724  C C   . LEU B 841  ? 1.1442 1.1442 1.1442 0.0000  0.0000  0.0000  838  LEU A C   
6725  O O   . LEU B 841  ? 1.1442 1.1442 1.1442 0.0000  0.0000  0.0000  838  LEU A O   
6726  C CB  . LEU B 841  ? 1.1442 1.1442 1.1442 0.0000  0.0000  0.0000  838  LEU A CB  
6727  C CG  . LEU B 841  ? 1.1442 1.1442 1.1442 0.0000  0.0000  0.0000  838  LEU A CG  
6728  C CD1 . LEU B 841  ? 1.1442 1.1442 1.1442 0.0000  0.0000  0.0000  838  LEU A CD1 
6729  C CD2 . LEU B 841  ? 1.1442 1.1442 1.1442 0.0000  0.0000  0.0000  838  LEU A CD2 
6730  N N   . SER B 842  ? 1.0767 1.0767 1.0767 0.0000  0.0000  0.0000  839  SER A N   
6731  C CA  . SER B 842  ? 1.0767 1.0767 1.0767 0.0000  0.0000  0.0000  839  SER A CA  
6732  C C   . SER B 842  ? 1.0767 1.0767 1.0767 0.0000  0.0000  0.0000  839  SER A C   
6733  O O   . SER B 842  ? 1.0767 1.0767 1.0767 0.0000  0.0000  0.0000  839  SER A O   
6734  C CB  . SER B 842  ? 1.0767 1.0767 1.0767 0.0000  0.0000  0.0000  839  SER A CB  
6735  O OG  . SER B 842  ? 1.0767 1.0767 1.0767 0.0000  0.0000  0.0000  839  SER A OG  
6736  N N   . ASP B 843  ? 1.0510 1.0510 1.0510 0.0000  0.0000  0.0000  840  ASP A N   
6737  C CA  . ASP B 843  ? 1.0510 1.0510 1.0510 0.0000  0.0000  0.0000  840  ASP A CA  
6738  C C   . ASP B 843  ? 1.0510 1.0510 1.0510 0.0000  0.0000  0.0000  840  ASP A C   
6739  O O   . ASP B 843  ? 1.0510 1.0510 1.0510 0.0000  0.0000  0.0000  840  ASP A O   
6740  C CB  . ASP B 843  ? 1.0510 1.0510 1.0510 0.0000  0.0000  0.0000  840  ASP A CB  
6741  C CG  . ASP B 843  ? 1.0510 1.0510 1.0510 0.0000  0.0000  0.0000  840  ASP A CG  
6742  O OD1 . ASP B 843  ? 1.0510 1.0510 1.0510 0.0000  0.0000  0.0000  840  ASP A OD1 
6743  O OD2 . ASP B 843  ? 1.0510 1.0510 1.0510 0.0000  0.0000  0.0000  840  ASP A OD2 
6744  N N   . GLU B 844  ? 0.9987 0.9987 0.9987 0.0000  0.0000  0.0000  841  GLU A N   
6745  C CA  . GLU B 844  ? 0.9987 0.9987 0.9987 0.0000  0.0000  0.0000  841  GLU A CA  
6746  C C   . GLU B 844  ? 0.9987 0.9987 0.9987 0.0000  0.0000  0.0000  841  GLU A C   
6747  O O   . GLU B 844  ? 0.9987 0.9987 0.9987 0.0000  0.0000  0.0000  841  GLU A O   
6748  C CB  . GLU B 844  ? 0.9987 0.9987 0.9987 0.0000  0.0000  0.0000  841  GLU A CB  
6749  C CG  . GLU B 844  ? 0.9987 0.9987 0.9987 0.0000  0.0000  0.0000  841  GLU A CG  
6750  C CD  . GLU B 844  ? 0.9987 0.9987 0.9987 0.0000  0.0000  0.0000  841  GLU A CD  
6751  O OE1 . GLU B 844  ? 0.9987 0.9987 0.9987 0.0000  0.0000  0.0000  841  GLU A OE1 
6752  O OE2 . GLU B 844  ? 0.9987 0.9987 0.9987 0.0000  0.0000  0.0000  841  GLU A OE2 
6753  N N   . ALA B 845  ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  842  ALA A N   
6754  C CA  . ALA B 845  ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  842  ALA A CA  
6755  C C   . ALA B 845  ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  842  ALA A C   
6756  O O   . ALA B 845  ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  842  ALA A O   
6757  C CB  . ALA B 845  ? 0.9655 0.9655 0.9655 0.0000  0.0000  0.0000  842  ALA A CB  
6758  N N   . ARG B 846  ? 1.0274 1.0274 1.0274 0.0000  0.0000  0.0000  843  ARG A N   
6759  C CA  . ARG B 846  ? 1.0274 1.0274 1.0274 0.0000  0.0000  0.0000  843  ARG A CA  
6760  C C   . ARG B 846  ? 1.0274 1.0274 1.0274 0.0000  0.0000  0.0000  843  ARG A C   
6761  O O   . ARG B 846  ? 1.0274 1.0274 1.0274 0.0000  0.0000  0.0000  843  ARG A O   
6762  C CB  . ARG B 846  ? 1.0274 1.0274 1.0274 0.0000  0.0000  0.0000  843  ARG A CB  
6763  C CG  . ARG B 846  ? 1.0274 1.0274 1.0274 0.0000  0.0000  0.0000  843  ARG A CG  
6764  C CD  . ARG B 846  ? 1.0274 1.0274 1.0274 0.0000  0.0000  0.0000  843  ARG A CD  
6765  N NE  . ARG B 846  ? 1.0274 1.0274 1.0274 0.0000  0.0000  0.0000  843  ARG A NE  
6766  C CZ  . ARG B 846  ? 1.0274 1.0274 1.0274 0.0000  0.0000  0.0000  843  ARG A CZ  
6767  N NH1 . ARG B 846  ? 1.0274 1.0274 1.0274 0.0000  0.0000  0.0000  843  ARG A NH1 
6768  N NH2 . ARG B 846  ? 1.0274 1.0274 1.0274 0.0000  0.0000  0.0000  843  ARG A NH2 
6769  N N   . ALA B 847  ? 0.8812 0.8812 0.8812 0.0000  0.0000  0.0000  844  ALA A N   
6770  C CA  . ALA B 847  ? 0.8812 0.8812 0.8812 0.0000  0.0000  0.0000  844  ALA A CA  
6771  C C   . ALA B 847  ? 0.8812 0.8812 0.8812 0.0000  0.0000  0.0000  844  ALA A C   
6772  O O   . ALA B 847  ? 0.8812 0.8812 0.8812 0.0000  0.0000  0.0000  844  ALA A O   
6773  C CB  . ALA B 847  ? 0.8812 0.8812 0.8812 0.0000  0.0000  0.0000  844  ALA A CB  
6774  N N   . LEU B 848  ? 0.8192 0.8192 0.8192 0.0000  0.0000  0.0000  845  LEU A N   
6775  C CA  . LEU B 848  ? 0.8192 0.8192 0.8192 0.0000  0.0000  0.0000  845  LEU A CA  
6776  C C   . LEU B 848  ? 0.8192 0.8192 0.8192 0.0000  0.0000  0.0000  845  LEU A C   
6777  O O   . LEU B 848  ? 0.8192 0.8192 0.8192 0.0000  0.0000  0.0000  845  LEU A O   
6778  C CB  . LEU B 848  ? 0.8192 0.8192 0.8192 0.0000  0.0000  0.0000  845  LEU A CB  
6779  C CG  . LEU B 848  ? 0.8192 0.8192 0.8192 0.0000  0.0000  0.0000  845  LEU A CG  
6780  C CD1 . LEU B 848  ? 0.8192 0.8192 0.8192 0.0000  0.0000  0.0000  845  LEU A CD1 
6781  C CD2 . LEU B 848  ? 0.8192 0.8192 0.8192 0.0000  0.0000  0.0000  845  LEU A CD2 
6782  N N   . LEU B 849  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  846  LEU A N   
6783  C CA  . LEU B 849  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  846  LEU A CA  
6784  C C   . LEU B 849  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  846  LEU A C   
6785  O O   . LEU B 849  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  846  LEU A O   
6786  C CB  . LEU B 849  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  846  LEU A CB  
6787  C CG  . LEU B 849  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  846  LEU A CG  
6788  C CD1 . LEU B 849  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  846  LEU A CD1 
6789  C CD2 . LEU B 849  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  846  LEU A CD2 
6790  N N   . PRO B 850  ? 0.7885 0.7885 0.7885 0.0000  0.0000  0.0000  847  PRO A N   
6791  C CA  . PRO B 850  ? 0.7885 0.7885 0.7885 0.0000  0.0000  0.0000  847  PRO A CA  
6792  C C   . PRO B 850  ? 0.7885 0.7885 0.7885 0.0000  0.0000  0.0000  847  PRO A C   
6793  O O   . PRO B 850  ? 0.7885 0.7885 0.7885 0.0000  0.0000  0.0000  847  PRO A O   
6794  C CB  . PRO B 850  ? 0.7885 0.7885 0.7885 0.0000  0.0000  0.0000  847  PRO A CB  
6795  C CG  . PRO B 850  ? 0.7885 0.7885 0.7885 0.0000  0.0000  0.0000  847  PRO A CG  
6796  C CD  . PRO B 850  ? 0.7885 0.7885 0.7885 0.0000  0.0000  0.0000  847  PRO A CD  
6797  N N   . ASN B 851  ? 0.7622 0.7622 0.7622 0.0000  0.0000  0.0000  848  ASN A N   
6798  C CA  . ASN B 851  ? 0.7622 0.7622 0.7622 0.0000  0.0000  0.0000  848  ASN A CA  
6799  C C   . ASN B 851  ? 0.7622 0.7622 0.7622 0.0000  0.0000  0.0000  848  ASN A C   
6800  O O   . ASN B 851  ? 0.7622 0.7622 0.7622 0.0000  0.0000  0.0000  848  ASN A O   
6801  C CB  . ASN B 851  ? 0.7622 0.7622 0.7622 0.0000  0.0000  0.0000  848  ASN A CB  
6802  C CG  . ASN B 851  ? 0.7622 0.7622 0.7622 0.0000  0.0000  0.0000  848  ASN A CG  
6803  O OD1 . ASN B 851  ? 0.7622 0.7622 0.7622 0.0000  0.0000  0.0000  848  ASN A OD1 
6804  N ND2 . ASN B 851  ? 0.7622 0.7622 0.7622 0.0000  0.0000  0.0000  848  ASN A ND2 
6805  N N   . VAL B 852  ? 0.7164 0.7164 0.7164 0.0000  0.0000  0.0000  849  VAL A N   
6806  C CA  . VAL B 852  ? 0.7164 0.7164 0.7164 0.0000  0.0000  0.0000  849  VAL A CA  
6807  C C   . VAL B 852  ? 0.7164 0.7164 0.7164 0.0000  0.0000  0.0000  849  VAL A C   
6808  O O   . VAL B 852  ? 0.7164 0.7164 0.7164 0.0000  0.0000  0.0000  849  VAL A O   
6809  C CB  . VAL B 852  ? 0.7164 0.7164 0.7164 0.0000  0.0000  0.0000  849  VAL A CB  
6810  C CG1 . VAL B 852  ? 0.7164 0.7164 0.7164 0.0000  0.0000  0.0000  849  VAL A CG1 
6811  C CG2 . VAL B 852  ? 0.7164 0.7164 0.7164 0.0000  0.0000  0.0000  849  VAL A CG2 
6812  N N   . ILE B 853  ? 0.7096 0.7096 0.7096 0.0000  0.0000  0.0000  850  ILE A N   
6813  C CA  . ILE B 853  ? 0.7096 0.7096 0.7096 0.0000  0.0000  0.0000  850  ILE A CA  
6814  C C   . ILE B 853  ? 0.7096 0.7096 0.7096 0.0000  0.0000  0.0000  850  ILE A C   
6815  O O   . ILE B 853  ? 0.7096 0.7096 0.7096 0.0000  0.0000  0.0000  850  ILE A O   
6816  C CB  . ILE B 853  ? 0.7096 0.7096 0.7096 0.0000  0.0000  0.0000  850  ILE A CB  
6817  C CG1 . ILE B 853  ? 0.7096 0.7096 0.7096 0.0000  0.0000  0.0000  850  ILE A CG1 
6818  C CG2 . ILE B 853  ? 0.7096 0.7096 0.7096 0.0000  0.0000  0.0000  850  ILE A CG2 
6819  C CD1 . ILE B 853  ? 0.7096 0.7096 0.7096 0.0000  0.0000  0.0000  850  ILE A CD1 
6820  N N   . THR B 854  ? 0.7228 0.7228 0.7228 0.0000  0.0000  0.0000  851  THR A N   
6821  C CA  . THR B 854  ? 0.7228 0.7228 0.7228 0.0000  0.0000  0.0000  851  THR A CA  
6822  C C   . THR B 854  ? 0.7228 0.7228 0.7228 0.0000  0.0000  0.0000  851  THR A C   
6823  O O   . THR B 854  ? 0.7228 0.7228 0.7228 0.0000  0.0000  0.0000  851  THR A O   
6824  C CB  . THR B 854  ? 0.7228 0.7228 0.7228 0.0000  0.0000  0.0000  851  THR A CB  
6825  O OG1 . THR B 854  ? 0.7228 0.7228 0.7228 0.0000  0.0000  0.0000  851  THR A OG1 
6826  C CG2 . THR B 854  ? 0.7228 0.7228 0.7228 0.0000  0.0000  0.0000  851  THR A CG2 
6827  N N   . LYS B 855  ? 0.7184 0.7184 0.7184 0.0000  0.0000  0.0000  852  LYS A N   
6828  C CA  . LYS B 855  ? 0.7184 0.7184 0.7184 0.0000  0.0000  0.0000  852  LYS A CA  
6829  C C   . LYS B 855  ? 0.7184 0.7184 0.7184 0.0000  0.0000  0.0000  852  LYS A C   
6830  O O   . LYS B 855  ? 0.7184 0.7184 0.7184 0.0000  0.0000  0.0000  852  LYS A O   
6831  C CB  . LYS B 855  ? 0.7184 0.7184 0.7184 0.0000  0.0000  0.0000  852  LYS A CB  
6832  C CG  . LYS B 855  ? 0.7184 0.7184 0.7184 0.0000  0.0000  0.0000  852  LYS A CG  
6833  C CD  . LYS B 855  ? 0.7184 0.7184 0.7184 0.0000  0.0000  0.0000  852  LYS A CD  
6834  C CE  . LYS B 855  ? 0.7184 0.7184 0.7184 0.0000  0.0000  0.0000  852  LYS A CE  
6835  N NZ  . LYS B 855  ? 0.7184 0.7184 0.7184 0.0000  0.0000  0.0000  852  LYS A NZ  
6836  N N   . GLU B 856  ? 0.7729 0.7729 0.7729 0.0000  0.0000  0.0000  853  GLU A N   
6837  C CA  . GLU B 856  ? 0.7729 0.7729 0.7729 0.0000  0.0000  0.0000  853  GLU A CA  
6838  C C   . GLU B 856  ? 0.7729 0.7729 0.7729 0.0000  0.0000  0.0000  853  GLU A C   
6839  O O   . GLU B 856  ? 0.7729 0.7729 0.7729 0.0000  0.0000  0.0000  853  GLU A O   
6845  N N   . VAL B 857  ? 0.7817 0.7817 0.7817 0.0000  0.0000  0.0000  854  VAL A N   
6846  C CA  . VAL B 857  ? 0.7817 0.7817 0.7817 0.0000  0.0000  0.0000  854  VAL A CA  
6847  C C   . VAL B 857  ? 0.7817 0.7817 0.7817 0.0000  0.0000  0.0000  854  VAL A C   
6848  O O   . VAL B 857  ? 0.7817 0.7817 0.7817 0.0000  0.0000  0.0000  854  VAL A O   
6849  C CB  . VAL B 857  ? 0.7817 0.7817 0.7817 0.0000  0.0000  0.0000  854  VAL A CB  
6850  C CG1 . VAL B 857  ? 0.7817 0.7817 0.7817 0.0000  0.0000  0.0000  854  VAL A CG1 
6851  C CG2 . VAL B 857  ? 0.7817 0.7817 0.7817 0.0000  0.0000  0.0000  854  VAL A CG2 
6852  N N   . SER B 858  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  855  SER A N   
6853  C CA  . SER B 858  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  855  SER A CA  
6854  C C   . SER B 858  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  855  SER A C   
6855  O O   . SER B 858  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  855  SER A O   
6856  C CB  . SER B 858  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  855  SER A CB  
6857  O OG  . SER B 858  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  855  SER A OG  
6858  N N   . HIS B 859  ? 0.7046 0.7046 0.7046 0.0000  0.0000  0.0000  856  HIS A N   
6859  C CA  . HIS B 859  ? 0.7046 0.7046 0.7046 0.0000  0.0000  0.0000  856  HIS A CA  
6860  C C   . HIS B 859  ? 0.7046 0.7046 0.7046 0.0000  0.0000  0.0000  856  HIS A C   
6861  O O   . HIS B 859  ? 0.7046 0.7046 0.7046 0.0000  0.0000  0.0000  856  HIS A O   
6862  C CB  . HIS B 859  ? 0.7046 0.7046 0.7046 0.0000  0.0000  0.0000  856  HIS A CB  
6863  C CG  . HIS B 859  ? 0.7046 0.7046 0.7046 0.0000  0.0000  0.0000  856  HIS A CG  
6864  N ND1 . HIS B 859  ? 0.7046 0.7046 0.7046 0.0000  0.0000  0.0000  856  HIS A ND1 
6865  C CD2 . HIS B 859  ? 0.7046 0.7046 0.7046 0.0000  0.0000  0.0000  856  HIS A CD2 
6866  C CE1 . HIS B 859  ? 0.7046 0.7046 0.7046 0.0000  0.0000  0.0000  856  HIS A CE1 
6867  N NE2 . HIS B 859  ? 0.7046 0.7046 0.7046 0.0000  0.0000  0.0000  856  HIS A NE2 
6868  N N   . GLU B 860  ? 0.6678 0.6678 0.6678 0.0000  0.0000  0.0000  857  GLU A N   
6869  C CA  . GLU B 860  ? 0.6678 0.6678 0.6678 0.0000  0.0000  0.0000  857  GLU A CA  
6870  C C   . GLU B 860  ? 0.6678 0.6678 0.6678 0.0000  0.0000  0.0000  857  GLU A C   
6871  O O   . GLU B 860  ? 0.6678 0.6678 0.6678 0.0000  0.0000  0.0000  857  GLU A O   
6872  C CB  . GLU B 860  ? 0.6678 0.6678 0.6678 0.0000  0.0000  0.0000  857  GLU A CB  
6873  C CG  . GLU B 860  ? 0.6678 0.6678 0.6678 0.0000  0.0000  0.0000  857  GLU A CG  
6874  C CD  . GLU B 860  ? 0.6678 0.6678 0.6678 0.0000  0.0000  0.0000  857  GLU A CD  
6875  O OE1 . GLU B 860  ? 0.6678 0.6678 0.6678 0.0000  0.0000  0.0000  857  GLU A OE1 
6876  O OE2 . GLU B 860  ? 0.6678 0.6678 0.6678 0.0000  0.0000  0.0000  857  GLU A OE2 
6877  N N   . ILE B 861  ? 0.6195 0.6195 0.6195 0.0000  0.0000  0.0000  858  ILE A N   
6878  C CA  . ILE B 861  ? 0.6195 0.6195 0.6195 0.0000  0.0000  0.0000  858  ILE A CA  
6879  C C   . ILE B 861  ? 0.6195 0.6195 0.6195 0.0000  0.0000  0.0000  858  ILE A C   
6880  O O   . ILE B 861  ? 0.6195 0.6195 0.6195 0.0000  0.0000  0.0000  858  ILE A O   
6881  C CB  . ILE B 861  ? 0.6195 0.6195 0.6195 0.0000  0.0000  0.0000  858  ILE A CB  
6882  C CG1 . ILE B 861  ? 0.6195 0.6195 0.6195 0.0000  0.0000  0.0000  858  ILE A CG1 
6883  C CG2 . ILE B 861  ? 0.6195 0.6195 0.6195 0.0000  0.0000  0.0000  858  ILE A CG2 
6884  C CD1 . ILE B 861  ? 0.6195 0.6195 0.6195 0.0000  0.0000  0.0000  858  ILE A CD1 
6885  N N   . ILE B 862  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  859  ILE A N   
6886  C CA  . ILE B 862  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  859  ILE A CA  
6887  C C   . ILE B 862  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  859  ILE A C   
6888  O O   . ILE B 862  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  859  ILE A O   
6889  C CB  . ILE B 862  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  859  ILE A CB  
6890  C CG1 . ILE B 862  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  859  ILE A CG1 
6891  C CG2 . ILE B 862  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  859  ILE A CG2 
6892  C CD1 . ILE B 862  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  859  ILE A CD1 
6893  N N   . LYS B 863  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  860  LYS A N   
6894  C CA  . LYS B 863  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  860  LYS A CA  
6895  C C   . LYS B 863  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  860  LYS A C   
6896  O O   . LYS B 863  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  860  LYS A O   
6897  C CB  . LYS B 863  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  860  LYS A CB  
6898  C CG  . LYS B 863  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  860  LYS A CG  
6899  C CD  . LYS B 863  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  860  LYS A CD  
6900  C CE  . LYS B 863  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  860  LYS A CE  
6901  N NZ  . LYS B 863  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  860  LYS A NZ  
6902  N N   . ASP B 864  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  861  ASP A N   
6903  C CA  . ASP B 864  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  861  ASP A CA  
6904  C C   . ASP B 864  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  861  ASP A C   
6905  O O   . ASP B 864  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  861  ASP A O   
6910  N N   . ARG B 865  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  862  ARG A N   
6911  C CA  . ARG B 865  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  862  ARG A CA  
6912  C C   . ARG B 865  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  862  ARG A C   
6913  O O   . ARG B 865  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  862  ARG A O   
6921  N N   . ARG B 866  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  863  ARG A N   
6922  C CA  . ARG B 866  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  863  ARG A CA  
6923  C C   . ARG B 866  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  863  ARG A C   
6924  O O   . ARG B 866  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  863  ARG A O   
6925  C CB  . ARG B 866  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  863  ARG A CB  
6926  C CG  . ARG B 866  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  863  ARG A CG  
6927  C CD  . ARG B 866  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  863  ARG A CD  
6928  N NE  . ARG B 866  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  863  ARG A NE  
6929  C CZ  . ARG B 866  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  863  ARG A CZ  
6930  N NH1 . ARG B 866  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  863  ARG A NH1 
6931  N NH2 . ARG B 866  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  863  ARG A NH2 
6932  N N   . PHE B 867  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  864  PHE A N   
6933  C CA  . PHE B 867  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  864  PHE A CA  
6934  C C   . PHE B 867  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  864  PHE A C   
6935  O O   . PHE B 867  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  864  PHE A O   
6936  C CB  . PHE B 867  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  864  PHE A CB  
6937  C CG  . PHE B 867  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  864  PHE A CG  
6938  C CD1 . PHE B 867  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  864  PHE A CD1 
6939  C CD2 . PHE B 867  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  864  PHE A CD2 
6940  C CE1 . PHE B 867  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  864  PHE A CE1 
6941  C CE2 . PHE B 867  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  864  PHE A CE2 
6942  C CZ  . PHE B 867  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  864  PHE A CZ  
6943  N N   . THR B 868  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  865  THR A N   
6944  C CA  . THR B 868  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  865  THR A CA  
6945  C C   . THR B 868  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  865  THR A C   
6946  O O   . THR B 868  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  865  THR A O   
6947  C CB  . THR B 868  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  865  THR A CB  
6948  O OG1 . THR B 868  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  865  THR A OG1 
6949  C CG2 . THR B 868  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  865  THR A CG2 
6950  N N   . SER B 869  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  866  SER A N   
6951  C CA  . SER B 869  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  866  SER A CA  
6952  C C   . SER B 869  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  866  SER A C   
6953  O O   . SER B 869  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  866  SER A O   
6954  C CB  . SER B 869  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  866  SER A CB  
6955  O OG  . SER B 869  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  866  SER A OG  
6956  N N   . ASP B 870  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  867  ASP A N   
6957  C CA  . ASP B 870  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  867  ASP A CA  
6958  C C   . ASP B 870  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  867  ASP A C   
6959  O O   . ASP B 870  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  867  ASP A O   
6960  C CB  . ASP B 870  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  867  ASP A CB  
6961  C CG  . ASP B 870  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  867  ASP A CG  
6962  O OD1 . ASP B 870  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  867  ASP A OD1 
6963  O OD2 . ASP B 870  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  867  ASP A OD2 
6964  N N   . LYS B 871  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  868  LYS A N   
6965  C CA  . LYS B 871  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  868  LYS A CA  
6966  C C   . LYS B 871  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  868  LYS A C   
6967  O O   . LYS B 871  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  868  LYS A O   
6968  C CB  . LYS B 871  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  868  LYS A CB  
6969  C CG  . LYS B 871  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  868  LYS A CG  
6970  C CD  . LYS B 871  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  868  LYS A CD  
6971  C CE  . LYS B 871  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  868  LYS A CE  
6972  N NZ  . LYS B 871  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  868  LYS A NZ  
6973  N N   . PHE B 872  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  869  PHE A N   
6974  C CA  . PHE B 872  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  869  PHE A CA  
6975  C C   . PHE B 872  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  869  PHE A C   
6976  O O   . PHE B 872  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  869  PHE A O   
6977  C CB  . PHE B 872  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  869  PHE A CB  
6978  C CG  . PHE B 872  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  869  PHE A CG  
6979  C CD1 . PHE B 872  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  869  PHE A CD1 
6980  C CD2 . PHE B 872  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  869  PHE A CD2 
6981  C CE1 . PHE B 872  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  869  PHE A CE1 
6982  C CE2 . PHE B 872  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  869  PHE A CE2 
6983  C CZ  . PHE B 872  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  869  PHE A CZ  
6984  N N   . PHE B 873  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  870  PHE A N   
6985  C CA  . PHE B 873  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  870  PHE A CA  
6986  C C   . PHE B 873  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  870  PHE A C   
6987  O O   . PHE B 873  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  870  PHE A O   
6988  C CB  . PHE B 873  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  870  PHE A CB  
6989  C CG  . PHE B 873  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  870  PHE A CG  
6990  C CD1 . PHE B 873  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  870  PHE A CD1 
6991  C CD2 . PHE B 873  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  870  PHE A CD2 
6992  C CE1 . PHE B 873  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  870  PHE A CE1 
6993  C CE2 . PHE B 873  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  870  PHE A CE2 
6994  C CZ  . PHE B 873  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  870  PHE A CZ  
6995  N N   . PHE B 874  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  871  PHE A N   
6996  C CA  . PHE B 874  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  871  PHE A CA  
6997  C C   . PHE B 874  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  871  PHE A C   
6998  O O   . PHE B 874  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  871  PHE A O   
6999  C CB  . PHE B 874  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  871  PHE A CB  
7000  C CG  . PHE B 874  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  871  PHE A CG  
7001  C CD1 . PHE B 874  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  871  PHE A CD1 
7002  C CD2 . PHE B 874  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  871  PHE A CD2 
7003  C CE1 . PHE B 874  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  871  PHE A CE1 
7004  C CE2 . PHE B 874  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  871  PHE A CE2 
7005  C CZ  . PHE B 874  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  871  PHE A CZ  
7006  N N   . HIS B 875  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  872  HIS A N   
7007  C CA  . HIS B 875  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  872  HIS A CA  
7008  C C   . HIS B 875  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  872  HIS A C   
7009  O O   . HIS B 875  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  872  HIS A O   
7010  C CB  . HIS B 875  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  872  HIS A CB  
7011  C CG  . HIS B 875  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  872  HIS A CG  
7012  N ND1 . HIS B 875  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  872  HIS A ND1 
7013  C CD2 . HIS B 875  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  872  HIS A CD2 
7014  C CE1 . HIS B 875  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  872  HIS A CE1 
7015  N NE2 . HIS B 875  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  872  HIS A NE2 
7016  N N   . VAL B 876  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  873  VAL A N   
7017  C CA  . VAL B 876  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  873  VAL A CA  
7018  C C   . VAL B 876  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  873  VAL A C   
7019  O O   . VAL B 876  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  873  VAL A O   
7020  C CB  . VAL B 876  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  873  VAL A CB  
7021  C CG1 . VAL B 876  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  873  VAL A CG1 
7022  C CG2 . VAL B 876  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  873  VAL A CG2 
7023  N N   . PRO B 877  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  874  PRO A N   
7024  C CA  . PRO B 877  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  874  PRO A CA  
7025  C C   . PRO B 877  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  874  PRO A C   
7026  O O   . PRO B 877  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  874  PRO A O   
7027  C CB  . PRO B 877  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  874  PRO A CB  
7028  C CG  . PRO B 877  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  874  PRO A CG  
7029  C CD  . PRO B 877  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  874  PRO A CD  
7030  N N   . ILE B 878  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  875  ILE A N   
7031  C CA  . ILE B 878  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  875  ILE A CA  
7032  C C   . ILE B 878  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  875  ILE A C   
7033  O O   . ILE B 878  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  875  ILE A O   
7034  C CB  . ILE B 878  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  875  ILE A CB  
7035  C CG1 . ILE B 878  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  875  ILE A CG1 
7036  C CG2 . ILE B 878  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  875  ILE A CG2 
7037  C CD1 . ILE B 878  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  875  ILE A CD1 
7038  N N   . THR B 879  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  876  THR A N   
7039  C CA  . THR B 879  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  876  THR A CA  
7040  C C   . THR B 879  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  876  THR A C   
7041  O O   . THR B 879  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  876  THR A O   
7042  C CB  . THR B 879  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  876  THR A CB  
7043  O OG1 . THR B 879  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  876  THR A OG1 
7044  C CG2 . THR B 879  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  876  THR A CG2 
7045  N N   . LEU B 880  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  877  LEU A N   
7046  C CA  . LEU B 880  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  877  LEU A CA  
7047  C C   . LEU B 880  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  877  LEU A C   
7048  O O   . LEU B 880  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  877  LEU A O   
7049  C CB  . LEU B 880  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  877  LEU A CB  
7050  C CG  . LEU B 880  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  877  LEU A CG  
7051  C CD1 . LEU B 880  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  877  LEU A CD1 
7052  C CD2 . LEU B 880  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  877  LEU A CD2 
7053  N N   . ASN B 881  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  878  ASN A N   
7054  C CA  . ASN B 881  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  878  ASN A CA  
7055  C C   . ASN B 881  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  878  ASN A C   
7056  O O   . ASN B 881  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  878  ASN A O   
7057  C CB  . ASN B 881  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  878  ASN A CB  
7058  C CG  . ASN B 881  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  878  ASN A CG  
7059  O OD1 . ASN B 881  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  878  ASN A OD1 
7060  N ND2 . ASN B 881  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  878  ASN A ND2 
7061  N N   . TYR B 882  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  879  TYR A N   
7062  C CA  . TYR B 882  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  879  TYR A CA  
7063  C C   . TYR B 882  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  879  TYR A C   
7064  O O   . TYR B 882  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  879  TYR A O   
7065  C CB  . TYR B 882  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  879  TYR A CB  
7066  C CG  . TYR B 882  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  879  TYR A CG  
7067  C CD1 . TYR B 882  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  879  TYR A CD1 
7068  C CD2 . TYR B 882  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  879  TYR A CD2 
7069  C CE1 . TYR B 882  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  879  TYR A CE1 
7070  C CE2 . TYR B 882  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  879  TYR A CE2 
7071  C CZ  . TYR B 882  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  879  TYR A CZ  
7072  O OH  . TYR B 882  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  879  TYR A OH  
7073  N N   . GLN B 883  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  880  GLN A N   
7074  C CA  . GLN B 883  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  880  GLN A CA  
7075  C C   . GLN B 883  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  880  GLN A C   
7076  O O   . GLN B 883  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  880  GLN A O   
7077  C CB  . GLN B 883  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  880  GLN A CB  
7078  C CG  . GLN B 883  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  880  GLN A CG  
7079  C CD  . GLN B 883  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  880  GLN A CD  
7080  O OE1 . GLN B 883  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  880  GLN A OE1 
7081  N NE2 . GLN B 883  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  880  GLN A NE2 
7082  N N   . ALA B 884  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  881  ALA A N   
7083  C CA  . ALA B 884  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  881  ALA A CA  
7084  C C   . ALA B 884  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  881  ALA A C   
7085  O O   . ALA B 884  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  881  ALA A O   
7086  C CB  . ALA B 884  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  881  ALA A CB  
7087  N N   . ALA B 885  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  882  ALA A N   
7088  C CA  . ALA B 885  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  882  ALA A CA  
7089  C C   . ALA B 885  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  882  ALA A C   
7090  O O   . ALA B 885  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  882  ALA A O   
7091  C CB  . ALA B 885  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  882  ALA A CB  
7092  N N   . ASN B 886  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  883  ASN A N   
7093  C CA  . ASN B 886  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  883  ASN A CA  
7094  C C   . ASN B 886  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  883  ASN A C   
7095  O O   . ASN B 886  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  883  ASN A O   
7096  C CB  . ASN B 886  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  883  ASN A CB  
7097  C CG  . ASN B 886  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  883  ASN A CG  
7098  O OD1 . ASN B 886  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  883  ASN A OD1 
7099  N ND2 . ASN B 886  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  883  ASN A ND2 
7100  N N   . SER B 887  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  884  SER A N   
7101  C CA  . SER B 887  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  884  SER A CA  
7102  C C   . SER B 887  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  884  SER A C   
7103  O O   . SER B 887  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  884  SER A O   
7104  C CB  . SER B 887  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  884  SER A CB  
7105  O OG  . SER B 887  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  884  SER A OG  
7106  N N   . PRO B 888  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  885  PRO A N   
7107  C CA  . PRO B 888  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  885  PRO A CA  
7108  C C   . PRO B 888  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  885  PRO A C   
7109  O O   . PRO B 888  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  885  PRO A O   
7110  C CB  . PRO B 888  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  885  PRO A CB  
7111  C CG  . PRO B 888  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  885  PRO A CG  
7112  C CD  . PRO B 888  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  885  PRO A CD  
7113  N N   . SER B 889  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  886  SER A N   
7114  C CA  . SER B 889  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  886  SER A CA  
7115  C C   . SER B 889  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  886  SER A C   
7116  O O   . SER B 889  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  886  SER A O   
7117  C CB  . SER B 889  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  886  SER A CB  
7118  O OG  . SER B 889  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  886  SER A OG  
7119  N N   . LYS B 890  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  887  LYS A N   
7120  C CA  . LYS B 890  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  887  LYS A CA  
7121  C C   . LYS B 890  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  887  LYS A C   
7122  O O   . LYS B 890  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  887  LYS A O   
7123  C CB  . LYS B 890  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  887  LYS A CB  
7124  C CG  . LYS B 890  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  887  LYS A CG  
7125  C CD  . LYS B 890  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  887  LYS A CD  
7126  C CE  . LYS B 890  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  887  LYS A CE  
7127  N NZ  . LYS B 890  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  887  LYS A NZ  
7128  N N   . PHE B 891  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  888  PHE A N   
7129  C CA  . PHE B 891  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  888  PHE A CA  
7130  C C   . PHE B 891  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  888  PHE A C   
7131  O O   . PHE B 891  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  888  PHE A O   
7132  C CB  . PHE B 891  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  888  PHE A CB  
7133  C CG  . PHE B 891  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  888  PHE A CG  
7134  C CD1 . PHE B 891  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  888  PHE A CD1 
7135  C CD2 . PHE B 891  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  888  PHE A CD2 
7136  C CE1 . PHE B 891  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  888  PHE A CE1 
7137  C CE2 . PHE B 891  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  888  PHE A CE2 
7138  C CZ  . PHE B 891  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  888  PHE A CZ  
7139  N N   . ASN B 892  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  889  ASN A N   
7140  C CA  . ASN B 892  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  889  ASN A CA  
7141  C C   . ASN B 892  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  889  ASN A C   
7142  O O   . ASN B 892  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  889  ASN A O   
7143  C CB  . ASN B 892  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  889  ASN A CB  
7144  C CG  . ASN B 892  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  889  ASN A CG  
7145  O OD1 . ASN B 892  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  889  ASN A OD1 
7146  N ND2 . ASN B 892  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  889  ASN A ND2 
7147  N N   . GLN B 893  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  890  GLN A N   
7148  C CA  . GLN B 893  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  890  GLN A CA  
7149  C C   . GLN B 893  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  890  GLN A C   
7150  O O   . GLN B 893  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  890  GLN A O   
7151  C CB  . GLN B 893  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  890  GLN A CB  
7152  C CG  . GLN B 893  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  890  GLN A CG  
7153  C CD  . GLN B 893  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  890  GLN A CD  
7154  O OE1 . GLN B 893  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  890  GLN A OE1 
7155  N NE2 . GLN B 893  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  890  GLN A NE2 
7156  N N   . ARG B 894  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  891  ARG A N   
7157  C CA  . ARG B 894  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  891  ARG A CA  
7158  C C   . ARG B 894  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  891  ARG A C   
7159  O O   . ARG B 894  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  891  ARG A O   
7160  C CB  . ARG B 894  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  891  ARG A CB  
7161  C CG  . ARG B 894  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  891  ARG A CG  
7162  C CD  . ARG B 894  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  891  ARG A CD  
7163  N NE  . ARG B 894  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  891  ARG A NE  
7164  C CZ  . ARG B 894  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  891  ARG A CZ  
7165  N NH1 . ARG B 894  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  891  ARG A NH1 
7166  N NH2 . ARG B 894  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  891  ARG A NH2 
7167  N N   . VAL B 895  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  892  VAL A N   
7168  C CA  . VAL B 895  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  892  VAL A CA  
7169  C C   . VAL B 895  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  892  VAL A C   
7170  O O   . VAL B 895  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  892  VAL A O   
7171  C CB  . VAL B 895  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  892  VAL A CB  
7172  C CG1 . VAL B 895  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  892  VAL A CG1 
7173  C CG2 . VAL B 895  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  892  VAL A CG2 
7174  N N   . ASN B 896  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  893  ASN A N   
7175  C CA  . ASN B 896  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  893  ASN A CA  
7176  C C   . ASN B 896  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  893  ASN A C   
7177  O O   . ASN B 896  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  893  ASN A O   
7178  C CB  . ASN B 896  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  893  ASN A CB  
7179  C CG  . ASN B 896  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  893  ASN A CG  
