data_9BE4
# 
_entry.id   9BE4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9BE4         pdb_00009be4 10.2210/pdb9be4/pdb 
WWPDB D_1000283163 ?            ?                   
# 
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 
1 'Structure model' 1 0 2024-11-20 
2 'Structure model' 1 1 2024-12-25 
3 'Structure model' 1 2 2025-02-19 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
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 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
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 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
4 3 'Structure model' citation_author 
# 
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  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.pdbx_database_id_DOI'    
7  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8  2 'Structure model' '_citation.title'                   
9  2 'Structure model' '_citation.year'                    
10 3 'Structure model' '_citation.journal_volume'          
11 3 'Structure model' '_citation.page_first'              
12 3 'Structure model' '_citation.page_last'               
13 3 'Structure model' '_citation.title'                   
14 3 'Structure model' '_citation.year'                    
15 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BE4 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-13 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              martin.schmeing@mcgill.ca 
_pdbx_contact_author.name_first         Thomas 
_pdbx_contact_author.name_last          Schmeing 
_pdbx_contact_author.name_mi            M 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8061-0436 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pistofidis, A.' 1 0000-0002-0969-9730 
'Schmeing, T.M.' 2 0000-0002-8061-0436 
# 
_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            Nature 
_citation.journal_id_ASTM           NATUAS 
_citation.journal_id_CSD            0006 
_citation.journal_id_ISSN           1476-4687 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            638 
_citation.language                  ? 
_citation.page_first                270 
_citation.page_last                 278 
_citation.title                     'Structures and mechanism of condensation in non-ribosomal peptide synthesis.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41586-024-08417-6 
_citation.pdbx_database_id_PubMed   39662504 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Pistofidis, A.' 1 ? 
primary 'Ma, P.'         2 ? 
primary 'Li, Z.'         3 ? 
primary 'Munro, K.'      4 ? 
primary 'Houk, K.N.'     5 ? 
primary 'Schmeing, T.M.' 6 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Linear gramicidin synthase subunit A' 206246.453 2   ? ? ? 
'Complex build by the protein-ligation of the two modules that comprise the first subunit of linear gramicidin synthetase' 
2 non-polymer syn GLYCEROL 92.094     3   ? ? ? ? 
3 non-polymer syn 
;N-formyl-L-valyl-N-[2-({N-[(2S)-2-hydroxy-4-{[(S)-hydroxy(oxo)-lambda~5~-phosphanyl]oxy}-3,3-dimethylbutanoyl]-beta-alanyl}amino)ethyl]glycinamide
;
525.490    1   ? ? ? ? 
4 non-polymer syn 'MANGANESE (II) ION' 54.938     1   ? ? ? ? 
5 water       nat water 18.015     350 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MGRILFLTTFMSKGNKVVRYLESLHHEVVICQEKVHAQSANLQEIDWIVSYAYGYILDKEIVSRFRGRIINLHPSLLPWN
KGRDPVFWSVWDETPKGVTIHLIDEHVDTGDILVQEEIAFADEDTLLDCYNKANQAIEELFIREWENIVHGRIAPYRQTA
GGTLHFKADRDFYKNLNMTTVRELLALKRLCAEPKRGEKPIDKTFHQLFEQQVEMTPDHVAVVDRGQSLTYKQLNERANQ
LAHHLRGKGVKPDDQVAIMLDKSLDMIVSILAVMKAGGAYVPIDPDYPGERIAYMLADSSAAILLTNALHEEKANGACDI
IDVHDPDSYSENTNNLPHVNRPDDLVYVMYTSGSTGLAKGVMIEHHNLVNFCEWYRPYFGVTPADKALVYSSFSFDGSAL
DIFTHLLAGAALHIVPSERKYDLDALNDYCNQEGITISYLPTGAAEQFMQMDNQSFRVVITGGDVLKKIERNGTYKLYNG
YGPTECTIMVTMFEVDKPYANIPIGKPIDRTRILILDEALALQPIGVAGELFIVGEGLGRGYLNRPELTAEKFIVHPQTG
ERMYRTGDRARFLPDGNIEFLGRLDNLVKIRGYRIEPGEIEPFLMNHPLIELTTVLAKEQADGRKYLVGYYVAPEEIPHG
ELREWLGNDLPDYMIPTYFVHMKAFPLTANGKVDRRALPDVQADAELLGEDYVAPTDELEQQLAQVWSHVLGIPQMGIDD
HFLERGGD(4HH)IKVMQLIHQLKNIGLSLRYDQLFTHPTIRQLKRLLTEQKQVNGLLEPLRELDEQAEYETSAVEKRMY
IIQQQDVESIAYNVVYTINFPLTVDTEQIRVALEQLVLRHEGLRSTYHMRGDEIVKRIVPRAELSFVRQTGEEESVQSLL
AEQIKPFDLAKAPLLRAGVIETADKKVLWFDSHHILLDGLSKSILARELQALLGQQVLSPVEKTYKSFARWQNEWFASDE
YEQQIAYWKTLLQGELPAVQLPTKKRPPQLTFDGAIQMYRVNPEITRKLKATAAKHDLTLYMLMLTIVSIWLSKMNSDSN
QVILGTVTDGRQHPDTRELLGMFVNTLPLLLSIDHEESFLHNLQQVKAKLLPALQNQYVPFDKILEAARVKREGNRHPLF
DVMFMMQGAPETELESNMHHINAGISKFDLTLEVLERENGLNIVFEYNTHLFDEGMILRMVAQFEHLLLQAVHGLDQQVK
RFELVTEDEKRDLFLRVNDTAKAYPNKLIMSMLEDWAAATPDKTALVFREQRVTYRELNERVNQLAHTLREKGVQPDDLV
MLMAERSVEMMVAIFAVLKAGGAYLPIDPHSPAERIAYIFADSGAKLVLAQSPFVEKASMAEVVLDLNSASSYAADTSNP
PLVNQPGDLVYVMYTSGSTGKPKGVMIEHGALLNVLHGMQDEYPLLQDDAFLLKTTYIFDISVAEIFGWVPGRGKLVILE
PEAEKNPKAIWQAVVGAGITHINFVPSMLIPFVEYLEGRTEANRLRYILACGEAMPDELVPKVYEVLPEVKLENIYGPTE
ATIYASRYSLAKGSQESPVPIGKPLPNYRMYIINRHGQLQPIGVPGELCIAGASLARGYLNNPALTEEKFTPHPLEKGER
IYRTGDLARYREDGNIEYLGRMDHQVKIRGYRIELDEIRSKLIQEETIQDAVVVARNDQNGQAYLCAYLLSEQEWTVGQL
RELLRRELPEYMIPAHFVLLKQFPLTANGKLDRKALPEPDGSVKAEAEYAAPRTELEATLAHIWGEVLGIERIGIRDNFF
ELGGDSIKGLQIASRLQRINWTMVINHLFLYPTIEQIAPFVTSEQVVIEAAAENLYFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGRILFLTTFMSKGNKVVRYLESLHHEVVICQEKVHAQSANLQEIDWIVSYAYGYILDKEIVSRFRGRIINLHPSLLPWN
KGRDPVFWSVWDETPKGVTIHLIDEHVDTGDILVQEEIAFADEDTLLDCYNKANQAIEELFIREWENIVHGRIAPYRQTA
GGTLHFKADRDFYKNLNMTTVRELLALKRLCAEPKRGEKPIDKTFHQLFEQQVEMTPDHVAVVDRGQSLTYKQLNERANQ
LAHHLRGKGVKPDDQVAIMLDKSLDMIVSILAVMKAGGAYVPIDPDYPGERIAYMLADSSAAILLTNALHEEKANGACDI
IDVHDPDSYSENTNNLPHVNRPDDLVYVMYTSGSTGLAKGVMIEHHNLVNFCEWYRPYFGVTPADKALVYSSFSFDGSAL
DIFTHLLAGAALHIVPSERKYDLDALNDYCNQEGITISYLPTGAAEQFMQMDNQSFRVVITGGDVLKKIERNGTYKLYNG
YGPTECTIMVTMFEVDKPYANIPIGKPIDRTRILILDEALALQPIGVAGELFIVGEGLGRGYLNRPELTAEKFIVHPQTG
ERMYRTGDRARFLPDGNIEFLGRLDNLVKIRGYRIEPGEIEPFLMNHPLIELTTVLAKEQADGRKYLVGYYVAPEEIPHG
ELREWLGNDLPDYMIPTYFVHMKAFPLTANGKVDRRALPDVQADAELLGEDYVAPTDELEQQLAQVWSHVLGIPQMGIDD
HFLERGGDXIKVMQLIHQLKNIGLSLRYDQLFTHPTIRQLKRLLTEQKQVNGLLEPLRELDEQAEYETSAVEKRMYIIQQ
QDVESIAYNVVYTINFPLTVDTEQIRVALEQLVLRHEGLRSTYHMRGDEIVKRIVPRAELSFVRQTGEEESVQSLLAEQI
KPFDLAKAPLLRAGVIETADKKVLWFDSHHILLDGLSKSILARELQALLGQQVLSPVEKTYKSFARWQNEWFASDEYEQQ
IAYWKTLLQGELPAVQLPTKKRPPQLTFDGAIQMYRVNPEITRKLKATAAKHDLTLYMLMLTIVSIWLSKMNSDSNQVIL
GTVTDGRQHPDTRELLGMFVNTLPLLLSIDHEESFLHNLQQVKAKLLPALQNQYVPFDKILEAARVKREGNRHPLFDVMF
MMQGAPETELESNMHHINAGISKFDLTLEVLERENGLNIVFEYNTHLFDEGMILRMVAQFEHLLLQAVHGLDQQVKRFEL
VTEDEKRDLFLRVNDTAKAYPNKLIMSMLEDWAAATPDKTALVFREQRVTYRELNERVNQLAHTLREKGVQPDDLVMLMA
ERSVEMMVAIFAVLKAGGAYLPIDPHSPAERIAYIFADSGAKLVLAQSPFVEKASMAEVVLDLNSASSYAADTSNPPLVN
QPGDLVYVMYTSGSTGKPKGVMIEHGALLNVLHGMQDEYPLLQDDAFLLKTTYIFDISVAEIFGWVPGRGKLVILEPEAE
KNPKAIWQAVVGAGITHINFVPSMLIPFVEYLEGRTEANRLRYILACGEAMPDELVPKVYEVLPEVKLENIYGPTEATIY
ASRYSLAKGSQESPVPIGKPLPNYRMYIINRHGQLQPIGVPGELCIAGASLARGYLNNPALTEEKFTPHPLEKGERIYRT
GDLARYREDGNIEYLGRMDHQVKIRGYRIELDEIRSKLIQEETIQDAVVVARNDQNGQAYLCAYLLSEQEWTVGQLRELL
RRELPEYMIPAHFVLLKQFPLTANGKLDRKALPEPDGSVKAEAEYAAPRTELEATLAHIWGEVLGIERIGIRDNFFELGG
DSIKGLQIASRLQRINWTMVINHLFLYPTIEQIAPFVTSEQVVIEAAAENLYFQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 GLYCEROL GOL   
3 
;N-formyl-L-valyl-N-[2-({N-[(2S)-2-hydroxy-4-{[(S)-hydroxy(oxo)-lambda~5~-phosphanyl]oxy}-3,3-dimethylbutanoyl]-beta-alanyl}amino)ethyl]glycinamide
;
A1AMN 
4 'MANGANESE (II) ION' MN    
5 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    GLY n 
1 3    ARG n 
1 4    ILE n 
1 5    LEU n 
1 6    PHE n 
1 7    LEU n 
1 8    THR n 
1 9    THR n 
1 10   PHE n 
1 11   MET n 
1 12   SER n 
1 13   LYS n 
1 14   GLY n 
1 15   ASN n 
1 16   LYS n 
1 17   VAL n 
1 18   VAL n 
1 19   ARG n 
1 20   TYR n 
1 21   LEU n 
1 22   GLU n 
1 23   SER n 
1 24   LEU n 
1 25   HIS n 
1 26   HIS n 
1 27   GLU n 
1 28   VAL n 
1 29   VAL n 
1 30   ILE n 
1 31   CYS n 
1 32   GLN n 
1 33   GLU n 
1 34   LYS n 
1 35   VAL n 
1 36   HIS n 
1 37   ALA n 
1 38   GLN n 
1 39   SER n 
1 40   ALA n 
1 41   ASN n 
1 42   LEU n 
1 43   GLN n 
1 44   GLU n 
1 45   ILE n 
1 46   ASP n 
1 47   TRP n 
1 48   ILE n 
1 49   VAL n 
1 50   SER n 
1 51   TYR n 
1 52   ALA n 
1 53   TYR n 
1 54   GLY n 
1 55   TYR n 
1 56   ILE n 
1 57   LEU n 
1 58   ASP n 
1 59   LYS n 
1 60   GLU n 
1 61   ILE n 
1 62   VAL n 
1 63   SER n 
1 64   ARG n 
1 65   PHE n 
1 66   ARG n 
1 67   GLY n 
1 68   ARG n 
1 69   ILE n 
1 70   ILE n 
1 71   ASN n 
1 72   LEU n 
1 73   HIS n 
1 74   PRO n 
1 75   SER n 
1 76   LEU n 
1 77   LEU n 
1 78   PRO n 
1 79   TRP n 
1 80   ASN n 
1 81   LYS n 
1 82   GLY n 
1 83   ARG n 
1 84   ASP n 
1 85   PRO n 
1 86   VAL n 
1 87   PHE n 
1 88   TRP n 
1 89   SER n 
1 90   VAL n 
1 91   TRP n 
1 92   ASP n 
1 93   GLU n 
1 94   THR n 
1 95   PRO n 
1 96   LYS n 
1 97   GLY n 
1 98   VAL n 
1 99   THR n 
1 100  ILE n 
1 101  HIS n 
1 102  LEU n 
1 103  ILE n 
1 104  ASP n 
1 105  GLU n 
1 106  HIS n 
1 107  VAL n 
1 108  ASP n 
1 109  THR n 
1 110  GLY n 
1 111  ASP n 
1 112  ILE n 
1 113  LEU n 
1 114  VAL n 
1 115  GLN n 
1 116  GLU n 
1 117  GLU n 
1 118  ILE n 
1 119  ALA n 
1 120  PHE n 
1 121  ALA n 
1 122  ASP n 
1 123  GLU n 
1 124  ASP n 
1 125  THR n 
1 126  LEU n 
1 127  LEU n 
1 128  ASP n 
1 129  CYS n 
1 130  TYR n 
1 131  ASN n 
1 132  LYS n 
1 133  ALA n 
1 134  ASN n 
1 135  GLN n 
1 136  ALA n 
1 137  ILE n 
1 138  GLU n 
1 139  GLU n 
1 140  LEU n 
1 141  PHE n 
1 142  ILE n 
1 143  ARG n 
1 144  GLU n 
1 145  TRP n 
1 146  GLU n 
1 147  ASN n 
1 148  ILE n 
1 149  VAL n 
1 150  HIS n 
1 151  GLY n 
1 152  ARG n 
1 153  ILE n 
1 154  ALA n 
1 155  PRO n 
1 156  TYR n 
1 157  ARG n 
1 158  GLN n 
1 159  THR n 
1 160  ALA n 
1 161  GLY n 
1 162  GLY n 
1 163  THR n 
1 164  LEU n 
1 165  HIS n 
1 166  PHE n 
1 167  LYS n 
1 168  ALA n 
1 169  ASP n 
1 170  ARG n 
1 171  ASP n 
1 172  PHE n 
1 173  TYR n 
1 174  LYS n 
1 175  ASN n 
1 176  LEU n 
1 177  ASN n 
1 178  MET n 
1 179  THR n 
1 180  THR n 
1 181  VAL n 
1 182  ARG n 
1 183  GLU n 
1 184  LEU n 
1 185  LEU n 
1 186  ALA n 
1 187  LEU n 
1 188  LYS n 
1 189  ARG n 
1 190  LEU n 
1 191  CYS n 
1 192  ALA n 
1 193  GLU n 
1 194  PRO n 
1 195  LYS n 
1 196  ARG n 
1 197  GLY n 
1 198  GLU n 
1 199  LYS n 
1 200  PRO n 
1 201  ILE n 
1 202  ASP n 
1 203  LYS n 
1 204  THR n 
1 205  PHE n 
1 206  HIS n 
1 207  GLN n 
1 208  LEU n 
1 209  PHE n 
1 210  GLU n 
1 211  GLN n 
1 212  GLN n 
1 213  VAL n 
1 214  GLU n 
1 215  MET n 
1 216  THR n 
1 217  PRO n 
1 218  ASP n 
1 219  HIS n 
1 220  VAL n 
1 221  ALA n 
1 222  VAL n 
1 223  VAL n 
1 224  ASP n 
1 225  ARG n 
1 226  GLY n 
1 227  GLN n 
1 228  SER n 
1 229  LEU n 
1 230  THR n 
1 231  TYR n 
1 232  LYS n 
1 233  GLN n 
1 234  LEU n 
1 235  ASN n 
1 236  GLU n 
1 237  ARG n 
1 238  ALA n 
1 239  ASN n 
1 240  GLN n 
1 241  LEU n 
1 242  ALA n 
1 243  HIS n 
1 244  HIS n 
1 245  LEU n 
1 246  ARG n 
1 247  GLY n 
1 248  LYS n 
1 249  GLY n 
1 250  VAL n 
1 251  LYS n 
1 252  PRO n 
1 253  ASP n 
1 254  ASP n 
1 255  GLN n 
1 256  VAL n 
1 257  ALA n 
1 258  ILE n 
1 259  MET n 
1 260  LEU n 
1 261  ASP n 
1 262  LYS n 
1 263  SER n 
1 264  LEU n 
1 265  ASP n 
1 266  MET n 
1 267  ILE n 
1 268  VAL n 
1 269  SER n 
1 270  ILE n 
1 271  LEU n 
1 272  ALA n 
1 273  VAL n 
1 274  MET n 
1 275  LYS n 
1 276  ALA n 
1 277  GLY n 
1 278  GLY n 
1 279  ALA n 
1 280  TYR n 
1 281  VAL n 
1 282  PRO n 
1 283  ILE n 
1 284  ASP n 
1 285  PRO n 
1 286  ASP n 
1 287  TYR n 
1 288  PRO n 
1 289  GLY n 
1 290  GLU n 
1 291  ARG n 
1 292  ILE n 
1 293  ALA n 
1 294  TYR n 
1 295  MET n 
1 296  LEU n 
1 297  ALA n 
1 298  ASP n 
1 299  SER n 
1 300  SER n 
1 301  ALA n 
1 302  ALA n 
1 303  ILE n 
1 304  LEU n 
1 305  LEU n 
1 306  THR n 
1 307  ASN n 
1 308  ALA n 
1 309  LEU n 
1 310  HIS n 
1 311  GLU n 
1 312  GLU n 
1 313  LYS n 
1 314  ALA n 
1 315  ASN n 
1 316  GLY n 
1 317  ALA n 
1 318  CYS n 
1 319  ASP n 
1 320  ILE n 
1 321  ILE n 
1 322  ASP n 
1 323  VAL n 
1 324  HIS n 
1 325  ASP n 
1 326  PRO n 
1 327  ASP n 
1 328  SER n 
1 329  TYR n 
1 330  SER n 
1 331  GLU n 
1 332  ASN n 
1 333  THR n 
1 334  ASN n 
1 335  ASN n 
1 336  LEU n 
1 337  PRO n 
1 338  HIS n 
1 339  VAL n 
1 340  ASN n 
1 341  ARG n 
1 342  PRO n 
1 343  ASP n 
1 344  ASP n 
1 345  LEU n 
1 346  VAL n 
1 347  TYR n 
1 348  VAL n 
1 349  MET n 
1 350  TYR n 
1 351  THR n 
1 352  SER n 
1 353  GLY n 
1 354  SER n 
1 355  THR n 
1 356  GLY n 
1 357  LEU n 
1 358  ALA n 
1 359  LYS n 
1 360  GLY n 
1 361  VAL n 
1 362  MET n 
1 363  ILE n 
1 364  GLU n 
1 365  HIS n 
1 366  HIS n 
1 367  ASN n 
1 368  LEU n 
1 369  VAL n 
1 370  ASN n 
1 371  PHE n 
1 372  CYS n 
1 373  GLU n 
1 374  TRP n 
1 375  TYR n 
1 376  ARG n 
1 377  PRO n 
1 378  TYR n 
1 379  PHE n 
1 380  GLY n 
1 381  VAL n 
1 382  THR n 
1 383  PRO n 
1 384  ALA n 
1 385  ASP n 
1 386  LYS n 
1 387  ALA n 
1 388  LEU n 
1 389  VAL n 
1 390  TYR n 
1 391  SER n 
1 392  SER n 
1 393  PHE n 
1 394  SER n 
1 395  PHE n 
1 396  ASP n 
1 397  GLY n 
1 398  SER n 
1 399  ALA n 
1 400  LEU n 
1 401  ASP n 
1 402  ILE n 
1 403  PHE n 
1 404  THR n 
1 405  HIS n 
1 406  LEU n 
1 407  LEU n 
1 408  ALA n 
1 409  GLY n 
1 410  ALA n 
1 411  ALA n 
1 412  LEU n 
1 413  HIS n 
1 414  ILE n 
1 415  VAL n 
1 416  PRO n 
1 417  SER n 
1 418  GLU n 
1 419  ARG n 
1 420  LYS n 
1 421  TYR n 
1 422  ASP n 
1 423  LEU n 
1 424  ASP n 
1 425  ALA n 
1 426  LEU n 
1 427  ASN n 
1 428  ASP n 
1 429  TYR n 
1 430  CYS n 
1 431  ASN n 
1 432  GLN n 
1 433  GLU n 
1 434  GLY n 
1 435  ILE n 
1 436  THR n 
1 437  ILE n 
1 438  SER n 
1 439  TYR n 
1 440  LEU n 
1 441  PRO n 
1 442  THR n 
1 443  GLY n 
1 444  ALA n 
1 445  ALA n 
1 446  GLU n 
1 447  GLN n 
1 448  PHE n 
1 449  MET n 
1 450  GLN n 
1 451  MET n 
1 452  ASP n 
1 453  ASN n 
1 454  GLN n 
1 455  SER n 
1 456  PHE n 
1 457  ARG n 
1 458  VAL n 
1 459  VAL n 
1 460  ILE n 
1 461  THR n 
1 462  GLY n 
1 463  GLY n 
1 464  ASP n 
1 465  VAL n 
1 466  LEU n 
1 467  LYS n 
1 468  LYS n 
1 469  ILE n 
1 470  GLU n 
1 471  ARG n 
1 472  ASN n 
1 473  GLY n 
1 474  THR n 
1 475  TYR n 
1 476  LYS n 
1 477  LEU n 
1 478  TYR n 
1 479  ASN n 
1 480  GLY n 
1 481  TYR n 
1 482  GLY n 
1 483  PRO n 
1 484  THR n 
1 485  GLU n 
1 486  CYS n 
1 487  THR n 
1 488  ILE n 
1 489  MET n 
1 490  VAL n 
1 491  THR n 
1 492  MET n 
1 493  PHE n 
1 494  GLU n 
1 495  VAL n 
1 496  ASP n 
1 497  LYS n 
1 498  PRO n 
1 499  TYR n 
1 500  ALA n 
1 501  ASN n 
1 502  ILE n 
1 503  PRO n 
1 504  ILE n 
1 505  GLY n 
1 506  LYS n 
1 507  PRO n 
1 508  ILE n 
1 509  ASP n 
1 510  ARG n 
1 511  THR n 
1 512  ARG n 
1 513  ILE n 
1 514  LEU n 
1 515  ILE n 
1 516  LEU n 
1 517  ASP n 
1 518  GLU n 
1 519  ALA n 
1 520  LEU n 
1 521  ALA n 
1 522  LEU n 
1 523  GLN n 
1 524  PRO n 
1 525  ILE n 
1 526  GLY n 
1 527  VAL n 
1 528  ALA n 
1 529  GLY n 
1 530  GLU n 
1 531  LEU n 
1 532  PHE n 
1 533  ILE n 
1 534  VAL n 
1 535  GLY n 
1 536  GLU n 
1 537  GLY n 
1 538  LEU n 
1 539  GLY n 
1 540  ARG n 
1 541  GLY n 
1 542  TYR n 
1 543  LEU n 
1 544  ASN n 
1 545  ARG n 
1 546  PRO n 
1 547  GLU n 
1 548  LEU n 
1 549  THR n 
1 550  ALA n 
1 551  GLU n 
1 552  LYS n 
1 553  PHE n 
1 554  ILE n 
1 555  VAL n 
1 556  HIS n 
1 557  PRO n 
1 558  GLN n 
1 559  THR n 
1 560  GLY n 
1 561  GLU n 
1 562  ARG n 
1 563  MET n 
1 564  TYR n 
1 565  ARG n 
1 566  THR n 
1 567  GLY n 
1 568  ASP n 
1 569  ARG n 
1 570  ALA n 
1 571  ARG n 
1 572  PHE n 
1 573  LEU n 
1 574  PRO n 
1 575  ASP n 
1 576  GLY n 
1 577  ASN n 
1 578  ILE n 
1 579  GLU n 
1 580  PHE n 
1 581  LEU n 
1 582  GLY n 
1 583  ARG n 
1 584  LEU n 
1 585  ASP n 
1 586  ASN n 
1 587  LEU n 
1 588  VAL n 
1 589  LYS n 
1 590  ILE n 
1 591  ARG n 
1 592  GLY n 
1 593  TYR n 
1 594  ARG n 
1 595  ILE n 
1 596  GLU n 
1 597  PRO n 
1 598  GLY n 
1 599  GLU n 
1 600  ILE n 
1 601  GLU n 
1 602  PRO n 
1 603  PHE n 
1 604  LEU n 
1 605  MET n 
1 606  ASN n 
1 607  HIS n 
1 608  PRO n 
1 609  LEU n 
1 610  ILE n 
1 611  GLU n 
1 612  LEU n 
1 613  THR n 
1 614  THR n 
1 615  VAL n 
1 616  LEU n 
1 617  ALA n 
1 618  LYS n 
1 619  GLU n 
1 620  GLN n 
1 621  ALA n 
1 622  ASP n 
1 623  GLY n 
1 624  ARG n 
1 625  LYS n 
1 626  TYR n 
1 627  LEU n 
1 628  VAL n 
1 629  GLY n 
1 630  TYR n 
1 631  TYR n 
1 632  VAL n 
1 633  ALA n 
1 634  PRO n 
1 635  GLU n 
1 636  GLU n 
1 637  ILE n 
1 638  PRO n 
1 639  HIS n 
1 640  GLY n 
1 641  GLU n 
1 642  LEU n 
1 643  ARG n 
1 644  GLU n 
1 645  TRP n 
1 646  LEU n 
1 647  GLY n 
1 648  ASN n 
1 649  ASP n 
1 650  LEU n 
1 651  PRO n 
1 652  ASP n 
1 653  TYR n 
1 654  MET n 
1 655  ILE n 
1 656  PRO n 
1 657  THR n 
1 658  TYR n 
1 659  PHE n 
1 660  VAL n 
1 661  HIS n 
1 662  MET n 
1 663  LYS n 
1 664  ALA n 
1 665  PHE n 
1 666  PRO n 
1 667  LEU n 
1 668  THR n 
1 669  ALA n 
1 670  ASN n 
1 671  GLY n 
1 672  LYS n 
1 673  VAL n 
1 674  ASP n 
1 675  ARG n 
1 676  ARG n 
1 677  ALA n 
1 678  LEU n 
1 679  PRO n 
1 680  ASP n 
1 681  VAL n 
1 682  GLN n 
1 683  ALA n 
1 684  ASP n 
1 685  ALA n 
1 686  GLU n 
1 687  LEU n 
1 688  LEU n 
1 689  GLY n 
1 690  GLU n 
1 691  ASP n 
1 692  TYR n 
1 693  VAL n 
1 694  ALA n 
1 695  PRO n 
1 696  THR n 
1 697  ASP n 
1 698  GLU n 
1 699  LEU n 
1 700  GLU n 
1 701  GLN n 
1 702  GLN n 
1 703  LEU n 
1 704  ALA n 
1 705  GLN n 
1 706  VAL n 
1 707  TRP n 
1 708  SER n 
1 709  HIS n 
1 710  VAL n 
1 711  LEU n 
1 712  GLY n 
1 713  ILE n 
1 714  PRO n 
1 715  GLN n 
1 716  MET n 
1 717  GLY n 
1 718  ILE n 
1 719  ASP n 
1 720  ASP n 
1 721  HIS n 
1 722  PHE n 
1 723  LEU n 
1 724  GLU n 
1 725  ARG n 
1 726  GLY n 
1 727  GLY n 
1 728  ASP n 
1 729  4HH n 
1 730  ILE n 
1 731  LYS n 
1 732  VAL n 
1 733  MET n 
1 734  GLN n 
1 735  LEU n 
1 736  ILE n 
1 737  HIS n 
1 738  GLN n 
1 739  LEU n 
1 740  LYS n 
1 741  ASN n 
1 742  ILE n 
1 743  GLY n 
1 744  LEU n 
1 745  SER n 
1 746  LEU n 
1 747  ARG n 
1 748  TYR n 
1 749  ASP n 
1 750  GLN n 
1 751  LEU n 
1 752  PHE n 
1 753  THR n 
1 754  HIS n 
1 755  PRO n 
1 756  THR n 
1 757  ILE n 
1 758  ARG n 
1 759  GLN n 
1 760  LEU n 
1 761  LYS n 
1 762  ARG n 
1 763  LEU n 
1 764  LEU n 
1 765  THR n 
1 766  GLU n 
1 767  GLN n 
1 768  LYS n 
1 769  GLN n 
1 770  VAL n 
1 771  ASN n 
1 772  GLY n 
1 773  LEU n 
1 774  LEU n 
1 775  GLU n 
1 776  PRO n 
1 777  LEU n 
1 778  ARG n 
1 779  GLU n 
1 780  LEU n 
1 781  ASP n 
1 782  GLU n 
1 783  GLN n 
1 784  ALA n 
1 785  GLU n 
1 786  TYR n 
1 787  GLU n 
1 788  THR n 
1 789  SER n 
1 790  ALA n 
1 791  VAL n 
1 792  GLU n 
1 793  LYS n 
1 794  ARG n 
1 795  MET n 
1 796  TYR n 
1 797  ILE n 
1 798  ILE n 
1 799  GLN n 
1 800  GLN n 
1 801  GLN n 
1 802  ASP n 
1 803  VAL n 
1 804  GLU n 
1 805  SER n 
1 806  ILE n 
1 807  ALA n 
1 808  TYR n 
1 809  ASN n 
1 810  VAL n 
1 811  VAL n 
1 812  TYR n 
1 813  THR n 
1 814  ILE n 
1 815  ASN n 
1 816  PHE n 
1 817  PRO n 
1 818  LEU n 
1 819  THR n 
1 820  VAL n 
1 821  ASP n 
1 822  THR n 
1 823  GLU n 
1 824  GLN n 
1 825  ILE n 
1 826  ARG n 
1 827  VAL n 
1 828  ALA n 
1 829  LEU n 
1 830  GLU n 
1 831  GLN n 
1 832  LEU n 
1 833  VAL n 
1 834  LEU n 
1 835  ARG n 
1 836  HIS n 
1 837  GLU n 
1 838  GLY n 
1 839  LEU n 
1 840  ARG n 
1 841  SER n 
1 842  THR n 
1 843  TYR n 
1 844  HIS n 
1 845  MET n 
1 846  ARG n 
1 847  GLY n 
1 848  ASP n 
1 849  GLU n 
1 850  ILE n 
1 851  VAL n 
1 852  LYS n 
1 853  ARG n 
1 854  ILE n 
1 855  VAL n 
1 856  PRO n 
1 857  ARG n 
1 858  ALA n 
1 859  GLU n 
1 860  LEU n 
1 861  SER n 
1 862  PHE n 
1 863  VAL n 
1 864  ARG n 
1 865  GLN n 
1 866  THR n 
1 867  GLY n 
1 868  GLU n 
1 869  GLU n 
1 870  GLU n 
1 871  SER n 
1 872  VAL n 
1 873  GLN n 
1 874  SER n 
1 875  LEU n 
1 876  LEU n 
1 877  ALA n 
1 878  GLU n 
1 879  GLN n 
1 880  ILE n 
1 881  LYS n 
1 882  PRO n 
1 883  PHE n 
1 884  ASP n 
1 885  LEU n 
1 886  ALA n 
1 887  LYS n 
1 888  ALA n 
1 889  PRO n 
1 890  LEU n 
1 891  LEU n 
1 892  ARG n 
1 893  ALA n 
1 894  GLY n 
1 895  VAL n 
1 896  ILE n 
1 897  GLU n 
1 898  THR n 
1 899  ALA n 
1 900  ASP n 
1 901  LYS n 
1 902  LYS n 
1 903  VAL n 
1 904  LEU n 
1 905  TRP n 
1 906  PHE n 
1 907  ASP n 
1 908  SER n 
1 909  HIS n 
1 910  HIS n 
1 911  ILE n 
1 912  LEU n 
1 913  LEU n 
1 914  ASP n 
1 915  GLY n 
1 916  LEU n 
1 917  SER n 
1 918  LYS n 
1 919  SER n 
1 920  ILE n 
1 921  LEU n 
1 922  ALA n 
1 923  ARG n 
1 924  GLU n 
1 925  LEU n 
1 926  GLN n 
1 927  ALA n 
1 928  LEU n 
1 929  LEU n 
1 930  GLY n 
1 931  GLN n 
1 932  GLN n 
1 933  VAL n 
1 934  LEU n 
1 935  SER n 
1 936  PRO n 
1 937  VAL n 
1 938  GLU n 
1 939  LYS n 
1 940  THR n 
1 941  TYR n 
1 942  LYS n 
1 943  SER n 
1 944  PHE n 
1 945  ALA n 
1 946  ARG n 
1 947  TRP n 
1 948  GLN n 
1 949  ASN n 
1 950  GLU n 
1 951  TRP n 
1 952  PHE n 
1 953  ALA n 
1 954  SER n 
1 955  ASP n 
1 956  GLU n 
1 957  TYR n 
1 958  GLU n 
1 959  GLN n 
1 960  GLN n 
1 961  ILE n 
1 962  ALA n 
1 963  TYR n 
1 964  TRP n 
1 965  LYS n 
1 966  THR n 
1 967  LEU n 
1 968  LEU n 
1 969  GLN n 
1 970  GLY n 
1 971  GLU n 
1 972  LEU n 
1 973  PRO n 
1 974  ALA n 
1 975  VAL n 
1 976  GLN n 
1 977  LEU n 
1 978  PRO n 
1 979  THR n 
1 980  LYS n 
1 981  LYS n 
1 982  ARG n 
1 983  PRO n 
1 984  PRO n 
1 985  GLN n 
1 986  LEU n 
1 987  THR n 
1 988  PHE n 
1 989  ASP n 
1 990  GLY n 
1 991  ALA n 
1 992  ILE n 
1 993  GLN n 
1 994  MET n 
1 995  TYR n 
1 996  ARG n 
1 997  VAL n 
1 998  ASN n 
1 999  PRO n 
1 1000 GLU n 
1 1001 ILE n 
1 1002 THR n 
1 1003 ARG n 
1 1004 LYS n 
1 1005 LEU n 
1 1006 LYS n 
1 1007 ALA n 
1 1008 THR n 
1 1009 ALA n 
1 1010 ALA n 
1 1011 LYS n 
1 1012 HIS n 
1 1013 ASP n 
1 1014 LEU n 
1 1015 THR n 
1 1016 LEU n 
1 1017 TYR n 
1 1018 MET n 
1 1019 LEU n 
1 1020 MET n 
1 1021 LEU n 
1 1022 THR n 
1 1023 ILE n 
1 1024 VAL n 
1 1025 SER n 
1 1026 ILE n 
1 1027 TRP n 
1 1028 LEU n 
1 1029 SER n 
1 1030 LYS n 
1 1031 MET n 
1 1032 ASN n 
1 1033 SER n 
1 1034 ASP n 
1 1035 SER n 
1 1036 ASN n 
1 1037 GLN n 
1 1038 VAL n 
1 1039 ILE n 
1 1040 LEU n 
1 1041 GLY n 
1 1042 THR n 
1 1043 VAL n 
1 1044 THR n 
1 1045 ASP n 
1 1046 GLY n 
1 1047 ARG n 
1 1048 GLN n 
1 1049 HIS n 
1 1050 PRO n 
1 1051 ASP n 
1 1052 THR n 
1 1053 ARG n 
1 1054 GLU n 
1 1055 LEU n 
1 1056 LEU n 
1 1057 GLY n 
1 1058 MET n 
1 1059 PHE n 
1 1060 VAL n 
1 1061 ASN n 
1 1062 THR n 
1 1063 LEU n 
1 1064 PRO n 
1 1065 LEU n 
1 1066 LEU n 
1 1067 LEU n 
1 1068 SER n 
1 1069 ILE n 
1 1070 ASP n 
1 1071 HIS n 
1 1072 GLU n 
1 1073 GLU n 
1 1074 SER n 
1 1075 PHE n 
1 1076 LEU n 
1 1077 HIS n 
1 1078 ASN n 
1 1079 LEU n 
1 1080 GLN n 
1 1081 GLN n 
1 1082 VAL n 
1 1083 LYS n 
1 1084 ALA n 
1 1085 LYS n 
1 1086 LEU n 
1 1087 LEU n 
1 1088 PRO n 
1 1089 ALA n 
1 1090 LEU n 
1 1091 GLN n 
1 1092 ASN n 
1 1093 GLN n 
1 1094 TYR n 
1 1095 VAL n 
1 1096 PRO n 
1 1097 PHE n 
1 1098 ASP n 
1 1099 LYS n 
1 1100 ILE n 
1 1101 LEU n 
1 1102 GLU n 
1 1103 ALA n 
1 1104 ALA n 
1 1105 ARG n 
1 1106 VAL n 
1 1107 LYS n 
1 1108 ARG n 
1 1109 GLU n 
1 1110 GLY n 
1 1111 ASN n 
1 1112 ARG n 
1 1113 HIS n 
1 1114 PRO n 
1 1115 LEU n 
1 1116 PHE n 
1 1117 ASP n 
1 1118 VAL n 
1 1119 MET n 
1 1120 PHE n 
1 1121 MET n 
1 1122 MET n 
1 1123 GLN n 
1 1124 GLY n 
1 1125 ALA n 
1 1126 PRO n 
1 1127 GLU n 
1 1128 THR n 
1 1129 GLU n 
1 1130 LEU n 
1 1131 GLU n 
1 1132 SER n 
1 1133 ASN n 
1 1134 MET n 
1 1135 HIS n 
1 1136 HIS n 
1 1137 ILE n 
1 1138 ASN n 
1 1139 ALA n 
1 1140 GLY n 
1 1141 ILE n 
1 1142 SER n 
1 1143 LYS n 
1 1144 PHE n 
1 1145 ASP n 
1 1146 LEU n 
1 1147 THR n 
1 1148 LEU n 
1 1149 GLU n 
1 1150 VAL n 
1 1151 LEU n 
1 1152 GLU n 
1 1153 ARG n 
1 1154 GLU n 
1 1155 ASN n 
1 1156 GLY n 
1 1157 LEU n 
1 1158 ASN n 
1 1159 ILE n 
1 1160 VAL n 
1 1161 PHE n 
1 1162 GLU n 
1 1163 TYR n 
1 1164 ASN n 
1 1165 THR n 
1 1166 HIS n 
1 1167 LEU n 
1 1168 PHE n 
1 1169 ASP n 
1 1170 GLU n 
1 1171 GLY n 
1 1172 MET n 
1 1173 ILE n 
1 1174 LEU n 
1 1175 ARG n 
1 1176 MET n 
1 1177 VAL n 
1 1178 ALA n 
1 1179 GLN n 
1 1180 PHE n 
1 1181 GLU n 
1 1182 HIS n 
1 1183 LEU n 
1 1184 LEU n 
1 1185 LEU n 
1 1186 GLN n 
1 1187 ALA n 
1 1188 VAL n 
1 1189 HIS n 
1 1190 GLY n 
1 1191 LEU n 
1 1192 ASP n 
1 1193 GLN n 
1 1194 GLN n 
1 1195 VAL n 
1 1196 LYS n 
1 1197 ARG n 
1 1198 PHE n 
1 1199 GLU n 
1 1200 LEU n 
1 1201 VAL n 
1 1202 THR n 
1 1203 GLU n 
1 1204 ASP n 
1 1205 GLU n 
1 1206 LYS n 
1 1207 ARG n 
1 1208 ASP n 
1 1209 LEU n 
1 1210 PHE n 
1 1211 LEU n 
1 1212 ARG n 
1 1213 VAL n 
1 1214 ASN n 
1 1215 ASP n 
1 1216 THR n 
1 1217 ALA n 
1 1218 LYS n 
1 1219 ALA n 
1 1220 TYR n 
1 1221 PRO n 
1 1222 ASN n 
1 1223 LYS n 
1 1224 LEU n 
1 1225 ILE n 
1 1226 MET n 
1 1227 SER n 
1 1228 MET n 
1 1229 LEU n 
1 1230 GLU n 
1 1231 ASP n 
1 1232 TRP n 
1 1233 ALA n 
1 1234 ALA n 
1 1235 ALA n 
1 1236 THR n 
1 1237 PRO n 
1 1238 ASP n 
1 1239 LYS n 
1 1240 THR n 
1 1241 ALA n 
1 1242 LEU n 
1 1243 VAL n 
1 1244 PHE n 
1 1245 ARG n 
1 1246 GLU n 
1 1247 GLN n 
1 1248 ARG n 
1 1249 VAL n 
1 1250 THR n 
1 1251 TYR n 
1 1252 ARG n 
1 1253 GLU n 
1 1254 LEU n 
1 1255 ASN n 
1 1256 GLU n 
1 1257 ARG n 
1 1258 VAL n 
1 1259 ASN n 
1 1260 GLN n 
1 1261 LEU n 
1 1262 ALA n 
1 1263 HIS n 
1 1264 THR n 
1 1265 LEU n 
1 1266 ARG n 
1 1267 GLU n 
1 1268 LYS n 
1 1269 GLY n 
1 1270 VAL n 
1 1271 GLN n 
1 1272 PRO n 
1 1273 ASP n 
1 1274 ASP n 
1 1275 LEU n 
1 1276 VAL n 
1 1277 MET n 
1 1278 LEU n 
1 1279 MET n 
1 1280 ALA n 
1 1281 GLU n 
1 1282 ARG n 
1 1283 SER n 
1 1284 VAL n 
1 1285 GLU n 
1 1286 MET n 
1 1287 MET n 
1 1288 VAL n 
1 1289 ALA n 
1 1290 ILE n 
1 1291 PHE n 
1 1292 ALA n 
1 1293 VAL n 
1 1294 LEU n 
1 1295 LYS n 
1 1296 ALA n 
1 1297 GLY n 
1 1298 GLY n 
1 1299 ALA n 
1 1300 TYR n 
1 1301 LEU n 
1 1302 PRO n 
1 1303 ILE n 
1 1304 ASP n 
1 1305 PRO n 
1 1306 HIS n 
1 1307 SER n 
1 1308 PRO n 
1 1309 ALA n 
1 1310 GLU n 
1 1311 ARG n 
1 1312 ILE n 
1 1313 ALA n 
1 1314 TYR n 
1 1315 ILE n 
1 1316 PHE n 
1 1317 ALA n 
1 1318 ASP n 
1 1319 SER n 
1 1320 GLY n 
1 1321 ALA n 
1 1322 LYS n 
1 1323 LEU n 
1 1324 VAL n 
1 1325 LEU n 
1 1326 ALA n 
1 1327 GLN n 
1 1328 SER n 
1 1329 PRO n 
1 1330 PHE n 
1 1331 VAL n 
1 1332 GLU n 
1 1333 LYS n 
1 1334 ALA n 
1 1335 SER n 
1 1336 MET n 
1 1337 ALA n 
1 1338 GLU n 
1 1339 VAL n 
1 1340 VAL n 
1 1341 LEU n 
1 1342 ASP n 
1 1343 LEU n 
1 1344 ASN n 
1 1345 SER n 
1 1346 ALA n 
1 1347 SER n 
1 1348 SER n 
1 1349 TYR n 
1 1350 ALA n 
1 1351 ALA n 
1 1352 ASP n 
1 1353 THR n 
1 1354 SER n 
1 1355 ASN n 
1 1356 PRO n 
1 1357 PRO n 
1 1358 LEU n 
1 1359 VAL n 
1 1360 ASN n 
1 1361 GLN n 
1 1362 PRO n 
1 1363 GLY n 
1 1364 ASP n 
1 1365 LEU n 
1 1366 VAL n 
1 1367 TYR n 
1 1368 VAL n 
1 1369 MET n 
1 1370 TYR n 
1 1371 THR n 
1 1372 SER n 
1 1373 GLY n 
1 1374 SER n 
1 1375 THR n 
1 1376 GLY n 
1 1377 LYS n 
1 1378 PRO n 
1 1379 LYS n 
1 1380 GLY n 
1 1381 VAL n 
1 1382 MET n 
1 1383 ILE n 
1 1384 GLU n 
1 1385 HIS n 
1 1386 GLY n 
1 1387 ALA n 
1 1388 LEU n 
1 1389 LEU n 
1 1390 ASN n 
1 1391 VAL n 
1 1392 LEU n 
1 1393 HIS n 
1 1394 GLY n 
1 1395 MET n 
1 1396 GLN n 
1 1397 ASP n 
1 1398 GLU n 
1 1399 TYR n 
1 1400 PRO n 
1 1401 LEU n 
1 1402 LEU n 
1 1403 GLN n 
1 1404 ASP n 
1 1405 ASP n 
1 1406 ALA n 
1 1407 PHE n 
1 1408 LEU n 
1 1409 LEU n 
1 1410 LYS n 
1 1411 THR n 
1 1412 THR n 
1 1413 TYR n 
1 1414 ILE n 
1 1415 PHE n 
1 1416 ASP n 
1 1417 ILE n 
1 1418 SER n 
1 1419 VAL n 
1 1420 ALA n 
1 1421 GLU n 
1 1422 ILE n 
1 1423 PHE n 
1 1424 GLY n 
1 1425 TRP n 
1 1426 VAL n 
1 1427 PRO n 
1 1428 GLY n 
1 1429 ARG n 
1 1430 GLY n 
1 1431 LYS n 
1 1432 LEU n 
1 1433 VAL n 
1 1434 ILE n 
1 1435 LEU n 
1 1436 GLU n 
1 1437 PRO n 
1 1438 GLU n 
1 1439 ALA n 
1 1440 GLU n 
1 1441 LYS n 
1 1442 ASN n 
1 1443 PRO n 
1 1444 LYS n 
1 1445 ALA n 
1 1446 ILE n 
1 1447 TRP n 
1 1448 GLN n 
1 1449 ALA n 
1 1450 VAL n 
1 1451 VAL n 
1 1452 GLY n 
1 1453 ALA n 
1 1454 GLY n 
1 1455 ILE n 
1 1456 THR n 
1 1457 HIS n 
1 1458 ILE n 
1 1459 ASN n 
1 1460 PHE n 
1 1461 VAL n 
1 1462 PRO n 
1 1463 SER n 
1 1464 MET n 
1 1465 LEU n 
1 1466 ILE n 
1 1467 PRO n 
1 1468 PHE n 
1 1469 VAL n 
1 1470 GLU n 
1 1471 TYR n 
1 1472 LEU n 
1 1473 GLU n 
1 1474 GLY n 
1 1475 ARG n 
1 1476 THR n 
1 1477 GLU n 
1 1478 ALA n 
1 1479 ASN n 
1 1480 ARG n 
1 1481 LEU n 
1 1482 ARG n 
1 1483 TYR n 
1 1484 ILE n 
1 1485 LEU n 
1 1486 ALA n 
1 1487 CYS n 
1 1488 GLY n 
1 1489 GLU n 
1 1490 ALA n 
1 1491 MET n 
1 1492 PRO n 
1 1493 ASP n 
1 1494 GLU n 
1 1495 LEU n 
1 1496 VAL n 
1 1497 PRO n 
1 1498 LYS n 
1 1499 VAL n 
1 1500 TYR n 
1 1501 GLU n 
1 1502 VAL n 
1 1503 LEU n 
1 1504 PRO n 
1 1505 GLU n 
1 1506 VAL n 
1 1507 LYS n 
1 1508 LEU n 
1 1509 GLU n 
1 1510 ASN n 
1 1511 ILE n 
1 1512 TYR n 
1 1513 GLY n 
1 1514 PRO n 
1 1515 THR n 
1 1516 GLU n 
1 1517 ALA n 
1 1518 THR n 
1 1519 ILE n 
1 1520 TYR n 
1 1521 ALA n 
1 1522 SER n 
1 1523 ARG n 
1 1524 TYR n 
1 1525 SER n 
1 1526 LEU n 
1 1527 ALA n 
1 1528 LYS n 
1 1529 GLY n 
1 1530 SER n 
1 1531 GLN n 
1 1532 GLU n 
1 1533 SER n 
1 1534 PRO n 
1 1535 VAL n 
1 1536 PRO n 
1 1537 ILE n 
1 1538 GLY n 
1 1539 LYS n 
1 1540 PRO n 
1 1541 LEU n 
1 1542 PRO n 
1 1543 ASN n 
1 1544 TYR n 
1 1545 ARG n 
1 1546 MET n 
1 1547 TYR n 
1 1548 ILE n 
1 1549 ILE n 
1 1550 ASN n 
1 1551 ARG n 
1 1552 HIS n 
1 1553 GLY n 
1 1554 GLN n 
1 1555 LEU n 
1 1556 GLN n 
1 1557 PRO n 
1 1558 ILE n 
1 1559 GLY n 
1 1560 VAL n 
1 1561 PRO n 
1 1562 GLY n 
1 1563 GLU n 
1 1564 LEU n 
1 1565 CYS n 
1 1566 ILE n 
1 1567 ALA n 
1 1568 GLY n 
1 1569 ALA n 
1 1570 SER n 
1 1571 LEU n 
1 1572 ALA n 
1 1573 ARG n 
1 1574 GLY n 
1 1575 TYR n 
1 1576 LEU n 
1 1577 ASN n 
1 1578 ASN n 
1 1579 PRO n 
1 1580 ALA n 
1 1581 LEU n 
1 1582 THR n 
1 1583 GLU n 
1 1584 GLU n 
1 1585 LYS n 
1 1586 PHE n 
1 1587 THR n 
1 1588 PRO n 
1 1589 HIS n 
1 1590 PRO n 
1 1591 LEU n 
1 1592 GLU n 
1 1593 LYS n 
1 1594 GLY n 
1 1595 GLU n 
1 1596 ARG n 
1 1597 ILE n 
1 1598 TYR n 
1 1599 ARG n 
1 1600 THR n 
1 1601 GLY n 
1 1602 ASP n 
1 1603 LEU n 
1 1604 ALA n 
1 1605 ARG n 
1 1606 TYR n 
1 1607 ARG n 
1 1608 GLU n 
1 1609 ASP n 
1 1610 GLY n 
1 1611 ASN n 
1 1612 ILE n 
1 1613 GLU n 
1 1614 TYR n 
1 1615 LEU n 
1 1616 GLY n 
1 1617 ARG n 
1 1618 MET n 
1 1619 ASP n 
1 1620 HIS n 
1 1621 GLN n 
1 1622 VAL n 
1 1623 LYS n 
1 1624 ILE n 
1 1625 ARG n 
1 1626 GLY n 
1 1627 TYR n 
1 1628 ARG n 
1 1629 ILE n 
1 1630 GLU n 
1 1631 LEU n 
1 1632 ASP n 
1 1633 GLU n 
1 1634 ILE n 
1 1635 ARG n 
1 1636 SER n 
1 1637 LYS n 
1 1638 LEU n 
1 1639 ILE n 
1 1640 GLN n 
1 1641 GLU n 
1 1642 GLU n 
1 1643 THR n 
1 1644 ILE n 
1 1645 GLN n 
1 1646 ASP n 
1 1647 ALA n 
1 1648 VAL n 
1 1649 VAL n 
1 1650 VAL n 
1 1651 ALA n 
1 1652 ARG n 
1 1653 ASN n 
1 1654 ASP n 
1 1655 GLN n 
1 1656 ASN n 
1 1657 GLY n 
1 1658 GLN n 
1 1659 ALA n 
1 1660 TYR n 
1 1661 LEU n 
1 1662 CYS n 
1 1663 ALA n 
1 1664 TYR n 
1 1665 LEU n 
1 1666 LEU n 
1 1667 SER n 
1 1668 GLU n 
1 1669 GLN n 
1 1670 GLU n 
1 1671 TRP n 
1 1672 THR n 
1 1673 VAL n 
1 1674 GLY n 
1 1675 GLN n 
1 1676 LEU n 
1 1677 ARG n 
1 1678 GLU n 
1 1679 LEU n 
1 1680 LEU n 
1 1681 ARG n 
1 1682 ARG n 
1 1683 GLU n 
1 1684 LEU n 
1 1685 PRO n 
1 1686 GLU n 
1 1687 TYR n 
1 1688 MET n 
1 1689 ILE n 
1 1690 PRO n 
1 1691 ALA n 
1 1692 HIS n 
1 1693 PHE n 
1 1694 VAL n 
1 1695 LEU n 
1 1696 LEU n 
1 1697 LYS n 
1 1698 GLN n 
1 1699 PHE n 
1 1700 PRO n 
1 1701 LEU n 
1 1702 THR n 
1 1703 ALA n 
1 1704 ASN n 
1 1705 GLY n 
1 1706 LYS n 
1 1707 LEU n 
1 1708 ASP n 
1 1709 ARG n 
1 1710 LYS n 
1 1711 ALA n 
1 1712 LEU n 
1 1713 PRO n 
1 1714 GLU n 
1 1715 PRO n 
1 1716 ASP n 
1 1717 GLY n 
1 1718 SER n 
1 1719 VAL n 
1 1720 LYS n 
1 1721 ALA n 
1 1722 GLU n 
1 1723 ALA n 
1 1724 GLU n 
1 1725 TYR n 
1 1726 ALA n 
1 1727 ALA n 
1 1728 PRO n 
1 1729 ARG n 
1 1730 THR n 
1 1731 GLU n 
1 1732 LEU n 
1 1733 GLU n 
1 1734 ALA n 
1 1735 THR n 
1 1736 LEU n 
1 1737 ALA n 
1 1738 HIS n 
1 1739 ILE n 
1 1740 TRP n 
1 1741 GLY n 
1 1742 GLU n 
1 1743 VAL n 
1 1744 LEU n 
1 1745 GLY n 
1 1746 ILE n 
1 1747 GLU n 
1 1748 ARG n 
1 1749 ILE n 
1 1750 GLY n 
1 1751 ILE n 
1 1752 ARG n 
1 1753 ASP n 
1 1754 ASN n 
1 1755 PHE n 
1 1756 PHE n 
1 1757 GLU n 
1 1758 LEU n 
1 1759 GLY n 
1 1760 GLY n 
1 1761 ASP n 
1 1762 SER n 
1 1763 ILE n 
1 1764 LYS n 
1 1765 GLY n 
1 1766 LEU n 
1 1767 GLN n 
1 1768 ILE n 
1 1769 ALA n 
1 1770 SER n 
1 1771 ARG n 
1 1772 LEU n 
1 1773 GLN n 
1 1774 ARG n 
1 1775 ILE n 
1 1776 ASN n 
1 1777 TRP n 
1 1778 THR n 
1 1779 MET n 
1 1780 VAL n 
1 1781 ILE n 
1 1782 ASN n 
1 1783 HIS n 
1 1784 LEU n 
1 1785 PHE n 
1 1786 LEU n 
1 1787 TYR n 
1 1788 PRO n 
1 1789 THR n 
1 1790 ILE n 
1 1791 GLU n 
1 1792 GLN n 
1 1793 ILE n 
1 1794 ALA n 
1 1795 PRO n 
1 1796 PHE n 
1 1797 VAL n 
1 1798 THR n 
1 1799 SER n 
1 1800 GLU n 
1 1801 GLN n 
1 1802 VAL n 
1 1803 VAL n 
1 1804 ILE n 
1 1805 GLU n 
1 1806 ALA n 
1 1807 ALA n 
1 1808 ALA n 
1 1809 GLU n 
1 1810 ASN n 
1 1811 LEU n 
1 1812 TYR n 
1 1813 PHE n 
1 1814 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   1814 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 lgrA 
_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      'Brevibacillus parabrevis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     54914 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
4HH   'L-peptide linking' n "4'-phosphopanthetheine-serine" 
'O-[(S)-hydroxy{[(3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl]oxy}phosphoryl]-L-serine' 
'C14 H28 N3 O9 P S' 445.426 
A1AMN non-polymer         . 
;N-formyl-L-valyl-N-[2-({N-[(2S)-2-hydroxy-4-{[(S)-hydroxy(oxo)-lambda~5~-phosphanyl]oxy}-3,3-dimethylbutanoyl]-beta-alanyl}amino)ethyl]glycinamide
;
? 'C19 H36 N5 O10 P'  525.490 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'        133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'      121.158 
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  
GOL   non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'          92.094  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER ? 'H2 O'              18.015  
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 
MN    non-polymer         . 'MANGANESE (II) ION' ? 'Mn 2'              54.938  
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    1    MET MET A . n 
A 1 2    GLY 2    2    2    GLY GLY A . n 
A 1 3    ARG 3    3    3    ARG ARG A . n 
A 1 4    ILE 4    4    4    ILE ILE A . n 
A 1 5    LEU 5    5    5    LEU LEU A . n 
A 1 6    PHE 6    6    6    PHE PHE A . n 
A 1 7    LEU 7    7    7    LEU LEU A . n 
A 1 8    THR 8    8    8    THR THR A . n 
A 1 9    THR 9    9    9    THR THR A . n 
A 1 10   PHE 10   10   10   PHE PHE A . n 
A 1 11   MET 11   11   11   MET MET A . n 
A 1 12   SER 12   12   12   SER SER A . n 
A 1 13   LYS 13   13   13   LYS LYS A . n 
A 1 14   GLY 14   14   14   GLY GLY A . n 
A 1 15   ASN 15   15   15   ASN ASN A . n 
A 1 16   LYS 16   16   16   LYS LYS A . n 
A 1 17   VAL 17   17   17   VAL VAL A . n 
A 1 18   VAL 18   18   18   VAL VAL A . n 
A 1 19   ARG 19   19   19   ARG ARG A . n 
A 1 20   TYR 20   20   20   TYR TYR A . n 
A 1 21   LEU 21   21   21   LEU LEU A . n 
A 1 22   GLU 22   22   22   GLU GLU A . n 
A 1 23   SER 23   23   23   SER SER A . n 
A 1 24   LEU 24   24   24   LEU LEU A . n 
A 1 25   HIS 25   25   25   HIS HIS A . n 
A 1 26   HIS 26   26   26   HIS HIS A . n 
A 1 27   GLU 27   27   27   GLU GLU A . n 
A 1 28   VAL 28   28   28   VAL VAL A . n 
A 1 29   VAL 29   29   29   VAL VAL A . n 
A 1 30   ILE 30   30   30   ILE ILE A . n 
A 1 31   CYS 31   31   31   CYS CYS A . n 
A 1 32   GLN 32   32   32   GLN GLN A . n 
A 1 33   GLU 33   33   33   GLU GLU A . n 
A 1 34   LYS 34   34   34   LYS LYS A . n 
A 1 35   VAL 35   35   35   VAL VAL A . n 
A 1 36   HIS 36   36   36   HIS HIS A . n 
A 1 37   ALA 37   37   37   ALA ALA A . n 
A 1 38   GLN 38   38   38   GLN GLN A . n 
A 1 39   SER 39   39   39   SER SER A . n 
A 1 40   ALA 40   40   40   ALA ALA A . n 
A 1 41   ASN 41   41   41   ASN ASN A . n 
A 1 42   LEU 42   42   42   LEU LEU A . n 
A 1 43   GLN 43   43   43   GLN GLN A . n 
A 1 44   GLU 44   44   44   GLU GLU A . n 
A 1 45   ILE 45   45   45   ILE ILE A . n 
A 1 46   ASP 46   46   46   ASP ASP A . n 
A 1 47   TRP 47   47   47   TRP TRP A . n 
A 1 48   ILE 48   48   48   ILE ILE A . n 
A 1 49   VAL 49   49   49   VAL VAL A . n 
A 1 50   SER 50   50   50   SER SER A . n 
A 1 51   TYR 51   51   51   TYR TYR A . n 
A 1 52   ALA 52   52   52   ALA ALA A . n 
A 1 53   TYR 53   53   53   TYR TYR A . n 
A 1 54   GLY 54   54   54   GLY GLY A . n 
A 1 55   TYR 55   55   55   TYR TYR A . n 
A 1 56   ILE 56   56   56   ILE ILE A . n 
A 1 57   LEU 57   57   57   LEU LEU A . n 
A 1 58   ASP 58   58   58   ASP ASP A . n 
A 1 59   LYS 59   59   59   LYS LYS A . n 
A 1 60   GLU 60   60   60   GLU GLU A . n 
A 1 61   ILE 61   61   61   ILE ILE A . n 
A 1 62   VAL 62   62   62   VAL VAL A . n 
A 1 63   SER 63   63   63   SER SER A . n 
A 1 64   ARG 64   64   64   ARG ARG A . n 
A 1 65   PHE 65   65   65   PHE PHE A . n 
A 1 66   ARG 66   66   66   ARG ARG A . n 
A 1 67   GLY 67   67   67   GLY GLY A . n 
A 1 68   ARG 68   68   68   ARG ARG A . n 
A 1 69   ILE 69   69   69   ILE ILE A . n 
A 1 70   ILE 70   70   70   ILE ILE A . n 
A 1 71   ASN 71   71   71   ASN ASN A . n 
A 1 72   LEU 72   72   72   LEU LEU A . n 
A 1 73   HIS 73   73   73   HIS HIS A . n 
A 1 74   PRO 74   74   74   PRO PRO A . n 
A 1 75   SER 75   75   75   SER SER A . n 
A 1 76   LEU 76   76   76   LEU LEU A . n 
A 1 77   LEU 77   77   77   LEU LEU A . n 
A 1 78   PRO 78   78   78   PRO PRO A . n 
A 1 79   TRP 79   79   79   TRP TRP A . n 
A 1 80   ASN 80   80   80   ASN ASN A . n 
A 1 81   LYS 81   81   81   LYS LYS A . n 
A 1 82   GLY 82   82   82   GLY GLY A . n 
A 1 83   ARG 83   83   83   ARG ARG A . n 
A 1 84   ASP 84   84   84   ASP ASP A . n 
A 1 85   PRO 85   85   85   PRO PRO A . n 
A 1 86   VAL 86   86   86   VAL VAL A . n 
A 1 87   PHE 87   87   87   PHE PHE A . n 
A 1 88   TRP 88   88   88   TRP TRP A . n 
A 1 89   SER 89   89   89   SER SER A . n 
A 1 90   VAL 90   90   90   VAL VAL A . n 
A 1 91   TRP 91   91   91   TRP TRP A . n 
A 1 92   ASP 92   92   92   ASP ASP A . n 
A 1 93   GLU 93   93   93   GLU GLU A . n 
A 1 94   THR 94   94   94   THR THR A . n 
A 1 95   PRO 95   95   95   PRO PRO A . n 
A 1 96   LYS 96   96   96   LYS LYS A . n 
A 1 97   GLY 97   97   97   GLY GLY A . n 
A 1 98   VAL 98   98   98   VAL VAL A . n 
A 1 99   THR 99   99   99   THR THR A . n 
A 1 100  ILE 100  100  100  ILE ILE A . n 
A 1 101  HIS 101  101  101  HIS HIS A . n 
A 1 102  LEU 102  102  102  LEU LEU A . n 
A 1 103  ILE 103  103  103  ILE ILE A . n 
A 1 104  ASP 104  104  104  ASP ASP A . n 
A 1 105  GLU 105  105  105  GLU GLU A . n 
A 1 106  HIS 106  106  106  HIS HIS A . n 
A 1 107  VAL 107  107  107  VAL VAL A . n 
A 1 108  ASP 108  108  108  ASP ASP A . n 
A 1 109  THR 109  109  109  THR THR A . n 
A 1 110  GLY 110  110  110  GLY GLY A . n 
A 1 111  ASP 111  111  111  ASP ASP A . n 
A 1 112  ILE 112  112  112  ILE ILE A . n 
A 1 113  LEU 113  113  113  LEU LEU A . n 
A 1 114  VAL 114  114  114  VAL VAL A . n 
A 1 115  GLN 115  115  115  GLN GLN A . n 
A 1 116  GLU 116  116  116  GLU GLU A . n 
A 1 117  GLU 117  117  117  GLU GLU A . n 
A 1 118  ILE 118  118  118  ILE ILE A . n 
A 1 119  ALA 119  119  119  ALA ALA A . n 
A 1 120  PHE 120  120  120  PHE PHE A . n 
A 1 121  ALA 121  121  121  ALA ALA A . n 
A 1 122  ASP 122  122  122  ASP ASP A . n 
A 1 123  GLU 123  123  123  GLU GLU A . n 
A 1 124  ASP 124  124  124  ASP ASP A . n 
A 1 125  THR 125  125  125  THR THR A . n 
A 1 126  LEU 126  126  126  LEU LEU A . n 
A 1 127  LEU 127  127  127  LEU LEU A . n 
A 1 128  ASP 128  128  128  ASP ASP A . n 
A 1 129  CYS 129  129  129  CYS CYS A . n 
A 1 130  TYR 130  130  130  TYR TYR A . n 
A 1 131  ASN 131  131  131  ASN ASN A . n 
A 1 132  LYS 132  132  132  LYS LYS A . n 
A 1 133  ALA 133  133  133  ALA ALA A . n 
A 1 134  ASN 134  134  134  ASN ASN A . n 
A 1 135  GLN 135  135  135  GLN GLN A . n 
A 1 136  ALA 136  136  136  ALA ALA A . n 
A 1 137  ILE 137  137  137  ILE ILE A . n 
A 1 138  GLU 138  138  138  GLU GLU A . n 
A 1 139  GLU 139  139  139  GLU GLU A . n 
A 1 140  LEU 140  140  140  LEU LEU A . n 
A 1 141  PHE 141  141  141  PHE PHE A . n 
A 1 142  ILE 142  142  142  ILE ILE A . n 
A 1 143  ARG 143  143  143  ARG ARG A . n 
A 1 144  GLU 144  144  144  GLU GLU A . n 
A 1 145  TRP 145  145  145  TRP TRP A . n 
A 1 146  GLU 146  146  146  GLU GLU A . n 
A 1 147  ASN 147  147  147  ASN ASN A . n 
A 1 148  ILE 148  148  148  ILE ILE A . n 
A 1 149  VAL 149  149  149  VAL VAL A . n 
A 1 150  HIS 150  150  150  HIS HIS A . n 
A 1 151  GLY 151  151  151  GLY GLY A . n 
A 1 152  ARG 152  152  152  ARG ARG A . n 
A 1 153  ILE 153  153  153  ILE ILE A . n 
A 1 154  ALA 154  154  154  ALA ALA A . n 
A 1 155  PRO 155  155  155  PRO PRO A . n 
A 1 156  TYR 156  156  156  TYR TYR A . n 
A 1 157  ARG 157  157  157  ARG ARG A . n 
A 1 158  GLN 158  158  158  GLN GLN A . n 
A 1 159  THR 159  159  159  THR THR A . n 
A 1 160  ALA 160  160  160  ALA ALA A . n 
A 1 161  GLY 161  161  161  GLY GLY A . n 
A 1 162  GLY 162  162  162  GLY GLY A . n 
A 1 163  THR 163  163  163  THR THR A . n 
A 1 164  LEU 164  164  164  LEU LEU A . n 
A 1 165  HIS 165  165  165  HIS HIS A . n 
A 1 166  PHE 166  166  166  PHE PHE A . n 
A 1 167  LYS 167  167  167  LYS LYS A . n 
A 1 168  ALA 168  168  168  ALA ALA A . n 
A 1 169  ASP 169  169  169  ASP ASP A . n 
A 1 170  ARG 170  170  170  ARG ARG A . n 
A 1 171  ASP 171  171  171  ASP ASP A . n 
A 1 172  PHE 172  172  172  PHE PHE A . n 
A 1 173  TYR 173  173  173  TYR TYR A . n 
A 1 174  LYS 174  174  174  LYS LYS A . n 
A 1 175  ASN 175  175  175  ASN ASN A . n 
A 1 176  LEU 176  176  176  LEU LEU A . n 
A 1 177  ASN 177  177  177  ASN ASN A . n 
A 1 178  MET 178  178  178  MET MET A . n 
A 1 179  THR 179  179  179  THR THR A . n 
A 1 180  THR 180  180  180  THR THR A . n 
A 1 181  VAL 181  181  181  VAL VAL A . n 
A 1 182  ARG 182  182  182  ARG ARG A . n 
A 1 183  GLU 183  183  183  GLU GLU A . n 
A 1 184  LEU 184  184  184  LEU LEU A . n 
A 1 185  LEU 185  185  185  LEU LEU A . n 
A 1 186  ALA 186  186  186  ALA ALA A . n 
A 1 187  LEU 187  187  187  LEU LEU A . n 
A 1 188  LYS 188  188  188  LYS LYS A . n 
A 1 189  ARG 189  189  189  ARG ARG A . n 
A 1 190  LEU 190  190  190  LEU LEU A . n 
A 1 191  CYS 191  191  191  CYS CYS A . n 
A 1 192  ALA 192  192  192  ALA ALA A . n 
A 1 193  GLU 193  193  193  GLU GLU A . n 
A 1 194  PRO 194  194  194  PRO PRO A . n 
A 1 195  LYS 195  195  195  LYS LYS A . n 
A 1 196  ARG 196  196  ?    ?   ?   A . n 
A 1 197  GLY 197  197  ?    ?   ?   A . n 
A 1 198  GLU 198  198  198  GLU GLU A . n 
A 1 199  LYS 199  199  199  LYS LYS A . n 
A 1 200  PRO 200  200  200  PRO PRO A . n 
A 1 201  ILE 201  201  201  ILE ILE A . n 
A 1 202  ASP 202  202  202  ASP ASP A . n 
A 1 203  LYS 203  203  203  LYS LYS A . n 
A 1 204  THR 204  204  204  THR THR A . n 
A 1 205  PHE 205  205  205  PHE PHE A . n 
A 1 206  HIS 206  206  206  HIS HIS A . n 
A 1 207  GLN 207  207  207  GLN GLN A . n 
A 1 208  LEU 208  208  208  LEU LEU A . n 
A 1 209  PHE 209  209  209  PHE PHE A . n 
A 1 210  GLU 210  210  210  GLU GLU A . n 
A 1 211  GLN 211  211  211  GLN GLN A . n 
A 1 212  GLN 212  212  212  GLN GLN A . n 
A 1 213  VAL 213  213  213  VAL VAL A . n 
A 1 214  GLU 214  214  214  GLU GLU A . n 
A 1 215  MET 215  215  215  MET MET A . n 
A 1 216  THR 216  216  216  THR THR A . n 
A 1 217  PRO 217  217  217  PRO PRO A . n 
A 1 218  ASP 218  218  218  ASP ASP A . n 
A 1 219  HIS 219  219  219  HIS HIS A . n 
A 1 220  VAL 220  220  220  VAL VAL A . n 
A 1 221  ALA 221  221  221  ALA ALA A . n 
A 1 222  VAL 222  222  222  VAL VAL A . n 
A 1 223  VAL 223  223  223  VAL VAL A . n 
A 1 224  ASP 224  224  224  ASP ASP A . n 
A 1 225  ARG 225  225  225  ARG ARG A . n 
A 1 226  GLY 226  226  226  GLY GLY A . n 
A 1 227  GLN 227  227  227  GLN GLN A . n 
A 1 228  SER 228  228  228  SER SER A . n 
A 1 229  LEU 229  229  229  LEU LEU A . n 
A 1 230  THR 230  230  230  THR THR A . n 
A 1 231  TYR 231  231  231  TYR TYR A . n 
A 1 232  LYS 232  232  232  LYS LYS A . n 
A 1 233  GLN 233  233  233  GLN GLN A . n 
A 1 234  LEU 234  234  234  LEU LEU A . n 
A 1 235  ASN 235  235  235  ASN ASN A . n 
A 1 236  GLU 236  236  236  GLU GLU A . n 
A 1 237  ARG 237  237  237  ARG ARG A . n 
A 1 238  ALA 238  238  238  ALA ALA A . n 
A 1 239  ASN 239  239  239  ASN ASN A . n 
A 1 240  GLN 240  240  240  GLN GLN A . n 
A 1 241  LEU 241  241  241  LEU LEU A . n 
A 1 242  ALA 242  242  242  ALA ALA A . n 
A 1 243  HIS 243  243  243  HIS HIS A . n 
A 1 244  HIS 244  244  244  HIS HIS A . n 
A 1 245  LEU 245  245  245  LEU LEU A . n 
A 1 246  ARG 246  246  246  ARG ARG A . n 
A 1 247  GLY 247  247  247  GLY GLY A . n 
A 1 248  LYS 248  248  248  LYS LYS A . n 
A 1 249  GLY 249  249  249  GLY GLY A . n 
A 1 250  VAL 250  250  250  VAL VAL A . n 
A 1 251  LYS 251  251  251  LYS LYS A . n 
A 1 252  PRO 252  252  252  PRO PRO A . n 
A 1 253  ASP 253  253  253  ASP ASP A . n 
A 1 254  ASP 254  254  254  ASP ASP A . n 
A 1 255  GLN 255  255  255  GLN GLN A . n 
A 1 256  VAL 256  256  256  VAL VAL A . n 
A 1 257  ALA 257  257  257  ALA ALA A . n 
A 1 258  ILE 258  258  258  ILE ILE A . n 
A 1 259  MET 259  259  259  MET MET A . n 
A 1 260  LEU 260  260  260  LEU LEU A . n 
A 1 261  ASP 261  261  261  ASP ASP A . n 
A 1 262  LYS 262  262  262  LYS LYS A . n 
A 1 263  SER 263  263  263  SER SER A . n 
A 1 264  LEU 264  264  264  LEU LEU A . n 
A 1 265  ASP 265  265  265  ASP ASP A . n 
A 1 266  MET 266  266  266  MET MET A . n 
A 1 267  ILE 267  267  267  ILE ILE A . n 
A 1 268  VAL 268  268  268  VAL VAL A . n 
A 1 269  SER 269  269  269  SER SER A . n 
A 1 270  ILE 270  270  270  ILE ILE A . n 
A 1 271  LEU 271  271  271  LEU LEU A . n 
A 1 272  ALA 272  272  272  ALA ALA A . n 
A 1 273  VAL 273  273  273  VAL VAL A . n 
A 1 274  MET 274  274  274  MET MET A . n 
A 1 275  LYS 275  275  275  LYS LYS A . n 
A 1 276  ALA 276  276  276  ALA ALA A . n 
A 1 277  GLY 277  277  277  GLY GLY A . n 
A 1 278  GLY 278  278  278  GLY GLY A . n 
A 1 279  ALA 279  279  279  ALA ALA A . n 
A 1 280  TYR 280  280  280  TYR TYR A . n 
A 1 281  VAL 281  281  281  VAL VAL A . n 
A 1 282  PRO 282  282  282  PRO PRO A . n 
A 1 283  ILE 283  283  283  ILE ILE A . n 
A 1 284  ASP 284  284  284  ASP ASP A . n 
A 1 285  PRO 285  285  285  PRO PRO A . n 
A 1 286  ASP 286  286  286  ASP ASP A . n 
A 1 287  TYR 287  287  287  TYR TYR A . n 
A 1 288  PRO 288  288  288  PRO PRO A . n 
A 1 289  GLY 289  289  289  GLY GLY A . n 
A 1 290  GLU 290  290  290  GLU GLU A . n 
A 1 291  ARG 291  291  291  ARG ARG A . n 
A 1 292  ILE 292  292  292  ILE ILE A . n 
A 1 293  ALA 293  293  293  ALA ALA A . n 
A 1 294  TYR 294  294  294  TYR TYR A . n 
A 1 295  MET 295  295  295  MET MET A . n 
A 1 296  LEU 296  296  296  LEU LEU A . n 
A 1 297  ALA 297  297  297  ALA ALA A . n 
A 1 298  ASP 298  298  298  ASP ASP A . n 
A 1 299  SER 299  299  299  SER SER A . n 
A 1 300  SER 300  300  300  SER SER A . n 
A 1 301  ALA 301  301  301  ALA ALA A . n 
A 1 302  ALA 302  302  302  ALA ALA A . n 
A 1 303  ILE 303  303  303  ILE ILE A . n 
A 1 304  LEU 304  304  304  LEU LEU A . n 
A 1 305  LEU 305  305  305  LEU LEU A . n 
A 1 306  THR 306  306  306  THR THR A . n 
A 1 307  ASN 307  307  307  ASN ASN A . n 
A 1 308  ALA 308  308  308  ALA ALA A . n 
A 1 309  LEU 309  309  309  LEU LEU A . n 
A 1 310  HIS 310  310  310  HIS HIS A . n 
A 1 311  GLU 311  311  311  GLU GLU A . n 
A 1 312  GLU 312  312  312  GLU GLU A . n 
A 1 313  LYS 313  313  313  LYS LYS A . n 
A 1 314  ALA 314  314  314  ALA ALA A . n 
A 1 315  ASN 315  315  315  ASN ASN A . n 
A 1 316  GLY 316  316  316  GLY GLY A . n 
A 1 317  ALA 317  317  317  ALA ALA A . n 
A 1 318  CYS 318  318  318  CYS CYS A . n 
A 1 319  ASP 319  319  319  ASP ASP A . n 
A 1 320  ILE 320  320  320  ILE ILE A . n 
A 1 321  ILE 321  321  321  ILE ILE A . n 
A 1 322  ASP 322  322  322  ASP ASP A . n 
A 1 323  VAL 323  323  323  VAL VAL A . n 
A 1 324  HIS 324  324  324  HIS HIS A . n 
A 1 325  ASP 325  325  325  ASP ASP A . n 
A 1 326  PRO 326  326  326  PRO PRO A . n 
A 1 327  ASP 327  327  327  ASP ASP A . n 
A 1 328  SER 328  328  328  SER SER A . n 
A 1 329  TYR 329  329  329  TYR TYR A . n 
A 1 330  SER 330  330  330  SER SER A . n 
A 1 331  GLU 331  331  331  GLU GLU A . n 
A 1 332  ASN 332  332  332  ASN ASN A . n 
A 1 333  THR 333  333  333  THR THR A . n 
A 1 334  ASN 334  334  334  ASN ASN A . n 
A 1 335  ASN 335  335  335  ASN ASN A . n 
A 1 336  LEU 336  336  336  LEU LEU A . n 
A 1 337  PRO 337  337  337  PRO PRO A . n 
A 1 338  HIS 338  338  338  HIS HIS A . n 
A 1 339  VAL 339  339  339  VAL VAL A . n 
A 1 340  ASN 340  340  340  ASN ASN A . n 
A 1 341  ARG 341  341  341  ARG ARG A . n 
A 1 342  PRO 342  342  342  PRO PRO A . n 
A 1 343  ASP 343  343  343  ASP ASP A . n 
A 1 344  ASP 344  344  344  ASP ASP A . n 
A 1 345  LEU 345  345  345  LEU LEU A . n 
A 1 346  VAL 346  346  346  VAL VAL A . n 
A 1 347  TYR 347  347  347  TYR TYR A . n 
A 1 348  VAL 348  348  348  VAL VAL A . n 
A 1 349  MET 349  349  349  MET MET A . n 
A 1 350  TYR 350  350  350  TYR TYR A . n 
A 1 351  THR 351  351  351  THR THR A . n 
A 1 352  SER 352  352  352  SER SER A . n 
A 1 353  GLY 353  353  353  GLY GLY A . n 
A 1 354  SER 354  354  354  SER SER A . n 
A 1 355  THR 355  355  ?    ?   ?   A . n 
A 1 356  GLY 356  356  ?    ?   ?   A . n 
A 1 357  LEU 357  357  357  LEU LEU A . n 
A 1 358  ALA 358  358  358  ALA ALA A . n 
A 1 359  LYS 359  359  359  LYS LYS A . n 
A 1 360  GLY 360  360  360  GLY GLY A . n 
A 1 361  VAL 361  361  361  VAL VAL A . n 
A 1 362  MET 362  362  362  MET MET A . n 
A 1 363  ILE 363  363  363  ILE ILE A . n 
A 1 364  GLU 364  364  364  GLU GLU A . n 
A 1 365  HIS 365  365  365  HIS HIS A . n 
A 1 366  HIS 366  366  366  HIS HIS A . n 
A 1 367  ASN 367  367  367  ASN ASN A . n 
A 1 368  LEU 368  368  368  LEU LEU A . n 
A 1 369  VAL 369  369  369  VAL VAL A . n 
A 1 370  ASN 370  370  370  ASN ASN A . n 
A 1 371  PHE 371  371  371  PHE PHE A . n 
A 1 372  CYS 372  372  372  CYS CYS A . n 
A 1 373  GLU 373  373  373  GLU GLU A . n 
A 1 374  TRP 374  374  374  TRP TRP A . n 
A 1 375  TYR 375  375  375  TYR TYR A . n 
A 1 376  ARG 376  376  376  ARG ARG A . n 
A 1 377  PRO 377  377  377  PRO PRO A . n 
A 1 378  TYR 378  378  378  TYR TYR A . n 
A 1 379  PHE 379  379  379  PHE PHE A . n 
A 1 380  GLY 380  380  380  GLY GLY A . n 
A 1 381  VAL 381  381  381  VAL VAL A . n 
A 1 382  THR 382  382  382  THR THR A . n 
A 1 383  PRO 383  383  383  PRO PRO A . n 
A 1 384  ALA 384  384  384  ALA ALA A . n 
A 1 385  ASP 385  385  385  ASP ASP A . n 
A 1 386  LYS 386  386  386  LYS LYS A . n 
A 1 387  ALA 387  387  387  ALA ALA A . n 
A 1 388  LEU 388  388  388  LEU LEU A . n 
A 1 389  VAL 389  389  389  VAL VAL A . n 
A 1 390  TYR 390  390  390  TYR TYR A . n 
A 1 391  SER 391  391  391  SER SER A . n 
A 1 392  SER 392  392  392  SER SER A . n 
A 1 393  PHE 393  393  393  PHE PHE A . n 
A 1 394  SER 394  394  394  SER SER A . n 
A 1 395  PHE 395  395  395  PHE PHE A . n 
A 1 396  ASP 396  396  396  ASP ASP A . n 
A 1 397  GLY 397  397  397  GLY GLY A . n 
A 1 398  SER 398  398  398  SER SER A . n 
A 1 399  ALA 399  399  399  ALA ALA A . n 
A 1 400  LEU 400  400  400  LEU LEU A . n 
A 1 401  ASP 401  401  401  ASP ASP A . n 
A 1 402  ILE 402  402  402  ILE ILE A . n 
A 1 403  PHE 403  403  403  PHE PHE A . n 
A 1 404  THR 404  404  404  THR THR A . n 
A 1 405  HIS 405  405  405  HIS HIS A . n 
A 1 406  LEU 406  406  406  LEU LEU A . n 
A 1 407  LEU 407  407  407  LEU LEU A . n 
A 1 408  ALA 408  408  408  ALA ALA A . n 
A 1 409  GLY 409  409  409  GLY GLY A . n 
A 1 410  ALA 410  410  410  ALA ALA A . n 
A 1 411  ALA 411  411  411  ALA ALA A . n 
A 1 412  LEU 412  412  412  LEU LEU A . n 
A 1 413  HIS 413  413  413  HIS HIS A . n 
A 1 414  ILE 414  414  414  ILE ILE A . n 
A 1 415  VAL 415  415  415  VAL VAL A . n 
A 1 416  PRO 416  416  416  PRO PRO A . n 
A 1 417  SER 417  417  417  SER SER A . n 
A 1 418  GLU 418  418  418  GLU GLU A . n 
A 1 419  ARG 419  419  419  ARG ARG A . n 
A 1 420  LYS 420  420  420  LYS LYS A . n 
A 1 421  TYR 421  421  421  TYR TYR A . n 
A 1 422  ASP 422  422  422  ASP ASP A . n 
A 1 423  LEU 423  423  423  LEU LEU A . n 
A 1 424  ASP 424  424  424  ASP ASP A . n 
A 1 425  ALA 425  425  425  ALA ALA A . n 
A 1 426  LEU 426  426  426  LEU LEU A . n 
A 1 427  ASN 427  427  427  ASN ASN A . n 
A 1 428  ASP 428  428  428  ASP ASP A . n 
A 1 429  TYR 429  429  429  TYR TYR A . n 
A 1 430  CYS 430  430  430  CYS CYS A . n 
A 1 431  ASN 431  431  431  ASN ASN A . n 
A 1 432  GLN 432  432  432  GLN GLN A . n 
A 1 433  GLU 433  433  433  GLU GLU A . n 
A 1 434  GLY 434  434  434  GLY GLY A . n 
A 1 435  ILE 435  435  435  ILE ILE A . n 
A 1 436  THR 436  436  436  THR THR A . n 
A 1 437  ILE 437  437  437  ILE ILE A . n 
A 1 438  SER 438  438  438  SER SER A . n 
A 1 439  TYR 439  439  439  TYR TYR A . n 
A 1 440  LEU 440  440  440  LEU LEU A . n 
A 1 441  PRO 441  441  441  PRO PRO A . n 
A 1 442  THR 442  442  442  THR THR A . n 
A 1 443  GLY 443  443  443  GLY GLY A . n 
A 1 444  ALA 444  444  444  ALA ALA A . n 
A 1 445  ALA 445  445  445  ALA ALA A . n 
A 1 446  GLU 446  446  446  GLU GLU A . n 
A 1 447  GLN 447  447  447  GLN GLN A . n 
A 1 448  PHE 448  448  448  PHE PHE A . n 
A 1 449  MET 449  449  449  MET MET A . n 
A 1 450  GLN 450  450  450  GLN GLN A . n 
A 1 451  MET 451  451  451  MET MET A . n 
A 1 452  ASP 452  452  452  ASP ASP A . n 
A 1 453  ASN 453  453  453  ASN ASN A . n 
A 1 454  GLN 454  454  454  GLN GLN A . n 
A 1 455  SER 455  455  455  SER SER A . n 
A 1 456  PHE 456  456  456  PHE PHE A . n 
A 1 457  ARG 457  457  457  ARG ARG A . n 
A 1 458  VAL 458  458  458  VAL VAL A . n 
A 1 459  VAL 459  459  459  VAL VAL A . n 
A 1 460  ILE 460  460  460  ILE ILE A . n 
A 1 461  THR 461  461  461  THR THR A . n 
A 1 462  GLY 462  462  462  GLY GLY A . n 
A 1 463  GLY 463  463  463  GLY GLY A . n 
A 1 464  ASP 464  464  464  ASP ASP A . n 
A 1 465  VAL 465  465  465  VAL VAL A . n 
A 1 466  LEU 466  466  466  LEU LEU A . n 
A 1 467  LYS 467  467  467  LYS LYS A . n 
A 1 468  LYS 468  468  468  LYS LYS A . n 
A 1 469  ILE 469  469  469  ILE ILE A . n 
A 1 470  GLU 470  470  470  GLU GLU A . n 
A 1 471  ARG 471  471  471  ARG ARG A . n 
A 1 472  ASN 472  472  472  ASN ASN A . n 
A 1 473  GLY 473  473  473  GLY GLY A . n 
A 1 474  THR 474  474  474  THR THR A . n 
A 1 475  TYR 475  475  475  TYR TYR A . n 
A 1 476  LYS 476  476  476  LYS LYS A . n 
A 1 477  LEU 477  477  477  LEU LEU A . n 
A 1 478  TYR 478  478  478  TYR TYR A . n 
A 1 479  ASN 479  479  479  ASN ASN A . n 
A 1 480  GLY 480  480  480  GLY GLY A . n 
A 1 481  TYR 481  481  481  TYR TYR A . n 
A 1 482  GLY 482  482  482  GLY GLY A . n 
A 1 483  PRO 483  483  483  PRO PRO A . n 
A 1 484  THR 484  484  484  THR THR A . n 
A 1 485  GLU 485  485  485  GLU GLU A . n 
A 1 486  CYS 486  486  486  CYS CYS A . n 
A 1 487  THR 487  487  487  THR THR A . n 
A 1 488  ILE 488  488  488  ILE ILE A . n 
A 1 489  MET 489  489  489  MET MET A . n 
A 1 490  VAL 490  490  490  VAL VAL A . n 
A 1 491  THR 491  491  491  THR THR A . n 
A 1 492  MET 492  492  492  MET MET A . n 
A 1 493  PHE 493  493  493  PHE PHE A . n 
A 1 494  GLU 494  494  494  GLU GLU A . n 
A 1 495  VAL 495  495  495  VAL VAL A . n 
A 1 496  ASP 496  496  496  ASP ASP A . n 
A 1 497  LYS 497  497  497  LYS LYS A . n 
A 1 498  PRO 498  498  498  PRO PRO A . n 
A 1 499  TYR 499  499  499  TYR TYR A . n 
A 1 500  ALA 500  500  500  ALA ALA A . n 
A 1 501  ASN 501  501  501  ASN ASN A . n 
A 1 502  ILE 502  502  502  ILE ILE A . n 
A 1 503  PRO 503  503  503  PRO PRO A . n 
A 1 504  ILE 504  504  504  ILE ILE A . n 
A 1 505  GLY 505  505  505  GLY GLY A . n 
A 1 506  LYS 506  506  506  LYS LYS A . n 
A 1 507  PRO 507  507  507  PRO PRO A . n 
A 1 508  ILE 508  508  508  ILE ILE A . n 
A 1 509  ASP 509  509  509  ASP ASP A . n 
A 1 510  ARG 510  510  510  ARG ARG A . n 
A 1 511  THR 511  511  511  THR THR A . n 
A 1 512  ARG 512  512  512  ARG ARG A . n 
A 1 513  ILE 513  513  513  ILE ILE A . n 
A 1 514  LEU 514  514  514  LEU LEU A . n 
A 1 515  ILE 515  515  515  ILE ILE A . n 
A 1 516  LEU 516  516  516  LEU LEU A . n 
A 1 517  ASP 517  517  517  ASP ASP A . n 
A 1 518  GLU 518  518  518  GLU GLU A . n 
A 1 519  ALA 519  519  519  ALA ALA A . n 
A 1 520  LEU 520  520  520  LEU LEU A . n 
A 1 521  ALA 521  521  521  ALA ALA A . n 
A 1 522  LEU 522  522  522  LEU LEU A . n 
A 1 523  GLN 523  523  523  GLN GLN A . n 
A 1 524  PRO 524  524  524  PRO PRO A . n 
A 1 525  ILE 525  525  525  ILE ILE A . n 
A 1 526  GLY 526  526  526  GLY GLY A . n 
A 1 527  VAL 527  527  527  VAL VAL A . n 
A 1 528  ALA 528  528  528  ALA ALA A . n 
A 1 529  GLY 529  529  529  GLY GLY A . n 
A 1 530  GLU 530  530  530  GLU GLU A . n 
A 1 531  LEU 531  531  531  LEU LEU A . n 
A 1 532  PHE 532  532  532  PHE PHE A . n 
A 1 533  ILE 533  533  533  ILE ILE A . n 
A 1 534  VAL 534  534  534  VAL VAL A . n 
A 1 535  GLY 535  535  535  GLY GLY A . n 
A 1 536  GLU 536  536  536  GLU GLU A . n 
A 1 537  GLY 537  537  537  GLY GLY A . n 
A 1 538  LEU 538  538  538  LEU LEU A . n 
A 1 539  GLY 539  539  539  GLY GLY A . n 
A 1 540  ARG 540  540  540  ARG ARG A . n 
A 1 541  GLY 541  541  541  GLY GLY A . n 
A 1 542  TYR 542  542  542  TYR TYR A . n 
A 1 543  LEU 543  543  543  LEU LEU A . n 
A 1 544  ASN 544  544  544  ASN ASN A . n 
A 1 545  ARG 545  545  545  ARG ARG A . n 
A 1 546  PRO 546  546  546  PRO PRO A . n 
A 1 547  GLU 547  547  547  GLU GLU A . n 
A 1 548  LEU 548  548  548  LEU LEU A . n 
A 1 549  THR 549  549  549  THR THR A . n 
A 1 550  ALA 550  550  550  ALA ALA A . n 
A 1 551  GLU 551  551  551  GLU GLU A . n 
A 1 552  LYS 552  552  552  LYS LYS A . n 
A 1 553  PHE 553  553  553  PHE PHE A . n 
A 1 554  ILE 554  554  554  ILE ILE A . n 
A 1 555  VAL 555  555  555  VAL VAL A . n 
A 1 556  HIS 556  556  556  HIS HIS A . n 
A 1 557  PRO 557  557  557  PRO PRO A . n 
A 1 558  GLN 558  558  558  GLN GLN A . n 
A 1 559  THR 559  559  559  THR THR A . n 
A 1 560  GLY 560  560  560  GLY GLY A . n 
A 1 561  GLU 561  561  561  GLU GLU A . n 
A 1 562  ARG 562  562  562  ARG ARG A . n 
A 1 563  MET 563  563  563  MET MET A . n 
A 1 564  TYR 564  564  564  TYR TYR A . n 
A 1 565  ARG 565  565  565  ARG ARG A . n 
A 1 566  THR 566  566  566  THR THR A . n 
A 1 567  GLY 567  567  567  GLY GLY A . n 
A 1 568  ASP 568  568  568  ASP ASP A . n 
A 1 569  ARG 569  569  569  ARG ARG A . n 
A 1 570  ALA 570  570  570  ALA ALA A . n 
A 1 571  ARG 571  571  571  ARG ARG A . n 
A 1 572  PHE 572  572  572  PHE PHE A . n 
A 1 573  LEU 573  573  573  LEU LEU A . n 
A 1 574  PRO 574  574  574  PRO PRO A . n 
A 1 575  ASP 575  575  575  ASP ASP A . n 
A 1 576  GLY 576  576  576  GLY GLY A . n 
A 1 577  ASN 577  577  577  ASN ASN A . n 
A 1 578  ILE 578  578  578  ILE ILE A . n 
A 1 579  GLU 579  579  579  GLU GLU A . n 
A 1 580  PHE 580  580  580  PHE PHE A . n 
A 1 581  LEU 581  581  581  LEU LEU A . n 
A 1 582  GLY 582  582  582  GLY GLY A . n 
A 1 583  ARG 583  583  583  ARG ARG A . n 
A 1 584  LEU 584  584  584  LEU LEU A . n 
A 1 585  ASP 585  585  585  ASP ASP A . n 
A 1 586  ASN 586  586  586  ASN ASN A . n 
A 1 587  LEU 587  587  587  LEU LEU A . n 
A 1 588  VAL 588  588  588  VAL VAL A . n 
A 1 589  LYS 589  589  589  LYS LYS A . n 
A 1 590  ILE 590  590  590  ILE ILE A . n 
A 1 591  ARG 591  591  591  ARG ARG A . n 
A 1 592  GLY 592  592  592  GLY GLY A . n 
A 1 593  TYR 593  593  593  TYR TYR A . n 
A 1 594  ARG 594  594  594  ARG ARG A . n 
A 1 595  ILE 595  595  595  ILE ILE A . n 
A 1 596  GLU 596  596  596  GLU GLU A . n 
A 1 597  PRO 597  597  597  PRO PRO A . n 
A 1 598  GLY 598  598  598  GLY GLY A . n 
A 1 599  GLU 599  599  599  GLU GLU A . n 
A 1 600  ILE 600  600  600  ILE ILE A . n 
A 1 601  GLU 601  601  601  GLU GLU A . n 
A 1 602  PRO 602  602  602  PRO PRO A . n 
A 1 603  PHE 603  603  603  PHE PHE A . n 
A 1 604  LEU 604  604  604  LEU LEU A . n 
A 1 605  MET 605  605  605  MET MET A . n 
A 1 606  ASN 606  606  606  ASN ASN A . n 
A 1 607  HIS 607  607  607  HIS HIS A . n 
A 1 608  PRO 608  608  608  PRO PRO A . n 
A 1 609  LEU 609  609  609  LEU LEU A . n 
A 1 610  ILE 610  610  610  ILE ILE A . n 
A 1 611  GLU 611  611  611  GLU GLU A . n 
A 1 612  LEU 612  612  612  LEU LEU A . n 
A 1 613  THR 613  613  613  THR THR A . n 
A 1 614  THR 614  614  614  THR THR A . n 
A 1 615  VAL 615  615  615  VAL VAL A . n 
A 1 616  LEU 616  616  616  LEU LEU A . n 
A 1 617  ALA 617  617  617  ALA ALA A . n 
A 1 618  LYS 618  618  618  LYS LYS A . n 
A 1 619  GLU 619  619  619  GLU GLU A . n 
A 1 620  GLN 620  620  620  GLN GLN A . n 
A 1 621  ALA 621  621  621  ALA ALA A . n 
A 1 622  ASP 622  622  622  ASP ASP A . n 
A 1 623  GLY 623  623  623  GLY GLY A . n 
A 1 624  ARG 624  624  624  ARG ARG A . n 
A 1 625  LYS 625  625  625  LYS LYS A . n 
A 1 626  TYR 626  626  626  TYR TYR A . n 
A 1 627  LEU 627  627  627  LEU LEU A . n 
A 1 628  VAL 628  628  628  VAL VAL A . n 
A 1 629  GLY 629  629  629  GLY GLY A . n 
A 1 630  TYR 630  630  630  TYR TYR A . n 
A 1 631  TYR 631  631  631  TYR TYR A . n 
A 1 632  VAL 632  632  632  VAL VAL A . n 
A 1 633  ALA 633  633  633  ALA ALA A . n 
A 1 634  PRO 634  634  634  PRO PRO A . n 
A 1 635  GLU 635  635  635  GLU GLU A . n 
A 1 636  GLU 636  636  636  GLU GLU A . n 
A 1 637  ILE 637  637  637  ILE ILE A . n 
A 1 638  PRO 638  638  638  PRO PRO A . n 
A 1 639  HIS 639  639  639  HIS HIS A . n 
A 1 640  GLY 640  640  640  GLY GLY A . n 
A 1 641  GLU 641  641  641  GLU GLU A . n 
A 1 642  LEU 642  642  642  LEU LEU A . n 
A 1 643  ARG 643  643  643  ARG ARG A . n 
A 1 644  GLU 644  644  644  GLU GLU A . n 
A 1 645  TRP 645  645  645  TRP TRP A . n 
A 1 646  LEU 646  646  646  LEU LEU A . n 
A 1 647  GLY 647  647  647  GLY GLY A . n 
A 1 648  ASN 648  648  648  ASN ASN A . n 
A 1 649  ASP 649  649  649  ASP ASP A . n 
A 1 650  LEU 650  650  650  LEU LEU A . n 
A 1 651  PRO 651  651  651  PRO PRO A . n 
A 1 652  ASP 652  652  652  ASP ASP A . n 
A 1 653  TYR 653  653  653  TYR TYR A . n 
A 1 654  MET 654  654  654  MET MET A . n 
A 1 655  ILE 655  655  655  ILE ILE A . n 
A 1 656  PRO 656  656  656  PRO PRO A . n 
A 1 657  THR 657  657  657  THR THR A . n 
A 1 658  TYR 658  658  658  TYR TYR A . n 
A 1 659  PHE 659  659  659  PHE PHE A . n 
A 1 660  VAL 660  660  660  VAL VAL A . n 
A 1 661  HIS 661  661  661  HIS HIS A . n 
A 1 662  MET 662  662  662  MET MET A . n 
A 1 663  LYS 663  663  663  LYS LYS A . n 
A 1 664  ALA 664  664  664  ALA ALA A . n 
A 1 665  PHE 665  665  665  PHE PHE A . n 
A 1 666  PRO 666  666  666  PRO PRO A . n 
A 1 667  LEU 667  667  667  LEU LEU A . n 
A 1 668  THR 668  668  668  THR THR A . n 
A 1 669  ALA 669  669  669  ALA ALA A . n 
A 1 670  ASN 670  670  670  ASN ASN A . n 
A 1 671  GLY 671  671  671  GLY GLY A . n 
A 1 672  LYS 672  672  672  LYS LYS A . n 
A 1 673  VAL 673  673  673  VAL VAL A . n 
A 1 674  ASP 674  674  674  ASP ASP A . n 
A 1 675  ARG 675  675  675  ARG ARG A . n 
A 1 676  ARG 676  676  676  ARG ARG A . n 
A 1 677  ALA 677  677  677  ALA ALA A . n 
A 1 678  LEU 678  678  678  LEU LEU A . n 
A 1 679  PRO 679  679  679  PRO PRO A . n 
A 1 680  ASP 680  680  680  ASP ASP A . n 
A 1 681  VAL 681  681  681  VAL VAL A . n 
A 1 682  GLN 682  682  682  GLN GLN A . n 
A 1 683  ALA 683  683  ?    ?   ?   A . n 
A 1 684  ASP 684  684  ?    ?   ?   A . n 
A 1 685  ALA 685  685  ?    ?   ?   A . n 
A 1 686  GLU 686  686  686  GLU GLU A . n 
A 1 687  LEU 687  687  687  LEU LEU A . n 
A 1 688  LEU 688  688  688  LEU LEU A . n 
A 1 689  GLY 689  689  689  GLY GLY A . n 
A 1 690  GLU 690  690  690  GLU GLU A . n 
A 1 691  ASP 691  691  691  ASP ASP A . n 
A 1 692  TYR 692  692  692  TYR TYR A . n 
A 1 693  VAL 693  693  693  VAL VAL A . n 
A 1 694  ALA 694  694  694  ALA ALA A . n 
A 1 695  PRO 695  695  695  PRO PRO A . n 
A 1 696  THR 696  696  696  THR THR A . n 
A 1 697  ASP 697  697  697  ASP ASP A . n 
A 1 698  GLU 698  698  698  GLU GLU A . n 
A 1 699  LEU 699  699  699  LEU LEU A . n 
A 1 700  GLU 700  700  700  GLU GLU A . n 
A 1 701  GLN 701  701  701  GLN GLN A . n 
A 1 702  GLN 702  702  702  GLN GLN A . n 
A 1 703  LEU 703  703  703  LEU LEU A . n 
A 1 704  ALA 704  704  704  ALA ALA A . n 
A 1 705  GLN 705  705  705  GLN GLN A . n 
A 1 706  VAL 706  706  706  VAL VAL A . n 
A 1 707  TRP 707  707  707  TRP TRP A . n 
A 1 708  SER 708  708  708  SER SER A . n 
A 1 709  HIS 709  709  709  HIS HIS A . n 
A 1 710  VAL 710  710  710  VAL VAL A . n 
A 1 711  LEU 711  711  711  LEU LEU A . n 
A 1 712  GLY 712  712  712  GLY GLY A . n 
A 1 713  ILE 713  713  713  ILE ILE A . n 
A 1 714  PRO 714  714  714  PRO PRO A . n 
A 1 715  GLN 715  715  715  GLN GLN A . n 
A 1 716  MET 716  716  716  MET MET A . n 
A 1 717  GLY 717  717  717  GLY GLY A . n 
A 1 718  ILE 718  718  718  ILE ILE A . n 
A 1 719  ASP 719  719  719  ASP ASP A . n 
A 1 720  ASP 720  720  720  ASP ASP A . n 
A 1 721  HIS 721  721  721  HIS HIS A . n 
A 1 722  PHE 722  722  722  PHE PHE A . n 
A 1 723  LEU 723  723  723  LEU LEU A . n 
A 1 724  GLU 724  724  724  GLU GLU A . n 
A 1 725  ARG 725  725  725  ARG ARG A . n 
A 1 726  GLY 726  726  726  GLY GLY A . n 
A 1 727  GLY 727  727  727  GLY GLY A . n 
A 1 728  ASP 728  728  728  ASP ASP A . n 
A 1 729  4HH 729  729  729  4HH 4HH A . n 
A 1 730  ILE 730  730  730  ILE ILE A . n 
A 1 731  LYS 731  731  731  LYS LYS A . n 
A 1 732  VAL 732  732  732  VAL VAL A . n 
A 1 733  MET 733  733  733  MET MET A . n 
A 1 734  GLN 734  734  734  GLN GLN A . n 
A 1 735  LEU 735  735  735  LEU LEU A . n 
A 1 736  ILE 736  736  736  ILE ILE A . n 
A 1 737  HIS 737  737  737  HIS HIS A . n 
A 1 738  GLN 738  738  738  GLN GLN A . n 
A 1 739  LEU 739  739  739  LEU LEU A . n 
A 1 740  LYS 740  740  740  LYS LYS A . n 
A 1 741  ASN 741  741  741  ASN ASN A . n 
A 1 742  ILE 742  742  742  ILE ILE A . n 
A 1 743  GLY 743  743  743  GLY GLY A . n 
A 1 744  LEU 744  744  744  LEU LEU A . n 
A 1 745  SER 745  745  745  SER SER A . n 
A 1 746  LEU 746  746  746  LEU LEU A . n 
A 1 747  ARG 747  747  747  ARG ARG A . n 
A 1 748  TYR 748  748  748  TYR TYR A . n 
A 1 749  ASP 749  749  749  ASP ASP A . n 
A 1 750  GLN 750  750  750  GLN GLN A . n 
A 1 751  LEU 751  751  751  LEU LEU A . n 
A 1 752  PHE 752  752  752  PHE PHE A . n 
A 1 753  THR 753  753  753  THR THR A . n 
A 1 754  HIS 754  754  754  HIS HIS A . n 
A 1 755  PRO 755  755  755  PRO PRO A . n 
A 1 756  THR 756  756  756  THR THR A . n 
A 1 757  ILE 757  757  757  ILE ILE A . n 
A 1 758  ARG 758  758  758  ARG ARG A . n 
A 1 759  GLN 759  759  759  GLN GLN A . n 
A 1 760  LEU 760  760  760  LEU LEU A . n 
A 1 761  LYS 761  761  761  LYS LYS A . n 
A 1 762  ARG 762  762  762  ARG ARG A . n 
A 1 763  LEU 763  763  763  LEU LEU A . n 
A 1 764  LEU 764  764  764  LEU LEU A . n 
A 1 765  THR 765  765  765  THR THR A . n 
A 1 766  GLU 766  766  766  GLU GLU A . n 
A 1 767  GLN 767  767  767  GLN GLN A . n 
A 1 768  LYS 768  768  768  LYS LYS A . n 
A 1 769  GLN 769  769  769  GLN GLN A . n 
A 1 770  VAL 770  770  770  VAL VAL A . n 
A 1 771  ASN 771  770  770  ASN ASN A A n 
A 1 772  GLY 772  770  770  GLY GLY A B n 
A 1 773  LEU 773  771  771  LEU LEU A . n 
A 1 774  LEU 774  772  772  LEU LEU A . n 
A 1 775  GLU 775  773  773  GLU GLU A . n 
A 1 776  PRO 776  774  774  PRO PRO A . n 
A 1 777  LEU 777  775  775  LEU LEU A . n 
A 1 778  ARG 778  776  776  ARG ARG A . n 
A 1 779  GLU 779  777  777  GLU GLU A . n 
A 1 780  LEU 780  778  778  LEU LEU A . n 
A 1 781  ASP 781  779  779  ASP ASP A . n 
A 1 782  GLU 782  780  780  GLU GLU A . n 
A 1 783  GLN 783  781  781  GLN GLN A . n 
A 1 784  ALA 784  782  782  ALA ALA A . n 
A 1 785  GLU 785  783  783  GLU GLU A . n 
A 1 786  TYR 786  784  784  TYR TYR A . n 
A 1 787  GLU 787  785  785  GLU GLU A . n 
A 1 788  THR 788  786  786  THR THR A . n 
A 1 789  SER 789  787  787  SER SER A . n 
A 1 790  ALA 790  788  788  ALA ALA A . n 
A 1 791  VAL 791  789  789  VAL VAL A . n 
A 1 792  GLU 792  790  790  GLU GLU A . n 
A 1 793  LYS 793  791  791  LYS LYS A . n 
A 1 794  ARG 794  792  792  ARG ARG A . n 
A 1 795  MET 795  793  793  MET MET A . n 
A 1 796  TYR 796  794  794  TYR TYR A . n 
A 1 797  ILE 797  795  795  ILE ILE A . n 
A 1 798  ILE 798  796  796  ILE ILE A . n 
A 1 799  GLN 799  797  797  GLN GLN A . n 
A 1 800  GLN 800  798  798  GLN GLN A . n 
A 1 801  GLN 801  799  799  GLN GLN A . n 
A 1 802  ASP 802  800  800  ASP ASP A . n 
A 1 803  VAL 803  801  801  VAL VAL A . n 
A 1 804  GLU 804  802  802  GLU GLU A . n 
A 1 805  SER 805  803  803  SER SER A . n 
A 1 806  ILE 806  804  804  ILE ILE A . n 
A 1 807  ALA 807  805  805  ALA ALA A . n 
A 1 808  TYR 808  806  806  TYR TYR A . n 
A 1 809  ASN 809  807  807  ASN ASN A . n 
A 1 810  VAL 810  808  808  VAL VAL A . n 
A 1 811  VAL 811  809  809  VAL VAL A . n 
A 1 812  TYR 812  810  810  TYR TYR A . n 
A 1 813  THR 813  811  811  THR THR A . n 
A 1 814  ILE 814  812  812  ILE ILE A . n 
A 1 815  ASN 815  813  813  ASN ASN A . n 
A 1 816  PHE 816  814  814  PHE PHE A . n 
A 1 817  PRO 817  815  815  PRO PRO A . n 
A 1 818  LEU 818  816  816  LEU LEU A . n 
A 1 819  THR 819  817  817  THR THR A . n 
A 1 820  VAL 820  818  818  VAL VAL A . n 
A 1 821  ASP 821  819  819  ASP ASP A . n 
A 1 822  THR 822  820  820  THR THR A . n 
A 1 823  GLU 823  821  821  GLU GLU A . n 
A 1 824  GLN 824  822  822  GLN GLN A . n 
A 1 825  ILE 825  823  823  ILE ILE A . n 
A 1 826  ARG 826  824  824  ARG ARG A . n 
A 1 827  VAL 827  825  825  VAL VAL A . n 
A 1 828  ALA 828  826  826  ALA ALA A . n 
A 1 829  LEU 829  827  827  LEU LEU A . n 
A 1 830  GLU 830  828  828  GLU GLU A . n 
A 1 831  GLN 831  829  829  GLN GLN A . n 
A 1 832  LEU 832  830  830  LEU LEU A . n 
A 1 833  VAL 833  831  831  VAL VAL A . n 
A 1 834  LEU 834  832  832  LEU LEU A . n 
A 1 835  ARG 835  833  833  ARG ARG A . n 
A 1 836  HIS 836  834  834  HIS HIS A . n 
A 1 837  GLU 837  835  835  GLU GLU A . n 
A 1 838  GLY 838  836  836  GLY GLY A . n 
A 1 839  LEU 839  837  837  LEU LEU A . n 
A 1 840  ARG 840  838  838  ARG ARG A . n 
A 1 841  SER 841  839  839  SER SER A . n 
A 1 842  THR 842  840  840  THR THR A . n 
A 1 843  TYR 843  841  841  TYR TYR A . n 
A 1 844  HIS 844  842  842  HIS HIS A . n 
A 1 845  MET 845  843  843  MET MET A . n 
A 1 846  ARG 846  844  844  ARG ARG A . n 
A 1 847  GLY 847  845  845  GLY GLY A . n 
A 1 848  ASP 848  846  846  ASP ASP A . n 
A 1 849  GLU 849  847  847  GLU GLU A . n 
A 1 850  ILE 850  848  848  ILE ILE A . n 
A 1 851  VAL 851  849  849  VAL VAL A . n 
A 1 852  LYS 852  850  850  LYS LYS A . n 
A 1 853  ARG 853  851  851  ARG ARG A . n 
A 1 854  ILE 854  852  852  ILE ILE A . n 
A 1 855  VAL 855  853  853  VAL VAL A . n 
A 1 856  PRO 856  854  854  PRO PRO A . n 
A 1 857  ARG 857  855  855  ARG ARG A . n 
A 1 858  ALA 858  856  856  ALA ALA A . n 
A 1 859  GLU 859  857  857  GLU GLU A . n 
A 1 860  LEU 860  858  858  LEU LEU A . n 
A 1 861  SER 861  859  859  SER SER A . n 
A 1 862  PHE 862  860  860  PHE PHE A . n 
A 1 863  VAL 863  861  861  VAL VAL A . n 
A 1 864  ARG 864  862  862  ARG ARG A . n 
A 1 865  GLN 865  863  863  GLN GLN A . n 
A 1 866  THR 866  864  864  THR THR A . n 
A 1 867  GLY 867  865  865  GLY GLY A . n 
A 1 868  GLU 868  866  866  GLU GLU A . n 
A 1 869  GLU 869  867  867  GLU GLU A . n 
A 1 870  GLU 870  868  868  GLU GLU A . n 
A 1 871  SER 871  869  869  SER SER A . n 
A 1 872  VAL 872  870  870  VAL VAL A . n 
A 1 873  GLN 873  871  871  GLN GLN A . n 
A 1 874  SER 874  872  872  SER SER A . n 
A 1 875  LEU 875  873  873  LEU LEU A . n 
A 1 876  LEU 876  874  874  LEU LEU A . n 
A 1 877  ALA 877  875  875  ALA ALA A . n 
A 1 878  GLU 878  876  876  GLU GLU A . n 
A 1 879  GLN 879  877  877  GLN GLN A . n 
A 1 880  ILE 880  878  878  ILE ILE A . n 
A 1 881  LYS 881  879  879  LYS LYS A . n 
A 1 882  PRO 882  880  880  PRO PRO A . n 
A 1 883  PHE 883  881  881  PHE PHE A . n 
A 1 884  ASP 884  882  882  ASP ASP A . n 
A 1 885  LEU 885  883  883  LEU LEU A . n 
A 1 886  ALA 886  884  884  ALA ALA A . n 
A 1 887  LYS 887  885  885  LYS LYS A . n 
A 1 888  ALA 888  886  886  ALA ALA A . n 
A 1 889  PRO 889  887  887  PRO PRO A . n 
A 1 890  LEU 890  888  888  LEU LEU A . n 
A 1 891  LEU 891  889  889  LEU LEU A . n 
A 1 892  ARG 892  890  890  ARG ARG A . n 
A 1 893  ALA 893  891  891  ALA ALA A . n 
A 1 894  GLY 894  892  892  GLY GLY A . n 
A 1 895  VAL 895  893  893  VAL VAL A . n 
A 1 896  ILE 896  894  894  ILE ILE A . n 
A 1 897  GLU 897  895  895  GLU GLU A . n 
A 1 898  THR 898  896  896  THR THR A . n 
A 1 899  ALA 899  897  897  ALA ALA A . n 
A 1 900  ASP 900  898  898  ASP ASP A . n 
A 1 901  LYS 901  899  899  LYS LYS A . n 
A 1 902  LYS 902  900  900  LYS LYS A . n 
A 1 903  VAL 903  901  901  VAL VAL A . n 
A 1 904  LEU 904  902  902  LEU LEU A . n 
A 1 905  TRP 905  903  903  TRP TRP A . n 
A 1 906  PHE 906  904  904  PHE PHE A . n 
A 1 907  ASP 907  905  905  ASP ASP A . n 
A 1 908  SER 908  906  906  SER SER A . n 
A 1 909  HIS 909  907  907  HIS HIS A . n 
A 1 910  HIS 910  908  908  HIS HIS A . n 
A 1 911  ILE 911  909  909  ILE ILE A . n 
A 1 912  LEU 912  910  910  LEU LEU A . n 
A 1 913  LEU 913  911  911  LEU LEU A . n 
A 1 914  ASP 914  912  912  ASP ASP A . n 
A 1 915  GLY 915  913  913  GLY GLY A . n 
A 1 916  LEU 916  914  914  LEU LEU A . n 
A 1 917  SER 917  915  915  SER SER A . n 
A 1 918  LYS 918  916  916  LYS LYS A . n 
A 1 919  SER 919  917  917  SER SER A . n 
A 1 920  ILE 920  918  918  ILE ILE A . n 
A 1 921  LEU 921  919  919  LEU LEU A . n 
A 1 922  ALA 922  920  920  ALA ALA A . n 
A 1 923  ARG 923  921  921  ARG ARG A . n 
A 1 924  GLU 924  922  922  GLU GLU A . n 
A 1 925  LEU 925  923  923  LEU LEU A . n 
A 1 926  GLN 926  924  924  GLN GLN A . n 
A 1 927  ALA 927  925  925  ALA ALA A . n 
A 1 928  LEU 928  926  926  LEU LEU A . n 
A 1 929  LEU 929  927  927  LEU LEU A . n 
A 1 930  GLY 930  928  928  GLY GLY A . n 
A 1 931  GLN 931  929  929  GLN GLN A . n 
A 1 932  GLN 932  930  930  GLN GLN A . n 
A 1 933  VAL 933  931  931  VAL VAL A . n 
A 1 934  LEU 934  932  932  LEU LEU A . n 
A 1 935  SER 935  933  933  SER SER A . n 
A 1 936  PRO 936  934  934  PRO PRO A . n 
A 1 937  VAL 937  935  935  VAL VAL A . n 
A 1 938  GLU 938  936  936  GLU GLU A . n 
A 1 939  LYS 939  937  937  LYS LYS A . n 
A 1 940  THR 940  938  938  THR THR A . n 
A 1 941  TYR 941  939  939  TYR TYR A . n 
A 1 942  LYS 942  940  940  LYS LYS A . n 
A 1 943  SER 943  941  941  SER SER A . n 
A 1 944  PHE 944  942  942  PHE PHE A . n 
A 1 945  ALA 945  943  943  ALA ALA A . n 
A 1 946  ARG 946  944  944  ARG ARG A . n 
A 1 947  TRP 947  945  945  TRP TRP A . n 
A 1 948  GLN 948  946  946  GLN GLN A . n 
A 1 949  ASN 949  947  947  ASN ASN A . n 
A 1 950  GLU 950  948  948  GLU GLU A . n 
A 1 951  TRP 951  949  949  TRP TRP A . n 
A 1 952  PHE 952  950  950  PHE PHE A . n 
A 1 953  ALA 953  951  951  ALA ALA A . n 
A 1 954  SER 954  952  952  SER SER A . n 
A 1 955  ASP 955  953  953  ASP ASP A . n 
A 1 956  GLU 956  954  954  GLU GLU A . n 
A 1 957  TYR 957  955  955  TYR TYR A . n 
A 1 958  GLU 958  956  956  GLU GLU A . n 
A 1 959  GLN 959  957  957  GLN GLN A . n 
A 1 960  GLN 960  958  958  GLN GLN A . n 
A 1 961  ILE 961  959  959  ILE ILE A . n 
A 1 962  ALA 962  960  960  ALA ALA A . n 
A 1 963  TYR 963  961  961  TYR TYR A . n 
A 1 964  TRP 964  962  962  TRP TRP A . n 
A 1 965  LYS 965  963  963  LYS LYS A . n 
A 1 966  THR 966  964  964  THR THR A . n 
A 1 967  LEU 967  965  965  LEU LEU A . n 
A 1 968  LEU 968  966  966  LEU LEU A . n 
A 1 969  GLN 969  967  967  GLN GLN A . n 
A 1 970  GLY 970  968  968  GLY GLY A . n 
A 1 971  GLU 971  969  969  GLU GLU A . n 
A 1 972  LEU 972  970  970  LEU LEU A . n 
A 1 973  PRO 973  971  971  PRO PRO A . n 
A 1 974  ALA 974  972  972  ALA ALA A . n 
A 1 975  VAL 975  973  973  VAL VAL A . n 
A 1 976  GLN 976  974  974  GLN GLN A . n 
A 1 977  LEU 977  975  975  LEU LEU A . n 
A 1 978  PRO 978  976  976  PRO PRO A . n 
A 1 979  THR 979  977  977  THR THR A . n 
A 1 980  LYS 980  978  978  LYS LYS A . n 
A 1 981  LYS 981  979  979  LYS LYS A . n 
A 1 982  ARG 982  980  980  ARG ARG A . n 
A 1 983  PRO 983  981  981  PRO PRO A . n 
A 1 984  PRO 984  982  982  PRO PRO A . n 
A 1 985  GLN 985  983  983  GLN GLN A . n 
A 1 986  LEU 986  984  984  LEU LEU A . n 
A 1 987  THR 987  985  985  THR THR A . n 
A 1 988  PHE 988  986  986  PHE PHE A . n 
A 1 989  ASP 989  987  987  ASP ASP A . n 
A 1 990  GLY 990  988  988  GLY GLY A . n 
A 1 991  ALA 991  989  989  ALA ALA A . n 
A 1 992  ILE 992  990  990  ILE ILE A . n 
A 1 993  GLN 993  991  991  GLN GLN A . n 
A 1 994  MET 994  992  992  MET MET A . n 
A 1 995  TYR 995  993  993  TYR TYR A . n 
A 1 996  ARG 996  994  994  ARG ARG A . n 
A 1 997  VAL 997  995  995  VAL VAL A . n 
A 1 998  ASN 998  996  996  ASN ASN A . n 
A 1 999  PRO 999  997  997  PRO PRO A . n 
A 1 1000 GLU 1000 998  998  GLU GLU A . n 
A 1 1001 ILE 1001 999  999  ILE ILE A . n 
A 1 1002 THR 1002 1000 1000 THR THR A . n 
A 1 1003 ARG 1003 1001 1001 ARG ARG A . n 
A 1 1004 LYS 1004 1002 1002 LYS LYS A . n 
A 1 1005 LEU 1005 1003 1003 LEU LEU A . n 
A 1 1006 LYS 1006 1004 1004 LYS LYS A . n 
A 1 1007 ALA 1007 1005 1005 ALA ALA A . n 
A 1 1008 THR 1008 1006 1006 THR THR A . n 
A 1 1009 ALA 1009 1007 1007 ALA ALA A . n 
A 1 1010 ALA 1010 1008 1008 ALA ALA A . n 
A 1 1011 LYS 1011 1009 1009 LYS LYS A . n 
A 1 1012 HIS 1012 1010 1010 HIS HIS A . n 
A 1 1013 ASP 1013 1011 1011 ASP ASP A . n 
A 1 1014 LEU 1014 1012 1012 LEU LEU A . n 
A 1 1015 THR 1015 1013 1013 THR THR A . n 
A 1 1016 LEU 1016 1014 1014 LEU LEU A . n 
A 1 1017 TYR 1017 1015 1015 TYR TYR A . n 
A 1 1018 MET 1018 1016 1016 MET MET A . n 
A 1 1019 LEU 1019 1017 1017 LEU LEU A . n 
A 1 1020 MET 1020 1018 1018 MET MET A . n 
A 1 1021 LEU 1021 1019 1019 LEU LEU A . n 
A 1 1022 THR 1022 1020 1020 THR THR A . n 
A 1 1023 ILE 1023 1021 1021 ILE ILE A . n 
A 1 1024 VAL 1024 1022 1022 VAL VAL A . n 
A 1 1025 SER 1025 1023 1023 SER SER A . n 
A 1 1026 ILE 1026 1024 1024 ILE ILE A . n 
A 1 1027 TRP 1027 1025 1025 TRP TRP A . n 
A 1 1028 LEU 1028 1026 1026 LEU LEU A . n 
A 1 1029 SER 1029 1027 1027 SER SER A . n 
A 1 1030 LYS 1030 1028 1028 LYS LYS A . n 
A 1 1031 MET 1031 1029 1029 MET MET A . n 
A 1 1032 ASN 1032 1030 1030 ASN ASN A . n 
A 1 1033 SER 1033 1031 1031 SER SER A . n 
A 1 1034 ASP 1034 1032 1032 ASP ASP A . n 
A 1 1035 SER 1035 1033 1033 SER SER A . n 
A 1 1036 ASN 1036 1034 1034 ASN ASN A . n 
A 1 1037 GLN 1037 1035 1035 GLN GLN A . n 
A 1 1038 VAL 1038 1036 1036 VAL VAL A . n 
A 1 1039 ILE 1039 1037 1037 ILE ILE A . n 
A 1 1040 LEU 1040 1038 1038 LEU LEU A . n 
A 1 1041 GLY 1041 1039 1039 GLY GLY A . n 
A 1 1042 THR 1042 1040 1040 THR THR A . n 
A 1 1043 VAL 1043 1041 1041 VAL VAL A . n 
A 1 1044 THR 1044 1042 1042 THR THR A . n 
A 1 1045 ASP 1045 1043 1043 ASP ASP A . n 
A 1 1046 GLY 1046 1044 1044 GLY GLY A . n 
A 1 1047 ARG 1047 1045 1045 ARG ARG A . n 
A 1 1048 GLN 1048 1046 1046 GLN GLN A . n 
A 1 1049 HIS 1049 1047 1047 HIS HIS A . n 
A 1 1050 PRO 1050 1048 1048 PRO PRO A . n 
A 1 1051 ASP 1051 1049 1049 ASP ASP A . n 
A 1 1052 THR 1052 1050 1050 THR THR A . n 
A 1 1053 ARG 1053 1051 1051 ARG ARG A . n 
A 1 1054 GLU 1054 1052 1052 GLU GLU A . n 
A 1 1055 LEU 1055 1053 1053 LEU LEU A . n 
A 1 1056 LEU 1056 1054 1054 LEU LEU A . n 
A 1 1057 GLY 1057 1055 1055 GLY GLY A . n 
A 1 1058 MET 1058 1056 1056 MET MET A . n 
A 1 1059 PHE 1059 1057 1057 PHE PHE A . n 
A 1 1060 VAL 1060 1058 1058 VAL VAL A . n 
A 1 1061 ASN 1061 1059 1059 ASN ASN A . n 
A 1 1062 THR 1062 1060 1060 THR THR A . n 
A 1 1063 LEU 1063 1061 1061 LEU LEU A . n 
A 1 1064 PRO 1064 1062 1062 PRO PRO A . n 
A 1 1065 LEU 1065 1063 1063 LEU LEU A . n 
A 1 1066 LEU 1066 1064 1064 LEU LEU A . n 
A 1 1067 LEU 1067 1065 1065 LEU LEU A . n 
A 1 1068 SER 1068 1066 1066 SER SER A . n 
A 1 1069 ILE 1069 1067 1067 ILE ILE A . n 
A 1 1070 ASP 1070 1068 1068 ASP ASP A . n 
A 1 1071 HIS 1071 1069 1069 HIS HIS A . n 
A 1 1072 GLU 1072 1070 1070 GLU GLU A . n 
A 1 1073 GLU 1073 1071 1071 GLU GLU A . n 
A 1 1074 SER 1074 1072 1072 SER SER A . n 
A 1 1075 PHE 1075 1073 1073 PHE PHE A . n 
A 1 1076 LEU 1076 1074 1074 LEU LEU A . n 
A 1 1077 HIS 1077 1075 1075 HIS HIS A . n 
A 1 1078 ASN 1078 1076 1076 ASN ASN A . n 
A 1 1079 LEU 1079 1077 1077 LEU LEU A . n 
A 1 1080 GLN 1080 1078 1078 GLN GLN A . n 
A 1 1081 GLN 1081 1079 1079 GLN GLN A . n 
A 1 1082 VAL 1082 1080 1080 VAL VAL A . n 
A 1 1083 LYS 1083 1081 1081 LYS LYS A . n 
A 1 1084 ALA 1084 1082 1082 ALA ALA A . n 
A 1 1085 LYS 1085 1083 1083 LYS LYS A . n 
A 1 1086 LEU 1086 1084 1084 LEU LEU A . n 
A 1 1087 LEU 1087 1085 1085 LEU LEU A . n 
A 1 1088 PRO 1088 1086 1086 PRO PRO A . n 
A 1 1089 ALA 1089 1087 1087 ALA ALA A . n 
A 1 1090 LEU 1090 1088 1088 LEU LEU A . n 
A 1 1091 GLN 1091 1089 1089 GLN GLN A . n 
A 1 1092 ASN 1092 1090 1090 ASN ASN A . n 
A 1 1093 GLN 1093 1091 1091 GLN GLN A . n 
A 1 1094 TYR 1094 1092 1092 TYR TYR A . n 
A 1 1095 VAL 1095 1093 1093 VAL VAL A . n 
A 1 1096 PRO 1096 1094 1094 PRO PRO A . n 
A 1 1097 PHE 1097 1095 1095 PHE PHE A . n 
A 1 1098 ASP 1098 1096 1096 ASP ASP A . n 
A 1 1099 LYS 1099 1097 1097 LYS LYS A . n 
A 1 1100 ILE 1100 1098 1098 ILE ILE A . n 
A 1 1101 LEU 1101 1099 1099 LEU LEU A . n 
A 1 1102 GLU 1102 1100 1100 GLU GLU A . n 
A 1 1103 ALA 1103 1101 1101 ALA ALA A . n 
A 1 1104 ALA 1104 1102 1102 ALA ALA A . n 
A 1 1105 ARG 1105 1103 1103 ARG ARG A . n 
A 1 1106 VAL 1106 1104 1104 VAL VAL A . n 
A 1 1107 LYS 1107 1105 1105 LYS LYS A . n 
A 1 1108 ARG 1108 1106 1106 ARG ARG A . n 
A 1 1109 GLU 1109 1107 1107 GLU GLU A . n 
A 1 1110 GLY 1110 1108 1108 GLY GLY A . n 
A 1 1111 ASN 1111 1109 1109 ASN ASN A . n 
A 1 1112 ARG 1112 1110 1110 ARG ARG A . n 
A 1 1113 HIS 1113 1111 1111 HIS HIS A . n 
A 1 1114 PRO 1114 1112 1112 PRO PRO A . n 
A 1 1115 LEU 1115 1113 1113 LEU LEU A . n 
A 1 1116 PHE 1116 1114 1114 PHE PHE A . n 
A 1 1117 ASP 1117 1115 1115 ASP ASP A . n 
A 1 1118 VAL 1118 1116 1116 VAL VAL A . n 
A 1 1119 MET 1119 1117 1117 MET MET A . n 
A 1 1120 PHE 1120 1118 1118 PHE PHE A . n 
A 1 1121 MET 1121 1119 1119 MET MET A . n 
A 1 1122 MET 1122 1120 1120 MET MET A . n 
A 1 1123 GLN 1123 1121 1121 GLN GLN A . n 
A 1 1124 GLY 1124 1122 1122 GLY GLY A . n 
A 1 1125 ALA 1125 1123 1123 ALA ALA A . n 
A 1 1126 PRO 1126 1124 1124 PRO PRO A . n 
A 1 1127 GLU 1127 1125 1125 GLU GLU A . n 
A 1 1128 THR 1128 1126 1126 THR THR A . n 
A 1 1129 GLU 1129 1127 1127 GLU GLU A . n 
A 1 1130 LEU 1130 1128 1128 LEU LEU A . n 
A 1 1131 GLU 1131 1129 1129 GLU GLU A . n 
A 1 1132 SER 1132 1130 1130 SER SER A . n 
A 1 1133 ASN 1133 1131 1131 ASN ASN A . n 
A 1 1134 MET 1134 1132 1132 MET MET A . n 
A 1 1135 HIS 1135 1133 1133 HIS HIS A . n 
A 1 1136 HIS 1136 1134 1134 HIS HIS A . n 
A 1 1137 ILE 1137 1135 1135 ILE ILE A . n 
A 1 1138 ASN 1138 1136 1136 ASN ASN A . n 
A 1 1139 ALA 1139 1137 1137 ALA ALA A . n 
A 1 1140 GLY 1140 1138 1138 GLY GLY A . n 
A 1 1141 ILE 1141 1139 1139 ILE ILE A . n 
A 1 1142 SER 1142 1140 1140 SER SER A . n 
A 1 1143 LYS 1143 1141 1141 LYS LYS A . n 
A 1 1144 PHE 1144 1142 1142 PHE PHE A . n 
A 1 1145 ASP 1145 1143 1143 ASP ASP A . n 
A 1 1146 LEU 1146 1144 1144 LEU LEU A . n 
A 1 1147 THR 1147 1145 1145 THR THR A . n 
A 1 1148 LEU 1148 1146 1146 LEU LEU A . n 
A 1 1149 GLU 1149 1147 1147 GLU GLU A . n 
A 1 1150 VAL 1150 1148 1148 VAL VAL A . n 
A 1 1151 LEU 1151 1149 1149 LEU LEU A . n 
A 1 1152 GLU 1152 1150 1150 GLU GLU A . n 
A 1 1153 ARG 1153 1151 1151 ARG ARG A . n 
A 1 1154 GLU 1154 1152 1152 GLU GLU A . n 
A 1 1155 ASN 1155 1153 1153 ASN ASN A . n 
A 1 1156 GLY 1156 1154 1154 GLY GLY A . n 
A 1 1157 LEU 1157 1155 1155 LEU LEU A . n 
A 1 1158 ASN 1158 1156 1156 ASN ASN A . n 
A 1 1159 ILE 1159 1157 1157 ILE ILE A . n 
A 1 1160 VAL 1160 1158 1158 VAL VAL A . n 
A 1 1161 PHE 1161 1159 1159 PHE PHE A . n 
A 1 1162 GLU 1162 1160 1160 GLU GLU A . n 
A 1 1163 TYR 1163 1161 1161 TYR TYR A . n 
A 1 1164 ASN 1164 1162 1162 ASN ASN A . n 
A 1 1165 THR 1165 1163 1163 THR THR A . n 
A 1 1166 HIS 1166 1164 1164 HIS HIS A . n 
A 1 1167 LEU 1167 1165 1165 LEU LEU A . n 
A 1 1168 PHE 1168 1166 1166 PHE PHE A . n 
A 1 1169 ASP 1169 1167 1167 ASP ASP A . n 
A 1 1170 GLU 1170 1168 1168 GLU GLU A . n 
A 1 1171 GLY 1171 1169 1169 GLY GLY A . n 
A 1 1172 MET 1172 1170 1170 MET MET A . n 
A 1 1173 ILE 1173 1171 1171 ILE ILE A . n 
A 1 1174 LEU 1174 1172 1172 LEU LEU A . n 
A 1 1175 ARG 1175 1173 1173 ARG ARG A . n 
A 1 1176 MET 1176 1174 1174 MET MET A . n 
A 1 1177 VAL 1177 1175 1175 VAL VAL A . n 
A 1 1178 ALA 1178 1176 1176 ALA ALA A . n 
A 1 1179 GLN 1179 1177 1177 GLN GLN A . n 
A 1 1180 PHE 1180 1178 1178 PHE PHE A . n 
A 1 1181 GLU 1181 1179 1179 GLU GLU A . n 
A 1 1182 HIS 1182 1180 1180 HIS HIS A . n 
A 1 1183 LEU 1183 1181 1181 LEU LEU A . n 
A 1 1184 LEU 1184 1182 1182 LEU LEU A . n 
A 1 1185 LEU 1185 1183 1183 LEU LEU A . n 
A 1 1186 GLN 1186 1184 1184 GLN GLN A . n 
A 1 1187 ALA 1187 1185 1185 ALA ALA A . n 
A 1 1188 VAL 1188 1186 1186 VAL VAL A . n 
A 1 1189 HIS 1189 1187 1187 HIS HIS A . n 
A 1 1190 GLY 1190 1188 1188 GLY GLY A . n 
A 1 1191 LEU 1191 1189 1189 LEU LEU A . n 
A 1 1192 ASP 1192 1190 1190 ASP ASP A . n 
A 1 1193 GLN 1193 1191 1191 GLN GLN A . n 
A 1 1194 GLN 1194 1192 1192 GLN GLN A . n 
A 1 1195 VAL 1195 1193 1193 VAL VAL A . n 
A 1 1196 LYS 1196 1194 1194 LYS LYS A . n 
A 1 1197 ARG 1197 1195 1195 ARG ARG A . n 
A 1 1198 PHE 1198 1196 1196 PHE PHE A . n 
A 1 1199 GLU 1199 1197 1197 GLU GLU A . n 
A 1 1200 LEU 1200 1198 1198 LEU LEU A . n 
A 1 1201 VAL 1201 1199 1199 VAL VAL A . n 
A 1 1202 THR 1202 1200 1200 THR THR A . n 
A 1 1203 GLU 1203 1201 1201 GLU GLU A . n 
A 1 1204 ASP 1204 1202 1202 ASP ASP A . n 
A 1 1205 GLU 1205 1203 1203 GLU GLU A . n 
A 1 1206 LYS 1206 1204 1204 LYS LYS A . n 
A 1 1207 ARG 1207 1205 1205 ARG ARG A . n 
A 1 1208 ASP 1208 1206 1206 ASP ASP A . n 
A 1 1209 LEU 1209 1207 1207 LEU LEU A . n 
A 1 1210 PHE 1210 1208 1208 PHE PHE A . n 
A 1 1211 LEU 1211 1209 1209 LEU LEU A . n 
A 1 1212 ARG 1212 1210 1210 ARG ARG A . n 
A 1 1213 VAL 1213 1211 1211 VAL VAL A . n 
A 1 1214 ASN 1214 1212 1212 ASN ASN A . n 
A 1 1215 ASP 1215 1213 1213 ASP ASP A . n 
A 1 1216 THR 1216 1214 1214 THR THR A . n 
A 1 1217 ALA 1217 1215 1215 ALA ALA A . n 
A 1 1218 LYS 1218 1216 1216 LYS LYS A . n 
A 1 1219 ALA 1219 1217 1217 ALA ALA A . n 
A 1 1220 TYR 1220 1218 1218 TYR TYR A . n 
A 1 1221 PRO 1221 1219 1219 PRO PRO A . n 
A 1 1222 ASN 1222 1220 1220 ASN ASN A . n 
A 1 1223 LYS 1223 1221 1221 LYS LYS A . n 
A 1 1224 LEU 1224 1222 1222 LEU LEU A . n 
A 1 1225 ILE 1225 1223 1223 ILE ILE A . n 
A 1 1226 MET 1226 1224 1224 MET MET A . n 
A 1 1227 SER 1227 1225 1225 SER SER A . n 
A 1 1228 MET 1228 1226 1226 MET MET A . n 
A 1 1229 LEU 1229 1227 1227 LEU LEU A . n 
A 1 1230 GLU 1230 1228 1228 GLU GLU A . n 
A 1 1231 ASP 1231 1229 1229 ASP ASP A . n 
A 1 1232 TRP 1232 1230 1230 TRP TRP A . n 
A 1 1233 ALA 1233 1231 1231 ALA ALA A . n 
A 1 1234 ALA 1234 1232 1232 ALA ALA A . n 
A 1 1235 ALA 1235 1233 1233 ALA ALA A . n 
A 1 1236 THR 1236 1234 1234 THR THR A . n 
A 1 1237 PRO 1237 1235 1235 PRO PRO A . n 
A 1 1238 ASP 1238 1236 1236 ASP ASP A . n 
A 1 1239 LYS 1239 1237 1237 LYS LYS A . n 
A 1 1240 THR 1240 1238 1238 THR THR A . n 
A 1 1241 ALA 1241 1239 1239 ALA ALA A . n 
A 1 1242 LEU 1242 1240 1240 LEU LEU A . n 
A 1 1243 VAL 1243 1241 1241 VAL VAL A . n 
A 1 1244 PHE 1244 1242 1242 PHE PHE A . n 
A 1 1245 ARG 1245 1243 1243 ARG ARG A . n 
A 1 1246 GLU 1246 1244 1244 GLU GLU A . n 
A 1 1247 GLN 1247 1245 1245 GLN GLN A . n 
A 1 1248 ARG 1248 1246 1246 ARG ARG A . n 
A 1 1249 VAL 1249 1247 1247 VAL VAL A . n 
A 1 1250 THR 1250 1248 1248 THR THR A . n 
A 1 1251 TYR 1251 1249 1249 TYR TYR A . n 
A 1 1252 ARG 1252 1250 1250 ARG ARG A . n 
A 1 1253 GLU 1253 1251 1251 GLU GLU A . n 
A 1 1254 LEU 1254 1252 1252 LEU LEU A . n 
A 1 1255 ASN 1255 1253 1253 ASN ASN A . n 
A 1 1256 GLU 1256 1254 1254 GLU GLU A . n 
A 1 1257 ARG 1257 1255 1255 ARG ARG A . n 
A 1 1258 VAL 1258 1256 1256 VAL VAL A . n 
A 1 1259 ASN 1259 1257 1257 ASN ASN A . n 
A 1 1260 GLN 1260 1258 1258 GLN GLN A . n 
A 1 1261 LEU 1261 1259 1259 LEU LEU A . n 
A 1 1262 ALA 1262 1260 1260 ALA ALA A . n 
A 1 1263 HIS 1263 1261 1261 HIS HIS A . n 
A 1 1264 THR 1264 1262 1262 THR THR A . n 
A 1 1265 LEU 1265 1263 1263 LEU LEU A . n 
A 1 1266 ARG 1266 1264 1264 ARG ARG A . n 
A 1 1267 GLU 1267 1265 1265 GLU GLU A . n 
A 1 1268 LYS 1268 1266 1266 LYS LYS A . n 
A 1 1269 GLY 1269 1267 1267 GLY GLY A . n 
A 1 1270 VAL 1270 1268 1268 VAL VAL A . n 
A 1 1271 GLN 1271 1269 1269 GLN GLN A . n 
A 1 1272 PRO 1272 1270 1270 PRO PRO A . n 
A 1 1273 ASP 1273 1271 1271 ASP ASP A . n 
A 1 1274 ASP 1274 1272 1272 ASP ASP A . n 
A 1 1275 LEU 1275 1273 1273 LEU LEU A . n 
A 1 1276 VAL 1276 1274 1274 VAL VAL A . n 
A 1 1277 MET 1277 1275 1275 MET MET A . n 
A 1 1278 LEU 1278 1276 1276 LEU LEU A . n 
A 1 1279 MET 1279 1277 1277 MET MET A . n 
A 1 1280 ALA 1280 1278 1278 ALA ALA A . n 
A 1 1281 GLU 1281 1279 1279 GLU GLU A . n 
A 1 1282 ARG 1282 1280 1280 ARG ARG A . n 
A 1 1283 SER 1283 1281 1281 SER SER A . n 
A 1 1284 VAL 1284 1282 1282 VAL VAL A . n 
A 1 1285 GLU 1285 1283 1283 GLU GLU A . n 
A 1 1286 MET 1286 1284 1284 MET MET A . n 
A 1 1287 MET 1287 1285 1285 MET MET A . n 
A 1 1288 VAL 1288 1286 1286 VAL VAL A . n 
A 1 1289 ALA 1289 1287 1287 ALA ALA A . n 
A 1 1290 ILE 1290 1288 1288 ILE ILE A . n 
A 1 1291 PHE 1291 1289 1289 PHE PHE A . n 
A 1 1292 ALA 1292 1290 1290 ALA ALA A . n 
A 1 1293 VAL 1293 1291 1291 VAL VAL A . n 
A 1 1294 LEU 1294 1292 1292 LEU LEU A . n 
A 1 1295 LYS 1295 1293 1293 LYS LYS A . n 
A 1 1296 ALA 1296 1294 1294 ALA ALA A . n 
A 1 1297 GLY 1297 1295 1295 GLY GLY A . n 
A 1 1298 GLY 1298 1296 1296 GLY GLY A . n 
A 1 1299 ALA 1299 1297 1297 ALA ALA A . n 
A 1 1300 TYR 1300 1298 1298 TYR TYR A . n 
A 1 1301 LEU 1301 1299 1299 LEU LEU A . n 
A 1 1302 PRO 1302 1300 1300 PRO PRO A . n 
A 1 1303 ILE 1303 1301 1301 ILE ILE A . n 
A 1 1304 ASP 1304 1302 1302 ASP ASP A . n 
A 1 1305 PRO 1305 1303 1303 PRO PRO A . n 
A 1 1306 HIS 1306 1304 1304 HIS HIS A . n 
A 1 1307 SER 1307 1305 1305 SER SER A . n 
A 1 1308 PRO 1308 1306 1306 PRO PRO A . n 
A 1 1309 ALA 1309 1307 1307 ALA ALA A . n 
A 1 1310 GLU 1310 1308 1308 GLU GLU A . n 
A 1 1311 ARG 1311 1309 1309 ARG ARG A . n 
A 1 1312 ILE 1312 1310 1310 ILE ILE A . n 
A 1 1313 ALA 1313 1311 1311 ALA ALA A . n 
A 1 1314 TYR 1314 1312 1312 TYR TYR A . n 
A 1 1315 ILE 1315 1313 1313 ILE ILE A . n 
A 1 1316 PHE 1316 1314 1314 PHE PHE A . n 
A 1 1317 ALA 1317 1315 1315 ALA ALA A . n 
A 1 1318 ASP 1318 1316 1316 ASP ASP A . n 
A 1 1319 SER 1319 1317 1317 SER SER A . n 
A 1 1320 GLY 1320 1318 1318 GLY GLY A . n 
A 1 1321 ALA 1321 1319 1319 ALA ALA A . n 
A 1 1322 LYS 1322 1320 1320 LYS LYS A . n 
A 1 1323 LEU 1323 1321 1321 LEU LEU A . n 
A 1 1324 VAL 1324 1322 1322 VAL VAL A . n 
A 1 1325 LEU 1325 1323 1323 LEU LEU A . n 
A 1 1326 ALA 1326 1324 1324 ALA ALA A . n 
A 1 1327 GLN 1327 1325 1325 GLN GLN A . n 
A 1 1328 SER 1328 1326 1326 SER SER A . n 
A 1 1329 PRO 1329 1327 1327 PRO PRO A . n 
A 1 1330 PHE 1330 1328 1328 PHE PHE A . n 
A 1 1331 VAL 1331 1329 1329 VAL VAL A . n 
A 1 1332 GLU 1332 1330 1330 GLU GLU A . n 
A 1 1333 LYS 1333 1331 1331 LYS LYS A . n 
A 1 1334 ALA 1334 1332 1332 ALA ALA A . n 
A 1 1335 SER 1335 1333 1333 SER SER A . n 
A 1 1336 MET 1336 1334 1334 MET MET A . n 
A 1 1337 ALA 1337 1335 1335 ALA ALA A . n 
A 1 1338 GLU 1338 1336 1336 GLU GLU A . n 
A 1 1339 VAL 1339 1337 1337 VAL VAL A . n 
A 1 1340 VAL 1340 1338 1338 VAL VAL A . n 
A 1 1341 LEU 1341 1339 1339 LEU LEU A . n 
A 1 1342 ASP 1342 1340 1340 ASP ASP A . n 
A 1 1343 LEU 1343 1341 1341 LEU LEU A . n 
A 1 1344 ASN 1344 1342 1342 ASN ASN A . n 
A 1 1345 SER 1345 1343 1343 SER SER A . n 
A 1 1346 ALA 1346 1344 1344 ALA ALA A . n 
A 1 1347 SER 1347 1345 1345 SER SER A . n 
A 1 1348 SER 1348 1346 1346 SER SER A . n 
A 1 1349 TYR 1349 1347 1347 TYR TYR A . n 
A 1 1350 ALA 1350 1348 1348 ALA ALA A . n 
A 1 1351 ALA 1351 1349 1349 ALA ALA A . n 
A 1 1352 ASP 1352 1350 1350 ASP ASP A . n 
A 1 1353 THR 1353 1351 1351 THR THR A . n 
A 1 1354 SER 1354 1352 1352 SER SER A . n 
A 1 1355 ASN 1355 1353 1353 ASN ASN A . n 
A 1 1356 PRO 1356 1354 1354 PRO PRO A . n 
A 1 1357 PRO 1357 1355 1355 PRO PRO A . n 
A 1 1358 LEU 1358 1356 1356 LEU LEU A . n 
A 1 1359 VAL 1359 1357 1357 VAL VAL A . n 
A 1 1360 ASN 1360 1358 1358 ASN ASN A . n 
A 1 1361 GLN 1361 1359 1359 GLN GLN A . n 
A 1 1362 PRO 1362 1360 1360 PRO PRO A . n 
A 1 1363 GLY 1363 1361 1361 GLY GLY A . n 
A 1 1364 ASP 1364 1362 1362 ASP ASP A . n 
A 1 1365 LEU 1365 1363 1363 LEU LEU A . n 
A 1 1366 VAL 1366 1364 1364 VAL VAL A . n 
A 1 1367 TYR 1367 1365 1365 TYR TYR A . n 
A 1 1368 VAL 1368 1366 1366 VAL VAL A . n 
A 1 1369 MET 1369 1367 1367 MET MET A . n 
A 1 1370 TYR 1370 1368 1368 TYR TYR A . n 
A 1 1371 THR 1371 1369 1369 THR THR A . n 
A 1 1372 SER 1372 1370 ?    ?   ?   A . n 
A 1 1373 GLY 1373 1371 ?    ?   ?   A . n 
A 1 1374 SER 1374 1372 ?    ?   ?   A . n 
A 1 1375 THR 1375 1373 ?    ?   ?   A . n 
A 1 1376 GLY 1376 1374 1374 GLY GLY A . n 
A 1 1377 LYS 1377 1375 1375 LYS LYS A . n 
A 1 1378 PRO 1378 1376 1376 PRO PRO A . n 
A 1 1379 LYS 1379 1377 1377 LYS LYS A . n 
A 1 1380 GLY 1380 1378 1378 GLY GLY A . n 
A 1 1381 VAL 1381 1379 1379 VAL VAL A . n 
A 1 1382 MET 1382 1380 1380 MET MET A . n 
A 1 1383 ILE 1383 1381 1381 ILE ILE A . n 
A 1 1384 GLU 1384 1382 1382 GLU GLU A . n 
A 1 1385 HIS 1385 1383 1383 HIS HIS A . n 
A 1 1386 GLY 1386 1384 1384 GLY GLY A . n 
A 1 1387 ALA 1387 1385 1385 ALA ALA A . n 
A 1 1388 LEU 1388 1386 1386 LEU LEU A . n 
A 1 1389 LEU 1389 1387 1387 LEU LEU A . n 
A 1 1390 ASN 1390 1388 1388 ASN ASN A . n 
A 1 1391 VAL 1391 1389 1389 VAL VAL A . n 
A 1 1392 LEU 1392 1390 1390 LEU LEU A . n 
A 1 1393 HIS 1393 1391 1391 HIS HIS A . n 
A 1 1394 GLY 1394 1392 1392 GLY GLY A . n 
A 1 1395 MET 1395 1393 1393 MET MET A . n 
A 1 1396 GLN 1396 1394 1394 GLN GLN A . n 
A 1 1397 ASP 1397 1395 1395 ASP ASP A . n 
A 1 1398 GLU 1398 1396 1396 GLU GLU A . n 
A 1 1399 TYR 1399 1397 1397 TYR TYR A . n 
A 1 1400 PRO 1400 1398 1398 PRO PRO A . n 
A 1 1401 LEU 1401 1399 1399 LEU LEU A . n 
A 1 1402 LEU 1402 1400 1400 LEU LEU A . n 
A 1 1403 GLN 1403 1401 1401 GLN GLN A . n 
A 1 1404 ASP 1404 1402 1402 ASP ASP A . n 
A 1 1405 ASP 1405 1403 1403 ASP ASP A . n 
A 1 1406 ALA 1406 1404 1404 ALA ALA A . n 
A 1 1407 PHE 1407 1405 1405 PHE PHE A . n 
A 1 1408 LEU 1408 1406 1406 LEU LEU A . n 
A 1 1409 LEU 1409 1407 1407 LEU LEU A . n 
A 1 1410 LYS 1410 1408 1408 LYS LYS A . n 
A 1 1411 THR 1411 1409 1409 THR THR A . n 
A 1 1412 THR 1412 1410 1410 THR THR A . n 
A 1 1413 TYR 1413 1411 1411 TYR TYR A . n 
A 1 1414 ILE 1414 1412 1412 ILE ILE A . n 
A 1 1415 PHE 1415 1413 1413 PHE PHE A . n 
A 1 1416 ASP 1416 1414 1414 ASP ASP A . n 
A 1 1417 ILE 1417 1415 1415 ILE ILE A . n 
A 1 1418 SER 1418 1416 1416 SER SER A . n 
A 1 1419 VAL 1419 1417 1417 VAL VAL A . n 
A 1 1420 ALA 1420 1418 1418 ALA ALA A . n 
A 1 1421 GLU 1421 1419 1419 GLU GLU A . n 
A 1 1422 ILE 1422 1420 1420 ILE ILE A . n 
A 1 1423 PHE 1423 1421 1421 PHE PHE A . n 
A 1 1424 GLY 1424 1422 1422 GLY GLY A . n 
A 1 1425 TRP 1425 1423 1423 TRP TRP A . n 
A 1 1426 VAL 1426 1424 1424 VAL VAL A . n 
A 1 1427 PRO 1427 1425 1425 PRO PRO A . n 
A 1 1428 GLY 1428 1426 1426 GLY GLY A . n 
A 1 1429 ARG 1429 1427 1427 ARG ARG A . n 
A 1 1430 GLY 1430 1428 1428 GLY GLY A . n 
A 1 1431 LYS 1431 1429 1429 LYS LYS A . n 
A 1 1432 LEU 1432 1430 1430 LEU LEU A . n 
A 1 1433 VAL 1433 1431 1431 VAL VAL A . n 
A 1 1434 ILE 1434 1432 1432 ILE ILE A . n 
A 1 1435 LEU 1435 1433 1433 LEU LEU A . n 
A 1 1436 GLU 1436 1434 1434 GLU GLU A . n 
A 1 1437 PRO 1437 1435 1435 PRO PRO A . n 
A 1 1438 GLU 1438 1436 1436 GLU GLU A . n 
A 1 1439 ALA 1439 1437 1437 ALA ALA A . n 
A 1 1440 GLU 1440 1438 1438 GLU GLU A . n 
A 1 1441 LYS 1441 1439 1439 LYS LYS A . n 
A 1 1442 ASN 1442 1440 1440 ASN ASN A . n 
A 1 1443 PRO 1443 1441 1441 PRO PRO A . n 
A 1 1444 LYS 1444 1442 1442 LYS LYS A . n 
A 1 1445 ALA 1445 1443 1443 ALA ALA A . n 
A 1 1446 ILE 1446 1444 1444 ILE ILE A . n 
A 1 1447 TRP 1447 1445 1445 TRP TRP A . n 
A 1 1448 GLN 1448 1446 1446 GLN GLN A . n 
A 1 1449 ALA 1449 1447 1447 ALA ALA A . n 
A 1 1450 VAL 1450 1448 1448 VAL VAL A . n 
A 1 1451 VAL 1451 1449 1449 VAL VAL A . n 
A 1 1452 GLY 1452 1450 1450 GLY GLY A . n 
A 1 1453 ALA 1453 1451 1451 ALA ALA A . n 
A 1 1454 GLY 1454 1452 1452 GLY GLY A . n 
A 1 1455 ILE 1455 1453 1453 ILE ILE A . n 
A 1 1456 THR 1456 1454 1454 THR THR A . n 
A 1 1457 HIS 1457 1455 1455 HIS HIS A . n 
A 1 1458 ILE 1458 1456 1456 ILE ILE A . n 
A 1 1459 ASN 1459 1457 1457 ASN ASN A . n 
A 1 1460 PHE 1460 1458 1458 PHE PHE A . n 
A 1 1461 VAL 1461 1459 1459 VAL VAL A . n 
A 1 1462 PRO 1462 1460 1460 PRO PRO A . n 
A 1 1463 SER 1463 1461 1461 SER SER A . n 
A 1 1464 MET 1464 1462 1462 MET MET A . n 
A 1 1465 LEU 1465 1463 1463 LEU LEU A . n 
A 1 1466 ILE 1466 1464 1464 ILE ILE A . n 
A 1 1467 PRO 1467 1465 1465 PRO PRO A . n 
A 1 1468 PHE 1468 1466 1466 PHE PHE A . n 
A 1 1469 VAL 1469 1467 1467 VAL VAL A . n 
A 1 1470 GLU 1470 1468 1468 GLU GLU A . n 
A 1 1471 TYR 1471 1469 1469 TYR TYR A . n 
A 1 1472 LEU 1472 1470 1470 LEU LEU A . n 
A 1 1473 GLU 1473 1471 1471 GLU GLU A . n 
A 1 1474 GLY 1474 1472 1472 GLY GLY A . n 
A 1 1475 ARG 1475 1473 1473 ARG ARG A . n 
A 1 1476 THR 1476 1474 1474 THR THR A . n 
A 1 1477 GLU 1477 1475 1475 GLU GLU A . n 
A 1 1478 ALA 1478 1476 1476 ALA ALA A . n 
A 1 1479 ASN 1479 1477 1477 ASN ASN A . n 
A 1 1480 ARG 1480 1478 1478 ARG ARG A . n 
A 1 1481 LEU 1481 1479 1479 LEU LEU A . n 
A 1 1482 ARG 1482 1480 1480 ARG ARG A . n 
A 1 1483 TYR 1483 1481 1481 TYR TYR A . n 
A 1 1484 ILE 1484 1482 1482 ILE ILE A . n 
A 1 1485 LEU 1485 1483 1483 LEU LEU A . n 
A 1 1486 ALA 1486 1484 1484 ALA ALA A . n 
A 1 1487 CYS 1487 1485 1485 CYS CYS A . n 
A 1 1488 GLY 1488 1486 1486 GLY GLY A . n 
A 1 1489 GLU 1489 1487 1487 GLU GLU A . n 
A 1 1490 ALA 1490 1488 1488 ALA ALA A . n 
A 1 1491 MET 1491 1489 1489 MET MET A . n 
A 1 1492 PRO 1492 1490 1490 PRO PRO A . n 
A 1 1493 ASP 1493 1491 1491 ASP ASP A . n 
A 1 1494 GLU 1494 1492 1492 GLU GLU A . n 
A 1 1495 LEU 1495 1493 1493 LEU LEU A . n 
A 1 1496 VAL 1496 1494 1494 VAL VAL A . n 
A 1 1497 PRO 1497 1495 1495 PRO PRO A . n 
A 1 1498 LYS 1498 1496 1496 LYS LYS A . n 
A 1 1499 VAL 1499 1497 1497 VAL VAL A . n 
A 1 1500 TYR 1500 1498 1498 TYR TYR A . n 
A 1 1501 GLU 1501 1499 1499 GLU GLU A . n 
A 1 1502 VAL 1502 1500 1500 VAL VAL A . n 
A 1 1503 LEU 1503 1501 1501 LEU LEU A . n 
A 1 1504 PRO 1504 1502 1502 PRO PRO A . n 
A 1 1505 GLU 1505 1503 1503 GLU GLU A . n 
A 1 1506 VAL 1506 1504 1504 VAL VAL A . n 
A 1 1507 LYS 1507 1505 1505 LYS LYS A . n 
A 1 1508 LEU 1508 1506 1506 LEU LEU A . n 
A 1 1509 GLU 1509 1507 1507 GLU GLU A . n 
A 1 1510 ASN 1510 1508 1508 ASN ASN A . n 
A 1 1511 ILE 1511 1509 1509 ILE ILE A . n 
A 1 1512 TYR 1512 1510 1510 TYR TYR A . n 
A 1 1513 GLY 1513 1511 1511 GLY GLY A . n 
A 1 1514 PRO 1514 1512 1512 PRO PRO A . n 
A 1 1515 THR 1515 1513 1513 THR THR A . n 
A 1 1516 GLU 1516 1514 1514 GLU GLU A . n 
A 1 1517 ALA 1517 1515 1515 ALA ALA A . n 
A 1 1518 THR 1518 1516 1516 THR THR A . n 
A 1 1519 ILE 1519 1517 1517 ILE ILE A . n 
A 1 1520 TYR 1520 1518 1518 TYR TYR A . n 
A 1 1521 ALA 1521 1519 1519 ALA ALA A . n 
A 1 1522 SER 1522 1520 1520 SER SER A . n 
A 1 1523 ARG 1523 1521 1521 ARG ARG A . n 
A 1 1524 TYR 1524 1522 1522 TYR TYR A . n 
A 1 1525 SER 1525 1523 1523 SER SER A . n 
A 1 1526 LEU 1526 1524 1524 LEU LEU A . n 
A 1 1527 ALA 1527 1525 1525 ALA ALA A . n 
A 1 1528 LYS 1528 1526 1526 LYS LYS A . n 
A 1 1529 GLY 1529 1527 1527 GLY GLY A . n 
A 1 1530 SER 1530 1528 1528 SER SER A . n 
A 1 1531 GLN 1531 1529 1529 GLN GLN A . n 
A 1 1532 GLU 1532 1530 1530 GLU GLU A . n 
A 1 1533 SER 1533 1531 1531 SER SER A . n 
A 1 1534 PRO 1534 1532 1532 PRO PRO A . n 
A 1 1535 VAL 1535 1533 1533 VAL VAL A . n 
A 1 1536 PRO 1536 1534 1534 PRO PRO A . n 
A 1 1537 ILE 1537 1535 1535 ILE ILE A . n 
A 1 1538 GLY 1538 1536 1536 GLY GLY A . n 
A 1 1539 LYS 1539 1537 1537 LYS LYS A . n 
A 1 1540 PRO 1540 1538 1538 PRO PRO A . n 
A 1 1541 LEU 1541 1539 1539 LEU LEU A . n 
A 1 1542 PRO 1542 1540 1540 PRO PRO A . n 
A 1 1543 ASN 1543 1541 1541 ASN ASN A . n 
A 1 1544 TYR 1544 1542 1542 TYR TYR A . n 
A 1 1545 ARG 1545 1543 1543 ARG ARG A . n 
A 1 1546 MET 1546 1544 1544 MET MET A . n 
A 1 1547 TYR 1547 1545 1545 TYR TYR A . n 
A 1 1548 ILE 1548 1546 1546 ILE ILE A . n 
A 1 1549 ILE 1549 1547 1547 ILE ILE A . n 
A 1 1550 ASN 1550 1548 1548 ASN ASN A . n 
A 1 1551 ARG 1551 1549 1549 ARG ARG A . n 
A 1 1552 HIS 1552 1550 1550 HIS HIS A . n 
A 1 1553 GLY 1553 1551 1551 GLY GLY A . n 
A 1 1554 GLN 1554 1552 1552 GLN GLN A . n 
A 1 1555 LEU 1555 1553 1553 LEU LEU A . n 
A 1 1556 GLN 1556 1554 1554 GLN GLN A . n 
A 1 1557 PRO 1557 1555 1555 PRO PRO A . n 
A 1 1558 ILE 1558 1556 1556 ILE ILE A . n 
A 1 1559 GLY 1559 1557 1557 GLY GLY A . n 
A 1 1560 VAL 1560 1558 1558 VAL VAL A . n 
A 1 1561 PRO 1561 1559 1559 PRO PRO A . n 
A 1 1562 GLY 1562 1560 1560 GLY GLY A . n 
A 1 1563 GLU 1563 1561 1561 GLU GLU A . n 
A 1 1564 LEU 1564 1562 1562 LEU LEU A . n 
A 1 1565 CYS 1565 1563 1563 CYS CYS A . n 
A 1 1566 ILE 1566 1564 1564 ILE ILE A . n 
A 1 1567 ALA 1567 1565 1565 ALA ALA A . n 
A 1 1568 GLY 1568 1566 1566 GLY GLY A . n 
A 1 1569 ALA 1569 1567 1567 ALA ALA A . n 
A 1 1570 SER 1570 1568 1568 SER SER A . n 
A 1 1571 LEU 1571 1569 1569 LEU LEU A . n 
A 1 1572 ALA 1572 1570 1570 ALA ALA A . n 
A 1 1573 ARG 1573 1571 1571 ARG ARG A . n 
A 1 1574 GLY 1574 1572 1572 GLY GLY A . n 
A 1 1575 TYR 1575 1573 1573 TYR TYR A . n 
A 1 1576 LEU 1576 1574 1574 LEU LEU A . n 
A 1 1577 ASN 1577 1575 1575 ASN ASN A . n 
A 1 1578 ASN 1578 1576 1576 ASN ASN A . n 
A 1 1579 PRO 1579 1577 1577 PRO PRO A . n 
A 1 1580 ALA 1580 1578 1578 ALA ALA A . n 
A 1 1581 LEU 1581 1579 1579 LEU LEU A . n 
A 1 1582 THR 1582 1580 1580 THR THR A . n 
A 1 1583 GLU 1583 1581 1581 GLU GLU A . n 
A 1 1584 GLU 1584 1582 1582 GLU GLU A . n 
A 1 1585 LYS 1585 1583 1583 LYS LYS A . n 
A 1 1586 PHE 1586 1584 1584 PHE PHE A . n 
A 1 1587 THR 1587 1585 1585 THR THR A . n 
A 1 1588 PRO 1588 1586 1586 PRO PRO A . n 
A 1 1589 HIS 1589 1587 1587 HIS HIS A . n 
A 1 1590 PRO 1590 1588 1588 PRO PRO A . n 
A 1 1591 LEU 1591 1589 1589 LEU LEU A . n 
A 1 1592 GLU 1592 1590 1590 GLU GLU A . n 
A 1 1593 LYS 1593 1591 1591 LYS LYS A . n 
A 1 1594 GLY 1594 1592 1592 GLY GLY A . n 
A 1 1595 GLU 1595 1593 1593 GLU GLU A . n 
A 1 1596 ARG 1596 1594 1594 ARG ARG A . n 
A 1 1597 ILE 1597 1595 1595 ILE ILE A . n 
A 1 1598 TYR 1598 1596 1596 TYR TYR A . n 
A 1 1599 ARG 1599 1597 1597 ARG ARG A . n 
A 1 1600 THR 1600 1598 1598 THR THR A . n 
A 1 1601 GLY 1601 1599 1599 GLY GLY A . n 
A 1 1602 ASP 1602 1600 1600 ASP ASP A . n 
A 1 1603 LEU 1603 1601 1601 LEU LEU A . n 
A 1 1604 ALA 1604 1602 1602 ALA ALA A . n 
A 1 1605 ARG 1605 1603 1603 ARG ARG A . n 
A 1 1606 TYR 1606 1604 1604 TYR TYR A . n 
A 1 1607 ARG 1607 1605 1605 ARG ARG A . n 
A 1 1608 GLU 1608 1606 1606 GLU GLU A . n 
A 1 1609 ASP 1609 1607 1607 ASP ASP A . n 
A 1 1610 GLY 1610 1608 1608 GLY GLY A . n 
A 1 1611 ASN 1611 1609 1609 ASN ASN A . n 
A 1 1612 ILE 1612 1610 1610 ILE ILE A . n 
A 1 1613 GLU 1613 1611 1611 GLU GLU A . n 
A 1 1614 TYR 1614 1612 1612 TYR TYR A . n 
A 1 1615 LEU 1615 1613 1613 LEU LEU A . n 
A 1 1616 GLY 1616 1614 1614 GLY GLY A . n 
A 1 1617 ARG 1617 1615 1615 ARG ARG A . n 
A 1 1618 MET 1618 1616 1616 MET MET A . n 
A 1 1619 ASP 1619 1617 1617 ASP ASP A . n 
A 1 1620 HIS 1620 1618 1618 HIS HIS A . n 
A 1 1621 GLN 1621 1619 1619 GLN GLN A . n 
A 1 1622 VAL 1622 1620 1620 VAL VAL A . n 
A 1 1623 LYS 1623 1621 1621 LYS LYS A . n 
A 1 1624 ILE 1624 1622 1622 ILE ILE A . n 
A 1 1625 ARG 1625 1623 1623 ARG ARG A . n 
A 1 1626 GLY 1626 1624 1624 GLY GLY A . n 
A 1 1627 TYR 1627 1625 1625 TYR TYR A . n 
A 1 1628 ARG 1628 1626 1626 ARG ARG A . n 
A 1 1629 ILE 1629 1627 1627 ILE ILE A . n 
A 1 1630 GLU 1630 1628 1628 GLU GLU A . n 
A 1 1631 LEU 1631 1629 1629 LEU LEU A . n 
A 1 1632 ASP 1632 1630 1630 ASP ASP A . n 
A 1 1633 GLU 1633 1631 1631 GLU GLU A . n 
A 1 1634 ILE 1634 1632 1632 ILE ILE A . n 
A 1 1635 ARG 1635 1633 1633 ARG ARG A . n 
A 1 1636 SER 1636 1634 1634 SER SER A . n 
A 1 1637 LYS 1637 1635 1635 LYS LYS A . n 
A 1 1638 LEU 1638 1636 1636 LEU LEU A . n 
A 1 1639 ILE 1639 1637 1637 ILE ILE A . n 
A 1 1640 GLN 1640 1638 1638 GLN GLN A . n 
A 1 1641 GLU 1641 1639 1639 GLU GLU A . n 
A 1 1642 GLU 1642 1640 1640 GLU GLU A . n 
A 1 1643 THR 1643 1641 1641 THR THR A . n 
A 1 1644 ILE 1644 1642 1642 ILE ILE A . n 
A 1 1645 GLN 1645 1643 1643 GLN GLN A . n 
A 1 1646 ASP 1646 1644 1644 ASP ASP A . n 
A 1 1647 ALA 1647 1645 1645 ALA ALA A . n 
A 1 1648 VAL 1648 1646 1646 VAL VAL A . n 
A 1 1649 VAL 1649 1647 1647 VAL VAL A . n 
A 1 1650 VAL 1650 1648 1648 VAL VAL A . n 
A 1 1651 ALA 1651 1649 1649 ALA ALA A . n 
A 1 1652 ARG 1652 1650 1650 ARG ARG A . n 
A 1 1653 ASN 1653 1651 1651 ASN ASN A . n 
A 1 1654 ASP 1654 1652 1652 ASP ALA A . n 
A 1 1655 GLN 1655 1653 ?    ?   ?   A . n 
A 1 1656 ASN 1656 1654 ?    ?   ?   A . n 
A 1 1657 GLY 1657 1655 ?    ?   ?   A . n 
A 1 1658 GLN 1658 1656 ?    ?   ?   A . n 
A 1 1659 ALA 1659 1657 1657 ALA ALA A . n 
A 1 1660 TYR 1660 1658 1658 TYR TYR A . n 
A 1 1661 LEU 1661 1659 1659 LEU LEU A . n 
A 1 1662 CYS 1662 1660 1660 CYS CYS A . n 
A 1 1663 ALA 1663 1661 1661 ALA ALA A . n 
A 1 1664 TYR 1664 1662 ?    ?   ?   A . n 
A 1 1665 LEU 1665 1663 ?    ?   ?   A . n 
A 1 1666 LEU 1666 1664 ?    ?   ?   A . n 
A 1 1667 SER 1667 1665 ?    ?   ?   A . n 
A 1 1668 GLU 1668 1666 ?    ?   ?   A . n 
A 1 1669 GLN 1669 1667 1667 GLN GLN A . n 
A 1 1670 GLU 1670 1668 1668 GLU GLU A . n 
A 1 1671 TRP 1671 1669 1669 TRP TRP A . n 
A 1 1672 THR 1672 1670 1670 THR THR A . n 
A 1 1673 VAL 1673 1671 1671 VAL VAL A . n 
A 1 1674 GLY 1674 1672 1672 GLY GLY A . n 
A 1 1675 GLN 1675 1673 1673 GLN GLN A . n 
A 1 1676 LEU 1676 1674 1674 LEU LEU A . n 
A 1 1677 ARG 1677 1675 1675 ARG ARG A . n 
A 1 1678 GLU 1678 1676 1676 GLU GLU A . n 
A 1 1679 LEU 1679 1677 1677 LEU LEU A . n 
A 1 1680 LEU 1680 1678 1678 LEU LEU A . n 
A 1 1681 ARG 1681 1679 1679 ARG ARG A . n 
A 1 1682 ARG 1682 1680 1680 ARG ARG A . n 
A 1 1683 GLU 1683 1681 1681 GLU GLU A . n 
A 1 1684 LEU 1684 1682 1682 LEU LEU A . n 
A 1 1685 PRO 1685 1683 1683 PRO PRO A . n 
A 1 1686 GLU 1686 1684 1684 GLU GLU A . n 
A 1 1687 TYR 1687 1685 1685 TYR TYR A . n 
A 1 1688 MET 1688 1686 1686 MET MET A . n 
A 1 1689 ILE 1689 1687 1687 ILE ILE A . n 
A 1 1690 PRO 1690 1688 1688 PRO PRO A . n 
A 1 1691 ALA 1691 1689 1689 ALA ALA A . n 
A 1 1692 HIS 1692 1690 1690 HIS HIS A . n 
A 1 1693 PHE 1693 1691 1691 PHE PHE A . n 
A 1 1694 VAL 1694 1692 ?    ?   ?   A . n 
A 1 1695 LEU 1695 1693 ?    ?   ?   A . n 
A 1 1696 LEU 1696 1694 ?    ?   ?   A . n 
A 1 1697 LYS 1697 1695 ?    ?   ?   A . n 
A 1 1698 GLN 1698 1696 ?    ?   ?   A . n 
A 1 1699 PHE 1699 1697 ?    ?   ?   A . n 
A 1 1700 PRO 1700 1698 ?    ?   ?   A . n 
A 1 1701 LEU 1701 1699 ?    ?   ?   A . n 
A 1 1702 THR 1702 1700 ?    ?   ?   A . n 
A 1 1703 ALA 1703 1701 ?    ?   ?   A . n 
A 1 1704 ASN 1704 1702 ?    ?   ?   A . n 
A 1 1705 GLY 1705 1703 ?    ?   ?   A . n 
A 1 1706 LYS 1706 1704 ?    ?   ?   A . n 
A 1 1707 LEU 1707 1705 ?    ?   ?   A . n 
A 1 1708 ASP 1708 1706 ?    ?   ?   A . n 
A 1 1709 ARG 1709 1707 ?    ?   ?   A . n 
A 1 1710 LYS 1710 1708 ?    ?   ?   A . n 
A 1 1711 ALA 1711 1709 ?    ?   ?   A . n 
A 1 1712 LEU 1712 1710 ?    ?   ?   A . n 
A 1 1713 PRO 1713 1711 ?    ?   ?   A . n 
A 1 1714 GLU 1714 1712 ?    ?   ?   A . n 
A 1 1715 PRO 1715 1713 ?    ?   ?   A . n 
A 1 1716 ASP 1716 1714 ?    ?   ?   A . n 
A 1 1717 GLY 1717 1715 ?    ?   ?   A . n 
A 1 1718 SER 1718 1716 ?    ?   ?   A . n 
A 1 1719 VAL 1719 1717 ?    ?   ?   A . n 
A 1 1720 LYS 1720 1718 ?    ?   ?   A . n 
A 1 1721 ALA 1721 1719 ?    ?   ?   A . n 
A 1 1722 GLU 1722 1720 ?    ?   ?   A . n 
A 1 1723 ALA 1723 1721 ?    ?   ?   A . n 
A 1 1724 GLU 1724 1722 ?    ?   ?   A . n 
A 1 1725 TYR 1725 1723 ?    ?   ?   A . n 
A 1 1726 ALA 1726 1724 1724 ALA ALA A . n 
A 1 1727 ALA 1727 1725 1725 ALA ALA A . n 
A 1 1728 PRO 1728 1726 1726 PRO PRO A . n 
A 1 1729 ARG 1729 1727 1727 ARG ARG A . n 
A 1 1730 THR 1730 1728 1728 THR THR A . n 
A 1 1731 GLU 1731 1729 1729 GLU GLU A . n 
A 1 1732 LEU 1732 1730 1730 LEU LEU A . n 
A 1 1733 GLU 1733 1731 1731 GLU GLU A . n 
A 1 1734 ALA 1734 1732 1732 ALA ALA A . n 
A 1 1735 THR 1735 1733 1733 THR THR A . n 
A 1 1736 LEU 1736 1734 1734 LEU LEU A . n 
A 1 1737 ALA 1737 1735 1735 ALA ALA A . n 
A 1 1738 HIS 1738 1736 1736 HIS HIS A . n 
A 1 1739 ILE 1739 1737 1737 ILE ILE A . n 
A 1 1740 TRP 1740 1738 1738 TRP TRP A . n 
A 1 1741 GLY 1741 1739 1739 GLY GLY A . n 
A 1 1742 GLU 1742 1740 1740 GLU GLU A . n 
A 1 1743 VAL 1743 1741 1741 VAL VAL A . n 
A 1 1744 LEU 1744 1742 1742 LEU LEU A . n 
A 1 1745 GLY 1745 1743 1743 GLY GLY A . n 
A 1 1746 ILE 1746 1744 1744 ILE ILE A . n 
A 1 1747 GLU 1747 1745 1745 GLU GLU A . n 
A 1 1748 ARG 1748 1746 1746 ARG ARG A . n 
A 1 1749 ILE 1749 1747 1747 ILE ILE A . n 
A 1 1750 GLY 1750 1748 1748 GLY GLY A . n 
A 1 1751 ILE 1751 1749 1749 ILE ILE A . n 
A 1 1752 ARG 1752 1750 1750 ARG ARG A . n 
A 1 1753 ASP 1753 1751 1751 ASP ASP A . n 
A 1 1754 ASN 1754 1752 1752 ASN ASN A . n 
A 1 1755 PHE 1755 1753 1753 PHE PHE A . n 
A 1 1756 PHE 1756 1754 1754 PHE PHE A . n 
A 1 1757 GLU 1757 1755 1755 GLU GLU A . n 
A 1 1758 LEU 1758 1756 1756 LEU LEU A . n 
A 1 1759 GLY 1759 1757 1757 GLY GLY A . n 
A 1 1760 GLY 1760 1758 1758 GLY GLY A . n 
A 1 1761 ASP 1761 1759 1759 ASP ASP A . n 
A 1 1762 SER 1762 1760 1760 SER SER A . n 
A 1 1763 ILE 1763 1761 1761 ILE ILE A . n 
A 1 1764 LYS 1764 1762 1762 LYS LYS A . n 
A 1 1765 GLY 1765 1763 1763 GLY GLY A . n 
A 1 1766 LEU 1766 1764 1764 LEU LEU A . n 
A 1 1767 GLN 1767 1765 1765 GLN GLN A . n 
A 1 1768 ILE 1768 1766 1766 ILE ILE A . n 
A 1 1769 ALA 1769 1767 1767 ALA ALA A . n 
A 1 1770 SER 1770 1768 1768 SER SER A . n 
A 1 1771 ARG 1771 1769 1769 ARG ARG A . n 
A 1 1772 LEU 1772 1770 1770 LEU LEU A . n 
A 1 1773 GLN 1773 1771 1771 GLN GLN A . n 
A 1 1774 ARG 1774 1772 1772 ARG ARG A . n 
A 1 1775 ILE 1775 1773 1773 ILE ILE A . n 
A 1 1776 ASN 1776 1774 1774 ASN ASN A . n 
A 1 1777 TRP 1777 1775 1775 TRP TRP A . n 
A 1 1778 THR 1778 1776 1776 THR THR A . n 
A 1 1779 MET 1779 1777 1777 MET MET A . n 
A 1 1780 VAL 1780 1778 1778 VAL VAL A . n 
A 1 1781 ILE 1781 1779 1779 ILE ILE A . n 
A 1 1782 ASN 1782 1780 1780 ASN ASN A . n 
A 1 1783 HIS 1783 1781 1781 HIS HIS A . n 
A 1 1784 LEU 1784 1782 1782 LEU LEU A . n 
A 1 1785 PHE 1785 1783 1783 PHE PHE A . n 
A 1 1786 LEU 1786 1784 1784 LEU LEU A . n 
A 1 1787 TYR 1787 1785 1785 TYR TYR A . n 
A 1 1788 PRO 1788 1786 1786 PRO PRO A . n 
A 1 1789 THR 1789 1787 1787 THR THR A . n 
A 1 1790 ILE 1790 1788 1788 ILE ILE A . n 
A 1 1791 GLU 1791 1789 1789 GLU GLU A . n 
A 1 1792 GLN 1792 1790 1790 GLN GLN A . n 
A 1 1793 ILE 1793 1791 1791 ILE ILE A . n 
A 1 1794 ALA 1794 1792 1792 ALA ALA A . n 
A 1 1795 PRO 1795 1793 1793 PRO PRO A . n 
A 1 1796 PHE 1796 1794 1794 PHE PHE A . n 
A 1 1797 VAL 1797 1795 1795 VAL VAL A . n 
A 1 1798 THR 1798 1796 1796 THR THR A . n 
A 1 1799 SER 1799 1797 1797 SER SER A . n 
A 1 1800 GLU 1800 1798 1798 GLU GLU A . n 
A 1 1801 GLN 1801 1799 1799 GLN GLN A . n 
A 1 1802 VAL 1802 1800 1800 VAL VAL A . n 
A 1 1803 VAL 1803 1801 1801 VAL VAL A . n 
A 1 1804 ILE 1804 1802 1802 ILE ILE A . n 
A 1 1805 GLU 1805 1803 1803 GLU GLU A . n 
A 1 1806 ALA 1806 1804 1804 ALA ALA A . n 
A 1 1807 ALA 1807 1805 1805 ALA ALA A . n 
A 1 1808 ALA 1808 1806 1806 ALA ALA A . n 
A 1 1809 GLU 1809 1807 1807 GLU GLU A . n 
A 1 1810 ASN 1810 1808 1808 ASN ASN A . n 
A 1 1811 LEU 1811 1809 1809 LEU LEU A . n 
A 1 1812 TYR 1812 1810 1810 TYR TYR A . n 
A 1 1813 PHE 1813 1811 1811 PHE PHE A . n 
A 1 1814 GLN 1814 1812 1812 GLN GLN A . n 
B 1 1    MET 1    1    1    MET MET B . n 
B 1 2    GLY 2    2    2    GLY GLY B . n 
B 1 3    ARG 3    3    3    ARG ARG B . n 
B 1 4    ILE 4    4    4    ILE ILE B . n 
B 1 5    LEU 5    5    5    LEU LEU B . n 
B 1 6    PHE 6    6    6    PHE PHE B . n 
B 1 7    LEU 7    7    7    LEU LEU B . n 
B 1 8    THR 8    8    8    THR THR B . n 
B 1 9    THR 9    9    9    THR THR B . n 
B 1 10   PHE 10   10   10   PHE PHE B . n 
B 1 11   MET 11   11   11   MET MET B . n 
B 1 12   SER 12   12   12   SER SER B . n 
B 1 13   LYS 13   13   13   LYS LYS B . n 
B 1 14   GLY 14   14   14   GLY GLY B . n 
B 1 15   ASN 15   15   15   ASN ASN B . n 
B 1 16   LYS 16   16   16   LYS LYS B . n 
B 1 17   VAL 17   17   17   VAL VAL B . n 
B 1 18   VAL 18   18   18   VAL VAL B . n 
B 1 19   ARG 19   19   19   ARG ARG B . n 
B 1 20   TYR 20   20   20   TYR TYR B . n 
B 1 21   LEU 21   21   21   LEU LEU B . n 
B 1 22   GLU 22   22   22   GLU GLU B . n 
B 1 23   SER 23   23   23   SER SER B . n 
B 1 24   LEU 24   24   24   LEU LEU B . n 
B 1 25   HIS 25   25   25   HIS HIS B . n 
B 1 26   HIS 26   26   26   HIS HIS B . n 
B 1 27   GLU 27   27   27   GLU GLU B . n 
B 1 28   VAL 28   28   28   VAL VAL B . n 
B 1 29   VAL 29   29   29   VAL VAL B . n 
B 1 30   ILE 30   30   30   ILE ILE B . n 
B 1 31   CYS 31   31   31   CYS CYS B . n 
B 1 32   GLN 32   32   32   GLN GLN B . n 
B 1 33   GLU 33   33   33   GLU GLU B . n 
B 1 34   LYS 34   34   34   LYS LYS B . n 
B 1 35   VAL 35   35   35   VAL VAL B . n 
B 1 36   HIS 36   36   36   HIS HIS B . n 
B 1 37   ALA 37   37   37   ALA ALA B . n 
B 1 38   GLN 38   38   38   GLN GLN B . n 
B 1 39   SER 39   39   39   SER SER B . n 
B 1 40   ALA 40   40   40   ALA ALA B . n 
B 1 41   ASN 41   41   41   ASN ASN B . n 
B 1 42   LEU 42   42   42   LEU LEU B . n 
B 1 43   GLN 43   43   43   GLN GLN B . n 
B 1 44   GLU 44   44   44   GLU GLU B . n 
B 1 45   ILE 45   45   45   ILE ILE B . n 
B 1 46   ASP 46   46   46   ASP ASP B . n 
B 1 47   TRP 47   47   47   TRP TRP B . n 
B 1 48   ILE 48   48   48   ILE ILE B . n 
B 1 49   VAL 49   49   49   VAL VAL B . n 
B 1 50   SER 50   50   50   SER SER B . n 
B 1 51   TYR 51   51   51   TYR TYR B . n 
B 1 52   ALA 52   52   52   ALA ALA B . n 
B 1 53   TYR 53   53   53   TYR TYR B . n 
B 1 54   GLY 54   54   54   GLY GLY B . n 
B 1 55   TYR 55   55   55   TYR TYR B . n 
B 1 56   ILE 56   56   56   ILE ILE B . n 
B 1 57   LEU 57   57   57   LEU LEU B . n 
B 1 58   ASP 58   58   58   ASP ASP B . n 
B 1 59   LYS 59   59   59   LYS LYS B . n 
B 1 60   GLU 60   60   60   GLU GLU B . n 
B 1 61   ILE 61   61   61   ILE ILE B . n 
B 1 62   VAL 62   62   62   VAL VAL B . n 
B 1 63   SER 63   63   63   SER SER B . n 
B 1 64   ARG 64   64   64   ARG ARG B . n 
B 1 65   PHE 65   65   65   PHE PHE B . n 
B 1 66   ARG 66   66   66   ARG ARG B . n 
B 1 67   GLY 67   67   67   GLY GLY B . n 
B 1 68   ARG 68   68   68   ARG ARG B . n 
B 1 69   ILE 69   69   69   ILE ILE B . n 
B 1 70   ILE 70   70   70   ILE ILE B . n 
B 1 71   ASN 71   71   71   ASN ASN B . n 
B 1 72   LEU 72   72   72   LEU LEU B . n 
B 1 73   HIS 73   73   73   HIS HIS B . n 
B 1 74   PRO 74   74   74   PRO PRO B . n 
B 1 75   SER 75   75   75   SER SER B . n 
B 1 76   LEU 76   76   76   LEU LEU B . n 
B 1 77   LEU 77   77   77   LEU LEU B . n 
B 1 78   PRO 78   78   78   PRO PRO B . n 
B 1 79   TRP 79   79   79   TRP TRP B . n 
B 1 80   ASN 80   80   80   ASN ASN B . n 
B 1 81   LYS 81   81   81   LYS LYS B . n 
B 1 82   GLY 82   82   82   GLY GLY B . n 
B 1 83   ARG 83   83   83   ARG ARG B . n 
B 1 84   ASP 84   84   84   ASP ASP B . n 
B 1 85   PRO 85   85   85   PRO PRO B . n 
B 1 86   VAL 86   86   86   VAL VAL B . n 
B 1 87   PHE 87   87   87   PHE PHE B . n 
B 1 88   TRP 88   88   88   TRP TRP B . n 
B 1 89   SER 89   89   89   SER SER B . n 
B 1 90   VAL 90   90   90   VAL VAL B . n 
B 1 91   TRP 91   91   91   TRP TRP B . n 
B 1 92   ASP 92   92   92   ASP ASP B . n 
B 1 93   GLU 93   93   93   GLU GLU B . n 
B 1 94   THR 94   94   94   THR THR B . n 
B 1 95   PRO 95   95   95   PRO PRO B . n 
B 1 96   LYS 96   96   96   LYS LYS B . n 
B 1 97   GLY 97   97   97   GLY GLY B . n 
B 1 98   VAL 98   98   98   VAL VAL B . n 
B 1 99   THR 99   99   99   THR THR B . n 
B 1 100  ILE 100  100  100  ILE ILE B . n 
B 1 101  HIS 101  101  101  HIS HIS B . n 
B 1 102  LEU 102  102  102  LEU LEU B . n 
B 1 103  ILE 103  103  103  ILE ILE B . n 
B 1 104  ASP 104  104  104  ASP ASP B . n 
B 1 105  GLU 105  105  105  GLU GLU B . n 
B 1 106  HIS 106  106  106  HIS HIS B . n 
B 1 107  VAL 107  107  107  VAL VAL B . n 
B 1 108  ASP 108  108  108  ASP ASP B . n 
B 1 109  THR 109  109  109  THR THR B . n 
B 1 110  GLY 110  110  110  GLY GLY B . n 
B 1 111  ASP 111  111  111  ASP ASP B . n 
B 1 112  ILE 112  112  112  ILE ILE B . n 
B 1 113  LEU 113  113  113  LEU LEU B . n 
B 1 114  VAL 114  114  114  VAL VAL B . n 
B 1 115  GLN 115  115  115  GLN GLN B . n 
B 1 116  GLU 116  116  116  GLU GLU B . n 
B 1 117  GLU 117  117  117  GLU GLU B . n 
B 1 118  ILE 118  118  118  ILE ILE B . n 
B 1 119  ALA 119  119  119  ALA ALA B . n 
B 1 120  PHE 120  120  120  PHE PHE B . n 
B 1 121  ALA 121  121  121  ALA ALA B . n 
B 1 122  ASP 122  122  122  ASP ASP B . n 
B 1 123  GLU 123  123  123  GLU GLU B . n 
B 1 124  ASP 124  124  124  ASP ASP B . n 
B 1 125  THR 125  125  125  THR THR B . n 
B 1 126  LEU 126  126  126  LEU LEU B . n 
B 1 127  LEU 127  127  127  LEU LEU B . n 
B 1 128  ASP 128  128  128  ASP ASP B . n 
B 1 129  CYS 129  129  129  CYS CYS B . n 
B 1 130  TYR 130  130  130  TYR TYR B . n 
B 1 131  ASN 131  131  131  ASN ASN B . n 
B 1 132  LYS 132  132  132  LYS LYS B . n 
B 1 133  ALA 133  133  133  ALA ALA B . n 
B 1 134  ASN 134  134  134  ASN ASN B . n 
B 1 135  GLN 135  135  135  GLN GLN B . n 
B 1 136  ALA 136  136  136  ALA ALA B . n 
B 1 137  ILE 137  137  137  ILE ILE B . n 
B 1 138  GLU 138  138  138  GLU GLU B . n 
B 1 139  GLU 139  139  139  GLU GLU B . n 
B 1 140  LEU 140  140  140  LEU LEU B . n 
B 1 141  PHE 141  141  141  PHE PHE B . n 
B 1 142  ILE 142  142  142  ILE ILE B . n 
B 1 143  ARG 143  143  143  ARG ARG B . n 
B 1 144  GLU 144  144  144  GLU GLU B . n 
B 1 145  TRP 145  145  145  TRP TRP B . n 
B 1 146  GLU 146  146  146  GLU GLU B . n 
B 1 147  ASN 147  147  147  ASN ASN B . n 
B 1 148  ILE 148  148  148  ILE ILE B . n 
B 1 149  VAL 149  149  149  VAL VAL B . n 
B 1 150  HIS 150  150  150  HIS HIS B . n 
B 1 151  GLY 151  151  151  GLY GLY B . n 
B 1 152  ARG 152  152  152  ARG ARG B . n 
B 1 153  ILE 153  153  153  ILE ILE B . n 
B 1 154  ALA 154  154  154  ALA ALA B . n 
B 1 155  PRO 155  155  155  PRO PRO B . n 
B 1 156  TYR 156  156  156  TYR TYR B . n 
B 1 157  ARG 157  157  157  ARG ARG B . n 
B 1 158  GLN 158  158  158  GLN GLN B . n 
B 1 159  THR 159  159  159  THR THR B . n 
B 1 160  ALA 160  160  160  ALA ALA B . n 
B 1 161  GLY 161  161  161  GLY GLY B . n 
B 1 162  GLY 162  162  162  GLY GLY B . n 
B 1 163  THR 163  163  163  THR THR B . n 
B 1 164  LEU 164  164  164  LEU LEU B . n 
B 1 165  HIS 165  165  165  HIS HIS B . n 
B 1 166  PHE 166  166  166  PHE PHE B . n 
B 1 167  LYS 167  167  167  LYS LYS B . n 
B 1 168  ALA 168  168  168  ALA ALA B . n 
B 1 169  ASP 169  169  169  ASP ASP B . n 
B 1 170  ARG 170  170  170  ARG ARG B . n 
B 1 171  ASP 171  171  171  ASP ASP B . n 
B 1 172  PHE 172  172  172  PHE PHE B . n 
B 1 173  TYR 173  173  173  TYR TYR B . n 
B 1 174  LYS 174  174  174  LYS LYS B . n 
B 1 175  ASN 175  175  175  ASN ASN B . n 
B 1 176  LEU 176  176  176  LEU LEU B . n 
B 1 177  ASN 177  177  177  ASN ASN B . n 
B 1 178  MET 178  178  178  MET MET B . n 
B 1 179  THR 179  179  179  THR THR B . n 
B 1 180  THR 180  180  180  THR THR B . n 
B 1 181  VAL 181  181  181  VAL VAL B . n 
B 1 182  ARG 182  182  182  ARG ARG B . n 
B 1 183  GLU 183  183  183  GLU GLU B . n 
B 1 184  LEU 184  184  184  LEU LEU B . n 
B 1 185  LEU 185  185  185  LEU LEU B . n 
B 1 186  ALA 186  186  186  ALA ALA B . n 
B 1 187  LEU 187  187  187  LEU LEU B . n 
B 1 188  LYS 188  188  188  LYS LYS B . n 
B 1 189  ARG 189  189  189  ARG ARG B . n 
B 1 190  LEU 190  190  190  LEU LEU B . n 
B 1 191  CYS 191  191  191  CYS CYS B . n 
B 1 192  ALA 192  192  192  ALA ALA B . n 
B 1 193  GLU 193  193  193  GLU GLU B . n 
B 1 194  PRO 194  194  194  PRO PRO B . n 
B 1 195  LYS 195  195  195  LYS LYS B . n 
B 1 196  ARG 196  196  ?    ?   ?   B . n 
B 1 197  GLY 197  197  ?    ?   ?   B . n 
B 1 198  GLU 198  198  198  GLU GLU B . n 
B 1 199  LYS 199  199  199  LYS LYS B . n 
B 1 200  PRO 200  200  200  PRO PRO B . n 
B 1 201  ILE 201  201  201  ILE ILE B . n 
B 1 202  ASP 202  202  202  ASP ASP B . n 
B 1 203  LYS 203  203  203  LYS LYS B . n 
B 1 204  THR 204  204  204  THR THR B . n 
B 1 205  PHE 205  205  205  PHE PHE B . n 
B 1 206  HIS 206  206  206  HIS HIS B . n 
B 1 207  GLN 207  207  207  GLN GLN B . n 
B 1 208  LEU 208  208  208  LEU LEU B . n 
B 1 209  PHE 209  209  209  PHE PHE B . n 
B 1 210  GLU 210  210  210  GLU GLU B . n 
B 1 211  GLN 211  211  211  GLN GLN B . n 
B 1 212  GLN 212  212  212  GLN GLN B . n 
B 1 213  VAL 213  213  213  VAL VAL B . n 
B 1 214  GLU 214  214  214  GLU GLU B . n 
B 1 215  MET 215  215  215  MET MET B . n 
B 1 216  THR 216  216  216  THR THR B . n 
B 1 217  PRO 217  217  217  PRO PRO B . n 
B 1 218  ASP 218  218  218  ASP ASP B . n 
B 1 219  HIS 219  219  219  HIS HIS B . n 
B 1 220  VAL 220  220  220  VAL VAL B . n 
B 1 221  ALA 221  221  221  ALA ALA B . n 
B 1 222  VAL 222  222  222  VAL VAL B . n 
B 1 223  VAL 223  223  223  VAL VAL B . n 
B 1 224  ASP 224  224  224  ASP ASP B . n 
B 1 225  ARG 225  225  225  ARG ARG B . n 
B 1 226  GLY 226  226  226  GLY GLY B . n 
B 1 227  GLN 227  227  227  GLN GLN B . n 
B 1 228  SER 228  228  228  SER SER B . n 
B 1 229  LEU 229  229  229  LEU LEU B . n 
B 1 230  THR 230  230  230  THR THR B . n 
B 1 231  TYR 231  231  231  TYR TYR B . n 
B 1 232  LYS 232  232  232  LYS LYS B . n 
B 1 233  GLN 233  233  233  GLN GLN B . n 
B 1 234  LEU 234  234  234  LEU LEU B . n 
B 1 235  ASN 235  235  235  ASN ASN B . n 
B 1 236  GLU 236  236  236  GLU GLU B . n 
B 1 237  ARG 237  237  237  ARG ARG B . n 
B 1 238  ALA 238  238  238  ALA ALA B . n 
B 1 239  ASN 239  239  239  ASN ASN B . n 
B 1 240  GLN 240  240  240  GLN GLN B . n 
B 1 241  LEU 241  241  241  LEU LEU B . n 
B 1 242  ALA 242  242  242  ALA ALA B . n 
B 1 243  HIS 243  243  243  HIS HIS B . n 
B 1 244  HIS 244  244  244  HIS HIS B . n 
B 1 245  LEU 245  245  245  LEU LEU B . n 
B 1 246  ARG 246  246  246  ARG ARG B . n 
B 1 247  GLY 247  247  247  GLY GLY B . n 
B 1 248  LYS 248  248  248  LYS LYS B . n 
B 1 249  GLY 249  249  249  GLY GLY B . n 
B 1 250  VAL 250  250  250  VAL VAL B . n 
B 1 251  LYS 251  251  251  LYS LYS B . n 
B 1 252  PRO 252  252  252  PRO PRO B . n 
B 1 253  ASP 253  253  253  ASP ASP B . n 
B 1 254  ASP 254  254  254  ASP ASP B . n 
B 1 255  GLN 255  255  255  GLN GLN B . n 
B 1 256  VAL 256  256  256  VAL VAL B . n 
B 1 257  ALA 257  257  257  ALA ALA B . n 
B 1 258  ILE 258  258  258  ILE ILE B . n 
B 1 259  MET 259  259  259  MET MET B . n 
B 1 260  LEU 260  260  260  LEU LEU B . n 
B 1 261  ASP 261  261  261  ASP ASP B . n 
B 1 262  LYS 262  262  262  LYS LYS B . n 
B 1 263  SER 263  263  263  SER SER B . n 
B 1 264  LEU 264  264  264  LEU LEU B . n 
B 1 265  ASP 265  265  265  ASP ASP B . n 
B 1 266  MET 266  266  266  MET MET B . n 
B 1 267  ILE 267  267  267  ILE ILE B . n 
B 1 268  VAL 268  268  268  VAL VAL B . n 
B 1 269  SER 269  269  269  SER SER B . n 
B 1 270  ILE 270  270  270  ILE ILE B . n 
B 1 271  LEU 271  271  271  LEU LEU B . n 
B 1 272  ALA 272  272  272  ALA ALA B . n 
B 1 273  VAL 273  273  273  VAL VAL B . n 
B 1 274  MET 274  274  274  MET MET B . n 
B 1 275  LYS 275  275  275  LYS LYS B . n 
B 1 276  ALA 276  276  276  ALA ALA B . n 
B 1 277  GLY 277  277  277  GLY GLY B . n 
B 1 278  GLY 278  278  278  GLY GLY B . n 
B 1 279  ALA 279  279  279  ALA ALA B . n 
B 1 280  TYR 280  280  280  TYR TYR B . n 
B 1 281  VAL 281  281  281  VAL VAL B . n 
B 1 282  PRO 282  282  282  PRO PRO B . n 
B 1 283  ILE 283  283  283  ILE ILE B . n 
B 1 284  ASP 284  284  284  ASP ASP B . n 
B 1 285  PRO 285  285  285  PRO PRO B . n 
B 1 286  ASP 286  286  286  ASP ASP B . n 
B 1 287  TYR 287  287  287  TYR TYR B . n 
B 1 288  PRO 288  288  288  PRO PRO B . n 
B 1 289  GLY 289  289  289  GLY GLY B . n 
B 1 290  GLU 290  290  290  GLU GLU B . n 
B 1 291  ARG 291  291  291  ARG ARG B . n 
B 1 292  ILE 292  292  292  ILE ILE B . n 
B 1 293  ALA 293  293  293  ALA ALA B . n 
B 1 294  TYR 294  294  294  TYR TYR B . n 
B 1 295  MET 295  295  295  MET MET B . n 
B 1 296  LEU 296  296  296  LEU LEU B . n 
B 1 297  ALA 297  297  297  ALA ALA B . n 
B 1 298  ASP 298  298  298  ASP ASP B . n 
B 1 299  SER 299  299  299  SER SER B . n 
B 1 300  SER 300  300  300  SER SER B . n 
B 1 301  ALA 301  301  301  ALA ALA B . n 
B 1 302  ALA 302  302  302  ALA ALA B . n 
B 1 303  ILE 303  303  303  ILE ILE B . n 
B 1 304  LEU 304  304  304  LEU LEU B . n 
B 1 305  LEU 305  305  305  LEU LEU B . n 
B 1 306  THR 306  306  306  THR THR B . n 
B 1 307  ASN 307  307  307  ASN ASN B . n 
B 1 308  ALA 308  308  308  ALA ALA B . n 
B 1 309  LEU 309  309  309  LEU LEU B . n 
B 1 310  HIS 310  310  310  HIS HIS B . n 
B 1 311  GLU 311  311  311  GLU GLU B . n 
B 1 312  GLU 312  312  312  GLU GLU B . n 
B 1 313  LYS 313  313  313  LYS LYS B . n 
B 1 314  ALA 314  314  314  ALA ALA B . n 
B 1 315  ASN 315  315  315  ASN ASN B . n 
B 1 316  GLY 316  316  316  GLY GLY B . n 
B 1 317  ALA 317  317  317  ALA ALA B . n 
B 1 318  CYS 318  318  318  CYS CYS B . n 
B 1 319  ASP 319  319  319  ASP ASP B . n 
B 1 320  ILE 320  320  320  ILE ILE B . n 
B 1 321  ILE 321  321  321  ILE ILE B . n 
B 1 322  ASP 322  322  322  ASP ASP B . n 
B 1 323  VAL 323  323  323  VAL VAL B . n 
B 1 324  HIS 324  324  324  HIS HIS B . n 
B 1 325  ASP 325  325  325  ASP ASP B . n 
B 1 326  PRO 326  326  326  PRO PRO B . n 
B 1 327  ASP 327  327  327  ASP ASP B . n 
B 1 328  SER 328  328  328  SER SER B . n 
B 1 329  TYR 329  329  329  TYR TYR B . n 
B 1 330  SER 330  330  330  SER SER B . n 
B 1 331  GLU 331  331  331  GLU GLU B . n 
B 1 332  ASN 332  332  332  ASN ASN B . n 
B 1 333  THR 333  333  333  THR THR B . n 
B 1 334  ASN 334  334  334  ASN ASN B . n 
B 1 335  ASN 335  335  335  ASN ASN B . n 
B 1 336  LEU 336  336  336  LEU LEU B . n 
B 1 337  PRO 337  337  337  PRO PRO B . n 
B 1 338  HIS 338  338  338  HIS HIS B . n 
B 1 339  VAL 339  339  339  VAL VAL B . n 
B 1 340  ASN 340  340  340  ASN ASN B . n 
B 1 341  ARG 341  341  341  ARG ARG B . n 
B 1 342  PRO 342  342  342  PRO PRO B . n 
B 1 343  ASP 343  343  343  ASP ASP B . n 
B 1 344  ASP 344  344  344  ASP ASP B . n 
B 1 345  LEU 345  345  345  LEU LEU B . n 
B 1 346  VAL 346  346  346  VAL VAL B . n 
B 1 347  TYR 347  347  347  TYR TYR B . n 
B 1 348  VAL 348  348  348  VAL VAL B . n 
B 1 349  MET 349  349  349  MET MET B . n 
B 1 350  TYR 350  350  350  TYR TYR B . n 
B 1 351  THR 351  351  351  THR THR B . n 
B 1 352  SER 352  352  352  SER SER B . n 
B 1 353  GLY 353  353  353  GLY GLY B . n 
B 1 354  SER 354  354  354  SER SER B . n 
B 1 355  THR 355  355  355  THR THR B . n 
B 1 356  GLY 356  356  356  GLY GLY B . n 
B 1 357  LEU 357  357  357  LEU LEU B . n 
B 1 358  ALA 358  358  358  ALA ALA B . n 
B 1 359  LYS 359  359  359  LYS LYS B . n 
B 1 360  GLY 360  360  360  GLY GLY B . n 
B 1 361  VAL 361  361  361  VAL VAL B . n 
B 1 362  MET 362  362  362  MET MET B . n 
B 1 363  ILE 363  363  363  ILE ILE B . n 
B 1 364  GLU 364  364  364  GLU GLU B . n 
B 1 365  HIS 365  365  365  HIS HIS B . n 
B 1 366  HIS 366  366  366  HIS HIS B . n 
B 1 367  ASN 367  367  367  ASN ASN B . n 
B 1 368  LEU 368  368  368  LEU LEU B . n 
B 1 369  VAL 369  369  369  VAL VAL B . n 
B 1 370  ASN 370  370  370  ASN ASN B . n 
B 1 371  PHE 371  371  371  PHE PHE B . n 
B 1 372  CYS 372  372  372  CYS CYS B . n 
B 1 373  GLU 373  373  373  GLU GLU B . n 
B 1 374  TRP 374  374  374  TRP TRP B . n 
B 1 375  TYR 375  375  375  TYR TYR B . n 
B 1 376  ARG 376  376  376  ARG ARG B . n 
B 1 377  PRO 377  377  377  PRO PRO B . n 
B 1 378  TYR 378  378  378  TYR TYR B . n 
B 1 379  PHE 379  379  379  PHE PHE B . n 
B 1 380  GLY 380  380  380  GLY GLY B . n 
B 1 381  VAL 381  381  381  VAL VAL B . n 
B 1 382  THR 382  382  382  THR THR B . n 
B 1 383  PRO 383  383  383  PRO PRO B . n 
B 1 384  ALA 384  384  384  ALA ALA B . n 
B 1 385  ASP 385  385  385  ASP ASP B . n 
B 1 386  LYS 386  386  386  LYS LYS B . n 
B 1 387  ALA 387  387  387  ALA ALA B . n 
B 1 388  LEU 388  388  388  LEU LEU B . n 
B 1 389  VAL 389  389  389  VAL VAL B . n 
B 1 390  TYR 390  390  390  TYR TYR B . n 
B 1 391  SER 391  391  391  SER SER B . n 
B 1 392  SER 392  392  392  SER SER B . n 
B 1 393  PHE 393  393  393  PHE PHE B . n 
B 1 394  SER 394  394  394  SER SER B . n 
B 1 395  PHE 395  395  395  PHE PHE B . n 
B 1 396  ASP 396  396  396  ASP ASP B . n 
B 1 397  GLY 397  397  397  GLY GLY B . n 
B 1 398  SER 398  398  398  SER SER B . n 
B 1 399  ALA 399  399  399  ALA ALA B . n 
B 1 400  LEU 400  400  400  LEU LEU B . n 
B 1 401  ASP 401  401  401  ASP ASP B . n 
B 1 402  ILE 402  402  402  ILE ILE B . n 
B 1 403  PHE 403  403  403  PHE PHE B . n 
B 1 404  THR 404  404  404  THR THR B . n 
B 1 405  HIS 405  405  405  HIS HIS B . n 
B 1 406  LEU 406  406  406  LEU LEU B . n 
B 1 407  LEU 407  407  407  LEU LEU B . n 
B 1 408  ALA 408  408  408  ALA ALA B . n 
B 1 409  GLY 409  409  409  GLY GLY B . n 
B 1 410  ALA 410  410  410  ALA ALA B . n 
B 1 411  ALA 411  411  411  ALA ALA B . n 
B 1 412  LEU 412  412  412  LEU LEU B . n 
B 1 413  HIS 413  413  413  HIS HIS B . n 
B 1 414  ILE 414  414  414  ILE ILE B . n 
B 1 415  VAL 415  415  415  VAL VAL B . n 
B 1 416  PRO 416  416  416  PRO PRO B . n 
B 1 417  SER 417  417  417  SER SER B . n 
B 1 418  GLU 418  418  418  GLU GLU B . n 
B 1 419  ARG 419  419  419  ARG ARG B . n 
B 1 420  LYS 420  420  420  LYS LYS B . n 
B 1 421  TYR 421  421  421  TYR TYR B . n 
B 1 422  ASP 422  422  422  ASP ASP B . n 
B 1 423  LEU 423  423  423  LEU LEU B . n 
B 1 424  ASP 424  424  424  ASP ASP B . n 
B 1 425  ALA 425  425  425  ALA ALA B . n 
B 1 426  LEU 426  426  426  LEU LEU B . n 
B 1 427  ASN 427  427  427  ASN ASN B . n 
B 1 428  ASP 428  428  428  ASP ASP B . n 
B 1 429  TYR 429  429  429  TYR TYR B . n 
B 1 430  CYS 430  430  430  CYS CYS B . n 
B 1 431  ASN 431  431  431  ASN ASN B . n 
B 1 432  GLN 432  432  432  GLN GLN B . n 
B 1 433  GLU 433  433  433  GLU GLU B . n 
B 1 434  GLY 434  434  434  GLY GLY B . n 
B 1 435  ILE 435  435  435  ILE ILE B . n 
B 1 436  THR 436  436  436  THR THR B . n 
B 1 437  ILE 437  437  437  ILE ILE B . n 
B 1 438  SER 438  438  438  SER SER B . n 
B 1 439  TYR 439  439  439  TYR TYR B . n 
B 1 440  LEU 440  440  440  LEU LEU B . n 
B 1 441  PRO 441  441  441  PRO PRO B . n 
B 1 442  THR 442  442  442  THR THR B . n 
B 1 443  GLY 443  443  443  GLY GLY B . n 
B 1 444  ALA 444  444  444  ALA ALA B . n 
B 1 445  ALA 445  445  445  ALA ALA B . n 
B 1 446  GLU 446  446  446  GLU GLU B . n 
B 1 447  GLN 447  447  447  GLN GLN B . n 
B 1 448  PHE 448  448  448  PHE PHE B . n 
B 1 449  MET 449  449  449  MET MET B . n 
B 1 450  GLN 450  450  450  GLN GLN B . n 
B 1 451  MET 451  451  451  MET MET B . n 
B 1 452  ASP 452  452  452  ASP ASP B . n 
B 1 453  ASN 453  453  453  ASN ASN B . n 
B 1 454  GLN 454  454  454  GLN GLN B . n 
B 1 455  SER 455  455  455  SER SER B . n 
B 1 456  PHE 456  456  456  PHE PHE B . n 
B 1 457  ARG 457  457  457  ARG ARG B . n 
B 1 458  VAL 458  458  458  VAL VAL B . n 
B 1 459  VAL 459  459  459  VAL VAL B . n 
B 1 460  ILE 460  460  460  ILE ILE B . n 
B 1 461  THR 461  461  461  THR THR B . n 
B 1 462  GLY 462  462  462  GLY GLY B . n 
B 1 463  GLY 463  463  463  GLY GLY B . n 
B 1 464  ASP 464  464  464  ASP ASP B . n 
B 1 465  VAL 465  465  465  VAL VAL B . n 
B 1 466  LEU 466  466  466  LEU LEU B . n 
B 1 467  LYS 467  467  467  LYS LYS B . n 
B 1 468  LYS 468  468  468  LYS LYS B . n 
B 1 469  ILE 469  469  469  ILE ILE B . n 
B 1 470  GLU 470  470  470  GLU GLU B . n 
B 1 471  ARG 471  471  471  ARG ARG B . n 
B 1 472  ASN 472  472  472  ASN ASN B . n 
B 1 473  GLY 473  473  473  GLY GLY B . n 
B 1 474  THR 474  474  474  THR THR B . n 
B 1 475  TYR 475  475  475  TYR TYR B . n 
B 1 476  LYS 476  476  476  LYS LYS B . n 
B 1 477  LEU 477  477  477  LEU LEU B . n 
B 1 478  TYR 478  478  478  TYR TYR B . n 
B 1 479  ASN 479  479  479  ASN ASN B . n 
B 1 480  GLY 480  480  480  GLY GLY B . n 
B 1 481  TYR 481  481  481  TYR TYR B . n 
B 1 482  GLY 482  482  482  GLY GLY B . n 
B 1 483  PRO 483  483  483  PRO PRO B . n 
B 1 484  THR 484  484  484  THR THR B . n 
B 1 485  GLU 485  485  485  GLU GLU B . n 
B 1 486  CYS 486  486  486  CYS CYS B . n 
B 1 487  THR 487  487  487  THR THR B . n 
B 1 488  ILE 488  488  488  ILE ILE B . n 
B 1 489  MET 489  489  489  MET MET B . n 
B 1 490  VAL 490  490  490  VAL VAL B . n 
B 1 491  THR 491  491  491  THR THR B . n 
B 1 492  MET 492  492  492  MET MET B . n 
B 1 493  PHE 493  493  493  PHE PHE B . n 
B 1 494  GLU 494  494  494  GLU GLU B . n 
B 1 495  VAL 495  495  495  VAL VAL B . n 
B 1 496  ASP 496  496  496  ASP ASP B . n 
B 1 497  LYS 497  497  497  LYS LYS B . n 
B 1 498  PRO 498  498  498  PRO PRO B . n 
B 1 499  TYR 499  499  499  TYR TYR B . n 
B 1 500  ALA 500  500  500  ALA ALA B . n 
B 1 501  ASN 501  501  501  ASN ASN B . n 
B 1 502  ILE 502  502  502  ILE ILE B . n 
B 1 503  PRO 503  503  503  PRO PRO B . n 
B 1 504  ILE 504  504  504  ILE ILE B . n 
B 1 505  GLY 505  505  505  GLY GLY B . n 
B 1 506  LYS 506  506  506  LYS LYS B . n 
B 1 507  PRO 507  507  507  PRO PRO B . n 
B 1 508  ILE 508  508  508  ILE ILE B . n 
B 1 509  ASP 509  509  509  ASP ASP B . n 
B 1 510  ARG 510  510  510  ARG ARG B . n 
B 1 511  THR 511  511  511  THR THR B . n 
B 1 512  ARG 512  512  512  ARG ARG B . n 
B 1 513  ILE 513  513  513  ILE ILE B . n 
B 1 514  LEU 514  514  514  LEU LEU B . n 
B 1 515  ILE 515  515  515  ILE ILE B . n 
B 1 516  LEU 516  516  516  LEU LEU B . n 
B 1 517  ASP 517  517  517  ASP ASP B . n 
B 1 518  GLU 518  518  518  GLU GLU B . n 
B 1 519  ALA 519  519  519  ALA ALA B . n 
B 1 520  LEU 520  520  520  LEU LEU B . n 
B 1 521  ALA 521  521  521  ALA ALA B . n 
B 1 522  LEU 522  522  522  LEU LEU B . n 
B 1 523  GLN 523  523  523  GLN GLN B . n 
B 1 524  PRO 524  524  524  PRO PRO B . n 
B 1 525  ILE 525  525  525  ILE ILE B . n 
B 1 526  GLY 526  526  526  GLY GLY B . n 
B 1 527  VAL 527  527  527  VAL VAL B . n 
B 1 528  ALA 528  528  528  ALA ALA B . n 
B 1 529  GLY 529  529  529  GLY GLY B . n 
B 1 530  GLU 530  530  530  GLU GLU B . n 
B 1 531  LEU 531  531  531  LEU LEU B . n 
B 1 532  PHE 532  532  532  PHE PHE B . n 
B 1 533  ILE 533  533  533  ILE ILE B . n 
B 1 534  VAL 534  534  534  VAL VAL B . n 
B 1 535  GLY 535  535  535  GLY GLY B . n 
B 1 536  GLU 536  536  536  GLU GLU B . n 
B 1 537  GLY 537  537  537  GLY GLY B . n 
B 1 538  LEU 538  538  538  LEU LEU B . n 
B 1 539  GLY 539  539  539  GLY GLY B . n 
B 1 540  ARG 540  540  540  ARG ARG B . n 
B 1 541  GLY 541  541  541  GLY GLY B . n 
B 1 542  TYR 542  542  542  TYR TYR B . n 
B 1 543  LEU 543  543  543  LEU LEU B . n 
B 1 544  ASN 544  544  544  ASN ASN B . n 
B 1 545  ARG 545  545  545  ARG ARG B . n 
B 1 546  PRO 546  546  546  PRO PRO B . n 
B 1 547  GLU 547  547  547  GLU GLU B . n 
B 1 548  LEU 548  548  548  LEU LEU B . n 
B 1 549  THR 549  549  549  THR THR B . n 
B 1 550  ALA 550  550  550  ALA ALA B . n 
B 1 551  GLU 551  551  551  GLU GLU B . n 
B 1 552  LYS 552  552  552  LYS LYS B . n 
B 1 553  PHE 553  553  553  PHE PHE B . n 
B 1 554  ILE 554  554  554  ILE ILE B . n 
B 1 555  VAL 555  555  555  VAL VAL B . n 
B 1 556  HIS 556  556  556  HIS HIS B . n 
B 1 557  PRO 557  557  557  PRO PRO B . n 
B 1 558  GLN 558  558  558  GLN GLN B . n 
B 1 559  THR 559  559  559  THR THR B . n 
B 1 560  GLY 560  560  560  GLY GLY B . n 
B 1 561  GLU 561  561  561  GLU GLU B . n 
B 1 562  ARG 562  562  562  ARG ARG B . n 
B 1 563  MET 563  563  563  MET MET B . n 
B 1 564  TYR 564  564  564  TYR TYR B . n 
B 1 565  ARG 565  565  565  ARG ARG B . n 
B 1 566  THR 566  566  566  THR THR B . n 
B 1 567  GLY 567  567  567  GLY GLY B . n 
B 1 568  ASP 568  568  568  ASP ASP B . n 
B 1 569  ARG 569  569  569  ARG ARG B . n 
B 1 570  ALA 570  570  570  ALA ALA B . n 
B 1 571  ARG 571  571  571  ARG ARG B . n 
B 1 572  PHE 572  572  572  PHE PHE B . n 
B 1 573  LEU 573  573  573  LEU LEU B . n 
B 1 574  PRO 574  574  574  PRO PRO B . n 
B 1 575  ASP 575  575  575  ASP ASP B . n 
B 1 576  GLY 576  576  576  GLY GLY B . n 
B 1 577  ASN 577  577  577  ASN ASN B . n 
B 1 578  ILE 578  578  578  ILE ILE B . n 
B 1 579  GLU 579  579  579  GLU GLU B . n 
B 1 580  PHE 580  580  580  PHE PHE B . n 
B 1 581  LEU 581  581  581  LEU LEU B . n 
B 1 582  GLY 582  582  582  GLY GLY B . n 
B 1 583  ARG 583  583  583  ARG ARG B . n 
B 1 584  LEU 584  584  584  LEU LEU B . n 
B 1 585  ASP 585  585  585  ASP ASP B . n 
B 1 586  ASN 586  586  586  ASN ASN B . n 
B 1 587  LEU 587  587  587  LEU LEU B . n 
B 1 588  VAL 588  588  588  VAL VAL B . n 
B 1 589  LYS 589  589  589  LYS LYS B . n 
B 1 590  ILE 590  590  590  ILE ILE B . n 
B 1 591  ARG 591  591  591  ARG ARG B . n 
B 1 592  GLY 592  592  592  GLY GLY B . n 
B 1 593  TYR 593  593  593  TYR TYR B . n 
B 1 594  ARG 594  594  594  ARG ARG B . n 
B 1 595  ILE 595  595  595  ILE ILE B . n 
B 1 596  GLU 596  596  596  GLU GLU B . n 
B 1 597  PRO 597  597  597  PRO PRO B . n 
B 1 598  GLY 598  598  598  GLY GLY B . n 
B 1 599  GLU 599  599  599  GLU GLU B . n 
B 1 600  ILE 600  600  600  ILE ILE B . n 
B 1 601  GLU 601  601  601  GLU GLU B . n 
B 1 602  PRO 602  602  602  PRO PRO B . n 
B 1 603  PHE 603  603  603  PHE PHE B . n 
B 1 604  LEU 604  604  604  LEU LEU B . n 
B 1 605  MET 605  605  605  MET MET B . n 
B 1 606  ASN 606  606  606  ASN ASN B . n 
B 1 607  HIS 607  607  607  HIS HIS B . n 
B 1 608  PRO 608  608  608  PRO PRO B . n 
B 1 609  LEU 609  609  609  LEU LEU B . n 
B 1 610  ILE 610  610  610  ILE ILE B . n 
B 1 611  GLU 611  611  611  GLU GLU B . n 
B 1 612  LEU 612  612  612  LEU LEU B . n 
B 1 613  THR 613  613  613  THR THR B . n 
B 1 614  THR 614  614  614  THR THR B . n 
B 1 615  VAL 615  615  615  VAL VAL B . n 
B 1 616  LEU 616  616  616  LEU LEU B . n 
B 1 617  ALA 617  617  617  ALA ALA B . n 
B 1 618  LYS 618  618  618  LYS LYS B . n 
B 1 619  GLU 619  619  619  GLU GLU B . n 
B 1 620  GLN 620  620  620  GLN GLN B . n 
B 1 621  ALA 621  621  621  ALA ALA B . n 
B 1 622  ASP 622  622  622  ASP ASP B . n 
B 1 623  GLY 623  623  623  GLY GLY B . n 
B 1 624  ARG 624  624  624  ARG ARG B . n 
B 1 625  LYS 625  625  625  LYS LYS B . n 
B 1 626  TYR 626  626  626  TYR TYR B . n 
B 1 627  LEU 627  627  627  LEU LEU B . n 
B 1 628  VAL 628  628  628  VAL VAL B . n 
B 1 629  GLY 629  629  629  GLY GLY B . n 
B 1 630  TYR 630  630  630  TYR TYR B . n 
B 1 631  TYR 631  631  631  TYR TYR B . n 
B 1 632  VAL 632  632  632  VAL VAL B . n 
B 1 633  ALA 633  633  633  ALA ALA B . n 
B 1 634  PRO 634  634  634  PRO PRO B . n 
B 1 635  GLU 635  635  635  GLU GLU B . n 
B 1 636  GLU 636  636  636  GLU GLU B . n 
B 1 637  ILE 637  637  637  ILE ILE B . n 
B 1 638  PRO 638  638  638  PRO PRO B . n 
B 1 639  HIS 639  639  639  HIS HIS B . n 
B 1 640  GLY 640  640  640  GLY GLY B . n 
B 1 641  GLU 641  641  641  GLU GLU B . n 
B 1 642  LEU 642  642  642  LEU LEU B . n 
B 1 643  ARG 643  643  643  ARG ARG B . n 
B 1 644  GLU 644  644  644  GLU GLU B . n 
B 1 645  TRP 645  645  645  TRP TRP B . n 
B 1 646  LEU 646  646  646  LEU LEU B . n 
B 1 647  GLY 647  647  647  GLY GLY B . n 
B 1 648  ASN 648  648  648  ASN ASN B . n 
B 1 649  ASP 649  649  649  ASP ASP B . n 
B 1 650  LEU 650  650  650  LEU LEU B . n 
B 1 651  PRO 651  651  651  PRO PRO B . n 
B 1 652  ASP 652  652  652  ASP ASP B . n 
B 1 653  TYR 653  653  653  TYR TYR B . n 
B 1 654  MET 654  654  654  MET MET B . n 
B 1 655  ILE 655  655  655  ILE ILE B . n 
B 1 656  PRO 656  656  656  PRO PRO B . n 
B 1 657  THR 657  657  657  THR THR B . n 
B 1 658  TYR 658  658  658  TYR TYR B . n 
B 1 659  PHE 659  659  659  PHE PHE B . n 
B 1 660  VAL 660  660  660  VAL VAL B . n 
B 1 661  HIS 661  661  661  HIS HIS B . n 
B 1 662  MET 662  662  662  MET MET B . n 
B 1 663  LYS 663  663  663  LYS LYS B . n 
B 1 664  ALA 664  664  664  ALA ALA B . n 
B 1 665  PHE 665  665  665  PHE PHE B . n 
B 1 666  PRO 666  666  666  PRO PRO B . n 
B 1 667  LEU 667  667  667  LEU LEU B . n 
B 1 668  THR 668  668  668  THR THR B . n 
B 1 669  ALA 669  669  669  ALA ALA B . n 
B 1 670  ASN 670  670  670  ASN ASN B . n 
B 1 671  GLY 671  671  671  GLY GLY B . n 
B 1 672  LYS 672  672  672  LYS LYS B . n 
B 1 673  VAL 673  673  673  VAL VAL B . n 
B 1 674  ASP 674  674  674  ASP ASP B . n 
B 1 675  ARG 675  675  675  ARG ARG B . n 
B 1 676  ARG 676  676  676  ARG ARG B . n 
B 1 677  ALA 677  677  677  ALA ALA B . n 
B 1 678  LEU 678  678  678  LEU LEU B . n 
B 1 679  PRO 679  679  679  PRO PRO B . n 
B 1 680  ASP 680  680  680  ASP ASP B . n 
B 1 681  VAL 681  681  681  VAL VAL B . n 
B 1 682  GLN 682  682  682  GLN GLN B . n 
B 1 683  ALA 683  683  683  ALA ALA B . n 
B 1 684  ASP 684  684  684  ASP ASP B . n 
B 1 685  ALA 685  685  685  ALA ALA B . n 
B 1 686  GLU 686  686  686  GLU GLU B . n 
B 1 687  LEU 687  687  687  LEU LEU B . n 
B 1 688  LEU 688  688  688  LEU LEU B . n 
B 1 689  GLY 689  689  689  GLY GLY B . n 
B 1 690  GLU 690  690  690  GLU GLU B . n 
B 1 691  ASP 691  691  691  ASP ALA B . n 
B 1 692  TYR 692  692  692  TYR TYR B . n 
B 1 693  VAL 693  693  693  VAL VAL B . n 
B 1 694  ALA 694  694  694  ALA ALA B . n 
B 1 695  PRO 695  695  695  PRO PRO B . n 
B 1 696  THR 696  696  696  THR THR B . n 
B 1 697  ASP 697  697  697  ASP ASP B . n 
B 1 698  GLU 698  698  698  GLU GLU B . n 
B 1 699  LEU 699  699  699  LEU LEU B . n 
B 1 700  GLU 700  700  700  GLU GLU B . n 
B 1 701  GLN 701  701  701  GLN GLN B . n 
B 1 702  GLN 702  702  702  GLN GLN B . n 
B 1 703  LEU 703  703  703  LEU LEU B . n 
B 1 704  ALA 704  704  704  ALA ALA B . n 
B 1 705  GLN 705  705  705  GLN GLN B . n 
B 1 706  VAL 706  706  706  VAL VAL B . n 
B 1 707  TRP 707  707  707  TRP TRP B . n 
B 1 708  SER 708  708  708  SER SER B . n 
B 1 709  HIS 709  709  709  HIS HIS B . n 
B 1 710  VAL 710  710  710  VAL VAL B . n 
B 1 711  LEU 711  711  711  LEU LEU B . n 
B 1 712  GLY 712  712  712  GLY GLY B . n 
B 1 713  ILE 713  713  713  ILE ILE B . n 
B 1 714  PRO 714  714  714  PRO PRO B . n 
B 1 715  GLN 715  715  715  GLN GLN B . n 
B 1 716  MET 716  716  716  MET MET B . n 
B 1 717  GLY 717  717  717  GLY GLY B . n 
B 1 718  ILE 718  718  718  ILE ILE B . n 
B 1 719  ASP 719  719  719  ASP ASP B . n 
B 1 720  ASP 720  720  720  ASP ASP B . n 
B 1 721  HIS 721  721  721  HIS HIS B . n 
B 1 722  PHE 722  722  722  PHE PHE B . n 
B 1 723  LEU 723  723  723  LEU LEU B . n 
B 1 724  GLU 724  724  724  GLU GLU B . n 
B 1 725  ARG 725  725  725  ARG ARG B . n 
B 1 726  GLY 726  726  726  GLY GLY B . n 
B 1 727  GLY 727  727  727  GLY GLY B . n 
B 1 728  ASP 728  728  728  ASP ASP B . n 
B 1 729  4HH 729  729  729  4HH 4HH B . n 
B 1 730  ILE 730  730  730  ILE ILE B . n 
B 1 731  LYS 731  731  731  LYS LYS B . n 
B 1 732  VAL 732  732  732  VAL VAL B . n 
B 1 733  MET 733  733  733  MET MET B . n 
B 1 734  GLN 734  734  734  GLN GLN B . n 
B 1 735  LEU 735  735  735  LEU LEU B . n 
B 1 736  ILE 736  736  736  ILE ILE B . n 
B 1 737  HIS 737  737  737  HIS HIS B . n 
B 1 738  GLN 738  738  738  GLN GLN B . n 
B 1 739  LEU 739  739  739  LEU LEU B . n 
B 1 740  LYS 740  740  740  LYS LYS B . n 
B 1 741  ASN 741  741  741  ASN ASN B . n 
B 1 742  ILE 742  742  742  ILE ILE B . n 
B 1 743  GLY 743  743  743  GLY GLY B . n 
B 1 744  LEU 744  744  744  LEU LEU B . n 
B 1 745  SER 745  745  745  SER SER B . n 
B 1 746  LEU 746  746  746  LEU LEU B . n 
B 1 747  ARG 747  747  747  ARG ARG B . n 
B 1 748  TYR 748  748  748  TYR TYR B . n 
B 1 749  ASP 749  749  749  ASP ASP B . n 
B 1 750  GLN 750  750  750  GLN GLN B . n 
B 1 751  LEU 751  751  751  LEU LEU B . n 
B 1 752  PHE 752  752  752  PHE PHE B . n 
B 1 753  THR 753  753  753  THR THR B . n 
B 1 754  HIS 754  754  754  HIS HIS B . n 
B 1 755  PRO 755  755  755  PRO PRO B . n 
B 1 756  THR 756  756  756  THR THR B . n 
B 1 757  ILE 757  757  757  ILE ILE B . n 
B 1 758  ARG 758  758  758  ARG ARG B . n 
B 1 759  GLN 759  759  759  GLN GLN B . n 
B 1 760  LEU 760  760  760  LEU LEU B . n 
B 1 761  LYS 761  761  761  LYS LYS B . n 
B 1 762  ARG 762  762  762  ARG ARG B . n 
B 1 763  LEU 763  763  763  LEU LEU B . n 
B 1 764  LEU 764  764  764  LEU LEU B . n 
B 1 765  THR 765  765  765  THR THR B . n 
B 1 766  GLU 766  766  766  GLU GLU B . n 
B 1 767  GLN 767  767  767  GLN GLN B . n 
B 1 768  LYS 768  768  768  LYS LYS B . n 
B 1 769  GLN 769  769  769  GLN GLN B . n 
B 1 770  VAL 770  770  770  VAL VAL B . n 
B 1 771  ASN 771  770  770  ASN ASN B A n 
B 1 772  GLY 772  770  770  GLY GLY B B n 
B 1 773  LEU 773  771  771  LEU LEU B . n 
B 1 774  LEU 774  772  772  LEU LEU B . n 
B 1 775  GLU 775  773  773  GLU GLU B . n 
B 1 776  PRO 776  774  774  PRO PRO B . n 
B 1 777  LEU 777  775  775  LEU LEU B . n 
B 1 778  ARG 778  776  776  ARG ARG B . n 
B 1 779  GLU 779  777  777  GLU GLU B . n 
B 1 780  LEU 780  778  778  LEU LEU B . n 
B 1 781  ASP 781  779  779  ASP ASP B . n 
B 1 782  GLU 782  780  780  GLU GLU B . n 
B 1 783  GLN 783  781  781  GLN GLN B . n 
B 1 784  ALA 784  782  782  ALA ALA B . n 
B 1 785  GLU 785  783  783  GLU GLU B . n 
B 1 786  TYR 786  784  784  TYR TYR B . n 
B 1 787  GLU 787  785  785  GLU GLU B . n 
B 1 788  THR 788  786  786  THR THR B . n 
B 1 789  SER 789  787  787  SER SER B . n 
B 1 790  ALA 790  788  788  ALA ALA B . n 
B 1 791  VAL 791  789  789  VAL VAL B . n 
B 1 792  GLU 792  790  790  GLU GLU B . n 
B 1 793  LYS 793  791  791  LYS LYS B . n 
B 1 794  ARG 794  792  792  ARG ARG B . n 
B 1 795  MET 795  793  793  MET MET B . n 
B 1 796  TYR 796  794  794  TYR TYR B . n 
B 1 797  ILE 797  795  795  ILE ILE B . n 
B 1 798  ILE 798  796  796  ILE ILE B . n 
B 1 799  GLN 799  797  797  GLN GLN B . n 
B 1 800  GLN 800  798  798  GLN GLN B . n 
B 1 801  GLN 801  799  799  GLN GLN B . n 
B 1 802  ASP 802  800  800  ASP ASP B . n 
B 1 803  VAL 803  801  801  VAL VAL B . n 
B 1 804  GLU 804  802  802  GLU GLU B . n 
B 1 805  SER 805  803  803  SER SER B . n 
B 1 806  ILE 806  804  804  ILE ILE B . n 
B 1 807  ALA 807  805  805  ALA ALA B . n 
B 1 808  TYR 808  806  806  TYR TYR B . n 
B 1 809  ASN 809  807  807  ASN ASN B . n 
B 1 810  VAL 810  808  808  VAL VAL B . n 
B 1 811  VAL 811  809  809  VAL VAL B . n 
B 1 812  TYR 812  810  810  TYR TYR B . n 
B 1 813  THR 813  811  811  THR THR B . n 
B 1 814  ILE 814  812  812  ILE ILE B . n 
B 1 815  ASN 815  813  813  ASN ASN B . n 
B 1 816  PHE 816  814  814  PHE PHE B . n 
B 1 817  PRO 817  815  815  PRO PRO B . n 
B 1 818  LEU 818  816  816  LEU LEU B . n 
B 1 819  THR 819  817  817  THR THR B . n 
B 1 820  VAL 820  818  818  VAL VAL B . n 
B 1 821  ASP 821  819  819  ASP ASP B . n 
B 1 822  THR 822  820  820  THR THR B . n 
B 1 823  GLU 823  821  821  GLU GLU B . n 
B 1 824  GLN 824  822  822  GLN GLN B . n 
B 1 825  ILE 825  823  823  ILE ILE B . n 
B 1 826  ARG 826  824  824  ARG ARG B . n 
B 1 827  VAL 827  825  825  VAL VAL B . n 
B 1 828  ALA 828  826  826  ALA ALA B . n 
B 1 829  LEU 829  827  827  LEU LEU B . n 
B 1 830  GLU 830  828  828  GLU GLU B . n 
B 1 831  GLN 831  829  829  GLN GLN B . n 
B 1 832  LEU 832  830  830  LEU LEU B . n 
B 1 833  VAL 833  831  831  VAL VAL B . n 
B 1 834  LEU 834  832  832  LEU LEU B . n 
B 1 835  ARG 835  833  833  ARG ARG B . n 
B 1 836  HIS 836  834  834  HIS HIS B . n 
B 1 837  GLU 837  835  835  GLU GLU B . n 
B 1 838  GLY 838  836  836  GLY GLY B . n 
B 1 839  LEU 839  837  837  LEU LEU B . n 
B 1 840  ARG 840  838  838  ARG ARG B . n 
B 1 841  SER 841  839  839  SER SER B . n 
B 1 842  THR 842  840  840  THR THR B . n 
B 1 843  TYR 843  841  841  TYR TYR B . n 
B 1 844  HIS 844  842  842  HIS HIS B . n 
B 1 845  MET 845  843  843  MET MET B . n 
B 1 846  ARG 846  844  844  ARG ARG B . n 
B 1 847  GLY 847  845  845  GLY GLY B . n 
B 1 848  ASP 848  846  846  ASP ASP B . n 
B 1 849  GLU 849  847  847  GLU GLU B . n 
B 1 850  ILE 850  848  848  ILE ILE B . n 
B 1 851  VAL 851  849  849  VAL VAL B . n 
B 1 852  LYS 852  850  850  LYS LYS B . n 
B 1 853  ARG 853  851  851  ARG ARG B . n 
B 1 854  ILE 854  852  852  ILE ILE B . n 
B 1 855  VAL 855  853  853  VAL VAL B . n 
B 1 856  PRO 856  854  854  PRO PRO B . n 
B 1 857  ARG 857  855  855  ARG ARG B . n 
B 1 858  ALA 858  856  856  ALA ALA B . n 
B 1 859  GLU 859  857  857  GLU GLU B . n 
B 1 860  LEU 860  858  858  LEU LEU B . n 
B 1 861  SER 861  859  859  SER SER B . n 
B 1 862  PHE 862  860  860  PHE PHE B . n 
B 1 863  VAL 863  861  861  VAL VAL B . n 
B 1 864  ARG 864  862  862  ARG ARG B . n 
B 1 865  GLN 865  863  863  GLN GLN B . n 
B 1 866  THR 866  864  864  THR THR B . n 
B 1 867  GLY 867  865  865  GLY GLY B . n 
B 1 868  GLU 868  866  866  GLU GLU B . n 
B 1 869  GLU 869  867  867  GLU GLU B . n 
B 1 870  GLU 870  868  868  GLU GLU B . n 
B 1 871  SER 871  869  869  SER SER B . n 
B 1 872  VAL 872  870  870  VAL VAL B . n 
B 1 873  GLN 873  871  871  GLN GLN B . n 
B 1 874  SER 874  872  872  SER SER B . n 
B 1 875  LEU 875  873  873  LEU LEU B . n 
B 1 876  LEU 876  874  874  LEU LEU B . n 
B 1 877  ALA 877  875  875  ALA ALA B . n 
B 1 878  GLU 878  876  876  GLU GLU B . n 
B 1 879  GLN 879  877  877  GLN GLN B . n 
B 1 880  ILE 880  878  878  ILE ILE B . n 
B 1 881  LYS 881  879  879  LYS LYS B . n 
B 1 882  PRO 882  880  880  PRO PRO B . n 
B 1 883  PHE 883  881  881  PHE PHE B . n 
B 1 884  ASP 884  882  882  ASP ASP B . n 
B 1 885  LEU 885  883  883  LEU LEU B . n 
B 1 886  ALA 886  884  884  ALA ALA B . n 
B 1 887  LYS 887  885  885  LYS LYS B . n 
B 1 888  ALA 888  886  886  ALA ALA B . n 
B 1 889  PRO 889  887  887  PRO PRO B . n 
B 1 890  LEU 890  888  888  LEU LEU B . n 
B 1 891  LEU 891  889  889  LEU LEU B . n 
B 1 892  ARG 892  890  890  ARG ARG B . n 
B 1 893  ALA 893  891  891  ALA ALA B . n 
B 1 894  GLY 894  892  892  GLY GLY B . n 
B 1 895  VAL 895  893  893  VAL VAL B . n 
B 1 896  ILE 896  894  894  ILE ILE B . n 
B 1 897  GLU 897  895  895  GLU GLU B . n 
B 1 898  THR 898  896  896  THR THR B . n 
B 1 899  ALA 899  897  897  ALA ALA B . n 
B 1 900  ASP 900  898  898  ASP ASP B . n 
B 1 901  LYS 901  899  899  LYS LYS B . n 
B 1 902  LYS 902  900  900  LYS LYS B . n 
B 1 903  VAL 903  901  901  VAL VAL B . n 
B 1 904  LEU 904  902  902  LEU LEU B . n 
B 1 905  TRP 905  903  903  TRP TRP B . n 
B 1 906  PHE 906  904  904  PHE PHE B . n 
B 1 907  ASP 907  905  905  ASP ASP B . n 
B 1 908  SER 908  906  906  SER SER B . n 
B 1 909  HIS 909  907  907  HIS HIS B . n 
B 1 910  HIS 910  908  908  HIS HIS B . n 
B 1 911  ILE 911  909  909  ILE ILE B . n 
B 1 912  LEU 912  910  910  LEU LEU B . n 
B 1 913  LEU 913  911  911  LEU LEU B . n 
B 1 914  ASP 914  912  912  ASP ASP B . n 
B 1 915  GLY 915  913  913  GLY GLY B . n 
B 1 916  LEU 916  914  914  LEU LEU B . n 
B 1 917  SER 917  915  915  SER SER B . n 
B 1 918  LYS 918  916  916  LYS LYS B . n 
B 1 919  SER 919  917  917  SER SER B . n 
B 1 920  ILE 920  918  918  ILE ILE B . n 
B 1 921  LEU 921  919  919  LEU LEU B . n 
B 1 922  ALA 922  920  920  ALA ALA B . n 
B 1 923  ARG 923  921  921  ARG ARG B . n 
B 1 924  GLU 924  922  922  GLU GLU B . n 
B 1 925  LEU 925  923  923  LEU LEU B . n 
B 1 926  GLN 926  924  924  GLN GLN B . n 
B 1 927  ALA 927  925  925  ALA ALA B . n 
B 1 928  LEU 928  926  926  LEU LEU B . n 
B 1 929  LEU 929  927  927  LEU LEU B . n 
B 1 930  GLY 930  928  928  GLY GLY B . n 
B 1 931  GLN 931  929  929  GLN GLN B . n 
B 1 932  GLN 932  930  930  GLN GLN B . n 
B 1 933  VAL 933  931  931  VAL VAL B . n 
B 1 934  LEU 934  932  932  LEU LEU B . n 
B 1 935  SER 935  933  933  SER SER B . n 
B 1 936  PRO 936  934  934  PRO PRO B . n 
B 1 937  VAL 937  935  935  VAL VAL B . n 
B 1 938  GLU 938  936  936  GLU GLU B . n 
B 1 939  LYS 939  937  937  LYS LYS B . n 
B 1 940  THR 940  938  938  THR THR B . n 
B 1 941  TYR 941  939  939  TYR TYR B . n 
B 1 942  LYS 942  940  940  LYS LYS B . n 
B 1 943  SER 943  941  941  SER SER B . n 
B 1 944  PHE 944  942  942  PHE PHE B . n 
B 1 945  ALA 945  943  943  ALA ALA B . n 
B 1 946  ARG 946  944  944  ARG ARG B . n 
B 1 947  TRP 947  945  945  TRP TRP B . n 
B 1 948  GLN 948  946  946  GLN GLN B . n 
B 1 949  ASN 949  947  947  ASN ASN B . n 
B 1 950  GLU 950  948  948  GLU GLU B . n 
B 1 951  TRP 951  949  949  TRP TRP B . n 
B 1 952  PHE 952  950  950  PHE PHE B . n 
B 1 953  ALA 953  951  951  ALA ALA B . n 
B 1 954  SER 954  952  952  SER SER B . n 
B 1 955  ASP 955  953  953  ASP ASP B . n 
B 1 956  GLU 956  954  954  GLU GLU B . n 
B 1 957  TYR 957  955  955  TYR TYR B . n 
B 1 958  GLU 958  956  956  GLU GLU B . n 
B 1 959  GLN 959  957  957  GLN GLN B . n 
B 1 960  GLN 960  958  958  GLN GLN B . n 
B 1 961  ILE 961  959  959  ILE ILE B . n 
B 1 962  ALA 962  960  960  ALA ALA B . n 
B 1 963  TYR 963  961  961  TYR TYR B . n 
B 1 964  TRP 964  962  962  TRP TRP B . n 
B 1 965  LYS 965  963  963  LYS LYS B . n 
B 1 966  THR 966  964  964  THR THR B . n 
B 1 967  LEU 967  965  965  LEU LEU B . n 
B 1 968  LEU 968  966  966  LEU LEU B . n 
B 1 969  GLN 969  967  967  GLN GLN B . n 
B 1 970  GLY 970  968  968  GLY GLY B . n 
B 1 971  GLU 971  969  969  GLU GLU B . n 
B 1 972  LEU 972  970  970  LEU LEU B . n 
B 1 973  PRO 973  971  971  PRO PRO B . n 
B 1 974  ALA 974  972  972  ALA ALA B . n 
B 1 975  VAL 975  973  973  VAL VAL B . n 
B 1 976  GLN 976  974  974  GLN GLN B . n 
B 1 977  LEU 977  975  975  LEU LEU B . n 
B 1 978  PRO 978  976  976  PRO PRO B . n 
B 1 979  THR 979  977  977  THR THR B . n 
B 1 980  LYS 980  978  978  LYS LYS B . n 
B 1 981  LYS 981  979  979  LYS LYS B . n 
B 1 982  ARG 982  980  980  ARG ARG B . n 
B 1 983  PRO 983  981  981  PRO PRO B . n 
B 1 984  PRO 984  982  982  PRO PRO B . n 
B 1 985  GLN 985  983  983  GLN GLN B . n 
B 1 986  LEU 986  984  984  LEU LEU B . n 
B 1 987  THR 987  985  985  THR THR B . n 
B 1 988  PHE 988  986  986  PHE PHE B . n 
B 1 989  ASP 989  987  987  ASP ASP B . n 
B 1 990  GLY 990  988  988  GLY GLY B . n 
B 1 991  ALA 991  989  989  ALA ALA B . n 
B 1 992  ILE 992  990  990  ILE ILE B . n 
B 1 993  GLN 993  991  991  GLN GLN B . n 
B 1 994  MET 994  992  992  MET MET B . n 
B 1 995  TYR 995  993  993  TYR TYR B . n 
B 1 996  ARG 996  994  994  ARG ARG B . n 
B 1 997  VAL 997  995  995  VAL VAL B . n 
B 1 998  ASN 998  996  996  ASN ASN B . n 
B 1 999  PRO 999  997  997  PRO PRO B . n 
B 1 1000 GLU 1000 998  998  GLU GLU B . n 
B 1 1001 ILE 1001 999  999  ILE ILE B . n 
B 1 1002 THR 1002 1000 1000 THR THR B . n 
B 1 1003 ARG 1003 1001 1001 ARG ARG B . n 
B 1 1004 LYS 1004 1002 1002 LYS LYS B . n 
B 1 1005 LEU 1005 1003 1003 LEU LEU B . n 
B 1 1006 LYS 1006 1004 1004 LYS LYS B . n 
B 1 1007 ALA 1007 1005 1005 ALA ALA B . n 
B 1 1008 THR 1008 1006 1006 THR THR B . n 
B 1 1009 ALA 1009 1007 1007 ALA ALA B . n 
B 1 1010 ALA 1010 1008 1008 ALA ALA B . n 
B 1 1011 LYS 1011 1009 1009 LYS LYS B . n 
B 1 1012 HIS 1012 1010 1010 HIS HIS B . n 
B 1 1013 ASP 1013 1011 1011 ASP ASP B . n 
B 1 1014 LEU 1014 1012 1012 LEU LEU B . n 
B 1 1015 THR 1015 1013 1013 THR THR B . n 
B 1 1016 LEU 1016 1014 1014 LEU LEU B . n 
B 1 1017 TYR 1017 1015 1015 TYR TYR B . n 
B 1 1018 MET 1018 1016 1016 MET MET B . n 
B 1 1019 LEU 1019 1017 1017 LEU LEU B . n 
B 1 1020 MET 1020 1018 1018 MET MET B . n 
B 1 1021 LEU 1021 1019 1019 LEU LEU B . n 
B 1 1022 THR 1022 1020 1020 THR THR B . n 
B 1 1023 ILE 1023 1021 1021 ILE ILE B . n 
B 1 1024 VAL 1024 1022 1022 VAL VAL B . n 
B 1 1025 SER 1025 1023 1023 SER SER B . n 
B 1 1026 ILE 1026 1024 1024 ILE ILE B . n 
B 1 1027 TRP 1027 1025 1025 TRP TRP B . n 
B 1 1028 LEU 1028 1026 1026 LEU LEU B . n 
B 1 1029 SER 1029 1027 1027 SER SER B . n 
B 1 1030 LYS 1030 1028 1028 LYS LYS B . n 
B 1 1031 MET 1031 1029 1029 MET MET B . n 
B 1 1032 ASN 1032 1030 1030 ASN ASN B . n 
B 1 1033 SER 1033 1031 1031 SER SER B . n 
B 1 1034 ASP 1034 1032 1032 ASP ASP B . n 
B 1 1035 SER 1035 1033 1033 SER SER B . n 
B 1 1036 ASN 1036 1034 1034 ASN ASN B . n 
B 1 1037 GLN 1037 1035 1035 GLN GLN B . n 
B 1 1038 VAL 1038 1036 1036 VAL VAL B . n 
B 1 1039 ILE 1039 1037 1037 ILE ILE B . n 
B 1 1040 LEU 1040 1038 1038 LEU LEU B . n 
B 1 1041 GLY 1041 1039 1039 GLY GLY B . n 
B 1 1042 THR 1042 1040 1040 THR THR B . n 
B 1 1043 VAL 1043 1041 1041 VAL VAL B . n 
B 1 1044 THR 1044 1042 1042 THR THR B . n 
B 1 1045 ASP 1045 1043 1043 ASP ASP B . n 
B 1 1046 GLY 1046 1044 1044 GLY GLY B . n 
B 1 1047 ARG 1047 1045 1045 ARG ARG B . n 
B 1 1048 GLN 1048 1046 1046 GLN GLN B . n 
B 1 1049 HIS 1049 1047 1047 HIS HIS B . n 
B 1 1050 PRO 1050 1048 1048 PRO PRO B . n 
B 1 1051 ASP 1051 1049 1049 ASP ASP B . n 
B 1 1052 THR 1052 1050 1050 THR THR B . n 
B 1 1053 ARG 1053 1051 1051 ARG ARG B . n 
B 1 1054 GLU 1054 1052 1052 GLU GLU B . n 
B 1 1055 LEU 1055 1053 1053 LEU LEU B . n 
B 1 1056 LEU 1056 1054 1054 LEU LEU B . n 
B 1 1057 GLY 1057 1055 1055 GLY GLY B . n 
B 1 1058 MET 1058 1056 1056 MET MET B . n 
B 1 1059 PHE 1059 1057 1057 PHE PHE B . n 
B 1 1060 VAL 1060 1058 1058 VAL VAL B . n 
B 1 1061 ASN 1061 1059 1059 ASN ASN B . n 
B 1 1062 THR 1062 1060 1060 THR THR B . n 
B 1 1063 LEU 1063 1061 1061 LEU LEU B . n 
B 1 1064 PRO 1064 1062 1062 PRO PRO B . n 
B 1 1065 LEU 1065 1063 1063 LEU LEU B . n 
B 1 1066 LEU 1066 1064 1064 LEU LEU B . n 
B 1 1067 LEU 1067 1065 1065 LEU LEU B . n 
B 1 1068 SER 1068 1066 1066 SER SER B . n 
B 1 1069 ILE 1069 1067 1067 ILE ILE B . n 
B 1 1070 ASP 1070 1068 1068 ASP ASP B . n 
B 1 1071 HIS 1071 1069 1069 HIS HIS B . n 
B 1 1072 GLU 1072 1070 1070 GLU GLU B . n 
B 1 1073 GLU 1073 1071 1071 GLU GLU B . n 
B 1 1074 SER 1074 1072 1072 SER SER B . n 
B 1 1075 PHE 1075 1073 1073 PHE PHE B . n 
B 1 1076 LEU 1076 1074 1074 LEU LEU B . n 
B 1 1077 HIS 1077 1075 1075 HIS HIS B . n 
B 1 1078 ASN 1078 1076 1076 ASN ASN B . n 
B 1 1079 LEU 1079 1077 1077 LEU LEU B . n 
B 1 1080 GLN 1080 1078 1078 GLN GLN B . n 
B 1 1081 GLN 1081 1079 1079 GLN GLN B . n 
B 1 1082 VAL 1082 1080 1080 VAL VAL B . n 
B 1 1083 LYS 1083 1081 1081 LYS LYS B . n 
B 1 1084 ALA 1084 1082 1082 ALA ALA B . n 
B 1 1085 LYS 1085 1083 1083 LYS LYS B . n 
B 1 1086 LEU 1086 1084 1084 LEU LEU B . n 
B 1 1087 LEU 1087 1085 1085 LEU LEU B . n 
B 1 1088 PRO 1088 1086 1086 PRO PRO B . n 
B 1 1089 ALA 1089 1087 1087 ALA ALA B . n 
B 1 1090 LEU 1090 1088 1088 LEU LEU B . n 
B 1 1091 GLN 1091 1089 1089 GLN GLN B . n 
B 1 1092 ASN 1092 1090 1090 ASN ASN B . n 
B 1 1093 GLN 1093 1091 1091 GLN GLN B . n 
B 1 1094 TYR 1094 1092 1092 TYR TYR B . n 
B 1 1095 VAL 1095 1093 1093 VAL VAL B . n 
B 1 1096 PRO 1096 1094 1094 PRO PRO B . n 
B 1 1097 PHE 1097 1095 1095 PHE PHE B . n 
B 1 1098 ASP 1098 1096 1096 ASP ASP B . n 
B 1 1099 LYS 1099 1097 1097 LYS LYS B . n 
B 1 1100 ILE 1100 1098 1098 ILE ILE B . n 
B 1 1101 LEU 1101 1099 1099 LEU LEU B . n 
B 1 1102 GLU 1102 1100 1100 GLU GLU B . n 
B 1 1103 ALA 1103 1101 1101 ALA ALA B . n 
B 1 1104 ALA 1104 1102 1102 ALA ALA B . n 
B 1 1105 ARG 1105 1103 1103 ARG ARG B . n 
B 1 1106 VAL 1106 1104 1104 VAL VAL B . n 
B 1 1107 LYS 1107 1105 1105 LYS LYS B . n 
B 1 1108 ARG 1108 1106 1106 ARG ARG B . n 
B 1 1109 GLU 1109 1107 1107 GLU GLU B . n 
B 1 1110 GLY 1110 1108 1108 GLY GLY B . n 
B 1 1111 ASN 1111 1109 1109 ASN ASN B . n 
B 1 1112 ARG 1112 1110 1110 ARG ARG B . n 
B 1 1113 HIS 1113 1111 1111 HIS HIS B . n 
B 1 1114 PRO 1114 1112 1112 PRO PRO B . n 
B 1 1115 LEU 1115 1113 1113 LEU LEU B . n 
B 1 1116 PHE 1116 1114 1114 PHE PHE B . n 
B 1 1117 ASP 1117 1115 1115 ASP ASP B . n 
B 1 1118 VAL 1118 1116 1116 VAL VAL B . n 
B 1 1119 MET 1119 1117 1117 MET MET B . n 
B 1 1120 PHE 1120 1118 1118 PHE PHE B . n 
B 1 1121 MET 1121 1119 1119 MET MET B . n 
B 1 1122 MET 1122 1120 1120 MET MET B . n 
B 1 1123 GLN 1123 1121 1121 GLN GLN B . n 
B 1 1124 GLY 1124 1122 1122 GLY GLY B . n 
B 1 1125 ALA 1125 1123 1123 ALA ALA B . n 
B 1 1126 PRO 1126 1124 1124 PRO PRO B . n 
B 1 1127 GLU 1127 1125 1125 GLU GLU B . n 
B 1 1128 THR 1128 1126 1126 THR THR B . n 
B 1 1129 GLU 1129 1127 1127 GLU GLU B . n 
B 1 1130 LEU 1130 1128 1128 LEU LEU B . n 
B 1 1131 GLU 1131 1129 1129 GLU GLU B . n 
B 1 1132 SER 1132 1130 1130 SER SER B . n 
B 1 1133 ASN 1133 1131 1131 ASN ASN B . n 
B 1 1134 MET 1134 1132 1132 MET MET B . n 
B 1 1135 HIS 1135 1133 1133 HIS HIS B . n 
B 1 1136 HIS 1136 1134 1134 HIS HIS B . n 
B 1 1137 ILE 1137 1135 1135 ILE ILE B . n 
B 1 1138 ASN 1138 1136 1136 ASN ASN B . n 
B 1 1139 ALA 1139 1137 1137 ALA ALA B . n 
B 1 1140 GLY 1140 1138 1138 GLY GLY B . n 
B 1 1141 ILE 1141 1139 1139 ILE ILE B . n 
B 1 1142 SER 1142 1140 1140 SER SER B . n 
B 1 1143 LYS 1143 1141 1141 LYS LYS B . n 
B 1 1144 PHE 1144 1142 1142 PHE PHE B . n 
B 1 1145 ASP 1145 1143 1143 ASP ASP B . n 
B 1 1146 LEU 1146 1144 1144 LEU LEU B . n 
B 1 1147 THR 1147 1145 1145 THR THR B . n 
B 1 1148 LEU 1148 1146 1146 LEU LEU B . n 
B 1 1149 GLU 1149 1147 1147 GLU GLU B . n 
B 1 1150 VAL 1150 1148 1148 VAL VAL B . n 
B 1 1151 LEU 1151 1149 1149 LEU LEU B . n 
B 1 1152 GLU 1152 1150 1150 GLU GLU B . n 
B 1 1153 ARG 1153 1151 1151 ARG ARG B . n 
B 1 1154 GLU 1154 1152 1152 GLU GLU B . n 
B 1 1155 ASN 1155 1153 1153 ASN ASN B . n 
B 1 1156 GLY 1156 1154 1154 GLY GLY B . n 
B 1 1157 LEU 1157 1155 1155 LEU LEU B . n 
B 1 1158 ASN 1158 1156 1156 ASN ASN B . n 
B 1 1159 ILE 1159 1157 1157 ILE ILE B . n 
B 1 1160 VAL 1160 1158 1158 VAL VAL B . n 
B 1 1161 PHE 1161 1159 1159 PHE PHE B . n 
B 1 1162 GLU 1162 1160 1160 GLU GLU B . n 
B 1 1163 TYR 1163 1161 1161 TYR TYR B . n 
B 1 1164 ASN 1164 1162 1162 ASN ASN B . n 
B 1 1165 THR 1165 1163 1163 THR THR B . n 
B 1 1166 HIS 1166 1164 1164 HIS HIS B . n 
B 1 1167 LEU 1167 1165 1165 LEU LEU B . n 
B 1 1168 PHE 1168 1166 1166 PHE PHE B . n 
B 1 1169 ASP 1169 1167 1167 ASP ASP B . n 
B 1 1170 GLU 1170 1168 1168 GLU GLU B . n 
B 1 1171 GLY 1171 1169 1169 GLY GLY B . n 
B 1 1172 MET 1172 1170 1170 MET MET B . n 
B 1 1173 ILE 1173 1171 1171 ILE ILE B . n 
B 1 1174 LEU 1174 1172 1172 LEU LEU B . n 
B 1 1175 ARG 1175 1173 1173 ARG ARG B . n 
B 1 1176 MET 1176 1174 1174 MET MET B . n 
B 1 1177 VAL 1177 1175 1175 VAL VAL B . n 
B 1 1178 ALA 1178 1176 1176 ALA ALA B . n 
B 1 1179 GLN 1179 1177 1177 GLN GLN B . n 
B 1 1180 PHE 1180 1178 1178 PHE PHE B . n 
B 1 1181 GLU 1181 1179 1179 GLU GLU B . n 
B 1 1182 HIS 1182 1180 1180 HIS HIS B . n 
B 1 1183 LEU 1183 1181 1181 LEU LEU B . n 
B 1 1184 LEU 1184 1182 1182 LEU LEU B . n 
B 1 1185 LEU 1185 1183 1183 LEU LEU B . n 
B 1 1186 GLN 1186 1184 1184 GLN GLN B . n 
B 1 1187 ALA 1187 1185 1185 ALA ALA B . n 
B 1 1188 VAL 1188 1186 1186 VAL VAL B . n 
B 1 1189 HIS 1189 1187 1187 HIS HIS B . n 
B 1 1190 GLY 1190 1188 1188 GLY GLY B . n 
B 1 1191 LEU 1191 1189 1189 LEU LEU B . n 
B 1 1192 ASP 1192 1190 1190 ASP ASP B . n 
B 1 1193 GLN 1193 1191 1191 GLN GLN B . n 
B 1 1194 GLN 1194 1192 1192 GLN GLN B . n 
B 1 1195 VAL 1195 1193 1193 VAL VAL B . n 
B 1 1196 LYS 1196 1194 1194 LYS LYS B . n 
B 1 1197 ARG 1197 1195 1195 ARG ARG B . n 
B 1 1198 PHE 1198 1196 1196 PHE PHE B . n 
B 1 1199 GLU 1199 1197 1197 GLU GLU B . n 
B 1 1200 LEU 1200 1198 1198 LEU LEU B . n 
B 1 1201 VAL 1201 1199 1199 VAL VAL B . n 
B 1 1202 THR 1202 1200 1200 THR THR B . n 
B 1 1203 GLU 1203 1201 1201 GLU GLU B . n 
B 1 1204 ASP 1204 1202 1202 ASP ASP B . n 
B 1 1205 GLU 1205 1203 1203 GLU GLU B . n 
B 1 1206 LYS 1206 1204 1204 LYS LYS B . n 
B 1 1207 ARG 1207 1205 1205 ARG ARG B . n 
B 1 1208 ASP 1208 1206 1206 ASP ASP B . n 
B 1 1209 LEU 1209 1207 1207 LEU LEU B . n 
B 1 1210 PHE 1210 1208 1208 PHE PHE B . n 
B 1 1211 LEU 1211 1209 1209 LEU LEU B . n 
B 1 1212 ARG 1212 1210 1210 ARG ARG B . n 
B 1 1213 VAL 1213 1211 1211 VAL VAL B . n 
B 1 1214 ASN 1214 1212 1212 ASN ASN B . n 
B 1 1215 ASP 1215 1213 1213 ASP ASP B . n 
B 1 1216 THR 1216 1214 1214 THR THR B . n 
B 1 1217 ALA 1217 1215 1215 ALA ALA B . n 
B 1 1218 LYS 1218 1216 1216 LYS LYS B . n 
B 1 1219 ALA 1219 1217 1217 ALA ALA B . n 
B 1 1220 TYR 1220 1218 1218 TYR TYR B . n 
B 1 1221 PRO 1221 1219 1219 PRO PRO B . n 
B 1 1222 ASN 1222 1220 1220 ASN ASN B . n 
B 1 1223 LYS 1223 1221 1221 LYS LYS B . n 
B 1 1224 LEU 1224 1222 1222 LEU LEU B . n 
B 1 1225 ILE 1225 1223 1223 ILE ILE B . n 
B 1 1226 MET 1226 1224 1224 MET MET B . n 
B 1 1227 SER 1227 1225 1225 SER SER B . n 
B 1 1228 MET 1228 1226 1226 MET MET B . n 
B 1 1229 LEU 1229 1227 1227 LEU LEU B . n 
B 1 1230 GLU 1230 1228 1228 GLU GLU B . n 
B 1 1231 ASP 1231 1229 1229 ASP ASP B . n 
B 1 1232 TRP 1232 1230 1230 TRP TRP B . n 
B 1 1233 ALA 1233 1231 1231 ALA ALA B . n 
B 1 1234 ALA 1234 1232 1232 ALA ALA B . n 
B 1 1235 ALA 1235 1233 1233 ALA ALA B . n 
B 1 1236 THR 1236 1234 1234 THR THR B . n 
B 1 1237 PRO 1237 1235 1235 PRO PRO B . n 
B 1 1238 ASP 1238 1236 1236 ASP ASP B . n 
B 1 1239 LYS 1239 1237 1237 LYS LYS B . n 
B 1 1240 THR 1240 1238 1238 THR THR B . n 
B 1 1241 ALA 1241 1239 1239 ALA ALA B . n 
B 1 1242 LEU 1242 1240 1240 LEU LEU B . n 
B 1 1243 VAL 1243 1241 1241 VAL VAL B . n 
B 1 1244 PHE 1244 1242 1242 PHE PHE B . n 
B 1 1245 ARG 1245 1243 1243 ARG ARG B . n 
B 1 1246 GLU 1246 1244 1244 GLU GLU B . n 
B 1 1247 GLN 1247 1245 1245 GLN GLN B . n 
B 1 1248 ARG 1248 1246 1246 ARG ARG B . n 
B 1 1249 VAL 1249 1247 1247 VAL VAL B . n 
B 1 1250 THR 1250 1248 1248 THR THR B . n 
B 1 1251 TYR 1251 1249 1249 TYR TYR B . n 
B 1 1252 ARG 1252 1250 1250 ARG ARG B . n 
B 1 1253 GLU 1253 1251 1251 GLU GLU B . n 
B 1 1254 LEU 1254 1252 1252 LEU LEU B . n 
B 1 1255 ASN 1255 1253 1253 ASN ASN B . n 
B 1 1256 GLU 1256 1254 1254 GLU GLU B . n 
B 1 1257 ARG 1257 1255 1255 ARG ARG B . n 
B 1 1258 VAL 1258 1256 1256 VAL VAL B . n 
B 1 1259 ASN 1259 1257 1257 ASN ASN B . n 
B 1 1260 GLN 1260 1258 1258 GLN GLN B . n 
B 1 1261 LEU 1261 1259 1259 LEU LEU B . n 
B 1 1262 ALA 1262 1260 1260 ALA ALA B . n 
B 1 1263 HIS 1263 1261 1261 HIS HIS B . n 
B 1 1264 THR 1264 1262 1262 THR THR B . n 
B 1 1265 LEU 1265 1263 1263 LEU LEU B . n 
B 1 1266 ARG 1266 1264 1264 ARG ARG B . n 
B 1 1267 GLU 1267 1265 1265 GLU GLU B . n 
B 1 1268 LYS 1268 1266 1266 LYS LYS B . n 
B 1 1269 GLY 1269 1267 1267 GLY GLY B . n 
B 1 1270 VAL 1270 1268 1268 VAL VAL B . n 
B 1 1271 GLN 1271 1269 1269 GLN GLN B . n 
B 1 1272 PRO 1272 1270 1270 PRO PRO B . n 
B 1 1273 ASP 1273 1271 1271 ASP ASP B . n 
B 1 1274 ASP 1274 1272 1272 ASP ASP B . n 
B 1 1275 LEU 1275 1273 1273 LEU LEU B . n 
B 1 1276 VAL 1276 1274 1274 VAL VAL B . n 
B 1 1277 MET 1277 1275 1275 MET MET B . n 
B 1 1278 LEU 1278 1276 1276 LEU LEU B . n 
B 1 1279 MET 1279 1277 1277 MET MET B . n 
B 1 1280 ALA 1280 1278 1278 ALA ALA B . n 
B 1 1281 GLU 1281 1279 1279 GLU GLU B . n 
B 1 1282 ARG 1282 1280 1280 ARG ARG B . n 
B 1 1283 SER 1283 1281 1281 SER SER B . n 
B 1 1284 VAL 1284 1282 1282 VAL VAL B . n 
B 1 1285 GLU 1285 1283 1283 GLU GLU B . n 
B 1 1286 MET 1286 1284 1284 MET MET B . n 
B 1 1287 MET 1287 1285 1285 MET MET B . n 
B 1 1288 VAL 1288 1286 1286 VAL VAL B . n 
B 1 1289 ALA 1289 1287 1287 ALA ALA B . n 
B 1 1290 ILE 1290 1288 1288 ILE ILE B . n 
B 1 1291 PHE 1291 1289 1289 PHE PHE B . n 
B 1 1292 ALA 1292 1290 1290 ALA ALA B . n 
B 1 1293 VAL 1293 1291 1291 VAL VAL B . n 
B 1 1294 LEU 1294 1292 1292 LEU LEU B . n 
B 1 1295 LYS 1295 1293 1293 LYS LYS B . n 
B 1 1296 ALA 1296 1294 1294 ALA ALA B . n 
B 1 1297 GLY 1297 1295 1295 GLY GLY B . n 
B 1 1298 GLY 1298 1296 1296 GLY GLY B . n 
B 1 1299 ALA 1299 1297 1297 ALA ALA B . n 
B 1 1300 TYR 1300 1298 1298 TYR TYR B . n 
B 1 1301 LEU 1301 1299 1299 LEU LEU B . n 
B 1 1302 PRO 1302 1300 1300 PRO PRO B . n 
B 1 1303 ILE 1303 1301 1301 ILE ILE B . n 
B 1 1304 ASP 1304 1302 1302 ASP ASP B . n 
B 1 1305 PRO 1305 1303 1303 PRO PRO B . n 
B 1 1306 HIS 1306 1304 1304 HIS HIS B . n 
B 1 1307 SER 1307 1305 1305 SER SER B . n 
B 1 1308 PRO 1308 1306 1306 PRO PRO B . n 
B 1 1309 ALA 1309 1307 1307 ALA ALA B . n 
B 1 1310 GLU 1310 1308 1308 GLU GLU B . n 
B 1 1311 ARG 1311 1309 1309 ARG ARG B . n 
B 1 1312 ILE 1312 1310 1310 ILE ILE B . n 
B 1 1313 ALA 1313 1311 1311 ALA ALA B . n 
B 1 1314 TYR 1314 1312 1312 TYR TYR B . n 
B 1 1315 ILE 1315 1313 1313 ILE ILE B . n 
B 1 1316 PHE 1316 1314 1314 PHE PHE B . n 
B 1 1317 ALA 1317 1315 1315 ALA ALA B . n 
B 1 1318 ASP 1318 1316 1316 ASP ASP B . n 
B 1 1319 SER 1319 1317 1317 SER SER B . n 
B 1 1320 GLY 1320 1318 1318 GLY GLY B . n 
B 1 1321 ALA 1321 1319 1319 ALA ALA B . n 
B 1 1322 LYS 1322 1320 1320 LYS LYS B . n 
B 1 1323 LEU 1323 1321 1321 LEU LEU B . n 
B 1 1324 VAL 1324 1322 1322 VAL VAL B . n 
B 1 1325 LEU 1325 1323 1323 LEU LEU B . n 
B 1 1326 ALA 1326 1324 1324 ALA ALA B . n 
B 1 1327 GLN 1327 1325 1325 GLN GLN B . n 
B 1 1328 SER 1328 1326 1326 SER SER B . n 
B 1 1329 PRO 1329 1327 1327 PRO PRO B . n 
B 1 1330 PHE 1330 1328 1328 PHE PHE B . n 
B 1 1331 VAL 1331 1329 1329 VAL VAL B . n 
B 1 1332 GLU 1332 1330 1330 GLU GLU B . n 
B 1 1333 LYS 1333 1331 1331 LYS LYS B . n 
B 1 1334 ALA 1334 1332 1332 ALA ALA B . n 
B 1 1335 SER 1335 1333 1333 SER SER B . n 
B 1 1336 MET 1336 1334 1334 MET MET B . n 
B 1 1337 ALA 1337 1335 1335 ALA ALA B . n 
B 1 1338 GLU 1338 1336 1336 GLU GLU B . n 
B 1 1339 VAL 1339 1337 1337 VAL VAL B . n 
B 1 1340 VAL 1340 1338 1338 VAL VAL B . n 
B 1 1341 LEU 1341 1339 1339 LEU LEU B . n 
B 1 1342 ASP 1342 1340 1340 ASP ASP B . n 
B 1 1343 LEU 1343 1341 1341 LEU LEU B . n 
B 1 1344 ASN 1344 1342 1342 ASN ASN B . n 
B 1 1345 SER 1345 1343 1343 SER SER B . n 
B 1 1346 ALA 1346 1344 1344 ALA ALA B . n 
B 1 1347 SER 1347 1345 1345 SER SER B . n 
B 1 1348 SER 1348 1346 1346 SER SER B . n 
B 1 1349 TYR 1349 1347 1347 TYR TYR B . n 
B 1 1350 ALA 1350 1348 1348 ALA ALA B . n 
B 1 1351 ALA 1351 1349 1349 ALA ALA B . n 
B 1 1352 ASP 1352 1350 1350 ASP ASP B . n 
B 1 1353 THR 1353 1351 1351 THR THR B . n 
B 1 1354 SER 1354 1352 1352 SER SER B . n 
B 1 1355 ASN 1355 1353 1353 ASN ASN B . n 
B 1 1356 PRO 1356 1354 1354 PRO PRO B . n 
B 1 1357 PRO 1357 1355 1355 PRO PRO B . n 
B 1 1358 LEU 1358 1356 1356 LEU LEU B . n 
B 1 1359 VAL 1359 1357 1357 VAL VAL B . n 
B 1 1360 ASN 1360 1358 1358 ASN ASN B . n 
B 1 1361 GLN 1361 1359 1359 GLN GLN B . n 
B 1 1362 PRO 1362 1360 1360 PRO PRO B . n 
B 1 1363 GLY 1363 1361 1361 GLY GLY B . n 
B 1 1364 ASP 1364 1362 1362 ASP ASP B . n 
B 1 1365 LEU 1365 1363 1363 LEU LEU B . n 
B 1 1366 VAL 1366 1364 1364 VAL VAL B . n 
B 1 1367 TYR 1367 1365 1365 TYR TYR B . n 
B 1 1368 VAL 1368 1366 1366 VAL VAL B . n 
B 1 1369 MET 1369 1367 1367 MET MET B . n 
B 1 1370 TYR 1370 1368 1368 TYR TYR B . n 
B 1 1371 THR 1371 1369 1369 THR THR B . n 
B 1 1372 SER 1372 1370 1370 SER SER B . n 
B 1 1373 GLY 1373 1371 ?    ?   ?   B . n 
B 1 1374 SER 1374 1372 ?    ?   ?   B . n 
B 1 1375 THR 1375 1373 1373 THR THR B . n 
B 1 1376 GLY 1376 1374 1374 GLY GLY B . n 
B 1 1377 LYS 1377 1375 1375 LYS LYS B . n 
B 1 1378 PRO 1378 1376 1376 PRO PRO B . n 
B 1 1379 LYS 1379 1377 1377 LYS LYS B . n 
B 1 1380 GLY 1380 1378 1378 GLY GLY B . n 
B 1 1381 VAL 1381 1379 1379 VAL VAL B . n 
B 1 1382 MET 1382 1380 1380 MET MET B . n 
B 1 1383 ILE 1383 1381 1381 ILE ILE B . n 
B 1 1384 GLU 1384 1382 1382 GLU GLU B . n 
B 1 1385 HIS 1385 1383 1383 HIS HIS B . n 
B 1 1386 GLY 1386 1384 1384 GLY GLY B . n 
B 1 1387 ALA 1387 1385 1385 ALA ALA B . n 
B 1 1388 LEU 1388 1386 1386 LEU LEU B . n 
B 1 1389 LEU 1389 1387 1387 LEU LEU B . n 
B 1 1390 ASN 1390 1388 1388 ASN ASN B . n 
B 1 1391 VAL 1391 1389 1389 VAL VAL B . n 
B 1 1392 LEU 1392 1390 1390 LEU LEU B . n 
B 1 1393 HIS 1393 1391 1391 HIS HIS B . n 
B 1 1394 GLY 1394 1392 1392 GLY GLY B . n 
B 1 1395 MET 1395 1393 1393 MET MET B . n 
B 1 1396 GLN 1396 1394 1394 GLN GLN B . n 
B 1 1397 ASP 1397 1395 1395 ASP ASP B . n 
B 1 1398 GLU 1398 1396 1396 GLU GLU B . n 
B 1 1399 TYR 1399 1397 1397 TYR TYR B . n 
B 1 1400 PRO 1400 1398 1398 PRO PRO B . n 
B 1 1401 LEU 1401 1399 1399 LEU LEU B . n 
B 1 1402 LEU 1402 1400 1400 LEU LEU B . n 
B 1 1403 GLN 1403 1401 1401 GLN GLN B . n 
B 1 1404 ASP 1404 1402 1402 ASP ASP B . n 
B 1 1405 ASP 1405 1403 1403 ASP ASP B . n 
B 1 1406 ALA 1406 1404 1404 ALA ALA B . n 
B 1 1407 PHE 1407 1405 1405 PHE PHE B . n 
B 1 1408 LEU 1408 1406 1406 LEU LEU B . n 
B 1 1409 LEU 1409 1407 1407 LEU LEU B . n 
B 1 1410 LYS 1410 1408 1408 LYS LYS B . n 
B 1 1411 THR 1411 1409 1409 THR THR B . n 
B 1 1412 THR 1412 1410 1410 THR THR B . n 
B 1 1413 TYR 1413 1411 1411 TYR TYR B . n 
B 1 1414 ILE 1414 1412 1412 ILE ILE B . n 
B 1 1415 PHE 1415 1413 1413 PHE PHE B . n 
B 1 1416 ASP 1416 1414 1414 ASP ASP B . n 
B 1 1417 ILE 1417 1415 1415 ILE ILE B . n 
B 1 1418 SER 1418 1416 1416 SER SER B . n 
B 1 1419 VAL 1419 1417 1417 VAL VAL B . n 
B 1 1420 ALA 1420 1418 1418 ALA ALA B . n 
B 1 1421 GLU 1421 1419 1419 GLU GLU B . n 
B 1 1422 ILE 1422 1420 1420 ILE ILE B . n 
B 1 1423 PHE 1423 1421 1421 PHE PHE B . n 
B 1 1424 GLY 1424 1422 1422 GLY GLY B . n 
B 1 1425 TRP 1425 1423 1423 TRP TRP B . n 
B 1 1426 VAL 1426 1424 1424 VAL VAL B . n 
B 1 1427 PRO 1427 1425 1425 PRO PRO B . n 
B 1 1428 GLY 1428 1426 1426 GLY GLY B . n 
B 1 1429 ARG 1429 1427 1427 ARG ARG B . n 
B 1 1430 GLY 1430 1428 1428 GLY GLY B . n 
B 1 1431 LYS 1431 1429 1429 LYS LYS B . n 
B 1 1432 LEU 1432 1430 1430 LEU LEU B . n 
B 1 1433 VAL 1433 1431 1431 VAL VAL B . n 
B 1 1434 ILE 1434 1432 1432 ILE ILE B . n 
B 1 1435 LEU 1435 1433 1433 LEU LEU B . n 
B 1 1436 GLU 1436 1434 1434 GLU GLU B . n 
B 1 1437 PRO 1437 1435 1435 PRO PRO B . n 
B 1 1438 GLU 1438 1436 1436 GLU GLU B . n 
B 1 1439 ALA 1439 1437 1437 ALA ALA B . n 
B 1 1440 GLU 1440 1438 1438 GLU GLU B . n 
B 1 1441 LYS 1441 1439 1439 LYS LYS B . n 
B 1 1442 ASN 1442 1440 1440 ASN ASN B . n 
B 1 1443 PRO 1443 1441 1441 PRO PRO B . n 
B 1 1444 LYS 1444 1442 1442 LYS LYS B . n 
B 1 1445 ALA 1445 1443 1443 ALA ALA B . n 
B 1 1446 ILE 1446 1444 1444 ILE ILE B . n 
B 1 1447 TRP 1447 1445 1445 TRP TRP B . n 
B 1 1448 GLN 1448 1446 1446 GLN GLN B . n 
B 1 1449 ALA 1449 1447 1447 ALA ALA B . n 
B 1 1450 VAL 1450 1448 1448 VAL VAL B . n 
B 1 1451 VAL 1451 1449 1449 VAL VAL B . n 
B 1 1452 GLY 1452 1450 1450 GLY GLY B . n 
B 1 1453 ALA 1453 1451 1451 ALA ALA B . n 
B 1 1454 GLY 1454 1452 1452 GLY GLY B . n 
B 1 1455 ILE 1455 1453 1453 ILE ILE B . n 
B 1 1456 THR 1456 1454 1454 THR THR B . n 
B 1 1457 HIS 1457 1455 1455 HIS HIS B . n 
B 1 1458 ILE 1458 1456 1456 ILE ILE B . n 
B 1 1459 ASN 1459 1457 1457 ASN ASN B . n 
B 1 1460 PHE 1460 1458 1458 PHE PHE B . n 
B 1 1461 VAL 1461 1459 1459 VAL VAL B . n 
B 1 1462 PRO 1462 1460 1460 PRO PRO B . n 
B 1 1463 SER 1463 1461 1461 SER SER B . n 
B 1 1464 MET 1464 1462 1462 MET MET B . n 
B 1 1465 LEU 1465 1463 1463 LEU LEU B . n 
B 1 1466 ILE 1466 1464 1464 ILE ILE B . n 
B 1 1467 PRO 1467 1465 1465 PRO PRO B . n 
B 1 1468 PHE 1468 1466 1466 PHE PHE B . n 
B 1 1469 VAL 1469 1467 1467 VAL VAL B . n 
B 1 1470 GLU 1470 1468 1468 GLU GLU B . n 
B 1 1471 TYR 1471 1469 1469 TYR TYR B . n 
B 1 1472 LEU 1472 1470 1470 LEU LEU B . n 
B 1 1473 GLU 1473 1471 1471 GLU GLU B . n 
B 1 1474 GLY 1474 1472 1472 GLY GLY B . n 
B 1 1475 ARG 1475 1473 1473 ARG ARG B . n 
B 1 1476 THR 1476 1474 1474 THR THR B . n 
B 1 1477 GLU 1477 1475 1475 GLU GLU B . n 
B 1 1478 ALA 1478 1476 1476 ALA ALA B . n 
B 1 1479 ASN 1479 1477 1477 ASN ASN B . n 
B 1 1480 ARG 1480 1478 1478 ARG ARG B . n 
B 1 1481 LEU 1481 1479 1479 LEU LEU B . n 
B 1 1482 ARG 1482 1480 1480 ARG ARG B . n 
B 1 1483 TYR 1483 1481 1481 TYR TYR B . n 
B 1 1484 ILE 1484 1482 1482 ILE ILE B . n 
B 1 1485 LEU 1485 1483 1483 LEU LEU B . n 
B 1 1486 ALA 1486 1484 1484 ALA ALA B . n 
B 1 1487 CYS 1487 1485 1485 CYS CYS B . n 
B 1 1488 GLY 1488 1486 1486 GLY GLY B . n 
B 1 1489 GLU 1489 1487 1487 GLU GLU B . n 
B 1 1490 ALA 1490 1488 1488 ALA ALA B . n 
B 1 1491 MET 1491 1489 1489 MET MET B . n 
B 1 1492 PRO 1492 1490 1490 PRO PRO B . n 
B 1 1493 ASP 1493 1491 1491 ASP ASP B . n 
B 1 1494 GLU 1494 1492 1492 GLU GLU B . n 
B 1 1495 LEU 1495 1493 1493 LEU LEU B . n 
B 1 1496 VAL 1496 1494 1494 VAL VAL B . n 
B 1 1497 PRO 1497 1495 1495 PRO PRO B . n 
B 1 1498 LYS 1498 1496 1496 LYS LYS B . n 
B 1 1499 VAL 1499 1497 1497 VAL VAL B . n 
B 1 1500 TYR 1500 1498 1498 TYR TYR B . n 
B 1 1501 GLU 1501 1499 1499 GLU GLU B . n 
B 1 1502 VAL 1502 1500 1500 VAL VAL B . n 
B 1 1503 LEU 1503 1501 1501 LEU LEU B . n 
B 1 1504 PRO 1504 1502 1502 PRO PRO B . n 
B 1 1505 GLU 1505 1503 1503 GLU GLU B . n 
B 1 1506 VAL 1506 1504 1504 VAL VAL B . n 
B 1 1507 LYS 1507 1505 1505 LYS LYS B . n 
B 1 1508 LEU 1508 1506 1506 LEU LEU B . n 
B 1 1509 GLU 1509 1507 1507 GLU GLU B . n 
B 1 1510 ASN 1510 1508 1508 ASN ASN B . n 
B 1 1511 ILE 1511 1509 1509 ILE ILE B . n 
B 1 1512 TYR 1512 1510 1510 TYR TYR B . n 
B 1 1513 GLY 1513 1511 1511 GLY GLY B . n 
B 1 1514 PRO 1514 1512 1512 PRO PRO B . n 
B 1 1515 THR 1515 1513 1513 THR THR B . n 
B 1 1516 GLU 1516 1514 1514 GLU GLU B . n 
B 1 1517 ALA 1517 1515 1515 ALA ALA B . n 
B 1 1518 THR 1518 1516 1516 THR THR B . n 
B 1 1519 ILE 1519 1517 1517 ILE ILE B . n 
B 1 1520 TYR 1520 1518 1518 TYR TYR B . n 
B 1 1521 ALA 1521 1519 1519 ALA ALA B . n 
B 1 1522 SER 1522 1520 1520 SER SER B . n 
B 1 1523 ARG 1523 1521 1521 ARG ARG B . n 
B 1 1524 TYR 1524 1522 1522 TYR TYR B . n 
B 1 1525 SER 1525 1523 1523 SER SER B . n 
B 1 1526 LEU 1526 1524 1524 LEU LEU B . n 
B 1 1527 ALA 1527 1525 1525 ALA ALA B . n 
B 1 1528 LYS 1528 1526 1526 LYS LYS B . n 
B 1 1529 GLY 1529 1527 1527 GLY GLY B . n 
B 1 1530 SER 1530 1528 1528 SER SER B . n 
B 1 1531 GLN 1531 1529 1529 GLN GLN B . n 
B 1 1532 GLU 1532 1530 1530 GLU GLU B . n 
B 1 1533 SER 1533 1531 1531 SER SER B . n 
B 1 1534 PRO 1534 1532 1532 PRO PRO B . n 
B 1 1535 VAL 1535 1533 1533 VAL VAL B . n 
B 1 1536 PRO 1536 1534 1534 PRO PRO B . n 
B 1 1537 ILE 1537 1535 1535 ILE ILE B . n 
B 1 1538 GLY 1538 1536 1536 GLY GLY B . n 
B 1 1539 LYS 1539 1537 1537 LYS LYS B . n 
B 1 1540 PRO 1540 1538 1538 PRO PRO B . n 
B 1 1541 LEU 1541 1539 1539 LEU LEU B . n 
B 1 1542 PRO 1542 1540 1540 PRO PRO B . n 
B 1 1543 ASN 1543 1541 1541 ASN ASN B . n 
B 1 1544 TYR 1544 1542 1542 TYR TYR B . n 
B 1 1545 ARG 1545 1543 1543 ARG ARG B . n 
B 1 1546 MET 1546 1544 1544 MET MET B . n 
B 1 1547 TYR 1547 1545 1545 TYR TYR B . n 
B 1 1548 ILE 1548 1546 1546 ILE ILE B . n 
B 1 1549 ILE 1549 1547 1547 ILE ILE B . n 
B 1 1550 ASN 1550 1548 1548 ASN ASN B . n 
B 1 1551 ARG 1551 1549 1549 ARG ARG B . n 
B 1 1552 HIS 1552 1550 1550 HIS HIS B . n 
B 1 1553 GLY 1553 1551 1551 GLY GLY B . n 
B 1 1554 GLN 1554 1552 1552 GLN GLN B . n 
B 1 1555 LEU 1555 1553 1553 LEU LEU B . n 
B 1 1556 GLN 1556 1554 1554 GLN GLN B . n 
B 1 1557 PRO 1557 1555 1555 PRO PRO B . n 
B 1 1558 ILE 1558 1556 1556 ILE ILE B . n 
B 1 1559 GLY 1559 1557 1557 GLY GLY B . n 
B 1 1560 VAL 1560 1558 1558 VAL VAL B . n 
B 1 1561 PRO 1561 1559 1559 PRO PRO B . n 
B 1 1562 GLY 1562 1560 1560 GLY GLY B . n 
B 1 1563 GLU 1563 1561 1561 GLU GLU B . n 
B 1 1564 LEU 1564 1562 1562 LEU LEU B . n 
B 1 1565 CYS 1565 1563 1563 CYS CYS B . n 
B 1 1566 ILE 1566 1564 1564 ILE ILE B . n 
B 1 1567 ALA 1567 1565 1565 ALA ALA B . n 
B 1 1568 GLY 1568 1566 1566 GLY GLY B . n 
B 1 1569 ALA 1569 1567 1567 ALA ALA B . n 
B 1 1570 SER 1570 1568 1568 SER SER B . n 
B 1 1571 LEU 1571 1569 1569 LEU LEU B . n 
B 1 1572 ALA 1572 1570 1570 ALA ALA B . n 
B 1 1573 ARG 1573 1571 1571 ARG ARG B . n 
B 1 1574 GLY 1574 1572 1572 GLY GLY B . n 
B 1 1575 TYR 1575 1573 1573 TYR TYR B . n 
B 1 1576 LEU 1576 1574 1574 LEU LEU B . n 
B 1 1577 ASN 1577 1575 1575 ASN ASN B . n 
B 1 1578 ASN 1578 1576 1576 ASN ASN B . n 
B 1 1579 PRO 1579 1577 1577 PRO PRO B . n 
B 1 1580 ALA 1580 1578 1578 ALA ALA B . n 
B 1 1581 LEU 1581 1579 1579 LEU LEU B . n 
B 1 1582 THR 1582 1580 1580 THR THR B . n 
B 1 1583 GLU 1583 1581 1581 GLU GLU B . n 
B 1 1584 GLU 1584 1582 1582 GLU GLU B . n 
B 1 1585 LYS 1585 1583 1583 LYS LYS B . n 
B 1 1586 PHE 1586 1584 1584 PHE PHE B . n 
B 1 1587 THR 1587 1585 1585 THR THR B . n 
B 1 1588 PRO 1588 1586 1586 PRO PRO B . n 
B 1 1589 HIS 1589 1587 1587 HIS HIS B . n 
B 1 1590 PRO 1590 1588 1588 PRO PRO B . n 
B 1 1591 LEU 1591 1589 1589 LEU LEU B . n 
B 1 1592 GLU 1592 1590 1590 GLU GLU B . n 
B 1 1593 LYS 1593 1591 1591 LYS LYS B . n 
B 1 1594 GLY 1594 1592 1592 GLY GLY B . n 
B 1 1595 GLU 1595 1593 1593 GLU GLU B . n 
B 1 1596 ARG 1596 1594 1594 ARG ARG B . n 
B 1 1597 ILE 1597 1595 1595 ILE ILE B . n 
B 1 1598 TYR 1598 1596 1596 TYR TYR B . n 
B 1 1599 ARG 1599 1597 1597 ARG ARG B . n 
B 1 1600 THR 1600 1598 1598 THR THR B . n 
B 1 1601 GLY 1601 1599 1599 GLY GLY B . n 
B 1 1602 ASP 1602 1600 1600 ASP ASP B . n 
B 1 1603 LEU 1603 1601 1601 LEU LEU B . n 
B 1 1604 ALA 1604 1602 1602 ALA ALA B . n 
B 1 1605 ARG 1605 1603 1603 ARG ARG B . n 
B 1 1606 TYR 1606 1604 1604 TYR TYR B . n 
B 1 1607 ARG 1607 1605 1605 ARG ARG B . n 
B 1 1608 GLU 1608 1606 1606 GLU GLU B . n 
B 1 1609 ASP 1609 1607 1607 ASP ASP B . n 
B 1 1610 GLY 1610 1608 1608 GLY GLY B . n 
B 1 1611 ASN 1611 1609 1609 ASN ASN B . n 
B 1 1612 ILE 1612 1610 1610 ILE ILE B . n 
B 1 1613 GLU 1613 1611 1611 GLU GLU B . n 
B 1 1614 TYR 1614 1612 1612 TYR TYR B . n 
B 1 1615 LEU 1615 1613 1613 LEU LEU B . n 
B 1 1616 GLY 1616 1614 1614 GLY GLY B . n 
B 1 1617 ARG 1617 1615 1615 ARG ARG B . n 
B 1 1618 MET 1618 1616 1616 MET MET B . n 
B 1 1619 ASP 1619 1617 1617 ASP ASP B . n 
B 1 1620 HIS 1620 1618 1618 HIS HIS B . n 
B 1 1621 GLN 1621 1619 1619 GLN GLN B . n 
B 1 1622 VAL 1622 1620 1620 VAL VAL B . n 
B 1 1623 LYS 1623 1621 1621 LYS LYS B . n 
B 1 1624 ILE 1624 1622 1622 ILE ILE B . n 
B 1 1625 ARG 1625 1623 1623 ARG ARG B . n 
B 1 1626 GLY 1626 1624 1624 GLY GLY B . n 
B 1 1627 TYR 1627 1625 1625 TYR TYR B . n 
B 1 1628 ARG 1628 1626 1626 ARG ARG B . n 
B 1 1629 ILE 1629 1627 1627 ILE ILE B . n 
B 1 1630 GLU 1630 1628 1628 GLU GLU B . n 
B 1 1631 LEU 1631 1629 1629 LEU LEU B . n 
B 1 1632 ASP 1632 1630 1630 ASP ASP B . n 
B 1 1633 GLU 1633 1631 1631 GLU GLU B . n 
B 1 1634 ILE 1634 1632 1632 ILE ILE B . n 
B 1 1635 ARG 1635 1633 1633 ARG ARG B . n 
B 1 1636 SER 1636 1634 1634 SER SER B . n 
B 1 1637 LYS 1637 1635 1635 LYS LYS B . n 
B 1 1638 LEU 1638 1636 1636 LEU LEU B . n 
B 1 1639 ILE 1639 1637 1637 ILE ILE B . n 
B 1 1640 GLN 1640 1638 ?    ?   ?   B . n 
B 1 1641 GLU 1641 1639 ?    ?   ?   B . n 
B 1 1642 GLU 1642 1640 ?    ?   ?   B . n 
B 1 1643 THR 1643 1641 ?    ?   ?   B . n 
B 1 1644 ILE 1644 1642 ?    ?   ?   B . n 
B 1 1645 GLN 1645 1643 ?    ?   ?   B . n 
B 1 1646 ASP 1646 1644 ?    ?   ?   B . n 
B 1 1647 ALA 1647 1645 ?    ?   ?   B . n 
B 1 1648 VAL 1648 1646 1646 VAL VAL B . n 
B 1 1649 VAL 1649 1647 1647 VAL VAL B . n 
B 1 1650 VAL 1650 1648 1648 VAL VAL B . n 
B 1 1651 ALA 1651 1649 1649 ALA ALA B . n 
B 1 1652 ARG 1652 1650 1650 ARG ARG B . n 
B 1 1653 ASN 1653 1651 1651 ASN ASN B . n 
B 1 1654 ASP 1654 1652 1652 ASP ASP B . n 
B 1 1655 GLN 1655 1653 1653 GLN GLN B . n 
B 1 1656 ASN 1656 1654 1654 ASN ASN B . n 
B 1 1657 GLY 1657 1655 1655 GLY GLY B . n 
B 1 1658 GLN 1658 1656 1656 GLN GLN B . n 
B 1 1659 ALA 1659 1657 1657 ALA ALA B . n 
B 1 1660 TYR 1660 1658 1658 TYR TYR B . n 
B 1 1661 LEU 1661 1659 1659 LEU LEU B . n 
B 1 1662 CYS 1662 1660 1660 CYS CYS B . n 
B 1 1663 ALA 1663 1661 ?    ?   ?   B . n 
B 1 1664 TYR 1664 1662 ?    ?   ?   B . n 
B 1 1665 LEU 1665 1663 ?    ?   ?   B . n 
B 1 1666 LEU 1666 1664 ?    ?   ?   B . n 
B 1 1667 SER 1667 1665 ?    ?   ?   B . n 
B 1 1668 GLU 1668 1666 ?    ?   ?   B . n 
B 1 1669 GLN 1669 1667 ?    ?   ?   B . n 
B 1 1670 GLU 1670 1668 ?    ?   ?   B . n 
B 1 1671 TRP 1671 1669 ?    ?   ?   B . n 
B 1 1672 THR 1672 1670 ?    ?   ?   B . n 
B 1 1673 VAL 1673 1671 ?    ?   ?   B . n 
B 1 1674 GLY 1674 1672 1672 GLY GLY B . n 
B 1 1675 GLN 1675 1673 1673 GLN GLN B . n 
B 1 1676 LEU 1676 1674 1674 LEU LEU B . n 
B 1 1677 ARG 1677 1675 1675 ARG ARG B . n 
B 1 1678 GLU 1678 1676 1676 GLU GLU B . n 
B 1 1679 LEU 1679 1677 1677 LEU LEU B . n 
B 1 1680 LEU 1680 1678 1678 LEU LEU B . n 
B 1 1681 ARG 1681 1679 1679 ARG ARG B . n 
B 1 1682 ARG 1682 1680 1680 ARG ARG B . n 
B 1 1683 GLU 1683 1681 1681 GLU GLU B . n 
B 1 1684 LEU 1684 1682 1682 LEU LEU B . n 
B 1 1685 PRO 1685 1683 1683 PRO PRO B . n 
B 1 1686 GLU 1686 1684 1684 GLU GLU B . n 
B 1 1687 TYR 1687 1685 1685 TYR TYR B . n 
B 1 1688 MET 1688 1686 1686 MET MET B . n 
B 1 1689 ILE 1689 1687 1687 ILE ILE B . n 
B 1 1690 PRO 1690 1688 1688 PRO PRO B . n 
B 1 1691 ALA 1691 1689 1689 ALA ALA B . n 
B 1 1692 HIS 1692 1690 ?    ?   ?   B . n 
B 1 1693 PHE 1693 1691 ?    ?   ?   B . n 
B 1 1694 VAL 1694 1692 ?    ?   ?   B . n 
B 1 1695 LEU 1695 1693 ?    ?   ?   B . n 
B 1 1696 LEU 1696 1694 ?    ?   ?   B . n 
B 1 1697 LYS 1697 1695 ?    ?   ?   B . n 
B 1 1698 GLN 1698 1696 ?    ?   ?   B . n 
B 1 1699 PHE 1699 1697 ?    ?   ?   B . n 
B 1 1700 PRO 1700 1698 ?    ?   ?   B . n 
B 1 1701 LEU 1701 1699 ?    ?   ?   B . n 
B 1 1702 THR 1702 1700 ?    ?   ?   B . n 
B 1 1703 ALA 1703 1701 ?    ?   ?   B . n 
B 1 1704 ASN 1704 1702 ?    ?   ?   B . n 
B 1 1705 GLY 1705 1703 ?    ?   ?   B . n 
B 1 1706 LYS 1706 1704 ?    ?   ?   B . n 
B 1 1707 LEU 1707 1705 ?    ?   ?   B . n 
B 1 1708 ASP 1708 1706 ?    ?   ?   B . n 
B 1 1709 ARG 1709 1707 ?    ?   ?   B . n 
B 1 1710 LYS 1710 1708 ?    ?   ?   B . n 
B 1 1711 ALA 1711 1709 ?    ?   ?   B . n 
B 1 1712 LEU 1712 1710 ?    ?   ?   B . n 
B 1 1713 PRO 1713 1711 ?    ?   ?   B . n 
B 1 1714 GLU 1714 1712 ?    ?   ?   B . n 
B 1 1715 PRO 1715 1713 ?    ?   ?   B . n 
B 1 1716 ASP 1716 1714 ?    ?   ?   B . n 
B 1 1717 GLY 1717 1715 ?    ?   ?   B . n 
B 1 1718 SER 1718 1716 ?    ?   ?   B . n 
B 1 1719 VAL 1719 1717 ?    ?   ?   B . n 
B 1 1720 LYS 1720 1718 ?    ?   ?   B . n 
B 1 1721 ALA 1721 1719 ?    ?   ?   B . n 
B 1 1722 GLU 1722 1720 ?    ?   ?   B . n 
B 1 1723 ALA 1723 1721 ?    ?   ?   B . n 
B 1 1724 GLU 1724 1722 ?    ?   ?   B . n 
B 1 1725 TYR 1725 1723 1723 TYR ALA B . n 
B 1 1726 ALA 1726 1724 1724 ALA ALA B . n 
B 1 1727 ALA 1727 1725 1725 ALA ALA B . n 
B 1 1728 PRO 1728 1726 1726 PRO PRO B . n 
B 1 1729 ARG 1729 1727 1727 ARG ARG B . n 
B 1 1730 THR 1730 1728 1728 THR THR B . n 
B 1 1731 GLU 1731 1729 1729 GLU GLU B . n 
B 1 1732 LEU 1732 1730 1730 LEU LEU B . n 
B 1 1733 GLU 1733 1731 1731 GLU GLU B . n 
B 1 1734 ALA 1734 1732 1732 ALA ALA B . n 
B 1 1735 THR 1735 1733 1733 THR THR B . n 
B 1 1736 LEU 1736 1734 1734 LEU LEU B . n 
B 1 1737 ALA 1737 1735 1735 ALA ALA B . n 
B 1 1738 HIS 1738 1736 1736 HIS HIS B . n 
B 1 1739 ILE 1739 1737 1737 ILE ILE B . n 
B 1 1740 TRP 1740 1738 1738 TRP TRP B . n 
B 1 1741 GLY 1741 1739 1739 GLY GLY B . n 
B 1 1742 GLU 1742 1740 1740 GLU GLU B . n 
B 1 1743 VAL 1743 1741 1741 VAL VAL B . n 
B 1 1744 LEU 1744 1742 1742 LEU LEU B . n 
B 1 1745 GLY 1745 1743 1743 GLY GLY B . n 
B 1 1746 ILE 1746 1744 1744 ILE ILE B . n 
B 1 1747 GLU 1747 1745 1745 GLU GLU B . n 
B 1 1748 ARG 1748 1746 1746 ARG ARG B . n 
B 1 1749 ILE 1749 1747 1747 ILE ILE B . n 
B 1 1750 GLY 1750 1748 1748 GLY GLY B . n 
B 1 1751 ILE 1751 1749 1749 ILE ILE B . n 
B 1 1752 ARG 1752 1750 1750 ARG ARG B . n 
B 1 1753 ASP 1753 1751 1751 ASP ASP B . n 
B 1 1754 ASN 1754 1752 1752 ASN ASN B . n 
B 1 1755 PHE 1755 1753 1753 PHE PHE B . n 
B 1 1756 PHE 1756 1754 1754 PHE PHE B . n 
B 1 1757 GLU 1757 1755 1755 GLU GLU B . n 
B 1 1758 LEU 1758 1756 1756 LEU LEU B . n 
B 1 1759 GLY 1759 1757 1757 GLY GLY B . n 
B 1 1760 GLY 1760 1758 1758 GLY GLY B . n 
B 1 1761 ASP 1761 1759 1759 ASP ASP B . n 
B 1 1762 SER 1762 1760 1760 SER SER B . n 
B 1 1763 ILE 1763 1761 1761 ILE ILE B . n 
B 1 1764 LYS 1764 1762 1762 LYS LYS B . n 
B 1 1765 GLY 1765 1763 1763 GLY GLY B . n 
B 1 1766 LEU 1766 1764 1764 LEU LEU B . n 
B 1 1767 GLN 1767 1765 1765 GLN GLN B . n 
B 1 1768 ILE 1768 1766 1766 ILE ILE B . n 
B 1 1769 ALA 1769 1767 1767 ALA ALA B . n 
B 1 1770 SER 1770 1768 1768 SER SER B . n 
B 1 1771 ARG 1771 1769 1769 ARG ARG B . n 
B 1 1772 LEU 1772 1770 1770 LEU LEU B . n 
B 1 1773 GLN 1773 1771 1771 GLN GLN B . n 
B 1 1774 ARG 1774 1772 1772 ARG ARG B . n 
B 1 1775 ILE 1775 1773 1773 ILE ILE B . n 
B 1 1776 ASN 1776 1774 1774 ASN ASN B . n 
B 1 1777 TRP 1777 1775 1775 TRP TRP B . n 
B 1 1778 THR 1778 1776 1776 THR THR B . n 
B 1 1779 MET 1779 1777 1777 MET MET B . n 
B 1 1780 VAL 1780 1778 1778 VAL VAL B . n 
B 1 1781 ILE 1781 1779 1779 ILE ILE B . n 
B 1 1782 ASN 1782 1780 1780 ASN ASN B . n 
B 1 1783 HIS 1783 1781 1781 HIS HIS B . n 
B 1 1784 LEU 1784 1782 1782 LEU LEU B . n 
B 1 1785 PHE 1785 1783 1783 PHE PHE B . n 
B 1 1786 LEU 1786 1784 1784 LEU LEU B . n 
B 1 1787 TYR 1787 1785 1785 TYR TYR B . n 
B 1 1788 PRO 1788 1786 1786 PRO PRO B . n 
B 1 1789 THR 1789 1787 1787 THR THR B . n 
B 1 1790 ILE 1790 1788 1788 ILE ILE B . n 
B 1 1791 GLU 1791 1789 1789 GLU GLU B . n 
B 1 1792 GLN 1792 1790 1790 GLN GLN B . n 
B 1 1793 ILE 1793 1791 1791 ILE ILE B . n 
B 1 1794 ALA 1794 1792 1792 ALA ALA B . n 
B 1 1795 PRO 1795 1793 1793 PRO PRO B . n 
B 1 1796 PHE 1796 1794 1794 PHE PHE B . n 
B 1 1797 VAL 1797 1795 1795 VAL VAL B . n 
B 1 1798 THR 1798 1796 1796 THR THR B . n 
B 1 1799 SER 1799 1797 1797 SER SER B . n 
B 1 1800 GLU 1800 1798 1798 GLU GLU B . n 
B 1 1801 GLN 1801 1799 1799 GLN GLN B . n 
B 1 1802 VAL 1802 1800 1800 VAL VAL B . n 
B 1 1803 VAL 1803 1801 1801 VAL VAL B . n 
B 1 1804 ILE 1804 1802 1802 ILE ILE B . n 
B 1 1805 GLU 1805 1803 1803 GLU GLU B . n 
B 1 1806 ALA 1806 1804 1804 ALA ALA B . n 
B 1 1807 ALA 1807 1805 1805 ALA ALA B . n 
B 1 1808 ALA 1808 1806 1806 ALA ALA B . n 
B 1 1809 GLU 1809 1807 1807 GLU GLU B . n 
B 1 1810 ASN 1810 1808 1808 ASN ASN B . n 
B 1 1811 LEU 1811 1809 1809 LEU LEU B . n 
B 1 1812 TYR 1812 1810 1810 TYR TYR B . n 
B 1 1813 PHE 1813 1811 1811 PHE PHE B . n 
B 1 1814 GLN 1814 1812 1812 GLN GLN B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AMN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AMN 
_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_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 GOL   1   1901 1901 GOL   LIG A . 
D 2 GOL   1   1902 1902 GOL   LIG A . 
E 3 A1AMN 1   1904 1903 A1AMN KPE A . 
F 2 GOL   1   1901 1902 GOL   LIG B . 
G 4 MN    1   1903 1    MN    MN  B . 
H 5 HOH   1   2001 822  HOH   HOH A . 
H 5 HOH   2   2002 542  HOH   HOH A . 
H 5 HOH   3   2003 709  HOH   HOH A . 
H 5 HOH   4   2004 127  HOH   HOH A . 
H 5 HOH   5   2005 116  HOH   HOH A . 
H 5 HOH   6   2006 43   HOH   HOH A . 
H 5 HOH   7   2007 65   HOH   HOH A . 
H 5 HOH   8   2008 361  HOH   HOH A . 
H 5 HOH   9   2009 813  HOH   HOH A . 
H 5 HOH   10  2010 142  HOH   HOH A . 
H 5 HOH   11  2011 903  HOH   HOH A . 
H 5 HOH   12  2012 354  HOH   HOH A . 
H 5 HOH   13  2013 786  HOH   HOH A . 
H 5 HOH   14  2014 99   HOH   HOH A . 
H 5 HOH   15  2015 292  HOH   HOH A . 
H 5 HOH   16  2016 96   HOH   HOH A . 
H 5 HOH   17  2017 734  HOH   HOH A . 
H 5 HOH   18  2018 80   HOH   HOH A . 
H 5 HOH   19  2019 136  HOH   HOH A . 
H 5 HOH   20  2020 12   HOH   HOH A . 
H 5 HOH   21  2021 328  HOH   HOH A . 
H 5 HOH   22  2022 122  HOH   HOH A . 
H 5 HOH   23  2023 718  HOH   HOH A . 
H 5 HOH   24  2024 280  HOH   HOH A . 
H 5 HOH   25  2025 453  HOH   HOH A . 
H 5 HOH   26  2026 32   HOH   HOH A . 
H 5 HOH   27  2027 433  HOH   HOH A . 
H 5 HOH   28  2028 370  HOH   HOH A . 
H 5 HOH   29  2029 310  HOH   HOH A . 
H 5 HOH   30  2030 157  HOH   HOH A . 
H 5 HOH   31  2031 184  HOH   HOH A . 
H 5 HOH   32  2032 400  HOH   HOH A . 
H 5 HOH   33  2033 432  HOH   HOH A . 
H 5 HOH   34  2034 76   HOH   HOH A . 
H 5 HOH   35  2035 496  HOH   HOH A . 
H 5 HOH   36  2036 700  HOH   HOH A . 
H 5 HOH   37  2037 371  HOH   HOH A . 
H 5 HOH   38  2038 628  HOH   HOH A . 
H 5 HOH   39  2039 874  HOH   HOH A . 
H 5 HOH   40  2040 287  HOH   HOH A . 
H 5 HOH   41  2041 141  HOH   HOH A . 
H 5 HOH   42  2042 391  HOH   HOH A . 
H 5 HOH   43  2043 139  HOH   HOH A . 
H 5 HOH   44  2044 695  HOH   HOH A . 
H 5 HOH   45  2045 44   HOH   HOH A . 
H 5 HOH   46  2046 775  HOH   HOH A . 
H 5 HOH   47  2047 303  HOH   HOH A . 
H 5 HOH   48  2048 226  HOH   HOH A . 
H 5 HOH   49  2049 31   HOH   HOH A . 
H 5 HOH   50  2050 336  HOH   HOH A . 
H 5 HOH   51  2051 128  HOH   HOH A . 
H 5 HOH   52  2052 556  HOH   HOH A . 
H 5 HOH   53  2053 190  HOH   HOH A . 
H 5 HOH   54  2054 539  HOH   HOH A . 
H 5 HOH   55  2055 894  HOH   HOH A . 
H 5 HOH   56  2056 654  HOH   HOH A . 
H 5 HOH   57  2057 487  HOH   HOH A . 
H 5 HOH   58  2058 135  HOH   HOH A . 
H 5 HOH   59  2059 331  HOH   HOH A . 
H 5 HOH   60  2060 197  HOH   HOH A . 
H 5 HOH   61  2061 315  HOH   HOH A . 
H 5 HOH   62  2062 112  HOH   HOH A . 
H 5 HOH   63  2063 816  HOH   HOH A . 
H 5 HOH   64  2064 244  HOH   HOH A . 
H 5 HOH   65  2065 441  HOH   HOH A . 
H 5 HOH   66  2066 167  HOH   HOH A . 
H 5 HOH   67  2067 274  HOH   HOH A . 
H 5 HOH   68  2068 876  HOH   HOH A . 
H 5 HOH   69  2069 686  HOH   HOH A . 
H 5 HOH   70  2070 774  HOH   HOH A . 
H 5 HOH   71  2071 898  HOH   HOH A . 
H 5 HOH   72  2072 13   HOH   HOH A . 
H 5 HOH   73  2073 710  HOH   HOH A . 
H 5 HOH   74  2074 763  HOH   HOH A . 
H 5 HOH   75  2075 248  HOH   HOH A . 
H 5 HOH   76  2076 90   HOH   HOH A . 
H 5 HOH   77  2077 717  HOH   HOH A . 
H 5 HOH   78  2078 73   HOH   HOH A . 
H 5 HOH   79  2079 655  HOH   HOH A . 
H 5 HOH   80  2080 761  HOH   HOH A . 
H 5 HOH   81  2081 600  HOH   HOH A . 
H 5 HOH   82  2082 535  HOH   HOH A . 
H 5 HOH   83  2083 624  HOH   HOH A . 
H 5 HOH   84  2084 222  HOH   HOH A . 
H 5 HOH   85  2085 642  HOH   HOH A . 
H 5 HOH   86  2086 100  HOH   HOH A . 
H 5 HOH   87  2087 817  HOH   HOH A . 
H 5 HOH   88  2088 27   HOH   HOH A . 
H 5 HOH   89  2089 296  HOH   HOH A . 
H 5 HOH   90  2090 283  HOH   HOH A . 
H 5 HOH   91  2091 64   HOH   HOH A . 
H 5 HOH   92  2092 525  HOH   HOH A . 
H 5 HOH   93  2093 312  HOH   HOH A . 
H 5 HOH   94  2094 182  HOH   HOH A . 
H 5 HOH   95  2095 880  HOH   HOH A . 
H 5 HOH   96  2096 420  HOH   HOH A . 
H 5 HOH   97  2097 548  HOH   HOH A . 
H 5 HOH   98  2098 264  HOH   HOH A . 
H 5 HOH   99  2099 238  HOH   HOH A . 
H 5 HOH   100 2100 900  HOH   HOH A . 
H 5 HOH   101 2101 137  HOH   HOH A . 
H 5 HOH   102 2102 325  HOH   HOH A . 
H 5 HOH   103 2103 369  HOH   HOH A . 
H 5 HOH   104 2104 749  HOH   HOH A . 
H 5 HOH   105 2105 40   HOH   HOH A . 
H 5 HOH   106 2106 856  HOH   HOH A . 
H 5 HOH   107 2107 89   HOH   HOH A . 
H 5 HOH   108 2108 514  HOH   HOH A . 
H 5 HOH   109 2109 798  HOH   HOH A . 
H 5 HOH   110 2110 546  HOH   HOH A . 
H 5 HOH   111 2111 757  HOH   HOH A . 
H 5 HOH   112 2112 242  HOH   HOH A . 
H 5 HOH   113 2113 704  HOH   HOH A . 
H 5 HOH   114 2114 234  HOH   HOH A . 
H 5 HOH   115 2115 841  HOH   HOH A . 
H 5 HOH   116 2116 48   HOH   HOH A . 
H 5 HOH   117 2117 877  HOH   HOH A . 
H 5 HOH   118 2118 901  HOH   HOH A . 
H 5 HOH   119 2119 745  HOH   HOH A . 
H 5 HOH   120 2120 623  HOH   HOH A . 
H 5 HOH   121 2121 779  HOH   HOH A . 
H 5 HOH   122 2122 20   HOH   HOH A . 
H 5 HOH   123 2123 815  HOH   HOH A . 
H 5 HOH   124 2124 850  HOH   HOH A . 
H 5 HOH   125 2125 737  HOH   HOH A . 
H 5 HOH   126 2126 666  HOH   HOH A . 
H 5 HOH   127 2127 198  HOH   HOH A . 
H 5 HOH   128 2128 422  HOH   HOH A . 
H 5 HOH   129 2129 165  HOH   HOH A . 
H 5 HOH   130 2130 713  HOH   HOH A . 
H 5 HOH   131 2131 585  HOH   HOH A . 
H 5 HOH   132 2132 658  HOH   HOH A . 
H 5 HOH   133 2133 428  HOH   HOH A . 
H 5 HOH   134 2134 398  HOH   HOH A . 
H 5 HOH   135 2135 853  HOH   HOH A . 
H 5 HOH   136 2136 811  HOH   HOH A . 
H 5 HOH   137 2137 810  HOH   HOH A . 
H 5 HOH   138 2138 721  HOH   HOH A . 
H 5 HOH   139 2139 272  HOH   HOH A . 
H 5 HOH   140 2140 486  HOH   HOH A . 
H 5 HOH   141 2141 838  HOH   HOH A . 
H 5 HOH   142 2142 85   HOH   HOH A . 
H 5 HOH   143 2143 644  HOH   HOH A . 
H 5 HOH   144 2144 896  HOH   HOH A . 
H 5 HOH   145 2145 836  HOH   HOH A . 
H 5 HOH   146 2146 324  HOH   HOH A . 
H 5 HOH   147 2147 892  HOH   HOH A . 
H 5 HOH   148 2148 148  HOH   HOH A . 
H 5 HOH   149 2149 294  HOH   HOH A . 
H 5 HOH   150 2150 638  HOH   HOH A . 
H 5 HOH   151 2151 323  HOH   HOH A . 
H 5 HOH   152 2152 474  HOH   HOH A . 
H 5 HOH   153 2153 180  HOH   HOH A . 
H 5 HOH   154 2154 282  HOH   HOH A . 
H 5 HOH   155 2155 891  HOH   HOH A . 
H 5 HOH   156 2156 440  HOH   HOH A . 
H 5 HOH   157 2157 727  HOH   HOH A . 