7180  O OD1 . ASN B 896  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  893  ASN A OD1 
7181  N ND2 . ASN B 896  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  893  ASN A ND2 
7182  N N   . ALA B 897  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  894  ALA A N   
7183  C CA  . ALA B 897  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  894  ALA A CA  
7184  C C   . ALA B 897  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  894  ALA A C   
7185  O O   . ALA B 897  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  894  ALA A O   
7186  C CB  . ALA B 897  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  894  ALA A CB  
7187  N N   . TYR B 898  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  895  TYR A N   
7188  C CA  . TYR B 898  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  895  TYR A CA  
7189  C C   . TYR B 898  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  895  TYR A C   
7190  O O   . TYR B 898  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  895  TYR A O   
7191  C CB  . TYR B 898  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  895  TYR A CB  
7192  C CG  . TYR B 898  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  895  TYR A CG  
7193  C CD1 . TYR B 898  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  895  TYR A CD1 
7194  C CD2 . TYR B 898  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  895  TYR A CD2 
7195  C CE1 . TYR B 898  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  895  TYR A CE1 
7196  C CE2 . TYR B 898  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  895  TYR A CE2 
7197  C CZ  . TYR B 898  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  895  TYR A CZ  
7198  O OH  . TYR B 898  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  895  TYR A OH  
7199  N N   . LEU B 899  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  896  LEU A N   
7200  C CA  . LEU B 899  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  896  LEU A CA  
7201  C C   . LEU B 899  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  896  LEU A C   
7202  O O   . LEU B 899  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  896  LEU A O   
7203  C CB  . LEU B 899  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  896  LEU A CB  
7204  C CG  . LEU B 899  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  896  LEU A CG  
7205  C CD1 . LEU B 899  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  896  LEU A CD1 
7206  C CD2 . LEU B 899  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  896  LEU A CD2 
7207  N N   . LYS B 900  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  897  LYS A N   
7208  C CA  . LYS B 900  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  897  LYS A CA  
7209  C C   . LYS B 900  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  897  LYS A C   
7210  O O   . LYS B 900  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  897  LYS A O   
7211  C CB  . LYS B 900  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  897  LYS A CB  
7212  C CG  . LYS B 900  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  897  LYS A CG  
7213  C CD  . LYS B 900  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  897  LYS A CD  
7214  C CE  . LYS B 900  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  897  LYS A CE  
7215  N NZ  . LYS B 900  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  897  LYS A NZ  
7216  N N   . GLU B 901  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  898  GLU A N   
7217  C CA  . GLU B 901  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  898  GLU A CA  
7218  C C   . GLU B 901  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  898  GLU A C   
7219  O O   . GLU B 901  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  898  GLU A O   
7220  C CB  . GLU B 901  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  898  GLU A CB  
7221  C CG  . GLU B 901  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  898  GLU A CG  
7222  C CD  . GLU B 901  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  898  GLU A CD  
7223  O OE1 . GLU B 901  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  898  GLU A OE1 
7224  O OE2 . GLU B 901  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  898  GLU A OE2 
7225  N N   . HIS B 902  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  899  HIS A N   
7226  C CA  . HIS B 902  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  899  HIS A CA  
7227  C C   . HIS B 902  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  899  HIS A C   
7228  O O   . HIS B 902  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  899  HIS A O   
7229  C CB  . HIS B 902  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  899  HIS A CB  
7230  C CG  . HIS B 902  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  899  HIS A CG  
7231  N ND1 . HIS B 902  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  899  HIS A ND1 
7232  C CD2 . HIS B 902  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  899  HIS A CD2 
7233  C CE1 . HIS B 902  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  899  HIS A CE1 
7234  N NE2 . HIS B 902  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  899  HIS A NE2 
7235  N N   . PRO B 903  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  900  PRO A N   
7236  C CA  . PRO B 903  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  900  PRO A CA  
7237  C C   . PRO B 903  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  900  PRO A C   
7238  O O   . PRO B 903  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  900  PRO A O   
7239  C CB  . PRO B 903  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  900  PRO A CB  
7240  C CG  . PRO B 903  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  900  PRO A CG  
7241  C CD  . PRO B 903  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  900  PRO A CD  
7242  N N   . GLU B 904  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  901  GLU A N   
7243  C CA  . GLU B 904  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  901  GLU A CA  
7244  C C   . GLU B 904  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  901  GLU A C   
7245  O O   . GLU B 904  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  901  GLU A O   
7246  C CB  . GLU B 904  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  901  GLU A CB  
7247  C CG  . GLU B 904  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  901  GLU A CG  
7248  C CD  . GLU B 904  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  901  GLU A CD  
7249  O OE1 . GLU B 904  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  901  GLU A OE1 
7250  O OE2 . GLU B 904  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  901  GLU A OE2 
7251  N N   . THR B 905  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  902  THR A N   
7252  C CA  . THR B 905  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  902  THR A CA  
7253  C C   . THR B 905  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  902  THR A C   
7254  O O   . THR B 905  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  902  THR A O   
7255  C CB  . THR B 905  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  902  THR A CB  
7256  O OG1 . THR B 905  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  902  THR A OG1 
7257  C CG2 . THR B 905  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  902  THR A CG2 
7258  N N   . PRO B 906  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  903  PRO A N   
7259  C CA  . PRO B 906  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  903  PRO A CA  
7260  C C   . PRO B 906  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  903  PRO A C   
7261  O O   . PRO B 906  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  903  PRO A O   
7262  C CB  . PRO B 906  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  903  PRO A CB  
7263  C CG  . PRO B 906  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  903  PRO A CG  
7264  C CD  . PRO B 906  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  903  PRO A CD  
7265  N N   . ILE B 907  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  904  ILE A N   
7266  C CA  . ILE B 907  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  904  ILE A CA  
7267  C C   . ILE B 907  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  904  ILE A C   
7268  O O   . ILE B 907  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  904  ILE A O   
7269  C CB  . ILE B 907  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  904  ILE A CB  
7270  C CG1 . ILE B 907  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  904  ILE A CG1 
7271  C CG2 . ILE B 907  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  904  ILE A CG2 
7272  C CD1 . ILE B 907  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  904  ILE A CD1 
7273  N N   . ILE B 908  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  905  ILE A N   
7274  C CA  . ILE B 908  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  905  ILE A CA  
7275  C C   . ILE B 908  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  905  ILE A C   
7276  O O   . ILE B 908  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  905  ILE A O   
7277  C CB  . ILE B 908  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  905  ILE A CB  
7278  C CG1 . ILE B 908  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  905  ILE A CG1 
7279  C CG2 . ILE B 908  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  905  ILE A CG2 
7280  C CD1 . ILE B 908  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  905  ILE A CD1 
7281  N N   . GLY B 909  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  906  GLY A N   
7282  C CA  . GLY B 909  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  906  GLY A CA  
7283  C C   . GLY B 909  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  906  GLY A C   
7284  O O   . GLY B 909  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  906  GLY A O   
7285  N N   . ILE B 910  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  907  ILE A N   
7286  C CA  . ILE B 910  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  907  ILE A CA  
7287  C C   . ILE B 910  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  907  ILE A C   
7288  O O   . ILE B 910  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  907  ILE A O   
7289  C CB  . ILE B 910  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  907  ILE A CB  
7290  C CG1 . ILE B 910  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  907  ILE A CG1 
7291  C CG2 . ILE B 910  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  907  ILE A CG2 
7292  C CD1 . ILE B 910  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  907  ILE A CD1 
7293  N N   . ASP B 911  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  908  ASP A N   
7294  C CA  . ASP B 911  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  908  ASP A CA  
7295  C C   . ASP B 911  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  908  ASP A C   
7296  O O   . ASP B 911  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  908  ASP A O   
7297  C CB  . ASP B 911  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  908  ASP A CB  
7298  C CG  . ASP B 911  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  908  ASP A CG  
7299  O OD1 . ASP B 911  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  908  ASP A OD1 
7300  O OD2 . ASP B 911  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  908  ASP A OD2 
7301  N N   . ARG B 912  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  909  ARG A N   
7302  C CA  . ARG B 912  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  909  ARG A CA  
7303  C C   . ARG B 912  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  909  ARG A C   
7304  O O   . ARG B 912  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  909  ARG A O   
7305  C CB  . ARG B 912  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  909  ARG A CB  
7306  C CG  . ARG B 912  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  909  ARG A CG  
7307  C CD  . ARG B 912  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  909  ARG A CD  
7308  N NE  . ARG B 912  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  909  ARG A NE  
7309  C CZ  . ARG B 912  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  909  ARG A CZ  
7310  N NH1 . ARG B 912  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  909  ARG A NH1 
7311  N NH2 . ARG B 912  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  909  ARG A NH2 
7312  N N   . GLY B 913  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  910  GLY A N   
7313  C CA  . GLY B 913  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  910  GLY A CA  
7314  C C   . GLY B 913  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  910  GLY A C   
7315  O O   . GLY B 913  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  910  GLY A O   
7316  N N   . GLU B 914  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  911  GLU A N   
7317  C CA  . GLU B 914  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  911  GLU A CA  
7318  C C   . GLU B 914  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  911  GLU A C   
7319  O O   . GLU B 914  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  911  GLU A O   
7320  C CB  . GLU B 914  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  911  GLU A CB  
7321  C CG  . GLU B 914  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  911  GLU A CG  
7322  C CD  . GLU B 914  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  911  GLU A CD  
7323  O OE1 . GLU B 914  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  911  GLU A OE1 
7324  O OE2 . GLU B 914  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  911  GLU A OE2 
7325  N N   . ARG B 915  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  912  ARG A N   
7326  C CA  . ARG B 915  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  912  ARG A CA  
7327  C C   . ARG B 915  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  912  ARG A C   
7328  O O   . ARG B 915  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  912  ARG A O   
7329  C CB  . ARG B 915  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  912  ARG A CB  
7330  C CG  . ARG B 915  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  912  ARG A CG  
7331  C CD  . ARG B 915  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  912  ARG A CD  
7332  N NE  . ARG B 915  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  912  ARG A NE  
7333  C CZ  . ARG B 915  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  912  ARG A CZ  
7334  N NH1 . ARG B 915  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  912  ARG A NH1 
7335  N NH2 . ARG B 915  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  912  ARG A NH2 
7336  N N   . ASN B 916  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  913  ASN A N   
7337  C CA  . ASN B 916  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  913  ASN A CA  
7338  C C   . ASN B 916  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  913  ASN A C   
7339  O O   . ASN B 916  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  913  ASN A O   
7340  C CB  . ASN B 916  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  913  ASN A CB  
7341  C CG  . ASN B 916  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  913  ASN A CG  
7342  O OD1 . ASN B 916  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  913  ASN A OD1 
7343  N ND2 . ASN B 916  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  913  ASN A ND2 
7344  N N   . LEU B 917  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  914  LEU A N   
7345  C CA  . LEU B 917  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  914  LEU A CA  
7346  C C   . LEU B 917  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  914  LEU A C   
7347  O O   . LEU B 917  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  914  LEU A O   
7348  C CB  . LEU B 917  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  914  LEU A CB  
7349  C CG  . LEU B 917  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  914  LEU A CG  
7350  C CD1 . LEU B 917  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  914  LEU A CD1 
7351  C CD2 . LEU B 917  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  914  LEU A CD2 
7352  N N   . ILE B 918  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  915  ILE A N   
7353  C CA  . ILE B 918  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  915  ILE A CA  
7354  C C   . ILE B 918  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  915  ILE A C   
7355  O O   . ILE B 918  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  915  ILE A O   
7356  C CB  . ILE B 918  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  915  ILE A CB  
7357  C CG1 . ILE B 918  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  915  ILE A CG1 
7358  C CG2 . ILE B 918  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  915  ILE A CG2 
7359  C CD1 . ILE B 918  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  915  ILE A CD1 
7360  N N   . TYR B 919  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  916  TYR A N   
7361  C CA  . TYR B 919  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  916  TYR A CA  
7362  C C   . TYR B 919  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  916  TYR A C   
7363  O O   . TYR B 919  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  916  TYR A O   
7364  C CB  . TYR B 919  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  916  TYR A CB  
7365  C CG  . TYR B 919  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  916  TYR A CG  
7366  C CD1 . TYR B 919  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  916  TYR A CD1 
7367  C CD2 . TYR B 919  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  916  TYR A CD2 
7368  C CE1 . TYR B 919  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  916  TYR A CE1 
7369  C CE2 . TYR B 919  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  916  TYR A CE2 
7370  C CZ  . TYR B 919  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  916  TYR A CZ  
7371  O OH  . TYR B 919  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  916  TYR A OH  
7372  N N   . ILE B 920  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  917  ILE A N   
7373  C CA  . ILE B 920  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  917  ILE A CA  
7374  C C   . ILE B 920  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  917  ILE A C   
7375  O O   . ILE B 920  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  917  ILE A O   
7376  C CB  . ILE B 920  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  917  ILE A CB  
7377  C CG1 . ILE B 920  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  917  ILE A CG1 
7378  C CG2 . ILE B 920  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  917  ILE A CG2 
7379  C CD1 . ILE B 920  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  917  ILE A CD1 
7380  N N   . THR B 921  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  918  THR A N   
7381  C CA  . THR B 921  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  918  THR A CA  
7382  C C   . THR B 921  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  918  THR A C   
7383  O O   . THR B 921  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  918  THR A O   
7384  C CB  . THR B 921  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  918  THR A CB  
7385  O OG1 . THR B 921  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  918  THR A OG1 
7386  C CG2 . THR B 921  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  918  THR A CG2 
7387  N N   . VAL B 922  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  919  VAL A N   
7388  C CA  . VAL B 922  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  919  VAL A CA  
7389  C C   . VAL B 922  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  919  VAL A C   
7390  O O   . VAL B 922  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  919  VAL A O   
7391  C CB  . VAL B 922  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  919  VAL A CB  
7392  C CG1 . VAL B 922  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  919  VAL A CG1 
7393  C CG2 . VAL B 922  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  919  VAL A CG2 
7394  N N   . ILE B 923  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  920  ILE A N   
7395  C CA  . ILE B 923  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  920  ILE A CA  
7396  C C   . ILE B 923  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  920  ILE A C   
7397  O O   . ILE B 923  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  920  ILE A O   
7398  C CB  . ILE B 923  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  920  ILE A CB  
7399  C CG1 . ILE B 923  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  920  ILE A CG1 
7400  C CG2 . ILE B 923  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  920  ILE A CG2 
7401  C CD1 . ILE B 923  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  920  ILE A CD1 
7402  N N   . ASP B 924  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  921  ASP A N   
7403  C CA  . ASP B 924  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  921  ASP A CA  
7404  C C   . ASP B 924  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  921  ASP A C   
7405  O O   . ASP B 924  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  921  ASP A O   
7406  C CB  . ASP B 924  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  921  ASP A CB  
7407  C CG  . ASP B 924  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  921  ASP A CG  
7408  O OD1 . ASP B 924  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  921  ASP A OD1 
7409  O OD2 . ASP B 924  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  921  ASP A OD2 
7410  N N   . SER B 925  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  922  SER A N   
7411  C CA  . SER B 925  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  922  SER A CA  
7412  C C   . SER B 925  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  922  SER A C   
7413  O O   . SER B 925  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  922  SER A O   
7414  C CB  . SER B 925  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  922  SER A CB  
7415  O OG  . SER B 925  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  922  SER A OG  
7416  N N   . THR B 926  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  923  THR A N   
7417  C CA  . THR B 926  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  923  THR A CA  
7418  C C   . THR B 926  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  923  THR A C   
7419  O O   . THR B 926  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  923  THR A O   
7420  C CB  . THR B 926  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  923  THR A CB  
7421  O OG1 . THR B 926  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  923  THR A OG1 
7422  C CG2 . THR B 926  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  923  THR A CG2 
7423  N N   . GLY B 927  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  924  GLY A N   
7424  C CA  . GLY B 927  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  924  GLY A CA  
7425  C C   . GLY B 927  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  924  GLY A C   
7426  O O   . GLY B 927  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  924  GLY A O   
7427  N N   . LYS B 928  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  925  LYS A N   
7428  C CA  . LYS B 928  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  925  LYS A CA  
7429  C C   . LYS B 928  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  925  LYS A C   
7430  O O   . LYS B 928  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  925  LYS A O   
7436  N N   . ILE B 929  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  926  ILE A N   
7437  C CA  . ILE B 929  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  926  ILE A CA  
7438  C C   . ILE B 929  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  926  ILE A C   
7439  O O   . ILE B 929  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  926  ILE A O   
7440  C CB  . ILE B 929  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  926  ILE A CB  
7441  C CG1 . ILE B 929  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  926  ILE A CG1 
7442  C CG2 . ILE B 929  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  926  ILE A CG2 
7443  C CD1 . ILE B 929  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  926  ILE A CD1 
7444  N N   . LEU B 930  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  927  LEU A N   
7445  C CA  . LEU B 930  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  927  LEU A CA  
7446  C C   . LEU B 930  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  927  LEU A C   
7447  O O   . LEU B 930  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  927  LEU A O   
7448  C CB  . LEU B 930  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  927  LEU A CB  
7449  C CG  . LEU B 930  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  927  LEU A CG  
7450  C CD1 . LEU B 930  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  927  LEU A CD1 
7451  C CD2 . LEU B 930  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  927  LEU A CD2 
7452  N N   . GLU B 931  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  928  GLU A N   
7453  C CA  . GLU B 931  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  928  GLU A CA  
7454  C C   . GLU B 931  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  928  GLU A C   
7455  O O   . GLU B 931  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  928  GLU A O   
7456  C CB  . GLU B 931  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  928  GLU A CB  
7457  C CG  . GLU B 931  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  928  GLU A CG  
7458  C CD  . GLU B 931  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  928  GLU A CD  
7459  O OE1 . GLU B 931  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  928  GLU A OE1 
7460  O OE2 . GLU B 931  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  928  GLU A OE2 
7461  N N   . GLN B 932  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  929  GLN A N   
7462  C CA  . GLN B 932  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  929  GLN A CA  
7463  C C   . GLN B 932  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  929  GLN A C   
7464  O O   . GLN B 932  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  929  GLN A O   
7465  C CB  . GLN B 932  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  929  GLN A CB  
7466  C CG  . GLN B 932  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  929  GLN A CG  
7467  C CD  . GLN B 932  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  929  GLN A CD  
7468  O OE1 . GLN B 932  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  929  GLN A OE1 
7469  N NE2 . GLN B 932  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  929  GLN A NE2 
7470  N N   . ARG B 933  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  930  ARG A N   
7471  C CA  . ARG B 933  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  930  ARG A CA  
7472  C C   . ARG B 933  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  930  ARG A C   
7473  O O   . ARG B 933  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  930  ARG A O   
7474  C CB  . ARG B 933  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  930  ARG A CB  
7475  C CG  . ARG B 933  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  930  ARG A CG  
7476  C CD  . ARG B 933  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  930  ARG A CD  
7477  N NE  . ARG B 933  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  930  ARG A NE  
7478  C CZ  . ARG B 933  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  930  ARG A CZ  
7479  N NH1 . ARG B 933  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  930  ARG A NH1 
7480  N NH2 . ARG B 933  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  930  ARG A NH2 
7481  N N   . SER B 934  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  931  SER A N   
7482  C CA  . SER B 934  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  931  SER A CA  
7483  C C   . SER B 934  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  931  SER A C   
7484  O O   . SER B 934  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  931  SER A O   
7485  C CB  . SER B 934  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  931  SER A CB  
7486  O OG  . SER B 934  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  931  SER A OG  
7487  N N   . LEU B 935  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  932  LEU A N   
7488  C CA  . LEU B 935  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  932  LEU A CA  
7489  C C   . LEU B 935  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  932  LEU A C   
7490  O O   . LEU B 935  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  932  LEU A O   
7491  C CB  . LEU B 935  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  932  LEU A CB  
7492  C CG  . LEU B 935  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  932  LEU A CG  
7493  C CD1 . LEU B 935  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  932  LEU A CD1 
7494  C CD2 . LEU B 935  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  932  LEU A CD2 
7495  N N   . ASN B 936  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  933  ASN A N   
7496  C CA  . ASN B 936  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  933  ASN A CA  
7497  C C   . ASN B 936  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  933  ASN A C   
7498  O O   . ASN B 936  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  933  ASN A O   
7499  C CB  . ASN B 936  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  933  ASN A CB  
7500  C CG  . ASN B 936  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  933  ASN A CG  
7501  O OD1 . ASN B 936  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  933  ASN A OD1 
7502  N ND2 . ASN B 936  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  933  ASN A ND2 
7503  N N   . THR B 937  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  934  THR A N   
7504  C CA  . THR B 937  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  934  THR A CA  
7505  C C   . THR B 937  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  934  THR A C   
7506  O O   . THR B 937  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  934  THR A O   
7507  C CB  . THR B 937  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  934  THR A CB  
7508  O OG1 . THR B 937  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  934  THR A OG1 
7509  C CG2 . THR B 937  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  934  THR A CG2 
7510  N N   . ILE B 938  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  935  ILE A N   
7511  C CA  . ILE B 938  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  935  ILE A CA  
7512  C C   . ILE B 938  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  935  ILE A C   
7513  O O   . ILE B 938  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  935  ILE A O   
7514  C CB  . ILE B 938  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  935  ILE A CB  
7515  C CG1 . ILE B 938  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  935  ILE A CG1 
7516  C CG2 . ILE B 938  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  935  ILE A CG2 
7517  C CD1 . ILE B 938  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  935  ILE A CD1 
7518  N N   . GLN B 939  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  936  GLN A N   
7519  C CA  . GLN B 939  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  936  GLN A CA  
7520  C C   . GLN B 939  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  936  GLN A C   
7521  O O   . GLN B 939  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  936  GLN A O   
7522  C CB  . GLN B 939  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  936  GLN A CB  
7523  C CG  . GLN B 939  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  936  GLN A CG  
7524  C CD  . GLN B 939  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  936  GLN A CD  
7525  O OE1 . GLN B 939  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  936  GLN A OE1 
7526  N NE2 . GLN B 939  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  936  GLN A NE2 
7527  N N   . GLN B 940  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  937  GLN A N   
7528  C CA  . GLN B 940  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  937  GLN A CA  
7529  C C   . GLN B 940  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  937  GLN A C   
7530  O O   . GLN B 940  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  937  GLN A O   
7536  N N   . PHE B 941  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  938  PHE A N   
7537  C CA  . PHE B 941  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  938  PHE A CA  
7538  C C   . PHE B 941  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  938  PHE A C   
7539  O O   . PHE B 941  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  938  PHE A O   
7540  C CB  . PHE B 941  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  938  PHE A CB  
7541  C CG  . PHE B 941  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  938  PHE A CG  
7542  C CD1 . PHE B 941  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  938  PHE A CD1 
7543  C CD2 . PHE B 941  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  938  PHE A CD2 
7544  C CE1 . PHE B 941  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  938  PHE A CE1 
7545  C CE2 . PHE B 941  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  938  PHE A CE2 
7546  C CZ  . PHE B 941  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  938  PHE A CZ  
7547  N N   . ASP B 942  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  939  ASP A N   
7548  C CA  . ASP B 942  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  939  ASP A CA  
7549  C C   . ASP B 942  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  939  ASP A C   
7550  O O   . ASP B 942  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  939  ASP A O   
7551  C CB  . ASP B 942  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  939  ASP A CB  
7552  C CG  . ASP B 942  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  939  ASP A CG  
7553  O OD1 . ASP B 942  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  939  ASP A OD1 
7554  O OD2 . ASP B 942  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  939  ASP A OD2 
7555  N N   . TYR B 943  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  940  TYR A N   
7556  C CA  . TYR B 943  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  940  TYR A CA  
7557  C C   . TYR B 943  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  940  TYR A C   
7558  O O   . TYR B 943  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  940  TYR A O   
7559  C CB  . TYR B 943  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  940  TYR A CB  
7560  C CG  . TYR B 943  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  940  TYR A CG  
7561  C CD1 . TYR B 943  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  940  TYR A CD1 
7562  C CD2 . TYR B 943  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  940  TYR A CD2 
7563  C CE1 . TYR B 943  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  940  TYR A CE1 
7564  C CE2 . TYR B 943  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  940  TYR A CE2 
7565  C CZ  . TYR B 943  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  940  TYR A CZ  
7566  O OH  . TYR B 943  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  940  TYR A OH  
7567  N N   . GLN B 944  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  941  GLN A N   
7568  C CA  . GLN B 944  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  941  GLN A CA  
7569  C C   . GLN B 944  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  941  GLN A C   
7570  O O   . GLN B 944  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  941  GLN A O   
7571  C CB  . GLN B 944  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  941  GLN A CB  
7572  C CG  . GLN B 944  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  941  GLN A CG  
7573  C CD  . GLN B 944  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  941  GLN A CD  
7574  O OE1 . GLN B 944  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  941  GLN A OE1 
7575  N NE2 . GLN B 944  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  941  GLN A NE2 
7576  N N   . LYS B 945  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  942  LYS A N   
7577  C CA  . LYS B 945  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  942  LYS A CA  
7578  C C   . LYS B 945  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  942  LYS A C   
7579  O O   . LYS B 945  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  942  LYS A O   
7585  N N   . LYS B 946  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  943  LYS A N   
7586  C CA  . LYS B 946  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  943  LYS A CA  
7587  C C   . LYS B 946  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  943  LYS A C   
7588  O O   . LYS B 946  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  943  LYS A O   
7589  C CB  . LYS B 946  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  943  LYS A CB  
7590  C CG  . LYS B 946  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  943  LYS A CG  
7591  C CD  . LYS B 946  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  943  LYS A CD  
7592  C CE  . LYS B 946  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  943  LYS A CE  
7593  N NZ  . LYS B 946  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  943  LYS A NZ  
7594  N N   . LEU B 947  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  944  LEU A N   
7595  C CA  . LEU B 947  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  944  LEU A CA  
7596  C C   . LEU B 947  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  944  LEU A C   
7597  O O   . LEU B 947  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  944  LEU A O   
7598  C CB  . LEU B 947  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  944  LEU A CB  
7599  C CG  . LEU B 947  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  944  LEU A CG  
7600  C CD1 . LEU B 947  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  944  LEU A CD1 
7601  C CD2 . LEU B 947  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  944  LEU A CD2 
7602  N N   . ASP B 948  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  945  ASP A N   
7603  C CA  . ASP B 948  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  945  ASP A CA  
7604  C C   . ASP B 948  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  945  ASP A C   
7605  O O   . ASP B 948  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  945  ASP A O   
7606  C CB  . ASP B 948  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  945  ASP A CB  
7607  C CG  . ASP B 948  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  945  ASP A CG  
7608  O OD1 . ASP B 948  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  945  ASP A OD1 
7609  O OD2 . ASP B 948  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  945  ASP A OD2 
7610  N N   . ASN B 949  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  946  ASN A N   
7611  C CA  . ASN B 949  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  946  ASN A CA  
7612  C C   . ASN B 949  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  946  ASN A C   
7613  O O   . ASN B 949  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  946  ASN A O   
7614  C CB  . ASN B 949  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  946  ASN A CB  
7615  C CG  . ASN B 949  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  946  ASN A CG  
7616  O OD1 . ASN B 949  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  946  ASN A OD1 
7617  N ND2 . ASN B 949  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  946  ASN A ND2 
7618  N N   . ARG B 950  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  947  ARG A N   
7619  C CA  . ARG B 950  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  947  ARG A CA  
7620  C C   . ARG B 950  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  947  ARG A C   
7621  O O   . ARG B 950  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  947  ARG A O   
7622  C CB  . ARG B 950  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  947  ARG A CB  
7623  C CG  . ARG B 950  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  947  ARG A CG  