H 5 HOH   158 2158 768  HOH   HOH A . 
H 5 HOH   159 2159 42   HOH   HOH A . 
H 5 HOH   160 2160 228  HOH   HOH A . 
H 5 HOH   161 2161 812  HOH   HOH A . 
H 5 HOH   162 2162 743  HOH   HOH A . 
H 5 HOH   163 2163 889  HOH   HOH A . 
H 5 HOH   164 2164 411  HOH   HOH A . 
H 5 HOH   165 2165 867  HOH   HOH A . 
H 5 HOH   166 2166 67   HOH   HOH A . 
H 5 HOH   167 2167 862  HOH   HOH A . 
H 5 HOH   168 2168 120  HOH   HOH A . 
H 5 HOH   169 2169 890  HOH   HOH A . 
H 5 HOH   170 2170 824  HOH   HOH A . 
H 5 HOH   171 2171 787  HOH   HOH A . 
H 5 HOH   172 2172 417  HOH   HOH A . 
H 5 HOH   173 2173 843  HOH   HOH A . 
H 5 HOH   174 2174 378  HOH   HOH A . 
H 5 HOH   175 2175 524  HOH   HOH A . 
H 5 HOH   176 2176 209  HOH   HOH A . 
H 5 HOH   177 2177 899  HOH   HOH A . 
H 5 HOH   178 2178 759  HOH   HOH A . 
H 5 HOH   179 2179 840  HOH   HOH A . 
H 5 HOH   180 2180 683  HOH   HOH A . 
H 5 HOH   181 2181 902  HOH   HOH A . 
H 5 HOH   182 2182 888  HOH   HOH A . 
H 5 HOH   183 2183 286  HOH   HOH A . 
H 5 HOH   184 2184 857  HOH   HOH A . 
H 5 HOH   185 2185 906  HOH   HOH A . 
H 5 HOH   186 2186 390  HOH   HOH A . 
H 5 HOH   187 2187 897  HOH   HOH A . 
H 5 HOH   188 2188 208  HOH   HOH A . 
H 5 HOH   189 2189 842  HOH   HOH A . 
I 5 HOH   1   2001 176  HOH   HOH B . 
I 5 HOH   2   2002 750  HOH   HOH B . 
I 5 HOH   3   2003 46   HOH   HOH B . 
I 5 HOH   4   2004 252  HOH   HOH B . 
I 5 HOH   5   2005 81   HOH   HOH B . 
I 5 HOH   6   2006 45   HOH   HOH B . 
I 5 HOH   7   2007 56   HOH   HOH B . 
I 5 HOH   8   2008 14   HOH   HOH B . 
I 5 HOH   9   2009 74   HOH   HOH B . 
I 5 HOH   10  2010 386  HOH   HOH B . 
I 5 HOH   11  2011 868  HOH   HOH B . 
I 5 HOH   12  2012 554  HOH   HOH B . 
I 5 HOH   13  2013 185  HOH   HOH B . 
I 5 HOH   14  2014 15   HOH   HOH B . 
I 5 HOH   15  2015 70   HOH   HOH B . 
I 5 HOH   16  2016 559  HOH   HOH B . 
I 5 HOH   17  2017 2    HOH   HOH B . 
I 5 HOH   18  2018 419  HOH   HOH B . 
I 5 HOH   19  2019 26   HOH   HOH B . 
I 5 HOH   20  2020 504  HOH   HOH B . 
I 5 HOH   21  2021 697  HOH   HOH B . 
I 5 HOH   22  2022 24   HOH   HOH B . 
I 5 HOH   23  2023 466  HOH   HOH B . 
I 5 HOH   24  2024 764  HOH   HOH B . 
I 5 HOH   25  2025 512  HOH   HOH B . 
I 5 HOH   26  2026 374  HOH   HOH B . 
I 5 HOH   27  2027 269  HOH   HOH B . 
I 5 HOH   28  2028 388  HOH   HOH B . 
I 5 HOH   29  2029 155  HOH   HOH B . 
I 5 HOH   30  2030 905  HOH   HOH B . 
I 5 HOH   31  2031 178  HOH   HOH B . 
I 5 HOH   32  2032 415  HOH   HOH B . 
I 5 HOH   33  2033 207  HOH   HOH B . 
I 5 HOH   34  2034 30   HOH   HOH B . 
I 5 HOH   35  2035 28   HOH   HOH B . 
I 5 HOH   36  2036 481  HOH   HOH B . 
I 5 HOH   37  2037 869  HOH   HOH B . 
I 5 HOH   38  2038 247  HOH   HOH B . 
I 5 HOH   39  2039 412  HOH   HOH B . 
I 5 HOH   40  2040 630  HOH   HOH B . 
I 5 HOH   41  2041 138  HOH   HOH B . 
I 5 HOH   42  2042 507  HOH   HOH B . 
I 5 HOH   43  2043 50   HOH   HOH B . 
I 5 HOH   44  2044 530  HOH   HOH B . 
I 5 HOH   45  2045 219  HOH   HOH B . 
I 5 HOH   46  2046 150  HOH   HOH B . 
I 5 HOH   47  2047 865  HOH   HOH B . 
I 5 HOH   48  2048 653  HOH   HOH B . 
I 5 HOH   49  2049 485  HOH   HOH B . 
I 5 HOH   50  2050 640  HOH   HOH B . 
I 5 HOH   51  2051 594  HOH   HOH B . 
I 5 HOH   52  2052 93   HOH   HOH B . 
I 5 HOH   53  2053 870  HOH   HOH B . 
I 5 HOH   54  2054 298  HOH   HOH B . 
I 5 HOH   55  2055 186  HOH   HOH B . 
I 5 HOH   56  2056 95   HOH   HOH B . 
I 5 HOH   57  2057 544  HOH   HOH B . 
I 5 HOH   58  2058 882  HOH   HOH B . 
I 5 HOH   59  2059 102  HOH   HOH B . 
I 5 HOH   60  2060 297  HOH   HOH B . 
I 5 HOH   61  2061 339  HOH   HOH B . 
I 5 HOH   62  2062 635  HOH   HOH B . 
I 5 HOH   63  2063 833  HOH   HOH B . 
I 5 HOH   64  2064 140  HOH   HOH B . 
I 5 HOH   65  2065 643  HOH   HOH B . 
I 5 HOH   66  2066 145  HOH   HOH B . 
I 5 HOH   67  2067 454  HOH   HOH B . 
I 5 HOH   68  2068 224  HOH   HOH B . 
I 5 HOH   69  2069 291  HOH   HOH B . 
I 5 HOH   70  2070 576  HOH   HOH B . 
I 5 HOH   71  2071 529  HOH   HOH B . 
I 5 HOH   72  2072 534  HOH   HOH B . 
I 5 HOH   73  2073 793  HOH   HOH B . 
I 5 HOH   74  2074 204  HOH   HOH B . 
I 5 HOH   75  2075 864  HOH   HOH B . 
I 5 HOH   76  2076 680  HOH   HOH B . 
I 5 HOH   77  2077 403  HOH   HOH B . 
I 5 HOH   78  2078 83   HOH   HOH B . 
I 5 HOH   79  2079 846  HOH   HOH B . 
I 5 HOH   80  2080 439  HOH   HOH B . 
I 5 HOH   81  2081 97   HOH   HOH B . 
I 5 HOH   82  2082 508  HOH   HOH B . 
I 5 HOH   83  2083 682  HOH   HOH B . 
I 5 HOH   84  2084 227  HOH   HOH B . 
I 5 HOH   85  2085 431  HOH   HOH B . 
I 5 HOH   86  2086 21   HOH   HOH B . 
I 5 HOH   87  2087 861  HOH   HOH B . 
I 5 HOH   88  2088 131  HOH   HOH B . 
I 5 HOH   89  2089 51   HOH   HOH B . 
I 5 HOH   90  2090 878  HOH   HOH B . 
I 5 HOH   91  2091 305  HOH   HOH B . 
I 5 HOH   92  2092 858  HOH   HOH B . 
I 5 HOH   93  2093 735  HOH   HOH B . 
I 5 HOH   94  2094 859  HOH   HOH B . 
I 5 HOH   95  2095 599  HOH   HOH B . 
I 5 HOH   96  2096 262  HOH   HOH B . 
I 5 HOH   97  2097 143  HOH   HOH B . 
I 5 HOH   98  2098 732  HOH   HOH B . 
I 5 HOH   99  2099 664  HOH   HOH B . 
I 5 HOH   100 2100 875  HOH   HOH B . 
I 5 HOH   101 2101 87   HOH   HOH B . 
I 5 HOH   102 2102 809  HOH   HOH B . 
I 5 HOH   103 2103 84   HOH   HOH B . 
I 5 HOH   104 2104 879  HOH   HOH B . 
I 5 HOH   105 2105 108  HOH   HOH B . 
I 5 HOH   106 2106 796  HOH   HOH B . 
I 5 HOH   107 2107 86   HOH   HOH B . 
I 5 HOH   108 2108 777  HOH   HOH B . 
I 5 HOH   109 2109 852  HOH   HOH B . 
I 5 HOH   110 2110 646  HOH   HOH B . 
I 5 HOH   111 2111 337  HOH   HOH B . 
I 5 HOH   112 2112 622  HOH   HOH B . 
I 5 HOH   113 2113 800  HOH   HOH B . 
I 5 HOH   114 2114 47   HOH   HOH B . 
I 5 HOH   115 2115 436  HOH   HOH B . 
I 5 HOH   116 2116 511  HOH   HOH B . 
I 5 HOH   117 2117 75   HOH   HOH B . 
I 5 HOH   118 2118 410  HOH   HOH B . 
I 5 HOH   119 2119 146  HOH   HOH B . 
I 5 HOH   120 2120 860  HOH   HOH B . 
I 5 HOH   121 2121 893  HOH   HOH B . 
I 5 HOH   122 2122 895  HOH   HOH B . 
I 5 HOH   123 2123 367  HOH   HOH B . 
I 5 HOH   124 2124 549  HOH   HOH B . 
I 5 HOH   125 2125 241  HOH   HOH B . 
I 5 HOH   126 2126 41   HOH   HOH B . 
I 5 HOH   127 2127 802  HOH   HOH B . 
I 5 HOH   128 2128 505  HOH   HOH B . 
I 5 HOH   129 2129 851  HOH   HOH B . 
I 5 HOH   130 2130 8    HOH   HOH B . 
I 5 HOH   131 2131 873  HOH   HOH B . 
I 5 HOH   132 2132 907  HOH   HOH B . 
I 5 HOH   133 2133 911  HOH   HOH B . 
I 5 HOH   134 2134 355  HOH   HOH B . 
I 5 HOH   135 2135 834  HOH   HOH B . 
I 5 HOH   136 2136 910  HOH   HOH B . 
I 5 HOH   137 2137 183  HOH   HOH B . 
I 5 HOH   138 2138 217  HOH   HOH B . 
I 5 HOH   139 2139 849  HOH   HOH B . 
I 5 HOH   140 2140 855  HOH   HOH B . 
I 5 HOH   141 2141 765  HOH   HOH B . 
I 5 HOH   142 2142 863  HOH   HOH B . 
I 5 HOH   143 2143 706  HOH   HOH B . 
I 5 HOH   144 2144 212  HOH   HOH B . 
I 5 HOH   145 2145 909  HOH   HOH B . 
I 5 HOH   146 2146 785  HOH   HOH B . 
I 5 HOH   147 2147 881  HOH   HOH B . 
I 5 HOH   148 2148 456  HOH   HOH B . 
I 5 HOH   149 2149 884  HOH   HOH B . 
I 5 HOH   150 2150 844  HOH   HOH B . 
I 5 HOH   151 2151 883  HOH   HOH B . 
I 5 HOH   152 2152 444  HOH   HOH B . 
I 5 HOH   153 2153 1    HOH   HOH B . 
I 5 HOH   154 2154 872  HOH   HOH B . 
I 5 HOH   155 2155 478  HOH   HOH B . 
I 5 HOH   156 2156 848  HOH   HOH B . 
I 5 HOH   157 2157 246  HOH   HOH B . 
I 5 HOH   158 2158 904  HOH   HOH B . 
I 5 HOH   159 2159 847  HOH   HOH B . 
I 5 HOH   160 2160 803  HOH   HOH B . 
I 5 HOH   161 2161 908  HOH   HOH B . 
# 
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 MET 1    ? CG  ? A MET 1    CG  
2   1 Y 1 A MET 1    ? SD  ? A MET 1    SD  
3   1 Y 1 A MET 1    ? CE  ? A MET 1    CE  
4   1 Y 1 A HIS 36   ? CG  ? A HIS 36   CG  
5   1 Y 1 A HIS 36   ? ND1 ? A HIS 36   ND1 
6   1 Y 1 A HIS 36   ? CD2 ? A HIS 36   CD2 
7   1 Y 1 A HIS 36   ? CE1 ? A HIS 36   CE1 
8   1 Y 1 A HIS 36   ? NE2 ? A HIS 36   NE2 
9   1 Y 1 A GLN 38   ? CG  ? A GLN 38   CG  
10  1 Y 1 A GLN 38   ? CD  ? A GLN 38   CD  
11  1 Y 1 A GLN 38   ? OE1 ? A GLN 38   OE1 
12  1 Y 1 A GLN 38   ? NE2 ? A GLN 38   NE2 
13  1 Y 1 A GLU 44   ? CG  ? A GLU 44   CG  
14  1 Y 1 A GLU 44   ? CD  ? A GLU 44   CD  
15  1 Y 1 A GLU 44   ? OE1 ? A GLU 44   OE1 
16  1 Y 1 A GLU 44   ? OE2 ? A GLU 44   OE2 
17  1 Y 1 A LYS 195  ? CG  ? A LYS 195  CG  
18  1 Y 1 A LYS 195  ? CD  ? A LYS 195  CD  
19  1 Y 1 A LYS 195  ? CE  ? A LYS 195  CE  
20  1 Y 1 A LYS 195  ? NZ  ? A LYS 195  NZ  
21  1 Y 1 A GLU 198  ? CG  ? A GLU 198  CG  
22  1 Y 1 A GLU 198  ? CD  ? A GLU 198  CD  
23  1 Y 1 A GLU 198  ? OE1 ? A GLU 198  OE1 
24  1 Y 1 A GLU 198  ? OE2 ? A GLU 198  OE2 
25  1 Y 1 A LYS 199  ? CG  ? A LYS 199  CG  
26  1 Y 1 A LYS 199  ? CD  ? A LYS 199  CD  
27  1 Y 1 A LYS 199  ? CE  ? A LYS 199  CE  
28  1 Y 1 A LYS 199  ? NZ  ? A LYS 199  NZ  
29  1 Y 1 A GLU 290  ? CG  ? A GLU 290  CG  
30  1 Y 1 A GLU 290  ? CD  ? A GLU 290  CD  
31  1 Y 1 A GLU 290  ? OE1 ? A GLU 290  OE1 
32  1 Y 1 A GLU 290  ? OE2 ? A GLU 290  OE2 
33  1 Y 1 A GLU 331  ? CG  ? A GLU 331  CG  
34  1 Y 1 A GLU 331  ? CD  ? A GLU 331  CD  
35  1 Y 1 A GLU 331  ? OE1 ? A GLU 331  OE1 
36  1 Y 1 A GLU 331  ? OE2 ? A GLU 331  OE2 
37  1 Y 1 A GLU 547  ? CG  ? A GLU 547  CG  
38  1 Y 1 A GLU 547  ? CD  ? A GLU 547  CD  
39  1 Y 1 A GLU 547  ? OE1 ? A GLU 547  OE1 
40  1 Y 1 A GLU 547  ? OE2 ? A GLU 547  OE2 
41  1 Y 1 A ARG 594  ? CG  ? A ARG 594  CG  
42  1 Y 1 A ARG 594  ? CD  ? A ARG 594  CD  
43  1 Y 1 A ARG 594  ? NE  ? A ARG 594  NE  
44  1 Y 1 A ARG 594  ? CZ  ? A ARG 594  CZ  
45  1 Y 1 A ARG 594  ? NH1 ? A ARG 594  NH1 
46  1 Y 1 A ARG 594  ? NH2 ? A ARG 594  NH2 
47  1 Y 1 A ARG 624  ? CG  ? A ARG 624  CG  
48  1 Y 1 A ARG 624  ? CD  ? A ARG 624  CD  
49  1 Y 1 A ARG 624  ? NE  ? A ARG 624  NE  
50  1 Y 1 A ARG 624  ? CZ  ? A ARG 624  CZ  
51  1 Y 1 A ARG 624  ? NH1 ? A ARG 624  NH1 
52  1 Y 1 A ARG 624  ? NH2 ? A ARG 624  NH2 
53  1 Y 1 A GLU 635  ? CG  ? A GLU 635  CG  
54  1 Y 1 A GLU 635  ? CD  ? A GLU 635  CD  
55  1 Y 1 A GLU 635  ? OE1 ? A GLU 635  OE1 
56  1 Y 1 A GLU 635  ? OE2 ? A GLU 635  OE2 
57  1 Y 1 A ARG 676  ? CG  ? A ARG 676  CG  
58  1 Y 1 A ARG 676  ? CD  ? A ARG 676  CD  
59  1 Y 1 A ARG 676  ? NE  ? A ARG 676  NE  
60  1 Y 1 A ARG 676  ? CZ  ? A ARG 676  CZ  
61  1 Y 1 A ARG 676  ? NH1 ? A ARG 676  NH1 
62  1 Y 1 A ARG 676  ? NH2 ? A ARG 676  NH2 
63  1 Y 1 A ARG 855  ? CG  ? A ARG 857  CG  
64  1 Y 1 A ARG 855  ? CD  ? A ARG 857  CD  
65  1 Y 1 A ARG 855  ? NE  ? A ARG 857  NE  
66  1 Y 1 A ARG 855  ? CZ  ? A ARG 857  CZ  
67  1 Y 1 A ARG 855  ? NH1 ? A ARG 857  NH1 
68  1 Y 1 A ARG 855  ? NH2 ? A ARG 857  NH2 
69  1 Y 1 A GLU 857  ? CG  ? A GLU 859  CG  
70  1 Y 1 A GLU 857  ? CD  ? A GLU 859  CD  
71  1 Y 1 A GLU 857  ? OE1 ? A GLU 859  OE1 
72  1 Y 1 A GLU 857  ? OE2 ? A GLU 859  OE2 
73  1 Y 1 A LYS 979  ? CG  ? A LYS 981  CG  
74  1 Y 1 A LYS 979  ? CD  ? A LYS 981  CD  
75  1 Y 1 A LYS 979  ? CE  ? A LYS 981  CE  
76  1 Y 1 A LYS 979  ? NZ  ? A LYS 981  NZ  
77  1 Y 1 A LYS 1105 ? CG  ? A LYS 1107 CG  
78  1 Y 1 A LYS 1105 ? CD  ? A LYS 1107 CD  
79  1 Y 1 A LYS 1105 ? CE  ? A LYS 1107 CE  
80  1 Y 1 A LYS 1105 ? NZ  ? A LYS 1107 NZ  
81  1 Y 1 A GLU 1308 ? CG  ? A GLU 1310 CG  
82  1 Y 1 A GLU 1308 ? CD  ? A GLU 1310 CD  
83  1 Y 1 A GLU 1308 ? OE1 ? A GLU 1310 OE1 
84  1 Y 1 A GLU 1308 ? OE2 ? A GLU 1310 OE2 
85  1 Y 1 A LYS 1320 ? CG  ? A LYS 1322 CG  
86  1 Y 1 A LYS 1320 ? CD  ? A LYS 1322 CD  
87  1 Y 1 A LYS 1320 ? CE  ? A LYS 1322 CE  
88  1 Y 1 A LYS 1320 ? NZ  ? A LYS 1322 NZ  
89  1 Y 1 A GLU 1330 ? CG  ? A GLU 1332 CG  
90  1 Y 1 A GLU 1330 ? CD  ? A GLU 1332 CD  
91  1 Y 1 A GLU 1330 ? OE1 ? A GLU 1332 OE1 
92  1 Y 1 A GLU 1330 ? OE2 ? A GLU 1332 OE2 
93  1 Y 1 A LYS 1375 ? CG  ? A LYS 1377 CG  
94  1 Y 1 A LYS 1375 ? CD  ? A LYS 1377 CD  
95  1 Y 1 A LYS 1375 ? CE  ? A LYS 1377 CE  
96  1 Y 1 A LYS 1375 ? NZ  ? A LYS 1377 NZ  
97  1 Y 1 A LYS 1377 ? CG  ? A LYS 1379 CG  
98  1 Y 1 A LYS 1377 ? CD  ? A LYS 1379 CD  
99  1 Y 1 A LYS 1377 ? CE  ? A LYS 1379 CE  
100 1 Y 1 A LYS 1377 ? NZ  ? A LYS 1379 NZ  
101 1 Y 1 A LYS 1442 ? CG  ? A LYS 1444 CG  
102 1 Y 1 A LYS 1442 ? CD  ? A LYS 1444 CD  
103 1 Y 1 A LYS 1442 ? CE  ? A LYS 1444 CE  
104 1 Y 1 A LYS 1442 ? NZ  ? A LYS 1444 NZ  
105 1 Y 1 A LYS 1526 ? CG  ? A LYS 1528 CG  
106 1 Y 1 A LYS 1526 ? CD  ? A LYS 1528 CD  
107 1 Y 1 A LYS 1526 ? CE  ? A LYS 1528 CE  
108 1 Y 1 A LYS 1526 ? NZ  ? A LYS 1528 NZ  
109 1 Y 1 A GLU 1628 ? CG  ? A GLU 1630 CG  
110 1 Y 1 A GLU 1628 ? CD  ? A GLU 1630 CD  
111 1 Y 1 A GLU 1628 ? OE1 ? A GLU 1630 OE1 
112 1 Y 1 A GLU 1628 ? OE2 ? A GLU 1630 OE2 
113 1 Y 1 A ASP 1630 ? CG  ? A ASP 1632 CG  
114 1 Y 1 A ASP 1630 ? OD1 ? A ASP 1632 OD1 
115 1 Y 1 A ASP 1630 ? OD2 ? A ASP 1632 OD2 
116 1 Y 1 A ILE 1637 ? CG1 ? A ILE 1639 CG1 
117 1 Y 1 A ILE 1637 ? CG2 ? A ILE 1639 CG2 
118 1 Y 1 A ILE 1637 ? CD1 ? A ILE 1639 CD1 
119 1 Y 1 A GLU 1639 ? CG  ? A GLU 1641 CG  
120 1 Y 1 A GLU 1639 ? CD  ? A GLU 1641 CD  
121 1 Y 1 A GLU 1639 ? OE1 ? A GLU 1641 OE1 
122 1 Y 1 A GLU 1639 ? OE2 ? A GLU 1641 OE2 
123 1 Y 1 A GLU 1640 ? CG  ? A GLU 1642 CG  
124 1 Y 1 A GLU 1640 ? CD  ? A GLU 1642 CD  
125 1 Y 1 A GLU 1640 ? OE1 ? A GLU 1642 OE1 
126 1 Y 1 A GLU 1640 ? OE2 ? A GLU 1642 OE2 
127 1 Y 1 A ARG 1650 ? CG  ? A ARG 1652 CG  
128 1 Y 1 A ARG 1650 ? CD  ? A ARG 1652 CD  
129 1 Y 1 A ARG 1650 ? NE  ? A ARG 1652 NE  
130 1 Y 1 A ARG 1650 ? CZ  ? A ARG 1652 CZ  
131 1 Y 1 A ARG 1650 ? NH1 ? A ARG 1652 NH1 
132 1 Y 1 A ARG 1650 ? NH2 ? A ARG 1652 NH2 
133 1 Y 1 A ASP 1652 ? CG  ? A ASP 1654 CG  
134 1 Y 1 A ASP 1652 ? OD1 ? A ASP 1654 OD1 
135 1 Y 1 A ASP 1652 ? OD2 ? A ASP 1654 OD2 
136 1 Y 1 A GLN 1667 ? CG  ? A GLN 1669 CG  
137 1 Y 1 A GLN 1667 ? CD  ? A GLN 1669 CD  
138 1 Y 1 A GLN 1667 ? OE1 ? A GLN 1669 OE1 
139 1 Y 1 A GLN 1667 ? NE2 ? A GLN 1669 NE2 
140 1 Y 1 A TRP 1669 ? CG  ? A TRP 1671 CG  
141 1 Y 1 A TRP 1669 ? CD1 ? A TRP 1671 CD1 
142 1 Y 1 A TRP 1669 ? CD2 ? A TRP 1671 CD2 
143 1 Y 1 A TRP 1669 ? NE1 ? A TRP 1671 NE1 
144 1 Y 1 A TRP 1669 ? CE2 ? A TRP 1671 CE2 
145 1 Y 1 A TRP 1669 ? CE3 ? A TRP 1671 CE3 
146 1 Y 1 A TRP 1669 ? CZ2 ? A TRP 1671 CZ2 
147 1 Y 1 A TRP 1669 ? CZ3 ? A TRP 1671 CZ3 
148 1 Y 1 A TRP 1669 ? CH2 ? A TRP 1671 CH2 
149 1 Y 1 A GLN 1673 ? CG  ? A GLN 1675 CG  
150 1 Y 1 A GLN 1673 ? CD  ? A GLN 1675 CD  
151 1 Y 1 A GLN 1673 ? OE1 ? A GLN 1675 OE1 
152 1 Y 1 A GLN 1673 ? NE2 ? A GLN 1675 NE2 
153 1 Y 1 A LEU 1674 ? CG  ? A LEU 1676 CG  
154 1 Y 1 A LEU 1674 ? CD1 ? A LEU 1676 CD1 
155 1 Y 1 A LEU 1674 ? CD2 ? A LEU 1676 CD2 
156 1 Y 1 A GLU 1676 ? CG  ? A GLU 1678 CG  
157 1 Y 1 A GLU 1676 ? CD  ? A GLU 1678 CD  
158 1 Y 1 A GLU 1676 ? OE1 ? A GLU 1678 OE1 
159 1 Y 1 A GLU 1676 ? OE2 ? A GLU 1678 OE2 
160 1 Y 1 A ARG 1680 ? CG  ? A ARG 1682 CG  
161 1 Y 1 A ARG 1680 ? CD  ? A ARG 1682 CD  
162 1 Y 1 A ARG 1680 ? NE  ? A ARG 1682 NE  
163 1 Y 1 A ARG 1680 ? CZ  ? A ARG 1682 CZ  
164 1 Y 1 A ARG 1680 ? NH1 ? A ARG 1682 NH1 
165 1 Y 1 A ARG 1680 ? NH2 ? A ARG 1682 NH2 
166 1 Y 1 A GLU 1745 ? CG  ? A GLU 1747 CG  
167 1 Y 1 A GLU 1745 ? CD  ? A GLU 1747 CD  
168 1 Y 1 A GLU 1745 ? OE1 ? A GLU 1747 OE1 
169 1 Y 1 A GLU 1745 ? OE2 ? A GLU 1747 OE2 
170 1 Y 1 A ARG 1746 ? CG  ? A ARG 1748 CG  
171 1 Y 1 A ARG 1746 ? CD  ? A ARG 1748 CD  
172 1 Y 1 A ARG 1746 ? NE  ? A ARG 1748 NE  
173 1 Y 1 A ARG 1746 ? CZ  ? A ARG 1748 CZ  
174 1 Y 1 A ARG 1746 ? NH1 ? A ARG 1748 NH1 
175 1 Y 1 A ARG 1746 ? NH2 ? A ARG 1748 NH2 
176 1 Y 1 A VAL 1800 ? CG1 ? A VAL 1802 CG1 
177 1 Y 1 A VAL 1800 ? CG2 ? A VAL 1802 CG2 
178 1 Y 1 B GLU 33   ? CG  ? B GLU 33   CG  
179 1 Y 1 B GLU 33   ? CD  ? B GLU 33   CD  
180 1 Y 1 B GLU 33   ? OE1 ? B GLU 33   OE1 
181 1 Y 1 B GLU 33   ? OE2 ? B GLU 33   OE2 
182 1 Y 1 B GLU 44   ? CG  ? B GLU 44   CG  
183 1 Y 1 B GLU 44   ? CD  ? B GLU 44   CD  
184 1 Y 1 B GLU 44   ? OE1 ? B GLU 44   OE1 
185 1 Y 1 B GLU 44   ? OE2 ? B GLU 44   OE2 
186 1 Y 1 B LYS 59   ? CG  ? B LYS 59   CG  
187 1 Y 1 B LYS 59   ? CD  ? B LYS 59   CD  
188 1 Y 1 B LYS 59   ? CE  ? B LYS 59   CE  
189 1 Y 1 B LYS 59   ? NZ  ? B LYS 59   NZ  
190 1 Y 1 B ARG 66   ? CG  ? B ARG 66   CG  
191 1 Y 1 B ARG 66   ? CD  ? B ARG 66   CD  
192 1 Y 1 B ARG 66   ? NE  ? B ARG 66   NE  
193 1 Y 1 B ARG 66   ? CZ  ? B ARG 66   CZ  
194 1 Y 1 B ARG 66   ? NH1 ? B ARG 66   NH1 
195 1 Y 1 B ARG 66   ? NH2 ? B ARG 66   NH2 
196 1 Y 1 B ARG 594  ? CG  ? B ARG 594  CG  
197 1 Y 1 B ARG 594  ? CD  ? B ARG 594  CD  
198 1 Y 1 B ARG 594  ? NE  ? B ARG 594  NE  
199 1 Y 1 B ARG 594  ? CZ  ? B ARG 594  CZ  
200 1 Y 1 B ARG 594  ? NH1 ? B ARG 594  NH1 
201 1 Y 1 B ARG 594  ? NH2 ? B ARG 594  NH2 
202 1 Y 1 B GLU 635  ? CG  ? B GLU 635  CG  
203 1 Y 1 B GLU 635  ? CD  ? B GLU 635  CD  
204 1 Y 1 B GLU 635  ? OE1 ? B GLU 635  OE1 
205 1 Y 1 B GLU 635  ? OE2 ? B GLU 635  OE2 
206 1 Y 1 B GLU 636  ? CG  ? B GLU 636  CG  
207 1 Y 1 B GLU 636  ? CD  ? B GLU 636  CD  
208 1 Y 1 B GLU 636  ? OE1 ? B GLU 636  OE1 
209 1 Y 1 B GLU 636  ? OE2 ? B GLU 636  OE2 
210 1 Y 1 B LYS 663  ? CG  ? B LYS 663  CG  
211 1 Y 1 B LYS 663  ? CD  ? B LYS 663  CD  
212 1 Y 1 B LYS 663  ? CE  ? B LYS 663  CE  
213 1 Y 1 B LYS 663  ? NZ  ? B LYS 663  NZ  
214 1 Y 1 B ARG 676  ? CG  ? B ARG 676  CG  
215 1 Y 1 B ARG 676  ? CD  ? B ARG 676  CD  
216 1 Y 1 B ARG 676  ? NE  ? B ARG 676  NE  
217 1 Y 1 B ARG 676  ? CZ  ? B ARG 676  CZ  
218 1 Y 1 B ARG 676  ? NH1 ? B ARG 676  NH1 
219 1 Y 1 B ARG 676  ? NH2 ? B ARG 676  NH2 
220 1 Y 1 B ASP 691  ? CG  ? B ASP 691  CG  
221 1 Y 1 B ASP 691  ? OD1 ? B ASP 691  OD1 
222 1 Y 1 B ASP 691  ? OD2 ? B ASP 691  OD2 
223 1 Y 1 B ARG 776  ? CG  ? B ARG 778  CG  
224 1 Y 1 B ARG 776  ? CD  ? B ARG 778  CD  
225 1 Y 1 B ARG 776  ? NE  ? B ARG 778  NE  
226 1 Y 1 B ARG 776  ? CZ  ? B ARG 778  CZ  
227 1 Y 1 B ARG 776  ? NH1 ? B ARG 778  NH1 
228 1 Y 1 B ARG 776  ? NH2 ? B ARG 778  NH2 
229 1 Y 1 B ARG 792  ? CG  ? B ARG 794  CG  
230 1 Y 1 B ARG 792  ? CD  ? B ARG 794  CD  
231 1 Y 1 B ARG 792  ? NE  ? B ARG 794  NE  
232 1 Y 1 B ARG 792  ? CZ  ? B ARG 794  CZ  
233 1 Y 1 B ARG 792  ? NH1 ? B ARG 794  NH1 
234 1 Y 1 B ARG 792  ? NH2 ? B ARG 794  NH2 
235 1 Y 1 B ARG 855  ? CG  ? B ARG 857  CG  
236 1 Y 1 B ARG 855  ? CD  ? B ARG 857  CD  
237 1 Y 1 B ARG 855  ? NE  ? B ARG 857  NE  
238 1 Y 1 B ARG 855  ? CZ  ? B ARG 857  CZ  
239 1 Y 1 B ARG 855  ? NH1 ? B ARG 857  NH1 
240 1 Y 1 B ARG 855  ? NH2 ? B ARG 857  NH2 
241 1 Y 1 B ARG 944  ? CG  ? B ARG 946  CG  
242 1 Y 1 B ARG 944  ? CD  ? B ARG 946  CD  
243 1 Y 1 B ARG 944  ? NE  ? B ARG 946  NE  
244 1 Y 1 B ARG 944  ? CZ  ? B ARG 946  CZ  
245 1 Y 1 B ARG 944  ? NH1 ? B ARG 946  NH1 
246 1 Y 1 B ARG 944  ? NH2 ? B ARG 946  NH2 
247 1 Y 1 B GLN 967  ? CG  ? B GLN 969  CG  
248 1 Y 1 B GLN 967  ? CD  ? B GLN 969  CD  
249 1 Y 1 B GLN 967  ? OE1 ? B GLN 969  OE1 
250 1 Y 1 B GLN 967  ? NE2 ? B GLN 969  NE2 
251 1 Y 1 B GLU 969  ? CG  ? B GLU 971  CG  
252 1 Y 1 B GLU 969  ? CD  ? B GLU 971  CD  
253 1 Y 1 B GLU 969  ? OE1 ? B GLU 971  OE1 
254 1 Y 1 B GLU 969  ? OE2 ? B GLU 971  OE2 
255 1 Y 1 B LYS 979  ? CG  ? B LYS 981  CG  
256 1 Y 1 B LYS 979  ? CD  ? B LYS 981  CD  
257 1 Y 1 B LYS 979  ? CE  ? B LYS 981  CE  
258 1 Y 1 B LYS 979  ? NZ  ? B LYS 981  NZ  
259 1 Y 1 B GLN 983  ? CG  ? B GLN 985  CG  
260 1 Y 1 B GLN 983  ? CD  ? B GLN 985  CD  
261 1 Y 1 B GLN 983  ? OE1 ? B GLN 985  OE1 
262 1 Y 1 B GLN 983  ? NE2 ? B GLN 985  NE2 
263 1 Y 1 B GLN 1078 ? CG  ? B GLN 1080 CG  
264 1 Y 1 B GLN 1078 ? CD  ? B GLN 1080 CD  
265 1 Y 1 B GLN 1078 ? OE1 ? B GLN 1080 OE1 
266 1 Y 1 B GLN 1078 ? NE2 ? B GLN 1080 NE2 
267 1 Y 1 B LYS 1083 ? CG  ? B LYS 1085 CG  
268 1 Y 1 B LYS 1083 ? CD  ? B LYS 1085 CD  
269 1 Y 1 B LYS 1083 ? CE  ? B LYS 1085 CE  
270 1 Y 1 B LYS 1083 ? NZ  ? B LYS 1085 NZ  
271 1 Y 1 B LYS 1097 ? CG  ? B LYS 1099 CG  
272 1 Y 1 B LYS 1097 ? CD  ? B LYS 1099 CD  
273 1 Y 1 B LYS 1097 ? CE  ? B LYS 1099 CE  
274 1 Y 1 B LYS 1097 ? NZ  ? B LYS 1099 NZ  
275 1 Y 1 B LYS 1105 ? CG  ? B LYS 1107 CG  
276 1 Y 1 B LYS 1105 ? CD  ? B LYS 1107 CD  
277 1 Y 1 B LYS 1105 ? CE  ? B LYS 1107 CE  
278 1 Y 1 B LYS 1105 ? NZ  ? B LYS 1107 NZ  
279 1 Y 1 B GLU 1168 ? CG  ? B GLU 1170 CG  
280 1 Y 1 B GLU 1168 ? CD  ? B GLU 1170 CD  
281 1 Y 1 B GLU 1168 ? OE1 ? B GLU 1170 OE1 
282 1 Y 1 B GLU 1168 ? OE2 ? B GLU 1170 OE2 
283 1 Y 1 B LYS 1221 ? CG  ? B LYS 1223 CG  
284 1 Y 1 B LYS 1221 ? CD  ? B LYS 1223 CD  
285 1 Y 1 B LYS 1221 ? CE  ? B LYS 1223 CE  
286 1 Y 1 B LYS 1221 ? NZ  ? B LYS 1223 NZ  
287 1 Y 1 B LYS 1375 ? CG  ? B LYS 1377 CG  
288 1 Y 1 B LYS 1375 ? CD  ? B LYS 1377 CD  
289 1 Y 1 B LYS 1375 ? CE  ? B LYS 1377 CE  
290 1 Y 1 B LYS 1375 ? NZ  ? B LYS 1377 NZ  
291 1 Y 1 B LYS 1377 ? CG  ? B LYS 1379 CG  
292 1 Y 1 B LYS 1377 ? CD  ? B LYS 1379 CD  
293 1 Y 1 B LYS 1377 ? CE  ? B LYS 1379 CE  
294 1 Y 1 B LYS 1377 ? NZ  ? B LYS 1379 NZ  
295 1 Y 1 B LYS 1429 ? CG  ? B LYS 1431 CG  
296 1 Y 1 B LYS 1429 ? CD  ? B LYS 1431 CD  
297 1 Y 1 B LYS 1429 ? CE  ? B LYS 1431 CE  
298 1 Y 1 B LYS 1429 ? NZ  ? B LYS 1431 NZ  
299 1 Y 1 B LYS 1442 ? CG  ? B LYS 1444 CG  
300 1 Y 1 B LYS 1442 ? CD  ? B LYS 1444 CD  
301 1 Y 1 B LYS 1442 ? CE  ? B LYS 1444 CE  
302 1 Y 1 B LYS 1442 ? NZ  ? B LYS 1444 NZ  
303 1 Y 1 B ARG 1473 ? CG  ? B ARG 1475 CG  
304 1 Y 1 B ARG 1473 ? CD  ? B ARG 1475 CD  
305 1 Y 1 B ARG 1473 ? NE  ? B ARG 1475 NE  
306 1 Y 1 B ARG 1473 ? CZ  ? B ARG 1475 CZ  
307 1 Y 1 B ARG 1473 ? NH1 ? B ARG 1475 NH1 
308 1 Y 1 B ARG 1473 ? NH2 ? B ARG 1475 NH2 
309 1 Y 1 B LYS 1496 ? CG  ? B LYS 1498 CG  
310 1 Y 1 B LYS 1496 ? CD  ? B LYS 1498 CD  
311 1 Y 1 B LYS 1496 ? CE  ? B LYS 1498 CE  
312 1 Y 1 B LYS 1496 ? NZ  ? B LYS 1498 NZ  
313 1 Y 1 B GLU 1499 ? CG  ? B GLU 1501 CG  
314 1 Y 1 B GLU 1499 ? CD  ? B GLU 1501 CD  
315 1 Y 1 B GLU 1499 ? OE1 ? B GLU 1501 OE1 
316 1 Y 1 B GLU 1499 ? OE2 ? B GLU 1501 OE2 
317 1 Y 1 B LYS 1505 ? CG  ? B LYS 1507 CG  
318 1 Y 1 B LYS 1505 ? CD  ? B LYS 1507 CD  
319 1 Y 1 B LYS 1505 ? CE  ? B LYS 1507 CE  
320 1 Y 1 B LYS 1505 ? NZ  ? B LYS 1507 NZ  
321 1 Y 1 B LYS 1526 ? CG  ? B LYS 1528 CG  
322 1 Y 1 B LYS 1526 ? CD  ? B LYS 1528 CD  
323 1 Y 1 B LYS 1526 ? CE  ? B LYS 1528 CE  
324 1 Y 1 B LYS 1526 ? NZ  ? B LYS 1528 NZ  
325 1 Y 1 B ASP 1617 ? CG  ? B ASP 1619 CG  
326 1 Y 1 B ASP 1617 ? OD1 ? B ASP 1619 OD1 
327 1 Y 1 B ASP 1617 ? OD2 ? B ASP 1619 OD2 
328 1 Y 1 B HIS 1618 ? CG  ? B HIS 1620 CG  
329 1 Y 1 B HIS 1618 ? ND1 ? B HIS 1620 ND1 
330 1 Y 1 B HIS 1618 ? CD2 ? B HIS 1620 CD2 
331 1 Y 1 B HIS 1618 ? CE1 ? B HIS 1620 CE1 
332 1 Y 1 B HIS 1618 ? NE2 ? B HIS 1620 NE2 
333 1 Y 1 B LYS 1621 ? CG  ? B LYS 1623 CG  
334 1 Y 1 B LYS 1621 ? CD  ? B LYS 1623 CD  
335 1 Y 1 B LYS 1621 ? CE  ? B LYS 1623 CE  
336 1 Y 1 B LYS 1621 ? NZ  ? B LYS 1623 NZ  
337 1 Y 1 B GLU 1628 ? CG  ? B GLU 1630 CG  
338 1 Y 1 B GLU 1628 ? CD  ? B GLU 1630 CD  
339 1 Y 1 B GLU 1628 ? OE1 ? B GLU 1630 OE1 
340 1 Y 1 B GLU 1628 ? OE2 ? B GLU 1630 OE2 
341 1 Y 1 B ARG 1633 ? CG  ? B ARG 1635 CG  
342 1 Y 1 B ARG 1633 ? CD  ? B ARG 1635 CD  
343 1 Y 1 B ARG 1633 ? NE  ? B ARG 1635 NE  
344 1 Y 1 B ARG 1633 ? CZ  ? B ARG 1635 CZ  
345 1 Y 1 B ARG 1633 ? NH1 ? B ARG 1635 NH1 
346 1 Y 1 B ARG 1633 ? NH2 ? B ARG 1635 NH2 
347 1 Y 1 B LYS 1635 ? CG  ? B LYS 1637 CG  
348 1 Y 1 B LYS 1635 ? CD  ? B LYS 1637 CD  
349 1 Y 1 B LYS 1635 ? CE  ? B LYS 1637 CE  
350 1 Y 1 B LYS 1635 ? NZ  ? B LYS 1637 NZ  
351 1 Y 1 B ILE 1637 ? CG1 ? B ILE 1639 CG1 
352 1 Y 1 B ILE 1637 ? CG2 ? B ILE 1639 CG2 
353 1 Y 1 B ILE 1637 ? CD1 ? B ILE 1639 CD1 
354 1 Y 1 B ARG 1650 ? CG  ? B ARG 1652 CG  
355 1 Y 1 B ARG 1650 ? CD  ? B ARG 1652 CD  
356 1 Y 1 B ARG 1650 ? NE  ? B ARG 1652 NE  
357 1 Y 1 B ARG 1650 ? CZ  ? B ARG 1652 CZ  
358 1 Y 1 B ARG 1650 ? NH1 ? B ARG 1652 NH1 
359 1 Y 1 B ARG 1650 ? NH2 ? B ARG 1652 NH2 
360 1 Y 1 B ASN 1651 ? CG  ? B ASN 1653 CG  
361 1 Y 1 B ASN 1651 ? OD1 ? B ASN 1653 OD1 
362 1 Y 1 B ASN 1651 ? ND2 ? B ASN 1653 ND2 
363 1 Y 1 B ASP 1652 ? CG  ? B ASP 1654 CG  
364 1 Y 1 B ASP 1652 ? OD1 ? B ASP 1654 OD1 
365 1 Y 1 B ASP 1652 ? OD2 ? B ASP 1654 OD2 
366 1 Y 1 B GLN 1653 ? CG  ? B GLN 1655 CG  
367 1 Y 1 B GLN 1653 ? CD  ? B GLN 1655 CD  
368 1 Y 1 B GLN 1653 ? OE1 ? B GLN 1655 OE1 
369 1 Y 1 B GLN 1653 ? NE2 ? B GLN 1655 NE2 
370 1 Y 1 B ASN 1654 ? CG  ? B ASN 1656 CG  
371 1 Y 1 B ASN 1654 ? OD1 ? B ASN 1656 OD1 
372 1 Y 1 B ASN 1654 ? ND2 ? B ASN 1656 ND2 
373 1 Y 1 B TYR 1658 ? CG  ? B TYR 1660 CG  
374 1 Y 1 B TYR 1658 ? CD1 ? B TYR 1660 CD1 
375 1 Y 1 B TYR 1658 ? CD2 ? B TYR 1660 CD2 
376 1 Y 1 B TYR 1658 ? CE1 ? B TYR 1660 CE1 
377 1 Y 1 B TYR 1658 ? CE2 ? B TYR 1660 CE2 
378 1 Y 1 B TYR 1658 ? CZ  ? B TYR 1660 CZ  
379 1 Y 1 B TYR 1658 ? OH  ? B TYR 1660 OH  
380 1 Y 1 B LEU 1674 ? CG  ? B LEU 1676 CG  
381 1 Y 1 B LEU 1674 ? CD1 ? B LEU 1676 CD1 
382 1 Y 1 B LEU 1674 ? CD2 ? B LEU 1676 CD2 
383 1 Y 1 B ARG 1675 ? CG  ? B ARG 1677 CG  
384 1 Y 1 B ARG 1675 ? CD  ? B ARG 1677 CD  
385 1 Y 1 B ARG 1675 ? NE  ? B ARG 1677 NE  
386 1 Y 1 B ARG 1675 ? CZ  ? B ARG 1677 CZ  
387 1 Y 1 B ARG 1675 ? NH1 ? B ARG 1677 NH1 
388 1 Y 1 B ARG 1675 ? NH2 ? B ARG 1677 NH2 
389 1 Y 1 B GLU 1676 ? CG  ? B GLU 1678 CG  
390 1 Y 1 B GLU 1676 ? CD  ? B GLU 1678 CD  
391 1 Y 1 B GLU 1676 ? OE1 ? B GLU 1678 OE1 
392 1 Y 1 B GLU 1676 ? OE2 ? B GLU 1678 OE2 
393 1 Y 1 B ARG 1679 ? CG  ? B ARG 1681 CG  
394 1 Y 1 B ARG 1679 ? CD  ? B ARG 1681 CD  
395 1 Y 1 B ARG 1679 ? NE  ? B ARG 1681 NE  
396 1 Y 1 B ARG 1679 ? CZ  ? B ARG 1681 CZ  
397 1 Y 1 B ARG 1679 ? NH1 ? B ARG 1681 NH1 
398 1 Y 1 B ARG 1679 ? NH2 ? B ARG 1681 NH2 
399 1 Y 1 B ARG 1680 ? CG  ? B ARG 1682 CG  
400 1 Y 1 B ARG 1680 ? CD  ? B ARG 1682 CD  
401 1 Y 1 B ARG 1680 ? NE  ? B ARG 1682 NE  
402 1 Y 1 B ARG 1680 ? CZ  ? B ARG 1682 CZ  
403 1 Y 1 B ARG 1680 ? NH1 ? B ARG 1682 NH1 
404 1 Y 1 B ARG 1680 ? NH2 ? B ARG 1682 NH2 
405 1 Y 1 B LEU 1682 ? CG  ? B LEU 1684 CG  
406 1 Y 1 B LEU 1682 ? CD1 ? B LEU 1684 CD1 
407 1 Y 1 B LEU 1682 ? CD2 ? B LEU 1684 CD2 
408 1 Y 1 B GLU 1684 ? CG  ? B GLU 1686 CG  
409 1 Y 1 B GLU 1684 ? CD  ? B GLU 1686 CD  
410 1 Y 1 B GLU 1684 ? OE1 ? B GLU 1686 OE1 
411 1 Y 1 B GLU 1684 ? OE2 ? B GLU 1686 OE2 
412 1 Y 1 B TYR 1685 ? CG  ? B TYR 1687 CG  
413 1 Y 1 B TYR 1685 ? CD1 ? B TYR 1687 CD1 
414 1 Y 1 B TYR 1685 ? CD2 ? B TYR 1687 CD2 
415 1 Y 1 B TYR 1685 ? CE1 ? B TYR 1687 CE1 
416 1 Y 1 B TYR 1685 ? CE2 ? B TYR 1687 CE2 
417 1 Y 1 B TYR 1685 ? CZ  ? B TYR 1687 CZ  
418 1 Y 1 B TYR 1685 ? OH  ? B TYR 1687 OH  
419 1 Y 1 B ILE 1687 ? CG1 ? B ILE 1689 CG1 
420 1 Y 1 B ILE 1687 ? CG2 ? B ILE 1689 CG2 
421 1 Y 1 B ILE 1687 ? CD1 ? B ILE 1689 CD1 
422 1 Y 1 B TYR 1723 ? CG  ? B TYR 1725 CG  
423 1 Y 1 B TYR 1723 ? CD1 ? B TYR 1725 CD1 
424 1 Y 1 B TYR 1723 ? CD2 ? B TYR 1725 CD2 
425 1 Y 1 B TYR 1723 ? CE1 ? B TYR 1725 CE1 
426 1 Y 1 B TYR 1723 ? CE2 ? B TYR 1725 CE2 
427 1 Y 1 B TYR 1723 ? CZ  ? B TYR 1725 CZ  
428 1 Y 1 B TYR 1723 ? OH  ? B TYR 1725 OH  
429 1 Y 1 B ARG 1727 ? CG  ? B ARG 1729 CG  
430 1 Y 1 B ARG 1727 ? CD  ? B ARG 1729 CD  
431 1 Y 1 B ARG 1727 ? NE  ? B ARG 1729 NE  
432 1 Y 1 B ARG 1727 ? CZ  ? B ARG 1729 CZ  
433 1 Y 1 B ARG 1727 ? NH1 ? B ARG 1729 NH1 
434 1 Y 1 B ARG 1727 ? NH2 ? B ARG 1729 NH2 
435 1 Y 1 B THR 1728 ? OG1 ? B THR 1730 OG1 
436 1 Y 1 B THR 1728 ? CG2 ? B THR 1730 CG2 
437 1 Y 1 B ARG 1746 ? CG  ? B ARG 1748 CG  
438 1 Y 1 B ARG 1746 ? CD  ? B ARG 1748 CD  
439 1 Y 1 B ARG 1746 ? NE  ? B ARG 1748 NE  
440 1 Y 1 B ARG 1746 ? CZ  ? B ARG 1748 CZ  
441 1 Y 1 B ARG 1746 ? NH1 ? B ARG 1748 NH1 
442 1 Y 1 B ARG 1746 ? NH2 ? B ARG 1748 NH2 
443 1 Y 1 B ARG 1750 ? CG  ? B ARG 1752 CG  
444 1 Y 1 B ARG 1750 ? CD  ? B ARG 1752 CD  
445 1 Y 1 B ARG 1750 ? NE  ? B ARG 1752 NE  
446 1 Y 1 B ARG 1750 ? CZ  ? B ARG 1752 CZ  
447 1 Y 1 B ARG 1750 ? NH1 ? B ARG 1752 NH1 
448 1 Y 1 B ARG 1750 ? NH2 ? B ARG 1752 NH2 
449 1 Y 1 B GLU 1789 ? CG  ? B GLU 1791 CG  
450 1 Y 1 B GLU 1789 ? CD  ? B GLU 1791 CD  
451 1 Y 1 B GLU 1789 ? OE1 ? B GLU 1791 OE1 
452 1 Y 1 B GLU 1789 ? OE2 ? B GLU 1791 OE2 
453 1 Y 1 B GLN 1790 ? CG  ? B GLN 1792 CG  
454 1 Y 1 B GLN 1790 ? CD  ? B GLN 1792 CD  
455 1 Y 1 B GLN 1790 ? OE1 ? B GLN 1792 OE1 
456 1 Y 1 B GLN 1790 ? NE2 ? B GLN 1792 NE2 
457 1 Y 1 B GLU 1798 ? CG  ? B GLU 1800 CG  
458 1 Y 1 B GLU 1798 ? CD  ? B GLU 1800 CD  
459 1 Y 1 B GLU 1798 ? OE1 ? B GLU 1800 OE1 
460 1 Y 1 B GLU 1798 ? OE2 ? B GLU 1800 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           3 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21.1_5286 4 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot     ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BE4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     184.406 
_cell.length_a_esd                 ? 
_cell.length_b                     426.580 
_cell.length_b_esd                 ? 
_cell.length_c                     77.298 
_cell.length_c_esd                 ? 
_cell.volume                       6080563.030 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9BE4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_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                   9BE4 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.69 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          66.68 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;1.0M sodium tartrate pH 7.0.
10mM Manganese Chloride
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-12-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.954 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'CLSI BEAMLINE 08ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.954 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08ID-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          62.04 
_reflns.entry_id                                       9BE4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.00 
_reflns.d_resolution_low                               50.00 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     123053 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.988 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.268 
_reflns.pdbx_Rpim_I_all                                0.084 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.985 
_reflns.pdbx_CC_star                                   0.996 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.00 
_reflns_shell.d_res_low                                     3.05 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5930 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               7.4 
_reflns_shell.pdbx_chi_squared                              0.959 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.558 
_reflns_shell.pdbx_Rpim_I_all                               0.551 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.348 
_reflns_shell.pdbx_CC_star                                  0.719 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.1 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               61.40 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BE4 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.00 
_refine.ls_d_res_low                             49.87 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     120084 
_refine.ls_number_reflns_R_free                  2624 
_refine.ls_number_reflns_R_work                  117460 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.56 
_refine.ls_percent_reflns_R_free                 2.19 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2189 
_refine.ls_R_factor_R_free                       0.2575 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2180 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.2167 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.4010 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.00 
_refine_hist.d_res_low                        49.87 
_refine_hist.number_atoms_solvent             350 
_refine_hist.number_atoms_total               28153 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        27708 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         95 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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 
'X-RAY DIFFRACTION' ? 0.0028  ? 28406 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5584  ? 38607 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0430  ? 4358  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0051  ? 5018  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.6081 ? 10475 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.00 3.05  . . 99  4704 74.95 . . . . 0.3559 . . . . . . . . . . . 0.3802 
'X-RAY DIFFRACTION' 3.05 3.10  . . 132 5970 94.02 . . . . 0.3393 . . . . . . . . . . . 0.3747 
'X-RAY DIFFRACTION' 3.10 3.17  . . 141 5958 94.73 . . . . 0.3050 . . . . . . . . . . . 0.3324 
'X-RAY DIFFRACTION' 3.17 3.24  . . 137 6117 96.16 . . . . 0.2937 . . . . . . . . . . . 0.3425 
'X-RAY DIFFRACTION' 3.24 3.31  . . 138 6074 96.84 . . . . 0.2782 . . . . . . . . . . . 0.3354 
'X-RAY DIFFRACTION' 3.31 3.39  . . 136 6231 97.41 . . . . 0.2754 . . . . . . . . . . . 0.3460 
'X-RAY DIFFRACTION' 3.39 3.49  . . 138 6173 97.56 . . . . 0.2640 . . . . . . . . . . . 0.3354 
'X-RAY DIFFRACTION' 3.49 3.59  . . 141 6188 98.12 . . . . 0.2604 . . . . . . . . . . . 0.2961 
'X-RAY DIFFRACTION' 3.59 3.70  . . 140 6312 98.70 . . . . 0.2385 . . . . . . . . . . . 0.3355 
'X-RAY DIFFRACTION' 3.70 3.84  . . 136 6261 98.42 . . . . 0.2205 . . . . . . . . . . . 0.2685 
'X-RAY DIFFRACTION' 3.84 3.99  . . 141 6258 98.78 . . . . 0.2085 . . . . . . . . . . . 0.2396 
'X-RAY DIFFRACTION' 3.99 4.17  . . 144 6324 99.16 . . . . 0.1913 . . . . . . . . . . . 0.2466 
'X-RAY DIFFRACTION' 4.17 4.39  . . 141 6318 98.82 . . . . 0.1897 . . . . . . . . . . . 0.2217 
'X-RAY DIFFRACTION' 4.39 4.67  . . 140 6349 99.27 . . . . 0.1742 . . . . . . . . . . . 0.1970 
'X-RAY DIFFRACTION' 4.67 5.03  . . 143 6377 99.15 . . . . 0.1731 . . . . . . . . . . . 0.2205 
'X-RAY DIFFRACTION' 5.03 5.53  . . 146 6416 98.81 . . . . 0.1929 . . . . . . . . . . . 0.2209 
'X-RAY DIFFRACTION' 5.53 6.33  . . 140 6375 98.64 . . . . 0.2138 . . . . . . . . . . . 0.2565 
'X-RAY DIFFRACTION' 6.33 7.97  . . 143 6483 98.63 . . . . 0.2067 . . . . . . . . . . . 0.2415 
'X-RAY DIFFRACTION' 7.97 49.87 . . 148 6572 96.03 . . . . 0.1807 . . . . . . . . . . . 0.1891 
# 
_struct.entry_id                     9BE4 
_struct.title                        'The post-condensation state of the dimodular NRPS protein LgrA' 
_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        9BE4 
_struct_keywords.text            
'Nornribosomal peptide synthetase, Condensation, Peptide bond, Linear gramicidin, BIOSYNTHETIC PROTEIN' 
_struct_keywords.pdbx_keywords   'BIOSYNTHETIC PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 2 ? 
G N N 4 ? 
H N N 5 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    LGRA_BREPA 
_struct_ref.pdbx_db_accession          Q70LM7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ILFLTTFMSKGNKVVRYLESLHHEVVICQEKVHAQSANLQEIDWIVSYAYGYILDKEIVSRFRGRIINLHPSLLPWNKGR
DPVFWSVWDETPKGVTIHLIDEHVDTGDILVQEEIAFADEDTLLDCYNKANQAIEELFIREWENIVHGRIAPYRQTAGGT
LHFKADRDFYKNLNMTTVRELLALKRLCAEPKRGEKPIDKTFHQLFEQQVEMTPDHVAVVDRGQSLTYKQLNERANQLAH
HLRGKGVKPDDQVAIMLDKSLDMIVSILAVMKAGGAYVPIDPDYPGERIAYMLADSSAAILLTNALHEEKANGACDIIDV
HDPDSYSENTNNLPHVNRPDDLVYVMYTSGSTGLAKGVMIEHHNLVNFCEWYRPYFGVTPADKALVYSSFSFDGSALDIF
THLLAGAALHIVPSERKYDLDALNDYCNQEGITISYLPTGAAEQFMQMDNQSFRVVITGGDVLKKIERNGTYKLYNGYGP
TECTIMVTMFEVDKPYANIPIGKPIDRTRILILDEALALQPIGVAGELFIVGEGLGRGYLNRPELTAEKFIVHPQTGERM
YRTGDRARFLPDGNIEFLGRLDNLVKIRGYRIEPGEIEPFLMNHPLIELTTVLAKEQADGRKYLVGYYVAPEEIPHGELR
EWLGNDLPDYMIPTYFVHMKAFPLTANGKVDRRALPDVQADAELLGEDYVAPTDELEQQLAQVWSHVLGIPQMGIDDHFL
ERGGDSIKVMQLIHQLKNIGLSLRYDQLFTHPTIRQLKRLLTEQKQVSLEPLRELDEQAEYETSAVEKRMYIIQQQDVES
IAYNVVYTINFPLTVDTEQIRVALEQLVLRHEGLRSTYHMRGDEIVKRIVPRAELSFVRQTGEEESVQSLLAEQIKPFDL
AKAPLLRAGVIETADKKVLWFDSHHILLDGLSKSILARELQALLGQQVLSPVEKTYKSFARWQNEWFASDEYEQQIAYWK
TLLQGELPAVQLPTKKRPPQLTFDGAIQMYRVNPEITRKLKATAAKHDLTLYMLMLTIVSIWLSKMNSDSNQVILGTVTD
GRQHPDTRELLGMFVNTLPLLLSIDHEESFLHNLQQVKAKLLPALQNQYVPFDKILEAARVKREGNRHPLFDVMFMMQGA
PETELESNMHHINAGISKFDLTLEVLERENGLNIVFEYNTHLFDEGMILRMVAQFEHLLLQAVHGLDQQVKRFELVTEDE
KRDLFLRVNDTAKAYPNKLIMSMLEDWAAATPDKTALVFREQRVTYRELNERVNQLAHTLREKGVQPDDLVMLMAERSVE
MMVAIFAVLKAGGAYLPIDPHSPAERIAYIFADSGAKLVLAQSPFVEKASMAEVVLDLNSASSYAADTSNPPLVNQPGDL
VYVMYTSGSTGKPKGVMIEHGALLNVLHGMQDEYPLLQDDAFLLKTTYIFDISVAEIFGWVPGRGKLVILEPEAEKNPKA
IWQAVVGAGITHINFVPSMLIPFVEYLEGRTEANRLRYILACGEAMPDELVPKVYEVLPEVKLENIYGPTEATIYASRYS
LAKGSQESPVPIGKPLPNYRMYIINRHGQLQPIGVPGELCIAGASLARGYLNNPALTEEKFTPHPLEKGERIYRTGDLAR
YREDGNIEYLGRMDHQVKIRGYRIELDEIRSKLIQEETIQDAVVVARNDQNGQAYLCAYLLSEQEWTVGQLRELLRRELP
EYMIPAHFVLLKQFPLTANGKLDRKALPEPDGSVKAEAEYAAPRTELEATLAHIWGEVLGIERIGIRDNFFELGGDSIKG
LQIASRLQRINWTMVINHLFLYPTIEQIAPFVTSEQVVIE
;
_struct_ref.pdbx_align_begin           3 
# 
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 9BE4 A 4 ? 1805 ? Q70LM7 3 ? 1802 ? 4 1803 
2 1 9BE4 B 4 ? 1805 ? Q70LM7 3 ? 1802 ? 4 1803 
# 
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 
1 9BE4 MET A 1    ? UNP Q70LM7 ?   ?   'initiating methionine' 1    1  
1 9BE4 GLY A 2    ? UNP Q70LM7 ?   ?   'expression tag'        2    2  
1 9BE4 ARG A 3    ? UNP Q70LM7 ?   ?   'expression tag'        3    3  
1 9BE4 ASN A 771  A UNP Q70LM7 ?   ?   insertion               770  4  
1 9BE4 GLY A 772  B UNP Q70LM7 ?   ?   insertion               770  5  
1 9BE4 LEU A 773  ? UNP Q70LM7 SER 770 conflict                771  6  
1 9BE4 ALA A 1806 ? UNP Q70LM7 ?   ?   'expression tag'        1804 7  
1 9BE4 ALA A 1807 ? UNP Q70LM7 ?   ?   'expression tag'        1805 8  
1 9BE4 ALA A 1808 ? UNP Q70LM7 ?   ?   'expression tag'        1806 9  
1 9BE4 GLU A 1809 ? UNP Q70LM7 ?   ?   'expression tag'        1807 10 
1 9BE4 ASN A 1810 ? UNP Q70LM7 ?   ?   'expression tag'        1808 11 
1 9BE4 LEU A 1811 ? UNP Q70LM7 ?   ?   'expression tag'        1809 12 
1 9BE4 TYR A 1812 ? UNP Q70LM7 ?   ?   'expression tag'        1810 13 
1 9BE4 PHE A 1813 ? UNP Q70LM7 ?   ?   'expression tag'        1811 14 
1 9BE4 GLN A 1814 ? UNP Q70LM7 ?   ?   'expression tag'        1812 15 
2 9BE4 MET B 1    ? UNP Q70LM7 ?   ?   'initiating methionine' 1    16 
2 9BE4 GLY B 2    ? UNP Q70LM7 ?   ?   'expression tag'        2    17 
2 9BE4 ARG B 3    ? UNP Q70LM7 ?   ?   'expression tag'        3    18 
2 9BE4 ASN B 771  A UNP Q70LM7 ?   ?   insertion               770  19 
2 9BE4 GLY B 772  B UNP Q70LM7 ?   ?   insertion               770  20 
2 9BE4 LEU B 773  ? UNP Q70LM7 SER 770 conflict                771  21 
2 9BE4 ALA B 1806 ? UNP Q70LM7 ?   ?   'expression tag'        1804 22 
2 9BE4 ALA B 1807 ? UNP Q70LM7 ?   ?   'expression tag'        1805 23 
2 9BE4 ALA B 1808 ? UNP Q70LM7 ?   ?   'expression tag'        1806 24 
2 9BE4 GLU B 1809 ? UNP Q70LM7 ?   ?   'expression tag'        1807 25 
2 9BE4 ASN B 1810 ? UNP Q70LM7 ?   ?   'expression tag'        1808 26 
2 9BE4 LEU B 1811 ? UNP Q70LM7 ?   ?   'expression tag'        1809 27 
2 9BE4 TYR B 1812 ? UNP Q70LM7 ?   ?   'expression tag'        1810 28 
2 9BE4 PHE B 1813 ? UNP Q70LM7 ?   ?   'expression tag'        1811 29 
2 9BE4 GLN B 1814 ? UNP Q70LM7 ?   ?   'expression tag'        1812 30 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,H 
2 1 B,F,G,I   
# 
_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]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 ASN A 15   ? LEU A 24   ? ASN A 15   LEU A 24   1 ? 10 
HELX_P HELX_P2   AA2 SER A 39   ? GLN A 43   ? SER A 39   GLN A 43   5 ? 5  
HELX_P HELX_P3   AA3 ASP A 58   ? PHE A 65   ? ASP A 58   PHE A 65   1 ? 8  
HELX_P HELX_P4   AA4 ASP A 84   ? ASP A 92   ? ASP A 84   ASP A 92   1 ? 9  
HELX_P HELX_P5   AA5 THR A 125  ? HIS A 150  ? THR A 125  HIS A 150  1 ? 26 
HELX_P HELX_P6   AA6 PHE A 166  ? ASP A 171  ? PHE A 166  ASP A 171  5 ? 6  
HELX_P HELX_P7   AA7 THR A 180  ? ALA A 192  ? THR A 180  ALA A 192  1 ? 13 
HELX_P HELX_P8   AA8 THR A 204  ? THR A 216  ? THR A 204  THR A 216  1 ? 13 
HELX_P HELX_P9   AA9 TYR A 231  ? GLY A 249  ? TYR A 231  GLY A 249  1 ? 19 
HELX_P HELX_P10  AB1 SER A 263  ? GLY A 277  ? SER A 263  GLY A 277  1 ? 15 
HELX_P HELX_P11  AB2 PRO A 288  ? SER A 300  ? PRO A 288  SER A 300  1 ? 13 
HELX_P HELX_P12  AB3 HIS A 310  ? ALA A 314  ? HIS A 310  ALA A 314  5 ? 5  
HELX_P HELX_P13  AB4 ASP A 325  ? TYR A 329  ? ASP A 325  TYR A 329  5 ? 5  
HELX_P HELX_P14  AB5 HIS A 365  ? GLY A 380  ? HIS A 365  GLY A 380  1 ? 16 
HELX_P HELX_P15  AB6 PHE A 395  ? LEU A 407  ? PHE A 395  LEU A 407  1 ? 13 
HELX_P HELX_P16  AB7 ASP A 422  ? GLY A 434  ? ASP A 422  GLY A 434  1 ? 13 
HELX_P HELX_P17  AB8 PRO A 441  ? MET A 449  ? PRO A 441  MET A 449  1 ? 9  
HELX_P HELX_P18  AB9 PRO A 483  ? THR A 487  ? PRO A 483  THR A 487  5 ? 5  
HELX_P HELX_P19  AC1 ARG A 545  ? LYS A 552  ? ARG A 545  LYS A 552  1 ? 8  
HELX_P HELX_P20  AC2 GLU A 596  ? GLU A 599  ? GLU A 596  GLU A 599  5 ? 4  
HELX_P HELX_P21  AC3 ILE A 600  ? ASN A 606  ? ILE A 600  ASN A 606  1 ? 7  
HELX_P HELX_P22  AC4 PRO A 638  ? ASN A 648  ? PRO A 638  ASN A 648  1 ? 11 
HELX_P HELX_P23  AC5 PRO A 651  ? ILE A 655  ? PRO A 651  ILE A 655  5 ? 5  
HELX_P HELX_P24  AC6 ASP A 697  ? GLY A 712  ? ASP A 697  GLY A 712  1 ? 16 
HELX_P HELX_P25  AC7 PHE A 722  ? GLY A 726  ? PHE A 722  GLY A 726  5 ? 5  
HELX_P HELX_P26  AC8 ASP A 728  ? GLY A 743  ? ASP A 728  GLY A 743  1 ? 16 
HELX_P HELX_P27  AC9 ARG A 747  ? HIS A 754  ? ARG A 747  HIS A 754  1 ? 8  
HELX_P HELX_P28  AD1 THR A 756  ? THR A 765  ? THR A 756  THR A 765  1 ? 10 
HELX_P HELX_P29  AD2 SER A 789  ? ASP A 802  ? SER A 787  ASP A 800  1 ? 14 
HELX_P HELX_P30  AD3 ASP A 821  ? HIS A 836  ? ASP A 819  HIS A 834  1 ? 16 
HELX_P HELX_P31  AD4 GLU A 837  ? LEU A 839  ? GLU A 835  LEU A 837  5 ? 3  
HELX_P HELX_P32  AD5 SER A 871  ? GLU A 878  ? SER A 869  GLU A 876  1 ? 8  
HELX_P HELX_P33  AD6 ASP A 914  ? GLY A 930  ? ASP A 912  GLY A 928  1 ? 17 
HELX_P HELX_P34  AD7 THR A 940  ? PHE A 952  ? THR A 938  PHE A 950  1 ? 13 
HELX_P HELX_P35  AD8 SER A 954  ? THR A 966  ? SER A 952  THR A 964  1 ? 13 
HELX_P HELX_P36  AD9 ASN A 998  ? HIS A 1012 ? ASN A 996  HIS A 1010 1 ? 15 
HELX_P HELX_P37  AE1 THR A 1015 ? ASN A 1032 ? THR A 1013 ASN A 1030 1 ? 18 
HELX_P HELX_P38  AE2 HIS A 1049 ? ARG A 1053 ? HIS A 1047 ARG A 1051 5 ? 5  
HELX_P HELX_P39  AE3 SER A 1074 ? ASN A 1092 ? SER A 1072 ASN A 1090 1 ? 19 
HELX_P HELX_P40  AE4 PRO A 1096 ? ARG A 1105 ? PRO A 1094 ARG A 1103 1 ? 10 
HELX_P HELX_P41  AE5 THR A 1128 ? ASN A 1133 ? THR A 1126 ASN A 1131 1 ? 6  
HELX_P HELX_P42  AE6 ASP A 1169 ? HIS A 1189 ? ASP A 1167 HIS A 1187 1 ? 21 
HELX_P HELX_P43  AE7 GLN A 1194 ? PHE A 1198 ? GLN A 1192 PHE A 1196 5 ? 5  
HELX_P HELX_P44  AE8 THR A 1202 ? VAL A 1213 ? THR A 1200 VAL A 1211 1 ? 12 
HELX_P HELX_P45  AE9 LEU A 1224 ? THR A 1236 ? LEU A 1222 THR A 1234 1 ? 13 
HELX_P HELX_P46  AF1 TYR A 1251 ? GLU A 1267 ? TYR A 1249 GLU A 1265 1 ? 17 
HELX_P HELX_P47  AF2 SER A 1283 ? GLY A 1297 ? SER A 1281 GLY A 1295 1 ? 15 
HELX_P HELX_P48  AF3 PRO A 1308 ? GLY A 1320 ? PRO A 1306 GLY A 1318 1 ? 13 
HELX_P HELX_P49  AF4 SER A 1328 ? VAL A 1331 ? SER A 1326 VAL A 1329 5 ? 4  
HELX_P HELX_P50  AF5 GLU A 1332 ? MET A 1336 ? GLU A 1330 MET A 1334 5 ? 5  
HELX_P HELX_P51  AF6 SER A 1345 ? TYR A 1349 ? SER A 1343 TYR A 1347 5 ? 5  
HELX_P HELX_P52  AF7 HIS A 1385 ? TYR A 1399 ? HIS A 1383 TYR A 1397 1 ? 15 
HELX_P HELX_P53  AF8 PHE A 1415 ? PHE A 1423 ? PHE A 1413 PHE A 1421 1 ? 9  
HELX_P HELX_P54  AF9 GLU A 1438 ? LYS A 1441 ? GLU A 1436 LYS A 1439 5 ? 4  
HELX_P HELX_P55  AG1 ASN A 1442 ? GLY A 1454 ? ASN A 1440 GLY A 1452 1 ? 13 
HELX_P HELX_P56  AG2 VAL A 1461 ? GLU A 1470 ? VAL A 1459 GLU A 1468 1 ? 10 
HELX_P HELX_P57  AG3 GLU A 1494 ? LEU A 1503 ? GLU A 1492 LEU A 1501 1 ? 10 
HELX_P HELX_P58  AG4 PRO A 1514 ? THR A 1518 ? PRO A 1512 THR A 1516 5 ? 5  
HELX_P HELX_P59  AG5 ASN A 1578 ? LYS A 1585 ? ASN A 1576 LYS A 1583 1 ? 8  
HELX_P HELX_P60  AG6 PRO A 1590 ? LYS A 1593 ? PRO A 1588 LYS A 1591 5 ? 4  
HELX_P HELX_P61  AG7 ASP A 1619 ? GLN A 1621 ? ASP A 1617 GLN A 1619 5 ? 3  
HELX_P HELX_P62  AG8 GLU A 1630 ? GLN A 1640 ? GLU A 1628 GLN A 1638 1 ? 11 
HELX_P HELX_P63  AG9 GLY A 1674 ? LEU A 1680 ? GLY A 1672 LEU A 1678 1 ? 7  
HELX_P HELX_P64  AH1 PRO A 1685 ? ILE A 1689 ? PRO A 1683 ILE A 1687 5 ? 5  
HELX_P HELX_P65  AH2 THR A 1730 ? GLY A 1745 ? THR A 1728 GLY A 1743 1 ? 16 
HELX_P HELX_P66  AH3 ASP A 1761 ? ILE A 1775 ? ASP A 1759 ILE A 1773 1 ? 15 
HELX_P HELX_P67  AH4 VAL A 1780 ? TYR A 1787 ? VAL A 1778 TYR A 1785 1 ? 8  
HELX_P HELX_P68  AH5 THR A 1789 ? VAL A 1797 ? THR A 1787 VAL A 1795 1 ? 9  
HELX_P HELX_P69  AH6 ASN B 15   ? LEU B 24   ? ASN B 15   LEU B 24   1 ? 10 
HELX_P HELX_P70  AH7 SER B 39   ? GLN B 43   ? SER B 39   GLN B 43   5 ? 5  
HELX_P HELX_P71  AH8 ASP B 58   ? PHE B 65   ? ASP B 58   PHE B 65   1 ? 8  
HELX_P HELX_P72  AH9 ASP B 84   ? ASP B 92   ? ASP B 84   ASP B 92   1 ? 9  
HELX_P HELX_P73  AI1 THR B 125  ? HIS B 150  ? THR B 125  HIS B 150  1 ? 26 
HELX_P HELX_P74  AI2 ARG B 170  ? ASN B 177  ? ARG B 170  ASN B 177  5 ? 8  
HELX_P HELX_P75  AI3 THR B 180  ? LEU B 190  ? THR B 180  LEU B 190  1 ? 11 
HELX_P HELX_P76  AI4 THR B 204  ? THR B 216  ? THR B 204  THR B 216  1 ? 13 
HELX_P HELX_P77  AI5 TYR B 231  ? LYS B 248  ? TYR B 231  LYS B 248  1 ? 18 
HELX_P HELX_P78  AI6 SER B 263  ? GLY B 277  ? SER B 263  GLY B 277  1 ? 15 
HELX_P HELX_P79  AI7 PRO B 288  ? SER B 299  ? PRO B 288  SER B 299  1 ? 12 
HELX_P HELX_P80  AI8 HIS B 310  ? ASN B 315  ? HIS B 310  ASN B 315  5 ? 6  
HELX_P HELX_P81  AI9 ASP B 325  ? TYR B 329  ? ASP B 325  TYR B 329  5 ? 5  
HELX_P HELX_P82  AJ1 HIS B 365  ? GLY B 380  ? HIS B 365  GLY B 380  1 ? 16 
HELX_P HELX_P83  AJ2 PHE B 395  ? LEU B 407  ? PHE B 395  LEU B 407  1 ? 13 
HELX_P HELX_P84  AJ3 ASP B 422  ? GLY B 434  ? ASP B 422  GLY B 434  1 ? 13 
HELX_P HELX_P85  AJ4 THR B 442  ? MET B 449  ? THR B 442  MET B 449  1 ? 8  
HELX_P HELX_P86  AJ5 PRO B 483  ? THR B 487  ? PRO B 483  THR B 487  5 ? 5  
HELX_P HELX_P87  AJ6 ARG B 545  ? LYS B 552  ? ARG B 545  LYS B 552  1 ? 8  
HELX_P HELX_P88  AJ7 GLU B 596  ? GLU B 599  ? GLU B 596  GLU B 599  5 ? 4  
HELX_P HELX_P89  AJ8 ILE B 600  ? ASN B 606  ? ILE B 600  ASN B 606  1 ? 7  
HELX_P HELX_P90  AJ9 PRO B 638  ? GLY B 647  ? PRO B 638  GLY B 647  1 ? 10 
HELX_P HELX_P91  AK1 ASP B 674  ? LEU B 678  ? ASP B 674  LEU B 678  5 ? 5  
HELX_P HELX_P92  AK2 ASP B 697  ? GLY B 712  ? ASP B 697  GLY B 712  1 ? 16 
HELX_P HELX_P93  AK3 PHE B 722  ? GLY B 726  ? PHE B 722  GLY B 726  5 ? 5  
HELX_P HELX_P94  AK4 4HH B 729  ? ASN B 741  ? 4HH B 729  ASN B 741  1 ? 13 
HELX_P HELX_P95  AK5 ARG B 747  ? HIS B 754  ? ARG B 747  HIS B 754  1 ? 8  
HELX_P HELX_P96  AK6 THR B 756  ? GLN B 767  ? THR B 756  GLN B 767  1 ? 12 
HELX_P HELX_P97  AK7 SER B 789  ? ASP B 802  ? SER B 787  ASP B 800  1 ? 14 
HELX_P HELX_P98  AK8 ASP B 821  ? HIS B 836  ? ASP B 819  HIS B 834  1 ? 16 
HELX_P HELX_P99  AK9 GLU B 837  ? LEU B 839  ? GLU B 835  LEU B 837  5 ? 3  
HELX_P HELX_P100 AL1 SER B 871  ? GLU B 878  ? SER B 869  GLU B 876  1 ? 8  
HELX_P HELX_P101 AL2 ASP B 914  ? GLY B 930  ? ASP B 912  GLY B 928  1 ? 17 
HELX_P HELX_P102 AL3 THR B 940  ? PHE B 952  ? THR B 938  PHE B 950  1 ? 13 
HELX_P HELX_P103 AL4 ASP B 955  ? THR B 966  ? ASP B 953  THR B 964  1 ? 12 
HELX_P HELX_P104 AL5 ASN B 998  ? HIS B 1012 ? ASN B 996  HIS B 1010 1 ? 15 
HELX_P HELX_P105 AL6 THR B 1015 ? ASN B 1032 ? THR B 1013 ASN B 1030 1 ? 18 
HELX_P HELX_P106 AL7 HIS B 1049 ? ARG B 1053 ? HIS B 1047 ARG B 1051 5 ? 5  
HELX_P HELX_P107 AL8 SER B 1074 ? ASN B 1092 ? SER B 1072 ASN B 1090 1 ? 19 
HELX_P HELX_P108 AL9 PRO B 1096 ? ARG B 1105 ? PRO B 1094 ARG B 1103 1 ? 10 
HELX_P HELX_P109 AM1 THR B 1128 ? ASN B 1133 ? THR B 1126 ASN B 1131 1 ? 6  
HELX_P HELX_P110 AM2 ASP B 1169 ? GLY B 1190 ? ASP B 1167 GLY B 1188 1 ? 22 
HELX_P HELX_P111 AM3 GLN B 1194 ? PHE B 1198 ? GLN B 1192 PHE B 1196 5 ? 5  
HELX_P HELX_P112 AM4 THR B 1202 ? VAL B 1213 ? THR B 1200 VAL B 1211 1 ? 12 
HELX_P HELX_P113 AM5 LEU B 1224 ? THR B 1236 ? LEU B 1222 THR B 1234 1 ? 13 
HELX_P HELX_P114 AM6 TYR B 1251 ? LYS B 1268 ? TYR B 1249 LYS B 1266 1 ? 18 
HELX_P HELX_P115 AM7 SER B 1283 ? GLY B 1297 ? SER B 1281 GLY B 1295 1 ? 15 
HELX_P HELX_P116 AM8 PRO B 1308 ? GLY B 1320 ? PRO B 1306 GLY B 1318 1 ? 13 
HELX_P HELX_P117 AM9 SER B 1328 ? VAL B 1331 ? SER B 1326 VAL B 1329 5 ? 4  
HELX_P HELX_P118 AN1 GLU B 1332 ? ALA B 1337 ? GLU B 1330 ALA B 1335 5 ? 6  
HELX_P HELX_P119 AN2 SER B 1345 ? TYR B 1349 ? SER B 1343 TYR B 1347 5 ? 5  
HELX_P HELX_P120 AN3 HIS B 1385 ? TYR B 1399 ? HIS B 1383 TYR B 1397 1 ? 15 
HELX_P HELX_P121 AN4 ASP B 1416 ? PHE B 1423 ? ASP B 1414 PHE B 1421 1 ? 8  
HELX_P HELX_P122 AN5 GLU B 1438 ? LYS B 1441 ? GLU B 1436 LYS B 1439 5 ? 4  
HELX_P HELX_P123 AN6 ASN B 1442 ? GLY B 1454 ? ASN B 1440 GLY B 1452 1 ? 13 
HELX_P HELX_P124 AN7 VAL B 1461 ? GLU B 1470 ? VAL B 1459 GLU B 1468 1 ? 10 
HELX_P HELX_P125 AN8 GLU B 1494 ? LEU B 1503 ? GLU B 1492 LEU B 1501 1 ? 10 
HELX_P HELX_P126 AN9 PRO B 1514 ? THR B 1518 ? PRO B 1512 THR B 1516 5 ? 5  
HELX_P HELX_P127 AO1 ASN B 1578 ? LYS B 1585 ? ASN B 1576 LYS B 1583 1 ? 8  
HELX_P HELX_P128 AO2 PRO B 1590 ? LYS B 1593 ? PRO B 1588 LYS B 1591 5 ? 4  
HELX_P HELX_P129 AO3 ASP B 1619 ? GLN B 1621 ? ASP B 1617 GLN B 1619 5 ? 3  
HELX_P HELX_P130 AO4 GLU B 1630 ? ARG B 1635 ? GLU B 1628 ARG B 1633 1 ? 6  
HELX_P HELX_P131 AO5 GLN B 1675 ? ARG B 1682 ? GLN B 1673 ARG B 1680 1 ? 8  
HELX_P HELX_P132 AO6 THR B 1730 ? GLY B 1745 ? THR B 1728 GLY B 1743 1 ? 16 
HELX_P HELX_P133 AO7 PHE B 1755 ? GLY B 1759 ? PHE B 1753 GLY B 1757 5 ? 5  
HELX_P HELX_P134 AO8 ASP B 1761 ? ARG B 1774 ? ASP B 1759 ARG B 1772 1 ? 14 
HELX_P HELX_P135 AO9 VAL B 1780 ? TYR B 1787 ? VAL B 1778 TYR B 1785 1 ? 8  
HELX_P HELX_P136 AP1 THR B 1789 ? VAL B 1797 ? THR B 1787 VAL B 1795 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A ASP 728  C   ? ? ? 1_555 A 4HH   729 N   ? ? A ASP 728  A 4HH   729  1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale2 covale both ? A 4HH 729  C   ? ? ? 1_555 A ILE   730 N   ? ? A 4HH 729  A ILE   730  1_555 ? ? ? ? ? ? ? 1.336 ? ? 
covale3 covale one  ? A SER 1762 OG  ? ? ? 1_555 E A1AMN .   P18 ? ? A SER 1760 A A1AMN 1904 1_555 ? ? ? ? ? ? ? 1.652 ? ? 
covale4 covale both ? B ASP 728  C   ? ? ? 1_555 B 4HH   729 N   ? ? B ASP 728  B 4HH   729  1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale5 covale both ? B 4HH 729  C   ? ? ? 1_555 B ILE   730 N   ? ? B 4HH 729  B ILE   730  1_555 ? ? ? ? ? ? ? 1.334 ? ? 
metalc1 metalc ?    ? B GLU 364  OE1 ? ? ? 1_555 G MN    .   MN  ? ? B GLU 364  B MN    1903 1_555 ? ? ? ? ? ? ? 2.131 ? ? 
metalc2 metalc ?    ? B HIS 366  NE2 ? ? ? 1_555 G MN    .   MN  ? ? B HIS 366  B MN    1903 1_555 ? ? ? ? ? ? ? 2.600 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   OE1 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   B 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   GLU 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    364 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    GLU 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     364 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   MN 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   G 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   MN 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    MN 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     1903 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   NE2 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   B 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   HIS 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    366 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    HIS 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     366 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 68.9 
_pdbx_struct_conn_angle.value_esd             ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 4HH   A 729 ? .   . .    . 4HH   A 729  ? 1_555 .   . .    . .     .   .  SER 1 4HH   4-Phosphopantetheine 
'Named protein modification'     
2 4HH   B 729 ? .   . .    . 4HH   B 729  ? 1_555 .   . .    . .     .   .  SER 1 4HH   4-Phosphopantetheine 
'Named protein modification'     
3 A1AMN E .   ? SER A 1762 ? A1AMN A 1904 ? 1_555 SER A 1760 ? 1_555 P18 OG SER 1 A1AMN None                 
'Covalent chemical modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 77  A . ? LEU 77  A PRO 78  A ? PRO 78  A 1 13.01 
2 ALA 888 A . ? ALA 886 A PRO 889 A ? PRO 887 A 1 10.65 
3 LEU 77  B . ? LEU 77  B PRO 78  B ? PRO 78  B 1 12.51 
4 ALA 888 B . ? ALA 886 B PRO 889 B ? PRO 887 B 1 -0.05 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 3 ? 
AA6 ? 5 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 2 ? 
AB1 ? 3 ? 
AB2 ? 3 ? 
AB3 ? 5 ? 
AB4 ? 4 ? 
AB5 ? 2 ? 
AB6 ? 4 ? 
AB7 ? 4 ? 
AB8 ? 3 ? 
AB9 ? 5 ? 
AC1 ? 4 ? 
AC2 ? 4 ? 
AC3 ? 2 ? 
AC4 ? 2 ? 
AC5 ? 2 ? 
AC6 ? 6 ? 
AC7 ? 2 ? 
AC8 ? 4 ? 
AC9 ? 4 ? 
AD1 ? 3 ? 
AD2 ? 5 ? 
AD3 ? 4 ? 
AD4 ? 4 ? 
AD5 ? 2 ? 
AD6 ? 3 ? 
AD7 ? 3 ? 
AD8 ? 5 ? 
AD9 ? 4 ? 
AE1 ? 2 ? 
AE2 ? 4 ? 
AE3 ? 4 ? 
AE4 ? 3 ? 
AE5 ? 5 ? 
AE6 ? 4 ? 
AE7 ? 4 ? 
AE8 ? 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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? parallel      
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB3 1 2 ? parallel      
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? parallel      
AB5 1 2 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB7 1 2 ? parallel      
AB7 2 3 ? parallel      
AB7 3 4 ? parallel      
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? parallel      
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC6 1 2 ? parallel      
AC6 2 3 ? parallel      
AC6 3 4 ? parallel      
AC6 4 5 ? anti-parallel 
AC6 5 6 ? anti-parallel 
AC7 1 2 ? parallel      
AC8 1 2 ? anti-parallel 
AC8 2 3 ? parallel      
AC8 3 4 ? parallel      
AC9 1 2 ? parallel      
AC9 2 3 ? parallel      
AC9 3 4 ? parallel      
AD1 1 2 ? anti-parallel 
AD1 2 3 ? anti-parallel 
AD2 1 2 ? parallel      
AD2 2 3 ? parallel      
AD2 3 4 ? anti-parallel 
AD2 4 5 ? anti-parallel 
AD3 1 2 ? anti-parallel 
AD3 2 3 ? anti-parallel 
AD3 3 4 ? anti-parallel 
AD4 1 2 ? anti-parallel 
AD4 2 3 ? anti-parallel 
AD4 3 4 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD6 2 3 ? parallel      
AD7 1 2 ? anti-parallel 
AD7 2 3 ? anti-parallel 
AD8 1 2 ? parallel      
AD8 2 3 ? anti-parallel 
AD8 3 4 ? anti-parallel 
AD8 4 5 ? anti-parallel 
AD9 1 2 ? anti-parallel 
AD9 2 3 ? anti-parallel 
AD9 3 4 ? parallel      
AE1 1 2 ? anti-parallel 
AE2 1 2 ? anti-parallel 
AE2 2 3 ? parallel      
AE2 3 4 ? parallel      
AE3 1 2 ? parallel      
AE3 2 3 ? parallel      
AE3 3 4 ? parallel      
AE4 1 2 ? anti-parallel 
AE4 2 3 ? anti-parallel 
AE5 1 2 ? parallel      
AE5 2 3 ? parallel      
AE5 3 4 ? anti-parallel 
AE5 4 5 ? anti-parallel 
AE6 1 2 ? anti-parallel 
AE6 2 3 ? anti-parallel 
AE6 3 4 ? anti-parallel 
AE7 1 2 ? anti-parallel 
AE7 2 3 ? anti-parallel 
AE7 3 4 ? anti-parallel 
AE8 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 GLU A 27   ? CYS A 31   ? GLU A 27   CYS A 31   
AA1 2 ARG A 3    ? LEU A 7    ? ARG A 3    LEU A 7    
AA1 3 TRP A 47   ? TYR A 51   ? TRP A 47   TYR A 51   
AA1 4 ILE A 69   ? HIS A 73   ? ILE A 69   HIS A 73   
AA1 5 VAL A 98   ? LEU A 102  ? VAL A 98   LEU A 102  
AA1 6 ILE A 112  ? GLU A 116  ? ILE A 112  GLU A 116  
AA2 1 LYS A 81   ? GLY A 82   ? LYS A 81   GLY A 82   
AA2 2 LEU A 164  ? HIS A 165  ? LEU A 164  HIS A 165  
AA3 1 GLN A 227  ? THR A 230  ? GLN A 227  THR A 230  
AA3 2 VAL A 220  ? ASP A 224  ? VAL A 220  ASP A 224  
AA3 3 ALA A 411  ? ILE A 414  ? ALA A 411  ILE A 414  
AA3 4 LYS A 386  ? VAL A 389  ? LYS A 386  VAL A 389  
AA4 1 ALA A 279  ? PRO A 282  ? ALA A 279  PRO A 282  
AA4 2 GLN A 255  ? MET A 259  ? GLN A 255  MET A 259  
AA4 3 ILE A 303  ? THR A 306  ? ILE A 303  THR A 306  
AA4 4 ASP A 319  ? ASP A 322  ? ASP A 319  ASP A 322  
AA5 1 LEU A 345  ? THR A 351  ? LEU A 345  THR A 351  
AA5 2 LYS A 359  ? GLU A 364  ? LYS A 359  GLU A 364  
AA5 3 GLY A 541  ? TYR A 542  ? GLY A 541  TYR A 542  
AA6 1 ILE A 437  ? LEU A 440  ? ILE A 437  LEU A 440  
AA6 2 VAL A 458  ? THR A 461  ? VAL A 458  THR A 461  
AA6 3 LYS A 476  ? TYR A 481  ? LYS A 476  TYR A 481  
AA6 4 THR A 491  ? GLU A 494  ? THR A 491  GLU A 494  
AA6 5 LYS A 506  ? PRO A 507  ? LYS A 506  PRO A 507  
AA7 1 THR A 511  ? LEU A 516  ? THR A 511  LEU A 516  
AA7 2 GLY A 529  ? GLY A 535  ? GLY A 529  GLY A 535  
AA7 3 ARG A 562  ? PHE A 572  ? ARG A 562  PHE A 572  
AA7 4 PHE A 553  ? VAL A 555  ? PHE A 553  VAL A 555  
AA8 1 THR A 511  ? LEU A 516  ? THR A 511  LEU A 516  
AA8 2 GLY A 529  ? GLY A 535  ? GLY A 529  GLY A 535  
AA8 3 ARG A 562  ? PHE A 572  ? ARG A 562  PHE A 572  
AA8 4 ILE A 578  ? ARG A 583  ? ILE A 578  ARG A 583  
AA9 1 VAL A 588  ? ILE A 590  ? VAL A 588  ILE A 590  
AA9 2 TYR A 593  ? ILE A 595  ? TYR A 593  ILE A 595  
AB1 1 LEU A 612  ? GLU A 619  ? LEU A 612  GLU A 619  
AB1 2 LYS A 625  ? VAL A 632  ? LYS A 625  VAL A 632  
AB1 3 TYR A 658  ? MET A 662  ? TYR A 658  MET A 662  
AB2 1 TYR A 786  ? GLU A 787  ? TYR A 784  GLU A 785  
AB2 2 GLU A 849  ? ILE A 854  ? GLU A 847  ILE A 852  
AB2 3 SER A 841  ? ARG A 846  ? SER A 839  ARG A 844  
AB3 1 SER A 861  ? THR A 866  ? SER A 859  THR A 864  
AB3 2 LEU A 891  ? GLU A 897  ? LEU A 889  GLU A 895  
AB3 3 LYS A 902  ? HIS A 909  ? LYS A 900  HIS A 907  
AB3 4 ASN A 809  ? PHE A 816  ? ASN A 807  PHE A 814  
AB3 5 MET A 1134 ? ILE A 1137 ? MET A 1132 ILE A 1135 
AB4 1 GLY A 990  ? VAL A 997  ? GLY A 988  VAL A 995  
AB4 2 GLY A 1156 ? ASN A 1164 ? GLY A 1154 ASN A 1162 
AB4 3 LEU A 1146 ? ARG A 1153 ? LEU A 1144 ARG A 1151 
AB4 4 VAL A 1118 ? GLN A 1123 ? VAL A 1116 GLN A 1121 
AB5 1 GLN A 1037 ? THR A 1044 ? GLN A 1035 THR A 1042 
AB5 2 ASN A 1061 ? SER A 1068 ? ASN A 1059 SER A 1066 
AB6 1 GLN A 1247 ? THR A 1250 ? GLN A 1245 THR A 1248 
AB6 2 THR A 1240 ? PHE A 1244 ? THR A 1238 PHE A 1242 
AB6 3 LYS A 1431 ? ILE A 1434 ? LYS A 1429 ILE A 1432 
AB6 4 ALA A 1406 ? LEU A 1409 ? ALA A 1404 LEU A 1407 
AB7 1 ALA A 1299 ? PRO A 1302 ? ALA A 1297 PRO A 1300 
AB7 2 LEU A 1275 ? MET A 1279 ? LEU A 1273 MET A 1277 
AB7 3 LEU A 1323 ? ALA A 1326 ? LEU A 1321 ALA A 1324 
AB7 4 VAL A 1339 ? ASP A 1342 ? VAL A 1337 ASP A 1340 
AB8 1 LEU A 1365 ? TYR A 1370 ? LEU A 1363 TYR A 1368 
AB8 2 GLY A 1380 ? GLU A 1384 ? GLY A 1378 GLU A 1382 
AB8 3 GLY A 1574 ? LEU A 1576 ? GLY A 1572 LEU A 1574 
AB9 1 HIS A 1457 ? PHE A 1460 ? HIS A 1455 PHE A 1458 
AB9 2 TYR A 1483 ? ALA A 1486 ? TYR A 1481 ALA A 1484 
AB9 3 LYS A 1507 ? TYR A 1512 ? LYS A 1505 TYR A 1510 
AB9 4 SER A 1522 ? SER A 1525 ? SER A 1520 SER A 1523 
AB9 5 LYS A 1539 ? PRO A 1540 ? LYS A 1537 PRO A 1538 
AC1 1 TYR A 1544 ? ILE A 1549 ? TYR A 1542 ILE A 1547 
AC1 2 PRO A 1561 ? GLY A 1568 ? PRO A 1559 GLY A 1566 
AC1 3 ARG A 1596 ? TYR A 1606 ? ARG A 1594 TYR A 1604 
AC1 4 PHE A 1586 ? PRO A 1588 ? PHE A 1584 PRO A 1586 
AC2 1 TYR A 1544 ? ILE A 1549 ? TYR A 1542 ILE A 1547 
AC2 2 PRO A 1561 ? GLY A 1568 ? PRO A 1559 GLY A 1566 
AC2 3 ARG A 1596 ? TYR A 1606 ? ARG A 1594 TYR A 1604 
AC2 4 ILE A 1612 ? ARG A 1617 ? ILE A 1610 ARG A 1615 
AC3 1 LYS A 1623 ? ILE A 1624 ? LYS A 1621 ILE A 1622 
AC3 2 TYR A 1627 ? ARG A 1628 ? TYR A 1625 ARG A 1626 
AC4 1 VAL A 1650 ? ARG A 1652 ? VAL A 1648 ARG A 1650 
AC4 2 TYR A 1660 ? CYS A 1662 ? TYR A 1658 CYS A 1660 
AC5 1 TRP A 1777 ? THR A 1778 ? TRP A 1775 THR A 1776 
AC5 2 SER A 1799 ? GLU A 1800 ? SER A 1797 GLU A 1798 
AC6 1 GLU B 27   ? CYS B 31   ? GLU B 27   CYS B 31   
AC6 2 ARG B 3    ? LEU B 7    ? ARG B 3    LEU B 7    
AC6 3 TRP B 47   ? SER B 50   ? TRP B 47   SER B 50   
AC6 4 ILE B 69   ? HIS B 73   ? ILE B 69   HIS B 73   
AC6 5 GLY B 97   ? LEU B 102  ? GLY B 97   LEU B 102  
AC6 6 ILE B 112  ? GLU B 117  ? ILE B 112  GLU B 117  
AC7 1 LYS B 81   ? GLY B 82   ? LYS B 81   GLY B 82   
AC7 2 LEU B 164  ? HIS B 165  ? LEU B 164  HIS B 165  
AC8 1 GLN B 227  ? THR B 230  ? GLN B 227  THR B 230  
AC8 2 VAL B 220  ? ASP B 224  ? VAL B 220  ASP B 224  
AC8 3 ALA B 411  ? ILE B 414  ? ALA B 411  ILE B 414  
AC8 4 LYS B 386  ? VAL B 389  ? LYS B 386  VAL B 389  
AC9 1 ALA B 279  ? PRO B 282  ? ALA B 279  PRO B 282  
AC9 2 GLN B 255  ? MET B 259  ? GLN B 255  MET B 259  
AC9 3 ILE B 303  ? THR B 306  ? ILE B 303  THR B 306  
AC9 4 ASP B 319  ? ASP B 322  ? ASP B 319  ASP B 322  
AD1 1 LEU B 345  ? TYR B 350  ? LEU B 345  TYR B 350  
AD1 2 GLY B 360  ? GLU B 364  ? GLY B 360  GLU B 364  
AD1 3 GLY B 541  ? TYR B 542  ? GLY B 541  TYR B 542  
AD2 1 ILE B 437  ? PRO B 441  ? ILE B 437  PRO B 441  
AD2 2 VAL B 458  ? GLY B 462  ? VAL B 458  GLY B 462  
AD2 3 LYS B 476  ? TYR B 481  ? LYS B 476  TYR B 481  
AD2 4 THR B 491  ? GLU B 494  ? THR B 491  GLU B 494  
AD2 5 LYS B 506  ? PRO B 507  ? LYS B 506  PRO B 507  
AD3 1 THR B 511  ? LEU B 516  ? THR B 511  LEU B 516  
AD3 2 GLY B 529  ? GLY B 535  ? GLY B 529  GLY B 535  
AD3 3 ARG B 562  ? PHE B 572  ? ARG B 562  PHE B 572  
AD3 4 PHE B 553  ? VAL B 555  ? PHE B 553  VAL B 555  
AD4 1 THR B 511  ? LEU B 516  ? THR B 511  LEU B 516  
AD4 2 GLY B 529  ? GLY B 535  ? GLY B 529  GLY B 535  
AD4 3 ARG B 562  ? PHE B 572  ? ARG B 562  PHE B 572  
AD4 4 ILE B 578  ? ARG B 583  ? ILE B 578  ARG B 583  
AD5 1 VAL B 588  ? LYS B 589  ? VAL B 588  LYS B 589  
AD5 2 ARG B 594  ? ILE B 595  ? ARG B 594  ILE B 595  
AD6 1 LEU B 612  ? GLU B 619  ? LEU B 612  GLU B 619  
AD6 2 LYS B 625  ? VAL B 632  ? LYS B 625  VAL B 632  
AD6 3 TYR B 658  ? MET B 662  ? TYR B 658  MET B 662  
AD7 1 TYR B 786  ? GLU B 787  ? TYR B 784  GLU B 785  
AD7 2 GLU B 849  ? ILE B 854  ? GLU B 847  ILE B 852  
AD7 3 SER B 841  ? ARG B 846  ? SER B 839  ARG B 844  
AD8 1 SER B 861  ? THR B 866  ? SER B 859  THR B 864  
AD8 2 LEU B 891  ? GLU B 897  ? LEU B 889  GLU B 895  
AD8 3 LYS B 902  ? HIS B 909  ? LYS B 900  HIS B 907  
AD8 4 ASN B 809  ? PHE B 816  ? ASN B 807  PHE B 814  
AD8 5 MET B 1134 ? ILE B 1137 ? MET B 1132 ILE B 1135 
AD9 1 GLY B 990  ? VAL B 997  ? GLY B 988  VAL B 995  
AD9 2 GLY B 1156 ? ASN B 1164 ? GLY B 1154 ASN B 1162 
AD9 3 LEU B 1146 ? ARG B 1153 ? LEU B 1144 ARG B 1151 
AD9 4 VAL B 1118 ? GLN B 1123 ? VAL B 1116 GLN B 1121 
AE1 1 GLN B 1037 ? THR B 1044 ? GLN B 1035 THR B 1042 
AE1 2 ASN B 1061 ? SER B 1068 ? ASN B 1059 SER B 1066 
AE2 1 GLN B 1247 ? THR B 1250 ? GLN B 1245 THR B 1248 
AE2 2 THR B 1240 ? PHE B 1244 ? THR B 1238 PHE B 1242 
AE2 3 LYS B 1431 ? ILE B 1434 ? LYS B 1429 ILE B 1432 
AE2 4 ALA B 1406 ? LEU B 1409 ? ALA B 1404 LEU B 1407 
AE3 1 ALA B 1299 ? PRO B 1302 ? ALA B 1297 PRO B 1300 
AE3 2 LEU B 1275 ? MET B 1279 ? LEU B 1273 MET B 1277 
AE3 3 LEU B 1323 ? ALA B 1326 ? LEU B 1321 ALA B 1324 
AE3 4 VAL B 1339 ? ASP B 1342 ? VAL B 1337 ASP B 1340 
AE4 1 LEU B 1365 ? TYR B 1370 ? LEU B 1363 TYR B 1368 
AE4 2 GLY B 1380 ? GLU B 1384 ? GLY B 1378 GLU B 1382 
AE4 3 GLY B 1574 ? TYR B 1575 ? GLY B 1572 TYR B 1573 
AE5 1 HIS B 1457 ? PHE B 1460 ? HIS B 1455 PHE B 1458 
AE5 2 TYR B 1483 ? ALA B 1486 ? TYR B 1481 ALA B 1484 
AE5 3 LYS B 1507 ? TYR B 1512 ? LYS B 1505 TYR B 1510 
AE5 4 SER B 1522 ? SER B 1525 ? SER B 1520 SER B 1523 
AE5 5 LYS B 1539 ? PRO B 1540 ? LYS B 1537 PRO B 1538 
AE6 1 TYR B 1544 ? ILE B 1549 ? TYR B 1542 ILE B 1547 
AE6 2 GLY B 1562 ? GLY B 1568 ? GLY B 1560 GLY B 1566 
AE6 3 ARG B 1596 ? TYR B 1606 ? ARG B 1594 TYR B 1604 
AE6 4 PHE B 1586 ? PRO B 1588 ? PHE B 1584 PRO B 1586 
AE7 1 TYR B 1544 ? ILE B 1549 ? TYR B 1542 ILE B 1547 
AE7 2 GLY B 1562 ? GLY B 1568 ? GLY B 1560 GLY B 1566 
AE7 3 ARG B 1596 ? TYR B 1606 ? ARG B 1594 TYR B 1604 
AE7 4 ILE B 1612 ? ARG B 1617 ? ILE B 1610 ARG B 1615 
AE8 1 TRP B 1777 ? THR B 1778 ? TRP B 1775 THR B 1776 
AE8 2 SER B 1799 ? GLU B 1800 ? SER B 1797 GLU B 1798 
# 
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 O VAL A 29   ? O VAL A 29   N ILE A 4    ? N ILE A 4    
AA1 2 3 N LEU A 7    ? N LEU A 7    O VAL A 49   ? O VAL A 49   
AA1 3 4 N SER A 50   ? N SER A 50   O ILE A 70   ? O ILE A 70   
AA1 4 5 N HIS A 73   ? N HIS A 73   O THR A 99   ? O THR A 99   
AA1 5 6 N ILE A 100  ? N ILE A 100  O LEU A 113  ? O LEU A 113  
AA2 1 2 N LYS A 81   ? N LYS A 81   O HIS A 165  ? O HIS A 165  
AA3 1 2 O LEU A 229  ? O LEU A 229  N ALA A 221  ? N ALA A 221  
AA3 2 3 N ALA A 221  ? N ALA A 221  O LEU A 412  ? O LEU A 412  
AA3 3 4 O HIS A 413  ? O HIS A 413  N ALA A 387  ? N ALA A 387  
AA4 1 2 O VAL A 281  ? O VAL A 281  N VAL A 256  ? N VAL A 256  
AA4 2 3 N ALA A 257  ? N ALA A 257  O LEU A 305  ? O LEU A 305  
AA4 3 4 N LEU A 304  ? N LEU A 304  O ILE A 321  ? O ILE A 321  
AA5 1 2 N MET A 349  ? N MET A 349  O VAL A 361  ? O VAL A 361  
AA5 2 3 N MET A 362  ? N MET A 362  O GLY A 541  ? O GLY A 541  
AA6 1 2 N LEU A 440  ? N LEU A 440  O ILE A 460  ? O ILE A 460  
AA6 2 3 N VAL A 459  ? N VAL A 459  O LYS A 476  ? O LYS A 476  
AA6 3 4 N ASN A 479  ? N ASN A 479  O PHE A 493  ? O PHE A 493  
AA6 4 5 N MET A 492  ? N MET A 492  O LYS A 506  ? O LYS A 506  
AA7 1 2 N ARG A 512  ? N ARG A 512  O VAL A 534  ? O VAL A 534  
AA7 2 3 N LEU A 531  ? N LEU A 531  O ASP A 568  ? O ASP A 568  
AA7 3 4 O MET A 563  ? O MET A 563  N ILE A 554  ? N ILE A 554  
AA8 1 2 N ARG A 512  ? N ARG A 512  O VAL A 534  ? O VAL A 534  
AA8 2 3 N LEU A 531  ? N LEU A 531  O ASP A 568  ? O ASP A 568  
AA8 3 4 N ARG A 569  ? N ARG A 569  O GLY A 582  ? O GLY A 582  
AA9 1 2 N VAL A 588  ? N VAL A 588  O ILE A 595  ? O ILE A 595  
AB1 1 2 N LYS A 618  ? N LYS A 618  O TYR A 626  ? O TYR A 626  
AB1 2 3 N GLY A 629  ? N GLY A 629  O TYR A 658  ? O TYR A 658  
AB2 1 2 N TYR A 786  ? N TYR A 784  O LYS A 852  ? O LYS A 850  
AB2 2 3 O VAL A 851  ? O VAL A 849  N HIS A 844  ? N HIS A 842  
AB3 1 2 N SER A 861  ? N SER A 859  O ALA A 893  ? O ALA A 891  
AB3 2 3 N ILE A 896  ? N ILE A 894  O VAL A 903  ? O VAL A 901  
AB3 3 4 O LYS A 902  ? O LYS A 900  N PHE A 816  ? N PHE A 814  
AB3 4 5 N VAL A 811  ? N VAL A 809  O ILE A 1137 ? O ILE A 1135 
AB4 1 2 N GLN A 993  ? N GLN A 991  O PHE A 1161 ? O PHE A 1159 
AB4 2 3 O GLU A 1162 ? O GLU A 1160 N THR A 1147 ? N THR A 1145 
AB4 3 4 O LEU A 1148 ? O LEU A 1146 N MET A 1121 ? N MET A 1119 
AB5 1 2 N LEU A 1040 ? N LEU A 1038 O LEU A 1065 ? O LEU A 1063 
AB6 1 2 O VAL A 1249 ? O VAL A 1247 N ALA A 1241 ? N ALA A 1239 
AB6 2 3 N VAL A 1243 ? N VAL A 1241 O ILE A 1434 ? O ILE A 1432 
AB6 3 4 O VAL A 1433 ? O VAL A 1431 N LEU A 1409 ? N LEU A 1407 
AB7 1 2 O LEU A 1301 ? O LEU A 1299 N LEU A 1278 ? N LEU A 1276 
AB7 2 3 N MET A 1277 ? N MET A 1275 O LEU A 1325 ? O LEU A 1323 
AB7 3 4 N VAL A 1324 ? N VAL A 1322 O VAL A 1339 ? O VAL A 1337 
AB8 1 2 N VAL A 1366 ? N VAL A 1364 O ILE A 1383 ? O ILE A 1381 
AB8 2 3 N GLY A 1380 ? N GLY A 1378 O LEU A 1576 ? O LEU A 1574 
AB9 1 2 N ILE A 1458 ? N ILE A 1456 O LEU A 1485 ? O LEU A 1483 
AB9 2 3 N ALA A 1486 ? N ALA A 1484 O ILE A 1511 ? O ILE A 1509 
AB9 3 4 N TYR A 1512 ? N TYR A 1510 O SER A 1522 ? O SER A 1520 
AB9 4 5 N ARG A 1523 ? N ARG A 1521 O LYS A 1539 ? O LYS A 1537 
AC1 1 2 N ARG A 1545 ? N ARG A 1543 O ALA A 1567 ? O ALA A 1565 
AC1 2 3 N GLY A 1562 ? N GLY A 1560 O ALA A 1604 ? O ALA A 1602 
AC1 3 4 O ILE A 1597 ? O ILE A 1595 N THR A 1587 ? N THR A 1585 
AC2 1 2 N ARG A 1545 ? N ARG A 1543 O ALA A 1567 ? O ALA A 1565 
AC2 2 3 N GLY A 1562 ? N GLY A 1560 O ALA A 1604 ? O ALA A 1602 
AC2 3 4 N LEU A 1603 ? N LEU A 1601 O GLY A 1616 ? O GLY A 1614 
AC3 1 2 N ILE A 1624 ? N ILE A 1622 O TYR A 1627 ? O TYR A 1625 
AC4 1 2 N ARG A 1652 ? N ARG A 1650 O TYR A 1660 ? O TYR A 1658 
AC5 1 2 N THR A 1778 ? N THR A 1776 O SER A 1799 ? O SER A 1797 
AC6 1 2 O VAL B 29   ? O VAL B 29   N ILE B 4    ? N ILE B 4    
AC6 2 3 N LEU B 7    ? N LEU B 7    O VAL B 49   ? O VAL B 49   
AC6 3 4 N SER B 50   ? N SER B 50   O ILE B 70   ? O ILE B 70   
AC6 4 5 N HIS B 73   ? N HIS B 73   O THR B 99   ? O THR B 99   
AC6 5 6 N VAL B 98   ? N VAL B 98   O GLU B 116  ? O GLU B 116  
AC7 1 2 N LYS B 81   ? N LYS B 81   O HIS B 165  ? O HIS B 165  
AC8 1 2 O LEU B 229  ? O LEU B 229  N ALA B 221  ? N ALA B 221  
AC8 2 3 N ALA B 221  ? N ALA B 221  O LEU B 412  ? O LEU B 412  
AC8 3 4 O ALA B 411  ? O ALA B 411  N ALA B 387  ? N ALA B 387  
AC9 1 2 O ALA B 279  ? O ALA B 279  N VAL B 256  ? N VAL B 256  
AC9 2 3 N ALA B 257  ? N ALA B 257  O LEU B 305  ? O LEU B 305  
AC9 3 4 N LEU B 304  ? N LEU B 304  O ASP B 319  ? O ASP B 319  
AD1 1 2 N MET B 349  ? N MET B 349  O VAL B 361  ? O VAL B 361  
AD1 2 3 N MET B 362  ? N MET B 362  O GLY B 541  ? O GLY B 541  
AD2 1 2 N LEU B 440  ? N LEU B 440  O ILE B 460  ? O ILE B 460  
AD2 2 3 N VAL B 459  ? N VAL B 459  O LYS B 476  ? O LYS B 476  
AD2 3 4 N ASN B 479  ? N ASN B 479  O PHE B 493  ? O PHE B 493  
AD2 4 5 N MET B 492  ? N MET B 492  O LYS B 506  ? O LYS B 506  
AD3 1 2 N ARG B 512  ? N ARG B 512  O VAL B 534  ? O VAL B 534  
AD3 2 3 N GLY B 529  ? N GLY B 529  O ALA B 570  ? O ALA B 570  
AD3 3 4 O MET B 563  ? O MET B 563  N ILE B 554  ? N ILE B 554  
AD4 1 2 N ARG B 512  ? N ARG B 512  O VAL B 534  ? O VAL B 534  
AD4 2 3 N GLY B 529  ? N GLY B 529  O ALA B 570  ? O ALA B 570  
AD4 3 4 N ARG B 569  ? N ARG B 569  O GLY B 582  ? O GLY B 582  
AD5 1 2 N VAL B 588  ? N VAL B 588  O ILE B 595  ? O ILE B 595  
AD6 1 2 N THR B 614  ? N THR B 614  O TYR B 630  ? O TYR B 630  
AD6 2 3 N GLY B 629  ? N GLY B 629  O TYR B 658  ? O TYR B 658  
AD7 1 2 N TYR B 786  ? N TYR B 784  O LYS B 852  ? O LYS B 850  
AD7 2 3 O ARG B 853  ? O ARG B 851  N THR B 842  ? N THR B 840  
AD8 1 2 N GLN B 865  ? N GLN B 863  O VAL B 895  ? O VAL B 893  
AD8 2 3 N GLY B 894  ? N GLY B 892  O TRP B 905  ? O TRP B 903  
AD8 3 4 O LEU B 904  ? O LEU B 902  N ILE B 814  ? N ILE B 812  
AD8 4 5 N VAL B 811  ? N VAL B 809  O ILE B 1137 ? O ILE B 1135 
AD9 1 2 N GLN B 993  ? N GLN B 991  O PHE B 1161 ? O PHE B 1159 
AD9 2 3 O VAL B 1160 ? O VAL B 1158 N GLU B 1149 ? N GLU B 1147 
AD9 3 4 O LEU B 1148 ? O LEU B 1146 N MET B 1119 ? N MET B 1117 
AE1 1 2 N THR B 1042 ? N THR B 1040 O LEU B 1063 ? O LEU B 1061 
AE2 1 2 O GLN B 1247 ? O GLN B 1245 N PHE B 1244 ? N PHE B 1242 
AE2 2 3 N ALA B 1241 ? N ALA B 1239 O LEU B 1432 ? O LEU B 1430 
AE2 3 4 O VAL B 1433 ? O VAL B 1431 N PHE B 1407 ? N PHE B 1405 
AE3 1 2 O LEU B 1301 ? O LEU B 1299 N VAL B 1276 ? N VAL B 1274 
AE3 2 3 N MET B 1277 ? N MET B 1275 O LEU B 1325 ? O LEU B 1323 
AE3 3 4 N VAL B 1324 ? N VAL B 1322 O LEU B 1341 ? O LEU B 1339 
AE4 1 2 N MET B 1369 ? N MET B 1367 O VAL B 1381 ? O VAL B 1379 
AE4 2 3 N MET B 1382 ? N MET B 1380 O GLY B 1574 ? O GLY B 1572 
AE5 1 2 N PHE B 1460 ? N PHE B 1458 O LEU B 1485 ? O LEU B 1483 
AE5 2 3 N ALA B 1486 ? N ALA B 1484 O ILE B 1511 ? O ILE B 1509 
AE5 3 4 N TYR B 1512 ? N TYR B 1510 O SER B 1522 ? O SER B 1520 
AE5 4 5 N ARG B 1523 ? N ARG B 1521 O LYS B 1539 ? O LYS B 1537 
AE6 1 2 N TYR B 1547 ? N TYR B 1545 O CYS B 1565 ? O CYS B 1563 
AE6 2 3 N GLY B 1562 ? N GLY B 1560 O ALA B 1604 ? O ALA B 1602 
AE6 3 4 O ILE B 1597 ? O ILE B 1595 N THR B 1587 ? N THR B 1585 
AE7 1 2 N TYR B 1547 ? N TYR B 1545 O CYS B 1565 ? O CYS B 1563 
AE7 2 3 N GLY B 1562 ? N GLY B 1560 O ALA B 1604 ? O ALA B 1602 
AE7 3 4 N LEU B 1603 ? N LEU B 1601 O GLY B 1616 ? O GLY B 1614 
AE8 1 2 N THR B 1778 ? N THR B 1776 O SER B 1799 ? O SER B 1797 
# 
_pdbx_entry_details.entry_id                   9BE4 
_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 OH  B TYR 130  ? ? NH2 B ARG 170  ? ? 2.10 
2 1 OD2 B ASP 697  ? ? NZ  B LYS 761  ? ? 2.14 
3 1 NZ  A LYS 248  ? ? OD2 A ASP 319  ? ? 2.14 
4 1 OE1 B GLU 1436 ? ? NZ  B LYS 1439 ? ? 2.15 
5 1 O   B ILE 1313 ? ? OG  B SER 1317 ? ? 2.18 
6 1 OE1 B GLN 1035 ? ? OG  B SER 1066 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NZ 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    LYS 
_pdbx_validate_symm_contact.auth_seq_id_1     167 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    OD2 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    ASP 
_pdbx_validate_symm_contact.auth_seq_id_2     953 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_556 
_pdbx_validate_symm_contact.dist              1.85 
# 
_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             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              1321 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_2              1321 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              1321 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                131.25 
_pdbx_validate_rmsd_angle.angle_target_value         115.30 
_pdbx_validate_rmsd_angle.angle_deviation            15.95 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.30 
_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 GLU A 33   ? ? -119.15 -167.93 
2   1 ASN A 41   ? ? -70.59  20.12   
3   1 TYR A 55   ? ? 68.73   149.70  
4   1 ASP A 104  ? ? -120.55 -161.44 
5   1 PHE A 166  ? ? -123.94 -169.56 
6   1 LYS A 174  ? ? -68.33  -177.33 
7   1 CYS A 191  ? ? -140.68 18.18   
8   1 ARG A 225  ? ? 56.50   -135.69 
9   1 ASN A 307  ? ? -104.59 -143.68 
10  1 PRO A 383  ? ? -66.21  0.29    
11  1 ARG A 419  ? ? -79.68  -131.76 
12  1 LYS A 420  ? ? 60.72   -48.84  
13  1 ASN A 472  ? ? -102.10 65.22   
14  1 CYS A 486  ? ? -112.38 61.30   
15  1 THR A 487  ? ? 65.52   -118.57 
16  1 ASP A 649  ? ? -160.57 38.15   
17  1 ARG A 676  ? ? -153.66 -24.03  
18  1 VAL A 681  ? ? -114.32 -93.62  
19  1 GLN A 715  ? ? 54.35   73.39   
20  1 ASP A 728  ? ? -110.69 -162.48 
21  1 GLU A 868  ? ? -91.82  34.21   
22  1 SER A 869  ? ? -153.05 -12.98  
23  1 LEU A 889  ? ? -161.06 111.81  
24  1 PRO A 976  ? ? -69.50  73.24   
25  1 GLN A 983  ? ? -96.39  -153.97 
26  1 ASN A 1030 ? ? -89.82  40.47   
27  1 ARG A 1106 ? ? -142.16 54.15   
28  1 LEU A 1113 ? ? 64.30   -55.86  
29  1 VAL A 1211 ? ? -132.90 -62.74  
30  1 ARG A 1243 ? ? 54.45   -115.03 
31  1 ALA A 1332 ? ? -76.61  29.30   
32  1 ALA A 1335 ? ? -124.83 -144.65 
33  1 GLU A 1336 ? ? -128.26 -63.32  
34  1 GLU A 1436 ? ? 67.85   -1.99   
35  1 TYR A 1469 ? ? 66.48   -59.80  
36  1 GLU A 1503 ? ? 69.62   -9.52   
37  1 THR A 1516 ? ? 56.67   -102.78 
38  1 ALA A 1519 ? ? -159.99 -38.27  
39  1 VAL A 1533 ? ? 51.20   77.13   
40  1 SER A 1568 ? ? -81.64  33.37   
41  1 ASN A 1576 ? ? -151.65 73.60   
42  1 HIS A 1618 ? ? -118.34 60.19   
43  1 VAL A 1795 ? ? -162.64 -133.68 
44  1 ALA A 1804 ? ? -167.86 -115.77 
45  1 ALA A 1805 ? ? 69.81   -113.77 
46  1 THR B 9    ? ? -140.14 -39.35  
47  1 MET B 11   ? ? -100.44 -166.96 
48  1 GLN B 38   ? ? -90.54  54.21   
49  1 ASP B 104  ? ? -104.79 -157.51 
50  1 TYR B 173  ? ? -96.67  36.97   
51  1 THR B 474  ? ? -94.56  35.76   
52  1 CYS B 486  ? ? -119.39 59.51   
53  1 THR B 487  ? ? 67.26   -121.44 
54  1 ILE B 488  ? ? -109.37 -61.24  
55  1 ASP B 517  ? ? -86.33  -154.77 
56  1 ASN B 586  ? ? -89.10  40.02   
57  1 ASP B 622  ? ? -66.87  2.47    
58  1 ASP B 649  ? ? -149.80 23.21   
59  1 MET B 654  ? ? -99.19  43.25   
60  1 ASP B 728  ? ? -109.74 -130.22 
61  1 GLN B 769  ? ? -90.76  34.39   
62  1 ASN B 770  A ? 63.31   62.22   
63  1 GLU B 868  ? ? -89.57  35.45   
64  1 SER B 869  ? ? -147.52 -16.04  
65  1 LEU B 883  ? ? -67.18  0.59    
66  1 LEU B 888  ? ? -78.00  44.51   
67  1 THR B 896  ? ? -97.01  -157.19 
68  1 ASP B 912  ? ? -115.24 -165.37 
69  1 GLU B 936  ? ? -105.34 -61.63  
70  1 LEU B 965  ? ? -134.46 -34.39  
71  1 PRO B 976  ? ? -65.25  89.05   
72  1 GLN B 983  ? ? -109.95 -161.95 
73  1 THR B 1020 ? ? -57.54  -76.24  
74  1 ASN B 1030 ? ? -86.33  40.40   
75  1 ASN B 1090 ? ? -100.52 41.79   
76  1 LEU B 1113 ? ? 62.97   -81.05  
77  1 MET B 1120 ? ? -152.28 89.85   
78  1 VAL B 1211 ? ? -132.58 -62.32  
79  1 ASN B 1212 ? ? -98.48  34.81   
80  1 ARG B 1243 ? ? 52.28   -118.49 
81  1 TYR B 1411 ? ? -69.04  0.22    
82  1 PHE B 1466 ? ? -49.90  -78.88  
83  1 TYR B 1469 ? ? -131.46 -34.81  
84  1 THR B 1516 ? ? 63.99   -114.87 
85  1 ILE B 1517 ? ? -105.43 -61.13  
86  1 ALA B 1519 ? ? -149.24 -29.58  
87  1 ASN B 1541 ? ? 58.75   19.67   
88  1 ASN B 1548 ? ? -111.01 -154.08 
89  1 SER B 1568 ? ? -89.61  42.35   
90  1 ASN B 1576 ? ? -150.20 74.97   
91  1 ARG B 1633 ? ? -80.53  31.75   
92  1 SER B 1634 ? ? -121.97 -167.46 
93  1 VAL B 1647 ? ? -130.04 -149.60 
94  1 VAL B 1648 ? ? -103.38 -162.74 
95  1 ALA B 1649 ? ? 76.77   -150.93 
96  1 ARG B 1650 ? ? 65.36   82.57   
97  1 GLU B 1681 ? ? -159.93 24.97   
98  1 ALA B 1724 ? ? -163.52 78.13   
99  1 ARG B 1727 ? ? -149.62 -30.70  
100 1 PHE B 1753 ? ? -99.62  -77.08  
101 1 ASP B 1759 ? ? -130.63 -142.73 
102 1 PRO B 1786 ? ? -69.16  9.31    
103 1 PHE B 1794 ? ? -54.71  -71.37  
104 1 VAL B 1795 ? ? -101.52 -140.34 
105 1 ALA B 1804 ? ? -169.86 -118.62 
106 1 ALA B 1805 ? ? 81.78   -124.09 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A 4HH 729 A 4HH 729 ? SER 'modified residue' 
2 B 4HH 729 B 4HH 729 ? SER 'modified residue' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x+1/2,y+1/2,-z 
4 -x,-y,z         
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A ARG 196  ? A ARG 196  
2   1 Y 1 A GLY 197  ? A GLY 197  
3   1 Y 1 A THR 355  ? A THR 355  
4   1 Y 1 A GLY 356  ? A GLY 356  
5   1 Y 1 A ALA 683  ? A ALA 683  
6   1 Y 1 A ASP 684  ? A ASP 684  
7   1 Y 1 A ALA 685  ? A ALA 685  
8   1 Y 1 A SER 1370 ? A SER 1372 
9   1 Y 1 A GLY 1371 ? A GLY 1373 
10  1 Y 1 A SER 1372 ? A SER 1374 
11  1 Y 1 A THR 1373 ? A THR 1375 
12  1 Y 1 A GLN 1653 ? A GLN 1655 
13  1 Y 1 A ASN 1654 ? A ASN 1656 
14  1 Y 1 A GLY 1655 ? A GLY 1657 
15  1 Y 1 A GLN 1656 ? A GLN 1658 
16  1 Y 1 A TYR 1662 ? A TYR 1664 
17  1 Y 1 A LEU 1663 ? A LEU 1665 
18  1 Y 1 A LEU 1664 ? A LEU 1666 
19  1 Y 1 A SER 1665 ? A SER 1667 
20  1 Y 1 A GLU 1666 ? A GLU 1668 
21  1 Y 1 A VAL 1692 ? A VAL 1694 
22  1 Y 1 A LEU 1693 ? A LEU 1695 
23  1 Y 1 A LEU 1694 ? A LEU 1696 
24  1 Y 1 A LYS 1695 ? A LYS 1697 
25  1 Y 1 A GLN 1696 ? A GLN 1698 
26  1 Y 1 A PHE 1697 ? A PHE 1699 
27  1 Y 1 A PRO 1698 ? A PRO 1700 
28  1 Y 1 A LEU 1699 ? A LEU 1701 
29  1 Y 1 A THR 1700 ? A THR 1702 
30  1 Y 1 A ALA 1701 ? A ALA 1703 
31  1 Y 1 A ASN 1702 ? A ASN 1704 
32  1 Y 1 A GLY 1703 ? A GLY 1705 
33  1 Y 1 A LYS 1704 ? A LYS 1706 
34  1 Y 1 A LEU 1705 ? A LEU 1707 
35  1 Y 1 A ASP 1706 ? A ASP 1708 
36  1 Y 1 A ARG 1707 ? A ARG 1709 
37  1 Y 1 A LYS 1708 ? A LYS 1710 
38  1 Y 1 A ALA 1709 ? A ALA 1711 
39  1 Y 1 A LEU 1710 ? A LEU 1712 
40  1 Y 1 A PRO 1711 ? A PRO 1713 
41  1 Y 1 A GLU 1712 ? A GLU 1714 
42  1 Y 1 A PRO 1713 ? A PRO 1715 
43  1 Y 1 A ASP 1714 ? A ASP 1716 
44  1 Y 1 A GLY 1715 ? A GLY 1717 
45  1 Y 1 A SER 1716 ? A SER 1718 
46  1 Y 1 A VAL 1717 ? A VAL 1719 
47  1 Y 1 A LYS 1718 ? A LYS 1720 
48  1 Y 1 A ALA 1719 ? A ALA 1721 
49  1 Y 1 A GLU 1720 ? A GLU 1722 
50  1 Y 1 A ALA 1721 ? A ALA 1723 
51  1 Y 1 A GLU 1722 ? A GLU 1724 
52  1 Y 1 A TYR 1723 ? A TYR 1725 
53  1 Y 1 B ARG 196  ? B ARG 196  
54  1 Y 1 B GLY 197  ? B GLY 197  
55  1 Y 1 B GLY 1371 ? B GLY 1373 
56  1 Y 1 B SER 1372 ? B SER 1374 
57  1 Y 1 B GLN 1638 ? B GLN 1640 
58  1 Y 1 B GLU 1639 ? B GLU 1641 
59  1 Y 1 B GLU 1640 ? B GLU 1642 
60  1 Y 1 B THR 1641 ? B THR 1643 
61  1 Y 1 B ILE 1642 ? B ILE 1644 
62  1 Y 1 B GLN 1643 ? B GLN 1645 
63  1 Y 1 B ASP 1644 ? B ASP 1646 
64  1 Y 1 B ALA 1645 ? B ALA 1647 
65  1 Y 1 B ALA 1661 ? B ALA 1663 
66  1 Y 1 B TYR 1662 ? B TYR 1664 
67  1 Y 1 B LEU 1663 ? B LEU 1665 
68  1 Y 1 B LEU 1664 ? B LEU 1666 
69  1 Y 1 B SER 1665 ? B SER 1667 
70  1 Y 1 B GLU 1666 ? B GLU 1668 
71  1 Y 1 B GLN 1667 ? B GLN 1669 
72  1 Y 1 B GLU 1668 ? B GLU 1670 
73  1 Y 1 B TRP 1669 ? B TRP 1671 
74  1 Y 1 B THR 1670 ? B THR 1672 
75  1 Y 1 B VAL 1671 ? B VAL 1673 
76  1 Y 1 B HIS 1690 ? B HIS 1692 
77  1 Y 1 B PHE 1691 ? B PHE 1693 
78  1 Y 1 B VAL 1692 ? B VAL 1694 
79  1 Y 1 B LEU 1693 ? B LEU 1695 
80  1 Y 1 B LEU 1694 ? B LEU 1696 
81  1 Y 1 B LYS 1695 ? B LYS 1697 
82  1 Y 1 B GLN 1696 ? B GLN 1698 
83  1 Y 1 B PHE 1697 ? B PHE 1699 
84  1 Y 1 B PRO 1698 ? B PRO 1700 
85  1 Y 1 B LEU 1699 ? B LEU 1701 
86  1 Y 1 B THR 1700 ? B THR 1702 
87  1 Y 1 B ALA 1701 ? B ALA 1703 
88  1 Y 1 B ASN 1702 ? B ASN 1704 
89  1 Y 1 B GLY 1703 ? B GLY 1705 
90  1 Y 1 B LYS 1704 ? B LYS 1706 
91  1 Y 1 B LEU 1705 ? B LEU 1707 
92  1 Y 1 B ASP 1706 ? B ASP 1708 
93  1 Y 1 B ARG 1707 ? B ARG 1709 
94  1 Y 1 B LYS 1708 ? B LYS 1710 
95  1 Y 1 B ALA 1709 ? B ALA 1711 
96  1 Y 1 B LEU 1710 ? B LEU 1712 
97  1 Y 1 B PRO 1711 ? B PRO 1713 
98  1 Y 1 B GLU 1712 ? B GLU 1714 
99  1 Y 1 B PRO 1713 ? B PRO 1715 
100 1 Y 1 B ASP 1714 ? B ASP 1716 
101 1 Y 1 B GLY 1715 ? B GLY 1717 
102 1 Y 1 B SER 1716 ? B SER 1718 
103 1 Y 1 B VAL 1717 ? B VAL 1719 
104 1 Y 1 B LYS 1718 ? B LYS 1720 
105 1 Y 1 B ALA 1719 ? B ALA 1721 
106 1 Y 1 B GLU 1720 ? B GLU 1722 
107 1 Y 1 B ALA 1721 ? B ALA 1723 
108 1 Y 1 B GLU 1722 ? B GLU 1724 
# 
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 
4HH   O    O  N N 1   
4HH   C    C  N N 2   
4HH   CA   C  N S 3   
4HH   N    N  N N 4   
4HH   CB   C  N N 5   
4HH   OG   O  N N 6   
4HH   CJ   C  N N 7   
4HH   CK   C  N N 8   
4HH   CL1  C  N N 9   
4HH   CL2  C  N N 10  
4HH   CL3  C  N N 11  
4HH   CM   C  N R 12  
4HH   OM   O  N N 13  
4HH   NN   N  N N 14  
4HH   ON   O  N N 15  
4HH   P    P  N N 16  
4HH   O1P  O  N N 17  
4HH   O2P  O  N N 18  
4HH   O3P  O  N N 19  
4HH   CO   C  N N 20  
4HH   CP   C  N N 21  
4HH   CQ   C  N N 22  
4HH   CS   C  N N 23  
4HH   CT   C  N N 24  
4HH   NR   N  N N 25  
4HH   OR   O  N N 26  
4HH   SU   S  N N 27  
4HH   HA   H  N N 28  
4HH   H    H  N N 29  
4HH   H2   H  N N 30  
4HH   HB3  H  N N 31  
4HH   HB2  H  N N 32  
4HH   HJ3  H  N N 33  
4HH   HJ2  H  N N 34  
4HH   HL13 H  N N 35  
4HH   HL12 H  N N 36  
4HH   HL11 H  N N 37  
4HH   HL21 H  N N 38  
4HH   HL23 H  N N 39  
4HH   HL22 H  N N 40  
4HH   HL3  H  N N 41  
4HH   HM   H  N N 42  
4HH   HN   H  N N 43  
4HH   H4   H  N N 44  
4HH   HO2  H  N N 45  
4HH   HO3  H  N N 46  
4HH   HP3  H  N N 47  
4HH   HP2  H  N N 48  
4HH   HS2  H  N N 49  
4HH   HS3  H  N N 50  
4HH   HT3  H  N N 51  
4HH   HT2  H  N N 52  
4HH   HR   H  N N 53  
4HH   HU   H  N N 54  
4HH   OXT  O  N N 55  
4HH   HXT  H  N N 56  
A1AMN C10  C  N N 57  
A1AMN C11  C  N N 58  
A1AMN C12  C  N R 59  
A1AMN C14  C  N N 60  
A1AMN C15  C  N N 61  
A1AMN C16  C  N N 62  
A1AMN C02  C  N N 63  
A1AMN C04  C  N N 64  
A1AMN C05  C  N N 65  
A1AMN C07  C  N N 66  
A1AMN C08  C  N N 67  
A1AMN C09  C  N N 68  
A1AMN C22  C  N N 69  
A1AMN C25  C  N N 70  
A1AMN C26  C  N N 71  
A1AMN C27  C  N N 72  
A1AMN C28  C  N N 73  
A1AMN C30  C  N N 74  
A1AMN C50  C  N S 75  
A1AMN N03  N  N N 76  
A1AMN N06  N  N N 77  
A1AMN N10  N  N N 78  
A1AMN N29  N  N N 79  
A1AMN N30  N  N N 80  
A1AMN O01  O  N N 81  
A1AMN O02  O  N N 82  
A1AMN O13  O  N N 83  
A1AMN O17  O  N N 84  
A1AMN O19  O  N N 85  
A1AMN O21  O  N N 86  
A1AMN O23  O  N N 87  
A1AMN O24  O  N N 88  
A1AMN O31  O  N N 89  
A1AMN P18  P  N N 90  
A1AMN H151 H  N N 91  
A1AMN H152 H  N N 92  
A1AMN H153 H  N N 93  
A1AMN H162 H  N N 94  
A1AMN H161 H  N N 95  
A1AMN H042 H  N N 96  
A1AMN H041 H  N N 97  
A1AMN H051 H  N N 98  
A1AMN H052 H  N N 99  
A1AMN H081 H  N N 100 
A1AMN H082 H  N N 101 
A1AMN H091 H  N N 102 
A1AMN H092 H  N N 103 
A1AMN H223 H  N N 104 
A1AMN H222 H  N N 105 
A1AMN H221 H  N N 106 
A1AMN H251 H  N N 107 
A1AMN H252 H  N N 108 
A1AMN H261 H  N N 109 
A1AMN H271 H  N N 110 
A1AMN H272 H  N N 111 
A1AMN H273 H  N N 112 
A1AMN H281 H  N N 113 
A1AMN H283 H  N N 114 
A1AMN H282 H  N N 115 
A1AMN H301 H  N N 116 
A1AMN H302 H  N N 117 
A1AMN H031 H  N N 118 
A1AMN H061 H  N N 119 
A1AMN H101 H  N N 120 
A1AMN H291 H  N N 121 
A1AMN H303 H  N N 122 
A1AMN H131 H  N N 123 
A1AMN H1   H  N N 124 
A1AMN H3   H  N N 125 
A1AMN O1   O  N N 126 
A1AMN H2   H  N N 127 
ALA   N    N  N N 128 
ALA   CA   C  N S 129 
ALA   C    C  N N 130 
ALA   O    O  N N 131 
ALA   CB   C  N N 132 
ALA   OXT  O  N N 133 
ALA   H    H  N N 134 
ALA   H2   H  N N 135 
ALA   HA   H  N N 136 
ALA   HB1  H  N N 137 
ALA   HB2  H  N N 138 
ALA   HB3  H  N N 139 
ALA   HXT  H  N N 140 
ARG   N    N  N N 141 
ARG   CA   C  N S 142 
ARG   C    C  N N 143 
ARG   O    O  N N 144 
ARG   CB   C  N N 145 
ARG   CG   C  N N 146 
ARG   CD   C  N N 147 
ARG   NE   N  N N 148 
ARG   CZ   C  N N 149 
ARG   NH1  N  N N 150 
ARG   NH2  N  N N 151 
ARG   OXT  O  N N 152 
ARG   H    H  N N 153 
ARG   H2   H  N N 154 
ARG   HA   H  N N 155 
ARG   HB2  H  N N 156 
ARG   HB3  H  N N 157 
ARG   HG2  H  N N 158 
ARG   HG3  H  N N 159 
ARG   HD2  H  N N 160 
ARG   HD3  H  N N 161 
ARG   HE   H  N N 162 
ARG   HH11 H  N N 163 
ARG   HH12 H  N N 164 
ARG   HH21 H  N N 165 
ARG   HH22 H  N N 166 
ARG   HXT  H  N N 167 
ASN   N    N  N N 168 
ASN   CA   C  N S 169 
ASN   C    C  N N 170 
ASN   O    O  N N 171 
ASN   CB   C  N N 172 
ASN   CG   C  N N 173 
ASN   OD1  O  N N 174 
ASN   ND2  N  N N 175 
ASN   OXT  O  N N 176 
ASN   H    H  N N 177 
ASN   H2   H  N N 178 
ASN   HA   H  N N 179 
ASN   HB2  H  N N 180 
ASN   HB3  H  N N 181 
ASN   HD21 H  N N 182 
ASN   HD22 H  N N 183 
ASN   HXT  H  N N 184 
ASP   N    N  N N 185 
ASP   CA   C  N S 186 
ASP   C    C  N N 187 
ASP   O    O  N N 188 
ASP   CB   C  N N 189 
ASP   CG   C  N N 190 
ASP   OD1  O  N N 191 
ASP   OD2  O  N N 192 
ASP   OXT  O  N N 193 
ASP   H    H  N N 194 
ASP   H2   H  N N 195 
ASP   HA   H  N N 196 
ASP   HB2  H  N N 197 
ASP   HB3  H  N N 198 
ASP   HD2  H  N N 199 
ASP   HXT  H  N N 200 
CYS   N    N  N N 201 
CYS   CA   C  N R 202 
CYS   C    C  N N 203 
CYS   O    O  N N 204 
CYS   CB   C  N N 205 
CYS   SG   S  N N 206 
CYS   OXT  O  N N 207 
CYS   H    H  N N 208 
CYS   H2   H  N N 209 
CYS   HA   H  N N 210 
CYS   HB2  H  N N 211 
CYS   HB3  H  N N 212 
CYS   HG   H  N N 213 
CYS   HXT  H  N N 214 
GLN   N    N  N N 215 
GLN   CA   C  N S 216 
GLN   C    C  N N 217 
GLN   O    O  N N 218 
GLN   CB   C  N N 219 
GLN   CG   C  N N 220 
GLN   CD   C  N N 221 
GLN   OE1  O  N N 222 
GLN   NE2  N  N N 223 
GLN   OXT  O  N N 224 
GLN   H    H  N N 225 
GLN   H2   H  N N 226 
GLN   HA   H  N N 227 
GLN   HB2  H  N N 228 
GLN   HB3  H  N N 229 
GLN   HG2  H  N N 230 
GLN   HG3  H  N N 231 
GLN   HE21 H  N N 232 
GLN   HE22 H  N N 233 
GLN   HXT  H  N N 234 
GLU   N    N  N N 235 
GLU   CA   C  N S 236 
GLU   C    C  N N 237 
GLU   O    O  N N 238 
GLU   CB   C  N N 239 
GLU   CG   C  N N 240 
GLU   CD   C  N N 241 
GLU   OE1  O  N N 242 
GLU   OE2  O  N N 243 
GLU   OXT  O  N N 244 
GLU   H    H  N N 245 
GLU   H2   H  N N 246 
GLU   HA   H  N N 247 
GLU   HB2  H  N N 248 
GLU   HB3  H  N N 249 
GLU   HG2  H  N N 250 
GLU   HG3  H  N N 251 
GLU   HE2  H  N N 252 
GLU   HXT  H  N N 253 
GLY   N    N  N N 254 
GLY   CA   C  N N 255 
GLY   C    C  N N 256 
GLY   O    O  N N 257 
GLY   OXT  O  N N 258 
GLY   H    H  N N 259 
GLY   H2   H  N N 260 
GLY   HA2  H  N N 261 
GLY   HA3  H  N N 262 
GLY   HXT  H  N N 263 
GOL   C1   C  N N 264 
GOL   O1   O  N N 265 
GOL   C2   C  N N 266 
GOL   O2   O  N N 267 
GOL   C3   C  N N 268 
GOL   O3   O  N N 269 
GOL   H11  H  N N 270 
GOL   H12  H  N N 271 
GOL   HO1  H  N N 272 
GOL   H2   H  N N 273 
GOL   HO2  H  N N 274 
GOL   H31  H  N N 275 
GOL   H32  H  N N 276 
GOL   HO3  H  N N 277 
HIS   N    N  N N 278 
HIS   CA   C  N S 279 
HIS   C    C  N N 280 
HIS   O    O  N N 281 
HIS   CB   C  N N 282 
HIS   CG   C  Y N 283 
HIS   ND1  N  Y N 284 
HIS   CD2  C  Y N 285 
HIS   CE1  C  Y N 286 
HIS   NE2  N  Y N 287 
HIS   OXT  O  N N 288 
HIS   H    H  N N 289 
HIS   H2   H  N N 290 
HIS   HA   H  N N 291 
HIS   HB2  H  N N 292 
HIS   HB3  H  N N 293 
HIS   HD1  H  N N 294 
HIS   HD2  H  N N 295 
HIS   HE1  H  N N 296 
HIS   HE2  H  N N 297 
HIS   HXT  H  N N 298 
HOH   O    O  N N 299 
HOH   H1   H  N N 300 
HOH   H2   H  N N 301 
ILE   N    N  N N 302 
ILE   CA   C  N S 303 
ILE   C    C  N N 304 
ILE   O    O  N N 305 
ILE   CB   C  N S 306 
ILE   CG1  C  N N 307 
ILE   CG2  C  N N 308 
ILE   CD1  C  N N 309 
ILE   OXT  O  N N 310 
ILE   H    H  N N 311 
ILE   H2   H  N N 312 
ILE   HA   H  N N 313 
ILE   HB   H  N N 314 
ILE   HG12 H  N N 315 
ILE   HG13 H  N N 316 
ILE   HG21 H  N N 317 
ILE   HG22 H  N N 318 
ILE   HG23 H  N N 319 
ILE   HD11 H  N N 320 
ILE   HD12 H  N N 321 
ILE   HD13 H  N N 322 
ILE   HXT  H  N N 323 
LEU   N    N  N N 324 
LEU   CA   C  N S 325 
LEU   C    C  N N 326 
LEU   O    O  N N 327 
LEU   CB   C  N N 328 
LEU   CG   C  N N 329 
LEU   CD1  C  N N 330 
LEU   CD2  C  N N 331 
LEU   OXT  O  N N 332 
LEU   H    H  N N 333 
LEU   H2   H  N N 334 
LEU   HA   H  N N 335 
LEU   HB2  H  N N 336 
LEU   HB3  H  N N 337 
LEU   HG   H  N N 338 
LEU   HD11 H  N N 339 
LEU   HD12 H  N N 340 
LEU   HD13 H  N N 341 
LEU   HD21 H  N N 342 
LEU   HD22 H  N N 343 
LEU   HD23 H  N N 344 
LEU   HXT  H  N N 345 
LYS   N    N  N N 346 
LYS   CA   C  N S 347 
LYS   C    C  N N 348 
LYS   O    O  N N 349 
LYS   CB   C  N N 350 
LYS   CG   C  N N 351 
LYS   CD   C  N N 352 
LYS   CE   C  N N 353 
LYS   NZ   N  N N 354 
LYS   OXT  O  N N 355 
LYS   H    H  N N 356 
LYS   H2   H  N N 357 
LYS   HA   H  N N 358 
LYS   HB2  H  N N 359 
LYS   HB3  H  N N 360 
LYS   HG2  H  N N 361 
LYS   HG3  H  N N 362 
LYS   HD2  H  N N 363 
LYS   HD3  H  N N 364 
LYS   HE2  H  N N 365 
LYS   HE3  H  N N 366 
LYS   HZ1  H  N N 367 
LYS   HZ2  H  N N 368 
LYS   HZ3  H  N N 369 
LYS   HXT  H  N N 370 
MET   N    N  N N 371 
MET   CA   C  N S 372 
MET   C    C  N N 373 
MET   O    O  N N 374 
MET   CB   C  N N 375 
MET   CG   C  N N 376 
MET   SD   S  N N 377 
MET   CE   C  N N 378 
MET   OXT  O  N N 379 
MET   H    H  N N 380 
MET   H2   H  N N 381 
MET   HA   H  N N 382 
MET   HB2  H  N N 383 
MET   HB3  H  N N 384 
MET   HG2  H  N N 385 
MET   HG3  H  N N 386 
MET   HE1  H  N N 387 
MET   HE2  H  N N 388 
MET   HE3  H  N N 389 
MET   HXT  H  N N 390 
MN    MN   MN N N 391 
PHE   N    N  N N 392 
PHE   CA   C  N S 393 
PHE   C    C  N N 394 
PHE   O    O  N N 395 
PHE   CB   C  N N 396 
PHE   CG   C  Y N 397 
PHE   CD1  C  Y N 398 
PHE   CD2  C  Y N 399 
PHE   CE1  C  Y N 400 
PHE   CE2  C  Y N 401 
PHE   CZ   C  Y N 402 
PHE   OXT  O  N N 403 
PHE   H    H  N N 404 
PHE   H2   H  N N 405 
PHE   HA   H  N N 406 
PHE   HB2  H  N N 407 
PHE   HB3  H  N N 408 
PHE   HD1  H  N N 409 
PHE   HD2  H  N N 410 
PHE   HE1  H  N N 411 
PHE   HE2  H  N N 412 
PHE   HZ   H  N N 413 
PHE   HXT  H  N N 414 
PRO   N    N  N N 415 
PRO   CA   C  N S 416 
PRO   C    C  N N 417 
PRO   O    O  N N 418 
PRO   CB   C  N N 419 
PRO   CG   C  N N 420 
PRO   CD   C  N N 421 
PRO   OXT  O  N N 422 
PRO   H    H  N N 423 
PRO   HA   H  N N 424 
PRO   HB2  H  N N 425 
PRO   HB3  H  N N 426 
PRO   HG2  H  N N 427 
PRO   HG3  H  N N 428 
PRO   HD2  H  N N 429 
PRO   HD3  H  N N 430 
PRO   HXT  H  N N 431 
SER   N    N  N N 432 
SER   CA   C  N S 433 
SER   C    C  N N 434 
SER   O    O  N N 435 
SER   CB   C  N N 436 
SER   OG   O  N N 437 
SER   OXT  O  N N 438 
SER   H    H  N N 439 
SER   H2   H  N N 440 
SER   HA   H  N N 441 
SER   HB2  H  N N 442 
SER   HB3  H  N N 443 
SER   HG   H  N N 444 
SER   HXT  H  N N 445 
THR   N    N  N N 446 
THR   CA   C  N S 447 
THR   C    C  N N 448 
THR   O    O  N N 449 
THR   CB   C  N R 450 
THR   OG1  O  N N 451 
THR   CG2  C  N N 452 
THR   OXT  O  N N 453 
THR   H    H  N N 454 
THR   H2   H  N N 455 
THR   HA   H  N N 456 
THR   HB   H  N N 457 
THR   HG1  H  N N 458 
THR   HG21 H  N N 459 
THR   HG22 H  N N 460 
THR   HG23 H  N N 461 
THR   HXT  H  N N 462 
TRP   N    N  N N 463 
TRP   CA   C  N S 464 
TRP   C    C  N N 465 
TRP   O    O  N N 466 
TRP   CB   C  N N 467 
TRP   CG   C  Y N 468 
TRP   CD1  C  Y N 469 
TRP   CD2  C  Y N 470 
TRP   NE1  N  Y N 471 
TRP   CE2  C  Y N 472 
TRP   CE3  C  Y N 473 
TRP   CZ2  C  Y N 474 
TRP   CZ3  C  Y N 475 
TRP   CH2  C  Y N 476 
TRP   OXT  O  N N 477 
TRP   H    H  N N 478 
TRP   H2   H  N N 479 
TRP   HA   H  N N 480 
TRP   HB2  H  N N 481 
TRP   HB3  H  N N 482 
TRP   HD1  H  N N 483 
TRP   HE1  H  N N 484 
TRP   HE3  H  N N 485 
TRP   HZ2  H  N N 486 
TRP   HZ3  H  N N 487 
TRP   HH2  H  N N 488 
TRP   HXT  H  N N 489 
TYR   N    N  N N 490 
TYR   CA   C  N S 491 
TYR   C    C  N N 492 
TYR   O    O  N N 493 
TYR   CB   C  N N 494 
TYR   CG   C  Y N 495 
TYR   CD1  C  Y N 496 
TYR   CD2  C  Y N 497 
TYR   CE1  C  Y N 498 
TYR   CE2  C  Y N 499 
TYR   CZ   C  Y N 500 
TYR   OH   O  N N 501 
TYR   OXT  O  N N 502 
TYR   H    H  N N 503 
TYR   H2   H  N N 504 
TYR   HA   H  N N 505 
TYR   HB2  H  N N 506 
TYR   HB3  H  N N 507 
TYR   HD1  H  N N 508 
TYR   HD2  H  N N 509 
TYR   HE1  H  N N 510 
TYR   HE2  H  N N 511 
TYR   HH   H  N N 512 
TYR   HXT  H  N N 513 
VAL   N    N  N N 514 
VAL   CA   C  N S 515 
VAL   C    C  N N 516 
VAL   O    O  N N 517 
VAL   CB   C  N N 518 
VAL   CG1  C  N N 519 
VAL   CG2  C  N N 520 
VAL   OXT  O  N N 521 
VAL   H    H  N N 522 
VAL   H2   H  N N 523 
VAL   HA   H  N N 524 
VAL   HB   H  N N 525 
VAL   HG11 H  N N 526 
VAL   HG12 H  N N 527 
VAL   HG13 H  N N 528 
VAL   HG21 H  N N 529 
VAL   HG22 H  N N 530 
VAL   HG23 H  N N 531 
VAL   HXT  H  N N 532 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
4HH   SU  CT   sing N N 1   
4HH   CB  CA   sing N N 2   
4HH   CB  OG   sing N N 3   
4HH   CL1 CK   sing N N 4   
4HH   CT  CS   sing N N 5   
4HH   CA  N    sing N N 6   
4HH   CA  C    sing N N 7   
4HH   O2P P    doub N N 8   
4HH   O   C    doub N N 9   
4HH   CS  NR   sing N N 10  
4HH   O3P P    sing N N 11  
4HH   O3P CJ   sing N N 12  
4HH   OG  P    sing N N 13  
4HH   P   O1P  sing N N 14  
4HH   CK  CL2  sing N N 15  
4HH   CK  CJ   sing N N 16  
4HH   CK  CM   sing N N 17  
4HH   CP  CQ   sing N N 18  
4HH   CP  CO   sing N N 19  
4HH   NN  CL3  sing N N 20  
4HH   NN  CO   sing N N 21  
4HH   NR  CQ   sing N N 22  
4HH   CL3 CM   sing N N 23  
4HH   CL3 ON   doub N N 24  
4HH   CQ  OR   doub N N 25  
4HH   CM  OM   sing N N 26  
4HH   CA  HA   sing N N 27  
4HH   N   H    sing N N 28  
4HH   N   H2   sing N N 29  
4HH   CB  HB3  sing N N 30  
4HH   CB  HB2  sing N N 31  
4HH   CJ  HJ3  sing N N 32  
4HH   CJ  HJ2  sing N N 33  
4HH   CL1 HL13 sing N N 34  
4HH   CL1 HL12 sing N N 35  
4HH   CL1 HL11 sing N N 36  
4HH   CL2 HL21 sing N N 37  
4HH   CL2 HL23 sing N N 38  
4HH   CL2 HL22 sing N N 39  
4HH   CM  HL3  sing N N 40  
4HH   OM  HM   sing N N 41  
4HH   NN  HN   sing N N 42  
4HH   O1P H4   sing N N 43  
4HH   CO  HO2  sing N N 44  
4HH   CO  HO3  sing N N 45  
4HH   CP  HP3  sing N N 46  
4HH   CP  HP2  sing N N 47  
4HH   CS  HS2  sing N N 48  
4HH   CS  HS3  sing N N 49  
4HH   CT  HT3  sing N N 50  
4HH   CT  HT2  sing N N 51  
4HH   NR  HR   sing N N 52  
4HH   SU  HU   sing N N 53  
4HH   C   OXT  sing N N 54  
4HH   OXT HXT  sing N N 55  
A1AMN C02 O01  doub N N 56  
A1AMN C04 N03  sing N N 57  
A1AMN C05 C04  sing N N 58  
A1AMN N06 C05  sing N N 59  
A1AMN C07 N06  sing N N 60  
A1AMN C09 C08  sing N N 61  
A1AMN N10 C09  sing N N 62  
A1AMN C11 N10  sing N N 63  
A1AMN O13 C12  sing N N 64  
A1AMN C14 C12  sing N N 65  
A1AMN C15 C14  sing N N 66  
A1AMN O17 C16  sing N N 67  
A1AMN P18 O17  sing N N 68  
A1AMN O19 P18  sing N N 69  
A1AMN O21 P18  doub N N 70  
A1AMN C16 C14  sing N N 71  
A1AMN C22 C14  sing N N 72  
A1AMN C12 C11  sing N N 73  
A1AMN O23 C11  doub N N 74  
A1AMN C08 C07  sing N N 75  
A1AMN O24 C07  doub N N 76  
A1AMN N03 C02  sing N N 77  
A1AMN C25 C02  sing N N 78  
A1AMN N29 C25  sing N N 79  
A1AMN N29 C10  sing N N 80  
A1AMN C10 O02  doub N N 81  
A1AMN C50 C10  sing N N 82  
A1AMN C26 C50  sing N N 83  
A1AMN C27 C26  sing N N 84  
A1AMN C28 C26  sing N N 85  
A1AMN N30 C50  sing N N 86  
A1AMN C30 N30  sing N N 87  
A1AMN O31 C30  doub N N 88  
A1AMN C15 H151 sing N N 89  
A1AMN C15 H152 sing N N 90  
A1AMN C15 H153 sing N N 91  
A1AMN C16 H162 sing N N 92  
A1AMN C16 H161 sing N N 93  
A1AMN C04 H042 sing N N 94  
A1AMN C04 H041 sing N N 95  
A1AMN C05 H051 sing N N 96  
A1AMN C05 H052 sing N N 97  
A1AMN C08 H081 sing N N 98  
A1AMN C08 H082 sing N N 99  
A1AMN C09 H091 sing N N 100 
A1AMN C09 H092 sing N N 101 
A1AMN C22 H223 sing N N 102 
A1AMN C22 H222 sing N N 103 
A1AMN C22 H221 sing N N 104 
A1AMN C25 H251 sing N N 105 
A1AMN C25 H252 sing N N 106 
A1AMN C26 H261 sing N N 107 
A1AMN C27 H271 sing N N 108 
A1AMN C27 H272 sing N N 109 
A1AMN C27 H273 sing N N 110 
A1AMN C28 H281 sing N N 111 
A1AMN C28 H283 sing N N 112 
A1AMN C28 H282 sing N N 113 
A1AMN C30 H301 sing N N 114 
A1AMN C50 H302 sing N N 115 
A1AMN N03 H031 sing N N 116 
A1AMN N06 H061 sing N N 117 
A1AMN N10 H101 sing N N 118 
A1AMN N29 H291 sing N N 119 
A1AMN N30 H303 sing N N 120 
A1AMN O13 H131 sing N N 121 
A1AMN O19 H1   sing N N 122 
A1AMN C12 H3   sing N N 123 
A1AMN P18 O1   sing N N 124 
A1AMN O1  H2   sing N N 125 
ALA   N   CA   sing N N 126 
ALA   N   H    sing N N 127 
ALA   N   H2   sing N N 128 
ALA   CA  C    sing N N 129 
ALA   CA  CB   sing N N 130 
ALA   CA  HA   sing N N 131 
ALA   C   O    doub N N 132 
ALA   C   OXT  sing N N 133 
ALA   CB  HB1  sing N N 134 
ALA   CB  HB2  sing N N 135 
ALA   CB  HB3  sing N N 136 
ALA   OXT HXT  sing N N 137 
ARG   N   CA   sing N N 138 
ARG   N   H    sing N N 139 
ARG   N   H2   sing N N 140 
ARG   CA  C    sing N N 141 
ARG   CA  CB   sing N N 142 
ARG   CA  HA   sing N N 143 
ARG   C   O    doub N N 144 
ARG   C   OXT  sing N N 145 
ARG   CB  CG   sing N N 146 
ARG   CB  HB2  sing N N 147 
ARG   CB  HB3  sing N N 148 
ARG   CG  CD   sing N N 149 
ARG   CG  HG2  sing N N 150 
ARG   CG  HG3  sing N N 151 
ARG   CD  NE   sing N N 152 
ARG   CD  HD2  sing N N 153 
ARG   CD  HD3  sing N N 154 
ARG   NE  CZ   sing N N 155 
ARG   NE  HE   sing N N 156 
ARG   CZ  NH1  sing N N 157 
ARG   CZ  NH2  doub N N 158 
ARG   NH1 HH11 sing N N 159 
ARG   NH1 HH12 sing N N 160 
ARG   NH2 HH21 sing N N 161 
ARG   NH2 HH22 sing N N 162 
ARG   OXT HXT  sing N N 163 
ASN   N   CA   sing N N 164 
ASN   N   H    sing N N 165 
ASN   N   H2   sing N N 166 
ASN   CA  C    sing N N 167 
ASN   CA  CB   sing N N 168 
ASN   CA  HA   sing N N 169 
ASN   C   O    doub N N 170 
ASN   C   OXT  sing N N 171 
ASN   CB  CG   sing N N 172 
ASN   CB  HB2  sing N N 173 
ASN   CB  HB3  sing N N 174 
ASN   CG  OD1  doub N N 175 
ASN   CG  ND2  sing N N 176 
ASN   ND2 HD21 sing N N 177 
ASN   ND2 HD22 sing N N 178 
ASN   OXT HXT  sing N N 179 
ASP   N   CA   sing N N 180 
ASP   N   H    sing N N 181 
ASP   N   H2   sing N N 182 
ASP   CA  C    sing N N 183 
ASP   CA  CB   sing N N 184 
ASP   CA  HA   sing N N 185 
ASP   C   O    doub N N 186 
ASP   C   OXT  sing N N 187 
ASP   CB  CG   sing N N 188 
ASP   CB  HB2  sing N N 189 
ASP   CB  HB3  sing N N 190 
ASP   CG  OD1  doub N N 191 
ASP   CG  OD2  sing N N 192 
ASP   OD2 HD2  sing N N 193 
ASP   OXT HXT  sing N N 194 
CYS   N   CA   sing N N 195 
CYS   N   H    sing N N 196 
CYS   N   H2   sing N N 197 
CYS   CA  C    sing N N 198 
CYS   CA  CB   sing N N 199 
CYS   CA  HA   sing N N 200 
CYS   C   O    doub N N 201 
CYS   C   OXT  sing N N 202 
CYS   CB  SG   sing N N 203 
CYS   CB  HB2  sing N N 204 
CYS   CB  HB3  sing N N 205 
CYS   SG  HG   sing N N 206 
CYS   OXT HXT  sing N N 207 
GLN   N   CA   sing N N 208 
GLN   N   H    sing N N 209 
GLN   N   H2   sing N N 210 
GLN   CA  C    sing N N 211 
GLN   CA  CB   sing N N 212 
GLN   CA  HA   sing N N 213 
GLN   C   O    doub N N 214 
GLN   C   OXT  sing N N 215 
GLN   CB  CG   sing N N 216 
GLN   CB  HB2  sing N N 217 
GLN   CB  HB3  sing N N 218 
GLN   CG  CD   sing N N 219 
GLN   CG  HG2  sing N N 220 
GLN   CG  HG3  sing N N 221 
GLN   CD  OE1  doub N N 222 
GLN   CD  NE2  sing N N 223 
GLN   NE2 HE21 sing N N 224 
GLN   NE2 HE22 sing N N 225 
GLN   OXT HXT  sing N N 226 
GLU   N   CA   sing N N 227 
GLU   N   H    sing N N 228 
GLU   N   H2   sing N N 229 
GLU   CA  C    sing N N 230 
GLU   CA  CB   sing N N 231 
GLU   CA  HA   sing N N 232 
GLU   C   O    doub N N 233 
GLU   C   OXT  sing N N 234 
GLU   CB  CG   sing N N 235 
GLU   CB  HB2  sing N N 236 
GLU   CB  HB3  sing N N 237 
GLU   CG  CD   sing N N 238 
GLU   CG  HG2  sing N N 239 
GLU   CG  HG3  sing N N 240 
GLU   CD  OE1  doub N N 241 
GLU   CD  OE2  sing N N 242 
GLU   OE2 HE2  sing N N 243 
GLU   OXT HXT  sing N N 244 
GLY   N   CA   sing N N 245 
GLY   N   H    sing N N 246 
GLY   N   H2   sing N N 247 
GLY   CA  C    sing N N 248 
GLY   CA  HA2  sing N N 249 
GLY   CA  HA3  sing N N 250 
GLY   C   O    doub N N 251 
GLY   C   OXT  sing N N 252 
GLY   OXT HXT  sing N N 253 
GOL   C1  O1   sing N N 254 
GOL   C1  C2   sing N N 255 
GOL   C1  H11  sing N N 256 
GOL   C1  H12  sing N N 257 
GOL   O1  HO1  sing N N 258 
GOL   C2  O2   sing N N 259 
GOL   C2  C3   sing N N 260 
GOL   C2  H2   sing N N 261 
GOL   O2  HO2  sing N N 262 
GOL   C3  O3   sing N N 263 
GOL   C3  H31  sing N N 264 
GOL   C3  H32  sing N N 265 
GOL   O3  HO3  sing N N 266 
HIS   N   CA   sing N N 267 
HIS   N   H    sing N N 268 
HIS   N   H2   sing N N 269 
HIS   CA  C    sing N N 270 
HIS   CA  CB   sing N N 271 
HIS   CA  HA   sing N N 272 
HIS   C   O    doub N N 273 
HIS   C   OXT  sing N N 274 
HIS   CB  CG   sing N N 275 
HIS   CB  HB2  sing N N 276 
HIS   CB  HB3  sing N N 277 
HIS   CG  ND1  sing Y N 278 
HIS   CG  CD2  doub Y N 279 
HIS   ND1 CE1  doub Y N 280 
HIS   ND1 HD1  sing N N 281 
HIS   CD2 NE2  sing Y N 282 
HIS   CD2 HD2  sing N N 283 
HIS   CE1 NE2  sing Y N 284 
HIS   CE1 HE1  sing N N 285 
HIS   NE2 HE2  sing N N 286 
HIS   OXT HXT  sing N N 287 
HOH   O   H1   sing N N 288 
HOH   O   H2   sing N N 289 
ILE   N   CA   sing N N 290 
ILE   N   H    sing N N 291 
ILE   N   H2   sing N N 292 
ILE   CA  C    sing N N 293 
ILE   CA  CB   sing N N 294 
ILE   CA  HA   sing N N 295 
ILE   C   O    doub N N 296 
ILE   C   OXT  sing N N 297 
ILE   CB  CG1  sing N N 298 
ILE   CB  CG2  sing N N 299 
ILE   CB  HB   sing N N 300 
ILE   CG1 CD1  sing N N 301 
ILE   CG1 HG12 sing N N 302 
ILE   CG1 HG13 sing N N 303 
ILE   CG2 HG21 sing N N 304 
ILE   CG2 HG22 sing N N 305 
ILE   CG2 HG23 sing N N 306 
ILE   CD1 HD11 sing N N 307 
ILE   CD1 HD12 sing N N 308 
ILE   CD1 HD13 sing N N 309 
ILE   OXT HXT  sing N N 310 
LEU   N   CA   sing N N 311 
LEU   N   H    sing N N 312 
LEU   N   H2   sing N N 313 
LEU   CA  C    sing N N 314 
LEU   CA  CB   sing N N 315 
LEU   CA  HA   sing N N 316 
LEU   C   O    doub N N 317 
LEU   C   OXT  sing N N 318 
LEU   CB  CG   sing N N 319 
LEU   CB  HB2  sing N N 320 
LEU   CB  HB3  sing N N 321 
LEU   CG  CD1  sing N N 322 
LEU   CG  CD2  sing N N 323 
LEU   CG  HG   sing N N 324 
LEU   CD1 HD11 sing N N 325 
LEU   CD1 HD12 sing N N 326 
LEU   CD1 HD13 sing N N 327 
LEU   CD2 HD21 sing N N 328 
LEU   CD2 HD22 sing N N 329 
LEU   CD2 HD23 sing N N 330 
LEU   OXT HXT  sing N N 331 
LYS   N   CA   sing N N 332 
LYS   N   H    sing N N 333 
LYS   N   H2   sing N N 334 
LYS   CA  C    sing N N 335 
LYS   CA  CB   sing N N 336 
LYS   CA  HA   sing N N 337 
LYS   C   O    doub N N 338 
LYS   C   OXT  sing N N 339 
LYS   CB  CG   sing N N 340 
LYS   CB  HB2  sing N N 341 
LYS   CB  HB3  sing N N 342 
LYS   CG  CD   sing N N 343 
LYS   CG  HG2  sing N N 344 
LYS   CG  HG3  sing N N 345 
LYS   CD  CE   sing N N 346 
LYS   CD  HD2  sing N N 347 
LYS   CD  HD3  sing N N 348 
LYS   CE  NZ   sing N N 349 
LYS   CE  HE2  sing N N 350 
LYS   CE  HE3  sing N N 351 
LYS   NZ  HZ1  sing N N 352 
LYS   NZ  HZ2  sing N N 353 
LYS   NZ  HZ3  sing N N 354 
LYS   OXT HXT  sing N N 355 
MET   N   CA   sing N N 356 
MET   N   H    sing N N 357 
MET   N   H2   sing N N 358 
MET   CA  C    sing N N 359 
MET   CA  CB   sing N N 360 
MET   CA  HA   sing N N 361 
MET   C   O    doub N N 362 
MET   C   OXT  sing N N 363 
MET   CB  CG   sing N N 364 
MET   CB  HB2  sing N N 365 
MET   CB  HB3  sing N N 366 
MET   CG  SD   sing N N 367 
MET   CG  HG2  sing N N 368 
MET   CG  HG3  sing N N 369 
MET   SD  CE   sing N N 370 
MET   CE  HE1  sing N N 371 
MET   CE  HE2  sing N N 372 
MET   CE  HE3  sing N N 373 
MET   OXT HXT  sing N N 374 
PHE   N   CA   sing N N 375 
PHE   N   H    sing N N 376 
PHE   N   H2   sing N N 377 
PHE   CA  C    sing N N 378 
PHE   CA  CB   sing N N 379 
PHE   CA  HA   sing N N 380 
PHE   C   O    doub N N 381 
PHE   C   OXT  sing N N 382 
PHE   CB  CG   sing N N 383 
PHE   CB  HB2  sing N N 384 
PHE   CB  HB3  sing N N 385 
PHE   CG  CD1  doub Y N 386 
PHE   CG  CD2  sing Y N 387 
PHE   CD1 CE1  sing Y N 388 
PHE   CD1 HD1  sing N N 389 
PHE   CD2 CE2  doub Y N 390 
PHE   CD2 HD2  sing N N 391 
PHE   CE1 CZ   doub Y N 392 
PHE   CE1 HE1  sing N N 393 
PHE   CE2 CZ   sing Y N 394 
PHE   CE2 HE2  sing N N 395 
PHE   CZ  HZ   sing N N 396 
PHE   OXT HXT  sing N N 397 
PRO   N   CA   sing N N 398 
PRO   N   CD   sing N N 399 
PRO   N   H    sing N N 400 
PRO   CA  C    sing N N 401 
PRO   CA  CB   sing N N 402 
PRO   CA  HA   sing N N 403 
PRO   C   O    doub N N 404 
PRO   C   OXT  sing N N 405 
PRO   CB  CG   sing N N 406 
PRO   CB  HB2  sing N N 407 
PRO   CB  HB3  sing N N 408 
PRO   CG  CD   sing N N 409 
PRO   CG  HG2  sing N N 410 
PRO   CG  HG3  sing N N 411 
PRO   CD  HD2  sing N N 412 
PRO   CD  HD3  sing N N 413 
PRO   OXT HXT  sing N N 414 
SER   N   CA   sing N N 415 
SER   N   H    sing N N 416 
SER   N   H2   sing N N 417 
SER   CA  C    sing N N 418 
SER   CA  CB   sing N N 419 
SER   CA  HA   sing N N 420 
SER   C   O    doub N N 421 
SER   C   OXT  sing N N 422 
SER   CB  OG   sing N N 423 
SER   CB  HB2  sing N N 424 
SER   CB  HB3  sing N N 425 
SER   OG  HG   sing N N 426 
SER   OXT HXT  sing N N 427 
THR   N   CA   sing N N 428 
THR   N   H    sing N N 429 
THR   N   H2   sing N N 430 
THR   CA  C    sing N N 431 
THR   CA  CB   sing N N 432 
THR   CA  HA   sing N N 433 
THR   C   O    doub N N 434 
THR   C   OXT  sing N N 435 
THR   CB  OG1  sing N N 436 
THR   CB  CG2  sing N N 437 
THR   CB  HB   sing N N 438 
THR   OG1 HG1  sing N N 439 
THR   CG2 HG21 sing N N 440 
THR   CG2 HG22 sing N N 441 
THR   CG2 HG23 sing N N 442 
THR   OXT HXT  sing N N 443 
TRP   N   CA   sing N N 444 
TRP   N   H    sing N N 445 
TRP   N   H2   sing N N 446 
TRP   CA  C    sing N N 447 
TRP   CA  CB   sing N N 448 
TRP   CA  HA   sing N N 449 