7624  C CD  . ARG B 950  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  947  ARG A CD  
7625  N NE  . ARG B 950  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  947  ARG A NE  
7626  C CZ  . ARG B 950  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  947  ARG A CZ  
7627  N NH1 . ARG B 950  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  947  ARG A NH1 
7628  N NH2 . ARG B 950  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  947  ARG A NH2 
7629  N N   . GLU B 951  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  948  GLU A N   
7630  C CA  . GLU B 951  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  948  GLU A CA  
7631  C C   . GLU B 951  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  948  GLU A C   
7632  O O   . GLU B 951  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  948  GLU A O   
7633  C CB  . GLU B 951  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  948  GLU A CB  
7634  C CG  . GLU B 951  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  948  GLU A CG  
7635  C CD  . GLU B 951  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  948  GLU A CD  
7636  O OE1 . GLU B 951  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  948  GLU A OE1 
7637  O OE2 . GLU B 951  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  948  GLU A OE2 
7638  N N   . LYS B 952  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  949  LYS A N   
7639  C CA  . LYS B 952  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  949  LYS A CA  
7640  C C   . LYS B 952  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  949  LYS A C   
7641  O O   . LYS B 952  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  949  LYS A O   
7642  C CB  . LYS B 952  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  949  LYS A CB  
7643  C CG  . LYS B 952  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  949  LYS A CG  
7644  C CD  . LYS B 952  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  949  LYS A CD  
7645  C CE  . LYS B 952  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  949  LYS A CE  
7646  N NZ  . LYS B 952  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  949  LYS A NZ  
7647  N N   . GLU B 953  ? 0.6355 0.6355 0.6355 0.0000  0.0000  0.0000  950  GLU A N   
7648  C CA  . GLU B 953  ? 0.6355 0.6355 0.6355 0.0000  0.0000  0.0000  950  GLU A CA  
7649  C C   . GLU B 953  ? 0.6355 0.6355 0.6355 0.0000  0.0000  0.0000  950  GLU A C   
7650  O O   . GLU B 953  ? 0.6355 0.6355 0.6355 0.0000  0.0000  0.0000  950  GLU A O   
7651  C CB  . GLU B 953  ? 0.6355 0.6355 0.6355 0.0000  0.0000  0.0000  950  GLU A CB  
7652  C CG  . GLU B 953  ? 0.6355 0.6355 0.6355 0.0000  0.0000  0.0000  950  GLU A CG  
7653  C CD  . GLU B 953  ? 0.6355 0.6355 0.6355 0.0000  0.0000  0.0000  950  GLU A CD  
7654  O OE1 . GLU B 953  ? 0.6355 0.6355 0.6355 0.0000  0.0000  0.0000  950  GLU A OE1 
7655  O OE2 . GLU B 953  ? 0.6355 0.6355 0.6355 0.0000  0.0000  0.0000  950  GLU A OE2 
7656  N N   . ARG B 954  ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  951  ARG A N   
7657  C CA  . ARG B 954  ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  951  ARG A CA  
7658  C C   . ARG B 954  ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  951  ARG A C   
7659  O O   . ARG B 954  ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  951  ARG A O   
7660  C CB  . ARG B 954  ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  951  ARG A CB  
7661  C CG  . ARG B 954  ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  951  ARG A CG  
7662  C CD  . ARG B 954  ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  951  ARG A CD  
7663  N NE  . ARG B 954  ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  951  ARG A NE  
7664  C CZ  . ARG B 954  ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  951  ARG A CZ  
7665  N NH1 . ARG B 954  ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  951  ARG A NH1 
7666  N NH2 . ARG B 954  ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  951  ARG A NH2 
7667  N N   . VAL B 955  ? 0.6798 0.6798 0.6798 0.0000  0.0000  0.0000  952  VAL A N   
7668  C CA  . VAL B 955  ? 0.6798 0.6798 0.6798 0.0000  0.0000  0.0000  952  VAL A CA  
7669  C C   . VAL B 955  ? 0.6798 0.6798 0.6798 0.0000  0.0000  0.0000  952  VAL A C   
7670  O O   . VAL B 955  ? 0.6798 0.6798 0.6798 0.0000  0.0000  0.0000  952  VAL A O   
7671  C CB  . VAL B 955  ? 0.6798 0.6798 0.6798 0.0000  0.0000  0.0000  952  VAL A CB  
7672  C CG1 . VAL B 955  ? 0.6798 0.6798 0.6798 0.0000  0.0000  0.0000  952  VAL A CG1 
7673  C CG2 . VAL B 955  ? 0.6798 0.6798 0.6798 0.0000  0.0000  0.0000  952  VAL A CG2 
7674  N N   . ALA B 956  ? 0.6684 0.6684 0.6684 0.0000  0.0000  0.0000  953  ALA A N   
7675  C CA  . ALA B 956  ? 0.6684 0.6684 0.6684 0.0000  0.0000  0.0000  953  ALA A CA  
7676  C C   . ALA B 956  ? 0.6684 0.6684 0.6684 0.0000  0.0000  0.0000  953  ALA A C   
7677  O O   . ALA B 956  ? 0.6684 0.6684 0.6684 0.0000  0.0000  0.0000  953  ALA A O   
7678  C CB  . ALA B 956  ? 0.6684 0.6684 0.6684 0.0000  0.0000  0.0000  953  ALA A CB  
7679  N N   . ALA B 957  ? 0.6979 0.6979 0.6979 0.0000  0.0000  0.0000  954  ALA A N   
7680  C CA  . ALA B 957  ? 0.6979 0.6979 0.6979 0.0000  0.0000  0.0000  954  ALA A CA  
7681  C C   . ALA B 957  ? 0.6979 0.6979 0.6979 0.0000  0.0000  0.0000  954  ALA A C   
7682  O O   . ALA B 957  ? 0.6979 0.6979 0.6979 0.0000  0.0000  0.0000  954  ALA A O   
7683  C CB  . ALA B 957  ? 0.6979 0.6979 0.6979 0.0000  0.0000  0.0000  954  ALA A CB  
7684  N N   . ARG B 958  ? 0.7696 0.7696 0.7696 0.0000  0.0000  0.0000  955  ARG A N   
7685  C CA  . ARG B 958  ? 0.7696 0.7696 0.7696 0.0000  0.0000  0.0000  955  ARG A CA  
7686  C C   . ARG B 958  ? 0.7696 0.7696 0.7696 0.0000  0.0000  0.0000  955  ARG A C   
7687  O O   . ARG B 958  ? 0.7696 0.7696 0.7696 0.0000  0.0000  0.0000  955  ARG A O   
7688  C CB  . ARG B 958  ? 0.7696 0.7696 0.7696 0.0000  0.0000  0.0000  955  ARG A CB  
7689  C CG  . ARG B 958  ? 0.7696 0.7696 0.7696 0.0000  0.0000  0.0000  955  ARG A CG  
7690  C CD  . ARG B 958  ? 0.7696 0.7696 0.7696 0.0000  0.0000  0.0000  955  ARG A CD  
7691  N NE  . ARG B 958  ? 0.7696 0.7696 0.7696 0.0000  0.0000  0.0000  955  ARG A NE  
7692  C CZ  . ARG B 958  ? 0.7696 0.7696 0.7696 0.0000  0.0000  0.0000  955  ARG A CZ  
7693  N NH1 . ARG B 958  ? 0.7696 0.7696 0.7696 0.0000  0.0000  0.0000  955  ARG A NH1 
7694  N NH2 . ARG B 958  ? 0.7696 0.7696 0.7696 0.0000  0.0000  0.0000  955  ARG A NH2 
7695  N N   . GLN B 959  ? 0.7625 0.7625 0.7625 0.0000  0.0000  0.0000  956  GLN A N   
7696  C CA  . GLN B 959  ? 0.7625 0.7625 0.7625 0.0000  0.0000  0.0000  956  GLN A CA  
7697  C C   . GLN B 959  ? 0.7625 0.7625 0.7625 0.0000  0.0000  0.0000  956  GLN A C   
7698  O O   . GLN B 959  ? 0.7625 0.7625 0.7625 0.0000  0.0000  0.0000  956  GLN A O   
7699  C CB  . GLN B 959  ? 0.7625 0.7625 0.7625 0.0000  0.0000  0.0000  956  GLN A CB  
7700  C CG  . GLN B 959  ? 0.7625 0.7625 0.7625 0.0000  0.0000  0.0000  956  GLN A CG  
7701  C CD  . GLN B 959  ? 0.7625 0.7625 0.7625 0.0000  0.0000  0.0000  956  GLN A CD  
7702  O OE1 . GLN B 959  ? 0.7625 0.7625 0.7625 0.0000  0.0000  0.0000  956  GLN A OE1 
7703  N NE2 . GLN B 959  ? 0.7625 0.7625 0.7625 0.0000  0.0000  0.0000  956  GLN A NE2 
7709  N N   . TRP B 961  ? 0.8989 0.8989 0.8989 0.0000  0.0000  0.0000  958  TRP A N   
7710  C CA  . TRP B 961  ? 0.8989 0.8989 0.8989 0.0000  0.0000  0.0000  958  TRP A CA  
7711  C C   . TRP B 961  ? 0.8989 0.8989 0.8989 0.0000  0.0000  0.0000  958  TRP A C   
7712  O O   . TRP B 961  ? 0.8989 0.8989 0.8989 0.0000  0.0000  0.0000  958  TRP A O   
7723  N N   . SER B 962  ? 0.7598 0.7598 0.7598 0.0000  0.0000  0.0000  959  SER A N   
7724  C CA  . SER B 962  ? 0.7598 0.7598 0.7598 0.0000  0.0000  0.0000  959  SER A CA  
7725  C C   . SER B 962  ? 0.7598 0.7598 0.7598 0.0000  0.0000  0.0000  959  SER A C   
7726  O O   . SER B 962  ? 0.7598 0.7598 0.7598 0.0000  0.0000  0.0000  959  SER A O   
7727  C CB  . SER B 962  ? 0.7598 0.7598 0.7598 0.0000  0.0000  0.0000  959  SER A CB  
7728  O OG  . SER B 962  ? 0.7598 0.7598 0.7598 0.0000  0.0000  0.0000  959  SER A OG  
7729  N N   . VAL B 963  ? 0.6783 0.6783 0.6783 0.0000  0.0000  0.0000  960  VAL A N   
7730  C CA  . VAL B 963  ? 0.6783 0.6783 0.6783 0.0000  0.0000  0.0000  960  VAL A CA  
7731  C C   . VAL B 963  ? 0.6783 0.6783 0.6783 0.0000  0.0000  0.0000  960  VAL A C   
7732  O O   . VAL B 963  ? 0.6783 0.6783 0.6783 0.0000  0.0000  0.0000  960  VAL A O   
7733  C CB  . VAL B 963  ? 0.6783 0.6783 0.6783 0.0000  0.0000  0.0000  960  VAL A CB  
7734  C CG1 . VAL B 963  ? 0.6783 0.6783 0.6783 0.0000  0.0000  0.0000  960  VAL A CG1 
7735  C CG2 . VAL B 963  ? 0.6783 0.6783 0.6783 0.0000  0.0000  0.0000  960  VAL A CG2 
7736  N N   . VAL B 964  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  961  VAL A N   
7737  C CA  . VAL B 964  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  961  VAL A CA  
7738  C C   . VAL B 964  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  961  VAL A C   
7739  O O   . VAL B 964  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  961  VAL A O   
7740  C CB  . VAL B 964  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  961  VAL A CB  
7741  C CG1 . VAL B 964  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  961  VAL A CG1 
7742  C CG2 . VAL B 964  ? 0.6569 0.6569 0.6569 0.0000  0.0000  0.0000  961  VAL A CG2 
7743  N N   . GLY B 965  ? 0.6218 0.6218 0.6218 0.0000  0.0000  0.0000  962  GLY A N   
7744  C CA  . GLY B 965  ? 0.6218 0.6218 0.6218 0.0000  0.0000  0.0000  962  GLY A CA  
7745  C C   . GLY B 965  ? 0.6218 0.6218 0.6218 0.0000  0.0000  0.0000  962  GLY A C   
7746  O O   . GLY B 965  ? 0.6218 0.6218 0.6218 0.0000  0.0000  0.0000  962  GLY A O   
7747  N N   . THR B 966  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  963  THR A N   
7748  C CA  . THR B 966  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  963  THR A CA  
7749  C C   . THR B 966  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  963  THR A C   
7750  O O   . THR B 966  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  963  THR A O   
7751  C CB  . THR B 966  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  963  THR A CB  
7752  O OG1 . THR B 966  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  963  THR A OG1 
7753  C CG2 . THR B 966  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  963  THR A CG2 
7754  N N   . ILE B 967  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  964  ILE A N   
7755  C CA  . ILE B 967  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  964  ILE A CA  
7756  C C   . ILE B 967  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  964  ILE A C   
7757  O O   . ILE B 967  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  964  ILE A O   
7758  C CB  . ILE B 967  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  964  ILE A CB  
7759  C CG1 . ILE B 967  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  964  ILE A CG1 
7760  C CG2 . ILE B 967  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  964  ILE A CG2 
7761  C CD1 . ILE B 967  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  964  ILE A CD1 
7762  N N   . LYS B 968  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  965  LYS A N   
7763  C CA  . LYS B 968  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  965  LYS A CA  
7764  C C   . LYS B 968  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  965  LYS A C   
7765  O O   . LYS B 968  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  965  LYS A O   
7766  C CB  . LYS B 968  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  965  LYS A CB  
7767  C CG  . LYS B 968  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  965  LYS A CG  
7768  C CD  . LYS B 968  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  965  LYS A CD  
7769  C CE  . LYS B 968  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  965  LYS A CE  
7770  N NZ  . LYS B 968  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  965  LYS A NZ  
7771  N N   . ASP B 969  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  966  ASP A N   
7772  C CA  . ASP B 969  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  966  ASP A CA  
7773  C C   . ASP B 969  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  966  ASP A C   
7774  O O   . ASP B 969  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  966  ASP A O   
7775  C CB  . ASP B 969  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  966  ASP A CB  
7776  C CG  . ASP B 969  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  966  ASP A CG  
7777  O OD1 . ASP B 969  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  966  ASP A OD1 
7778  O OD2 . ASP B 969  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  966  ASP A OD2 
7779  N N   . LEU B 970  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  967  LEU A N   
7780  C CA  . LEU B 970  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  967  LEU A CA  
7781  C C   . LEU B 970  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  967  LEU A C   
7782  O O   . LEU B 970  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  967  LEU A O   
7783  C CB  . LEU B 970  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  967  LEU A CB  
7784  C CG  . LEU B 970  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  967  LEU A CG  
7785  C CD1 . LEU B 970  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  967  LEU A CD1 
7786  C CD2 . LEU B 970  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  967  LEU A CD2 
7787  N N   . LYS B 971  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  968  LYS A N   
7788  C CA  . LYS B 971  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  968  LYS A CA  
7789  C C   . LYS B 971  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  968  LYS A C   
7790  O O   . LYS B 971  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  968  LYS A O   
7791  C CB  . LYS B 971  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  968  LYS A CB  
7792  C CG  . LYS B 971  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  968  LYS A CG  
7793  C CD  . LYS B 971  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  968  LYS A CD  
7794  C CE  . LYS B 971  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  968  LYS A CE  
7795  N NZ  . LYS B 971  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  968  LYS A NZ  
7796  N N   . GLN B 972  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  969  GLN A N   
7797  C CA  . GLN B 972  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  969  GLN A CA  
7798  C C   . GLN B 972  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  969  GLN A C   
7799  O O   . GLN B 972  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  969  GLN A O   
7805  N N   . GLY B 973  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  970  GLY A N   
7806  C CA  . GLY B 973  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  970  GLY A CA  
7807  C C   . GLY B 973  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  970  GLY A C   
7808  O O   . GLY B 973  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  970  GLY A O   
7809  N N   . TYR B 974  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  971  TYR A N   
7810  C CA  . TYR B 974  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  971  TYR A CA  
7811  C C   . TYR B 974  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  971  TYR A C   
7812  O O   . TYR B 974  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  971  TYR A O   
7813  C CB  . TYR B 974  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  971  TYR A CB  
7814  C CG  . TYR B 974  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  971  TYR A CG  
7815  C CD1 . TYR B 974  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  971  TYR A CD1 
7816  C CD2 . TYR B 974  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  971  TYR A CD2 
7817  C CE1 . TYR B 974  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  971  TYR A CE1 
7818  C CE2 . TYR B 974  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  971  TYR A CE2 
7819  C CZ  . TYR B 974  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  971  TYR A CZ  
7820  O OH  . TYR B 974  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  971  TYR A OH  
7821  N N   . LEU B 975  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  972  LEU A N   
7822  C CA  . LEU B 975  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  972  LEU A CA  
7823  C C   . LEU B 975  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  972  LEU A C   
7824  O O   . LEU B 975  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  972  LEU A O   
7825  C CB  . LEU B 975  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  972  LEU A CB  
7826  C CG  . LEU B 975  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  972  LEU A CG  
7827  C CD1 . LEU B 975  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  972  LEU A CD1 
7828  C CD2 . LEU B 975  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  972  LEU A CD2 
7829  N N   . SER B 976  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  973  SER A N   
7830  C CA  . SER B 976  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  973  SER A CA  
7831  C C   . SER B 976  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  973  SER A C   
7832  O O   . SER B 976  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  973  SER A O   
7833  C CB  . SER B 976  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  973  SER A CB  
7834  O OG  . SER B 976  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  973  SER A OG  
7835  N N   . GLN B 977  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  974  GLN A N   
7836  C CA  . GLN B 977  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  974  GLN A CA  
7837  C C   . GLN B 977  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  974  GLN A C   
7838  O O   . GLN B 977  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  974  GLN A O   
7839  C CB  . GLN B 977  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  974  GLN A CB  
7840  C CG  . GLN B 977  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  974  GLN A CG  
7841  C CD  . GLN B 977  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  974  GLN A CD  
7842  O OE1 . GLN B 977  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  974  GLN A OE1 
7843  N NE2 . GLN B 977  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  974  GLN A NE2 
7844  N N   . VAL B 978  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  975  VAL A N   
7845  C CA  . VAL B 978  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  975  VAL A CA  
7846  C C   . VAL B 978  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  975  VAL A C   
7847  O O   . VAL B 978  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  975  VAL A O   
7848  C CB  . VAL B 978  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  975  VAL A CB  
7849  C CG1 . VAL B 978  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  975  VAL A CG1 
7850  C CG2 . VAL B 978  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  975  VAL A CG2 
7851  N N   . ILE B 979  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  976  ILE A N   
7852  C CA  . ILE B 979  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  976  ILE A CA  
7853  C C   . ILE B 979  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  976  ILE A C   
7854  O O   . ILE B 979  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  976  ILE A O   
7855  C CB  . ILE B 979  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  976  ILE A CB  
7856  C CG1 . ILE B 979  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  976  ILE A CG1 
7857  C CG2 . ILE B 979  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  976  ILE A CG2 
7858  C CD1 . ILE B 979  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  976  ILE A CD1 
7859  N N   . HIS B 980  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  977  HIS A N   
7860  C CA  . HIS B 980  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  977  HIS A CA  
7861  C C   . HIS B 980  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  977  HIS A C   
7862  O O   . HIS B 980  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  977  HIS A O   
7863  C CB  . HIS B 980  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  977  HIS A CB  
7864  C CG  . HIS B 980  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  977  HIS A CG  
7865  N ND1 . HIS B 980  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  977  HIS A ND1 
7866  C CD2 . HIS B 980  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  977  HIS A CD2 
7867  C CE1 . HIS B 980  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  977  HIS A CE1 
7868  N NE2 . HIS B 980  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  977  HIS A NE2 
7869  N N   . GLU B 981  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  978  GLU A N   
7870  C CA  . GLU B 981  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  978  GLU A CA  
7871  C C   . GLU B 981  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  978  GLU A C   
7872  O O   . GLU B 981  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  978  GLU A O   
7873  C CB  . GLU B 981  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  978  GLU A CB  
7874  C CG  . GLU B 981  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  978  GLU A CG  
7875  C CD  . GLU B 981  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  978  GLU A CD  
7876  O OE1 . GLU B 981  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  978  GLU A OE1 
7877  O OE2 . GLU B 981  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  978  GLU A OE2 
7878  N N   . ILE B 982  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  979  ILE A N   
7879  C CA  . ILE B 982  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  979  ILE A CA  
7880  C C   . ILE B 982  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  979  ILE A C   
7881  O O   . ILE B 982  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  979  ILE A O   
7882  C CB  . ILE B 982  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  979  ILE A CB  
7883  C CG1 . ILE B 982  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  979  ILE A CG1 
7884  C CG2 . ILE B 982  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  979  ILE A CG2 
7885  C CD1 . ILE B 982  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  979  ILE A CD1 
7886  N N   . VAL B 983  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  980  VAL A N   
7887  C CA  . VAL B 983  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  980  VAL A CA  
7888  C C   . VAL B 983  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  980  VAL A C   
7889  O O   . VAL B 983  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  980  VAL A O   
7890  C CB  . VAL B 983  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  980  VAL A CB  
7891  C CG1 . VAL B 983  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  980  VAL A CG1 
7892  C CG2 . VAL B 983  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  980  VAL A CG2 
7893  N N   . ASP B 984  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  981  ASP A N   
7894  C CA  . ASP B 984  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  981  ASP A CA  
7895  C C   . ASP B 984  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  981  ASP A C   
7896  O O   . ASP B 984  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  981  ASP A O   
7897  C CB  . ASP B 984  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  981  ASP A CB  
7898  C CG  . ASP B 984  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  981  ASP A CG  
7899  O OD1 . ASP B 984  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  981  ASP A OD1 
7900  O OD2 . ASP B 984  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  981  ASP A OD2 
7901  N N   . LEU B 985  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  982  LEU A N   
7902  C CA  . LEU B 985  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  982  LEU A CA  
7903  C C   . LEU B 985  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  982  LEU A C   
7904  O O   . LEU B 985  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  982  LEU A O   
7905  C CB  . LEU B 985  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  982  LEU A CB  
7906  C CG  . LEU B 985  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  982  LEU A CG  
7907  C CD1 . LEU B 985  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  982  LEU A CD1 
7908  C CD2 . LEU B 985  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  982  LEU A CD2 
7909  N N   . MET B 986  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  983  MET A N   
7910  C CA  . MET B 986  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  983  MET A CA  
7911  C C   . MET B 986  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  983  MET A C   
7912  O O   . MET B 986  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  983  MET A O   
7913  C CB  . MET B 986  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  983  MET A CB  
7914  C CG  . MET B 986  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  983  MET A CG  
7915  S SD  . MET B 986  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  983  MET A SD  
7916  C CE  . MET B 986  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  983  MET A CE  
7917  N N   . ILE B 987  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  984  ILE A N   
7918  C CA  . ILE B 987  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  984  ILE A CA  
7919  C C   . ILE B 987  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  984  ILE A C   
7920  O O   . ILE B 987  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  984  ILE A O   
7921  C CB  . ILE B 987  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  984  ILE A CB  
7922  C CG1 . ILE B 987  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  984  ILE A CG1 
7923  C CG2 . ILE B 987  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  984  ILE A CG2 
7924  C CD1 . ILE B 987  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  984  ILE A CD1 
7925  N N   . HIS B 988  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  985  HIS A N   
7926  C CA  . HIS B 988  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  985  HIS A CA  
7927  C C   . HIS B 988  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  985  HIS A C   
7928  O O   . HIS B 988  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  985  HIS A O   
7929  C CB  . HIS B 988  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  985  HIS A CB  
7930  C CG  . HIS B 988  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  985  HIS A CG  
7931  N ND1 . HIS B 988  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  985  HIS A ND1 
7932  C CD2 . HIS B 988  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  985  HIS A CD2 
7933  C CE1 . HIS B 988  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  985  HIS A CE1 
7934  N NE2 . HIS B 988  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  985  HIS A NE2 
7935  N N   . TYR B 989  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  986  TYR A N   
7936  C CA  . TYR B 989  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  986  TYR A CA  
7937  C C   . TYR B 989  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  986  TYR A C   
7938  O O   . TYR B 989  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  986  TYR A O   
7939  C CB  . TYR B 989  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  986  TYR A CB  
7940  C CG  . TYR B 989  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  986  TYR A CG  
7941  C CD1 . TYR B 989  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  986  TYR A CD1 
7942  C CD2 . TYR B 989  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  986  TYR A CD2 
7943  C CE1 . TYR B 989  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  986  TYR A CE1 
7944  C CE2 . TYR B 989  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  986  TYR A CE2 
7945  C CZ  . TYR B 989  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  986  TYR A CZ  
7946  O OH  . TYR B 989  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  986  TYR A OH  
7947  N N   . GLN B 990  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  987  GLN A N   
7948  C CA  . GLN B 990  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  987  GLN A CA  
7949  C C   . GLN B 990  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  987  GLN A C   
7950  O O   . GLN B 990  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  987  GLN A O   
7951  C CB  . GLN B 990  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  987  GLN A CB  
7952  C CG  . GLN B 990  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  987  GLN A CG  
7953  C CD  . GLN B 990  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  987  GLN A CD  
7954  O OE1 . GLN B 990  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  987  GLN A OE1 
7955  N NE2 . GLN B 990  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  987  GLN A NE2 
7956  N N   . ALA B 991  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  988  ALA A N   
7957  C CA  . ALA B 991  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  988  ALA A CA  
7958  C C   . ALA B 991  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  988  ALA A C   
7959  O O   . ALA B 991  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  988  ALA A O   
7960  C CB  . ALA B 991  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  988  ALA A CB  
7961  N N   . VAL B 992  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  989  VAL A N   
7962  C CA  . VAL B 992  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  989  VAL A CA  
7963  C C   . VAL B 992  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  989  VAL A C   
7964  O O   . VAL B 992  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  989  VAL A O   
7965  C CB  . VAL B 992  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  989  VAL A CB  
7966  C CG1 . VAL B 992  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  989  VAL A CG1 
7967  C CG2 . VAL B 992  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  989  VAL A CG2 
7968  N N   . VAL B 993  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  990  VAL A N   
7969  C CA  . VAL B 993  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  990  VAL A CA  
7970  C C   . VAL B 993  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  990  VAL A C   
7971  O O   . VAL B 993  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  990  VAL A O   
7972  C CB  . VAL B 993  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  990  VAL A CB  
7973  C CG1 . VAL B 993  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  990  VAL A CG1 
7974  C CG2 . VAL B 993  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  990  VAL A CG2 
7975  N N   . VAL B 994  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  991  VAL A N   
7976  C CA  . VAL B 994  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  991  VAL A CA  
7977  C C   . VAL B 994  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  991  VAL A C   
7978  O O   . VAL B 994  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  991  VAL A O   
7979  C CB  . VAL B 994  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  991  VAL A CB  
7980  C CG1 . VAL B 994  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  991  VAL A CG1 
7981  C CG2 . VAL B 994  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  991  VAL A CG2 
7982  N N   . LEU B 995  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  992  LEU A N   
7983  C CA  . LEU B 995  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  992  LEU A CA  
7984  C C   . LEU B 995  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  992  LEU A C   
7985  O O   . LEU B 995  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  992  LEU A O   
7986  C CB  . LEU B 995  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  992  LEU A CB  
7987  C CG  . LEU B 995  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  992  LEU A CG  
7988  C CD1 . LEU B 995  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  992  LEU A CD1 
7989  C CD2 . LEU B 995  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  992  LEU A CD2 
7990  N N   . GLU B 996  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  993  GLU A N   
7991  C CA  . GLU B 996  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  993  GLU A CA  
7992  C C   . GLU B 996  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  993  GLU A C   
7993  O O   . GLU B 996  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  993  GLU A O   
7994  C CB  . GLU B 996  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  993  GLU A CB  
7995  C CG  . GLU B 996  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  993  GLU A CG  
7996  C CD  . GLU B 996  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  993  GLU A CD  
7997  O OE1 . GLU B 996  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  993  GLU A OE1 
7998  O OE2 . GLU B 996  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  993  GLU A OE2 
7999  N N   . ASN B 997  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  994  ASN A N   
8000  C CA  . ASN B 997  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  994  ASN A CA  
8001  C C   . ASN B 997  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  994  ASN A C   
8002  O O   . ASN B 997  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  994  ASN A O   
8003  C CB  . ASN B 997  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  994  ASN A CB  
8004  C CG  . ASN B 997  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  994  ASN A CG  
8005  O OD1 . ASN B 997  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  994  ASN A OD1 
8006  N ND2 . ASN B 997  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  994  ASN A ND2 
8007  N N   . LEU B 998  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  995  LEU A N   
8008  C CA  . LEU B 998  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  995  LEU A CA  
8009  C C   . LEU B 998  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  995  LEU A C   
8010  O O   . LEU B 998  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  995  LEU A O   
8011  C CB  . LEU B 998  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  995  LEU A CB  
8012  C CG  . LEU B 998  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  995  LEU A CG  
8013  C CD1 . LEU B 998  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  995  LEU A CD1 
8014  C CD2 . LEU B 998  ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  995  LEU A CD2 
8131  N N   . VAL B 1014 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1011 VAL A N   
8132  C CA  . VAL B 1014 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1011 VAL A CA  
8133  C C   . VAL B 1014 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1011 VAL A C   
8134  O O   . VAL B 1014 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1011 VAL A O   
8135  C CB  . VAL B 1014 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1011 VAL A CB  
8136  C CG1 . VAL B 1014 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1011 VAL A CG1 
8137  C CG2 . VAL B 1014 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1011 VAL A CG2 
8138  N N   . TYR B 1015 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1012 TYR A N   
8139  C CA  . TYR B 1015 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1012 TYR A CA  
8140  C C   . TYR B 1015 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1012 TYR A C   
8141  O O   . TYR B 1015 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1012 TYR A O   
8142  C CB  . TYR B 1015 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1012 TYR A CB  
8143  C CG  . TYR B 1015 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1012 TYR A CG  
8144  C CD1 . TYR B 1015 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1012 TYR A CD1 
8145  C CD2 . TYR B 1015 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1012 TYR A CD2 
8146  C CE1 . TYR B 1015 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1012 TYR A CE1 
8147  C CE2 . TYR B 1015 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1012 TYR A CE2 
8148  C CZ  . TYR B 1015 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1012 TYR A CZ  
8149  O OH  . TYR B 1015 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1012 TYR A OH  
8150  N N   . GLN B 1016 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1013 GLN A N   
8151  C CA  . GLN B 1016 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1013 GLN A CA  
8152  C C   . GLN B 1016 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1013 GLN A C   
8153  O O   . GLN B 1016 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1013 GLN A O   
8154  C CB  . GLN B 1016 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1013 GLN A CB  
8155  C CG  . GLN B 1016 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1013 GLN A CG  
8156  C CD  . GLN B 1016 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1013 GLN A CD  
8157  O OE1 . GLN B 1016 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1013 GLN A OE1 
8158  N NE2 . GLN B 1016 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1013 GLN A NE2 
8159  N N   . GLN B 1017 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1014 GLN A N   
8160  C CA  . GLN B 1017 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1014 GLN A CA  
8161  C C   . GLN B 1017 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1014 GLN A C   
8162  O O   . GLN B 1017 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1014 GLN A O   
8163  C CB  . GLN B 1017 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1014 GLN A CB  
8164  C CG  . GLN B 1017 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1014 GLN A CG  
8165  C CD  . GLN B 1017 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1014 GLN A CD  
8166  O OE1 . GLN B 1017 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1014 GLN A OE1 
8167  N NE2 . GLN B 1017 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1014 GLN A NE2 
8168  N N   . PHE B 1018 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1015 PHE A N   
8169  C CA  . PHE B 1018 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1015 PHE A CA  
8170  C C   . PHE B 1018 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1015 PHE A C   
8171  O O   . PHE B 1018 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1015 PHE A O   
8172  C CB  . PHE B 1018 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1015 PHE A CB  
8173  C CG  . PHE B 1018 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1015 PHE A CG  
8174  C CD1 . PHE B 1018 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1015 PHE A CD1 
8175  C CD2 . PHE B 1018 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1015 PHE A CD2 
8176  C CE1 . PHE B 1018 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1015 PHE A CE1 
8177  C CE2 . PHE B 1018 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1015 PHE A CE2 
8178  C CZ  . PHE B 1018 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1015 PHE A CZ  
8179  N N   . GLU B 1019 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1016 GLU A N   
8180  C CA  . GLU B 1019 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1016 GLU A CA  
8181  C C   . GLU B 1019 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1016 GLU A C   
8182  O O   . GLU B 1019 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1016 GLU A O   
8183  C CB  . GLU B 1019 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1016 GLU A CB  
8184  C CG  . GLU B 1019 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1016 GLU A CG  
8185  C CD  . GLU B 1019 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1016 GLU A CD  
8186  O OE1 . GLU B 1019 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1016 GLU A OE1 
8187  O OE2 . GLU B 1019 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1016 GLU A OE2 
8188  N N   . LYS B 1020 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1017 LYS A N   
8189  C CA  . LYS B 1020 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1017 LYS A CA  
8190  C C   . LYS B 1020 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1017 LYS A C   
8191  O O   . LYS B 1020 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1017 LYS A O   
8192  C CB  . LYS B 1020 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1017 LYS A CB  
8193  C CG  . LYS B 1020 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1017 LYS A CG  
8194  C CD  . LYS B 1020 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1017 LYS A CD  
8195  C CE  . LYS B 1020 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1017 LYS A CE  
8196  N NZ  . LYS B 1020 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1017 LYS A NZ  
8197  N N   . MET B 1021 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1018 MET A N   
8198  C CA  . MET B 1021 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1018 MET A CA  
8199  C C   . MET B 1021 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1018 MET A C   
8200  O O   . MET B 1021 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1018 MET A O   
8201  C CB  . MET B 1021 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1018 MET A CB  
8202  C CG  . MET B 1021 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1018 MET A CG  
8203  S SD  . MET B 1021 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1018 MET A SD  
8204  C CE  . MET B 1021 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1018 MET A CE  
8205  N N   . LEU B 1022 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1019 LEU A N   
8206  C CA  . LEU B 1022 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1019 LEU A CA  
8207  C C   . LEU B 1022 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1019 LEU A C   
8208  O O   . LEU B 1022 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1019 LEU A O   
8209  C CB  . LEU B 1022 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1019 LEU A CB  
8210  C CG  . LEU B 1022 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1019 LEU A CG  
8211  C CD1 . LEU B 1022 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1019 LEU A CD1 
8212  C CD2 . LEU B 1022 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1019 LEU A CD2 
8213  N N   . ILE B 1023 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1020 ILE A N   
8214  C CA  . ILE B 1023 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1020 ILE A CA  
8215  C C   . ILE B 1023 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1020 ILE A C   
8216  O O   . ILE B 1023 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1020 ILE A O   
8217  C CB  . ILE B 1023 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1020 ILE A CB  
8218  C CG1 . ILE B 1023 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1020 ILE A CG1 
8219  C CG2 . ILE B 1023 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1020 ILE A CG2 
8220  C CD1 . ILE B 1023 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1020 ILE A CD1 
8221  N N   . ASP B 1024 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1021 ASP A N   
8222  C CA  . ASP B 1024 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1021 ASP A CA  
8223  C C   . ASP B 1024 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1021 ASP A C   
8224  O O   . ASP B 1024 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1021 ASP A O   
8225  C CB  . ASP B 1024 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1021 ASP A CB  
8226  C CG  . ASP B 1024 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1021 ASP A CG  
8227  O OD1 . ASP B 1024 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1021 ASP A OD1 
8228  O OD2 . ASP B 1024 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1021 ASP A OD2 
8229  N N   . LYS B 1025 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1022 LYS A N   
8230  C CA  . LYS B 1025 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1022 LYS A CA  
8231  C C   . LYS B 1025 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1022 LYS A C   
8232  O O   . LYS B 1025 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1022 LYS A O   
8233  C CB  . LYS B 1025 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1022 LYS A CB  
8234  C CG  . LYS B 1025 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1022 LYS A CG  
8235  C CD  . LYS B 1025 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1022 LYS A CD  
8236  C CE  . LYS B 1025 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1022 LYS A CE  
8237  N NZ  . LYS B 1025 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1022 LYS A NZ  
8238  N N   . LEU B 1026 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1023 LEU A N   
8239  C CA  . LEU B 1026 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1023 LEU A CA  
8240  C C   . LEU B 1026 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1023 LEU A C   
8241  O O   . LEU B 1026 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1023 LEU A O   
8242  C CB  . LEU B 1026 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1023 LEU A CB  
8243  C CG  . LEU B 1026 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1023 LEU A CG  
8244  C CD1 . LEU B 1026 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1023 LEU A CD1 
8245  C CD2 . LEU B 1026 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1023 LEU A CD2 
8246  N N   . ASN B 1027 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1024 ASN A N   
8247  C CA  . ASN B 1027 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1024 ASN A CA  
8248  C C   . ASN B 1027 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1024 ASN A C   
8249  O O   . ASN B 1027 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1024 ASN A O   
8250  C CB  . ASN B 1027 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1024 ASN A CB  
8251  C CG  . ASN B 1027 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1024 ASN A CG  
8252  O OD1 . ASN B 1027 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1024 ASN A OD1 
8253  N ND2 . ASN B 1027 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1024 ASN A ND2 
8254  N N   . CYS B 1028 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1025 CYS A N   
8255  C CA  . CYS B 1028 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1025 CYS A CA  
8256  C C   . CYS B 1028 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1025 CYS A C   
8257  O O   . CYS B 1028 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1025 CYS A O   
8258  C CB  . CYS B 1028 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1025 CYS A CB  
8259  S SG  . CYS B 1028 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1025 CYS A SG  
8260  N N   . LEU B 1029 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1026 LEU A N   
8261  C CA  . LEU B 1029 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1026 LEU A CA  
8262  C C   . LEU B 1029 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1026 LEU A C   
8263  O O   . LEU B 1029 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1026 LEU A O   
8264  C CB  . LEU B 1029 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1026 LEU A CB  
8265  C CG  . LEU B 1029 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1026 LEU A CG  
8266  C CD1 . LEU B 1029 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1026 LEU A CD1 
8267  C CD2 . LEU B 1029 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1026 LEU A CD2 
8268  N N   . VAL B 1030 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1027 VAL A N   
8269  C CA  . VAL B 1030 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1027 VAL A CA  
8270  C C   . VAL B 1030 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1027 VAL A C   
8271  O O   . VAL B 1030 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1027 VAL A O   
8272  C CB  . VAL B 1030 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1027 VAL A CB  
8273  C CG1 . VAL B 1030 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1027 VAL A CG1 
8274  C CG2 . VAL B 1030 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1027 VAL A CG2 
8275  N N   . LEU B 1031 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1028 LEU A N   
8276  C CA  . LEU B 1031 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1028 LEU A CA  
8277  C C   . LEU B 1031 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1028 LEU A C   
8278  O O   . LEU B 1031 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1028 LEU A O   
8279  C CB  . LEU B 1031 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1028 LEU A CB  
8280  C CG  . LEU B 1031 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1028 LEU A CG  
8281  C CD1 . LEU B 1031 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1028 LEU A CD1 
8282  C CD2 . LEU B 1031 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1028 LEU A CD2 
8283  N N   . LYS B 1032 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1029 LYS A N   
8284  C CA  . LYS B 1032 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1029 LYS A CA  
8285  C C   . LYS B 1032 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1029 LYS A C   
8286  O O   . LYS B 1032 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1029 LYS A O   
8287  C CB  . LYS B 1032 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1029 LYS A CB  
8288  C CG  . LYS B 1032 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1029 LYS A CG  
8289  C CD  . LYS B 1032 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1029 LYS A CD  
8290  C CE  . LYS B 1032 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1029 LYS A CE  
8291  N NZ  . LYS B 1032 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1029 LYS A NZ  
8292  N N   . ASP B 1033 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1030 ASP A N   
8293  C CA  . ASP B 1033 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1030 ASP A CA  
8294  C C   . ASP B 1033 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1030 ASP A C   
8295  O O   . ASP B 1033 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1030 ASP A O   
8296  C CB  . ASP B 1033 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1030 ASP A CB  
8297  C CG  . ASP B 1033 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1030 ASP A CG  
8298  O OD1 . ASP B 1033 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1030 ASP A OD1 
8299  O OD2 . ASP B 1033 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1030 ASP A OD2 
8300  N N   . TYR B 1034 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1031 TYR A N   
8301  C CA  . TYR B 1034 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1031 TYR A CA  
8302  C C   . TYR B 1034 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1031 TYR A C   
8303  O O   . TYR B 1034 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1031 TYR A O   
8304  C CB  . TYR B 1034 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1031 TYR A CB  
8305  C CG  . TYR B 1034 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1031 TYR A CG  
8306  C CD1 . TYR B 1034 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1031 TYR A CD1 
8307  C CD2 . TYR B 1034 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1031 TYR A CD2 
8308  C CE1 . TYR B 1034 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1031 TYR A CE1 
8309  C CE2 . TYR B 1034 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1031 TYR A CE2 
8310  C CZ  . TYR B 1034 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1031 TYR A CZ  
8311  O OH  . TYR B 1034 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1031 TYR A OH  
8312  N N   . PRO B 1035 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1032 PRO A N   
8313  C CA  . PRO B 1035 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1032 PRO A CA  
8314  C C   . PRO B 1035 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1032 PRO A C   
8315  O O   . PRO B 1035 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1032 PRO A O   
8316  C CB  . PRO B 1035 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1032 PRO A CB  
8317  C CG  . PRO B 1035 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1032 PRO A CG  
8318  C CD  . PRO B 1035 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1032 PRO A CD  
8319  N N   . ALA B 1036 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1033 ALA A N   
8320  C CA  . ALA B 1036 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1033 ALA A CA  
8321  C C   . ALA B 1036 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1033 ALA A C   
8322  O O   . ALA B 1036 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1033 ALA A O   
8323  C CB  . ALA B 1036 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1033 ALA A CB  
8324  N N   . GLU B 1037 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1034 GLU A N   
8325  C CA  . GLU B 1037 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1034 GLU A CA  
8326  C C   . GLU B 1037 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1034 GLU A C   
8327  O O   . GLU B 1037 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1034 GLU A O   
8333  N N   . LYS B 1038 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1035 LYS A N   
8334  C CA  . LYS B 1038 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1035 LYS A CA  
8335  C C   . LYS B 1038 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1035 LYS A C   
8336  O O   . LYS B 1038 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1035 LYS A O   
8342  N N   . VAL B 1039 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1036 VAL A N   
8343  C CA  . VAL B 1039 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1036 VAL A CA  
8344  C C   . VAL B 1039 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1036 VAL A C   
8345  O O   . VAL B 1039 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1036 VAL A O   
8346  C CB  . VAL B 1039 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1036 VAL A CB  
8347  C CG1 . VAL B 1039 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1036 VAL A CG1 
8348  C CG2 . VAL B 1039 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1036 VAL A CG2 
8349  N N   . GLY B 1040 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1037 GLY A N   
8350  C CA  . GLY B 1040 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1037 GLY A CA  
8351  C C   . GLY B 1040 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1037 GLY A C   
8352  O O   . GLY B 1040 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1037 GLY A O   
8353  N N   . GLY B 1041 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1038 GLY A N   
8354  C CA  . GLY B 1041 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1038 GLY A CA  
8355  C C   . GLY B 1041 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1038 GLY A C   
8356  O O   . GLY B 1041 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1038 GLY A O   
8357  N N   . VAL B 1042 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1039 VAL A N   
8358  C CA  . VAL B 1042 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1039 VAL A CA  
8359  C C   . VAL B 1042 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1039 VAL A C   
8360  O O   . VAL B 1042 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1039 VAL A O   
8361  C CB  . VAL B 1042 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1039 VAL A CB  
8362  C CG1 . VAL B 1042 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1039 VAL A CG1 
8363  C CG2 . VAL B 1042 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1039 VAL A CG2 
8364  N N   . LEU B 1043 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1040 LEU A N   
8365  C CA  . LEU B 1043 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1040 LEU A CA  
8366  C C   . LEU B 1043 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1040 LEU A C   
8367  O O   . LEU B 1043 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1040 LEU A O   
8368  C CB  . LEU B 1043 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1040 LEU A CB  
8369  C CG  . LEU B 1043 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1040 LEU A CG  
8370  C CD1 . LEU B 1043 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1040 LEU A CD1 
8371  C CD2 . LEU B 1043 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1040 LEU A CD2 
8372  N N   . ASN B 1044 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1041 ASN A N   
8373  C CA  . ASN B 1044 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1041 ASN A CA  
8374  C C   . ASN B 1044 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1041 ASN A C   
8375  O O   . ASN B 1044 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1041 ASN A O   
8376  C CB  . ASN B 1044 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1041 ASN A CB  
8377  C CG  . ASN B 1044 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1041 ASN A CG  
8378  O OD1 . ASN B 1044 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1041 ASN A OD1 
8379  N ND2 . ASN B 1044 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1041 ASN A ND2 
8380  N N   . PRO B 1045 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1042 PRO A N   
8381  C CA  . PRO B 1045 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1042 PRO A CA  
8382  C C   . PRO B 1045 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1042 PRO A C   
8383  O O   . PRO B 1045 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1042 PRO A O   
8384  C CB  . PRO B 1045 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1042 PRO A CB  
8385  C CG  . PRO B 1045 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1042 PRO A CG  
8386  C CD  . PRO B 1045 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1042 PRO A CD  
8387  N N   . TYR B 1046 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1043 TYR A N   
8388  C CA  . TYR B 1046 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1043 TYR A CA  
8389  C C   . TYR B 1046 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1043 TYR A C   
8390  O O   . TYR B 1046 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1043 TYR A O   
8391  C CB  . TYR B 1046 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1043 TYR A CB  
8392  C CG  . TYR B 1046 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1043 TYR A CG  
8393  C CD1 . TYR B 1046 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1043 TYR A CD1 
8394  C CD2 . TYR B 1046 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1043 TYR A CD2 
8395  C CE1 . TYR B 1046 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1043 TYR A CE1 
8396  C CE2 . TYR B 1046 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1043 TYR A CE2 
8397  C CZ  . TYR B 1046 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1043 TYR A CZ  
8398  O OH  . TYR B 1046 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1043 TYR A OH  
8399  N N   . GLN B 1047 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1044 GLN A N   
8400  C CA  . GLN B 1047 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1044 GLN A CA  
8401  C C   . GLN B 1047 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1044 GLN A C   
8402  O O   . GLN B 1047 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1044 GLN A O   
8403  C CB  . GLN B 1047 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1044 GLN A CB  
8404  C CG  . GLN B 1047 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1044 GLN A CG  
8405  C CD  . GLN B 1047 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1044 GLN A CD  
8406  O OE1 . GLN B 1047 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1044 GLN A OE1 
8407  N NE2 . GLN B 1047 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1044 GLN A NE2 
8408  N N   . LEU B 1048 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1045 LEU A N   
8409  C CA  . LEU B 1048 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1045 LEU A CA  
8410  C C   . LEU B 1048 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1045 LEU A C   
8411  O O   . LEU B 1048 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1045 LEU A O   
8412  C CB  . LEU B 1048 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1045 LEU A CB  
8413  C CG  . LEU B 1048 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1045 LEU A CG  
8414  C CD1 . LEU B 1048 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1045 LEU A CD1 
8415  C CD2 . LEU B 1048 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1045 LEU A CD2 
8416  N N   . THR B 1049 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1046 THR A N   
8417  C CA  . THR B 1049 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1046 THR A CA  
8418  C C   . THR B 1049 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1046 THR A C   
8419  O O   . THR B 1049 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1046 THR A O   
8420  C CB  . THR B 1049 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1046 THR A CB  
8421  O OG1 . THR B 1049 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1046 THR A OG1 
8422  C CG2 . THR B 1049 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1046 THR A CG2 
8423  N N   . ASP B 1050 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1047 ASP A N   
8424  C CA  . ASP B 1050 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1047 ASP A CA  
8425  C C   . ASP B 1050 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1047 ASP A C   
8426  O O   . ASP B 1050 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1047 ASP A O   
8427  C CB  . ASP B 1050 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1047 ASP A CB  
8428  C CG  . ASP B 1050 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1047 ASP A CG  
8429  O OD1 . ASP B 1050 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1047 ASP A OD1 
8430  O OD2 . ASP B 1050 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1047 ASP A OD2 
8431  N N   . GLN B 1051 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1048 GLN A N   
8432  C CA  . GLN B 1051 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1048 GLN A CA  
8433  C C   . GLN B 1051 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1048 GLN A C   
8434  O O   . GLN B 1051 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1048 GLN A O   
8435  C CB  . GLN B 1051 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1048 GLN A CB  
8436  C CG  . GLN B 1051 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1048 GLN A CG  
8437  C CD  . GLN B 1051 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1048 GLN A CD  
8438  O OE1 . GLN B 1051 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1048 GLN A OE1 
8439  N NE2 . GLN B 1051 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1048 GLN A NE2 
8440  N N   . PHE B 1052 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1049 PHE A N   
8441  C CA  . PHE B 1052 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1049 PHE A CA  
8442  C C   . PHE B 1052 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1049 PHE A C   
8443  O O   . PHE B 1052 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1049 PHE A O   
8444  C CB  . PHE B 1052 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1049 PHE A CB  
8445  C CG  . PHE B 1052 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1049 PHE A CG  
8446  C CD1 . PHE B 1052 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1049 PHE A CD1 
8447  C CD2 . PHE B 1052 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1049 PHE A CD2 
8448  C CE1 . PHE B 1052 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1049 PHE A CE1 
8449  C CE2 . PHE B 1052 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1049 PHE A CE2 
8450  C CZ  . PHE B 1052 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1049 PHE A CZ  
8451  N N   . THR B 1053 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1050 THR A N   
8452  C CA  . THR B 1053 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1050 THR A CA  
8453  C C   . THR B 1053 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1050 THR A C   
8454  O O   . THR B 1053 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1050 THR A O   
8455  C CB  . THR B 1053 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1050 THR A CB  
8456  O OG1 . THR B 1053 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1050 THR A OG1 
8457  C CG2 . THR B 1053 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1050 THR A CG2 
8458  N N   . SER B 1054 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1051 SER A N   
8459  C CA  . SER B 1054 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1051 SER A CA  
8460  C C   . SER B 1054 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1051 SER A C   
8461  O O   . SER B 1054 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1051 SER A O   
8462  C CB  . SER B 1054 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1051 SER A CB  
8463  O OG  . SER B 1054 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1051 SER A OG  
8464  N N   . PHE B 1055 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1052 PHE A N   
8465  C CA  . PHE B 1055 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1052 PHE A CA  
8466  C C   . PHE B 1055 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1052 PHE A C   
8467  O O   . PHE B 1055 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1052 PHE A O   
8468  C CB  . PHE B 1055 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1052 PHE A CB  
8469  C CG  . PHE B 1055 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1052 PHE A CG  
8470  C CD1 . PHE B 1055 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1052 PHE A CD1 
8471  C CD2 . PHE B 1055 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1052 PHE A CD2 
8472  C CE1 . PHE B 1055 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1052 PHE A CE1 
8473  C CE2 . PHE B 1055 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1052 PHE A CE2 
8474  C CZ  . PHE B 1055 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1052 PHE A CZ  
8475  N N   . ALA B 1056 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1053 ALA A N   
8476  C CA  . ALA B 1056 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1053 ALA A CA  
8477  C C   . ALA B 1056 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1053 ALA A C   
8478  O O   . ALA B 1056 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1053 ALA A O   
8479  C CB  . ALA B 1056 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1053 ALA A CB  
8480  N N   . LYS B 1057 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1054 LYS A N   
8481  C CA  . LYS B 1057 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1054 LYS A CA  
8482  C C   . LYS B 1057 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1054 LYS A C   
8483  O O   . LYS B 1057 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1054 LYS A O   
8484  C CB  . LYS B 1057 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1054 LYS A CB  
8485  C CG  . LYS B 1057 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1054 LYS A CG  
8486  C CD  . LYS B 1057 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1054 LYS A CD  
8487  C CE  . LYS B 1057 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1054 LYS A CE  
8488  N NZ  . LYS B 1057 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1054 LYS A NZ  
8489  N N   . MET B 1058 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1055 MET A N   
8490  C CA  . MET B 1058 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1055 MET A CA  
8491  C C   . MET B 1058 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1055 MET A C   
8492  O O   . MET B 1058 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1055 MET A O   
8493  C CB  . MET B 1058 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1055 MET A CB  
8494  C CG  . MET B 1058 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1055 MET A CG  
8495  S SD  . MET B 1058 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1055 MET A SD  
8496  C CE  . MET B 1058 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1055 MET A CE  
8497  N N   . GLY B 1059 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1056 GLY A N   
8498  C CA  . GLY B 1059 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1056 GLY A CA  
8499  C C   . GLY B 1059 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1056 GLY A C   
8500  O O   . GLY B 1059 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1056 GLY A O   
8501  N N   . THR B 1060 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1057 THR A N   
8502  C CA  . THR B 1060 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1057 THR A CA  
8503  C C   . THR B 1060 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1057 THR A C   
8504  O O   . THR B 1060 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1057 THR A O   
8505  C CB  . THR B 1060 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1057 THR A CB  
8506  O OG1 . THR B 1060 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1057 THR A OG1 
8507  C CG2 . THR B 1060 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1057 THR A CG2 
8508  N N   . GLN B 1061 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1058 GLN A N   
8509  C CA  . GLN B 1061 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1058 GLN A CA  
8510  C C   . GLN B 1061 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1058 GLN A C   
8511  O O   . GLN B 1061 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1058 GLN A O   
8512  C CB  . GLN B 1061 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1058 GLN A CB  
8513  C CG  . GLN B 1061 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1058 GLN A CG  
8514  C CD  . GLN B 1061 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1058 GLN A CD  
8515  O OE1 . GLN B 1061 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1058 GLN A OE1 
8516  N NE2 . GLN B 1061 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1058 GLN A NE2 
8517  N N   . SER B 1062 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1059 SER A N   
8518  C CA  . SER B 1062 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1059 SER A CA  
8519  C C   . SER B 1062 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1059 SER A C   
8520  O O   . SER B 1062 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1059 SER A O   
8521  C CB  . SER B 1062 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1059 SER A CB  
8522  O OG  . SER B 1062 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1059 SER A OG  
8523  N N   . GLY B 1063 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1060 GLY A N   
8524  C CA  . GLY B 1063 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1060 GLY A CA  
8525  C C   . GLY B 1063 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1060 GLY A C   
8526  O O   . GLY B 1063 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1060 GLY A O   
8527  N N   . PHE B 1064 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1061 PHE A N   
8528  C CA  . PHE B 1064 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1061 PHE A CA  
8529  C C   . PHE B 1064 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1061 PHE A C   
8530  O O   . PHE B 1064 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1061 PHE A O   
8531  C CB  . PHE B 1064 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1061 PHE A CB  
8532  C CG  . PHE B 1064 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1061 PHE A CG  
8533  C CD1 . PHE B 1064 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1061 PHE A CD1 
8534  C CD2 . PHE B 1064 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1061 PHE A CD2 
8535  C CE1 . PHE B 1064 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1061 PHE A CE1 
8536  C CE2 . PHE B 1064 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1061 PHE A CE2 
8537  C CZ  . PHE B 1064 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1061 PHE A CZ  
8538  N N   . LEU B 1065 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1062 LEU A N   
8539  C CA  . LEU B 1065 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1062 LEU A CA  
8540  C C   . LEU B 1065 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1062 LEU A C   
8541  O O   . LEU B 1065 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1062 LEU A O   
8542  C CB  . LEU B 1065 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1062 LEU A CB  
8543  C CG  . LEU B 1065 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1062 LEU A CG  
8544  C CD1 . LEU B 1065 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1062 LEU A CD1 
8545  C CD2 . LEU B 1065 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1062 LEU A CD2 
8546  N N   . PHE B 1066 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1063 PHE A N   
8547  C CA  . PHE B 1066 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1063 PHE A CA  
8548  C C   . PHE B 1066 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1063 PHE A C   
8549  O O   . PHE B 1066 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1063 PHE A O   
8550  C CB  . PHE B 1066 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1063 PHE A CB  
8551  C CG  . PHE B 1066 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1063 PHE A CG  
8552  C CD1 . PHE B 1066 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1063 PHE A CD1 
8553  C CD2 . PHE B 1066 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1063 PHE A CD2 
8554  C CE1 . PHE B 1066 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1063 PHE A CE1 
8555  C CE2 . PHE B 1066 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1063 PHE A CE2 
8556  C CZ  . PHE B 1066 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1063 PHE A CZ  
8557  N N   . TYR B 1067 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1064 TYR A N   
8558  C CA  . TYR B 1067 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1064 TYR A CA  
8559  C C   . TYR B 1067 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1064 TYR A C   
8560  O O   . TYR B 1067 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1064 TYR A O   
8561  C CB  . TYR B 1067 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1064 TYR A CB  
8562  C CG  . TYR B 1067 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1064 TYR A CG  
8563  C CD1 . TYR B 1067 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1064 TYR A CD1 
8564  C CD2 . TYR B 1067 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1064 TYR A CD2 
8565  C CE1 . TYR B 1067 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1064 TYR A CE1 
8566  C CE2 . TYR B 1067 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1064 TYR A CE2 
8567  C CZ  . TYR B 1067 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1064 TYR A CZ  
8568  O OH  . TYR B 1067 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1064 TYR A OH  
8569  N N   . VAL B 1068 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1065 VAL A N   
8570  C CA  . VAL B 1068 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1065 VAL A CA  
8571  C C   . VAL B 1068 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1065 VAL A C   
8572  O O   . VAL B 1068 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1065 VAL A O   
8573  C CB  . VAL B 1068 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1065 VAL A CB  
8574  C CG1 . VAL B 1068 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1065 VAL A CG1 
8575  C CG2 . VAL B 1068 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1065 VAL A CG2 
8576  N N   . PRO B 1069 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1066 PRO A N   
8577  C CA  . PRO B 1069 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1066 PRO A CA  
8578  C C   . PRO B 1069 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1066 PRO A C   
8579  O O   . PRO B 1069 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1066 PRO A O   
8580  C CB  . PRO B 1069 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1066 PRO A CB  
8581  C CG  . PRO B 1069 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1066 PRO A CG  
8582  C CD  . PRO B 1069 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1066 PRO A CD  
8583  N N   . ALA B 1070 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1067 ALA A N   
8584  C CA  . ALA B 1070 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1067 ALA A CA  
8585  C C   . ALA B 1070 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1067 ALA A C   
8586  O O   . ALA B 1070 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1067 ALA A O   
8587  C CB  . ALA B 1070 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1067 ALA A CB  
8588  N N   . PRO B 1071 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1068 PRO A N   
8589  C CA  . PRO B 1071 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1068 PRO A CA  
8590  C C   . PRO B 1071 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1068 PRO A C   
8591  O O   . PRO B 1071 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1068 PRO A O   
8592  C CB  . PRO B 1071 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1068 PRO A CB  
8593  C CG  . PRO B 1071 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1068 PRO A CG  
8594  C CD  . PRO B 1071 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1068 PRO A CD  
8595  N N   . TYR B 1072 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1069 TYR A N   
8596  C CA  . TYR B 1072 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1069 TYR A CA  
8597  C C   . TYR B 1072 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1069 TYR A C   
8598  O O   . TYR B 1072 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1069 TYR A O   
8599  C CB  . TYR B 1072 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1069 TYR A CB  
8600  C CG  . TYR B 1072 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1069 TYR A CG  
8601  C CD1 . TYR B 1072 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1069 TYR A CD1 
8602  C CD2 . TYR B 1072 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1069 TYR A CD2 
8603  C CE1 . TYR B 1072 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1069 TYR A CE1 
8604  C CE2 . TYR B 1072 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1069 TYR A CE2 
8605  C CZ  . TYR B 1072 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1069 TYR A CZ  
8606  O OH  . TYR B 1072 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1069 TYR A OH  
8607  N N   . THR B 1073 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1070 THR A N   
8608  C CA  . THR B 1073 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1070 THR A CA  
8609  C C   . THR B 1073 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1070 THR A C   
8610  O O   . THR B 1073 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1070 THR A O   
8611  C CB  . THR B 1073 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1070 THR A CB  
8612  O OG1 . THR B 1073 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1070 THR A OG1 
8613  C CG2 . THR B 1073 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1070 THR A CG2 
8614  N N   . SER B 1074 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1071 SER A N   
8615  C CA  . SER B 1074 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1071 SER A CA  
8616  C C   . SER B 1074 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1071 SER A C   
8617  O O   . SER B 1074 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1071 SER A O   
8618  C CB  . SER B 1074 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1071 SER A CB  
8619  O OG  . SER B 1074 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1071 SER A OG  
8620  N N   . LYS B 1075 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1072 LYS A N   
8621  C CA  . LYS B 1075 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1072 LYS A CA  
8622  C C   . LYS B 1075 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1072 LYS A C   
8623  O O   . LYS B 1075 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1072 LYS A O   
8624  C CB  . LYS B 1075 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1072 LYS A CB  
8625  C CG  . LYS B 1075 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1072 LYS A CG  
8626  C CD  . LYS B 1075 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1072 LYS A CD  
8627  C CE  . LYS B 1075 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1072 LYS A CE  
8628  N NZ  . LYS B 1075 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1072 LYS A NZ  
8629  N N   . ILE B 1076 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1073 ILE A N   
8630  C CA  . ILE B 1076 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1073 ILE A CA  
8631  C C   . ILE B 1076 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1073 ILE A C   
8632  O O   . ILE B 1076 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1073 ILE A O   
8633  C CB  . ILE B 1076 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1073 ILE A CB  
8634  C CG1 . ILE B 1076 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1073 ILE A CG1 
8635  C CG2 . ILE B 1076 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1073 ILE A CG2 
8636  C CD1 . ILE B 1076 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1073 ILE A CD1 
8637  N N   . ASP B 1077 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1074 ASP A N   
8638  C CA  . ASP B 1077 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1074 ASP A CA  
8639  C C   . ASP B 1077 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1074 ASP A C   
8640  O O   . ASP B 1077 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1074 ASP A O   
8641  C CB  . ASP B 1077 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1074 ASP A CB  
8642  C CG  . ASP B 1077 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1074 ASP A CG  
8643  O OD1 . ASP B 1077 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1074 ASP A OD1 