TRP   C   O    doub N N 450 
TRP   C   OXT  sing N N 451 
TRP   CB  CG   sing N N 452 
TRP   CB  HB2  sing N N 453 
TRP   CB  HB3  sing N N 454 
TRP   CG  CD1  doub Y N 455 
TRP   CG  CD2  sing Y N 456 
TRP   CD1 NE1  sing Y N 457 
TRP   CD1 HD1  sing N N 458 
TRP   CD2 CE2  doub Y N 459 
TRP   CD2 CE3  sing Y N 460 
TRP   NE1 CE2  sing Y N 461 
TRP   NE1 HE1  sing N N 462 
TRP   CE2 CZ2  sing Y N 463 
TRP   CE3 CZ3  doub Y N 464 
TRP   CE3 HE3  sing N N 465 
TRP   CZ2 CH2  doub Y N 466 
TRP   CZ2 HZ2  sing N N 467 
TRP   CZ3 CH2  sing Y N 468 
TRP   CZ3 HZ3  sing N N 469 
TRP   CH2 HH2  sing N N 470 
TRP   OXT HXT  sing N N 471 
TYR   N   CA   sing N N 472 
TYR   N   H    sing N N 473 
TYR   N   H2   sing N N 474 
TYR   CA  C    sing N N 475 
TYR   CA  CB   sing N N 476 
TYR   CA  HA   sing N N 477 
TYR   C   O    doub N N 478 
TYR   C   OXT  sing N N 479 
TYR   CB  CG   sing N N 480 
TYR   CB  HB2  sing N N 481 
TYR   CB  HB3  sing N N 482 
TYR   CG  CD1  doub Y N 483 
TYR   CG  CD2  sing Y N 484 
TYR   CD1 CE1  sing Y N 485 
TYR   CD1 HD1  sing N N 486 
TYR   CD2 CE2  doub Y N 487 
TYR   CD2 HD2  sing N N 488 
TYR   CE1 CZ   doub Y N 489 
TYR   CE1 HE1  sing N N 490 
TYR   CE2 CZ   sing Y N 491 
TYR   CE2 HE2  sing N N 492 
TYR   CZ  OH   sing N N 493 
TYR   OH  HH   sing N N 494 
TYR   OXT HXT  sing N N 495 
VAL   N   CA   sing N N 496 
VAL   N   H    sing N N 497 
VAL   N   H2   sing N N 498 
VAL   CA  C    sing N N 499 
VAL   CA  CB   sing N N 500 
VAL   CA  HA   sing N N 501 
VAL   C   O    doub N N 502 
VAL   C   OXT  sing N N 503 
VAL   CB  CG1  sing N N 504 
VAL   CB  CG2  sing N N 505 
VAL   CB  HB   sing N N 506 
VAL   CG1 HG11 sing N N 507 
VAL   CG1 HG12 sing N N 508 
VAL   CG1 HG13 sing N N 509 
VAL   CG2 HG21 sing N N 510 
VAL   CG2 HG22 sing N N 511 
VAL   CG2 HG23 sing N N 512 
VAL   OXT HXT  sing N N 513 
# 
_pdbx_audit_support.funding_organization   'Canadian Institutes of Health Research (CIHR)' 
_pdbx_audit_support.country                Canada 
_pdbx_audit_support.grant_number           PJT-178084 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6MFZ 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 2' 
_space_group.name_Hall        'P 2 2ab' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BE4 
_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]   0.005423 
_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]   0.002344 
_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]   0.012937 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MN  ? ? 20.23591 4.67902 ? ? 2.76514  44.01191 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 6.96715  ?       ? ? 11.43723 ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 7.96527  ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366  3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P   ? ? 9.51135  5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . MET   A 1 1    ? -80.90900  49.47400  28.58100  1.000 74.15593  ?  1    MET   A N   1 
ATOM   2     C  CA  . MET   A 1 1    ? -80.85300  50.89600  28.26400  1.000 79.23367  ?  1    MET   A CA  1 
ATOM   3     C  C   . MET   A 1 1    ? -80.95200  51.74300  29.52800  1.000 90.72776  ?  1    MET   A C   1 
ATOM   4     O  O   . MET   A 1 1    ? -81.34700  51.25200  30.58600  1.000 105.24219 ?  1    MET   A O   1 
ATOM   5     C  CB  . MET   A 1 1    ? -81.97000  51.27300  27.28900  1.000 77.96198  ?  1    MET   A CB  1 
ATOM   6     N  N   . GLY   A 1 2    ? -80.59300  53.01500  29.41000  1.000 82.13211  ?  2    GLY   A N   1 
ATOM   7     C  CA  . GLY   A 1 2    ? -80.64700  53.91700  30.54300  1.000 59.49167  ?  2    GLY   A CA  1 
ATOM   8     C  C   . GLY   A 1 2    ? -80.34700  55.33500  30.11700  1.000 61.73195  ?  2    GLY   A C   1 
ATOM   9     O  O   . GLY   A 1 2    ? -79.71800  55.57600  29.08100  1.000 67.36713  ?  2    GLY   A O   1 
ATOM   10    N  N   . ARG   A 1 3    ? -80.81100  56.27400  30.93600  1.000 57.48642  ?  3    ARG   A N   1 
ATOM   11    C  CA  . ARG   A 1 3    ? -80.59100  57.68900  30.67600  1.000 61.37061  ?  3    ARG   A CA  1 
ATOM   12    C  C   . ARG   A 1 3    ? -79.19500  58.08300  31.14300  1.000 54.48147  ?  3    ARG   A C   1 
ATOM   13    O  O   . ARG   A 1 3    ? -78.77400  57.71800  32.24500  1.000 50.73109  ?  3    ARG   A O   1 
ATOM   14    C  CB  . ARG   A 1 3    ? -81.65500  58.52500  31.38400  1.000 62.28468  ?  3    ARG   A CB  1 
ATOM   15    C  CG  . ARG   A 1 3    ? -82.17900  59.70400  30.58300  1.000 64.13541  ?  3    ARG   A CG  1 
ATOM   16    C  CD  . ARG   A 1 3    ? -83.53700  60.14500  31.11100  1.000 54.46969  ?  3    ARG   A CD  1 
ATOM   17    N  NE  . ARG   A 1 3    ? -83.97700  61.40700  30.52900  1.000 64.74327  ?  3    ARG   A NE  1 
ATOM   18    C  CZ  . ARG   A 1 3    ? -83.79900  62.59300  31.09600  1.000 74.30642  ?  3    ARG   A CZ  1 
ATOM   19    N  NH1 . ARG   A 1 3    ? -83.19400  62.71600  32.26600  1.000 52.85493  ?  3    ARG   A NH1 1 
ATOM   20    N  NH2 . ARG   A 1 3    ? -84.24200  63.68300  30.47400  1.000 68.19531  ?  3    ARG   A NH2 1 
ATOM   21    N  N   . ILE   A 1 4    ? -78.47300  58.81500  30.29700  1.000 54.54744  ?  4    ILE   A N   1 
ATOM   22    C  CA  . ILE   A 1 4    ? -77.10100  59.22200  30.57500  1.000 51.41790  ?  4    ILE   A CA  1 
ATOM   23    C  C   . ILE   A 1 4    ? -77.00100  60.72900  30.40500  1.000 49.79259  ?  4    ILE   A C   1 
ATOM   24    O  O   . ILE   A 1 4    ? -77.46400  61.27500  29.39700  1.000 61.52919  ?  4    ILE   A O   1 
ATOM   25    C  CB  . ILE   A 1 4    ? -76.09300  58.51600  29.65000  1.000 50.98099  ?  4    ILE   A CB  1 
ATOM   26    C  CG1 . ILE   A 1 4    ? -76.46500  57.04500  29.47200  1.000 53.15729  ?  4    ILE   A CG1 1 
ATOM   27    C  CG2 . ILE   A 1 4    ? -74.68100  58.64200  30.20400  1.000 55.98879  ?  4    ILE   A CG2 1 
ATOM   28    C  CD1 . ILE   A 1 4    ? -75.88700  56.43200  28.22200  1.000 57.65262  ?  4    ILE   A CD1 1 
ATOM   29    N  N   . LEU   A 1 5    ? -76.39700  61.39700  31.38200  1.000 46.51326  ?  5    LEU   A N   1 
ATOM   30    C  CA  . LEU   A 1 5    ? -76.12900  62.83000  31.30600  1.000 48.31929  ?  5    LEU   A CA  1 
ATOM   31    C  C   . LEU   A 1 5    ? -74.67900  63.00600  30.87000  1.000 62.66123  ?  5    LEU   A C   1 
ATOM   32    O  O   . LEU   A 1 5    ? -73.75400  62.82600  31.66700  1.000 70.55634  ?  5    LEU   A O   1 
ATOM   33    C  CB  . LEU   A 1 5    ? -76.39500  63.50900  32.64400  1.000 34.08447  ?  5    LEU   A CB  1 
ATOM   34    C  CG  . LEU   A 1 5    ? -75.96500  64.97600  32.70800  1.000 51.18069  ?  5    LEU   A CG  1 
ATOM   35    C  CD1 . LEU   A 1 5    ? -76.84300  65.83800  31.81000  1.000 59.23194  ?  5    LEU   A CD1 1 
ATOM   36    C  CD2 . LEU   A 1 5    ? -75.97500  65.48400  34.14100  1.000 67.00609  ?  5    LEU   A CD2 1 
ATOM   37    N  N   . PHE   A 1 6    ? -74.47900  63.35300  29.60200  1.000 46.35830  ?  6    PHE   A N   1 
ATOM   38    C  CA  . PHE   A 1 6    ? -73.14000  63.55800  29.07000  1.000 37.40342  ?  6    PHE   A CA  1 
ATOM   39    C  C   . PHE   A 1 6    ? -72.70600  64.99300  29.34100  1.000 48.03365  ?  6    PHE   A C   1 
ATOM   40    O  O   . PHE   A 1 6    ? -73.31300  65.94000  28.82800  1.000 46.47973  ?  6    PHE   A O   1 
ATOM   41    C  CB  . PHE   A 1 6    ? -73.08500  63.25300  27.57500  1.000 41.56000  ?  6    PHE   A CB  1 
ATOM   42    C  CG  . PHE   A 1 6    ? -71.69200  63.11400  27.05000  1.000 42.75571  ?  6    PHE   A CG  1 
ATOM   43    C  CD1 . PHE   A 1 6    ? -71.01800  61.90900  27.15600  1.000 38.87977  ?  6    PHE   A CD1 1 
ATOM   44    C  CD2 . PHE   A 1 6    ? -71.04400  64.19100  26.47400  1.000 47.87950  ?  6    PHE   A CD2 1 
ATOM   45    C  CE1 . PHE   A 1 6    ? -69.73100  61.77800  26.68400  1.000 46.53293  ?  6    PHE   A CE1 1 
ATOM   46    C  CE2 . PHE   A 1 6    ? -69.75500  64.06700  26.00200  1.000 41.94689  ?  6    PHE   A CE2 1 
ATOM   47    C  CZ  . PHE   A 1 6    ? -69.09800  62.86000  26.10600  1.000 43.61214  ?  6    PHE   A CZ  1 
ATOM   48    N  N   . LEU   A 1 7    ? -71.65500  65.14900  30.14100  1.000 52.52159  ?  7    LEU   A N   1 
ATOM   49    C  CA  . LEU   A 1 7    ? -71.16000  66.45400  30.56500  1.000 52.11813  ?  7    LEU   A CA  1 
ATOM   50    C  C   . LEU   A 1 7    ? -69.87100  66.75400  29.81300  1.000 48.16073  ?  7    LEU   A C   1 
ATOM   51    O  O   . LEU   A 1 7    ? -68.83500  66.13200  30.07300  1.000 46.19399  ?  7    LEU   A O   1 
ATOM   52    C  CB  . LEU   A 1 7    ? -70.93000  66.47900  32.07400  1.000 53.95030  ?  7    LEU   A CB  1 
ATOM   53    C  CG  . LEU   A 1 7    ? -72.15100  66.22100  32.95400  1.000 58.07850  ?  7    LEU   A CG  1 
ATOM   54    C  CD1 . LEU   A 1 7    ? -71.71100  65.97100  34.38100  1.000 61.51490  ?  7    LEU   A CD1 1 
ATOM   55    C  CD2 . LEU   A 1 7    ? -73.10400  67.40000  32.89200  1.000 59.91646  ?  7    LEU   A CD2 1 
ATOM   56    N  N   . THR   A 1 8    ? -69.93500  67.70800  28.88800  1.000 53.87386  ?  8    THR   A N   1 
ATOM   57    C  CA  . THR   A 1 8    ? -68.77100  68.13300  28.12600  1.000 48.03059  ?  8    THR   A CA  1 
ATOM   58    C  C   . THR   A 1 8    ? -68.79700  69.64400  27.96800  1.000 49.73960  ?  8    THR   A C   1 
ATOM   59    O  O   . THR   A 1 8    ? -69.85200  70.23000  27.71700  1.000 57.72292  ?  8    THR   A O   1 
ATOM   60    C  CB  . THR   A 1 8    ? -68.72600  67.47300  26.74400  1.000 36.97279  ?  8    THR   A CB  1 
ATOM   61    O  OG1 . THR   A 1 8    ? -67.74100  68.13200  25.94300  1.000 67.07124  ?  8    THR   A OG1 1 
ATOM   62    C  CG2 . THR   A 1 8    ? -70.07700  67.58000  26.05600  1.000 47.99221  ?  8    THR   A CG2 1 
ATOM   63    N  N   . THR   A 1 9    ? -67.63400  70.27300  28.11300  1.000 43.53631  ?  9    THR   A N   1 
ATOM   64    C  CA  . THR   A 1 9    ? -67.52000  71.71800  27.95300  1.000 47.64259  ?  9    THR   A CA  1 
ATOM   65    C  C   . THR   A 1 9    ? -66.59500  72.10200  26.81200  1.000 55.08766  ?  9    THR   A C   1 
ATOM   66    O  O   . THR   A 1 9    ? -66.95400  72.94700  25.98300  1.000 66.65298  ?  9    THR   A O   1 
ATOM   67    C  CB  . THR   A 1 9    ? -67.02800  72.36300  29.25600  1.000 50.73766  ?  9    THR   A CB  1 
ATOM   68    O  OG1 . THR   A 1 9    ? -67.83700  71.91300  30.34900  1.000 76.41697  ?  9    THR   A OG1 1 
ATOM   69    C  CG2 . THR   A 1 9    ? -67.10500  73.88200  29.16100  1.000 48.35674  ?  9    THR   A CG2 1 
ATOM   70    N  N   . PHE   A 1 10   ? -65.40900  71.50400  26.74800  1.000 59.47332  ?  10   PHE   A N   1 
ATOM   71    C  CA  . PHE   A 1 10   ? -64.43800  71.80300  25.70800  1.000 54.04484  ?  10   PHE   A CA  1 
ATOM   72    C  C   . PHE   A 1 10   ? -64.44700  70.77500  24.58400  1.000 52.84917  ?  10   PHE   A C   1 
ATOM   73    O  O   . PHE   A 1 10   ? -63.69900  70.92800  23.61500  1.000 54.61022  ?  10   PHE   A O   1 
ATOM   74    C  CB  . PHE   A 1 10   ? -63.04200  71.91800  26.32400  1.000 40.78814  ?  10   PHE   A CB  1 
ATOM   75    C  CG  . PHE   A 1 10   ? -62.96700  72.90800  27.45100  1.000 44.88465  ?  10   PHE   A CG  1 
ATOM   76    C  CD1 . PHE   A 1 10   ? -63.06000  74.26800  27.20100  1.000 48.25376  ?  10   PHE   A CD1 1 
ATOM   77    C  CD2 . PHE   A 1 10   ? -62.82000  72.48100  28.76000  1.000 46.78280  ?  10   PHE   A CD2 1 
ATOM   78    C  CE1 . PHE   A 1 10   ? -63.00100  75.18500  28.23400  1.000 48.72335  ?  10   PHE   A CE1 1 
ATOM   79    C  CE2 . PHE   A 1 10   ? -62.76000  73.39300  29.79900  1.000 46.32570  ?  10   PHE   A CE2 1 
ATOM   80    C  CZ  . PHE   A 1 10   ? -62.85000  74.74600  29.53500  1.000 55.74058  ?  10   PHE   A CZ  1 
ATOM   81    N  N   . MET   A 1 11   ? -65.27100  69.73600  24.69200  1.000 45.15849  ?  11   MET   A N   1 
ATOM   82    C  CA  . MET   A 1 11   ? -65.53000  68.82300  23.59300  1.000 38.58985  ?  11   MET   A CA  1 
ATOM   83    C  C   . MET   A 1 11   ? -66.89300  69.13900  22.98600  1.000 57.60611  ?  11   MET   A C   1 
ATOM   84    O  O   . MET   A 1 11   ? -67.58700  70.07300  23.39200  1.000 63.10381  ?  11   MET   A O   1 
ATOM   85    C  CB  . MET   A 1 11   ? -65.45800  67.36600  24.05900  1.000 47.87308  ?  11   MET   A CB  1 
ATOM   86    C  CG  . MET   A 1 11   ? -64.63200  66.46700  23.16000  1.000 49.65227  ?  11   MET   A CG  1 
ATOM   87    S  SD  . MET   A 1 11   ? -62.86800  66.74200  23.37800  1.000 54.49887  ?  11   MET   A SD  1 
ATOM   88    C  CE  . MET   A 1 11   ? -62.28700  66.50900  21.70600  1.000 44.52883  ?  11   MET   A CE  1 
ATOM   89    N  N   . SER   A 1 12   ? -67.28900  68.33500  22.00600  1.000 63.72921  ?  12   SER   A N   1 
ATOM   90    C  CA  . SER   A 1 12   ? -68.49100  68.62000  21.24200  1.000 56.64856  ?  12   SER   A CA  1 
ATOM   91    C  C   . SER   A 1 12   ? -69.70600  67.92500  21.84900  1.000 57.46059  ?  12   SER   A C   1 
ATOM   92    O  O   . SER   A 1 12   ? -69.61300  67.16900  22.82100  1.000 73.35658  ?  12   SER   A O   1 
ATOM   93    C  CB  . SER   A 1 12   ? -68.30000  68.20600  19.78600  1.000 57.76905  ?  12   SER   A CB  1 
ATOM   94    O  OG  . SER   A 1 12   ? -67.20300  67.31800  19.64400  1.000 74.28727  ?  12   SER   A OG  1 
ATOM   95    N  N   . LYS   A 1 13   ? -70.86900  68.20200  21.26600  1.000 50.35831  ?  13   LYS   A N   1 
ATOM   96    C  CA  . LYS   A 1 13   ? -72.11300  67.54300  21.63200  1.000 48.70879  ?  13   LYS   A CA  1 
ATOM   97    C  C   . LYS   A 1 13   ? -72.40000  66.31900  20.77400  1.000 51.91264  ?  13   LYS   A C   1 
ATOM   98    O  O   . LYS   A 1 13   ? -73.26900  65.51800  21.13400  1.000 53.32739  ?  13   LYS   A O   1 
ATOM   99    C  CB  . LYS   A 1 13   ? -73.28500  68.52400  21.52400  1.000 45.34861  ?  13   LYS   A CB  1 
ATOM   100   C  CG  . LYS   A 1 13   ? -72.89100  69.99000  21.65100  1.000 67.80213  ?  13   LYS   A CG  1 
ATOM   101   C  CD  . LYS   A 1 13   ? -72.89700  70.67800  20.29000  1.000 74.76944  ?  13   LYS   A CD  1 
ATOM   102   C  CE  . LYS   A 1 13   ? -71.49400  71.01400  19.80000  1.000 54.45822  ?  13   LYS   A CE  1 
ATOM   103   N  NZ  . LYS   A 1 13   ? -70.83500  72.08100  20.60200  1.000 43.61480  ?  13   LYS   A NZ  1 
ATOM   104   N  N   . GLY   A 1 14   ? -71.70300  66.16400  19.65100  1.000 65.64939  ?  14   GLY   A N   1 
ATOM   105   C  CA  . GLY   A 1 14   ? -71.84300  64.98900  18.81600  1.000 64.74926  ?  14   GLY   A CA  1 
ATOM   106   C  C   . GLY   A 1 14   ? -70.53100  64.25100  18.66000  1.000 57.01714  ?  14   GLY   A C   1 
ATOM   107   O  O   . GLY   A 1 14   ? -69.96500  64.18800  17.56500  1.000 68.11275  ?  14   GLY   A O   1 
ATOM   108   N  N   . ASN   A 1 15   ? -70.03000  63.70200  19.75900  1.000 54.06993  ?  15   ASN   A N   1 
ATOM   109   C  CA  . ASN   A 1 15   ? -68.78500  62.95800  19.74000  1.000 54.15104  ?  15   ASN   A CA  1 
ATOM   110   C  C   . ASN   A 1 15   ? -69.04400  61.50200  19.37600  1.000 52.21922  ?  15   ASN   A C   1 
ATOM   111   O  O   . ASN   A 1 15   ? -70.18200  61.02400  19.36400  1.000 60.52044  ?  15   ASN   A O   1 
ATOM   112   C  CB  . ASN   A 1 15   ? -68.08300  63.04500  21.09500  1.000 51.87921  ?  15   ASN   A CB  1 
ATOM   113   C  CG  . ASN   A 1 15   ? -68.39600  64.33200  21.82800  1.000 67.46434  ?  15   ASN   A CG  1 
ATOM   114   O  OD1 . ASN   A 1 15   ? -67.95900  65.40900  21.42600  1.000 97.98389  ?  15   ASN   A OD1 1 
ATOM   115   N  ND2 . ASN   A 1 15   ? -69.15100  64.22600  22.91300  1.000 60.19366  ?  15   ASN   A ND2 1 
ATOM   116   N  N   . LYS   A 1 16   ? -67.95600  60.79600  19.07100  1.000 50.72713  ?  16   LYS   A N   1 
ATOM   117   C  CA  . LYS   A 1 16   ? -68.03800  59.35900  18.84400  1.000 41.75497  ?  16   LYS   A CA  1 
ATOM   118   C  C   . LYS   A 1 16   ? -68.67800  58.65400  20.03500  1.000 50.89938  ?  16   LYS   A C   1 
ATOM   119   O  O   . LYS   A 1 16   ? -69.46000  57.71200  19.86400  1.000 59.95948  ?  16   LYS   A O   1 
ATOM   120   C  CB  . LYS   A 1 16   ? -66.64100  58.80400  18.57500  1.000 40.78079  ?  16   LYS   A CB  1 
ATOM   121   C  CG  . LYS   A 1 16   ? -66.60400  57.63900  17.61100  1.000 47.03371  ?  16   LYS   A CG  1 
ATOM   122   C  CD  . LYS   A 1 16   ? -65.21700  57.02200  17.55400  1.000 32.36003  ?  16   LYS   A CD  1 
ATOM   123   C  CE  . LYS   A 1 16   ? -64.83900  56.64500  16.13100  1.000 50.57898  ?  16   LYS   A CE  1 
ATOM   124   N  NZ  . LYS   A 1 16   ? -63.96500  55.44100  16.09000  1.000 58.43784  ?  16   LYS   A NZ  1 
ATOM   125   N  N   . VAL   A 1 17   ? -68.37400  59.11500  21.25000  1.000 40.51373  ?  17   VAL   A N   1 
ATOM   126   C  CA  . VAL   A 1 17   ? -68.89800  58.46900  22.45100  1.000 48.47786  ?  17   VAL   A CA  1 
ATOM   127   C  C   . VAL   A 1 17   ? -70.41500  58.62000  22.52500  1.000 54.86589  ?  17   VAL   A C   1 
ATOM   128   O  O   . VAL   A 1 17   ? -71.14000  57.64500  22.75100  1.000 70.46506  ?  17   VAL   A O   1 
ATOM   129   C  CB  . VAL   A 1 17   ? -68.20300  59.03200  23.70500  1.000 56.09457  ?  17   VAL   A CB  1 
ATOM   130   C  CG1 . VAL   A 1 17   ? -66.76800  58.55800  23.75200  1.000 53.77125  ?  17   VAL   A CG1 1 
ATOM   131   C  CG2 . VAL   A 1 17   ? -68.23100  60.54400  23.69300  1.000 64.34937  ?  17   VAL   A CG2 1 
ATOM   132   N  N   . VAL   A 1 18   ? -70.91700  59.84400  22.32700  1.000 48.14556  ?  18   VAL   A N   1 
ATOM   133   C  CA  . VAL   A 1 18   ? -72.35700  60.08300  22.40700  1.000 48.06824  ?  18   VAL   A CA  1 
ATOM   134   C  C   . VAL   A 1 18   ? -73.08900  59.28200  21.33900  1.000 51.63288  ?  18   VAL   A C   1 
ATOM   135   O  O   . VAL   A 1 18   ? -74.12100  58.65400  21.60900  1.000 48.55466  ?  18   VAL   A O   1 
ATOM   136   C  CB  . VAL   A 1 18   ? -72.65800  61.58900  22.29300  1.000 40.32539  ?  18   VAL   A CB  1 
ATOM   137   C  CG1 . VAL   A 1 18   ? -74.13900  61.82300  22.03100  1.000 52.56083  ?  18   VAL   A CG1 1 
ATOM   138   C  CG2 . VAL   A 1 18   ? -72.22100  62.31200  23.55800  1.000 42.60889  ?  18   VAL   A CG2 1 
ATOM   139   N  N   . ARG   A 1 19   ? -72.56100  59.27800  20.11400  1.000 52.37788  ?  19   ARG   A N   1 
ATOM   140   C  CA  . ARG   A 1 19   ? -73.19300  58.51700  19.04300  1.000 50.44632  ?  19   ARG   A CA  1 
ATOM   141   C  C   . ARG   A 1 19   ? -73.12100  57.01900  19.31200  1.000 46.04574  ?  19   ARG   A C   1 
ATOM   142   O  O   . ARG   A 1 19   ? -74.05800  56.28100  18.98800  1.000 56.55456  ?  19   ARG   A O   1 
ATOM   143   C  CB  . ARG   A 1 19   ? -72.54500  58.86200  17.70300  1.000 40.63378  ?  19   ARG   A CB  1 
ATOM   144   C  CG  . ARG   A 1 19   ? -72.62200  60.33800  17.34700  1.000 44.65462  ?  19   ARG   A CG  1 
ATOM   145   C  CD  . ARG   A 1 19   ? -72.36300  60.56400  15.86800  1.000 52.08902  ?  19   ARG   A CD  1 
ATOM   146   N  NE  . ARG   A 1 19   ? -71.08500  60.00700  15.44200  1.000 60.20468  ?  19   ARG   A NE  1 
ATOM   147   C  CZ  . ARG   A 1 19   ? -69.95800  60.69900  15.35100  1.000 64.92096  ?  19   ARG   A CZ  1 
ATOM   148   N  NH1 . ARG   A 1 19   ? -69.91200  61.98800  15.64500  1.000 52.42848  ?  19   ARG   A NH1 1 
ATOM   149   N  NH2 . ARG   A 1 19   ? -68.84900  60.08300  14.95200  1.000 55.94769  ?  19   ARG   A NH2 1 
ATOM   150   N  N   . TYR   A 1 20   ? -72.02000  56.54900  19.90600  1.000 46.08866  ?  20   TYR   A N   1 
ATOM   151   C  CA  . TYR   A 1 20   ? -71.94300  55.14400  20.29200  1.000 46.11755  ?  20   TYR   A CA  1 
ATOM   152   C  C   . TYR   A 1 20   ? -72.96700  54.81700  21.36900  1.000 53.70669  ?  20   TYR   A C   1 
ATOM   153   O  O   . TYR   A 1 20   ? -73.60400  53.75800  21.33000  1.000 57.37139  ?  20   TYR   A O   1 
ATOM   154   C  CB  . TYR   A 1 20   ? -70.53600  54.79900  20.77500  1.000 37.65807  ?  20   TYR   A CB  1 
ATOM   155   C  CG  . TYR   A 1 20   ? -70.45400  53.46500  21.48500  1.000 43.91340  ?  20   TYR   A CG  1 
ATOM   156   C  CD1 . TYR   A 1 20   ? -70.45900  52.27500  20.76900  1.000 42.61320  ?  20   TYR   A CD1 1 
ATOM   157   C  CD2 . TYR   A 1 20   ? -70.37300  53.39700  22.87000  1.000 45.72625  ?  20   TYR   A CD2 1 
ATOM   158   C  CE1 . TYR   A 1 20   ? -70.38500  51.05200  21.41300  1.000 49.61005  ?  20   TYR   A CE1 1 
ATOM   159   C  CE2 . TYR   A 1 20   ? -70.29800  52.17900  23.52300  1.000 50.39817  ?  20   TYR   A CE2 1 
ATOM   160   C  CZ  . TYR   A 1 20   ? -70.30400  51.01000  22.79000  1.000 56.59939  ?  20   TYR   A CZ  1 
ATOM   161   O  OH  . TYR   A 1 20   ? -70.23000  49.79600  23.43500  1.000 56.12892  ?  20   TYR   A OH  1 
ATOM   162   N  N   . LEU   A 1 21   ? -73.13100  55.71000  22.34700  1.000 54.07552  ?  21   LEU   A N   1 
ATOM   163   C  CA  . LEU   A 1 21   ? -74.14900  55.50200  23.37100  1.000 56.67072  ?  21   LEU   A CA  1 
ATOM   164   C  C   . LEU   A 1 21   ? -75.54400  55.49600  22.76100  1.000 56.22477  ?  21   LEU   A C   1 
ATOM   165   O  O   . LEU   A 1 21   ? -76.39800  54.69200  23.15300  1.000 63.47026  ?  21   LEU   A O   1 
ATOM   166   C  CB  . LEU   A 1 21   ? -74.03500  56.57800  24.45100  1.000 46.61646  ?  21   LEU   A CB  1 
ATOM   167   C  CG  . LEU   A 1 21   ? -72.75900  56.55700  25.29400  1.000 44.03446  ?  21   LEU   A CG  1 
ATOM   168   C  CD1 . LEU   A 1 21   ? -72.75200  57.70700  26.28800  1.000 29.49191  ?  21   LEU   A CD1 1 
ATOM   169   C  CD2 . LEU   A 1 21   ? -72.60900  55.22400  26.00800  1.000 44.68878  ?  21   LEU   A CD2 1 
ATOM   170   N  N   . GLU   A 1 22   ? -75.79100  56.37900  21.79100  1.000 55.43527  ?  22   GLU   A N   1 
ATOM   171   C  CA  . GLU   A 1 22   ? -77.08600  56.38800  21.12000  1.000 51.36206  ?  22   GLU   A CA  1 
ATOM   172   C  C   . GLU   A 1 22   ? -77.27300  55.15400  20.24600  1.000 53.89865  ?  22   GLU   A C   1 
ATOM   173   O  O   . GLU   A 1 22   ? -78.40600  54.69400  20.06400  1.000 59.30243  ?  22   GLU   A O   1 
ATOM   174   C  CB  . GLU   A 1 22   ? -77.24000  57.66200  20.29000  1.000 47.91596  ?  22   GLU   A CB  1 
ATOM   175   C  CG  . GLU   A 1 22   ? -77.26500  58.93600  21.12200  1.000 49.42146  ?  22   GLU   A CG  1 
ATOM   176   C  CD  . GLU   A 1 22   ? -77.44800  60.18200  20.27900  1.000 58.09702  ?  22   GLU   A CD  1 
ATOM   177   O  OE1 . GLU   A 1 22   ? -77.51700  60.05900  19.03800  1.000 72.19756  ?  22   GLU   A OE1 1 
ATOM   178   O  OE2 . GLU   A 1 22   ? -77.52300  61.28600  20.85900  1.000 58.36799  -1 22   GLU   A OE2 1 
ATOM   179   N  N   . SER   A 1 23   ? -76.18200  54.60300  19.70400  1.000 45.38238  ?  23   SER   A N   1 
ATOM   180   C  CA  . SER   A 1 23   ? -76.29300  53.38300  18.91200  1.000 42.13444  ?  23   SER   A CA  1 
ATOM   181   C  C   . SER   A 1 23   ? -76.73700  52.20400  19.76700  1.000 49.07476  ?  23   SER   A C   1 
ATOM   182   O  O   . SER   A 1 23   ? -77.45300  51.32100  19.28000  1.000 47.73935  ?  23   SER   A O   1 
ATOM   183   C  CB  . SER   A 1 23   ? -74.96300  53.06900  18.22800  1.000 45.61193  ?  23   SER   A CB  1 
ATOM   184   O  OG  . SER   A 1 23   ? -74.10300  52.34200  19.08800  1.000 59.27806  ?  23   SER   A OG  1 
ATOM   185   N  N   . LEU   A 1 24   ? -76.32800  52.17100  21.03600  1.000 54.03938  ?  24   LEU   A N   1 
ATOM   186   C  CA  . LEU   A 1 24   ? -76.78400  51.15800  21.98000  1.000 48.96803  ?  24   LEU   A CA  1 
ATOM   187   C  C   . LEU   A 1 24   ? -78.18500  51.43800  22.51100  1.000 55.18269  ?  24   LEU   A C   1 
ATOM   188   O  O   . LEU   A 1 24   ? -78.58900  50.82500  23.50500  1.000 56.20972  ?  24   LEU   A O   1 
ATOM   189   C  CB  . LEU   A 1 24   ? -75.80000  51.04500  23.14900  1.000 44.04975  ?  24   LEU   A CB  1 
ATOM   190   C  CG  . LEU   A 1 24   ? -74.40200  50.51600  22.82200  1.000 48.42415  ?  24   LEU   A CG  1 
ATOM   191   C  CD1 . LEU   A 1 24   ? -73.57400  50.37700  24.09000  1.000 64.57090  ?  24   LEU   A CD1 1 
ATOM   192   C  CD2 . LEU   A 1 24   ? -74.48600  49.18700  22.08600  1.000 59.74578  ?  24   LEU   A CD2 1 
ATOM   193   N  N   . HIS   A 1 25   ? -78.91900  52.35000  21.87000  1.000 53.09579  ?  25   HIS   A N   1 
ATOM   194   C  CA  . HIS   A 1 25   ? -80.28900  52.69700  22.24900  1.000 57.08640  ?  25   HIS   A CA  1 
ATOM   195   C  C   . HIS   A 1 25   ? -80.35200  53.23900  23.67700  1.000 52.36501  ?  25   HIS   A C   1 
ATOM   196   O  O   . HIS   A 1 25   ? -81.16300  52.81000  24.50000  1.000 56.74164  ?  25   HIS   A O   1 
ATOM   197   C  CB  . HIS   A 1 25   ? -81.23200  51.50600  22.06100  1.000 54.04483  ?  25   HIS   A CB  1 
ATOM   198   C  CG  . HIS   A 1 25   ? -81.41700  51.10600  20.63000  1.000 46.11890  ?  25   HIS   A CG  1 
ATOM   199   N  ND1 . HIS   A 1 25   ? -81.85800  51.98500  19.66400  1.000 48.40721  ?  25   HIS   A ND1 1 
ATOM   200   C  CD2 . HIS   A 1 25   ? -81.21900  49.92300  20.00100  1.000 48.11118  ?  25   HIS   A CD2 1 
ATOM   201   C  CE1 . HIS   A 1 25   ? -81.92300  51.36100  18.50100  1.000 55.19368  ?  25   HIS   A CE1 1 
ATOM   202   N  NE2 . HIS   A 1 25   ? -81.54200  50.10900  18.67800  1.000 54.86481  ?  25   HIS   A NE2 1 
ATOM   203   N  N   . HIS   A 1 26   ? -79.47700  54.19500  23.96400  1.000 47.33769  ?  26   HIS   A N   1 
ATOM   204   C  CA  . HIS   A 1 26   ? -79.53500  54.98600  25.18200  1.000 51.35580  ?  26   HIS   A CA  1 
ATOM   205   C  C   . HIS   A 1 26   ? -80.14200  56.35000  24.88100  1.000 45.66041  ?  26   HIS   A C   1 
ATOM   206   O  O   . HIS   A 1 26   ? -80.18300  56.79900  23.73300  1.000 57.78315  ?  26   HIS   A O   1 
ATOM   207   C  CB  . HIS   A 1 26   ? -78.14100  55.17700  25.78600  1.000 59.61720  ?  26   HIS   A CB  1 
ATOM   208   C  CG  . HIS   A 1 26   ? -77.55800  53.94000  26.39600  1.000 59.85342  ?  26   HIS   A CG  1 
ATOM   209   N  ND1 . HIS   A 1 26   ? -77.88100  53.51300  27.66600  1.000 59.85946  ?  26   HIS   A ND1 1 
ATOM   210   C  CD2 . HIS   A 1 26   ? -76.65000  53.05400  25.92200  1.000 54.74553  ?  26   HIS   A CD2 1 
ATOM   211   C  CE1 . HIS   A 1 26   ? -77.20900  52.41000  27.94200  1.000 63.49356  ?  26   HIS   A CE1 1 
ATOM   212   N  NE2 . HIS   A 1 26   ? -76.45400  52.11100  26.90100  1.000 46.04122  ?  26   HIS   A NE2 1 
ATOM   213   N  N   . GLU   A 1 27   ? -80.61300  57.01300  25.93300  1.000 49.01789  ?  27   GLU   A N   1 
ATOM   214   C  CA  . GLU   A 1 27   ? -81.02700  58.40800  25.84900  1.000 63.36054  ?  27   GLU   A CA  1 
ATOM   215   C  C   . GLU   A 1 27   ? -79.91900  59.26100  26.45200  1.000 65.92926  ?  27   GLU   A C   1 
ATOM   216   O  O   . GLU   A 1 27   ? -79.72500  59.26800  27.67200  1.000 68.38821  ?  27   GLU   A O   1 
ATOM   217   C  CB  . GLU   A 1 27   ? -82.35300  58.65100  26.56300  1.000 63.63041  ?  27   GLU   A CB  1 
ATOM   218   C  CG  . GLU   A 1 27   ? -82.73900  60.12300  26.58500  1.000 69.90961  ?  27   GLU   A CG  1 
ATOM   219   C  CD  . GLU   A 1 27   ? -84.11200  60.37000  27.16800  1.000 70.94395  ?  27   GLU   A CD  1 
ATOM   220   O  OE1 . GLU   A 1 27   ? -84.73600  59.40800  27.66400  1.000 75.91633  ?  27   GLU   A OE1 1 
ATOM   221   O  OE2 . GLU   A 1 27   ? -84.57100  61.53100  27.12700  1.000 72.05874  -1 27   GLU   A OE2 1 
ATOM   222   N  N   . VAL   A 1 28   ? -79.19600  59.97600  25.59900  1.000 55.47571  ?  28   VAL   A N   1 
ATOM   223   C  CA  . VAL   A 1 28   ? -78.06100  60.78800  26.01700  1.000 52.54909  ?  28   VAL   A CA  1 
ATOM   224   C  C   . VAL   A 1 28   ? -78.53300  62.23100  26.13300  1.000 51.80999  ?  28   VAL   A C   1 
ATOM   225   O  O   . VAL   A 1 28   ? -78.82100  62.88500  25.12500  1.000 45.08156  ?  28   VAL   A O   1 
ATOM   226   C  CB  . VAL   A 1 28   ? -76.88600  60.65900  25.04100  1.000 43.61450  ?  28   VAL   A CB  1 
ATOM   227   C  CG1 . VAL   A 1 28   ? -75.67600  61.41700  25.56700  1.000 47.72424  ?  28   VAL   A CG1 1 
ATOM   228   C  CG2 . VAL   A 1 28   ? -76.55100  59.19500  24.81100  1.000 43.39638  ?  28   VAL   A CG2 1 
ATOM   229   N  N   . VAL   A 1 29   ? -78.62000  62.72400  27.36400  1.000 50.93113  ?  29   VAL   A N   1 
ATOM   230   C  CA  . VAL   A 1 29   ? -78.89800  64.13100  27.62500  1.000 47.47826  ?  29   VAL   A CA  1 
ATOM   231   C  C   . VAL   A 1 29   ? -77.56200  64.84200  27.78900  1.000 58.63750  ?  29   VAL   A C   1 
ATOM   232   O  O   . VAL   A 1 29   ? -76.76100  64.48400  28.66000  1.000 52.56558  ?  29   VAL   A O   1 
ATOM   233   C  CB  . VAL   A 1 29   ? -79.77600  64.30600  28.87200  1.000 47.06308  ?  29   VAL   A CB  1 
ATOM   234   C  CG1 . VAL   A 1 29   ? -80.27300  65.74200  28.97200  1.000 52.45489  ?  29   VAL   A CG1 1 
ATOM   235   C  CG2 . VAL   A 1 29   ? -80.93800  63.32600  28.84600  1.000 52.73355  ?  29   VAL   A CG2 1 
ATOM   236   N  N   . ILE   A 1 30   ? -77.31600  65.84500  26.95100  1.000 67.76762  ?  30   ILE   A N   1 
ATOM   237   C  CA  . ILE   A 1 30   ? -76.03800  66.54500  26.90400  1.000 59.69745  ?  30   ILE   A CA  1 
ATOM   238   C  C   . ILE   A 1 30   ? -76.20200  67.90800  27.55700  1.000 48.57647  ?  30   ILE   A C   1 
ATOM   239   O  O   . ILE   A 1 30   ? -77.10900  68.67100  27.20200  1.000 50.46607  ?  30   ILE   A O   1 
ATOM   240   C  CB  . ILE   A 1 30   ? -75.52500  66.68300  25.46000  1.000 46.06788  ?  30   ILE   A CB  1 
ATOM   241   C  CG1 . ILE   A 1 30   ? -75.22900  65.30400  24.86800  1.000 46.55329  ?  30   ILE   A CG1 1 
ATOM   242   C  CG2 . ILE   A 1 30   ? -74.28400  67.56300  25.41600  1.000 51.48995  ?  30   ILE   A CG2 1 
ATOM   243   C  CD1 . ILE   A 1 30   ? -75.96300  65.02200  23.57900  1.000 52.30252  ?  30   ILE   A CD1 1 
ATOM   244   N  N   . CYS   A 1 31   ? -75.32600  68.21100  28.51100  1.000 59.59667  ?  31   CYS   A N   1 
ATOM   245   C  CA  . CYS   A 1 31   ? -75.28600  69.51600  29.15700  1.000 77.57798  ?  31   CYS   A CA  1 
ATOM   246   C  C   . CYS   A 1 31   ? -73.87000  70.05600  29.04400  1.000 74.27663  ?  31   CYS   A C   1 
ATOM   247   O  O   . CYS   A 1 31   ? -72.92500  69.43600  29.54400  1.000 59.05262  ?  31   CYS   A O   1 
ATOM   248   C  CB  . CYS   A 1 31   ? -75.72000  69.42500  30.62300  1.000 63.29560  ?  31   CYS   A CB  1 
ATOM   249   S  SG  . CYS   A 1 31   ? -76.28000  70.99500  31.32300  1.000 101.39839 ?  31   CYS   A SG  1 
ATOM   250   N  N   . GLN   A 1 32   ? -73.72400  71.19900  28.37900  1.000 72.15253  ?  32   GLN   A N   1 
ATOM   251   C  CA  . GLN   A 1 32   ? -72.42600  71.82600  28.17500  1.000 66.11098  ?  32   GLN   A CA  1 
ATOM   252   C  C   . GLN   A 1 32   ? -72.10100  72.88200  29.22100  1.000 72.28778  ?  32   GLN   A C   1 
ATOM   253   O  O   . GLN   A 1 32   ? -71.01500  73.46700  29.17300  1.000 74.74951  ?  32   GLN   A O   1 
ATOM   254   C  CB  . GLN   A 1 32   ? -72.35200  72.44600  26.77500  1.000 66.43320  ?  32   GLN   A CB  1 
ATOM   255   C  CG  . GLN   A 1 32   ? -72.25200  71.42300  25.65500  1.000 62.84456  ?  32   GLN   A CG  1 
ATOM   256   C  CD  . GLN   A 1 32   ? -71.35700  71.88700  24.52300  1.000 61.00425  ?  32   GLN   A CD  1 
ATOM   257   O  OE1 . GLN   A 1 32   ? -70.36500  71.23600  24.19300  1.000 73.06940  ?  32   GLN   A OE1 1 
ATOM   258   N  NE2 . GLN   A 1 32   ? -71.70300  73.01900  23.92100  1.000 63.03892  ?  32   GLN   A NE2 1 
ATOM   259   N  N   . GLU   A 1 33   ? -72.99900  73.13100  30.16400  1.000 74.83238  ?  33   GLU   A N   1 
ATOM   260   C  CA  . GLU   A 1 33   ? -72.83300  74.20700  31.12900  1.000 82.92845  ?  33   GLU   A CA  1 
ATOM   261   C  C   . GLU   A 1 33   ? -72.78900  73.63300  32.54400  1.000 88.33966  ?  33   GLU   A C   1 
ATOM   262   O  O   . GLU   A 1 33   ? -72.67500  72.42100  32.74500  1.000 73.90132  ?  33   GLU   A O   1 
ATOM   263   C  CB  . GLU   A 1 33   ? -73.96300  75.22800  30.98300  1.000 83.89495  ?  33   GLU   A CB  1 
ATOM   264   C  CG  . GLU   A 1 33   ? -74.42300  75.45900  29.55100  1.000 90.52878  ?  33   GLU   A CG  1 
ATOM   265   C  CD  . GLU   A 1 33   ? -73.66100  76.56900  28.85100  1.000 97.97614  ?  33   GLU   A CD  1 
ATOM   266   O  OE1 . GLU   A 1 33   ? -72.59900  76.98400  29.36200  1.000 94.89009  ?  33   GLU   A OE1 1 
ATOM   267   O  OE2 . GLU   A 1 33   ? -74.13300  77.02900  27.78800  1.000 112.83370 -1 33   GLU   A OE2 1 
ATOM   268   N  N   . LYS   A 1 34   ? -72.89200  74.52600  33.52700  1.000 90.47943  ?  34   LYS   A N   1 
ATOM   269   C  CA  . LYS   A 1 34   ? -72.95500  74.12100  34.92500  1.000 74.04113  ?  34   LYS   A CA  1 
ATOM   270   C  C   . LYS   A 1 34   ? -74.21500  73.30400  35.18800  1.000 76.55762  ?  34   LYS   A C   1 
ATOM   271   O  O   . LYS   A 1 34   ? -75.21200  73.41300  34.46700  1.000 76.23229  ?  34   LYS   A O   1 
ATOM   272   C  CB  . LYS   A 1 34   ? -72.91500  75.35500  35.83400  1.000 82.94859  ?  34   LYS   A CB  1 
ATOM   273   C  CG  . LYS   A 1 34   ? -73.64700  76.57400  35.27600  1.000 68.35870  ?  34   LYS   A CG  1 
ATOM   274   C  CD  . LYS   A 1 34   ? -75.16000  76.41100  35.41400  1.000 87.49142  ?  34   LYS   A CD  1 
ATOM   275   C  CE  . LYS   A 1 34   ? -75.97400  77.50600  34.71800  1.000 94.08645  ?  34   LYS   A CE  1 
ATOM   276   N  NZ  . LYS   A 1 34   ? -77.42600  77.15200  34.76700  1.000 77.46962  ?  34   LYS   A NZ  1 
ATOM   277   N  N   . VAL   A 1 35   ? -74.16700  72.47500  36.23000  1.000 72.91810  ?  35   VAL   A N   1 
ATOM   278   C  CA  . VAL   A 1 35   ? -75.33800  71.72800  36.67700  1.000 95.64909  ?  35   VAL   A CA  1 
ATOM   279   C  C   . VAL   A 1 35   ? -75.42000  71.82300  38.19300  1.000 96.48585  ?  35   VAL   A C   1 
ATOM   280   O  O   . VAL   A 1 35   ? -74.49000  71.41400  38.89900  1.000 96.52898  ?  35   VAL   A O   1 
ATOM   281   C  CB  . VAL   A 1 35   ? -75.31100  70.26100  36.21400  1.000 73.28454  ?  35   VAL   A CB  1 
ATOM   282   C  CG1 . VAL   A 1 35   ? -75.62800  70.17800  34.73500  1.000 62.71168  ?  35   VAL   A CG1 1 
ATOM   283   C  CG2 . VAL   A 1 35   ? -73.96100  69.64200  36.48400  1.000 81.65990  ?  35   VAL   A CG2 1 
ATOM   284   N  N   . HIS   A 1 36   ? -76.51200  72.38900  38.68700  1.000 84.57346  ?  36   HIS   A N   1 
ATOM   285   C  CA  . HIS   A 1 36   ? -76.78200  72.41100  40.11300  1.000 83.42040  ?  36   HIS   A CA  1 
ATOM   286   C  C   . HIS   A 1 36   ? -77.49200  71.12500  40.51600  1.000 96.88219  ?  36   HIS   A C   1 
ATOM   287   O  O   . HIS   A 1 36   ? -78.18600  70.50100  39.70900  1.000 99.25212  ?  36   HIS   A O   1 
ATOM   288   C  CB  . HIS   A 1 36   ? -77.63400  73.62400  40.48400  1.000 86.49634  ?  36   HIS   A CB  1 
ATOM   289   N  N   . ALA   A 1 37   ? -77.31000  70.73300  41.78100  1.000 87.01208  ?  37   ALA   A N   1 
ATOM   290   C  CA  . ALA   A 1 37   ? -77.90100  69.49100  42.27100  1.000 87.31836  ?  37   ALA   A CA  1 
ATOM   291   C  C   . ALA   A 1 37   ? -79.40600  69.44600  42.04400  1.000 95.54789  ?  37   ALA   A C   1 
ATOM   292   O  O   . ALA   A 1 37   ? -79.97000  68.36700  41.82900  1.000 84.85423  ?  37   ALA   A O   1 
ATOM   293   C  CB  . ALA   A 1 37   ? -77.58300  69.31200  43.75700  1.000 82.58850  ?  37   ALA   A CB  1 
ATOM   294   N  N   . GLN   A 1 38   ? -80.06900  70.60200  42.07200  1.000 112.60308 ?  38   GLN   A N   1 
ATOM   295   C  CA  . GLN   A 1 38   ? -81.50500  70.69400  41.85000  1.000 108.08652 ?  38   GLN   A CA  1 
ATOM   296   C  C   . GLN   A 1 38   ? -81.86900  70.94300  40.39000  1.000 110.78810 ?  38   GLN   A C   1 
ATOM   297   O  O   . GLN   A 1 38   ? -83.03100  71.24200  40.10100  1.000 94.35876  ?  38   GLN   A O   1 
ATOM   298   C  CB  . GLN   A 1 38   ? -82.10300  71.79900  42.72600  1.000 79.29334  ?  38   GLN   A CB  1 
ATOM   299   N  N   . SER   A 1 39   ? -80.91600  70.83200  39.46800  1.000 105.72012 ?  39   SER   A N   1 
ATOM   300   C  CA  . SER   A 1 39   ? -81.23400  70.99600  38.05500  1.000 99.21194  ?  39   SER   A CA  1 
ATOM   301   C  C   . SER   A 1 39   ? -82.02500  69.79500  37.54800  1.000 87.46065  ?  39   SER   A C   1 
ATOM   302   O  O   . SER   A 1 39   ? -81.76700  68.65300  37.93900  1.000 77.33156  ?  39   SER   A O   1 
ATOM   303   C  CB  . SER   A 1 39   ? -79.95500  71.16600  37.23200  1.000 90.66689  ?  39   SER   A CB  1 
ATOM   304   O  OG  . SER   A 1 39   ? -80.02700  72.31200  36.40000  1.000 69.53241  ?  39   SER   A OG  1 
ATOM   305   N  N   . ALA   A 1 40   ? -82.99500  70.05900  36.66600  1.000 92.86797  ?  40   ALA   A N   1 
ATOM   306   C  CA  . ALA   A 1 40   ? -83.77100  68.98100  36.06000  1.000 90.17574  ?  40   ALA   A CA  1 
ATOM   307   C  C   . ALA   A 1 40   ? -82.89800  68.04300  35.23500  1.000 96.60470  ?  40   ALA   A C   1 
ATOM   308   O  O   . ALA   A 1 40   ? -83.30200  66.90400  34.96900  1.000 93.35856  ?  40   ALA   A O   1 
ATOM   309   C  CB  . ALA   A 1 40   ? -84.88800  69.55900  35.18900  1.000 65.11026  ?  40   ALA   A CB  1 
ATOM   310   N  N   . ASN   A 1 41   ? -81.70400  68.49400  34.83800  1.000 91.99010  ?  41   ASN   A N   1 
ATOM   311   C  CA  . ASN   A 1 41   ? -80.71200  67.65400  34.18100  1.000 89.65869  ?  41   ASN   A CA  1 
ATOM   312   C  C   . ASN   A 1 41   ? -80.07900  66.62400  35.11600  1.000 88.84496  ?  41   ASN   A C   1 
ATOM   313   O  O   . ASN   A 1 41   ? -78.98500  66.14300  34.81500  1.000 102.83169 ?  41   ASN   A O   1 
ATOM   314   C  CB  . ASN   A 1 41   ? -79.61800  68.52500  33.56000  1.000 88.16880  ?  41   ASN   A CB  1 
ATOM   315   C  CG  . ASN   A 1 41   ? -80.12900  69.36800  32.42900  1.000 91.26846  ?  41   ASN   A CG  1 
ATOM   316   O  OD1 . ASN   A 1 41   ? -80.98600  68.93000  31.66400  1.000 90.88812  ?  41   ASN   A OD1 1 
ATOM   317   N  ND2 . ASN   A 1 41   ? -79.61900  70.58500  32.31700  1.000 77.51578  ?  41   ASN   A ND2 1 
ATOM   318   N  N   . LEU   A 1 42   ? -80.72400  66.29700  36.24700  1.000 82.42573  ?  42   LEU   A N   1 
ATOM   319   C  CA  . LEU   A 1 42   ? -80.22300  65.27800  37.16600  1.000 79.07713  ?  42   LEU   A CA  1 
ATOM   320   C  C   . LEU   A 1 42   ? -81.34000  64.36000  37.65400  1.000 86.29845  ?  42   LEU   A C   1 
ATOM   321   O  O   . LEU   A 1 42   ? -81.21400  63.75600  38.72600  1.000 90.27514  ?  42   LEU   A O   1 
ATOM   322   C  CB  . LEU   A 1 42   ? -79.51200  65.92300  38.36000  1.000 70.17232  ?  42   LEU   A CB  1 
ATOM   323   C  CG  . LEU   A 1 42   ? -78.08600  66.37600  38.05000  1.000 72.21119  ?  42   LEU   A CG  1 
ATOM   324   C  CD1 . LEU   A 1 42   ? -77.67800  67.55700  38.90300  1.000 71.71454  ?  42   LEU   A CD1 1 
ATOM   325   C  CD2 . LEU   A 1 42   ? -77.13100  65.21800  38.25700  1.000 61.56123  ?  42   LEU   A CD2 1 
ATOM   326   N  N   . GLN   A 1 43   ? -82.42600  64.24500  36.89200  1.000 84.14970  ?  43   GLN   A N   1 
ATOM   327   C  CA  . GLN   A 1 43   ? -83.58600  63.45100  37.26500  1.000 76.20112  ?  43   GLN   A CA  1 
ATOM   328   C  C   . GLN   A 1 43   ? -83.77900  62.31900  36.26700  1.000 67.16480  ?  43   GLN   A C   1 
ATOM   329   O  O   . GLN   A 1 43   ? -83.69500  62.52900  35.05200  1.000 79.48061  ?  43   GLN   A O   1 
ATOM   330   C  CB  . GLN   A 1 43   ? -84.84800  64.31500  37.31400  1.000 73.09862  ?  43   GLN   A CB  1 
ATOM   331   C  CG  . GLN   A 1 43   ? -84.72600  65.53000  38.20900  1.000 93.05917  ?  43   GLN   A CG  1 
ATOM   332   C  CD  . GLN   A 1 43   ? -85.90900  66.46700  38.08500  1.000 109.73675 ?  43   GLN   A CD  1 
ATOM   333   O  OE1 . GLN   A 1 43   ? -85.92000  67.54700  38.67400  1.000 101.09291 ?  43   GLN   A OE1 1 
ATOM   334   N  NE2 . GLN   A 1 43   ? -86.91400  66.05900  37.31700  1.000 102.51575 ?  43   GLN   A NE2 1 
ATOM   335   N  N   . GLU   A 1 44   ? -84.04800  61.12300  36.79500  1.000 60.28519  ?  44   GLU   A N   1 
ATOM   336   C  CA  . GLU   A 1 44   ? -84.31400  59.92700  35.99300  1.000 70.22746  ?  44   GLU   A CA  1 
ATOM   337   C  C   . GLU   A 1 44   ? -83.10800  59.52000  35.15000  1.000 72.40812  ?  44   GLU   A C   1 
ATOM   338   O  O   . GLU   A 1 44   ? -83.26000  58.92300  34.08200  1.000 79.42054  ?  44   GLU   A O   1 
ATOM   339   C  CB  . GLU   A 1 44   ? -85.54800  60.11400  35.10200  1.000 86.56184  ?  44   GLU   A CB  1 
ATOM   340   N  N   . ILE   A 1 45   ? -81.90300  59.82200  35.62800  1.000 75.52733  ?  45   ILE   A N   1 
ATOM   341   C  CA  . ILE   A 1 45   ? -80.66400  59.53100  34.91500  1.000 64.90404  ?  45   ILE   A CA  1 
ATOM   342   C  C   . ILE   A 1 45   ? -79.89900  58.46900  35.68800  1.000 57.80112  ?  45   ILE   A C   1 
ATOM   343   O  O   . ILE   A 1 45   ? -79.70100  58.59700  36.90200  1.000 66.42084  ?  45   ILE   A O   1 
ATOM   344   C  CB  . ILE   A 1 45   ? -79.81400  60.79800  34.73400  1.000 65.17571  ?  45   ILE   A CB  1 
ATOM   345   C  CG1 . ILE   A 1 45   ? -80.71500  61.96300  34.35300  1.000 70.69883  ?  45   ILE   A CG1 1 
ATOM   346   C  CG2 . ILE   A 1 45   ? -78.76100  60.59100  33.65900  1.000 69.99986  ?  45   ILE   A CG2 1 
ATOM   347   C  CD1 . ILE   A 1 45   ? -79.98600  63.25400  34.23900  1.000 69.71082  ?  45   ILE   A CD1 1 
ATOM   348   N  N   . ASP   A 1 46   ? -79.45800  57.43100  34.98100  1.000 52.78569  ?  46   ASP   A N   1 
ATOM   349   C  CA  . ASP   A 1 46   ? -78.81100  56.29200  35.61700  1.000 53.33328  ?  46   ASP   A CA  1 
ATOM   350   C  C   . ASP   A 1 46   ? -77.29400  56.40100  35.63300  1.000 62.80728  ?  46   ASP   A C   1 
ATOM   351   O  O   . ASP   A 1 46   ? -76.65300  55.85700  36.53900  1.000 72.93886  ?  46   ASP   A O   1 
ATOM   352   C  CB  . ASP   A 1 46   ? -79.22100  54.99900  34.90800  1.000 65.30559  ?  46   ASP   A CB  1 
ATOM   353   C  CG  . ASP   A 1 46   ? -80.71100  54.93500  34.63700  1.000 70.43769  ?  46   ASP   A CG  1 
ATOM   354   O  OD1 . ASP   A 1 46   ? -81.49700  55.29000  35.54000  1.000 74.56720  ?  46   ASP   A OD1 1 
ATOM   355   O  OD2 . ASP   A 1 46   ? -81.09500  54.54000  33.51500  1.000 62.69043  -1 46   ASP   A OD2 1 
ATOM   356   N  N   . TRP   A 1 47   ? -76.70300  57.08100  34.65400  1.000 69.17189  ?  47   TRP   A N   1 
ATOM   357   C  CA  . TRP   A 1 47   ? -75.25900  57.24700  34.59500  1.000 55.87272  ?  47   TRP   A CA  1 
ATOM   358   C  C   . TRP   A 1 47   ? -74.92800  58.68700  34.24000  1.000 54.90055  ?  47   TRP   A C   1 
ATOM   359   O  O   . TRP   A 1 47   ? -75.72800  59.39200  33.62100  1.000 58.05535  ?  47   TRP   A O   1 
ATOM   360   C  CB  . TRP   A 1 47   ? -74.61200  56.30600  33.57000  1.000 46.34767  ?  47   TRP   A CB  1 
ATOM   361   C  CG  . TRP   A 1 47   ? -74.67700  54.86100  33.94600  1.000 46.49577  ?  47   TRP   A CG  1 
ATOM   362   C  CD1 . TRP   A 1 47   ? -75.65900  53.97400  33.62100  1.000 46.79645  ?  47   TRP   A CD1 1 
ATOM   363   C  CD2 . TRP   A 1 47   ? -73.71400  54.12900  34.71400  1.000 55.03795  ?  47   TRP   A CD2 1 
ATOM   364   N  NE1 . TRP   A 1 47   ? -75.37100  52.73600  34.14000  1.000 51.77958  ?  47   TRP   A NE1 1 
ATOM   365   C  CE2 . TRP   A 1 47   ? -74.18100  52.80400  34.81500  1.000 51.42279  ?  47   TRP   A CE2 1 
ATOM   366   C  CE3 . TRP   A 1 47   ? -72.50200  54.46600  35.32600  1.000 61.38430  ?  47   TRP   A CE3 1 
ATOM   367   C  CZ2 . TRP   A 1 47   ? -73.48100  51.81600  35.50400  1.000 62.05132  ?  47   TRP   A CZ2 1 
ATOM   368   C  CZ3 . TRP   A 1 47   ? -71.80800  53.48300  36.01000  1.000 67.12584  ?  47   TRP   A CZ3 1 
ATOM   369   C  CH2 . TRP   A 1 47   ? -72.30000  52.17400  36.09300  1.000 73.54181  ?  47   TRP   A CH2 1 
ATOM   370   N  N   . ILE   A 1 48   ? -73.73400  59.11300  34.64200  1.000 54.31152  ?  48   ILE   A N   1 
ATOM   371   C  CA  . ILE   A 1 48   ? -73.19900  60.42200  34.29300  1.000 50.71035  ?  48   ILE   A CA  1 
ATOM   372   C  C   . ILE   A 1 48   ? -71.81300  60.21100  33.70400  1.000 55.46699  ?  48   ILE   A C   1 
ATOM   373   O  O   . ILE   A 1 48   ? -70.91300  59.71200  34.39000  1.000 58.32633  ?  48   ILE   A O   1 
ATOM   374   C  CB  . ILE   A 1 48   ? -73.13600  61.36900  35.50100  1.000 50.53555  ?  48   ILE   A CB  1 
ATOM   375   C  CG1 . ILE   A 1 48   ? -74.53600  61.85900  35.87500  1.000 53.52508  ?  48   ILE   A CG1 1 
ATOM   376   C  CG2 . ILE   A 1 48   ? -72.23500  62.54600  35.19800  1.000 51.48794  ?  48   ILE   A CG2 1 
ATOM   377   C  CD1 . ILE   A 1 48   ? -74.54500  62.87200  37.00100  1.000 53.79913  ?  48   ILE   A CD1 1 
ATOM   378   N  N   . VAL   A 1 49   ? -71.64200  60.57900  32.43800  1.000 60.45310  ?  49   VAL   A N   1 
ATOM   379   C  CA  . VAL   A 1 49   ? -70.37800  60.42000  31.73000  1.000 49.08524  ?  49   VAL   A CA  1 
ATOM   380   C  C   . VAL   A 1 49   ? -69.83300  61.80400  31.41800  1.000 44.61952  ?  49   VAL   A C   1 
ATOM   381   O  O   . VAL   A 1 49   ? -70.50000  62.61000  30.75700  1.000 49.40952  ?  49   VAL   A O   1 
ATOM   382   C  CB  . VAL   A 1 49   ? -70.54500  59.58800  30.45000  1.000 56.69814  ?  49   VAL   A CB  1 
ATOM   383   C  CG1 . VAL   A 1 49   ? -69.26600  59.62200  29.62800  1.000 37.76228  ?  49   VAL   A CG1 1 
ATOM   384   C  CG2 . VAL   A 1 49   ? -70.91900  58.15700  30.80000  1.000 49.14338  ?  49   VAL   A CG2 1 
ATOM   385   N  N   . SER   A 1 50   ? -68.62500  62.08300  31.89800  1.000 50.37104  ?  50   SER   A N   1 
ATOM   386   C  CA  . SER   A 1 50   ? -67.96400  63.35700  31.66500  1.000 50.82762  ?  50   SER   A CA  1 
ATOM   387   C  C   . SER   A 1 50   ? -66.78800  63.17000  30.71500  1.000 56.80448  ?  50   SER   A C   1 
ATOM   388   O  O   . SER   A 1 50   ? -66.13200  62.12300  30.70500  1.000 59.17190  ?  50   SER   A O   1 
ATOM   389   C  CB  . SER   A 1 50   ? -67.48800  63.98200  32.98000  1.000 48.17264  ?  50   SER   A CB  1 
ATOM   390   O  OG  . SER   A 1 50   ? -66.98000  63.00000  33.86400  1.000 61.76274  ?  50   SER   A OG  1 
ATOM   391   N  N   . TYR   A 1 51   ? -66.53200  64.20100  29.91300  1.000 48.58627  ?  51   TYR   A N   1 
ATOM   392   C  CA  . TYR   A 1 51   ? -65.48700  64.14300  28.89400  1.000 33.70575  ?  51   TYR   A CA  1 
ATOM   393   C  C   . TYR   A 1 51   ? -65.09400  65.57600  28.57100  1.000 44.50059  ?  51   TYR   A C   1 
ATOM   394   O  O   . TYR   A 1 51   ? -65.84600  66.28200  27.89100  1.000 47.85215  ?  51   TYR   A O   1 
ATOM   395   C  CB  . TYR   A 1 51   ? -65.98500  63.40700  27.65600  1.000 36.63526  ?  51   TYR   A CB  1 
ATOM   396   C  CG  . TYR   A 1 51   ? -64.94100  63.16300  26.58600  1.000 52.05582  ?  51   TYR   A CG  1 
ATOM   397   C  CD1 . TYR   A 1 51   ? -63.58500  63.27400  26.86300  1.000 50.74041  ?  51   TYR   A CD1 1 
ATOM   398   C  CD2 . TYR   A 1 51   ? -65.31900  62.82500  25.29200  1.000 51.11472  ?  51   TYR   A CD2 1 
ATOM   399   C  CE1 . TYR   A 1 51   ? -62.63500  63.05200  25.88300  1.000 50.25186  ?  51   TYR   A CE1 1 
ATOM   400   C  CE2 . TYR   A 1 51   ? -64.37800  62.60200  24.30700  1.000 63.00110  ?  51   TYR   A CE2 1 
ATOM   401   C  CZ  . TYR   A 1 51   ? -63.03700  62.71600  24.60600  1.000 57.19773  ?  51   TYR   A CZ  1 
ATOM   402   O  OH  . TYR   A 1 51   ? -62.09700  62.49400  23.62600  1.000 56.90841  ?  51   TYR   A OH  1 
ATOM   403   N  N   . ALA   A 1 52   ? -63.92800  66.00000  29.05700  1.000 50.38970  ?  52   ALA   A N   1 
ATOM   404   C  CA  . ALA   A 1 52   ? -63.44800  67.37400  28.90300  1.000 44.81082  ?  52   ALA   A CA  1 
ATOM   405   C  C   . ALA   A 1 52   ? -64.49600  68.36700  29.39900  1.000 50.66231  ?  52   ALA   A C   1 
ATOM   406   O  O   . ALA   A 1 52   ? -64.92800  69.27700  28.68800  1.000 54.45318  ?  52   ALA   A O   1 
ATOM   407   C  CB  . ALA   A 1 52   ? -63.05600  67.66000  27.45100  1.000 45.68413  ?  52   ALA   A CB  1 
ATOM   408   N  N   . TYR   A 1 53   ? -64.90700  68.16800  30.64900  1.000 42.55890  ?  53   TYR   A N   1 
ATOM   409   C  CA  . TYR   A 1 53   ? -65.94100  68.98400  31.27600  1.000 51.87064  ?  53   TYR   A CA  1 
ATOM   410   C  C   . TYR   A 1 53   ? -65.28200  70.01900  32.17900  1.000 52.54949  ?  53   TYR   A C   1 
ATOM   411   O  O   . TYR   A 1 53   ? -64.79100  69.68700  33.26300  1.000 65.50577  ?  53   TYR   A O   1 
ATOM   412   C  CB  . TYR   A 1 53   ? -66.92100  68.11800  32.06400  1.000 54.40626  ?  53   TYR   A CB  1 
ATOM   413   C  CG  . TYR   A 1 53   ? -68.01800  68.90700  32.75000  1.000 61.92207  ?  53   TYR   A CG  1 
ATOM   414   C  CD1 . TYR   A 1 53   ? -69.03600  69.49800  32.01400  1.000 69.81695  ?  53   TYR   A CD1 1 
ATOM   415   C  CD2 . TYR   A 1 53   ? -68.03800  69.05500  34.13200  1.000 63.58350  ?  53   TYR   A CD2 1 
ATOM   416   C  CE1 . TYR   A 1 53   ? -70.04100  70.22000  32.63200  1.000 71.72637  ?  53   TYR   A CE1 1 
ATOM   417   C  CE2 . TYR   A 1 53   ? -69.04100  69.77700  34.76000  1.000 59.33964  ?  53   TYR   A CE2 1 
ATOM   418   C  CZ  . TYR   A 1 53   ? -70.03900  70.35700  34.00300  1.000 62.40969  ?  53   TYR   A CZ  1 
ATOM   419   O  OH  . TYR   A 1 53   ? -71.03900  71.07400  34.62000  1.000 75.04053  ?  53   TYR   A OH  1 
ATOM   420   N  N   . GLY   A 1 54   ? -65.26400  71.26700  31.72500  1.000 53.75589  ?  54   GLY   A N   1 
ATOM   421   C  CA  . GLY   A 1 54   ? -64.96500  72.37400  32.60800  1.000 63.88442  ?  54   GLY   A CA  1 
ATOM   422   C  C   . GLY   A 1 54   ? -65.99800  72.48300  33.71400  1.000 78.36358  ?  54   GLY   A C   1 
ATOM   423   O  O   . GLY   A 1 54   ? -67.07600  71.88800  33.66400  1.000 95.00081  ?  54   GLY   A O   1 
ATOM   424   N  N   . TYR   A 1 55   ? -65.65200  73.26900  34.73300  1.000 59.83587  ?  55   TYR   A N   1 
ATOM   425   C  CA  . TYR   A 1 55   ? -66.40700  73.36700  35.98300  1.000 75.75179  ?  55   TYR   A CA  1 
ATOM   426   C  C   . TYR   A 1 55   ? -66.29900  72.06800  36.77700  1.000 73.86018  ?  55   TYR   A C   1 
ATOM   427   O  O   . TYR   A 1 55   ? -66.16300  70.98400  36.19900  1.000 57.19230  ?  55   TYR   A O   1 
ATOM   428   C  CB  . TYR   A 1 55   ? -67.88700  73.70200  35.74500  1.000 61.50084  ?  55   TYR   A CB  1 
ATOM   429   C  CG  . TYR   A 1 55   ? -68.16500  74.68300  34.62400  1.000 61.02230  ?  55   TYR   A CG  1 
ATOM   430   C  CD1 . TYR   A 1 55   ? -67.46900  75.88000  34.52500  1.000 74.22099  ?  55   TYR   A CD1 1 
ATOM   431   C  CD2 . TYR   A 1 55   ? -69.13500  74.40900  33.66700  1.000 70.38525  ?  55   TYR   A CD2 1 
ATOM   432   C  CE1 . TYR   A 1 55   ? -67.73100  76.77700  33.50400  1.000 78.18880  ?  55   TYR   A CE1 1 
ATOM   433   C  CE2 . TYR   A 1 55   ? -69.40300  75.29700  32.64300  1.000 75.95827  ?  55   TYR   A CE2 1 
ATOM   434   C  CZ  . TYR   A 1 55   ? -68.69900  76.47900  32.56600  1.000 70.09040  ?  55   TYR   A CZ  1 
ATOM   435   O  OH  . TYR   A 1 55   ? -68.96300  77.36500  31.54700  1.000 68.76749  ?  55   TYR   A OH  1 
ATOM   436   N  N   . ILE   A 1 56   ? -66.36100  72.16600  38.10100  1.000 73.81505  ?  56   ILE   A N   1 
ATOM   437   C  CA  . ILE   A 1 56   ? -66.31200  71.00800  38.98700  1.000 68.49266  ?  56   ILE   A CA  1 
ATOM   438   C  C   . ILE   A 1 56   ? -67.72100  70.72700  39.49000  1.000 71.22480  ?  56   ILE   A C   1 
ATOM   439   O  O   . ILE   A 1 56   ? -68.44000  71.65000  39.89500  1.000 71.82618  ?  56   ILE   A O   1 
ATOM   440   C  CB  . ILE   A 1 56   ? -65.33800  71.24100  40.15500  1.000 68.31820  ?  56   ILE   A CB  1 
ATOM   441   C  CG1 . ILE   A 1 56   ? -63.88800  71.12800  39.67500  1.000 56.67452  ?  56   ILE   A CG1 1 
ATOM   442   C  CG2 . ILE   A 1 56   ? -65.59800  70.25300  41.28400  1.000 46.71402  ?  56   ILE   A CG2 1 
ATOM   443   C  CD1 . ILE   A 1 56   ? -63.44700  69.70500  39.38100  1.000 64.95285  ?  56   ILE   A CD1 1 
ATOM   444   N  N   . LEU   A 1 57   ? -68.11700  69.45700  39.45800  1.000 73.06801  ?  57   LEU   A N   1 
ATOM   445   C  CA  . LEU   A 1 57   ? -69.45100  69.06600  39.88800  1.000 66.88591  ?  57   LEU   A CA  1 
ATOM   446   C  C   . LEU   A 1 57   ? -69.64000  69.32000  41.38000  1.000 79.22464  ?  57   LEU   A C   1 
ATOM   447   O  O   . LEU   A 1 57   ? -68.69100  69.28200  42.16700  1.000 82.82928  ?  57   LEU   A O   1 
ATOM   448   C  CB  . LEU   A 1 57   ? -69.69800  67.59000  39.57700  1.000 54.66534  ?  57   LEU   A CB  1 
ATOM   449   C  CG  . LEU   A 1 57   ? -71.00400  67.27100  38.85400  1.000 44.64611  ?  57   LEU   A CG  1 
ATOM   450   C  CD1 . LEU   A 1 57   ? -71.04300  68.01100  37.53500  1.000 58.16628  ?  57   LEU   A CD1 1 
ATOM   451   C  CD2 . LEU   A 1 57   ? -71.14700  65.77500  38.63500  1.000 51.91709  ?  57   LEU   A CD2 1 
ATOM   452   N  N   . ASP   A 1 58   ? -70.88900  69.57400  41.76400  1.000 88.25415  ?  58   ASP   A N   1 
ATOM   453   C  CA  . ASP   A 1 58   ? -71.20300  69.85600  43.15500  1.000 88.64298  ?  58   ASP   A CA  1 
ATOM   454   C  C   . ASP   A 1 58   ? -71.00900  68.60900  44.01400  1.000 87.49933  ?  58   ASP   A C   1 
ATOM   455   O  O   . ASP   A 1 58   ? -71.00200  67.47400  43.52900  1.000 80.62465  ?  58   ASP   A O   1 
ATOM   456   C  CB  . ASP   A 1 58   ? -72.63500  70.37400  43.29500  1.000 101.83517 ?  58   ASP   A CB  1 
ATOM   457   C  CG  . ASP   A 1 58   ? -72.91300  70.96100  44.66900  1.000 111.00110 ?  58   ASP   A CG  1 
ATOM   458   O  OD1 . ASP   A 1 58   ? -72.56600  72.14000  44.89600  1.000 104.36070 ?  58   ASP   A OD1 1 
ATOM   459   O  OD2 . ASP   A 1 58   ? -73.46800  70.24000  45.52500  1.000 101.62111 -1 58   ASP   A OD2 1 
ATOM   460   N  N   . LYS   A 1 59   ? -70.85600  68.84300  45.31800  1.000 87.67181  ?  59   LYS   A N   1 
ATOM   461   C  CA  . LYS   A 1 59   ? -70.53600  67.76600  46.24800  1.000 87.67542  ?  59   LYS   A CA  1 
ATOM   462   C  C   . LYS   A 1 59   ? -71.68900  66.77700  46.36500  1.000 86.37390  ?  59   LYS   A C   1 
ATOM   463   O  O   . LYS   A 1 59   ? -71.48000  65.55700  46.34800  1.000 69.99537  ?  59   LYS   A O   1 
ATOM   464   C  CB  . LYS   A 1 59   ? -70.18800  68.35400  47.61700  1.000 86.51968  ?  59   LYS   A CB  1 
ATOM   465   C  CG  . LYS   A 1 59   ? -68.76000  68.89000  47.75000  1.000 92.85095  ?  59   LYS   A CG  1 
ATOM   466   C  CD  . LYS   A 1 59   ? -68.47300  70.09900  46.86600  1.000 97.19792  ?  59   LYS   A CD  1 
ATOM   467   C  CE  . LYS   A 1 59   ? -69.38300  71.26700  47.20200  1.000 98.58750  ?  59   LYS   A CE  1 
ATOM   468   N  NZ  . LYS   A 1 59   ? -68.69000  72.56000  46.96800  1.000 82.86393  ?  59   LYS   A NZ  1 
ATOM   469   N  N   . GLU   A 1 60   ? -72.91500  67.28900  46.50000  1.000 85.97439  ?  60   GLU   A N   1 
ATOM   470   C  CA  . GLU   A 1 60   ? -74.08200  66.42100  46.61400  1.000 84.68223  ?  60   GLU   A CA  1 
ATOM   471   C  C   . GLU   A 1 60   ? -74.22300  65.50900  45.40400  1.000 90.20987  ?  60   GLU   A C   1 
ATOM   472   O  O   . GLU   A 1 60   ? -74.66600  64.36300  45.53900  1.000 82.70344  ?  60   GLU   A O   1 
ATOM   473   C  CB  . GLU   A 1 60   ? -75.34300  67.26700  46.79000  1.000 94.05143  ?  60   GLU   A CB  1 
ATOM   474   C  CG  . GLU   A 1 60   ? -75.32500  68.16900  48.01500  1.000 109.99663 ?  60   GLU   A CG  1 
ATOM   475   C  CD  . GLU   A 1 60   ? -75.69100  67.43600  49.29200  1.000 127.78885 ?  60   GLU   A CD  1 
ATOM   476   O  OE1 . GLU   A 1 60   ? -75.21400  66.29800  49.48800  1.000 121.80115 ?  60   GLU   A OE1 1 
ATOM   477   O  OE2 . GLU   A 1 60   ? -76.46200  67.99800  50.09800  1.000 127.03635 -1 60   GLU   A OE2 1 
ATOM   478   N  N   . ILE   A 1 61   ? -73.84300  65.99200  44.22000  1.000 90.42148  ?  61   ILE   A N   1 
ATOM   479   C  CA  . ILE   A 1 61   ? -73.97800  65.18700  43.01200  1.000 68.18227  ?  61   ILE   A CA  1 
ATOM   480   C  C   . ILE   A 1 61   ? -72.99300  64.02500  43.02900  1.000 68.76448  ?  61   ILE   A C   1 
ATOM   481   O  O   . ILE   A 1 61   ? -73.32200  62.91000  42.60800  1.000 74.37033  ?  61   ILE   A O   1 
ATOM   482   C  CB  . ILE   A 1 61   ? -73.79200  66.06800  41.76500  1.000 68.43104  ?  61   ILE   A CB  1 
ATOM   483   C  CG1 . ILE   A 1 61   ? -74.53300  67.39500  41.93900  1.000 65.14241  ?  61   ILE   A CG1 1 
ATOM   484   C  CG2 . ILE   A 1 61   ? -74.28500  65.34000  40.52600  1.000 72.38670  ?  61   ILE   A CG2 1 
ATOM   485   C  CD1 . ILE   A 1 61   ? -74.48800  68.28800  40.71800  1.000 71.08757  ?  61   ILE   A CD1 1 
ATOM   486   N  N   . VAL   A 1 62   ? -71.77300  64.26500  43.51600  1.000 64.87610  ?  62   VAL   A N   1 
ATOM   487   C  CA  . VAL   A 1 62   ? -70.75900  63.21400  43.54200  1.000 67.13907  ?  62   VAL   A CA  1 
ATOM   488   C  C   . VAL   A 1 62   ? -71.18400  62.08400  44.47100  1.000 81.93547  ?  62   VAL   A C   1 
ATOM   489   O  O   . VAL   A 1 62   ? -70.94600  60.90300  44.18700  1.000 82.58084  ?  62   VAL   A O   1 
ATOM   490   C  CB  . VAL   A 1 62   ? -69.39300  63.79900  43.94600  1.000 68.94029  ?  62   VAL   A CB  1 
ATOM   491   C  CG1 . VAL   A 1 62   ? -68.32300  62.71600  43.93300  1.000 60.36615  ?  62   VAL   A CG1 1 
ATOM   492   C  CG2 . VAL   A 1 62   ? -69.01300  64.94400  43.01900  1.000 58.70164  ?  62   VAL   A CG2 1 
ATOM   493   N  N   . SER   A 1 63   ? -71.82800  62.42400  45.58800  1.000 85.51992  ?  63   SER   A N   1 
ATOM   494   C  CA  . SER   A 1 63   ? -72.28000  61.40400  46.52700  1.000 81.67757  ?  63   SER   A CA  1 
ATOM   495   C  C   . SER   A 1 63   ? -73.58500  60.76000  46.07400  1.000 81.83000  ?  63   SER   A C   1 
ATOM   496   O  O   . SER   A 1 63   ? -73.78600  59.55600  46.26800  1.000 73.69057  ?  63   SER   A O   1 
ATOM   497   C  CB  . SER   A 1 63   ? -72.43800  62.01600  47.91900  1.000 88.75126  ?  63   SER   A CB  1 
ATOM   498   O  OG  . SER   A 1 63   ? -73.11000  63.26200  47.85000  1.000 89.69728  ?  63   SER   A OG  1 
ATOM   499   N  N   . ARG   A 1 64   ? -74.47900  61.54600  45.46700  1.000 70.41995  ?  64   ARG   A N   1 
ATOM   500   C  CA  . ARG   A 1 64   ? -75.76300  61.01300  45.02500  1.000 67.83681  ?  64   ARG   A CA  1 
ATOM   501   C  C   . ARG   A 1 64   ? -75.58800  60.01100  43.88900  1.000 73.07584  ?  64   ARG   A C   1 
ATOM   502   O  O   . ARG   A 1 64   ? -76.23400  58.95600  43.87900  1.000 65.28030  ?  64   ARG   A O   1 
ATOM   503   C  CB  . ARG   A 1 64   ? -76.67600  62.16500  44.60400  1.000 56.52025  ?  64   ARG   A CB  1 
ATOM   504   C  CG  . ARG   A 1 64   ? -78.06300  61.77100  44.13200  1.000 64.59522  ?  64   ARG   A CG  1 
ATOM   505   C  CD  . ARG   A 1 64   ? -78.90800  63.02100  43.93800  1.000 68.04232  ?  64   ARG   A CD  1 
ATOM   506   N  NE  . ARG   A 1 64   ? -79.90400  62.87300  42.88400  1.000 83.83332  ?  64   ARG   A NE  1 
ATOM   507   C  CZ  . ARG   A 1 64   ? -80.58200  63.88200  42.35400  1.000 83.55742  ?  64   ARG   A CZ  1 
ATOM   508   N  NH1 . ARG   A 1 64   ? -80.39400  65.12800  42.75700  1.000 69.28843  ?  64   ARG   A NH1 1 
ATOM   509   N  NH2 . ARG   A 1 64   ? -81.46800  63.63500  41.39300  1.000 78.84405  ?  64   ARG   A NH2 1 
ATOM   510   N  N   . PHE   A 1 65   ? -74.71100  60.31400  42.93100  1.000 75.11609  ?  65   PHE   A N   1 
ATOM   511   C  CA  . PHE   A 1 65   ? -74.43800  59.43600  41.80000  1.000 72.84885  ?  65   PHE   A CA  1 
ATOM   512   C  C   . PHE   A 1 65   ? -73.13800  58.65500  41.97100  1.000 73.35292  ?  65   PHE   A C   1 
ATOM   513   O  O   . PHE   A 1 65   ? -72.47800  58.32900  40.97900  1.000 69.74097  ?  65   PHE   A O   1 
ATOM   514   C  CB  . PHE   A 1 65   ? -74.40400  60.24100  40.50000  1.000 65.74787  ?  65   PHE   A CB  1 
ATOM   515   C  CG  . PHE   A 1 65   ? -75.75200  60.73500  40.05400  1.000 68.42399  ?  65   PHE   A CG  1 
ATOM   516   C  CD1 . PHE   A 1 65   ? -76.31700  61.86300  40.62700  1.000 71.22231  ?  65   PHE   A CD1 1 
ATOM   517   C  CD2 . PHE   A 1 65   ? -76.45100  60.07700  39.05500  1.000 67.39523  ?  65   PHE   A CD2 1 
ATOM   518   C  CE1 . PHE   A 1 65   ? -77.55500  62.32000  40.21800  1.000 65.00655  ?  65   PHE   A CE1 1 
ATOM   519   C  CE2 . PHE   A 1 65   ? -77.68900  60.53100  38.64000  1.000 66.09349  ?  65   PHE   A CE2 1 
ATOM   520   C  CZ  . PHE   A 1 65   ? -78.24200  61.65400  39.22200  1.000 74.35187  ?  65   PHE   A CZ  1 
ATOM   521   N  N   . ARG   A 1 66   ? -72.76200  58.34500  43.21200  1.000 81.80115  ?  66   ARG   A N   1 
ATOM   522   C  CA  . ARG   A 1 66   ? -71.50700  57.64500  43.46600  1.000 78.02195  ?  66   ARG   A CA  1 
ATOM   523   C  C   . ARG   A 1 66   ? -71.50100  56.28700  42.77700  1.000 72.36898  ?  66   ARG   A C   1 
ATOM   524   O  O   . ARG   A 1 66   ? -72.48000  55.53800  42.83900  1.000 77.32166  ?  66   ARG   A O   1 
ATOM   525   C  CB  . ARG   A 1 66   ? -71.28700  57.48300  44.97000  1.000 83.38846  ?  66   ARG   A CB  1 
ATOM   526   C  CG  . ARG   A 1 66   ? -70.05800  56.66200  45.33500  1.000 78.59482  ?  66   ARG   A CG  1 
ATOM   527   C  CD  . ARG   A 1 66   ? -69.50500  57.07900  46.68700  1.000 74.31238  ?  66   ARG   A CD  1 
ATOM   528   N  NE  . ARG   A 1 66   ? -68.92700  58.41700  46.64100  1.000 105.62721 ?  66   ARG   A NE  1 
ATOM   529   C  CZ  . ARG   A 1 66   ? -67.62500  58.67100  46.60600  1.000 120.59333 ?  66   ARG   A CZ  1 
ATOM   530   N  NH1 . ARG   A 1 66   ? -66.73000  57.69800  46.64500  1.000 116.97883 ?  66   ARG   A NH1 1 
ATOM   531   N  NH2 . ARG   A 1 66   ? -67.21200  59.93400  46.53600  1.000 94.77330  ?  66   ARG   A NH2 1 
ATOM   532   N  N   . GLY   A 1 67   ? -70.38700  55.97300  42.11800  1.000 65.31828  ?  67   GLY   A N   1 
ATOM   533   C  CA  . GLY   A 1 67   ? -70.29900  54.79300  41.28800  1.000 61.44568  ?  67   GLY   A CA  1 
ATOM   534   C  C   . GLY   A 1 67   ? -70.98200  54.91700  39.94600  1.000 70.08608  ?  67   GLY   A C   1 
ATOM   535   O  O   . GLY   A 1 67   ? -70.97300  53.95000  39.17300  1.000 74.52257  ?  67   GLY   A O   1 
ATOM   536   N  N   . ARG   A 1 68   ? -71.57700  56.07300  39.64400  1.000 67.73983  ?  68   ARG   A N   1 
ATOM   537   C  CA  . ARG   A 1 68   ? -72.26900  56.29100  38.38100  1.000 69.36410  ?  68   ARG   A CA  1 
ATOM   538   C  C   . ARG   A 1 68   ? -71.79100  57.55300  37.67100  1.000 72.48399  ?  68   ARG   A C   1 
ATOM   539   O  O   . ARG   A 1 68   ? -72.43100  57.98700  36.70600  1.000 79.92959  ?  68   ARG   A O   1 
ATOM   540   C  CB  . ARG   A 1 68   ? -73.78600  56.34900  38.60600  1.000 68.68081  ?  68   ARG   A CB  1 
ATOM   541   C  CG  . ARG   A 1 68   ? -74.33000  55.15400  39.38400  1.000 77.62065  ?  68   ARG   A CG  1 
ATOM   542   C  CD  . ARG   A 1 68   ? -75.84900  55.16300  39.48200  1.000 70.39157  ?  68   ARG   A CD  1 
ATOM   543   N  NE  . ARG   A 1 68   ? -76.36300  56.37100  40.11600  1.000 77.64042  ?  68   ARG   A NE  1 
ATOM   544   C  CZ  . ARG   A 1 68   ? -77.64700  56.59900  40.35700  1.000 83.91125  ?  68   ARG   A CZ  1 
ATOM   545   N  NH1 . ARG   A 1 68   ? -78.57900  55.71500  40.03700  1.000 96.51077  ?  68   ARG   A NH1 1 
ATOM   546   N  NH2 . ARG   A 1 68   ? -78.00600  57.74200  40.93500  1.000 80.62369  ?  68   ARG   A NH2 1 
ATOM   547   N  N   . ILE   A 1 69   ? -70.69400  58.15300  38.12500  1.000 60.92295  ?  69   ILE   A N   1 
ATOM   548   C  CA  . ILE   A 1 69   ? -70.06500  59.28500  37.45400  1.000 59.34956  ?  69   ILE   A CA  1 
ATOM   549   C  C   . ILE   A 1 69   ? -68.76600  58.78600  36.84100  1.000 63.62211  ?  69   ILE   A C   1 
ATOM   550   O  O   . ILE   A 1 69   ? -67.87600  58.31000  37.55600  1.000 69.31928  ?  69   ILE   A O   1 
ATOM   551   C  CB  . ILE   A 1 69   ? -69.80700  60.45100  38.41700  1.000 56.86159  ?  69   ILE   A CB  1 
ATOM   552   C  CG1 . ILE   A 1 69   ? -70.92600  60.54100  39.44700  1.000 59.25062  ?  69   ILE   A CG1 1 
ATOM   553   C  CG2 . ILE   A 1 69   ? -69.70900  61.76100  37.65300  1.000 49.23605  ?  69   ILE   A CG2 1 
ATOM   554   C  CD1 . ILE   A 1 69   ? -70.81500  61.73700  40.34200  1.000 72.40714  ?  69   ILE   A CD1 1 
ATOM   555   N  N   . ILE   A 1 70   ? -68.65400  58.89300  35.52000  1.000 58.71269  ?  70   ILE   A N   1 
ATOM   556   C  CA  . ILE   A 1 70   ? -67.52900  58.33700  34.78000  1.000 59.71715  ?  70   ILE   A CA  1 
ATOM   557   C  C   . ILE   A 1 70   ? -66.89600  59.44900  33.95700  1.000 62.79152  ?  70   ILE   A C   1 
ATOM   558   O  O   . ILE   A 1 70   ? -67.57700  60.09700  33.15400  1.000 62.32206  ?  70   ILE   A O   1 
ATOM   559   C  CB  . ILE   A 1 70   ? -67.96200  57.17200  33.87600  1.000 35.86399  ?  70   ILE   A CB  1 
ATOM   560   C  CG1 . ILE   A 1 70   ? -68.47100  56.00900  34.72600  1.000 41.23129  ?  70   ILE   A CG1 1 
ATOM   561   C  CG2 . ILE   A 1 70   ? -66.81600  56.72700  32.99200  1.000 44.18364  ?  70   ILE   A CG2 1 
ATOM   562   C  CD1 . ILE   A 1 70   ? -68.83000  54.78800  33.92300  1.000 56.81610  ?  70   ILE   A CD1 1 
ATOM   563   N  N   . ASN   A 1 71   ? -65.60000  59.66700  34.15200  1.000 59.28165  ?  71   ASN   A N   1 
ATOM   564   C  CA  . ASN   A 1 71   ? -64.85200  60.65800  33.39700  1.000 50.88246  ?  71   ASN   A CA  1 
ATOM   565   C  C   . ASN   A 1 71   ? -63.87400  59.96900  32.45600  1.000 58.99040  ?  71   ASN   A C   1 
ATOM   566   O  O   . ASN   A 1 71   ? -63.33300  58.90300  32.76400  1.000 59.80125  ?  71   ASN   A O   1 
ATOM   567   C  CB  . ASN   A 1 71   ? -64.09600  61.61200  34.32800  1.000 38.99660  ?  71   ASN   A CB  1 
ATOM   568   C  CG  . ASN   A 1 71   ? -63.45800  62.76700  33.58100  1.000 47.56816  ?  71   ASN   A CG  1 
ATOM   569   O  OD1 . ASN   A 1 71   ? -64.13800  63.71100  33.17900  1.000 43.82160  ?  71   ASN   A OD1 1 
ATOM   570   N  ND2 . ASN   A 1 71   ? -62.14500  62.70000  33.39300  1.000 57.88545  ?  71   ASN   A ND2 1 
ATOM   571   N  N   . LEU   A 1 72   ? -63.65900  60.58800  31.30100  1.000 60.89113  ?  72   LEU   A N   1 
ATOM   572   C  CA  . LEU   A 1 72   ? -62.71400  60.10600  30.30000  1.000 57.43153  ?  72   LEU   A CA  1 
ATOM   573   C  C   . LEU   A 1 72   ? -61.54100  61.08000  30.28200  1.000 54.72132  ?  72   LEU   A C   1 
ATOM   574   O  O   . LEU   A 1 72   ? -61.63600  62.17200  29.71500  1.000 53.04219  ?  72   LEU   A O   1 
ATOM   575   C  CB  . LEU   A 1 72   ? -63.37400  59.98700  28.92800  1.000 59.76926  ?  72   LEU   A CB  1 
ATOM   576   C  CG  . LEU   A 1 72   ? -64.30900  58.79500  28.68900  1.000 53.64326  ?  72   LEU   A CG  1 
ATOM   577   C  CD1 . LEU   A 1 72   ? -65.65200  58.98500  29.37700  1.000 42.86767  ?  72   LEU   A CD1 1 
ATOM   578   C  CD2 . LEU   A 1 72   ? -64.49700  58.55200  27.20000  1.000 49.50414  ?  72   LEU   A CD2 1 
ATOM   579   N  N   . HIS   A 1 73   ? -60.43700  60.68400  30.91700  1.000 50.10043  ?  73   HIS   A N   1 
ATOM   580   C  CA  . HIS   A 1 73   ? -59.26900  61.54000  31.03300  1.000 42.00538  ?  73   HIS   A CA  1 
ATOM   581   C  C   . HIS   A 1 73   ? -58.15700  61.02900  30.13200  1.000 47.86798  ?  73   HIS   A C   1 
ATOM   582   O  O   . HIS   A 1 73   ? -57.81100  59.84100  30.19400  1.000 51.14641  ?  73   HIS   A O   1 
ATOM   583   C  CB  . HIS   A 1 73   ? -58.78000  61.59600  32.48300  1.000 47.26018  ?  73   HIS   A CB  1 
ATOM   584   C  CG  . HIS   A 1 73   ? -57.80500  62.70000  32.74600  1.000 45.63175  ?  73   HIS   A CG  1 
ATOM   585   N  ND1 . HIS   A 1 73   ? -58.18100  64.02500  32.81100  1.000 56.95473  ?  73   HIS   A ND1 1 
ATOM   586   C  CD2 . HIS   A 1 73   ? -56.46700  62.67900  32.94900  1.000 39.91567  ?  73   HIS   A CD2 1 
ATOM   587   C  CE1 . HIS   A 1 73   ? -57.11800  64.77200  33.04800  1.000 51.29862  ?  73   HIS   A CE1 1 
ATOM   588   N  NE2 . HIS   A 1 73   ? -56.06500  63.97900  33.13700  1.000 50.83554  ?  73   HIS   A NE2 1 
ATOM   589   N  N   . PRO   A 1 74   ? -57.58000  61.88800  29.27900  1.000 47.48197  ?  74   PRO   A N   1 
ATOM   590   C  CA  . PRO   A 1 74   ? -56.52500  61.47500  28.34400  1.000 45.85750  ?  74   PRO   A CA  1 
ATOM   591   C  C   . PRO   A 1 74   ? -55.13400  61.39200  28.97100  1.000 53.41381  ?  74   PRO   A C   1 
ATOM   592   O  O   . PRO   A 1 74   ? -54.17000  61.97200  28.47000  1.000 56.12008  ?  74   PRO   A O   1 
ATOM   593   C  CB  . PRO   A 1 74   ? -56.59500  62.55700  27.26200  1.000 42.43332  ?  74   PRO   A CB  1 
ATOM   594   C  CG  . PRO   A 1 74   ? -57.05400  63.76800  27.99400  1.000 40.33125  ?  74   PRO   A CG  1 
ATOM   595   C  CD  . PRO   A 1 74   ? -58.00100  63.28200  29.05800  1.000 34.95707  ?  74   PRO   A CD  1 
ATOM   596   N  N   . SER   A 1 75   ? -55.03000  60.66100  30.07800  1.000 50.73954  ?  75   SER   A N   1 
ATOM   597   C  CA  . SER   A 1 75   ? -53.75300  60.47300  30.74500  1.000 45.53320  ?  75   SER   A CA  1 
ATOM   598   C  C   . SER   A 1 75   ? -53.78000  59.15200  31.49500  1.000 54.92875  ?  75   SER   A C   1 
ATOM   599   O  O   . SER   A 1 75   ? -54.84200  58.57600  31.73800  1.000 66.91458  ?  75   SER   A O   1 
ATOM   600   C  CB  . SER   A 1 75   ? -53.43200  61.62800  31.70100  1.000 51.70589  ?  75   SER   A CB  1 
ATOM   601   O  OG  . SER   A 1 75   ? -53.46200  61.19500  33.05000  1.000 52.10880  ?  75   SER   A OG  1 
ATOM   602   N  N   . LEU   A 1 76   ? -52.58900  58.67800  31.85800  1.000 63.89559  ?  76   LEU   A N   1 
ATOM   603   C  CA  . LEU   A 1 76   ? -52.45000  57.45700  32.65000  1.000 61.96459  ?  76   LEU   A CA  1 
ATOM   604   C  C   . LEU   A 1 76   ? -52.39600  57.85700  34.12300  1.000 63.42027  ?  76   LEU   A C   1 
ATOM   605   O  O   . LEU   A 1 76   ? -51.33700  57.90000  34.75400  1.000 65.42185  ?  76   LEU   A O   1 
ATOM   606   C  CB  . LEU   A 1 76   ? -51.21000  56.67900  32.22600  1.000 58.57900  ?  76   LEU   A CB  1 
ATOM   607   C  CG  . LEU   A 1 76   ? -51.17800  55.19500  32.60700  1.000 57.66993  ?  76   LEU   A CG  1 
ATOM   608   C  CD1 . LEU   A 1 76   ? -51.83900  54.34300  31.53100  1.000 64.23298  ?  76   LEU   A CD1 1 
ATOM   609   C  CD2 . LEU   A 1 76   ? -49.76100  54.70900  32.89100  1.000 55.44702  ?  76   LEU   A CD2 1 
ATOM   610   N  N   . LEU   A 1 77   ? -53.57200  58.17600  34.66500  1.000 54.31806  ?  77   LEU   A N   1 
ATOM   611   C  CA  . LEU   A 1 77   ? -53.68800  58.52600  36.07300  1.000 54.91111  ?  77   LEU   A CA  1 
ATOM   612   C  C   . LEU   A 1 77   ? -53.06700  57.42400  36.92700  1.000 64.91485  ?  77   LEU   A C   1 
ATOM   613   O  O   . LEU   A 1 77   ? -53.25500  56.23600  36.63300  1.000 61.94890  ?  77   LEU   A O   1 
ATOM   614   C  CB  . LEU   A 1 77   ? -55.15600  58.73000  36.45400  1.000 47.48485  ?  77   LEU   A CB  1 
ATOM   615   C  CG  . LEU   A 1 77   ? -55.89700  59.75200  35.59100  1.000 55.88548  ?  77   LEU   A CG  1 
ATOM   616   C  CD1 . LEU   A 1 77   ? -57.37500  59.81700  35.94700  1.000 44.15922  ?  77   LEU   A CD1 1 
ATOM   617   C  CD2 . LEU   A 1 77   ? -55.25000  61.12400  35.70300  1.000 55.03910  ?  77   LEU   A CD2 1 
ATOM   618   N  N   . PRO   A 1 78   ? -52.34100  57.76500  37.99400  1.000 63.96945  ?  78   PRO   A N   1 
ATOM   619   C  CA  . PRO   A 1 78   ? -52.22000  59.06500  38.67300  1.000 55.07690  ?  78   PRO   A CA  1 
ATOM   620   C  C   . PRO   A 1 78   ? -51.32200  60.11700  38.02000  1.000 58.18831  ?  78   PRO   A C   1 
ATOM   621   O  O   . PRO   A 1 78   ? -50.98700  61.08800  38.68300  1.000 58.32858  ?  78   PRO   A O   1 
ATOM   622   C  CB  . PRO   A 1 78   ? -51.62800  58.66000  40.02300  1.000 61.95174  ?  78   PRO   A CB  1 
ATOM   623   C  CG  . PRO   A 1 78   ? -50.67800  57.55500  39.63700  1.000 57.34049  ?  78   PRO   A CG  1 
ATOM   624   C  CD  . PRO   A 1 78   ? -51.39500  56.78400  38.55400  1.000 58.79250  ?  78   PRO   A CD  1 
ATOM   625   N  N   . TRP   A 1 79   ? -50.89200  59.99300  36.77000  1.000 62.86879  ?  79   TRP   A N   1 
ATOM   626   C  CA  . TRP   A 1 79   ? -50.00400  60.97900  36.17100  1.000 49.45633  ?  79   TRP   A CA  1 
ATOM   627   C  C   . TRP   A 1 79   ? -50.80200  61.98600  35.35500  1.000 43.10025  ?  79   TRP   A C   1 
ATOM   628   O  O   . TRP   A 1 79   ? -51.75000  61.62100  34.65200  1.000 49.50623  ?  79   TRP   A O   1 
ATOM   629   C  CB  . TRP   A 1 79   ? -48.95000  60.30500  35.29100  1.000 50.28999  ?  79   TRP   A CB  1 
ATOM   630   C  CG  . TRP   A 1 79   ? -48.04400  59.39200  36.05400  1.000 49.19481  ?  79   TRP   A CG  1 
ATOM   631   C  CD1 . TRP   A 1 79   ? -48.23600  58.06300  36.29600  1.000 47.55917  ?  79   TRP   A CD1 1 
ATOM   632   C  CD2 . TRP   A 1 79   ? -46.80600  59.74000  36.68400  1.000 54.82761  ?  79   TRP   A CD2 1 
ATOM   633   N  NE1 . TRP   A 1 79   ? -47.19300  57.56100  37.03400  1.000 50.45562  ?  79   TRP   A NE1 1 
ATOM   634   C  CE2 . TRP   A 1 79   ? -46.30100  58.57000  37.28600  1.000 66.04857  ?  79   TRP   A CE2 1 
ATOM   635   C  CE3 . TRP   A 1 79   ? -46.07400  60.92600  36.79600  1.000 66.70051  ?  79   TRP   A CE3 1 
ATOM   636   C  CZ2 . TRP   A 1 79   ? -45.09800  58.55200  37.99000  1.000 71.82942  ?  79   TRP   A CZ2 1 
ATOM   637   C  CZ3 . TRP   A 1 79   ? -44.87900  60.90500  37.49500  1.000 64.09271  ?  79   TRP   A CZ3 1 
ATOM   638   C  CH2 . TRP   A 1 79   ? -44.40400  59.72700  38.08300  1.000 63.73268  ?  79   TRP   A CH2 1 
ATOM   639   N  N   . ASN   A 1 80   ? -50.42100  63.26000  35.47300  1.000 47.78724  ?  80   ASN   A N   1 
ATOM   640   C  CA  . ASN   A 1 80   ? -50.99400  64.35200  34.68500  1.000 43.44921  ?  80   ASN   A CA  1 
ATOM   641   C  C   . ASN   A 1 80   ? -52.49400  64.50800  34.94900  1.000 45.19473  ?  80   ASN   A C   1 
ATOM   642   O  O   . ASN   A 1 80   ? -53.32900  64.42300  34.04600  1.000 50.98295  ?  80   ASN   A O   1 
ATOM   643   C  CB  . ASN   A 1 80   ? -50.71100  64.14400  33.19400  1.000 53.66482  ?  80   ASN   A CB  1 
ATOM   644   C  CG  . ASN   A 1 80   ? -49.26400  63.80200  32.92600  1.000 50.21982  ?  80   ASN   A CG  1 
ATOM   645   O  OD1 . ASN   A 1 80   ? -48.35800  64.54400  33.30800  1.000 52.90059  ?  80   ASN   A OD1 1 
ATOM   646   N  ND2 . ASN   A 1 80   ? -49.03500  62.66100  32.28800  1.000 57.53472  ?  80   ASN   A ND2 1 
ATOM   647   N  N   . LYS   A 1 81   ? -52.82200  64.74700  36.21600  1.000 53.53896  ?  81   LYS   A N   1 
ATOM   648   C  CA  . LYS   A 1 81   ? -54.19200  65.02500  36.62400  1.000 52.35014  ?  81   LYS   A CA  1 
ATOM   649   C  C   . LYS   A 1 81   ? -54.47600  66.51200  36.46800  1.000 54.31046  ?  81   LYS   A C   1 
ATOM   650   O  O   . LYS   A 1 81   ? -53.65900  67.35100  36.86200  1.000 60.41243  ?  81   LYS   A O   1 
ATOM   651   C  CB  . LYS   A 1 81   ? -54.42700  64.59500  38.07400  1.000 52.51027  ?  81   LYS   A CB  1 
ATOM   652   C  CG  . LYS   A 1 81   ? -54.14600  63.13000  38.34000  1.000 65.34372  ?  81   LYS   A CG  1 
ATOM   653   C  CD  . LYS   A 1 81   ? -53.19500  62.94700  39.50600  1.000 63.46209  ?  81   LYS   A CD  1 
ATOM   654   C  CE  . LYS   A 1 81   ? -53.89200  63.06500  40.84400  1.000 61.10213  ?  81   LYS   A CE  1 
ATOM   655   N  NZ  . LYS   A 1 81   ? -52.90900  62.92000  41.95300  1.000 93.80806  ?  81   LYS   A NZ  1 
ATOM   656   N  N   . GLY   A 1 82   ? -55.62900  66.83700  35.89200  1.000 48.10466  ?  82   GLY   A N   1 
ATOM   657   C  CA  . GLY   A 1 82   ? -56.02200  68.22500  35.76400  1.000 45.35303  ?  82   GLY   A CA  1 
ATOM   658   C  C   . GLY   A 1 82   ? -56.16600  68.70200  34.33400  1.000 53.36833  ?  82   GLY   A C   1 
ATOM   659   O  O   . GLY   A 1 82   ? -56.84900  68.07000  33.52300  1.000 59.01835  ?  82   GLY   A O   1 
ATOM   660   N  N   . ARG   A 1 83   ? -55.52100  69.82000  34.01700  1.000 42.98564  ?  83   ARG   A N   1 
ATOM   661   C  CA  . ARG   A 1 83   ? -55.65300  70.47300  32.72500  1.000 44.34827  ?  83   ARG   A CA  1 
ATOM   662   C  C   . ARG   A 1 83   ? -54.38900  70.29000  31.89600  1.000 48.43126  ?  83   ARG   A C   1 
ATOM   663   O  O   . ARG   A 1 83   ? -53.29000  70.10000  32.42700  1.000 46.71438  ?  83   ARG   A O   1 
ATOM   664   C  CB  . ARG   A 1 83   ? -55.95500  71.96400  32.90000  1.000 37.59690  ?  83   ARG   A CB  1 
ATOM   665   C  CG  . ARG   A 1 83   ? -57.26500  72.24000  33.61500  1.000 61.87014  ?  83   ARG   A CG  1 
ATOM   666   C  CD  . ARG   A 1 83   ? -58.45000  71.80200  32.77200  1.000 50.04835  ?  83   ARG   A CD  1 
ATOM   667   N  NE  . ARG   A 1 83   ? -58.54700  72.58300  31.54500  1.000 64.46523  ?  83   ARG   A NE  1 
ATOM   668   C  CZ  . ARG   A 1 83   ? -59.17300  73.74700  31.45000  1.000 79.30721  ?  83   ARG   A CZ  1 
ATOM   669   N  NH1 . ARG   A 1 83   ? -59.78200  74.29100  32.49100  1.000 62.51156  ?  83   ARG   A NH1 1 
ATOM   670   N  NH2 . ARG   A 1 83   ? -59.18800  74.38300  30.28100  1.000 63.65195  ?  83   ARG   A NH2 1 
ATOM   671   N  N   . ASP   A 1 84   ? -54.56700  70.36400  30.58000  1.000 51.37213  ?  84   ASP   A N   1 
ATOM   672   C  CA  . ASP   A 1 84   ? -53.49700  70.15900  29.61100  1.000 42.73481  ?  84   ASP   A CA  1 
ATOM   673   C  C   . ASP   A 1 84   ? -52.69900  68.88700  29.91400  1.000 55.97196  ?  84   ASP   A C   1 
ATOM   674   O  O   . ASP   A 1 84   ? -51.47400  68.93700  30.06400  1.000 49.04554  ?  84   ASP   A O   1 
ATOM   675   C  CB  . ASP   A 1 84   ? -52.58100  71.37400  29.55900  1.000 38.59555  ?  84   ASP   A CB  1 
ATOM   676   C  CG  . ASP   A 1 84   ? -53.33000  72.65600  29.23400  1.000 49.57759  ?  84   ASP   A CG  1 
ATOM   677   O  OD1 . ASP   A 1 84   ? -54.18200  72.63600  28.32100  1.000 56.40787  ?  84   ASP   A OD1 1 
ATOM   678   O  OD2 . ASP   A 1 84   ? -53.07300  73.68400  29.89700  1.000 62.14509  -1 84   ASP   A OD2 1 
ATOM   679   N  N   . PRO   A 1 85   ? -53.36300  67.73000  30.00200  1.000 54.61027  ?  85   PRO   A N   1 
ATOM   680   C  CA  . PRO   A 1 85   ? -52.65700  66.54000  30.50500  1.000 51.85262  ?  85   PRO   A CA  1 
ATOM   681   C  C   . PRO   A 1 85   ? -51.68600  65.93800  29.50500  1.000 46.23017  ?  85   PRO   A C   1 
ATOM   682   O  O   . PRO   A 1 85   ? -50.62100  65.45200  29.90700  1.000 56.11212  ?  85   PRO   A O   1 
ATOM   683   C  CB  . PRO   A 1 85   ? -53.80600  65.58000  30.83900  1.000 39.08306  ?  85   PRO   A CB  1 
ATOM   684   C  CG  . PRO   A 1 85   ? -54.87000  65.94100  29.86300  1.000 44.53484  ?  85   PRO   A CG  1 
ATOM   685   C  CD  . PRO   A 1 85   ? -54.76000  67.42800  29.63700  1.000 44.43021  ?  85   PRO   A CD  1 
ATOM   686   N  N   . VAL   A 1 86   ? -52.01700  65.95300  28.21300  1.000 51.22514  ?  86   VAL   A N   1 
ATOM   687   C  CA  . VAL   A 1 86   ? -51.15300  65.31300  27.22500  1.000 51.26280  ?  86   VAL   A CA  1 
ATOM   688   C  C   . VAL   A 1 86   ? -49.84200  66.07400  27.08300  1.000 49.81256  ?  86   VAL   A C   1 
ATOM   689   O  O   . VAL   A 1 86   ? -48.76600  65.47000  26.99900  1.000 50.55983  ?  86   VAL   A O   1 
ATOM   690   C  CB  . VAL   A 1 86   ? -51.88300  65.18100  25.87700  1.000 57.92437  ?  86   VAL   A CB  1 
ATOM   691   C  CG1 . VAL   A 1 86   ? -50.94500  64.61900  24.81900  1.000 48.60586  ?  86   VAL   A CG1 1 
ATOM   692   C  CG2 . VAL   A 1 86   ? -53.10700  64.29600  26.02900  1.000 46.46118  ?  86   VAL   A CG2 1 
ATOM   693   N  N   . PHE   A 1 87   ? -49.90500  67.40800  27.05500  1.000 45.40471  ?  87   PHE   A N   1 
ATOM   694   C  CA  . PHE   A 1 87   ? -48.67900  68.19500  26.98200  1.000 47.51775  ?  87   PHE   A CA  1 
ATOM   695   C  C   . PHE   A 1 87   ? -47.77400  67.91800  28.17600  1.000 49.66728  ?  87   PHE   A C   1 
ATOM   696   O  O   . PHE   A 1 87   ? -46.56100  67.74000  28.01700  1.000 60.70190  ?  87   PHE   A O   1 
ATOM   697   C  CB  . PHE   A 1 87   ? -49.00400  69.68500  26.90000  1.000 44.46585  ?  87   PHE   A CB  1 
ATOM   698   C  CG  . PHE   A 1 87   ? -47.83200  70.56400  27.21300  1.000 41.09319  ?  87   PHE   A CG  1 
ATOM   699   C  CD1 . PHE   A 1 87   ? -46.83200  70.76100  26.27900  1.000 53.71414  ?  87   PHE   A CD1 1 
ATOM   700   C  CD2 . PHE   A 1 87   ? -47.71800  71.17600  28.45000  1.000 40.33638  ?  87   PHE   A CD2 1 
ATOM   701   C  CE1 . PHE   A 1 87   ? -45.74700  71.55800  26.56500  1.000 58.03254  ?  87   PHE   A CE1 1 
ATOM   702   C  CE2 . PHE   A 1 87   ? -46.63500  71.97400  28.74100  1.000 56.40556  ?  87   PHE   A CE2 1 
ATOM   703   C  CZ  . PHE   A 1 87   ? -45.64800  72.16000  27.79800  1.000 53.66588  ?  87   PHE   A CZ  1 
ATOM   704   N  N   . TRP   A 1 88   ? -48.34500  67.88000  29.38200  1.000 45.70813  ?  88   TRP   A N   1 
ATOM   705   C  CA  . TRP   A 1 88   ? -47.54000  67.60400  30.56300  1.000 41.21201  ?  88   TRP   A CA  1 
ATOM   706   C  C   . TRP   A 1 88   ? -47.06700  66.15900  30.61500  1.000 49.43806  ?  88   TRP   A C   1 
ATOM   707   O  O   . TRP   A 1 88   ? -46.07800  65.87300  31.29800  1.000 65.43930  ?  88   TRP   A O   1 
ATOM   708   C  CB  . TRP   A 1 88   ? -48.32100  67.95100  31.83000  1.000 42.51111  ?  88   TRP   A CB  1 
ATOM   709   C  CG  . TRP   A 1 88   ? -48.47200  69.42500  32.03100  1.000 47.66723  ?  88   TRP   A CG  1 
ATOM   710   C  CD1 . TRP   A 1 88   ? -49.63700  70.13200  32.08300  1.000 48.90134  ?  88   TRP   A CD1 1 
ATOM   711   C  CD2 . TRP   A 1 88   ? -47.41600  70.38000  32.18800  1.000 49.41341  ?  88   TRP   A CD2 1 
ATOM   712   N  NE1 . TRP   A 1 88   ? -49.37300  71.46700  32.27100  1.000 46.19202  ?  88   TRP   A NE1 1 
ATOM   713   C  CE2 . TRP   A 1 88   ? -48.01600  71.64500  32.33800  1.000 51.13120  ?  88   TRP   A CE2 1 
ATOM   714   C  CE3 . TRP   A 1 88   ? -46.02100  70.28600  32.22100  1.000 44.05638  ?  88   TRP   A CE3 1 
ATOM   715   C  CZ2 . TRP   A 1 88   ? -47.27100  72.80600  32.51800  1.000 49.24980  ?  88   TRP   A CZ2 1 
ATOM   716   C  CZ3 . TRP   A 1 88   ? -45.28300  71.44100  32.39900  1.000 54.74553  ?  88   TRP   A CZ3 1 
ATOM   717   C  CH2 . TRP   A 1 88   ? -45.90900  72.68400  32.54500  1.000 51.06520  ?  88   TRP   A CH2 1 
ATOM   718   N  N   . SER   A 1 89   ? -47.74200  65.24600  29.91200  1.000 42.13516  ?  89   SER   A N   1 
ATOM   719   C  CA  . SER   A 1 89   ? -47.23800  63.88200  29.80600  1.000 52.76453  ?  89   SER   A CA  1 
ATOM   720   C  C   . SER   A 1 89   ? -45.91600  63.83200  29.05300  1.000 55.12419  ?  89   SER   A C   1 
ATOM   721   O  O   . SER   A 1 89   ? -45.14500  62.88400  29.23200  1.000 47.11347  ?  89   SER   A O   1 
ATOM   722   C  CB  . SER   A 1 89   ? -48.26600  62.98400  29.11500  1.000 40.02558  ?  89   SER   A CB  1 
ATOM   723   O  OG  . SER   A 1 89   ? -48.20200  63.13100  27.70900  1.000 59.57357  ?  89   SER   A OG  1 
ATOM   724   N  N   . VAL   A 1 90   ? -45.63700  64.83900  28.23400  1.000 56.02112  ?  90   VAL   A N   1 
ATOM   725   C  CA  . VAL   A 1 90   ? -44.39600  64.92900  27.47600  1.000 60.83498  ?  90   VAL   A CA  1 
ATOM   726   C  C   . VAL   A 1 90   ? -43.35800  65.76900  28.21400  1.000 51.75537  ?  90   VAL   A C   1 
ATOM   727   O  O   . VAL   A 1 90   ? -42.24200  65.31200  28.45900  1.000 52.09856  ?  90   VAL   A O   1 
ATOM   728   C  CB  . VAL   A 1 90   ? -44.67100  65.49700  26.06600  1.000 56.79286  ?  90   VAL   A CB  1 
ATOM   729   C  CG1 . VAL   A 1 90   ? -43.48500  65.24400  25.15500  1.000 55.95968  ?  90   VAL   A CG1 1 
ATOM   730   C  CG2 . VAL   A 1 90   ? -45.94400  64.89400  25.49500  1.000 30.84180  ?  90   VAL   A CG2 1 
ATOM   731   N  N   . TRP   A 1 91   ? -43.71500  67.00800  28.58100  1.000 55.47462  ?  91   TRP   A N   1 
ATOM   732   C  CA  . TRP   A 1 91   ? -42.74500  67.91700  29.18100  1.000 51.76677  ?  91   TRP   A CA  1 
ATOM   733   C  C   . TRP   A 1 91   ? -42.19400  67.36500  30.49000  1.000 45.38725  ?  91   TRP   A C   1 
ATOM   734   O  O   . TRP   A 1 91   ? -40.98400  67.41500  30.73200  1.000 63.16302  ?  91   TRP   A O   1 
ATOM   735   C  CB  . TRP   A 1 91   ? -43.38100  69.28600  29.39500  1.000 37.82137  ?  91   TRP   A CB  1 
ATOM   736   C  CG  . TRP   A 1 91   ? -42.41400  70.32300  29.84100  1.000 43.33906  ?  91   TRP   A CG  1 
ATOM   737   C  CD1 . TRP   A 1 91   ? -42.10200  70.65200  31.12600  1.000 57.50276  ?  91   TRP   A CD1 1 
ATOM   738   C  CD2 . TRP   A 1 91   ? -41.62000  71.17000  29.00500  1.000 56.03627  ?  91   TRP   A CD2 1 
ATOM   739   N  NE1 . TRP   A 1 91   ? -41.16200  71.65300  31.14300  1.000 82.72420  ?  91   TRP   A NE1 1 
ATOM   740   C  CE2 . TRP   A 1 91   ? -40.85000  71.98900  29.85200  1.000 57.30895  ?  91   TRP   A CE2 1 
ATOM   741   C  CE3 . TRP   A 1 91   ? -41.48600  71.31600  27.62100  1.000 58.67887  ?  91   TRP   A CE3 1 
ATOM   742   C  CZ2 . TRP   A 1 91   ? -39.95800  72.93900  29.36200  1.000 55.37086  ?  91   TRP   A CZ2 1 
ATOM   743   C  CZ3 . TRP   A 1 91   ? -40.60100  72.26000  27.13600  1.000 61.42890  ?  91   TRP   A CZ3 1 
ATOM   744   C  CH2 . TRP   A 1 91   ? -39.84900  73.06000  28.00500  1.000 60.32275  ?  91   TRP   A CH2 1 
ATOM   745   N  N   . ASP   A 1 92   ? -43.06300  66.83900  31.34900  1.000 48.91979  ?  92   ASP   A N   1 
ATOM   746   C  CA  . ASP   A 1 92   ? -42.60700  66.23700  32.59500  1.000 40.29229  ?  92   ASP   A CA  1 
ATOM   747   C  C   . ASP   A 1 92   ? -42.15800  64.79100  32.42400  1.000 33.45643  ?  92   ASP   A C   1 
ATOM   748   O  O   . ASP   A 1 92   ? -41.82300  64.14600  33.42200  1.000 49.17251  ?  92   ASP   A O   1 
ATOM   749   C  CB  . ASP   A 1 92   ? -43.70500  66.32100  33.65600  1.000 28.30171  ?  92   ASP   A CB  1 
ATOM   750   C  CG  . ASP   A 1 92   ? -43.92500  67.73700  34.15300  1.000 58.36077  ?  92   ASP   A CG  1 
ATOM   751   O  OD1 . ASP   A 1 92   ? -43.01000  68.57300  33.99000  1.000 47.70719  ?  92   ASP   A OD1 1 
ATOM   752   O  OD2 . ASP   A 1 92   ? -45.00800  68.00900  34.71300  1.000 62.03947  -1 92   ASP   A OD2 1 
ATOM   753   N  N   . GLU   A 1 93   ? -42.14300  64.27800  31.19200  1.000 37.56646  ?  93   GLU   A N   1 
ATOM   754   C  CA  . GLU   A 1 93   ? -41.64300  62.93600  30.88100  1.000 45.96528  ?  93   GLU   A CA  1 
ATOM   755   C  C   . GLU   A 1 93   ? -42.30300  61.87700  31.76400  1.000 51.36009  ?  93   GLU   A C   1 
ATOM   756   O  O   . GLU   A 1 93   ? -41.64000  61.06200  32.40900  1.000 64.47593  ?  93   GLU   A O   1 
ATOM   757   C  CB  . GLU   A 1 93   ? -40.11900  62.88400  30.99600  1.000 51.84723  ?  93   GLU   A CB  1 
ATOM   758   C  CG  . GLU   A 1 93   ? -39.40700  64.00900  30.25500  1.000 56.12455  ?  93   GLU   A CG  1 
ATOM   759   C  CD  . GLU   A 1 93   ? -38.04900  63.59500  29.72300  1.000 72.73236  ?  93   GLU   A CD  1 
ATOM   760   O  OE1 . GLU   A 1 93   ? -37.85600  62.38900  29.45900  1.000 67.27039  ?  93   GLU   A OE1 1 
ATOM   761   O  OE2 . GLU   A 1 93   ? -37.17600  64.47500  29.56700  1.000 87.79470  -1 93   GLU   A OE2 1 
ATOM   762   N  N   . THR   A 1 94   ? -43.62900  61.89700  31.78500  1.000 57.71724  ?  94   THR   A N   1 
ATOM   763   C  CA  . THR   A 1 94   ? -44.44000  60.98700  32.57600  1.000 50.82797  ?  94   THR   A CA  1 
ATOM   764   C  C   . THR   A 1 94   ? -44.91000  59.81600  31.72600  1.000 49.74667  ?  94   THR   A C   1 
ATOM   765   O  O   . THR   A 1 94   ? -44.84700  59.86500  30.49400  1.000 58.76083  ?  94   THR   A O   1 
ATOM   766   C  CB  . THR   A 1 94   ? -45.65700  61.72100  33.15100  1.000 52.44260  ?  94   THR   A CB  1 
ATOM   767   O  OG1 . THR   A 1 94   ? -46.73500  61.66900  32.20900  1.000 59.91387  ?  94   THR   A OG1 1 
ATOM   768   C  CG2 . THR   A 1 94   ? -45.31600  63.17100  33.43800  1.000 53.35116  ?  94   THR   A CG2 1 
ATOM   769   N  N   . PRO   A 1 95   ? -45.37400  58.73200  32.35200  1.000 50.30569  ?  95   PRO   A N   1 
ATOM   770   C  CA  . PRO   A 1 95   ? -45.97600  57.64200  31.57600  1.000 54.55511  ?  95   PRO   A CA  1 
ATOM   771   C  C   . PRO   A 1 95   ? -47.15300  58.13300  30.74600  1.000 60.23447  ?  95   PRO   A C   1 
ATOM   772   O  O   . PRO   A 1 95   ? -47.88700  59.04200  31.14100  1.000 60.33968  ?  95   PRO   A O   1 
ATOM   773   C  CB  . PRO   A 1 95   ? -46.42400  56.64800  32.65300  1.000 51.75491  ?  95   PRO   A CB  1 
ATOM   774   C  CG  . PRO   A 1 95   ? -45.49000  56.89000  33.78400  1.000 53.11069  ?  95   PRO   A CG  1 
ATOM   775   C  CD  . PRO   A 1 95   ? -45.20000  58.36600  33.77000  1.000 56.07711  ?  95   PRO   A CD  1 
ATOM   776   N  N   . LYS   A 1 96   ? -47.32200  57.51900  29.57900  1.000 59.92847  ?  96   LYS   A N   1 
ATOM   777   C  CA  . LYS   A 1 96   ? -48.33500  57.91500  28.61300  1.000 66.83017  ?  96   LYS   A CA  1 
ATOM   778   C  C   . LYS   A 1 96   ? -49.46700  56.89600  28.59900  1.000 59.08403  ?  96   LYS   A C   1 
ATOM   779   O  O   . LYS   A 1 96   ? -49.22600  55.68600  28.63900  1.000 65.26468  ?  96   LYS   A O   1 
ATOM   780   C  CB  . LYS   A 1 96   ? -47.73500  58.03500  27.20900  1.000 46.82705  ?  96   LYS   A CB  1 
ATOM   781   C  CG  . LYS   A 1 96   ? -46.36000  58.68500  27.15300  1.000 45.36526  ?  96   LYS   A CG  1 
ATOM   782   C  CD  . LYS   A 1 96   ? -46.45300  60.19900  27.10100  1.000 41.02031  ?  96   LYS   A CD  1 
ATOM   783   C  CE  . LYS   A 1 96   ? -45.09500  60.82000  26.81100  1.000 52.99820  ?  96   LYS   A CE  1 
ATOM   784   N  NZ  . LYS   A 1 96   ? -44.14700  60.65000  27.94600  1.000 51.53817  ?  96   LYS   A NZ  1 
ATOM   785   N  N   . GLY   A 1 97   ? -50.69900  57.38600  28.53100  1.000 56.37962  ?  97   GLY   A N   1 
ATOM   786   C  CA  . GLY   A 1 97   ? -51.84000  56.49800  28.47400  1.000 53.78331  ?  97   GLY   A CA  1 
ATOM   787   C  C   . GLY   A 1 97   ? -53.14100  57.27300  28.54600  1.000 53.48412  ?  97   GLY   A C   1 
ATOM   788   O  O   . GLY   A 1 97   ? -53.16700  58.49700  28.40300  1.000 57.11011  ?  97   GLY   A O   1 
ATOM   789   N  N   . VAL   A 1 98   ? -54.22300  56.52200  28.75900  1.000 61.42654  ?  98   VAL   A N   1 
ATOM   790   C  CA  . VAL   A 1 98   ? -55.56500  57.07300  28.90100  1.000 55.05245  ?  98   VAL   A CA  1 
ATOM   791   C  C   . VAL   A 1 98   ? -56.29500  56.28600  29.98200  1.000 51.12277  ?  98   VAL   A C   1 
ATOM   792   O  O   . VAL   A 1 98   ? -56.03400  55.09800  30.19600  1.000 43.23906  ?  98   VAL   A O   1 
ATOM   793   C  CB  . VAL   A 1 98   ? -56.35800  57.04000  27.57500  1.000 36.31350  ?  98   VAL   A CB  1 
ATOM   794   C  CG1 . VAL   A 1 98   ? -55.89800  58.15500  26.65000  1.000 36.03676  ?  98   VAL   A CG1 1 
ATOM   795   C  CG2 . VAL   A 1 98   ? -56.20900  55.68600  26.89800  1.000 36.21228  ?  98   VAL   A CG2 1 
ATOM   796   N  N   . THR   A 1 99   ? -57.22500  56.95400  30.66100  1.000 51.66512  ?  99   THR   A N   1 
ATOM   797   C  CA  . THR   A 1 99   ? -57.85500  56.37800  31.84100  1.000 61.83544  ?  99   THR   A CA  1 
ATOM   798   C  C   . THR   A 1 99   ? -59.34000  56.70400  31.88000  1.000 54.42981  ?  99   THR   A C   1 
ATOM   799   O  O   . THR   A 1 99   ? -59.72500  57.87300  31.79100  1.000 49.44916  ?  99   THR   A O   1 
ATOM   800   C  CB  . THR   A 1 99   ? -57.18800  56.89200  33.12000  1.000 55.66173  ?  99   THR   A CB  1 
ATOM   801   O  OG1 . THR   A 1 99   ? -55.77800  56.64900  33.05900  1.000 58.56538  ?  99   THR   A OG1 1 
ATOM   802   C  CG2 . THR   A 1 99   ? -57.76500  56.19100  34.32800  1.000 48.57076  ?  99   THR   A CG2 1 
ATOM   803   N  N   . ILE   A 1 100  ? -60.16200  55.67100  32.02600  1.000 45.41266  ?  100  ILE   A N   1 
ATOM   804   C  CA  . ILE   A 1 100  ? -61.57900  55.81900  32.33800  1.000 60.35229  ?  100  ILE   A CA  1 
ATOM   805   C  C   . ILE   A 1 100  ? -61.72900  55.56700  33.83200  1.000 62.40668  ?  100  ILE   A C   1 
ATOM   806   O  O   . ILE   A 1 100  ? -61.54700  54.43900  34.30100  1.000 61.05020  ?  100  ILE   A O   1 
ATOM   807   C  CB  . ILE   A 1 100  ? -62.44900  54.85800  31.51900  1.000 55.86376  ?  100  ILE   A CB  1 
ATOM   808   C  CG1 . ILE   A 1 100  ? -62.26700  55.10400  30.02300  1.000 54.33801  ?  100  ILE   A CG1 1 
ATOM   809   C  CG2 . ILE   A 1 100  ? -63.90600  55.00300  31.90600  1.000 33.65994  ?  100  ILE   A CG2 1 
ATOM   810   C  CD1 . ILE   A 1 100  ? -63.12400  54.21600  29.15400  1.000 47.53459  ?  100  ILE   A CD1 1 
ATOM   811   N  N   . HIS   A 1 101  ? -62.05800  56.61300  34.58600  1.000 59.72493  ?  101  HIS   A N   1 
ATOM   812   C  CA  . HIS   A 1 101  ? -62.04900  56.55700  36.04100  1.000 42.69527  ?  101  HIS   A CA  1 
ATOM   813   C  C   . HIS   A 1 101  ? -63.38100  57.05500  36.59000  1.000 58.47775  ?  101  HIS   A C   1 
ATOM   814   O  O   . HIS   A 1 101  ? -64.25800  57.51000  35.85000  1.000 60.41707  ?  101  HIS   A O   1 
ATOM   815   C  CB  . HIS   A 1 101  ? -60.89200  57.38500  36.61100  1.000 45.83132  ?  101  HIS   A CB  1 
ATOM   816   C  CG  . HIS   A 1 101  ? -61.02100  58.85400  36.35600  1.000 42.41485  ?  101  HIS   A CG  1 
ATOM   817   N  ND1 . HIS   A 1 101  ? -61.49500  59.73600  37.30300  1.000 42.95329  ?  101  HIS   A ND1 1 
ATOM   818   C  CD2 . HIS   A 1 101  ? -60.74700  59.59500  35.25600  1.000 56.64584  ?  101  HIS   A CD2 1 
ATOM   819   C  CE1 . HIS   A 1 101  ? -61.50100  60.95800  36.80000  1.000 49.35163  ?  101  HIS   A CE1 1 
ATOM   820   N  NE2 . HIS   A 1 101  ? -61.05200  60.90000  35.56000  1.000 54.25708  ?  101  HIS   A NE2 1 
ATOM   821   N  N   . LEU   A 1 102  ? -63.52100  56.96500  37.90900  1.000 59.59614  ?  102  LEU   A N   1 
ATOM   822   C  CA  . LEU   A 1 102  ? -64.68200  57.46500  38.62700  1.000 46.53274  ?  102  LEU   A CA  1 
ATOM   823   C  C   . LEU   A 1 102  ? -64.39400  58.85400  39.18500  1.000 44.51901  ?  102  LEU   A C   1 
ATOM   824   O  O   . LEU   A 1 102  ? -63.25000  59.19300  39.49900  1.000 54.70362  ?  102  LEU   A O   1 
ATOM   825   C  CB  . LEU   A 1 102  ? -65.07200  56.51500  39.76200  1.000 48.71785  ?  102  LEU   A CB  1 
ATOM   826   C  CG  . LEU   A 1 102  ? -65.78000  55.22300  39.35000  1.000 59.54474  ?  102  LEU   A CG  1 
ATOM   827   C  CD1 . LEU   A 1 102  ? -65.58100  54.14200  40.39700  1.000 54.06343  ?  102  LEU   A CD1 1 
ATOM   828   C  CD2 . LEU   A 1 102  ? -67.26200  55.48200  39.12800  1.000 48.76484  ?  102  LEU   A CD2 1 
ATOM   829   N  N   . ILE   A 1 103  ? -65.44600  59.65600  39.30200  1.000 40.39445  ?  103  ILE   A N   1 
ATOM   830   C  CA  . ILE   A 1 103  ? -65.32900  61.03400  39.76500  1.000 48.27532  ?  103  ILE   A CA  1 
ATOM   831   C  C   . ILE   A 1 103  ? -65.49900  61.07000  41.27700  1.000 55.96498  ?  103  ILE   A C   1 
ATOM   832   O  O   . ILE   A 1 103  ? -66.44400  60.48500  41.82200  1.000 69.28430  ?  103  ILE   A O   1 
ATOM   833   C  CB  . ILE   A 1 103  ? -66.36200  61.93600  39.06700  1.000 49.89789  ?  103  ILE   A CB  1 
ATOM   834   C  CG1 . ILE   A 1 103  ? -65.80200  62.47400  37.74800  1.000 50.41079  ?  103  ILE   A CG1 1 
ATOM   835   C  CG2 . ILE   A 1 103  ? -66.78800  63.08400  39.97300  1.000 48.71365  ?  103  ILE   A CG2 1 
ATOM   836   C  CD1 . ILE   A 1 103  ? -64.72100  63.52100  37.92700  1.000 64.09203  ?  103  ILE   A CD1 1 
ATOM   837   N  N   . ASP   A 1 104  ? -64.57600  61.74900  41.95900  1.000 65.93585  ?  104  ASP   A N   1 
ATOM   838   C  CA  . ASP   A 1 104  ? -64.68000  61.94700  43.39900  1.000 60.33891  ?  104  ASP   A CA  1 
ATOM   839   C  C   . ASP   A 1 104  ? -64.72200  63.43500  43.72500  1.000 68.72155  ?  104  ASP   A C   1 
ATOM   840   O  O   . ASP   A 1 104  ? -65.00900  64.26000  42.85100  1.000 57.21292  ?  104  ASP   A O   1 
ATOM   841   C  CB  . ASP   A 1 104  ? -63.51400  61.27500  44.13000  1.000 58.05246  ?  104  ASP   A CB  1 
ATOM   842   C  CG  . ASP   A 1 104  ? -62.17600  61.91600  43.81200  1.000 72.46106  ?  104  ASP   A CG  1 
ATOM   843   O  OD1 . ASP   A 1 104  ? -61.75300  61.86800  42.63900  1.000 83.95032  ?  104  ASP   A OD1 1 
ATOM   844   O  OD2 . ASP   A 1 104  ? -61.55200  62.47800  44.73600  1.000 81.37559  -1 104  ASP   A OD2 1 
ATOM   845   N  N   . GLU   A 1 105  ? -64.43600  63.78800  44.97700  1.000 75.40496  ?  105  GLU   A N   1 
ATOM   846   C  CA  . GLU   A 1 105  ? -64.44100  65.18100  45.40400  1.000 75.94384  ?  105  GLU   A CA  1 
ATOM   847   C  C   . GLU   A 1 105  ? -63.18100  65.93600  45.00600  1.000 78.11107  ?  105  GLU   A C   1 
ATOM   848   O  O   . GLU   A 1 105  ? -63.05900  67.11900  45.34100  1.000 71.19270  ?  105  GLU   A O   1 
ATOM   849   C  CB  . GLU   A 1 105  ? -64.62100  65.27000  46.92000  1.000 73.75001  ?  105  GLU   A CB  1 
ATOM   850   C  CG  . GLU   A 1 105  ? -66.05600  65.14000  47.38000  1.000 78.31108  ?  105  GLU   A CG  1 
ATOM   851   C  CD  . GLU   A 1 105  ? -66.40000  66.13500  48.46900  1.000 102.85750 ?  105  GLU   A CD  1 
ATOM   852   O  OE1 . GLU   A 1 105  ? -65.48100  66.56200  49.20100  1.000 103.49005 ?  105  GLU   A OE1 1 
ATOM   853   O  OE2 . GLU   A 1 105  ? -67.59000  66.49600  48.58400  1.000 105.99527 -1 105  GLU   A OE2 1 
ATOM   854   N  N   . HIS   A 1 106  ? -62.24700  65.29500  44.31100  1.000 75.17373  ?  106  HIS   A N   1 
ATOM   855   C  CA  . HIS   A 1 106  ? -60.98600  65.92100  43.94700  1.000 82.16424  ?  106  HIS   A CA  1 
ATOM   856   C  C   . HIS   A 1 106  ? -60.77600  65.78800  42.44300  1.000 83.65159  ?  106  HIS   A C   1 
ATOM   857   O  O   . HIS   A 1 106  ? -61.59400  65.20300  41.72600  1.000 81.84266  ?  106  HIS   A O   1 
ATOM   858   C  CB  . HIS   A 1 106  ? -59.82600  65.31300  44.74500  1.000 86.36614  ?  106  HIS   A CB  1 
ATOM   859   C  CG  . HIS   A 1 106  ? -60.01200  65.40000  46.22800  1.000 89.38993  ?  106  HIS   A CG  1 
ATOM   860   N  ND1 . HIS   A 1 106  ? -60.18100  66.60000  46.88600  1.000 75.91089  ?  106  HIS   A ND1 1 
ATOM   861   C  CD2 . HIS   A 1 106  ? -60.06300  64.43900  47.18000  1.000 81.63809  ?  106  HIS   A CD2 1 
ATOM   862   C  CE1 . HIS   A 1 106  ? -60.32700  66.37300  48.17900  1.000 76.40988  ?  106  HIS   A CE1 1 
ATOM   863   N  NE2 . HIS   A 1 106  ? -60.25800  65.07000  48.38500  1.000 78.26688  ?  106  HIS   A NE2 1 
ATOM   864   N  N   . VAL   A 1 107  ? -59.66300  66.34000  41.96600  1.000 75.43706  ?  107  VAL   A N   1 
ATOM   865   C  CA  . VAL   A 1 107  ? -59.42100  66.50400  40.53600  1.000 59.89008  ?  107  VAL   A CA  1 
ATOM   866   C  C   . VAL   A 1 107  ? -58.73000  65.24500  40.02200  1.000 61.11651  ?  107  VAL   A C   1 
ATOM   867   O  O   . VAL   A 1 107  ? -57.51400  65.09100  40.14900  1.000 73.29758  ?  107  VAL   A O   1 
ATOM   868   C  CB  . VAL   A 1 107  ? -58.59700  67.75800  40.24600  1.000 52.83567  ?  107  VAL   A CB  1 
ATOM   869   C  CG1 . VAL   A 1 107  ? -58.56600  68.03600  38.75100  1.000 58.73997  ?  107  VAL   A CG1 1 
ATOM   870   C  CG2 . VAL   A 1 107  ? -59.16100  68.94800  41.00800  1.000 67.16210  ?  107  VAL   A CG2 1 
ATOM   871   N  N   . ASP   A 1 108  ? -59.51900  64.34100  39.43500  1.000 69.42822  ?  108  ASP   A N   1 
ATOM   872   C  CA  . ASP   A 1 108  ? -59.00500  63.17100  38.72100  1.000 66.76483  ?  108  ASP   A CA  1 
ATOM   873   C  C   . ASP   A 1 108  ? -58.19400  62.25400  39.63700  1.000 64.42652  ?  108  ASP   A C   1 
ATOM   874   O  O   . ASP   A 1 108  ? -57.19200  61.66500  39.22600  1.000 58.83048  ?  108  ASP   A O   1 
ATOM   875   C  CB  . ASP   A 1 108  ? -58.17800  63.59200  37.50300  1.000 62.25481  ?  108  ASP   A CB  1 
ATOM   876   C  CG  . ASP   A 1 108  ? -58.92000  64.56400  36.60400  1.000 68.74233  ?  108  ASP   A CG  1 
ATOM   877   O  OD1 . ASP   A 1 108  ? -60.16500  64.48200  36.53900  1.000 76.45589  ?  108  ASP   A OD1 1 
ATOM   878   O  OD2 . ASP   A 1 108  ? -58.26000  65.41300  35.96600  1.000 64.57852  -1 108  ASP   A OD2 1 
ATOM   879   N  N   . THR   A 1 109  ? -58.63400  62.12500  40.88800  1.000 71.92310  ?  109  THR   A N   1 
ATOM   880   C  CA  . THR   A 1 109  ? -57.99700  61.23100  41.84500  1.000 73.18713  ?  109  THR   A CA  1 
ATOM   881   C  C   . THR   A 1 109  ? -58.84000  60.00200  42.15600  1.000 70.22593  ?  109  THR   A C   1 
ATOM   882   O  O   . THR   A 1 109  ? -58.42300  59.17400  42.97300  1.000 75.76006  ?  109  THR   A O   1 
ATOM   883   C  CB  . THR   A 1 109  ? -57.68700  61.97200  43.15100  1.000 69.48990  ?  109  THR   A CB  1 
ATOM   884   O  OG1 . THR   A 1 109  ? -58.83100  61.92100  44.01300  1.000 76.37966  ?  109  THR   A OG1 1 
ATOM   885   C  CG2 . THR   A 1 109  ? -57.34000  63.42400  42.87200  1.000 75.32742  ?  109  THR   A CG2 1 
ATOM   886   N  N   . GLY   A 1 110  ? -60.00600  59.86100  41.53300  1.000 72.17531  ?  110  GLY   A N   1 
ATOM   887   C  CA  . GLY   A 1 110  ? -60.88800  58.75200  41.83100  1.000 62.17365  ?  110  GLY   A CA  1 
ATOM   888   C  C   . GLY   A 1 110  ? -60.35300  57.42100  41.33500  1.000 59.71932  ?  110  GLY   A C   1 
ATOM   889   O  O   . GLY   A 1 110  ? -59.34100  57.32800  40.63900  1.000 73.30639  ?  110  GLY   A O   1 
ATOM   890   N  N   . ASP   A 1 111  ? -61.06600  56.36300  41.71300  1.000 64.77281  ?  111  ASP   A N   1 
ATOM   891   C  CA  . ASP   A 1 111  ? -60.67000  55.01300  41.34100  1.000 70.41755  ?  111  ASP   A CA  1 
ATOM   892   C  C   . ASP   A 1 111  ? -60.80200  54.80600  39.83600  1.000 57.68324  ?  111  ASP   A C   1 
ATOM   893   O  O   . ASP   A 1 111  ? -61.64300  55.41700  39.17100  1.000 75.53077  ?  111  ASP   A O   1 
ATOM   894   C  CB  . ASP   A 1 111  ? -61.51800  53.98400  42.08900  1.000 80.62959  ?  111  ASP   A CB  1 
ATOM   895   C  CG  . ASP   A 1 111  ? -61.42500  54.13800  43.59500  1.000 83.47486  ?  111  ASP   A CG  1 
ATOM   896   O  OD1 . ASP   A 1 111  ? -61.88500  55.17600  44.11700  1.000 85.77984  ?  111  ASP   A OD1 1 
ATOM   897   O  OD2 . ASP   A 1 111  ? -60.89400  53.22000  44.25600  1.000 64.15098  -1 111  ASP   A OD2 1 
ATOM   898   N  N   . ILE   A 1 112  ? -59.95600  53.92900  39.30100  1.000 51.28523  ?  112  ILE   A N   1 
ATOM   899   C  CA  . ILE   A 1 112  ? -59.88500  53.66300  37.86800  1.000 66.16762  ?  112  ILE   A CA  1 
ATOM   900   C  C   . ILE   A 1 112  ? -60.74500  52.45400  37.53600  1.000 70.64076  ?  112  ILE   A C   1 
ATOM   901   O  O   . ILE   A 1 112  ? -60.78700  51.47500  38.29200  1.000 71.74698  ?  112  ILE   A O   1 
ATOM   902   C  CB  . ILE   A 1 112  ? -58.42600  53.44300  37.41600  1.000 67.77375  ?  112  ILE   A CB  1 
ATOM   903   C  CG1 . ILE   A 1 112  ? -57.64200  54.75100  37.47800  1.000 71.47137  ?  112  ILE   A CG1 1 
ATOM   904   C  CG2 . ILE   A 1 112  ? -58.36100  52.86400  36.00900  1.000 60.08411  ?  112  ILE   A CG2 1 
ATOM   905   C  CD1 . ILE   A 1 112  ? -56.75200  54.86400  38.66900  1.000 57.44717  ?  112  ILE   A CD1 1 
ATOM   906   N  N   . LEU   A 1 113  ? -61.44300  52.52600  36.40200  1.000 67.42199  ?  113  LEU   A N   1 
ATOM   907   C  CA  . LEU   A 1 113  ? -62.17800  51.39200  35.85200  1.000 51.82964  ?  113  LEU   A CA  1 
ATOM   908   C  C   . LEU   A 1 113  ? -61.35300  50.64200  34.81200  1.000 54.93979  ?  113  LEU   A C   1 
ATOM   909   O  O   . LEU   A 1 113  ? -61.14100  49.43300  34.93600  1.000 66.82686  ?  113  LEU   A O   1 
ATOM   910   C  CB  . LEU   A 1 113  ? -63.50500  51.87300  35.25200  1.000 58.51824  ?  113  LEU   A CB  1 
ATOM   911   C  CG  . LEU   A 1 113  ? -64.43100  52.58100  36.24300  1.000 68.10265  ?  113  LEU   A CG  1 
ATOM   912   C  CD1 . LEU   A 1 113  ? -65.60300  53.23500  35.53000  1.000 56.08851  ?  113  LEU   A CD1 1 
ATOM   913   C  CD2 . LEU   A 1 113  ? -64.92100  51.60400  37.29800  1.000 69.39026  ?  113  LEU   A CD2 1 
ATOM   914   N  N   . VAL   A 1 114  ? -60.88000  51.34300  33.77900  1.000 50.95045  ?  114  VAL   A N   1 
ATOM   915   C  CA  . VAL   A 1 114  ? -59.99200  50.76400  32.78100  1.000 51.62704  ?  114  VAL   A CA  1 
ATOM   916   C  C   . VAL   A 1 114  ? -58.89100  51.76300  32.46200  1.000 60.48009  ?  114  VAL   A C   1 
ATOM   917   O  O   . VAL   A 1 114  ? -59.03500  52.97200  32.66000  1.000 55.76950  ?  114  VAL   A O   1 
ATOM   918   C  CB  . VAL   A 1 114  ? -60.72300  50.35400  31.48200  1.000 51.58029  ?  114  VAL   A CB  1 
ATOM   919   C  CG1 . VAL   A 1 114  ? -61.36000  48.98900  31.64100  1.000 65.40967  ?  114  VAL   A CG1 1 
ATOM   920   C  CG2 . VAL   A 1 114  ? -61.76700  51.38700  31.11000  1.000 64.81340  ?  114  VAL   A CG2 1 
ATOM   921   N  N   . GLN   A 1 115  ? -57.78100  51.23500  31.95400  1.000 57.57962  ?  115  GLN   A N   1 
ATOM   922   C  CA  . GLN   A 1 115  ? -56.61300  52.04000  31.63900  1.000 47.52236  ?  115  GLN   A CA  1 
ATOM   923   C  C   . GLN   A 1 115  ? -55.85700  51.37400  30.50000  1.000 58.13690  ?  115  GLN   A C   1 
ATOM   924   O  O   . GLN   A 1 115  ? -55.73200  50.14800  30.46400  1.000 61.36777  ?  115  GLN   A O   1 
ATOM   925   C  CB  . GLN   A 1 115  ? -55.70900  52.19700  32.86600  1.000 58.64491  ?  115  GLN   A CB  1 
ATOM   926   C  CG  . GLN   A 1 115  ? -55.10300  53.57400  33.02500  1.000 63.38970  ?  115  GLN   A CG  1 
ATOM   927   C  CD  . GLN   A 1 115  ? -54.52900  53.79800  34.41100  1.000 66.88786  ?  115  GLN   A CD  1 
ATOM   928   O  OE1 . GLN   A 1 115  ? -54.24900  52.84600  35.13900  1.000 58.47947  ?  115  GLN   A OE1 1 
ATOM   929   N  NE2 . GLN   A 1 115  ? -54.36100  55.06100  34.78600  1.000 65.89661  ?  115  GLN   A NE2 1 
ATOM   930   N  N   . GLU   A 1 116  ? -55.36400  52.18800  29.57000  1.000 56.36896  ?  116  GLU   A N   1 
ATOM   931   C  CA  . GLU   A 1 116  ? -54.59000  51.70800  28.43500  1.000 53.59633  ?  116  GLU   A CA  1 
ATOM   932   C  C   . GLU   A 1 116  ? -53.34800  52.57300  28.28100  1.000 60.28955  ?  116  GLU   A C   1 
ATOM   933   O  O   . GLU   A 1 116  ? -53.39500  53.78400  28.51100  1.000 50.63395  ?  116  GLU   A O   1 
ATOM   934   C  CB  . GLU   A 1 116  ? -55.41900  51.73300  27.14400  1.000 52.18525  ?  116  GLU   A CB  1 
ATOM   935   C  CG  . GLU   A 1 116  ? -54.69400  51.19000  25.92400  1.000 76.09067  ?  116  GLU   A CG  1 
ATOM   936   C  CD  . GLU   A 1 116  ? -55.50600  51.33400  24.65300  1.000 89.19801  ?  116  GLU   A CD  1 
ATOM   937   O  OE1 . GLU   A 1 116  ? -56.75000  51.25200  24.72700  1.000 83.69277  ?  116  GLU   A OE1 1 
ATOM   938   O  OE2 . GLU   A 1 116  ? -54.89800  51.53700  23.58100  1.000 89.76808  -1 116  GLU   A OE2 1 
ATOM   939   N  N   . GLU   A 1 117  ? -52.23900  51.94800  27.89700  1.000 66.18345  ?  117  GLU   A N   1 
ATOM   940   C  CA  . GLU   A 1 117  ? -50.96100  52.63700  27.75800  1.000 63.92991  ?  117  GLU   A CA  1 
ATOM   941   C  C   . GLU   A 1 117  ? -50.74000  52.97400  26.28700  1.000 68.63763  ?  117  GLU   A C   1 
ATOM   942   O  O   . GLU   A 1 117  ? -50.45300  52.08600  25.47700  1.000 85.39021  ?  117  GLU   A O   1 
ATOM   943   C  CB  . GLU   A 1 117  ? -49.82200  51.77900  28.30400  1.000 69.42291  ?  117  GLU   A CB  1 
ATOM   944   C  CG  . GLU   A 1 117  ? -48.81300  52.56000  29.12400  1.000 87.91624  ?  117  GLU   A CG  1 
ATOM   945   C  CD  . GLU   A 1 117  ? -47.51000  51.81500  29.32200  1.000 96.19361  ?  117  GLU   A CD  1 
ATOM   946   O  OE1 . GLU   A 1 117  ? -47.52500  50.56600  29.31100  1.000 100.91814 ?  117  GLU   A OE1 1 