8644  O OD2 . ASP B 1077 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1074 ASP A OD2 
8645  N N   . PRO B 1078 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1075 PRO A N   
8646  C CA  . PRO B 1078 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1075 PRO A CA  
8647  C C   . PRO B 1078 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1075 PRO A C   
8648  O O   . PRO B 1078 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1075 PRO A O   
8649  C CB  . PRO B 1078 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1075 PRO A CB  
8650  C CG  . PRO B 1078 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1075 PRO A CG  
8651  C CD  . PRO B 1078 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1075 PRO A CD  
8652  N N   . LEU B 1079 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1076 LEU A N   
8653  C CA  . LEU B 1079 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1076 LEU A CA  
8654  C C   . LEU B 1079 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1076 LEU A C   
8655  O O   . LEU B 1079 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1076 LEU A O   
8656  C CB  . LEU B 1079 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1076 LEU A CB  
8657  C CG  . LEU B 1079 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1076 LEU A CG  
8658  C CD1 . LEU B 1079 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1076 LEU A CD1 
8659  C CD2 . LEU B 1079 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1076 LEU A CD2 
8660  N N   . THR B 1080 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1077 THR A N   
8661  C CA  . THR B 1080 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1077 THR A CA  
8662  C C   . THR B 1080 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1077 THR A C   
8663  O O   . THR B 1080 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1077 THR A O   
8664  C CB  . THR B 1080 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1077 THR A CB  
8665  O OG1 . THR B 1080 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1077 THR A OG1 
8666  C CG2 . THR B 1080 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1077 THR A CG2 
8667  N N   . GLY B 1081 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1078 GLY A N   
8668  C CA  . GLY B 1081 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1078 GLY A CA  
8669  C C   . GLY B 1081 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1078 GLY A C   
8670  O O   . GLY B 1081 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1078 GLY A O   
8671  N N   . PHE B 1082 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1079 PHE A N   
8672  C CA  . PHE B 1082 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1079 PHE A CA  
8673  C C   . PHE B 1082 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1079 PHE A C   
8674  O O   . PHE B 1082 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1079 PHE A O   
8675  C CB  . PHE B 1082 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1079 PHE A CB  
8676  C CG  . PHE B 1082 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1079 PHE A CG  
8677  C CD1 . PHE B 1082 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1079 PHE A CD1 
8678  C CD2 . PHE B 1082 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1079 PHE A CD2 
8679  C CE1 . PHE B 1082 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1079 PHE A CE1 
8680  C CE2 . PHE B 1082 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1079 PHE A CE2 
8681  C CZ  . PHE B 1082 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1079 PHE A CZ  
8682  N N   . VAL B 1083 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1080 VAL A N   
8683  C CA  . VAL B 1083 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1080 VAL A CA  
8684  C C   . VAL B 1083 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1080 VAL A C   
8685  O O   . VAL B 1083 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1080 VAL A O   
8686  C CB  . VAL B 1083 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1080 VAL A CB  
8687  C CG1 . VAL B 1083 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1080 VAL A CG1 
8688  C CG2 . VAL B 1083 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1080 VAL A CG2 
8689  N N   . ASP B 1084 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1081 ASP A N   
8690  C CA  . ASP B 1084 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1081 ASP A CA  
8691  C C   . ASP B 1084 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1081 ASP A C   
8692  O O   . ASP B 1084 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1081 ASP A O   
8693  C CB  . ASP B 1084 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1081 ASP A CB  
8694  C CG  . ASP B 1084 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1081 ASP A CG  
8695  O OD1 . ASP B 1084 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1081 ASP A OD1 
8696  O OD2 . ASP B 1084 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1081 ASP A OD2 
8697  N N   . PRO B 1085 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1082 PRO A N   
8698  C CA  . PRO B 1085 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1082 PRO A CA  
8699  C C   . PRO B 1085 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1082 PRO A C   
8700  O O   . PRO B 1085 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1082 PRO A O   
8701  C CB  . PRO B 1085 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1082 PRO A CB  
8702  C CG  . PRO B 1085 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1082 PRO A CG  
8703  C CD  . PRO B 1085 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1082 PRO A CD  
8704  N N   . PHE B 1086 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1083 PHE A N   
8705  C CA  . PHE B 1086 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1083 PHE A CA  
8706  C C   . PHE B 1086 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1083 PHE A C   
8707  O O   . PHE B 1086 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1083 PHE A O   
8708  C CB  . PHE B 1086 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1083 PHE A CB  
8709  C CG  . PHE B 1086 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1083 PHE A CG  
8710  C CD1 . PHE B 1086 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1083 PHE A CD1 
8711  C CD2 . PHE B 1086 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1083 PHE A CD2 
8712  C CE1 . PHE B 1086 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1083 PHE A CE1 
8713  C CE2 . PHE B 1086 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1083 PHE A CE2 
8714  C CZ  . PHE B 1086 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1083 PHE A CZ  
8715  N N   . VAL B 1087 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1084 VAL A N   
8716  C CA  . VAL B 1087 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1084 VAL A CA  
8717  C C   . VAL B 1087 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1084 VAL A C   
8718  O O   . VAL B 1087 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1084 VAL A O   
8719  C CB  . VAL B 1087 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1084 VAL A CB  
8720  C CG1 . VAL B 1087 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1084 VAL A CG1 
8721  C CG2 . VAL B 1087 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1084 VAL A CG2 
8722  N N   . TRP B 1088 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1085 TRP A N   
8723  C CA  . TRP B 1088 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1085 TRP A CA  
8724  C C   . TRP B 1088 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1085 TRP A C   
8725  O O   . TRP B 1088 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1085 TRP A O   
8726  C CB  . TRP B 1088 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1085 TRP A CB  
8727  C CG  . TRP B 1088 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1085 TRP A CG  
8728  C CD1 . TRP B 1088 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1085 TRP A CD1 
8729  C CD2 . TRP B 1088 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1085 TRP A CD2 
8730  N NE1 . TRP B 1088 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1085 TRP A NE1 
8731  C CE2 . TRP B 1088 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1085 TRP A CE2 
8732  C CE3 . TRP B 1088 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1085 TRP A CE3 
8733  C CZ2 . TRP B 1088 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1085 TRP A CZ2 
8734  C CZ3 . TRP B 1088 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1085 TRP A CZ3 
8735  C CH2 . TRP B 1088 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1085 TRP A CH2 
8736  N N   . LYS B 1089 ? 0.7376 0.7376 0.7376 0.0000  0.0000  0.0000  1086 LYS A N   
8737  C CA  . LYS B 1089 ? 0.7376 0.7376 0.7376 0.0000  0.0000  0.0000  1086 LYS A CA  
8738  C C   . LYS B 1089 ? 0.7376 0.7376 0.7376 0.0000  0.0000  0.0000  1086 LYS A C   
8739  O O   . LYS B 1089 ? 0.7376 0.7376 0.7376 0.0000  0.0000  0.0000  1086 LYS A O   
8740  C CB  . LYS B 1089 ? 0.7376 0.7376 0.7376 0.0000  0.0000  0.0000  1086 LYS A CB  
8741  C CG  . LYS B 1089 ? 0.7376 0.7376 0.7376 0.0000  0.0000  0.0000  1086 LYS A CG  
8742  C CD  . LYS B 1089 ? 0.7376 0.7376 0.7376 0.0000  0.0000  0.0000  1086 LYS A CD  
8743  C CE  . LYS B 1089 ? 0.7376 0.7376 0.7376 0.0000  0.0000  0.0000  1086 LYS A CE  
8744  N NZ  . LYS B 1089 ? 0.7376 0.7376 0.7376 0.0000  0.0000  0.0000  1086 LYS A NZ  
8745  N N   . THR B 1090 ? 0.6170 0.6170 0.6170 0.0000  0.0000  0.0000  1087 THR A N   
8746  C CA  . THR B 1090 ? 0.6170 0.6170 0.6170 0.0000  0.0000  0.0000  1087 THR A CA  
8747  C C   . THR B 1090 ? 0.6170 0.6170 0.6170 0.0000  0.0000  0.0000  1087 THR A C   
8748  O O   . THR B 1090 ? 0.6170 0.6170 0.6170 0.0000  0.0000  0.0000  1087 THR A O   
8749  C CB  . THR B 1090 ? 0.6170 0.6170 0.6170 0.0000  0.0000  0.0000  1087 THR A CB  
8750  O OG1 . THR B 1090 ? 0.6170 0.6170 0.6170 0.0000  0.0000  0.0000  1087 THR A OG1 
8751  C CG2 . THR B 1090 ? 0.6170 0.6170 0.6170 0.0000  0.0000  0.0000  1087 THR A CG2 
8752  N N   . ILE B 1091 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1088 ILE A N   
8753  C CA  . ILE B 1091 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1088 ILE A CA  
8754  C C   . ILE B 1091 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1088 ILE A C   
8755  O O   . ILE B 1091 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1088 ILE A O   
8756  C CB  . ILE B 1091 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1088 ILE A CB  
8757  C CG1 . ILE B 1091 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1088 ILE A CG1 
8758  C CG2 . ILE B 1091 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1088 ILE A CG2 
8759  C CD1 . ILE B 1091 ? 0.6296 0.6296 0.6296 0.0000  0.0000  0.0000  1088 ILE A CD1 
8760  N N   . LYS B 1092 ? 0.6961 0.6961 0.6961 0.0000  0.0000  0.0000  1089 LYS A N   
8761  C CA  . LYS B 1092 ? 0.6961 0.6961 0.6961 0.0000  0.0000  0.0000  1089 LYS A CA  
8762  C C   . LYS B 1092 ? 0.6961 0.6961 0.6961 0.0000  0.0000  0.0000  1089 LYS A C   
8763  O O   . LYS B 1092 ? 0.6961 0.6961 0.6961 0.0000  0.0000  0.0000  1089 LYS A O   
8769  N N   . ASN B 1093 ? 0.6854 0.6854 0.6854 0.0000  0.0000  0.0000  1090 ASN A N   
8770  C CA  . ASN B 1093 ? 0.6854 0.6854 0.6854 0.0000  0.0000  0.0000  1090 ASN A CA  
8771  C C   . ASN B 1093 ? 0.6854 0.6854 0.6854 0.0000  0.0000  0.0000  1090 ASN A C   
8772  O O   . ASN B 1093 ? 0.6854 0.6854 0.6854 0.0000  0.0000  0.0000  1090 ASN A O   
8773  C CB  . ASN B 1093 ? 0.6854 0.6854 0.6854 0.0000  0.0000  0.0000  1090 ASN A CB  
8774  C CG  . ASN B 1093 ? 0.6854 0.6854 0.6854 0.0000  0.0000  0.0000  1090 ASN A CG  
8775  O OD1 . ASN B 1093 ? 0.6854 0.6854 0.6854 0.0000  0.0000  0.0000  1090 ASN A OD1 
8776  N ND2 . ASN B 1093 ? 0.6854 0.6854 0.6854 0.0000  0.0000  0.0000  1090 ASN A ND2 
8777  N N   . HIS B 1094 ? 0.6769 0.6769 0.6769 0.0000  0.0000  0.0000  1091 HIS A N   
8778  C CA  . HIS B 1094 ? 0.6769 0.6769 0.6769 0.0000  0.0000  0.0000  1091 HIS A CA  
8779  C C   . HIS B 1094 ? 0.6769 0.6769 0.6769 0.0000  0.0000  0.0000  1091 HIS A C   
8780  O O   . HIS B 1094 ? 0.6769 0.6769 0.6769 0.0000  0.0000  0.0000  1091 HIS A O   
8781  C CB  . HIS B 1094 ? 0.6769 0.6769 0.6769 0.0000  0.0000  0.0000  1091 HIS A CB  
8782  C CG  . HIS B 1094 ? 0.6769 0.6769 0.6769 0.0000  0.0000  0.0000  1091 HIS A CG  
8783  N ND1 . HIS B 1094 ? 0.6769 0.6769 0.6769 0.0000  0.0000  0.0000  1091 HIS A ND1 
8784  C CD2 . HIS B 1094 ? 0.6769 0.6769 0.6769 0.0000  0.0000  0.0000  1091 HIS A CD2 
8785  C CE1 . HIS B 1094 ? 0.6769 0.6769 0.6769 0.0000  0.0000  0.0000  1091 HIS A CE1 
8786  N NE2 . HIS B 1094 ? 0.6769 0.6769 0.6769 0.0000  0.0000  0.0000  1091 HIS A NE2 
8787  N N   . GLU B 1095 ? 0.7132 0.7132 0.7132 0.0000  0.0000  0.0000  1092 GLU A N   
8788  C CA  . GLU B 1095 ? 0.7132 0.7132 0.7132 0.0000  0.0000  0.0000  1092 GLU A CA  
8789  C C   . GLU B 1095 ? 0.7132 0.7132 0.7132 0.0000  0.0000  0.0000  1092 GLU A C   
8790  O O   . GLU B 1095 ? 0.7132 0.7132 0.7132 0.0000  0.0000  0.0000  1092 GLU A O   
8791  C CB  . GLU B 1095 ? 0.7132 0.7132 0.7132 0.0000  0.0000  0.0000  1092 GLU A CB  
8792  C CG  . GLU B 1095 ? 0.7132 0.7132 0.7132 0.0000  0.0000  0.0000  1092 GLU A CG  
8793  C CD  . GLU B 1095 ? 0.7132 0.7132 0.7132 0.0000  0.0000  0.0000  1092 GLU A CD  
8794  O OE1 . GLU B 1095 ? 0.7132 0.7132 0.7132 0.0000  0.0000  0.0000  1092 GLU A OE1 
8795  O OE2 . GLU B 1095 ? 0.7132 0.7132 0.7132 0.0000  0.0000  0.0000  1092 GLU A OE2 
8796  N N   . SER B 1096 ? 0.6607 0.6607 0.6607 0.0000  0.0000  0.0000  1093 SER A N   
8797  C CA  . SER B 1096 ? 0.6607 0.6607 0.6607 0.0000  0.0000  0.0000  1093 SER A CA  
8798  C C   . SER B 1096 ? 0.6607 0.6607 0.6607 0.0000  0.0000  0.0000  1093 SER A C   
8799  O O   . SER B 1096 ? 0.6607 0.6607 0.6607 0.0000  0.0000  0.0000  1093 SER A O   
8800  C CB  . SER B 1096 ? 0.6607 0.6607 0.6607 0.0000  0.0000  0.0000  1093 SER A CB  
8801  O OG  . SER B 1096 ? 0.6607 0.6607 0.6607 0.0000  0.0000  0.0000  1093 SER A OG  
8802  N N   . ARG B 1097 ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  1094 ARG A N   
8803  C CA  . ARG B 1097 ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  1094 ARG A CA  
8804  C C   . ARG B 1097 ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  1094 ARG A C   
8805  O O   . ARG B 1097 ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  1094 ARG A O   
8806  C CB  . ARG B 1097 ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  1094 ARG A CB  
8807  C CG  . ARG B 1097 ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  1094 ARG A CG  
8808  C CD  . ARG B 1097 ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  1094 ARG A CD  
8809  N NE  . ARG B 1097 ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  1094 ARG A NE  
8810  C CZ  . ARG B 1097 ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  1094 ARG A CZ  
8811  N NH1 . ARG B 1097 ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  1094 ARG A NH1 
8812  N NH2 . ARG B 1097 ? 0.6478 0.6478 0.6478 0.0000  0.0000  0.0000  1094 ARG A NH2 
8813  N N   . LYS B 1098 ? 0.6638 0.6638 0.6638 0.0000  0.0000  0.0000  1095 LYS A N   
8814  C CA  . LYS B 1098 ? 0.6638 0.6638 0.6638 0.0000  0.0000  0.0000  1095 LYS A CA  
8815  C C   . LYS B 1098 ? 0.6638 0.6638 0.6638 0.0000  0.0000  0.0000  1095 LYS A C   
8816  O O   . LYS B 1098 ? 0.6638 0.6638 0.6638 0.0000  0.0000  0.0000  1095 LYS A O   
8822  N N   . HIS B 1099 ? 0.6198 0.6198 0.6198 0.0000  0.0000  0.0000  1096 HIS A N   
8823  C CA  . HIS B 1099 ? 0.6198 0.6198 0.6198 0.0000  0.0000  0.0000  1096 HIS A CA  
8824  C C   . HIS B 1099 ? 0.6198 0.6198 0.6198 0.0000  0.0000  0.0000  1096 HIS A C   
8825  O O   . HIS B 1099 ? 0.6198 0.6198 0.6198 0.0000  0.0000  0.0000  1096 HIS A O   
8826  C CB  . HIS B 1099 ? 0.6198 0.6198 0.6198 0.0000  0.0000  0.0000  1096 HIS A CB  
8827  C CG  . HIS B 1099 ? 0.6198 0.6198 0.6198 0.0000  0.0000  0.0000  1096 HIS A CG  
8828  N ND1 . HIS B 1099 ? 0.6198 0.6198 0.6198 0.0000  0.0000  0.0000  1096 HIS A ND1 
8829  C CD2 . HIS B 1099 ? 0.6198 0.6198 0.6198 0.0000  0.0000  0.0000  1096 HIS A CD2 
8830  C CE1 . HIS B 1099 ? 0.6198 0.6198 0.6198 0.0000  0.0000  0.0000  1096 HIS A CE1 
8831  N NE2 . HIS B 1099 ? 0.6198 0.6198 0.6198 0.0000  0.0000  0.0000  1096 HIS A NE2 
8832  N N   . PHE B 1100 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1097 PHE A N   
8833  C CA  . PHE B 1100 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1097 PHE A CA  
8834  C C   . PHE B 1100 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1097 PHE A C   
8835  O O   . PHE B 1100 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1097 PHE A O   
8836  C CB  . PHE B 1100 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1097 PHE A CB  
8837  C CG  . PHE B 1100 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1097 PHE A CG  
8838  C CD1 . PHE B 1100 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1097 PHE A CD1 
8839  C CD2 . PHE B 1100 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1097 PHE A CD2 
8840  C CE1 . PHE B 1100 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1097 PHE A CE1 
8841  C CE2 . PHE B 1100 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1097 PHE A CE2 
8842  C CZ  . PHE B 1100 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1097 PHE A CZ  
8843  N N   . LEU B 1101 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1098 LEU A N   
8844  C CA  . LEU B 1101 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1098 LEU A CA  
8845  C C   . LEU B 1101 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1098 LEU A C   
8846  O O   . LEU B 1101 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1098 LEU A O   
8847  C CB  . LEU B 1101 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1098 LEU A CB  
8848  C CG  . LEU B 1101 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1098 LEU A CG  
8849  C CD1 . LEU B 1101 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1098 LEU A CD1 
8850  C CD2 . LEU B 1101 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1098 LEU A CD2 
8851  N N   . GLU B 1102 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1099 GLU A N   
8852  C CA  . GLU B 1102 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1099 GLU A CA  
8853  C C   . GLU B 1102 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1099 GLU A C   
8854  O O   . GLU B 1102 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1099 GLU A O   
8855  C CB  . GLU B 1102 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1099 GLU A CB  
8856  C CG  . GLU B 1102 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1099 GLU A CG  
8857  C CD  . GLU B 1102 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1099 GLU A CD  
8858  O OE1 . GLU B 1102 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1099 GLU A OE1 
8859  O OE2 . GLU B 1102 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1099 GLU A OE2 
8860  N N   . GLY B 1103 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1100 GLY A N   
8861  C CA  . GLY B 1103 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1100 GLY A CA  
8862  C C   . GLY B 1103 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1100 GLY A C   
8863  O O   . GLY B 1103 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1100 GLY A O   
8864  N N   . PHE B 1104 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1101 PHE A N   
8865  C CA  . PHE B 1104 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1101 PHE A CA  
8866  C C   . PHE B 1104 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1101 PHE A C   
8867  O O   . PHE B 1104 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1101 PHE A O   
8868  C CB  . PHE B 1104 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1101 PHE A CB  
8869  C CG  . PHE B 1104 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1101 PHE A CG  
8870  C CD1 . PHE B 1104 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1101 PHE A CD1 
8871  C CD2 . PHE B 1104 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1101 PHE A CD2 
8872  C CE1 . PHE B 1104 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1101 PHE A CE1 
8873  C CE2 . PHE B 1104 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1101 PHE A CE2 
8874  C CZ  . PHE B 1104 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1101 PHE A CZ  
8875  N N   . ASP B 1105 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1102 ASP A N   
8876  C CA  . ASP B 1105 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1102 ASP A CA  
8877  C C   . ASP B 1105 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1102 ASP A C   
8878  O O   . ASP B 1105 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1102 ASP A O   
8879  C CB  . ASP B 1105 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1102 ASP A CB  
8880  C CG  . ASP B 1105 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1102 ASP A CG  
8881  O OD1 . ASP B 1105 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1102 ASP A OD1 
8882  O OD2 . ASP B 1105 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1102 ASP A OD2 
8883  N N   . PHE B 1106 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1103 PHE A N   
8884  C CA  . PHE B 1106 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1103 PHE A CA  
8885  C C   . PHE B 1106 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1103 PHE A C   
8886  O O   . PHE B 1106 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1103 PHE A O   
8887  C CB  . PHE B 1106 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1103 PHE A CB  
8888  C CG  . PHE B 1106 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1103 PHE A CG  
8889  C CD1 . PHE B 1106 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1103 PHE A CD1 
8890  C CD2 . PHE B 1106 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1103 PHE A CD2 
8891  C CE1 . PHE B 1106 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1103 PHE A CE1 
8892  C CE2 . PHE B 1106 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1103 PHE A CE2 
8893  C CZ  . PHE B 1106 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1103 PHE A CZ  
8894  N N   . LEU B 1107 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1104 LEU A N   
8895  C CA  . LEU B 1107 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1104 LEU A CA  
8896  C C   . LEU B 1107 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1104 LEU A C   
8897  O O   . LEU B 1107 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1104 LEU A O   
8898  C CB  . LEU B 1107 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1104 LEU A CB  
8899  C CG  . LEU B 1107 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1104 LEU A CG  
8900  C CD1 . LEU B 1107 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1104 LEU A CD1 
8901  C CD2 . LEU B 1107 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1104 LEU A CD2 
8902  N N   . HIS B 1108 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1105 HIS A N   
8903  C CA  . HIS B 1108 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1105 HIS A CA  
8904  C C   . HIS B 1108 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1105 HIS A C   
8905  O O   . HIS B 1108 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1105 HIS A O   
8906  C CB  . HIS B 1108 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1105 HIS A CB  
8907  C CG  . HIS B 1108 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1105 HIS A CG  
8908  N ND1 . HIS B 1108 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1105 HIS A ND1 
8909  C CD2 . HIS B 1108 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1105 HIS A CD2 
8910  C CE1 . HIS B 1108 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1105 HIS A CE1 
8911  N NE2 . HIS B 1108 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1105 HIS A NE2 
8912  N N   . TYR B 1109 ? 0.6476 0.6476 0.6476 0.0000  0.0000  0.0000  1106 TYR A N   
8913  C CA  . TYR B 1109 ? 0.6476 0.6476 0.6476 0.0000  0.0000  0.0000  1106 TYR A CA  
8914  C C   . TYR B 1109 ? 0.6476 0.6476 0.6476 0.0000  0.0000  0.0000  1106 TYR A C   
8915  O O   . TYR B 1109 ? 0.6476 0.6476 0.6476 0.0000  0.0000  0.0000  1106 TYR A O   
8916  C CB  . TYR B 1109 ? 0.6476 0.6476 0.6476 0.0000  0.0000  0.0000  1106 TYR A CB  
8917  C CG  . TYR B 1109 ? 0.6476 0.6476 0.6476 0.0000  0.0000  0.0000  1106 TYR A CG  
8918  C CD1 . TYR B 1109 ? 0.6476 0.6476 0.6476 0.0000  0.0000  0.0000  1106 TYR A CD1 
8919  C CD2 . TYR B 1109 ? 0.6476 0.6476 0.6476 0.0000  0.0000  0.0000  1106 TYR A CD2 
8920  C CE1 . TYR B 1109 ? 0.6476 0.6476 0.6476 0.0000  0.0000  0.0000  1106 TYR A CE1 
8921  C CE2 . TYR B 1109 ? 0.6476 0.6476 0.6476 0.0000  0.0000  0.0000  1106 TYR A CE2 
8922  C CZ  . TYR B 1109 ? 0.6476 0.6476 0.6476 0.0000  0.0000  0.0000  1106 TYR A CZ  
8923  O OH  . TYR B 1109 ? 0.6476 0.6476 0.6476 0.0000  0.0000  0.0000  1106 TYR A OH  
8924  N N   . ASP B 1110 ? 0.7390 0.7390 0.7390 0.0000  0.0000  0.0000  1107 ASP A N   
8925  C CA  . ASP B 1110 ? 0.7390 0.7390 0.7390 0.0000  0.0000  0.0000  1107 ASP A CA  
8926  C C   . ASP B 1110 ? 0.7390 0.7390 0.7390 0.0000  0.0000  0.0000  1107 ASP A C   
8927  O O   . ASP B 1110 ? 0.7390 0.7390 0.7390 0.0000  0.0000  0.0000  1107 ASP A O   
8928  C CB  . ASP B 1110 ? 0.7390 0.7390 0.7390 0.0000  0.0000  0.0000  1107 ASP A CB  
8929  C CG  . ASP B 1110 ? 0.7390 0.7390 0.7390 0.0000  0.0000  0.0000  1107 ASP A CG  
8930  O OD1 . ASP B 1110 ? 0.7390 0.7390 0.7390 0.0000  0.0000  0.0000  1107 ASP A OD1 
8931  O OD2 . ASP B 1110 ? 0.7390 0.7390 0.7390 0.0000  0.0000  0.0000  1107 ASP A OD2 
8932  N N   . VAL B 1111 ? 0.7470 0.7470 0.7470 0.0000  0.0000  0.0000  1108 VAL A N   
8933  C CA  . VAL B 1111 ? 0.7470 0.7470 0.7470 0.0000  0.0000  0.0000  1108 VAL A CA  
8934  C C   . VAL B 1111 ? 0.7470 0.7470 0.7470 0.0000  0.0000  0.0000  1108 VAL A C   
8935  O O   . VAL B 1111 ? 0.7470 0.7470 0.7470 0.0000  0.0000  0.0000  1108 VAL A O   
8936  C CB  . VAL B 1111 ? 0.7470 0.7470 0.7470 0.0000  0.0000  0.0000  1108 VAL A CB  
8937  C CG1 . VAL B 1111 ? 0.7470 0.7470 0.7470 0.0000  0.0000  0.0000  1108 VAL A CG1 
8938  C CG2 . VAL B 1111 ? 0.7470 0.7470 0.7470 0.0000  0.0000  0.0000  1108 VAL A CG2 
8939  N N   . LYS B 1112 ? 0.7826 0.7826 0.7826 0.0000  0.0000  0.0000  1109 LYS A N   
8940  C CA  . LYS B 1112 ? 0.7826 0.7826 0.7826 0.0000  0.0000  0.0000  1109 LYS A CA  
8941  C C   . LYS B 1112 ? 0.7826 0.7826 0.7826 0.0000  0.0000  0.0000  1109 LYS A C   
8942  O O   . LYS B 1112 ? 0.7826 0.7826 0.7826 0.0000  0.0000  0.0000  1109 LYS A O   
8948  N N   . THR B 1113 ? 0.7263 0.7263 0.7263 0.0000  0.0000  0.0000  1110 THR A N   
8949  C CA  . THR B 1113 ? 0.7263 0.7263 0.7263 0.0000  0.0000  0.0000  1110 THR A CA  
8950  C C   . THR B 1113 ? 0.7263 0.7263 0.7263 0.0000  0.0000  0.0000  1110 THR A C   
8951  O O   . THR B 1113 ? 0.7263 0.7263 0.7263 0.0000  0.0000  0.0000  1110 THR A O   
8952  C CB  . THR B 1113 ? 0.7263 0.7263 0.7263 0.0000  0.0000  0.0000  1110 THR A CB  
8953  O OG1 . THR B 1113 ? 0.7263 0.7263 0.7263 0.0000  0.0000  0.0000  1110 THR A OG1 
8954  C CG2 . THR B 1113 ? 0.7263 0.7263 0.7263 0.0000  0.0000  0.0000  1110 THR A CG2 
8955  N N   . GLY B 1114 ? 0.6359 0.6359 0.6359 0.0000  0.0000  0.0000  1111 GLY A N   
8956  C CA  . GLY B 1114 ? 0.6359 0.6359 0.6359 0.0000  0.0000  0.0000  1111 GLY A CA  
8957  C C   . GLY B 1114 ? 0.6359 0.6359 0.6359 0.0000  0.0000  0.0000  1111 GLY A C   
8958  O O   . GLY B 1114 ? 0.6359 0.6359 0.6359 0.0000  0.0000  0.0000  1111 GLY A O   
8959  N N   . ASP B 1115 ? 0.6190 0.6190 0.6190 0.0000  0.0000  0.0000  1112 ASP A N   
8960  C CA  . ASP B 1115 ? 0.6190 0.6190 0.6190 0.0000  0.0000  0.0000  1112 ASP A CA  
8961  C C   . ASP B 1115 ? 0.6190 0.6190 0.6190 0.0000  0.0000  0.0000  1112 ASP A C   
8962  O O   . ASP B 1115 ? 0.6190 0.6190 0.6190 0.0000  0.0000  0.0000  1112 ASP A O   
8963  C CB  . ASP B 1115 ? 0.6190 0.6190 0.6190 0.0000  0.0000  0.0000  1112 ASP A CB  
8964  C CG  . ASP B 1115 ? 0.6190 0.6190 0.6190 0.0000  0.0000  0.0000  1112 ASP A CG  
8965  O OD1 . ASP B 1115 ? 0.6190 0.6190 0.6190 0.0000  0.0000  0.0000  1112 ASP A OD1 
8966  O OD2 . ASP B 1115 ? 0.6190 0.6190 0.6190 0.0000  0.0000  0.0000  1112 ASP A OD2 
8967  N N   . PHE B 1116 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1113 PHE A N   
8968  C CA  . PHE B 1116 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1113 PHE A CA  
8969  C C   . PHE B 1116 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1113 PHE A C   
8970  O O   . PHE B 1116 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1113 PHE A O   
8971  C CB  . PHE B 1116 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1113 PHE A CB  
8972  C CG  . PHE B 1116 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1113 PHE A CG  
8973  C CD1 . PHE B 1116 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1113 PHE A CD1 
8974  C CD2 . PHE B 1116 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1113 PHE A CD2 
8975  C CE1 . PHE B 1116 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1113 PHE A CE1 
8976  C CE2 . PHE B 1116 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1113 PHE A CE2 
8977  C CZ  . PHE B 1116 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1113 PHE A CZ  
8978  N N   . ILE B 1117 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1114 ILE A N   
8979  C CA  . ILE B 1117 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1114 ILE A CA  
8980  C C   . ILE B 1117 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1114 ILE A C   
8981  O O   . ILE B 1117 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1114 ILE A O   
8982  C CB  . ILE B 1117 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1114 ILE A CB  
8983  C CG1 . ILE B 1117 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1114 ILE A CG1 
8984  C CG2 . ILE B 1117 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1114 ILE A CG2 
8985  C CD1 . ILE B 1117 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1114 ILE A CD1 
8986  N N   . LEU B 1118 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1115 LEU A N   
8987  C CA  . LEU B 1118 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1115 LEU A CA  
8988  C C   . LEU B 1118 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1115 LEU A C   
8989  O O   . LEU B 1118 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1115 LEU A O   
8990  C CB  . LEU B 1118 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1115 LEU A CB  
8991  C CG  . LEU B 1118 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1115 LEU A CG  
8992  C CD1 . LEU B 1118 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1115 LEU A CD1 
8993  C CD2 . LEU B 1118 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1115 LEU A CD2 
8994  N N   . HIS B 1119 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1116 HIS A N   
8995  C CA  . HIS B 1119 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1116 HIS A CA  
8996  C C   . HIS B 1119 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1116 HIS A C   
8997  O O   . HIS B 1119 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1116 HIS A O   
8998  C CB  . HIS B 1119 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1116 HIS A CB  
8999  C CG  . HIS B 1119 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1116 HIS A CG  
9000  N ND1 . HIS B 1119 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1116 HIS A ND1 
9001  C CD2 . HIS B 1119 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1116 HIS A CD2 
9002  C CE1 . HIS B 1119 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1116 HIS A CE1 
9003  N NE2 . HIS B 1119 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1116 HIS A NE2 
9004  N N   . PHE B 1120 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1117 PHE A N   
9005  C CA  . PHE B 1120 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1117 PHE A CA  
9006  C C   . PHE B 1120 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1117 PHE A C   
9007  O O   . PHE B 1120 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1117 PHE A O   
9008  C CB  . PHE B 1120 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1117 PHE A CB  
9009  C CG  . PHE B 1120 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1117 PHE A CG  
9010  C CD1 . PHE B 1120 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1117 PHE A CD1 
9011  C CD2 . PHE B 1120 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1117 PHE A CD2 
9012  C CE1 . PHE B 1120 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1117 PHE A CE1 
9013  C CE2 . PHE B 1120 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1117 PHE A CE2 
9014  C CZ  . PHE B 1120 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1117 PHE A CZ  
9015  N N   . LYS B 1121 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1118 LYS A N   
9016  C CA  . LYS B 1121 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1118 LYS A CA  
9017  C C   . LYS B 1121 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1118 LYS A C   
9018  O O   . LYS B 1121 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1118 LYS A O   
9019  C CB  . LYS B 1121 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1118 LYS A CB  
9020  C CG  . LYS B 1121 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1118 LYS A CG  
9021  C CD  . LYS B 1121 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1118 LYS A CD  
9022  C CE  . LYS B 1121 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1118 LYS A CE  
9023  N NZ  . LYS B 1121 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1118 LYS A NZ  
9024  N N   . MET B 1122 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1119 MET A N   
9025  C CA  . MET B 1122 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1119 MET A CA  
9026  C C   . MET B 1122 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1119 MET A C   
9027  O O   . MET B 1122 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1119 MET A O   
9028  C CB  . MET B 1122 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1119 MET A CB  
9029  C CG  . MET B 1122 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1119 MET A CG  
9030  S SD  . MET B 1122 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1119 MET A SD  
9031  C CE  . MET B 1122 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1119 MET A CE  
9032  N N   . ASN B 1123 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1120 ASN A N   
9033  C CA  . ASN B 1123 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1120 ASN A CA  
9034  C C   . ASN B 1123 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1120 ASN A C   
9035  O O   . ASN B 1123 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1120 ASN A O   
9036  C CB  . ASN B 1123 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1120 ASN A CB  
9037  C CG  . ASN B 1123 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1120 ASN A CG  
9038  O OD1 . ASN B 1123 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1120 ASN A OD1 
9039  N ND2 . ASN B 1123 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1120 ASN A ND2 
9040  N N   . ARG B 1124 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1121 ARG A N   
9041  C CA  . ARG B 1124 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1121 ARG A CA  
9042  C C   . ARG B 1124 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1121 ARG A C   
9043  O O   . ARG B 1124 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1121 ARG A O   
9044  C CB  . ARG B 1124 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1121 ARG A CB  
9045  C CG  . ARG B 1124 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1121 ARG A CG  
9046  C CD  . ARG B 1124 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1121 ARG A CD  
9047  N NE  . ARG B 1124 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1121 ARG A NE  
9048  C CZ  . ARG B 1124 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1121 ARG A CZ  
9049  N NH1 . ARG B 1124 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1121 ARG A NH1 
9050  N NH2 . ARG B 1124 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1121 ARG A NH2 
9051  N N   . ASN B 1125 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1122 ASN A N   
9052  C CA  . ASN B 1125 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1122 ASN A CA  
9053  C C   . ASN B 1125 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1122 ASN A C   
9054  O O   . ASN B 1125 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1122 ASN A O   
9055  C CB  . ASN B 1125 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1122 ASN A CB  
9056  C CG  . ASN B 1125 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1122 ASN A CG  
9057  O OD1 . ASN B 1125 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1122 ASN A OD1 
9058  N ND2 . ASN B 1125 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1122 ASN A ND2 
9059  N N   . LEU B 1126 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1123 LEU A N   
9060  C CA  . LEU B 1126 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1123 LEU A CA  
9061  C C   . LEU B 1126 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1123 LEU A C   
9062  O O   . LEU B 1126 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1123 LEU A O   
9063  C CB  . LEU B 1126 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1123 LEU A CB  
9064  C CG  . LEU B 1126 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1123 LEU A CG  
9065  C CD1 . LEU B 1126 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1123 LEU A CD1 
9066  C CD2 . LEU B 1126 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1123 LEU A CD2 
9067  N N   . SER B 1127 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1124 SER A N   
9068  C CA  . SER B 1127 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1124 SER A CA  
9069  C C   . SER B 1127 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1124 SER A C   
9070  O O   . SER B 1127 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1124 SER A O   
9071  C CB  . SER B 1127 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1124 SER A CB  
9072  O OG  . SER B 1127 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1124 SER A OG  
9073  N N   . PHE B 1128 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1125 PHE A N   
9074  C CA  . PHE B 1128 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1125 PHE A CA  
9075  C C   . PHE B 1128 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1125 PHE A C   
9076  O O   . PHE B 1128 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1125 PHE A O   
9077  C CB  . PHE B 1128 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1125 PHE A CB  
9078  C CG  . PHE B 1128 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1125 PHE A CG  
9079  C CD1 . PHE B 1128 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1125 PHE A CD1 
9080  C CD2 . PHE B 1128 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1125 PHE A CD2 
9081  C CE1 . PHE B 1128 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1125 PHE A CE1 
9082  C CE2 . PHE B 1128 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1125 PHE A CE2 
9083  C CZ  . PHE B 1128 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1125 PHE A CZ  
9084  N N   . GLN B 1129 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1126 GLN A N   
9085  C CA  . GLN B 1129 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1126 GLN A CA  
9086  C C   . GLN B 1129 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1126 GLN A C   
9087  O O   . GLN B 1129 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1126 GLN A O   
9088  C CB  . GLN B 1129 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1126 GLN A CB  
9089  C CG  . GLN B 1129 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1126 GLN A CG  
9090  C CD  . GLN B 1129 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1126 GLN A CD  
9091  O OE1 . GLN B 1129 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1126 GLN A OE1 
9092  N NE2 . GLN B 1129 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1126 GLN A NE2 
9093  N N   . ARG B 1130 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1127 ARG A N   
9094  C CA  . ARG B 1130 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1127 ARG A CA  
9095  C C   . ARG B 1130 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1127 ARG A C   
9096  O O   . ARG B 1130 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1127 ARG A O   
9097  C CB  . ARG B 1130 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1127 ARG A CB  
9098  C CG  . ARG B 1130 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1127 ARG A CG  
9099  C CD  . ARG B 1130 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1127 ARG A CD  
9100  N NE  . ARG B 1130 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1127 ARG A NE  
9101  C CZ  . ARG B 1130 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1127 ARG A CZ  
9102  N NH1 . ARG B 1130 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1127 ARG A NH1 
9103  N NH2 . ARG B 1130 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1127 ARG A NH2 
9104  N N   . GLY B 1131 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1128 GLY A N   
9105  C CA  . GLY B 1131 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1128 GLY A CA  
9106  C C   . GLY B 1131 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1128 GLY A C   
9107  O O   . GLY B 1131 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1128 GLY A O   
9108  N N   . LEU B 1132 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1129 LEU A N   
9109  C CA  . LEU B 1132 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1129 LEU A CA  
9110  C C   . LEU B 1132 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1129 LEU A C   
9111  O O   . LEU B 1132 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1129 LEU A O   
9112  C CB  . LEU B 1132 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1129 LEU A CB  
9113  C CG  . LEU B 1132 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1129 LEU A CG  
9114  C CD1 . LEU B 1132 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1129 LEU A CD1 
9115  C CD2 . LEU B 1132 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1129 LEU A CD2 
9116  N N   . PRO B 1133 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1130 PRO A N   
9117  C CA  . PRO B 1133 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1130 PRO A CA  
9118  C C   . PRO B 1133 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1130 PRO A C   
9119  O O   . PRO B 1133 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1130 PRO A O   
9120  C CB  . PRO B 1133 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1130 PRO A CB  
9121  C CG  . PRO B 1133 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1130 PRO A CG  
9122  C CD  . PRO B 1133 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1130 PRO A CD  
9123  N N   . GLY B 1134 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1131 GLY A N   
9124  C CA  . GLY B 1134 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1131 GLY A CA  
9125  C C   . GLY B 1134 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1131 GLY A C   
9126  O O   . GLY B 1134 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1131 GLY A O   
9127  N N   . PHE B 1135 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1132 PHE A N   
9128  C CA  . PHE B 1135 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1132 PHE A CA  
9129  C C   . PHE B 1135 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1132 PHE A C   
9130  O O   . PHE B 1135 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1132 PHE A O   
9131  C CB  . PHE B 1135 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1132 PHE A CB  
9132  C CG  . PHE B 1135 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1132 PHE A CG  
9133  C CD1 . PHE B 1135 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1132 PHE A CD1 
9134  C CD2 . PHE B 1135 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1132 PHE A CD2 
9135  C CE1 . PHE B 1135 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1132 PHE A CE1 
9136  C CE2 . PHE B 1135 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1132 PHE A CE2 
9137  C CZ  . PHE B 1135 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1132 PHE A CZ  
9138  N N   . MET B 1136 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1133 MET A N   
9139  C CA  . MET B 1136 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1133 MET A CA  
9140  C C   . MET B 1136 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1133 MET A C   
9141  O O   . MET B 1136 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1133 MET A O   
9142  C CB  . MET B 1136 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1133 MET A CB  
9143  C CG  . MET B 1136 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1133 MET A CG  
9144  S SD  . MET B 1136 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1133 MET A SD  
9145  C CE  . MET B 1136 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1133 MET A CE  
9146  N N   . PRO B 1137 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1134 PRO A N   
9147  C CA  . PRO B 1137 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1134 PRO A CA  
9148  C C   . PRO B 1137 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1134 PRO A C   
9149  O O   . PRO B 1137 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1134 PRO A O   
9150  C CB  . PRO B 1137 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1134 PRO A CB  
9151  C CG  . PRO B 1137 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1134 PRO A CG  
9152  C CD  . PRO B 1137 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1134 PRO A CD  
9153  N N   . ALA B 1138 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1135 ALA A N   
9154  C CA  . ALA B 1138 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1135 ALA A CA  
9155  C C   . ALA B 1138 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1135 ALA A C   
9156  O O   . ALA B 1138 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1135 ALA A O   
9157  C CB  . ALA B 1138 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1135 ALA A CB  
9158  N N   . TRP B 1139 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1136 TRP A N   
9159  C CA  . TRP B 1139 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1136 TRP A CA  
9160  C C   . TRP B 1139 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1136 TRP A C   
9161  O O   . TRP B 1139 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1136 TRP A O   
9162  C CB  . TRP B 1139 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1136 TRP A CB  
9163  C CG  . TRP B 1139 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1136 TRP A CG  
9164  C CD1 . TRP B 1139 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1136 TRP A CD1 
9165  C CD2 . TRP B 1139 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1136 TRP A CD2 
9166  N NE1 . TRP B 1139 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1136 TRP A NE1 
9167  C CE2 . TRP B 1139 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1136 TRP A CE2 
9168  C CE3 . TRP B 1139 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1136 TRP A CE3 
9169  C CZ2 . TRP B 1139 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1136 TRP A CZ2 
9170  C CZ3 . TRP B 1139 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1136 TRP A CZ3 
9171  C CH2 . TRP B 1139 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1136 TRP A CH2 
9172  N N   . ASP B 1140 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1137 ASP A N   
9173  C CA  . ASP B 1140 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1137 ASP A CA  
9174  C C   . ASP B 1140 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1137 ASP A C   
9175  O O   . ASP B 1140 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1137 ASP A O   
9176  C CB  . ASP B 1140 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1137 ASP A CB  
9177  C CG  . ASP B 1140 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1137 ASP A CG  
9178  O OD1 . ASP B 1140 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1137 ASP A OD1 
9179  O OD2 . ASP B 1140 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1137 ASP A OD2 
9180  N N   . ILE B 1141 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1138 ILE A N   
9181  C CA  . ILE B 1141 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1138 ILE A CA  
9182  C C   . ILE B 1141 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1138 ILE A C   
9183  O O   . ILE B 1141 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1138 ILE A O   
9184  C CB  . ILE B 1141 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1138 ILE A CB  
9185  C CG1 . ILE B 1141 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1138 ILE A CG1 
9186  C CG2 . ILE B 1141 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1138 ILE A CG2 
9187  C CD1 . ILE B 1141 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1138 ILE A CD1 
9188  N N   . VAL B 1142 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1139 VAL A N   
9189  C CA  . VAL B 1142 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1139 VAL A CA  
9190  C C   . VAL B 1142 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1139 VAL A C   
9191  O O   . VAL B 1142 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1139 VAL A O   
9192  C CB  . VAL B 1142 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1139 VAL A CB  
9193  C CG1 . VAL B 1142 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1139 VAL A CG1 
9194  C CG2 . VAL B 1142 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1139 VAL A CG2 
9195  N N   . PHE B 1143 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1140 PHE A N   
9196  C CA  . PHE B 1143 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1140 PHE A CA  
9197  C C   . PHE B 1143 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1140 PHE A C   
9198  O O   . PHE B 1143 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1140 PHE A O   
9199  C CB  . PHE B 1143 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1140 PHE A CB  
9200  C CG  . PHE B 1143 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1140 PHE A CG  
9201  C CD1 . PHE B 1143 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1140 PHE A CD1 
9202  C CD2 . PHE B 1143 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1140 PHE A CD2 
9203  C CE1 . PHE B 1143 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1140 PHE A CE1 
9204  C CE2 . PHE B 1143 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1140 PHE A CE2 
9205  C CZ  . PHE B 1143 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1140 PHE A CZ  
9206  N N   . GLU B 1144 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1141 GLU A N   
9207  C CA  . GLU B 1144 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1141 GLU A CA  
9208  C C   . GLU B 1144 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1141 GLU A C   
9209  O O   . GLU B 1144 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1141 GLU A O   
9210  C CB  . GLU B 1144 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1141 GLU A CB  
9211  C CG  . GLU B 1144 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1141 GLU A CG  
9212  C CD  . GLU B 1144 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1141 GLU A CD  
9213  O OE1 . GLU B 1144 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1141 GLU A OE1 
9214  O OE2 . GLU B 1144 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1141 GLU A OE2 
9215  N N   . LYS B 1145 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1142 LYS A N   
9216  C CA  . LYS B 1145 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1142 LYS A CA  
9217  C C   . LYS B 1145 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1142 LYS A C   
9218  O O   . LYS B 1145 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1142 LYS A O   
9219  C CB  . LYS B 1145 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1142 LYS A CB  
9220  C CG  . LYS B 1145 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1142 LYS A CG  
9221  C CD  . LYS B 1145 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1142 LYS A CD  
9222  C CE  . LYS B 1145 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1142 LYS A CE  
9223  N NZ  . LYS B 1145 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1142 LYS A NZ  
9224  N N   . ASN B 1146 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1143 ASN A N   
9225  C CA  . ASN B 1146 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1143 ASN A CA  
9226  C C   . ASN B 1146 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1143 ASN A C   
9227  O O   . ASN B 1146 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1143 ASN A O   
9228  C CB  . ASN B 1146 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1143 ASN A CB  
9229  C CG  . ASN B 1146 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1143 ASN A CG  
9230  O OD1 . ASN B 1146 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1143 ASN A OD1 
9231  N ND2 . ASN B 1146 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1143 ASN A ND2 
9232  N N   . GLU B 1147 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1144 GLU A N   
9233  C CA  . GLU B 1147 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1144 GLU A CA  
9234  C C   . GLU B 1147 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1144 GLU A C   
9235  O O   . GLU B 1147 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1144 GLU A O   
9236  C CB  . GLU B 1147 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1144 GLU A CB  
9237  C CG  . GLU B 1147 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1144 GLU A CG  
9238  C CD  . GLU B 1147 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1144 GLU A CD  
9239  O OE1 . GLU B 1147 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1144 GLU A OE1 
9240  O OE2 . GLU B 1147 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1144 GLU A OE2 
9241  N N   . THR B 1148 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1145 THR A N   
9242  C CA  . THR B 1148 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1145 THR A CA  
9243  C C   . THR B 1148 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1145 THR A C   
9244  O O   . THR B 1148 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1145 THR A O   
9245  C CB  . THR B 1148 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1145 THR A CB  
9246  O OG1 . THR B 1148 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1145 THR A OG1 
9247  C CG2 . THR B 1148 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1145 THR A CG2 
9248  N N   . GLN B 1149 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1146 GLN A N   
9249  C CA  . GLN B 1149 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1146 GLN A CA  
9250  C C   . GLN B 1149 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1146 GLN A C   
9251  O O   . GLN B 1149 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1146 GLN A O   
9252  C CB  . GLN B 1149 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1146 GLN A CB  
9253  C CG  . GLN B 1149 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1146 GLN A CG  
9254  C CD  . GLN B 1149 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1146 GLN A CD  
9255  O OE1 . GLN B 1149 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1146 GLN A OE1 
9256  N NE2 . GLN B 1149 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1146 GLN A NE2 
9257  N N   . PHE B 1150 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1147 PHE A N   
9258  C CA  . PHE B 1150 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1147 PHE A CA  
9259  C C   . PHE B 1150 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1147 PHE A C   
9260  O O   . PHE B 1150 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1147 PHE A O   
9261  C CB  . PHE B 1150 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1147 PHE A CB  
9262  C CG  . PHE B 1150 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1147 PHE A CG  
9263  C CD1 . PHE B 1150 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1147 PHE A CD1 
9264  C CD2 . PHE B 1150 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1147 PHE A CD2 
9265  C CE1 . PHE B 1150 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1147 PHE A CE1 
9266  C CE2 . PHE B 1150 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1147 PHE A CE2 
9267  C CZ  . PHE B 1150 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1147 PHE A CZ  
9268  N N   . ASP B 1151 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1148 ASP A N   
9269  C CA  . ASP B 1151 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1148 ASP A CA  
9270  C C   . ASP B 1151 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1148 ASP A C   
9271  O O   . ASP B 1151 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1148 ASP A O   
9272  C CB  . ASP B 1151 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1148 ASP A CB  
9273  C CG  . ASP B 1151 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1148 ASP A CG  
9274  O OD1 . ASP B 1151 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1148 ASP A OD1 
9275  O OD2 . ASP B 1151 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1148 ASP A OD2 
9276  N N   . ALA B 1152 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1149 ALA A N   
9277  C CA  . ALA B 1152 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1149 ALA A CA  
9278  C C   . ALA B 1152 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1149 ALA A C   
9279  O O   . ALA B 1152 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1149 ALA A O   
9280  C CB  . ALA B 1152 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1149 ALA A CB  
9281  N N   . LYS B 1153 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1150 LYS A N   
9282  C CA  . LYS B 1153 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1150 LYS A CA  
9283  C C   . LYS B 1153 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1150 LYS A C   
9284  O O   . LYS B 1153 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1150 LYS A O   
9290  N N   . GLY B 1154 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1151 GLY A N   
9291  C CA  . GLY B 1154 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1151 GLY A CA  
9292  C C   . GLY B 1154 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1151 GLY A C   
9293  O O   . GLY B 1154 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1151 GLY A O   
9294  N N   . THR B 1155 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1152 THR A N   
9295  C CA  . THR B 1155 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1152 THR A CA  
9296  C C   . THR B 1155 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1152 THR A C   
9297  O O   . THR B 1155 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1152 THR A O   
9298  C CB  . THR B 1155 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1152 THR A CB  
9299  O OG1 . THR B 1155 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1152 THR A OG1 
9300  C CG2 . THR B 1155 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1152 THR A CG2 
9301  N N   . PRO B 1156 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1153 PRO A N   
9302  C CA  . PRO B 1156 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1153 PRO A CA  
9303  C C   . PRO B 1156 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1153 PRO A C   
9304  O O   . PRO B 1156 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1153 PRO A O   
9305  C CB  . PRO B 1156 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1153 PRO A CB  
9306  C CG  . PRO B 1156 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1153 PRO A CG  
9307  C CD  . PRO B 1156 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1153 PRO A CD  
9308  N N   . PHE B 1157 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1154 PHE A N   
9309  C CA  . PHE B 1157 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1154 PHE A CA  
9310  C C   . PHE B 1157 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1154 PHE A C   
9311  O O   . PHE B 1157 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1154 PHE A O   
9312  C CB  . PHE B 1157 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1154 PHE A CB  
9313  C CG  . PHE B 1157 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1154 PHE A CG  
9314  C CD1 . PHE B 1157 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1154 PHE A CD1 
9315  C CD2 . PHE B 1157 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1154 PHE A CD2 
9316  C CE1 . PHE B 1157 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1154 PHE A CE1 
9317  C CE2 . PHE B 1157 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1154 PHE A CE2 
9318  C CZ  . PHE B 1157 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1154 PHE A CZ  
9319  N N   . ILE B 1158 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1155 ILE A N   
9320  C CA  . ILE B 1158 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1155 ILE A CA  
9321  C C   . ILE B 1158 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1155 ILE A C   
9322  O O   . ILE B 1158 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1155 ILE A O   
9323  C CB  . ILE B 1158 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1155 ILE A CB  
9324  C CG1 . ILE B 1158 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1155 ILE A CG1 
9325  C CG2 . ILE B 1158 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1155 ILE A CG2 
9326  C CD1 . ILE B 1158 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1155 ILE A CD1 
9327  N N   . ALA B 1159 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1156 ALA A N   
9328  C CA  . ALA B 1159 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1156 ALA A CA  
9329  C C   . ALA B 1159 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1156 ALA A C   
9330  O O   . ALA B 1159 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1156 ALA A O   
9331  C CB  . ALA B 1159 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1156 ALA A CB  
9332  N N   . GLY B 1160 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1157 GLY A N   
9333  C CA  . GLY B 1160 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1157 GLY A CA  
9334  C C   . GLY B 1160 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1157 GLY A C   
9335  O O   . GLY B 1160 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1157 GLY A O   
9336  N N   . LYS B 1161 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1158 LYS A N   
9337  C CA  . LYS B 1161 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1158 LYS A CA  
9338  C C   . LYS B 1161 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1158 LYS A C   
9339  O O   . LYS B 1161 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1158 LYS A O   
9340  C CB  . LYS B 1161 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1158 LYS A CB  
9341  C CG  . LYS B 1161 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1158 LYS A CG  
9342  C CD  . LYS B 1161 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1158 LYS A CD  
9343  C CE  . LYS B 1161 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1158 LYS A CE  
9344  N NZ  . LYS B 1161 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1158 LYS A NZ  
9345  N N   . ARG B 1162 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1159 ARG A N   
9346  C CA  . ARG B 1162 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1159 ARG A CA  
9347  C C   . ARG B 1162 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1159 ARG A C   
9348  O O   . ARG B 1162 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1159 ARG A O   
9349  C CB  . ARG B 1162 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1159 ARG A CB  
9350  C CG  . ARG B 1162 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1159 ARG A CG  
9351  C CD  . ARG B 1162 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1159 ARG A CD  
9352  N NE  . ARG B 1162 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1159 ARG A NE  
9353  C CZ  . ARG B 1162 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1159 ARG A CZ  
9354  N NH1 . ARG B 1162 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1159 ARG A NH1 
9355  N NH2 . ARG B 1162 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1159 ARG A NH2 
9356  N N   . ILE B 1163 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1160 ILE A N   
9357  C CA  . ILE B 1163 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1160 ILE A CA  
9358  C C   . ILE B 1163 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1160 ILE A C   
9359  O O   . ILE B 1163 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1160 ILE A O   
9360  C CB  . ILE B 1163 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1160 ILE A CB  
9361  C CG1 . ILE B 1163 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1160 ILE A CG1 
9362  C CG2 . ILE B 1163 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1160 ILE A CG2 
9363  C CD1 . ILE B 1163 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1160 ILE A CD1 
9364  N N   . VAL B 1164 ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  1161 VAL A N   
9365  C CA  . VAL B 1164 ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  1161 VAL A CA  
9366  C C   . VAL B 1164 ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  1161 VAL A C   
9367  O O   . VAL B 1164 ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  1161 VAL A O   
9368  C CB  . VAL B 1164 ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  1161 VAL A CB  
9369  C CG1 . VAL B 1164 ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  1161 VAL A CG1 
9370  C CG2 . VAL B 1164 ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  1161 VAL A CG2 
9371  N N   . PRO B 1165 ? 1.0205 1.0205 1.0205 0.0000  0.0000  0.0000  1162 PRO A N   
9372  C CA  . PRO B 1165 ? 1.0205 1.0205 1.0205 0.0000  0.0000  0.0000  1162 PRO A CA  
9373  C C   . PRO B 1165 ? 1.0205 1.0205 1.0205 0.0000  0.0000  0.0000  1162 PRO A C   
9374  O O   . PRO B 1165 ? 1.0205 1.0205 1.0205 0.0000  0.0000  0.0000  1162 PRO A O   
9375  C CB  . PRO B 1165 ? 1.0205 1.0205 1.0205 0.0000  0.0000  0.0000  1162 PRO A CB  
9376  C CG  . PRO B 1165 ? 1.0205 1.0205 1.0205 0.0000  0.0000  0.0000  1162 PRO A CG  
9377  C CD  . PRO B 1165 ? 1.0205 1.0205 1.0205 0.0000  0.0000  0.0000  1162 PRO A CD  
9464  N N   . TYR B 1176 ? 0.8987 0.8987 0.8987 0.0000  0.0000  0.0000  1173 TYR A N   
9465  C CA  . TYR B 1176 ? 0.8987 0.8987 0.8987 0.0000  0.0000  0.0000  1173 TYR A CA  
9466  C C   . TYR B 1176 ? 0.8987 0.8987 0.8987 0.0000  0.0000  0.0000  1173 TYR A C   
9467  O O   . TYR B 1176 ? 0.8987 0.8987 0.8987 0.0000  0.0000  0.0000  1173 TYR A O   
9468  C CB  . TYR B 1176 ? 0.8987 0.8987 0.8987 0.0000  0.0000  0.0000  1173 TYR A CB  
9469  C CG  . TYR B 1176 ? 0.8987 0.8987 0.8987 0.0000  0.0000  0.0000  1173 TYR A CG  
9470  C CD1 . TYR B 1176 ? 0.8987 0.8987 0.8987 0.0000  0.0000  0.0000  1173 TYR A CD1 
9471  C CD2 . TYR B 1176 ? 0.8987 0.8987 0.8987 0.0000  0.0000  0.0000  1173 TYR A CD2 
9472  C CE1 . TYR B 1176 ? 0.8987 0.8987 0.8987 0.0000  0.0000  0.0000  1173 TYR A CE1 
9473  C CE2 . TYR B 1176 ? 0.8987 0.8987 0.8987 0.0000  0.0000  0.0000  1173 TYR A CE2 
9474  C CZ  . TYR B 1176 ? 0.8987 0.8987 0.8987 0.0000  0.0000  0.0000  1173 TYR A CZ  
9475  O OH  . TYR B 1176 ? 0.8987 0.8987 0.8987 0.0000  0.0000  0.0000  1173 TYR A OH  
9476  N N   . ARG B 1177 ? 0.7336 0.7336 0.7336 0.0000  0.0000  0.0000  1174 ARG A N   
9477  C CA  . ARG B 1177 ? 0.7336 0.7336 0.7336 0.0000  0.0000  0.0000  1174 ARG A CA  
9478  C C   . ARG B 1177 ? 0.7336 0.7336 0.7336 0.0000  0.0000  0.0000  1174 ARG A C   
9479  O O   . ARG B 1177 ? 0.7336 0.7336 0.7336 0.0000  0.0000  0.0000  1174 ARG A O   
9480  C CB  . ARG B 1177 ? 0.7336 0.7336 0.7336 0.0000  0.0000  0.0000  1174 ARG A CB  
9481  C CG  . ARG B 1177 ? 0.7336 0.7336 0.7336 0.0000  0.0000  0.0000  1174 ARG A CG  
9482  C CD  . ARG B 1177 ? 0.7336 0.7336 0.7336 0.0000  0.0000  0.0000  1174 ARG A CD  
9483  N NE  . ARG B 1177 ? 0.7336 0.7336 0.7336 0.0000  0.0000  0.0000  1174 ARG A NE  
9484  C CZ  . ARG B 1177 ? 0.7336 0.7336 0.7336 0.0000  0.0000  0.0000  1174 ARG A CZ  
9485  N NH1 . ARG B 1177 ? 0.7336 0.7336 0.7336 0.0000  0.0000  0.0000  1174 ARG A NH1 
9486  N NH2 . ARG B 1177 ? 0.7336 0.7336 0.7336 0.0000  0.0000  0.0000  1174 ARG A NH2 
9487  N N   . ASP B 1178 ? 0.6269 0.6269 0.6269 0.0000  0.0000  0.0000  1175 ASP A N   
9488  C CA  . ASP B 1178 ? 0.6269 0.6269 0.6269 0.0000  0.0000  0.0000  1175 ASP A CA  
9489  C C   . ASP B 1178 ? 0.6269 0.6269 0.6269 0.0000  0.0000  0.0000  1175 ASP A C   
9490  O O   . ASP B 1178 ? 0.6269 0.6269 0.6269 0.0000  0.0000  0.0000  1175 ASP A O   
9491  C CB  . ASP B 1178 ? 0.6269 0.6269 0.6269 0.0000  0.0000  0.0000  1175 ASP A CB  
9492  C CG  . ASP B 1178 ? 0.6269 0.6269 0.6269 0.0000  0.0000  0.0000  1175 ASP A CG  
9493  O OD1 . ASP B 1178 ? 0.6269 0.6269 0.6269 0.0000  0.0000  0.0000  1175 ASP A OD1 
9494  O OD2 . ASP B 1178 ? 0.6269 0.6269 0.6269 0.0000  0.0000  0.0000  1175 ASP A OD2 
9495  N N   . LEU B 1179 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1176 LEU A N   
9496  C CA  . LEU B 1179 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1176 LEU A CA  
9497  C C   . LEU B 1179 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1176 LEU A C   
9498  O O   . LEU B 1179 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1176 LEU A O   
9499  C CB  . LEU B 1179 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1176 LEU A CB  
9500  C CG  . LEU B 1179 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1176 LEU A CG  
9501  C CD1 . LEU B 1179 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1176 LEU A CD1 
9502  C CD2 . LEU B 1179 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1176 LEU A CD2 
9503  N N   . TYR B 1180 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1177 TYR A N   
9504  C CA  . TYR B 1180 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1177 TYR A CA  
9505  C C   . TYR B 1180 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1177 TYR A C   
9506  O O   . TYR B 1180 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1177 TYR A O   
9507  C CB  . TYR B 1180 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1177 TYR A CB  
9508  C CG  . TYR B 1180 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1177 TYR A CG  
9509  C CD1 . TYR B 1180 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1177 TYR A CD1 
9510  C CD2 . TYR B 1180 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1177 TYR A CD2 
9511  C CE1 . TYR B 1180 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1177 TYR A CE1 
9512  C CE2 . TYR B 1180 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1177 TYR A CE2 
9513  C CZ  . TYR B 1180 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1177 TYR A CZ  
9514  O OH  . TYR B 1180 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1177 TYR A OH  
9515  N N   . PRO B 1181 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1178 PRO A N   
9516  C CA  . PRO B 1181 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1178 PRO A CA  
9517  C C   . PRO B 1181 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1178 PRO A C   
9518  O O   . PRO B 1181 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1178 PRO A O   
9519  C CB  . PRO B 1181 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1178 PRO A CB  
9520  C CG  . PRO B 1181 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1178 PRO A CG  
9521  C CD  . PRO B 1181 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1178 PRO A CD  
9522  N N   . ALA B 1182 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1179 ALA A N   
9523  C CA  . ALA B 1182 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1179 ALA A CA  
9524  C C   . ALA B 1182 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1179 ALA A C   
9525  O O   . ALA B 1182 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1179 ALA A O   
9526  C CB  . ALA B 1182 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1179 ALA A CB  
9527  N N   . ASN B 1183 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1180 ASN A N   
9528  C CA  . ASN B 1183 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1180 ASN A CA  
9529  C C   . ASN B 1183 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1180 ASN A C   
9530  O O   . ASN B 1183 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1180 ASN A O   
9531  C CB  . ASN B 1183 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1180 ASN A CB  
9532  C CG  . ASN B 1183 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1180 ASN A CG  
9533  O OD1 . ASN B 1183 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1180 ASN A OD1 
9534  N ND2 . ASN B 1183 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1180 ASN A ND2 
9535  N N   . GLU B 1184 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1181 GLU A N   
9536  C CA  . GLU B 1184 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1181 GLU A CA  
9537  C C   . GLU B 1184 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1181 GLU A C   
9538  O O   . GLU B 1184 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1181 GLU A O   
9539  C CB  . GLU B 1184 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1181 GLU A CB  
9540  C CG  . GLU B 1184 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1181 GLU A CG  
9541  C CD  . GLU B 1184 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1181 GLU A CD  
9542  O OE1 . GLU B 1184 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1181 GLU A OE1 
9543  O OE2 . GLU B 1184 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1181 GLU A OE2 
9544  N N   . LEU B 1185 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1182 LEU A N   
9545  C CA  . LEU B 1185 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1182 LEU A CA  
9546  C C   . LEU B 1185 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1182 LEU A C   
9547  O O   . LEU B 1185 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1182 LEU A O   
9548  C CB  . LEU B 1185 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1182 LEU A CB  
9549  C CG  . LEU B 1185 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1182 LEU A CG  
9550  C CD1 . LEU B 1185 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1182 LEU A CD1 
9551  C CD2 . LEU B 1185 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1182 LEU A CD2 
9552  N N   . ILE B 1186 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1183 ILE A N   
9553  C CA  . ILE B 1186 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1183 ILE A CA  
9554  C C   . ILE B 1186 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1183 ILE A C   
9555  O O   . ILE B 1186 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1183 ILE A O   
9556  C CB  . ILE B 1186 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1183 ILE A CB  
9557  C CG1 . ILE B 1186 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1183 ILE A CG1 
9558  C CG2 . ILE B 1186 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1183 ILE A CG2 
9559  C CD1 . ILE B 1186 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1183 ILE A CD1 
9560  N N   . ALA B 1187 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1184 ALA A N   
9561  C CA  . ALA B 1187 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1184 ALA A CA  
9562  C C   . ALA B 1187 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1184 ALA A C   
9563  O O   . ALA B 1187 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1184 ALA A O   
9564  C CB  . ALA B 1187 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1184 ALA A CB  
9565  N N   . LEU B 1188 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1185 LEU A N   
9566  C CA  . LEU B 1188 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1185 LEU A CA  
9567  C C   . LEU B 1188 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1185 LEU A C   
9568  O O   . LEU B 1188 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1185 LEU A O   
9569  C CB  . LEU B 1188 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1185 LEU A CB  
9570  C CG  . LEU B 1188 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1185 LEU A CG  
9571  C CD1 . LEU B 1188 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1185 LEU A CD1 
9572  C CD2 . LEU B 1188 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1185 LEU A CD2 
9573  N N   . LEU B 1189 ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  1186 LEU A N   
9574  C CA  . LEU B 1189 ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  1186 LEU A CA  
9575  C C   . LEU B 1189 ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  1186 LEU A C   
9576  O O   . LEU B 1189 ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  1186 LEU A O   
9577  C CB  . LEU B 1189 ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  1186 LEU A CB  
9578  C CG  . LEU B 1189 ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  1186 LEU A CG  
9579  C CD1 . LEU B 1189 ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  1186 LEU A CD1 
9580  C CD2 . LEU B 1189 ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  1186 LEU A CD2 
9581  N N   . GLU B 1190 ? 0.6245 0.6245 0.6245 0.0000  0.0000  0.0000  1187 GLU A N   
9582  C CA  . GLU B 1190 ? 0.6245 0.6245 0.6245 0.0000  0.0000  0.0000  1187 GLU A CA  
9583  C C   . GLU B 1190 ? 0.6245 0.6245 0.6245 0.0000  0.0000  0.0000  1187 GLU A C   
9584  O O   . GLU B 1190 ? 0.6245 0.6245 0.6245 0.0000  0.0000  0.0000  1187 GLU A O   
9585  C CB  . GLU B 1190 ? 0.6245 0.6245 0.6245 0.0000  0.0000  0.0000  1187 GLU A CB  
9586  C CG  . GLU B 1190 ? 0.6245 0.6245 0.6245 0.0000  0.0000  0.0000  1187 GLU A CG  
9587  C CD  . GLU B 1190 ? 0.6245 0.6245 0.6245 0.0000  0.0000  0.0000  1187 GLU A CD  
9588  O OE1 . GLU B 1190 ? 0.6245 0.6245 0.6245 0.0000  0.0000  0.0000  1187 GLU A OE1 
9589  O OE2 . GLU B 1190 ? 0.6245 0.6245 0.6245 0.0000  0.0000  0.0000  1187 GLU A OE2 
9590  N N   . GLU B 1191 ? 0.6568 0.6568 0.6568 0.0000  0.0000  0.0000  1188 GLU A N   
9591  C CA  . GLU B 1191 ? 0.6568 0.6568 0.6568 0.0000  0.0000  0.0000  1188 GLU A CA  
9592  C C   . GLU B 1191 ? 0.6568 0.6568 0.6568 0.0000  0.0000  0.0000  1188 GLU A C   
9593  O O   . GLU B 1191 ? 0.6568 0.6568 0.6568 0.0000  0.0000  0.0000  1188 GLU A O   
9594  C CB  . GLU B 1191 ? 0.6568 0.6568 0.6568 0.0000  0.0000  0.0000  1188 GLU A CB  
9595  C CG  . GLU B 1191 ? 0.6568 0.6568 0.6568 0.0000  0.0000  0.0000  1188 GLU A CG  
9596  C CD  . GLU B 1191 ? 0.6568 0.6568 0.6568 0.0000  0.0000  0.0000  1188 GLU A CD  
9597  O OE1 . GLU B 1191 ? 0.6568 0.6568 0.6568 0.0000  0.0000  0.0000  1188 GLU A OE1 
9598  O OE2 . GLU B 1191 ? 0.6568 0.6568 0.6568 0.0000  0.0000  0.0000  1188 GLU A OE2 
9599  N N   . LYS B 1192 ? 0.6719 0.6719 0.6719 0.0000  0.0000  0.0000  1189 LYS A N   
9600  C CA  . LYS B 1192 ? 0.6719 0.6719 0.6719 0.0000  0.0000  0.0000  1189 LYS A CA  
9601  C C   . LYS B 1192 ? 0.6719 0.6719 0.6719 0.0000  0.0000  0.0000  1189 LYS A C   
9602  O O   . LYS B 1192 ? 0.6719 0.6719 0.6719 0.0000  0.0000  0.0000  1189 LYS A O   
9603  C CB  . LYS B 1192 ? 0.6719 0.6719 0.6719 0.0000  0.0000  0.0000  1189 LYS A CB  
9604  C CG  . LYS B 1192 ? 0.6719 0.6719 0.6719 0.0000  0.0000  0.0000  1189 LYS A CG  
9605  C CD  . LYS B 1192 ? 0.6719 0.6719 0.6719 0.0000  0.0000  0.0000  1189 LYS A CD  
9606  C CE  . LYS B 1192 ? 0.6719 0.6719 0.6719 0.0000  0.0000  0.0000  1189 LYS A CE  
9607  N NZ  . LYS B 1192 ? 0.6719 0.6719 0.6719 0.0000  0.0000  0.0000  1189 LYS A NZ  
9608  N N   . GLY B 1193 ? 0.6697 0.6697 0.6697 0.0000  0.0000  0.0000  1190 GLY A N   
9609  C CA  . GLY B 1193 ? 0.6697 0.6697 0.6697 0.0000  0.0000  0.0000  1190 GLY A CA  
9610  C C   . GLY B 1193 ? 0.6697 0.6697 0.6697 0.0000  0.0000  0.0000  1190 GLY A C   
9611  O O   . GLY B 1193 ? 0.6697 0.6697 0.6697 0.0000  0.0000  0.0000  1190 GLY A O   
9612  N N   . ILE B 1194 ? 0.6750 0.6750 0.6750 0.0000  0.0000  0.0000  1191 ILE A N   
9613  C CA  . ILE B 1194 ? 0.6750 0.6750 0.6750 0.0000  0.0000  0.0000  1191 ILE A CA  
9614  C C   . ILE B 1194 ? 0.6750 0.6750 0.6750 0.0000  0.0000  0.0000  1191 ILE A C   
9615  O O   . ILE B 1194 ? 0.6750 0.6750 0.6750 0.0000  0.0000  0.0000  1191 ILE A O   
9616  C CB  . ILE B 1194 ? 0.6750 0.6750 0.6750 0.0000  0.0000  0.0000  1191 ILE A CB  
9617  C CG1 . ILE B 1194 ? 0.6750 0.6750 0.6750 0.0000  0.0000  0.0000  1191 ILE A CG1 
9618  C CG2 . ILE B 1194 ? 0.6750 0.6750 0.6750 0.0000  0.0000  0.0000  1191 ILE A CG2 
9619  C CD1 . ILE B 1194 ? 0.6750 0.6750 0.6750 0.0000  0.0000  0.0000  1191 ILE A CD1 
9620  N N   . VAL B 1195 ? 0.6709 0.6709 0.6709 0.0000  0.0000  0.0000  1192 VAL A N   
9621  C CA  . VAL B 1195 ? 0.6709 0.6709 0.6709 0.0000  0.0000  0.0000  1192 VAL A CA  
9622  C C   . VAL B 1195 ? 0.6709 0.6709 0.6709 0.0000  0.0000  0.0000  1192 VAL A C   
9623  O O   . VAL B 1195 ? 0.6709 0.6709 0.6709 0.0000  0.0000  0.0000  1192 VAL A O   
9624  C CB  . VAL B 1195 ? 0.6709 0.6709 0.6709 0.0000  0.0000  0.0000  1192 VAL A CB  
9625  C CG1 . VAL B 1195 ? 0.6709 0.6709 0.6709 0.0000  0.0000  0.0000  1192 VAL A CG1 
9626  C CG2 . VAL B 1195 ? 0.6709 0.6709 0.6709 0.0000  0.0000  0.0000  1192 VAL A CG2 
9627  N N   . PHE B 1196 ? 0.6465 0.6465 0.6465 0.0000  0.0000  0.0000  1193 PHE A N   
9628  C CA  . PHE B 1196 ? 0.6465 0.6465 0.6465 0.0000  0.0000  0.0000  1193 PHE A CA  
9629  C C   . PHE B 1196 ? 0.6465 0.6465 0.6465 0.0000  0.0000  0.0000  1193 PHE A C   
9630  O O   . PHE B 1196 ? 0.6465 0.6465 0.6465 0.0000  0.0000  0.0000  1193 PHE A O   
9631  C CB  . PHE B 1196 ? 0.6465 0.6465 0.6465 0.0000  0.0000  0.0000  1193 PHE A CB  
9632  C CG  . PHE B 1196 ? 0.6465 0.6465 0.6465 0.0000  0.0000  0.0000  1193 PHE A CG  
9633  C CD1 . PHE B 1196 ? 0.6465 0.6465 0.6465 0.0000  0.0000  0.0000  1193 PHE A CD1 
9634  C CD2 . PHE B 1196 ? 0.6465 0.6465 0.6465 0.0000  0.0000  0.0000  1193 PHE A CD2 
9635  C CE1 . PHE B 1196 ? 0.6465 0.6465 0.6465 0.0000  0.0000  0.0000  1193 PHE A CE1 
9636  C CE2 . PHE B 1196 ? 0.6465 0.6465 0.6465 0.0000  0.0000  0.0000  1193 PHE A CE2 
9637  C CZ  . PHE B 1196 ? 0.6465 0.6465 0.6465 0.0000  0.0000  0.0000  1193 PHE A CZ  
9638  N N   . ARG B 1197 ? 0.6817 0.6817 0.6817 0.0000  0.0000  0.0000  1194 ARG A N   