ATOM   947   O  OE2 . GLU   A 1 117  ? -46.46700  52.48400  29.48100  1.000 91.48028  -1 117  GLU   A OE2 1 
ATOM   948   N  N   . ILE   A 1 118  ? -50.87800  54.25100  25.94300  1.000 65.86946  ?  118  ILE   A N   1 
ATOM   949   C  CA  . ILE   A 1 118  ? -50.59100  54.70800  24.59200  1.000 68.90758  ?  118  ILE   A CA  1 
ATOM   950   C  C   . ILE   A 1 118  ? -49.14800  55.19300  24.53600  1.000 64.64781  ?  118  ILE   A C   1 
ATOM   951   O  O   . ILE   A 1 118  ? -48.52400  55.48600  25.55800  1.000 63.10761  ?  118  ILE   A O   1 
ATOM   952   C  CB  . ILE   A 1 118  ? -51.56800  55.80900  24.13800  1.000 40.59842  ?  118  ILE   A CB  1 
ATOM   953   C  CG1 . ILE   A 1 118  ? -51.12600  57.16900  24.67500  1.000 46.60608  ?  118  ILE   A CG1 1 
ATOM   954   C  CG2 . ILE   A 1 118  ? -52.97800  55.48400  24.60200  1.000 59.33722  ?  118  ILE   A CG2 1 
ATOM   955   C  CD1 . ILE   A 1 118  ? -51.76500  58.32900  23.95000  1.000 44.74063  ?  118  ILE   A CD1 1 
ATOM   956   N  N   . ALA   A 1 119  ? -48.60600  55.27500  23.32300  1.000 55.50301  ?  119  ALA   A N   1 
ATOM   957   C  CA  . ALA   A 1 119  ? -47.20500  55.61700  23.12000  1.000 48.56536  ?  119  ALA   A CA  1 
ATOM   958   C  C   . ALA   A 1 119  ? -47.08800  56.72000  22.08100  1.000 57.61415  ?  119  ALA   A C   1 
ATOM   959   O  O   . ALA   A 1 119  ? -47.62600  56.59700  20.97500  1.000 59.38355  ?  119  ALA   A O   1 
ATOM   960   C  CB  . ALA   A 1 119  ? -46.39400  54.39300  22.68400  1.000 53.40126  ?  119  ALA   A CB  1 
ATOM   961   N  N   . PHE   A 1 120  ? -46.38400  57.78900  22.43800  1.000 50.64000  ?  120  PHE   A N   1 
ATOM   962   C  CA  . PHE   A 1 120  ? -46.11200  58.88600  21.52300  1.000 48.79760  ?  120  PHE   A CA  1 
ATOM   963   C  C   . PHE   A 1 120  ? -44.77200  58.67500  20.83200  1.000 60.94451  ?  120  PHE   A C   1 
ATOM   964   O  O   . PHE   A 1 120  ? -43.83800  58.10500  21.40400  1.000 68.31033  ?  120  PHE   A O   1 
ATOM   965   C  CB  . PHE   A 1 120  ? -46.10600  60.22400  22.26300  1.000 41.12117  ?  120  PHE   A CB  1 
ATOM   966   C  CG  . PHE   A 1 120  ? -47.45200  60.63800  22.77900  1.000 44.48057  ?  120  PHE   A CG  1 
ATOM   967   C  CD1 . PHE   A 1 120  ? -48.60100  60.33500  22.07200  1.000 51.86408  ?  120  PHE   A CD1 1 
ATOM   968   C  CD2 . PHE   A 1 120  ? -47.56700  61.32900  23.97300  1.000 52.76486  ?  120  PHE   A CD2 1 
ATOM   969   C  CE1 . PHE   A 1 120  ? -49.84100  60.70900  22.54500  1.000 51.64939  ?  120  PHE   A CE1 1 
ATOM   970   C  CE2 . PHE   A 1 120  ? -48.80500  61.71000  24.45200  1.000 50.74950  ?  120  PHE   A CE2 1 
ATOM   971   C  CZ  . PHE   A 1 120  ? -49.94400  61.40000  23.73500  1.000 44.34055  ?  120  PHE   A CZ  1 
ATOM   972   N  N   . ALA   A 1 121  ? -44.68500  59.14300  19.59100  1.000 51.58474  ?  121  ALA   A N   1 
ATOM   973   C  CA  . ALA   A 1 121  ? -43.45600  59.05200  18.81700  1.000 43.96344  ?  121  ALA   A CA  1 
ATOM   974   C  C   . ALA   A 1 121  ? -42.63300  60.32100  18.99500  1.000 61.38871  ?  121  ALA   A C   1 
ATOM   975   O  O   . ALA   A 1 121  ? -43.18400  61.41900  19.11200  1.000 74.82058  ?  121  ALA   A O   1 
ATOM   976   C  CB  . ALA   A 1 121  ? -43.76400  58.83000  17.33600  1.000 68.20611  ?  121  ALA   A CB  1 
ATOM   977   N  N   . ASP   A 1 122  ? -41.30600  60.16000  19.02000  1.000 72.23503  ?  122  ASP   A N   1 
ATOM   978   C  CA  . ASP   A 1 122  ? -40.42100  61.31200  19.17100  1.000 70.56445  ?  122  ASP   A CA  1 
ATOM   979   C  C   . ASP   A 1 122  ? -40.60400  62.31200  18.03800  1.000 61.00964  ?  122  ASP   A C   1 
ATOM   980   O  O   . ASP   A 1 122  ? -40.41900  63.51900  18.23500  1.000 59.82600  ?  122  ASP   A O   1 
ATOM   981   C  CB  . ASP   A 1 122  ? -38.96200  60.85400  19.23100  1.000 58.46307  ?  122  ASP   A CB  1 
ATOM   982   C  CG  . ASP   A 1 122  ? -38.66800  59.98900  20.44200  1.000 79.92705  ?  122  ASP   A CG  1 
ATOM   983   O  OD1 . ASP   A 1 122  ? -39.62200  59.60000  21.14800  1.000 95.53885  ?  122  ASP   A OD1 1 
ATOM   984   O  OD2 . ASP   A 1 122  ? -37.47700  59.70300  20.68900  1.000 74.65975  -1 122  ASP   A OD2 1 
ATOM   985   N  N   . GLU   A 1 123  ? -40.97000  61.83300  16.85500  1.000 59.34230  ?  123  GLU   A N   1 
ATOM   986   C  CA  . GLU   A 1 123  ? -41.11800  62.65800  15.66700  1.000 62.23397  ?  123  GLU   A CA  1 
ATOM   987   C  C   . GLU   A 1 123  ? -42.53800  63.17900  15.49200  1.000 66.56515  ?  123  GLU   A C   1 
ATOM   988   O  O   . GLU   A 1 123  ? -42.82300  63.84100  14.48900  1.000 66.35745  ?  123  GLU   A O   1 
ATOM   989   C  CB  . GLU   A 1 123  ? -40.69900  61.86100  14.42300  1.000 77.04487  ?  123  GLU   A CB  1 
ATOM   990   C  CG  . GLU   A 1 123  ? -39.49400  60.93200  14.63000  1.000 85.99993  ?  123  GLU   A CG  1 
ATOM   991   C  CD  . GLU   A 1 123  ? -39.84100  59.65100  15.38600  1.000 96.55180  ?  123  GLU   A CD  1 
ATOM   992   O  OE1 . GLU   A 1 123  ? -40.54500  59.74200  16.41500  1.000 98.89141  ?  123  GLU   A OE1 1 
ATOM   993   O  OE2 . GLU   A 1 123  ? -39.41400  58.55900  14.95400  1.000 116.02822 -1 123  GLU   A OE2 1 
ATOM   994   N  N   . ASP   A 1 124  ? -43.42900  62.88400  16.43400  1.000 63.90532  ?  124  ASP   A N   1 
ATOM   995   C  CA  . ASP   A 1 124  ? -44.79000  63.39500  16.41100  1.000 53.60126  ?  124  ASP   A CA  1 
ATOM   996   C  C   . ASP   A 1 124  ? -44.83800  64.77600  17.04700  1.000 49.71713  ?  124  ASP   A C   1 
ATOM   997   O  O   . ASP   A 1 124  ? -44.15900  65.03700  18.04400  1.000 51.18468  ?  124  ASP   A O   1 
ATOM   998   C  CB  . ASP   A 1 124  ? -45.73700  62.45300  17.15900  1.000 50.98875  ?  124  ASP   A CB  1 
ATOM   999   C  CG  . ASP   A 1 124  ? -46.19600  61.28500  16.31000  1.000 72.13587  ?  124  ASP   A CG  1 
ATOM   1000  O  OD1 . ASP   A 1 124  ? -45.92600  61.28600  15.09100  1.000 86.35428  ?  124  ASP   A OD1 1 
ATOM   1001  O  OD2 . ASP   A 1 124  ? -46.83200  60.36600  16.86700  1.000 72.41051  -1 124  ASP   A OD2 1 
ATOM   1002  N  N   . THR   A 1 125  ? -45.64000  65.65900  16.46300  1.000 47.94359  ?  125  THR   A N   1 
ATOM   1003  C  CA  . THR   A 1 125  ? -45.87800  66.94900  17.08700  1.000 50.32165  ?  125  THR   A CA  1 
ATOM   1004  C  C   . THR   A 1 125  ? -46.82300  66.78300  18.27400  1.000 53.37209  ?  125  THR   A C   1 
ATOM   1005  O  O   . THR   A 1 125  ? -47.49300  65.75800  18.43000  1.000 50.22392  ?  125  THR   A O   1 
ATOM   1006  C  CB  . THR   A 1 125  ? -46.46300  67.94600  16.08500  1.000 52.39842  ?  125  THR   A CB  1 
ATOM   1007  O  OG1 . THR   A 1 125  ? -47.82300  67.60100  15.79700  1.000 50.90207  ?  125  THR   A OG1 1 
ATOM   1008  C  CG2 . THR   A 1 125  ? -45.66400  67.93100  14.79200  1.000 61.02833  ?  125  THR   A CG2 1 
ATOM   1009  N  N   . LEU   A 1 126  ? -46.86100  67.81000  19.12500  1.000 44.63703  ?  126  LEU   A N   1 
ATOM   1010  C  CA  . LEU   A 1 126  ? -47.77000  67.78100  20.26600  1.000 45.98573  ?  126  LEU   A CA  1 
ATOM   1011  C  C   . LEU   A 1 126  ? -49.21800  67.65900  19.81200  1.000 49.11171  ?  126  LEU   A C   1 
ATOM   1012  O  O   . LEU   A 1 126  ? -50.00600  66.92100  20.41600  1.000 51.61712  ?  126  LEU   A O   1 
ATOM   1013  C  CB  . LEU   A 1 126  ? -47.57700  69.03000  21.12500  1.000 49.46086  ?  126  LEU   A CB  1 
ATOM   1014  C  CG  . LEU   A 1 126  ? -46.62900  68.88500  22.31600  1.000 58.29557  ?  126  LEU   A CG  1 
ATOM   1015  C  CD1 . LEU   A 1 126  ? -46.18300  70.25000  22.80300  1.000 62.21162  ?  126  LEU   A CD1 1 
ATOM   1016  C  CD2 . LEU   A 1 126  ? -47.30300  68.11000  23.44100  1.000 58.46030  ?  126  LEU   A CD2 1 
ATOM   1017  N  N   . LEU   A 1 127  ? -49.58400  68.36800  18.74200  1.000 45.37646  ?  127  LEU   A N   1 
ATOM   1018  C  CA  . LEU   A 1 127  ? -50.93800  68.25500  18.21000  1.000 41.64068  ?  127  LEU   A CA  1 
ATOM   1019  C  C   . LEU   A 1 127  ? -51.22700  66.83500  17.73800  1.000 42.15338  ?  127  LEU   A C   1 
ATOM   1020  O  O   . LEU   A 1 127  ? -52.34600  66.33500  17.90100  1.000 49.06932  ?  127  LEU   A O   1 
ATOM   1021  C  CB  . LEU   A 1 127  ? -51.14100  69.25600  17.07300  1.000 36.01692  ?  127  LEU   A CB  1 
ATOM   1022  C  CG  . LEU   A 1 127  ? -51.10100  70.73600  17.45800  1.000 36.01289  ?  127  LEU   A CG  1 
ATOM   1023  C  CD1 . LEU   A 1 127  ? -51.39500  71.61400  16.25100  1.000 39.30981  ?  127  LEU   A CD1 1 
ATOM   1024  C  CD2 . LEU   A 1 127  ? -52.08100  71.02900  18.58400  1.000 48.95751  ?  127  LEU   A CD2 1 
ATOM   1025  N  N   . ASP   A 1 128  ? -50.22900  66.16800  17.15000  1.000 46.82775  ?  128  ASP   A N   1 
ATOM   1026  C  CA  . ASP   A 1 128  ? -50.39300  64.76200  16.79700  1.000 49.49359  ?  128  ASP   A CA  1 
ATOM   1027  C  C   . ASP   A 1 128  ? -50.64900  63.91800  18.03800  1.000 51.16400  ?  128  ASP   A C   1 
ATOM   1028  O  O   . ASP   A 1 128  ? -51.46000  62.98400  18.01000  1.000 53.60625  ?  128  ASP   A O   1 
ATOM   1029  C  CB  . ASP   A 1 128  ? -49.15700  64.25100  16.05400  1.000 48.05714  ?  128  ASP   A CB  1 
ATOM   1030  C  CG  . ASP   A 1 128  ? -48.88800  65.01100  14.77200  1.000 65.46963  ?  128  ASP   A CG  1 
ATOM   1031  O  OD1 . ASP   A 1 128  ? -49.54200  66.05100  14.54500  1.000 86.11425  ?  128  ASP   A OD1 1 
ATOM   1032  O  OD2 . ASP   A 1 128  ? -48.01900  64.56900  13.99000  1.000 64.38657  -1 128  ASP   A OD2 1 
ATOM   1033  N  N   . CYS   A 1 129  ? -49.96700  64.23800  19.14000  1.000 50.62356  ?  129  CYS   A N   1 
ATOM   1034  C  CA  . CYS   A 1 129  ? -50.18100  63.51500  20.38700  1.000 41.84685  ?  129  CYS   A CA  1 
ATOM   1035  C  C   . CYS   A 1 129  ? -51.58100  63.74800  20.94000  1.000 49.32023  ?  129  CYS   A C   1 
ATOM   1036  O  O   . CYS   A 1 129  ? -52.17300  62.83400  21.52700  1.000 47.92524  ?  129  CYS   A O   1 
ATOM   1037  C  CB  . CYS   A 1 129  ? -49.12900  63.92900  21.41400  1.000 46.28589  ?  129  CYS   A CB  1 
ATOM   1038  S  SG  . CYS   A 1 129  ? -47.42700  63.65200  20.88600  1.000 49.88430  ?  129  CYS   A SG  1 
ATOM   1039  N  N   . TYR   A 1 130  ? -52.12500  64.95500  20.76300  1.000 50.91601  ?  130  TYR   A N   1 
ATOM   1040  C  CA  . TYR   A 1 130  ? -53.47800  65.23400  21.23300  1.000 45.06209  ?  130  TYR   A CA  1 
ATOM   1041  C  C   . TYR   A 1 130  ? -54.49200  64.35200  20.51800  1.000 43.66887  ?  130  TYR   A C   1 
ATOM   1042  O  O   . TYR   A 1 130  ? -55.33500  63.71100  21.15500  1.000 55.62565  ?  130  TYR   A O   1 
ATOM   1043  C  CB  . TYR   A 1 130  ? -53.82400  66.71200  21.02500  1.000 38.30642  ?  130  TYR   A CB  1 
ATOM   1044  C  CG  . TYR   A 1 130  ? -52.92100  67.70000  21.73300  1.000 46.78438  ?  130  TYR   A CG  1 
ATOM   1045  C  CD1 . TYR   A 1 130  ? -52.05500  67.29300  22.74000  1.000 49.79211  ?  130  TYR   A CD1 1 
ATOM   1046  C  CD2 . TYR   A 1 130  ? -52.94300  69.04700  21.39400  1.000 33.72811  ?  130  TYR   A CD2 1 
ATOM   1047  C  CE1 . TYR   A 1 130  ? -51.22900  68.19800  23.38200  1.000 64.88662  ?  130  TYR   A CE1 1 
ATOM   1048  C  CE2 . TYR   A 1 130  ? -52.12300  69.95900  22.03100  1.000 42.06245  ?  130  TYR   A CE2 1 
ATOM   1049  C  CZ  . TYR   A 1 130  ? -51.26800  69.53000  23.02400  1.000 63.69016  ?  130  TYR   A CZ  1 
ATOM   1050  O  OH  . TYR   A 1 130  ? -50.45100  70.43700  23.65900  1.000 65.17417  ?  130  TYR   A OH  1 
ATOM   1051  N  N   . ASN   A 1 131  ? -54.42700  64.31400  19.18400  1.000 44.65119  ?  131  ASN   A N   1 
ATOM   1052  C  CA  . ASN   A 1 131  ? -55.36900  63.50500  18.41700  1.000 50.30189  ?  131  ASN   A CA  1 
ATOM   1053  C  C   . ASN   A 1 131  ? -55.24200  62.02900  18.76900  1.000 54.50164  ?  131  ASN   A C   1 
ATOM   1054  O  O   . ASN   A 1 131  ? -56.25100  61.33300  18.92500  1.000 61.02864  ?  131  ASN   A O   1 
ATOM   1055  C  CB  . ASN   A 1 131  ? -55.14900  63.72000  16.92000  1.000 43.81829  ?  131  ASN   A CB  1 
ATOM   1056  C  CG  . ASN   A 1 131  ? -55.47500  65.13200  16.48000  1.000 51.55089  ?  131  ASN   A CG  1 
ATOM   1057  O  OD1 . ASN   A 1 131  ? -54.60600  65.86100  16.00300  1.000 54.47432  ?  131  ASN   A OD1 1 
ATOM   1058  N  ND2 . ASN   A 1 131  ? -56.73400  65.52500  16.63500  1.000 54.90085  ?  131  ASN   A ND2 1 
ATOM   1059  N  N   . LYS   A 1 132  ? -54.00900  61.53800  18.90600  1.000 42.88758  ?  132  LYS   A N   1 
ATOM   1060  C  CA  . LYS   A 1 132  ? -53.80600  60.13500  19.25000  1.000 50.40410  ?  132  LYS   A CA  1 
ATOM   1061  C  C   . LYS   A 1 132  ? -54.37700  59.81300  20.62500  1.000 54.09591  ?  132  LYS   A C   1 
ATOM   1062  O  O   . LYS   A 1 132  ? -54.97900  58.75100  20.82300  1.000 51.84423  ?  132  LYS   A O   1 
ATOM   1063  C  CB  . LYS   A 1 132  ? -52.31800  59.79700  19.19900  1.000 43.08551  ?  132  LYS   A CB  1 
ATOM   1064  C  CG  . LYS   A 1 132  ? -52.01300  58.31900  19.35800  1.000 60.21650  ?  132  LYS   A CG  1 
ATOM   1065  C  CD  . LYS   A 1 132  ? -50.53600  58.04000  19.14000  1.000 65.75754  ?  132  LYS   A CD  1 
ATOM   1066  C  CE  . LYS   A 1 132  ? -50.02600  58.71900  17.87600  1.000 61.94124  ?  132  LYS   A CE  1 
ATOM   1067  N  NZ  . LYS   A 1 132  ? -50.83000  58.35900  16.67400  1.000 70.92362  ?  132  LYS   A NZ  1 
ATOM   1068  N  N   . ALA   A 1 133  ? -54.20200  60.72100  21.58600  1.000 49.49659  ?  133  ALA   A N   1 
ATOM   1069  C  CA  . ALA   A 1 133  ? -54.67600  60.46600  22.94200  1.000 57.49644  ?  133  ALA   A CA  1 
ATOM   1070  C  C   . ALA   A 1 133  ? -56.19800  60.52100  23.01600  1.000 57.67095  ?  133  ALA   A C   1 
ATOM   1071  O  O   . ALA   A 1 133  ? -56.83100  59.65000  23.62400  1.000 52.89924  ?  133  ALA   A O   1 
ATOM   1072  C  CB  . ALA   A 1 133  ? -54.05100  61.46900  23.91100  1.000 46.77201  ?  133  ALA   A CB  1 
ATOM   1073  N  N   . ASN   A 1 134  ? -56.80300  61.54100  22.40200  1.000 58.24810  ?  134  ASN   A N   1 
ATOM   1074  C  CA  . ASN   A 1 134  ? -58.25500  61.67800  22.46100  1.000 40.65431  ?  134  ASN   A CA  1 
ATOM   1075  C  C   . ASN   A 1 134  ? -58.96200  60.54200  21.73200  1.000 58.03791  ?  134  ASN   A C   1 
ATOM   1076  O  O   . ASN   A 1 134  ? -60.05900  60.14100  22.13400  1.000 64.00539  ?  134  ASN   A O   1 
ATOM   1077  C  CB  . ASN   A 1 134  ? -58.68100  63.03000  21.88900  1.000 34.52068  ?  134  ASN   A CB  1 
ATOM   1078  C  CG  . ASN   A 1 134  ? -58.43700  64.17500  22.85600  1.000 62.85323  ?  134  ASN   A CG  1 
ATOM   1079  O  OD1 . ASN   A 1 134  ? -59.28000  64.48200  23.70000  1.000 52.03571  ?  134  ASN   A OD1 1 
ATOM   1080  N  ND2 . ASN   A 1 134  ? -57.28000  64.81600  22.73500  1.000 64.46066  ?  134  ASN   A ND2 1 
ATOM   1081  N  N   . GLN   A 1 135  ? -58.35700  60.01100  20.66700  1.000 51.13899  ?  135  GLN   A N   1 
ATOM   1082  C  CA  . GLN   A 1 135  ? -58.94900  58.86400  19.98600  1.000 48.55615  ?  135  GLN   A CA  1 
ATOM   1083  C  C   . GLN   A 1 135  ? -58.86300  57.60900  20.84500  1.000 59.80213  ?  135  GLN   A C   1 
ATOM   1084  O  O   . GLN   A 1 135  ? -59.77400  56.77300  20.82800  1.000 74.23382  ?  135  GLN   A O   1 
ATOM   1085  C  CB  . GLN   A 1 135  ? -58.26200  58.63300  18.64200  1.000 55.37443  ?  135  GLN   A CB  1 
ATOM   1086  C  CG  . GLN   A 1 135  ? -58.52600  59.70800  17.60500  1.000 71.57849  ?  135  GLN   A CG  1 
ATOM   1087  C  CD  . GLN   A 1 135  ? -57.50500  59.68800  16.48500  1.000 74.88487  ?  135  GLN   A CD  1 
ATOM   1088  O  OE1 . GLN   A 1 135  ? -56.96100  58.63700  16.14400  1.000 63.75183  ?  135  GLN   A OE1 1 
ATOM   1089  N  NE2 . GLN   A 1 135  ? -57.22900  60.85500  15.91500  1.000 67.71524  ?  135  GLN   A NE2 1 
ATOM   1090  N  N   . ALA   A 1 136  ? -57.77300  57.46200  21.60300  1.000 57.74811  ?  136  ALA   A N   1 
ATOM   1091  C  CA  . ALA   A 1 136  ? -57.59500  56.26600  22.42000  1.000 48.19999  ?  136  ALA   A CA  1 
ATOM   1092  C  C   . ALA   A 1 136  ? -58.62900  56.19400  23.53600  1.000 45.80435  ?  136  ALA   A C   1 
ATOM   1093  O  O   . ALA   A 1 136  ? -59.16200  55.11600  23.82500  1.000 47.11258  ?  136  ALA   A O   1 
ATOM   1094  C  CB  . ALA   A 1 136  ? -56.18100  56.23000  22.99700  1.000 45.17674  ?  136  ALA   A CB  1 
ATOM   1095  N  N   . ILE   A 1 137  ? -58.92800  57.32800  24.17300  1.000 45.30665  ?  137  ILE   A N   1 
ATOM   1096  C  CA  . ILE   A 1 137  ? -59.90000  57.31100  25.25900  1.000 52.87830  ?  137  ILE   A CA  1 
ATOM   1097  C  C   . ILE   A 1 137  ? -61.31000  57.11200  24.71500  1.000 50.37417  ?  137  ILE   A C   1 
ATOM   1098  O  O   . ILE   A 1 137  ? -62.17700  56.56100  25.40500  1.000 50.99686  ?  137  ILE   A O   1 
ATOM   1099  C  CB  . ILE   A 1 137  ? -59.78500  58.59300  26.10700  1.000 36.54637  ?  137  ILE   A CB  1 
ATOM   1100  C  CG1 . ILE   A 1 137  ? -60.49200  58.40400  27.44800  1.000 35.81530  ?  137  ILE   A CG1 1 
ATOM   1101  C  CG2 . ILE   A 1 137  ? -60.35600  59.79400  25.36600  1.000 46.25264  ?  137  ILE   A CG2 1 
ATOM   1102  C  CD1 . ILE   A 1 137  ? -60.06400  57.15300  28.17900  1.000 52.52443  ?  137  ILE   A CD1 1 
ATOM   1103  N  N   . GLU   A 1 138  ? -61.56300  57.53600  23.47400  1.000 40.79569  ?  138  GLU   A N   1 
ATOM   1104  C  CA  . GLU   A 1 138  ? -62.87000  57.30700  22.87000  1.000 40.62530  ?  138  GLU   A CA  1 
ATOM   1105  C  C   . GLU   A 1 138  ? -63.04300  55.84300  22.48800  1.000 44.61319  ?  138  GLU   A C   1 
ATOM   1106  O  O   . GLU   A 1 138  ? -64.08400  55.23700  22.76400  1.000 52.65669  ?  138  GLU   A O   1 
ATOM   1107  C  CB  . GLU   A 1 138  ? -63.05300  58.21100  21.65000  1.000 42.81766  ?  138  GLU   A CB  1 
ATOM   1108  C  CG  . GLU   A 1 138  ? -63.21400  59.68600  21.98400  1.000 46.23551  ?  138  GLU   A CG  1 
ATOM   1109  C  CD  . GLU   A 1 138  ? -63.26400  60.56100  20.74500  1.000 68.02224  ?  138  GLU   A CD  1 
ATOM   1110  O  OE1 . GLU   A 1 138  ? -63.02900  60.03700  19.63500  1.000 65.57698  ?  138  GLU   A OE1 1 
ATOM   1111  O  OE2 . GLU   A 1 138  ? -63.53800  61.77300  20.88100  1.000 65.23930  -1 138  GLU   A OE2 1 
ATOM   1112  N  N   . GLU   A 1 139  ? -62.02500  55.25500  21.85700  1.000 48.25649  ?  139  GLU   A N   1 
ATOM   1113  C  CA  . GLU   A 1 139  ? -62.11600  53.85300  21.46600  1.000 53.27187  ?  139  GLU   A CA  1 
ATOM   1114  C  C   . GLU   A 1 139  ? -62.12800  52.93500  22.68100  1.000 56.14896  ?  139  GLU   A C   1 
ATOM   1115  O  O   . GLU   A 1 139  ? -62.76500  51.87600  22.64900  1.000 53.48023  ?  139  GLU   A O   1 
ATOM   1116  C  CB  . GLU   A 1 139  ? -60.96000  53.49100  20.53400  1.000 44.07801  ?  139  GLU   A CB  1 
ATOM   1117  C  CG  . GLU   A 1 139  ? -61.34700  52.54000  19.41200  1.000 69.03308  ?  139  GLU   A CG  1 
ATOM   1118  C  CD  . GLU   A 1 139  ? -62.20900  53.20700  18.35500  1.000 84.33933  ?  139  GLU   A CD  1 
ATOM   1119  O  OE1 . GLU   A 1 139  ? -62.07100  54.43400  18.16000  1.000 78.02964  ?  139  GLU   A OE1 1 
ATOM   1120  O  OE2 . GLU   A 1 139  ? -63.02500  52.50600  17.72000  1.000 72.22656  -1 139  GLU   A OE2 1 
ATOM   1121  N  N   . LEU   A 1 140  ? -61.43500  53.32100  23.75600  1.000 52.61864  ?  140  LEU   A N   1 
ATOM   1122  C  CA  . LEU   A 1 140  ? -61.47500  52.53400  24.98500  1.000 52.70781  ?  140  LEU   A CA  1 
ATOM   1123  C  C   . LEU   A 1 140  ? -62.86900  52.54200  25.59600  1.000 49.02134  ?  140  LEU   A C   1 
ATOM   1124  O  O   . LEU   A 1 140  ? -63.32800  51.52200  26.12600  1.000 49.48926  ?  140  LEU   A O   1 
ATOM   1125  C  CB  . LEU   A 1 140  ? -60.44600  53.06600  25.98300  1.000 57.76741  ?  140  LEU   A CB  1 
ATOM   1126  C  CG  . LEU   A 1 140  ? -60.40100  52.38400  27.35200  1.000 60.14596  ?  140  LEU   A CG  1 
ATOM   1127  C  CD1 . LEU   A 1 140  ? -60.09000  50.90200  27.20900  1.000 52.52888  ?  140  LEU   A CD1 1 
ATOM   1128  C  CD2 . LEU   A 1 140  ? -59.38900  53.06600  28.26100  1.000 40.66680  ?  140  LEU   A CD2 1 
ATOM   1129  N  N   . PHE   A 1 141  ? -63.55800  53.68300  25.53200  1.000 38.40092  ?  141  PHE   A N   1 
ATOM   1130  C  CA  . PHE   A 1 141  ? -64.93000  53.74700  26.02300  1.000 44.24940  ?  141  PHE   A CA  1 
ATOM   1131  C  C   . PHE   A 1 141  ? -65.85000  52.86800  25.18700  1.000 51.18730  ?  141  PHE   A C   1 
ATOM   1132  O  O   . PHE   A 1 141  ? -66.70500  52.15800  25.72900  1.000 57.46763  ?  141  PHE   A O   1 
ATOM   1133  C  CB  . PHE   A 1 141  ? -65.41800  55.19600  26.02000  1.000 41.61913  ?  141  PHE   A CB  1 
ATOM   1134  C  CG  . PHE   A 1 141  ? -66.71100  55.40500  26.75400  1.000 55.06620  ?  141  PHE   A CG  1 
ATOM   1135  C  CD1 . PHE   A 1 141  ? -67.92500  55.27700  26.09900  1.000 51.63213  ?  141  PHE   A CD1 1 
ATOM   1136  C  CD2 . PHE   A 1 141  ? -66.71200  55.73600  28.09900  1.000 60.95364  ?  141  PHE   A CD2 1 
ATOM   1137  C  CE1 . PHE   A 1 141  ? -69.11500  55.47100  26.77300  1.000 57.87725  ?  141  PHE   A CE1 1 
ATOM   1138  C  CE2 . PHE   A 1 141  ? -67.90000  55.93300  28.77800  1.000 61.62832  ?  141  PHE   A CE2 1 
ATOM   1139  C  CZ  . PHE   A 1 141  ? -69.10200  55.80200  28.11400  1.000 52.58642  ?  141  PHE   A CZ  1 
ATOM   1140  N  N   . ILE   A 1 142  ? -65.68600  52.89800  23.86200  1.000 45.14291  ?  142  ILE   A N   1 
ATOM   1141  C  CA  . ILE   A 1 142  ? -66.48500  52.04400  22.98800  1.000 40.55242  ?  142  ILE   A CA  1 
ATOM   1142  C  C   . ILE   A 1 142  ? -66.21400  50.57400  23.27800  1.000 45.97629  ?  142  ILE   A C   1 
ATOM   1143  O  O   . ILE   A 1 142  ? -67.08200  49.71700  23.07200  1.000 55.84132  ?  142  ILE   A O   1 
ATOM   1144  C  CB  . ILE   A 1 142  ? -66.20100  52.40100  21.51400  1.000 35.44199  ?  142  ILE   A CB  1 
ATOM   1145  C  CG1 . ILE   A 1 142  ? -66.56000  53.86400  21.24600  1.000 42.11318  ?  142  ILE   A CG1 1 
ATOM   1146  C  CG2 . ILE   A 1 142  ? -66.96900  51.49400  20.56900  1.000 41.98007  ?  142  ILE   A CG2 1 
ATOM   1147  C  CD1 . ILE   A 1 142  ? -66.29300  54.30900  19.82500  1.000 54.64210  ?  142  ILE   A CD1 1 
ATOM   1148  N  N   . ARG   A 1 143  ? -65.02600  50.26300  23.79000  1.000 47.24142  ?  143  ARG   A N   1 
ATOM   1149  C  CA  . ARG   A 1 143  ? -64.64000  48.87400  24.00300  1.000 54.18478  ?  143  ARG   A CA  1 
ATOM   1150  C  C   . ARG   A 1 143  ? -65.10900  48.33900  25.35000  1.000 51.68948  ?  143  ARG   A C   1 
ATOM   1151  O  O   . ARG   A 1 143  ? -65.41600  47.14700  25.46300  1.000 56.75305  ?  143  ARG   A O   1 
ATOM   1152  C  CB  . ARG   A 1 143  ? -63.12000  48.74500  23.88300  1.000 49.24760  ?  143  ARG   A CB  1 
ATOM   1153  C  CG  . ARG   A 1 143  ? -62.57600  47.33200  23.97100  1.000 61.64120  ?  143  ARG   A CG  1 
ATOM   1154  C  CD  . ARG   A 1 143  ? -61.08000  47.38500  24.22500  1.000 64.55232  ?  143  ARG   A CD  1 
ATOM   1155  N  NE  . ARG   A 1 143  ? -60.46200  48.46900  23.46900  1.000 68.98333  ?  143  ARG   A NE  1 
ATOM   1156  C  CZ  . ARG   A 1 143  ? -59.33800  49.08100  23.81600  1.000 64.92325  ?  143  ARG   A CZ  1 
ATOM   1157  N  NH1 . ARG   A 1 143  ? -58.67400  48.74100  24.90900  1.000 57.71363  ?  143  ARG   A NH1 1 
ATOM   1158  N  NH2 . ARG   A 1 143  ? -58.87400  50.06600  23.05200  1.000 60.93824  ?  143  ARG   A NH2 1 
ATOM   1159  N  N   . GLU   A 1 144  ? -65.18800  49.19300  26.37000  1.000 49.02501  ?  144  GLU   A N   1 
ATOM   1160  C  CA  . GLU   A 1 144  ? -65.42600  48.74100  27.73200  1.000 58.01017  ?  144  GLU   A CA  1 
ATOM   1161  C  C   . GLU   A 1 144  ? -66.73500  49.23300  28.33600  1.000 52.69648  ?  144  GLU   A C   1 
ATOM   1162  O  O   . GLU   A 1 144  ? -67.04400  48.86000  29.47400  1.000 60.95609  ?  144  GLU   A O   1 
ATOM   1163  C  CB  . GLU   A 1 144  ? -64.26400  49.17300  28.64100  1.000 44.78416  ?  144  GLU   A CB  1 
ATOM   1164  C  CG  . GLU   A 1 144  ? -62.89400  48.67400  28.19700  1.000 65.63451  ?  144  GLU   A CG  1 
ATOM   1165  C  CD  . GLU   A 1 144  ? -62.68100  47.19500  28.47400  1.000 75.03886  ?  144  GLU   A CD  1 
ATOM   1166  O  OE1 . GLU   A 1 144  ? -63.38200  46.64200  29.34700  1.000 61.41877  ?  144  GLU   A OE1 1 
ATOM   1167  O  OE2 . GLU   A 1 144  ? -61.80800  46.58700  27.81800  1.000 74.79748  -1 144  GLU   A OE2 1 
ATOM   1168  N  N   . TRP   A 1 145  ? -67.51700  50.04700  27.62000  1.000 45.70052  ?  145  TRP   A N   1 
ATOM   1169  C  CA  . TRP   A 1 145  ? -68.71500  50.63000  28.22100  1.000 53.33668  ?  145  TRP   A CA  1 
ATOM   1170  C  C   . TRP   A 1 145  ? -69.71200  49.55900  28.64300  1.000 65.79035  ?  145  TRP   A C   1 
ATOM   1171  O  O   . TRP   A 1 145  ? -70.31100  49.65200  29.72100  1.000 70.85922  ?  145  TRP   A O   1 
ATOM   1172  C  CB  . TRP   A 1 145  ? -69.37300  51.61400  27.25500  1.000 58.97372  ?  145  TRP   A CB  1 
ATOM   1173  C  CG  . TRP   A 1 145  ? -70.74400  52.03900  27.68500  1.000 63.16049  ?  145  TRP   A CG  1 
ATOM   1174  C  CD1 . TRP   A 1 145  ? -71.91600  51.80800  27.02700  1.000 54.07498  ?  145  TRP   A CD1 1 
ATOM   1175  C  CD2 . TRP   A 1 145  ? -71.08800  52.75900  28.87700  1.000 63.10780  ?  145  TRP   A CD2 1 
ATOM   1176  N  NE1 . TRP   A 1 145  ? -72.96700  52.34600  27.72800  1.000 56.85928  ?  145  TRP   A NE1 1 
ATOM   1177  C  CE2 . TRP   A 1 145  ? -72.48600  52.93500  28.86800  1.000 60.06517  ?  145  TRP   A CE2 1 
ATOM   1178  C  CE3 . TRP   A 1 145  ? -70.35000  53.27400  29.94800  1.000 49.94278  ?  145  TRP   A CE3 1 
ATOM   1179  C  CZ2 . TRP   A 1 145  ? -73.16100  53.60400  29.88700  1.000 55.49454  ?  145  TRP   A CZ2 1 
ATOM   1180  C  CZ3 . TRP   A 1 145  ? -71.02300  53.94000  30.95800  1.000 47.19258  ?  145  TRP   A CZ3 1 
ATOM   1181  C  CH2 . TRP   A 1 145  ? -72.41400  54.09700  30.92100  1.000 53.24292  ?  145  TRP   A CH2 1 
ATOM   1182  N  N   . GLU   A 1 146  ? -69.91000  48.53700  27.80800  1.000 63.40569  ?  146  GLU   A N   1 
ATOM   1183  C  CA  . GLU   A 1 146  ? -70.82000  47.46000  28.18100  1.000 58.87865  ?  146  GLU   A CA  1 
ATOM   1184  C  C   . GLU   A 1 146  ? -70.29300  46.68500  29.38300  1.000 59.03896  ?  146  GLU   A C   1 
ATOM   1185  O  O   . GLU   A 1 146  ? -71.07100  46.27800  30.25400  1.000 65.46342  ?  146  GLU   A O   1 
ATOM   1186  C  CB  . GLU   A 1 146  ? -71.05300  46.52600  26.99400  1.000 65.00109  ?  146  GLU   A CB  1 
ATOM   1187  C  CG  . GLU   A 1 146  ? -72.12200  47.01600  26.03000  1.000 71.15909  ?  146  GLU   A CG  1 
ATOM   1188  C  CD  . GLU   A 1 146  ? -72.33400  46.07500  24.86000  1.000 86.37540  ?  146  GLU   A CD  1 
ATOM   1189  O  OE1 . GLU   A 1 146  ? -72.10200  44.85800  25.02100  1.000 84.43410  ?  146  GLU   A OE1 1 
ATOM   1190  O  OE2 . GLU   A 1 146  ? -72.72800  46.55600  23.77600  1.000 78.64713  -1 146  GLU   A OE2 1 
ATOM   1191  N  N   . ASN   A 1 147  ? -68.97500  46.48100  29.45500  1.000 69.42430  ?  147  ASN   A N   1 
ATOM   1192  C  CA  . ASN   A 1 147  ? -68.39400  45.81600  30.61500  1.000 67.84696  ?  147  ASN   A CA  1 
ATOM   1193  C  C   . ASN   A 1 147  ? -68.47900  46.66800  31.87300  1.000 69.22634  ?  147  ASN   A C   1 
ATOM   1194  O  O   . ASN   A 1 147  ? -68.32600  46.13700  32.97700  1.000 77.31986  ?  147  ASN   A O   1 
ATOM   1195  C  CB  . ASN   A 1 147  ? -66.93600  45.44100  30.33800  1.000 46.52903  ?  147  ASN   A CB  1 
ATOM   1196  C  CG  . ASN   A 1 147  ? -66.80500  44.31800  29.32900  1.000 66.47424  ?  147  ASN   A CG  1 
ATOM   1197  O  OD1 . ASN   A 1 147  ? -67.53400  44.26800  28.33900  1.000 85.01122  ?  147  ASN   A OD1 1 
ATOM   1198  N  ND2 . ASN   A 1 147  ? -65.87900  43.39900  29.58300  1.000 72.57935  ?  147  ASN   A ND2 1 
ATOM   1199  N  N   . ILE   A 1 148  ? -68.71900  47.96900  31.73400  1.000 65.63839  ?  148  ILE   A N   1 
ATOM   1200  C  CA  . ILE   A 1 148  ? -68.85500  48.85100  32.88900  1.000 71.73851  ?  148  ILE   A CA  1 
ATOM   1201  C  C   . ILE   A 1 148  ? -70.29800  48.92000  33.36500  1.000 65.68972  ?  148  ILE   A C   1 
ATOM   1202  O  O   . ILE   A 1 148  ? -70.58000  48.75400  34.55400  1.000 78.47024  ?  148  ILE   A O   1 
ATOM   1203  C  CB  . ILE   A 1 148  ? -68.31300  50.25600  32.55200  1.000 63.86364  ?  148  ILE   A CB  1 
ATOM   1204  C  CG1 . ILE   A 1 148  ? -66.81100  50.20100  32.26700  1.000 59.63039  ?  148  ILE   A CG1 1 
ATOM   1205  C  CG2 . ILE   A 1 148  ? -68.60700  51.21700  33.69000  1.000 39.18104  ?  148  ILE   A CG2 1 
ATOM   1206  C  CD1 . ILE   A 1 148  ? -66.26000  51.47100  31.65300  1.000 50.41051  ?  148  ILE   A CD1 1 
ATOM   1207  N  N   . VAL   A 1 149  ? -71.23000  49.16800  32.44100  1.000 71.48624  ?  149  VAL   A N   1 
ATOM   1208  C  CA  . VAL   A 1 149  ? -72.63200  49.32100  32.81600  1.000 71.04881  ?  149  VAL   A CA  1 
ATOM   1209  C  C   . VAL   A 1 149  ? -73.19100  48.01900  33.37600  1.000 68.33766  ?  149  VAL   A C   1 
ATOM   1210  O  O   . VAL   A 1 149  ? -74.12300  48.03200  34.18900  1.000 67.67910  ?  149  VAL   A O   1 
ATOM   1211  C  CB  . VAL   A 1 149  ? -73.45000  49.82700  31.60800  1.000 57.72804  ?  149  VAL   A CB  1 
ATOM   1212  C  CG1 . VAL   A 1 149  ? -73.49400  48.77600  30.50600  1.000 62.88186  ?  149  VAL   A CG1 1 
ATOM   1213  C  CG2 . VAL   A 1 149  ? -74.85300  50.23300  32.03500  1.000 53.15739  ?  149  VAL   A CG2 1 
ATOM   1214  N  N   . HIS   A 1 150  ? -72.62700  46.88200  32.97300  1.000 67.46450  ?  150  HIS   A N   1 
ATOM   1215  C  CA  . HIS   A 1 150  ? -73.06100  45.58100  33.46100  1.000 70.80736  ?  150  HIS   A CA  1 
ATOM   1216  C  C   . HIS   A 1 150  ? -72.27200  45.11000  34.67700  1.000 75.71183  ?  150  HIS   A C   1 
ATOM   1217  O  O   . HIS   A 1 150  ? -72.39800  43.94500  35.06700  1.000 88.93592  ?  150  HIS   A O   1 
ATOM   1218  C  CB  . HIS   A 1 150  ? -72.97000  44.54200  32.34100  1.000 76.97132  ?  150  HIS   A CB  1 
ATOM   1219  C  CG  . HIS   A 1 150  ? -74.17900  44.50100  31.45900  1.000 72.33207  ?  150  HIS   A CG  1 
ATOM   1220  N  ND1 . HIS   A 1 150  ? -74.09800  44.46600  30.08400  1.000 73.98770  ?  150  HIS   A ND1 1 
ATOM   1221  C  CD2 . HIS   A 1 150  ? -75.49900  44.48300  31.75900  1.000 82.62311  ?  150  HIS   A CD2 1 
ATOM   1222  C  CE1 . HIS   A 1 150  ? -75.31600  44.43200  29.57400  1.000 90.27868  ?  150  HIS   A CE1 1 
ATOM   1223  N  NE2 . HIS   A 1 150  ? -76.18500  44.44100  30.57000  1.000 111.66765 ?  150  HIS   A NE2 1 
ATOM   1224  N  N   . GLY   A 1 151  ? -71.46700  45.98200  35.27700  1.000 75.50107  ?  151  GLY   A N   1 
ATOM   1225  C  CA  . GLY   A 1 151  ? -70.75900  45.63900  36.50100  1.000 71.00119  ?  151  GLY   A CA  1 
ATOM   1226  C  C   . GLY   A 1 151  ? -69.78400  44.49000  36.36600  1.000 71.93844  ?  151  GLY   A C   1 
ATOM   1227  O  O   . GLY   A 1 151  ? -69.65400  43.67900  37.29100  1.000 88.93608  ?  151  GLY   A O   1 
ATOM   1228  N  N   . ARG   A 1 152  ? -69.09300  44.39900  35.23200  1.000 69.99656  ?  152  ARG   A N   1 
ATOM   1229  C  CA  . ARG   A 1 152  ? -68.10300  43.35600  35.00800  1.000 67.30794  ?  152  ARG   A CA  1 
ATOM   1230  C  C   . ARG   A 1 152  ? -66.68000  43.83000  35.26100  1.000 71.27539  ?  152  ARG   A C   1 
ATOM   1231  O  O   . ARG   A 1 152  ? -65.74100  43.04500  35.09900  1.000 75.37018  ?  152  ARG   A O   1 
ATOM   1232  C  CB  . ARG   A 1 152  ? -68.21200  42.81700  33.57900  1.000 72.96481  ?  152  ARG   A CB  1 
ATOM   1233  C  CG  . ARG   A 1 152  ? -69.63000  42.56900  33.09900  1.000 79.44461  ?  152  ARG   A CG  1 
ATOM   1234  C  CD  . ARG   A 1 152  ? -69.60400  41.89500  31.73900  1.000 84.52773  ?  152  ARG   A CD  1 
ATOM   1235  N  NE  . ARG   A 1 152  ? -70.75400  42.24400  30.91500  1.000 83.83766  ?  152  ARG   A NE  1 
ATOM   1236  C  CZ  . ARG   A 1 152  ? -70.82200  42.03300  29.60800  1.000 84.37263  ?  152  ARG   A CZ  1 
ATOM   1237  N  NH1 . ARG   A 1 152  ? -69.81900  41.47800  28.94600  1.000 94.33234  ?  152  ARG   A NH1 1 
ATOM   1238  N  NH2 . ARG   A 1 152  ? -71.91900  42.39200  28.94700  1.000 88.93536  ?  152  ARG   A NH2 1 
ATOM   1239  N  N   . ILE   A 1 153  ? -66.49900  45.08900  35.64700  1.000 74.00925  ?  153  ILE   A N   1 
ATOM   1240  C  CA  . ILE   A 1 153  ? -65.18500  45.66900  35.89400  1.000 70.11665  ?  153  ILE   A CA  1 
ATOM   1241  C  C   . ILE   A 1 153  ? -65.14500  46.16700  37.33000  1.000 68.50084  ?  153  ILE   A C   1 
ATOM   1242  O  O   . ILE   A 1 153  ? -66.03700  46.90800  37.76200  1.000 64.83448  ?  153  ILE   A O   1 
ATOM   1243  C  CB  . ILE   A 1 153  ? -64.87500  46.80600  34.90200  1.000 73.67965  ?  153  ILE   A CB  1 
ATOM   1244  C  CG1 . ILE   A 1 153  ? -64.28900  46.23300  33.60900  1.000 62.31064  ?  153  ILE   A CG1 1 
ATOM   1245  C  CG2 . ILE   A 1 153  ? -63.93600  47.83000  35.52600  1.000 62.85156  ?  153  ILE   A CG2 1 
ATOM   1246  C  CD1 . ILE   A 1 153  ? -64.29500  47.20300  32.45000  1.000 59.12733  ?  153  ILE   A CD1 1 
ATOM   1247  N  N   . ALA   A 1 154  ? -64.11800  45.75200  38.06900  1.000 61.07162  ?  154  ALA   A N   1 
ATOM   1248  C  CA  . ALA   A 1 154  ? -63.96600  46.15100  39.46000  1.000 62.36784  ?  154  ALA   A CA  1 
ATOM   1249  C  C   . ALA   A 1 154  ? -63.07800  47.38300  39.54600  1.000 68.10642  ?  154  ALA   A C   1 
ATOM   1250  O  O   . ALA   A 1 154  ? -61.94100  47.34700  39.05600  1.000 82.22909  ?  154  ALA   A O   1 
ATOM   1251  C  CB  . ALA   A 1 154  ? -63.36700  45.02100  40.28000  1.000 61.71563  ?  154  ALA   A CB  1 
ATOM   1252  N  N   . PRO   A 1 155  ? -63.54400  48.48100  40.13800  1.000 57.11463  ?  155  PRO   A N   1 
ATOM   1253  C  CA  . PRO   A 1 155  ? -62.68700  49.66600  40.26600  1.000 62.64959  ?  155  PRO   A CA  1 
ATOM   1254  C  C   . PRO   A 1 155  ? -61.50400  49.39400  41.18100  1.000 71.73879  ?  155  PRO   A C   1 
ATOM   1255  O  O   . PRO   A 1 155  ? -61.62100  48.68100  42.18000  1.000 92.31991  ?  155  PRO   A O   1 
ATOM   1256  C  CB  . PRO   A 1 155  ? -63.62400  50.72300  40.86600  1.000 53.55507  ?  155  PRO   A CB  1 
ATOM   1257  C  CG  . PRO   A 1 155  ? -65.00900  50.21100  40.61900  1.000 69.51196  ?  155  PRO   A CG  1 
ATOM   1258  C  CD  . PRO   A 1 155  ? -64.90300  48.72000  40.64800  1.000 57.89609  ?  155  PRO   A CD  1 
ATOM   1259  N  N   . TYR   A 1 156  ? -60.35400  49.96500  40.82800  1.000 70.24987  ?  156  TYR   A N   1 
ATOM   1260  C  CA  . TYR   A 1 156  ? -59.16400  49.87400  41.65900  1.000 66.40140  ?  156  TYR   A CA  1 
ATOM   1261  C  C   . TYR   A 1 156  ? -58.60800  51.26700  41.91600  1.000 65.84542  ?  156  TYR   A C   1 
ATOM   1262  O  O   . TYR   A 1 156  ? -58.73100  52.16600  41.08000  1.000 75.43126  ?  156  TYR   A O   1 
ATOM   1263  C  CB  . TYR   A 1 156  ? -58.08200  48.96400  41.03000  1.000 55.79368  ?  156  TYR   A CB  1 
ATOM   1264  C  CG  . TYR   A 1 156  ? -57.61800  49.33200  39.63100  1.000 65.25662  ?  156  TYR   A CG  1 
ATOM   1265  C  CD1 . TYR   A 1 156  ? -56.77300  50.41500  39.41600  1.000 70.85565  ?  156  TYR   A CD1 1 
ATOM   1266  C  CD2 . TYR   A 1 156  ? -57.98800  48.56500  38.53200  1.000 60.57691  ?  156  TYR   A CD2 1 
ATOM   1267  C  CE1 . TYR   A 1 156  ? -56.33600  50.74200  38.14600  1.000 73.70288  ?  156  TYR   A CE1 1 
ATOM   1268  C  CE2 . TYR   A 1 156  ? -57.55300  48.88400  37.25700  1.000 72.03023  ?  156  TYR   A CE2 1 
ATOM   1269  C  CZ  . TYR   A 1 156  ? -56.72700  49.97300  37.07100  1.000 67.21931  ?  156  TYR   A CZ  1 
ATOM   1270  O  OH  . TYR   A 1 156  ? -56.29200  50.29500  35.80500  1.000 88.85001  ?  156  TYR   A OH  1 
ATOM   1271  N  N   . ARG   A 1 157  ? -58.00500  51.43900  43.09000  1.000 68.83598  ?  157  ARG   A N   1 
ATOM   1272  C  CA  . ARG   A 1 157  ? -57.43300  52.72500  43.45700  1.000 66.85374  ?  157  ARG   A CA  1 
ATOM   1273  C  C   . ARG   A 1 157  ? -56.18800  53.01900  42.62400  1.000 78.00362  ?  157  ARG   A C   1 
ATOM   1274  O  O   . ARG   A 1 157  ? -55.61200  52.13700  41.98100  1.000 77.45669  ?  157  ARG   A O   1 
ATOM   1275  C  CB  . ARG   A 1 157  ? -57.07600  52.75900  44.94500  1.000 81.31112  ?  157  ARG   A CB  1 
ATOM   1276  C  CG  . ARG   A 1 157  ? -58.24100  52.51900  45.89300  1.000 89.16985  ?  157  ARG   A CG  1 
ATOM   1277  C  CD  . ARG   A 1 157  ? -58.05000  53.29400  47.19200  1.000 91.73454  ?  157  ARG   A CD  1 
ATOM   1278  N  NE  . ARG   A 1 157  ? -58.53400  52.56100  48.35700  1.000 110.66119 ?  157  ARG   A NE  1 
ATOM   1279  C  CZ  . ARG   A 1 157  ? -57.75300  52.05400  49.30200  1.000 94.87233  ?  157  ARG   A CZ  1 
ATOM   1280  N  NH1 . ARG   A 1 157  ? -56.43900  52.20300  49.26600  1.000 72.84281  ?  157  ARG   A NH1 1 
ATOM   1281  N  NH2 . ARG   A 1 157  ? -58.30500  51.38800  50.31200  1.000 78.20727  ?  157  ARG   A NH2 1 
ATOM   1282  N  N   . GLN   A 1 158  ? -55.77100  54.28100  42.65000  1.000 71.22945  ?  158  GLN   A N   1 
ATOM   1283  C  CA  . GLN   A 1 158  ? -54.60200  54.70500  41.89600  1.000 68.33657  ?  158  GLN   A CA  1 
ATOM   1284  C  C   . GLN   A 1 158  ? -53.32000  54.32500  42.62300  1.000 86.16483  ?  158  GLN   A C   1 
ATOM   1285  O  O   . GLN   A 1 158  ? -53.26100  54.31000  43.85500  1.000 93.95102  ?  158  GLN   A O   1 
ATOM   1286  C  CB  . GLN   A 1 158  ? -54.61900  56.21800  41.66700  1.000 73.73919  ?  158  GLN   A CB  1 
ATOM   1287  C  CG  . GLN   A 1 158  ? -55.98400  56.81600  41.38500  1.000 78.13363  ?  158  GLN   A CG  1 
ATOM   1288  C  CD  . GLN   A 1 158  ? -55.89400  58.12100  40.61600  1.000 72.51131  ?  158  GLN   A CD  1 
ATOM   1289  O  OE1 . GLN   A 1 158  ? -54.98200  58.92100  40.83000  1.000 68.28690  ?  158  GLN   A OE1 1 
ATOM   1290  N  NE2 . GLN   A 1 158  ? -56.83700  58.33700  39.70600  1.000 65.54682  ?  158  GLN   A NE2 1 
ATOM   1291  N  N   . THR   A 1 159  ? -52.28600  54.01300  41.84200  1.000 75.24944  ?  159  THR   A N   1 
ATOM   1292  C  CA  . THR   A 1 159  ? -50.93800  53.96500  42.39000  1.000 70.68752  ?  159  THR   A CA  1 
ATOM   1293  C  C   . THR   A 1 159  ? -50.59700  55.33100  42.97900  1.000 78.61771  ?  159  THR   A C   1 
ATOM   1294  O  O   . THR   A 1 159  ? -51.01100  56.36700  42.45400  1.000 89.12418  ?  159  THR   A O   1 
ATOM   1295  C  CB  . THR   A 1 159  ? -49.94200  53.55100  41.29800  1.000 83.71384  ?  159  THR   A CB  1 
ATOM   1296  O  OG1 . THR   A 1 159  ? -49.97900  52.12600  41.13400  1.000 89.14210  ?  159  THR   A OG1 1 
ATOM   1297  C  CG2 . THR   A 1 159  ? -48.52000  53.98100  41.63200  1.000 81.68178  ?  159  THR   A CG2 1 
ATOM   1298  N  N   . ALA   A 1 160  ? -49.85300  55.32400  44.08900  1.000 69.67499  ?  160  ALA   A N   1 
ATOM   1299  C  CA  . ALA   A 1 160  ? -49.78600  56.47500  44.98900  1.000 88.65115  ?  160  ALA   A CA  1 
ATOM   1300  C  C   . ALA   A 1 160  ? -49.43300  57.77800  44.27200  1.000 91.60032  ?  160  ALA   A C   1 
ATOM   1301  O  O   . ALA   A 1 160  ? -50.22600  58.72600  44.25400  1.000 83.90416  ?  160  ALA   A O   1 
ATOM   1302  C  CB  . ALA   A 1 160  ? -48.78000  56.19200  46.10700  1.000 79.66987  ?  160  ALA   A CB  1 
ATOM   1303  N  N   . GLY   A 1 161  ? -48.24100  57.85000  43.68700  1.000 73.23969  ?  161  GLY   A N   1 
ATOM   1304  C  CA  . GLY   A 1 161  ? -47.66200  59.11800  43.26000  1.000 70.80800  ?  161  GLY   A CA  1 
ATOM   1305  C  C   . GLY   A 1 161  ? -47.92400  59.44800  41.80000  1.000 79.33639  ?  161  GLY   A C   1 
ATOM   1306  O  O   . GLY   A 1 161  ? -47.91800  58.56800  40.94000  1.000 90.31083  ?  161  GLY   A O   1 
ATOM   1307  N  N   . GLY   A 1 162  ? -48.13200  60.73900  41.53400  1.000 78.89222  ?  162  GLY   A N   1 
ATOM   1308  C  CA  . GLY   A 1 162  ? -48.34100  61.22500  40.18300  1.000 65.29464  ?  162  GLY   A CA  1 
ATOM   1309  C  C   . GLY   A 1 162  ? -48.08600  62.71100  40.02100  1.000 58.10738  ?  162  GLY   A C   1 
ATOM   1310  O  O   . GLY   A 1 162  ? -47.17000  63.25700  40.64300  1.000 77.44176  ?  162  GLY   A O   1 
ATOM   1311  N  N   . THR   A 1 163  ? -48.88700  63.38100  39.19100  1.000 61.62692  ?  163  THR   A N   1 
ATOM   1312  C  CA  . THR   A 1 163  ? -48.70300  64.79800  38.91200  1.000 53.93756  ?  163  THR   A CA  1 
ATOM   1313  C  C   . THR   A 1 163  ? -50.05400  65.47600  38.74900  1.000 52.37406  ?  163  THR   A C   1 
ATOM   1314  O  O   . THR   A 1 163  ? -50.98900  64.89000  38.19700  1.000 55.28830  ?  163  THR   A O   1 
ATOM   1315  C  CB  . THR   A 1 163  ? -47.87000  65.02000  37.64200  1.000 67.93011  ?  163  THR   A CB  1 
ATOM   1316  O  OG1 . THR   A 1 163  ? -46.87000  64.00000  37.53800  1.000 99.31146  ?  163  THR   A OG1 1 
ATOM   1317  C  CG2 . THR   A 1 163  ? -47.19200  66.38200  37.68500  1.000 70.68369  ?  163  THR   A CG2 1 
ATOM   1318  N  N   . LEU   A 1 164  ? -50.14400  66.71800  39.22000  1.000 53.65789  ?  164  LEU   A N   1 
ATOM   1319  C  CA  . LEU   A 1 164  ? -51.34500  67.53100  39.09500  1.000 50.37582  ?  164  LEU   A CA  1 
ATOM   1320  C  C   . LEU   A 1 164  ? -50.98100  68.86000  38.44800  1.000 48.49499  ?  164  LEU   A C   1 
ATOM   1321  O  O   . LEU   A 1 164  ? -49.95800  69.46400  38.78700  1.000 50.56980  ?  164  LEU   A O   1 
ATOM   1322  C  CB  . LEU   A 1 164  ? -52.00400  67.77200  40.46200  1.000 47.11620  ?  164  LEU   A CB  1 
ATOM   1323  C  CG  . LEU   A 1 164  ? -53.30900  68.57200  40.48700  1.000 44.93392  ?  164  LEU   A CG  1 
ATOM   1324  C  CD1 . LEU   A 1 164  ? -54.48900  67.70800  40.06500  1.000 52.39999  ?  164  LEU   A CD1 1 
ATOM   1325  C  CD2 . LEU   A 1 164  ? -53.54600  69.18200  41.86000  1.000 35.24357  ?  164  LEU   A CD2 1 
ATOM   1326  N  N   . HIS   A 1 165  ? -51.81600  69.31100  37.51400  1.000 44.63553  ?  165  HIS   A N   1 
ATOM   1327  C  CA  . HIS   A 1 165  ? -51.59300  70.57300  36.82600  1.000 43.86062  ?  165  HIS   A CA  1 
ATOM   1328  C  C   . HIS   A 1 165  ? -52.90400  71.33500  36.72000  1.000 48.53753  ?  165  HIS   A C   1 
ATOM   1329  O  O   . HIS   A 1 165  ? -53.99000  70.77000  36.86300  1.000 58.41186  ?  165  HIS   A O   1 
ATOM   1330  C  CB  . HIS   A 1 165  ? -50.99200  70.36200  35.43000  1.000 56.06397  ?  165  HIS   A CB  1 
ATOM   1331  C  CG  . HIS   A 1 165  ? -49.55800  69.93400  35.45000  1.000 57.04230  ?  165  HIS   A CG  1 
ATOM   1332  N  ND1 . HIS   A 1 165  ? -48.51700  70.82900  35.57700  1.000 50.33099  ?  165  HIS   A ND1 1 
ATOM   1333  C  CD2 . HIS   A 1 165  ? -48.99200  68.70800  35.36100  1.000 55.42359  ?  165  HIS   A CD2 1 
ATOM   1334  C  CE1 . HIS   A 1 165  ? -47.37100  70.17200  35.56500  1.000 59.44326  ?  165  HIS   A CE1 1 
ATOM   1335  N  NE2 . HIS   A 1 165  ? -47.63100  68.88300  35.43400  1.000 69.18183  ?  165  HIS   A NE2 1 
ATOM   1336  N  N   . PHE   A 1 166  ? -52.78800  72.63200  36.46400  1.000 43.91015  ?  166  PHE   A N   1 
ATOM   1337  C  CA  . PHE   A 1 166  ? -53.93800  73.51800  36.36200  1.000 49.64737  ?  166  PHE   A CA  1 
ATOM   1338  C  C   . PHE   A 1 166  ? -53.93100  74.23100  35.00700  1.000 66.29816  ?  166  PHE   A C   1 
ATOM   1339  O  O   . PHE   A 1 166  ? -53.15300  73.90300  34.10800  1.000 77.18844  ?  166  PHE   A O   1 
ATOM   1340  C  CB  . PHE   A 1 166  ? -53.95600  74.50100  37.53400  1.000 59.30753  ?  166  PHE   A CB  1 
ATOM   1341  C  CG  . PHE   A 1 166  ? -54.42000  73.88600  38.82200  1.000 74.73951  ?  166  PHE   A CG  1 
ATOM   1342  C  CD1 . PHE   A 1 166  ? -53.54700  73.15900  39.61500  1.000 73.63169  ?  166  PHE   A CD1 1 
ATOM   1343  C  CD2 . PHE   A 1 166  ? -55.73600  74.02000  39.23100  1.000 85.14657  ?  166  PHE   A CD2 1 
ATOM   1344  C  CE1 . PHE   A 1 166  ? -53.97600  72.58400  40.79700  1.000 60.56328  ?  166  PHE   A CE1 1 
ATOM   1345  C  CE2 . PHE   A 1 166  ? -56.17000  73.44700  40.41100  1.000 90.43289  ?  166  PHE   A CE2 1 
ATOM   1346  C  CZ  . PHE   A 1 166  ? -55.29000  72.73000  41.19500  1.000 72.01271  ?  166  PHE   A CZ  1 
ATOM   1347  N  N   . LYS   A 1 167  ? -54.80800  75.22600  34.87900  1.000 48.70538  ?  167  LYS   A N   1 
ATOM   1348  C  CA  . LYS   A 1 167  ? -55.10900  75.81700  33.57900  1.000 58.86267  ?  167  LYS   A CA  1 
ATOM   1349  C  C   . LYS   A 1 167  ? -53.98700  76.73000  33.09300  1.000 64.27193  ?  167  LYS   A C   1 
ATOM   1350  O  O   . LYS   A 1 167  ? -53.50500  76.58400  31.96500  1.000 75.11002  ?  167  LYS   A O   1 
ATOM   1351  C  CB  . LYS   A 1 167  ? -56.42800  76.58900  33.65200  1.000 58.98492  ?  167  LYS   A CB  1 
ATOM   1352  C  CG  . LYS   A 1 167  ? -57.47300  75.93600  34.53100  1.000 67.67823  ?  167  LYS   A CG  1 
ATOM   1353  C  CD  . LYS   A 1 167  ? -57.39400  76.45800  35.94500  1.000 85.05081  ?  167  LYS   A CD  1 
ATOM   1354  C  CE  . LYS   A 1 167  ? -58.23100  75.61100  36.87000  1.000 91.40290  ?  167  LYS   A CE  1 
ATOM   1355  N  NZ  . LYS   A 1 167  ? -58.30600  76.26400  38.19100  1.000 101.30660 ?  167  LYS   A NZ  1 
ATOM   1356  N  N   . ALA   A 1 168  ? -53.55900  77.67700  33.92800  1.000 59.49189  ?  168  ALA   A N   1 
ATOM   1357  C  CA  . ALA   A 1 168  ? -52.57400  78.67500  33.53000  1.000 64.17861  ?  168  ALA   A CA  1 
ATOM   1358  C  C   . ALA   A 1 168  ? -51.13600  78.18200  33.65100  1.000 58.48420  ?  168  ALA   A C   1 
ATOM   1359  O  O   . ALA   A 1 168  ? -50.20900  78.99100  33.53100  1.000 68.03868  ?  168  ALA   A O   1 
ATOM   1360  C  CB  . ALA   A 1 168  ? -52.75200  79.94600  34.36100  1.000 72.48247  ?  168  ALA   A CB  1 
ATOM   1361  N  N   . ASP   A 1 169  ? -50.92500  76.88700  33.88000  1.000 48.63661  ?  169  ASP   A N   1 
ATOM   1362  C  CA  . ASP   A 1 169  ? -49.57700  76.34700  34.00300  1.000 51.38287  ?  169  ASP   A CA  1 
ATOM   1363  C  C   . ASP   A 1 169  ? -48.88300  76.15400  32.66100  1.000 53.47903  ?  169  ASP   A C   1 
ATOM   1364  O  O   . ASP   A 1 169  ? -47.69500  75.81600  32.64000  1.000 68.58847  ?  169  ASP   A O   1 
ATOM   1365  C  CB  . ASP   A 1 169  ? -49.61300  75.01700  34.75800  1.000 60.16292  ?  169  ASP   A CB  1 
ATOM   1366  C  CG  . ASP   A 1 169  ? -50.03500  75.18500  36.20000  1.000 60.16796  ?  169  ASP   A CG  1 
ATOM   1367  O  OD1 . ASP   A 1 169  ? -50.36000  76.32500  36.59100  1.000 60.09718  ?  169  ASP   A OD1 1 
ATOM   1368  O  OD2 . ASP   A 1 169  ? -50.03900  74.17900  36.94200  1.000 56.39611  -1 169  ASP   A OD2 1 
ATOM   1369  N  N   . ARG   A 1 170  ? -49.57700  76.37600  31.54600  1.000 63.97428  ?  170  ARG   A N   1 
ATOM   1370  C  CA  . ARG   A 1 170  ? -49.00600  76.18800  30.22100  1.000 56.68283  ?  170  ARG   A CA  1 
ATOM   1371  C  C   . ARG   A 1 170  ? -48.86400  77.50200  29.45500  1.000 50.10715  ?  170  ARG   A C   1 
ATOM   1372  O  O   . ARG   A 1 170  ? -48.34800  77.49700  28.33100  1.000 56.94383  ?  170  ARG   A O   1 
ATOM   1373  C  CB  . ARG   A 1 170  ? -49.87200  75.18500  29.43800  1.000 40.97844  ?  170  ARG   A CB  1 
ATOM   1374  C  CG  . ARG   A 1 170  ? -49.26100  74.50100  28.20800  1.000 60.72322  ?  170  ARG   A CG  1 
ATOM   1375  C  CD  . ARG   A 1 170  ? -50.21800  74.77800  27.03200  1.000 65.85679  ?  170  ARG   A CD  1 
ATOM   1376  N  NE  . ARG   A 1 170  ? -49.67300  74.47200  25.71700  1.000 51.98587  ?  170  ARG   A NE  1 
ATOM   1377  C  CZ  . ARG   A 1 170  ? -50.03400  73.42300  24.98500  1.000 57.97381  ?  170  ARG   A CZ  1 
ATOM   1378  N  NH1 . ARG   A 1 170  ? -51.07000  72.66600  25.31900  1.000 67.85652  ?  170  ARG   A NH1 1 
ATOM   1379  N  NH2 . ARG   A 1 170  ? -49.32300  73.10400  23.90600  1.000 55.41091  ?  170  ARG   A NH2 1 
ATOM   1380  N  N   . ASP   A 1 171  ? -49.28000  78.63200  30.03800  1.000 51.30138  ?  171  ASP   A N   1 
ATOM   1381  C  CA  . ASP   A 1 171  ? -49.28300  79.91700  29.34000  1.000 57.90334  ?  171  ASP   A CA  1 
ATOM   1382  C  C   . ASP   A 1 171  ? -47.89300  80.41000  28.95600  1.000 65.67307  ?  171  ASP   A C   1 
ATOM   1383  O  O   . ASP   A 1 171  ? -47.78700  81.46700  28.31800  1.000 75.99651  ?  171  ASP   A O   1 
ATOM   1384  C  CB  . ASP   A 1 171  ? -49.98700  80.96800  30.19600  1.000 55.91286  ?  171  ASP   A CB  1 
ATOM   1385  C  CG  . ASP   A 1 171  ? -51.46300  80.69500  30.33500  1.000 70.95815  ?  171  ASP   A CG  1 
ATOM   1386  O  OD1 . ASP   A 1 171  ? -51.94300  79.70700  29.73900  1.000 74.47528  ?  171  ASP   A OD1 1 
ATOM   1387  O  OD2 . ASP   A 1 171  ? -52.14300  81.47200  31.03900  1.000 81.57810  -1 171  ASP   A OD2 1 
ATOM   1388  N  N   . PHE   A 1 172  ? -46.83500  79.69300  29.32700  1.000 63.31532  ?  172  PHE   A N   1 
ATOM   1389  C  CA  . PHE   A 1 172  ? -45.47800  79.99500  28.89500  1.000 47.89543  ?  172  PHE   A CA  1 
ATOM   1390  C  C   . PHE   A 1 172  ? -44.95700  79.01800  27.85000  1.000 53.07592  ?  172  PHE   A C   1 
ATOM   1391  O  O   . PHE   A 1 172  ? -44.14100  79.40500  27.00900  1.000 57.99983  ?  172  PHE   A O   1 
ATOM   1392  C  CB  . PHE   A 1 172  ? -44.53200  79.99400  30.10500  1.000 59.70466  ?  172  PHE   A CB  1 
ATOM   1393  C  CG  . PHE   A 1 172  ? -43.08500  80.21900  29.76200  1.000 66.36968  ?  172  PHE   A CG  1 
ATOM   1394  C  CD1 . PHE   A 1 172  ? -42.66900  81.40000  29.17000  1.000 59.12279  ?  172  PHE   A CD1 1 
ATOM   1395  C  CD2 . PHE   A 1 172  ? -42.13600  79.25300  30.05900  1.000 53.49979  ?  172  PHE   A CD2 1 
ATOM   1396  C  CE1 . PHE   A 1 172  ? -41.33500  81.60700  28.86400  1.000 53.23189  ?  172  PHE   A CE1 1 
ATOM   1397  C  CE2 . PHE   A 1 172  ? -40.80200  79.45500  29.75700  1.000 55.98260  ?  172  PHE   A CE2 1 
ATOM   1398  C  CZ  . PHE   A 1 172  ? -40.40100  80.63200  29.15900  1.000 50.50969  ?  172  PHE   A CZ  1 
ATOM   1399  N  N   . TYR   A 1 173  ? -45.43200  77.76900  27.87500  1.000 56.92652  ?  173  TYR   A N   1 
ATOM   1400  C  CA  . TYR   A 1 173  ? -45.04100  76.73100  26.93300  1.000 66.22558  ?  173  TYR   A CA  1 
ATOM   1401  C  C   . TYR   A 1 173  ? -45.95700  76.66900  25.71300  1.000 64.39867  ?  173  TYR   A C   1 
ATOM   1402  O  O   . TYR   A 1 173  ? -46.01100  75.63600  25.03600  1.000 63.07948  ?  173  TYR   A O   1 
ATOM   1403  C  CB  . TYR   A 1 173  ? -44.99900  75.38200  27.64900  1.000 63.77346  ?  173  TYR   A CB  1 
ATOM   1404  C  CG  . TYR   A 1 173  ? -44.17700  75.41300  28.91800  1.000 62.42638  ?  173  TYR   A CG  1 
ATOM   1405  C  CD1 . TYR   A 1 173  ? -42.79300  75.50700  28.86200  1.000 66.45087  ?  173  TYR   A CD1 1 
ATOM   1406  C  CD2 . TYR   A 1 173  ? -44.78100  75.36900  30.16800  1.000 63.74085  ?  173  TYR   A CD2 1 
ATOM   1407  C  CE1 . TYR   A 1 173  ? -42.03200  75.55200  30.01500  1.000 70.38675  ?  173  TYR   A CE1 1 
ATOM   1408  C  CE2 . TYR   A 1 173  ? -44.02600  75.41100  31.33000  1.000 68.77431  ?  173  TYR   A CE2 1 
ATOM   1409  C  CZ  . TYR   A 1 173  ? -42.65100  75.50200  31.24600  1.000 67.75489  ?  173  TYR   A CZ  1 
ATOM   1410  O  OH  . TYR   A 1 173  ? -41.89200  75.54400  32.39400  1.000 73.32941  ?  173  TYR   A OH  1 
ATOM   1411  N  N   . LYS   A 1 174  ? -46.68800  77.74800  25.43800  1.000 60.82685  ?  174  LYS   A N   1 
ATOM   1412  C  CA  . LYS   A 1 174  ? -47.36600  77.93600  24.16700  1.000 40.36763  ?  174  LYS   A CA  1 
ATOM   1413  C  C   . LYS   A 1 174  ? -46.33100  78.14500  23.06200  1.000 59.16051  ?  174  LYS   A C   1 
ATOM   1414  O  O   . LYS   A 1 174  ? -45.11900  78.10600  23.28800  1.000 74.99680  ?  174  LYS   A O   1 
ATOM   1415  C  CB  . LYS   A 1 174  ? -48.31600  79.12600  24.25200  1.000 35.26191  ?  174  LYS   A CB  1 
ATOM   1416  C  CG  . LYS   A 1 174  ? -47.90500  80.12300  25.31700  1.000 51.55761  ?  174  LYS   A CG  1 
ATOM   1417  C  CD  . LYS   A 1 174  ? -48.69500  81.41300  25.22600  1.000 56.53388  ?  174  LYS   A CD  1 
ATOM   1418  C  CE  . LYS   A 1 174  ? -50.07900  81.26800  25.83000  1.000 75.96625  ?  174  LYS   A CE  1 
ATOM   1419  N  NZ  . LYS   A 1 174  ? -50.77500  82.58100  25.91500  1.000 80.39631  ?  174  LYS   A NZ  1 
ATOM   1420  N  N   . ASN   A 1 175  ? -46.82400  78.38600  21.84600  1.000 51.30542  ?  175  ASN   A N   1 
ATOM   1421  C  CA  . ASN   A 1 175  ? -46.00700  78.49200  20.63900  1.000 58.36299  ?  175  ASN   A CA  1 
ATOM   1422  C  C   . ASN   A 1 175  ? -45.23500  77.21000  20.35200  1.000 40.96394  ?  175  ASN   A C   1 
ATOM   1423  O  O   . ASN   A 1 175  ? -44.37500  77.19800  19.46600  1.000 60.94362  ?  175  ASN   A O   1 
ATOM   1424  C  CB  . ASN   A 1 175  ? -45.02200  79.67100  20.71000  1.000 39.11048  ?  175  ASN   A CB  1 
ATOM   1425  C  CG  . ASN   A 1 175  ? -45.71200  81.02400  20.75800  1.000 65.17887  ?  175  ASN   A CG  1 
ATOM   1426  O  OD1 . ASN   A 1 175  ? -45.05100  82.06100  20.82800  1.000 52.84374  ?  175  ASN   A OD1 1 
ATOM   1427  N  ND2 . ASN   A 1 175  ? -47.03900  81.02200  20.72600  1.000 83.16151  ?  175  ASN   A ND2 1 
ATOM   1428  N  N   . LEU   A 1 176  ? -45.51900  76.13100  21.08300  1.000 38.88316  ?  176  LEU   A N   1 
ATOM   1429  C  CA  . LEU   A 1 176  ? -44.75900  74.88900  20.99600  1.000 42.48823  ?  176  LEU   A CA  1 
ATOM   1430  C  C   . LEU   A 1 176  ? -45.60600  73.70800  20.54100  1.000 49.68035  ?  176  LEU   A C   1 
ATOM   1431  O  O   . LEU   A 1 176  ? -45.15100  72.56200  20.63600  1.000 52.72954  ?  176  LEU   A O   1 
ATOM   1432  C  CB  . LEU   A 1 176  ? -44.11700  74.55900  22.35100  1.000 49.41255  ?  176  LEU   A CB  1 
ATOM   1433  C  CG  . LEU   A 1 176  ? -42.69300  75.00500  22.70000  1.000 52.05337  ?  176  LEU   A CG  1 
ATOM   1434  C  CD1 . LEU   A 1 176  ? -42.52700  76.51000  22.60200  1.000 49.30470  ?  176  LEU   A CD1 1 
ATOM   1435  C  CD2 . LEU   A 1 176  ? -42.33900  74.53400  24.10200  1.000 43.84288  ?  176  LEU   A CD2 1 
ATOM   1436  N  N   . ASN   A 1 177  ? -46.82300  73.95100  20.05100  1.000 47.78819  ?  177  ASN   A N   1 
ATOM   1437  C  CA  . ASN   A 1 177  ? -47.73600  72.85500  19.74400  1.000 46.08623  ?  177  ASN   A CA  1 
ATOM   1438  C  C   . ASN   A 1 177  ? -47.35200  72.10800  18.47600  1.000 55.37740  ?  177  ASN   A C   1 
ATOM   1439  O  O   . ASN   A 1 177  ? -47.62800  70.90700  18.36300  1.000 48.43699  ?  177  ASN   A O   1 
ATOM   1440  C  CB  . ASN   A 1 177  ? -49.16300  73.38100  19.62400  1.000 44.39104  ?  177  ASN   A CB  1 
ATOM   1441  C  CG  . ASN   A 1 177  ? -49.86600  73.44100  20.95400  1.000 70.21174  ?  177  ASN   A CG  1 
ATOM   1442  O  OD1 . ASN   A 1 177  ? -49.79400  72.50200  21.74700  1.000 79.69370  ?  177  ASN   A OD1 1 
ATOM   1443  N  ND2 . ASN   A 1 177  ? -50.54100  74.55100  21.21800  1.000 72.39466  ?  177  ASN   A ND2 1 
ATOM   1444  N  N   . MET   A 1 178  ? -46.73700  72.79100  17.51600  1.000 51.88209  ?  178  MET   A N   1 
ATOM   1445  C  CA  . MET   A 1 178  ? -46.28600  72.16200  16.28300  1.000 46.22825  ?  178  MET   A CA  1 
ATOM   1446  C  C   . MET   A 1 178  ? -44.91300  71.51900  16.41900  1.000 42.19997  ?  178  MET   A C   1 
ATOM   1447  O  O   . MET   A 1 178  ? -44.42300  70.92800  15.45200  1.000 52.12221  ?  178  MET   A O   1 
ATOM   1448  C  CB  . MET   A 1 178  ? -46.25500  73.19000  15.14700  1.000 49.47558  ?  178  MET   A CB  1 
ATOM   1449  C  CG  . MET   A 1 178  ? -47.61500  73.74300  14.73700  1.000 59.31827  ?  178  MET   A CG  1 
ATOM   1450  S  SD  . MET   A 1 178  ? -48.57400  72.63800  13.67700  1.000 96.64062  ?  178  MET   A SD  1 
ATOM   1451  C  CE  . MET   A 1 178  ? -47.28000  71.71600  12.84100  1.000 65.85781  ?  178  MET   A CE  1 
ATOM   1452  N  N   . THR   A 1 179  ? -44.28600  71.62100  17.58600  1.000 43.03341  ?  179  THR   A N   1 
ATOM   1453  C  CA  . THR   A 1 179  ? -42.93600  71.12000  17.79500  1.000 44.81103  ?  179  THR   A CA  1 
ATOM   1454  C  C   . THR   A 1 179  ? -42.97300  69.64100  18.15800  1.000 48.74048  ?  179  THR   A C   1 
ATOM   1455  O  O   . THR   A 1 179  ? -43.84800  69.19400  18.90400  1.000 54.80121  ?  179  THR   A O   1 
ATOM   1456  C  CB  . THR   A 1 179  ? -42.24100  71.92400  18.89600  1.000 41.98296  ?  179  THR   A CB  1 
ATOM   1457  O  OG1 . THR   A 1 179  ? -42.28900  73.31900  18.56900  1.000 41.69687  ?  179  THR   A OG1 1 
ATOM   1458  C  CG2 . THR   A 1 179  ? -40.79100  71.50400  19.04000  1.000 48.09262  ?  179  THR   A CG2 1 
ATOM   1459  N  N   . THR   A 1 180  ? -42.01700  68.88400  17.62100  1.000 59.80086  ?  180  THR   A N   1 
ATOM   1460  C  CA  . THR   A 1 180  ? -41.97500  67.44900  17.85000  1.000 52.65853  ?  180  THR   A CA  1 
ATOM   1461  C  C   . THR   A 1 180  ? -41.63400  67.14200  19.30800  1.000 41.32781  ?  180  THR   A C   1 
ATOM   1462  O  O   . THR   A 1 180  ? -41.26500  68.01900  20.09300  1.000 49.56873  ?  180  THR   A O   1 
ATOM   1463  C  CB  . THR   A 1 180  ? -40.95700  66.78500  16.92500  1.000 49.24873  ?  180  THR   A CB  1 
ATOM   1464  O  OG1 . THR   A 1 180  ? -39.63200  67.09900  17.37000  1.000 57.79681  ?  180  THR   A OG1 1 
ATOM   1465  C  CG2 . THR   A 1 180  ? -41.13700  67.28000  15.49900  1.000 50.47775  ?  180  THR   A CG2 1 
ATOM   1466  N  N   . VAL   A 1 181  ? -41.76000  65.86200  19.66200  1.000 38.95234  ?  181  VAL   A N   1 
ATOM   1467  C  CA  . VAL   A 1 181  ? -41.49900  65.43700  21.03400  1.000 47.00890  ?  181  VAL   A CA  1 
ATOM   1468  C  C   . VAL   A 1 181  ? -40.01700  65.57300  21.36400  1.000 53.67137  ?  181  VAL   A C   1 
ATOM   1469  O  O   . VAL   A 1 181  ? -39.64600  66.07700  22.43200  1.000 50.55194  ?  181  VAL   A O   1 
ATOM   1470  C  CB  . VAL   A 1 181  ? -41.99800  63.99700  21.25000  1.000 44.82653  ?  181  VAL   A CB  1 
ATOM   1471  C  CG1 . VAL   A 1 181  ? -41.58900  63.48600  22.62100  1.000 47.03912  ?  181  VAL   A CG1 1 
ATOM   1472  C  CG2 . VAL   A 1 181  ? -43.50700  63.93700  21.08700  1.000 48.14138  ?  181  VAL   A CG2 1 
ATOM   1473  N  N   . ARG   A 1 182  ? -39.14700  65.13000  20.45300  1.000 53.45871  ?  182  ARG   A N   1 
ATOM   1474  C  CA  . ARG   A 1 182  ? -37.71100  65.22900  20.69600  1.000 55.54901  ?  182  ARG   A CA  1 
ATOM   1475  C  C   . ARG   A 1 182  ? -37.26200  66.68200  20.77900  1.000 54.35154  ?  182  ARG   A C   1 
ATOM   1476  O  O   . ARG   A 1 182  ? -36.47500  67.04700  21.66100  1.000 72.31399  ?  182  ARG   A O   1 
ATOM   1477  C  CB  . ARG   A 1 182  ? -36.93600  64.48900  19.60500  1.000 51.50547  ?  182  ARG   A CB  1 
ATOM   1478  C  CG  . ARG   A 1 182  ? -37.45500  64.73000  18.19700  1.000 69.24841  ?  182  ARG   A CG  1 
ATOM   1479  C  CD  . ARG   A 1 182  ? -36.48400  64.20900  17.14900  1.000 85.41763  ?  182  ARG   A CD  1 
ATOM   1480  N  NE  . ARG   A 1 182  ? -37.16900  63.77700  15.93600  1.000 98.37104  ?  182  ARG   A NE  1 
ATOM   1481  C  CZ  . ARG   A 1 182  ? -37.50100  64.57600  14.93200  1.000 83.60787  ?  182  ARG   A CZ  1 
ATOM   1482  N  NH1 . ARG   A 1 182  ? -37.23100  65.87100  14.95900  1.000 80.82126  ?  182  ARG   A NH1 1 
ATOM   1483  N  NH2 . ARG   A 1 182  ? -38.12300  64.06300  13.87300  1.000 56.96394  ?  182  ARG   A NH2 1 
ATOM   1484  N  N   . GLU   A 1 183  ? -37.75500  67.52900  19.87200  1.000 37.33996  ?  183  GLU   A N   1 
ATOM   1485  C  CA  . GLU   A 1 183  ? -37.37700  68.93800  19.90200  1.000 51.53792  ?  183  GLU   A CA  1 
ATOM   1486  C  C   . GLU   A 1 183  ? -37.95600  69.64800  21.11900  1.000 53.46011  ?  183  GLU   A C   1 
ATOM   1487  O  O   . GLU   A 1 183  ? -37.39600  70.65100  21.57600  1.000 48.19328  ?  183  GLU   A O   1 
ATOM   1488  C  CB  . GLU   A 1 183  ? -37.82400  69.62900  18.61500  1.000 54.03061  ?  183  GLU   A CB  1 
ATOM   1489  C  CG  . GLU   A 1 183  ? -37.11800  69.13800  17.36300  1.000 62.10761  ?  183  GLU   A CG  1 
ATOM   1490  C  CD  . GLU   A 1 183  ? -37.70400  69.73200  16.09700  1.000 70.04762  ?  183  GLU   A CD  1 
ATOM   1491  O  OE1 . GLU   A 1 183  ? -38.83700  70.25600  16.15400  1.000 82.42277  ?  183  GLU   A OE1 1 
ATOM   1492  O  OE2 . GLU   A 1 183  ? -37.03200  69.67700  15.04600  1.000 81.46860  -1 183  GLU   A OE2 1 
ATOM   1493  N  N   . LEU   A 1 184  ? -39.07000  69.14600  21.65500  1.000 52.01952  ?  184  LEU   A N   1 
ATOM   1494  C  CA  . LEU   A 1 184  ? -39.63000  69.72600  22.87100  1.000 51.40546  ?  184  LEU   A CA  1 
ATOM   1495  C  C   . LEU   A 1 184  ? -38.78100  69.36700  24.08300  1.000 55.05667  ?  184  LEU   A C   1 
ATOM   1496  O  O   . LEU   A 1 184  ? -38.44700  70.23300  24.90100  1.000 48.25247  ?  184  LEU   A O   1 
ATOM   1497  C  CB  . LEU   A 1 184  ? -41.06900  69.24900  23.06400  1.000 46.45242  ?  184  LEU   A CB  1 
ATOM   1498  C  CG  . LEU   A 1 184  ? -41.98900  70.18900  23.84400  1.000 42.29571  ?  184  LEU   A CG  1 
ATOM   1499  C  CD1 . LEU   A 1 184  ? -42.59300  71.22300  22.90900  1.000 39.72318  ?  184  LEU   A CD1 1 
ATOM   1500  C  CD2 . LEU   A 1 184  ? -43.07200  69.41100  24.57100  1.000 59.51648  ?  184  LEU   A CD2 1 
ATOM   1501  N  N   . LEU   A 1 185  ? -38.41800  68.08800  24.21200  1.000 48.40871  ?  185  LEU   A N   1 
ATOM   1502  C  CA  . LEU   A 1 185  ? -37.59800  67.65700  25.33800  1.000 50.83608  ?  185  LEU   A CA  1 
ATOM   1503  C  C   . LEU   A 1 185  ? -36.19400  68.24200  25.27100  1.000 66.11237  ?  185  LEU   A C   1 
ATOM   1504  O  O   . LEU   A 1 185  ? -35.53600  68.38900  26.30700  1.000 71.64826  ?  185  LEU   A O   1 
ATOM   1505  C  CB  . LEU   A 1 185  ? -37.54200  66.13100  25.38800  1.000 42.47617  ?  185  LEU   A CB  1 
ATOM   1506  C  CG  . LEU   A 1 185  ? -38.89100  65.44900  25.61400  1.000 45.91498  ?  185  LEU   A CG  1 
ATOM   1507  C  CD1 . LEU   A 1 185  ? -38.71200  63.95300  25.81500  1.000 52.98762  ?  185  LEU   A CD1 1 
ATOM   1508  C  CD2 . LEU   A 1 185  ? -39.60400  66.07500  26.80000  1.000 57.74640  ?  185  LEU   A CD2 1 
ATOM   1509  N  N   . ALA   A 1 186  ? -35.71900  68.57700  24.07000  1.000 56.50722  ?  186  ALA   A N   1 
ATOM   1510  C  CA  . ALA   A 1 186  ? -34.43900  69.26600  23.95000  1.000 54.05057  ?  186  ALA   A CA  1 
ATOM   1511  C  C   . ALA   A 1 186  ? -34.53500  70.68700  24.48800  1.000 54.83681  ?  186  ALA   A C   1 
ATOM   1512  O  O   . ALA   A 1 186  ? -33.74200  71.09200  25.34600  1.000 68.16893  ?  186  ALA   A O   1 
ATOM   1513  C  CB  . ALA   A 1 186  ? -33.97600  69.26700  22.49300  1.000 48.24447  ?  186  ALA   A CB  1 
ATOM   1514  N  N   . LEU   A 1 187  ? -35.51700  71.45600  24.00400  1.000 47.56967  ?  187  LEU   A N   1 
ATOM   1515  C  CA  . LEU   A 1 187  ? -35.73300  72.80900  24.51000  1.000 50.69059  ?  187  LEU   A CA  1 
ATOM   1516  C  C   . LEU   A 1 187  ? -35.89700  72.82400  26.02300  1.000 55.28824  ?  187  LEU   A C   1 
ATOM   1517  O  O   . LEU   A 1 187  ? -35.53800  73.80900  26.67900  1.000 62.43809  ?  187  LEU   A O   1 
ATOM   1518  C  CB  . LEU   A 1 187  ? -36.96200  73.42800  23.84300  1.000 48.56087  ?  187  LEU   A CB  1 
ATOM   1519  C  CG  . LEU   A 1 187  ? -37.32700  74.85200  24.27300  1.000 48.19086  ?  187  LEU   A CG  1 
ATOM   1520  C  CD1 . LEU   A 1 187  ? -36.31400  75.85500  23.73900  1.000 56.86508  ?  187  LEU   A CD1 1 
ATOM   1521  C  CD2 . LEU   A 1 187  ? -38.73500  75.21300  23.83000  1.000 46.51037  ?  187  LEU   A CD2 1 
ATOM   1522  N  N   . LYS   A 1 188  ? -36.43600  71.74500  26.59300  1.000 50.81670  ?  188  LYS   A N   1 
ATOM   1523  C  CA  . LYS   A 1 188  ? -36.52700  71.63600  28.04400  1.000 53.53744  ?  188  LYS   A CA  1 
ATOM   1524  C  C   . LYS   A 1 188  ? -35.14300  71.70700  28.67900  1.000 64.84818  ?  188  LYS   A C   1 
ATOM   1525  O  O   . LYS   A 1 188  ? -34.85600  72.61100  29.47000  1.000 75.88937  ?  188  LYS   A O   1 
ATOM   1526  C  CB  . LYS   A 1 188  ? -37.24200  70.33700  28.42000  1.000 46.74729  ?  188  LYS   A CB  1 
ATOM   1527  C  CG  . LYS   A 1 188  ? -37.34400  70.08200  29.91100  1.000 55.31705  ?  188  LYS   A CG  1 
ATOM   1528  C  CD  . LYS   A 1 188  ? -38.23700  68.88400  30.18700  1.000 57.47624  ?  188  LYS   A CD  1 
ATOM   1529  C  CE  . LYS   A 1 188  ? -37.93000  68.26000  31.54000  1.000 58.13456  ?  188  LYS   A CE  1 
ATOM   1530  N  NZ  . LYS   A 1 188  ? -39.13300  68.15500  32.41300  1.000 56.38742  ?  188  LYS   A NZ  1 
ATOM   1531  N  N   . ARG   A 1 189  ? -34.26000  70.77200  28.31700  1.000 66.40476  ?  189  ARG   A N   1 
ATOM   1532  C  CA  . ARG   A 1 189  ? -32.91400  70.75300  28.88400  1.000 65.52513  ?  189  ARG   A CA  1 
ATOM   1533  C  C   . ARG   A 1 189  ? -32.18700  72.06900  28.63200  1.000 56.95926  ?  189  ARG   A C   1 
ATOM   1534  O  O   . ARG   A 1 189  ? -31.55300  72.62600  29.53500  1.000 65.47292  ?  189  ARG   A O   1 
ATOM   1535  C  CB  . ARG   A 1 189  ? -32.12000  69.58700  28.29700  1.000 50.88285  ?  189  ARG   A CB  1 
ATOM   1536  C  CG  . ARG   A 1 189  ? -32.86300  68.26600  28.30600  1.000 73.68284  ?  189  ARG   A CG  1 
ATOM   1537  C  CD  . ARG   A 1 189  ? -32.36400  67.36800  27.19000  1.000 86.37259  ?  189  ARG   A CD  1 
ATOM   1538  N  NE  . ARG   A 1 189  ? -33.20100  66.18700  27.01700  1.000 100.05444 ?  189  ARG   A NE  1 
ATOM   1539  C  CZ  . ARG   A 1 189  ? -33.20900  65.43300  25.92700  1.000 90.01857  ?  189  ARG   A CZ  1 
ATOM   1540  N  NH1 . ARG   A 1 189  ? -32.44900  65.72100  24.88300  1.000 80.82178  ?  189  ARG   A NH1 1 
ATOM   1541  N  NH2 . ARG   A 1 189  ? -34.00500  64.36900  25.88100  1.000 88.81964  ?  189  ARG   A NH2 1 
ATOM   1542  N  N   . LEU   A 1 190  ? -32.27400  72.58600  27.40500  1.000 45.62310  ?  190  LEU   A N   1 
ATOM   1543  C  CA  . LEU   A 1 190  ? -31.57000  73.81200  27.05300  1.000 47.95164  ?  190  LEU   A CA  1 
ATOM   1544  C  C   . LEU   A 1 190  ? -32.13100  75.04900  27.74300  1.000 61.68541  ?  190  LEU   A C   1 
ATOM   1545  O  O   . LEU   A 1 190  ? -31.46500  76.09000  27.73200  1.000 68.98989  ?  190  LEU   A O   1 
ATOM   1546  C  CB  . LEU   A 1 190  ? -31.59900  74.02300  25.53800  1.000 40.17232  ?  190  LEU   A CB  1 
ATOM   1547  C  CG  . LEU   A 1 190  ? -30.53500  73.32100  24.69100  1.000 50.15803  ?  190  LEU   A CG  1 
ATOM   1548  C  CD1 . LEU   A 1 190  ? -30.92700  71.89200  24.35300  1.000 46.23885  ?  190  LEU   A CD1 1 
ATOM   1549  C  CD2 . LEU   A 1 190  ? -30.27000  74.11900  23.42800  1.000 53.76065  ?  190  LEU   A CD2 1 
ATOM   1550  N  N   . CYS   A 1 191  ? -33.32600  74.97300  28.34100  1.000 74.29670  ?  191  CYS   A N   1 
ATOM   1551  C  CA  . CYS   A 1 191  ? -33.93300  76.16900  28.91500  1.000 88.77685  ?  191  CYS   A CA  1 
ATOM   1552  C  C   . CYS   A 1 191  ? -34.64500  75.91500  30.24200  1.000 88.90525  ?  191  CYS   A C   1 
ATOM   1553  O  O   . CYS   A 1 191  ? -35.46700  76.74200  30.65600  1.000 82.88555  ?  191  CYS   A O   1 
ATOM   1554  C  CB  . CYS   A 1 191  ? -34.92100  76.80400  27.92400  1.000 72.52411  ?  191  CYS   A CB  1 
ATOM   1555  S  SG  . CYS   A 1 191  ? -34.15400  77.57500  26.47400  1.000 100.27821 ?  191  CYS   A SG  1 
ATOM   1556  N  N   . ALA   A 1 192  ? -34.36000  74.80900  30.92500  1.000 83.84566  ?  192  ALA   A N   1 
ATOM   1557  C  CA  . ALA   A 1 192  ? -34.93200  74.55700  32.24000  1.000 92.69720  ?  192  ALA   A CA  1 
ATOM   1558  C  C   . ALA   A 1 192  ? -33.90600  74.85100  33.32500  1.000 111.09032 ?  192  ALA   A C   1 
ATOM   1559  O  O   . ALA   A 1 192  ? -32.69600  74.73900  33.11100  1.000 100.03914 ?  192  ALA   A O   1 
ATOM   1560  C  CB  . ALA   A 1 192  ? -35.42400  73.11500  32.38000  1.000 89.13827  ?  192  ALA   A CB  1 
ATOM   1561  N  N   . GLU   A 1 193  ? -34.40700  75.22000  34.49600  1.000 126.31945 ?  193  GLU   A N   1 
ATOM   1562  C  CA  . GLU   A 1 193  ? -33.56600  75.60100  35.62200  1.000 119.85434 ?  193  GLU   A CA  1 
ATOM   1563  C  C   . GLU   A 1 193  ? -32.64200  74.45800  36.02600  1.000 117.23196 ?  193  GLU   A C   1 
ATOM   1564  O  O   . GLU   A 1 193  ? -33.12900  73.40300  36.45500  1.000 104.06611 ?  193  GLU   A O   1 
ATOM   1565  C  CB  . GLU   A 1 193  ? -34.42800  76.00500  36.81800  1.000 117.53617 ?  193  GLU   A CB  1 
ATOM   1566  C  CG  . GLU   A 1 193  ? -35.19000  77.31300  36.66700  1.000 113.96111 ?  193  GLU   A CG  1 
ATOM   1567  C  CD  . GLU   A 1 193  ? -36.36800  77.21500  35.71600  1.000 110.14633 ?  193  GLU   A CD  1 
ATOM   1568  O  OE1 . GLU   A 1 193  ? -36.84000  76.08800  35.45800  1.000 112.50453 ?  193  GLU   A OE1 1 
ATOM   1569  O  OE2 . GLU   A 1 193  ? -36.82000  78.27000  35.22500  1.000 104.29316 -1 193  GLU   A OE2 1 
ATOM   1570  N  N   . PRO   A 1 194  ? -31.32600  74.61600  35.91900  1.000 120.23422 ?  194  PRO   A N   1 
ATOM   1571  C  CA  . PRO   A 1 194  ? -30.42300  73.63600  36.53000  1.000 121.31089 ?  194  PRO   A CA  1 
ATOM   1572  C  C   . PRO   A 1 194  ? -30.47800  73.73600  38.04800  1.000 133.81644 ?  194  PRO   A C   1 
ATOM   1573  O  O   . PRO   A 1 194  ? -30.96500  74.71600  38.61600  1.000 125.24113 ?  194  PRO   A O   1 
ATOM   1574  C  CB  . PRO   A 1 194  ? -29.04400  74.02200  35.98700  1.000 107.13872 ?  194  PRO   A CB  1 
ATOM   1575  C  CG  . PRO   A 1 194  ? -29.16100  75.47200  35.66600  1.000 111.53552 ?  194  PRO   A CG  1 
ATOM   1576  C  CD  . PRO   A 1 194  ? -30.58800  75.69100  35.23000  1.000 121.47598 ?  194  PRO   A CD  1 
ATOM   1577  N  N   . LYS   A 1 195  ? -29.96300  72.69500  38.70200  1.000 130.31976 ?  195  LYS   A N   1 
ATOM   1578  C  CA  . LYS   A 1 195  ? -30.04600  72.55400  40.15800  1.000 118.11357 ?  195  LYS   A CA  1 
ATOM   1579  C  C   . LYS   A 1 195  ? -29.59900  73.80100  40.92200  1.000 125.23876 ?  195  LYS   A C   1 
ATOM   1580  O  O   . LYS   A 1 195  ? -28.49600  74.30700  40.71900  1.000 127.99269 ?  195  LYS   A O   1 
ATOM   1581  C  CB  . LYS   A 1 195  ? -29.21500  71.35300  40.61800  1.000 91.59310  ?  195  LYS   A CB  1 
ATOM   1582  N  N   . GLU   A 1 198  ? -26.17400  74.84800  42.42400  1.000 108.31799 ?  198  GLU   A N   1 
ATOM   1583  C  CA  . GLU   A 1 198  ? -24.79700  75.28400  42.62600  1.000 105.08335 ?  198  GLU   A CA  1 
ATOM   1584  C  C   . GLU   A 1 198  ? -24.67000  76.13700  43.88400  1.000 106.63394 ?  198  GLU   A C   1 
ATOM   1585  O  O   . GLU   A 1 198  ? -25.67000  76.58600  44.44700  1.000 95.90947  ?  198  GLU   A O   1 
ATOM   1586  C  CB  . GLU   A 1 198  ? -24.29800  76.06300  41.40700  1.000 70.08315  ?  198  GLU   A CB  1 
ATOM   1587  N  N   . LYS   A 1 199  ? -23.43300  76.35800  44.32100  1.000 94.03044  ?  199  LYS   A N   1 
ATOM   1588  C  CA  . LYS   A 1 199  ? -23.19200  77.15500  45.51600  1.000 93.58427  ?  199  LYS   A CA  1 
ATOM   1589  C  C   . LYS   A 1 199  ? -23.30300  78.64400  45.18900  1.000 91.53896  ?  199  LYS   A C   1 
ATOM   1590  O  O   . LYS   A 1 199  ? -22.89500  79.07500  44.10700  1.000 93.73075  ?  199  LYS   A O   1 
ATOM   1591  C  CB  . LYS   A 1 199  ? -21.81100  76.85200  46.09500  1.000 72.44179  ?  199  LYS   A CB  1 
ATOM   1592  N  N   . PRO   A 1 200  ? -23.85100  79.44500  46.09500  1.000 91.16131  ?  200  PRO   A N   1 
ATOM   1593  C  CA  . PRO   A 1 200  ? -23.95300  80.88800  45.86400  1.000 90.22614  ?  200  PRO   A CA  1 
ATOM   1594  C  C   . PRO   A 1 200  ? -22.60400  81.56600  46.08600  1.000 83.23759  ?  200  PRO   A C   1 
ATOM   1595  O  O   . PRO   A 1 200  ? -21.60200  80.92900  46.40500  1.000 80.41084  ?  200  PRO   A O   1 
ATOM   1596  C  CB  . PRO   A 1 200  ? -24.98600  81.33100  46.90200  1.000 84.99216  ?  200  PRO   A CB  1 
ATOM   1597  C  CG  . PRO   A 1 200  ? -24.81000  80.36200  48.02100  1.000 83.94085  ?  200  PRO   A CG  1 
ATOM   1598  C  CD  . PRO   A 1 200  ? -24.45800  79.04500  47.37700  1.000 92.47744  ?  200  PRO   A CD  1 
ATOM   1599  N  N   . ILE   A 1 201  ? -22.59600  82.88300  45.91300  1.000 73.97828  ?  201  ILE   A N   1 
ATOM   1600  C  CA  . ILE   A 1 201  ? -21.39100  83.69100  46.06600  1.000 70.49115  ?  201  ILE   A CA  1 
ATOM   1601  C  C   . ILE   A 1 201  ? -21.46100  84.38200  47.42200  1.000 63.36517  ?  201  ILE   A C   1 
ATOM   1602  O  O   . ILE   A 1 201  ? -22.32000  85.24000  47.65200  1.000 74.55911  ?  201  ILE   A O   1 
ATOM   1603  C  CB  . ILE   A 1 201  ? -21.23800  84.71100  44.93000  1.000 63.42948  ?  201  ILE   A CB  1 
ATOM   1604  C  CG1 . ILE   A 1 201  ? -20.99500  84.00400  43.59500  1.000 51.91127  ?  201  ILE   A CG1 1 
ATOM   1605  C  CG2 . ILE   A 1 201  ? -20.10400  85.68100  45.23300  1.000 63.61708  ?  201  ILE   A CG2 1 
ATOM   1606  C  CD1 . ILE   A 1 201  ? -22.25700  83.66500  42.84400  1.000 57.21154  ?  201  ILE   A CD1 1 
ATOM   1607  N  N   . ASP   A 1 202  ? -20.55200  84.00900  48.32100  1.000 64.44934  ?  202  ASP   A N   1 
ATOM   1608  C  CA  . ASP   A 1 202  ? -20.45400  84.61100  49.64400  1.000 61.73162  ?  202  ASP   A CA  1 
ATOM   1609  C  C   . ASP   A 1 202  ? -19.19400  85.45200  49.80600  1.000 71.27009  ?  202  ASP   A C   1 
ATOM   1610  O  O   . ASP   A 1 202  ? -18.83600  85.80800  50.93400  1.000 80.29964  ?  202  ASP   A O   1 
ATOM   1611  C  CB  . ASP   A 1 202  ? -20.50500  83.52300  50.71800  1.000 59.64008  ?  202  ASP   A CB  1 
ATOM   1612  C  CG  . ASP   A 1 202  ? -19.78700  82.25400  50.29400  1.000 90.92831  ?  202  ASP   A CG  1 
ATOM   1613  O  OD1 . ASP   A 1 202  ? -19.11800  82.27400  49.23800  1.000 80.90523  ?  202  ASP   A OD1 1 
ATOM   1614  O  OD2 . ASP   A 1 202  ? -19.89600  81.23600  51.01000  1.000 93.31367  -1 202  ASP   A OD2 1 
ATOM   1615  N  N   . LYS   A 1 203  ? -18.52000  85.78200  48.70800  1.000 64.31527  ?  203  LYS   A N   1 
ATOM   1616  C  CA  . LYS   A 1 203  ? -17.25400  86.49500  48.73500  1.000 54.83206  ?  203  LYS   A CA  1 
ATOM   1617  C  C   . LYS   A 1 203  ? -17.35700  87.77900  47.92200  1.000 50.59927  ?  203  LYS   A C   1 
ATOM   1618  O  O   . LYS   A 1 203  ? -18.17800  87.90100  47.01000  1.000 62.55513  ?  203  LYS   A O   1 
ATOM   1619  C  CB  . LYS   A 1 203  ? -16.11700  85.62300  48.17500  1.000 52.35889  ?  203  LYS   A CB  1 
ATOM   1620  C  CG  . LYS   A 1 203  ? -15.89100  84.30900  48.91600  1.000 67.74968  ?  203  LYS   A CG  1 
ATOM   1621  C  CD  . LYS   A 1 203  ? -14.96800  84.50100  50.11100  1.000 70.77611  ?  203  LYS   A CD  1 
ATOM   1622  C  CE  . LYS   A 1 203  ? -15.01500  83.31000  51.06300  1.000 87.11608  ?  203  LYS   A CE  1 
ATOM   1623  N  NZ  . LYS   A 1 203  ? -14.06700  82.21900  50.69600  1.000 86.66652  ?  203  LYS   A NZ  1 
ATOM   1624  N  N   . THR   A 1 204  ? -16.51200  88.74200  48.26900  1.000 39.19121  ?  204  THR   A N   1 
ATOM   1625  C  CA  . THR   A 1 204  ? -16.29700  89.93200  47.46200  1.000 50.86116  ?  204  THR   A CA  1 
ATOM   1626  C  C   . THR   A 1 204  ? -14.93700  89.82600  46.78300  1.000 49.62392  ?  204  THR   A C   1 
ATOM   1627  O  O   . THR   A 1 204  ? -14.12700  88.95400  47.10500  1.000 55.55206  ?  204  THR   A O   1 
ATOM   1628  C  CB  . THR   A 1 204  ? -16.37500  91.20200  48.31500  1.000 48.39904  ?  204  THR   A CB  1 
ATOM   1629  O  OG1 . THR   A 1 204  ? -15.19100  91.31000  49.11200  1.000 52.70412  ?  204  THR   A OG1 1 
ATOM   1630  C  CG2 . THR   A 1 204  ? -17.58400  91.14900  49.23200  1.000 49.26531  ?  204  THR   A CG2 1 
ATOM   1631  N  N   . PHE   A 1 205  ? -14.68300  90.72600  45.83200  1.000 37.28461  ?  205  PHE   A N   1 
ATOM   1632  C  CA  . PHE   A 1 205  ? -13.44300  90.62500  45.06800  1.000 41.56744  ?  205  PHE   A CA  1 
ATOM   1633  C  C   . PHE   A 1 205  ? -12.22400  90.87400  45.94800  1.000 51.94054  ?  205  PHE   A C   1 
ATOM   1634  O  O   . PHE   A 1 205  ? -11.23600  90.13500  45.86500  1.000 54.51740  ?  205  PHE   A O   1 
ATOM   1635  C  CB  . PHE   A 1 205  ? -13.45500  91.59300  43.88700  1.000 38.61133  ?  205  PHE   A CB  1 
ATOM   1636  C  CG  . PHE   A 1 205  ? -12.24800  91.47100  42.99600  1.000 43.44280  ?  205  PHE   A CG  1 
ATOM   1637  C  CD1 . PHE   A 1 205  ? -12.21800  90.53700  41.97400  1.000 41.74289  ?  205  PHE   A CD1 1 
ATOM   1638  C  CD2 . PHE   A 1 205  ? -11.14200  92.28500  43.18200  1.000 46.32135  ?  205  PHE   A CD2 1 
ATOM   1639  C  CE1 . PHE   A 1 205  ? -11.11100  90.42000  41.15500  1.000 35.92363  ?  205  PHE   A CE1 1 
ATOM   1640  C  CE2 . PHE   A 1 205  ? -10.03300  92.17200  42.36600  1.000 41.25445  ?  205  PHE   A CE2 1 
ATOM   1641  C  CZ  . PHE   A 1 205  ? -10.01800  91.23900  41.35200  1.000 37.85974  ?  205  PHE   A CZ  1 
ATOM   1642  N  N   . HIS   A 1 206  ? -12.26700  91.91000  46.79100  1.000 49.12544  ?  206  HIS   A N   1 
ATOM   1643  C  CA  . HIS   A 1 206  ? -11.11100  92.20900  47.63100  1.000 48.47217  ?  206  HIS   A CA  1 
ATOM   1644  C  C   . HIS   A 1 206  ? -10.81100  91.06000  48.58500  1.000 50.28063  ?  206  HIS   A C   1 
ATOM   1645  O  O   . HIS   A 1 206  ? -9.64300   90.75800  48.85200  1.000 58.51766  ?  206  HIS   A O   1 
ATOM   1646  C  CB  . HIS   A 1 206  ? -11.32200  93.51900  48.39400  1.000 46.62760  ?  206  HIS   A CB  1 
ATOM   1647  C  CG  . HIS   A 1 206  ? -12.71500  93.71200  48.90900  1.000 56.24080  ?  206  HIS   A CG  1 
ATOM   1648  N  ND1 . HIS   A 1 206  ? -13.70400  94.32000  48.16600  1.000 62.02421  ?  206  HIS   A ND1 1 
ATOM   1649  C  CD2 . HIS   A 1 206  ? -13.27900  93.39600  50.09800  1.000 71.80566  ?  206  HIS   A CD2 1 
ATOM   1650  C  CE1 . HIS   A 1 206  ? -14.82000  94.36000  48.87100  1.000 65.11974  ?  206  HIS   A CE1 1 
ATOM   1651  N  NE2 . HIS   A 1 206  ? -14.59000  93.80500  50.04700  1.000 66.36598  ?  206  HIS   A NE2 1 
ATOM   1652  N  N   . GLN   A 1 207  ? -11.85000  90.39400  49.09600  1.000 48.20422  ?  207  GLN   A N   1 
ATOM   1653  C  CA  . GLN   A 1 207  ? -11.63100  89.20500  49.91600  1.000 49.39121  ?  207  GLN   A CA  1 
ATOM   1654  C  C   . GLN   A 1 207  ? -10.86800  88.14200  49.13600  1.000 50.79933  ?  207  GLN   A C   1 
ATOM   1655  O  O   . GLN   A 1 207  ? -9.91400   87.54300  49.64500  1.000 61.63731  ?  207  GLN   A O   1 
ATOM   1656  C  CB  . GLN   A 1 207  ? -12.96600  88.64600  50.40800  1.000 41.29632  ?  207  GLN   A CB  1 
ATOM   1657  C  CG  . GLN   A 1 207  ? -13.73900  89.56100  51.33800  1.000 60.82616  ?  207  GLN   A CG  1 
ATOM   1658  C  CD  . GLN   A 1 207  ? -15.04000  88.93900  51.80700  1.000 72.30707  ?  207  GLN   A CD  1 
ATOM   1659  O  OE1 . GLN   A 1 207  ? -15.26200  87.73800  51.64100  1.000 56.33469  ?  207  GLN   A OE1 1 
ATOM   1660  N  NE2 . GLN   A 1 207  ? -15.91000  89.75400  52.39300  1.000 75.76923  ?  207  GLN   A NE2 1 
ATOM   1661  N  N   . LEU   A 1 208  ? -11.27600  87.90000  47.88900  1.000 43.30586  ?  208  LEU   A N   1 
ATOM   1662  C  CA  . LEU   A 1 208  ? -10.61000  86.88900  47.07600  1.000 49.11649  ?  208  LEU   A CA  1 
ATOM   1663  C  C   . LEU   A 1 208  ? -9.23500   87.36100  46.62400  1.000 48.81602  ?  208  LEU   A C   1 
ATOM   1664  O  O   . LEU   A 1 208  ? -8.29200   86.56400  46.55200  1.000 45.53381  ?  208  LEU   A O   1 
ATOM   1665  C  CB  . LEU   A 1 208  ? -11.48300  86.53100  45.87600  1.000 42.19283  ?  208  LEU   A CB  1 
ATOM   1666  C  CG  . LEU   A 1 208  ? -12.81200  85.86000  46.22400  1.000 41.91002  ?  208  LEU   A CG  1 
ATOM   1667  C  CD1 . LEU   A 1 208  ? -13.72500  85.83800  45.01600  1.000 40.96094  ?  208  LEU   A CD1 1 
ATOM   1668  C  CD2 . LEU   A 1 208  ? -12.57000  84.45100  46.73700  1.000 49.08007  ?  208  LEU   A CD2 1 
ATOM   1669  N  N   . PHE   A 1 209  ? -9.10000   88.65300  46.31200  1.000 48.83678  ?  209  PHE   A N   1 
ATOM   1670  C  CA  . PHE   A 1 209  ? -7.79000   89.18700  45.95600  1.000 42.54464  ?  209  PHE   A CA  1 
ATOM   1671  C  C   . PHE   A 1 209  ? -6.83100   89.10800  47.13500  1.000 51.71963  ?  209  PHE   A C   1 
ATOM   1672  O  O   . PHE   A 1 209  ? -5.66000   88.74900  46.96900  1.000 55.18561  ?  209  PHE   A O   1 
ATOM   1673  C  CB  . PHE   A 1 209  ? -7.92100   90.62800  45.46700  1.000 35.85869  ?  209  PHE   A CB  1 
ATOM   1674  C  CG  . PHE   A 1 209  ? -6.60600   91.28700  45.16700  1.000 38.80379  ?  209  PHE   A CG  1 
ATOM   1675  C  CD1 . PHE   A 1 209  ? -5.89300   90.95500  44.02600  1.000 39.61117  ?  209  PHE   A CD1 1 
ATOM   1676  C  CD2 . PHE   A 1 209  ? -6.08500   92.24500  46.02100  1.000 39.69725  ?  209  PHE   A CD2 1 
ATOM   1677  C  CE1 . PHE   A 1 209  ? -4.68300   91.56300  43.74500  1.000 39.10137  ?  209  PHE   A CE1 1 
ATOM   1678  C  CE2 . PHE   A 1 209  ? -4.87700   92.85700  45.74700  1.000 39.75596  ?  209  PHE   A CE2 1 
ATOM   1679  C  CZ  . PHE   A 1 209  ? -4.17400   92.51500  44.60700  1.000 39.54127  ?  209  PHE   A CZ  1 
ATOM   1680  N  N   . GLU   A 1 210  ? -7.31300   89.43100  48.33700  1.000 54.96179  ?  210  GLU   A N   1 
ATOM   1681  C  CA  . GLU   A 1 210  ? -6.48000   89.31800  49.52700  1.000 49.06100  ?  210  GLU   A CA  1 
ATOM   1682  C  C   . GLU   A 1 210  ? -6.12200   87.87300  49.84600  1.000 49.46746  ?  210  GLU   A C   1 
ATOM   1683  O  O   . GLU   A 1 210  ? -5.11400   87.63400  50.52000  1.000 45.61046  ?  210  GLU   A O   1 
ATOM   1684  C  CB  . GLU   A 1 210  ? -7.18000   89.96600  50.72200  1.000 37.01654  ?  210  GLU   A CB  1 
ATOM   1685  C  CG  . GLU   A 1 210  ? -7.21900   91.48500  50.65600  1.000 35.57705  ?  210  GLU   A CG  1 
ATOM   1686  C  CD  . GLU   A 1 210  ? -8.20900   92.08100  51.63200  1.000 43.40907  ?  210  GLU   A CD  1 
ATOM   1687  O  OE1 . GLU   A 1 210  ? -8.76600   91.31500  52.44500  1.000 41.07370  ?  210  GLU   A OE1 1 
ATOM   1688  O  OE2 . GLU   A 1 210  ? -8.43500   93.30900  51.58300  1.000 45.76609  -1 210  GLU   A OE2 1 
ATOM   1689  N  N   . GLN   A 1 211  ? -6.91700   86.90600  49.38100  1.000 47.97030  ?  211  GLN   A N   1 
ATOM   1690  C  CA  . GLN   A 1 211  ? -6.54200   85.50500  49.53400  1.000 52.54058  ?  211  GLN   A CA  1 
ATOM   1691  C  C   . GLN   A 1 211  ? -5.46700   85.10400  48.53300  1.000 53.42335  ?  211  GLN   A C   1 
ATOM   1692  O  O   . GLN   A 1 211  ? -4.52200   84.39000  48.88700  1.000 65.07693  ?  211  GLN   A O   1 
ATOM   1693  C  CB  . GLN   A 1 211  ? -7.76700   84.60300  49.38000  1.000 62.46726  ?  211  GLN   A CB  1 
ATOM   1694  C  CG  . GLN   A 1 211  ? -8.65000   84.52900  50.61200  1.000 74.18820  ?  211  GLN   A CG  1 
ATOM   1695  C  CD  . GLN   A 1 211  ? -9.80000   83.55700  50.44100  1.000 88.61894  ?  211  GLN   A CD  1 
ATOM   1696  O  OE1 . GLN   A 1 211  ? -10.85400  83.70900  51.05900  1.000 103.35421 ?  211  GLN   A OE1 1 
ATOM   1697  N  NE2 . GLN   A 1 211  ? -9.60200   82.54700  49.60100  1.000 71.53706  ?  211  GLN   A NE2 1 
ATOM   1698  N  N   . GLN   A 1 212  ? -5.59400   85.54800  47.28000  1.000 56.22894  ?  212  GLN   A N   1 
ATOM   1699  C  CA  . GLN   A 1 212  ? -4.57700   85.23200  46.28400  1.000 55.30130  ?  212  GLN   A CA  1 
ATOM   1700  C  C   . GLN   A 1 212  ? -3.26500   85.94200  46.58800  1.000 51.57392  ?  212  GLN   A C   1 
ATOM   1701  O  O   . GLN   A 1 212  ? -2.19100   85.41700  46.27300  1.000 45.92890  ?  212  GLN   A O   1 
ATOM   1702  C  CB  . GLN   A 1 212  ? -5.07300   85.60000  44.88500  1.000 43.73873  ?  212  GLN   A CB  1 
ATOM   1703  C  CG  . GLN   A 1 212  ? -4.23400   85.02200  43.75500  1.000 30.69265  ?  212  GLN   A CG  1 
ATOM   1704  C  CD  . GLN   A 1 212  ? -4.38100   83.51800  43.63200  1.000 50.63685  ?  212  GLN   A CD  1 
ATOM   1705  O  OE1 . GLN   A 1 212  ? -5.45800   82.96600  43.86000  1.000 50.60248  ?  212  GLN   A OE1 1 
ATOM   1706  N  NE2 . GLN   A 1 212  ? -3.29400   82.84500  43.27200  1.000 51.16177  ?  212  GLN   A NE2 1 
ATOM   1707  N  N   . VAL   A 1 213  ? -3.33200   87.12900  47.19800  1.000 48.48397  ?  213  VAL   A N   1 
ATOM   1708  C  CA  . VAL   A 1 213  ? -2.11900   87.84000  47.59200  1.000 43.95106  ?  213  VAL   A CA  1 
ATOM   1709  C  C   . VAL   A 1 213  ? -1.31100   87.01300  48.58300  1.000 46.81451  ?  213  VAL   A C   1 
ATOM   1710  O  O   . VAL   A 1 213  ? -0.07600   87.03000  48.55500  1.000 49.77889  ?  213  VAL   A O   1 
ATOM   1711  C  CB  . VAL   A 1 213  ? -2.47800   89.23200  48.15500  1.000 40.04459  ?  213  VAL   A CB  1 
ATOM   1712  C  CG1 . VAL   A 1 213  ? -1.33000   89.80900  48.96900  1.000 42.30644  ?  213  VAL   A CG1 1 
ATOM   1713  C  CG2 . VAL   A 1 213  ? -2.83600   90.17800  47.02200  1.000 30.34194  ?  213  VAL   A CG2 1 
ATOM   1714  N  N   . GLU   A 1 214  ? -1.98200   86.26000  49.45400  1.000 50.71755  ?  214  GLU   A N   1 
ATOM   1715  C  CA  . GLU   A 1 214  ? -1.27600   85.35600  50.35200  1.000 47.85050  ?  214  GLU   A CA  1 
ATOM   1716  C  C   . GLU   A 1 214  ? -0.76600   84.11000  49.64100  1.000 52.54110  ?  214  GLU   A C   1 
ATOM   1717  O  O   . GLU   A 1 214  ? 0.20000    83.49700  50.10800  1.000 64.61002  ?  214  GLU   A O   1 
ATOM   1718  C  CB  . GLU   A 1 214  ? -2.18700   84.94900  51.51100  1.000 49.93457  ?  214  GLU   A CB  1 
ATOM   1719  C  CG  . GLU   A 1 214  ? -2.91000   86.11500  52.16600  1.000 67.24400  ?  214  GLU   A CG  1 
ATOM   1720  C  CD  . GLU   A 1 214  ? -2.13900   86.72000  53.32300  1.000 89.60047  ?  214  GLU   A CD  1 
ATOM   1721  O  OE1 . GLU   A 1 214  ? -2.19000   86.15000  54.43300  1.000 103.18522 ?  214  GLU   A OE1 1 
ATOM   1722  O  OE2 . GLU   A 1 214  ? -1.48300   87.76600  53.12400  1.000 90.84141  -1 214  GLU   A OE2 1 
ATOM   1723  N  N   . MET   A 1 215  ? -1.38800   83.72600  48.52300  1.000 45.07627  ?  215  MET   A N   1 
ATOM   1724  C  CA  . MET   A 1 215  ? -0.98100   82.51700  47.81400  1.000 48.52603  ?  215  MET   A CA  1 
ATOM   1725  C  C   . MET   A 1 215  ? 0.21600    82.77300  46.90600  1.000 60.70237  ?  215  MET   A C   1 
ATOM   1726  O  O   . MET   A 1 215  ? 1.13800    81.95200  46.84400  1.000 55.13771  ?  215  MET   A O   1 
ATOM   1727  C  CB  . MET   A 1 215  ? -2.15500   81.96600  47.00400  1.000 44.62045  ?  215  MET   A CB  1 
ATOM   1728  C  CG  . MET   A 1 215  ? -2.37200   80.47200  47.16400  1.000 48.55917  ?  215  MET   A CG  1 
ATOM   1729  S  SD  . MET   A 1 215  ? -2.95800   80.04600  48.81500  1.000 96.94163  ?  215  MET   A SD  1 
ATOM   1730  C  CE  . MET   A 1 215  ? -2.96500   78.25700  48.72600  1.000 73.06489  ?  215  MET   A CE  1 
ATOM   1731  N  N   . THR   A 1 216  ? 0.21700    83.89800  46.19300  1.000 57.73120  ?  216  THR   A N   1 
ATOM   1732  C  CA  . THR   A 1 216  ? 1.32900    84.30100  45.33200  1.000 39.52177  ?  216  THR   A CA  1 
ATOM   1733  C  C   . THR   A 1 216  ? 1.77500    85.70300  45.73100  1.000 42.80031  ?  216  THR   A C   1 
ATOM   1734  O  O   . THR   A 1 216  ? 1.56600    86.67100  44.99000  1.000 44.81714  ?  216  THR   A O   1 
ATOM   1735  C  CB  . THR   A 1 216  ? 0.93100    84.25000  43.85500  1.000 31.83431  ?  216  THR   A CB  1 
ATOM   1736  O  OG1 . THR   A 1 216  ? -0.23100   85.06100  43.63900  1.000 50.22325  ?  216  THR   A OG1 1 
ATOM   1737  C  CG2 . THR   A 1 216  ? 0.63000    82.82000  43.43200  1.000 31.67659  ?  216  THR   A CG2 1 
ATOM   1738  N  N   . PRO   A 1 217  ? 2.40200    85.84500  46.90400  1.000 39.22178  ?  217  PRO   A N   1 
ATOM   1739  C  CA  . PRO   A 1 217  ? 2.75200    87.19700  47.37200  1.000 33.95075  ?  217  PRO   A CA  1 
ATOM   1740  C  C   . PRO   A 1 217  ? 3.84400    87.85300  46.55300  1.000 45.61336  ?  217  PRO   A C   1 
ATOM   1741  O  O   . PRO   A 1 217  ? 3.73100    89.03700  46.21000  1.000 49.57232  ?  217  PRO   A O   1 
ATOM   1742  C  CB  . PRO   A 1 217  ? 3.19800    86.96300  48.82500  1.000 32.82726  ?  217  PRO   A CB  1 
ATOM   1743  C  CG  . PRO   A 1 217  ? 2.74700    85.56600  49.16800  1.000 46.12657  ?  217  PRO   A CG  1 
ATOM   1744  C  CD  . PRO   A 1 217  ? 2.77900    84.81400  47.88200  1.000 41.89677  ?  217  PRO   A CD  1 
ATOM   1745  N  N   . ASP   A 1 218  ? 4.90300    87.11800  46.23200  1.000 44.91968  ?  218  ASP   A N   1 
ATOM   1746  C  CA  . ASP   A 1 218  ? 6.04400    87.67000  45.51900  1.000 41.72923  ?  218  ASP   A CA  1 
ATOM   1747  C  C   . ASP   A 1 218  ? 5.93300    87.49900  44.00900  1.000 50.64655  ?  218  ASP   A C   1 
ATOM   1748  O  O   . ASP   A 1 218  ? 6.90500    87.76500  43.29400  1.000 51.90044  ?  218  ASP   A O   1 
ATOM   1749  C  CB  . ASP   A 1 218  ? 7.33400    87.03100  46.03700  1.000 47.95276  ?  218  ASP   A CB  1 
ATOM   1750  C  CG  . ASP   A 1 218  ? 7.41700    87.03500  47.55700  1.000 41.41222  ?  218  ASP   A CG  1 
ATOM   1751  O  OD1 . ASP   A 1 218  ? 6.80400    87.92100  48.19000  1.000 30.33785  ?  218  ASP   A OD1 1 
ATOM   1752  O  OD2 . ASP   A 1 218  ? 8.09200    86.14800  48.11900  1.000 46.82646  -1 218  ASP   A OD2 1 
ATOM   1753  N  N   . HIS   A 1 219  ? 4.77700    87.06300  43.51000  1.000 44.21304  ?  219  HIS   A N   1 
ATOM   1754  C  CA  . HIS   A 1 219  ? 4.54300    86.99400  42.07400  1.000 49.10809  ?  219  HIS   A CA  1 
ATOM   1755  C  C   . HIS   A 1 219  ? 4.27500    88.38300  41.51300  1.000 49.32543  ?  219  HIS   A C   1 
ATOM   1756  O  O   . HIS   A 1 219  ? 3.57300    89.19000  42.12800  1.000 41.27285  ?  219  HIS   A O   1 
ATOM   1757  C  CB  . HIS   A 1 219  ? 3.35700    86.08200  41.76200  1.000 38.56277  ?  219  HIS   A CB  1 
ATOM   1758  C  CG  . HIS   A 1 219  ? 3.71300    84.63300  41.66600  1.000 42.19330  ?  219  HIS   A CG  1 
ATOM   1759  N  ND1 . HIS   A 1 219  ? 4.05300    83.87400  42.76500  1.000 39.62315  ?  219  HIS   A ND1 1 
ATOM   1760  C  CD2 . HIS   A 1 219  ? 3.77700    83.80100  40.60000  1.000 40.59331  ?  219  HIS   A CD2 1 
ATOM   1761  C  CE1 . HIS   A 1 219  ? 4.31200    82.63700  42.38000  1.000 38.83131  ?  219  HIS   A CE1 1 
ATOM   1762  N  NE2 . HIS   A 1 219  ? 4.15200    82.56600  41.07100  1.000 43.60619  ?  219  HIS   A NE2 1 
ATOM   1763  N  N   . VAL   A 1 220  ? 4.83000    88.65300  40.33200  1.000 42.86803  ?  220  VAL   A N   1 
ATOM   1764  C  CA  . VAL   A 1 220  ? 4.61400    89.93700  39.67500  1.000 33.91858  ?  220  VAL   A CA  1 
ATOM   1765  C  C   . VAL   A 1 220  ? 3.14200    90.05800  39.30200  1.000 43.34575  ?  220  VAL   A C   1 
ATOM   1766  O  O   . VAL   A 1 220  ? 2.59600    89.21000  38.58700  1.000 43.22515  ?  220  VAL   A O   1 
ATOM   1767  C  CB  . VAL   A 1 220  ? 5.51400    90.08100  38.44300  1.000 23.56025  ?  220  VAL   A CB  1 
ATOM   1768  C  CG1 . VAL   A 1 220  ? 5.43100    91.49600  37.89400  1.000 30.52792  ?  220  VAL   A CG1 1 
ATOM   1769  C  CG2 . VAL   A 1 220  ? 6.94800    89.71900  38.79300  1.000 38.30871  ?  220  VAL   A CG2 1 
ATOM   1770  N  N   . ALA   A 1 221  ? 2.49200    91.11400  39.79000  1.000 46.10900  ?  221  ALA   A N   1 
ATOM   1771  C  CA  . ALA   A 1 221  ? 1.06600    91.32700  39.57500  1.000 34.26538  ?  221  ALA   A CA  1 
ATOM   1772  C  C   . ALA   A 1 221  ? 0.78200    92.30600  38.44400  1.000 37.65582  ?  221  ALA   A C   1 
ATOM   1773  O  O   . ALA   A 1 221  ? 0.00100    91.99800  37.53900  1.000 54.73297  ?  221  ALA   A O   1 
ATOM   1774  C  CB  . ALA   A 1 221  ? 0.40800    91.82000  40.86900  1.000 38.73082  ?  221  ALA   A CB  1 
ATOM   1775  N  N   . VAL   A 1 222  ? 1.39400    93.48800  38.48100  1.000 30.61481  ?  222  VAL   A N   1 
ATOM   1776  C  CA  . VAL   A 1 222  ? 1.20400    94.50200  37.45300  1.000 46.93973  ?  222  VAL   A CA  1 
ATOM   1777  C  C   . VAL   A 1 222  ? 2.56800    94.92000  36.92400  1.000 47.10147  ?  222  VAL   A C   1 
ATOM   1778  O  O   . VAL   A 1 222  ? 3.56100    94.94900  37.65900  1.000 44.93528  ?  222  VAL   A O   1 
ATOM   1779  C  CB  . VAL   A 1 222  ? 0.42500    95.72800  37.98300  1.000 42.42357  ?  222  VAL   A CB  1 
ATOM   1780  C  CG1 . VAL   A 1 222  ? -0.14600   96.54100  36.82900  1.000 40.13029  ?  222  VAL   A CG1 1 
ATOM   1781  C  CG2 . VAL   A 1 222  ? -0.68000   95.29200  38.93500  1.000 45.41304  ?  222  VAL   A CG2 1 
ATOM   1782  N  N   . VAL   A 1 223  ? 2.61200    95.23700  35.63100  1.000 35.89842  ?  223  VAL   A N   1 
ATOM   1783  C  CA  . VAL   A 1 223  ? 3.82700    95.68100  34.95500  1.000 38.58071  ?  223  VAL   A CA  1 
ATOM   1784  C  C   . VAL   A 1 223  ? 3.48300    96.93500  34.16400  1.000 47.82540  ?  223  VAL   A C   1 
ATOM   1785  O  O   . VAL   A 1 223  ? 2.72600    96.87200  33.18600  1.000 59.32009  ?  223  VAL   A O   1 
ATOM   1786  C  CB  . VAL   A 1 223  ? 4.41900    94.60300  34.03700  1.000 40.98662  ?  223  VAL   A CB  1 
ATOM   1787  C  CG1 . VAL   A 1 223  ? 5.64000    95.14600  33.30200  1.000 33.06125  ?  223  VAL   A CG1 1 
ATOM   1788  C  CG2 . VAL   A 1 223  ? 4.78400    93.36700  34.83800  1.000 42.90875  ?  223  VAL   A CG2 1 
ATOM   1789  N  N   . ASP   A 1 224  ? 4.04200    98.06600  34.58300  1.000 42.41367  ?  224  ASP   A N   1 
ATOM   1790  C  CA  . ASP   A 1 224  ? 3.85400    99.35700  33.93600  1.000 55.46424  ?  224  ASP   A CA  1 
ATOM   1791  C  C   . ASP   A 1 224  ? 5.22300    99.92600  33.59200  1.000 55.71700  ?  224  ASP   A C   1 
ATOM   1792  O  O   . ASP   A 1 224  ? 6.07600    100.05200 34.47500  1.000 54.21546  ?  224  ASP   A O   1 
ATOM   1793  C  CB  . ASP   A 1 224  ? 3.10300    100.32500 34.84800  1.000 62.64019  ?  224  ASP   A CB  1 
ATOM   1794  C  CG  . ASP   A 1 224  ? 2.55900    101.50500 34.10000  1.000 62.76149  ?  224  ASP   A CG  1 
ATOM   1795  O  OD1 . ASP   A 1 224  ? 2.20000    101.31100 32.91700  1.000 58.45355  ?  224  ASP   A OD1 1 
ATOM   1796  O  OD2 . ASP   A 1 224  ? 2.53600    102.61700 34.67600  1.000 54.90023  -1 224  ASP   A OD2 1 
ATOM   1797  N  N   . ARG   A 1 225  ? 5.42800    100.27100 32.32500  1.000 54.44807  ?  225  ARG   A N   1 
ATOM   1798  C  CA  . ARG   A 1 225  ? 6.74600    100.71100 31.80100  1.000 64.73509  ?  225  ARG   A CA  1 
ATOM   1799  C  C   . ARG   A 1 225  ? 7.75700    99.59900  32.10200  1.000 66.81562  ?  225  ARG   A C   1 
ATOM   1800  O  O   . ARG   A 1 225  ? 7.45800    98.41500  31.88300  1.000 70.96062  ?  225  ARG   A O   1 
ATOM   1801  C  CB  . ARG   A 1 225  ? 7.12800    102.07700 32.35200  1.000 73.37291  ?  225  ARG   A CB  1 
ATOM   1802  C  CG  . ARG   A 1 225  ? 6.18100    103.19300 31.96800  1.000 84.24873  ?  225  ARG   A CG  1 
ATOM   1803  C  CD  . ARG   A 1 225  ? 5.74800    103.09600 30.51900  1.000 76.05353  ?  225  ARG   A CD  1 
ATOM   1804  N  NE  . ARG   A 1 225  ? 4.55100    103.90300 30.31600  1.000 81.87985  ?  225  ARG   A NE  1 
ATOM   1805  C  CZ  . ARG   A 1 225  ? 3.31600    103.50800 30.62400  1.000 83.93832  ?  225  ARG   A CZ  1 
ATOM   1806  N  NH1 . ARG   A 1 225  ? 3.06000    102.29200 31.09800  1.000 67.17871  ?  225  ARG   A NH1 1 
ATOM   1807  N  NH2 . ARG   A 1 225  ? 2.30500    104.35700 30.46500  1.000 76.45626  ?  225  ARG   A NH2 1 
ATOM   1808  N  N   . GLY   A 1 226  ? 8.95600    99.93100  32.58600  1.000 48.71697  ?  226  GLY   A N   1 
ATOM   1809  C  CA  . GLY   A 1 226  ? 9.89000    98.92700  33.05500  1.000 51.76079  ?  226  GLY   A CA  1 
ATOM   1810  C  C   . GLY   A 1 226  ? 9.76200    98.57900  34.51800  1.000 52.06510  ?  226  GLY   A C   1 
ATOM   1811  O  O   . GLY   A 1 226  ? 10.42900   97.65700  34.99100  1.000 60.48599  ?  226  GLY   A O   1 
ATOM   1812  N  N   . GLN   A 1 227  ? 8.91900    99.29900  35.25200  1.000 67.55484  ?  227  GLN   A N   1 
ATOM   1813  C  CA  . GLN   A 1 227  ? 8.69300    99.02100  36.66000  1.000 57.69481  ?  227  GLN   A CA  1 
ATOM   1814  C  C   . GLN   A 1 227  ? 7.64300    97.92600  36.82200  1.000 53.56459  ?  227  GLN   A C   1 
ATOM   1815  O  O   . GLN   A 1 227  ? 6.86300    97.63600  35.91100  1.000 47.45268  ?  227  GLN   A O   1 
ATOM   1816  C  CB  . GLN   A 1 227  ? 8.25400    100.29000 37.38900  1.000 55.90523  ?  227  GLN   A CB  1 
ATOM   1817  C  CG  . GLN   A 1 227  ? 9.07600    101.52000 37.03700  1.000 58.16053  ?  227  GLN   A CG  1 
ATOM   1818  C  CD  . GLN   A 1 227  ? 8.21900    102.75800 36.86200  1.000 87.19911  ?  227  GLN   A CD  1 
ATOM   1819  O  OE1 . GLN   A 1 227  ? 6.99900    102.70800 37.02000  1.000 81.36295  ?  227  GLN   A OE1 1 
ATOM   1820  N  NE2 . GLN   A 1 227  ? 8.85300    103.87700 36.52900  1.000 88.61722  ?  227  GLN   A NE2 1 
ATOM   1821  N  N   . SER   A 1 228  ? 7.62700    97.31700  38.00500  1.000 39.77110  ?  228  SER   A N   1 
ATOM   1822  C  CA  . SER   A 1 228  ? 6.72100    96.21400  38.28500  1.000 31.23816  ?  228  SER   A CA  1 
ATOM   1823  C  C   . SER   A 1 228  ? 6.15800    96.35500  39.69100  1.000 39.17581  ?  228  SER   A C   1 
ATOM   1824  O  O   . SER   A 1 228  ? 6.62800    97.15800  40.50100  1.000 49.89073  ?  228  SER   A O   1 
ATOM   1825  C  CB  . SER   A 1 228  ? 7.42000    94.85800  38.12900  1.000 31.14250  ?  228  SER   A CB  1 
ATOM   1826  O  OG  . SER   A 1 228  ? 7.92900    94.69800  36.81900  1.000 37.28624  ?  228  SER   A OG  1 
ATOM   1827  N  N   . LEU   A 1 229  ? 5.13300    95.55200  39.96800  1.000 46.78567  ?  229  LEU   A N   1 
ATOM   1828  C  CA  . LEU   A 1 229  ? 4.50500    95.47500  41.27900  1.000 45.45109  ?  229  LEU   A CA  1 
ATOM   1829  C  C   . LEU   A 1 229  ? 4.10200    94.03300  41.53400  1.000 41.46113  ?  229  LEU   A C   1 
ATOM   1830  O  O   . LEU   A 1 229  ? 3.39400    93.43600  40.71800  1.000 46.71611  ?  229  LEU   A O   1 
ATOM   1831  C  CB  . LEU   A 1 229  ? 3.27000    96.38000  41.36900  1.000 50.21989  ?  229  LEU   A CB  1 
ATOM   1832  C  CG  . LEU   A 1 229  ? 3.44500    97.80900  41.87800  1.000 53.32556  ?  229  LEU   A CG  1 
ATOM   1833  C  CD1 . LEU   A 1 229  ? 2.09200    98.48300  42.02800  1.000 34.21132  ?  229  LEU   A CD1 1 
ATOM   1834  C  CD2 . LEU   A 1 229  ? 4.17900    97.80100  43.19600  1.000 53.86094  ?  229  LEU   A CD2 1 
ATOM   1835  N  N   . THR   A 1 230  ? 4.55100    93.47300  42.65200  1.000 32.45933  ?  230  THR   A N   1 
ATOM   1836  C  CA  . THR   A 1 230  ? 4.09000    92.14200  43.00500  1.000 44.39822  ?  230  THR   A CA  1 
ATOM   1837  C  C   . THR   A 1 230  ? 2.73800    92.22600  43.70800  1.000 44.34414  ?  230  THR   A C   1 
ATOM   1838  O  O   . THR   A 1 230  ? 2.23400    93.30700  44.02100  1.000 51.49307  ?  230  THR   A O   1 
ATOM   1839  C  CB  . THR   A 1 230  ? 5.10200    91.42100  43.89400  1.000 45.00538  ?  230  THR   A CB  1 
ATOM   1840  O  OG1 . THR   A 1 230  ? 5.21500    92.10600  45.14500  1.000 43.49998  ?  230  THR   A OG1 1 
ATOM   1841  C  CG2 . THR   A 1 230  ? 6.46400    91.35500  43.21500  1.000 47.02299  ?  230  THR   A CG2 1 
ATOM   1842  N  N   . TYR   A 1 231  ? 2.15000    91.05400  43.95600  1.000 46.48888  ?  231  TYR   A N   1 
ATOM   1843  C  CA  . TYR   A 1 231  ? 0.82400    91.00400  44.56500  1.000 40.68718  ?  231  TYR   A CA  1 
ATOM   1844  C  C   . TYR   A 1 231  ? 0.83200    91.62100  45.95700  1.000 45.04099  ?  231  TYR   A C   1 
ATOM   1845  O  O   . TYR   A 1 231  ? -0.04700   92.42100  46.30000  1.000 43.74577  ?  231  TYR   A O   1 
ATOM   1846  C  CB  . TYR   A 1 231  ? 0.32700    89.56100  44.61500  1.000 37.73073  ?  231  TYR   A CB  1 
ATOM   1847  C  CG  . TYR   A 1 231  ? -0.35500   89.11800  43.34300  1.000 40.72192  ?  231  TYR   A CG  1 
ATOM   1848  C  CD1 . TYR   A 1 231  ? -1.71400   89.33200  43.15500  1.000 49.50504  ?  231  TYR   A CD1 1 
ATOM   1849  C  CD2 . TYR   A 1 231  ? 0.35700    88.49200  42.32900  1.000 38.52973  ?  231  TYR   A CD2 1 
ATOM   1850  C  CE1 . TYR   A 1 231  ? -2.34500   88.93500  41.99700  1.000 41.42108  ?  231  TYR   A CE1 1 
ATOM   1851  C  CE2 . TYR   A 1 231  ? -0.26800   88.09100  41.16300  1.000 48.15699  ?  231  TYR   A CE2 1 
ATOM   1852  C  CZ  . TYR   A 1 231  ? -1.62000   88.31500  41.00400  1.000 45.25968  ?  231  TYR   A CZ  1 
ATOM   1853  O  OH  . TYR   A 1 231  ? -2.25200   87.92200  39.84700  1.000 45.42390  ?  231  TYR   A OH  1 
ATOM   1854  N  N   . LYS   A 1 232  ? 1.82200    91.26100  46.77500  1.000 36.38404  ?  232  LYS   A N   1 
ATOM   1855  C  CA  . LYS   A 1 232  ? 1.91000    91.82000  48.11900  1.000 35.54606  ?  232  LYS   A CA  1 
ATOM   1856  C  C   . LYS   A 1 232  ? 2.14700    93.32500  48.07700  1.000 33.92661  ?  232  LYS   A C   1 
ATOM   1857  O  O   . LYS   A 1 232  ? 1.59600    94.07100  48.89500  1.000 48.72959  ?  232  LYS   A O   1 
ATOM   1858  C  CB  . LYS   A 1 232  ? 3.01700    91.11400  48.90100  1.000 31.91124  ?  232  LYS   A CB  1 
ATOM   1859  C  CG  . LYS   A 1 232  ? 3.37900    91.76500  50.22200  1.000 48.78261  ?  232  LYS   A CG  1 
ATOM   1860  C  CD  . LYS   A 1 232  ? 4.17400    90.80000  51.08000  1.000 42.45922  ?  232  LYS   A CD  1 
ATOM   1861  C  CE  . LYS   A 1 232  ? 5.15800    91.52200  51.97900  1.000 60.09462  ?  232  LYS   A CE  1 
ATOM   1862  N  NZ  . LYS   A 1 232  ? 6.05500    90.54900  52.66200  1.000 67.62657  ?  232  LYS   A NZ  1 
ATOM   1863  N  N   . GLN   A 1 233  ? 2.95200    93.79100  47.12100  1.000 26.23690  ?  233  GLN   A N   1 
ATOM   1864  C  CA  . GLN   A 1 233  ? 3.21200    95.22300  47.01100  1.000 37.03992  ?  233  GLN   A CA  1 
ATOM   1865  C  C   . GLN   A 1 233  ? 1.97800    95.97300  46.52600  1.000 43.47607  ?  233  GLN   A C   1 
ATOM   1866  O  O   . GLN   A 1 233  ? 1.69500    97.08200  46.99400  1.000 50.67394  ?  233  GLN   A O   1 
ATOM   1867  C  CB  . GLN   A 1 233  ? 4.39900    95.46400  46.07900  1.000 48.46270  ?  233  GLN   A CB  1 
ATOM   1868  C  CG  . GLN   A 1 233  ? 5.70400    94.89300  46.60900  1.000 52.23230  ?  233  GLN   A CG  1 
ATOM   1869  C  CD  . GLN   A 1 233  ? 6.74900    94.70600  45.52600  1.000 49.25014  ?  233  GLN   A CD  1 
ATOM   1870  O  OE1 . GLN   A 1 233  ? 7.22400    93.59600  45.29700  1.000 75.85073  ?  233  GLN   A OE1 1 
ATOM   1871  N  NE2 . GLN   A 1 233  ? 7.11700    95.79100  44.85800  1.000 39.09256  ?  233  GLN   A NE2 1 
ATOM   1872  N  N   . LEU   A 1 234  ? 1.23100    95.38300  45.59000  1.000 52.21962  ?  234  LEU   A N   1 
ATOM   1873  C  CA  . LEU   A 1 234  ? -0.02900   95.98200  45.16200  1.000 43.68512  ?  234  LEU   A CA  1 
ATOM   1874  C  C   . LEU   A 1 234  ? -1.04300   95.99300  46.29900  1.000 45.22212  ?  234  LEU   A C   1 
ATOM   1875  O  O   . LEU   A 1 234  ? -1.73700   96.99400  46.51200  1.000 38.57318  ?  234  LEU   A O   1 
ATOM   1876  C  CB  . LEU   A 1 234  ? -0.58300   95.22400  43.95500  1.000 38.03787  ?  234  LEU   A CB  1 
ATOM   1877  C  CG  . LEU   A 1 234  ? -1.91800   95.69400  43.37400  1.000 27.79315  ?  234  LEU   A CG  1 
ATOM   1878  C  CD1 . LEU   A 1 234  ? -1.79500   97.09500  42.79600  1.000 23.43889  ?  234  LEU   A CD1 1 
ATOM   1879  C  CD2 . LEU   A 1 234  ? -2.41900   94.71600  42.32300  1.000 24.57626  ?  234  LEU   A CD2 1 
ATOM   1880  N  N   . ASN   A 1 235  ? -1.13200   94.89000  47.04600  1.000 32.22161  ?  235  ASN   A N   1 
ATOM   1881  C  CA  . ASN   A 1 235  ? -2.09100   94.81100  48.14100  1.000 32.13217  ?  235  ASN   A CA  1 
ATOM   1882  C  C   . ASN   A 1 235  ? -1.78700   95.84100  49.22100  1.000 43.66975  ?  235  ASN   A C   1 
ATOM   1883  O  O   . ASN   A 1 235  ? -2.70000   96.48400  49.75100  1.000 50.50100  ?  235  ASN   A O   1 
ATOM   1884  C  CB  . ASN   A 1 235  ? -2.08900   93.40100  48.73000  1.000 27.34556  ?  235  ASN   A CB  1 
ATOM   1885  C  CG  . ASN   A 1 235  ? -3.32300   93.11500  49.55500  1.000 42.15186  ?  235  ASN   A CG  1 
ATOM   1886  O  OD1 . ASN   A 1 235  ? -4.41600   93.58500  49.23900  1.000 62.77954  ?  235  ASN   A OD1 1 
ATOM   1887  N  ND2 . ASN   A 1 235  ? -3.15700   92.34300  50.62100  1.000 53.88715  ?  235  ASN   A ND2 1 
ATOM   1888  N  N   . GLU   A 1 236  ? -0.50600   96.02000  49.55400  1.000 50.17131  ?  236  GLU   A N   1 
ATOM   1889  C  CA  . GLU   A 1 236  ? -0.14800   96.94000  50.62900  1.000 38.99893  ?  236  GLU   A CA  1 
ATOM   1890  C  C   . GLU   A 1 236  ? -0.31100   98.39300  50.19900  1.000 36.67336  ?  236  GLU   A C   1 
ATOM   1891  O  O   . GLU   A 1 236  ? -0.72900   99.23600  51.00000  1.000 43.74617  ?  236  GLU   A O   1 
ATOM   1892  C  CB  . GLU   A 1 236  ? 1.28200    96.67300  51.09700  1.000 37.64705  ?  236  GLU   A CB  1 
ATOM   1893  C  CG  . GLU   A 1 236  ? 1.44400    95.36800  51.85700  1.000 41.71980  ?  236  GLU   A CG  1 
ATOM   1894  C  CD  . GLU   A 1 236  ? 2.82400    95.21500  52.46200  1.000 65.19762  ?  236  GLU   A CD  1 
ATOM   1895  O  OE1 . GLU   A 1 236  ? 3.74400    95.95000  52.04400  1.000 58.33123  ?  236  GLU   A OE1 1 
ATOM   1896  O  OE2 . GLU   A 1 236  ? 2.98700    94.36200  53.36100  1.000 76.06405  -1 236  GLU   A OE2 1 
ATOM   1897  N  N   . ARG   A 1 237  ? 0.01600    98.70800  48.94300  1.000 33.61198  ?  237  ARG   A N   1 
ATOM   1898  C  CA  . ARG   A 1 237  ? -0.16800   100.07700 48.47200  1.000 33.79916  ?  237  ARG   A CA  1 
ATOM   1899  C  C   . ARG   A 1 237  ? -1.64400   100.43300 48.36200  1.000 46.46933  ?  237  ARG   A C   1 
ATOM   1900  O  O   . ARG   A 1 237  ? -2.01700   101.59500 48.55700  1.000 52.70556  ?  237  ARG   A O   1 
ATOM   1901  C  CB  . ARG   A 1 237  ? 0.52600    100.27700 47.12600  1.000 36.19924  ?  237  ARG   A CB  1 
ATOM   1902  C  CG  . ARG   A 1 237  ? 0.77600    101.73600 46.78200  1.000 41.86665  ?  237  ARG   A CG  1 
ATOM   1903  C  CD  . ARG   A 1 237  ? 1.70300    102.37400 47.80300  1.000 54.34964  ?  237  ARG   A CD  1 
ATOM   1904  N  NE  . ARG   A 1 237  ? 1.93700    103.78700 47.53500  1.000 71.90404  ?  237  ARG   A NE  1 
ATOM   1905  C  CZ  . ARG   A 1 237  ? 2.98500    104.46700 47.98100  1.000 87.22556  ?  237  ARG   A CZ  1 
ATOM   1906  N  NH1 . ARG   A 1 237  ? 3.93000    103.88500 48.70200  1.000 99.86924  ?  237  ARG   A NH1 1 
ATOM   1907  N  NH2 . ARG   A 1 237  ? 3.09200    105.76000 47.68800  1.000 77.32212  ?  237  ARG   A NH2 1 
ATOM   1908  N  N   . ALA   A 1 238  ? -2.49500   99.45200  48.05200  1.000 45.75124  ?  238  ALA   A N   1 
ATOM   1909  C  CA  . ALA   A 1 238  ? -3.93000   99.70700  48.02200  1.000 36.00212  ?  238  ALA   A CA  1 
ATOM   1910  C  C   . ALA   A 1 238  ? -4.48400   99.89400  49.42800  1.000 40.05119  ?  238  ALA   A C   1 
ATOM   1911  O  O   . ALA   A 1 238  ? -5.31100   100.78400 49.66200  1.000 41.89959  ?  238  ALA   A O   1 
ATOM   1912  C  CB  . ALA   A 1 238  ? -4.65100   98.56700  47.30500  1.000 43.64899  ?  238  ALA   A CB  1 
ATOM   1913  N  N   . ASN   A 1 239  ? -4.03200   99.07100  50.37900  1.000 43.89629  ?  239  ASN   A N   1 
ATOM   1914  C  CA  . ASN   A 1 239  ? -4.50200   99.19200  51.75600  1.000 48.70270  ?  239  ASN   A CA  1 
ATOM   1915  C  C   . ASN   A 1 239  ? -4.13800   100.54200 52.36100  1.000 48.66741  ?  239  ASN   A C   1 
ATOM   1916  O  O   . ASN   A 1 239  ? -4.89900   101.08200 53.17300  1.000 48.03981  ?  239  ASN   A O   1 
ATOM   1917  C  CB  . ASN   A 1 239  ? -3.93200   98.05800  52.60900  1.000 38.68233  ?  239  ASN   A CB  1 
ATOM   1918  C  CG  . ASN   A 1 239  ? -4.47400   96.69900  52.21100  1.000 52.36004  ?  239  ASN   A CG  1 