9639  C CA  . ARG B 1197 ? 0.6817 0.6817 0.6817 0.0000  0.0000  0.0000  1194 ARG A CA  
9640  C C   . ARG B 1197 ? 0.6817 0.6817 0.6817 0.0000  0.0000  0.0000  1194 ARG A C   
9641  O O   . ARG B 1197 ? 0.6817 0.6817 0.6817 0.0000  0.0000  0.0000  1194 ARG A O   
9642  C CB  . ARG B 1197 ? 0.6817 0.6817 0.6817 0.0000  0.0000  0.0000  1194 ARG A CB  
9643  C CG  . ARG B 1197 ? 0.6817 0.6817 0.6817 0.0000  0.0000  0.0000  1194 ARG A CG  
9644  C CD  . ARG B 1197 ? 0.6817 0.6817 0.6817 0.0000  0.0000  0.0000  1194 ARG A CD  
9645  N NE  . ARG B 1197 ? 0.6817 0.6817 0.6817 0.0000  0.0000  0.0000  1194 ARG A NE  
9646  C CZ  . ARG B 1197 ? 0.6817 0.6817 0.6817 0.0000  0.0000  0.0000  1194 ARG A CZ  
9647  N NH1 . ARG B 1197 ? 0.6817 0.6817 0.6817 0.0000  0.0000  0.0000  1194 ARG A NH1 
9648  N NH2 . ARG B 1197 ? 0.6817 0.6817 0.6817 0.0000  0.0000  0.0000  1194 ARG A NH2 
9649  N N   . ASP B 1198 ? 0.6768 0.6768 0.6768 0.0000  0.0000  0.0000  1195 ASP A N   
9650  C CA  . ASP B 1198 ? 0.6768 0.6768 0.6768 0.0000  0.0000  0.0000  1195 ASP A CA  
9651  C C   . ASP B 1198 ? 0.6768 0.6768 0.6768 0.0000  0.0000  0.0000  1195 ASP A C   
9652  O O   . ASP B 1198 ? 0.6768 0.6768 0.6768 0.0000  0.0000  0.0000  1195 ASP A O   
9653  C CB  . ASP B 1198 ? 0.6768 0.6768 0.6768 0.0000  0.0000  0.0000  1195 ASP A CB  
9654  C CG  . ASP B 1198 ? 0.6768 0.6768 0.6768 0.0000  0.0000  0.0000  1195 ASP A CG  
9655  O OD1 . ASP B 1198 ? 0.6768 0.6768 0.6768 0.0000  0.0000  0.0000  1195 ASP A OD1 
9656  O OD2 . ASP B 1198 ? 0.6768 0.6768 0.6768 0.0000  0.0000  0.0000  1195 ASP A OD2 
9657  N N   . GLY B 1199 ? 0.6851 0.6851 0.6851 0.0000  0.0000  0.0000  1196 GLY A N   
9658  C CA  . GLY B 1199 ? 0.6851 0.6851 0.6851 0.0000  0.0000  0.0000  1196 GLY A CA  
9659  C C   . GLY B 1199 ? 0.6851 0.6851 0.6851 0.0000  0.0000  0.0000  1196 GLY A C   
9660  O O   . GLY B 1199 ? 0.6851 0.6851 0.6851 0.0000  0.0000  0.0000  1196 GLY A O   
9661  N N   . SER B 1200 ? 0.6470 0.6470 0.6470 0.0000  0.0000  0.0000  1197 SER A N   
9662  C CA  . SER B 1200 ? 0.6470 0.6470 0.6470 0.0000  0.0000  0.0000  1197 SER A CA  
9663  C C   . SER B 1200 ? 0.6470 0.6470 0.6470 0.0000  0.0000  0.0000  1197 SER A C   
9664  O O   . SER B 1200 ? 0.6470 0.6470 0.6470 0.0000  0.0000  0.0000  1197 SER A O   
9665  C CB  . SER B 1200 ? 0.6470 0.6470 0.6470 0.0000  0.0000  0.0000  1197 SER A CB  
9666  O OG  . SER B 1200 ? 0.6470 0.6470 0.6470 0.0000  0.0000  0.0000  1197 SER A OG  
9667  N N   . ASN B 1201 ? 0.6219 0.6219 0.6219 0.0000  0.0000  0.0000  1198 ASN A N   
9668  C CA  . ASN B 1201 ? 0.6219 0.6219 0.6219 0.0000  0.0000  0.0000  1198 ASN A CA  
9669  C C   . ASN B 1201 ? 0.6219 0.6219 0.6219 0.0000  0.0000  0.0000  1198 ASN A C   
9670  O O   . ASN B 1201 ? 0.6219 0.6219 0.6219 0.0000  0.0000  0.0000  1198 ASN A O   
9671  C CB  . ASN B 1201 ? 0.6219 0.6219 0.6219 0.0000  0.0000  0.0000  1198 ASN A CB  
9672  C CG  . ASN B 1201 ? 0.6219 0.6219 0.6219 0.0000  0.0000  0.0000  1198 ASN A CG  
9673  O OD1 . ASN B 1201 ? 0.6219 0.6219 0.6219 0.0000  0.0000  0.0000  1198 ASN A OD1 
9674  N ND2 . ASN B 1201 ? 0.6219 0.6219 0.6219 0.0000  0.0000  0.0000  1198 ASN A ND2 
9675  N N   . ILE B 1202 ? 0.6708 0.6708 0.6708 0.0000  0.0000  0.0000  1199 ILE A N   
9676  C CA  . ILE B 1202 ? 0.6708 0.6708 0.6708 0.0000  0.0000  0.0000  1199 ILE A CA  
9677  C C   . ILE B 1202 ? 0.6708 0.6708 0.6708 0.0000  0.0000  0.0000  1199 ILE A C   
9678  O O   . ILE B 1202 ? 0.6708 0.6708 0.6708 0.0000  0.0000  0.0000  1199 ILE A O   
9679  C CB  . ILE B 1202 ? 0.6708 0.6708 0.6708 0.0000  0.0000  0.0000  1199 ILE A CB  
9680  C CG1 . ILE B 1202 ? 0.6708 0.6708 0.6708 0.0000  0.0000  0.0000  1199 ILE A CG1 
9681  C CG2 . ILE B 1202 ? 0.6708 0.6708 0.6708 0.0000  0.0000  0.0000  1199 ILE A CG2 
9682  C CD1 . ILE B 1202 ? 0.6708 0.6708 0.6708 0.0000  0.0000  0.0000  1199 ILE A CD1 
9683  N N   . LEU B 1203 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1200 LEU A N   
9684  C CA  . LEU B 1203 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1200 LEU A CA  
9685  C C   . LEU B 1203 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1200 LEU A C   
9686  O O   . LEU B 1203 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1200 LEU A O   
9687  C CB  . LEU B 1203 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1200 LEU A CB  
9688  C CG  . LEU B 1203 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1200 LEU A CG  
9689  C CD1 . LEU B 1203 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1200 LEU A CD1 
9690  C CD2 . LEU B 1203 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1200 LEU A CD2 
9691  N N   . PRO B 1204 ? 0.6746 0.6746 0.6746 0.0000  0.0000  0.0000  1201 PRO A N   
9692  C CA  . PRO B 1204 ? 0.6746 0.6746 0.6746 0.0000  0.0000  0.0000  1201 PRO A CA  
9693  C C   . PRO B 1204 ? 0.6746 0.6746 0.6746 0.0000  0.0000  0.0000  1201 PRO A C   
9694  O O   . PRO B 1204 ? 0.6746 0.6746 0.6746 0.0000  0.0000  0.0000  1201 PRO A O   
9695  C CB  . PRO B 1204 ? 0.6746 0.6746 0.6746 0.0000  0.0000  0.0000  1201 PRO A CB  
9696  C CG  . PRO B 1204 ? 0.6746 0.6746 0.6746 0.0000  0.0000  0.0000  1201 PRO A CG  
9697  C CD  . PRO B 1204 ? 0.6746 0.6746 0.6746 0.0000  0.0000  0.0000  1201 PRO A CD  
9698  N N   . LYS B 1205 ? 0.6827 0.6827 0.6827 0.0000  0.0000  0.0000  1202 LYS A N   
9699  C CA  . LYS B 1205 ? 0.6827 0.6827 0.6827 0.0000  0.0000  0.0000  1202 LYS A CA  
9700  C C   . LYS B 1205 ? 0.6827 0.6827 0.6827 0.0000  0.0000  0.0000  1202 LYS A C   
9701  O O   . LYS B 1205 ? 0.6827 0.6827 0.6827 0.0000  0.0000  0.0000  1202 LYS A O   
9702  C CB  . LYS B 1205 ? 0.6827 0.6827 0.6827 0.0000  0.0000  0.0000  1202 LYS A CB  
9703  C CG  . LYS B 1205 ? 0.6827 0.6827 0.6827 0.0000  0.0000  0.0000  1202 LYS A CG  
9704  C CD  . LYS B 1205 ? 0.6827 0.6827 0.6827 0.0000  0.0000  0.0000  1202 LYS A CD  
9705  C CE  . LYS B 1205 ? 0.6827 0.6827 0.6827 0.0000  0.0000  0.0000  1202 LYS A CE  
9706  N NZ  . LYS B 1205 ? 0.6827 0.6827 0.6827 0.0000  0.0000  0.0000  1202 LYS A NZ  
9707  N N   . LEU B 1206 ? 0.7026 0.7026 0.7026 0.0000  0.0000  0.0000  1203 LEU A N   
9708  C CA  . LEU B 1206 ? 0.7026 0.7026 0.7026 0.0000  0.0000  0.0000  1203 LEU A CA  
9709  C C   . LEU B 1206 ? 0.7026 0.7026 0.7026 0.0000  0.0000  0.0000  1203 LEU A C   
9710  O O   . LEU B 1206 ? 0.7026 0.7026 0.7026 0.0000  0.0000  0.0000  1203 LEU A O   
9711  C CB  . LEU B 1206 ? 0.7026 0.7026 0.7026 0.0000  0.0000  0.0000  1203 LEU A CB  
9712  C CG  . LEU B 1206 ? 0.7026 0.7026 0.7026 0.0000  0.0000  0.0000  1203 LEU A CG  
9713  C CD1 . LEU B 1206 ? 0.7026 0.7026 0.7026 0.0000  0.0000  0.0000  1203 LEU A CD1 
9714  C CD2 . LEU B 1206 ? 0.7026 0.7026 0.7026 0.0000  0.0000  0.0000  1203 LEU A CD2 
9715  N N   . LEU B 1207 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1204 LEU A N   
9716  C CA  . LEU B 1207 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1204 LEU A CA  
9717  C C   . LEU B 1207 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1204 LEU A C   
9718  O O   . LEU B 1207 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1204 LEU A O   
9719  C CB  . LEU B 1207 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1204 LEU A CB  
9720  C CG  . LEU B 1207 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1204 LEU A CG  
9721  C CD1 . LEU B 1207 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1204 LEU A CD1 
9722  C CD2 . LEU B 1207 ? 0.7243 0.7243 0.7243 0.0000  0.0000  0.0000  1204 LEU A CD2 
9723  N N   . GLU B 1208 ? 0.7797 0.7797 0.7797 0.0000  0.0000  0.0000  1205 GLU A N   
9724  C CA  . GLU B 1208 ? 0.7797 0.7797 0.7797 0.0000  0.0000  0.0000  1205 GLU A CA  
9725  C C   . GLU B 1208 ? 0.7797 0.7797 0.7797 0.0000  0.0000  0.0000  1205 GLU A C   
9726  O O   . GLU B 1208 ? 0.7797 0.7797 0.7797 0.0000  0.0000  0.0000  1205 GLU A O   
9732  N N   . ASN B 1209 ? 0.7655 0.7655 0.7655 0.0000  0.0000  0.0000  1206 ASN A N   
9733  C CA  . ASN B 1209 ? 0.7655 0.7655 0.7655 0.0000  0.0000  0.0000  1206 ASN A CA  
9734  C C   . ASN B 1209 ? 0.7655 0.7655 0.7655 0.0000  0.0000  0.0000  1206 ASN A C   
9735  O O   . ASN B 1209 ? 0.7655 0.7655 0.7655 0.0000  0.0000  0.0000  1206 ASN A O   
9736  C CB  . ASN B 1209 ? 0.7655 0.7655 0.7655 0.0000  0.0000  0.0000  1206 ASN A CB  
9737  C CG  . ASN B 1209 ? 0.7655 0.7655 0.7655 0.0000  0.0000  0.0000  1206 ASN A CG  
9738  O OD1 . ASN B 1209 ? 0.7655 0.7655 0.7655 0.0000  0.0000  0.0000  1206 ASN A OD1 
9739  N ND2 . ASN B 1209 ? 0.7655 0.7655 0.7655 0.0000  0.0000  0.0000  1206 ASN A ND2 
9740  N N   . ASP B 1210 ? 0.7918 0.7918 0.7918 0.0000  0.0000  0.0000  1207 ASP A N   
9741  C CA  . ASP B 1210 ? 0.7918 0.7918 0.7918 0.0000  0.0000  0.0000  1207 ASP A CA  
9742  C C   . ASP B 1210 ? 0.7918 0.7918 0.7918 0.0000  0.0000  0.0000  1207 ASP A C   
9743  O O   . ASP B 1210 ? 0.7918 0.7918 0.7918 0.0000  0.0000  0.0000  1207 ASP A O   
9744  C CB  . ASP B 1210 ? 0.7918 0.7918 0.7918 0.0000  0.0000  0.0000  1207 ASP A CB  
9745  C CG  . ASP B 1210 ? 0.7918 0.7918 0.7918 0.0000  0.0000  0.0000  1207 ASP A CG  
9746  O OD1 . ASP B 1210 ? 0.7918 0.7918 0.7918 0.0000  0.0000  0.0000  1207 ASP A OD1 
9747  O OD2 . ASP B 1210 ? 0.7918 0.7918 0.7918 0.0000  0.0000  0.0000  1207 ASP A OD2 
9748  N N   . ASP B 1211 ? 0.7490 0.7490 0.7490 0.0000  0.0000  0.0000  1208 ASP A N   
9749  C CA  . ASP B 1211 ? 0.7490 0.7490 0.7490 0.0000  0.0000  0.0000  1208 ASP A CA  
9750  C C   . ASP B 1211 ? 0.7490 0.7490 0.7490 0.0000  0.0000  0.0000  1208 ASP A C   
9751  O O   . ASP B 1211 ? 0.7490 0.7490 0.7490 0.0000  0.0000  0.0000  1208 ASP A O   
9752  C CB  . ASP B 1211 ? 0.7490 0.7490 0.7490 0.0000  0.0000  0.0000  1208 ASP A CB  
9753  C CG  . ASP B 1211 ? 0.7490 0.7490 0.7490 0.0000  0.0000  0.0000  1208 ASP A CG  
9754  O OD1 . ASP B 1211 ? 0.7490 0.7490 0.7490 0.0000  0.0000  0.0000  1208 ASP A OD1 
9755  O OD2 . ASP B 1211 ? 0.7490 0.7490 0.7490 0.0000  0.0000  0.0000  1208 ASP A OD2 
9756  N N   . SER B 1212 ? 0.7088 0.7088 0.7088 0.0000  0.0000  0.0000  1209 SER A N   
9757  C CA  . SER B 1212 ? 0.7088 0.7088 0.7088 0.0000  0.0000  0.0000  1209 SER A CA  
9758  C C   . SER B 1212 ? 0.7088 0.7088 0.7088 0.0000  0.0000  0.0000  1209 SER A C   
9759  O O   . SER B 1212 ? 0.7088 0.7088 0.7088 0.0000  0.0000  0.0000  1209 SER A O   
9760  C CB  . SER B 1212 ? 0.7088 0.7088 0.7088 0.0000  0.0000  0.0000  1209 SER A CB  
9761  O OG  . SER B 1212 ? 0.7088 0.7088 0.7088 0.0000  0.0000  0.0000  1209 SER A OG  
9762  N N   . HIS B 1213 ? 0.7045 0.7045 0.7045 0.0000  0.0000  0.0000  1210 HIS A N   
9763  C CA  . HIS B 1213 ? 0.7045 0.7045 0.7045 0.0000  0.0000  0.0000  1210 HIS A CA  
9764  C C   . HIS B 1213 ? 0.7045 0.7045 0.7045 0.0000  0.0000  0.0000  1210 HIS A C   
9765  O O   . HIS B 1213 ? 0.7045 0.7045 0.7045 0.0000  0.0000  0.0000  1210 HIS A O   
9766  C CB  . HIS B 1213 ? 0.7045 0.7045 0.7045 0.0000  0.0000  0.0000  1210 HIS A CB  
9767  C CG  . HIS B 1213 ? 0.7045 0.7045 0.7045 0.0000  0.0000  0.0000  1210 HIS A CG  
9768  N ND1 . HIS B 1213 ? 0.7045 0.7045 0.7045 0.0000  0.0000  0.0000  1210 HIS A ND1 
9769  C CD2 . HIS B 1213 ? 0.7045 0.7045 0.7045 0.0000  0.0000  0.0000  1210 HIS A CD2 
9770  C CE1 . HIS B 1213 ? 0.7045 0.7045 0.7045 0.0000  0.0000  0.0000  1210 HIS A CE1 
9771  N NE2 . HIS B 1213 ? 0.7045 0.7045 0.7045 0.0000  0.0000  0.0000  1210 HIS A NE2 
9772  N N   . ALA B 1214 ? 0.6239 0.6239 0.6239 0.0000  0.0000  0.0000  1211 ALA A N   
9773  C CA  . ALA B 1214 ? 0.6239 0.6239 0.6239 0.0000  0.0000  0.0000  1211 ALA A CA  
9774  C C   . ALA B 1214 ? 0.6239 0.6239 0.6239 0.0000  0.0000  0.0000  1211 ALA A C   
9775  O O   . ALA B 1214 ? 0.6239 0.6239 0.6239 0.0000  0.0000  0.0000  1211 ALA A O   
9776  C CB  . ALA B 1214 ? 0.6239 0.6239 0.6239 0.0000  0.0000  0.0000  1211 ALA A CB  
9777  N N   . ILE B 1215 ? 0.6538 0.6538 0.6538 0.0000  0.0000  0.0000  1212 ILE A N   
9778  C CA  . ILE B 1215 ? 0.6538 0.6538 0.6538 0.0000  0.0000  0.0000  1212 ILE A CA  
9779  C C   . ILE B 1215 ? 0.6538 0.6538 0.6538 0.0000  0.0000  0.0000  1212 ILE A C   
9780  O O   . ILE B 1215 ? 0.6538 0.6538 0.6538 0.0000  0.0000  0.0000  1212 ILE A O   
9781  C CB  . ILE B 1215 ? 0.6538 0.6538 0.6538 0.0000  0.0000  0.0000  1212 ILE A CB  
9782  C CG1 . ILE B 1215 ? 0.6538 0.6538 0.6538 0.0000  0.0000  0.0000  1212 ILE A CG1 
9783  C CG2 . ILE B 1215 ? 0.6538 0.6538 0.6538 0.0000  0.0000  0.0000  1212 ILE A CG2 
9784  C CD1 . ILE B 1215 ? 0.6538 0.6538 0.6538 0.0000  0.0000  0.0000  1212 ILE A CD1 
9785  N N   . ASP B 1216 ? 0.6448 0.6448 0.6448 0.0000  0.0000  0.0000  1213 ASP A N   
9786  C CA  . ASP B 1216 ? 0.6448 0.6448 0.6448 0.0000  0.0000  0.0000  1213 ASP A CA  
9787  C C   . ASP B 1216 ? 0.6448 0.6448 0.6448 0.0000  0.0000  0.0000  1213 ASP A C   
9788  O O   . ASP B 1216 ? 0.6448 0.6448 0.6448 0.0000  0.0000  0.0000  1213 ASP A O   
9789  C CB  . ASP B 1216 ? 0.6448 0.6448 0.6448 0.0000  0.0000  0.0000  1213 ASP A CB  
9790  C CG  . ASP B 1216 ? 0.6448 0.6448 0.6448 0.0000  0.0000  0.0000  1213 ASP A CG  
9791  O OD1 . ASP B 1216 ? 0.6448 0.6448 0.6448 0.0000  0.0000  0.0000  1213 ASP A OD1 
9792  O OD2 . ASP B 1216 ? 0.6448 0.6448 0.6448 0.0000  0.0000  0.0000  1213 ASP A OD2 
9793  N N   . THR B 1217 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1214 THR A N   
9794  C CA  . THR B 1217 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1214 THR A CA  
9795  C C   . THR B 1217 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1214 THR A C   
9796  O O   . THR B 1217 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1214 THR A O   
9797  C CB  . THR B 1217 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1214 THR A CB  
9798  O OG1 . THR B 1217 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1214 THR A OG1 
9799  C CG2 . THR B 1217 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1214 THR A CG2 
9800  N N   . MET B 1218 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1215 MET A N   
9801  C CA  . MET B 1218 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1215 MET A CA  
9802  C C   . MET B 1218 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1215 MET A C   
9803  O O   . MET B 1218 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1215 MET A O   
9804  C CB  . MET B 1218 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1215 MET A CB  
9805  C CG  . MET B 1218 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1215 MET A CG  
9806  S SD  . MET B 1218 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1215 MET A SD  
9807  C CE  . MET B 1218 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1215 MET A CE  
9808  N N   . VAL B 1219 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1216 VAL A N   
9809  C CA  . VAL B 1219 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1216 VAL A CA  
9810  C C   . VAL B 1219 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1216 VAL A C   
9811  O O   . VAL B 1219 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1216 VAL A O   
9812  C CB  . VAL B 1219 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1216 VAL A CB  
9813  C CG1 . VAL B 1219 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1216 VAL A CG1 
9814  C CG2 . VAL B 1219 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1216 VAL A CG2 
9815  N N   . ALA B 1220 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1217 ALA A N   
9816  C CA  . ALA B 1220 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1217 ALA A CA  
9817  C C   . ALA B 1220 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1217 ALA A C   
9818  O O   . ALA B 1220 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1217 ALA A O   
9819  C CB  . ALA B 1220 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1217 ALA A CB  
9820  N N   . LEU B 1221 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1218 LEU A N   
9821  C CA  . LEU B 1221 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1218 LEU A CA  
9822  C C   . LEU B 1221 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1218 LEU A C   
9823  O O   . LEU B 1221 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1218 LEU A O   
9824  C CB  . LEU B 1221 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1218 LEU A CB  
9825  C CG  . LEU B 1221 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1218 LEU A CG  
9826  C CD1 . LEU B 1221 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1218 LEU A CD1 
9827  C CD2 . LEU B 1221 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1218 LEU A CD2 
9828  N N   . ILE B 1222 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1219 ILE A N   
9829  C CA  . ILE B 1222 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1219 ILE A CA  
9830  C C   . ILE B 1222 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1219 ILE A C   
9831  O O   . ILE B 1222 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1219 ILE A O   
9832  C CB  . ILE B 1222 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1219 ILE A CB  
9833  C CG1 . ILE B 1222 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1219 ILE A CG1 
9834  C CG2 . ILE B 1222 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1219 ILE A CG2 
9835  C CD1 . ILE B 1222 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1219 ILE A CD1 
9836  N N   . ARG B 1223 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1220 ARG A N   
9837  C CA  . ARG B 1223 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1220 ARG A CA  
9838  C C   . ARG B 1223 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1220 ARG A C   
9839  O O   . ARG B 1223 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1220 ARG A O   
9840  C CB  . ARG B 1223 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1220 ARG A CB  
9841  C CG  . ARG B 1223 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1220 ARG A CG  
9842  C CD  . ARG B 1223 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1220 ARG A CD  
9843  N NE  . ARG B 1223 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1220 ARG A NE  
9844  C CZ  . ARG B 1223 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1220 ARG A CZ  
9845  N NH1 . ARG B 1223 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1220 ARG A NH1 
9846  N NH2 . ARG B 1223 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1220 ARG A NH2 
9847  N N   . SER B 1224 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1221 SER A N   
9848  C CA  . SER B 1224 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1221 SER A CA  
9849  C C   . SER B 1224 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1221 SER A C   
9850  O O   . SER B 1224 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1221 SER A O   
9851  C CB  . SER B 1224 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1221 SER A CB  
9852  O OG  . SER B 1224 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1221 SER A OG  
9853  N N   . VAL B 1225 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1222 VAL A N   
9854  C CA  . VAL B 1225 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1222 VAL A CA  
9855  C C   . VAL B 1225 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1222 VAL A C   
9856  O O   . VAL B 1225 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1222 VAL A O   
9857  C CB  . VAL B 1225 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1222 VAL A CB  
9858  C CG1 . VAL B 1225 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1222 VAL A CG1 
9859  C CG2 . VAL B 1225 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1222 VAL A CG2 
9860  N N   . LEU B 1226 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1223 LEU A N   
9861  C CA  . LEU B 1226 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1223 LEU A CA  
9862  C C   . LEU B 1226 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1223 LEU A C   
9863  O O   . LEU B 1226 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1223 LEU A O   
9864  C CB  . LEU B 1226 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1223 LEU A CB  
9865  C CG  . LEU B 1226 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1223 LEU A CG  
9866  C CD1 . LEU B 1226 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1223 LEU A CD1 
9867  C CD2 . LEU B 1226 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1223 LEU A CD2 
9868  N N   . GLN B 1227 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1224 GLN A N   
9869  C CA  . GLN B 1227 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1224 GLN A CA  
9870  C C   . GLN B 1227 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1224 GLN A C   
9871  O O   . GLN B 1227 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1224 GLN A O   
9872  C CB  . GLN B 1227 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1224 GLN A CB  
9873  C CG  . GLN B 1227 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1224 GLN A CG  
9874  C CD  . GLN B 1227 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1224 GLN A CD  
9875  O OE1 . GLN B 1227 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1224 GLN A OE1 
9876  N NE2 . GLN B 1227 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1224 GLN A NE2 
9877  N N   . MET B 1228 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1225 MET A N   
9878  C CA  . MET B 1228 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1225 MET A CA  
9879  C C   . MET B 1228 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1225 MET A C   
9880  O O   . MET B 1228 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1225 MET A O   
9881  C CB  . MET B 1228 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1225 MET A CB  
9882  C CG  . MET B 1228 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1225 MET A CG  
9883  S SD  . MET B 1228 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1225 MET A SD  
9884  C CE  . MET B 1228 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1225 MET A CE  
9885  N N   . ARG B 1229 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1226 ARG A N   
9886  C CA  . ARG B 1229 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1226 ARG A CA  
9887  C C   . ARG B 1229 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1226 ARG A C   
9888  O O   . ARG B 1229 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1226 ARG A O   
9889  C CB  . ARG B 1229 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1226 ARG A CB  
9890  C CG  . ARG B 1229 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1226 ARG A CG  
9891  C CD  . ARG B 1229 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1226 ARG A CD  
9892  N NE  . ARG B 1229 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1226 ARG A NE  
9893  C CZ  . ARG B 1229 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1226 ARG A CZ  
9894  N NH1 . ARG B 1229 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1226 ARG A NH1 
9895  N NH2 . ARG B 1229 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1226 ARG A NH2 
9896  N N   . ASN B 1230 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1227 ASN A N   
9897  C CA  . ASN B 1230 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1227 ASN A CA  
9898  C C   . ASN B 1230 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1227 ASN A C   
9899  O O   . ASN B 1230 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1227 ASN A O   
9900  C CB  . ASN B 1230 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1227 ASN A CB  
9901  C CG  . ASN B 1230 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1227 ASN A CG  
9902  O OD1 . ASN B 1230 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1227 ASN A OD1 
9903  N ND2 . ASN B 1230 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1227 ASN A ND2 
9904  N N   . SER B 1231 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1228 SER A N   
9905  C CA  . SER B 1231 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1228 SER A CA  
9906  C C   . SER B 1231 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1228 SER A C   
9907  O O   . SER B 1231 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1228 SER A O   
9908  C CB  . SER B 1231 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1228 SER A CB  
9909  O OG  . SER B 1231 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1228 SER A OG  
9910  N N   . ASN B 1232 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1229 ASN A N   
9911  C CA  . ASN B 1232 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1229 ASN A CA  
9912  C C   . ASN B 1232 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1229 ASN A C   
9913  O O   . ASN B 1232 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1229 ASN A O   
9914  C CB  . ASN B 1232 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1229 ASN A CB  
9915  C CG  . ASN B 1232 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1229 ASN A CG  
9916  O OD1 . ASN B 1232 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1229 ASN A OD1 
9917  N ND2 . ASN B 1232 ? 0.6835 0.6835 0.6835 0.0000  0.0000  0.0000  1229 ASN A ND2 
9918  N N   . ALA B 1233 ? 0.6824 0.6824 0.6824 0.0000  0.0000  0.0000  1230 ALA A N   
9919  C CA  . ALA B 1233 ? 0.6824 0.6824 0.6824 0.0000  0.0000  0.0000  1230 ALA A CA  
9920  C C   . ALA B 1233 ? 0.6824 0.6824 0.6824 0.0000  0.0000  0.0000  1230 ALA A C   
9921  O O   . ALA B 1233 ? 0.6824 0.6824 0.6824 0.0000  0.0000  0.0000  1230 ALA A O   
9922  C CB  . ALA B 1233 ? 0.6824 0.6824 0.6824 0.0000  0.0000  0.0000  1230 ALA A CB  
9923  N N   . ALA B 1234 ? 0.6596 0.6596 0.6596 0.0000  0.0000  0.0000  1231 ALA A N   
9924  C CA  . ALA B 1234 ? 0.6596 0.6596 0.6596 0.0000  0.0000  0.0000  1231 ALA A CA  
9925  C C   . ALA B 1234 ? 0.6596 0.6596 0.6596 0.0000  0.0000  0.0000  1231 ALA A C   
9926  O O   . ALA B 1234 ? 0.6596 0.6596 0.6596 0.0000  0.0000  0.0000  1231 ALA A O   
9927  C CB  . ALA B 1234 ? 0.6596 0.6596 0.6596 0.0000  0.0000  0.0000  1231 ALA A CB  
9928  N N   . THR B 1235 ? 0.6883 0.6883 0.6883 0.0000  0.0000  0.0000  1232 THR A N   
9929  C CA  . THR B 1235 ? 0.6883 0.6883 0.6883 0.0000  0.0000  0.0000  1232 THR A CA  
9930  C C   . THR B 1235 ? 0.6883 0.6883 0.6883 0.0000  0.0000  0.0000  1232 THR A C   
9931  O O   . THR B 1235 ? 0.6883 0.6883 0.6883 0.0000  0.0000  0.0000  1232 THR A O   
9932  C CB  . THR B 1235 ? 0.6883 0.6883 0.6883 0.0000  0.0000  0.0000  1232 THR A CB  
9933  O OG1 . THR B 1235 ? 0.6883 0.6883 0.6883 0.0000  0.0000  0.0000  1232 THR A OG1 
9934  C CG2 . THR B 1235 ? 0.6883 0.6883 0.6883 0.0000  0.0000  0.0000  1232 THR A CG2 
9935  N N   . GLY B 1236 ? 0.6811 0.6811 0.6811 0.0000  0.0000  0.0000  1233 GLY A N   
9936  C CA  . GLY B 1236 ? 0.6811 0.6811 0.6811 0.0000  0.0000  0.0000  1233 GLY A CA  
9937  C C   . GLY B 1236 ? 0.6811 0.6811 0.6811 0.0000  0.0000  0.0000  1233 GLY A C   
9938  O O   . GLY B 1236 ? 0.6811 0.6811 0.6811 0.0000  0.0000  0.0000  1233 GLY A O   
9939  N N   . GLU B 1237 ? 0.6297 0.6297 0.6297 0.0000  0.0000  0.0000  1234 GLU A N   
9940  C CA  . GLU B 1237 ? 0.6297 0.6297 0.6297 0.0000  0.0000  0.0000  1234 GLU A CA  
9941  C C   . GLU B 1237 ? 0.6297 0.6297 0.6297 0.0000  0.0000  0.0000  1234 GLU A C   
9942  O O   . GLU B 1237 ? 0.6297 0.6297 0.6297 0.0000  0.0000  0.0000  1234 GLU A O   
9943  C CB  . GLU B 1237 ? 0.6297 0.6297 0.6297 0.0000  0.0000  0.0000  1234 GLU A CB  
9944  C CG  . GLU B 1237 ? 0.6297 0.6297 0.6297 0.0000  0.0000  0.0000  1234 GLU A CG  
9945  C CD  . GLU B 1237 ? 0.6297 0.6297 0.6297 0.0000  0.0000  0.0000  1234 GLU A CD  
9946  O OE1 . GLU B 1237 ? 0.6297 0.6297 0.6297 0.0000  0.0000  0.0000  1234 GLU A OE1 
9947  O OE2 . GLU B 1237 ? 0.6297 0.6297 0.6297 0.0000  0.0000  0.0000  1234 GLU A OE2 
9948  N N   . ASP B 1238 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1235 ASP A N   
9949  C CA  . ASP B 1238 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1235 ASP A CA  
9950  C C   . ASP B 1238 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1235 ASP A C   
9951  O O   . ASP B 1238 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1235 ASP A O   
9952  C CB  . ASP B 1238 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1235 ASP A CB  
9953  C CG  . ASP B 1238 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1235 ASP A CG  
9954  O OD1 . ASP B 1238 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1235 ASP A OD1 
9955  O OD2 . ASP B 1238 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1235 ASP A OD2 
9956  N N   . TYR B 1239 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1236 TYR A N   
9957  C CA  . TYR B 1239 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1236 TYR A CA  
9958  C C   . TYR B 1239 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1236 TYR A C   
9959  O O   . TYR B 1239 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1236 TYR A O   
9960  C CB  . TYR B 1239 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1236 TYR A CB  
9961  C CG  . TYR B 1239 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1236 TYR A CG  
9962  C CD1 . TYR B 1239 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1236 TYR A CD1 
9963  C CD2 . TYR B 1239 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1236 TYR A CD2 
9964  C CE1 . TYR B 1239 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1236 TYR A CE1 
9965  C CE2 . TYR B 1239 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1236 TYR A CE2 
9966  C CZ  . TYR B 1239 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1236 TYR A CZ  
9967  O OH  . TYR B 1239 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1236 TYR A OH  
9968  N N   . ILE B 1240 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1237 ILE A N   
9969  C CA  . ILE B 1240 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1237 ILE A CA  
9970  C C   . ILE B 1240 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1237 ILE A C   
9971  O O   . ILE B 1240 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1237 ILE A O   
9972  C CB  . ILE B 1240 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1237 ILE A CB  
9973  C CG1 . ILE B 1240 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1237 ILE A CG1 
9974  C CG2 . ILE B 1240 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1237 ILE A CG2 
9975  C CD1 . ILE B 1240 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1237 ILE A CD1 
9976  N N   . ASN B 1241 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1238 ASN A N   
9977  C CA  . ASN B 1241 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1238 ASN A CA  
9978  C C   . ASN B 1241 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1238 ASN A C   
9979  O O   . ASN B 1241 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1238 ASN A O   
9980  C CB  . ASN B 1241 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1238 ASN A CB  
9981  C CG  . ASN B 1241 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1238 ASN A CG  
9982  O OD1 . ASN B 1241 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1238 ASN A OD1 
9983  N ND2 . ASN B 1241 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1238 ASN A ND2 
9984  N N   . SER B 1242 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1239 SER A N   
9985  C CA  . SER B 1242 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1239 SER A CA  
9986  C C   . SER B 1242 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1239 SER A C   
9987  O O   . SER B 1242 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1239 SER A O   
9988  C CB  . SER B 1242 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1239 SER A CB  
9989  O OG  . SER B 1242 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1239 SER A OG  
9990  N N   . PRO B 1243 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1240 PRO A N   
9991  C CA  . PRO B 1243 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1240 PRO A CA  
9992  C C   . PRO B 1243 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1240 PRO A C   
9993  O O   . PRO B 1243 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1240 PRO A O   
9994  C CB  . PRO B 1243 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1240 PRO A CB  
9995  C CG  . PRO B 1243 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1240 PRO A CG  
9996  C CD  . PRO B 1243 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1240 PRO A CD  
9997  N N   . VAL B 1244 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1241 VAL A N   
9998  C CA  . VAL B 1244 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1241 VAL A CA  
9999  C C   . VAL B 1244 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1241 VAL A C   
10000 O O   . VAL B 1244 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1241 VAL A O   
10001 C CB  . VAL B 1244 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1241 VAL A CB  
10002 C CG1 . VAL B 1244 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1241 VAL A CG1 
10003 C CG2 . VAL B 1244 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1241 VAL A CG2 
10004 N N   . ARG B 1245 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1242 ARG A N   
10005 C CA  . ARG B 1245 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1242 ARG A CA  
10006 C C   . ARG B 1245 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1242 ARG A C   
10007 O O   . ARG B 1245 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1242 ARG A O   
10008 C CB  . ARG B 1245 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1242 ARG A CB  
10009 C CG  . ARG B 1245 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1242 ARG A CG  
10010 C CD  . ARG B 1245 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1242 ARG A CD  
10011 N NE  . ARG B 1245 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1242 ARG A NE  
10012 C CZ  . ARG B 1245 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1242 ARG A CZ  
10013 N NH1 . ARG B 1245 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1242 ARG A NH1 
10014 N NH2 . ARG B 1245 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1242 ARG A NH2 
10015 N N   . ASP B 1246 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1243 ASP A N   
10016 C CA  . ASP B 1246 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1243 ASP A CA  
10017 C C   . ASP B 1246 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1243 ASP A C   
10018 O O   . ASP B 1246 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1243 ASP A O   
10019 C CB  . ASP B 1246 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1243 ASP A CB  
10020 C CG  . ASP B 1246 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1243 ASP A CG  
10021 O OD1 . ASP B 1246 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1243 ASP A OD1 
10022 O OD2 . ASP B 1246 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1243 ASP A OD2 
10023 N N   . LEU B 1247 ? 0.6461 0.6461 0.6461 0.0000  0.0000  0.0000  1244 LEU A N   
10024 C CA  . LEU B 1247 ? 0.6461 0.6461 0.6461 0.0000  0.0000  0.0000  1244 LEU A CA  
10025 C C   . LEU B 1247 ? 0.6461 0.6461 0.6461 0.0000  0.0000  0.0000  1244 LEU A C   
10026 O O   . LEU B 1247 ? 0.6461 0.6461 0.6461 0.0000  0.0000  0.0000  1244 LEU A O   
10027 C CB  . LEU B 1247 ? 0.6461 0.6461 0.6461 0.0000  0.0000  0.0000  1244 LEU A CB  
10028 C CG  . LEU B 1247 ? 0.6461 0.6461 0.6461 0.0000  0.0000  0.0000  1244 LEU A CG  
10029 C CD1 . LEU B 1247 ? 0.6461 0.6461 0.6461 0.0000  0.0000  0.0000  1244 LEU A CD1 
10030 C CD2 . LEU B 1247 ? 0.6461 0.6461 0.6461 0.0000  0.0000  0.0000  1244 LEU A CD2 
10031 N N   . ASN B 1248 ? 0.6683 0.6683 0.6683 0.0000  0.0000  0.0000  1245 ASN A N   
10032 C CA  . ASN B 1248 ? 0.6683 0.6683 0.6683 0.0000  0.0000  0.0000  1245 ASN A CA  
10033 C C   . ASN B 1248 ? 0.6683 0.6683 0.6683 0.0000  0.0000  0.0000  1245 ASN A C   
10034 O O   . ASN B 1248 ? 0.6683 0.6683 0.6683 0.0000  0.0000  0.0000  1245 ASN A O   
10035 C CB  . ASN B 1248 ? 0.6683 0.6683 0.6683 0.0000  0.0000  0.0000  1245 ASN A CB  
10036 C CG  . ASN B 1248 ? 0.6683 0.6683 0.6683 0.0000  0.0000  0.0000  1245 ASN A CG  
10037 O OD1 . ASN B 1248 ? 0.6683 0.6683 0.6683 0.0000  0.0000  0.0000  1245 ASN A OD1 
10038 N ND2 . ASN B 1248 ? 0.6683 0.6683 0.6683 0.0000  0.0000  0.0000  1245 ASN A ND2 
10039 N N   . GLY B 1249 ? 0.6327 0.6327 0.6327 0.0000  0.0000  0.0000  1246 GLY A N   
10040 C CA  . GLY B 1249 ? 0.6327 0.6327 0.6327 0.0000  0.0000  0.0000  1246 GLY A CA  
10041 C C   . GLY B 1249 ? 0.6327 0.6327 0.6327 0.0000  0.0000  0.0000  1246 GLY A C   
10042 O O   . GLY B 1249 ? 0.6327 0.6327 0.6327 0.0000  0.0000  0.0000  1246 GLY A O   
10043 N N   . VAL B 1250 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1247 VAL A N   
10044 C CA  . VAL B 1250 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1247 VAL A CA  
10045 C C   . VAL B 1250 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1247 VAL A C   
10046 O O   . VAL B 1250 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1247 VAL A O   
10047 C CB  . VAL B 1250 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1247 VAL A CB  
10048 C CG1 . VAL B 1250 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1247 VAL A CG1 
10049 C CG2 . VAL B 1250 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1247 VAL A CG2 
10050 N N   . CYS B 1251 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1248 CYS A N   
10051 C CA  . CYS B 1251 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1248 CYS A CA  
10052 C C   . CYS B 1251 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1248 CYS A C   
10053 O O   . CYS B 1251 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1248 CYS A O   
10054 C CB  . CYS B 1251 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1248 CYS A CB  
10055 S SG  . CYS B 1251 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1248 CYS A SG  
10056 N N   . PHE B 1252 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1249 PHE A N   
10057 C CA  . PHE B 1252 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1249 PHE A CA  
10058 C C   . PHE B 1252 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1249 PHE A C   
10059 O O   . PHE B 1252 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1249 PHE A O   
10060 C CB  . PHE B 1252 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1249 PHE A CB  
10061 C CG  . PHE B 1252 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1249 PHE A CG  
10062 C CD1 . PHE B 1252 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1249 PHE A CD1 
10063 C CD2 . PHE B 1252 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1249 PHE A CD2 
10064 C CE1 . PHE B 1252 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1249 PHE A CE1 
10065 C CE2 . PHE B 1252 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1249 PHE A CE2 
10066 C CZ  . PHE B 1252 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1249 PHE A CZ  
10067 N N   . ASP B 1253 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1250 ASP A N   
10068 C CA  . ASP B 1253 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1250 ASP A CA  
10069 C C   . ASP B 1253 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1250 ASP A C   
10070 O O   . ASP B 1253 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1250 ASP A O   
10071 C CB  . ASP B 1253 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1250 ASP A CB  
10072 C CG  . ASP B 1253 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1250 ASP A CG  
10073 O OD1 . ASP B 1253 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1250 ASP A OD1 
10074 O OD2 . ASP B 1253 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1250 ASP A OD2 
10075 N N   . SER B 1254 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1251 SER A N   
10076 C CA  . SER B 1254 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1251 SER A CA  
10077 C C   . SER B 1254 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1251 SER A C   
10078 O O   . SER B 1254 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1251 SER A O   
10079 C CB  . SER B 1254 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1251 SER A CB  
10080 O OG  . SER B 1254 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1251 SER A OG  
10081 N N   . ARG B 1255 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1252 ARG A N   
10082 C CA  . ARG B 1255 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1252 ARG A CA  
10083 C C   . ARG B 1255 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1252 ARG A C   
10084 O O   . ARG B 1255 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1252 ARG A O   
10085 C CB  . ARG B 1255 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1252 ARG A CB  
10086 C CG  . ARG B 1255 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1252 ARG A CG  
10087 C CD  . ARG B 1255 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1252 ARG A CD  
10088 N NE  . ARG B 1255 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1252 ARG A NE  
10089 C CZ  . ARG B 1255 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1252 ARG A CZ  
10090 N NH1 . ARG B 1255 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1252 ARG A NH1 
10091 N NH2 . ARG B 1255 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1252 ARG A NH2 
10092 N N   . PHE B 1256 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1253 PHE A N   
10093 C CA  . PHE B 1256 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1253 PHE A CA  