ATOM   1919  O  OD1 . ASN   A 1 239  ? -5.59800   96.58500  51.72400  1.000 70.09606  ?  239  ASN   A OD1 1 
ATOM   1920  N  ND2 . ASN   A 1 239  ? -3.67500   95.66000  52.41700  1.000 55.22489  ?  239  ASN   A ND2 1 
ATOM   1921  N  N   . GLN   A 1 240  ? -2.98400   101.09900 51.98800  1.000 47.97027  ?  240  GLN   A N   1 
ATOM   1922  C  CA  . GLN   A 1 240  ? -2.61300   102.42400 52.47800  1.000 60.08085  ?  240  GLN   A CA  1 
ATOM   1923  C  C   . GLN   A 1 240  ? -3.58500   103.48200 51.97300  1.000 57.90768  ?  240  GLN   A C   1 
ATOM   1924  O  O   . GLN   A 1 240  ? -4.04100   104.34100 52.73700  1.000 57.72600  ?  240  GLN   A O   1 
ATOM   1925  C  CB  . GLN   A 1 240  ? -1.18400   102.76300 52.05200  1.000 49.59102  ?  240  GLN   A CB  1 
ATOM   1926  C  CG  . GLN   A 1 240  ? -0.11500   101.87700 52.66500  1.000 53.50116  ?  240  GLN   A CG  1 
ATOM   1927  C  CD  . GLN   A 1 240  ? 1.27600    102.24500 52.19000  1.000 56.68569  ?  240  GLN   A CD  1 
ATOM   1928  O  OE1 . GLN   A 1 240  ? 2.03400    101.39100 51.73100  1.000 63.26717  ?  240  GLN   A OE1 1 
ATOM   1929  N  NE2 . GLN   A 1 240  ? 1.62000    103.52400 52.29700  1.000 49.56684  ?  240  GLN   A NE2 1 
ATOM   1930  N  N   . LEU   A 1 241  ? -3.91500   103.43300 50.68000  1.000 49.18425  ?  241  LEU   A N   1 
ATOM   1931  C  CA  . LEU   A 1 241  ? -4.84000   104.40800 50.11500  1.000 51.89470  ?  241  LEU   A CA  1 
ATOM   1932  C  C   . LEU   A 1 241  ? -6.26400   104.18300 50.60800  1.000 53.41725  ?  241  LEU   A C   1 
ATOM   1933  O  O   . LEU   A 1 241  ? -7.00900   105.15100 50.80000  1.000 47.75852  ?  241  LEU   A O   1 
ATOM   1934  C  CB  . LEU   A 1 241  ? -4.78000   104.35500 48.58800  1.000 35.56215  ?  241  LEU   A CB  1 
ATOM   1935  C  CG  . LEU   A 1 241  ? -5.59900   105.39500 47.82100  1.000 38.40442  ?  241  LEU   A CG  1 
ATOM   1936  C  CD1 . LEU   A 1 241  ? -5.22500   106.79900 48.25700  1.000 32.81297  ?  241  LEU   A CD1 1 
ATOM   1937  C  CD2 . LEU   A 1 241  ? -5.39500   105.22600 46.32500  1.000 35.43972  ?  241  LEU   A CD2 1 
ATOM   1938  N  N   . ALA   A 1 242  ? -6.65300   102.92300 50.83300  1.000 49.80137  ?  242  ALA   A N   1 
ATOM   1939  C  CA  . ALA   A 1 242  ? -8.01000   102.62900 51.28500  1.000 49.66858  ?  242  ALA   A CA  1 
ATOM   1940  C  C   . ALA   A 1 242  ? -8.23000   103.03300 52.73700  1.000 49.86745  ?  242  ALA   A C   1 
ATOM   1941  O  O   . ALA   A 1 242  ? -9.33100   103.46800 53.09500  1.000 59.95920  ?  242  ALA   A O   1 
ATOM   1942  C  CB  . ALA   A 1 242  ? -8.31300   101.14300 51.10300  1.000 43.79841  ?  242  ALA   A CB  1 
ATOM   1943  N  N   . HIS   A 1 243  ? -7.21500   102.87200 53.59200  1.000 41.65417  ?  243  HIS   A N   1 
ATOM   1944  C  CA  . HIS   A 1 243  ? -7.30000   103.42100 54.94100  1.000 44.99722  ?  243  HIS   A CA  1 
ATOM   1945  C  C   . HIS   A 1 243  ? -7.55100   104.92100 54.89700  1.000 50.97489  ?  243  HIS   A C   1 
ATOM   1946  O  O   . HIS   A 1 243  ? -8.36600   105.44700 55.66400  1.000 54.96355  ?  243  HIS   A O   1 
ATOM   1947  C  CB  . HIS   A 1 243  ? -6.01800   103.12300 55.71900  1.000 52.59185  ?  243  HIS   A CB  1 
ATOM   1948  C  CG  . HIS   A 1 243  ? -5.98000   101.75700 56.33100  1.000 52.21114  ?  243  HIS   A CG  1 
ATOM   1949  N  ND1 . HIS   A 1 243  ? -5.16300   100.75200 55.86000  1.000 50.54762  ?  243  HIS   A ND1 1 
ATOM   1950  C  CD2 . HIS   A 1 243  ? -6.65100   101.23400 57.38400  1.000 60.17387  ?  243  HIS   A CD2 1 
ATOM   1951  C  CE1 . HIS   A 1 243  ? -5.33500   99.66700  56.59300  1.000 47.90191  ?  243  HIS   A CE1 1 
ATOM   1952  N  NE2 . HIS   A 1 243  ? -6.23400   99.93200  57.52500  1.000 56.03004  ?  243  HIS   A NE2 1 
ATOM   1953  N  N   . HIS   A 1 244  ? -6.85600   105.62600 54.00200  1.000 50.61372  ?  244  HIS   A N   1 
ATOM   1954  C  CA  . HIS   A 1 244  ? -7.06800   107.06000 53.85100  1.000 51.71745  ?  244  HIS   A CA  1 
ATOM   1955  C  C   . HIS   A 1 244  ? -8.44600   107.36200 53.28100  1.000 53.08552  ?  244  HIS   A C   1 
ATOM   1956  O  O   . HIS   A 1 244  ? -9.04600   108.38700 53.62500  1.000 53.36029  ?  244  HIS   A O   1 
ATOM   1957  C  CB  . HIS   A 1 244  ? -5.97600   107.65300 52.96100  1.000 43.52489  ?  244  HIS   A CB  1 
ATOM   1958  C  CG  . HIS   A 1 244  ? -6.04500   109.14200 52.82000  1.000 50.70806  ?  244  HIS   A CG  1 
ATOM   1959  N  ND1 . HIS   A 1 244  ? -6.64400   109.76100 51.74500  1.000 62.96467  ?  244  HIS   A ND1 1 
ATOM   1960  C  CD2 . HIS   A 1 244  ? -5.58000   110.13500 53.61400  1.000 67.44860  ?  244  HIS   A CD2 1 
ATOM   1961  C  CE1 . HIS   A 1 244  ? -6.55000   111.07100 51.88500  1.000 59.19617  ?  244  HIS   A CE1 1 
ATOM   1962  N  NE2 . HIS   A 1 244  ? -5.90800   111.32500 53.01100  1.000 75.42154  ?  244  HIS   A NE2 1 
ATOM   1963  N  N   . LEU   A 1 245  ? -8.96600   106.48500 52.42000  1.000 57.94944  ?  245  LEU   A N   1 
ATOM   1964  C  CA  . LEU   A 1 245  ? -10.28500  106.70900 51.83700  1.000 54.87098  ?  245  LEU   A CA  1 
ATOM   1965  C  C   . LEU   A 1 245  ? -11.38800  106.45300 52.85600  1.000 57.95527  ?  245  LEU   A C   1 
ATOM   1966  O  O   . LEU   A 1 245  ? -12.30100  107.27200 53.01500  1.000 60.84462  ?  245  LEU   A O   1 
ATOM   1967  C  CB  . LEU   A 1 245  ? -10.47300  105.82900 50.60100  1.000 49.15124  ?  245  LEU   A CB  1 
ATOM   1968  C  CG  . LEU   A 1 245  ? -9.67400   106.22900 49.35900  1.000 45.76464  ?  245  LEU   A CG  1 
ATOM   1969  C  CD1 . LEU   A 1 245  ? -10.00100  105.31600 48.18800  1.000 47.78506  ?  245  LEU   A CD1 1 
ATOM   1970  C  CD2 . LEU   A 1 245  ? -9.93200   107.68600 49.00100  1.000 37.68449  ?  245  LEU   A CD2 1 
ATOM   1971  N  N   . ARG   A 1 246  ? -11.32200  105.31900 53.56000  1.000 46.56703  ?  246  ARG   A N   1 
ATOM   1972  C  CA  . ARG   A 1 246  ? -12.35900  105.00300 54.53900  1.000 49.80823  ?  246  ARG   A CA  1 
ATOM   1973  C  C   . ARG   A 1 246  ? -12.39700  106.03700 55.65700  1.000 57.16502  ?  246  ARG   A C   1 
ATOM   1974  O  O   . ARG   A 1 246  ? -13.47800  106.42300 56.11800  1.000 69.88900  ?  246  ARG   A O   1 
ATOM   1975  C  CB  . ARG   A 1 246  ? -12.14200  103.60300 55.11100  1.000 43.29126  ?  246  ARG   A CB  1 
ATOM   1976  C  CG  . ARG   A 1 246  ? -13.18200  103.20900 56.14700  1.000 30.75148  ?  246  ARG   A CG  1 
ATOM   1977  C  CD  . ARG   A 1 246  ? -12.96400  101.79500 56.64800  1.000 26.89177  ?  246  ARG   A CD  1 
ATOM   1978  N  NE  . ARG   A 1 246  ? -12.96600  100.82500 55.56000  1.000 22.78719  ?  246  ARG   A NE  1 
ATOM   1979  C  CZ  . ARG   A 1 246  ? -13.02800  99.51200  55.73300  1.000 38.06369  ?  246  ARG   A CZ  1 
ATOM   1980  N  NH1 . ARG   A 1 246  ? -13.11800  98.97700  56.94000  1.000 42.42696  ?  246  ARG   A NH1 1 
ATOM   1981  N  NH2 . ARG   A 1 246  ? -13.00400  98.71500  54.66900  1.000 46.68561  ?  246  ARG   A NH2 1 
ATOM   1982  N  N   . GLY   A 1 247  ? -11.23000  106.49800 56.10700  1.000 50.24986  ?  247  GLY   A N   1 
ATOM   1983  C  CA  . GLY   A 1 247  ? -11.20100  107.53800 57.12000  1.000 50.61243  ?  247  GLY   A CA  1 
ATOM   1984  C  C   . GLY   A 1 247  ? -11.79700  108.84500 56.63400  1.000 57.81556  ?  247  GLY   A C   1 
ATOM   1985  O  O   . GLY   A 1 247  ? -12.40600  109.58300 57.41300  1.000 80.41414  ?  247  GLY   A O   1 
ATOM   1986  N  N   . LYS   A 1 248  ? -11.63400  109.14800 55.34400  1.000 56.20075  ?  248  LYS   A N   1 
ATOM   1987  C  CA  . LYS   A 1 248  ? -12.23300  110.35400 54.78300  1.000 60.77570  ?  248  LYS   A CA  1 
ATOM   1988  C  C   . LYS   A 1 248  ? -13.75400  110.27600 54.77900  1.000 67.07810  ?  248  LYS   A C   1 
ATOM   1989  O  O   . LYS   A 1 248  ? -14.42500  111.31200 54.84200  1.000 81.27999  ?  248  LYS   A O   1 
ATOM   1990  C  CB  . LYS   A 1 248  ? -11.70700  110.59300 53.36800  1.000 53.16455  ?  248  LYS   A CB  1 
ATOM   1991  C  CG  . LYS   A 1 248  ? -10.53700  111.56100 53.29300  1.000 56.19998  ?  248  LYS   A CG  1 
ATOM   1992  C  CD  . LYS   A 1 248  ? -11.00500  112.97500 52.98400  1.000 69.86947  ?  248  LYS   A CD  1 
ATOM   1993  C  CE  . LYS   A 1 248  ? -9.83200   113.94000 52.94200  1.000 70.56833  ?  248  LYS   A CE  1 
ATOM   1994  N  NZ  . LYS   A 1 248  ? -10.18200  115.21400 52.25400  1.000 99.60205  ?  248  LYS   A NZ  1 
ATOM   1995  N  N   . GLY   A 1 249  ? -14.31500  109.07000 54.70800  1.000 50.43031  ?  249  GLY   A N   1 
ATOM   1996  C  CA  . GLY   A 1 249  ? -15.75300  108.90900 54.79700  1.000 56.06046  ?  249  GLY   A CA  1 
ATOM   1997  C  C   . GLY   A 1 249  ? -16.36500  108.03700 53.72000  1.000 53.57575  ?  249  GLY   A C   1 
ATOM   1998  O  O   . GLY   A 1 249  ? -17.45000  108.34300 53.21700  1.000 69.72114  ?  249  GLY   A O   1 
ATOM   1999  N  N   . VAL   A 1 250  ? -15.69300  106.94700 53.36200  1.000 46.63554  ?  250  VAL   A N   1 
ATOM   2000  C  CA  . VAL   A 1 250  ? -16.20500  106.01200 52.36500  1.000 43.46042  ?  250  VAL   A CA  1 
ATOM   2001  C  C   . VAL   A 1 250  ? -16.94500  104.89000 53.08300  1.000 50.97503  ?  250  VAL   A C   1 
ATOM   2002  O  O   . VAL   A 1 250  ? -16.35100  104.14500 53.87000  1.000 42.43441  ?  250  VAL   A O   1 
ATOM   2003  C  CB  . VAL   A 1 250  ? -15.07600  105.45100 51.48800  1.000 52.54981  ?  250  VAL   A CB  1 
ATOM   2004  C  CG1 . VAL   A 1 250  ? -15.62000  104.40200 50.53000  1.000 45.39773  ?  250  VAL   A CG1 1 
ATOM   2005  C  CG2 . VAL   A 1 250  ? -14.39800  106.56600 50.71400  1.000 47.15349  ?  250  VAL   A CG2 1 
ATOM   2006  N  N   . LYS   A 1 251  ? -18.24100  104.77300 52.81600  1.000 60.28895  ?  251  LYS   A N   1 
ATOM   2007  C  CA  . LYS   A 1 251  ? -19.07500  103.68200 53.29500  1.000 54.00837  ?  251  LYS   A CA  1 
ATOM   2008  C  C   . LYS   A 1 251  ? -19.52600  102.81500 52.12300  1.000 43.67180  ?  251  LYS   A C   1 
ATOM   2009  O  O   . LYS   A 1 251  ? -19.45800  103.24400 50.96600  1.000 32.92201  ?  251  LYS   A O   1 
ATOM   2010  C  CB  . LYS   A 1 251  ? -20.29900  104.22400 54.05300  1.000 48.60857  ?  251  LYS   A CB  1 
ATOM   2011  C  CG  . LYS   A 1 251  ? -20.19900  104.12000 55.58100  1.000 50.69583  ?  251  LYS   A CG  1 
ATOM   2012  C  CD  . LYS   A 1 251  ? -20.71500  102.77000 56.09500  1.000 69.86268  ?  251  LYS   A CD  1 
ATOM   2013  C  CE  . LYS   A 1 251  ? -19.83900  102.21700 57.22300  1.000 60.38193  ?  251  LYS   A CE  1 
ATOM   2014  N  NZ  . LYS   A 1 251  ? -19.88000  100.72500 57.31500  1.000 51.43620  ?  251  LYS   A NZ  1 
ATOM   2015  N  N   . PRO   A 1 252  ? -19.94200  101.57000 52.37900  1.000 33.66585  ?  252  PRO   A N   1 
ATOM   2016  C  CA  . PRO   A 1 252  ? -20.46900  100.72500 51.30200  1.000 37.62140  ?  252  PRO   A CA  1 
ATOM   2017  C  C   . PRO   A 1 252  ? -21.48100  101.44200 50.41800  1.000 48.92826  ?  252  PRO   A C   1 
ATOM   2018  O  O   . PRO   A 1 252  ? -22.23200  102.31200 50.86800  1.000 49.79183  ?  252  PRO   A O   1 
ATOM   2019  C  CB  . PRO   A 1 252  ? -21.11400  99.56500  52.06200  1.000 45.54841  ?  252  PRO   A CB  1 
ATOM   2020  C  CG  . PRO   A 1 252  ? -20.23400  99.39800  53.25300  1.000 48.16347  ?  252  PRO   A CG  1 
ATOM   2021  C  CD  . PRO   A 1 252  ? -19.62700  100.76500 53.57400  1.000 46.20315  ?  252  PRO   A CD  1 
ATOM   2022  N  N   . ASP   A 1 253  ? -21.48100  101.05400 49.14100  1.000 46.29157  ?  253  ASP   A N   1 
ATOM   2023  C  CA  . ASP   A 1 253  ? -22.32100  101.65100 48.10200  1.000 37.23870  ?  253  ASP   A CA  1 
ATOM   2024  C  C   . ASP   A 1 253  ? -21.98900  103.12400 47.87200  1.000 43.00030  ?  253  ASP   A C   1 
ATOM   2025  O  O   . ASP   A 1 253  ? -22.86400  103.92200 47.52800  1.000 61.23488  ?  253  ASP   A O   1 
ATOM   2026  C  CB  . ASP   A 1 253  ? -23.81200  101.46900 48.40600  1.000 44.73516  ?  253  ASP   A CB  1 
ATOM   2027  C  CG  . ASP   A 1 253  ? -24.30200  100.06400 48.09400  1.000 64.44887  ?  253  ASP   A CG  1 
ATOM   2028  O  OD1 . ASP   A 1 253  ? -23.64500  99.36800  47.29000  1.000 61.58057  ?  253  ASP   A OD1 1 
ATOM   2029  O  OD2 . ASP   A 1 253  ? -25.34600  99.65700  48.64500  1.000 72.98481  -1 253  ASP   A OD2 1 
ATOM   2030  N  N   . ASP   A 1 254  ? -20.72600  103.49700 48.05200  1.000 49.47303  ?  254  ASP   A N   1 
ATOM   2031  C  CA  . ASP   A 1 254  ? -20.24700  104.80100 47.61900  1.000 37.14642  ?  254  ASP   A CA  1 
ATOM   2032  C  C   . ASP   A 1 254  ? -19.72700  104.71400 46.18900  1.000 42.09885  ?  254  ASP   A C   1 
ATOM   2033  O  O   . ASP   A 1 254  ? -19.45900  103.63100 45.66400  1.000 65.89883  ?  254  ASP   A O   1 
ATOM   2034  C  CB  . ASP   A 1 254  ? -19.15000  105.32600 48.54700  1.000 72.30773  ?  254  ASP   A CB  1 
ATOM   2035  C  CG  . ASP   A 1 254  ? -19.70500  106.06300 49.75100  1.000 62.00777  ?  254  ASP   A CG  1 
ATOM   2036  O  OD1 . ASP   A 1 254  ? -20.91900  105.94200 50.01600  1.000 50.22478  ?  254  ASP   A OD1 1 
ATOM   2037  O  OD2 . ASP   A 1 254  ? -18.92900  106.77200 50.42600  1.000 77.98212  -1 254  ASP   A OD2 1 
ATOM   2038  N  N   . GLN   A 1 255  ? -19.58300  105.87800 45.55800  1.000 33.72677  ?  255  GLN   A N   1 
ATOM   2039  C  CA  . GLN   A 1 255  ? -19.19200  105.96200 44.15300  1.000 53.83603  ?  255  GLN   A CA  1 
ATOM   2040  C  C   . GLN   A 1 255  ? -17.99300  106.89700 44.00000  1.000 49.29825  ?  255  GLN   A C   1 
ATOM   2041  O  O   . GLN   A 1 255  ? -18.06300  107.94200 43.35500  1.000 61.65422  ?  255  GLN   A O   1 
ATOM   2042  C  CB  . GLN   A 1 255  ? -20.36900  106.41000 43.29000  1.000 42.85348  ?  255  GLN   A CB  1 
ATOM   2043  C  CG  . GLN   A 1 255  ? -21.27900  105.26500 42.87900  1.000 36.02851  ?  255  GLN   A CG  1 
ATOM   2044  C  CD  . GLN   A 1 255  ? -22.74300  105.64200 42.89300  1.000 49.25939  ?  255  GLN   A CD  1 
ATOM   2045  O  OE1 . GLN   A 1 255  ? -23.19100  106.47600 42.10600  1.000 71.95141  ?  255  GLN   A OE1 1 
ATOM   2046  N  NE2 . GLN   A 1 255  ? -23.50200  105.02700 43.79200  1.000 53.75264  ?  255  GLN   A NE2 1 
ATOM   2047  N  N   . VAL   A 1 256  ? -16.86900  106.50400 44.60100  1.000 49.55912  ?  256  VAL   A N   1 
ATOM   2048  C  CA  . VAL   A 1 256  ? -15.62700  107.24900 44.43400  1.000 50.87902  ?  256  VAL   A CA  1 
ATOM   2049  C  C   . VAL   A 1 256  ? -15.17200  107.14500 42.98600  1.000 37.03359  ?  256  VAL   A C   1 
ATOM   2050  O  O   . VAL   A 1 256  ? -15.02400  106.04300 42.44200  1.000 40.38103  ?  256  VAL   A O   1 
ATOM   2051  C  CB  . VAL   A 1 256  ? -14.54800  106.72600 45.39400  1.000 40.60545  ?  256  VAL   A CB  1 
ATOM   2052  C  CG1 . VAL   A 1 256  ? -13.21200  107.40300 45.11200  1.000 59.38023  ?  256  VAL   A CG1 1 
ATOM   2053  C  CG2 . VAL   A 1 256  ? -14.96600  106.94100 46.84300  1.000 47.27331  ?  256  VAL   A CG2 1 
ATOM   2054  N  N   . ALA   A 1 257  ? -14.95100  108.29200 42.35400  1.000 43.63797  ?  257  ALA   A N   1 
ATOM   2055  C  CA  . ALA   A 1 257  ? -14.54400  108.33200 40.95800  1.000 50.71652  ?  257  ALA   A CA  1 
ATOM   2056  C  C   . ALA   A 1 257  ? -13.02500  108.35800 40.83300  1.000 52.00971  ?  257  ALA   A C   1 
ATOM   2057  O  O   . ALA   A 1 257  ? -12.31300  108.82100 41.73000  1.000 50.97195  ?  257  ALA   A O   1 
ATOM   2058  C  CB  . ALA   A 1 257  ? -15.14100  109.55000 40.25200  1.000 34.04401  ?  257  ALA   A CB  1 
ATOM   2059  N  N   . ILE   A 1 258  ? -12.53700  107.85500 39.70100  1.000 42.61440  ?  258  ILE   A N   1 
ATOM   2060  C  CA  . ILE   A 1 258  ? -11.11200  107.79200 39.39900  1.000 35.35542  ?  258  ILE   A CA  1 
ATOM   2061  C  C   . ILE   A 1 258  ? -10.90600  108.34100 37.99500  1.000 32.93526  ?  258  ILE   A C   1 
ATOM   2062  O  O   . ILE   A 1 258  ? -11.49800  107.83300 37.03500  1.000 43.08389  ?  258  ILE   A O   1 
ATOM   2063  C  CB  . ILE   A 1 258  ? -10.56300  106.36000 39.50200  1.000 29.86490  ?  258  ILE   A CB  1 
ATOM   2064  C  CG1 . ILE   A 1 258  ? -10.84200  105.77200 40.88600  1.000 36.97888  ?  258  ILE   A CG1 1 
ATOM   2065  C  CG2 . ILE   A 1 258  ? -9.07500   106.35200 39.21900  1.000 34.42272  ?  258  ILE   A CG2 1 
ATOM   2066  C  CD1 . ILE   A 1 258  ? -10.53400  104.29400 41.00100  1.000 39.27876  ?  258  ILE   A CD1 1 
ATOM   2067  N  N   . MET   A 1 259  ? -10.07000  109.37000 37.87300  1.000 40.83985  ?  259  MET   A N   1 
ATOM   2068  C  CA  . MET   A 1 259  ? -9.73000   109.96800 36.58100  1.000 47.27412  ?  259  MET   A CA  1 
ATOM   2069  C  C   . MET   A 1 259  ? -8.21200   109.90800 36.42200  1.000 51.49897  ?  259  MET   A C   1 
ATOM   2070  O  O   . MET   A 1 259  ? -7.50300   110.88700 36.66500  1.000 60.85695  ?  259  MET   A O   1 
ATOM   2071  C  CB  . MET   A 1 259  ? -10.25500  111.40500 36.47500  1.000 49.79807  ?  259  MET   A CB  1 
ATOM   2072  C  CG  . MET   A 1 259  ? -10.13600  111.99500 35.07800  1.000 55.59998  ?  259  MET   A CG  1 
ATOM   2073  S  SD  . MET   A 1 259  ? -10.36900  113.78100 35.01200  1.000 62.54513  ?  259  MET   A SD  1 
ATOM   2074  C  CE  . MET   A 1 259  ? -11.12400  114.09500 36.60200  1.000 55.07706  ?  259  MET   A CE  1 
ATOM   2075  N  N   . LEU   A 1 260  ? -7.71800   108.74400 36.01100  1.000 48.15377  ?  260  LEU   A N   1 
ATOM   2076  C  CA  . LEU   A 1 260  ? -6.29900   108.52200 35.79200  1.000 42.66624  ?  260  LEU   A CA  1 
ATOM   2077  C  C   . LEU   A 1 260  ? -6.09500   107.83700 34.44800  1.000 49.72664  ?  260  LEU   A C   1 
ATOM   2078  O  O   . LEU   A 1 260  ? -7.01900   107.25300 33.87400  1.000 47.63968  ?  260  LEU   A O   1 
ATOM   2079  C  CB  . LEU   A 1 260  ? -5.68100   107.67300 36.91100  1.000 30.23210  ?  260  LEU   A CB  1 
ATOM   2080  C  CG  . LEU   A 1 260  ? -5.51300   108.36400 38.26700  1.000 39.43818  ?  260  LEU   A CG  1 
ATOM   2081  C  CD1 . LEU   A 1 260  ? -5.18800   107.35400 39.35900  1.000 37.16715  ?  260  LEU   A CD1 1 
ATOM   2082  C  CD2 . LEU   A 1 260  ? -4.44000   109.44600 38.19700  1.000 51.99795  ?  260  LEU   A CD2 1 
ATOM   2083  N  N   . ASP   A 1 261  ? -4.87000   107.92200 33.94800  1.000 45.57918  ?  261  ASP   A N   1 
ATOM   2084  C  CA  . ASP   A 1 261  ? -4.48100   107.18700 32.75600  1.000 50.32179  ?  261  ASP   A CA  1 
ATOM   2085  C  C   . ASP   A 1 261  ? -3.87200   105.84700 33.15100  1.000 40.90268  ?  261  ASP   A C   1 
ATOM   2086  O  O   . ASP   A 1 261  ? -3.45300   105.64300 34.29400  1.000 59.18095  ?  261  ASP   A O   1 
ATOM   2087  C  CB  . ASP   A 1 261  ? -3.50200   108.00500 31.91400  1.000 45.76884  ?  261  ASP   A CB  1 
ATOM   2088  C  CG  . ASP   A 1 261  ? -4.20900   108.91300 30.92600  1.000 66.52818  ?  261  ASP   A CG  1 
ATOM   2089  O  OD1 . ASP   A 1 261  ? -5.15600   108.44100 30.26400  1.000 66.72526  ?  261  ASP   A OD1 1 
ATOM   2090  O  OD2 . ASP   A 1 261  ? -3.82600   110.09800 30.81500  1.000 64.49177  -1 261  ASP   A OD2 1 
ATOM   2091  N  N   . LYS   A 1 262  ? -3.84700   104.92500 32.19000  1.000 30.39250  ?  262  LYS   A N   1 
ATOM   2092  C  CA  . LYS   A 1 262  ? -3.38200   103.56600 32.44400  1.000 43.19570  ?  262  LYS   A CA  1 
ATOM   2093  C  C   . LYS   A 1 262  ? -1.99000   103.56800 33.05500  1.000 49.68269  ?  262  LYS   A C   1 
ATOM   2094  O  O   . LYS   A 1 262  ? -1.01900   103.98500 32.41700  1.000 46.38326  ?  262  LYS   A O   1 
ATOM   2095  C  CB  . LYS   A 1 262  ? -3.39100   102.75500 31.14700  1.000 35.84306  ?  262  LYS   A CB  1 
ATOM   2096  C  CG  . LYS   A 1 262  ? -4.75700   102.21500 30.75600  1.000 49.96342  ?  262  LYS   A CG  1 
ATOM   2097  C  CD  . LYS   A 1 262  ? -4.66400   101.32000 29.53200  1.000 54.02238  ?  262  LYS   A CD  1 
ATOM   2098  C  CE  . LYS   A 1 262  ? -5.88500   101.48300 28.65000  1.000 53.02887  ?  262  LYS   A CE  1 
ATOM   2099  N  NZ  . LYS   A 1 262  ? -6.06000   102.90200 28.23800  1.000 59.49210  ?  262  LYS   A NZ  1 
ATOM   2100  N  N   . SER   A 1 263  ? -1.90200   103.09900 34.29600  1.000 38.08381  ?  263  SER   A N   1 
ATOM   2101  C  CA  . SER   A 1 263  ? -0.65800   103.12500 35.05300  1.000 45.40564  ?  263  SER   A CA  1 
ATOM   2102  C  C   . SER   A 1 263  ? -0.79300   102.17100 36.23400  1.000 48.88082  ?  263  SER   A C   1 
ATOM   2103  O  O   . SER   A 1 263  ? -1.81400   101.49900 36.40300  1.000 50.50251  ?  263  SER   A O   1 
ATOM   2104  C  CB  . SER   A 1 263  ? -0.33200   104.54600 35.52100  1.000 50.57407  ?  263  SER   A CB  1 
ATOM   2105  O  OG  . SER   A 1 263  ? -1.37700   105.06000 36.32900  1.000 47.51287  ?  263  SER   A OG  1 
ATOM   2106  N  N   . LEU   A 1 264  ? 0.25900    102.11900 37.05500  1.000 52.96602  ?  264  LEU   A N   1 
ATOM   2107  C  CA  . LEU   A 1 264  ? 0.19300    101.35000 38.29400  1.000 49.81995  ?  264  LEU   A CA  1 
ATOM   2108  C  C   . LEU   A 1 264  ? -0.78000   101.98100 39.28100  1.000 53.06804  ?  264  LEU   A C   1 
ATOM   2109  O  O   . LEU   A 1 264  ? -1.48100   101.27000 40.01100  1.000 46.90834  ?  264  LEU   A O   1 
ATOM   2110  C  CB  . LEU   A 1 264  ? 1.58000    101.24100 38.92600  1.000 44.17015  ?  264  LEU   A CB  1 
ATOM   2111  C  CG  . LEU   A 1 264  ? 2.66800    100.48600 38.16700  1.000 58.44163  ?  264  LEU   A CG  1 
ATOM   2112  C  CD1 . LEU   A 1 264  ? 4.03200    100.68800 38.80800  1.000 46.55847  ?  264  LEU   A CD1 1 
ATOM   2113  C  CD2 . LEU   A 1 264  ? 2.33400    99.00600  38.06300  1.000 58.55921  ?  264  LEU   A CD2 1 
ATOM   2114  N  N   . ASP   A 1 265  ? -0.83000   103.31500 39.32100  1.000 40.26088  ?  265  ASP   A N   1 
ATOM   2115  C  CA  . ASP   A 1 265  ? -1.69400   103.99900 40.27800  1.000 49.88468  ?  265  ASP   A CA  1 
ATOM   2116  C  C   . ASP   A 1 265  ? -3.16500   103.70100 40.02400  1.000 58.49077  ?  265  ASP   A C   1 
ATOM   2117  O  O   . ASP   A 1 265  ? -3.97500   103.74700 40.95700  1.000 47.76839  ?  265  ASP   A O   1 
ATOM   2118  C  CB  . ASP   A 1 265  ? -1.44000   105.50500 40.23000  1.000 51.79384  ?  265  ASP   A CB  1 
ATOM   2119  C  CG  . ASP   A 1 265  ? -0.05900   105.87800 40.73000  1.000 46.54877  ?  265  ASP   A CG  1 
ATOM   2120  O  OD1 . ASP   A 1 265  ? 0.42400    105.23200 41.68400  1.000 50.69816  ?  265  ASP   A OD1 1 
ATOM   2121  O  OD2 . ASP   A 1 265  ? 0.54400    106.81600 40.16800  1.000 60.42652  -1 265  ASP   A OD2 1 
ATOM   2122  N  N   . MET   A 1 266  ? -3.52900   103.39600 38.77800  1.000 51.69679  ?  266  MET   A N   1 
ATOM   2123  C  CA  . MET   A 1 266  ? -4.91200   103.03800 38.48100  1.000 49.45973  ?  266  MET   A CA  1 
ATOM   2124  C  C   . MET   A 1 266  ? -5.30500   101.74500 39.18400  1.000 48.52536  ?  266  MET   A C   1 
ATOM   2125  O  O   . MET   A 1 266  ? -6.36700   101.66400 39.81200  1.000 42.35506  ?  266  MET   A O   1 
ATOM   2126  C  CB  . MET   A 1 266  ? -5.10900   102.91000 36.97100  1.000 49.77941  ?  266  MET   A CB  1 
ATOM   2127  C  CG  . MET   A 1 266  ? -6.43400   102.28100 36.58000  1.000 40.51124  ?  266  MET   A CG  1 
ATOM   2128  S  SD  . MET   A 1 266  ? -6.65600   102.21600 34.79500  1.000 44.49547  ?  266  MET   A SD  1 
ATOM   2129  C  CE  . MET   A 1 266  ? -6.61600   103.95900 34.39200  1.000 33.26807  ?  266  MET   A CE  1 
ATOM   2130  N  N   . ILE   A 1 267  ? -4.45400   100.71900 39.09000  1.000 43.84990  ?  267  ILE   A N   1 
ATOM   2131  C  CA  . ILE   A 1 267  ? -4.74700   99.44900  39.74900  1.000 37.51641  ?  267  ILE   A CA  1 
ATOM   2132  C  C   . ILE   A 1 267  ? -4.78800   99.63300  41.26000  1.000 42.09398  ?  267  ILE   A C   1 
ATOM   2133  O  O   . ILE   A 1 267  ? -5.63700   99.05300  41.95000  1.000 52.32471  ?  267  ILE   A O   1 
ATOM   2134  C  CB  . ILE   A 1 267  ? -3.71800   98.38100  39.33900  1.000 30.62013  ?  267  ILE   A CB  1 
ATOM   2135  C  CG1 . ILE   A 1 267  ? -3.58000   98.32400  37.81600  1.000 26.04041  ?  267  ILE   A CG1 1 
ATOM   2136  C  CG2 . ILE   A 1 267  ? -4.12000   97.02200  39.89400  1.000 18.84328  ?  267  ILE   A CG2 1 
ATOM   2137  C  CD1 . ILE   A 1 267  ? -4.81800   97.82600  37.10800  1.000 26.32510  ?  267  ILE   A CD1 1 
ATOM   2138  N  N   . VAL   A 1 268  ? -3.87100   100.44000 41.79900  1.000 44.15948  ?  268  VAL   A N   1 
ATOM   2139  C  CA  . VAL   A 1 268  ? -3.89000   100.73300 43.22900  1.000 56.67438  ?  268  VAL   A CA  1 
ATOM   2140  C  C   . VAL   A 1 268  ? -5.16200   101.48500 43.59700  1.000 43.72972  ?  268  VAL   A C   1 
ATOM   2141  O  O   . VAL   A 1 268  ? -5.80900   101.18400 44.60900  1.000 35.77250  ?  268  VAL   A O   1 
ATOM   2142  C  CB  . VAL   A 1 268  ? -2.62700   101.51800 43.63000  1.000 52.11185  ?  268  VAL   A CB  1 
ATOM   2143  C  CG1 . VAL   A 1 268  ? -2.77200   102.09100 45.03300  1.000 42.02262  ?  268  VAL   A CG1 1 
ATOM   2144  C  CG2 . VAL   A 1 268  ? -1.40100   100.62600 43.54400  1.000 35.87694  ?  268  VAL   A CG2 1 
ATOM   2145  N  N   . SER   A 1 269  ? -5.54800   102.46400 42.77600  1.000 40.76189  ?  269  SER   A N   1 
ATOM   2146  C  CA  . SER   A 1 269  ? -6.74800   103.24200 43.06300  1.000 43.16995  ?  269  SER   A CA  1 
ATOM   2147  C  C   . SER   A 1 269  ? -7.98800   102.35800 43.06700  1.000 42.31774  ?  269  SER   A C   1 
ATOM   2148  O  O   . SER   A 1 269  ? -8.80500   102.42200 43.99200  1.000 50.60397  ?  269  SER   A O   1 
ATOM   2149  C  CB  . SER   A 1 269  ? -6.89400   104.37400 42.04400  1.000 39.76359  ?  269  SER   A CB  1 
ATOM   2150  O  OG  . SER   A 1 269  ? -5.77300   105.24100 42.08000  1.000 50.38948  ?  269  SER   A OG  1 
ATOM   2151  N  N   . ILE   A 1 270  ? -8.13300   101.51000 42.04500  1.000 33.60469  ?  270  ILE   A N   1 
ATOM   2152  C  CA  . ILE   A 1 270  ? -9.33400   100.68600 41.91100  1.000 30.53864  ?  270  ILE   A CA  1 
ATOM   2153  C  C   . ILE   A 1 270  ? -9.50900   99.78800  43.12900  1.000 40.50225  ?  270  ILE   A C   1 
ATOM   2154  O  O   . ILE   A 1 270  ? -10.58600  99.73500  43.73400  1.000 48.41767  ?  270  ILE   A O   1 
ATOM   2155  C  CB  . ILE   A 1 270  ? -9.27700   99.86500  40.61100  1.000 34.69821  ?  270  ILE   A CB  1 
ATOM   2156  C  CG1 . ILE   A 1 270  ? -9.41500   100.78100 39.39400  1.000 25.64725  ?  270  ILE   A CG1 1 
ATOM   2157  C  CG2 . ILE   A 1 270  ? -10.34900  98.78500  40.61800  1.000 29.08615  ?  270  ILE   A CG2 1 
ATOM   2158  C  CD1 . ILE   A 1 270  ? -9.20400   100.07400 38.07800  1.000 16.79154  ?  270  ILE   A CD1 1 
ATOM   2159  N  N   . LEU   A 1 271  ? -8.45100   99.06500  43.50700  1.000 39.02646  ?  271  LEU   A N   1 
ATOM   2160  C  CA  . LEU   A 1 271  ? -8.52300   98.20100  44.67900  1.000 42.97622  ?  271  LEU   A CA  1 
ATOM   2161  C  C   . LEU   A 1 271  ? -8.68500   98.98300  45.97600  1.000 35.88434  ?  271  LEU   A C   1 
ATOM   2162  O  O   . LEU   A 1 271  ? -9.21800   98.43700  46.94800  1.000 34.06152  ?  271  LEU   A O   1 
ATOM   2163  C  CB  . LEU   A 1 271  ? -7.28000   97.31100  44.74900  1.000 35.02472  ?  271  LEU   A CB  1 
ATOM   2164  C  CG  . LEU   A 1 271  ? -7.32100   96.07600  43.84400  1.000 41.21687  ?  271  LEU   A CG  1 
ATOM   2165  C  CD1 . LEU   A 1 271  ? -5.91900   95.57300  43.55100  1.000 32.59688  ?  271  LEU   A CD1 1 
ATOM   2166  C  CD2 . LEU   A 1 271  ? -8.16900   94.97700  44.47500  1.000 43.78388  ?  271  LEU   A CD2 1 
ATOM   2167  N  N   . ALA   A 1 272  ? -8.24500   100.24300 46.01700  1.000 38.71377  ?  272  ALA   A N   1 
ATOM   2168  C  CA  . ALA   A 1 272  ? -8.41400   101.04200 47.22600  1.000 40.91134  ?  272  ALA   A CA  1 
ATOM   2169  C  C   . ALA   A 1 272  ? -9.88300   101.35100 47.48600  1.000 53.67559  ?  272  ALA   A C   1 
ATOM   2170  O  O   . ALA   A 1 272  ? -10.33500  101.30800 48.63600  1.000 62.64297  ?  272  ALA   A O   1 
ATOM   2171  C  CB  . ALA   A 1 272  ? -7.60800   102.33600 47.12200  1.000 49.45656  ?  272  ALA   A CB  1 
ATOM   2172  N  N   . VAL   A 1 273  ? -10.64000  101.67500 46.43400  1.000 46.60525  ?  273  VAL   A N   1 
ATOM   2173  C  CA  . VAL   A 1 273  ? -12.05500  101.99700 46.60800  1.000 32.54660  ?  273  VAL   A CA  1 
ATOM   2174  C  C   . VAL   A 1 273  ? -12.80400  100.79500 47.17000  1.000 34.85871  ?  273  VAL   A C   1 
ATOM   2175  O  O   . VAL   A 1 273  ? -13.58000  100.91300 48.12500  1.000 51.33117  ?  273  VAL   A O   1 
ATOM   2176  C  CB  . VAL   A 1 273  ? -12.67300  102.46700 45.28000  1.000 38.58783  ?  273  VAL   A CB  1 
ATOM   2177  C  CG1 . VAL   A 1 273  ? -13.96400  103.21600 45.54400  1.000 47.35081  ?  273  VAL   A CG1 1 
ATOM   2178  C  CG2 . VAL   A 1 273  ? -11.70000  103.33800 44.50900  1.000 28.01087  ?  273  VAL   A CG2 1 
ATOM   2179  N  N   . MET   A 1 274  ? -12.57500  99.61900  46.58400  1.000 28.47092  ?  274  MET   A N   1 
ATOM   2180  C  CA  . MET   A 1 274  ? -13.28100  98.41900  47.02000  1.000 54.86055  ?  274  MET   A CA  1 
ATOM   2181  C  C   . MET   A 1 274  ? -12.90500  98.03800  48.44500  1.000 45.07295  ?  274  MET   A C   1 
ATOM   2182  O  O   . MET   A 1 274  ? -13.76200  97.60500  49.22500  1.000 50.44406  ?  274  MET   A O   1 
ATOM   2183  C  CB  . MET   A 1 274  ? -12.97800  97.26700  46.06600  1.000 43.75073  ?  274  MET   A CB  1 
ATOM   2184  C  CG  . MET   A 1 274  ? -13.07000  97.63800  44.59600  1.000 58.29350  ?  274  MET   A CG  1 
ATOM   2185  S  SD  . MET   A 1 274  ? -12.53300  96.27800  43.54300  1.000 56.18100  ?  274  MET   A SD  1 
ATOM   2186  C  CE  . MET   A 1 274  ? -12.67700  94.92100  44.69800  1.000 42.20310  ?  274  MET   A CE  1 
ATOM   2187  N  N   . LYS   A 1 275  ? -11.62600  98.18000  48.80000  1.000 52.76804  ?  275  LYS   A N   1 
ATOM   2188  C  CA  . LYS   A 1 275  ? -11.19500  97.86700  50.15800  1.000 53.98909  ?  275  LYS   A CA  1 
ATOM   2189  C  C   . LYS   A 1 275  ? -11.79900  98.83800  51.16400  1.000 45.36250  ?  275  LYS   A C   1 
ATOM   2190  O  O   . LYS   A 1 275  ? -12.20400  98.43300  52.25900  1.000 47.59694  ?  275  LYS   A O   1 
ATOM   2191  C  CB  . LYS   A 1 275  ? -9.67000   97.88300  50.24000  1.000 49.95579  ?  275  LYS   A CB  1 
ATOM   2192  C  CG  . LYS   A 1 275  ? -9.01100   96.62500  49.70100  1.000 49.47473  ?  275  LYS   A CG  1 
ATOM   2193  C  CD  . LYS   A 1 275  ? -7.59000   96.89900  49.24300  1.000 42.69485  ?  275  LYS   A CD  1 
ATOM   2194  C  CE  . LYS   A 1 275  ? -6.90600   95.62400  48.78900  1.000 31.02541  ?  275  LYS   A CE  1 
ATOM   2195  N  NZ  . LYS   A 1 275  ? -6.64900   94.71300  49.93700  1.000 35.91389  ?  275  LYS   A NZ  1 
ATOM   2196  N  N   . ALA   A 1 276  ? -11.86600  100.12500 50.81000  1.000 36.65410  ?  276  ALA   A N   1 
ATOM   2197  C  CA  . ALA   A 1 276  ? -12.53000  101.09100 51.67600  1.000 35.70016  ?  276  ALA   A CA  1 
ATOM   2198  C  C   . ALA   A 1 276  ? -14.01000  100.77200 51.82900  1.000 51.78936  ?  276  ALA   A C   1 
ATOM   2199  O  O   . ALA   A 1 276  ? -14.59600  101.03500 52.88500  1.000 64.22900  ?  276  ALA   A O   1 
ATOM   2200  C  CB  . ALA   A 1 276  ? -12.34000  102.50600 51.12800  1.000 46.38179  ?  276  ALA   A CB  1 
ATOM   2201  N  N   . GLY   A 1 277  ? -14.62800  100.20400 50.79400  1.000 54.60434  ?  277  GLY   A N   1 
ATOM   2202  C  CA  . GLY   A 1 277  ? -16.01200  99.78100  50.87500  1.000 39.22618  ?  277  GLY   A CA  1 
ATOM   2203  C  C   . GLY   A 1 277  ? -16.87800  100.23100 49.71600  1.000 44.34509  ?  277  GLY   A C   1 
ATOM   2204  O  O   . GLY   A 1 277  ? -18.00200  99.74600  49.55500  1.000 55.44962  ?  277  GLY   A O   1 
ATOM   2205  N  N   . GLY   A 1 278  ? -16.36700  101.14600 48.89100  1.000 39.34396  ?  278  GLY   A N   1 
ATOM   2206  C  CA  . GLY   A 1 278  ? -17.14700  101.76600 47.84400  1.000 52.44283  ?  278  GLY   A CA  1 
ATOM   2207  C  C   . GLY   A 1 278  ? -16.96000  101.11600 46.48300  1.000 47.37155  ?  278  GLY   A C   1 
ATOM   2208  O  O   . GLY   A 1 278  ? -16.33900  100.06200 46.33300  1.000 40.29554  ?  278  GLY   A O   1 
ATOM   2209  N  N   . ALA   A 1 279  ? -17.52700  101.77400 45.47300  1.000 39.03456  ?  279  ALA   A N   1 
ATOM   2210  C  CA  . ALA   A 1 279  ? -17.45100  101.34500 44.08400  1.000 38.61600  ?  279  ALA   A CA  1 
ATOM   2211  C  C   . ALA   A 1 279  ? -16.79300  102.44100 43.25900  1.000 41.33492  ?  279  ALA   A C   1 
ATOM   2212  O  O   . ALA   A 1 279  ? -17.03500  103.63000 43.48800  1.000 48.56794  ?  279  ALA   A O   1 
ATOM   2213  C  CB  . ALA   A 1 279  ? -18.84100  101.03100 43.52500  1.000 44.23473  ?  279  ALA   A CB  1 
ATOM   2214  N  N   . TYR   A 1 280  ? -15.96300  102.04600 42.29700  1.000 34.46390  ?  280  TYR   A N   1 
ATOM   2215  C  CA  . TYR   A 1 280  ? -15.19500  103.01400 41.52800  1.000 39.32569  ?  280  TYR   A CA  1 
ATOM   2216  C  C   . TYR   A 1 280  ? -15.92700  103.38800 40.24500  1.000 37.28623  ?  280  TYR   A C   1 
ATOM   2217  O  O   . TYR   A 1 280  ? -16.48000  102.52900 39.55200  1.000 39.34341  ?  280  TYR   A O   1 
ATOM   2218  C  CB  . TYR   A 1 280  ? -13.79100  102.48000 41.21700  1.000 40.21458  ?  280  TYR   A CB  1 
ATOM   2219  C  CG  . TYR   A 1 280  ? -13.70300  101.45200 40.10800  1.000 42.42495  ?  280  TYR   A CG  1 
ATOM   2220  C  CD1 . TYR   A 1 280  ? -13.88200  100.09800 40.36900  1.000 26.00286  ?  280  TYR   A CD1 1 
ATOM   2221  C  CD2 . TYR   A 1 280  ? -13.40900  101.83400 38.80500  1.000 35.58823  ?  280  TYR   A CD2 1 
ATOM   2222  C  CE1 . TYR   A 1 280  ? -13.78700  99.15700  39.35700  1.000 20.82498  ?  280  TYR   A CE1 1 
ATOM   2223  C  CE2 . TYR   A 1 280  ? -13.31600  100.90300 37.78900  1.000 35.69450  ?  280  TYR   A CE2 1 
ATOM   2224  C  CZ  . TYR   A 1 280  ? -13.50500  99.56700  38.07000  1.000 24.68223  ?  280  TYR   A CZ  1 
ATOM   2225  O  OH  . TYR   A 1 280  ? -13.41000  98.64000  37.05700  1.000 37.01621  ?  280  TYR   A OH  1 
ATOM   2226  N  N   . VAL   A 1 281  ? -15.93900  104.68400 39.94700  1.000 31.84480  ?  281  VAL   A N   1 
ATOM   2227  C  CA  . VAL   A 1 281  ? -16.58200  105.21100 38.74700  1.000 34.12819  ?  281  VAL   A CA  1 
ATOM   2228  C  C   . VAL   A 1 281  ? -15.49900  105.71100 37.79900  1.000 41.40185  ?  281  VAL   A C   1 
ATOM   2229  O  O   . VAL   A 1 281  ? -14.98800  106.82700 37.97300  1.000 44.33565  ?  281  VAL   A O   1 
ATOM   2230  C  CB  . VAL   A 1 281  ? -17.58000  106.32800 39.09000  1.000 40.83971  ?  281  VAL   A CB  1 
ATOM   2231  C  CG1 . VAL   A 1 281  ? -18.31200  106.78800 37.83700  1.000 45.56414  ?  281  VAL   A CG1 1 
ATOM   2232  C  CG2 . VAL   A 1 281  ? -18.56300  105.85200 40.14700  1.000 43.66941  ?  281  VAL   A CG2 1 
ATOM   2233  N  N   . PRO   A 1 282  ? -15.12200  104.92900 36.78900  1.000 31.01454  ?  282  PRO   A N   1 
ATOM   2234  C  CA  . PRO   A 1 282  ? -14.01800  105.33300 35.90900  1.000 29.37814  ?  282  PRO   A CA  1 
ATOM   2235  C  C   . PRO   A 1 282  ? -14.40200  106.51600 35.03000  1.000 36.21216  ?  282  PRO   A C   1 
ATOM   2236  O  O   . PRO   A 1 282  ? -15.42800  106.49600 34.34700  1.000 48.69910  ?  282  PRO   A O   1 
ATOM   2237  C  CB  . PRO   A 1 282  ? -13.75500  104.07600 35.07500  1.000 33.06854  ?  282  PRO   A CB  1 
ATOM   2238  C  CG  . PRO   A 1 282  ? -15.05200  103.33900 35.09400  1.000 48.20537  ?  282  PRO   A CG  1 
ATOM   2239  C  CD  . PRO   A 1 282  ? -15.65300  103.60000 36.44200  1.000 44.44264  ?  282  PRO   A CD  1 
ATOM   2240  N  N   . ILE   A 1 283  ? -13.55800  107.54300 35.04600  1.000 36.61103  ?  283  ILE   A N   1 
ATOM   2241  C  CA  . ILE   A 1 283  ? -13.73500  108.73700 34.22800  1.000 48.88879  ?  283  ILE   A CA  1 
ATOM   2242  C  C   . ILE   A 1 283  ? -12.50900  108.87800 33.33800  1.000 48.08970  ?  283  ILE   A C   1 
ATOM   2243  O  O   . ILE   A 1 283  ? -11.38200  108.98200 33.83700  1.000 37.87650  ?  283  ILE   A O   1 
ATOM   2244  C  CB  . ILE   A 1 283  ? -13.93800  109.99200 35.09000  1.000 33.76136  ?  283  ILE   A CB  1 
ATOM   2245  C  CG1 . ILE   A 1 283  ? -15.29000  109.92600 35.79900  1.000 37.14568  ?  283  ILE   A CG1 1 
ATOM   2246  C  CG2 . ILE   A 1 283  ? -13.83000  111.25100 34.24100  1.000 45.30676  ?  283  ILE   A CG2 1 
ATOM   2247  C  CD1 . ILE   A 1 283  ? -15.49400  111.02100 36.80700  1.000 59.75841  ?  283  ILE   A CD1 1 
ATOM   2248  N  N   . ASP   A 1 284  ? -12.72700  108.87900 32.02900  1.000 50.70238  ?  284  ASP   A N   1 
ATOM   2249  C  CA  . ASP   A 1 284  ? -11.61400  108.99800 31.09400  1.000 50.65212  ?  284  ASP   A CA  1 
ATOM   2250  C  C   . ASP   A 1 284  ? -11.04300  110.41100 31.14600  1.000 53.96857  ?  284  ASP   A C   1 
ATOM   2251  O  O   . ASP   A 1 284  ? -11.79500  111.38400 31.01400  1.000 57.59488  ?  284  ASP   A O   1 
ATOM   2252  C  CB  . ASP   A 1 284  ? -12.06700  108.66200 29.67600  1.000 53.56244  ?  284  ASP   A CB  1 
ATOM   2253  C  CG  . ASP   A 1 284  ? -10.90600  108.53200 28.71100  1.000 69.99184  ?  284  ASP   A CG  1 
ATOM   2254  O  OD1 . ASP   A 1 284  ? -10.21700  107.49000 28.74600  1.000 74.40581  ?  284  ASP   A OD1 1 
ATOM   2255  O  OD2 . ASP   A 1 284  ? -10.68000  109.47100 27.91900  1.000 76.56314  -1 284  ASP   A OD2 1 
ATOM   2256  N  N   . PRO   A 1 285  ? -9.72800   110.56800 31.33200  1.000 47.80459  ?  285  PRO   A N   1 
ATOM   2257  C  CA  . PRO   A 1 285  ? -9.14400   111.91700 31.41000  1.000 49.15979  ?  285  PRO   A CA  1 
ATOM   2258  C  C   . PRO   A 1 285  ? -9.27600   112.72400 30.12800  1.000 59.41409  ?  285  PRO   A C   1 
ATOM   2259  O  O   . PRO   A 1 285  ? -9.07700   113.94600 30.16600  1.000 63.06227  ?  285  PRO   A O   1 
ATOM   2260  C  CB  . PRO   A 1 285  ? -7.66700   111.64300 31.73300  1.000 57.00080  ?  285  PRO   A CB  1 
ATOM   2261  C  CG  . PRO   A 1 285  ? -7.64100   110.25100 32.28800  1.000 58.90497  ?  285  PRO   A CG  1 
ATOM   2262  C  CD  . PRO   A 1 285  ? -8.72100   109.51800 31.55500  1.000 53.29715  ?  285  PRO   A CD  1 
ATOM   2263  N  N   . ASP   A 1 286  ? -9.60100   112.08900 29.00300  1.000 57.24662  ?  286  ASP   A N   1 
ATOM   2264  C  CA  . ASP   A 1 286  ? -9.70100   112.76200 27.71700  1.000 58.07589  ?  286  ASP   A CA  1 
ATOM   2265  C  C   . ASP   A 1 286  ? -11.13200  113.12100 27.34200  1.000 72.63056  ?  286  ASP   A C   1 
ATOM   2266  O  O   . ASP   A 1 286  ? -11.34800  113.71800 26.28200  1.000 71.27260  ?  286  ASP   A O   1 
ATOM   2267  C  CB  . ASP   A 1 286  ? -9.08700   111.88400 26.62000  1.000 63.31854  ?  286  ASP   A CB  1 
ATOM   2268  C  CG  . ASP   A 1 286  ? -7.73000   111.32900 27.01100  1.000 82.08660  ?  286  ASP   A CG  1 
ATOM   2269  O  OD1 . ASP   A 1 286  ? -6.82100   112.13000 27.31600  1.000 78.60633  ?  286  ASP   A OD1 1 
ATOM   2270  O  OD2 . ASP   A 1 286  ? -7.57900   110.08800 27.02700  1.000 74.47512  -1 286  ASP   A OD2 1 
ATOM   2271  N  N   . TYR   A 1 287  ? -12.11300  112.77000 28.17900  1.000 81.38184  ?  287  TYR   A N   1 
ATOM   2272  C  CA  . TYR   A 1 287  ? -13.50300  113.08200 27.88500  1.000 73.78850  ?  287  TYR   A CA  1 
ATOM   2273  C  C   . TYR   A 1 287  ? -13.71300  114.59400 27.85100  1.000 62.48323  ?  287  TYR   A C   1 
ATOM   2274  O  O   . TYR   A 1 287  ? -12.90800  115.35600 28.39200  1.000 71.06399  ?  287  TYR   A O   1 
ATOM   2275  C  CB  . TYR   A 1 287  ? -14.42800  112.45200 28.92900  1.000 58.20191  ?  287  TYR   A CB  1 
ATOM   2276  C  CG  . TYR   A 1 287  ? -14.76900  111.00000 28.67100  1.000 50.84251  ?  287  TYR   A CG  1 
ATOM   2277  C  CD1 . TYR   A 1 287  ? -14.49400  110.40700 27.44700  1.000 61.38766  ?  287  TYR   A CD1 1 
ATOM   2278  C  CD2 . TYR   A 1 287  ? -15.37500  110.22600 29.65200  1.000 47.16670  ?  287  TYR   A CD2 1 
ATOM   2279  C  CE1 . TYR   A 1 287  ? -14.80600  109.08100 27.20800  1.000 59.71502  ?  287  TYR   A CE1 1 
ATOM   2280  C  CE2 . TYR   A 1 287  ? -15.69100  108.90000 29.42300  1.000 53.72344  ?  287  TYR   A CE2 1 
ATOM   2281  C  CZ  . TYR   A 1 287  ? -15.40500  108.33300 28.20000  1.000 55.94478  ?  287  TYR   A CZ  1 
ATOM   2282  O  OH  . TYR   A 1 287  ? -15.71900  107.01300 27.97100  1.000 65.74051  ?  287  TYR   A OH  1 
ATOM   2283  N  N   . PRO   A 1 288  ? -14.77800  115.05300 27.19400  1.000 63.25528  ?  288  PRO   A N   1 
ATOM   2284  C  CA  . PRO   A 1 288  ? -15.12800  116.47500 27.27400  1.000 58.81702  ?  288  PRO   A CA  1 
ATOM   2285  C  C   . PRO   A 1 288  ? -15.41000  116.88900 28.71100  1.000 67.97679  ?  288  PRO   A C   1 
ATOM   2286  O  O   . PRO   A 1 288  ? -15.83500  116.08200 29.54200  1.000 71.09169  ?  288  PRO   A O   1 
ATOM   2287  C  CB  . PRO   A 1 288  ? -16.38300  116.58200 26.40100  1.000 71.81323  ?  288  PRO   A CB  1 
ATOM   2288  C  CG  . PRO   A 1 288  ? -16.25500  115.45400 25.43100  1.000 81.73202  ?  288  PRO   A CG  1 
ATOM   2289  C  CD  . PRO   A 1 288  ? -15.58800  114.34000 26.19000  1.000 73.37149  ?  288  PRO   A CD  1 
ATOM   2290  N  N   . GLY   A 1 289  ? -15.15500  118.16700 28.99900  1.000 59.09165  ?  289  GLY   A N   1 
ATOM   2291  C  CA  . GLY   A 1 289  ? -15.33800  118.66100 30.35600  1.000 67.46984  ?  289  GLY   A CA  1 
ATOM   2292  C  C   . GLY   A 1 289  ? -16.77000  118.53700 30.83900  1.000 75.75851  ?  289  GLY   A C   1 
ATOM   2293  O  O   . GLY   A 1 289  ? -17.01700  118.21600 32.00500  1.000 70.76978  ?  289  GLY   A O   1 
ATOM   2294  N  N   . GLU   A 1 290  ? -17.73400  118.79200 29.95100  1.000 73.53292  ?  290  GLU   A N   1 
ATOM   2295  C  CA  . GLU   A 1 290  ? -19.13600  118.62700 30.31700  1.000 60.17748  ?  290  GLU   A CA  1 
ATOM   2296  C  C   . GLU   A 1 290  ? -19.46400  117.16500 30.59100  1.000 62.54544  ?  290  GLU   A C   1 
ATOM   2297  O  O   . GLU   A 1 290  ? -20.27000  116.86000 31.47800  1.000 63.24584  ?  290  GLU   A O   1 
ATOM   2298  C  CB  . GLU   A 1 290  ? -20.03700  119.18400 29.21400  1.000 62.39209  ?  290  GLU   A CB  1 
ATOM   2299  N  N   . ARG   A 1 291  ? -18.85100  116.24600 29.84200  1.000 65.90141  ?  291  ARG   A N   1 
ATOM   2300  C  CA  . ARG   A 1 291  ? -19.06900  114.82800 30.10200  1.000 64.98526  ?  291  ARG   A CA  1 
ATOM   2301  C  C   . ARG   A 1 291  ? -18.49800  114.43200 31.45800  1.000 70.04369  ?  291  ARG   A C   1 
ATOM   2302  O  O   . ARG   A 1 291  ? -19.15700  113.74000 32.24200  1.000 74.29202  ?  291  ARG   A O   1 
ATOM   2303  C  CB  . ARG   A 1 291  ? -18.45400  113.98200 28.98800  1.000 55.48055  ?  291  ARG   A CB  1 
ATOM   2304  C  CG  . ARG   A 1 291  ? -19.15200  112.64500 28.79000  1.000 55.14143  ?  291  ARG   A CG  1 
ATOM   2305  C  CD  . ARG   A 1 291  ? -18.35300  111.70700 27.90000  1.000 58.45028  ?  291  ARG   A CD  1 
ATOM   2306  N  NE  . ARG   A 1 291  ? -19.12000  110.51800 27.54400  1.000 84.60002  ?  291  ARG   A NE  1 
ATOM   2307  C  CZ  . ARG   A 1 291  ? -19.33800  109.49300 28.35700  1.000 86.60837  ?  291  ARG   A CZ  1 
ATOM   2308  N  NH1 . ARG   A 1 291  ? -18.86300  109.47500 29.59100  1.000 77.39537  ?  291  ARG   A NH1 1 
ATOM   2309  N  NH2 . ARG   A 1 291  ? -20.05800  108.46200 27.92200  1.000 77.67688  ?  291  ARG   A NH2 1 
ATOM   2310  N  N   . ILE   A 1 292  ? -17.27200  114.87600 31.75400  1.000 55.09286  ?  292  ILE   A N   1 
ATOM   2311  C  CA  . ILE   A 1 292  ? -16.64700  114.57700 33.04100  1.000 60.74794  ?  292  ILE   A CA  1 
ATOM   2312  C  C   . ILE   A 1 292  ? -17.52500  115.05700 34.19000  1.000 61.20900  ?  292  ILE   A C   1 
ATOM   2313  O  O   . ILE   A 1 292  ? -17.72800  114.34100 35.17900  1.000 57.03719  ?  292  ILE   A O   1 
ATOM   2314  C  CB  . ILE   A 1 292  ? -15.24300  115.20500 33.10200  1.000 65.43746  ?  292  ILE   A CB  1 
ATOM   2315  C  CG1 . ILE   A 1 292  ? -14.27500  114.41600 32.22200  1.000 73.40063  ?  292  ILE   A CG1 1 
ATOM   2316  C  CG2 . ILE   A 1 292  ? -14.73900  115.28700 34.54000  1.000 44.51295  ?  292  ILE   A CG2 1 
ATOM   2317  C  CD1 . ILE   A 1 292  ? -13.23100  115.27600 31.56200  1.000 58.69400  ?  292  ILE   A CD1 1 
ATOM   2318  N  N   . ALA   A 1 293  ? -18.07300  116.26800 34.07000  1.000 58.28893  ?  293  ALA   A N   1 
ATOM   2319  C  CA  . ALA   A 1 293  ? -18.88800  116.82000 35.14700  1.000 52.84136  ?  293  ALA   A CA  1 
ATOM   2320  C  C   . ALA   A 1 293  ? -20.20700  116.06900 35.29200  1.000 51.15294  ?  293  ALA   A C   1 
ATOM   2321  O  O   . ALA   A 1 293  ? -20.69100  115.87000 36.41200  1.000 42.83594  ?  293  ALA   A O   1 
ATOM   2322  C  CB  . ALA   A 1 293  ? -19.13800  118.30800 34.90700  1.000 42.95803  ?  293  ALA   A CB  1 
ATOM   2323  N  N   . TYR   A 1 294  ? -20.80700  115.65000 34.17400  1.000 56.08699  ?  294  TYR   A N   1 
ATOM   2324  C  CA  . TYR   A 1 294  ? -22.05000  114.88900 34.25400  1.000 52.92113  ?  294  TYR   A CA  1 
ATOM   2325  C  C   . TYR   A 1 294  ? -21.84500  113.57900 34.99900  1.000 59.90755  ?  294  TYR   A C   1 
ATOM   2326  O  O   . TYR   A 1 294  ? -22.66400  113.20100 35.84500  1.000 57.70248  ?  294  TYR   A O   1 
ATOM   2327  C  CB  . TYR   A 1 294  ? -22.60700  114.61200 32.85800  1.000 52.51271  ?  294  TYR   A CB  1 
ATOM   2328  C  CG  . TYR   A 1 294  ? -23.66800  113.53200 32.86100  1.000 65.56595  ?  294  TYR   A CG  1 
ATOM   2329  C  CD1 . TYR   A 1 294  ? -24.91600  113.76100 33.42500  1.000 71.91575  ?  294  TYR   A CD1 1 
ATOM   2330  C  CD2 . TYR   A 1 294  ? -23.41600  112.27800 32.31500  1.000 64.75753  ?  294  TYR   A CD2 1 
ATOM   2331  C  CE1 . TYR   A 1 294  ? -25.88600  112.77700 33.44000  1.000 67.60949  ?  294  TYR   A CE1 1 
ATOM   2332  C  CE2 . TYR   A 1 294  ? -24.38200  111.28800 32.32400  1.000 63.63584  ?  294  TYR   A CE2 1 
ATOM   2333  C  CZ  . TYR   A 1 294  ? -25.61600  111.54400 32.88800  1.000 64.89164  ?  294  TYR   A CZ  1 
ATOM   2334  O  OH  . TYR   A 1 294  ? -26.58300  110.56400 32.90200  1.000 69.91406  ?  294  TYR   A OH  1 
ATOM   2335  N  N   . MET   A 1 295  ? -20.75800  112.87100 34.69200  1.000 54.40504  ?  295  MET   A N   1 
ATOM   2336  C  CA  . MET   A 1 295  ? -20.48400  111.60800 35.36500  1.000 49.00312  ?  295  MET   A CA  1 
ATOM   2337  C  C   . MET   A 1 295  ? -20.26100  111.81900 36.85500  1.000 52.52341  ?  295  MET   A C   1 
ATOM   2338  O  O   . MET   A 1 295  ? -20.74400  111.03600 37.67900  1.000 59.33217  ?  295  MET   A O   1 
ATOM   2339  C  CB  . MET   A 1 295  ? -19.27800  110.93300 34.71800  1.000 43.11392  ?  295  MET   A CB  1 
ATOM   2340  C  CG  . MET   A 1 295  ? -19.39400  110.84800 33.20400  1.000 55.29509  ?  295  MET   A CG  1 
ATOM   2341  S  SD  . MET   A 1 295  ? -18.28900  109.63100 32.47900  1.000 67.49112  ?  295  MET   A SD  1 
ATOM   2342  C  CE  . MET   A 1 295  ? -18.54200  108.28500 33.63000  1.000 62.01335  ?  295  MET   A CE  1 
ATOM   2343  N  N   . LEU   A 1 296  ? -19.54300  112.88300 37.22200  1.000 46.76983  ?  296  LEU   A N   1 
ATOM   2344  C  CA  . LEU   A 1 296  ? -19.33300  113.18100 38.63400  1.000 51.95870  ?  296  LEU   A CA  1 
ATOM   2345  C  C   . LEU   A 1 296  ? -20.63600  113.57100 39.32000  1.000 50.00477  ?  296  LEU   A C   1 
ATOM   2346  O  O   . LEU   A 1 296  ? -20.90500  113.13800 40.44600  1.000 54.51343  ?  296  LEU   A O   1 
ATOM   2347  C  CB  . LEU   A 1 296  ? -18.29600  114.29200 38.78800  1.000 53.06008  ?  296  LEU   A CB  1 
ATOM   2348  C  CG  . LEU   A 1 296  ? -16.83600  113.86000 38.67400  1.000 44.67648  ?  296  LEU   A CG  1 
ATOM   2349  C  CD1 . LEU   A 1 296  ? -15.90900  115.06200 38.75600  1.000 47.16014  ?  296  LEU   A CD1 1 
ATOM   2350  C  CD2 . LEU   A 1 296  ? -16.51500  112.85600 39.76500  1.000 41.18504  ?  296  LEU   A CD2 1 
ATOM   2351  N  N   . ALA   A 1 297  ? -21.45700  114.39000 38.65700  1.000 63.84980  ?  297  ALA   A N   1 
ATOM   2352  C  CA  . ALA   A 1 297  ? -22.72000  114.81000 39.25600  1.000 68.26897  ?  297  ALA   A CA  1 
ATOM   2353  C  C   . ALA   A 1 297  ? -23.68900  113.64200 39.38300  1.000 67.68870  ?  297  ALA   A C   1 
ATOM   2354  O  O   . ALA   A 1 297  ? -24.37200  113.50300 40.40500  1.000 67.06143  ?  297  ALA   A O   1 
ATOM   2355  C  CB  . ALA   A 1 297  ? -23.34300  115.93700 38.43300  1.000 64.88932  ?  297  ALA   A CB  1 
ATOM   2356  N  N   . ASP   A 1 298  ? -23.76200  112.79000 38.35800  1.000 51.74726  ?  298  ASP   A N   1 
ATOM   2357  C  CA  . ASP   A 1 298  ? -24.68300  111.66000 38.41300  1.000 60.93899  ?  298  ASP   A CA  1 
ATOM   2358  C  C   . ASP   A 1 298  ? -24.20200  110.60200 39.40000  1.000 67.56140  ?  298  ASP   A C   1 
ATOM   2359  O  O   . ASP   A 1 298  ? -25.01100  110.00700 40.12200  1.000 74.72823  ?  298  ASP   A O   1 
ATOM   2360  C  CB  . ASP   A 1 298  ? -24.86400  111.06200 37.01800  1.000 55.73422  ?  298  ASP   A CB  1 
ATOM   2361  C  CG  . ASP   A 1 298  ? -26.09700  110.18600 36.91600  1.000 72.91251  ?  298  ASP   A CG  1 
ATOM   2362  O  OD1 . ASP   A 1 298  ? -27.19500  110.66100 37.27900  1.000 72.67076  ?  298  ASP   A OD1 1 
ATOM   2363  O  OD2 . ASP   A 1 298  ? -25.97400  109.02700 36.46500  1.000 69.17784  -1 298  ASP   A OD2 1 
ATOM   2364  N  N   . SER   A 1 299  ? -22.88900  110.35900 39.45500  1.000 61.02118  ?  299  SER   A N   1 
ATOM   2365  C  CA  . SER   A 1 299  ? -22.35200  109.37100 40.38400  1.000 63.75940  ?  299  SER   A CA  1 
ATOM   2366  C  C   . SER   A 1 299  ? -22.45600  109.80800 41.83700  1.000 64.04495  ?  299  SER   A C   1 
ATOM   2367  O  O   . SER   A 1 299  ? -22.27800  108.96900 42.72600  1.000 58.04629  ?  299  SER   A O   1 
ATOM   2368  C  CB  . SER   A 1 299  ? -20.88800  109.06900 40.05400  1.000 54.19374  ?  299  SER   A CB  1 
ATOM   2369  O  OG  . SER   A 1 299  ? -20.08300  110.22500 40.21400  1.000 56.52458  ?  299  SER   A OG  1 
ATOM   2370  N  N   . SER   A 1 300  ? -22.73900  111.08400 42.09500  1.000 61.85501  ?  300  SER   A N   1 
ATOM   2371  C  CA  . SER   A 1 300  ? -22.79300  111.63200 43.44800  1.000 58.78882  ?  300  SER   A CA  1 
ATOM   2372  C  C   . SER   A 1 300  ? -21.51600  111.28900 44.21400  1.000 58.64113  ?  300  SER   A C   1 
ATOM   2373  O  O   . SER   A 1 300  ? -21.53400  110.69100 45.29000  1.000 69.97952  ?  300  SER   A O   1 
ATOM   2374  C  CB  . SER   A 1 300  ? -24.03900  111.14000 44.18900  1.000 76.89590  ?  300  SER   A CB  1 
ATOM   2375  O  OG  . SER   A 1 300  ? -25.22000  111.68400 43.62300  1.000 83.76551  ?  300  SER   A OG  1 
ATOM   2376  N  N   . ALA   A 1 301  ? -20.39100  111.67400 43.61800  1.000 63.63868  ?  301  ALA   A N   1 
ATOM   2377  C  CA  . ALA   A 1 301  ? -19.07000  111.37100 44.14900  1.000 48.88175  ?  301  ALA   A CA  1 
ATOM   2378  C  C   . ALA   A 1 301  ? -18.55400  112.55100 44.95900  1.000 61.38970  ?  301  ALA   A C   1 
ATOM   2379  O  O   . ALA   A 1 301  ? -18.64700  113.70100 44.51800  1.000 71.19873  ?  301  ALA   A O   1 
ATOM   2380  C  CB  . ALA   A 1 301  ? -18.09500  111.04400 43.01700  1.000 47.27211  ?  301  ALA   A CB  1 
ATOM   2381  N  N   . ALA   A 1 302  ? -18.01200  112.26400 46.14300  1.000 56.30351  ?  302  ALA   A N   1 
ATOM   2382  C  CA  . ALA   A 1 302  ? -17.39600  113.28800 46.97400  1.000 50.94146  ?  302  ALA   A CA  1 
ATOM   2383  C  C   . ALA   A 1 302  ? -15.87700  113.28900 46.89000  1.000 61.07222  ?  302  ALA   A C   1 
ATOM   2384  O  O   . ALA   A 1 302  ? -15.25400  114.29100 47.25500  1.000 73.34874  ?  302  ALA   A O   1 
ATOM   2385  C  CB  . ALA   A 1 302  ? -17.81400  113.11000 48.43900  1.000 57.62267  ?  302  ALA   A CB  1 
ATOM   2386  N  N   . ILE   A 1 303  ? -15.27700  112.20100 46.41300  1.000 61.68834  ?  303  ILE   A N   1 
ATOM   2387  C  CA  . ILE   A 1 303  ? -13.83000  112.03800 46.37400  1.000 52.52432  ?  303  ILE   A CA  1 
ATOM   2388  C  C   . ILE   A 1 303  ? -13.41800  111.69100 44.95100  1.000 52.55042  ?  303  ILE   A C   1 
ATOM   2389  O  O   . ILE   A 1 303  ? -14.07400  110.88400 44.28300  1.000 39.26143  ?  303  ILE   A O   1 
ATOM   2390  C  CB  . ILE   A 1 303  ? -13.36400  110.94500 47.35700  1.000 52.70455  ?  303  ILE   A CB  1 
ATOM   2391  C  CG1 . ILE   A 1 303  ? -14.01900  111.15000 48.72300  1.000 45.05044  ?  303  ILE   A CG1 1 
ATOM   2392  C  CG2 . ILE   A 1 303  ? -11.85600  110.96000 47.49200  1.000 68.11815  ?  303  ILE   A CG2 1 
ATOM   2393  C  CD1 . ILE   A 1 303  ? -13.99300  109.92700 49.59900  1.000 49.93931  ?  303  ILE   A CD1 1 
ATOM   2394  N  N   . LEU   A 1 304  ? -12.32900  112.30000 44.48900  1.000 54.18530  ?  304  LEU   A N   1 
ATOM   2395  C  CA  . LEU   A 1 304  ? -11.80800  112.07800 43.14600  1.000 48.03167  ?  304  LEU   A CA  1 
ATOM   2396  C  C   . LEU   A 1 304  ? -10.36900  111.59500 43.25100  1.000 57.34970  ?  304  LEU   A C   1 
ATOM   2397  O  O   . LEU   A 1 304  ? -9.51300   112.29800 43.79700  1.000 65.74848  ?  304  LEU   A O   1 
ATOM   2398  C  CB  . LEU   A 1 304  ? -11.89000  113.35600 42.30900  1.000 46.60132  ?  304  LEU   A CB  1 
ATOM   2399  C  CG  . LEU   A 1 304  ? -11.33200  113.28100 40.88600  1.000 39.74389  ?  304  LEU   A CG  1 
ATOM   2400  C  CD1 . LEU   A 1 304  ? -12.02000  112.18000 40.09900  1.000 28.52131  ?  304  LEU   A CD1 1 
ATOM   2401  C  CD2 . LEU   A 1 304  ? -11.48500  114.61900 40.18400  1.000 41.86059  ?  304  LEU   A CD2 1 
ATOM   2402  N  N   . LEU   A 1 305  ? -10.10800  110.39600 42.73300  1.000 50.83069  ?  305  LEU   A N   1 
ATOM   2403  C  CA  . LEU   A 1 305  ? -8.75600   109.84000 42.70200  1.000 46.98940  ?  305  LEU   A CA  1 
ATOM   2404  C  C   . LEU   A 1 305  ? -8.13800   110.18200 41.35200  1.000 41.34066  ?  305  LEU   A C   1 
ATOM   2405  O  O   . LEU   A 1 305  ? -8.23200   109.42200 40.38800  1.000 50.92447  ?  305  LEU   A O   1 
ATOM   2406  C  CB  . LEU   A 1 305  ? -8.77900   108.33800 42.95600  1.000 43.29654  ?  305  LEU   A CB  1 
ATOM   2407  C  CG  . LEU   A 1 305  ? -9.08600   107.89100 44.38800  1.000 41.41721  ?  305  LEU   A CG  1 
ATOM   2408  C  CD1 . LEU   A 1 305  ? -8.97400   106.37900 44.51700  1.000 55.69704  ?  305  LEU   A CD1 1 
ATOM   2409  C  CD2 . LEU   A 1 305  ? -8.15700   108.58300 45.37000  1.000 43.41053  ?  305  LEU   A CD2 1 
ATOM   2410  N  N   . THR   A 1 306  ? -7.50300   111.35000 41.28300  1.000 39.65712  ?  306  THR   A N   1 
ATOM   2411  C  CA  . THR   A 1 306  ? -6.82200   111.82200 40.08500  1.000 51.42992  ?  306  THR   A CA  1 
ATOM   2412  C  C   . THR   A 1 306  ? -5.41700   112.28100 40.46500  1.000 53.29766  ?  306  THR   A C   1 
ATOM   2413  O  O   . THR   A 1 306  ? -5.00800   112.20500 41.62700  1.000 44.62307  ?  306  THR   A O   1 
ATOM   2414  C  CB  . THR   A 1 306  ? -7.60600   112.95500 39.41000  1.000 39.02515  ?  306  THR   A CB  1 
ATOM   2415  O  OG1 . THR   A 1 306  ? -6.97300   113.31000 38.17500  1.000 46.31416  ?  306  THR   A OG1 1 
ATOM   2416  C  CG2 . THR   A 1 306  ? -7.65700   114.17500 40.31300  1.000 36.53554  ?  306  THR   A CG2 1 
ATOM   2417  N  N   . ASN   A 1 307  ? -4.66700   112.76000 39.47200  1.000 43.19275  ?  307  ASN   A N   1 
ATOM   2418  C  CA  . ASN   A 1 307  ? -3.32300   113.26200 39.73000  1.000 42.37085  ?  307  ASN   A CA  1 
ATOM   2419  C  C   . ASN   A 1 307  ? -3.30700   114.78600 39.69600  1.000 62.76180  ?  307  ASN   A C   1 
ATOM   2420  O  O   . ASN   A 1 307  ? -4.26500   115.43100 40.13400  1.000 62.62513  ?  307  ASN   A O   1 
ATOM   2421  C  CB  . ASN   A 1 307  ? -2.32100   112.68300 38.72100  1.000 39.85751  ?  307  ASN   A CB  1 
ATOM   2422  C  CG  . ASN   A 1 307  ? -2.62800   113.07500 37.27900  1.000 64.14556  ?  307  ASN   A CG  1 
ATOM   2423  O  OD1 . ASN   A 1 307  ? -3.51400   113.88700 37.00800  1.000 77.16876  ?  307  ASN   A OD1 1 
ATOM   2424  N  ND2 . ASN   A 1 307  ? -1.87600   112.50300 36.34600  1.000 64.55742  ?  307  ASN   A ND2 1 
ATOM   2425  N  N   . ALA   A 1 308  ? -2.22400   115.36700 39.18200  1.000 61.80714  ?  308  ALA   A N   1 
ATOM   2426  C  CA  . ALA   A 1 308  ? -2.13700   116.80400 38.96900  1.000 57.16501  ?  308  ALA   A CA  1 
ATOM   2427  C  C   . ALA   A 1 308  ? -2.33200   117.20200 37.51300  1.000 67.75223  ?  308  ALA   A C   1 
ATOM   2428  O  O   . ALA   A 1 308  ? -2.46000   118.39700 37.22600  1.000 91.06598  ?  308  ALA   A O   1 
ATOM   2429  C  CB  . ALA   A 1 308  ? -0.78700   117.33600 39.46400  1.000 61.49618  ?  308  ALA   A CB  1 
ATOM   2430  N  N   . LEU   A 1 309  ? -2.34900   116.23800 36.59200  1.000 58.95669  ?  309  LEU   A N   1 
ATOM   2431  C  CA  . LEU   A 1 309  ? -2.59000   116.54900 35.18800  1.000 55.88497  ?  309  LEU   A CA  1 
ATOM   2432  C  C   . LEU   A 1 309  ? -4.08000   116.69700 34.91000  1.000 67.85303  ?  309  LEU   A C   1 
ATOM   2433  O  O   . LEU   A 1 309  ? -4.48800   117.54700 34.11000  1.000 78.24116  ?  309  LEU   A O   1 
ATOM   2434  C  CB  . LEU   A 1 309  ? -1.97900   115.45900 34.30200  1.000 50.45212  ?  309  LEU   A CB  1 
ATOM   2435  C  CG  . LEU   A 1 309  ? -1.44200   115.78900 32.90400  1.000 60.76986  ?  309  LEU   A CG  1 
ATOM   2436  C  CD1 . LEU   A 1 309  ? -0.72600   114.57600 32.32000  1.000 65.23321  ?  309  LEU   A CD1 1 
ATOM   2437  C  CD2 . LEU   A 1 309  ? -2.53800   116.26000 31.95700  1.000 83.28558  ?  309  LEU   A CD2 1 
ATOM   2438  N  N   . HIS   A 1 310  ? -4.90600   115.89100 35.57200  1.000 65.66949  ?  310  HIS   A N   1 
ATOM   2439  C  CA  . HIS   A 1 310  ? -6.34200   115.87200 35.33400  1.000 56.70689  ?  310  HIS   A CA  1 
ATOM   2440  C  C   . HIS   A 1 310  ? -7.13600   116.43000 36.50800  1.000 65.65672  ?  310  HIS   A C   1 
ATOM   2441  O  O   . HIS   A 1 310  ? -8.36000   116.26600 36.55100  1.000 73.13512  ?  310  HIS   A O   1 
ATOM   2442  C  CB  . HIS   A 1 310  ? -6.79600   114.44700 35.01900  1.000 56.85474  ?  310  HIS   A CB  1 
ATOM   2443  C  CG  . HIS   A 1 310  ? -5.83200   113.68100 34.16600  1.000 57.47374  ?  310  HIS   A CG  1 
ATOM   2444  N  ND1 . HIS   A 1 310  ? -5.46000   114.09400 32.90500  1.000 46.43286  ?  310  HIS   A ND1 1 
ATOM   2445  C  CD2 . HIS   A 1 310  ? -5.16700   112.52400 34.39400  1.000 54.72054  ?  310  HIS   A CD2 1 
ATOM   2446  C  CE1 . HIS   A 1 310  ? -4.60600   113.22600 32.39300  1.000 54.72982  ?  310  HIS   A CE1 1 
ATOM   2447  N  NE2 . HIS   A 1 310  ? -4.41100   112.26300 33.27700  1.000 47.13739  ?  310  HIS   A NE2 1 
ATOM   2448  N  N   . GLU   A 1 311  ? -6.46900   117.08400 37.46200  1.000 69.64238  ?  311  GLU   A N   1 
ATOM   2449  C  CA  . GLU   A 1 311  ? -7.16800   117.63000 38.62100  1.000 63.13713  ?  311  GLU   A CA  1 
ATOM   2450  C  C   . GLU   A 1 311  ? -8.04000   118.81700 38.23500  1.000 59.95728  ?  311  GLU   A C   1 
ATOM   2451  O  O   . GLU   A 1 311  ? -9.17100   118.95100 38.71800  1.000 67.07183  ?  311  GLU   A O   1 
ATOM   2452  C  CB  . GLU   A 1 311  ? -6.15300   118.03300 39.69100  1.000 64.15103  ?  311  GLU   A CB  1 
ATOM   2453  C  CG  . GLU   A 1 311  ? -6.73500   118.79700 40.86500  1.000 80.38074  ?  311  GLU   A CG  1 
ATOM   2454  C  CD  . GLU   A 1 311  ? -5.67000   119.21800 41.86000  1.000 92.79950  ?  311  GLU   A CD  1 
ATOM   2455  O  OE1 . GLU   A 1 311  ? -4.51600   118.75700 41.72700  1.000 78.33918  ?  311  GLU   A OE1 1 
ATOM   2456  O  OE2 . GLU   A 1 311  ? -5.98400   120.01200 42.77200  1.000 100.55473 -1 311  GLU   A OE2 1 
ATOM   2457  N  N   . GLU   A 1 312  ? -7.53300   119.68300 37.36200  1.000 73.18282  ?  312  GLU   A N   1 
ATOM   2458  C  CA  . GLU   A 1 312  ? -8.24500   120.87700 36.92900  1.000 69.84372  ?  312  GLU   A CA  1 
ATOM   2459  C  C   . GLU   A 1 312  ? -9.36300   120.57100 35.94300  1.000 69.91463  ?  312  GLU   A C   1 
ATOM   2460  O  O   . GLU   A 1 312  ? -10.06300  121.49700 35.51800  1.000 82.76577  ?  312  GLU   A O   1 
ATOM   2461  C  CB  . GLU   A 1 312  ? -7.25800   121.87400 36.31300  1.000 65.55549  ?  312  GLU   A CB  1 
ATOM   2462  C  CG  . GLU   A 1 312  ? -6.10900   122.28700 37.23700  1.000 80.83442  ?  312  GLU   A CG  1 
ATOM   2463  C  CD  . GLU   A 1 312  ? -5.01300   121.23200 37.34800  1.000 101.57337 ?  312  GLU   A CD  1 
ATOM   2464  O  OE1 . GLU   A 1 312  ? -5.22700   120.08900 36.89000  1.000 96.37189  ?  312  GLU   A OE1 1 
ATOM   2465  O  OE2 . GLU   A 1 312  ? -3.93500   121.54700 37.89600  1.000 99.05523  -1 312  GLU   A OE2 1 
ATOM   2466  N  N   . LYS   A 1 313  ? -9.53900   119.30700 35.56600  1.000 63.08085  ?  313  LYS   A N   1 
ATOM   2467  C  CA  . LYS   A 1 313  ? -10.65800  118.89400 34.73200  1.000 59.40130  ?  313  LYS   A CA  1 
ATOM   2468  C  C   . LYS   A 1 313  ? -11.92300  118.64100 35.54000  1.000 64.80960  ?  313  LYS   A C   1 
ATOM   2469  O  O   . LYS   A 1 313  ? -12.96800  118.34000 34.95200  1.000 64.79208  ?  313  LYS   A O   1 
ATOM   2470  C  CB  . LYS   A 1 313  ? -10.28000  117.64100 33.93800  1.000 56.19835  ?  313  LYS   A CB  1 
ATOM   2471  C  CG  . LYS   A 1 313  ? -9.00700   117.79200 33.11000  1.000 64.18157  ?  313  LYS   A CG  1 
ATOM   2472  C  CD  . LYS   A 1 313  ? -8.74600   116.55600 32.26000  1.000 62.13279  ?  313  LYS   A CD  1 
ATOM   2473  C  CE  . LYS   A 1 313  ? -7.59900   116.77200 31.28100  1.000 63.44101  ?  313  LYS   A CE  1 
ATOM   2474  N  NZ  . LYS   A 1 313  ? -6.27900   116.85900 31.96400  1.000 60.11318  ?  313  LYS   A NZ  1 
ATOM   2475  N  N   . ALA   A 1 314  ? -11.85100  118.75000 36.86700  1.000 67.40472  ?  314  ALA   A N   1 
ATOM   2476  C  CA  . ALA   A 1 314  ? -13.02500  118.62100 37.71800  1.000 71.13148  ?  314  ALA   A CA  1 
ATOM   2477  C  C   . ALA   A 1 314  ? -13.66100  119.96700 38.03300  1.000 71.86108  ?  314  ALA   A C   1 
ATOM   2478  O  O   . ALA   A 1 314  ? -14.88000  120.03700 38.22400  1.000 52.63786  ?  314  ALA   A O   1 
ATOM   2479  C  CB  . ALA   A 1 314  ? -12.65600  117.90800 39.02200  1.000 49.56078  ?  314  ALA   A CB  1 
ATOM   2480  N  N   . ASN   A 1 315  ? -12.86100  121.03500 38.07100  1.000 81.33263  ?  315  ASN   A N   1 
ATOM   2481  C  CA  . ASN   A 1 315  ? -13.33700  122.38600 38.37000  1.000 76.39128  ?  315  ASN   A CA  1 
ATOM   2482  C  C   . ASN   A 1 315  ? -13.95000  122.44800 39.76800  1.000 67.17325  ?  315  ASN   A C   1 
ATOM   2483  O  O   . ASN   A 1 315  ? -15.08900  122.88200 39.95700  1.000 75.81114  ?  315  ASN   A O   1 
ATOM   2484  C  CB  . ASN   A 1 315  ? -14.32900  122.87400 37.30800  1.000 80.74781  ?  315  ASN   A CB  1 
ATOM   2485  C  CG  . ASN   A 1 315  ? -13.87100  122.57000 35.89300  1.000 84.13577  ?  315  ASN   A CG  1 
ATOM   2486  O  OD1 . ASN   A 1 315  ? -12.98700  123.23700 35.35700  1.000 93.51166  ?  315  ASN   A OD1 1 
ATOM   2487  N  ND2 . ASN   A 1 315  ? -14.48200  121.56400 35.27600  1.000 76.16043  ?  315  ASN   A ND2 1 
ATOM   2488  N  N   . GLY   A 1 316  ? -13.17500  122.00500 40.75400  1.000 73.25354  ?  316  GLY   A N   1 
ATOM   2489  C  CA  . GLY   A 1 316  ? -13.64100  122.00300 42.13300  1.000 76.95396  ?  316  GLY   A CA  1 
ATOM   2490  C  C   . GLY   A 1 316  ? -14.88100  121.16600 42.35300  1.000 71.84326  ?  316  GLY   A C   1 
ATOM   2491  O  O   . GLY   A 1 316  ? -15.75500  121.55000 43.14100  1.000 69.71784  ?  316  GLY   A O   1 
ATOM   2492  N  N   . ALA   A 1 317  ? -14.97900  120.02400 41.67300  1.000 77.29370  ?  317  ALA   A N   1 
ATOM   2493  C  CA  . ALA   A 1 317  ? -16.18700  119.21100 41.71800  1.000 61.88861  ?  317  ALA   A CA  1 
ATOM   2494  C  C   . ALA   A 1 317  ? -16.18800  118.17800 42.83300  1.000 77.28542  ?  317  ALA   A C   1 
ATOM   2495  O  O   . ALA   A 1 317  ? -17.26200  117.68200 43.18900  1.000 101.68225 ?  317  ALA   A O   1 
ATOM   2496  C  CB  . ALA   A 1 317  ? -16.39600  118.48900 40.38400  1.000 65.52876  ?  317  ALA   A CB  1 
ATOM   2497  N  N   . CYS   A 1 318  ? -15.02600  117.82100 43.37400  1.000 64.69044  ?  318  CYS   A N   1 
ATOM   2498  C  CA  . CYS   A 1 318  ? -14.94900  116.81700 44.42500  1.000 54.92048  ?  318  CYS   A CA  1 
ATOM   2499  C  C   . CYS   A 1 318  ? -13.77700  117.14800 45.33800  1.000 68.64706  ?  318  CYS   A C   1 
ATOM   2500  O  O   . CYS   A 1 318  ? -13.08400  118.15300 45.15700  1.000 70.96676  ?  318  CYS   A O   1 
ATOM   2501  C  CB  . CYS   A 1 318  ? -14.79000  115.40400 43.84900  1.000 61.55580  ?  318  CYS   A CB  1 
ATOM   2502  S  SG  . CYS   A 1 318  ? -16.11700  114.83300 42.76500  1.000 74.91349  ?  318  CYS   A SG  1 
ATOM   2503  N  N   . ASP   A 1 319  ? -13.56100  116.28500 46.32600  1.000 61.95864  ?  319  ASP   A N   1 
ATOM   2504  C  CA  . ASP   A 1 319  ? -12.36700  116.34700 47.16300  1.000 61.25864  ?  319  ASP   A CA  1 
ATOM   2505  C  C   . ASP   A 1 319  ? -11.25800  115.59800 46.43600  1.000 64.98045  ?  319  ASP   A C   1 
ATOM   2506  O  O   . ASP   A 1 319  ? -11.17000  114.37000 46.50500  1.000 76.58250  ?  319  ASP   A O   1 
ATOM   2507  C  CB  . ASP   A 1 319  ? -12.64000  115.74900 48.53800  1.000 57.37629  ?  319  ASP   A CB  1 
ATOM   2508  C  CG  . ASP   A 1 319  ? -11.45500  115.87500 49.47800  1.000 91.60779  ?  319  ASP   A CG  1 
ATOM   2509  O  OD1 . ASP   A 1 319  ? -10.48900  116.59400 49.14100  1.000 96.18408  ?  319  ASP   A OD1 1 
ATOM   2510  O  OD2 . ASP   A 1 319  ? -11.49100  115.25100 50.55800  1.000 97.26435  -1 319  ASP   A OD2 1 
ATOM   2511  N  N   . ILE   A 1 320  ? -10.41200  116.34100 45.72400  1.000 67.14398  ?  320  ILE   A N   1 
ATOM   2512  C  CA  . ILE   A 1 320  ? -9.34500   115.72900 44.94300  1.000 58.42895  ?  320  ILE   A CA  1 
ATOM   2513  C  C   . ILE   A 1 320  ? -8.33000   115.09100 45.88100  1.000 63.90469  ?  320  ILE   A C   1 
ATOM   2514  O  O   . ILE   A 1 320  ? -7.89000   115.70800 46.86100  1.000 60.72788  ?  320  ILE   A O   1 
ATOM   2515  C  CB  . ILE   A 1 320  ? -8.68500   116.76800 44.02200  1.000 64.23727  ?  320  ILE   A CB  1 
ATOM   2516  C  CG1 . ILE   A 1 320  ? -9.49300   116.94400 42.73200  1.000 61.96545  ?  320  ILE   A CG1 1 
ATOM   2517  C  CG2 . ILE   A 1 320  ? -7.24900   116.37400 43.69800  1.000 69.41580  ?  320  ILE   A CG2 1 
ATOM   2518  C  CD1 . ILE   A 1 320  ? -10.74900  117.77900 42.88400  1.000 74.89358  ?  320  ILE   A CD1 1 
ATOM   2519  N  N   . ILE   A 1 321  ? -7.96400   113.84500 45.59300  1.000 58.01482  ?  321  ILE   A N   1 
ATOM   2520  C  CA  . ILE   A 1 321  ? -6.95000   113.11500 46.34500  1.000 56.72265  ?  321  ILE   A CA  1 
ATOM   2521  C  C   . ILE   A 1 321  ? -5.86200   112.72800 45.35200  1.000 54.19534  ?  321  ILE   A C   1 
ATOM   2522  O  O   . ILE   A 1 321  ? -6.03900   111.80400 44.54800  1.000 58.73195  ?  321  ILE   A O   1 
ATOM   2523  C  CB  . ILE   A 1 321  ? -7.52400   111.88700 47.06000  1.000 42.00870  ?  321  ILE   A CB  1 
ATOM   2524  C  CG1 . ILE   A 1 321  ? -8.48800   112.32600 48.16500  1.000 57.10163  ?  321  ILE   A CG1 1 
ATOM   2525  C  CG2 . ILE   A 1 321  ? -6.40600   111.02700 47.63000  1.000 55.55224  ?  321  ILE   A CG2 1 
ATOM   2526  C  CD1 . ILE   A 1 321  ? -8.75900   111.26100 49.20700  1.000 47.44957  ?  321  ILE   A CD1 1 
ATOM   2527  N  N   . ASP   A 1 322  ? -4.73500   113.43600 45.39800  1.000 53.20582  ?  322  ASP   A N   1 
ATOM   2528  C  CA  . ASP   A 1 322  ? -3.64000   113.17200 44.47400  1.000 57.89088  ?  322  ASP   A CA  1 
ATOM   2529  C  C   . ASP   A 1 322  ? -3.01900   111.81200 44.76700  1.000 57.45002  ?  322  ASP   A C   1 
ATOM   2530  O  O   . ASP   A 1 322  ? -2.63800   111.52300 45.90500  1.000 73.25366  ?  322  ASP   A O   1 
ATOM   2531  C  CB  . ASP   A 1 322  ? -2.58600   114.27500 44.57800  1.000 50.19633  ?  322  ASP   A CB  1 
ATOM   2532  C  CG  . ASP   A 1 322  ? -1.55300   114.20900 43.46500  1.000 56.90203  ?  322  ASP   A CG  1 
ATOM   2533  O  OD1 . ASP   A 1 322  ? -1.62200   113.28600 42.62700  1.000 64.64936  ?  322  ASP   A OD1 1 
ATOM   2534  O  OD2 . ASP   A 1 322  ? -0.66900   115.09100 43.42600  1.000 70.62308  -1 322  ASP   A OD2 1 
ATOM   2535  N  N   . VAL   A 1 323  ? -2.91600   110.97300 43.73100  1.000 53.08601  ?  323  VAL   A N   1 
ATOM   2536  C  CA  . VAL   A 1 323  ? -2.31500   109.65000 43.88900  1.000 45.93296  ?  323  VAL   A CA  1 
ATOM   2537  C  C   . VAL   A 1 323  ? -0.79600   109.69300 43.91200  1.000 44.03920  ?  323  VAL   A C   1 
ATOM   2538  O  O   . VAL   A 1 323  ? -0.16300   108.65800 44.15300  1.000 51.81303  ?  323  VAL   A O   1 
ATOM   2539  C  CB  . VAL   A 1 323  ? -2.78500   108.70200 42.77000  1.000 46.80967  ?  323  VAL   A CB  1 
ATOM   2540  C  CG1 . VAL   A 1 323  ? -4.24200   108.32100 42.98000  1.000 38.88605  ?  323  VAL   A CG1 1 
ATOM   2541  C  CG2 . VAL   A 1 323  ? -2.59700   109.35500 41.41200  1.000 59.15322  ?  323  VAL   A CG2 1 
ATOM   2542  N  N   . HIS   A 1 324  ? -0.19400   110.85400 43.66600  1.000 52.56713  ?  324  HIS   A N   1 
ATOM   2543  C  CA  . HIS   A 1 324  ? 1.24700    111.03100 43.76600  1.000 50.11016  ?  324  HIS   A CA  1 
ATOM   2544  C  C   . HIS   A 1 324  ? 1.65800    111.76000 45.03600  1.000 59.79866  ?  324  HIS   A C   1 
ATOM   2545  O  O   . HIS   A 1 324  ? 2.85700    111.94400 45.27000  1.000 62.10612  ?  324  HIS   A O   1 
ATOM   2546  C  CB  . HIS   A 1 324  ? 1.77400    111.78900 42.54400  1.000 53.88148  ?  324  HIS   A CB  1 
ATOM   2547  C  CG  . HIS   A 1 324  ? 1.48700    111.10800 41.24300  1.000 63.72570  ?  324  HIS   A CG  1 
ATOM   2548  N  ND1 . HIS   A 1 324  ? 0.97600    111.77500 40.15100  1.000 57.33581  ?  324  HIS   A ND1 1 
ATOM   2549  C  CD2 . HIS   A 1 324  ? 1.64300    109.81900 40.85800  1.000 65.53876  ?  324  HIS   A CD2 1 
ATOM   2550  C  CE1 . HIS   A 1 324  ? 0.82600    110.92600 39.15000  1.000 66.98370  ?  324  HIS   A CE1 1 
ATOM   2551  N  NE2 . HIS   A 1 324  ? 1.22400    109.73300 39.55200  1.000 82.38237  ?  324  HIS   A NE2 1 
ATOM   2552  N  N   . ASP   A 1 325  ? 0.69900    112.18100 45.85200  1.000 61.58557  ?  325  ASP   A N   1 
ATOM   2553  C  CA  . ASP   A 1 325  ? 0.99500    112.87700 47.09800  1.000 66.60890  ?  325  ASP   A CA  1 
ATOM   2554  C  C   . ASP   A 1 325  ? 1.13000    111.86800 48.23100  1.000 69.27125  ?  325  ASP   A C   1 
ATOM   2555  O  O   . ASP   A 1 325  ? 0.22000    111.05700 48.44000  1.000 59.96936  ?  325  ASP   A O   1 
ATOM   2556  C  CB  . ASP   A 1 325  ? -0.09900   113.88400 47.42300  1.000 65.55942  ?  325  ASP   A CB  1 
ATOM   2557  C  CG  . ASP   A 1 325  ? 0.36200    114.95500 48.39100  1.000 79.32350  ?  325  ASP   A CG  1 
ATOM   2558  O  OD1 . ASP   A 1 325  ? 0.62700    114.62700 49.56700  1.000 75.21312  ?  325  ASP   A OD1 1 
ATOM   2559  O  OD2 . ASP   A 1 325  ? 0.47200    116.12500 47.96800  1.000 89.95860  -1 325  ASP   A OD2 1 
ATOM   2560  N  N   . PRO   A 1 326  ? 2.24300    111.88200 48.97200  1.000 71.59476  ?  326  PRO   A N   1 
ATOM   2561  C  CA  . PRO   A 1 326  ? 2.43000    110.87800 50.03200  1.000 66.40766  ?  326  PRO   A CA  1 
ATOM   2562  C  C   . PRO   A 1 326  ? 1.43800    111.00500 51.17300  1.000 68.95341  ?  326  PRO   A C   1 
ATOM   2563  O  O   . PRO   A 1 326  ? 1.19200    110.01200 51.86900  1.000 61.60800  ?  326  PRO   A O   1 
ATOM   2564  C  CB  . PRO   A 1 326  ? 3.86500    111.13500 50.50900  1.000 78.84887  ?  326  PRO   A CB  1 
ATOM   2565  C  CG  . PRO   A 1 326  ? 4.11200    112.57200 50.17900  1.000 76.85243  ?  326  PRO   A CG  1 
ATOM   2566  C  CD  . PRO   A 1 326  ? 3.36700    112.83000 48.90000  1.000 72.03866  ?  326  PRO   A CD  1 
ATOM   2567  N  N   . ASP   A 1 327  ? 0.86000    112.18600 51.38800  1.000 71.20926  ?  327  ASP   A N   1 
ATOM   2568  C  CA  . ASP   A 1 327  ? -0.14400   112.35800 52.43100  1.000 70.89565  ?  327  ASP   A CA  1 
ATOM   2569  C  C   . ASP   A 1 327  ? -1.47900   111.72500 52.07200  1.000 68.02474  ?  327  ASP   A C   1 
ATOM   2570  O  O   . ASP   A 1 327  ? -2.39500   111.74000 52.90300  1.000 66.29736  ?  327  ASP   A O   1 
ATOM   2571  C  CB  . ASP   A 1 327  ? -0.33200   113.84500 52.73400  1.000 58.97680  ?  327  ASP   A CB  1 
ATOM   2572  C  CG  . ASP   A 1 327  ? 0.92100    114.48400 53.30300  1.000 87.98195  ?  327  ASP   A CG  1 
ATOM   2573  O  OD1 . ASP   A 1 327  ? 1.71100    113.76800 53.95500  1.000 85.63642  ?  327  ASP   A OD1 1 
ATOM   2574  O  OD2 . ASP   A 1 327  ? 1.11800    115.69900 53.09700  1.000 94.55116  -1 327  ASP   A OD2 1 
ATOM   2575  N  N   . SER   A 1 328  ? -1.61400   111.17800 50.86500  1.000 73.59852  ?  328  SER   A N   1 
ATOM   2576  C  CA  . SER   A 1 328  ? -2.81000   110.45100 50.46600  1.000 67.36711  ?  328  SER   A CA  1 
ATOM   2577  C  C   . SER   A 1 328  ? -2.74700   108.97300 50.82400  1.000 53.30921  ?  328  SER   A C   1 
ATOM   2578  O  O   . SER   A 1 328  ? -3.77500   108.29300 50.75900  1.000 58.28460  ?  328  SER   A O   1 
ATOM   2579  C  CB  . SER   A 1 328  ? -3.04200   110.59600 48.95800  1.000 52.16533  ?  328  SER   A CB  1 
ATOM   2580  O  OG  . SER   A 1 328  ? -3.17700   111.95700 48.58500  1.000 63.28976  ?  328  SER   A OG  1 
ATOM   2581  N  N   . TYR   A 1 329  ? -1.57500   108.46600 51.19300  1.000 52.10138  ?  329  TYR   A N   1 
ATOM   2582  C  CA  . TYR   A 1 329  ? -1.39500   107.07000 51.56100  1.000 53.65784  ?  329  TYR   A CA  1 
ATOM   2583  C  C   . TYR   A 1 329  ? -1.05100   106.96900 53.04000  1.000 54.76349  ?  329  TYR   A C   1 
ATOM   2584  O  O   . TYR   A 1 329  ? -0.22400   107.73200 53.55000  1.000 61.07185  ?  329  TYR   A O   1 
ATOM   2585  C  CB  . TYR   A 1 329  ? -0.29400   106.41500 50.72000  1.000 46.35621  ?  329  TYR   A CB  1 
ATOM   2586  C  CG  . TYR   A 1 329  ? -0.57300   106.43200 49.23400  1.000 45.08809  ?  329  TYR   A CG  1 
ATOM   2587  C  CD1 . TYR   A 1 329  ? -0.22500   107.52900 48.45600  1.000 54.50655  ?  329  TYR   A CD1 1 
ATOM   2588  C  CD2 . TYR   A 1 329  ? -1.19000   105.35600 48.61000  1.000 49.90382  ?  329  TYR   A CD2 1 
ATOM   2589  C  CE1 . TYR   A 1 329  ? -0.48200   107.55400 47.09900  1.000 52.85044  ?  329  TYR   A CE1 1 
ATOM   2590  C  CE2 . TYR   A 1 329  ? -1.45000   105.37100 47.25100  1.000 58.57168  ?  329  TYR   A CE2 1 
ATOM   2591  C  CZ  . TYR   A 1 329  ? -1.09400   106.47300 46.50100  1.000 44.49428  ?  329  TYR   A CZ  1 
ATOM   2592  O  OH  . TYR   A 1 329  ? -1.34900   106.49800 45.14900  1.000 41.09172  ?  329  TYR   A OH  1 
ATOM   2593  N  N   . SER   A 1 330  ? -1.69300   106.02700 53.72300  1.000 56.01601  ?  330  SER   A N   1 
ATOM   2594  C  CA  . SER   A 1 330  ? -1.46200   105.83000 55.14300  1.000 50.97961  ?  330  SER   A CA  1 
ATOM   2595  C  C   . SER   A 1 330  ? -0.18700   105.02200 55.37400  1.000 66.69998  ?  330  SER   A C   1 
ATOM   2596  O  O   . SER   A 1 330  ? 0.45200    104.52600 54.44100  1.000 66.81705  ?  330  SER   A O   1 
ATOM   2597  C  CB  . SER   A 1 330  ? -2.65800   105.12900 55.78500  1.000 52.17110  ?  330  SER   A CB  1 
ATOM   2598  O  OG  . SER   A 1 330  ? -2.39400   104.79900 57.13800  1.000 58.60115  ?  330  SER   A OG  1 
ATOM   2599  N  N   . GLU   A 1 331  ? 0.18800    104.90400 56.64400  1.000 70.50664  ?  331  GLU   A N   1 
ATOM   2600  C  CA  . GLU   A 1 331  ? 1.27700    104.03000 57.05400  1.000 50.16819  ?  331  GLU   A CA  1 
ATOM   2601  C  C   . GLU   A 1 331  ? 0.79800    102.61900 57.36000  1.000 56.87987  ?  331  GLU   A C   1 
ATOM   2602  O  O   . GLU   A 1 331  ? 1.61500    101.76300 57.71600  1.000 67.39626  ?  331  GLU   A O   1 
ATOM   2603  C  CB  . GLU   A 1 331  ? 1.99100    104.61300 58.27800  1.000 49.20189  ?  331  GLU   A CB  1 
ATOM   2604  N  N   . ASN   A 1 332  ? -0.50000   102.35900 57.22600  1.000 50.39717  ?  332  ASN   A N   1 
ATOM   2605  C  CA  . ASN   A 1 332  ? -1.07700   101.05600 57.53500  1.000 54.93674  ?  332  ASN   A CA  1 
ATOM   2606  C  C   . ASN   A 1 332  ? -1.05100   100.20000 56.27400  1.000 53.16213  ?  332  ASN   A C   1 
ATOM   2607  O  O   . ASN   A 1 332  ? -1.83100   100.42800 55.34400  1.000 53.99482  ?  332  ASN   A O   1 
ATOM   2608  C  CB  . ASN   A 1 332  ? -2.50000   101.21100 58.06300  1.000 52.29178  ?  332  ASN   A CB  1 
ATOM   2609  C  CG  . ASN   A 1 332  ? -2.82100   100.23100 59.17500  1.000 67.60423  ?  332  ASN   A CG  1 
ATOM   2610  O  OD1 . ASN   A 1 332  ? -2.91600   99.02400  58.94800  1.000 68.24404  ?  332  ASN   A OD1 1 
ATOM   2611  N  ND2 . ASN   A 1 332  ? -2.99800   100.74900 60.38500  1.000 74.95438  ?  332  ASN   A ND2 1 
ATOM   2612  N  N   . THR   A 1 333  ? -0.15000   99.22100  56.23900  1.000 61.03809  ?  333  THR   A N   1 
ATOM   2613  C  CA  . THR   A 1 333  ? -0.07300   98.27600  55.13500  1.000 48.85785  ?  333  THR   A CA  1 
ATOM   2614  C  C   . THR   A 1 333  ? -0.82600   96.98500  55.42500  1.000 41.51138  ?  333  THR   A C   1 
ATOM   2615  O  O   . THR   A 1 333  ? -0.68400   96.01400  54.67700  1.000 58.96667  ?  333  THR   A O   1 
ATOM   2616  C  CB  . THR   A 1 333  ? 1.38600    97.96400  54.79900  1.000 41.46369  ?  333  THR   A CB  1 
ATOM   2617  O  OG1 . THR   A 1 333  ? 2.03200    97.38900  55.94200  1.000 46.36362  ?  333  THR   A OG1 1 
ATOM   2618  C  CG2 . THR   A 1 333  ? 2.11700    99.23400  54.39200  1.000 35.88978  ?  333  THR   A CG2 1 
ATOM   2619  N  N   . ASN   A 1 334  ? -1.61600   96.95200  56.49300  1.000 48.97528  ?  334  ASN   A N   1 
ATOM   2620  C  CA  . ASN   A 1 334  ? -2.41200   95.78200  56.82900  1.000 51.85487  ?  334  ASN   A CA  1 
ATOM   2621  C  C   . ASN   A 1 334  ? -3.77900   95.86700  56.16500  1.000 69.40572  ?  334  ASN   A C   1 
ATOM   2622  O  O   . ASN   A 1 334  ? -4.31200   96.95600  55.93400  1.000 69.06842  ?  334  ASN   A O   1 
ATOM   2623  C  CB  . ASN   A 1 334  ? -2.57000   95.65100  58.34500  1.000 50.17140  ?  334  ASN   A CB  1 
ATOM   2624  C  CG  . ASN   A 1 334  ? -1.29700   95.18800  59.02600  1.000 77.31577  ?  334  ASN   A CG  1 
ATOM   2625  O  OD1 . ASN   A 1 334  ? -0.52500   94.41000  58.46400  1.000 77.51406  ?  334  ASN   A OD1 1 
ATOM   2626  N  ND2 . ASN   A 1 334  ? -1.07100   95.66400  60.24600  1.000 87.96401  ?  334  ASN   A ND2 1 
ATOM   2627  N  N   . ASN   A 1 335  ? -4.33900   94.70100  55.85000  1.000 68.44717  ?  335  ASN   A N   1 
ATOM   2628  C  CA  . ASN   A 1 335  ? -5.64500   94.64600  55.20700  1.000 50.15183  ?  335  ASN   A CA  1 
ATOM   2629  C  C   . ASN   A 1 335  ? -6.69900   95.32700  56.07000  1.000 66.82508  ?  335  ASN   A C   1 
ATOM   2630  O  O   . ASN   A 1 335  ? -6.75100   95.13400  57.28800  1.000 70.26778  ?  335  ASN   A O   1 
ATOM   2631  C  CB  . ASN   A 1 335  ? -6.04900   93.19600  54.93900  1.000 32.59218  ?  335  ASN   A CB  1 
ATOM   2632  C  CG  . ASN   A 1 335  ? -5.36700   92.61600  53.71800  1.000 42.99808  ?  335  ASN   A CG  1 
ATOM   2633  O  OD1 . ASN   A 1 335  ? -5.10800   93.32300  52.74300  1.000 41.88666  ?  335  ASN   A OD1 1 
ATOM   2634  N  ND2 . ASN   A 1 335  ? -5.07700   91.32100  53.76200  1.000 42.30050  ?  335  ASN   A ND2 1 
ATOM   2635  N  N   . LEU   A 1 336  ? -7.54000   96.13400  55.42900  1.000 65.76649  ?  336  LEU   A N   1 
ATOM   2636  C  CA  . LEU   A 1 336  ? -8.58300   96.83600  56.15300  1.000 56.21903  ?  336  LEU   A CA  1 
ATOM   2637  C  C   . LEU   A 1 336  ? -9.64000   95.85400  56.65700  1.000 54.06924  ?  336  LEU   A C   1 
ATOM   2638  O  O   . LEU   A 1 336  ? -9.82100   94.77400  56.08700  1.000 55.39229  ?  336  LEU   A O   1 
ATOM   2639  C  CB  . LEU   A 1 336  ? -9.24100   97.89300  55.26900  1.000 32.84017  ?  336  LEU   A CB  1 
ATOM   2640  C  CG  . LEU   A 1 336  ? -8.48700   99.21400  55.10800  1.000 53.20148  ?  336  LEU   A CG  1 
ATOM   2641  C  CD1 . LEU   A 1 336  ? -7.55600   99.17600  53.90500  1.000 50.52414  ?  336  LEU   A CD1 1 
ATOM   2642  C  CD2 . LEU   A 1 336  ? -9.45200   100.38700 55.01700  1.000 45.70436  ?  336  LEU   A CD2 1 
ATOM   2643  N  N   . PRO   A 1 337  ? -10.33900  96.20100  57.73600  1.000 53.94928  ?  337  PRO   A N   1 
ATOM   2644  C  CA  . PRO   A 1 337  ? -11.47900  95.38400  58.16400  1.000 57.40444  ?  337  PRO   A CA  1 
ATOM   2645  C  C   . PRO   A 1 337  ? -12.60100  95.45200  57.13900  1.000 54.61765  ?  337  PRO   A C   1 
ATOM   2646  O  O   . PRO   A 1 337  ? -12.85000  96.49600  56.53200  1.000 51.49624  ?  337  PRO   A O   1 
ATOM   2647  C  CB  . PRO   A 1 337  ? -11.89100  96.01900  59.49700  1.000 56.24455  ?  337  PRO   A CB  1 
ATOM   2648  C  CG  . PRO   A 1 337  ? -11.39400  97.42400  59.41200  1.000 58.87394  ?  337  PRO   A CG  1 
ATOM   2649  C  CD  . PRO   A 1 337  ? -10.11500  97.35000  58.63000  1.000 53.27704  ?  337  PRO   A CD  1 
ATOM   2650  N  N   . HIS   A 1 338  ? -13.27800  94.32300  56.95100  1.000 49.84236  ?  338  HIS   A N   1 
ATOM   2651  C  CA  . HIS   A 1 338  ? -14.26700  94.20200  55.88900  1.000 59.67529  ?  338  HIS   A CA  1 
ATOM   2652  C  C   . HIS   A 1 338  ? -15.60300  94.78800  56.32500  1.000 61.24651  ?  338  HIS   A C   1 
ATOM   2653  O  O   . HIS   A 1 338  ? -16.09000  94.51300  57.42700  1.000 63.75749  ?  338  HIS   A O   1 
ATOM   2654  C  CB  . HIS   A 1 338  ? -14.43000  92.73900  55.47800  1.000 48.92717  ?  338  HIS   A CB  1 
ATOM   2655  C  CG  . HIS   A 1 338  ? -13.26500  92.20300  54.70700  1.000 79.98181  ?  338  HIS   A CG  1 
ATOM   2656  N  ND1 . HIS   A 1 338  ? -12.29700  93.02000  54.16400  1.000 84.62493  ?  338  HIS   A ND1 1 
ATOM   2657  C  CD2 . HIS   A 1 338  ? -12.91100  90.93600  54.38700  1.000 70.41294  ?  338  HIS   A CD2 1 
ATOM   2658  C  CE1 . HIS   A 1 338  ? -11.39700  92.28100  53.54100  1.000 69.07310  ?  338  HIS   A CE1 1 
ATOM   2659  N  NE2 . HIS   A 1 338  ? -11.74600  91.01300  53.66100  1.000 72.37954  ?  338  HIS   A NE2 1 
ATOM   2660  N  N   . VAL   A 1 339  ? -16.18900  95.60900  55.45200  1.000 45.65367  ?  339  VAL   A N   1 
ATOM   2661  C  CA  . VAL   A 1 339  ? -17.49800  96.20200  55.68500  1.000 43.33631  ?  339  VAL   A CA  1 
ATOM   2662  C  C   . VAL   A 1 339  ? -18.46400  95.91000  54.55000  1.000 47.01778  ?  339  VAL   A C   1 
ATOM   2663  O  O   . VAL   A 1 339  ? -19.59100  96.41000  54.56100  1.000 54.87627  ?  339  VAL   A O   1 
ATOM   2664  C  CB  . VAL   A 1 339  ? -17.39100  97.72400  55.91000  1.000 52.59188  ?  339  VAL   A CB  1 
ATOM   2665  C  CG1 . VAL   A 1 339  ? -16.43300  98.02900  57.05200  1.000 52.27955  ?  339  VAL   A CG1 1 
ATOM   2666  C  CG2 . VAL   A 1 339  ? -16.95200  98.43200  54.62700  1.000 46.61635  ?  339  VAL   A CG2 1 
ATOM   2667  N  N   . ASN   A 1 340  ? -18.06000  95.11700  53.56400  1.000 62.24835  ?  340  ASN   A N   1 
ATOM   2668  C  CA  . ASN   A 1 340  ? -18.85000  94.90200  52.36000  1.000 59.17876  ?  340  ASN   A CA  1 
ATOM   2669  C  C   . ASN   A 1 340  ? -19.53400  93.54100  52.36900  1.000 58.12128  ?  340  ASN   A C   1 
ATOM   2670  O  O   . ASN   A 1 340  ? -19.15600  92.62300  53.10200  1.000 47.52764  ?  340  ASN   A O   1 
ATOM   2671  C  CB  . ASN   A 1 340  ? -17.98100  95.02700  51.10400  1.000 32.94141  ?  340  ASN   A CB  1 
ATOM   2672  C  CG  . ASN   A 1 340  ? -17.70800  96.46500  50.72900  1.000 48.59245  ?  340  ASN   A CG  1 
ATOM   2673  O  OD1 . ASN   A 1 340  ? -16.63500  96.79300  50.22500  1.000 53.16861  ?  340  ASN   A OD1 1 
ATOM   2674  N  ND2 . ASN   A 1 340  ? -18.67600  97.33600  50.98200  1.000 54.37694  ?  340  ASN   A ND2 1 
ATOM   2675  N  N   . ARG   A 1 341  ? -20.54900  93.42800  51.52100  1.000 59.52105  ?  341  ARG   A N   1 
ATOM   2676  C  CA  . ARG   A 1 341  ? -21.35200  92.23800  51.30600  1.000 50.50977  ?  341  ARG   A CA  1 
ATOM   2677  C  C   . ARG   A 1 341  ? -21.34800  91.89400  49.82600  1.000 48.14079  ?  341  ARG   A C   1 
ATOM   2678  O  O   . ARG   A 1 341  ? -21.17500  92.78200  48.98500  1.000 49.01870  ?  341  ARG   A O   1 
ATOM   2679  C  CB  . ARG   A 1 341  ? -22.79500  92.45800  51.77900  1.000 66.77107  ?  341  ARG   A CB  1 
ATOM   2680  C  CG  . ARG   A 1 341  ? -23.27700  93.87600  51.56000  1.000 66.48166  ?  341  ARG   A CG  1 
ATOM   2681  C  CD  . ARG   A 1 341  ? -24.63500  94.09300  52.18500  1.000 69.41067  ?  341  ARG   A CD  1 
ATOM   2682  N  NE  . ARG   A 1 341  ? -24.81500  93.30200  53.39700  1.000 83.12492  ?  341  ARG   A NE  1 
ATOM   2683  C  CZ  . ARG   A 1 341  ? -24.30200  93.60600  54.58200  1.000 79.48064  ?  341  ARG   A CZ  1 
ATOM   2684  N  NH1 . ARG   A 1 341  ? -23.52400  94.66400  54.74800  1.000 85.23019  ?  341  ARG   A NH1 1 
ATOM   2685  N  NH2 . ARG   A 1 341  ? -24.57700  92.83000  55.62600  1.000 54.31911  ?  341  ARG   A NH2 1 
ATOM   2686  N  N   . PRO   A 1 342  ? -21.53400  90.61600  49.47700  1.000 41.24391  ?  342  PRO   A N   1 
ATOM   2687  C  CA  . PRO   A 1 342  ? -21.49900  90.23000  48.05300  1.000 41.52465  ?  342  PRO   A CA  1 
ATOM   2688  C  C   . PRO   A 1 342  ? -22.50800  90.96700  47.18700  1.000 43.37500  ?  342  PRO   A C   1 
ATOM   2689  O  O   . PRO   A 1 342  ? -22.36500  90.96200  45.95800  1.000 55.60334  ?  342  PRO   A O   1 
ATOM   2690  C  CB  . PRO   A 1 342  ? -21.78800  88.72400  48.09100  1.000 36.63504  ?  342  PRO   A CB  1 
ATOM   2691  C  CG  . PRO   A 1 342  ? -21.35800  88.29500  49.45200  1.000 40.91358  ?  342  PRO   A CG  1 
ATOM   2692  C  CD  . PRO   A 1 342  ? -21.66100  89.44600  50.36400  1.000 36.85895  ?  342  PRO   A CD  1 
ATOM   2693  N  N   . ASP   A 1 343  ? -23.51300  91.60900  47.78500  1.000 49.45034  ?  343  ASP   A N   1 
ATOM   2694  C  CA  . ASP   A 1 343  ? -24.52600  92.35700  47.05300  1.000 51.99355  ?  343  ASP   A CA  1 
ATOM   2695  C  C   . ASP   A 1 343  ? -24.29100  93.86600  47.10400  1.000 46.93951  ?  343  ASP   A C   1 
ATOM   2696  O  O   . ASP   A 1 343  ? -25.24700  94.64600  47.02600  1.000 60.55195  ?  343  ASP   A O   1 
ATOM   2697  C  CB  . ASP   A 1 343  ? -25.91800  92.01300  47.58200  1.000 60.42974  ?  343  ASP   A CB  1 
ATOM   2698  C  CG  . ASP   A 1 343  ? -26.31400  90.57900  47.28600  1.000 87.82000  ?  343  ASP   A CG  1 
ATOM   2699  O  OD1 . ASP   A 1 343  ? -25.80700  89.66400  47.97000  1.000 67.62141  ?  343  ASP   A OD1 1 
ATOM   2700  O  OD2 . ASP   A 1 343  ? -27.13600  90.36900  46.36900  1.000 91.90963  -1 343  ASP   A OD2 1 
ATOM   2701  N  N   . ASP   A 1 344  ? -23.03700  94.29500  47.22300  1.000 42.89095  ?  344  ASP   A N   1 
ATOM   2702  C  CA  . ASP   A 1 344  ? -22.68800  95.70800  47.22500  1.000 48.75074  ?  344  ASP   A CA  1 
ATOM   2703  C  C   . ASP   A 1 344  ? -22.09600  96.11100  45.88000  1.000 46.74609  ?  344  ASP   A C   1 
ATOM   2704  O  O   . ASP   A 1 344  ? -21.51700  95.29000  45.16600  1.000 53.66854  ?  344  ASP   A O   1 
ATOM   2705  C  CB  . ASP   A 1 344  ? -21.69400  96.03000  48.34700  1.000 60.43017  ?  344  ASP   A CB  1 
ATOM   2706  C  CG  . ASP   A 1 344  ? -22.36100  96.66300  49.55400  1.000 67.79424  ?  344  ASP   A CG  1 
ATOM   2707  O  OD1 . ASP   A 1 344  ? -23.53600  97.07100  49.43600  1.000 79.37919  ?  344  ASP   A OD1 1 
ATOM   2708  O  OD2 . ASP   A 1 344  ? -21.71200  96.74800  50.62200  1.000 58.08322  -1 344  ASP   A OD2 1 
ATOM   2709  N  N   . LEU   A 1 345  ? -22.24500  97.39200  45.54300  1.000 41.25472  ?  345  LEU   A N   1 
ATOM   2710  C  CA  . LEU   A 1 345  ? -21.73500  97.89800  44.27400  1.000 42.93869  ?  345  LEU   A CA  1 
ATOM   2711  C  C   . LEU   A 1 345  ? -20.21700  97.78500  44.21300  1.000 55.84969  ?  345  LEU   A C   1 
ATOM   2712  O  O   . LEU   A 1 345  ? -19.51400  98.10500  45.17500  1.000 53.56897  ?  345  LEU   A O   1 
ATOM   2713  C  CB  . LEU   A 1 345  ? -22.15000  99.35600  44.07700  1.000 30.44180  ?  345  LEU   A CB  1 
ATOM   2714  C  CG  . LEU   A 1 345  ? -23.27700  99.62400  43.08100  1.000 33.50383  ?  345  LEU   A CG  1 
ATOM   2715  C  CD1 . LEU   A 1 345  ? -24.54700  98.92900  43.52100  1.000 49.16628  ?  345  LEU   A CD1 1 
ATOM   2716  C  CD2 . LEU   A 1 345  ? -23.50100  101.11900 42.92700  1.000 26.51946  ?  345  LEU   A CD2 1 
ATOM   2717  N  N   . VAL   A 1 346  ? -19.71000  97.33200  43.06800  1.000 55.93385  ?  346  VAL   A N   1 
ATOM   2718  C  CA  . VAL   A 1 346  ? -18.27800  97.23900  42.82900  1.000 38.09208  ?  346  VAL   A CA  1 
ATOM   2719  C  C   . VAL   A 1 346  ? -17.80200  98.29400  41.83500  1.000 36.09673  ?  346  VAL   A C   1 
ATOM   2720  O  O   . VAL   A 1 346  ? -16.73300  98.88000  42.01900  1.000 54.84648  ?  346  VAL   A O   1 
ATOM   2721  C  CB  . VAL   A 1 346  ? -17.87800  95.81700  42.37000  1.000 37.14920  ?  346  VAL   A CB  1 
ATOM   2722  C  CG1 . VAL   A 1 346  ? -18.59400  95.42700  41.08400  1.000 45.83383  ?  346  VAL   A CG1 1 
ATOM   2723  C  CG2 . VAL   A 1 346  ? -16.36700  95.71000  42.20900  1.000 43.88784  ?  346  VAL   A CG2 1 
ATOM   2724  N  N   . TYR   A 1 347  ? -18.58400  98.56800  40.79000  1.000 27.90663  ?  347  TYR   A N   1 
ATOM   2725  C  CA  . TYR   A 1 347  ? -18.26400  99.65100  39.87000  1.000 37.52099  ?  347  TYR   A CA  1 
ATOM   2726  C  C   . TYR   A 1 347  ? -19.53600  100.14300 39.19500  1.000 44.97879  ?  347  TYR   A C   1 
ATOM   2727  O  O   . TYR   A 1 347  ? -20.56200  99.45700  39.17200  1.000 47.23861  ?  347  TYR   A O   1 
ATOM   2728  C  CB  . TYR   A 1 347  ? -17.22100  99.23800  38.81600  1.000 30.31636  ?  347  TYR   A CB  1 
ATOM   2729  C  CG  . TYR   A 1 347  ? -17.60200  98.08500  37.90300  1.000 32.20375  ?  347  TYR   A CG  1 
ATOM   2730  C  CD1 . TYR   A 1 347  ? -18.46100  98.27400  36.82700  1.000 39.76025  ?  347  TYR   A CD1 1 
ATOM   2731  C  CD2 . TYR   A 1 347  ? -17.06300  96.81600  38.09200  1.000 31.87959  ?  347  TYR   A CD2 1 
ATOM   2732  C  CE1 . TYR   A 1 347  ? -18.79700  97.22800  35.98500  1.000 35.34586  ?  347  TYR   A CE1 1 
ATOM   2733  C  CE2 . TYR   A 1 347  ? -17.39400  95.76200  37.25300  1.000 25.78887  ?  347  TYR   A CE2 1 
ATOM   2734  C  CZ  . TYR   A 1 347  ? -18.26300  95.97600  36.20100  1.000 38.82028  ?  347  TYR   A CZ  1 
ATOM   2735  O  OH  . TYR   A 1 347  ? -18.60200  94.94200  35.35700  1.000 45.85490  ?  347  TYR   A OH  1 
ATOM   2736  N  N   . VAL   A 1 348  ? -19.44900  101.35300 38.64900  1.000 29.53388  ?  348  VAL   A N   1 
ATOM   2737  C  CA  . VAL   A 1 348  ? -20.53300  101.97500 37.89900  1.000 38.73595  ?  348  VAL   A CA  1 
ATOM   2738  C  C   . VAL   A 1 348  ? -19.92800  102.46600 36.59300  1.000 44.86577  ?  348  VAL   A C   1 
ATOM   2739  O  O   . VAL   A 1 348  ? -19.25500  103.50300 36.56200  1.000 55.41086  ?  348  VAL   A O   1 
ATOM   2740  C  CB  . VAL   A 1 348  ? -21.20200  103.12200 38.66300  1.000 42.76863  ?  348  VAL   A CB  1 
ATOM   2741  C  CG1 . VAL   A 1 348  ? -22.24900  103.79600 37.78700  1.000 33.94975  ?  348  VAL   A CG1 1 
ATOM   2742  C  CG2 . VAL   A 1 348  ? -21.83200  102.60400 39.94200  1.000 28.75675  ?  348  VAL   A CG2 1 
ATOM   2743  N  N   . MET   A 1 349  ? -20.15300  101.72400 35.51500  1.000 47.27542  ?  349  MET   A N   1 
ATOM   2744  C  CA  . MET   A 1 349  ? -19.68800  102.11000 34.19200  1.000 49.25941  ?  349  MET   A CA  1 
ATOM   2745  C  C   . MET   A 1 349  ? -20.84400  102.67500 33.38100  1.000 45.32553  ?  349  MET   A C   1 
ATOM   2746  O  O   . MET   A 1 349  ? -21.95400  102.13600 33.39900  1.000 40.55991  ?  349  MET   A O   1 
ATOM   2747  C  CB  . MET   A 1 349  ? -19.06100  100.92200 33.46300  1.000 43.94989  ?  349  MET   A CB  1 
ATOM   2748  C  CG  . MET   A 1 349  ? -17.56900  100.80600 33.69500  1.000 41.61662  ?  349  MET   A CG  1 
ATOM   2749  S  SD  . MET   A 1 349  ? -16.97900  99.10900  33.63500  1.000 54.33452  ?  349  MET   A SD  1 
ATOM   2750  C  CE  . MET   A 1 349  ? -15.34500  99.30000  34.34300  1.000 65.71752  ?  349  MET   A CE  1 
ATOM   2751  N  N   . TYR   A 1 350  ? -20.57100  103.76400 32.67200  1.000 48.65185  ?  350  TYR   A N   1 
ATOM   2752  C  CA  . TYR   A 1 350  ? -21.58300  104.45900 31.89400  1.000 53.18044  ?  350  TYR   A CA  1 
ATOM   2753  C  C   . TYR   A 1 350  ? -21.61200  103.94700 30.46000  1.000 57.58169  ?  350  TYR   A C   1 
ATOM   2754  O  O   . TYR   A 1 350  ? -20.58200  103.58100 29.88600  1.000 57.68567  ?  350  TYR   A O   1 
ATOM   2755  C  CB  . TYR   A 1 350  ? -21.33000  105.96700 31.91400  1.000 55.29635  ?  350  TYR   A CB  1 
ATOM   2756  C  CG  . TYR   A 1 350  ? -21.72600  106.63500 33.21400  1.000 64.33015  ?  350  TYR   A CG  1 
ATOM   2757  C  CD1 . TYR   A 1 350  ? -21.17700  106.22900 34.42500  1.000 57.78459  ?  350  TYR   A CD1 1 
ATOM   2758  C  CD2 . TYR   A 1 350  ? -22.64500  107.67600 33.22900  1.000 62.43903  ?  350  TYR   A CD2 1 
ATOM   2759  C  CE1 . TYR   A 1 350  ? -21.53400  106.83700 35.61200  1.000 63.61178  ?  350  TYR   A CE1 1 
ATOM   2760  C  CE2 . TYR   A 1 350  ? -23.00700  108.29100 34.41300  1.000 61.29060  ?  350  TYR   A CE2 1 
ATOM   2761  C  CZ  . TYR   A 1 350  ? -22.45000  107.86800 35.60100  1.000 68.37812  ?  350  TYR   A CZ  1 
ATOM   2762  O  OH  . TYR   A 1 350  ? -22.80800  108.47700 36.78000  1.000 69.24097  ?  350  TYR   A OH  1 
ATOM   2763  N  N   . THR   A 1 351  ? -22.81600  103.92200 29.89000  1.000 62.75524  ?  351  THR   A N   1 
ATOM   2764  C  CA  . THR   A 1 351  ? -23.06500  103.40900 28.54500  1.000 65.43048  ?  351  THR   A CA  1 
ATOM   2765  C  C   . THR   A 1 351  ? -23.66700  104.52700 27.70400  1.000 79.18705  ?  351  THR   A C   1 
ATOM   2766  O  O   . THR   A 1 351  ? -24.83900  104.88400 27.88000  1.000 86.45066  ?  351  THR   A O   1 
ATOM   2767  C  CB  . THR   A 1 351  ? -23.99000  102.19000 28.57500  1.000 75.57043  ?  351  THR   A CB  1 
ATOM   2768  O  OG1 . THR   A 1 351  ? -25.13800  102.45900 29.39100  1.000 71.50479  ?  351  THR   A OG1 1 
ATOM   2769  C  CG2 . THR   A 1 351  ? -23.25100  100.97700 29.12100  1.000 67.23210  ?  351  THR   A CG2 1 
ATOM   2770  N  N   . SER   A 1 352  ? -22.86300  105.08000 26.79600  1.000 75.48921  ?  352  SER   A N   1 
ATOM   2771  C  CA  . SER   A 1 352  ? -23.32300  106.13100 25.89000  1.000 97.55416  ?  352  SER   A CA  1 
ATOM   2772  C  C   . SER   A 1 352  ? -24.02900  105.46800 24.71200  1.000 108.58988 ?  352  SER   A C   1 
ATOM   2773  O  O   . SER   A 1 352  ? -23.48600  105.31200 23.61400  1.000 96.05459  ?  352  SER   A O   1 
ATOM   2774  C  CB  . SER   A 1 352  ? -22.16200  107.00900 25.44200  1.000 103.28713 ?  352  SER   A CB  1 
ATOM   2775  O  OG  . SER   A 1 352  ? -22.25900  108.30000 26.02200  1.000 86.46223  ?  352  SER   A OG  1 
ATOM   2776  N  N   . GLY   A 1 353  ? -25.26400  105.05000 24.96400  1.000 108.55020 ?  353  GLY   A N   1 
ATOM   2777  C  CA  . GLY   A 1 353  ? -26.15100  104.53700 23.94600  1.000 106.13043 ?  353  GLY   A CA  1 
ATOM   2778  C  C   . GLY   A 1 353  ? -26.95200  105.59800 23.22300  1.000 131.17097 ?  353  GLY   A C   1 
ATOM   2779  O  O   . GLY   A 1 353  ? -27.77300  105.25500 22.36600  1.000 125.43817 ?  353  GLY   A O   1 
ATOM   2780  N  N   . SER   A 1 354  ? -26.73700  106.87400 23.54600  1.000 123.51902 ?  354  SER   A N   1 
ATOM   2781  C  CA  . SER   A 1 354  ? -27.41500  107.99800 22.89500  1.000 98.71716  ?  354  SER   A CA  1 
ATOM   2782  C  C   . SER   A 1 354  ? -28.93800  107.84600 22.90500  1.000 91.63686  ?  354  SER   A C   1 
ATOM   2783  O  O   . SER   A 1 354  ? -29.67300  108.80300 22.65700  1.000 83.42593  ?  354  SER   A O   1 
ATOM   2784  C  CB  . SER   A 1 354  ? -26.91300  108.16400 21.45800  1.000 91.29224  ?  354  SER   A CB  1 
ATOM   2785  O  OG  . SER   A 1 354  ? -25.49900  108.26500 21.42400  1.000 89.42342  ?  354  SER   A OG  1 
ATOM   2786  N  N   . LEU   A 1 357  ? -27.43200  111.96300 26.89300  1.000 69.81165  ?  357  LEU   A N   1 
ATOM   2787  C  CA  . LEU   A 1 357  ? -26.60300  111.70900 28.06700  1.000 78.40653  ?  357  LEU   A CA  1 
ATOM   2788  C  C   . LEU   A 1 357  ? -26.49500  110.21000 28.33900  1.000 95.55866  ?  357  LEU   A C   1 
ATOM   2789  O  O   . LEU   A 1 357  ? -27.34300  109.42900 27.90500  1.000 101.49150 ?  357  LEU   A O   1 
ATOM   2790  C  CB  . LEU   A 1 357  ? -27.15800  112.44000 29.29700  1.000 81.03670  ?  357  LEU   A CB  1 
ATOM   2791  C  CG  . LEU   A 1 357  ? -28.48700  112.01000 29.93400  1.000 99.81890  ?  357  LEU   A CG  1 
ATOM   2792  C  CD1 . LEU   A 1 357  ? -28.64000  112.66000 31.30100  1.000 76.54687  ?  357  LEU   A CD1 1 
ATOM   2793  C  CD2 . LEU   A 1 357  ? -29.68900  112.34900 29.05800  1.000 80.07534  ?  357  LEU   A CD2 1 
ATOM   2794  N  N   . ALA   A 1 358  ? -25.44800  109.81700 29.05800  1.000 79.29271  ?  358  ALA   A N   1 
ATOM   2795  C  CA  . ALA   A 1 358  ? -25.16300  108.41300 29.30800  1.000 67.29199  ?  358  ALA   A CA  1 
ATOM   2796  C  C   . ALA   A 1 358  ? -25.88700  107.91900 30.55700  1.000 58.71977  ?  358  ALA   A C   1 
ATOM   2797  O  O   . ALA   A 1 358  ? -26.41100  108.69300 31.36000  1.000 68.57649  ?  358  ALA   A O   1 
ATOM   2798  C  CB  . ALA   A 1 358  ? -23.65800  108.18700 29.44600  1.000 77.62223  ?  358  ALA   A CB  1 
ATOM   2799  N  N   . LYS   A 1 359  ? -25.90100  106.59900 30.71500  1.000 51.86291  ?  359  LYS   A N   1 
ATOM   2800  C  CA  . LYS   A 1 359  ? -26.58700  105.93200 31.81100  1.000 53.48857  ?  359  LYS   A CA  1 
ATOM   2801  C  C   . LYS   A 1 359  ? -25.57700  105.11900 32.60400  1.000 51.55716  ?  359  LYS   A C   1 
ATOM   2802  O  O   . LYS   A 1 359  ? -24.87500  104.27500 32.03800  1.000 48.97500  ?  359  LYS   A O   1 
ATOM   2803  C  CB  . LYS   A 1 359  ? -27.70300  105.02700 31.28100  1.000 60.65380  ?  359  LYS   A CB  1 
ATOM   2804  C  CG  . LYS   A 1 359  ? -28.25500  105.46200 29.93000  1.000 76.60943  ?  359  LYS   A CG  1 
ATOM   2805  C  CD  . LYS   A 1 359  ? -29.26000  104.46500 29.37300  1.000 80.02389  ?  359  LYS   A CD  1 
ATOM   2806  C  CE  . LYS   A 1 359  ? -28.58400  103.34600 28.59800  1.000 88.99735  ?  359  LYS   A CE  1 
ATOM   2807  N  NZ  . LYS   A 1 359  ? -29.53000  102.68000 27.65700  1.000 92.70711  ?  359  LYS   A NZ  1 
ATOM   2808  N  N   . GLY   A 1 360  ? -25.50300  105.37200 33.90800  1.000 56.75893  ?  360  GLY   A N   1 
ATOM   2809  C  CA  . GLY   A 1 360  ? -24.57100  104.65800 34.75700  1.000 37.76556  ?  360  GLY   A CA  1 
ATOM   2810  C  C   . GLY   A 1 360  ? -25.04600  103.26900 35.13200  1.000 38.50023  ?  360  GLY   A C   1 
ATOM   2811  O  O   . GLY   A 1 360  ? -25.96000  103.12100 35.94800  1.000 41.55965  ?  360  GLY   A O   1 
ATOM   2812  N  N   . VAL   A 1 361  ? -24.43400  102.24400 34.54400  1.000 44.77609  ?  361  VAL   A N   1 
ATOM   2813  C  CA  . VAL   A 1 361  ? -24.79400  100.86200 34.84500  1.000 35.29738  ?  361  VAL   A CA  1 
ATOM   2814  C  C   . VAL   A 1 361  ? -24.12700  100.45100 36.14900  1.000 33.71783  ?  361  VAL   A C   1 
ATOM   2815  O  O   . VAL   A 1 361  ? -22.93100  100.68700 36.35000  1.000 41.98925  ?  361  VAL   A O   1 
ATOM   2816  C  CB  . VAL   A 1 361  ? -24.38700  99.92800  33.69500  1.000 45.38330  ?  361  VAL   A CB  1 
ATOM   2817  C  CG1 . VAL   A 1 361  ? -24.80200  98.49700  34.00300  1.000 39.48214  ?  361  VAL   A CG1 1 
ATOM   2818  C  CG2 . VAL   A 1 361  ? -25.00000  100.39800 32.38500  1.000 40.34888  ?  361  VAL   A CG2 1 
ATOM   2819  N  N   . MET   A 1 362  ? -24.89600  99.82700  37.03400  1.000 34.67877  ?  362  MET   A N   1 
ATOM   2820  C  CA  . MET   A 1 362  ? -24.43800  99.47100  38.37100  1.000 40.64806  ?  362  MET   A CA  1 
ATOM   2821  C  C   . MET   A 1 362  ? -24.21200  97.96700  38.44300  1.000 43.19522  ?  362  MET   A C   1 
ATOM   2822  O  O   . MET   A 1 362  ? -25.14200  97.18500  38.21800  1.000 42.08168  ?  362  MET   A O   1 
ATOM   2823  C  CB  . MET   A 1 362  ? -25.45300  99.91900  39.42100  1.000 36.10034  ?  362  MET   A CB  1 
ATOM   2824  C  CG  . MET   A 1 362  ? -25.76900  101.40800 39.37000  1.000 38.20599  ?  362  MET   A CG  1 
ATOM   2825  S  SD  . MET   A 1 362  ? -27.27600  101.83000 40.26300  1.000 59.11812  ?  362  MET   A SD  1 
ATOM   2826  C  CE  . MET   A 1 362  ? -27.26500  100.58700 41.55200  1.000 41.25410  ?  362  MET   A CE  1 
ATOM   2827  N  N   . ILE   A 1 363  ? -22.98300  97.56900  38.76200  1.000 35.86744  ?  363  ILE   A N   1 
ATOM   2828  C  CA  . ILE   A 1 363  ? -22.60000  96.16800  38.88300  1.000 39.79595  ?  363  ILE   A CA  1 
ATOM   2829  C  C   . ILE   A 1 363  ? -22.15600  95.91400  40.31700  1.000 44.24678  ?  363  ILE   A C   1 
ATOM   2830  O  O   . ILE   A 1 363  ? -21.52200  96.77200  40.94000  1.000 38.13152  ?  363  ILE   A O   1 
ATOM   2831  C  CB  . ILE   A 1 363  ? -21.48600  95.80200  37.88100  1.000 34.32670  ?  363  ILE   A CB  1 
ATOM   2832  C  CG1 . ILE   A 1 363  ? -21.98000  96.00000  36.44600  1.000 28.87383  ?  363  ILE   A CG1 1 
ATOM   2833  C  CG2 . ILE   A 1 363  ? -21.01800  94.36800  38.08200  1.000 46.82490  ?  363  ILE   A CG2 1 
ATOM   2834  C  CD1 . ILE   A 1 363  ? -22.96300  94.94800  35.98700  1.000 37.46406  ?  363  ILE   A CD1 1 
ATOM   2835  N  N   . GLU   A 1 364  ? -22.49700  94.74000  40.84000  1.000 46.60706  ?  364  GLU   A N   1 
ATOM   2836  C  CA  . GLU   A 1 364  ? -22.23200  94.37800  42.22500  1.000 46.98525  ?  364  GLU   A CA  1 
ATOM   2837  C  C   . GLU   A 1 364  ? -21.09300  93.36700  42.31300  1.000 53.98436  ?  364  GLU   A C   1 
ATOM   2838  O  O   . GLU   A 1 364  ? -20.59500  92.85900  41.30600  1.000 67.02821  ?  364  GLU   A O   1 
ATOM   2839  C  CB  . GLU   A 1 364  ? -23.49700  93.82200  42.88400  1.000 50.52045  ?  364  GLU   A CB  1 
ATOM   2840  C  CG  . GLU   A 1 364  ? -24.59300  94.85500  43.05600  1.000 51.90600  ?  364  GLU   A CG  1 
ATOM   2841  C  CD  . GLU   A 1 364  ? -25.92300  94.23700  43.43100  1.000 64.00677  ?  364  GLU   A CD  1 
ATOM   2842  O  OE1 . GLU   A 1 364  ? -26.25500  93.15900  42.89500  1.000 71.41264  ?  364  GLU   A OE1 1 
ATOM   2843  O  OE2 . GLU   A 1 364  ? -26.63800  94.82800  44.26700  1.000 68.26455  -1 364  GLU   A OE2 1 
ATOM   2844  N  N   . HIS   A 1 365  ? -20.68900  93.07700  43.55400  1.000 41.23032  ?  365  HIS   A N   1 
ATOM   2845  C  CA  . HIS   A 1 365  ? -19.52800  92.22100  43.78100  1.000 43.67672  ?  365  HIS   A CA  1 
ATOM   2846  C  C   . HIS   A 1 365  ? -19.78600  90.79100  43.32000  1.000 47.31170  ?  365  HIS   A C   1 
ATOM   2847  O  O   . HIS   A 1 365  ? -18.94000  90.18300  42.65500  1.000 54.93015  ?  365  HIS   A O   1 
ATOM   2848  C  CB  . HIS   A 1 365  ? -19.13500  92.24600  45.25900  1.000 42.20324  ?  365  HIS   A CB  1 
ATOM   2849  C  CG  . HIS   A 1 365  ? -18.16000  93.32600  45.60600  1.000 51.53127  ?  365  HIS   A CG  1 
ATOM   2850  N  ND1 . HIS   A 1 365  ? -16.79600  93.16300  45.48600  1.000 43.73157  ?  365  HIS   A ND1 1 
ATOM   2851  C  CD2 . HIS   A 1 365  ? -18.34800  94.58500  46.06700  1.000 36.33116  ?  365  HIS   A CD2 1 
ATOM   2852  C  CE1 . HIS   A 1 365  ? -16.18700  94.27500  45.85700  1.000 51.06316  ?  365  HIS   A CE1 1 
ATOM   2853  N  NE2 . HIS   A 1 365  ? -17.10600  95.15400  46.21500  1.000 40.82406  ?  365  HIS   A NE2 1 
ATOM   2854  N  N   . HIS   A 1 366  ? -20.94900  90.23500  43.66700  1.000 43.52130  ?  366  HIS   A N   1 
ATOM   2855  C  CA  . HIS   A 1 366  ? -21.25100  88.85900  43.28900  1.000 36.81369  ?  366  HIS   A CA  1 
ATOM   2856  C  C   . HIS   A 1 366  ? -21.32400  88.67900  41.77900  1.000 40.83005  ?  366  HIS   A C   1 
ATOM   2857  O  O   . HIS   A 1 366  ? -21.15900  87.55600  41.29100  1.000 36.51458  ?  366  HIS   A O   1 
ATOM   2858  C  CB  . HIS   A 1 366  ? -22.56400  88.40900  43.93200  1.000 46.45633  ?  366  HIS   A CB  1 
ATOM   2859  C  CG  . HIS   A 1 366  ? -23.76400  89.15900  43.44300  1.000 52.06194  ?  366  HIS   A CG  1 
ATOM   2860  N  ND1 . HIS   A 1 366  ? -24.78900  88.55200  42.75100  1.000 41.38791  ?  366  HIS   A ND1 1 
ATOM   2861  C  CD2 . HIS   A 1 366  ? -24.10000  90.46700  43.54200  1.000 50.36902  ?  366  HIS   A CD2 1 
ATOM   2862  C  CE1 . HIS   A 1 366  ? -25.70700  89.45300  42.44700  1.000 56.68057  ?  366  HIS   A CE1 1 
ATOM   2863  N  NE2 . HIS   A 1 366  ? -25.31200  90.62300  42.91600  1.000 55.73111  ?  366  HIS   A NE2 1 
ATOM   2864  N  N   . ASN   A 1 367  ? -21.56500  89.75800  41.03000  1.000 39.94492  ?  367  ASN   A N   1 
ATOM   2865  C  CA  . ASN   A 1 367  ? -21.58100  89.65900  39.57400  1.000 40.84324  ?  367  ASN   A CA  1 
ATOM   2866  C  C   . ASN   A 1 367  ? -20.17400  89.46700  39.02500  1.000 40.30747  ?  367  ASN   A C   1 
ATOM   2867  O  O   . ASN   A 1 367  ? -19.94000  88.59900  38.17600  1.000 38.22918  ?  367  ASN   A O   1 
ATOM   2868  C  CB  . ASN   A 1 367  ? -22.22600  90.90500  38.96500  1.000 41.61079  ?  367  ASN   A CB  1 
ATOM   2869  C  CG  . ASN   A 1 367  ? -23.69200  91.03300  39.31700  1.000 40.48155  ?  367  ASN   A CG  1 
ATOM   2870  O  OD1 . ASN   A 1 367  ? -24.21000  92.13900  39.46700  1.000 46.27004  ?  367  ASN   A OD1 1 
ATOM   2871  N  ND2 . ASN   A 1 367  ? -24.37000  89.89800  39.45500  1.000 35.53211  ?  367  ASN   A ND2 1 
ATOM   2872  N  N   . LEU   A 1 368  ? -19.22400  90.27400  39.50100  1.000 49.65779  ?  368  LEU   A N   1 
ATOM   2873  C  CA  . LEU   A 1 368  ? -17.84500  90.14900  39.04500  1.000 38.28939  ?  368  LEU   A CA  1 
ATOM   2874  C  C   . LEU   A 1 368  ? -17.22200  88.84200  39.52000  1.000 34.33576  ?  368  LEU   A C   1 
ATOM   2875  O  O   . LEU   A 1 368  ? -16.51000  88.17700  38.75800  1.000 45.64880  ?  368  LEU   A O   1 
ATOM   2876  C  CB  . LEU   A 1 368  ? -17.02500  91.34100  39.53500  1.000 34.98157  ?  368  LEU   A CB  1 
ATOM   2877  C  CG  . LEU   A 1 368  ? -15.59200  91.44300  39.01600  1.000 36.84306  ?  368  LEU   A CG  1 
ATOM   2878  C  CD1 . LEU   A 1 368  ? -15.57800  91.85500  37.55000  1.000 39.20893  ?  368  LEU   A CD1 1 
ATOM   2879  C  CD2 . LEU   A 1 368  ? -14.79300  92.41400  39.86600  1.000 32.27538  ?  368  LEU   A CD2 1 
ATOM   2880  N  N   . VAL   A 1 369  ? -17.48200  88.45900  40.77400  1.000 28.40157  ?  369  VAL   A N   1 
ATOM   2881  C  CA  . VAL   A 1 369  ? -16.91300  87.23000  41.32100  1.000 34.85964  ?  369  VAL   A CA  1 
ATOM   2882  C  C   . VAL   A 1 369  ? -17.36200  86.02300  40.50900  1.000 34.77240  ?  369  VAL   A C   1 
ATOM   2883  O  O   . VAL   A 1 369  ? -16.56200  85.13200  40.19600  1.000 52.51518  ?  369  VAL   A O   1 
ATOM   2884  C  CB  . VAL   A 1 369  ? -17.28700  87.08400  42.80900  1.000 27.31088  ?  369  VAL   A CB  1 
ATOM   2885  C  CG1 . VAL   A 1 369  ? -16.94300  85.69200  43.31400  1.000 37.74381  ?  369  VAL   A CG1 1 
ATOM   2886  C  CG2 . VAL   A 1 369  ? -16.57900  88.14100  43.64100  1.000 35.27406  ?  369  VAL   A CG2 1 
ATOM   2887  N  N   . ASN   A 1 370  ? -18.64600  85.97600  40.14800  1.000 37.85653  ?  370  ASN   A N   1 
ATOM   2888  C  CA  . ASN   A 1 370  ? -19.14400  84.87000  39.33800  1.000 52.87594  ?  370  ASN   A CA  1 
ATOM   2889  C  C   . ASN   A 1 370  ? -18.44000  84.80600  37.98900  1.000 46.92786  ?  370  ASN   A C   1 
ATOM   2890  O  O   . ASN   A 1 370  ? -18.23700  83.71400  37.44500  1.000 42.91656  ?  370  ASN   A O   1 
ATOM   2891  C  CB  . ASN   A 1 370  ? -20.65600  84.99700  39.15200  1.000 41.64785  ?  370  ASN   A CB  1 