10094 C C   . PHE B 1256 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1253 PHE A C   
10095 O O   . PHE B 1256 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1253 PHE A O   
10096 C CB  . PHE B 1256 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1253 PHE A CB  
10097 C CG  . PHE B 1256 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1253 PHE A CG  
10098 C CD1 . PHE B 1256 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1253 PHE A CD1 
10099 C CD2 . PHE B 1256 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1253 PHE A CD2 
10100 C CE1 . PHE B 1256 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1253 PHE A CE1 
10101 C CE2 . PHE B 1256 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1253 PHE A CE2 
10102 C CZ  . PHE B 1256 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1253 PHE A CZ  
10103 N N   . GLN B 1257 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1254 GLN A N   
10104 C CA  . GLN B 1257 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1254 GLN A CA  
10105 C C   . GLN B 1257 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1254 GLN A C   
10106 O O   . GLN B 1257 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1254 GLN A O   
10107 C CB  . GLN B 1257 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1254 GLN A CB  
10108 C CG  . GLN B 1257 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1254 GLN A CG  
10109 C CD  . GLN B 1257 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1254 GLN A CD  
10110 O OE1 . GLN B 1257 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1254 GLN A OE1 
10111 N NE2 . GLN B 1257 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1254 GLN A NE2 
10112 N N   . ASN B 1258 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1255 ASN A N   
10113 C CA  . ASN B 1258 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1255 ASN A CA  
10114 C C   . ASN B 1258 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1255 ASN A C   
10115 O O   . ASN B 1258 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1255 ASN A O   
10116 C CB  . ASN B 1258 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1255 ASN A CB  
10117 C CG  . ASN B 1258 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1255 ASN A CG  
10118 O OD1 . ASN B 1258 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1255 ASN A OD1 
10119 N ND2 . ASN B 1258 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1255 ASN A ND2 
10120 N N   . PRO B 1259 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1256 PRO A N   
10121 C CA  . PRO B 1259 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1256 PRO A CA  
10122 C C   . PRO B 1259 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1256 PRO A C   
10123 O O   . PRO B 1259 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1256 PRO A O   
10124 C CB  . PRO B 1259 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1256 PRO A CB  
10125 C CG  . PRO B 1259 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1256 PRO A CG  
10126 C CD  . PRO B 1259 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1256 PRO A CD  
10127 N N   . GLU B 1260 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1257 GLU A N   
10128 C CA  . GLU B 1260 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1257 GLU A CA  
10129 C C   . GLU B 1260 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1257 GLU A C   
10130 O O   . GLU B 1260 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1257 GLU A O   
10131 C CB  . GLU B 1260 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1257 GLU A CB  
10132 C CG  . GLU B 1260 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1257 GLU A CG  
10133 C CD  . GLU B 1260 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1257 GLU A CD  
10134 O OE1 . GLU B 1260 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1257 GLU A OE1 
10135 O OE2 . GLU B 1260 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1257 GLU A OE2 
10136 N N   . TRP B 1261 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1258 TRP A N   
10137 C CA  . TRP B 1261 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1258 TRP A CA  
10138 C C   . TRP B 1261 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1258 TRP A C   
10139 O O   . TRP B 1261 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1258 TRP A O   
10140 C CB  . TRP B 1261 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1258 TRP A CB  
10141 C CG  . TRP B 1261 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1258 TRP A CG  
10142 C CD1 . TRP B 1261 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1258 TRP A CD1 
10143 C CD2 . TRP B 1261 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1258 TRP A CD2 
10144 N NE1 . TRP B 1261 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1258 TRP A NE1 
10145 C CE2 . TRP B 1261 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1258 TRP A CE2 
10146 C CE3 . TRP B 1261 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1258 TRP A CE3 
10147 C CZ2 . TRP B 1261 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1258 TRP A CZ2 
10148 C CZ3 . TRP B 1261 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1258 TRP A CZ3 
10149 C CH2 . TRP B 1261 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1258 TRP A CH2 
10150 N N   . PRO B 1262 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1259 PRO A N   
10151 C CA  . PRO B 1262 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1259 PRO A CA  
10152 C C   . PRO B 1262 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1259 PRO A C   
10153 O O   . PRO B 1262 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1259 PRO A O   
10154 C CB  . PRO B 1262 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1259 PRO A CB  
10155 C CG  . PRO B 1262 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1259 PRO A CG  
10156 C CD  . PRO B 1262 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1259 PRO A CD  
10157 N N   . MET B 1263 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1260 MET A N   
10158 C CA  . MET B 1263 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1260 MET A CA  
10159 C C   . MET B 1263 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1260 MET A C   
10160 O O   . MET B 1263 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1260 MET A O   
10161 C CB  . MET B 1263 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1260 MET A CB  
10162 C CG  . MET B 1263 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1260 MET A CG  
10163 S SD  . MET B 1263 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1260 MET A SD  
10164 C CE  . MET B 1263 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1260 MET A CE  
10165 N N   . ASP B 1264 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1261 ASP A N   
10166 C CA  . ASP B 1264 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1261 ASP A CA  
10167 C C   . ASP B 1264 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1261 ASP A C   
10168 O O   . ASP B 1264 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1261 ASP A O   
10169 C CB  . ASP B 1264 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1261 ASP A CB  
10170 C CG  . ASP B 1264 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1261 ASP A CG  
10171 O OD1 . ASP B 1264 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1261 ASP A OD1 
10172 O OD2 . ASP B 1264 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1261 ASP A OD2 
10173 N N   . ALA B 1265 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1262 ALA A N   
10174 C CA  . ALA B 1265 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1262 ALA A CA  
10175 C C   . ALA B 1265 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1262 ALA A C   
10176 O O   . ALA B 1265 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1262 ALA A O   
10177 C CB  . ALA B 1265 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1262 ALA A CB  
10178 N N   . ASP B 1266 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1263 ASP A N   
10179 C CA  . ASP B 1266 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1263 ASP A CA  
10180 C C   . ASP B 1266 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1263 ASP A C   
10181 O O   . ASP B 1266 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1263 ASP A O   
10182 C CB  . ASP B 1266 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1263 ASP A CB  
10183 C CG  . ASP B 1266 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1263 ASP A CG  
10184 O OD1 . ASP B 1266 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1263 ASP A OD1 
10185 O OD2 . ASP B 1266 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1263 ASP A OD2 
10186 N N   . ALA B 1267 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1264 ALA A N   
10187 C CA  . ALA B 1267 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1264 ALA A CA  
10188 C C   . ALA B 1267 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1264 ALA A C   
10189 O O   . ALA B 1267 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1264 ALA A O   
10190 C CB  . ALA B 1267 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1264 ALA A CB  
10191 N N   . ASN B 1268 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1265 ASN A N   
10192 C CA  . ASN B 1268 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1265 ASN A CA  
10193 C C   . ASN B 1268 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1265 ASN A C   
10194 O O   . ASN B 1268 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1265 ASN A O   
10195 C CB  . ASN B 1268 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1265 ASN A CB  
10196 C CG  . ASN B 1268 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1265 ASN A CG  
10197 O OD1 . ASN B 1268 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1265 ASN A OD1 
10198 N ND2 . ASN B 1268 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1265 ASN A ND2 
10199 N N   . GLY B 1269 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1266 GLY A N   
10200 C CA  . GLY B 1269 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1266 GLY A CA  
10201 C C   . GLY B 1269 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1266 GLY A C   
10202 O O   . GLY B 1269 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1266 GLY A O   
10203 N N   . ALA B 1270 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1267 ALA A N   
10204 C CA  . ALA B 1270 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1267 ALA A CA  
10205 C C   . ALA B 1270 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1267 ALA A C   
10206 O O   . ALA B 1270 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1267 ALA A O   
10207 C CB  . ALA B 1270 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1267 ALA A CB  
10208 N N   . TYR B 1271 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1268 TYR A N   
10209 C CA  . TYR B 1271 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1268 TYR A CA  
10210 C C   . TYR B 1271 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1268 TYR A C   
10211 O O   . TYR B 1271 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1268 TYR A O   
10212 C CB  . TYR B 1271 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1268 TYR A CB  
10213 C CG  . TYR B 1271 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1268 TYR A CG  
10214 C CD1 . TYR B 1271 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1268 TYR A CD1 
10215 C CD2 . TYR B 1271 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1268 TYR A CD2 
10216 C CE1 . TYR B 1271 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1268 TYR A CE1 
10217 C CE2 . TYR B 1271 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1268 TYR A CE2 
10218 C CZ  . TYR B 1271 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1268 TYR A CZ  
10219 O OH  . TYR B 1271 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1268 TYR A OH  
10220 N N   . HIS B 1272 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1269 HIS A N   
10221 C CA  . HIS B 1272 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1269 HIS A CA  
10222 C C   . HIS B 1272 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1269 HIS A C   
10223 O O   . HIS B 1272 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1269 HIS A O   
10224 C CB  . HIS B 1272 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1269 HIS A CB  
10225 C CG  . HIS B 1272 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1269 HIS A CG  
10226 N ND1 . HIS B 1272 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1269 HIS A ND1 
10227 C CD2 . HIS B 1272 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1269 HIS A CD2 
10228 C CE1 . HIS B 1272 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1269 HIS A CE1 
10229 N NE2 . HIS B 1272 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1269 HIS A NE2 
10230 N N   . ILE B 1273 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1270 ILE A N   
10231 C CA  . ILE B 1273 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1270 ILE A CA  
10232 C C   . ILE B 1273 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1270 ILE A C   
10233 O O   . ILE B 1273 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1270 ILE A O   
10234 C CB  . ILE B 1273 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1270 ILE A CB  
10235 C CG1 . ILE B 1273 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1270 ILE A CG1 
10236 C CG2 . ILE B 1273 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1270 ILE A CG2 
10237 C CD1 . ILE B 1273 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1270 ILE A CD1 
10238 N N   . ALA B 1274 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1271 ALA A N   
10239 C CA  . ALA B 1274 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1271 ALA A CA  
10240 C C   . ALA B 1274 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1271 ALA A C   
10241 O O   . ALA B 1274 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1271 ALA A O   
10242 C CB  . ALA B 1274 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1271 ALA A CB  
10243 N N   . LEU B 1275 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1272 LEU A N   
10244 C CA  . LEU B 1275 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1272 LEU A CA  
10245 C C   . LEU B 1275 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1272 LEU A C   
10246 O O   . LEU B 1275 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1272 LEU A O   
10247 C CB  . LEU B 1275 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1272 LEU A CB  
10248 C CG  . LEU B 1275 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1272 LEU A CG  
10249 C CD1 . LEU B 1275 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1272 LEU A CD1 
10250 C CD2 . LEU B 1275 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1272 LEU A CD2 
10251 N N   . LYS B 1276 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1273 LYS A N   
10252 C CA  . LYS B 1276 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1273 LYS A CA  
10253 C C   . LYS B 1276 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1273 LYS A C   
10254 O O   . LYS B 1276 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1273 LYS A O   
10255 C CB  . LYS B 1276 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1273 LYS A CB  
10256 C CG  . LYS B 1276 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1273 LYS A CG  
10257 C CD  . LYS B 1276 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1273 LYS A CD  
10258 C CE  . LYS B 1276 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1273 LYS A CE  
10259 N NZ  . LYS B 1276 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1273 LYS A NZ  
10260 N N   . GLY B 1277 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1274 GLY A N   
10261 C CA  . GLY B 1277 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1274 GLY A CA  
10262 C C   . GLY B 1277 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1274 GLY A C   
10263 O O   . GLY B 1277 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1274 GLY A O   
10264 N N   . GLN B 1278 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1275 GLN A N   
10265 C CA  . GLN B 1278 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1275 GLN A CA  
10266 C C   . GLN B 1278 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1275 GLN A C   
10267 O O   . GLN B 1278 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1275 GLN A O   
10268 C CB  . GLN B 1278 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1275 GLN A CB  
10269 C CG  . GLN B 1278 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1275 GLN A CG  
10270 C CD  . GLN B 1278 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1275 GLN A CD  
10271 O OE1 . GLN B 1278 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1275 GLN A OE1 
10272 N NE2 . GLN B 1278 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1275 GLN A NE2 
10273 N N   . LEU B 1279 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1276 LEU A N   
10274 C CA  . LEU B 1279 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1276 LEU A CA  
10275 C C   . LEU B 1279 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1276 LEU A C   
10276 O O   . LEU B 1279 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1276 LEU A O   
10277 C CB  . LEU B 1279 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1276 LEU A CB  
10278 C CG  . LEU B 1279 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1276 LEU A CG  
10279 C CD1 . LEU B 1279 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1276 LEU A CD1 
10280 C CD2 . LEU B 1279 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1276 LEU A CD2 
10281 N N   . LEU B 1280 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1277 LEU A N   
10282 C CA  . LEU B 1280 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1277 LEU A CA  
10283 C C   . LEU B 1280 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1277 LEU A C   
10284 O O   . LEU B 1280 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1277 LEU A O   
10285 C CB  . LEU B 1280 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1277 LEU A CB  
10286 C CG  . LEU B 1280 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1277 LEU A CG  
10287 C CD1 . LEU B 1280 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1277 LEU A CD1 
10288 C CD2 . LEU B 1280 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1277 LEU A CD2 
10289 N N   . LEU B 1281 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1278 LEU A N   
10290 C CA  . LEU B 1281 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1278 LEU A CA  
10291 C C   . LEU B 1281 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1278 LEU A C   
10292 O O   . LEU B 1281 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1278 LEU A O   
10293 C CB  . LEU B 1281 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1278 LEU A CB  
10294 C CG  . LEU B 1281 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1278 LEU A CG  
10295 C CD1 . LEU B 1281 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1278 LEU A CD1 
10296 C CD2 . LEU B 1281 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1278 LEU A CD2 
10297 N N   . ASN B 1282 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1279 ASN A N   
10298 C CA  . ASN B 1282 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1279 ASN A CA  
10299 C C   . ASN B 1282 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1279 ASN A C   
10300 O O   . ASN B 1282 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1279 ASN A O   
10301 C CB  . ASN B 1282 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1279 ASN A CB  
10302 C CG  . ASN B 1282 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1279 ASN A CG  
10303 O OD1 . ASN B 1282 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1279 ASN A OD1 
10304 N ND2 . ASN B 1282 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1279 ASN A ND2 
10305 N N   . HIS B 1283 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1280 HIS A N   
10306 C CA  . HIS B 1283 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1280 HIS A CA  
10307 C C   . HIS B 1283 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1280 HIS A C   
10308 O O   . HIS B 1283 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1280 HIS A O   
10309 C CB  . HIS B 1283 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1280 HIS A CB  
10310 C CG  . HIS B 1283 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1280 HIS A CG  
10311 N ND1 . HIS B 1283 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1280 HIS A ND1 
10312 C CD2 . HIS B 1283 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1280 HIS A CD2 
10313 C CE1 . HIS B 1283 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1280 HIS A CE1 
10314 N NE2 . HIS B 1283 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1280 HIS A NE2 
10315 N N   . LEU B 1284 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1281 LEU A N   
10316 C CA  . LEU B 1284 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1281 LEU A CA  
10317 C C   . LEU B 1284 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1281 LEU A C   
10318 O O   . LEU B 1284 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1281 LEU A O   
10319 C CB  . LEU B 1284 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1281 LEU A CB  
10320 C CG  . LEU B 1284 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1281 LEU A CG  
10321 C CD1 . LEU B 1284 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1281 LEU A CD1 
10322 C CD2 . LEU B 1284 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1281 LEU A CD2 
10323 N N   . LYS B 1285 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1282 LYS A N   
10324 C CA  . LYS B 1285 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1282 LYS A CA  
10325 C C   . LYS B 1285 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1282 LYS A C   
10326 O O   . LYS B 1285 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1282 LYS A O   
10327 C CB  . LYS B 1285 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1282 LYS A CB  
10328 C CG  . LYS B 1285 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1282 LYS A CG  
10329 C CD  . LYS B 1285 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1282 LYS A CD  
10330 C CE  . LYS B 1285 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1282 LYS A CE  
10331 N NZ  . LYS B 1285 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1282 LYS A NZ  
10332 N N   . GLU B 1286 ? 0.6630 0.6630 0.6630 0.0000  0.0000  0.0000  1283 GLU A N   
10333 C CA  . GLU B 1286 ? 0.6630 0.6630 0.6630 0.0000  0.0000  0.0000  1283 GLU A CA  
10334 C C   . GLU B 1286 ? 0.6630 0.6630 0.6630 0.0000  0.0000  0.0000  1283 GLU A C   
10335 O O   . GLU B 1286 ? 0.6630 0.6630 0.6630 0.0000  0.0000  0.0000  1283 GLU A O   
10336 C CB  . GLU B 1286 ? 0.6630 0.6630 0.6630 0.0000  0.0000  0.0000  1283 GLU A CB  
10337 C CG  . GLU B 1286 ? 0.6630 0.6630 0.6630 0.0000  0.0000  0.0000  1283 GLU A CG  
10338 C CD  . GLU B 1286 ? 0.6630 0.6630 0.6630 0.0000  0.0000  0.0000  1283 GLU A CD  
10339 O OE1 . GLU B 1286 ? 0.6630 0.6630 0.6630 0.0000  0.0000  0.0000  1283 GLU A OE1 
10340 O OE2 . GLU B 1286 ? 0.6630 0.6630 0.6630 0.0000  0.0000  0.0000  1283 GLU A OE2 
10341 N N   . SER B 1287 ? 0.7029 0.7029 0.7029 0.0000  0.0000  0.0000  1284 SER A N   
10342 C CA  . SER B 1287 ? 0.7029 0.7029 0.7029 0.0000  0.0000  0.0000  1284 SER A CA  
10343 C C   . SER B 1287 ? 0.7029 0.7029 0.7029 0.0000  0.0000  0.0000  1284 SER A C   
10344 O O   . SER B 1287 ? 0.7029 0.7029 0.7029 0.0000  0.0000  0.0000  1284 SER A O   
10345 C CB  . SER B 1287 ? 0.7029 0.7029 0.7029 0.0000  0.0000  0.0000  1284 SER A CB  
10346 O OG  . SER B 1287 ? 0.7029 0.7029 0.7029 0.0000  0.0000  0.0000  1284 SER A OG  
10347 N N   . LYS B 1288 ? 0.8116 0.8116 0.8116 0.0000  0.0000  0.0000  1285 LYS A N   
10348 C CA  . LYS B 1288 ? 0.8116 0.8116 0.8116 0.0000  0.0000  0.0000  1285 LYS A CA  
10349 C C   . LYS B 1288 ? 0.8116 0.8116 0.8116 0.0000  0.0000  0.0000  1285 LYS A C   
10350 O O   . LYS B 1288 ? 0.8116 0.8116 0.8116 0.0000  0.0000  0.0000  1285 LYS A O   
10356 N N   . ASP B 1289 ? 0.7788 0.7788 0.7788 0.0000  0.0000  0.0000  1286 ASP A N   
10357 C CA  . ASP B 1289 ? 0.7788 0.7788 0.7788 0.0000  0.0000  0.0000  1286 ASP A CA  
10358 C C   . ASP B 1289 ? 0.7788 0.7788 0.7788 0.0000  0.0000  0.0000  1286 ASP A C   
10359 O O   . ASP B 1289 ? 0.7788 0.7788 0.7788 0.0000  0.0000  0.0000  1286 ASP A O   
10360 C CB  . ASP B 1289 ? 0.7788 0.7788 0.7788 0.0000  0.0000  0.0000  1286 ASP A CB  
10361 C CG  . ASP B 1289 ? 0.7788 0.7788 0.7788 0.0000  0.0000  0.0000  1286 ASP A CG  
10362 O OD1 . ASP B 1289 ? 0.7788 0.7788 0.7788 0.0000  0.0000  0.0000  1286 ASP A OD1 
10363 O OD2 . ASP B 1289 ? 0.7788 0.7788 0.7788 0.0000  0.0000  0.0000  1286 ASP A OD2 
10364 N N   . LEU B 1290 ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  1287 LEU A N   
10365 C CA  . LEU B 1290 ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  1287 LEU A CA  
10366 C C   . LEU B 1290 ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  1287 LEU A C   
10367 O O   . LEU B 1290 ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  1287 LEU A O   
10368 C CB  . LEU B 1290 ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  1287 LEU A CB  
10369 C CG  . LEU B 1290 ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  1287 LEU A CG  
10370 C CD1 . LEU B 1290 ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  1287 LEU A CD1 
10371 C CD2 . LEU B 1290 ? 0.6976 0.6976 0.6976 0.0000  0.0000  0.0000  1287 LEU A CD2 
10372 N N   . LYS B 1291 ? 0.7849 0.7849 0.7849 0.0000  0.0000  0.0000  1288 LYS A N   
10373 C CA  . LYS B 1291 ? 0.7849 0.7849 0.7849 0.0000  0.0000  0.0000  1288 LYS A CA  
10374 C C   . LYS B 1291 ? 0.7849 0.7849 0.7849 0.0000  0.0000  0.0000  1288 LYS A C   
10375 O O   . LYS B 1291 ? 0.7849 0.7849 0.7849 0.0000  0.0000  0.0000  1288 LYS A O   
10376 C CB  . LYS B 1291 ? 0.7849 0.7849 0.7849 0.0000  0.0000  0.0000  1288 LYS A CB  
10377 C CG  . LYS B 1291 ? 0.7849 0.7849 0.7849 0.0000  0.0000  0.0000  1288 LYS A CG  
10378 C CD  . LYS B 1291 ? 0.7849 0.7849 0.7849 0.0000  0.0000  0.0000  1288 LYS A CD  
10379 C CE  . LYS B 1291 ? 0.7849 0.7849 0.7849 0.0000  0.0000  0.0000  1288 LYS A CE  
10380 N NZ  . LYS B 1291 ? 0.7849 0.7849 0.7849 0.0000  0.0000  0.0000  1288 LYS A NZ  
10381 N N   . LEU B 1292 ? 0.6841 0.6841 0.6841 0.0000  0.0000  0.0000  1289 LEU A N   
10382 C CA  . LEU B 1292 ? 0.6841 0.6841 0.6841 0.0000  0.0000  0.0000  1289 LEU A CA  
10383 C C   . LEU B 1292 ? 0.6841 0.6841 0.6841 0.0000  0.0000  0.0000  1289 LEU A C   
10384 O O   . LEU B 1292 ? 0.6841 0.6841 0.6841 0.0000  0.0000  0.0000  1289 LEU A O   
10385 C CB  . LEU B 1292 ? 0.6841 0.6841 0.6841 0.0000  0.0000  0.0000  1289 LEU A CB  
10386 C CG  . LEU B 1292 ? 0.6841 0.6841 0.6841 0.0000  0.0000  0.0000  1289 LEU A CG  
10387 C CD1 . LEU B 1292 ? 0.6841 0.6841 0.6841 0.0000  0.0000  0.0000  1289 LEU A CD1 
10388 C CD2 . LEU B 1292 ? 0.6841 0.6841 0.6841 0.0000  0.0000  0.0000  1289 LEU A CD2 
10389 N N   . GLN B 1293 ? 0.7725 0.7725 0.7725 0.0000  0.0000  0.0000  1290 GLN A N   
10390 C CA  . GLN B 1293 ? 0.7725 0.7725 0.7725 0.0000  0.0000  0.0000  1290 GLN A CA  
10391 C C   . GLN B 1293 ? 0.7725 0.7725 0.7725 0.0000  0.0000  0.0000  1290 GLN A C   
10392 O O   . GLN B 1293 ? 0.7725 0.7725 0.7725 0.0000  0.0000  0.0000  1290 GLN A O   
10393 C CB  . GLN B 1293 ? 0.7725 0.7725 0.7725 0.0000  0.0000  0.0000  1290 GLN A CB  
10394 C CG  . GLN B 1293 ? 0.7725 0.7725 0.7725 0.0000  0.0000  0.0000  1290 GLN A CG  
10395 C CD  . GLN B 1293 ? 0.7725 0.7725 0.7725 0.0000  0.0000  0.0000  1290 GLN A CD  
10396 O OE1 . GLN B 1293 ? 0.7725 0.7725 0.7725 0.0000  0.0000  0.0000  1290 GLN A OE1 
10397 N NE2 . GLN B 1293 ? 0.7725 0.7725 0.7725 0.0000  0.0000  0.0000  1290 GLN A NE2 
10398 N N   . ASN B 1294 ? 0.8073 0.8073 0.8073 0.0000  0.0000  0.0000  1291 ASN A N   
10399 C CA  . ASN B 1294 ? 0.8073 0.8073 0.8073 0.0000  0.0000  0.0000  1291 ASN A CA  
10400 C C   . ASN B 1294 ? 0.8073 0.8073 0.8073 0.0000  0.0000  0.0000  1291 ASN A C   
10401 O O   . ASN B 1294 ? 0.8073 0.8073 0.8073 0.0000  0.0000  0.0000  1291 ASN A O   
10402 C CB  . ASN B 1294 ? 0.8073 0.8073 0.8073 0.0000  0.0000  0.0000  1291 ASN A CB  
10403 C CG  . ASN B 1294 ? 0.8073 0.8073 0.8073 0.0000  0.0000  0.0000  1291 ASN A CG  
10404 O OD1 . ASN B 1294 ? 0.8073 0.8073 0.8073 0.0000  0.0000  0.0000  1291 ASN A OD1 
10405 N ND2 . ASN B 1294 ? 0.8073 0.8073 0.8073 0.0000  0.0000  0.0000  1291 ASN A ND2 
10406 N N   . GLY B 1295 ? 0.7006 0.7006 0.7006 0.0000  0.0000  0.0000  1292 GLY A N   
10407 C CA  . GLY B 1295 ? 0.7006 0.7006 0.7006 0.0000  0.0000  0.0000  1292 GLY A CA  
10408 C C   . GLY B 1295 ? 0.7006 0.7006 0.7006 0.0000  0.0000  0.0000  1292 GLY A C   
10409 O O   . GLY B 1295 ? 0.7006 0.7006 0.7006 0.0000  0.0000  0.0000  1292 GLY A O   
10410 N N   . ILE B 1296 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1293 ILE A N   
10411 C CA  . ILE B 1296 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1293 ILE A CA  
10412 C C   . ILE B 1296 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1293 ILE A C   
10413 O O   . ILE B 1296 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1293 ILE A O   
10414 C CB  . ILE B 1296 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1293 ILE A CB  
10415 C CG1 . ILE B 1296 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1293 ILE A CG1 
10416 C CG2 . ILE B 1296 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1293 ILE A CG2 
10417 C CD1 . ILE B 1296 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1293 ILE A CD1 
10418 N N   . SER B 1297 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1294 SER A N   
10419 C CA  . SER B 1297 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1294 SER A CA  
10420 C C   . SER B 1297 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1294 SER A C   
10421 O O   . SER B 1297 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1294 SER A O   
10422 C CB  . SER B 1297 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1294 SER A CB  
10423 O OG  . SER B 1297 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1294 SER A OG  
10424 N N   . ASN B 1298 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1295 ASN A N   
10425 C CA  . ASN B 1298 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1295 ASN A CA  
10426 C C   . ASN B 1298 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1295 ASN A C   
10427 O O   . ASN B 1298 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1295 ASN A O   
10428 C CB  . ASN B 1298 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1295 ASN A CB  
10429 C CG  . ASN B 1298 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1295 ASN A CG  
10430 O OD1 . ASN B 1298 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1295 ASN A OD1 
10431 N ND2 . ASN B 1298 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1295 ASN A ND2 
10432 N N   . GLN B 1299 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1296 GLN A N   
10433 C CA  . GLN B 1299 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1296 GLN A CA  
10434 C C   . GLN B 1299 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1296 GLN A C   
10435 O O   . GLN B 1299 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1296 GLN A O   
10436 C CB  . GLN B 1299 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1296 GLN A CB  
10437 C CG  . GLN B 1299 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1296 GLN A CG  
10438 C CD  . GLN B 1299 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1296 GLN A CD  
10439 O OE1 . GLN B 1299 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1296 GLN A OE1 
10440 N NE2 . GLN B 1299 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1296 GLN A NE2 
10441 N N   . ASP B 1300 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1297 ASP A N   
10442 C CA  . ASP B 1300 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1297 ASP A CA  
10443 C C   . ASP B 1300 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1297 ASP A C   
10444 O O   . ASP B 1300 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1297 ASP A O   
10445 C CB  . ASP B 1300 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1297 ASP A CB  
10446 C CG  . ASP B 1300 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1297 ASP A CG  
10447 O OD1 . ASP B 1300 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1297 ASP A OD1 
10448 O OD2 . ASP B 1300 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1297 ASP A OD2 
10449 N N   . TRP B 1301 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1298 TRP A N   
10450 C CA  . TRP B 1301 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1298 TRP A CA  
10451 C C   . TRP B 1301 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1298 TRP A C   
10452 O O   . TRP B 1301 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1298 TRP A O   
10453 C CB  . TRP B 1301 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1298 TRP A CB  
10454 C CG  . TRP B 1301 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1298 TRP A CG  
10455 C CD1 . TRP B 1301 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1298 TRP A CD1 
10456 C CD2 . TRP B 1301 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1298 TRP A CD2 
10457 N NE1 . TRP B 1301 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1298 TRP A NE1 
10458 C CE2 . TRP B 1301 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1298 TRP A CE2 
10459 C CE3 . TRP B 1301 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1298 TRP A CE3 
10460 C CZ2 . TRP B 1301 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1298 TRP A CZ2 
10461 C CZ3 . TRP B 1301 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1298 TRP A CZ3 
10462 C CH2 . TRP B 1301 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1298 TRP A CH2 
10463 N N   . LEU B 1302 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1299 LEU A N   
10464 C CA  . LEU B 1302 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1299 LEU A CA  
10465 C C   . LEU B 1302 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1299 LEU A C   
10466 O O   . LEU B 1302 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1299 LEU A O   
10467 C CB  . LEU B 1302 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1299 LEU A CB  
10468 C CG  . LEU B 1302 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1299 LEU A CG  
10469 C CD1 . LEU B 1302 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1299 LEU A CD1 
10470 C CD2 . LEU B 1302 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1299 LEU A CD2 
10471 N N   . ALA B 1303 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1300 ALA A N   
10472 C CA  . ALA B 1303 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1300 ALA A CA  
10473 C C   . ALA B 1303 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1300 ALA A C   
10474 O O   . ALA B 1303 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1300 ALA A O   
10475 C CB  . ALA B 1303 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1300 ALA A CB  
10476 N N   . TYR B 1304 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1301 TYR A N   
10477 C CA  . TYR B 1304 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1301 TYR A CA  
10478 C C   . TYR B 1304 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1301 TYR A C   
10479 O O   . TYR B 1304 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1301 TYR A O   
10480 C CB  . TYR B 1304 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1301 TYR A CB  
10481 C CG  . TYR B 1304 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1301 TYR A CG  
10482 C CD1 . TYR B 1304 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1301 TYR A CD1 
10483 C CD2 . TYR B 1304 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1301 TYR A CD2 
10484 C CE1 . TYR B 1304 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1301 TYR A CE1 
10485 C CE2 . TYR B 1304 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1301 TYR A CE2 
10486 C CZ  . TYR B 1304 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1301 TYR A CZ  
10487 O OH  . TYR B 1304 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1301 TYR A OH  
10488 N N   . ILE B 1305 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1302 ILE A N   
10489 C CA  . ILE B 1305 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1302 ILE A CA  
10490 C C   . ILE B 1305 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1302 ILE A C   
10491 O O   . ILE B 1305 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1302 ILE A O   
10492 C CB  . ILE B 1305 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1302 ILE A CB  
10493 C CG1 . ILE B 1305 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1302 ILE A CG1 
10494 C CG2 . ILE B 1305 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1302 ILE A CG2 
10495 C CD1 . ILE B 1305 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1302 ILE A CD1 
10496 N N   . GLN B 1306 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1303 GLN A N   
10497 C CA  . GLN B 1306 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1303 GLN A CA  
10498 C C   . GLN B 1306 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1303 GLN A C   
10499 O O   . GLN B 1306 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1303 GLN A O   
10500 C CB  . GLN B 1306 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1303 GLN A CB  
10501 C CG  . GLN B 1306 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1303 GLN A CG  
10502 C CD  . GLN B 1306 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1303 GLN A CD  
10503 O OE1 . GLN B 1306 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1303 GLN A OE1 
10504 N NE2 . GLN B 1306 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1303 GLN A NE2 
10505 N N   . GLU B 1307 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1304 GLU A N   
10506 C CA  . GLU B 1307 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1304 GLU A CA  
10507 C C   . GLU B 1307 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1304 GLU A C   
10508 O O   . GLU B 1307 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1304 GLU A O   
10509 C CB  . GLU B 1307 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1304 GLU A CB  
10510 C CG  . GLU B 1307 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1304 GLU A CG  
10511 C CD  . GLU B 1307 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1304 GLU A CD  
10512 O OE1 . GLU B 1307 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1304 GLU A OE1 
10513 O OE2 . GLU B 1307 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1304 GLU A OE2 
10514 N N   . LEU B 1308 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1305 LEU A N   
10515 C CA  . LEU B 1308 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1305 LEU A CA  
10516 C C   . LEU B 1308 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1305 LEU A C   
10517 O O   . LEU B 1308 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1305 LEU A O   
10518 C CB  . LEU B 1308 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1305 LEU A CB  
10519 C CG  . LEU B 1308 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1305 LEU A CG  
10520 C CD1 . LEU B 1308 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1305 LEU A CD1 
10521 C CD2 . LEU B 1308 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1305 LEU A CD2 
10522 N N   . ARG B 1309 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1306 ARG A N   
10523 C CA  . ARG B 1309 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1306 ARG A CA  
10524 C C   . ARG B 1309 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1306 ARG A C   
10525 O O   . ARG B 1309 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1306 ARG A O   
10526 C CB  . ARG B 1309 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1306 ARG A CB  
10527 C CG  . ARG B 1309 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1306 ARG A CG  
10528 C CD  . ARG B 1309 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1306 ARG A CD  
10529 N NE  . ARG B 1309 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1306 ARG A NE  
10530 C CZ  . ARG B 1309 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1306 ARG A CZ  
10531 N NH1 . ARG B 1309 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1306 ARG A NH1 
10532 N NH2 . ARG B 1309 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1306 ARG A NH2 
10533 N N   . ASN B 1310 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1307 ASN A N   
10534 C CA  . ASN B 1310 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1307 ASN A CA  
10535 C C   . ASN B 1310 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1307 ASN A C   
10536 O O   . ASN B 1310 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1307 ASN A O   
10537 C CB  . ASN B 1310 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1307 ASN A CB  
10538 C CG  . ASN B 1310 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1307 ASN A CG  
10539 O OD1 . ASN B 1310 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1307 ASN A OD1 
10540 N ND2 . ASN B 1310 ? 0.6149 0.6149 0.6149 0.0000  0.0000  0.0000  1307 ASN A ND2 
# 