ATOM   2892  C  CG  . ASN   A 1 370  ? -21.23200  83.89300  38.29100  1.000 32.98292  ?  370  ASN   A CG  1 
ATOM   2893  O  OD1 . ASN   A 1 370  ? -21.33000  82.74300  38.71800  1.000 39.69524  ?  370  ASN   A OD1 1 
ATOM   2894  N  ND2 . ASN   A 1 370  ? -21.62500  84.24000  37.07200  1.000 37.79434  ?  370  ASN   A ND2 1 
ATOM   2895  N  N   . PHE   A 1 371  ? -18.04800  85.95800  37.44100  1.000 39.10240  ?  371  PHE   A N   1 
ATOM   2896  C  CA  . PHE   A 1 371  ? -17.32600  85.96700  36.17500  1.000 39.37110  ?  371  PHE   A CA  1 
ATOM   2897  C  C   . PHE   A 1 371  ? -15.86900  85.56100  36.36300  1.000 40.07116  ?  371  PHE   A C   1 
ATOM   2898  O  O   . PHE   A 1 371  ? -15.33600  84.77300  35.57400  1.000 41.90881  ?  371  PHE   A O   1 
ATOM   2899  C  CB  . PHE   A 1 371  ? -17.41700  87.35000  35.52900  1.000 27.63806  ?  371  PHE   A CB  1 
ATOM   2900  C  CG  . PHE   A 1 371  ? -16.95900  87.38200  34.10100  1.000 42.34044  ?  371  PHE   A CG  1 
ATOM   2901  C  CD1 . PHE   A 1 371  ? -17.79600  86.95400  33.08300  1.000 48.23745  ?  371  PHE   A CD1 1 
ATOM   2902  C  CD2 . PHE   A 1 371  ? -15.69400  87.84200  33.77300  1.000 45.64171  ?  371  PHE   A CD2 1 
ATOM   2903  C  CE1 . PHE   A 1 371  ? -17.37800  86.98100  31.76400  1.000 47.33325  ?  371  PHE   A CE1 1 
ATOM   2904  C  CE2 . PHE   A 1 371  ? -15.27100  87.87200  32.45700  1.000 49.84763  ?  371  PHE   A CE2 1 
ATOM   2905  C  CZ  . PHE   A 1 371  ? -16.11500  87.44100  31.45200  1.000 37.68199  ?  371  PHE   A CZ  1 
ATOM   2906  N  N   . CYS   A 1 372  ? -15.21700  86.08200  37.40500  1.000 45.95025  ?  372  CYS   A N   1 
ATOM   2907  C  CA  . CYS   A 1 372  ? -13.81600  85.75300  37.64600  1.000 36.05219  ?  372  CYS   A CA  1 
ATOM   2908  C  C   . CYS   A 1 372  ? -13.64700  84.29100  38.03900  1.000 49.51855  ?  372  CYS   A C   1 
ATOM   2909  O  O   . CYS   A 1 372  ? -12.70200  83.62900  37.59400  1.000 57.06323  ?  372  CYS   A O   1 
ATOM   2910  C  CB  . CYS   A 1 372  ? -13.24100  86.66900  38.72500  1.000 27.58983  ?  372  CYS   A CB  1 
ATOM   2911  S  SG  . CYS   A 1 372  ? -13.23100  88.42200  38.28400  1.000 42.95158  ?  372  CYS   A SG  1 
ATOM   2912  N  N   . GLU   A 1 373  ? -14.55100  83.76900  38.87100  1.000 48.06175  ?  373  GLU   A N   1 
ATOM   2913  C  CA  . GLU   A 1 373  ? -14.48300  82.36900  39.27300  1.000 41.07032  ?  373  GLU   A CA  1 
ATOM   2914  C  C   . GLU   A 1 373  ? -14.90300  81.41700  38.16200  1.000 41.06964  ?  373  GLU   A C   1 
ATOM   2915  O  O   . GLU   A 1 373  ? -14.77500  80.20000  38.33300  1.000 42.00911  ?  373  GLU   A O   1 
ATOM   2916  C  CB  . GLU   A 1 373  ? -15.34300  82.13800  40.51500  1.000 39.98222  ?  373  GLU   A CB  1 
ATOM   2917  C  CG  . GLU   A 1 373  ? -14.82600  82.84300  41.75900  1.000 44.61026  ?  373  GLU   A CG  1 
ATOM   2918  C  CD  . GLU   A 1 373  ? -13.51900  82.26000  42.26100  1.000 64.93149  ?  373  GLU   A CD  1 
ATOM   2919  O  OE1 . GLU   A 1 373  ? -13.34400  81.02600  42.17300  1.000 68.21341  ?  373  GLU   A OE1 1 
ATOM   2920  O  OE2 . GLU   A 1 373  ? -12.66600  83.03600  42.74000  1.000 75.74601  -1 373  GLU   A OE2 1 
ATOM   2921  N  N   . TRP   A 1 374  ? -15.40900  81.93500  37.04400  1.000 39.94572  ?  374  TRP   A N   1 
ATOM   2922  C  CA  . TRP   A 1 374  ? -15.63000  81.14800  35.83800  1.000 38.32409  ?  374  TRP   A CA  1 
ATOM   2923  C  C   . TRP   A 1 374  ? -14.51000  81.32000  34.82200  1.000 49.35040  ?  374  TRP   A C   1 
ATOM   2924  O  O   . TRP   A 1 374  ? -14.14900  80.36000  34.13600  1.000 42.13360  ?  374  TRP   A O   1 
ATOM   2925  C  CB  . TRP   A 1 374  ? -16.96700  81.52600  35.18700  1.000 32.18400  ?  374  TRP   A CB  1 
ATOM   2926  C  CG  . TRP   A 1 374  ? -17.09500  81.03000  33.77800  1.000 22.41491  ?  374  TRP   A CG  1 
ATOM   2927  C  CD1 . TRP   A 1 374  ? -17.52700  79.80000  33.37700  1.000 27.57599  ?  374  TRP   A CD1 1 
ATOM   2928  C  CD2 . TRP   A 1 374  ? -16.77400  81.75200  32.58100  1.000 29.87828  ?  374  TRP   A CD2 1 
ATOM   2929  N  NE1 . TRP   A 1 374  ? -17.49900  79.71100  32.00600  1.000 37.55678  ?  374  TRP   A NE1 1 
ATOM   2930  C  CE2 . TRP   A 1 374  ? -17.03900  80.89600  31.49300  1.000 31.19695  ?  374  TRP   A CE2 1 
ATOM   2931  C  CE3 . TRP   A 1 374  ? -16.28700  83.03700  32.32400  1.000 40.17551  ?  374  TRP   A CE3 1 
ATOM   2932  C  CZ2 . TRP   A 1 374  ? -16.83600  81.28500  30.17000  1.000 31.24691  ?  374  TRP   A CZ2 1 
ATOM   2933  C  CZ3 . TRP   A 1 374  ? -16.08700  83.42200  31.00900  1.000 30.19842  ?  374  TRP   A CZ3 1 
ATOM   2934  C  CH2 . TRP   A 1 374  ? -16.36100  82.54900  29.95000  1.000 33.05895  ?  374  TRP   A CH2 1 
ATOM   2935  N  N   . TYR   A 1 375  ? -13.94800  82.52700  34.72700  1.000 48.42610  ?  375  TYR   A N   1 
ATOM   2936  C  CA  . TYR   A 1 375  ? -12.90900  82.80300  33.74000  1.000 34.48739  ?  375  TYR   A CA  1 
ATOM   2937  C  C   . TYR   A 1 375  ? -11.66100  81.96700  34.00200  1.000 42.56752  ?  375  TYR   A C   1 
ATOM   2938  O  O   . TYR   A 1 375  ? -11.08000  81.39100  33.07400  1.000 47.06911  ?  375  TYR   A O   1 
ATOM   2939  C  CB  . TYR   A 1 375  ? -12.57700  84.29600  33.75600  1.000 41.36709  ?  375  TYR   A CB  1 
ATOM   2940  C  CG  . TYR   A 1 375  ? -11.62500  84.75800  32.67600  1.000 44.16249  ?  375  TYR   A CG  1 
ATOM   2941  C  CD1 . TYR   A 1 375  ? -10.25000  84.63200  32.83100  1.000 38.79313  ?  375  TYR   A CD1 1 
ATOM   2942  C  CD2 . TYR   A 1 375  ? -12.10200  85.34600  31.51300  1.000 43.47850  ?  375  TYR   A CD2 1 
ATOM   2943  C  CE1 . TYR   A 1 375  ? -9.37900   85.06300  31.85100  1.000 43.51436  ?  375  TYR   A CE1 1 
ATOM   2944  C  CE2 . TYR   A 1 375  ? -11.23800  85.78000  30.52800  1.000 44.70139  ?  375  TYR   A CE2 1 
ATOM   2945  C  CZ  . TYR   A 1 375  ? -9.87800   85.63700  30.70200  1.000 41.54686  ?  375  TYR   A CZ  1 
ATOM   2946  O  OH  . TYR   A 1 375  ? -9.01300   86.07000  29.72400  1.000 52.45257  ?  375  TYR   A OH  1 
ATOM   2947  N  N   . ARG   A 1 376  ? -11.23300  81.89200  35.26300  1.000 49.01838  ?  376  ARG   A N   1 
ATOM   2948  C  CA  . ARG   A 1 376  ? -9.99900   81.17800  35.58800  1.000 41.13108  ?  376  ARG   A CA  1 
ATOM   2949  C  C   . ARG   A 1 376  ? -10.06300  79.69200  35.25500  1.000 34.82479  ?  376  ARG   A C   1 
ATOM   2950  O  O   . ARG   A 1 376  ? -9.17500   79.21000  34.53000  1.000 44.39087  ?  376  ARG   A O   1 
ATOM   2951  C  CB  . ARG   A 1 376  ? -9.64500   81.40500  37.06300  1.000 47.65641  ?  376  ARG   A CB  1 
ATOM   2952  C  CG  . ARG   A 1 376  ? -8.34800   80.74000  37.49900  1.000 42.35475  ?  376  ARG   A CG  1 
ATOM   2953  C  CD  . ARG   A 1 376  ? -8.27000   80.57500  39.01200  1.000 44.98900  ?  376  ARG   A CD  1 
ATOM   2954  N  NE  . ARG   A 1 376  ? -8.90500   81.67400  39.73000  1.000 76.33718  ?  376  ARG   A NE  1 
ATOM   2955  C  CZ  . ARG   A 1 376  ? -10.01700  81.55800  40.44400  1.000 61.59583  ?  376  ARG   A CZ  1 
ATOM   2956  N  NH1 . ARG   A 1 376  ? -10.63500  80.39600  40.57900  1.000 53.59219  ?  376  ARG   A NH1 1 
ATOM   2957  N  NH2 . ARG   A 1 376  ? -10.52000  82.63600  41.04100  1.000 52.75824  ?  376  ARG   A NH2 1 
ATOM   2958  N  N   . PRO   A 1 377  ? -11.04700  78.91400  35.72500  1.000 33.49337  ?  377  PRO   A N   1 
ATOM   2959  C  CA  . PRO   A 1 377  ? -11.04600  77.48100  35.39200  1.000 26.34364  ?  377  PRO   A CA  1 
ATOM   2960  C  C   . PRO   A 1 377  ? -11.39700  77.19500  33.94400  1.000 34.00204  ?  377  PRO   A C   1 
ATOM   2961  O  O   . PRO   A 1 377  ? -11.00100  76.14400  33.42700  1.000 46.23009  ?  377  PRO   A O   1 
ATOM   2962  C  CB  . PRO   A 1 377  ? -12.09600  76.89900  36.34500  1.000 27.55425  ?  377  PRO   A CB  1 
ATOM   2963  C  CG  . PRO   A 1 377  ? -13.04300  78.01600  36.55700  1.000 47.71026  ?  377  PRO   A CG  1 
ATOM   2964  C  CD  . PRO   A 1 377  ? -12.20900  79.26800  36.56400  1.000 41.99891  ?  377  PRO   A CD  1 
ATOM   2965  N  N   . TYR   A 1 378  ? -12.12200  78.09400  33.27400  1.000 49.11708  ?  378  TYR   A N   1 
ATOM   2966  C  CA  . TYR   A 1 378  ? -12.50300  77.86100  31.88500  1.000 36.79304  ?  378  TYR   A CA  1 
ATOM   2967  C  C   . TYR   A 1 378  ? -11.28800  77.91800  30.96800  1.000 38.63357  ?  378  TYR   A C   1 
ATOM   2968  O  O   . TYR   A 1 378  ? -11.04300  76.99100  30.18600  1.000 45.06775  ?  378  TYR   A O   1 
ATOM   2969  C  CB  . TYR   A 1 378  ? -13.55400  78.88800  31.45700  1.000 43.50254  ?  378  TYR   A CB  1 
ATOM   2970  C  CG  . TYR   A 1 378  ? -14.18400  78.63600  30.10500  1.000 36.92374  ?  378  TYR   A CG  1 
ATOM   2971  C  CD1 . TYR   A 1 378  ? -15.29300  77.81000  29.97800  1.000 29.60330  ?  378  TYR   A CD1 1 
ATOM   2972  C  CD2 . TYR   A 1 378  ? -13.68200  79.23900  28.95900  1.000 43.09032  ?  378  TYR   A CD2 1 
ATOM   2973  C  CE1 . TYR   A 1 378  ? -15.87800  77.58300  28.74700  1.000 26.54183  ?  378  TYR   A CE1 1 
ATOM   2974  C  CE2 . TYR   A 1 378  ? -14.26100  79.01800  27.72200  1.000 41.24916  ?  378  TYR   A CE2 1 
ATOM   2975  C  CZ  . TYR   A 1 378  ? -15.35800  78.18900  27.62300  1.000 36.11043  ?  378  TYR   A CZ  1 
ATOM   2976  O  OH  . TYR   A 1 378  ? -15.93800  77.96500  26.39500  1.000 33.27384  ?  378  TYR   A OH  1 
ATOM   2977  N  N   . PHE   A 1 379  ? -10.51400  78.99700  31.05100  1.000 41.46628  ?  379  PHE   A N   1 
ATOM   2978  C  CA  . PHE   A 1 379  ? -9.33400   79.17500  30.21800  1.000 40.13646  ?  379  PHE   A CA  1 
ATOM   2979  C  C   . PHE   A 1 379  ? -8.06100   78.65000  30.86900  1.000 42.15593  ?  379  PHE   A C   1 
ATOM   2980  O  O   . PHE   A 1 379  ? -6.98200   78.79000  30.28500  1.000 44.94223  ?  379  PHE   A O   1 
ATOM   2981  C  CB  . PHE   A 1 379  ? -9.15900   80.65400  29.86200  1.000 34.78657  ?  379  PHE   A CB  1 
ATOM   2982  C  CG  . PHE   A 1 379  ? -10.33200  81.24400  29.13100  1.000 48.87614  ?  379  PHE   A CG  1 
ATOM   2983  C  CD1 . PHE   A 1 379  ? -10.56500  80.92800  27.80200  1.000 40.62552  ?  379  PHE   A CD1 1 
ATOM   2984  C  CD2 . PHE   A 1 379  ? -11.19800  82.11700  29.77000  1.000 51.84217  ?  379  PHE   A CD2 1 
ATOM   2985  C  CE1 . PHE   A 1 379  ? -11.64300  81.46800  27.12500  1.000 44.79381  ?  379  PHE   A CE1 1 
ATOM   2986  C  CE2 . PHE   A 1 379  ? -12.27800  82.66100  29.09900  1.000 32.33960  ?  379  PHE   A CE2 1 
ATOM   2987  C  CZ  . PHE   A 1 379  ? -12.50200  82.33500  27.77500  1.000 46.91305  ?  379  PHE   A CZ  1 
ATOM   2988  N  N   . GLY   A 1 380  ? -8.16000   78.05200  32.05300  1.000 37.23500  ?  380  GLY   A N   1 
ATOM   2989  C  CA  . GLY   A 1 380  ? -6.98700   77.49600  32.71000  1.000 36.65278  ?  380  GLY   A CA  1 
ATOM   2990  C  C   . GLY   A 1 380  ? -5.94500   78.52800  33.07600  1.000 39.56294  ?  380  GLY   A C   1 
ATOM   2991  O  O   . GLY   A 1 380  ? -4.74400   78.28200  32.90700  1.000 47.30660  ?  380  GLY   A O   1 
ATOM   2992  N  N   . VAL   A 1 381  ? -6.37600   79.68500  33.57400  1.000 40.87047  ?  381  VAL   A N   1 
ATOM   2993  C  CA  . VAL   A 1 381  ? -5.43900   80.74900  33.91400  1.000 39.95441  ?  381  VAL   A CA  1 
ATOM   2994  C  C   . VAL   A 1 381  ? -4.62000   80.31700  35.12500  1.000 46.60194  ?  381  VAL   A C   1 
ATOM   2995  O  O   . VAL   A 1 381  ? -5.17300   79.96700  36.17500  1.000 46.47526  ?  381  VAL   A O   1 
ATOM   2996  C  CB  . VAL   A 1 381  ? -6.17500   82.06800  34.17800  1.000 25.95913  ?  381  VAL   A CB  1 
ATOM   2997  C  CG1 . VAL   A 1 381  ? -5.19500   83.22800  34.15100  1.000 29.96483  ?  381  VAL   A CG1 1 
ATOM   2998  C  CG2 . VAL   A 1 381  ? -7.28200   82.27300  33.15400  1.000 33.75586  ?  381  VAL   A CG2 1 
ATOM   2999  N  N   . THR   A 1 382  ? -3.30200   80.33000  34.97800  1.000 46.31703  ?  382  THR   A N   1 
ATOM   3000  C  CA  . THR   A 1 382  ? -2.35800   79.94500  36.01400  1.000 40.92418  ?  382  THR   A CA  1 
ATOM   3001  C  C   . THR   A 1 382  ? -1.54700   81.14900  36.46500  1.000 39.10006  ?  382  THR   A C   1 
ATOM   3002  O  O   . THR   A 1 382  ? -1.56200   82.19900  35.81500  1.000 42.12750  ?  382  THR   A O   1 
ATOM   3003  C  CB  . THR   A 1 382  ? -1.40400   78.85800  35.49900  1.000 37.34033  ?  382  THR   A CB  1 
ATOM   3004  O  OG1 . THR   A 1 382  ? -0.88400   79.24700  34.22100  1.000 42.30351  ?  382  THR   A OG1 1 
ATOM   3005  C  CG2 . THR   A 1 382  ? -2.12100   77.52400  35.38200  1.000 44.66378  ?  382  THR   A CG2 1 
ATOM   3006  N  N   . PRO   A 1 383  ? -0.82100   81.04400  37.58500  1.000 30.87120  ?  383  PRO   A N   1 
ATOM   3007  C  CA  . PRO   A 1 383  ? 0.04400    82.16200  37.99500  1.000 28.91157  ?  383  PRO   A CA  1 
ATOM   3008  C  C   . PRO   A 1 383  ? 1.19500    82.40300  37.03100  1.000 48.93212  ?  383  PRO   A C   1 
ATOM   3009  O  O   . PRO   A 1 383  ? 2.01400    83.31100  37.22900  1.000 57.33254  ?  383  PRO   A O   1 
ATOM   3010  C  CB  . PRO   A 1 383  ? 0.55100    81.72600  39.37400  1.000 31.07281  ?  383  PRO   A CB  1 
ATOM   3011  C  CG  . PRO   A 1 383  ? -0.50400   80.81500  39.88700  1.000 41.99896  ?  383  PRO   A CG  1 
ATOM   3012  C  CD  . PRO   A 1 383  ? -1.03600   80.08600  38.68400  1.000 38.08527  ?  383  PRO   A CD  1 
ATOM   3013  N  N   . ALA   A 1 384  ? 1.26500    81.60100  35.97200  1.000 43.79320  ?  384  ALA   A N   1 
ATOM   3014  C  CA  . ALA   A 1 384  ? 2.31100    81.72400  34.97200  1.000 42.01072  ?  384  ALA   A CA  1 
ATOM   3015  C  C   . ALA   A 1 384  ? 1.84500    82.45600  33.71900  1.000 36.80123  ?  384  ALA   A C   1 
ATOM   3016  O  O   . ALA   A 1 384  ? 2.61000    82.56100  32.75600  1.000 38.71660  ?  384  ALA   A O   1 
ATOM   3017  C  CB  . ALA   A 1 384  ? 2.85200    80.34000  34.61300  1.000 35.76890  ?  384  ALA   A CB  1 
ATOM   3018  N  N   . ASP   A 1 385  ? 0.62100    82.97600  33.71400  1.000 39.02933  ?  385  ASP   A N   1 
ATOM   3019  C  CA  . ASP   A 1 385  ? 0.07700    83.65000  32.54600  1.000 38.26233  ?  385  ASP   A CA  1 
ATOM   3020  C  C   . ASP   A 1 385  ? 0.44400    85.13400  32.54800  1.000 39.02709  ?  385  ASP   A C   1 
ATOM   3021  O  O   . ASP   A 1 385  ? 0.90700    85.69200  33.54500  1.000 43.94263  ?  385  ASP   A O   1 
ATOM   3022  C  CB  . ASP   A 1 385  ? -1.44200   83.47600  32.48600  1.000 39.47800  ?  385  ASP   A CB  1 
ATOM   3023  C  CG  . ASP   A 1 385  ? -1.85500   82.15900  31.85200  1.000 42.26571  ?  385  ASP   A CG  1 
ATOM   3024  O  OD1 . ASP   A 1 385  ? -1.41300   81.87600  30.71900  1.000 32.40588  ?  385  ASP   A OD1 1 
ATOM   3025  O  OD2 . ASP   A 1 385  ? -2.62100   81.40400  32.48900  1.000 49.05397  -1 385  ASP   A OD2 1 
ATOM   3026  N  N   . LYS   A 1 386  ? 0.23100    85.77100  31.39900  1.000 35.02255  ?  386  LYS   A N   1 
ATOM   3027  C  CA  . LYS   A 1 386  ? 0.47800    87.19600  31.22900  1.000 39.10819  ?  386  LYS   A CA  1 
ATOM   3028  C  C   . LYS   A 1 386  ? -0.63400   87.78400  30.37600  1.000 39.70408  ?  386  LYS   A C   1 
ATOM   3029  O  O   . LYS   A 1 386  ? -0.90800   87.28400  29.28100  1.000 44.87919  ?  386  LYS   A O   1 
ATOM   3030  C  CB  . LYS   A 1 386  ? 1.84300    87.45200  30.57700  1.000 37.37976  ?  386  LYS   A CB  1 
ATOM   3031  C  CG  . LYS   A 1 386  ? 3.01900    87.40800  31.54000  1.000 40.77117  ?  386  LYS   A CG  1 
ATOM   3032  C  CD  . LYS   A 1 386  ? 4.27100    86.88700  30.84800  1.000 47.37802  ?  386  LYS   A CD  1 
ATOM   3033  C  CE  . LYS   A 1 386  ? 5.53200    87.20400  31.63900  1.000 35.33268  ?  386  LYS   A CE  1 
ATOM   3034  N  NZ  . LYS   A 1 386  ? 5.92800    88.63600  31.51300  1.000 52.61178  ?  386  LYS   A NZ  1 
ATOM   3035  N  N   . ALA   A 1 387  ? -1.27300   88.83500  30.88200  1.000 34.32514  ?  387  ALA   A N   1 
ATOM   3036  C  CA  . ALA   A 1 387  ? -2.35500   89.50800  30.18100  1.000 29.74416  ?  387  ALA   A CA  1 
ATOM   3037  C  C   . ALA   A 1 387  ? -2.07000   91.00000  30.12800  1.000 47.68700  ?  387  ALA   A C   1 
ATOM   3038  O  O   . ALA   A 1 387  ? -1.36000   91.54300  30.98200  1.000 54.92061  ?  387  ALA   A O   1 
ATOM   3039  C  CB  . ALA   A 1 387  ? -3.70800   89.25900  30.85900  1.000 27.45912  ?  387  ALA   A CB  1 
ATOM   3040  N  N   . LEU   A 1 388  ? -2.62800   91.66400  29.12100  1.000 33.34158  ?  388  LEU   A N   1 
ATOM   3041  C  CA  . LEU   A 1 388  ? -2.45900   93.10100  28.95500  1.000 42.92119  ?  388  LEU   A CA  1 
ATOM   3042  C  C   . LEU   A 1 388  ? -3.75900   93.82900  29.26600  1.000 43.22302  ?  388  LEU   A C   1 
ATOM   3043  O  O   . LEU   A 1 388  ? -4.84400   93.38000  28.88000  1.000 38.20876  ?  388  LEU   A O   1 
ATOM   3044  C  CB  . LEU   A 1 388  ? -1.98300   93.45600  27.53800  1.000 39.50408  ?  388  LEU   A CB  1 
ATOM   3045  C  CG  . LEU   A 1 388  ? -2.69800   92.91600  26.29900  1.000 42.50852  ?  388  LEU   A CG  1 
ATOM   3046  C  CD1 . LEU   A 1 388  ? -2.66900   93.92400  25.16800  1.000 38.21712  ?  388  LEU   A CD1 1 
ATOM   3047  C  CD2 . LEU   A 1 388  ? -2.01800   91.66000  25.84000  1.000 40.42461  ?  388  LEU   A CD2 1 
ATOM   3048  N  N   . VAL   A 1 389  ? -3.63900   94.95000  29.97900  1.000 45.22185  ?  389  VAL   A N   1 
ATOM   3049  C  CA  . VAL   A 1 389  ? -4.77100   95.83000  30.24500  1.000 30.92550  ?  389  VAL   A CA  1 
ATOM   3050  C  C   . VAL   A 1 389  ? -4.95400   96.72100  29.02500  1.000 46.42216  ?  389  VAL   A C   1 
ATOM   3051  O  O   . VAL   A 1 389  ? -4.43000   97.84000  28.96200  1.000 58.26887  ?  389  VAL   A O   1 
ATOM   3052  C  CB  . VAL   A 1 389  ? -4.55800   96.65300  31.52500  1.000 24.04955  ?  389  VAL   A CB  1 
ATOM   3053  C  CG1 . VAL   A 1 389  ? -5.78300   97.50000  31.82600  1.000 49.47679  ?  389  VAL   A CG1 1 
ATOM   3054  C  CG2 . VAL   A 1 389  ? -4.25900   95.73100  32.69600  1.000 28.46447  ?  389  VAL   A CG2 1 
ATOM   3055  N  N   . TYR   A 1 390  ? -5.69500   96.21800  28.04000  1.000 40.69789  ?  390  TYR   A N   1 
ATOM   3056  C  CA  . TYR   A 1 390  ? -5.85100   96.86500  26.74100  1.000 50.00649  ?  390  TYR   A CA  1 
ATOM   3057  C  C   . TYR   A 1 390  ? -6.99700   97.87500  26.75400  1.000 49.45239  ?  390  TYR   A C   1 
ATOM   3058  O  O   . TYR   A 1 390  ? -6.78800   99.06700  26.50600  1.000 45.42293  ?  390  TYR   A O   1 
ATOM   3059  C  CB  . TYR   A 1 390  ? -6.07000   95.79200  25.66400  1.000 38.30999  ?  390  TYR   A CB  1 
ATOM   3060  C  CG  . TYR   A 1 390  ? -6.20700   96.30900  24.24700  1.000 41.37987  ?  390  TYR   A CG  1 
ATOM   3061  C  CD1 . TYR   A 1 390  ? -5.09200   96.47200  23.43400  1.000 52.02546  ?  390  TYR   A CD1 1 
ATOM   3062  C  CD2 . TYR   A 1 390  ? -7.45500   96.61000  23.71200  1.000 48.20693  ?  390  TYR   A CD2 1 
ATOM   3063  C  CE1 . TYR   A 1 390  ? -5.21500   96.93100  22.13300  1.000 54.47257  ?  390  TYR   A CE1 1 
ATOM   3064  C  CE2 . TYR   A 1 390  ? -7.58500   97.07400  22.41200  1.000 46.64134  ?  390  TYR   A CE2 1 
ATOM   3065  C  CZ  . TYR   A 1 390  ? -6.46100   97.23400  21.62900  1.000 55.00069  ?  390  TYR   A CZ  1 
ATOM   3066  O  OH  . TYR   A 1 390  ? -6.58100   97.69300  20.33700  1.000 57.78420  ?  390  TYR   A OH  1 
ATOM   3067  N  N   . SER   A 1 391  ? -8.20800   97.40700  27.05000  1.000 49.47013  ?  391  SER   A N   1 
ATOM   3068  C  CA  . SER   A 1 391  ? -9.38100   98.26600  26.98600  1.000 46.08787  ?  391  SER   A CA  1 
ATOM   3069  C  C   . SER   A 1 391  ? -9.31200   99.36100  28.04300  1.000 44.51062  ?  391  SER   A C   1 
ATOM   3070  O  O   . SER   A 1 391  ? -8.70800   99.19400  29.10500  1.000 55.24651  ?  391  SER   A O   1 
ATOM   3071  C  CB  . SER   A 1 391  ? -10.64900  97.43400  27.17200  1.000 41.76263  ?  391  SER   A CB  1 
ATOM   3072  O  OG  . SER   A 1 391  ? -10.59300  96.24900  26.39700  1.000 50.30783  ?  391  SER   A OG  1 
ATOM   3073  N  N   . SER   A 1 392  ? -9.93800   100.49500 27.73500  1.000 36.24328  ?  392  SER   A N   1 
ATOM   3074  C  CA  . SER   A 1 392  ? -10.00700  101.59700 28.68400  1.000 36.99261  ?  392  SER   A CA  1 
ATOM   3075  C  C   . SER   A 1 392  ? -10.74700  101.17100 29.94600  1.000 50.58404  ?  392  SER   A C   1 
ATOM   3076  O  O   . SER   A 1 392  ? -11.66000  100.34400 29.90600  1.000 51.46855  ?  392  SER   A O   1 
ATOM   3077  C  CB  . SER   A 1 392  ? -10.70400  102.79700 28.04500  1.000 42.38933  ?  392  SER   A CB  1 
ATOM   3078  O  OG  . SER   A 1 392  ? -11.47000  103.50900 29.00100  1.000 51.79832  ?  392  SER   A OG  1 
ATOM   3079  N  N   . PHE   A 1 393  ? -10.34900  101.75000 31.08200  1.000 42.64384  ?  393  PHE   A N   1 
ATOM   3080  C  CA  . PHE   A 1 393  ? -10.99000  101.37700 32.33700  1.000 51.66713  ?  393  PHE   A CA  1 
ATOM   3081  C  C   . PHE   A 1 393  ? -12.42400  101.88600 32.43800  1.000 56.90012  ?  393  PHE   A C   1 
ATOM   3082  O  O   . PHE   A 1 393  ? -13.12800  101.50900 33.38200  1.000 63.34698  ?  393  PHE   A O   1 
ATOM   3083  C  CB  . PHE   A 1 393  ? -10.15000  101.84700 33.53600  1.000 44.88591  ?  393  PHE   A CB  1 
ATOM   3084  C  CG  . PHE   A 1 393  ? -10.26800  103.32000 33.86000  1.000 48.16857  ?  393  PHE   A CG  1 
ATOM   3085  C  CD1 . PHE   A 1 393  ? -10.30900  104.28500 32.86500  1.000 48.30399  ?  393  PHE   A CD1 1 
ATOM   3086  C  CD2 . PHE   A 1 393  ? -10.30800  103.73200 35.18600  1.000 30.71289  ?  393  PHE   A CD2 1 
ATOM   3087  C  CE1 . PHE   A 1 393  ? -10.40800  105.63000 33.18600  1.000 50.60460  ?  393  PHE   A CE1 1 
ATOM   3088  C  CE2 . PHE   A 1 393  ? -10.40400  105.07300 35.51200  1.000 38.10252  ?  393  PHE   A CE2 1 
ATOM   3089  C  CZ  . PHE   A 1 393  ? -10.45400  106.02300 34.51200  1.000 41.57017  ?  393  PHE   A CZ  1 
ATOM   3090  N  N   . SER   A 1 394  ? -12.87900  102.70200 31.48300  1.000 40.92389  ?  394  SER   A N   1 
ATOM   3091  C  CA  . SER   A 1 394  ? -14.25800  103.17100 31.41500  1.000 53.90598  ?  394  SER   A CA  1 
ATOM   3092  C  C   . SER   A 1 394  ? -15.19700  102.17600 30.73500  1.000 52.84612  ?  394  SER   A C   1 
ATOM   3093  O  O   . SER   A 1 394  ? -16.37600  102.49200 30.54000  1.000 66.78379  ?  394  SER   A O   1 
ATOM   3094  C  CB  . SER   A 1 394  ? -14.31800  104.51600 30.68400  1.000 51.68960  ?  394  SER   A CB  1 
ATOM   3095  O  OG  . SER   A 1 394  ? -13.44100  105.45600 31.27800  1.000 56.22633  ?  394  SER   A OG  1 
ATOM   3096  N  N   . PHE   A 1 395  ? -14.71000  100.99200 30.36800  1.000 48.93842  ?  395  PHE   A N   1 
ATOM   3097  C  CA  . PHE   A 1 395  ? -15.53000  99.96200  29.74800  1.000 45.92723  ?  395  PHE   A CA  1 
ATOM   3098  C  C   . PHE   A 1 395  ? -15.34200  98.64600  30.48900  1.000 40.96763  ?  395  PHE   A C   1 
ATOM   3099  O  O   . PHE   A 1 395  ? -14.30400  98.41000  31.11200  1.000 55.04326  ?  395  PHE   A O   1 
ATOM   3100  C  CB  . PHE   A 1 395  ? -15.18600  99.77700  28.26200  1.000 46.33542  ?  395  PHE   A CB  1 
ATOM   3101  C  CG  . PHE   A 1 395  ? -15.40200  101.00900 27.43000  1.000 66.15546  ?  395  PHE   A CG  1 
ATOM   3102  C  CD1 . PHE   A 1 395  ? -16.67200  101.53500 27.26600  1.000 71.69872  ?  395  PHE   A CD1 1 
ATOM   3103  C  CD2 . PHE   A 1 395  ? -14.33700  101.63300 26.80200  1.000 76.82587  ?  395  PHE   A CD2 1 
ATOM   3104  C  CE1 . PHE   A 1 395  ? -16.87600  102.66700 26.49900  1.000 73.10489  ?  395  PHE   A CE1 1 
ATOM   3105  C  CE2 . PHE   A 1 395  ? -14.53400  102.76600 26.03200  1.000 66.53904  ?  395  PHE   A CE2 1 
ATOM   3106  C  CZ  . PHE   A 1 395  ? -15.80500  103.28300 25.88100  1.000 62.25212  ?  395  PHE   A CZ  1 
ATOM   3107  N  N   . ASP   A 1 396  ? -16.36000  97.78600  30.41100  1.000 58.63261  ?  396  ASP   A N   1 
ATOM   3108  C  CA  . ASP   A 1 396  ? -16.32800  96.51100  31.11900  1.000 45.37129  ?  396  ASP   A CA  1 
ATOM   3109  C  C   . ASP   A 1 396  ? -15.26800  95.56000  30.58000  1.000 47.22106  ?  396  ASP   A C   1 
ATOM   3110  O  O   . ASP   A 1 396  ? -15.00900  94.53100  31.21400  1.000 57.77084  ?  396  ASP   A O   1 
ATOM   3111  C  CB  . ASP   A 1 396  ? -17.70600  95.84400  31.06400  1.000 54.31944  ?  396  ASP   A CB  1 
ATOM   3112  C  CG  . ASP   A 1 396  ? -18.19500  95.63000  29.64500  1.000 68.57542  ?  396  ASP   A CG  1 
ATOM   3113  O  OD1 . ASP   A 1 396  ? -17.68800  96.31200  28.72900  1.000 82.38624  ?  396  ASP   A OD1 1 
ATOM   3114  O  OD2 . ASP   A 1 396  ? -19.09300  94.78300  29.44900  1.000 56.10958  -1 396  ASP   A OD2 1 
ATOM   3115  N  N   . GLY   A 1 397  ? -14.65700  95.87200  29.43500  1.000 45.88469  ?  397  GLY   A N   1 
ATOM   3116  C  CA  . GLY   A 1 397  ? -13.54900  95.06700  28.95300  1.000 49.45539  ?  397  GLY   A CA  1 
ATOM   3117  C  C   . GLY   A 1 397  ? -12.34700  95.09200  29.87200  1.000 43.02042  ?  397  GLY   A C   1 
ATOM   3118  O  O   . GLY   A 1 397  ? -11.64900  94.08400  30.00800  1.000 46.52472  ?  397  GLY   A O   1 
ATOM   3119  N  N   . SER   A 1 398  ? -12.08800  96.23500  30.51900  1.000 40.64938  ?  398  SER   A N   1 
ATOM   3120  C  CA  . SER   A 1 398  ? -10.97800  96.32000  31.46300  1.000 40.16585  ?  398  SER   A CA  1 
ATOM   3121  C  C   . SER   A 1 398  ? -11.22900  95.47800  32.70600  1.000 32.37009  ?  398  SER   A C   1 
ATOM   3122  O  O   . SER   A 1 398  ? -10.27500  95.02000  33.34400  1.000 43.07300  ?  398  SER   A O   1 
ATOM   3123  C  CB  . SER   A 1 398  ? -10.72900  97.77300  31.86200  1.000 37.58006  ?  398  SER   A CB  1 
ATOM   3124  O  OG  . SER   A 1 398  ? -11.80400  98.27900  32.63100  1.000 44.03088  ?  398  SER   A OG  1 
ATOM   3125  N  N   . ALA   A 1 399  ? -12.49700  95.27600  33.07300  1.000 36.41849  ?  399  ALA   A N   1 
ATOM   3126  C  CA  . ALA   A 1 399  ? -12.80300  94.40400  34.20100  1.000 39.30374  ?  399  ALA   A CA  1 
ATOM   3127  C  C   . ALA   A 1 399  ? -12.34500  92.97800  33.92700  1.000 42.77298  ?  399  ALA   A C   1 
ATOM   3128  O  O   . ALA   A 1 399  ? -11.80800  92.30700  34.81600  1.000 45.23447  ?  399  ALA   A O   1 
ATOM   3129  C  CB  . ALA   A 1 399  ? -14.30000  94.44100  34.50600  1.000 38.10586  ?  399  ALA   A CB  1 
ATOM   3130  N  N   . LEU   A 1 400  ? -12.54700  92.49900  32.69800  1.000 41.98472  ?  400  LEU   A N   1 
ATOM   3131  C  CA  . LEU   A 1 400  ? -12.01300  91.19600  32.31700  1.000 41.11195  ?  400  LEU   A CA  1 
ATOM   3132  C  C   . LEU   A 1 400  ? -10.49000  91.22300  32.28300  1.000 45.91620  ?  400  LEU   A C   1 
ATOM   3133  O  O   . LEU   A 1 400  ? -9.83600   90.24000  32.65000  1.000 44.00958  ?  400  LEU   A O   1 
ATOM   3134  C  CB  . LEU   A 1 400  ? -12.58400  90.77700  30.96000  1.000 34.23205  ?  400  LEU   A CB  1 
ATOM   3135  C  CG  . LEU   A 1 400  ? -12.35500  89.35200  30.44600  1.000 40.19709  ?  400  LEU   A CG  1 
ATOM   3136  C  CD1 . LEU   A 1 400  ? -13.47900  88.95800  29.50500  1.000 36.49665  ?  400  LEU   A CD1 1 
ATOM   3137  C  CD2 . LEU   A 1 400  ? -11.01400  89.21300  29.73700  1.000 42.82290  ?  400  LEU   A CD2 1 
ATOM   3138  N  N   . ASP   A 1 401  ? -9.90900   92.34300  31.84800  1.000 40.36125  ?  401  ASP   A N   1 
ATOM   3139  C  CA  . ASP   A 1 401  ? -8.45600   92.44800  31.78400  1.000 31.78499  ?  401  ASP   A CA  1 
ATOM   3140  C  C   . ASP   A 1 401  ? -7.83700   92.44200  33.17600  1.000 40.31446  ?  401  ASP   A C   1 
ATOM   3141  O  O   . ASP   A 1 401  ? -6.82300   91.77300  33.40800  1.000 49.90055  ?  401  ASP   A O   1 
ATOM   3142  C  CB  . ASP   A 1 401  ? -8.05200   93.71800  31.03200  1.000 29.31561  ?  401  ASP   A CB  1 
ATOM   3143  C  CG  . ASP   A 1 401  ? -8.47300   93.69800  29.57500  1.000 48.20684  ?  401  ASP   A CG  1 
ATOM   3144  O  OD1 . ASP   A 1 401  ? -8.96700   92.65000  29.10800  1.000 58.48555  ?  401  ASP   A OD1 1 
ATOM   3145  O  OD2 . ASP   A 1 401  ? -8.30700   94.73300  28.89500  1.000 52.10103  -1 401  ASP   A OD2 1 
ATOM   3146  N  N   . ILE   A 1 402  ? -8.43700   93.16700  34.11500  1.000 30.33979  ?  402  ILE   A N   1 
ATOM   3147  C  CA  . ILE   A 1 402  ? -7.80600   93.42100  35.40700  1.000 26.85023  ?  402  ILE   A CA  1 
ATOM   3148  C  C   . ILE   A 1 402  ? -8.20900   92.38500  36.44700  1.000 36.39434  ?  402  ILE   A C   1 
ATOM   3149  O  O   . ILE   A 1 402  ? -7.35900   91.83200  37.14900  1.000 48.67724  ?  402  ILE   A O   1 
ATOM   3150  C  CB  . ILE   A 1 402  ? -8.14900   94.85000  35.88100  1.000 23.65958  ?  402  ILE   A CB  1 
ATOM   3151  C  CG1 . ILE   A 1 402  ? -7.56200   95.88500  34.92100  1.000 25.22871  ?  402  ILE   A CG1 1 
ATOM   3152  C  CG2 . ILE   A 1 402  ? -7.64600   95.07800  37.29600  1.000 34.81486  ?  402  ILE   A CG2 1 
ATOM   3153  C  CD1 . ILE   A 1 402  ? -7.97900   97.30400  35.23100  1.000 27.40769  ?  402  ILE   A CD1 1 
ATOM   3154  N  N   . PHE   A 1 403  ? -9.50500   92.10100  36.56100  1.000 42.00507  ?  403  PHE   A N   1 
ATOM   3155  C  CA  . PHE   A 1 403  ? -10.01800  91.34500  37.69800  1.000 37.76093  ?  403  PHE   A CA  1 
ATOM   3156  C  C   . PHE   A 1 403  ? -9.95700   89.83500  37.50700  1.000 32.64389  ?  403  PHE   A C   1 
ATOM   3157  O  O   . PHE   A 1 403  ? -9.76800   89.10600  38.48700  1.000 30.92879  ?  403  PHE   A O   1 
ATOM   3158  C  CB  . PHE   A 1 403  ? -11.46000  91.76800  37.99000  1.000 36.61448  ?  403  PHE   A CB  1 
ATOM   3159  C  CG  . PHE   A 1 403  ? -11.60700  93.23200  38.29000  1.000 37.26307  ?  403  PHE   A CG  1 
ATOM   3160  C  CD1 . PHE   A 1 403  ? -10.74200  93.86200  39.17000  1.000 41.74519  ?  403  PHE   A CD1 1 
ATOM   3161  C  CD2 . PHE   A 1 403  ? -12.59500  93.98400  37.67700  1.000 36.05222  ?  403  PHE   A CD2 1 
ATOM   3162  C  CE1 . PHE   A 1 403  ? -10.87000  95.21100  39.44500  1.000 48.78777  ?  403  PHE   A CE1 1 
ATOM   3163  C  CE2 . PHE   A 1 403  ? -12.72700  95.33400  37.94800  1.000 40.50123  ?  403  PHE   A CE2 1 
ATOM   3164  C  CZ  . PHE   A 1 403  ? -11.86300  95.94800  38.83200  1.000 28.77070  ?  403  PHE   A CZ  1 
ATOM   3165  N  N   . THR   A 1 404  ? -10.11400  89.34300  36.27700  1.000 30.58345  ?  404  THR   A N   1 
ATOM   3166  C  CA  . THR   A 1 404  ? -10.14500  87.89800  36.07300  1.000 29.13399  ?  404  THR   A CA  1 
ATOM   3167  C  C   . THR   A 1 404  ? -8.77000   87.27600  36.27700  1.000 37.27995  ?  404  THR   A C   1 
ATOM   3168  O  O   . THR   A 1 404  ? -8.65800   86.17100  36.82100  1.000 42.00310  ?  404  THR   A O   1 
ATOM   3169  C  CB  . THR   A 1 404  ? -10.67300  87.57100  34.67700  1.000 32.77512  ?  404  THR   A CB  1 
ATOM   3170  O  OG1 . THR   A 1 404  ? -9.78800   88.11700  33.69100  1.000 35.49117  ?  404  THR   A OG1 1 
ATOM   3171  C  CG2 . THR   A 1 404  ? -12.06600  88.15200  34.48500  1.000 48.72130  ?  404  THR   A CG2 1 
ATOM   3172  N  N   . HIS   A 1 405  ? -7.71300   87.97000  35.85600  1.000 42.42563  ?  405  HIS   A N   1 
ATOM   3173  C  CA  . HIS   A 1 405  ? -6.36500   87.42200  35.92700  1.000 36.92367  ?  405  HIS   A CA  1 
ATOM   3174  C  C   . HIS   A 1 405  ? -5.69800   87.64900  37.27800  1.000 42.41606  ?  405  HIS   A C   1 
ATOM   3175  O  O   . HIS   A 1 405  ? -4.86600   86.83200  37.69100  1.000 46.85678  ?  405  HIS   A O   1 
ATOM   3176  C  CB  . HIS   A 1 405  ? -5.50000   88.02000  34.81600  1.000 37.70399  ?  405  HIS   A CB  1 
ATOM   3177  C  CG  . HIS   A 1 405  ? -6.13200   87.95000  33.46100  1.000 43.87838  ?  405  HIS   A CG  1 
ATOM   3178  N  ND1 . HIS   A 1 405  ? -6.58700   89.06700  32.79300  1.000 36.36491  ?  405  HIS   A ND1 1 
ATOM   3179  C  CD2 . HIS   A 1 405  ? -6.40100   86.89500  32.65500  1.000 37.35763  ?  405  HIS   A CD2 1 
ATOM   3180  C  CE1 . HIS   A 1 405  ? -7.10000   88.70400  31.63100  1.000 40.42066  ?  405  HIS   A CE1 1 
ATOM   3181  N  NE2 . HIS   A 1 405  ? -7.00000   87.39200  31.52300  1.000 43.43963  ?  405  HIS   A NE2 1 
ATOM   3182  N  N   . LEU   A 1 406  ? -6.03800   88.73800  37.97500  1.000 29.50570  ?  406  LEU   A N   1 
ATOM   3183  C  CA  . LEU   A 1 406  ? -5.48100   88.95900  39.30600  1.000 30.95268  ?  406  LEU   A CA  1 
ATOM   3184  C  C   . LEU   A 1 406  ? -5.88900   87.85600  40.27600  1.000 44.27242  ?  406  LEU   A C   1 
ATOM   3185  O  O   . LEU   A 1 406  ? -5.12100   87.51200  41.18100  1.000 50.34198  ?  406  LEU   A O   1 
ATOM   3186  C  CB  . LEU   A 1 406  ? -5.91200   90.32300  39.84900  1.000 26.86327  ?  406  LEU   A CB  1 
ATOM   3187  C  CG  . LEU   A 1 406  ? -5.07900   91.53400  39.42700  1.000 39.50753  ?  406  LEU   A CG  1 
ATOM   3188  C  CD1 . LEU   A 1 406  ? -5.47700   92.76900  40.22400  1.000 37.05644  ?  406  LEU   A CD1 1 
ATOM   3189  C  CD2 . LEU   A 1 406  ? -3.59500   91.24800  39.58500  1.000 44.13631  ?  406  LEU   A CD2 1 
ATOM   3190  N  N   . LEU   A 1 407  ? -7.08200   87.28900  40.10600  1.000 34.80044  ?  407  LEU   A N   1 
ATOM   3191  C  CA  . LEU   A 1 407  ? -7.52700   86.20300  40.96800  1.000 34.10731  ?  407  LEU   A CA  1 
ATOM   3192  C  C   . LEU   A 1 407  ? -6.90100   84.86300  40.61100  1.000 45.71358  ?  407  LEU   A C   1 
ATOM   3193  O  O   . LEU   A 1 407  ? -7.22700   83.85600  41.25000  1.000 46.55024  ?  407  LEU   A O   1 
ATOM   3194  C  CB  . LEU   A 1 407  ? -9.05400   86.08300  40.92700  1.000 37.43961  ?  407  LEU   A CB  1 
ATOM   3195  C  CG  . LEU   A 1 407  ? -9.84400   87.15900  41.67500  1.000 43.35538  ?  407  LEU   A CG  1 
ATOM   3196  C  CD1 . LEU   A 1 407  ? -11.27900  86.71400  41.91000  1.000 40.31447  ?  407  LEU   A CD1 1 
ATOM   3197  C  CD2 . LEU   A 1 407  ? -9.17300   87.51500  42.99200  1.000 38.41666  ?  407  LEU   A CD2 1 
ATOM   3198  N  N   . ALA   A 1 408  ? -6.01600   84.81900  39.61900  1.000 37.91807  ?  408  ALA   A N   1 
ATOM   3199  C  CA  . ALA   A 1 408  ? -5.37900   83.57900  39.20300  1.000 43.27273  ?  408  ALA   A CA  1 
ATOM   3200  C  C   . ALA   A 1 408  ? -3.87300   83.59600  39.40100  1.000 39.06328  ?  408  ALA   A C   1 
ATOM   3201  O  O   . ALA   A 1 408  ? -3.22200   82.56500  39.20100  1.000 42.94655  ?  408  ALA   A O   1 
ATOM   3202  C  CB  . ALA   A 1 408  ? -5.70900   83.28000  37.73800  1.000 35.41282  ?  408  ALA   A CB  1 
ATOM   3203  N  N   . GLY   A 1 409  ? -3.30700   84.72900  39.80200  1.000 35.33614  ?  409  GLY   A N   1 
ATOM   3204  C  CA  . GLY   A 1 409  ? -1.88200   84.84400  40.00400  1.000 44.82518  ?  409  GLY   A CA  1 
ATOM   3205  C  C   . GLY   A 1 409  ? -1.10100   85.30700  38.79600  1.000 48.90693  ?  409  GLY   A C   1 
ATOM   3206  O  O   . GLY   A 1 409  ? 0.13500    85.29300  38.83900  1.000 47.76940  ?  409  GLY   A O   1 
ATOM   3207  N  N   . ALA   A 1 410  ? -1.77600   85.71700  37.72500  1.000 43.32682  ?  410  ALA   A N   1 
ATOM   3208  C  CA  . ALA   A 1 410  ? -1.10600   86.12600  36.50100  1.000 36.84792  ?  410  ALA   A CA  1 
ATOM   3209  C  C   . ALA   A 1 410  ? -0.57700   87.55300  36.63100  1.000 42.25919  ?  410  ALA   A C   1 
ATOM   3210  O  O   . ALA   A 1 410  ? -0.76800   88.23100  37.64500  1.000 42.21164  ?  410  ALA   A O   1 
ATOM   3211  C  CB  . ALA   A 1 410  ? -2.05000   85.99700  35.30900  1.000 43.15862  ?  410  ALA   A CB  1 
ATOM   3212  N  N   . ALA   A 1 411  ? 0.09200    88.02000  35.58000  1.000 29.22092  ?  411  ALA   A N   1 
ATOM   3213  C  CA  . ALA   A 1 411  ? 0.72900    89.33100  35.56200  1.000 34.50235  ?  411  ALA   A CA  1 
ATOM   3214  C  C   . ALA   A 1 411  ? 0.01200    90.22600  34.56200  1.000 48.03373  ?  411  ALA   A C   1 
ATOM   3215  O  O   . ALA   A 1 411  ? -0.10400   89.87700  33.38200  1.000 55.51853  ?  411  ALA   A O   1 
ATOM   3216  C  CB  . ALA   A 1 411  ? 2.21100    89.21300  35.21000  1.000 44.95198  ?  411  ALA   A CB  1 
ATOM   3217  N  N   . LEU   A 1 412  ? -0.46300   91.37600  35.03400  1.000 45.62431  ?  412  LEU   A N   1 
ATOM   3218  C  CA  . LEU   A 1 412  ? -1.08800   92.37100  34.17400  1.000 40.99070  ?  412  LEU   A CA  1 
ATOM   3219  C  C   . LEU   A 1 412  ? -0.01700   93.28700  33.59800  1.000 41.45968  ?  412  LEU   A C   1 
ATOM   3220  O  O   . LEU   A 1 412  ? 0.85100    93.77200  34.33000  1.000 40.63214  ?  412  LEU   A O   1 
ATOM   3221  C  CB  . LEU   A 1 412  ? -2.11700   93.19300  34.95100  1.000 40.00999  ?  412  LEU   A CB  1 
ATOM   3222  C  CG  . LEU   A 1 412  ? -3.16600   92.43000  35.75800  1.000 40.79457  ?  412  LEU   A CG  1 
ATOM   3223  C  CD1 . LEU   A 1 412  ? -4.10600   93.40600  36.44800  1.000 44.94443  ?  412  LEU   A CD1 1 
ATOM   3224  C  CD2 . LEU   A 1 412  ? -3.93900   91.47200  34.86800  1.000 37.33960  ?  412  LEU   A CD2 1 
ATOM   3225  N  N   . HIS   A 1 413  ? -0.08000   93.52300  32.29100  1.000 37.15893  ?  413  HIS   A N   1 
ATOM   3226  C  CA  . HIS   A 1 413  ? 0.85000    94.41400  31.60600  1.000 46.22754  ?  413  HIS   A CA  1 
ATOM   3227  C  C   . HIS   A 1 413  ? 0.07400    95.62500  31.10500  1.000 43.53235  ?  413  HIS   A C   1 
ATOM   3228  O  O   . HIS   A 1 413  ? -0.75900   95.50600  30.20100  1.000 46.81237  ?  413  HIS   A O   1 
ATOM   3229  C  CB  . HIS   A 1 413  ? 1.55800    93.69100  30.46300  1.000 39.75837  ?  413  HIS   A CB  1 
ATOM   3230  C  CG  . HIS   A 1 413  ? 2.58800    92.70800  30.92300  1.000 39.65962  ?  413  HIS   A CG  1 
ATOM   3231  N  ND1 . HIS   A 1 413  ? 3.94100    92.96400  30.86300  1.000 34.00390  ?  413  HIS   A ND1 1 
ATOM   3232  C  CD2 . HIS   A 1 413  ? 2.46300    91.47200  31.46200  1.000 50.36911  ?  413  HIS   A CD2 1 
ATOM   3233  C  CE1 . HIS   A 1 413  ? 4.60500    91.92600  31.33800  1.000 54.14794  ?  413  HIS   A CE1 1 
ATOM   3234  N  NE2 . HIS   A 1 413  ? 3.73200    91.00700  31.71000  1.000 42.74685  ?  413  HIS   A NE2 1 
ATOM   3235  N  N   . ILE   A 1 414  ? 0.34700    96.78700  31.69700  1.000 34.50832  ?  414  ILE   A N   1 
ATOM   3236  C  CA  . ILE   A 1 414  ? -0.34600   98.00800  31.30700  1.000 38.05967  ?  414  ILE   A CA  1 
ATOM   3237  C  C   . ILE   A 1 414  ? 0.07800    98.40300  29.90000  1.000 47.55851  ?  414  ILE   A C   1 
ATOM   3238  O  O   . ILE   A 1 414  ? 1.27300    98.53300  29.60600  1.000 53.99353  ?  414  ILE   A O   1 
ATOM   3239  C  CB  . ILE   A 1 414  ? -0.06300   99.13300  32.31200  1.000 37.43855  ?  414  ILE   A CB  1 
ATOM   3240  C  CG1 . ILE   A 1 414  ? -0.58200   98.75300  33.69900  1.000 36.03741  ?  414  ILE   A CG1 1 
ATOM   3241  C  CG2 . ILE   A 1 414  ? -0.68900   100.43500 31.84100  1.000 34.24946  ?  414  ILE   A CG2 1 
ATOM   3242  C  CD1 . ILE   A 1 414  ? -2.06900   98.49500  33.74100  1.000 49.79662  ?  414  ILE   A CD1 1 
ATOM   3243  N  N   . VAL   A 1 415  ? -0.90200   98.59500  29.02500  1.000 51.70488  ?  415  VAL   A N   1 
ATOM   3244  C  CA  . VAL   A 1 415  ? -0.65400   98.96400  27.63500  1.000 61.06526  ?  415  VAL   A CA  1 
ATOM   3245  C  C   . VAL   A 1 415  ? -0.70700   100.48500 27.53400  1.000 75.57405  ?  415  VAL   A C   1 
ATOM   3246  O  O   . VAL   A 1 415  ? -1.76900   101.07300 27.79800  1.000 65.06097  ?  415  VAL   A O   1 
ATOM   3247  C  CB  . VAL   A 1 415  ? -1.67200   98.31900  26.69000  1.000 63.66021  ?  415  VAL   A CB  1 
ATOM   3248  C  CG1 . VAL   A 1 415  ? -1.59200   98.95000  25.31000  1.000 67.60608  ?  415  VAL   A CG1 1 
ATOM   3249  C  CG2 . VAL   A 1 415  ? -1.42000   96.83800  26.60200  1.000 62.95572  ?  415  VAL   A CG2 1 
ATOM   3250  N  N   . PRO   A 1 416  ? 0.38700    101.15000 27.16800  1.000 82.35386  ?  416  PRO   A N   1 
ATOM   3251  C  CA  . PRO   A 1 416  ? 0.31600    102.59100 26.90200  1.000 75.60379  ?  416  PRO   A CA  1 
ATOM   3252  C  C   . PRO   A 1 416  ? -0.56200   102.86000 25.68900  1.000 93.58421  ?  416  PRO   A C   1 
ATOM   3253  O  O   . PRO   A 1 416  ? -0.42700   102.20700 24.65200  1.000 99.68896  ?  416  PRO   A O   1 
ATOM   3254  C  CB  . PRO   A 1 416  ? 1.77600    102.97900 26.64300  1.000 71.17226  ?  416  PRO   A CB  1 
ATOM   3255  C  CG  . PRO   A 1 416  ? 2.42200    101.71100 26.18200  1.000 72.96522  ?  416  PRO   A CG  1 
ATOM   3256  C  CD  . PRO   A 1 416  ? 1.73900    100.60900 26.94400  1.000 62.77580  ?  416  PRO   A CD  1 
ATOM   3257  N  N   . SER   A 1 417  ? -1.47200   103.82600 25.82800  1.000 93.25063  ?  417  SER   A N   1 
ATOM   3258  C  CA  . SER   A 1 417  ? -2.33100   104.20000 24.71200  1.000 96.95757  ?  417  SER   A CA  1 
ATOM   3259  C  C   . SER   A 1 417  ? -1.54000   104.71000 23.51300  1.000 94.10787  ?  417  SER   A C   1 
ATOM   3260  O  O   . SER   A 1 417  ? -2.10500   104.80400 22.41700  1.000 81.54594  ?  417  SER   A O   1 
ATOM   3261  C  CB  . SER   A 1 417  ? -3.34800   105.24900 25.16300  1.000 75.33446  ?  417  SER   A CB  1 
ATOM   3262  O  OG  . SER   A 1 417  ? -4.18400   104.73200 26.18500  1.000 68.97687  ?  417  SER   A OG  1 
ATOM   3263  N  N   . GLU   A 1 418  ? -0.25800   105.04600 23.69400  1.000 100.08561 ?  418  GLU   A N   1 
ATOM   3264  C  CA  . GLU   A 1 418  ? 0.60700    105.31300 22.54900  1.000 108.25644 ?  418  GLU   A CA  1 
ATOM   3265  C  C   . GLU   A 1 418  ? 0.66800    104.10600 21.62100  1.000 103.52227 ?  418  GLU   A C   1 
ATOM   3266  O  O   . GLU   A 1 418  ? 0.58500    104.24900 20.39600  1.000 106.62465 ?  418  GLU   A O   1 
ATOM   3267  C  CB  . GLU   A 1 418  ? 2.01200    105.69500 23.01900  1.000 99.87079  ?  418  GLU   A CB  1 
ATOM   3268  C  CG  . GLU   A 1 418  ? 2.12300    107.07100 23.66300  1.000 101.01652 ?  418  GLU   A CG  1 
ATOM   3269  C  CD  . GLU   A 1 418  ? 1.87600    107.04900 25.16100  1.000 110.97395 ?  418  GLU   A CD  1 
ATOM   3270  O  OE1 . GLU   A 1 418  ? 0.87500    106.44200 25.59700  1.000 93.51341  ?  418  GLU   A OE1 1 
ATOM   3271  O  OE2 . GLU   A 1 418  ? 2.69100    107.63700 25.90300  1.000 117.55000 -1 418  GLU   A OE2 1 
ATOM   3272  N  N   . ARG   A 1 419  ? 0.81600    102.90800 22.18800  1.000 87.93946  ?  419  ARG   A N   1 
ATOM   3273  C  CA  . ARG   A 1 419  ? 0.68300    101.68400 21.41000  1.000 94.92512  ?  419  ARG   A CA  1 
ATOM   3274  C  C   . ARG   A 1 419  ? -0.79700   101.37800 21.22700  1.000 107.52607 ?  419  ARG   A C   1 
ATOM   3275  O  O   . ARG   A 1 419  ? -1.56900   102.26400 20.84200  1.000 117.65445 ?  419  ARG   A O   1 
ATOM   3276  C  CB  . ARG   A 1 419  ? 1.40400    100.51800 22.08900  1.000 87.20771  ?  419  ARG   A CB  1 
ATOM   3277  C  CG  . ARG   A 1 419  ? 2.85700    100.80600 22.43500  1.000 88.69031  ?  419  ARG   A CG  1 
ATOM   3278  C  CD  . ARG   A 1 419  ? 3.65100    99.51900  22.61100  1.000 87.27433  ?  419  ARG   A CD  1 
ATOM   3279  N  NE  . ARG   A 1 419  ? 3.07900    98.64800  23.63000  1.000 96.76225  ?  419  ARG   A NE  1 
ATOM   3280  C  CZ  . ARG   A 1 419  ? 3.50900    98.57500  24.88200  1.000 87.72551  ?  419  ARG   A CZ  1 
ATOM   3281  N  NH1 . ARG   A 1 419  ? 4.52400    99.30900  25.30900  1.000 72.11641  ?  419  ARG   A NH1 1 
ATOM   3282  N  NH2 . ARG   A 1 419  ? 2.90400    97.74500  25.72800  1.000 72.97838  ?  419  ARG   A NH2 1 
ATOM   3283  N  N   . LYS   A 1 420  ? -1.20400   100.13200 21.48600  1.000 88.50997  ?  420  LYS   A N   1 
ATOM   3284  C  CA  . LYS   A 1 420  ? -2.61100   99.73600  21.44500  1.000 78.71734  ?  420  LYS   A CA  1 
ATOM   3285  C  C   . LYS   A 1 420  ? -3.23300   99.93800  20.06500  1.000 85.24679  ?  420  LYS   A C   1 
ATOM   3286  O  O   . LYS   A 1 420  ? -3.89700   99.03700  19.54200  1.000 83.19088  ?  420  LYS   A O   1 
ATOM   3287  C  CB  . LYS   A 1 420  ? -3.41000   100.50400 22.50400  1.000 72.42402  ?  420  LYS   A CB  1 
ATOM   3288  C  CG  . LYS   A 1 420  ? -4.90800   100.26900 22.44300  1.000 75.55458  ?  420  LYS   A CG  1 
ATOM   3289  C  CD  . LYS   A 1 420  ? -5.64700   100.99700 23.55200  1.000 67.61227  ?  420  LYS   A CD  1 
ATOM   3290  C  CE  . LYS   A 1 420  ? -7.12900   100.65700 23.52300  1.000 60.65235  ?  420  LYS   A CE  1 
ATOM   3291  N  NZ  . LYS   A 1 420  ? -7.94400   101.63500 24.29500  1.000 76.87437  ?  420  LYS   A NZ  1 
ATOM   3292  N  N   . TYR   A 1 421  ? -3.04000   101.11900 19.47600  1.000 83.52032  ?  421  TYR   A N   1 
ATOM   3293  C  CA  . TYR   A 1 421  ? -3.55000   101.41300 18.14500  1.000 82.58957  ?  421  TYR   A CA  1 
ATOM   3294  C  C   . TYR   A 1 421  ? -2.61100   100.93700 17.04700  1.000 81.32243  ?  421  TYR   A C   1 
ATOM   3295  O  O   . TYR   A 1 421  ? -3.03600   100.81100 15.89300  1.000 88.49227  ?  421  TYR   A O   1 
ATOM   3296  C  CB  . TYR   A 1 421  ? -3.79500   102.92000 17.98500  1.000 86.94702  ?  421  TYR   A CB  1 
ATOM   3297  C  CG  . TYR   A 1 421  ? -4.55600   103.57300 19.12600  1.000 98.45071  ?  421  TYR   A CG  1 
ATOM   3298  C  CD1 . TYR   A 1 421  ? -5.37100   102.82700 19.97100  1.000 93.23273  ?  421  TYR   A CD1 1 
ATOM   3299  C  CD2 . TYR   A 1 421  ? -4.46000   104.94100 19.35300  1.000 103.71438 ?  421  TYR   A CD2 1 
ATOM   3300  C  CE1 . TYR   A 1 421  ? -6.06000   103.42100 21.01100  1.000 89.54896  ?  421  TYR   A CE1 1 
ATOM   3301  C  CE2 . TYR   A 1 421  ? -5.15000   105.54500 20.39100  1.000 110.43233 ?  421  TYR   A CE2 1 
ATOM   3302  C  CZ  . TYR   A 1 421  ? -5.94800   104.78000 21.21600  1.000 103.86673 ?  421  TYR   A CZ  1 
ATOM   3303  O  OH  . TYR   A 1 421  ? -6.63600   105.37400 22.24900  1.000 92.67833  ?  421  TYR   A OH  1 
ATOM   3304  N  N   . ASP   A 1 422  ? -1.35000   100.67500 17.38100  1.000 70.85028  ?  422  ASP   A N   1 
ATOM   3305  C  CA  . ASP   A 1 422  ? -0.37700   100.10700 16.45100  1.000 67.83321  ?  422  ASP   A CA  1 
ATOM   3306  C  C   . ASP   A 1 422  ? -0.32400   98.60900  16.73500  1.000 63.90584  ?  422  ASP   A C   1 
ATOM   3307  O  O   . ASP   A 1 422  ? 0.46000    98.14000  17.56100  1.000 71.49368  ?  422  ASP   A O   1 
ATOM   3308  C  CB  . ASP   A 1 422  ? 0.98400    100.77600 16.61400  1.000 57.64715  ?  422  ASP   A CB  1 
ATOM   3309  C  CG  . ASP   A 1 422  ? 1.94000    100.44300 15.48600  1.000 65.38367  ?  422  ASP   A CG  1 
ATOM   3310  O  OD1 . ASP   A 1 422  ? 2.23300    99.24700  15.28000  1.000 69.60784  ?  422  ASP   A OD1 1 
ATOM   3311  O  OD2 . ASP   A 1 422  ? 2.39400    101.38100 14.79800  1.000 82.97740  -1 422  ASP   A OD2 1 
ATOM   3312  N  N   . LEU   A 1 423  ? -1.18300   97.85400  16.04300  1.000 47.24778  ?  423  LEU   A N   1 
ATOM   3313  C  CA  . LEU   A 1 423  ? -1.27200   96.41500  16.27100  1.000 53.47822  ?  423  LEU   A CA  1 
ATOM   3314  C  C   . LEU   A 1 423  ? 0.02800    95.69600  15.93900  1.000 63.53484  ?  423  LEU   A C   1 
ATOM   3315  O  O   . LEU   A 1 423  ? 0.24300    94.57600  16.41500  1.000 66.82338  ?  423  LEU   A O   1 
ATOM   3316  C  CB  . LEU   A 1 423  ? -2.41900   95.81500  15.45400  1.000 65.64342  ?  423  LEU   A CB  1 
ATOM   3317  C  CG  . LEU   A 1 423  ? -3.85400   96.02200  15.95200  1.000 59.68332  ?  423  LEU   A CG  1 
ATOM   3318  C  CD1 . LEU   A 1 423  ? -3.96700   95.71500  17.44200  1.000 48.43740  ?  423  LEU   A CD1 1 
ATOM   3319  C  CD2 . LEU   A 1 423  ? -4.36600   97.42300  15.64300  1.000 77.54113  ?  423  LEU   A CD2 1 
ATOM   3320  N  N   . ASP   A 1 424  ? 0.89500    96.31000  15.13300  1.000 70.62450  ?  424  ASP   A N   1 
ATOM   3321  C  CA  . ASP   A 1 424  ? 2.19400    95.70900  14.85600  1.000 71.81600  ?  424  ASP   A CA  1 
ATOM   3322  C  C   . ASP   A 1 424  ? 3.10800    95.80800  16.07100  1.000 63.34463  ?  424  ASP   A C   1 
ATOM   3323  O  O   . ASP   A 1 424  ? 3.81000    94.84700  16.40600  1.000 59.73126  ?  424  ASP   A O   1 
ATOM   3324  C  CB  . ASP   A 1 424  ? 2.82700    96.37600  13.63500  1.000 73.00076  ?  424  ASP   A CB  1 
ATOM   3325  C  CG  . ASP   A 1 424  ? 3.69600    95.42800  12.83500  1.000 87.83759  ?  424  ASP   A CG  1 
ATOM   3326  O  OD1 . ASP   A 1 424  ? 4.37900    94.58800  13.45400  1.000 94.14954  ?  424  ASP   A OD1 1 
ATOM   3327  O  OD2 . ASP   A 1 424  ? 3.70200    95.52900  11.58900  1.000 93.49870  -1 424  ASP   A OD2 1 
ATOM   3328  N  N   . ALA   A 1 425  ? 3.10200    96.95800  16.75300  1.000 63.48797  ?  425  ALA   A N   1 
ATOM   3329  C  CA  . ALA   A 1 425  ? 3.89600    97.10500  17.96800  1.000 56.60535  ?  425  ALA   A CA  1 
ATOM   3330  C  C   . ALA   A 1 425  ? 3.34100    96.26300  19.10900  1.000 63.28800  ?  425  ALA   A C   1 
ATOM   3331  O  O   . ALA   A 1 425  ? 4.11000    95.76800  19.94200  1.000 64.71861  ?  425  ALA   A O   1 
ATOM   3332  C  CB  . ALA   A 1 425  ? 3.96200    98.57600  18.37800  1.000 52.72227  ?  425  ALA   A CB  1 
ATOM   3333  N  N   . LEU   A 1 426  ? 2.01800    96.09400  19.16800  1.000 55.70846  ?  426  LEU   A N   1 
ATOM   3334  C  CA  . LEU   A 1 426  ? 1.42800    95.25600  20.20600  1.000 45.38395  ?  426  LEU   A CA  1 
ATOM   3335  C  C   . LEU   A 1 426  ? 1.83900    93.80000  20.03300  1.000 44.45629  ?  426  LEU   A C   1 
ATOM   3336  O  O   . LEU   A 1 426  ? 2.12400    93.10800  21.01800  1.000 45.42627  ?  426  LEU   A O   1 
ATOM   3337  C  CB  . LEU   A 1 426  ? -0.09400   95.39300  20.19000  1.000 44.38949  ?  426  LEU   A CB  1 
ATOM   3338  C  CG  . LEU   A 1 426  ? -0.83300   94.85400  21.41600  1.000 27.13942  ?  426  LEU   A CG  1 
ATOM   3339  C  CD1 . LEU   A 1 426  ? -0.45700   95.65300  22.65300  1.000 56.73014  ?  426  LEU   A CD1 1 
ATOM   3340  C  CD2 . LEU   A 1 426  ? -2.33500   94.88100  21.19600  1.000 35.88974  ?  426  LEU   A CD2 1 
ATOM   3341  N  N   . ASN   A 1 427  ? 1.87800    93.31800  18.78800  1.000 51.07338  ?  427  ASN   A N   1 
ATOM   3342  C  CA  . ASN   A 1 427  ? 2.34900    91.96000  18.54000  1.000 52.74012  ?  427  ASN   A CA  1 
ATOM   3343  C  C   . ASN   A 1 427  ? 3.81100    91.80200  18.93000  1.000 55.91363  ?  427  ASN   A C   1 
ATOM   3344  O  O   . ASN   A 1 427  ? 4.22200    90.72500  19.37700  1.000 57.68818  ?  427  ASN   A O   1 
ATOM   3345  C  CB  . ASN   A 1 427  ? 2.14900    91.59000  17.07000  1.000 50.80096  ?  427  ASN   A CB  1 
ATOM   3346  C  CG  . ASN   A 1 427  ? 2.44900    90.13000  16.79200  1.000 60.51316  ?  427  ASN   A CG  1 
ATOM   3347  O  OD1 . ASN   A 1 427  ? 2.16100    89.26000  17.61300  1.000 50.19228  ?  427  ASN   A OD1 1 
ATOM   3348  N  ND2 . ASN   A 1 427  ? 3.03800    89.85600  15.63300  1.000 63.08461  ?  427  ASN   A ND2 1 
ATOM   3349  N  N   . ASP   A 1 428  ? 4.60900    92.85900  18.76800  1.000 55.09099  ?  428  ASP   A N   1 
ATOM   3350  C  CA  . ASP   A 1 428  ? 5.99400    92.82000  19.22400  1.000 47.23275  ?  428  ASP   A CA  1 
ATOM   3351  C  C   . ASP   A 1 428  ? 6.06000    92.68500  20.74000  1.000 52.05332  ?  428  ASP   A C   1 
ATOM   3352  O  O   . ASP   A 1 428  ? 6.67800    91.75300  21.26700  1.000 49.43736  ?  428  ASP   A O   1 
ATOM   3353  C  CB  . ASP   A 1 428  ? 6.73800    94.07400  18.76000  1.000 50.41620  ?  428  ASP   A CB  1 
ATOM   3354  C  CG  . ASP   A 1 428  ? 7.07000    94.04400  17.28000  1.000 59.39940  ?  428  ASP   A CG  1 
ATOM   3355  O  OD1 . ASP   A 1 428  ? 7.11200    92.93900  16.69800  1.000 55.85517  ?  428  ASP   A OD1 1 
ATOM   3356  O  OD2 . ASP   A 1 428  ? 7.29900    95.12700  16.70000  1.000 53.55749  -1 428  ASP   A OD2 1 
ATOM   3357  N  N   . TYR   A 1 429  ? 5.41400    93.61100  21.45700  1.000 61.19175  ?  429  TYR   A N   1 
ATOM   3358  C  CA  . TYR   A 1 429  ? 5.42300    93.57100  22.91700  1.000 51.38185  ?  429  TYR   A CA  1 
ATOM   3359  C  C   . TYR   A 1 429  ? 4.89700    92.24000  23.43800  1.000 46.37219  ?  429  TYR   A C   1 
ATOM   3360  O  O   . TYR   A 1 429  ? 5.44300    91.68300  24.39700  1.000 50.34673  ?  429  TYR   A O   1 
ATOM   3361  C  CB  . TYR   A 1 429  ? 4.59800    94.73100  23.47900  1.000 41.82736  ?  429  TYR   A CB  1 
ATOM   3362  C  CG  . TYR   A 1 429  ? 4.61100    94.82700  24.99100  1.000 39.96558  ?  429  TYR   A CG  1 
ATOM   3363  C  CD1 . TYR   A 1 429  ? 3.72200    94.08800  25.76500  1.000 40.92413  ?  429  TYR   A CD1 1 
ATOM   3364  C  CD2 . TYR   A 1 429  ? 5.50400    95.66500  25.64500  1.000 47.04213  ?  429  TYR   A CD2 1 
ATOM   3365  C  CE1 . TYR   A 1 429  ? 3.73000    94.17300  27.14400  1.000 40.11656  ?  429  TYR   A CE1 1 
ATOM   3366  C  CE2 . TYR   A 1 429  ? 5.51700    95.75900  27.02500  1.000 45.82105  ?  429  TYR   A CE2 1 
ATOM   3367  C  CZ  . TYR   A 1 429  ? 4.62800    95.01100  27.76900  1.000 52.38853  ?  429  TYR   A CZ  1 
ATOM   3368  O  OH  . TYR   A 1 429  ? 4.63800    95.10100  29.14200  1.000 50.56063  ?  429  TYR   A OH  1 
ATOM   3369  N  N   . CYS   A 1 430  ? 3.83600    91.71600  22.82300  1.000 49.63179  ?  430  CYS   A N   1 
ATOM   3370  C  CA  . CYS   A 1 430  ? 3.31000    90.42400  23.25000  1.000 50.44618  ?  430  CYS   A CA  1 
ATOM   3371  C  C   . CYS   A 1 430  ? 4.33000    89.31500  23.03100  1.000 38.03717  ?  430  CYS   A C   1 
ATOM   3372  O  O   . CYS   A 1 430  ? 4.43600    88.39000  23.84400  1.000 49.09142  ?  430  CYS   A O   1 
ATOM   3373  C  CB  . CYS   A 1 430  ? 2.01000    90.11100  22.51100  1.000 48.57089  ?  430  CYS   A CB  1 
ATOM   3374  S  SG  . CYS   A 1 430  ? 0.60300    91.10300  23.04500  1.000 52.63845  ?  430  CYS   A SG  1 
ATOM   3375  N  N   . ASN   A 1 431  ? 5.10200    89.39800  21.94700  1.000 47.09238  ?  431  ASN   A N   1 
ATOM   3376  C  CA  . ASN   A 1 431  ? 6.04500    88.33100  21.62900  1.000 51.91339  ?  431  ASN   A CA  1 
ATOM   3377  C  C   . ASN   A 1 431  ? 7.29300    88.39300  22.50100  1.000 41.05595  ?  431  ASN   A C   1 
ATOM   3378  O  O   . ASN   A 1 431  ? 7.82200    87.35000  22.90100  1.000 45.91375  ?  431  ASN   A O   1 
ATOM   3379  C  CB  . ASN   A 1 431  ? 6.42600    88.38900  20.15000  1.000 36.34444  ?  431  ASN   A CB  1 
ATOM   3380  C  CG  . ASN   A 1 431  ? 5.32100    87.88400  19.24700  1.000 48.70872  ?  431  ASN   A CG  1 
ATOM   3381  O  OD1 . ASN   A 1 431  ? 4.46200    87.11000  19.67100  1.000 56.13619  ?  431  ASN   A OD1 1 
ATOM   3382  N  ND2 . ASN   A 1 431  ? 5.34300    88.31100  17.99000  1.000 50.54878  ?  431  ASN   A ND2 1 
ATOM   3383  N  N   . GLN   A 1 432  ? 7.78100    89.59400  22.80600  1.000 40.34975  ?  432  GLN   A N   1 
ATOM   3384  C  CA  . GLN   A 1 432  ? 8.98900    89.73400  23.60800  1.000 44.01620  ?  432  GLN   A CA  1 
ATOM   3385  C  C   . GLN   A 1 432  ? 8.71800    89.72800  25.10700  1.000 42.68194  ?  432  GLN   A C   1 
ATOM   3386  O  O   . GLN   A 1 432  ? 9.67300    89.73900  25.89100  1.000 68.37907  ?  432  GLN   A O   1 
ATOM   3387  C  CB  . GLN   A 1 432  ? 9.74000    91.01500  23.22100  1.000 55.26771  ?  432  GLN   A CB  1 
ATOM   3388  C  CG  . GLN   A 1 432  ? 8.93900    92.29600  23.36900  1.000 59.69782  ?  432  GLN   A CG  1 
ATOM   3389  C  CD  . GLN   A 1 432  ? 9.51200    93.43100  22.54000  1.000 73.91525  ?  432  GLN   A CD  1 
ATOM   3390  O  OE1 . GLN   A 1 432  ? 10.23800   93.20200  21.57100  1.000 61.17892  ?  432  GLN   A OE1 1 
ATOM   3391  N  NE2 . GLN   A 1 432  ? 9.19000    94.66400  22.91700  1.000 72.67585  ?  432  GLN   A NE2 1 
ATOM   3392  N  N   . GLU   A 1 433  ? 7.45100    89.70800  25.52300  1.000 45.64831  ?  433  GLU   A N   1 
ATOM   3393  C  CA  . GLU   A 1 433  ? 7.09900    89.56400  26.92700  1.000 43.95115  ?  433  GLU   A CA  1 
ATOM   3394  C  C   . GLU   A 1 433  ? 6.32700    88.28900  27.22600  1.000 42.71571  ?  433  GLU   A C   1 
ATOM   3395  O  O   . GLU   A 1 433  ? 6.11000    87.98100  28.40300  1.000 40.16957  ?  433  GLU   A O   1 
ATOM   3396  C  CB  . GLU   A 1 433  ? 6.27700    90.77100  27.40700  1.000 38.58582  ?  433  GLU   A CB  1 
ATOM   3397  C  CG  . GLU   A 1 433  ? 6.93800    92.11700  27.16300  1.000 57.17467  ?  433  GLU   A CG  1 
ATOM   3398  C  CD  . GLU   A 1 433  ? 8.23100    92.28300  27.93200  1.000 63.86812  ?  433  GLU   A CD  1 
ATOM   3399  O  OE1 . GLU   A 1 433  ? 8.34100    91.72100  29.04200  1.000 69.88748  ?  433  GLU   A OE1 1 
ATOM   3400  O  OE2 . GLU   A 1 433  ? 9.13900    92.97400  27.42300  1.000 72.15021  -1 433  GLU   A OE2 1 
ATOM   3401  N  N   . GLY   A 1 434  ? 5.90800    87.54400  26.20500  1.000 48.73087  ?  434  GLY   A N   1 
ATOM   3402  C  CA  . GLY   A 1 434  ? 5.24100    86.27400  26.40800  1.000 44.71712  ?  434  GLY   A CA  1 
ATOM   3403  C  C   . GLY   A 1 434  ? 3.84200    86.39000  26.97700  1.000 49.39850  ?  434  GLY   A C   1 
ATOM   3404  O  O   . GLY   A 1 434  ? 3.48500    85.65900  27.90600  1.000 43.40356  ?  434  GLY   A O   1 
ATOM   3405  N  N   . ILE   A 1 435  ? 3.03900    87.30400  26.43300  1.000 44.91583  ?  435  ILE   A N   1 
ATOM   3406  C  CA  . ILE   A 1 435  ? 1.64800    87.41200  26.85200  1.000 43.85316  ?  435  ILE   A CA  1 
ATOM   3407  C  C   . ILE   A 1 435  ? 0.87600    86.20800  26.33000  1.000 48.29416  ?  435  ILE   A C   1 
ATOM   3408  O  O   . ILE   A 1 435  ? 0.91600    85.89500  25.13400  1.000 48.00424  ?  435  ILE   A O   1 
ATOM   3409  C  CB  . ILE   A 1 435  ? 1.02800    88.72900  26.36200  1.000 34.92357  ?  435  ILE   A CB  1 
ATOM   3410  C  CG1 . ILE   A 1 435  ? 1.38500    89.88300  27.30200  1.000 36.34583  ?  435  ILE   A CG1 1 
ATOM   3411  C  CG2 . ILE   A 1 435  ? -0.47000   88.59500  26.28700  1.000 42.19320  ?  435  ILE   A CG2 1 
ATOM   3412  C  CD1 . ILE   A 1 435  ? 2.77500    90.42600  27.12100  1.000 35.95917  ?  435  ILE   A CD1 1 
ATOM   3413  N  N   . THR   A 1 436  ? 0.16200    85.53000  27.22700  1.000 37.23191  ?  436  THR   A N   1 
ATOM   3414  C  CA  . THR   A 1 436  ? -0.46900   84.25300  26.91400  1.000 41.38536  ?  436  THR   A CA  1 
ATOM   3415  C  C   . THR   A 1 436  ? -1.97200   84.35100  26.68900  1.000 52.31643  ?  436  THR   A C   1 
ATOM   3416  O  O   . THR   A 1 436  ? -2.51200   83.63100  25.84400  1.000 43.31496  ?  436  THR   A O   1 
ATOM   3417  C  CB  . THR   A 1 436  ? -0.19400   83.24700  28.03400  1.000 32.01090  ?  436  THR   A CB  1 
ATOM   3418  O  OG1 . THR   A 1 436  ? -0.71500   83.75400  29.26900  1.000 36.34279  ?  436  THR   A OG1 1 
ATOM   3419  C  CG2 . THR   A 1 436  ? 1.30100    83.01400  28.17800  1.000 43.31811  ?  436  THR   A CG2 1 
ATOM   3420  N  N   . ILE   A 1 437  ? -2.66600   85.21700  27.42300  1.000 47.43523  ?  437  ILE   A N   1 
ATOM   3421  C  CA  . ILE   A 1 437  ? -4.11900   85.31300  27.34800  1.000 36.89315  ?  437  ILE   A CA  1 
ATOM   3422  C  C   . ILE   A 1 437  ? -4.51400   86.78000  27.42600  1.000 30.85952  ?  437  ILE   A C   1 
ATOM   3423  O  O   . ILE   A 1 437  ? -3.86400   87.56800  28.12100  1.000 41.69038  ?  437  ILE   A O   1 
ATOM   3424  C  CB  . ILE   A 1 437  ? -4.79100   84.48800  28.46700  1.000 34.66124  ?  437  ILE   A CB  1 
ATOM   3425  C  CG1 . ILE   A 1 437  ? -6.30800   84.45700  28.28600  1.000 31.73691  ?  437  ILE   A CG1 1 
ATOM   3426  C  CG2 . ILE   A 1 437  ? -4.42200   85.03300  29.84200  1.000 34.80796  ?  437  ILE   A CG2 1 
ATOM   3427  C  CD1 . ILE   A 1 437  ? -6.97800   83.36000  29.06700  1.000 32.99323  ?  437  ILE   A CD1 1 
ATOM   3428  N  N   . SER   A 1 438  ? -5.56600   87.15200  26.69800  1.000 35.62918  ?  438  SER   A N   1 
ATOM   3429  C  CA  . SER   A 1 438  ? -6.08700   88.51500  26.73600  1.000 41.64018  ?  438  SER   A CA  1 
ATOM   3430  C  C   . SER   A 1 438  ? -7.39700   88.57600  25.96400  1.000 40.79544  ?  438  SER   A C   1 
ATOM   3431  O  O   . SER   A 1 438  ? -7.79100   87.62400  25.28400  1.000 36.44769  ?  438  SER   A O   1 
ATOM   3432  C  CB  . SER   A 1 438  ? -5.08500   89.52300  26.17000  1.000 22.53908  ?  438  SER   A CB  1 
ATOM   3433  O  OG  . SER   A 1 438  ? -4.00800   89.69500  27.07200  1.000 46.87116  ?  438  SER   A OG  1 
ATOM   3434  N  N   . TYR   A 1 439  ? -8.06800   89.72100  26.08200  1.000 36.29122  ?  439  TYR   A N   1 
ATOM   3435  C  CA  . TYR   A 1 439  ? -9.31900   89.99300  25.38700  1.000 37.18364  ?  439  TYR   A CA  1 
ATOM   3436  C  C   . TYR   A 1 439  ? -9.11900   91.18100  24.46000  1.000 34.30099  ?  439  TYR   A C   1 
ATOM   3437  O  O   . TYR   A 1 439  ? -8.79600   92.28300  24.91800  1.000 42.37559  ?  439  TYR   A O   1 
ATOM   3438  C  CB  . TYR   A 1 439  ? -10.45600  90.27100  26.37400  1.000 45.28721  ?  439  TYR   A CB  1 
ATOM   3439  C  CG  . TYR   A 1 439  ? -11.57700  91.10300  25.78900  1.000 43.88699  ?  439  TYR   A CG  1 
ATOM   3440  C  CD1 . TYR   A 1 439  ? -12.46400  90.56200  24.86900  1.000 40.97599  ?  439  TYR   A CD1 1 
ATOM   3441  C  CD2 . TYR   A 1 439  ? -11.74500  92.43200  26.15700  1.000 40.79054  ?  439  TYR   A CD2 1 
ATOM   3442  C  CE1 . TYR   A 1 439  ? -13.48500  91.32100  24.33000  1.000 43.11203  ?  439  TYR   A CE1 1 
ATOM   3443  C  CE2 . TYR   A 1 439  ? -12.76300  93.19800  25.62400  1.000 33.18986  ?  439  TYR   A CE2 1 
ATOM   3444  C  CZ  . TYR   A 1 439  ? -13.63000  92.63700  24.71200  1.000 42.33964  ?  439  TYR   A CZ  1 
ATOM   3445  O  OH  . TYR   A 1 439  ? -14.64600  93.39700  24.18000  1.000 57.38333  ?  439  TYR   A OH  1 
ATOM   3446  N  N   . LEU   A 1 440  ? -9.31000   90.95600  23.16500  1.000 36.38196  ?  440  LEU   A N   1 
ATOM   3447  C  CA  . LEU   A 1 440  ? -9.25100   92.00600  22.16400  1.000 43.28870  ?  440  LEU   A CA  1 
ATOM   3448  C  C   . LEU   A 1 440  ? -10.63200  92.23200  21.57400  1.000 57.14471  ?  440  LEU   A C   1 
ATOM   3449  O  O   . LEU   A 1 440  ? -11.29800  91.26100  21.19400  1.000 59.10845  ?  440  LEU   A O   1 
ATOM   3450  C  CB  . LEU   A 1 440  ? -8.26600   91.63700  21.05000  1.000 34.63125  ?  440  LEU   A CB  1 
ATOM   3451  C  CG  . LEU   A 1 440  ? -6.77900   91.82100  21.34700  1.000 30.98311  ?  440  LEU   A CG  1 
ATOM   3452  C  CD1 . LEU   A 1 440  ? -5.94600   91.05600  20.33600  1.000 23.87426  ?  440  LEU   A CD1 1 
ATOM   3453  C  CD2 . LEU   A 1 440  ? -6.41600   93.29800  21.33100  1.000 47.27019  ?  440  LEU   A CD2 1 
ATOM   3454  N  N   . PRO   A 1 441  ? -11.10200  93.47700  21.49400  1.000 47.27530  ?  441  PRO   A N   1 
ATOM   3455  C  CA  . PRO   A 1 441  ? -12.37200  93.74200  20.81000  1.000 38.64799  ?  441  PRO   A CA  1 
ATOM   3456  C  C   . PRO   A 1 441  ? -12.34600  93.24000  19.37200  1.000 52.01812  ?  441  PRO   A C   1 
ATOM   3457  O  O   . PRO   A 1 441  ? -11.28700  93.00800  18.78400  1.000 64.46760  ?  441  PRO   A O   1 
ATOM   3458  C  CB  . PRO   A 1 441  ? -12.49500  95.26800  20.87300  1.000 36.98614  ?  441  PRO   A CB  1 
ATOM   3459  C  CG  . PRO   A 1 441  ? -11.73000  95.63900  22.09900  1.000 49.73327  ?  441  PRO   A CG  1 
ATOM   3460  C  CD  . PRO   A 1 441  ? -10.57000  94.68000  22.15600  1.000 57.65493  ?  441  PRO   A CD  1 
ATOM   3461  N  N   . THR   A 1 442  ? -13.54700  93.08000  18.80800  1.000 46.44327  ?  442  THR   A N   1 
ATOM   3462  C  CA  . THR   A 1 442  ? -13.69400  92.39500  17.52400  1.000 45.11556  ?  442  THR   A CA  1 
ATOM   3463  C  C   . THR   A 1 442  ? -12.85500  93.05300  16.43400  1.000 44.60223  ?  442  THR   A C   1 
ATOM   3464  O  O   . THR   A 1 442  ? -12.10600  92.37600  15.72000  1.000 48.38107  ?  442  THR   A O   1 
ATOM   3465  C  CB  . THR   A 1 442  ? -15.16800  92.35300  17.11900  1.000 40.01408  ?  442  THR   A CB  1 
ATOM   3466  O  OG1 . THR   A 1 442  ? -15.88400  91.47400  17.99700  1.000 28.22184  ?  442  THR   A OG1 1 
ATOM   3467  C  CG2 . THR   A 1 442  ? -15.31400  91.85900  15.68800  1.000 36.77651  ?  442  THR   A CG2 1 
ATOM   3468  N  N   . GLY   A 1 443  ? -12.96400  94.37500  16.29200  1.000 48.47971  ?  443  GLY   A N   1 
ATOM   3469  C  CA  . GLY   A 1 443  ? -12.23600  95.05400  15.23100  1.000 54.08984  ?  443  GLY   A CA  1 
ATOM   3470  C  C   . GLY   A 1 443  ? -10.73300  94.91500  15.37400  1.000 56.50594  ?  443  GLY   A C   1 
ATOM   3471  O  O   . GLY   A 1 443  ? -10.03000  94.60300  14.40900  1.000 70.29667  ?  443  GLY   A O   1 
ATOM   3472  N  N   . ALA   A 1 444  ? -10.22100  95.14000  16.58600  1.000 62.39054  ?  444  ALA   A N   1 
ATOM   3473  C  CA  . ALA   A 1 444  ? -8.78500   95.01800  16.81400  1.000 51.86045  ?  444  ALA   A CA  1 
ATOM   3474  C  C   . ALA   A 1 444  ? -8.32000   93.57800  16.64800  1.000 53.70243  ?  444  ALA   A C   1 
ATOM   3475  O  O   . ALA   A 1 444  ? -7.20700   93.33200  16.16600  1.000 49.25917  ?  444  ALA   A O   1 
ATOM   3476  C  CB  . ALA   A 1 444  ? -8.42900   95.54500  18.20400  1.000 44.45259  ?  444  ALA   A CB  1 
ATOM   3477  N  N   . ALA   A 1 445  ? -9.15900   92.61500  17.03600  1.000 45.39307  ?  445  ALA   A N   1 
ATOM   3478  C  CA  . ALA   A 1 445  ? -8.81400   91.20700  16.86800  1.000 46.57989  ?  445  ALA   A CA  1 
ATOM   3479  C  C   . ALA   A 1 445  ? -8.60200   90.87000  15.39700  1.000 54.44982  ?  445  ALA   A C   1 
ATOM   3480  O  O   . ALA   A 1 445  ? -7.50400   90.47400  14.98900  1.000 58.67309  ?  445  ALA   A O   1 
ATOM   3481  C  CB  . ALA   A 1 445  ? -9.90700   90.32400  17.47300  1.000 37.92626  ?  445  ALA   A CB  1 
ATOM   3482  N  N   . GLU   A 1 446  ? -9.64700   91.04500  14.58000  1.000 49.01636  ?  446  GLU   A N   1 
ATOM   3483  C  CA  . GLU   A 1 446  ? -9.57400   90.71600  13.15900  1.000 51.62745  ?  446  GLU   A CA  1 
ATOM   3484  C  C   . GLU   A 1 446  ? -8.39200   91.37500  12.46300  1.000 55.26810  ?  446  GLU   A C   1 
ATOM   3485  O  O   . GLU   A 1 446  ? -7.93500   90.87300  11.43000  1.000 60.91783  ?  446  GLU   A O   1 
ATOM   3486  C  CB  . GLU   A 1 446  ? -10.87800  91.11600  12.46200  1.000 51.53193  ?  446  GLU   A CB  1 
ATOM   3487  C  CG  . GLU   A 1 446  ? -12.08100  90.27200  12.85800  1.000 46.79283  ?  446  GLU   A CG  1 
ATOM   3488  C  CD  . GLU   A 1 446  ? -13.33800  90.64200  12.09300  1.000 48.68021  ?  446  GLU   A CD  1 
ATOM   3489  O  OE1 . GLU   A 1 446  ? -13.48400  91.82400  11.71400  1.000 52.42804  ?  446  GLU   A OE1 1 
ATOM   3490  O  OE2 . GLU   A 1 446  ? -14.18100  89.74900  11.86500  1.000 52.26269  -1 446  GLU   A OE2 1 
ATOM   3491  N  N   . GLN   A 1 447  ? -7.88300   92.48300  13.00000  1.000 44.51657  ?  447  GLN   A N   1 
ATOM   3492  C  CA  . GLN   A 1 447  ? -6.65900   93.07700  12.48000  1.000 49.28908  ?  447  GLN   A CA  1 
ATOM   3493  C  C   . GLN   A 1 447  ? -5.41000   92.48400  13.11500  1.000 55.95736  ?  447  GLN   A C   1 
ATOM   3494  O  O   . GLN   A 1 447  ? -4.37000   92.39700  12.45200  1.000 65.86715  ?  447  GLN   A O   1 
ATOM   3495  C  CB  . GLN   A 1 447  ? -6.67700   94.59300  12.68800  1.000 44.60714  ?  447  GLN   A CB  1 
ATOM   3496  C  CG  . GLN   A 1 447  ? -7.89500   95.26700  12.08500  1.000 76.02117  ?  447  GLN   A CG  1 
ATOM   3497  C  CD  . GLN   A 1 447  ? -7.58000   96.63100  11.51100  1.000 92.04104  ?  447  GLN   A CD  1 
ATOM   3498  O  OE1 . GLN   A 1 447  ? -8.21900   97.07800  10.55800  1.000 75.64612  ?  447  GLN   A OE1 1 
ATOM   3499  N  NE2 . GLN   A 1 447  ? -6.59200   97.30400  12.09100  1.000 69.75286  ?  447  GLN   A NE2 1 
ATOM   3500  N  N   . PHE   A 1 448  ? -5.49000   92.07000  14.38200  1.000 54.86192  ?  448  PHE   A N   1 
ATOM   3501  C  CA  . PHE   A 1 448  ? -4.36100   91.41700  15.03400  1.000 46.59876  ?  448  PHE   A CA  1 
ATOM   3502  C  C   . PHE   A 1 448  ? -4.14900   89.99600  14.52700  1.000 48.48316  ?  448  PHE   A C   1 
ATOM   3503  O  O   . PHE   A 1 448  ? -3.03200   89.47700  14.62000  1.000 47.66999  ?  448  PHE   A O   1 
ATOM   3504  C  CB  . PHE   A 1 448  ? -4.56800   91.41000  16.55200  1.000 48.34773  ?  448  PHE   A CB  1 
ATOM   3505  C  CG  . PHE   A 1 448  ? -3.42400   90.80700  17.32500  1.000 63.13873  ?  448  PHE   A CG  1 
ATOM   3506  C  CD1 . PHE   A 1 448  ? -2.29900   91.55900  17.62500  1.000 52.97064  ?  448  PHE   A CD1 1 
ATOM   3507  C  CD2 . PHE   A 1 448  ? -3.48100   89.49200  17.76300  1.000 52.40107  ?  448  PHE   A CD2 1 
ATOM   3508  C  CE1 . PHE   A 1 448  ? -1.24800   91.00800  18.33800  1.000 55.39668  ?  448  PHE   A CE1 1 
ATOM   3509  C  CE2 . PHE   A 1 448  ? -2.43300   88.93600  18.47600  1.000 43.57042  ?  448  PHE   A CE2 1 
ATOM   3510  C  CZ  . PHE   A 1 448  ? -1.31600   89.69500  18.76400  1.000 50.97653  ?  448  PHE   A CZ  1 
ATOM   3511  N  N   . MET   A 1 449  ? -5.19000   89.36000  13.98600  1.000 48.85013  ?  449  MET   A N   1 
ATOM   3512  C  CA  . MET   A 1 449  ? -5.05700   88.00100  13.47600  1.000 60.29621  ?  449  MET   A CA  1 
ATOM   3513  C  C   . MET   A 1 449  ? -4.20500   87.92700  12.21500  1.000 63.35368  ?  449  MET   A C   1 
ATOM   3514  O  O   . MET   A 1 449  ? -3.91900   86.82000  11.74600  1.000 69.91420  ?  449  MET   A O   1 
ATOM   3515  C  CB  . MET   A 1 449  ? -6.44500   87.40600  13.22000  1.000 51.02864  ?  449  MET   A CB  1 
ATOM   3516  C  CG  . MET   A 1 449  ? -7.35700   87.46600  14.44300  1.000 60.72761  ?  449  MET   A CG  1 
ATOM   3517  S  SD  . MET   A 1 449  ? -8.94900   86.62500  14.28600  1.000 58.55713  ?  449  MET   A SD  1 
ATOM   3518  C  CE  . MET   A 1 449  ? -8.79400   85.89800  12.66200  1.000 59.58189  ?  449  MET   A CE  1 
ATOM   3519  N  N   . GLN   A 1 450  ? -3.79600   89.06600  11.66000  1.000 50.26681  ?  450  GLN   A N   1 
ATOM   3520  C  CA  . GLN   A 1 450  ? -2.86800   89.11400  10.54000  1.000 55.20235  ?  450  GLN   A CA  1 
ATOM   3521  C  C   . GLN   A 1 450  ? -1.43000   89.34000  10.99100  1.000 67.87170  ?  450  GLN   A C   1 
ATOM   3522  O  O   . GLN   A 1 450  ? -0.56700   89.63200  10.15700  1.000 77.81408  ?  450  GLN   A O   1 
ATOM   3523  C  CB  . GLN   A 1 450  ? -3.29400   90.20400  9.55300   1.000 57.89470  ?  450  GLN   A CB  1 
ATOM   3524  C  CG  . GLN   A 1 450  ? -4.57400   89.87200  8.80000   1.000 77.82514  ?  450  GLN   A CG  1 
ATOM   3525  C  CD  . GLN   A 1 450  ? -5.48200   91.07300  8.61400   1.000 85.06090  ?  450  GLN   A CD  1 
ATOM   3526  O  OE1 . GLN   A 1 450  ? -6.69300   90.92600  8.44100   1.000 74.00831  ?  450  GLN   A OE1 1 
ATOM   3527  N  NE2 . GLN   A 1 450  ? -4.90300   92.26700  8.64900   1.000 79.63699  ?  450  GLN   A NE2 1 
ATOM   3528  N  N   . MET   A 1 451  ? -1.15800   89.20700  12.28700  1.000 72.74343  ?  451  MET   A N   1 
ATOM   3529  C  CA  . MET   A 1 451  ? 0.16200    89.42500  12.85900  1.000 47.82736  ?  451  MET   A CA  1 
ATOM   3530  C  C   . MET   A 1 451  ? 0.76500    88.09700  13.29200  1.000 51.96057  ?  451  MET   A C   1 
ATOM   3531  O  O   . MET   A 1 451  ? 0.05900    87.22900  13.81500  1.000 60.21349  ?  451  MET   A O   1 
ATOM   3532  C  CB  . MET   A 1 451  ? 0.09300    90.36200  14.06800  1.000 39.01939  ?  451  MET   A CB  1 
ATOM   3533  C  CG  . MET   A 1 451  ? -0.71700   91.63000  13.86100  1.000 49.40566  ?  451  MET   A CG  1 
ATOM   3534  S  SD  . MET   A 1 451  ? 0.09700    92.85600  12.82000  1.000 59.74928  ?  451  MET   A SD  1 
ATOM   3535  C  CE  . MET   A 1 451  ? 1.82500    92.55300  13.19400  1.000 72.73882  ?  451  MET   A CE  1 
ATOM   3536  N  N   . ASP   A 1 452  ? 2.07200    87.94700  13.09000  1.000 56.96701  ?  452  ASP   A N   1 
ATOM   3537  C  CA  A ASP   A 1 452  ? 2.78100    86.73100  13.48200  0.500 61.47313  ?  452  ASP   A CA  1 
ATOM   3538  C  CA  B ASP   A 1 452  ? 2.77700    86.72900  13.48300  0.500 71.22339  ?  452  ASP   A CA  1 
ATOM   3539  C  C   . ASP   A 1 452  ? 2.98000    86.75000  14.99300  1.000 57.21197  ?  452  ASP   A C   1 
ATOM   3540  O  O   . ASP   A 1 452  ? 3.85900    87.44500  15.50800  1.000 64.77511  ?  452  ASP   A O   1 
ATOM   3541  C  CB  A ASP   A 1 452  ? 4.11100    86.61900  12.74500  0.500 66.28141  ?  452  ASP   A CB  1 
ATOM   3542  C  CB  B ASP   A 1 452  ? 4.10500    86.60900  12.74600  0.500 69.13141  ?  452  ASP   A CB  1 
ATOM   3543  C  CG  A ASP   A 1 452  ? 4.90100    87.91300  12.76800  0.500 65.03934  ?  452  ASP   A CG  1 
ATOM   3544  C  CG  B ASP   A 1 452  ? 4.83900    85.32600  13.08000  0.500 55.57870  ?  452  ASP   A CG  1 
ATOM   3545  O  OD1 A ASP   A 1 452  ? 4.36800    88.94500  12.31000  0.500 53.35717  ?  452  ASP   A OD1 1 
ATOM   3546  O  OD1 B ASP   A 1 452  ? 4.26400    84.23900  12.86100  0.500 52.39084  ?  452  ASP   A OD1 1 
ATOM   3547  O  OD2 A ASP   A 1 452  ? 6.05200    87.89900  13.25600  0.500 74.49430  -1 452  ASP   A OD2 1 
ATOM   3548  O  OD2 B ASP   A 1 452  ? 5.98800    85.40200  13.56200  0.500 58.93042  -1 452  ASP   A OD2 1 
ATOM   3549  N  N   . ASN   A 1 453  ? 2.16300    85.98500  15.70800  1.000 48.18278  ?  453  ASN   A N   1 
ATOM   3550  C  CA  . ASN   A 1 453  ? 2.23400    85.89700  17.15800  1.000 44.53467  ?  453  ASN   A CA  1 
ATOM   3551  C  C   . ASN   A 1 453  ? 2.54200    84.46400  17.56500  1.000 57.28617  ?  453  ASN   A C   1 
ATOM   3552  O  O   . ASN   A 1 453  ? 1.98800    83.51600  17.00100  1.000 56.19967  ?  453  ASN   A O   1 
ATOM   3553  C  CB  . ASN   A 1 453  ? 0.92400    86.35500  17.80700  1.000 41.19414  ?  453  ASN   A CB  1 
ATOM   3554  C  CG  . ASN   A 1 453  ? 0.95100    86.24000  19.31800  1.000 46.79018  ?  453  ASN   A CG  1 
ATOM   3555  O  OD1 . ASN   A 1 453  ? 0.58700    85.20800  19.88000  1.000 46.56111  ?  453  ASN   A OD1 1 
ATOM   3556  N  ND2 . ASN   A 1 453  ? 1.38600    87.30300  19.98400  1.000 44.67471  ?  453  ASN   A ND2 1 
ATOM   3557  N  N   . GLN   A 1 454  ? 3.43600    84.31300  18.54400  1.000 59.15716  ?  454  GLN   A N   1 
ATOM   3558  C  CA  . GLN   A 1 454  ? 3.75100    83.00500  19.09600  1.000 61.02418  ?  454  GLN   A CA  1 
ATOM   3559  C  C   . GLN   A 1 454  ? 3.57900    82.93800  20.60600  1.000 56.51829  ?  454  GLN   A C   1 
ATOM   3560  O  O   . GLN   A 1 454  ? 3.74700    81.85700  21.18200  1.000 72.20840  ?  454  GLN   A O   1 
ATOM   3561  C  CB  . GLN   A 1 454  ? 5.18800    82.59100  18.73900  1.000 77.16250  ?  454  GLN   A CB  1 
ATOM   3562  C  CG  . GLN   A 1 454  ? 5.71100    83.14700  17.42400  1.000 75.15165  ?  454  GLN   A CG  1 
ATOM   3563  C  CD  . GLN   A 1 454  ? 6.48200    84.43800  17.61100  1.000 81.96795  ?  454  GLN   A CD  1 
ATOM   3564  O  OE1 . GLN   A 1 454  ? 6.27500    85.16000  18.58500  1.000 80.53916  ?  454  GLN   A OE1 1 
ATOM   3565  N  NE2 . GLN   A 1 454  ? 7.38700    84.72700  16.68400  1.000 94.05068  ?  454  GLN   A NE2 1 
ATOM   3566  N  N   . SER   A 1 455  ? 3.24900    84.05100  21.26200  1.000 50.26361  ?  455  SER   A N   1 
ATOM   3567  C  CA  . SER   A 1 455  ? 3.13100    84.08200  22.71500  1.000 53.67483  ?  455  SER   A CA  1 
ATOM   3568  C  C   . SER   A 1 455  ? 1.73400    83.71700  23.19800  1.000 53.57321  ?  455  SER   A C   1 
ATOM   3569  O  O   . SER   A 1 455  ? 1.59100    83.05900  24.23500  1.000 56.52708  ?  455  SER   A O   1 
ATOM   3570  C  CB  . SER   A 1 455  ? 3.50600    85.46700  23.24300  1.000 53.40270  ?  455  SER   A CB  1 
ATOM   3571  O  OG  . SER   A 1 455  ? 2.54700    86.43500  22.84900  1.000 40.31300  ?  455  SER   A OG  1 
ATOM   3572  N  N   . PHE   A 1 456  ? 0.70000    84.14200  22.47700  1.000 49.89874  ?  456  PHE   A N   1 
ATOM   3573  C  CA  . PHE   A 1 456  ? -0.66700   83.87500  22.90000  1.000 35.27561  ?  456  PHE   A CA  1 
ATOM   3574  C  C   . PHE   A 1 456  ? -0.99000   82.39000  22.81200  1.000 37.36038  ?  456  PHE   A C   1 
ATOM   3575  O  O   . PHE   A 1 456  ? -0.57300   81.69700  21.88000  1.000 51.49863  ?  456  PHE   A O   1 
ATOM   3576  C  CB  . PHE   A 1 456  ? -1.65700   84.65800  22.04000  1.000 38.15137  ?  456  PHE   A CB  1 
ATOM   3577  C  CG  . PHE   A 1 456  ? -1.86200   86.07600  22.47900  1.000 37.58697  ?  456  PHE   A CG  1 
ATOM   3578  C  CD1 . PHE   A 1 456  ? -2.60800   86.36200  23.60900  1.000 32.82871  ?  456  PHE   A CD1 1 
ATOM   3579  C  CD2 . PHE   A 1 456  ? -1.32900   87.12600  21.74900  1.000 40.78771  ?  456  PHE   A CD2 1 
ATOM   3580  C  CE1 . PHE   A 1 456  ? -2.81100   87.66600  24.00900  1.000 33.23450  ?  456  PHE   A CE1 1 
ATOM   3581  C  CE2 . PHE   A 1 456  ? -1.52500   88.43300  22.14700  1.000 34.75651  ?  456  PHE   A CE2 1 
ATOM   3582  C  CZ  . PHE   A 1 456  ? -2.26700   88.70400  23.27900  1.000 23.88231  ?  456  PHE   A CZ  1 
ATOM   3583  N  N   . ARG   A 1 457  ? -1.74200   81.90400  23.80000  1.000 32.12449  ?  457  ARG   A N   1 
ATOM   3584  C  CA  . ARG   A 1 457  ? -2.37500   80.59700  23.72400  1.000 35.86729  ?  457  ARG   A CA  1 
ATOM   3585  C  C   . ARG   A 1 457  ? -3.89100   80.68000  23.65900  1.000 44.47220  ?  457  ARG   A C   1 
ATOM   3586  O  O   . ARG   A 1 457  ? -4.52400   79.75400  23.14100  1.000 41.61909  ?  457  ARG   A O   1 
ATOM   3587  C  CB  . ARG   A 1 457  ? -1.97100   79.72900  24.92500  1.000 26.06948  ?  457  ARG   A CB  1 
ATOM   3588  C  CG  . ARG   A 1 457  ? -2.36600   80.30700  26.27400  1.000 37.02398  ?  457  ARG   A CG  1 
ATOM   3589  C  CD  . ARG   A 1 457  ? -2.05300   79.33700  27.40200  1.000 32.17232  ?  457  ARG   A CD  1 
ATOM   3590  N  NE  . ARG   A 1 457  ? -2.53300   79.82500  28.69000  1.000 34.89802  ?  457  ARG   A NE  1 
ATOM   3591  C  CZ  . ARG   A 1 457  ? -3.75700   79.62400  29.15700  1.000 35.86003  ?  457  ARG   A CZ  1 
ATOM   3592  N  NH1 . ARG   A 1 457  ? -4.65900   78.94700  28.46300  1.000 36.17260  ?  457  ARG   A NH1 1 
ATOM   3593  N  NH2 . ARG   A 1 457  ? -4.08600   80.11600  30.34800  1.000 26.83541  ?  457  ARG   A NH2 1 
ATOM   3594  N  N   . VAL   A 1 458  ? -4.48000   81.76600  24.16100  1.000 40.21294  ?  458  VAL   A N   1 
ATOM   3595  C  CA  . VAL   A 1 458  ? -5.92100   81.99300  24.13800  1.000 30.35786  ?  458  VAL   A CA  1 
ATOM   3596  C  C   . VAL   A 1 458  ? -6.16300   83.47400  23.88600  1.000 36.83979  ?  458  VAL   A C   1 
ATOM   3597  O  O   . VAL   A 1 458  ? -5.63900   84.32500  24.61300  1.000 37.60945  ?  458  VAL   A O   1 
ATOM   3598  C  CB  . VAL   A 1 458  ? -6.59600   81.56100  25.45600  1.000 25.95692  ?  458  VAL   A CB  1 
ATOM   3599  C  CG1 . VAL   A 1 458  ? -8.00600   82.12400  25.54000  1.000 34.36024  ?  458  VAL   A CG1 1 
ATOM   3600  C  CG2 . VAL   A 1 458  ? -6.61600   80.04400  25.58200  1.000 25.98872  ?  458  VAL   A CG2 1 
ATOM   3601  N  N   . VAL   A 1 459  ? -6.95100   83.78500  22.85900  1.000 49.36104  ?  459  VAL   A N   1 
ATOM   3602  C  CA  . VAL   A 1 459  ? -7.35600   85.15600  22.56000  1.000 41.63315  ?  459  VAL   A CA  1 
ATOM   3603  C  C   . VAL   A 1 459  ? -8.87400   85.18900  22.47400  1.000 38.13064  ?  459  VAL   A C   1 
ATOM   3604  O  O   . VAL   A 1 459  ? -9.47000   84.47200  21.66200  1.000 43.81317  ?  459  VAL   A O   1 
ATOM   3605  C  CB  . VAL   A 1 459  ? -6.72800   85.68100  21.25900  1.000 29.33608  ?  459  VAL   A CB  1 
ATOM   3606  C  CG1 . VAL   A 1 459  ? -7.29200   87.05300  20.91900  1.000 23.98819  ?  459  VAL   A CG1 1 
ATOM   3607  C  CG2 . VAL   A 1 459  ? -5.22200   85.75200  21.39800  1.000 25.76649  ?  459  VAL   A CG2 1 
ATOM   3608  N  N   . ILE   A 1 460  ? -9.49600   86.01900  23.30700  1.000 40.22211  ?  460  ILE   A N   1 
ATOM   3609  C  CA  . ILE   A 1 460  ? -10.94600  86.13700  23.38400  1.000 34.69728  ?  460  ILE   A CA  1 
ATOM   3610  C  C   . ILE   A 1 460  ? -11.36100  87.44200  22.72500  1.000 39.35872  ?  460  ILE   A C   1 
ATOM   3611  O  O   . ILE   A 1 460  ? -10.72900  88.48400  22.93600  1.000 42.77608  ?  460  ILE   A O   1 
ATOM   3612  C  CB  . ILE   A 1 460  ? -11.43200  86.08400  24.84500  1.000 40.52044  ?  460  ILE   A CB  1 
ATOM   3613  C  CG1 . ILE   A 1 460  ? -10.75900  84.92500  25.57900  1.000 41.72233  ?  460  ILE   A CG1 1 
ATOM   3614  C  CG2 . ILE   A 1 460  ? -12.94600  85.95100  24.89900  1.000 40.17569  ?  460  ILE   A CG2 1 
ATOM   3615  C  CD1 . ILE   A 1 460  ? -10.61900  85.15000  27.06200  1.000 35.16774  ?  460  ILE   A CD1 1 
ATOM   3616  N  N   . THR   A 1 461  ? -12.42400  87.38800  21.92700  1.000 49.54087  ?  461  THR   A N   1 
ATOM   3617  C  CA  . THR   A 1 461  ? -12.94000  88.56400  21.24600  1.000 40.00739  ?  461  THR   A CA  1 
ATOM   3618  C  C   . THR   A 1 461  ? -14.44600  88.65900  21.44500  1.000 47.12216  ?  461  THR   A C   1 
ATOM   3619  O  O   . THR   A 1 461  ? -15.10800  87.69200  21.83200  1.000 42.18629  ?  461  THR   A O   1 
ATOM   3620  C  CB  . THR   A 1 461  ? -12.60200  88.54400  19.75000  1.000 36.67575  ?  461  THR   A CB  1 
ATOM   3621  O  OG1 . THR   A 1 461  ? -13.24600  89.64600  19.09900  1.000 51.11999  ?  461  THR   A OG1 1 
ATOM   3622  C  CG2 . THR   A 1 461  ? -13.06300  87.24400  19.11600  1.000 47.78210  ?  461  THR   A CG2 1 
ATOM   3623  N  N   . GLY   A 1 462  ? -14.98000  89.84900  21.17800  1.000 43.45038  ?  462  GLY   A N   1 
ATOM   3624  C  CA  . GLY   A 1 462  ? -16.39400  90.10900  21.36000  1.000 30.51862  ?  462  GLY   A CA  1 
ATOM   3625  C  C   . GLY   A 1 462  ? -16.71200  91.58900  21.40700  1.000 36.34450  ?  462  GLY   A C   1 
ATOM   3626  O  O   . GLY   A 1 462  ? -15.87400  92.39700  21.81500  1.000 54.75746  ?  462  GLY   A O   1 
ATOM   3627  N  N   . GLY   A 1 463  ? -17.92300  91.95500  20.99600  1.000 45.72049  ?  463  GLY   A N   1 
ATOM   3628  C  CA  . GLY   A 1 463  ? -18.31800  93.34900  20.92800  1.000 53.40524  ?  463  GLY   A CA  1 
ATOM   3629  C  C   . GLY   A 1 463  ? -19.08700  93.64500  19.65900  1.000 44.54531  ?  463  GLY   A C   1 
ATOM   3630  O  O   . GLY   A 1 463  ? -20.19100  94.19700  19.70000  1.000 62.94963  ?  463  GLY   A O   1 
ATOM   3631  N  N   . ASP   A 1 464  ? -18.50100  93.28900  18.52400  1.000 44.34823  ?  464  ASP   A N   1 
ATOM   3632  C  CA  . ASP   A 1 464  ? -19.16800  93.29500  17.23100  1.000 41.35229  ?  464  ASP   A CA  1 
ATOM   3633  C  C   . ASP   A 1 464  ? -19.25800  91.86300  16.71600  1.000 54.74900  ?  464  ASP   A C   1 
ATOM   3634  O  O   . ASP   A 1 464  ? -18.80400  90.91500  17.36200  1.000 55.62861  ?  464  ASP   A O   1 
ATOM   3635  C  CB  . ASP   A 1 464  ? -18.43600  94.19700  16.23200  1.000 28.46116  ?  464  ASP   A CB  1 
ATOM   3636  C  CG  . ASP   A 1 464  ? -18.82500  95.65400  16.36800  1.000 54.58317  ?  464  ASP   A CG  1 
ATOM   3637  O  OD1 . ASP   A 1 464  ? -19.64600  95.97200  17.25400  1.000 73.79683  ?  464  ASP   A OD1 1 
ATOM   3638  O  OD2 . ASP   A 1 464  ? -18.31500  96.48200  15.58500  1.000 81.77993  -1 464  ASP   A OD2 1 
ATOM   3639  N  N   . VAL   A 1 465  ? -19.85300  91.70900  15.53600  1.000 47.68503  ?  465  VAL   A N   1 
ATOM   3640  C  CA  . VAL   A 1 465  ? -20.02500  90.38300  14.95500  1.000 38.81908  ?  465  VAL   A CA  1 
ATOM   3641  C  C   . VAL   A 1 465  ? -18.67900  89.89400  14.43500  1.000 42.11358  ?  465  VAL   A C   1 
ATOM   3642  O  O   . VAL   A 1 465  ? -18.09300  90.49300  13.52600  1.000 40.99801  ?  465  VAL   A O   1 
ATOM   3643  C  CB  . VAL   A 1 465  ? -21.07800  90.40600  13.84100  1.000 50.52884  ?  465  VAL   A CB  1 
ATOM   3644  C  CG1 . VAL   A 1 465  ? -21.60400  89.00300  13.58600  1.000 44.81944  ?  465  VAL   A CG1 1 
ATOM   3645  C  CG2 . VAL   A 1 465  ? -22.20900  91.35900  14.19900  1.000 59.05228  ?  465  VAL   A CG2 1 
ATOM   3646  N  N   . LEU   A 1 466  ? -18.18100  88.80500  15.01500  1.000 40.35863  ?  466  LEU   A N   1 
ATOM   3647  C  CA  . LEU   A 1 466  ? -16.92300  88.21900  14.57500  1.000 39.88691  ?  466  LEU   A CA  1 
ATOM   3648  C  C   . LEU   A 1 466  ? -17.13500  87.40000  13.30800  1.000 49.98291  ?  466  LEU   A C   1 
ATOM   3649  O  O   . LEU   A 1 466  ? -18.10500  86.64500  13.19400  1.000 59.24031  ?  466  LEU   A O   1 
ATOM   3650  C  CB  . LEU   A 1 466  ? -16.32700  87.33800  15.67200  1.000 33.63311  ?  466  LEU   A CB  1 
ATOM   3651  C  CG  . LEU   A 1 466  ? -15.02400  86.62000  15.31000  1.000 31.20138  ?  466  LEU   A CG  1 
ATOM   3652  C  CD1 . LEU   A 1 466  ? -13.86800  87.60600  15.20400  1.000 31.89776  ?  466  LEU   A CD1 1 
ATOM   3653  C  CD2 . LEU   A 1 466  ? -14.71200  85.51300  16.30600  1.000 33.15951  ?  466  LEU   A CD2 1 
ATOM   3654  N  N   . LYS   A 1 467  ? -16.22100  87.55100  12.35800  1.000 48.52473  ?  467  LYS   A N   1 
ATOM   3655  C  CA  . LYS   A 1 467  ? -16.31300  86.88300  11.06400  1.000 39.40392  ?  467  LYS   A CA  1 
ATOM   3656  C  C   . LYS   A 1 467  ? -15.03900  86.14800  10.67800  1.000 47.60305  ?  467  LYS   A C   1 
ATOM   3657  O  O   . LYS   A 1 467  ? -15.11200  85.02400  10.17500  1.000 47.44735  ?  467  LYS   A O   1 
ATOM   3658  C  CB  . LYS   A 1 467  ? -16.66900  87.91700  9.98100   1.000 25.91418  ?  467  LYS   A CB  1 
ATOM   3659  C  CG  . LYS   A 1 467  ? -17.96200  88.66800  10.25400  1.000 34.38232  ?  467  LYS   A CG  1 
ATOM   3660  C  CD  . LYS   A 1 467  ? -18.09500  89.91300  9.39000   1.000 24.55305  ?  467  LYS   A CD  1 
ATOM   3661  C  CE  . LYS   A 1 467  ? -17.10200  90.98500  9.80400   1.000 37.69521  ?  467  LYS   A CE  1 
ATOM   3662  N  NZ  . LYS   A 1 467  ? -17.46300  92.31600  9.24200   1.000 45.35964  ?  467  LYS   A NZ  1 
ATOM   3663  N  N   . LYS   A 1 468  ? -13.87600  86.75100  10.90900  1.000 50.02950  ?  468  LYS   A N   1 
ATOM   3664  C  CA  . LYS   A 1 468  ? -12.59600  86.19200  10.49400  1.000 49.51522  ?  468  LYS   A CA  1 
ATOM   3665  C  C   . LYS   A 1 468  ? -12.08300  85.20500  11.53600  1.000 52.26799  ?  468  LYS   A C   1 
ATOM   3666  O  O   . LYS   A 1 468  ? -12.14300  85.46800  12.74100  1.000 65.61456  ?  468  LYS   A O   1 
ATOM   3667  C  CB  . LYS   A 1 468  ? -11.58600  87.32200  10.28600  1.000 37.16712  ?  468  LYS   A CB  1 
ATOM   3668  C  CG  . LYS   A 1 468  ? -10.28200  86.92600  9.62000   1.000 50.78356  ?  468  LYS   A CG  1 
ATOM   3669  C  CD  . LYS   A 1 468  ? -9.42200   88.16300  9.40000   1.000 46.96945  ?  468  LYS   A CD  1 
ATOM   3670  C  CE  . LYS   A 1 468  ? -7.94000   87.85400  9.52800   1.000 61.28122  ?  468  LYS   A CE  1 
ATOM   3671  N  NZ  . LYS   A 1 468  ? -7.25000   87.83100  8.21000   1.000 74.68336  ?  468  LYS   A NZ  1 
ATOM   3672  N  N   . ILE   A 1 469  ? -11.58300  84.06000  11.06500  1.000 40.53330  ?  469  ILE   A N   1 
ATOM   3673  C  CA  . ILE   A 1 469  ? -11.07000  83.02100  11.95700  1.000 48.09330  ?  469  ILE   A CA  1 
ATOM   3674  C  C   . ILE   A 1 469  ? -9.63900   82.66800  11.57600  1.000 57.61703  ?  469  ILE   A C   1 
ATOM   3675  O  O   . ILE   A 1 469  ? -8.92800   82.00600  12.34100  1.000 51.29936  ?  469  ILE   A O   1 
ATOM   3676  C  CB  . ILE   A 1 469  ? -11.95300  81.76000  11.93100  1.000 41.48154  ?  469  ILE   A CB  1 
ATOM   3677  C  CG1 . ILE   A 1 469  ? -11.59500  80.88400  10.73100  1.000 63.29792  ?  469  ILE   A CG1 1 
ATOM   3678  C  CG2 . ILE   A 1 469  ? -13.41400  82.13100  11.86600  1.000 42.32501  ?  469  ILE   A CG2 1 
ATOM   3679  C  CD1 . ILE   A 1 469  ? -11.87700  79.41600  10.94700  1.000 62.35954  ?  469  ILE   A CD1 1 
ATOM   3680  N  N   . GLU   A 1 470  ? -9.21100   83.09400  10.38900  1.000 68.00694  ?  470  GLU   A N   1 
ATOM   3681  C  CA  . GLU   A 1 470  ? -7.88000   82.77100  9.88500   1.000 61.12898  ?  470  GLU   A CA  1 
ATOM   3682  C  C   . GLU   A 1 470  ? -6.86000   83.67900  10.56000  1.000 58.01523  ?  470  GLU   A C   1 
ATOM   3683  O  O   . GLU   A 1 470  ? -6.84900   84.89200  10.33000  1.000 64.32436  ?  470  GLU   A O   1 
ATOM   3684  C  CB  . GLU   A 1 470  ? -7.83500   82.92100  8.36700   1.000 73.07951  ?  470  GLU   A CB  1 
ATOM   3685  C  CG  . GLU   A 1 470  ? -8.70100   81.91600  7.62500   1.000 75.06686  ?  470  GLU   A CG  1 
ATOM   3686  C  CD  . GLU   A 1 470  ? -8.09200   80.52700  7.60100   1.000 100.61344 ?  470  GLU   A CD  1 
ATOM   3687  O  OE1 . GLU   A 1 470  ? -7.02900   80.35700  6.96800   1.000 108.91848 ?  470  GLU   A OE1 1 
ATOM   3688  O  OE2 . GLU   A 1 470  ? -8.67000   79.60900  8.22100   1.000 98.14775  -1 470  GLU   A OE2 1 
ATOM   3689  N  N   . ARG   A 1 471  ? -5.99500   83.09400  11.38200  1.000 63.43225  ?  471  ARG   A N   1 
ATOM   3690  C  CA  . ARG   A 1 471  ? -5.06200   83.85000  12.20100  1.000 69.29700  ?  471  ARG   A CA  1 
ATOM   3691  C  C   . ARG   A 1 471  ? -3.63200   83.39500  11.93800  1.000 72.77596  ?  471  ARG   A C   1 
ATOM   3692  O  O   . ARG   A 1 471  ? -3.38300   82.26900  11.49800  1.000 73.75693  ?  471  ARG   A O   1 
ATOM   3693  C  CB  . ARG   A 1 471  ? -5.39900   83.69900  13.69100  1.000 62.01270  ?  471  ARG   A CB  1 
ATOM   3694  C  CG  . ARG   A 1 471  ? -5.22300   82.28600  14.22900  1.000 60.91940  ?  471  ARG   A CG  1 
ATOM   3695  C  CD  . ARG   A 1 471  ? -6.05900   82.06600  15.47700  1.000 40.03961  ?  471  ARG   A CD  1 
ATOM   3696  N  NE  . ARG   A 1 471  ? -7.41100   81.62400  15.15900  1.000 33.50297  ?  471  ARG   A NE  1 
ATOM   3697  C  CZ  . ARG   A 1 471  ? -7.97300   80.52500  15.64200  1.000 45.40567  ?  471  ARG   A CZ  1 
ATOM   3698  N  NH1 . ARG   A 1 471  ? -7.34600   79.75400  16.51500  1.000 34.73702  ?  471  ARG   A NH1 1 
ATOM   3699  N  NH2 . ARG   A 1 471  ? -9.20000   80.19500  15.24700  1.000 61.22222  ?  471  ARG   A NH2 1 
ATOM   3700  N  N   . ASN   A 1 472  ? -2.68800   84.29600  12.21100  1.000 63.73869  ?  472  ASN   A N   1 
ATOM   3701  C  CA  . ASN   A 1 472  ? -1.26200   83.98700  12.10600  1.000 66.33829  ?  472  ASN   A CA  1 
ATOM   3702  C  C   . ASN   A 1 472  ? -0.69100   83.74400  13.50300  1.000 57.81182  ?  472  ASN   A C   1 
ATOM   3703  O  O   . ASN   A 1 472  ? 0.15100    84.48400  14.01000  1.000 69.27601  ?  472  ASN   A O   1 
ATOM   3704  C  CB  . ASN   A 1 472  ? -0.52200   85.11100  11.38500  1.000 57.63965  ?  472  ASN   A CB  1 
ATOM   3705  C  CG  . ASN   A 1 472  ? -0.89300   85.21100  9.92000   1.000 71.15880  ?  472  ASN   A CG  1 
ATOM   3706  O  OD1 . ASN   A 1 472  ? -1.24100   84.21400  9.28700   1.000 89.06378  ?  472  ASN   A OD1 1 
ATOM   3707  N  ND2 . ASN   A 1 472  ? -0.81600   86.41800  9.37100   1.000 55.92376  ?  472  ASN   A ND2 1 
ATOM   3708  N  N   . GLY   A 1 473  ? -1.17600   82.67600  14.12400  1.000 46.70403  ?  473  GLY   A N   1 
ATOM   3709  C  CA  . GLY   A 1 473  ? -0.73100   82.33000  15.45900  1.000 40.44955  ?  473  GLY   A CA  1 
ATOM   3710  C  C   . GLY   A 1 473  ? -1.26400   80.98100  15.87900  1.000 53.78289  ?  473  GLY   A C   1 
ATOM   3711  O  O   . GLY   A 1 473  ? -2.19500   80.44000  15.27200  1.000 71.72030  ?  473  GLY   A O   1 
ATOM   3712  N  N   . THR   A 1 474  ? -0.65500   80.44400  16.93500  1.000 57.25962  ?  474  THR   A N   1 
ATOM   3713  C  CA  . THR   A 1 474  ? -1.03600   79.15700  17.49800  1.000 63.81418  ?  474  THR   A CA  1 
ATOM   3714  C  C   . THR   A 1 474  ? -2.02200   79.28800  18.65500  1.000 60.98945  ?  474  THR   A C   1 
ATOM   3715  O  O   . THR   A 1 474  ? -2.15100   78.35400  19.45500  1.000 58.78875  ?  474  THR   A O   1 
ATOM   3716  C  CB  . THR   A 1 474  ? 0.20900    78.39400  17.95900  1.000 60.39024  ?  474  THR   A CB  1 
ATOM   3717  O  OG1 . THR   A 1 474  ? 1.11700    79.29800  18.60400  1.000 61.39265  ?  474  THR   A OG1 1 
ATOM   3718  C  CG2 . THR   A 1 474  ? 0.90400    77.74000  16.77700  1.000 52.45790  ?  474  THR   A CG2 1 
ATOM   3719  N  N   . TYR   A 1 475  ? -2.72000   80.41400  18.75800  1.000 53.29385  ?  475  TYR   A N   1 
ATOM   3720  C  CA  . TYR   A 1 475  ? -3.61900   80.66000  19.87500  1.000 44.78464  ?  475  TYR   A CA  1 
ATOM   3721  C  C   . TYR   A 1 475  ? -5.04800   80.25600  19.53200  1.000 47.16798  ?  475  TYR   A C   1 
ATOM   3722  O  O   . TYR   A 1 475  ? -5.48700   80.35600  18.38400  1.000 51.93204  ?  475  TYR   A O   1 
ATOM   3723  C  CB  . TYR   A 1 475  ? -3.57900   82.13300  20.28900  1.000 34.26700  ?  475  TYR   A CB  1 
ATOM   3724  C  CG  . TYR   A 1 475  ? -3.71100   83.12400  19.14900  1.000 37.62001  ?  475  TYR   A CG  1 
ATOM   3725  C  CD1 . TYR   A 1 475  ? -4.95800   83.55800  18.71600  1.000 44.94380  ?  475  TYR   A CD1 1 
ATOM   3726  C  CD2 . TYR   A 1 475  ? -2.58500   83.64200  18.52200  1.000 52.05770  ?  475  TYR   A CD2 1 
ATOM   3727  C  CE1 . TYR   A 1 475  ? -5.07900   84.47400  17.68400  1.000 44.35190  ?  475  TYR   A CE1 1 
ATOM   3728  C  CE2 . TYR   A 1 475  ? -2.69700   84.55500  17.48800  1.000 49.64146  ?  475  TYR   A CE2 1 
ATOM   3729  C  CZ  . TYR   A 1 475  ? -3.94500   84.96600  17.07300  1.000 41.74537  ?  475  TYR   A CZ  1 
ATOM   3730  O  OH  . TYR   A 1 475  ? -4.05500   85.87400  16.04400  1.000 56.13453  ?  475  TYR   A OH  1 
ATOM   3731  N  N   . LYS   A 1 476  ? -5.77000   79.79300  20.55000  1.000 41.78604  ?  476  LYS   A N   1 
ATOM   3732  C  CA  . LYS   A 1 476  ? -7.17500   79.44900  20.39000  1.000 44.13489  ?  476  LYS   A CA  1 
ATOM   3733  C  C   . LYS   A 1 476  ? -8.02800   80.71100  20.38100  1.000 47.83139  ?  476  LYS   A C   1 
ATOM   3734  O  O   . LYS   A 1 476  ? -7.75600   81.66800  21.11100  1.000 43.04292  ?  476  LYS   A O   1 
ATOM   3735  C  CB  . LYS   A 1 476  ? -7.63200   78.50900  21.50700  1.000 27.03765  ?  476  LYS   A CB  1 
ATOM   3736  C  CG  . LYS   A 1 476  ? -6.94200   77.15300  21.47800  1.000 43.60892  ?  476  LYS   A CG  1 
ATOM   3737  C  CD  . LYS   A 1 476  ? -7.72000   76.08700  22.23900  1.000 29.56940  ?  476  LYS   A CD  1 
ATOM   3738  C  CE  . LYS   A 1 476  ? -7.53000   76.20900  23.74200  1.000 50.85848  ?  476  LYS   A CE  1 
ATOM   3739  N  NZ  . LYS   A 1 476  ? -7.84600   74.92900  24.44100  1.000 40.77841  ?  476  LYS   A NZ  1 
ATOM   3740  N  N   . LEU   A 1 477  ? -9.06000   80.70900  19.54300  1.000 49.06285  ?  477  LEU   A N   1 
ATOM   3741  C  CA  . LEU   A 1 477  ? -9.93700   81.86000  19.37700  1.000 42.16907  ?  477  LEU   A CA  1 
ATOM   3742  C  C   . LEU   A 1 477  ? -11.25700  81.60500  20.09100  1.000 41.76133  ?  477  LEU   A C   1 
ATOM   3743  O  O   . LEU   A 1 477  ? -11.85400  80.53300  19.94100  1.000 40.36015  ?  477  LEU   A O   1 
ATOM   3744  C  CB  . LEU   A 1 477  ? -10.18000  82.15100  17.89500  1.000 35.37254  ?  477  LEU   A CB  1 
ATOM   3745  C  CG  . LEU   A 1 477  ? -10.89400  83.46300  17.57200  1.000 30.03859  ?  477  LEU   A CG  1 
ATOM   3746  C  CD1 . LEU   A 1 477  ? -10.19000  84.62800  18.24600  1.000 31.95556  ?  477  LEU   A CD1 1 
ATOM   3747  C  CD2 . LEU   A 1 477  ? -10.95700  83.67400  16.06900  1.000 35.83514  ?  477  LEU   A CD2 1 
ATOM   3748  N  N   . TYR   A 1 478  ? -11.70600  82.59000  20.86500  1.000 44.52122  ?  478  TYR   A N   1 
ATOM   3749  C  CA  . TYR   A 1 478  ? -12.95500  82.50400  21.60600  1.000 34.91640  ?  478  TYR   A CA  1 
ATOM   3750  C  C   . TYR   A 1 478  ? -13.82400  83.71000  21.28600  1.000 35.84882  ?  478  TYR   A C   1 
ATOM   3751  O  O   . TYR   A 1 478  ? -13.32000  84.82600  21.13200  1.000 38.51437  ?  478  TYR   A O   1 
ATOM   3752  C  CB  . TYR   A 1 478  ? -12.71000  82.43000  23.11700  1.000 38.85796  ?  478  TYR   A CB  1 
ATOM   3753  C  CG  . TYR   A 1 478  ? -12.25000  81.07500  23.60700  1.000 42.31777  ?  478  TYR   A CG  1 
ATOM   3754  C  CD1 . TYR   A 1 478  ? -10.90300  80.73800  23.61800  1.000 41.26965  ?  478  TYR   A CD1 1 
ATOM   3755  C  CD2 . TYR   A 1 478  ? -13.16400  80.13800  24.07000  1.000 42.91872  ?  478  TYR   A CD2 1 
ATOM   3756  C  CE1 . TYR   A 1 478  ? -10.48000  79.50300  24.07000  1.000 45.85059  ?  478  TYR   A CE1 1 
ATOM   3757  C  CE2 . TYR   A 1 478  ? -12.75000  78.90100  24.52500  1.000 38.34806  ?  478  TYR   A CE2 1 
ATOM   3758  C  CZ  . TYR   A 1 478  ? -11.40700  78.58800  24.52200  1.000 49.30804  ?  478  TYR   A CZ  1 
ATOM   3759  O  OH  . TYR   A 1 478  ? -10.99000  77.35700  24.97200  1.000 46.72723  ?  478  TYR   A OH  1 
ATOM   3760  N  N   . ASN   A 1 479  ? -15.13100  83.47800  21.19100  1.000 40.51314  ?  479  ASN   A N   1 
ATOM   3761  C  CA  . ASN   A 1 479  ? -16.10800  84.52600  20.93400  1.000 39.73538  ?  479  ASN   A CA  1 
ATOM   3762  C  C   . ASN   A 1 479  ? -17.04600  84.64200  22.12700  1.000 41.72623  ?  479  ASN   A C   1 
ATOM   3763  O  O   . ASN   A 1 479  ? -17.48700  83.62900  22.68100  1.000 44.14169  ?  479  ASN   A O   1 
ATOM   3764  C  CB  . ASN   A 1 479  ? -16.90700  84.23200  19.66000  1.000 35.52613  ?  479  ASN   A CB  1 
ATOM   3765  C  CG  . ASN   A 1 479  ? -17.48500  85.48400  19.03200  1.000 44.20058  ?  479  ASN   A CG  1 
ATOM   3766  O  OD1 . ASN   A 1 479  ? -16.88100  86.55700  19.09000  1.000 40.11488  ?  479  ASN   A OD1 1 
ATOM   3767  N  ND2 . ASN   A 1 479  ? -18.66100  85.35600  18.42800  1.000 45.21477  ?  479  ASN   A ND2 1 
ATOM   3768  N  N   . GLY   A 1 480  ? -17.35100  85.87300  22.52000  1.000 44.07402  ?  480  GLY   A N   1 
ATOM   3769  C  CA  . GLY   A 1 480  ? -18.18400  86.11300  23.68100  1.000 38.00077  ?  480  GLY   A CA  1 
ATOM   3770  C  C   . GLY   A 1 480  ? -19.25000  87.15400  23.41300  1.000 42.30590  ?  480  GLY   A C   1 
ATOM   3771  O  O   . GLY   A 1 480  ? -19.09900  88.02800  22.55800  1.000 41.16559  ?  480  GLY   A O   1 
ATOM   3772  N  N   . TYR   A 1 481  ? -20.34100  87.04800  24.16900  1.000 42.67949  ?  481  TYR   A N   1 
ATOM   3773  C  CA  . TYR   A 1 481  ? -21.46500  87.96900  24.08100  1.000 34.62569  ?  481  TYR   A CA  1 
ATOM   3774  C  C   . TYR   A 1 481  ? -21.87100  88.39400  25.48400  1.000 37.78546  ?  481  TYR   A C   1 
ATOM   3775  O  O   . TYR   A 1 481  ? -21.79800  87.60000  26.42600  1.000 44.68459  ?  481  TYR   A O   1 
ATOM   3776  C  CB  . TYR   A 1 481  ? -22.66000  87.32500  23.36400  1.000 38.01667  ?  481  TYR   A CB  1 
ATOM   3777  C  CG  . TYR   A 1 481  ? -23.95600  88.09900  23.48400  1.000 32.32408  ?  481  TYR   A CG  1 
ATOM   3778  C  CD1 . TYR   A 1 481  ? -24.21600  89.18400  22.65800  1.000 24.06126  ?  481  TYR   A CD1 1 
ATOM   3779  C  CD2 . TYR   A 1 481  ? -24.92200  87.73800  24.41600  1.000 35.11629  ?  481  TYR   A CD2 1 
ATOM   3780  C  CE1 . TYR   A 1 481  ? -25.39800  89.89200  22.76100  1.000 50.99455  ?  481  TYR   A CE1 1 
ATOM   3781  C  CE2 . TYR   A 1 481  ? -26.10600  88.44100  24.52700  1.000 31.67374  ?  481  TYR   A CE2 1 
ATOM   3782  C  CZ  . TYR   A 1 481  ? -26.34000  89.51600  23.69600  1.000 52.01743  ?  481  TYR   A CZ  1 
ATOM   3783  O  OH  . TYR   A 1 481  ? -27.52000  90.21900  23.80200  1.000 59.84986  ?  481  TYR   A OH  1 
ATOM   3784  N  N   . GLY   A 1 482  ? -22.30000  89.64700  25.61900  1.000 35.61453  ?  482  GLY   A N   1 
ATOM   3785  C  CA  . GLY   A 1 482  ? -22.74600  90.14900  26.89500  1.000 38.03611  ?  482  GLY   A CA  1 
ATOM   3786  C  C   . GLY   A 1 482  ? -22.88100  91.65700  26.93500  1.000 42.40251  ?  482  GLY   A C   1 
ATOM   3787  O  O   . GLY   A 1 482  ? -22.01600  92.39800  26.45700  1.000 45.73194  ?  482  GLY   A O   1 
ATOM   3788  N  N   . PRO   A 1 483  ? -23.98400  92.14100  27.49800  1.000 38.40686  ?  483  PRO   A N   1 
ATOM   3789  C  CA  . PRO   A 1 483  ? -24.13400  93.57900  27.71900  1.000 32.47383  ?  483  PRO   A CA  1 
ATOM   3790  C  C   . PRO   A 1 483  ? -23.48400  94.00400  29.02600  1.000 46.23240  ?  483  PRO   A C   1 
ATOM   3791  O  O   . PRO   A 1 483  ? -23.26200  93.20100  29.93500  1.000 50.40826  ?  483  PRO   A O   1 
ATOM   3792  C  CB  . PRO   A 1 483  ? -25.65300  93.76500  27.77400  1.000 33.09612  ?  483  PRO   A CB  1 
ATOM   3793  C  CG  . PRO   A 1 483  ? -26.14000  92.47700  28.35300  1.000 23.22602  ?  483  PRO   A CG  1 
ATOM   3794  C  CD  . PRO   A 1 483  ? -25.21400  91.40100  27.83400  1.000 29.23354  ?  483  PRO   A CD  1 
ATOM   3795  N  N   . THR   A 1 484  ? -23.17300  95.30200  29.10400  1.000 41.25667  ?  484  THR   A N   1 
ATOM   3796  C  CA  . THR   A 1 484  ? -22.60800  95.85100  30.33300  1.000 27.61700  ?  484  THR   A CA  1 
ATOM   3797  C  C   . THR   A 1 484  ? -23.55500  95.66300  31.51200  1.000 35.93402  ?  484  THR   A C   1 
ATOM   3798  O  O   . THR   A 1 484  ? -23.10600  95.53400  32.65600  1.000 40.33527  ?  484  THR   A O   1 
ATOM   3799  C  CB  . THR   A 1 484  ? -22.28600  97.33500  30.15000  1.000 21.54245  ?  484  THR   A CB  1 
ATOM   3800  O  OG1 . THR   A 1 484  ? -21.77400  97.55700  28.83000  1.000 35.14888  ?  484  THR   A OG1 1 
ATOM   3801  C  CG2 . THR   A 1 484  ? -21.25000  97.78100  31.16600  1.000 37.94325  ?  484  THR   A CG2 1 
ATOM   3802  N  N   . GLU   A 1 485  ? -24.86400  95.63900  31.25000  1.000 47.31460  ?  485  GLU   A N   1 
ATOM   3803  C  CA  . GLU   A 1 485  ? -25.84400  95.46000  32.31400  1.000 39.18091  ?  485  GLU   A CA  1 
ATOM   3804  C  C   . GLU   A 1 485  ? -25.72200  94.09100  32.97000  1.000 45.05560  ?  485  GLU   A C   1 
ATOM   3805  O  O   . GLU   A 1 485  ? -26.09700  93.92900  34.13800  1.000 42.90826  ?  485  GLU   A O   1 
ATOM   3806  C  CB  . GLU   A 1 485  ? -27.25600  95.66200  31.75800  1.000 33.88818  ?  485  GLU   A CB  1 
ATOM   3807  C  CG  . GLU   A 1 485  ? -27.57800  97.09500  31.33100  1.000 38.31163  ?  485  GLU   A CG  1 
ATOM   3808  C  CD  . GLU   A 1 485  ? -26.96800  97.48500  29.99000  1.000 40.64567  ?  485  GLU   A CD  1 
ATOM   3809  O  OE1 . GLU   A 1 485  ? -26.13300  96.72500  29.45500  1.000 37.18260  ?  485  GLU   A OE1 1 
ATOM   3810  O  OE2 . GLU   A 1 485  ? -27.33200  98.55900  29.46800  1.000 49.88481  -1 485  GLU   A OE2 1 
ATOM   3811  N  N   . CYS   A 1 486  ? -25.20700  93.10000  32.24100  1.000 47.95220  ?  486  CYS   A N   1 
ATOM   3812  C  CA  . CYS   A 1 486  ? -24.98400  91.77300  32.79900  1.000 49.65982  ?  486  CYS   A CA  1 
ATOM   3813  C  C   . CYS   A 1 486  ? -23.49500  91.47000  32.89800  1.000 43.44143  ?  486  CYS   A C   1 
ATOM   3814  O  O   . CYS   A 1 486  ? -22.99400  90.52000  32.28800  1.000 53.61120  ?  486  CYS   A O   1 
ATOM   3815  C  CB  . CYS   A 1 486  ? -25.69500  90.70300  31.96400  1.000 57.76638  ?  486  CYS   A CB  1 
ATOM   3816  S  SG  . CYS   A 1 486  ? -27.50500  90.81700  31.97900  1.000 47.60327  ?  486  CYS   A SG  1 
ATOM   3817  N  N   . THR   A 1 487  ? -22.79200  92.29000  33.68700  1.000 45.14625  ?  487  THR   A N   1 
ATOM   3818  C  CA  . THR   A 1 487  ? -21.36200  92.15400  33.99000  1.000 61.72767  ?  487  THR   A CA  1 
ATOM   3819  C  C   . THR   A 1 487  ? -20.59300  92.37400  32.69500  1.000 66.76594  ?  487  THR   A C   1 
ATOM   3820  O  O   . THR   A 1 487  ? -20.70600  93.46700  32.11200  1.000 69.96183  ?  487  THR   A O   1 
ATOM   3821  C  CB  . THR   A 1 487  ? -21.09700  90.82200  34.71800  1.000 51.18796  ?  487  THR   A CB  1 
ATOM   3822  O  OG1 . THR   A 1 487  ? -22.13200  90.59400  35.68200  1.000 52.55816  ?  487  THR   A OG1 1 
ATOM   3823  C  CG2 . THR   A 1 487  ? -19.75700  90.85700  35.46200  1.000 50.75401  ?  487  THR   A CG2 1 
ATOM   3824  N  N   . ILE   A 1 488  ? -19.83600  91.39900  32.20200  1.000 39.85210  ?  488  ILE   A N   1 
ATOM   3825  C  CA  . ILE   A 1 488  ? -18.97900  91.56700  31.03200  1.000 44.99823  ?  488  ILE   A CA  1 
ATOM   3826  C  C   . ILE   A 1 488  ? -19.47500  90.70900  29.87400  1.000 45.86540  ?  488  ILE   A C   1 
ATOM   3827  O  O   . ILE   A 1 488  ? -19.80700  91.22300  28.80100  1.000 55.46852  ?  488  ILE   A O   1 
ATOM   3828  C  CB  . ILE   A 1 488  ? -17.50900  91.24500  31.39200  1.000 36.39540  ?  488  ILE   A CB  1 
ATOM   3829  C  CG1 . ILE   A 1 488  ? -17.00500  92.17800  32.50000  1.000 39.17455  ?  488  ILE   A CG1 1 
ATOM   3830  C  CG2 . ILE   A 1 488  ? -16.59800  91.25500  30.15700  1.000 41.02282  ?  488  ILE   A CG2 1 
ATOM   3831  C  CD1 . ILE   A 1 488  ? -16.30800  91.43900  33.64000  1.000 34.47505  ?  488  ILE   A CD1 1 
ATOM   3832  N  N   . MET   A 1 489  ? -19.55800  89.39900  30.08400  1.000 35.72140  ?  489  MET   A N   1 
ATOM   3833  C  CA  . MET   A 1 489  ? -20.05200  88.46400  29.09200  1.000 30.66876  ?  489  MET   A CA  1 
ATOM   3834  C  C   . MET   A 1 489  ? -20.90900  87.40700  29.77300  1.000 42.35947  ?  489  MET   A C   1 
ATOM   3835  O  O   . MET   A 1 489  ? -20.71700  87.08900  30.95000  1.000 44.85157  ?  489  MET   A O   1 
ATOM   3836  C  CB  . MET   A 1 489  ? -18.90100  87.79700  28.33200  1.000 46.10187  ?  489  MET   A CB  1 
ATOM   3837  C  CG  . MET   A 1 489  ? -18.01300  88.77500  27.57800  1.000 48.12022  ?  489  MET   A CG  1 
ATOM   3838  S  SD  . MET   A 1 489  ? -16.79100  87.94200  26.55000  1.000 50.20825  ?  489  MET   A SD  1 
ATOM   3839  C  CE  . MET   A 1 489  ? -15.98600  89.33700  25.76700  1.000 55.10633  ?  489  MET   A CE  1 
ATOM   3840  N  N   . VAL   A 1 490  ? -21.85700  86.86600  29.01300  1.000 38.29072  ?  490  VAL   A N   1 
ATOM   3841  C  CA  . VAL   A 1 490  ? -22.74100  85.82100  29.50800  1.000 28.69891  ?  490  VAL   A CA  1 
ATOM   3842  C  C   . VAL   A 1 490  ? -22.62000  84.52200  28.72600  1.000 38.28845  ?  490  VAL   A C   1 
ATOM   3843  O  O   . VAL   A 1 490  ? -23.01900  83.46700  29.24600  1.000 36.60631  ?  490  VAL   A O   1 
ATOM   3844  C  CB  . VAL   A 1 490  ? -24.20800  86.30100  29.51900  1.000 31.86849  ?  490  VAL   A CB  1 
ATOM   3845  C  CG1 . VAL   A 1 490  ? -24.39300  87.39500  30.55800  1.000 36.78149  ?  490  VAL   A CG1 1 
ATOM   3846  C  CG2 . VAL   A 1 490  ? -24.61700  86.79800  28.13900  1.000 34.57140  ?  490  VAL   A CG2 1 
ATOM   3847  N  N   . THR   A 1 491  ? -22.09200  84.54200  27.50300  1.000 43.32636  ?  491  THR   A N   1 
ATOM   3848  C  CA  . THR   A 1 491  ? -21.88400  83.33500  26.71700  1.000 38.90219  ?  491  THR   A CA  1 
ATOM   3849  C  C   . THR   A 1 491  ? -20.48400  83.35000  26.12100  1.000 44.46231  ?  491  THR   A C   1 
ATOM   3850  O  O   . THR   A 1 491  ? -19.92400  84.41300  25.83900  1.000 37.30275  ?  491  THR   A O   1 
ATOM   3851  C  CB  . THR   A 1 491  ? -22.92300  83.19900  25.59300  1.000 41.00902  ?  491  THR   A CB  1 
ATOM   3852  O  OG1 . THR   A 1 491  ? -22.84100  84.33600  24.72400  1.000 50.45583  ?  491  THR   A OG1 1 
ATOM   3853  C  CG2 . THR   A 1 491  ? -24.32600  83.10600  26.16800  1.000 42.32261  ?  491  THR   A CG2 1 
ATOM   3854  N  N   . MET   A 1 492  ? -19.92500  82.15700  25.92900  1.000 33.33810  ?  492  MET   A N   1 
ATOM   3855  C  CA  . MET   A 1 492  ? -18.58800  82.00600  25.37500  1.000 36.15901  ?  492  MET   A CA  1 
ATOM   3856  C  C   . MET   A 1 492  ? -18.57900  80.84800  24.39000  1.000 42.41692  ?  492  MET   A C   1 
ATOM   3857  O  O   . MET   A 1 492  ? -19.15900  79.79200  24.65800  1.000 43.59586  ?  492  MET   A O   1 
ATOM   3858  C  CB  . MET   A 1 492  ? -17.54800  81.76400  26.47700  1.000 32.12612  ?  492  MET   A CB  1 
ATOM   3859  C  CG  . MET   A 1 492  ? -16.11100  81.77900  25.98800  1.000 24.81092  ?  492  MET   A CG  1 
ATOM   3860  S  SD  . MET   A 1 492  ? -15.64500  83.38200  25.30900  1.000 38.18882  ?  492  MET   A SD  1 
ATOM   3861  C  CE  . MET   A 1 492  ? -15.96800  84.44800  26.71100  1.000 23.67474  ?  492  MET   A CE  1 
ATOM   3862  N  N   . PHE   A 1 493  ? -17.91600  81.05200  23.25200  1.000 46.22918  ?  493  PHE   A N   1 
ATOM   3863  C  CA  . PHE   A 1 493  ? -17.79400  80.03600  22.21800  1.000 42.93182  ?  493  PHE   A CA  1 
ATOM   3864  C  C   . PHE   A 1 493  ? -16.35200  79.95900  21.74600  1.000 46.67603  ?  493  PHE   A C   1 
ATOM   3865  O  O   . PHE   A 1 493  ? -15.69400  80.98700  21.56900  1.000 47.38242  ?  493  PHE   A O   1 
ATOM   3866  C  CB  . PHE   A 1 493  ? -18.70400  80.33500  21.02200  1.000 33.99158  ?  493  PHE   A CB  1 
ATOM   3867  C  CG  . PHE   A 1 493  ? -18.63400  79.30200  19.93400  1.000 40.65998  ?  493  PHE   A CG  1 
ATOM   3868  C  CD1 . PHE   A 1 493  ? -19.14100  78.03000  20.13600  1.000 36.78218  ?  493  PHE   A CD1 1 
ATOM   3869  C  CD2 . PHE   A 1 493  ? -18.06500  79.60500  18.70800  1.000 41.25648  ?  493  PHE   A CD2 1 
ATOM   3870  C  CE1 . PHE   A 1 493  ? -19.07800  77.07600  19.13800  1.000 47.17254  ?  493  PHE   A CE1 1 
ATOM   3871  C  CE2 . PHE   A 1 493  ? -17.99900  78.65600  17.70600  1.000 45.58163  ?  493  PHE   A CE2 1 
ATOM   3872  C  CZ  . PHE   A 1 493  ? -18.50700  77.39000  17.92100  1.000 47.22592  ?  493  PHE   A CZ  1 
ATOM   3873  N  N   . GLU   A 1 494  ? -15.86600  78.73700  21.54000  1.000 43.81764  ?  494  GLU   A N   1 
ATOM   3874  C  CA  . GLU   A 1 494  ? -14.53000  78.51800  20.99900  1.000 38.95312  ?  494  GLU   A CA  1 
ATOM   3875  C  C   . GLU   A 1 494  ? -14.64800  78.36800  19.48700  1.000 37.38623  ?  494  GLU   A C   1 
ATOM   3876  O  O   . GLU   A 1 494  ? -15.26500  77.41800  18.99600  1.000 43.41493  ?  494  GLU   A O   1 
ATOM   3877  C  CB  . GLU   A 1 494  ? -13.88100  77.28900  21.63000  1.000 37.45557  ?  494  GLU   A CB  1 
ATOM   3878  C  CG  . GLU   A 1 494  ? -12.46000  77.03800  21.15400  1.000 44.76672  ?  494  GLU   A CG  1 
ATOM   3879  C  CD  . GLU   A 1 494  ? -11.85700  75.77600  21.73800  1.000 48.82256  ?  494  GLU   A CD  1 
ATOM   3880  O  OE1 . GLU   A 1 494  ? -12.43600  75.22400  22.69800  1.000 53.09623  ?  494  GLU   A OE1 1 
ATOM   3881  O  OE2 . GLU   A 1 494  ? -10.80100  75.33600  21.23500  1.000 54.29363  -1 494  GLU   A OE2 1 
ATOM   3882  N  N   . VAL   A 1 495  ? -14.06400  79.31100  18.75000  1.000 38.86360  ?  495  VAL   A N   1 
ATOM   3883  C  CA  . VAL   A 1 495  ? -14.08700  79.27600  17.29300  1.000 37.10867  ?  495  VAL   A CA  1 
ATOM   3884  C  C   . VAL   A 1 495  ? -13.17000  78.16200  16.80500  1.000 44.26573  ?  495  VAL   A C   1 
ATOM   3885  O  O   . VAL   A 1 495  ? -11.96500  78.37100  16.62400  1.000 55.09459  ?  495  VAL   A O   1 
ATOM   3886  C  CB  . VAL   A 1 495  ? -13.67300  80.63300  16.69700  1.000 34.70969  ?  495  VAL   A CB  1 
ATOM   3887  C  CG1 . VAL   A 1 495  ? -13.87700  80.63300  15.19200  1.000 45.11603  ?  495  VAL   A CG1 1 
ATOM   3888  C  CG2 . VAL   A 1 495  ? -14.45600  81.75900  17.35200  1.000 41.87069  ?  495  VAL   A CG2 1 
ATOM   3889  N  N   . ASP   A 1 496  ? -13.73400  76.97300  16.59000  1.000 45.35946  ?  496  ASP   A N   1 
ATOM   3890  C  CA  . ASP   A 1 496  ? -12.97300  75.81500  16.12900  1.000 51.46728  ?  496  ASP   A CA  1 
ATOM   3891  C  C   . ASP   A 1 496  ? -13.03700  75.65800  14.61300  1.000 57.98734  ?  496  ASP   A C   1 
ATOM   3892  O  O   . ASP   A 1 496  ? -11.99900  75.59600  13.94600  1.000 71.52199  ?  496  ASP   A O   1 
ATOM   3893  C  CB  . ASP   A 1 496  ? -13.47900  74.54400  16.82900  1.000 53.19655  ?  496  ASP   A CB  1 
ATOM   3894  C  CG  . ASP   A 1 496  ? -14.98600  74.37700  16.72600  1.000 65.39867  ?  496  ASP   A CG  1 
ATOM   3895  O  OD1 . ASP   A 1 496  ? -15.70200  75.40200  16.72200  1.000 62.02941  ?  496  ASP   A OD1 1 
ATOM   3896  O  OD2 . ASP   A 1 496  ? -15.45400  73.22200  16.64400  1.000 66.17926  -1 496  ASP   A OD2 1 
ATOM   3897  N  N   . LYS   A 1 497  ? -14.23500  75.59200  14.05700  1.000 51.64363  ?  497  LYS   A N   1 
ATOM   3898  C  CA  . LYS   A 1 497  ? -14.46100  75.47100  12.62700  1.000 56.69384  ?  497  LYS   A CA  1 
ATOM   3899  C  C   . LYS   A 1 497  ? -14.73100  76.83800  12.02100  1.000 63.44776  ?  497  LYS   A C   1 
ATOM   3900  O  O   . LYS   A 1 497  ? -14.96800  77.81700  12.73400  1.000 69.62797  ?  497  LYS   A O   1 
ATOM   3901  C  CB  . LYS   A 1 497  ? -15.64200  74.53100  12.36200  1.000 59.79511  ?  497  LYS   A CB  1 
ATOM   3902  C  CG  . LYS   A 1 497  ? -15.57100  73.19900  13.09900  1.000 77.29844  ?  497  LYS   A CG  1 
ATOM   3903  C  CD  . LYS   A 1 497  ? -16.59900  72.20800  12.55900  1.000 77.00570  ?  497  LYS   A CD  1 
ATOM   3904  C  CE  . LYS   A 1 497  ? -18.02100  72.56600  12.97300  1.000 77.58909  ?  497  LYS   A CE  1 
ATOM   3905  N  NZ  . LYS   A 1 497  ? -18.35300  72.07000  14.34000  1.000 76.86745  ?  497  LYS   A NZ  1 
ATOM   3906  N  N   . PRO   A 1 498  ? -14.67400  76.95600  10.69500  1.000 53.62848  ?  498  PRO   A N   1 
ATOM   3907  C  CA  . PRO   A 1 498  ? -15.20000  78.16700  10.04800  1.000 38.23448  ?  498  PRO   A CA  1 
ATOM   3908  C  C   . PRO   A 1 498  ? -16.72200  78.14000  10.04400  1.000 51.68312  ?  498  PRO   A C   1 
ATOM   3909  O  O   . PRO   A 1 498  ? -17.33700  77.13100  9.69000   1.000 44.92083  ?  498  PRO   A O   1 
ATOM   3910  C  CB  . PRO   A 1 498  ? -14.62800  78.09600  8.62700   1.000 40.70812  ?  498  PRO   A CB  1 
ATOM   3911  C  CG  . PRO   A 1 498  ? -13.50200  77.10800  8.70200   1.000 63.52979  ?  498  PRO   A CG  1 
ATOM   3912  C  CD  . PRO   A 1 498  ? -13.90200  76.12600  9.75700   1.000 55.96849  ?  498  PRO   A CD  1 
ATOM   3913  N  N   . TYR   A 1 499  ? -17.32800  79.25300  10.45200  1.000 51.22187  ?  499  TYR   A N   1 
ATOM   3914  C  CA  . TYR   A 1 499  ? -18.77700  79.37300  10.51200  1.000 44.82852  ?  499  TYR   A CA  1 
ATOM   3915  C  C   . TYR   A 1 499  ? -19.22700  80.58700  9.71400   1.000 43.99306  ?  499  TYR   A C   1 
ATOM   3916  O  O   . TYR   A 1 499  ? -18.52800  81.60200  9.64800   1.000 43.81346  ?  499  TYR   A O   1 
ATOM   3917  C  CB  . TYR   A 1 499  ? -19.28400  79.49900  11.96000  1.000 36.05542  ?  499  TYR   A CB  1 
ATOM   3918  C  CG  . TYR   A 1 499  ? -18.99800  78.29900  12.83400  1.000 39.72070  ?  499  TYR   A CG  1 
ATOM   3919  C  CD1 . TYR   A 1 499  ? -19.87800  77.22600  12.88400  1.000 37.45407  ?  499  TYR   A CD1 1 
ATOM   3920  C  CD2 . TYR   A 1 499  ? -17.85400  78.24300  13.61900  1.000 47.03560  ?  499  TYR   A CD2 1 
ATOM   3921  C  CE1 . TYR   A 1 499  ? -19.62100  76.12700  13.68600  1.000 42.86623  ?  499  TYR   A CE1 1 
ATOM   3922  C  CE2 . TYR   A 1 499  ? -17.58800  77.14900  14.42200  1.000 47.51604  ?  499  TYR   A CE2 1 
ATOM   3923  C  CZ  . TYR   A 1 499  ? -18.47600  76.09300  14.45200  1.000 48.85167  ?  499  TYR   A CZ  1 
ATOM   3924  O  OH  . TYR   A 1 499  ? -18.21700  75.00200  15.25000  1.000 48.62433  ?  499  TYR   A OH  1 
ATOM   3925  N  N   . ALA   A 1 500  ? -20.40700  80.47000  9.10000   1.000 40.04548  ?  500  ALA   A N   1 
ATOM   3926  C  CA  . ALA   A 1 500  ? -21.02600  81.62800  8.46500   1.000 36.92919  ?  500  ALA   A CA  1 
ATOM   3927  C  C   . ALA   A 1 500  ? -21.42400  82.65900  9.51300   1.000 42.75921  ?  500  ALA   A C   1 
ATOM   3928  O  O   . ALA   A 1 500  ? -21.01300  83.82300  9.45000   1.000 65.92405  ?  500  ALA   A O   1 
ATOM   3929  C  CB  . ALA   A 1 500  ? -22.23800  81.19300  7.64100   1.000 49.53373  ?  500  ALA   A CB  1 
ATOM   3930  N  N   . ASN   A 1 501  ? -22.22500  82.24300  10.48800  1.000 33.40320  ?  501  ASN   A N   1 
ATOM   3931  C  CA  . ASN   A 1 501  ? -22.53400  83.04300  11.66800  1.000 35.36025  ?  501  ASN   A CA  1 
ATOM   3932  C  C   . ASN   A 1 501  ? -21.84500  82.36800  12.84800  1.000 53.18272  ?  501  ASN   A C   1 
ATOM   3933  O  O   . ASN   A 1 501  ? -22.30900  81.33400  13.33900  1.000 57.88472  ?  501  ASN   A O   1 
ATOM   3934  C  CB  . ASN   A 1 501  ? -24.03900  83.15600  11.88900  1.000 39.51387  ?  501  ASN   A CB  1 
ATOM   3935  C  CG  . ASN   A 1 501  ? -24.38800  84.05500  13.05800  1.000 39.73160  ?  501  ASN   A CG  1 
ATOM   3936  O  OD1 . ASN   A 1 501  ? -24.27900  83.65700  14.21700  1.000 44.00634  ?  501  ASN   A OD1 1 
ATOM   3937  N  ND2 . ASN   A 1 501  ? -24.80500  85.27900  12.75700  1.000 52.79606  ?  501  ASN   A ND2 1 
ATOM   3938  N  N   . ILE   A 1 502  ? -20.73300  82.94400  13.29100  1.000 46.50803  ?  502  ILE   A N   1 
ATOM   3939  C  CA  . ILE   A 1 502  ? -19.98100  82.38300  14.40900  1.000 44.35677  ?  502  ILE   A CA  1 
ATOM   3940  C  C   . ILE   A 1 502  ? -20.83800  82.45900  15.66600  1.000 45.78068  ?  502  ILE   A C   1 
ATOM   3941  O  O   . ILE   A 1 502  ? -21.25000  83.55600  16.07300  1.000 39.82051  ?  502  ILE   A O   1 
ATOM   3942  C  CB  . ILE   A 1 502  ? -18.64100  83.10300  14.60600  1.000 45.67342  ?  502  ILE   A CB  1 
ATOM   3943  C  CG1 . ILE   A 1 502  ? -17.77100  82.92900  13.36100  1.000 39.55020  ?  502  ILE   A CG1 1 
ATOM   3944  C  CG2 . ILE   A 1 502  ? -17.93900  82.58200  15.85600  1.000 49.00683  ?  502  ILE   A CG2 1 
ATOM   3945  C  CD1 . ILE   A 1 502  ? -16.30100  83.08900  13.62300  1.000 45.74372  ?  502  ILE   A CD1 1 
ATOM   3946  N  N   . PRO   A 1 503  ? -21.13500  81.32700  16.30000  1.000 36.95280  ?  503  PRO   A N   1 
ATOM   3947  C  CA  . PRO   A 1 503  ? -22.01300  81.34600  17.47400  1.000 43.36167  ?  503  PRO   A CA  1 
ATOM   3948  C  C   . PRO   A 1 503  ? -21.40800  82.14600  18.61500  1.000 40.52445  ?  503  PRO   A C   1 
ATOM   3949  O  O   . PRO   A 1 503  ? -20.19000  82.17300  18.81200  1.000 43.95085  ?  503  PRO   A O   1 
ATOM   3950  C  CB  . PRO   A 1 503  ? -22.14300  79.86400  17.84400  1.000 39.72448  ?  503  PRO   A CB  1 
ATOM   3951  C  CG  . PRO   A 1 503  ? -21.78500  79.12200  16.60000  1.000 33.56588  ?  503  PRO   A CG  1 
ATOM   3952  C  CD  . PRO   A 1 503  ? -20.74900  79.95900  15.92000  1.000 38.62289  ?  503  PRO   A CD  1 
ATOM   3953  N  N   . ILE   A 1 504  ? -22.28400  82.81300  19.37000  1.000 33.72166  ?  504  ILE   A N   1 
ATOM   3954  C  CA  . ILE   A 1 504  ? -21.85100  83.49000  20.58900  1.000 34.09043  ?  504  ILE   A CA  1 
ATOM   3955  C  C   . ILE   A 1 504  ? -21.65000  82.52000  21.73900  1.000 42.50696  ?  504  ILE   A C   1 
ATOM   3956  O  O   . ILE   A 1 504  ? -21.09500  82.90800  22.77500  1.000 49.73999  ?  504  ILE   A O   1 
ATOM   3957  C  CB  . ILE   A 1 504  ? -22.85100  84.58500  21.00600  1.000 38.61368  ?  504  ILE   A CB  1 
ATOM   3958  C  CG1 . ILE   A 1 504  ? -24.18900  83.96800  21.41400  1.000 48.51714  ?  504  ILE   A CG1 1 
ATOM   3959  C  CG2 . ILE   A 1 504  ? -23.03700  85.58700  19.87700  1.000 40.16017  ?  504  ILE   A CG2 1 
ATOM   3960  C  CD1 . ILE   A 1 504  ? -25.25300  84.99100  21.74800  1.000 37.26105  ?  504  ILE   A CD1 1 
ATOM   3961  N  N   . GLY   A 1 505  ? -22.08700  81.27700  21.59100  1.000 33.63869  ?  505  GLY   A N   1 
ATOM   3962  C  CA  . GLY   A 1 505  ? -21.76200  80.23300  22.53700  1.000 34.94827  ?  505  GLY   A CA  1 
ATOM   3963  C  C   . GLY   A 1 505  ? -22.89800  79.86300  23.46700  1.000 45.21469  ?  505  GLY   A C   1 
ATOM   3964  O  O   . GLY   A 1 505  ? -24.07800  80.12800  23.22200  1.000 40.94780  ?  505  GLY   A O   1 
ATOM   3965  N  N   . LYS   A 1 506  ? -22.51200  79.22000  24.56400  1.000 39.37277  ?  506  LYS   A N   1 
ATOM   3966  C  CA  . LYS   A 1 506  ? -23.37500  78.72400  25.61600  1.000 32.59860  ?  506  LYS   A CA  1 
ATOM   3967  C  C   . LYS   A 1 506  ? -23.22300  79.57200  26.87500  1.000 34.24121  ?  506  LYS   A C   1 
ATOM   3968  O  O   . LYS   A 1 506  ? -22.17000  80.18000  27.09400  1.000 33.54343  ?  506  LYS   A O   1 
ATOM   3969  C  CB  . LYS   A 1 506  ? -23.04600  77.26100  25.93600  1.000 29.38019  ?  506  LYS   A CB  1 
ATOM   3970  C  CG  . LYS   A 1 506  ? -23.21800  76.31800  24.75500  1.000 32.25086  ?  506  LYS   A CG  1 
ATOM   3971  C  CD  . LYS   A 1 506  ? -23.04500  74.87200  25.18300  1.000 34.13913  ?  506  LYS   A CD  1 
ATOM   3972  C  CE  . LYS   A 1 506  ? -23.49800  73.91300  24.09500  1.000 42.57401  ?  506  LYS   A CE  1 
ATOM   3973  N  NZ  . LYS   A 1 506  ? -23.70300  72.54000  24.63400  1.000 44.37926  ?  506  LYS   A NZ  1 
ATOM   3974  N  N   . PRO   A 1 507  ? -24.25400  79.63900  27.71800  1.000 49.30307  ?  507  PRO   A N   1 
ATOM   3975  C  CA  . PRO   A 1 507  ? -24.17700  80.48700  28.91300  1.000 40.53194  ?  507  PRO   A CA  1 
ATOM   3976  C  C   . PRO   A 1 507  ? -23.07600  80.03900  29.86300  1.000 43.99644  ?  507  PRO   A C   1 
ATOM   3977  O  O   . PRO   A 1 507  ? -22.66500  78.87600  29.88400  1.000 47.25643  ?  507  PRO   A O   1 
ATOM   3978  C  CB  . PRO   A 1 507  ? -25.56100  80.32600  29.55400  1.000 32.40292  ?  507  PRO   A CB  1 
ATOM   3979  C  CG  . PRO   A 1 507  ? -26.44400  79.85300  28.44900  1.000 45.27797  ?  507  PRO   A CG  1 
ATOM   3980  C  CD  . PRO   A 1 507  ? -25.57700  79.00900  27.57400  1.000 38.43828  ?  507  PRO   A CD  1 
ATOM   3981  N  N   . ILE   A 1 508  ? -22.59900  80.99100  30.66500  1.000 49.61240  ?  508  ILE   A N   1 
ATOM   3982  C  CA  . ILE   A 1 508  ? -21.50700  80.74000  31.60000  1.000 37.06857  ?  508  ILE   A CA  1 
ATOM   3983  C  C   . ILE   A 1 508  ? -22.06800  80.26400  32.93500  1.000 41.43264  ?  508  ILE   A C   1 
ATOM   3984  O  O   . ILE   A 1 508  ? -23.23800  79.87400  33.02600  1.000 51.48820  ?  508  ILE   A O   1 
ATOM   3985  C  CB  . ILE   A 1 508  ? -20.63000  81.99400  31.78100  1.000 27.80838  ?  508  ILE   A CB  1 
ATOM   3986  C  CG1 . ILE   A 1 508  ? -21.40900  83.11100  32.48100  1.000 44.18134  ?  508  ILE   A CG1 1 
ATOM   3987  C  CG2 . ILE   A 1 508  ? -20.11500  82.47700  30.43500  1.000 25.98781  ?  508  ILE   A CG2 1 
ATOM   3988  C  CD1 . ILE   A 1 508  ? -20.53800  84.26500  32.94300  1.000 27.40261  ?  508  ILE   A CD1 1 
ATOM   3989  N  N   . ASP   A 1 509  ? -21.23400  80.28800  33.97400  1.000 44.60109  ?  509  ASP   A N   1 
ATOM   3990  C  CA  . ASP   A 1 509  ? -21.64300  79.80500  35.28700  1.000 38.42420  ?  509  ASP   A CA  1 
ATOM   3991  C  C   . ASP   A 1 509  ? -22.77800  80.64800  35.85600  1.000 48.39243  ?  509  ASP   A C   1 
ATOM   3992  O  O   . ASP   A 1 509  ? -22.76700  81.87900  35.76200  1.000 50.43004  ?  509  ASP   A O   1 
ATOM   3993  C  CB  . ASP   A 1 509  ? -20.45400  79.82000  36.25000  1.000 34.67681  ?  509  ASP   A CB  1 
ATOM   3994  C  CG  . ASP   A 1 509  ? -19.46500  78.70600  35.97500  1.000 36.79419  ?  509  ASP   A CG  1 
ATOM   3995  O  OD1 . ASP   A 1 509  ? -19.76900  77.83100  35.13800  1.000 42.48455  ?  509  ASP   A OD1 1 
ATOM   3996  O  OD2 . ASP   A 1 509  ? -18.38200  78.70500  36.59800  1.000 56.33157  -1 509  ASP   A OD2 1 
ATOM   3997  N  N   . ARG   A 1 510  ? -23.76200  79.96700  36.45200  1.000 54.15640  ?  510  ARG   A N   1 
ATOM   3998  C  CA  . ARG   A 1 510  ? -24.89700  80.61200  37.11800  1.000 43.27452  ?  510  ARG   A CA  1 
ATOM   3999  C  C   . ARG   A 1 510  ? -25.60000  81.60100  36.19300  1.000 50.93607  ?  510  ARG   A C   1 
ATOM   4000  O  O   . ARG   A 1 510  ? -26.00900  82.68700  36.60600  1.000 54.95873  ?  510  ARG   A O   1 
ATOM   4001  C  CB  . ARG   A 1 510  ? -24.45600  81.30200  38.41000  1.000 43.42052  ?  510  ARG   A CB  1 
ATOM   4002  C  CG  . ARG   A 1 510  ? -23.80400  80.38000  39.42000  1.000 44.01243  ?  510  ARG   A CG  1 
ATOM   4003  C  CD  . ARG   A 1 510  ? -23.42600  81.14500  40.67000  1.000 49.52777  ?  510  ARG   A CD  1 
ATOM   4004  N  NE  . ARG   A 1 510  ? -22.57900  80.36100  41.56000  1.000 62.17364  ?  510  ARG   A NE  1 
ATOM   4005  C  CZ  . ARG   A 1 510  ? -21.26100  80.27600  41.45200  1.000 48.48793  ?  510  ARG   A CZ  1 
ATOM   4006  N  NH1 . ARG   A 1 510  ? -20.60300  80.91000  40.49500  1.000 47.32025  ?  510  ARG   A NH1 1 
ATOM   4007  N  NH2 . ARG   A 1 510  ? -20.58500  79.53500  42.32500  1.000 68.90140  ?  510  ARG   A NH2 1 
ATOM   4008  N  N   . THR   A 1 511  ? -25.73300  81.22100  34.92400  1.000 49.20742  ?  511  THR   A N   1 
ATOM   4009  C  CA  . THR   A 1 511  ? -26.33500  82.07200  33.90700  1.000 45.15651  ?  511  THR   A CA  1 
ATOM   4010  C  C   . THR   A 1 511  ? -27.14900  81.20000  32.96400  1.000 53.18028  ?  511  THR   A C   1 
ATOM   4011  O  O   . THR   A 1 511  ? -26.66600  80.15900  32.51000  1.000 62.36931  ?  511  THR   A O   1 
ATOM   4012  C  CB  . THR   A 1 511  ? -25.27000  82.84900  33.12000  1.000 41.46728  ?  511  THR   A CB  1 
ATOM   4013  O  OG1 . THR   A 1 511  ? -24.52400  83.68500  34.01300  1.000 38.25492  ?  511  THR   A OG1 1 
ATOM   4014  C  CG2 . THR   A 1 511  ? -25.92000  83.72000  32.05400  1.000 54.60520  ?  511  THR   A CG2 1 
ATOM   4015  N  N   . ARG   A 1 512  ? -28.38200  81.61800  32.68300  1.000 50.45153  ?  512  ARG   A N   1 
ATOM   4016  C  CA  . ARG   A 1 512  ? -29.25600  80.91200  31.75900  1.000 44.32910  ?  512  ARG   A CA  1 
ATOM   4017  C  C   . ARG   A 1 512  ? -29.83900  81.89700  30.75600  1.000 49.16218  ?  512  ARG   A C   1 
ATOM   4018  O  O   . ARG   A 1 512  ? -30.28600  82.98800  31.12700  1.000 43.89764  ?  512  ARG   A O   1 
ATOM   4019  C  CB  . ARG   A 1 512  ? -30.38700  80.17300  32.48800  1.000 37.52571  ?  512  ARG   A CB  1 
ATOM   4020  C  CG  . ARG   A 1 512  ? -31.35000  79.48300  31.52900  1.000 75.14528  ?  512  ARG   A CG  1 
ATOM   4021  C  CD  . ARG   A 1 512  ? -32.21000  78.42900  32.20400  1.000 81.58492  ?  512  ARG   A CD  1 
ATOM   4022  N  NE  . ARG   A 1 512  ? -33.29700  79.01800  32.97100  1.000 79.30038  ?  512  ARG   A NE  1 
ATOM   4023  C  CZ  . ARG   A 1 512  ? -33.25700  79.22700  34.27900  1.000 85.25873  ?  512  ARG   A CZ  1 
ATOM   4024  N  NH1 . ARG   A 1 512  ? -32.20300  78.88300  35.00200  1.000 86.05816  ?  512  ARG   A NH1 1 
ATOM   4025  N  NH2 . ARG   A 1 512  ? -34.29800  79.79900  34.87600  1.000 86.67114  ?  512  ARG   A NH2 1 
ATOM   4026  N  N   . ILE   A 1 513  ? -29.82100  81.50300  29.48500  1.000 44.28957  ?  513  ILE   A N   1 
ATOM   4027  C  CA  . ILE   A 1 513  ? -30.30300  82.32300  28.38000  1.000 48.53153  ?  513  ILE   A CA  1 
ATOM   4028  C  C   . ILE   A 1 513  ? -31.62300  81.74700  27.89100  1.000 50.96257  ?  513  ILE   A C   1 
ATOM   4029  O  O   . ILE   A 1 513  ? -31.78400  80.52400  27.80000  1.000 48.54503  ?  513  ILE   A O   1 
ATOM   4030  C  CB  . ILE   A 1 513  ? -29.26900  82.38400  27.23900  1.000 37.74681  ?  513  ILE   A CB  1 
ATOM   4031  C  CG1 . ILE   A 1 513  ? -27.96800  83.02200  27.73000  1.000 42.79245  ?  513  ILE   A CG1 1 
ATOM   4032  C  CG2 . ILE   A 1 513  ? -29.82000  83.15400  26.05300  1.000 39.87029  ?  513  ILE   A CG2 1 
ATOM   4033  C  CD1 . ILE   A 1 513  ? -28.14200  84.42300  28.26600  1.000 37.98440  ?  513  ILE   A CD1 1 
ATOM   4034  N  N   . LEU   A 1 514  ? -32.57000  82.63300  27.58500  1.000 37.17920  ?  514  LEU   A N   1 
ATOM   4035  C  CA  . LEU   A 1 514  ? -33.89200  82.24900  27.11000  1.000 42.50477  ?  514  LEU   A CA  1 
ATOM   4036  C  C   . LEU   A 1 514  ? -34.24000  83.05700  25.86900  1.000 47.75978  ?  514  LEU   A C   1 
ATOM   4037  O  O   . LEU   A 1 514  ? -34.17600  84.29100  25.89000  1.000 50.31031  ?  514  LEU   A O   1 
ATOM   4038  C  CB  . LEU   A 1 514  ? -34.95300  82.47100  28.19400  1.000 33.21988  ?  514  LEU   A CB  1 
ATOM   4039  C  CG  . LEU   A 1 514  ? -34.92900  81.51000  29.38300  1.000 41.70432  ?  514  LEU   A CG  1 
ATOM   4040  C  CD1 . LEU   A 1 514  ? -35.46800  82.18400  30.63600  1.000 34.37897  ?  514  LEU   A CD1 1 
ATOM   4041  C  CD2 . LEU   A 1 514  ? -35.72700  80.25400  29.06900  1.000 47.00862  ?  514  LEU   A CD2 1 
ATOM   4042  N  N   . ILE   A 1 515  ? -34.60800  82.35900  24.79900  1.000 39.22113  ?  515  ILE   A N   1 
ATOM   4043  C  CA  . ILE   A 1 515  ? -35.08800  82.99000  23.57500  1.000 39.77376  ?  515  ILE   A CA  1 
ATOM   4044  C  C   . ILE   A 1 515  ? -36.61100  83.04000  23.64000  1.000 43.38077  ?  515  ILE   A C   1 
ATOM   4045  O  O   . ILE   A 1 515  ? -37.28100  82.01000  23.52100  1.000 33.85514  ?  515  ILE   A O   1 
ATOM   4046  C  CB  . ILE   A 1 515  ? -34.60900  82.23700  22.33000  1.000 38.79342  ?  515  ILE   A CB  1 
ATOM   4047  C  CG1 . ILE   A 1 515  ? -33.07900  82.19700  22.28200  1.000 41.95913  ?  515  ILE   A CG1 1 
ATOM   4048  C  CG2 . ILE   A 1 515  ? -35.17300  82.88400  21.08000  1.000 38.16060  ?  515  ILE   A CG2 1 
ATOM   4049  C  CD1 . ILE   A 1 515  ? -32.43200  83.56500  22.21100  1.000 51.98989  ?  515  ILE   A CD1 1 
ATOM   4050  N  N   . LEU   A 1 516  ? -37.15500  84.23900  23.82100  1.000 42.79330  ?  516  LEU   A N   1 
ATOM   4051  C  CA  . LEU   A 1 516  ? -38.58000  84.45100  24.01500  1.000 40.28900  ?  516  LEU   A CA  1 
ATOM   4052  C  C   . LEU   A 1 516  ? -39.13800  85.32500  22.89900  1.000 38.83080  ?  516  LEU   A C   1 
ATOM   4053  O  O   . LEU   A 1 516  ? -38.40300  85.90000  22.09100  1.000 48.45106  ?  516  LEU   A O   1 
ATOM   4054  C  CB  . LEU   A 1 516  ? -38.85500  85.09200  25.38200  1.000 37.46936  ?  516  LEU   A CB  1 
ATOM   4055  C  CG  . LEU   A 1 516  ? -38.21200  84.40000  26.58900  1.000 34.73242  ?  516  LEU   A CG  1 
ATOM   4056  C  CD1 . LEU   A 1 516  ? -38.56200  85.11800  27.88800  1.000 31.58029  ?  516  LEU   A CD1 1 
ATOM   4057  C  CD2 . LEU   A 1 516  ? -38.60500  82.93000  26.66100  1.000 38.85738  ?  516  LEU   A CD2 1 
ATOM   4058  N  N   . ASP   A 1 517  ? -40.46000  85.42800  22.87000  1.000 38.06884  ?  517  ASP   A N   1 
ATOM   4059  C  CA  . ASP   A 1 517  ? -41.17400  86.17600  21.85000  1.000 52.60665  ?  517  ASP   A CA  1 
ATOM   4060  C  C   . ASP   A 1 517  ? -41.56600  87.54700  22.41200  1.000 59.61287  ?  517  ASP   A C   1 
ATOM   4061  O  O   . ASP   A 1 517  ? -41.06200  87.96800  23.45800  1.000 67.15764  ?  517  ASP   A O   1 
ATOM   4062  C  CB  . ASP   A 1 517  ? -42.37000  85.33900  21.37500  1.000 46.76887  ?  517  ASP   A CB  1 
ATOM   4063  C  CG  . ASP   A 1 517  ? -43.46200  85.23400  22.42200  1.000 64.10303  ?  517  ASP   A CG  1 
ATOM   4064  O  OD1 . ASP   A 1 517  ? -43.13900  85.26500  23.63300  1.000 68.26890  ?  517  ASP   A OD1 1 
ATOM   4065  O  OD2 . ASP   A 1 517  ? -44.64300  85.13500  22.03600  1.000 55.01951  -1 517  ASP   A OD2 1 
ATOM   4066  N  N   . GLU   A 1 518  ? -42.46800  88.25400  21.71900  1.000 56.72056  ?  518  GLU   A N   1 
ATOM   4067  C  CA  . GLU   A 1 518  ? -42.95900  89.54100  22.20000  1.000 45.67943  ?  518  GLU   A CA  1 
ATOM   4068  C  C   . GLU   A 1 518  ? -43.85500  89.41000  23.42700  1.000 46.04396  ?  518  GLU   A C   1 
ATOM   4069  O  O   . GLU   A 1 518  ? -44.03400  90.39700  24.15200  1.000 58.74425  ?  518  GLU   A O   1 
ATOM   4070  C  CB  . GLU   A 1 518  ? -43.72100  90.26700  21.09000  1.000 47.28753  ?  518  GLU   A CB  1 
ATOM   4071  C  CG  . GLU   A 1 518  ? -42.83500  91.11700  20.19900  1.000 72.08601  ?  518  GLU   A CG  1 
ATOM   4072  C  CD  . GLU   A 1 518  ? -43.58000  91.70300  19.01800  1.000 93.89456  ?  518  GLU   A CD  1 
ATOM   4073  O  OE1 . GLU   A 1 518  ? -44.80300  91.46900  18.90500  1.000 102.21541 ?  518  GLU   A OE1 1 
ATOM   4074  O  OE2 . GLU   A 1 518  ? -42.93900  92.39500  18.20100  1.000 85.77328  -1 518  GLU   A OE2 1 
ATOM   4075  N  N   . ALA   A 1 519  ? -44.42600  88.22900  23.67400  1.000 47.92098  ?  519  ALA   A N   1 
ATOM   4076  C  CA  . ALA   A 1 519  ? -45.24300  87.97900  24.85400  1.000 46.05724  ?  519  ALA   A CA  1 
ATOM   4077  C  C   . ALA   A 1 519  ? -44.47400  87.24000  25.94700  1.000 49.01622  ?  519  ALA   A C   1 
ATOM   4078  O  O   . ALA   A 1 519  ? -45.09100  86.68200  26.86100  1.000 54.31413  ?  519  ALA   A O   1 
ATOM   4079  C  CB  . ALA   A 1 519  ? -46.49800  87.19500  24.47500  1.000 56.24546  ?  519  ALA   A CB  1 
ATOM   4080  N  N   . LEU   A 1 520  ? -43.14000  87.22400  25.86600  1.000 44.84151  ?  520  LEU   A N   1 
ATOM   4081  C  CA  . LEU   A 1 520  ? -42.28000  86.58500  26.86700  1.000 39.62081  ?  520  LEU   A CA  1 
ATOM   4082  C  C   . LEU   A 1 520  ? -42.60600  85.10100  27.01500  1.000 38.50517  ?  520  LEU   A C   1 
ATOM   4083  O  O   . LEU   A 1 520  ? -42.62300  84.55600  28.12000  1.000 51.04065  ?  520  LEU   A O   1 
ATOM   4084  C  CB  . LEU   A 1 520  ? -42.37200  87.30000  28.21800  1.000 37.50441  ?  520  LEU   A CB  1 
ATOM   4085  C  CG  . LEU   A 1 520  ? -42.33200  88.82900  28.18800  1.000 50.83435  ?  520  LEU   A CG  1 
ATOM   4086  C  CD1 . LEU   A 1 520  ? -42.35800  89.39600  29.59900  1.000 39.10200  ?  520  LEU   A CD1 1 
ATOM   4087  C  CD2 . LEU   A 1 520  ? -41.12200  89.33800  27.42000  1.000 36.92132  ?  520  LEU   A CD2 1 
ATOM   4088  N  N   . ALA   A 1 521  ? -42.86900  84.44400  25.89100  1.000 34.03321  ?  521  ALA   A N   1 
ATOM   4089  C  CA  . ALA   A 1 521  ? -43.14600  83.01800  25.85500  1.000 46.19016  ?  521  ALA   A CA  1 
ATOM   4090  C  C   . ALA   A 1 521  ? -42.00000  82.28900  25.16800  1.000 52.52827  ?  521  ALA   A C   1 
ATOM   4091  O  O   . ALA   A 1 521  ? -41.33500  82.83400  24.28200  1.000 46.14320  ?  521  ALA   A O   1 
ATOM   4092  C  CB  . ALA   A 1 521  ? -44.46300  82.72600  25.13000  1.000 49.18811  ?  521  ALA   A CB  1 
ATOM   4093  N  N   . LEU   A 1 522  ? -41.78200  81.04400  25.58400  1.000 44.28607  ?  522  LEU   A N   1 
ATOM   4094  C  CA  . LEU   A 1 522  ? -40.65000  80.27400  25.09100  1.000 40.07252  ?  522  LEU   A CA  1 
ATOM   4095  C  C   . LEU   A 1 522  ? -40.78400  80.02600  23.59500  1.000 46.13147  ?  522  LEU   A C   1 
ATOM   4096  O  O   . LEU   A 1 522  ? -41.82900  79.57600  23.11900  1.000 61.73264  ?  522  LEU   A O   1 
ATOM   4097  C  CB  . LEU   A 1 522  ? -40.55300  78.95400  25.85300  1.000 49.93304  ?  522  LEU   A CB  1 
ATOM   4098  C  CG  . LEU   A 1 522  ? -39.17700  78.29600  25.96800  1.000 52.45172  ?  522  LEU   A CG  1 
ATOM   4099  C  CD1 . LEU   A 1 522  ? -38.09600  79.33500  26.21700  1.000 47.55736  ?  522  LEU   A CD1 1 
ATOM   4100  C  CD2 . LEU   A 1 522  ? -39.19000  77.27000  27.08800  1.000 60.56189  ?  522  LEU   A CD2 1 
ATOM   4101  N  N   . GLN   A 1 523  ? -39.72900  80.34900  22.85300  1.000 44.86043  ?  523  GLN   A N   1 
ATOM   4102  C  CA  . GLN   A 1 523  ? -39.72000  80.04700  21.42700  1.000 45.01418  ?  523  GLN   A CA  1 
ATOM   4103  C  C   . GLN   A 1 523  ? -39.06400  78.69200  21.18700  1.000 45.07787  ?  523  GLN   A C   1 
ATOM   4104  O  O   . GLN   A 1 523  ? -38.10700  78.33600  21.88300  1.000 43.88952  ?  523  GLN   A O   1 
ATOM   4105  C  CB  . GLN   A 1 523  ? -38.95900  81.11700  20.64900  1.000 41.03238  ?  523  GLN   A CB  1 
ATOM   4106  C  CG  . GLN   A 1 523  ? -39.64400  82.47100  20.58900  1.000 47.06762  ?  523  GLN   A CG  1 
ATOM   4107  C  CD  . GLN   A 1 523  ? -40.50200  82.64000  19.35000  1.000 49.52774  ?  523  GLN   A CD  1 
ATOM   4108  O  OE1 . GLN   A 1 523  ? -41.34400  81.79600  19.04200  1.000 53.10721  ?  523  GLN   A OE1 1 
ATOM   4109  N  NE2 . GLN   A 1 523  ? -40.28700  83.73400  18.62800  1.000 54.81345  ?  523  GLN   A NE2 1 
ATOM   4110  N  N   . PRO   A 1 524  ? -39.55400  77.91600  20.22200  1.000 49.89911  ?  524  PRO   A N   1 
ATOM   4111  C  CA  . PRO   A 1 524  ? -38.93000  76.62000  19.94000  1.000 45.49342  ?  524  PRO   A CA  1 
ATOM   4112  C  C   . PRO   A 1 524  ? -37.50700  76.79800  19.43200  1.000 59.52920  ?  524  PRO   A C   1 
ATOM   4113  O  O   . PRO   A 1 524  ? -37.14500  77.83700  18.87400  1.000 70.17405  ?  524  PRO   A O   1 
ATOM   4114  C  CB  . PRO   A 1 524  ? -39.83600  76.01400  18.86300  1.000 43.28359  ?  524  PRO   A CB  1 
ATOM   4115  C  CG  . PRO   A 1 524  ? -41.12500  76.76000  18.97000  1.000 42.21925  ?  524  PRO   A CG  1 
ATOM   4116  C  CD  . PRO   A 1 524  ? -40.76000  78.14400  19.40800  1.000 51.17967  ?  524  PRO   A CD  1 
ATOM   4117  N  N   . ILE   A 1 525  ? -36.69500  75.76100  19.64200  1.000 51.08585  ?  525  ILE   A N   1 
ATOM   4118  C  CA  . ILE   A 1 525  ? -35.30900  75.79400  19.19100  1.000 48.65174  ?  525  ILE   A CA  1 
ATOM   4119  C  C   . ILE   A 1 525  ? -35.27100  76.01100  17.68700  1.000 48.73691  ?  525  ILE   A C   1 
ATOM   4120  O  O   . ILE   A 1 525  ? -35.96700  75.32900  16.92100  1.000 48.48874  ?  525  ILE   A O   1 
ATOM   4121  C  CB  . ILE   A 1 525  ? -34.58100  74.50500  19.60100  1.000 44.49832  ?  525  ILE   A CB  1 
ATOM   4122  C  CG1 . ILE   A 1 525  ? -33.97900  74.66300  20.99600  1.000 52.49199  ?  525  ILE   A CG1 1 
ATOM   4123  C  CG2 . ILE   A 1 525  ? -33.49500  74.15500  18.60200  1.000 46.85269  ?  525  ILE   A CG2 1 
ATOM   4124  C  CD1 . ILE   A 1 525  ? -33.23600  73.44000  21.47700  1.000 54.28405  ?  525  ILE   A CD1 1 
ATOM   4125  N  N   . GLY   A 1 526  ? -34.46100  76.98000  17.25700  1.000 46.25974  ?  526  GLY   A N   1 
ATOM   4126  C  CA  . GLY   A 1 526  ? -34.35600  77.36800  15.87300  1.000 55.12604  ?  526  GLY   A CA  1 
ATOM   4127  C  C   . GLY   A 1 526  ? -35.16700  78.59900  15.52500  1.000 45.56907  ?  526  GLY   A C   1 
ATOM   4128  O  O   . GLY   A 1 526  ? -34.76500  79.36900  14.64600  1.000 49.85494  ?  526  GLY   A O   1 
ATOM   4129  N  N   . VAL   A 1 527  ? -36.29900  78.79800  16.19200  1.000 40.54455  ?  527  VAL   A N   1 
ATOM   4130  C  CA  . VAL   A 1 527  ? -37.08600  80.00900  16.00800  1.000 44.67318  ?  527  VAL   A CA  1 
ATOM   4131  C  C   . VAL   A 1 527  ? -36.42500  81.14500  16.77000  1.000 40.84310  ?  527  VAL   A C   1 
ATOM   4132  O  O   . VAL   A 1 527  ? -36.00600  80.98200  17.92300  1.000 46.68044  ?  527  VAL   A O   1 
ATOM   4133  C  CB  . VAL   A 1 527  ? -38.53500  79.79000  16.47100  1.000 37.45996  ?  527  VAL   A CB  1 
ATOM   4134  C  CG1 . VAL   A 1 527  ? -39.42100  80.92500  15.97800  1.000 41.29284  ?  527  VAL   A CG1 1 
ATOM   4135  C  CG2 . VAL   A 1 527  ? -39.04500  78.44900  15.98000  1.000 41.50133  ?  527  VAL   A CG2 1 
ATOM   4136  N  N   . ALA   A 1 528  ? -36.32800  82.30300  16.12900  1.000 30.48769  ?  528  ALA   A N   1 
ATOM   4137  C  CA  . ALA   A 1 528  ? -35.61700  83.42200  16.72000  1.000 40.09083  ?  528  ALA   A CA  1 
ATOM   4138  C  C   . ALA   A 1 528  ? -36.51300  84.19200  17.68400  1.000 49.44472  ?  528  ALA   A C   1 
ATOM   4139  O  O   . ALA   A 1 528  ? -37.72400  83.97400  17.77500  1.000 47.28589  ?  528  ALA   A O   1 
ATOM   4140  C  CB  . ALA   A 1 528  ? -35.08600  84.35600  15.63500  1.000 34.83132  ?  528  ALA   A CB  1 
ATOM   4141  N  N   . GLY   A 1 529  ? -35.88900  85.11400  18.40400  1.000 44.29206  ?  529  GLY   A N   1 
ATOM   4142  C  CA  . GLY   A 1 529  ? -36.60600  85.91300  19.37400  1.000 48.75214  ?  529  GLY   A CA  1 
ATOM   4143  C  C   . GLY   A 1 529  ? -35.64400  86.79600  20.13000  1.000 45.05922  ?  529  GLY   A C   1 
ATOM   4144  O  O   . GLY   A 1 529  ? -34.49000  86.96600  19.73100  1.000 56.72664  ?  529  GLY   A O   1 
ATOM   4145  N  N   . GLU   A 1 530  ? -36.12800  87.35000  21.23700  1.000 52.84855  ?  530  GLU   A N   1 
ATOM   4146  C  CA  . GLU   A 1 530  ? -35.32900  88.24400  22.05900  1.000 42.29332  ?  530  GLU   A CA  1 
ATOM   4147  C  C   . GLU   A 1 530  ? -34.50400  87.44100  23.05200  1.000 50.57327  ?  530  GLU   A C   1 
ATOM   4148  O  O   . GLU   A 1 530  ? -35.02600  86.55100  23.73200  1.000 45.16077  ?  530  GLU   A O   1 
ATOM   4149  C  CB  . GLU   A 1 530  ? -36.21700  89.24000  22.79800  1.000 42.28820  ?  530  GLU   A CB  1 
ATOM   4150  C  CG  . GLU   A 1 530  ? -35.44700  90.41300  23.36400  1.000 49.47649  ?  530  GLU   A CG  1 
ATOM   4151  C  CD  . GLU   A 1 530  ? -36.26900  91.67800  23.39100  1.000 63.87994  ?  530  GLU   A CD  1 
ATOM   4152  O  OE1 . GLU   A 1 530  ? -37.51100  91.58000  23.30900  1.000 91.08376  ?  530  GLU   A OE1 1 
ATOM   4153  O  OE2 . GLU   A 1 530  ? -35.67500  92.77200  23.49700  1.000 56.55429  -1 530  GLU   A OE2 1 
ATOM   4154  N  N   . LEU   A 1 531  ? -33.21400  87.75800  23.12900  1.000 42.56686  ?  531  LEU   A N   1 
ATOM   4155  C  CA  . LEU   A 1 531  ? -32.35500  87.13400  24.12300  1.000 43.23743  ?  531  LEU   A CA  1 
ATOM   4156  C  C   . LEU   A 1 531  ? -32.66200  87.71600  25.49600  1.000 35.78345  ?  531  LEU   A C   1 
ATOM   4157  O  O   . LEU   A 1 531  ? -32.64000  88.93700  25.68400  1.000 41.36551  ?  531  LEU   A O   1 
ATOM   4158  C  CB  . LEU   A 1 531  ? -30.88600  87.34600  23.75700  1.000 37.55769  ?  531  LEU   A CB  1 
ATOM   4159  C  CG  . LEU   A 1 531  ? -29.86600  86.35700  24.32900  1.000 28.49947  ?  531  LEU   A CG  1 
ATOM   4160  C  CD1 . LEU   A 1 531  ? -28.64800  86.27400  23.42700  1.000 37.48361  ?  531  LEU   A CD1 1 
ATOM   4161  C  CD2 . LEU   A 1 531  ? -29.44900  86.74300  25.73600  1.000 32.17692  ?  531  LEU   A CD2 1 
ATOM   4162  N  N   . PHE   A 1 532  ? -32.97000  86.83800  26.44700  1.000 36.19678  ?  532  PHE   A N   1 
ATOM   4163  C  CA  . PHE   A 1 532  ? -33.22000  87.21400  27.83000  1.000 40.34324  ?  532  PHE   A CA  1 
ATOM   4164  C  C   . PHE   A 1 532  ? -32.19600  86.52800  28.72000  1.000 44.73148  ?  532  PHE   A C   1 
ATOM   4165  O  O   . PHE   A 1 532  ? -32.04300  85.30200  28.66600  1.000 50.68470  ?  532  PHE   A O   1 
ATOM   4166  C  CB  . PHE   A 1 532  ? -34.63900  86.83300  28.26200  1.000 39.11549  ?  532  PHE   A CB  1 
ATOM   4167  C  CG  . PHE   A 1 532  ? -35.69900  87.78100  27.78000  1.000 43.15831  ?  532  PHE   A CG  1 
ATOM   4168  C  CD1 . PHE   A 1 532  ? -36.05500  88.88300  28.54000  1.000 47.55638  ?  532  PHE   A CD1 1 
ATOM   4169  C  CD2 . PHE   A 1 532  ? -36.33900  87.57200  26.57000  1.000 41.00337  ?  532  PHE   A CD2 1 
ATOM   4170  C  CE1 . PHE   A 1 532  ? -37.02900  89.75800  28.10200  1.000 36.17848  ?  532  PHE   A CE1 1 
ATOM   4171  C  CE2 . PHE   A 1 532  ? -37.31600  88.44400  26.12800  1.000 45.17203  ?  532  PHE   A CE2 1 
ATOM   4172  C  CZ  . PHE   A 1 532  ? -37.66000  89.53700  26.89400  1.000 45.06942  ?  532  PHE   A CZ  1 
ATOM   4173  N  N   . ILE   A 1 533  ? -31.50000  87.31800  29.53400  1.000 42.26469  ?  533  ILE   A N   1 
ATOM   4174  C  CA  . ILE   A 1 533  ? -30.43200  86.82300  30.39300  1.000 42.30411  ?  533  ILE   A CA  1 
ATOM   4175  C  C   . ILE   A 1 533  ? -30.96900  86.65700  31.80600  1.000 43.88953  ?  533  ILE   A C   1 
ATOM   4176  O  O   . ILE   A 1 533  ? -31.60700  87.56900  32.35000  1.000 44.18450  ?  533  ILE   A O   1 
ATOM   4177  C  CB  . ILE   A 1 533  ? -29.22000  87.76700  30.37700  1.000 36.56098  ?  533  ILE   A CB  1 
ATOM   4178  C  CG1 . ILE   A 1 533  ? -28.87100  88.15400  28.94300  1.000 26.23869  ?  533  ILE   A CG1 1 
ATOM   4179  C  CG2 . ILE   A 1 533  ? -28.02800  87.09300  31.02500  1.000 33.93463  ?  533  ILE   A CG2 1 
ATOM   4180  C  CD1 . ILE   A 1 533  ? -27.58200  88.92700  28.81800  1.000 29.39633  ?  533  ILE   A CD1 1 
ATOM   4181  N  N   . VAL   A 1 534  ? -30.71500  85.49200  32.39500  1.000 36.81777  ?  534  VAL   A N   1 
ATOM   4182  C  CA  . VAL   A 1 534  ? -31.08600  85.18900  33.77100  1.000 29.01431  ?  534  VAL   A CA  1 
ATOM   4183  C  C   . VAL   A 1 534  ? -29.86600  84.59700  34.45800  1.000 44.76716  ?  534  VAL   A C   1 
ATOM   4184  O  O   . VAL   A 1 534  ? -29.26400  83.64900  33.94300  1.000 53.96768  ?  534  VAL   A O   1 
ATOM   4185  C  CB  . VAL   A 1 534  ? -32.26900  84.20500  33.84600  1.000 44.66220  ?  534  VAL   A CB  1 
ATOM   4186  C  CG1 . VAL   A 1 534  ? -32.73600  84.05600  35.28300  1.000 53.15239  ?  534  VAL   A CG1 1 
ATOM   4187  C  CG2 . VAL   A 1 534  ? -33.40800  84.65400  32.94800  1.000 43.12330  ?  534  VAL   A CG2 1 
ATOM   4188  N  N   . GLY   A 1 535  ? -29.50100  85.14700  35.60500  1.000 47.68513  ?  535  GLY   A N   1 
ATOM   4189  C  CA  . GLY   A 1 535  ? -28.40600  84.60100  36.37700  1.000 38.97798  ?  535  GLY   A CA  1 
ATOM   4190  C  C   . GLY   A 1 535  ? -27.73200  85.66500  37.22000  1.000 47.39228  ?  535  GLY   A C   1 
ATOM   4191  O  O   . GLY   A 1 535  ? -28.23600  86.77400  37.38100  1.000 37.64430  ?  535  GLY   A O   1 
ATOM   4192  N  N   . GLU   A 1 536  ? -26.56700  85.29000  37.75600  1.000 56.43090  ?  536  GLU   A N   1 
ATOM   4193  C  CA  . GLU   A 1 536  ? -25.77600  86.11500  38.66100  1.000 48.77952  ?  536  GLU   A CA  1 
ATOM   4194  C  C   . GLU   A 1 536  ? -24.93500  87.16500  37.92600  1.000 45.38524  ?  536  GLU   A C   1 
ATOM   4195  O  O   . GLU   A 1 536  ? -23.94700  87.66300  38.48000  1.000 54.54597  ?  536  GLU   A O   1 
ATOM   4196  C  CB  . GLU   A 1 536  ? -24.88200  85.21800  39.52700  1.000 39.33225  ?  536  GLU   A CB  1 
ATOM   4197  C  CG  . GLU   A 1 536  ? -24.34700  85.85500  40.81000  1.000 47.78175  ?  536  GLU   A CG  1 
ATOM   4198  C  CD  . GLU   A 1 536  ? -25.14900  85.48500  42.04000  1.000 60.24584  ?  536  GLU   A CD  1 
ATOM   4199  O  OE1 . GLU   A 1 536  ? -25.71300  84.37300  42.06900  1.000 64.93527  ?  536  GLU   A OE1 1 
ATOM   4200  O  OE2 . GLU   A 1 536  ? -25.21100  86.30400  42.98100  1.000 65.53188  -1 536  GLU   A OE2 1 
ATOM   4201  N  N   . GLY   A 1 537  ? -25.29200  87.51800  36.69500  1.000 31.94424  ?  537  GLY   A N   1 
ATOM   4202  C  CA  . GLY   A 1 537  ? -24.61900  88.60600  36.01100  1.000 32.11964  ?  537  GLY   A CA  1 
ATOM   4203  C  C   . GLY   A 1 537  ? -25.44800  89.87300  36.03000  1.000 43.56263  ?  537  GLY   A C   1 
ATOM   4204  O  O   . GLY   A 1 537  ? -24.92600  90.97800  35.85300  1.000 54.20755  ?  537  GLY   A O   1 
ATOM   4205  N  N   . LEU   A 1 538  ? -26.75000  89.71800  36.26100  1.000 48.14134  ?  538  LEU   A N   1 
ATOM   4206  C  CA  . LEU   A 1 538  ? -27.67500  90.84600  36.26900  1.000 44.00378  ?  538  LEU   A CA  1 
ATOM   4207  C  C   . LEU   A 1 538  ? -27.36000  91.76700  37.44100  1.000 36.59598  ?  538  LEU   A C   1 
ATOM   4208  O  O   . LEU   A 1 538  ? -27.54200  91.39400  38.60500  1.000 36.99988  ?  538  LEU   A O   1 
ATOM   4209  C  CB  . LEU   A 1 538  ? -29.11700  90.35100  36.33700  1.000 51.44141  ?  538  LEU   A CB  1 
ATOM   4210  C  CG  . LEU   A 1 538  ? -29.73000  89.80900  35.04100  1.000 51.88263  ?  538  LEU   A CG  1 
ATOM   4211  C  CD1 . LEU   A 1 538  ? -29.42200  88.33100  34.84500  1.000 50.27895  ?  538  LEU   A CD1 1 
ATOM   4212  C  CD2 . LEU   A 1 538  ? -31.22900  90.05400  35.00700  1.000 45.42981  ?  538  LEU   A CD2 1 
ATOM   4213  N  N   . GLY   A 1 539  ? -26.89400  92.97500  37.13300  1.000 35.89992  ?  539  GLY   A N   1 
ATOM   4214  C  CA  . GLY   A 1 539  ? -26.61900  93.96900  38.14600  1.000 55.89225  ?  539  GLY   A CA  1 
ATOM   4215  C  C   . GLY   A 1 539  ? -27.88500  94.61200  38.67900  1.000 47.05282  ?  539  GLY   A C   1 
ATOM   4216  O  O   . GLY   A 1 539  ? -29.00700  94.23100  38.34700  1.000 51.20089  ?  539  GLY   A O   1 
ATOM   4217  N  N   . ARG   A 1 540  ? -27.68500  95.61800  39.53300  1.000 44.43214  ?  540  ARG   A N   1 
ATOM   4218  C  CA  . ARG   A 1 540  ? -28.81800  96.31300  40.13900  1.000 58.38792  ?  540  ARG   A CA  1 
ATOM   4219  C  C   . ARG   A 1 540  ? -29.62000  97.08600  39.09900  1.000 41.43470  ?  540  ARG   A C   1 
ATOM   4220  O  O   . ARG   A 1 540  ? -30.85300  97.13200  39.16900  1.000 54.89268  ?  540  ARG   A O   1 
ATOM   4221  C  CB  . ARG   A 1 540  ? -28.33700  97.25600  41.24300  1.000 46.85764  ?  540  ARG   A CB  1 
ATOM   4222  C  CG  . ARG   A 1 540  ? -28.29500  96.63500  42.62900  1.000 59.80391  ?  540  ARG   A CG  1 
ATOM   4223  C  CD  . ARG   A 1 540  ? -27.92700  97.67600  43.67500  1.000 51.46087  ?  540  ARG   A CD  1 
ATOM   4224  N  NE  . ARG   A 1 540  ? -27.25300  97.08400  44.82400  1.000 57.53668  ?  540  ARG   A NE  1 
ATOM   4225  C  CZ  . ARG   A 1 540  ? -26.77000  97.77400  45.84900  1.000 56.33064  ?  540  ARG   A CZ  1 
ATOM   4226  N  NH1 . ARG   A 1 540  ? -26.88300  99.09100  45.91100  1.000 54.03287  ?  540  ARG   A NH1 1 
ATOM   4227  N  NH2 . ARG   A 1 540  ? -26.15400  97.12700  46.83400  1.000 52.00222  ?  540  ARG   A NH2 1 
ATOM   4228  N  N   . GLY   A 1 541  ? -28.94300  97.70100  38.13200  1.000 33.31253  ?  541  GLY   A N   1 
ATOM   4229  C  CA  . GLY   A 1 541  ? -29.63100  98.45300  37.10100  1.000 31.53193  ?  541  GLY   A CA  1 
ATOM   4230  C  C   . GLY   A 1 541  ? -28.93800  99.74600  36.72600  1.000 46.25170  ?  541  GLY   A C   1 
ATOM   4231  O  O   . GLY   A 1 541  ? -27.71000  99.84800  36.80700  1.000 64.61950  ?  541  GLY   A O   1 
ATOM   4232  N  N   . TYR   A 1 542  ? -29.71300  100.74200 36.31000  1.000 41.18669  ?  542  TYR   A N   1 
ATOM   4233  C  CA  . TYR   A 1 542  ? -29.18000  102.03600 35.91600  1.000 39.20518  ?  542  TYR   A CA  1 
ATOM   4234  C  C   . TYR   A 1 542  ? -29.24500  103.01000 37.08600  1.000 51.35911  ?  542  TYR   A C   1 
ATOM   4235  O  O   . TYR   A 1 542  ? -30.11400  102.91000 37.95500  1.000 64.01728  ?  542  TYR   A O   1 
ATOM   4236  C  CB  . TYR   A 1 542  ? -29.94500  102.59700 34.71500  1.000 50.27619  ?  542  TYR   A CB  1 
ATOM   4237  C  CG  . TYR   A 1 542  ? -29.94300  101.67800 33.51200  1.000 56.99212  ?  542  TYR   A CG  1 
ATOM   4238  C  CD1 . TYR   A 1 542  ? -28.88700  101.68400 32.60900  1.000 48.11590  ?  542  TYR   A CD1 1 
ATOM   4239  C  CD2 . TYR   A 1 542  ? -30.99700  100.80300 33.28000  1.000 46.11533  ?  542  TYR   A CD2 1 
ATOM   4240  C  CE1 . TYR   A 1 542  ? -28.88100  100.84500 31.50900  1.000 47.89967  ?  542  TYR   A CE1 1 
ATOM   4241  C  CE2 . TYR   A 1 542  ? -31.00000  99.96100  32.18200  1.000 44.31468  ?  542  TYR   A CE2 1 
ATOM   4242  C  CZ  . TYR   A 1 542  ? -29.94000  99.98600  31.30100  1.000 50.60603  ?  542  TYR   A CZ  1 
ATOM   4243  O  OH  . TYR   A 1 542  ? -29.93900  99.14900  30.20900  1.000 53.44744  ?  542  TYR   A OH  1 
ATOM   4244  N  N   . LEU   A 1 543  ? -28.30900  103.95600 37.09900  1.000 58.69122  ?  543  LEU   A N   1 
ATOM   4245  C  CA  . LEU   A 1 543  ? -28.16400  104.89000 38.20800  1.000 61.44062  ?  543  LEU   A CA  1 
ATOM   4246  C  C   . LEU   A 1 543  ? -29.09100  106.08500 38.01900  1.000 60.60291  ?  543  LEU   A C   1 
ATOM   4247  O  O   . LEU   A 1 543  ? -29.07400  106.73000 36.96500  1.000 62.62895  ?  543  LEU   A O   1 
ATOM   4248  C  CB  . LEU   A 1 543  ? -26.71500  105.36100 38.32200  1.000 63.16165  ?  543  LEU   A CB  1 
ATOM   4249  C  CG  . LEU   A 1 543  ? -26.37300  106.22300 39.53700  1.000 45.17935  ?  543  LEU   A CG  1 
ATOM   4250  C  CD1 . LEU   A 1 543  ? -26.47000  105.40600 40.81600  1.000 31.22246  ?  543  LEU   A CD1 1 
ATOM   4251  C  CD2 . LEU   A 1 543  ? -24.98900  106.83000 39.38200  1.000 50.75073  ?  543  LEU   A CD2 1 
ATOM   4252  N  N   . ASN   A 1 544  ? -29.89300  106.37400 39.04800  1.000 68.76005  ?  544  ASN   A N   1 
ATOM   4253  C  CA  . ASN   A 1 544  ? -30.82400  107.50500 39.05100  1.000 80.27153  ?  544  ASN   A CA  1 
ATOM   4254  C  C   . ASN   A 1 544  ? -31.81700  107.43200 37.89500  1.000 72.48740  ?  544  ASN   A C   1 
ATOM   4255  O  O   . ASN   A 1 544  ? -32.29900  108.45900 37.41000  1.000 74.90483  ?  544  ASN   A O   1 
ATOM   4256  C  CB  . ASN   A 1 544  ? -30.07800  108.84400 39.02800  1.000 70.77708  ?  544  ASN   A CB  1 
ATOM   4257  C  CG  . ASN   A 1 544  ? -29.30200  109.10400 40.30400  1.000 63.26761  ?  544  ASN   A CG  1 
ATOM   4258  O  OD1 . ASN   A 1 544  ? -29.72500  108.71400 41.39300  1.000 52.55383  ?  544  ASN   A OD1 1 
ATOM   4259  N  ND2 . ASN   A 1 544  ? -28.15900  109.76900 40.17700  1.000 64.28379  ?  544  ASN   A ND2 1 
ATOM   4260  N  N   . ARG   A 1 545  ? -32.13400  106.21900 37.44700  1.000 61.34179  ?  545  ARG   A N   1 
ATOM   4261  C  CA  . ARG   A 1 545  ? -33.04200  106.00000 36.32100  1.000 57.18884  ?  545  ARG   A CA  1 
ATOM   4262  C  C   . ARG   A 1 545  ? -33.85600  104.74500 36.58800  1.000 68.89686  ?  545  ARG   A C   1 
ATOM   4263  O  O   . ARG   A 1 545  ? -33.60500  103.68200 36.00600  1.000 59.37700  ?  545  ARG   A O   1 
ATOM   4264  C  CB  . ARG   A 1 545  ? -32.26800  105.88900 35.00500  1.000 41.34455  ?  545  ARG   A CB  1 
ATOM   4265  C  CG  . ARG   A 1 545  ? -31.73200  107.21000 34.47900  1.000 45.26614  ?  545  ARG   A CG  1 
ATOM   4266  C  CD  . ARG   A 1 545  ? -30.55200  106.98500 33.55200  1.000 55.09504  ?  545  ARG   A CD  1 
ATOM   4267  N  NE  . ARG   A 1 545  ? -30.30400  108.12900 32.68300  1.000 79.09403  ?  545  ARG   A NE  1 
ATOM   4268  C  CZ  . ARG   A 1 545  ? -30.76800  108.23800 31.44600  1.000 83.63656  ?  545  ARG   A CZ  1 
ATOM   4269  N  NH1 . ARG   A 1 545  ? -31.52000  107.29400 30.90400  1.000 68.70132  ?  545  ARG   A NH1 1 
ATOM   4270  N  NH2 . ARG   A 1 545  ? -30.46700  109.32000 30.73300  1.000 69.94536  ?  545  ARG   A NH2 1 
ATOM   4271  N  N   . PRO   A 1 546  ? -34.85500  104.83100 37.47300  1.000 71.79226  ?  546  PRO   A N   1 
ATOM   4272  C  CA  . PRO   A 1 546  ? -35.64500  103.63500 37.80100  1.000 64.86989  ?  546  PRO   A CA  1 
ATOM   4273  C  C   . PRO   A 1 546  ? -36.64600  103.24300 36.73000  1.000 60.23064  ?  546  PRO   A C   1 
ATOM   4274  O  O   . PRO   A 1 546  ? -37.02800  102.06600 36.67300  1.000 44.82607  ?  546  PRO   A O   1 
ATOM   4275  C  CB  . PRO   A 1 546  ? -36.36000  104.03700 39.09700  1.000 59.51224  ?  546  PRO   A CB  1 
ATOM   4276  C  CG  . PRO   A 1 546  ? -36.52200  105.51700 38.96900  1.000 57.04041  ?  546  PRO   A CG  1 
ATOM   4277  C  CD  . PRO   A 1 546  ? -35.30400  106.01500 38.22700  1.000 57.52023  ?  546  PRO   A CD  1 
ATOM   4278  N  N   . GLU   A 1 547  ? -37.08400  104.18000 35.88700  1.000 59.86659  ?  547  GLU   A N   1 
ATOM   4279  C  CA  . GLU   A 1 547  ? -38.05400  103.84600 34.84900  1.000 61.33244  ?  547  GLU   A CA  1 
ATOM   4280  C  C   . GLU   A 1 547  ? -37.44600  102.90700 33.81600  1.000 61.68987  ?  547  GLU   A C   1 
ATOM   4281  O  O   . GLU   A 1 547  ? -38.05100  101.89100 33.45200  1.000 59.68478  ?  547  GLU   A O   1 
ATOM   4282  C  CB  . GLU   A 1 547  ? -38.57300  105.12000 34.18100  1.000 45.59271  ?  547  GLU   A CB  1 
ATOM   4283  N  N   . LEU   A 1 548  ? -36.24400  103.23000 33.33500  1.000 62.89517  ?  548  LEU   A N   1 
ATOM   4284  C  CA  . LEU   A 1 548  ? -35.59400  102.37300 32.35000  1.000 56.69683  ?  548  LEU   A CA  1 
ATOM   4285  C  C   . LEU   A 1 548  ? -35.19000  101.03600 32.95900  1.000 52.75154  ?  548  LEU   A C   1 
ATOM   4286  O  O   . LEU   A 1 548  ? -35.25500  99.99800  32.29000  1.000 46.88045  ?  548  LEU   A O   1 
ATOM   4287  C  CB  . LEU   A 1 548  ? -34.37600  103.08100 31.75900  1.000 34.35004  ?  548  LEU   A CB  1 
ATOM   4288  C  CG  . LEU   A 1 548  ? -33.60200  102.25500 30.73100  1.000 60.42583  ?  548  LEU   A CG  1 
ATOM   4289  C  CD1 . LEU   A 1 548  ? -34.45100  102.00800 29.49000  1.000 75.49753  ?  548  LEU   A CD1 1 
ATOM   4290  C  CD2 . LEU   A 1 548  ? -32.28600  102.92100 30.37300  1.000 71.77739  ?  548  LEU   A CD2 1 
ATOM   4291  N  N   . THR   A 1 549  ? -34.77000  101.04100 34.22800  1.000 37.73315  ?  549  THR   A N   1 
ATOM   4292  C  CA  . THR   A 1 549  ? -34.39400  99.79300  34.88500  1.000 37.05090  ?  549  THR   A CA  1 
ATOM   4293  C  C   . THR   A 1 549  ? -35.57800  98.83900  34.96600  1.000 48.73412  ?  549  THR   A C   1 
ATOM   4294  O  O   . THR   A 1 549  ? -35.41900  97.62400  34.80000  1.000 47.10665  ?  549  THR   A O   1 
ATOM   4295  C  CB  . THR   A 1 549  ? -33.83400  100.08000 36.27800  1.000 38.51462  ?  549  THR   A CB  1 
ATOM   4296  O  OG1 . THR   A 1 549  ? -32.74400  101.00500 36.17300  1.000 54.61981  ?  549  THR   A OG1 1 
ATOM   4297  C  CG2 . THR   A 1 549  ? -33.33700  98.79800  36.92800  1.000 23.83578  ?  549  THR   A CG2 1 
ATOM   4298  N  N   . ALA   A 1 550  ? -36.77800  99.37200  35.21000  1.000 54.37741  ?  550  ALA   A N   1 
ATOM   4299  C  CA  . ALA   A 1 550  ? -37.97800  98.54700  35.16700  1.000 43.43219  ?  550  ALA   A CA  1 
ATOM   4300  C  C   . ALA   A 1 550  ? -38.29300  98.06300  33.75800  1.000 44.16160  ?  550  ALA   A C   1 
ATOM   4301  O  O   . ALA   A 1 550  ? -38.95000  97.02800  33.60300  1.000 41.02166  ?  550  ALA   A O   1 
ATOM   4302  C  CB  . ALA   A 1 550  ? -39.16900  99.32200  35.73100  1.000 59.65954  ?  550  ALA   A CB  1 
ATOM   4303  N  N   . GLU   A 1 551  ? -37.83900  98.78700  32.73000  1.000 40.47768  ?  551  GLU   A N   1 
ATOM   4304  C  CA  . GLU   A 1 551  ? -38.11500  98.40100  31.35100  1.000 39.97188  ?  551  GLU   A CA  1 
ATOM   4305  C  C   . GLU   A 1 551  ? -37.20500  97.26800  30.88800  1.000 57.97623  ?  551  GLU   A C   1 
ATOM   4306  O  O   . GLU   A 1 551  ? -37.67000  96.32200  30.24400  1.000 72.04414  ?  551  GLU   A O   1 
ATOM   4307  C  CB  . GLU   A 1 551  ? -37.97000  99.61900  30.43600  1.000 47.46885  ?  551  GLU   A CB  1 
ATOM   4308  C  CG  . GLU   A 1 551  ? -38.29400  99.35700  28.97100  1.000 68.03646  ?  551  GLU   A CG  1 
ATOM   4309  C  CD  . GLU   A 1 551  ? -38.25100  100.62200 28.13200  1.000 77.87393  ?  551  GLU   A CD  1 
ATOM   4310  O  OE1 . GLU   A 1 551  ? -38.18300  101.72600 28.71400  1.000 69.93955  ?  551  GLU   A OE1 1 
ATOM   4311  O  OE2 . GLU   A 1 551  ? -38.28400  100.51000 26.88800  1.000 81.53892  -1 551  GLU   A OE2 1 
ATOM   4312  N  N   . LYS   A 1 552  ? -35.91100  97.34600  31.20100  1.000 54.15141  ?  552  LYS   A N   1 
ATOM   4313  C  CA  . LYS   A 1 552  ? -34.95500  96.33500  30.76300  1.000 39.08036  ?  552  LYS   A CA  1 
ATOM   4314  C  C   . LYS   A 1 552  ? -34.82800  95.18400  31.75500  1.000 45.50369  ?  552  LYS   A C   1 
ATOM   4315  O  O   . LYS   A 1 552  ? -34.80400  94.01800  31.34700  1.000 50.23554  ?  552  LYS   A O   1 
ATOM   4316  C  CB  . LYS   A 1 552  ? -33.58600  96.97800  30.52500  1.000 42.21792  ?  552  LYS   A CB  1 
ATOM   4317  C  CG  . LYS   A 1 552  ? -33.57700  98.02800  29.42000  1.000 48.30280  ?  552  LYS   A CG  1 
ATOM   4318  C  CD  . LYS   A 1 552  ? -33.64800  97.39400  28.03500  1.000 62.66049  ?  552  LYS   A CD  1 
ATOM   4319  C  CE  . LYS   A 1 552  ? -32.31500  97.50600  27.30400  1.000 67.93810  ?  552  LYS   A CE  1 
ATOM   4320  N  NZ  . LYS   A 1 552  ? -32.32100  96.79200  25.99300  1.000 43.68777  ?  552  LYS   A NZ  1 
ATOM   4321  N  N   . PHE   A 1 553  ? -34.73900  95.48500  33.04900  1.000 40.69768  ?  553  PHE   A N   1 
ATOM   4322  C  CA  . PHE   A 1 553  ? -34.71100  94.45600  34.08700  1.000 42.39995  ?  553  PHE   A CA  1 
ATOM   4323  C  C   . PHE   A 1 553  ? -36.15000  94.16000  34.48800  1.000 57.44427  ?  553  PHE   A C   1 
ATOM   4324  O  O   . PHE   A 1 553  ? -36.75600  94.89900  35.26700  1.000 59.06937  ?  553  PHE   A O   1 
ATOM   4325  C  CB  . PHE   A 1 553  ? -33.88100  94.90600  35.28500  1.000 48.28377  ?  553  PHE   A CB  1 
ATOM   4326  C  CG  . PHE   A 1 553  ? -32.41300  95.03100  34.99500  1.000 41.28248  ?  553  PHE   A CG  1 
ATOM   4327  C  CD1 . PHE   A 1 553  ? -31.89100  96.20700  34.48500  1.000 33.81071  ?  553  PHE   A CD1 1 
ATOM   4328  C  CD2 . PHE   A 1 553  ? -31.55500  93.97200  35.24100  1.000 40.65979  ?  553  PHE   A CD2 1 
ATOM   4329  C  CE1 . PHE   A 1 553  ? -30.54200  96.32400  34.21900  1.000 30.57835  ?  553  PHE   A CE1 1 
ATOM   4330  C  CE2 . PHE   A 1 553  ? -30.20400  94.08300  34.97800  1.000 31.70579  ?  553  PHE   A CE2 1 
ATOM   4331  C  CZ  . PHE   A 1 553  ? -29.69700  95.26000  34.46600  1.000 36.11634  ?  553  PHE   A CZ  1 
ATOM   4332  N  N   . ILE   A 1 554  ? -36.70000  93.07600  33.95200  1.000 59.85972  ?  554  ILE   A N   1 
ATOM   4333  C  CA  . ILE   A 1 554  ? -38.08300  92.70000  34.20300  1.000 46.16090  ?  554  ILE   A CA  1 
ATOM   4334  C  C   . ILE   A 1 554  ? -38.11300  91.39000  34.97700  1.000 51.02711  ?  554  ILE   A C   1 
ATOM   4335  O  O   . ILE   A 1 554  ? -37.18100  90.58100  34.93000  1.000 55.31295  ?  554  ILE   A O   1 
ATOM   4336  C  CB  . ILE   A 1 554  ? -38.89200  92.57000  32.89700  1.000 36.66860  ?  554  ILE   A CB  1 
ATOM   4337  C  CG1 . ILE   A 1 554  ? -38.36400  91.39900  32.06700  1.000 40.68381  ?  554  ILE   A CG1 1 
ATOM   4338  C  CG2 . ILE   A 1 554  ? -38.82400  93.85800  32.09600  1.000 41.51608  ?  554  ILE   A CG2 1 
ATOM   4339  C  CD1 . ILE   A 1 554  ? -39.44400  90.58100  31.41100  1.000 33.05011  ?  554  ILE   A CD1 1 
ATOM   4340  N  N   . VAL   A 1 555  ? -39.20700  91.18600  35.70200  1.000 57.17056  ?  555  VAL   A N   1 
ATOM   4341  C  CA  . VAL   A 1 555  ? -39.51600  89.89800  36.30700  1.000 64.97317  ?  555  VAL   A CA  1 
ATOM   4342  C  C   . VAL   A 1 555  ? -40.49600  89.18600  35.38700  1.000 56.31214  ?  555  VAL   A C   1 
ATOM   4343  O  O   . VAL   A 1 555  ? -41.33400  89.82600  34.73800  1.000 60.31327  ?  555  VAL   A O   1 
ATOM   4344  C  CB  . VAL   A 1 555  ? -40.08000  90.05800  37.73500  1.000 62.34249  ?  555  VAL   A CB  1 
ATOM   4345  C  CG1 . VAL   A 1 555  ? -41.55800  90.43500  37.71300  1.000 64.43409  ?  555  VAL   A CG1 1 
ATOM   4346  C  CG2 . VAL   A 1 555  ? -39.84800  88.79000  38.54700  1.000 71.19563  ?  555  VAL   A CG2 1 
ATOM   4347  N  N   . HIS   A 1 556  ? -40.37300  87.87500  35.29400  1.000 58.51674  ?  556  HIS   A N   1 
ATOM   4348  C  CA  . HIS   A 1 556  ? -41.19700  87.16400  34.32700  1.000 61.76935  ?  556  HIS   A CA  1 
ATOM   4349  C  C   . HIS   A 1 556  ? -42.58700  86.92700  34.90200  1.000 78.27039  ?  556  HIS   A C   1 
ATOM   4350  O  O   . HIS   A 1 556  ? -42.71000  86.49900  36.05400  1.000 76.99151  ?  556  HIS   A O   1 
ATOM   4351  C  CB  . HIS   A 1 556  ? -40.56400  85.83900  33.93200  1.000 55.56215  ?  556  HIS   A CB  1 
ATOM   4352  C  CG  . HIS   A 1 556  ? -41.03900  85.32700  32.60900  1.000 55.47216  ?  556  HIS   A CG  1 
ATOM   4353  N  ND1 . HIS   A 1 556  ? -41.93900  84.29000  32.48900  1.000 67.75356  ?  556  HIS   A ND1 1 
ATOM   4354  C  CD2 . HIS   A 1 556  ? -40.75300  85.72500  31.34700  1.000 45.10182  ?  556  HIS   A CD2 1 
ATOM   4355  C  CE1 . HIS   A 1 556  ? -42.17700  84.06300  31.21000  1.000 66.88397  ?  556  HIS   A CE1 1 
ATOM   4356  N  NE2 . HIS   A 1 556  ? -41.47100  84.92100  30.49600  1.000 56.97455  ?  556  HIS   A NE2 1 
ATOM   4357  N  N   . PRO   A 1 557  ? -43.64900  87.18700  34.13500  1.000 82.80580  ?  557  PRO   A N   1 
ATOM   4358  C  CA  . PRO   A 1 557  ? -45.00400  86.99900  34.67200  1.000 79.52899  ?  557  PRO   A CA  1 
ATOM   4359  C  C   . PRO   A 1 557  ? -45.35900  85.54700  34.94300  1.000 72.46029  ?  557  PRO   A C   1 
ATOM   4360  O  O   . PRO   A 1 557  ? -46.32400  85.29400  35.67400  1.000 71.92180  ?  557  PRO   A O   1 
ATOM   4361  C  CB  . PRO   A 1 557  ? -45.90000  87.59900  33.58100  1.000 70.57827  ?  557  PRO   A CB  1 
ATOM   4362  C  CG  . PRO   A 1 557  ? -45.09000  87.48300  32.33000  1.000 60.83211  ?  557  PRO   A CG  1 
ATOM   4363  C  CD  . PRO   A 1 557  ? -43.66200  87.68100  32.74700  1.000 62.71294  ?  557  PRO   A CD  1 
ATOM   4364  N  N   . GLN   A 1 558  ? -44.61500  84.58800  34.39000  1.000 66.54045  ?  558  GLN   A N   1 
ATOM   4365  C  CA  . GLN   A 1 558  ? -44.91300  83.17700  34.58400  1.000 65.60441  ?  558  GLN   A CA  1 
ATOM   4366  C  C   . GLN   A 1 558  ? -43.80300  82.39000  35.26300  1.000 63.52858  ?  558  GLN   A C   1 
ATOM   4367  O  O   . GLN   A 1 558  ? -44.08000  81.30900  35.79400  1.000 79.45969  ?  558  GLN   A O   1 
ATOM   4368  C  CB  . GLN   A 1 558  ? -45.24000  82.50500  33.24000  1.000 57.79309  ?  558  GLN   A CB  1 
ATOM   4369  C  CG  . GLN   A 1 558  ? -46.55300  82.96400  32.62400  1.000 61.22241  ?  558  GLN   A CG  1 
ATOM   4370  C  CD  . GLN   A 1 558  ? -46.36500  83.67700  31.29900  1.000 60.77085  ?  558  GLN   A CD  1 
ATOM   4371  O  OE1 . GLN   A 1 558  ? -45.40500  83.42200  30.57300  1.000 60.07580  ?  558  GLN   A OE1 1 
ATOM   4372  N  NE2 . GLN   A 1 558  ? -47.28600  84.57900  30.97800  1.000 55.77122  ?  558  GLN   A NE2 1 
ATOM   4373  N  N   . THR   A 1 559  ? -42.56600  82.88700  35.26400  1.000 62.36255  ?  559  THR   A N   1 
ATOM   4374  C  CA  . THR   A 1 559  ? -41.45800  82.18200  35.89200  1.000 81.06763  ?  559  THR   A CA  1 
ATOM   4375  C  C   . THR   A 1 559  ? -40.97900  82.84000  37.17900  1.000 66.45005  ?  559  THR   A C   1 
ATOM   4376  O  O   . THR   A 1 559  ? -40.25300  82.20000  37.94700  1.000 48.68210  ?  559  THR   A O   1 
ATOM   4377  C  CB  . THR   A 1 559  ? -40.27700  82.06200  34.91500  1.000 74.94743  ?  559  THR   A CB  1 
ATOM   4378  O  OG1 . THR   A 1 559  ? -40.77300  81.98200  33.57300  1.000 71.83017  ?  559  THR   A OG1 1 
ATOM   4379  C  CG2 . THR   A 1 559  ? -39.46700  80.80900  35.20900  1.000 70.67334  ?  559  THR   A CG2 1 
ATOM   4380  N  N   . GLY   A 1 560  ? -41.37100  84.08600  37.43900  1.000 70.30454  ?  560  GLY   A N   1 
ATOM   4381  C  CA  . GLY   A 1 560  ? -40.94300  84.76100  38.64800  1.000 74.18056  ?  560  GLY   A CA  1 
ATOM   4382  C  C   . GLY   A 1 560  ? -39.45900  85.02400  38.72800  1.000 69.56621  ?  560  GLY   A C   1 
ATOM   4383  O  O   . GLY   A 1 560  ? -38.93500  85.23600  39.82400  1.000 78.46709  ?  560  GLY   A O   1 
ATOM   4384  N  N   . GLU   A 1 561  ? -38.76500  85.01600  37.59600  1.000 71.55184  ?  561  GLU   A N   1 
ATOM   4385  C  CA  . GLU   A 1 561  ? -37.32600  85.21500  37.55400  1.000 53.96679  ?  561  GLU   A CA  1 
ATOM   4386  C  C   . GLU   A 1 561  ? -37.01100  86.59100  36.98600  1.000 48.93726  ?  561  GLU   A C   1 
ATOM   4387  O  O   . GLU   A 1 561  ? -37.70200  87.07600  36.08500  1.000 53.22021  ?  561  GLU   A O   1 
ATOM   4388  C  CB  . GLU   A 1 561  ? -36.64800  84.13500  36.70800  1.000 64.29203  ?  561  GLU   A CB  1 
ATOM   4389  C  CG  . GLU   A 1 561  ? -37.02900  82.72200  37.10200  1.000 74.27366  ?  561  GLU   A CG  1 
ATOM   4390  C  CD  . GLU   A 1 561  ? -36.14100  81.68000  36.45600  1.000 101.84632 ?  561  GLU   A CD  1 
ATOM   4391  O  OE1 . GLU   A 1 561  ? -36.23300  81.48900  35.22400  1.000 88.10887  ?  561  GLU   A OE1 1 
ATOM   4392  O  OE2 . GLU   A 1 561  ? -35.33700  81.05800  37.18300  1.000 109.73285 -1 561  GLU   A OE2 1 
ATOM   4393  N  N   . ARG   A 1 562  ? -35.96900  87.21300  37.52300  1.000 35.52711  ?  562  ARG   A N   1 
ATOM   4394  C  CA  . ARG   A 1 562  ? -35.51000  88.49700  37.01800  1.000 46.27447  ?  562  ARG   A CA  1 
ATOM   4395  C  C   . ARG   A 1 562  ? -34.73700  88.28100  35.72200  1.000 50.43401  ?  562  ARG   A C   1 
ATOM   4396  O  O   . ARG   A 1 562  ? -33.81000  87.46700  35.67100  1.000 54.57104  ?  562  ARG   A O   1 
ATOM   4397  C  CB  . ARG   A 1 562  ? -34.64000  89.18700  38.06600  1.000 39.74964  ?  562  ARG   A CB  1 
ATOM   4398  C  CG  . ARG   A 1 562  ? -34.53000  90.68800  37.91800  1.000 40.26089  ?  562  ARG   A CG  1 
ATOM   4399  C  CD  . ARG   A 1 562  ? -33.67000  91.24700  39.03300  1.000 47.80947  ?  562  ARG   A CD  1 
ATOM   4400  N  NE  . ARG   A 1 562  ? -32.98400  92.46800  38.63600  1.000 59.37017  ?  562  ARG   A NE  1 
ATOM   4401  C  CZ  . ARG   A 1 562  ? -31.78000  92.81500  39.06800  1.000 51.63809  ?  562  ARG   A CZ  1 
ATOM   4402  N  NH1 . ARG   A 1 562  ? -31.09200  92.04200  39.89200  1.000 48.28728  ?  562  ARG   A NH1 1 
ATOM   4403  N  NH2 . ARG   A 1 562  ? -31.24900  93.96200  38.65500  1.000 54.58824  ?  562  ARG   A NH2 1 
ATOM   4404  N  N   . MET   A 1 563  ? -35.13100  88.99500  34.67100  1.000 33.41053  ?  563  MET   A N   1 
ATOM   4405  C  CA  . MET   A 1 563  ? -34.52800  88.84100  33.35600  1.000 33.51991  ?  563  MET   A CA  1 
ATOM   4406  C  C   . MET   A 1 563  ? -34.10000  90.19900  32.82400  1.000 45.55903  ?  563  MET   A C   1 
ATOM   4407  O  O   . MET   A 1 563  ? -34.65600  91.23500  33.20000  1.000 46.83422  ?  563  MET   A O   1 
ATOM   4408  C  CB  . MET   A 1 563  ? -35.49700  88.18400  32.36300  1.000 40.02704  ?  563  MET   A CB  1 
ATOM   4409  C  CG  . MET   A 1 563  ? -36.14900  86.91200  32.87200  1.000 31.94079  ?  563  MET   A CG  1 
ATOM   4410  S  SD  . MET   A 1 563  ? -36.96500  85.99000  31.55400  1.000 45.28687  ?  563  MET   A SD  1 
ATOM   4411  C  CE  . MET   A 1 563  ? -37.57000  84.56400  32.45700  1.000 40.64871  ?  563  MET   A CE  1 
ATOM   4412  N  N   . TYR   A 1 564  ? -33.10600  90.18700  31.94000  1.000 34.62315  ?  564  TYR   A N   1 
ATOM   4413  C  CA  . TYR   A 1 564  ? -32.63900  91.39500  31.27700  1.000 42.15183  ?  564  TYR   A CA  1 
ATOM   4414  C  C   . TYR   A 1 564  ? -33.08800  91.38700  29.82100  1.000 55.44160  ?  564  TYR   A C   1 
ATOM   4415  O  O   . TYR   A 1 564  ? -32.88200  90.40100  29.10500  1.000 52.40028  ?  564  TYR   A O   1 
ATOM   4416  C  CB  . TYR   A 1 564  ? -31.11800  91.53100  31.36000  1.000 33.26289  ?  564  TYR   A CB  1 
ATOM   4417  C  CG  . TYR   A 1 564  ? -30.60700  92.73400  30.60400  1.000 31.23839  ?  564  TYR   A CG  1 
ATOM   4418  C  CD1 . TYR   A 1 564  ? -30.87500  94.02100  31.05100  1.000 30.09289  ?  564  TYR   A CD1 1 
ATOM   4419  C  CD2 . TYR   A 1 564  ? -29.87200  92.58600  29.43600  1.000 38.79634  ?  564  TYR   A CD2 1 
ATOM   4420  C  CE1 . TYR   A 1 564  ? -30.42100  95.12700  30.35900  1.000 27.43671  ?  564  TYR   A CE1 1 
ATOM   4421  C  CE2 . TYR   A 1 564  ? -29.41100  93.68700  28.73800  1.000 45.77332  ?  564  TYR   A CE2 1 
ATOM   4422  C  CZ  . TYR   A 1 564  ? -29.68800  94.95400  29.20400  1.000 34.41339  ?  564  TYR   A CZ  1 
ATOM   4423  O  OH  . TYR   A 1 564  ? -29.23000  96.05100  28.51000  1.000 41.62933  ?  564  TYR   A OH  1 
ATOM   4424  N  N   . ARG   A 1 565  ? -33.69800  92.48900  29.39500  1.000 47.66479  ?  565  ARG   A N   1 
ATOM   4425  C  CA  . ARG   A 1 565  ? -34.17200  92.66300  28.02500  1.000 46.65816  ?  565  ARG   A CA  1 
ATOM   4426  C  C   . ARG   A 1 565  ? -33.01100  93.16400  27.17300  1.000 46.03939  ?  565  ARG   A C   1 
ATOM   4427  O  O   . ARG   A 1 565  ? -32.73100  94.36400  27.12900  1.000 44.19914  ?  565  ARG   A O   1 
ATOM   4428  C  CB  . ARG   A 1 565  ? -35.34300  93.64000  28.00200  1.000 62.01323  ?  565  ARG   A CB  1 
ATOM   4429  C  CG  . ARG   A 1 565  ? -35.95900  93.87900  26.63900  1.000 65.02880  ?  565  ARG   A CG  1 
ATOM   4430  C  CD  . ARG   A 1 565  ? -36.98500  92.81700  26.31700  1.000 72.15819  ?  565  ARG   A CD  1 
ATOM   4431  N  NE  . ARG   A 1 565  ? -38.06600  92.76800  27.29300  1.000 79.37584  ?  565  ARG   A NE  1 
ATOM   4432  C  CZ  . ARG   A 1 565  ? -39.19400  93.45800  27.19400  1.000 57.84555  ?  565  ARG   A CZ  1 
ATOM   4433  N  NH1 . ARG   A 1 565  ? -39.41700  94.27500  26.17700  1.000 75.05222  ?  565  ARG   A NH1 1 
ATOM   4434  N  NH2 . ARG   A 1 565  ? -40.12100  93.32400  28.13700  1.000 68.36294  ?  565  ARG   A NH2 1 
ATOM   4435  N  N   . THR   A 1 566  ? -32.32400  92.24500  26.49000  1.000 29.71950  ?  566  THR   A N   1 
ATOM   4436  C  CA  . THR   A 1 566  ? -31.15600  92.64000  25.70800  1.000 37.29759  ?  566  THR   A CA  1 
ATOM   4437  C  C   . THR   A 1 566  ? -31.53500  93.50300  24.51100  1.000 51.10170  ?  566  THR   A C   1 
ATOM   4438  O  O   . THR   A 1 566  ? -30.76100  94.38100  24.11300  1.000 53.94844  ?  566  THR   A O   1 
ATOM   4439  C  CB  . THR   A 1 566  ? -30.38600  91.40800  25.23100  1.000 35.87305  ?  566  THR   A CB  1 
ATOM   4440  O  OG1 . THR   A 1 566  ? -31.22100  90.62300  24.36900  1.000 39.91110  ?  566  THR   A OG1 1 
ATOM   4441  C  CG2 . THR   A 1 566  ? -29.94500  90.56400  26.41500  1.000 33.29406  ?  566  THR   A CG2 1 
ATOM   4442  N  N   . GLY   A 1 567  ? -32.71200  93.27900  23.93400  1.000 49.45543  ?  567  GLY   A N   1 
ATOM   4443  C  CA  . GLY   A 1 567  ? -33.06900  93.93700  22.69500  1.000 44.76550  ?  567  GLY   A CA  1 
ATOM   4444  C  C   . GLY   A 1 567  ? -32.41400  93.35100  21.46800  1.000 53.78165  ?  567  GLY   A C   1 
ATOM   4445  O  O   . GLY   A 1 567  ? -32.52500  93.93600  20.38400  1.000 54.41860  ?  567  GLY   A O   1 
ATOM   4446  N  N   . ASP   A 1 568  ? -31.73300  92.21800  21.60400  1.000 51.17306  ?  568  ASP   A N   1 
ATOM   4447  C  CA  . ASP   A 1 568  ? -31.05200  91.55500  20.50500  1.000 57.47361  ?  568  ASP   A CA  1 
ATOM   4448  C  C   . ASP   A 1 568  ? -31.80400  90.29200  20.11000  1.000 50.15870  ?  568  ASP   A C   1 
ATOM   4449  O  O   . ASP   A 1 568  ? -32.45500  89.64900  20.93900  1.000 45.99471  ?  568  ASP   A O   1 
ATOM   4450  C  CB  . ASP   A 1 568  ? -29.61100  91.20300  20.88400  1.000 53.50845  ?  568  ASP   A CB  1 
ATOM   4451  C  CG  . ASP   A 1 568  ? -28.77500  92.42600  21.19700  1.000 62.34961  ?  568  ASP   A CG  1 
ATOM   4452  O  OD1 . ASP   A 1 568  ? -29.24800  93.55300  20.93700  1.000 67.64152  ?  568  ASP   A OD1 1 
ATOM   4453  O  OD2 . ASP   A 1 568  ? -27.64700  92.25900  21.70600  1.000 60.03633  -1 568  ASP   A OD2 1 
ATOM   4454  N  N   . ARG   A 1 569  ? -31.70300  89.94100  18.83400  1.000 47.96797  ?  569  ARG   A N   1 
ATOM   4455  C  CA  . ARG   A 1 569  ? -32.36300  88.76600  18.28900  1.000 40.62404  ?  569  ARG   A CA  1 
ATOM   4456  C  C   . ARG   A 1 569  ? -31.36500  87.62200  18.17700  1.000 42.37877  ?  569  ARG   A C   1 
ATOM   4457  O  O   . ARG   A 1 569  ? -30.22900  87.81500  17.73600  1.000 42.03759  ?  569  ARG   A O   1 
ATOM   4458  C  CB  . ARG   A 1 569  ? -32.97300  89.08000  16.92200  1.000 55.59722  ?  569  ARG   A CB  1 
ATOM   4459  C  CG  . ARG   A 1 569  ? -33.92500  88.03000  16.37900  1.000 60.79938  ?  569  ARG   A CG  1 
ATOM   4460  C  CD  . ARG   A 1 569  ? -34.72600  88.61800  15.23000  1.000 58.74406  ?  569  ARG   A CD  1 
ATOM   4461  N  NE  . ARG   A 1 569  ? -33.95900  89.64300  14.53200  1.000 60.36042  ?  569  ARG   A NE  1 
ATOM   4462  C  CZ  . ARG   A 1 569  ? -33.33200  89.45800  13.37900  1.000 75.68643  ?  569  ARG   A CZ  1 
ATOM   4463  N  NH1 . ARG   A 1 569  ? -33.40800  88.30900  12.72800  1.000 74.30017  ?  569  ARG   A NH1 1 
ATOM   4464  N  NH2 . ARG   A 1 569  ? -32.61100  90.45200  12.86600  1.000 81.49057  ?  569  ARG   A NH2 1 
ATOM   4465  N  N   . ALA   A 1 570  ? -31.79400  86.43200  18.58700  1.000 33.21371  ?  570  ALA   A N   1 
ATOM   4466  C  CA  . ALA   A 1 570  ? -30.92800  85.26200  18.56600  1.000 35.73657  ?  570  ALA   A CA  1 
ATOM   4467  C  C   . ALA   A 1 570  ? -31.80100  84.01700  18.52900  1.000 41.09829  ?  570  ALA   A C   1 
ATOM   4468  O  O   . ALA   A 1 570  ? -33.00800  84.07200  18.77400  1.000 55.67584  ?  570  ALA   A O   1 
ATOM   4469  C  CB  . ALA   A 1 570  ? -29.98200  85.24600  19.77200  1.000 40.27229  ?  570  ALA   A CB  1 
ATOM   4470  N  N   . ARG   A 1 571  ? -31.17200  82.88800  18.20900  1.000 41.41933  ?  571  ARG   A N   1 
ATOM   4471  C  CA  . ARG   A 1 571  ? -31.86000  81.60900  18.15300  1.000 41.11332  ?  571  ARG   A CA  1 
ATOM   4472  C  C   . ARG   A 1 571  ? -30.94800  80.52900  18.71100  1.000 46.65359  ?  571  ARG   A C   1 
ATOM   4473  O  O   . ARG   A 1 571  ? -29.72100  80.61200  18.60200  1.000 47.43878  ?  571  ARG   A O   1 
ATOM   4474  C  CB  . ARG   A 1 571  ? -32.28800  81.25100  16.71900  1.000 47.93487  ?  571  ARG   A CB  1 
ATOM   4475  C  CG  . ARG   A 1 571  ? -31.16800  80.69000  15.85900  1.000 52.18863  ?  571  ARG   A CG  1 
ATOM   4476  C  CD  . ARG   A 1 571  ? -31.60100  80.49200  14.41800  1.000 54.54170  ?  571  ARG   A CD  1 
ATOM   4477  N  NE  . ARG   A 1 571  ? -30.96400  79.32100  13.82900  1.000 58.45778  ?  571  ARG   A NE  1 
ATOM   4478  C  CZ  . ARG   A 1 571  ? -30.75300  79.15200  12.53200  1.000 80.80926  ?  571  ARG   A CZ  1 
ATOM   4479  N  NH1 . ARG   A 1 571  ? -31.08500  80.08300  11.65100  1.000 87.85150  ?  571  ARG   A NH1 1 
ATOM   4480  N  NH2 . ARG   A 1 571  ? -30.18900  78.02500  12.10700  1.000 68.90264  ?  571  ARG   A NH2 1 
ATOM   4481  N  N   . PHE   A 1 572  ? -31.55800  79.52300  19.32900  1.000 59.48231  ?  572  PHE   A N   1 
ATOM   4482  C  CA  . PHE   A 1 572  ? -30.80600  78.37800  19.82000  1.000 43.53425  ?  572  PHE   A CA  1 
ATOM   4483  C  C   . PHE   A 1 572  ? -30.55100  77.40300  18.68000  1.000 50.96746  ?  572  PHE   A C   1 
ATOM   4484  O  O   . PHE   A 1 572  ? -31.45100  77.10700  17.88700  1.000 52.07754  ?  572  PHE   A O   1 
ATOM   4485  C  CB  . PHE   A 1 572  ? -31.56000  77.67700  20.95100  1.000 34.81564  ?  572  PHE   A CB  1 
ATOM   4486  C  CG  . PHE   A 1 572  ? -31.12000  78.09200  22.32400  1.000 35.80537  ?  572  PHE   A CG  1 
ATOM   4487  C  CD1 . PHE   A 1 572  ? -29.91800  77.64300  22.84400  1.000 50.17417  ?  572  PHE   A CD1 1 
ATOM   4488  C  CD2 . PHE   A 1 572  ? -31.91500  78.91500  23.10300  1.000 40.33330  ?  572  PHE   A CD2 1 
ATOM   4489  C  CE1 . PHE   A 1 572  ? -29.51100  78.01600  24.11100  1.000 56.96915  ?  572  PHE   A CE1 1 
ATOM   4490  C  CE2 . PHE   A 1 572  ? -31.51500  79.29200  24.37100  1.000 52.24209  ?  572  PHE   A CE2 1 
ATOM   4491  C  CZ  . PHE   A 1 572  ? -30.31100  78.84200  24.87600  1.000 58.34664  ?  572  PHE   A CZ  1 
ATOM   4492  N  N   . LEU   A 1 573  ? -29.32600  76.92100  18.59100  1.000 45.09713  ?  573  LEU   A N   1 
ATOM   4493  C  CA  . LEU   A 1 573  ? -28.97900  75.84300  17.68300  1.000 39.02630  ?  573  LEU   A CA  1 
ATOM   4494  C  C   . LEU   A 1 573  ? -29.20600  74.50200  18.36800  1.000 44.66773  ?  573  LEU   A C   1 
ATOM   4495  O  O   . LEU   A 1 573  ? -29.27600  74.42900  19.59900  1.000 53.78822  ?  573  LEU   A O   1 
ATOM   4496  C  CB  . LEU   A 1 573  ? -27.52300  75.98300  17.24300  1.000 35.07872  ?  573  LEU   A CB  1 
ATOM   4497  C  CG  . LEU   A 1 573  ? -27.16900  77.25900  16.47700  1.000 37.30173  ?  573  LEU   A CG  1 
ATOM   4498  C  CD1 . LEU   A 1 573  ? -25.66900  77.50300  16.50300  1.000 45.69313  ?  573  LEU   A CD1 1 
ATOM   4499  C  CD2 . LEU   A 1 573  ? -27.67000  77.17500  15.04600  1.000 50.61619  ?  573  LEU   A CD2 1 
ATOM   4500  N  N   . PRO   A 1 574  ? -29.34700  73.41600  17.60300  1.000 50.59458  ?  574  PRO   A N   1 
ATOM   4501  C  CA  . PRO   A 1 574  ? -29.56300  72.10600  18.24200  1.000 46.13679  ?  574  PRO   A CA  1 
ATOM   4502  C  C   . PRO   A 1 574  ? -28.42900  71.67300  19.15800  1.000 61.09394  ?  574  PRO   A C   1 
ATOM   4503  O  O   . PRO   A 1 574  ? -28.67600  70.94100  20.12400  1.000 65.40979  ?  574  PRO   A O   1 
ATOM   4504  C  CB  . PRO   A 1 574  ? -29.72000  71.15400  17.04600  1.000 48.47156  ?  574  PRO   A CB  1 
ATOM   4505  C  CG  . PRO   A 1 574  ? -29.14000  71.88900  15.87600  1.000 45.67968  ?  574  PRO   A CG  1 
ATOM   4506  C  CD  . PRO   A 1 574  ? -29.43200  73.33000  16.13500  1.000 58.46520  ?  574  PRO   A CD  1 
ATOM   4507  N  N   . ASP   A 1 575  ? -27.19400  72.10900  18.89500  1.000 68.50323  ?  575  ASP   A N   1 
ATOM   4508  C  CA  . ASP   A 1 575  ? -26.06200  71.68100  19.71100  1.000 54.53485  ?  575  ASP   A CA  1 
ATOM   4509  C  C   . ASP   A 1 575  ? -26.06900  72.30400  21.10200  1.000 64.21281  ?  575  ASP   A C   1 
ATOM   4510  O  O   . ASP   A 1 575  ? -25.41800  71.77300  22.00800  1.000 74.64769  ?  575  ASP   A O   1 
ATOM   4511  C  CB  . ASP   A 1 575  ? -24.74700  72.00800  19.00100  1.000 43.15858  ?  575  ASP   A CB  1 
ATOM   4512  C  CG  . ASP   A 1 575  ? -24.64800  73.46600  18.59100  1.000 56.54723  ?  575  ASP   A CG  1 
ATOM   4513  O  OD1 . ASP   A 1 575  ? -25.54200  74.25600  18.96000  1.000 63.99229  ?  575  ASP   A OD1 1 
ATOM   4514  O  OD2 . ASP   A 1 575  ? -23.67400  73.82100  17.89400  1.000 69.89707  -1 575  ASP   A OD2 1 
ATOM   4515  N  N   . GLY   A 1 576  ? -26.78300  73.41000  21.29200  1.000 54.62014  ?  576  GLY   A N   1 
ATOM   4516  C  CA  . GLY   A 1 576  ? -26.83000  74.11200  22.56000  1.000 47.41571  ?  576  GLY   A CA  1 
ATOM   4517  C  C   . GLY   A 1 576  ? -26.31000  75.53100  22.50500  1.000 42.44387  ?  576  GLY   A C   1 
ATOM   4518  O  O   . GLY   A 1 576  ? -26.64200  76.33700  23.38700  1.000 49.61883  ?  576  GLY   A O   1 
ATOM   4519  N  N   . ASN   A 1 577  ? -25.50900  75.86900  21.49900  1.000 41.76049  ?  577  ASN   A N   1 
ATOM   4520  C  CA  . ASN   A 1 577  ? -24.97700  77.21500  21.38600  1.000 49.91295  ?  577  ASN   A CA  1 
ATOM   4521  C  C   . ASN   A 1 577  ? -26.06000  78.18500  20.92300  1.000 40.07645  ?  577  ASN   A C   1 
ATOM   4522  O  O   . ASN   A 1 577  ? -27.07400  77.80100  20.33500  1.000 45.43858  ?  577  ASN   A O   1 
ATOM   4523  C  CB  . ASN   A 1 577  ? -23.79700  77.25100  20.41300  1.000 47.68391  ?  577  ASN   A CB  1 
ATOM   4524  C  CG  . ASN   A 1 577  ? -22.60600  76.46000  20.91300  1.000 42.23278  ?  577  ASN   A CG  1 
ATOM   4525  O  OD1 . ASN   A 1 577  ? -21.80100  76.95900  21.69900  1.000 58.27944  ?  577  ASN   A OD1 1 
ATOM   4526  N  ND2 . ASN   A 1 577  ? -22.48500  75.21900  20.45600  1.000 34.13779  ?  577  ASN   A ND2 1 
ATOM   4527  N  N   . ILE   A 1 578  ? -25.82900  79.46000  21.20100  1.000 38.01009  ?  578  ILE   A N   1 
ATOM   4528  C  CA  . ILE   A 1 578  ? -26.72300  80.53400  20.79200  1.000 41.86225  ?  578  ILE   A CA  1 
ATOM   4529  C  C   . ILE   A 1 578  ? -26.09300  81.25700  19.61200  1.000 35.49110  ?  578  ILE   A C   1 
ATOM   4530  O  O   . ILE   A 1 578  ? -24.87200  81.44900  19.56500  1.000 39.87082  ?  578  ILE   A O   1 
ATOM   4531  C  CB  . ILE   A 1 578  ? -26.99700  81.49700  21.96100  1.000 47.23810  ?  578  ILE   A CB  1 
ATOM   4532  C  CG1 . ILE   A 1 578  ? -27.40300  80.70200  23.20100  1.000 35.13853  ?  578  ILE   A CG1 1 
ATOM   4533  C  CG2 . ILE   A 1 578  ? -28.08700  82.49400  21.59200  1.000 44.30312  ?  578  ILE   A CG2 1 
ATOM   4534  C  CD1 . ILE   A 1 578  ? -27.04500  81.37700  24.49700  1.000 41.83527  ?  578  ILE   A CD1 1 
ATOM   4535  N  N   . GLU   A 1 579  ? -26.92400  81.64800  18.65200  1.000 51.72387  ?  579  GLU   A N   1 
ATOM   4536  C  CA  . GLU   A 1 579  ? -26.47400  82.30200  17.43100  1.000 48.26661  ?  579  GLU   A CA  1 
ATOM   4537  C  C   . GLU   A 1 579  ? -27.05900  83.70600  17.38100  1.000 44.00961  ?  579  GLU   A C   1 
ATOM   4538  O  O   . GLU   A 1 579  ? -28.28300  83.87000  17.37800  1.000 47.81990  ?  579  GLU   A O   1 
ATOM   4539  C  CB  . GLU   A 1 579  ? -26.88700  81.49100  16.20100  1.000 36.80851  ?  579  GLU   A CB  1 
ATOM   4540  C  CG  . GLU   A 1 579  ? -26.97600  82.29200  14.91800  1.000 60.43675  ?  579  GLU   A CG  1 
ATOM   4541  C  CD  . GLU   A 1 579  ? -27.29800  81.42800  13.71600  1.000 68.79855  ?  579  GLU   A CD  1 
ATOM   4542  O  OE1 . GLU   A 1 579  ? -27.37300  80.19200  13.87700  1.000 43.41162  ?  579  GLU   A OE1 1 
ATOM   4543  O  OE2 . GLU   A 1 579  ? -27.47400  81.98400  12.61100  1.000 88.69515  -1 579  GLU   A OE2 1 
ATOM   4544  N  N   . PHE   A 1 580  ? -26.18800  84.71100  17.35300  1.000 38.29826  ?  580  PHE   A N   1 
ATOM   4545  C  CA  . PHE   A 1 580  ? -26.64300  86.09300  17.27000  1.000 33.10914  ?  580  PHE   A CA  1 
ATOM   4546  C  C   . PHE   A 1 580  ? -27.16900  86.38600  15.87100  1.000 43.72703  ?  580  PHE   A C   1 
ATOM   4547  O  O   . PHE   A 1 580  ? -26.49400  86.11200  14.87400  1.000 42.03598  ?  580  PHE   A O   1 
ATOM   4548  C  CB  . PHE   A 1 580  ? -25.50500  87.04800  17.62200  1.000 36.83198  ?  580  PHE   A CB  1 
ATOM   4549  C  CG  . PHE   A 1 580  ? -25.90300  88.49600  17.62200  1.000 31.55957  ?  580  PHE   A CG  1 
ATOM   4550  C  CD1 . PHE   A 1 580  ? -26.61400  89.03100  18.68300  1.000 29.78643  ?  580  PHE   A CD1 1 
ATOM   4551  C  CD2 . PHE   A 1 580  ? -25.55600  89.32600  16.56900  1.000 30.51066  ?  580  PHE   A CD2 1 
ATOM   4552  C  CE1 . PHE   A 1 580  ? -26.97700  90.36400  18.68900  1.000 48.42495  ?  580  PHE   A CE1 1 
ATOM   4553  C  CE2 . PHE   A 1 580  ? -25.91600  90.66000  16.57000  1.000 29.64255  ?  580  PHE   A CE2 1 
ATOM   4554  C  CZ  . PHE   A 1 580  ? -26.62800  91.17900  17.63200  1.000 42.78112  ?  580  PHE   A CZ  1 
ATOM   4555  N  N   . LEU   A 1 581  ? -28.37700  86.94700  15.79800  1.000 48.03434  ?  581  LEU   A N   1 
ATOM   4556  C  CA  . LEU   A 1 581  ? -29.02700  87.21600  14.52400  1.000 38.35507  ?  581  LEU   A CA  1 
ATOM   4557  C  C   . LEU   A 1 581  ? -29.19200  88.69800  14.21600  1.000 40.10041  ?  581  LEU   A C   1 
ATOM   4558  O  O   . LEU   A 1 581  ? -29.55600  89.03700  13.08400  1.000 72.16970  ?  581  LEU   A O   1 
ATOM   4559  C  CB  . LEU   A 1 581  ? -30.40100  86.53000  14.47600  1.000 33.89019  ?  581  LEU   A CB  1 
ATOM   4560  C  CG  . LEU   A 1 581  ? -30.36300  85.00000  14.45700  1.000 31.50603  ?  581  LEU   A CG  1 
ATOM   4561  C  CD1 . LEU   A 1 581  ? -31.75800  84.42800  14.32000  1.000 54.35857  ?  581  LEU   A CD1 1 
ATOM   4562  C  CD2 . LEU   A 1 581  ? -29.47300  84.50100  13.33100  1.000 46.62402  ?  581  LEU   A CD2 1 
ATOM   4563  N  N   . GLY   A 1 582  ? -28.93600  89.58300  15.17300  1.000 36.78934  ?  582  GLY   A N   1 
ATOM   4564  C  CA  . GLY   A 1 582  ? -29.03500  91.01200  14.96800  1.000 32.34031  ?  582  GLY   A CA  1 
ATOM   4565  C  C   . GLY   A 1 582  ? -29.86700  91.67300  16.04400  1.000 47.68958  ?  582  GLY   A C   1 
ATOM   4566  O  O   . GLY   A 1 582  ? -30.42700  91.02700  16.92700  1.000 54.89947  ?  582  GLY   A O   1 
ATOM   4567  N  N   . ARG   A 1 583  ? -29.93800  92.99900  15.96300  1.000 52.12249  ?  583  ARG   A N   1 
ATOM   4568  C  CA  . ARG   A 1 583  ? -30.76400  93.76500  16.88600  1.000 56.61049  ?  583  ARG   A CA  1 
ATOM   4569  C  C   . ARG   A 1 583  ? -32.20300  93.81400  16.39300  1.000 54.88518  ?  583  ARG   A C   1 
ATOM   4570  O  O   . ARG   A 1 583  ? -32.46200  93.91400  15.19000  1.000 68.40097  ?  583  ARG   A O   1 
ATOM   4571  C  CB  . ARG   A 1 583  ? -30.22000  95.18400  17.06100  1.000 55.92668  ?  583  ARG   A CB  1 
ATOM   4572  C  CG  . ARG   A 1 583  ? -29.05800  95.29000  18.03800  1.000 62.13505  ?  583  ARG   A CG  1 
ATOM   4573  C  CD  . ARG   A 1 583  ? -29.07500  96.62900  18.76200  1.000 65.06489  ?  583  ARG   A CD  1 
ATOM   4574  N  NE  . ARG   A 1 583  ? -30.24400  96.76700  19.62300  1.000 84.09796  ?  583  ARG   A NE  1 
ATOM   4575  C  CZ  . ARG   A 1 583  ? -30.22400  96.64900  20.94400  1.000 69.74084  ?  583  ARG   A CZ  1 
ATOM   4576  N  NH1 . ARG   A 1 583  ? -29.09900  96.41700  21.60100  1.000 56.09636  ?  583  ARG   A NH1 1 
ATOM   4577  N  NH2 . ARG   A 1 583  ? -31.36100  96.77000  21.62400  1.000 68.35509  ?  583  ARG   A NH2 1 
ATOM   4578  N  N   . LEU   A 1 584  ? -33.14300  93.74800  17.33800  1.000 64.68081  ?  584  LEU   A N   1 
ATOM   4579  C  CA  . LEU   A 1 584  ? -34.56100  93.67200  17.00600  1.000 65.36712  ?  584  LEU   A CA  1 
ATOM   4580  C  C   . LEU   A 1 584  ? -35.09600  94.93700  16.34800  1.000 62.41319  ?  584  LEU   A C   1 
ATOM   4581  O  O   . LEU   A 1 584  ? -36.22300  94.91800  15.84300  1.000 71.45325  ?  584  LEU   A O   1 
ATOM   4582  C  CB  . LEU   A 1 584  ? -35.37400  93.36200  18.26300  1.000 45.73873  ?  584  LEU   A CB  1 
ATOM   4583  C  CG  . LEU   A 1 584  ? -35.38300  91.89700  18.69900  1.000 50.71297  ?  584  LEU   A CG  1 
ATOM   4584  C  CD1 . LEU   A 1 584  ? -36.13700  91.73400  20.00200  1.000 44.83546  ?  584  LEU   A CD1 1 
ATOM   4585  C  CD2 . LEU   A 1 584  ? -36.01000  91.04000  17.61600  1.000 74.88101  ?  584  LEU   A CD2 1 
ATOM   4586  N  N   . ASP   A 1 585  ? -34.32900  96.02800  16.33800  1.000 63.12540  ?  585  ASP   A N   1 
ATOM   4587  C  CA  . ASP   A 1 585  ? -34.76300  97.26100  15.70200  1.000 68.98772  ?  585  ASP   A CA  1 
ATOM   4588  C  C   . ASP   A 1 585  ? -33.92800  97.65400  14.49200  1.000 75.38379  ?  585  ASP   A C   1 
ATOM   4589  O  O   . ASP   A 1 585  ? -34.40600  98.43500  13.66300  1.000 85.11427  ?  585  ASP   A O   1 
ATOM   4590  C  CB  . ASP   A 1 585  ? -34.74900  98.41800  16.71400  1.000 82.83613  ?  585  ASP   A CB  1 
ATOM   4591  C  CG  . ASP   A 1 585  ? -33.41600  98.55600  17.42800  1.000 87.80279  ?  585  ASP   A CG  1 
ATOM   4592  O  OD1 . ASP   A 1 585  ? -32.50200  97.75100  17.15000  1.000 97.89214  ?  585  ASP   A OD1 1 
ATOM   4593  O  OD2 . ASP   A 1 585  ? -33.28400  99.47000  18.26900  1.000 86.13924  -1 585  ASP   A OD2 1 
ATOM   4594  N  N   . ASN   A 1 586  ? -32.71100  97.12900  14.36300  1.000 79.73708  ?  586  ASN   A N   1 
ATOM   4595  C  CA  . ASN   A 1 586  ? -31.80900  97.50800  13.27400  1.000 86.18499  ?  586  ASN   A CA  1 
ATOM   4596  C  C   . ASN   A 1 586  ? -32.08000  96.66400  12.02600  1.000 83.51552  ?  586  ASN   A C   1 
ATOM   4597  O  O   . ASN   A 1 586  ? -31.23400  95.91100  11.54400  1.000 86.00601  ?  586  ASN   A O   1 
ATOM   4598  C  CB  . ASN   A 1 586  ? -30.35700  97.38000  13.72500  1.000 88.46801  ?  586  ASN   A CB  1 
ATOM   4599  C  CG  . ASN   A 1 586  ? -29.91200  98.53400  14.60800  1.000 105.12599 ?  586  ASN   A CG  1 
ATOM   4600  O  OD1 . ASN   A 1 586  ? -28.97200  99.25700  14.27500  1.000 115.44614 ?  586  ASN   A OD1 1 
ATOM   4601  N  ND2 . ASN   A 1 586  ? -30.58900  98.71500  15.73600  1.000 100.57817 ?  586  ASN   A ND2 1 
ATOM   4602  N  N   . LEU   A 1 587  ? -33.29600  96.80600  11.50300  1.000 81.15676  ?  587  LEU   A N   1 
ATOM   4603  C  CA  . LEU   A 1 587  ? -33.70700  96.14700  10.26900  1.000 82.71142  ?  587  LEU   A CA  1 
ATOM   4604  C  C   . LEU   A 1 587  ? -34.08700  97.21300  9.25100   1.000 78.48918  ?  587  LEU   A C   1 
ATOM   4605  O  O   . LEU   A 1 587  ? -34.98800  98.02100  9.49900   1.000 74.29994  ?  587  LEU   A O   1 
ATOM   4606  C  CB  . LEU   A 1 587  ? -34.87300  95.18500  10.51200  1.000 82.63196  ?  587  LEU   A CB  1 
ATOM   4607  C  CG  . LEU   A 1 587  ? -34.49500  93.71700  10.73400  1.000 70.53961  ?  587  LEU   A CG  1 
ATOM   4608  C  CD1 . LEU   A 1 587  ? -33.70200  93.53400  12.02100  1.000 75.88808  ?  587  LEU   A CD1 1 
ATOM   4609  C  CD2 . LEU   A 1 587  ? -35.73300  92.83600  10.73400  1.000 50.67061  ?  587  LEU   A CD2 1 
ATOM   4610  N  N   . VAL   A 1 588  ? -33.39600  97.21400  8.11400   1.000 57.45329  ?  588  VAL   A N   1 
ATOM   4611  C  CA  . VAL   A 1 588  ? -33.61300  98.19000  7.05300   1.000 53.13645  ?  588  VAL   A CA  1 
ATOM   4612  C  C   . VAL   A 1 588  ? -34.42900  97.54500  5.94400   1.000 69.69398  ?  588  VAL   A C   1 
ATOM   4613  O  O   . VAL   A 1 588  ? -34.36900  96.33000  5.72000   1.000 65.37148  ?  588  VAL   A O   1 
ATOM   4614  C  CB  . VAL   A 1 588  ? -32.27300  98.73500  6.51800   1.000 55.23299  ?  588  VAL   A CB  1 
ATOM   4615  C  CG1 . VAL   A 1 588  ? -31.74300  99.82600  7.43100   1.000 70.17743  ?  588  VAL   A CG1 1 
ATOM   4616  C  CG2 . VAL   A 1 588  ? -31.26000  97.60700  6.39900   1.000 47.73414  ?  588  VAL   A CG2 1 
ATOM   4617  N  N   . LYS   A 1 589  ? -35.20100  98.36900  5.23800   1.000 64.85568  ?  589  LYS   A N   1 
ATOM   4618  C  CA  . LYS   A 1 589  ? -36.08900  97.91400  4.17300   1.000 61.93390  ?  589  LYS   A CA  1 
ATOM   4619  C  C   . LYS   A 1 589  ? -35.52200  98.36200  2.83300   1.000 64.22637  ?  589  LYS   A C   1 
ATOM   4620  O  O   . LYS   A 1 589  ? -35.55100  99.55300  2.50500   1.000 81.42238  ?  589  LYS   A O   1 
ATOM   4621  C  CB  . LYS   A 1 589  ? -37.50500  98.44500  4.37900   1.000 76.41545  ?  589  LYS   A CB  1 
ATOM   4622  C  CG  . LYS   A 1 589  ? -38.39300  97.51100  5.17900   1.000 90.40531  ?  589  LYS   A CG  1 
ATOM   4623  C  CD  . LYS   A 1 589  ? -39.06500  98.23800  6.32600   1.000 92.20669  ?  589  LYS   A CD  1 
ATOM   4624  C  CE  . LYS   A 1 589  ? -39.93700  97.29300  7.13900   1.000 82.34906  ?  589  LYS   A CE  1 
ATOM   4625  N  NZ  . LYS   A 1 589  ? -39.13400  96.31200  7.92700   1.000 67.69101  ?  589  LYS   A NZ  1 
ATOM   4626  N  N   . ILE   A 1 590  ? -35.00700  97.40800  2.06400   1.000 53.94756  ?  590  ILE   A N   1 
ATOM   4627  C  CA  . ILE   A 1 590  ? -34.44000  97.66600  0.74600   1.000 51.69734  ?  590  ILE   A CA  1 
ATOM   4628  C  C   . ILE   A 1 590  ? -35.36300  97.02800  -0.28300  1.000 53.51956  ?  590  ILE   A C   1 
ATOM   4629  O  O   . ILE   A 1 590  ? -35.65100  95.82600  -0.20400  1.000 58.16153  ?  590  ILE   A O   1 
ATOM   4630  C  CB  . ILE   A 1 590  ? -33.00900  97.11300  0.62000   1.000 51.01290  ?  590  ILE   A CB  1 
ATOM   4631  C  CG1 . ILE   A 1 590  ? -32.07300  97.68400  1.70200   1.000 48.09924  ?  590  ILE   A CG1 1 
ATOM   4632  C  CG2 . ILE   A 1 590  ? -32.46700  97.34100  -0.78400  1.000 48.18915  ?  590  ILE   A CG2 1 
ATOM   4633  C  CD1 . ILE   A 1 590  ? -32.26200  99.16200  2.01200   1.000 59.88572  ?  590  ILE   A CD1 1 
ATOM   4634  N  N   . ARG   A 1 591  ? -35.82600  97.82900  -1.24600  1.000 54.04162  ?  591  ARG   A N   1 
ATOM   4635  C  CA  . ARG   A 1 591  ? -36.77600  97.37600  -2.26500  1.000 62.71200  ?  591  ARG   A CA  1 
ATOM   4636  C  C   . ARG   A 1 591  ? -38.02300  96.76800  -1.62700  1.000 59.92790  ?  591  ARG   A C   1 
ATOM   4637  O  O   . ARG   A 1 591  ? -38.63600  95.85400  -2.18300  1.000 58.03440  ?  591  ARG   A O   1 
ATOM   4638  C  CB  . ARG   A 1 591  ? -36.12400  96.38100  -3.23200  1.000 80.00504  ?  591  ARG   A CB  1 
ATOM   4639  C  CG  . ARG   A 1 591  ? -36.38900  96.66700  -4.70200  1.000 72.99380  ?  591  ARG   A CG  1 
ATOM   4640  C  CD  . ARG   A 1 591  ? -35.35300  95.99400  -5.59800  1.000 66.10530  ?  591  ARG   A CD  1 
ATOM   4641  N  NE  . ARG   A 1 591  ? -35.64400  94.58700  -5.85200  1.000 79.99182  ?  591  ARG   A NE  1 
ATOM   4642  C  CZ  . ARG   A 1 591  ? -34.85400  93.77000  -6.53600  1.000 75.95114  ?  591  ARG   A CZ  1 
ATOM   4643  N  NH1 . ARG   A 1 591  ? -33.69800  94.18100  -7.03300  1.000 63.57149  ?  591  ARG   A NH1 1 
ATOM   4644  N  NH2 . ARG   A 1 591  ? -35.23100  92.50800  -6.72400  1.000 66.71234  ?  591  ARG   A NH2 1 
ATOM   4645  N  N   . GLY   A 1 592  ? -38.39700  97.26700  -0.45000  1.000 54.60254  ?  592  GLY   A N   1 
ATOM   4646  C  CA  . GLY   A 1 592  ? -39.51100  96.70100  0.28300   1.000 53.39655  ?  592  GLY   A CA  1 
ATOM   4647  C  C   . GLY   A 1 592  ? -39.22300  95.38500  0.96500   1.000 61.86458  ?  592  GLY   A C   1 
ATOM   4648  O  O   . GLY   A 1 592  ? -40.15300  94.61600  1.22400   1.000 76.52644  ?  592  GLY   A O   1 
ATOM   4649  N  N   . TYR   A 1 593  ? -37.95900  95.09800  1.26600   1.000 66.59368  ?  593  TYR   A N   1 
ATOM   4650  C  CA  . TYR   A 1 593  ? -37.56900  93.86200  1.93200   1.000 55.51220  ?  593  TYR   A CA  1 
ATOM   4651  C  C   . TYR   A 1 593  ? -36.78400  94.20300  3.19000   1.000 68.07102  ?  593  TYR   A C   1 
ATOM   4652  O  O   . TYR   A 1 593  ? -35.71900  94.82400  3.11100   1.000 70.09321  ?  593  TYR   A O   1 
ATOM   4653  C  CB  . TYR   A 1 593  ? -36.74200  92.97100  1.00400   1.000 46.83059  ?  593  TYR   A CB  1 
ATOM   4654  C  CG  . TYR   A 1 593  ? -37.56400  92.21200  -0.01400  1.000 67.56006  ?  593  TYR   A CG  1 
ATOM   4655  C  CD1 . TYR   A 1 593  ? -38.33000  91.11700  0.36500   1.000 91.84152  ?  593  TYR   A CD1 1 
ATOM   4656  C  CD2 . TYR   A 1 593  ? -37.56900  92.58400  -1.35200  1.000 76.42141  ?  593  TYR   A CD2 1 
ATOM   4657  C  CE1 . TYR   A 1 593  ? -39.08200  90.41700  -0.55700  1.000 97.59496  ?  593  TYR   A CE1 1 
ATOM   4658  C  CE2 . TYR   A 1 593  ? -38.31900  91.88800  -2.28400  1.000 79.47141  ?  593  TYR   A CE2 1 
ATOM   4659  C  CZ  . TYR   A 1 593  ? -39.07400  90.80500  -1.87900  1.000 79.54258  ?  593  TYR   A CZ  1 
ATOM   4660  O  OH  . TYR   A 1 593  ? -39.82600  90.10200  -2.79300  1.000 78.85307  ?  593  TYR   A OH  1 
ATOM   4661  N  N   . ARG   A 1 594  ? -37.31200  93.79900  4.34300   1.000 72.59403  ?  594  ARG   A N   1 
ATOM   4662  C  CA  . ARG   A 1 594  ? -36.62300  93.99300  5.61400   1.000 60.13257  ?  594  ARG   A CA  1 
ATOM   4663  C  C   . ARG   A 1 594  ? -35.45900  93.01600  5.70300   1.000 67.00453  ?  594  ARG   A C   1 
ATOM   4664  O  O   . ARG   A 1 594  ? -35.66400  91.80100  5.79100   1.000 52.73045  ?  594  ARG   A O   1 
ATOM   4665  C  CB  . ARG   A 1 594  ? -37.59000  93.79500  6.77700   1.000 67.95528  ?  594  ARG   A CB  1 
ATOM   4666  N  N   . ILE   A 1 595  ? -34.23300  93.54000  5.67700   1.000 64.68873  ?  595  ILE   A N   1 
ATOM   4667  C  CA  . ILE   A 1 595  ? -33.03700  92.71100  5.67000   1.000 48.99895  ?  595  ILE   A CA  1 
ATOM   4668  C  C   . ILE   A 1 595  ? -32.12300  93.12500  6.81400   1.000 48.60086  ?  595  ILE   A C   1 
ATOM   4669  O  O   . ILE   A 1 595  ? -32.22900  94.22000  7.37100   1.000 47.05365  ?  595  ILE   A O   1 
ATOM   4670  C  CB  . ILE   A 1 595  ? -32.27100  92.79700  4.33300   1.000 61.31200  ?  595  ILE   A CB  1 
ATOM   4671  C  CG1 . ILE   A 1 595  ? -31.70800  94.20500  4.13600   1.000 44.79824  ?  595  ILE   A CG1 1 
ATOM   4672  C  CG2 . ILE   A 1 595  ? -33.17000  92.40500  3.17000   1.000 58.38159  ?  595  ILE   A CG2 1 
ATOM   4673  C  CD1 . ILE   A 1 595  ? -30.31900  94.22000  3.55200   1.000 46.56513  ?  595  ILE   A CD1 1 
ATOM   4674  N  N   . GLU   A 1 596  ? -31.21200  92.21900  7.15600   1.000 58.24522  ?  596  GLU   A N   1 
ATOM   4675  C  CA  . GLU   A 1 596  ? -30.12800  92.50200  8.08800   1.000 54.23585  ?  596  GLU   A CA  1 
ATOM   4676  C  C   . GLU   A 1 596  ? -28.83900  92.63900  7.29300   1.000 53.65777  ?  596  GLU   A C   1 
ATOM   4677  O  O   . GLU   A 1 596  ? -28.35400  91.63900  6.73900   1.000 53.33403  ?  596  GLU   A O   1 
ATOM   4678  C  CB  . GLU   A 1 596  ? -30.00100  91.39200  9.13200   1.000 49.39495  ?  596  GLU   A CB  1 
ATOM   4679  C  CG  . GLU   A 1 596  ? -28.77800  91.51700  10.02600  1.000 61.95837  ?  596  GLU   A CG  1 
ATOM   4680  C  CD  . GLU   A 1 596  ? -28.81000  92.76100  10.89000  1.000 63.16671  ?  596  GLU   A CD  1 
ATOM   4681  O  OE1 . GLU   A 1 596  ? -29.88000  93.06500  11.45900  1.000 63.08732  ?  596  GLU   A OE1 1 
ATOM   4682  O  OE2 . GLU   A 1 596  ? -27.76500  93.43700  10.99500  1.000 63.22075  -1 596  GLU   A OE2 1 
ATOM   4683  N  N   . PRO   A 1 597  ? -28.25900  93.83700  7.18900   1.000 53.37689  ?  597  PRO   A N   1 
ATOM   4684  C  CA  . PRO   A 1 597  ? -27.03800  93.99500  6.38200   1.000 43.80426  ?  597  PRO   A CA  1 
ATOM   4685  C  C   . PRO   A 1 597  ? -25.89000  93.11600  6.84000   1.000 50.66612  ?  597  PRO   A C   1 
ATOM   4686  O  O   . PRO   A 1 597  ? -25.01100  92.79800  6.02900   1.000 60.04652  ?  597  PRO   A O   1 
ATOM   4687  C  CB  . PRO   A 1 597  ? -26.70000  95.48400  6.54300   1.000 42.33620  ?  597  PRO   A CB  1 
ATOM   4688  C  CG  . PRO   A 1 597  ? -27.98800  96.12900  6.92100   1.000 52.74556  ?  597  PRO   A CG  1 
ATOM   4689  C  CD  . PRO   A 1 597  ? -28.72400  95.11800  7.74800   1.000 57.55676  ?  597  PRO   A CD  1 
ATOM   4690  N  N   . GLY   A 1 598  ? -25.87100  92.71000  8.11000   1.000 40.07921  ?  598  GLY   A N   1 
ATOM   4691  C  CA  . GLY   A 1 598  ? -24.81700  91.84200  8.60200   1.000 52.25480  ?  598  GLY   A CA  1 
ATOM   4692  C  C   . GLY   A 1 598  ? -24.82000  90.45700  7.99100   1.000 48.08837  ?  598  GLY   A C   1 
ATOM   4693  O  O   . GLY   A 1 598  ? -23.81100  89.75100  8.08200   1.000 53.77827  ?  598  GLY   A O   1 
ATOM   4694  N  N   . GLU   A 1 599  ? -25.93100  90.04900  7.37600   1.000 38.69027  ?  599  GLU   A N   1 
ATOM   4695  C  CA  . GLU   A 1 599  ? -25.99700  88.75500  6.71000   1.000 38.69523  ?  599  GLU   A CA  1 
ATOM   4696  C  C   . GLU   A 1 599  ? -25.26100  88.73800  5.37700   1.000 41.99831  ?  599  GLU   A C   1 
ATOM   4697  O  O   . GLU   A 1 599  ? -25.03600  87.65500  4.82600   1.000 34.77070  ?  599  GLU   A O   1 
ATOM   4698  C  CB  . GLU   A 1 599  ? -27.45600  88.34500  6.49600   1.000 27.73595  ?  599  GLU   A CB  1 
ATOM   4699  C  CG  . GLU   A 1 599  ? -28.24400  88.16300  7.78300   1.000 55.75415  ?  599  GLU   A CG  1 
ATOM   4700  C  CD  . GLU   A 1 599  ? -29.61300  87.55600  7.54600   1.000 57.25788  ?  599  GLU   A CD  1 
ATOM   4701  O  OE1 . GLU   A 1 599  ? -29.95400  87.29600  6.37400   1.000 60.11757  ?  599  GLU   A OE1 1 
ATOM   4702  O  OE2 . GLU   A 1 599  ? -30.34700  87.33600  8.53300   1.000 72.93220  -1 599  GLU   A OE2 1 
ATOM   4703  N  N   . ILE   A 1 600  ? -24.88600  89.90200  4.85200   1.000 43.78914  ?  600  ILE   A N   1 
ATOM   4704  C  CA  . ILE   A 1 600  ? -24.17200  89.96600  3.58300   1.000 42.60500  ?  600  ILE   A CA  1 
ATOM   4705  C  C   . ILE   A 1 600  ? -22.66000  89.92000  3.78400   1.000 52.17160  ?  600  ILE   A C   1 
ATOM   4706  O  O   . ILE   A 1 600  ? -21.93300  89.44600  2.90500   1.000 40.18598  ?  600  ILE   A O   1 
ATOM   4707  C  CB  . ILE   A 1 600  ? -24.58800  91.23300  2.81700   1.000 39.13230  ?  600  ILE   A CB  1 
ATOM   4708  C  CG1 . ILE   A 1 600  ? -26.10300  91.43200  2.90600   1.000 48.68642  ?  600  ILE   A CG1 1 
ATOM   4709  C  CG2 . ILE   A 1 600  ? -24.14800  91.15100  1.36500   1.000 40.74744  ?  600  ILE   A CG2 1 
ATOM   4710  C  CD1 . ILE   A 1 600  ? -26.56500  92.81000  2.48900   1.000 38.07165  ?  600  ILE   A CD1 1 
ATOM   4711  N  N   . GLU   A 1 601  ? -22.17600  90.39800  4.93000   1.000 56.04310  ?  601  GLU   A N   1 
ATOM   4712  C  CA  . GLU   A 1 601  ? -20.73700  90.45600  5.17000   1.000 50.16066  ?  601  GLU   A CA  1 
ATOM   4713  C  C   . GLU   A 1 601  ? -20.04100  89.09600  5.13400   1.000 41.23978  ?  601  GLU   A C   1 
ATOM   4714  O  O   . GLU   A 1 601  ? -18.93100  89.02600  4.57900   1.000 48.54550  ?  601  GLU   A O   1 
ATOM   4715  C  CB  . GLU   A 1 601  ? -20.47600  91.17100  6.50300   1.000 42.39162  ?  601  GLU   A CB  1 
ATOM   4716  C  CG  . GLU   A 1 601  ? -20.79600  92.65900  6.46500   1.000 47.46420  ?  601  GLU   A CG  1 
ATOM   4717  C  CD  . GLU   A 1 601  ? -20.95300  93.26900  7.84600   1.000 72.20077  ?  601  GLU   A CD  1 
ATOM   4718  O  OE1 . GLU   A 1 601  ? -20.64500  92.58200  8.84400   1.000 83.23966  ?  601  GLU   A OE1 1 
ATOM   4719  O  OE2 . GLU   A 1 601  ? -21.38600  94.43800  7.93200   1.000 64.62741  -1 601  GLU   A OE2 1 
ATOM   4720  N  N   . PRO   A 1 602  ? -20.59100  88.00900  5.69300   1.000 40.28785  ?  602  PRO   A N   1 
ATOM   4721  C  CA  . PRO   A 1 602  ? -19.88400  86.72000  5.59600   1.000 45.98866  ?  602  PRO   A CA  1 
ATOM   4722  C  C   . PRO   A 1 602  ? -19.67100  86.24800  4.17000   1.000 45.38446  ?  602  PRO   A C   1 
ATOM   4723  O  O   . PRO   A 1 602  ? -18.65600  85.59900  3.88900   1.000 61.69719  ?  602  PRO   A O   1 
ATOM   4724  C  CB  . PRO   A 1 602  ? -20.79500  85.76100  6.37500   1.000 36.85006  ?  602  PRO   A CB  1 
ATOM   4725  C  CG  . PRO   A 1 602  ? -21.52700  86.62600  7.31800   1.000 41.97900  ?  602  PRO   A CG  1 
ATOM   4726  C  CD  . PRO   A 1 602  ? -21.76800  87.90500  6.57500   1.000 56.71317  ?  602  PRO   A CD  1 
ATOM   4727  N  N   . PHE   A 1 603  ? -20.59400  86.55500  3.25600   1.000 40.16427  ?  603  PHE   A N   1 
ATOM   4728  C  CA  . PHE   A 1 603  ? -20.42700  86.11900  1.87400   1.000 45.46556  ?  603  PHE   A CA  1 
ATOM   4729  C  C   . PHE   A 1 603  ? -19.35600  86.92400  1.14800   1.000 44.08585  ?  603  PHE   A C   1 
ATOM   4730  O  O   . PHE   A 1 603  ? -18.63700  86.37400  0.30600   1.000 39.83610  ?  603  PHE   A O   1 
ATOM   4731  C  CB  . PHE   A 1 603  ? -21.75900  86.21100  1.12800   1.000 25.15551  ?  603  PHE   A CB  1 
ATOM   4732  C  CG  . PHE   A 1 603  ? -22.79800  85.25300  1.63000   1.000 31.29632  ?  603  PHE   A CG  1 
ATOM   4733  C  CD1 . PHE   A 1 603  ? -22.89200  83.97400  1.10700   1.000 42.37216  ?  603  PHE   A CD1 1 
ATOM   4734  C  CD2 . PHE   A 1 603  ? -23.68100  85.62900  2.62700   1.000 38.21373  ?  603  PHE   A CD2 1 
ATOM   4735  C  CE1 . PHE   A 1 603  ? -23.84700  83.09000  1.56700   1.000 33.01627  ?  603  PHE   A CE1 1 
ATOM   4736  C  CE2 . PHE   A 1 603  ? -24.63600  84.75200  3.09300   1.000 33.99674  ?  603  PHE   A CE2 1 
ATOM   4737  C  CZ  . PHE   A 1 603  ? -24.72100  83.47900  2.56400   1.000 37.99883  ?  603  PHE   A CZ  1 
ATOM   4738  N  N   . LEU   A 1 604  ? -19.22900  88.22000  1.45400   1.000 44.32794  ?  604  LEU   A N   1 
ATOM   4739  C  CA  . LEU   A 1 604  ? -18.21300  89.03200  0.79000   1.000 45.69693  ?  604  LEU   A CA  1 
ATOM   4740  C  C   . LEU   A 1 604  ? -16.81200  88.66800  1.25900   1.000 49.57609  ?  604  LEU   A C   1 
ATOM   4741  O  O   . LEU   A 1 604  ? -15.86600  88.68000  0.46400   1.000 44.78551  ?  604  LEU   A O   1 
ATOM   4742  C  CB  . LEU   A 1 604  ? -18.48000  90.51900  1.02400   1.000 41.73854  ?  604  LEU   A CB  1 
ATOM   4743  C  CG  . LEU   A 1 604  ? -19.10400  91.29000  -0.13900  1.000 46.41310  ?  604  LEU   A CG  1 
ATOM   4744  C  CD1 . LEU   A 1 604  ? -19.05900  92.78600  0.12700   1.000 29.95817  ?  604  LEU   A CD1 1 
ATOM   4745  C  CD2 . LEU   A 1 604  ? -18.40400  90.95000  -1.44600  1.000 51.00498  ?  604  LEU   A CD2 1 
ATOM   4746  N  N   . MET   A 1 605  ? -16.65200  88.35500  2.54600   1.000 43.02978  ?  605  MET   A N   1 
ATOM   4747  C  CA  . MET   A 1 605  ? -15.33600  87.97400  3.04300   1.000 52.02458  ?  605  MET   A CA  1 
ATOM   4748  C  C   . MET   A 1 605  ? -14.89600  86.61200  2.52500   1.000 55.60098  ?  605  MET   A C   1 
ATOM   4749  O  O   . MET   A 1 605  ? -13.69000  86.34300  2.47200   1.000 71.72250  ?  605  MET   A O   1 
ATOM   4750  C  CB  . MET   A 1 605  ? -15.31700  87.97700  4.57000   1.000 47.63409  ?  605  MET   A CB  1 
ATOM   4751  C  CG  . MET   A 1 605  ? -14.54600  89.14300  5.16100   1.000 57.48132  ?  605  MET   A CG  1 
ATOM   4752  S  SD  . MET   A 1 605  ? -14.04400  88.83900  6.86000   1.000 60.57731  ?  605  MET   A SD  1 
ATOM   4753  C  CE  . MET   A 1 605  ? -13.22000  87.26100  6.67100   1.000 59.73333  ?  605  MET   A CE  1 
ATOM   4754  N  N   . ASN   A 1 606  ? -15.84000  85.75000  2.13700   1.000 36.94874  ?  606  ASN   A N   1 
ATOM   4755  C  CA  . ASN   A 1 606  ? -15.47600  84.47800  1.52400   1.000 44.57753  ?  606  ASN   A CA  1 
ATOM   4756  C  C   . ASN   A 1 606  ? -14.79000  84.65800  0.17800   1.000 57.55380  ?  606  ASN   A C   1 
ATOM   4757  O  O   . ASN   A 1 606  ? -14.24700  83.68300  -0.35500  1.000 67.70808  ?  606  ASN   A O   1 
ATOM   4758  C  CB  . ASN   A 1 606  ? -16.71400  83.59600  1.36300   1.000 38.56607  ?  606  ASN   A CB  1 
ATOM   4759  C  CG  . ASN   A 1 606  ? -17.20700  83.04200  2.68300   1.000 53.99298  ?  606  ASN   A CG  1 
ATOM   4760  O  OD1 . ASN   A 1 606  ? -16.44400  82.91300  3.63900   1.000 67.81788  ?  606  ASN   A OD1 1 
ATOM   4761  N  ND2 . ASN   A 1 606  ? -18.49100  82.70600  2.74100   1.000 66.79082  ?  606  ASN   A ND2 1 
ATOM   4762  N  N   . HIS   A 1 607  ? -14.81200  85.86300  -0.38300  1.000 50.20187  ?  607  HIS   A N   1 
ATOM   4763  C  CA  . HIS   A 1 607  ? -14.05600  86.13500  -1.59300  1.000 54.42222  ?  607  HIS   A CA  1 
ATOM   4764  C  C   . HIS   A 1 607  ? -12.57200  85.88900  -1.33200  1.000 63.00057  ?  607  HIS   A C   1 
ATOM   4765  O  O   . HIS   A 1 607  ? -12.07100  86.21000  -0.24600  1.000 55.66338  ?  607  HIS   A O   1 
ATOM   4766  C  CB  . HIS   A 1 607  ? -14.28400  87.57800  -2.05000  1.000 55.70684  ?  607  HIS   A CB  1 
ATOM   4767  C  CG  . HIS   A 1 607  ? -13.78300  87.86500  -3.43000  1.000 60.60796  ?  607  HIS   A CG  1 
ATOM   4768  N  ND1 . HIS   A 1 607  ? -12.45600  88.11800  -3.70400  1.000 65.81866  ?  607  HIS   A ND1 1 
ATOM   4769  C  CD2 . HIS   A 1 607  ? -14.43300  87.94700  -4.61500  1.000 60.74008  ?  607  HIS   A CD2 1 
ATOM   4770  C  CE1 . HIS   A 1 607  ? -12.30900  88.33800  -4.99900  1.000 72.44359  ?  607  HIS   A CE1 1 
ATOM   4771  N  NE2 . HIS   A 1 607  ? -13.49400  88.24100  -5.57400  1.000 67.23299  ?  607  HIS   A NE2 1 
ATOM   4772  N  N   . PRO   A 1 608  ? -11.84500  85.30900  -2.28900  1.000 74.80949  ?  608  PRO   A N   1 
ATOM   4773  C  CA  . PRO   A 1 608  ? -10.42800  84.98800  -2.04400  1.000 59.08374  ?  608  PRO   A CA  1 
ATOM   4774  C  C   . PRO   A 1 608  ? -9.56700   86.19600  -1.72100  1.000 55.03422  ?  608  PRO   A C   1 
ATOM   4775  O  O   . PRO   A 1 608  ? -8.51400   86.03300  -1.09200  1.000 68.55767  ?  608  PRO   A O   1 
ATOM   4776  C  CB  . PRO   A 1 608  ? -9.98700   84.32600  -3.35700  1.000 60.80715  ?  608  PRO   A CB  1 
ATOM   4777  C  CG  . PRO   A 1 608  ? -11.25000  83.81000  -3.96500  1.000 60.88783  ?  608  PRO   A CG  1 
ATOM   4778  C  CD  . PRO   A 1 608  ? -12.31500  84.79400  -3.58700  1.000 69.04327  ?  608  PRO   A CD  1 
ATOM   4779  N  N   . LEU   A 1 609  ? -9.97900   87.40200  -2.11600  1.000 59.10038  ?  609  LEU   A N   1 
ATOM   4780  C  CA  . LEU   A 1 609  ? -9.15200   88.58900  -1.94900  1.000 55.11675  ?  609  LEU   A CA  1 
ATOM   4781  C  C   . LEU   A 1 609  ? -9.61800   89.51900  -0.84000  1.000 60.94662  ?  609  LEU   A C   1 
ATOM   4782  O  O   . LEU   A 1 609  ? -8.81800   90.33200  -0.36700  1.000 64.23167  ?  609  LEU   A O   1 
ATOM   4783  C  CB  . LEU   A 1 609  ? -9.08500   89.38300  -3.26400  1.000 58.82311  ?  609  LEU   A CB  1 
ATOM   4784  C  CG  . LEU   A 1 609  ? -8.12200   88.91100  -4.36100  1.000 73.62155  ?  609  LEU   A CG  1 
ATOM   4785  C  CD1 . LEU   A 1 609  ? -8.45300   87.51100  -4.86800  1.000 71.18470  ?  609  LEU   A CD1 1 
ATOM   4786  C  CD2 . LEU   A 1 609  ? -8.11000   89.90300  -5.51500  1.000 64.18972  ?  609  LEU   A CD2 1 
ATOM   4787  N  N   . ILE   A 1 610  ? -10.87300  89.42600  -0.41300  1.000 62.27245  ?  610  ILE   A N   1 
ATOM   4788  C  CA  . ILE   A 1 610  ? -11.38300  90.29600  0.64100   1.000 55.38207  ?  610  ILE   A CA  1 
ATOM   4789  C  C   . ILE   A 1 610  ? -11.02800  89.69900  1.99600   1.000 59.45246  ?  610  ILE   A C   1 
ATOM   4790  O  O   . ILE   A 1 610  ? -11.27300  88.51400  2.25100   1.000 55.92873  ?  610  ILE   A O   1 
ATOM   4791  C  CB  . ILE   A 1 610  ? -12.90000  90.49300  0.50000   1.000 48.38954  ?  610  ILE   A CB  1 
ATOM   4792  C  CG1 . ILE   A 1 610  ? -13.22900  91.14000  -0.84500  1.000 49.83659  ?  610  ILE   A CG1 1 
ATOM   4793  C  CG2 . ILE   A 1 610  ? -13.42700  91.35000  1.63200   1.000 48.09990  ?  610  ILE   A CG2 1 
ATOM   4794  C  CD1 . ILE   A 1 610  ? -14.69000  91.48600  -1.01300  1.000 45.53531  ?  610  ILE   A CD1 1 
ATOM   4795  N  N   . GLU   A 1 611  ? -10.44500  90.52400  2.87000   1.000 60.45238  ?  611  GLU   A N   1 
ATOM   4796  C  CA  . GLU   A 1 611  ? -10.05100  90.09400  4.20500   1.000 60.34779  ?  611  GLU   A CA  1 
ATOM   4797  C  C   . GLU   A 1 611  ? -10.85600  90.74700  5.31900   1.000 53.21315  ?  611  GLU   A C   1 
ATOM   4798  O  O   . GLU   A 1 611  ? -10.89300  90.20300  6.42700   1.000 57.97645  ?  611  GLU   A O   1 
ATOM   4799  C  CB  . GLU   A 1 611  ? -8.55900   90.38000  4.43600   1.000 69.75529  ?  611  GLU   A CB  1 
ATOM   4800  C  CG  . GLU   A 1 611  ? -7.63700   89.78200  3.37800   1.000 78.22158  ?  611  GLU   A CG  1 
ATOM   4801  C  CD  . GLU   A 1 611  ? -7.39900   88.29700  3.57400   1.000 80.43451  ?  611  GLU   A CD  1 
ATOM   4802  O  OE1 . GLU   A 1 611  ? -7.31300   87.85800  4.74100   1.000 78.75852  ?  611  GLU   A OE1 1 
ATOM   4803  O  OE2 . GLU   A 1 611  ? -7.29800   87.56900  2.56400   1.000 81.34541  -1 611  GLU   A OE2 1 
ATOM   4804  N  N   . LEU   A 1 612  ? -11.48800  91.89000  5.05900   1.000 58.92132  ?  612  LEU   A N   1 
ATOM   4805  C  CA  . LEU   A 1 612  ? -12.36600  92.55400  6.01400   1.000 59.49525  ?  612  LEU   A CA  1 
ATOM   4806  C  C   . LEU   A 1 612  ? -13.56200  93.12200  5.26700   1.000 53.58848  ?  612  LEU   A C   1 
ATOM   4807  O  O   . LEU   A 1 612  ? -13.41600  93.63900  4.15600   1.000 51.11304  ?  612  LEU   A O   1 
ATOM   4808  C  CB  . LEU   A 1 612  ? -11.64100  93.67500  6.77400   1.000 58.15482  ?  612  LEU   A CB  1 
ATOM   4809  C  CG  . LEU   A 1 612  ? -10.59900  93.27500  7.82000   1.000 60.70760  ?  612  LEU   A CG  1 
ATOM   4810  C  CD1 . LEU   A 1 612  ? -10.03000  94.51000  8.50100   1.000 50.63480  ?  612  LEU   A CD1 1 
ATOM   4811  C  CD2 . LEU   A 1 612  ? -11.19900  92.32500  8.84600   1.000 58.70521  ?  612  LEU   A CD2 1 
ATOM   4812  N  N   . THR   A 1 613  ? -14.74300  93.02600  5.87700   1.000 56.98156  ?  613  THR   A N   1 
ATOM   4813  C  CA  . THR   A 1 613  ? -15.97600  93.47100  5.24100   1.000 48.41764  ?  613  THR   A CA  1 
ATOM   4814  C  C   . THR   A 1 613  ? -16.88900  94.11600  6.27400   1.000 54.21573  ?  613  THR   A C   1 
ATOM   4815  O  O   . THR   A 1 613  ? -16.92700  93.70600  7.43700   1.000 64.56914  ?  613  THR   A O   1 
ATOM   4816  C  CB  . THR   A 1 613  ? -16.71500  92.31000  4.55600   1.000 37.16054  ?  613  THR   A CB  1 
ATOM   4817  O  OG1 . THR   A 1 613  ? -15.80300  91.58700  3.72300   1.000 67.37480  ?  613  THR   A OG1 1 
ATOM   4818  C  CG2 . THR   A 1 613  ? -17.84600  92.83300  3.69000   1.000 46.05825  ?  613  THR   A CG2 1 
ATOM   4819  N  N   . THR   A 1 614  ? -17.62000  95.13700  5.83100   1.000 42.84537  ?  614  THR   A N   1 
ATOM   4820  C  CA  . THR   A 1 614  ? -18.64500  95.77700  6.64800   1.000 48.60816  ?  614  THR   A CA  1 
ATOM   4821  C  C   . THR   A 1 614  ? -19.65700  96.42300  5.71700   1.000 52.84402  ?  614  THR   A C   1 
ATOM   4822  O  O   . THR   A 1 614  ? -19.30500  97.31300  4.93700   1.000 48.85741  ?  614  THR   A O   1 
ATOM   4823  C  CB  . THR   A 1 614  ? -18.04000  96.81400  7.59600   1.000 46.47422  ?  614  THR   A CB  1 
ATOM   4824  O  OG1 . THR   A 1 614  ? -17.32400  96.14400  8.64100   1.000 59.81030  ?  614  THR   A OG1 1 
ATOM   4825  C  CG2 . THR   A 1 614  ? -19.13100  97.68000  8.21000   1.000 50.69171  ?  614  THR   A CG2 1 
ATOM   4826  N  N   . VAL   A 1 615  ? -20.90400  95.96400  5.79100   1.000 47.77242  ?  615  VAL   A N   1 
ATOM   4827  C  CA  . VAL   A 1 615  ? -21.99200  96.48300  4.97000   1.000 50.94345  ?  615  VAL   A CA  1 
ATOM   4828  C  C   . VAL   A 1 615  ? -22.79200  97.47400  5.80100   1.000 44.35190  ?  615  VAL   A C   1 
ATOM   4829  O  O   . VAL   A 1 615  ? -23.25000  97.14700  6.90400   1.000 42.84566  ?  615  VAL   A O   1 
ATOM   4830  C  CB  . VAL   A 1 615  ? -22.89100  95.34800  4.45200   1.000 53.54413  ?  615  VAL   A CB  1 
ATOM   4831  C  CG1 . VAL   A 1 615  ? -24.09300  95.92000  3.72000   1.000 46.71584  ?  615  VAL   A CG1 1 
ATOM   4832  C  CG2 . VAL   A 1 615  ? -22.10100  94.42000  3.54200   1.000 57.78115  ?  615  VAL   A CG2 1 
ATOM   4833  N  N   . LEU   A 1 616  ? -22.96300  98.68400  5.27600   1.000 52.28660  ?  616  LEU   A N   1 
ATOM   4834  C  CA  . LEU   A 1 616  ? -23.69800  99.73600  5.95800   1.000 62.45439  ?  616  LEU   A CA  1 
ATOM   4835  C  C   . LEU   A 1 616  ? -24.92900  100.12800 5.15400   1.000 58.92037  ?  616  LEU   A C   1 
ATOM   4836  O  O   . LEU   A 1 616  ? -24.95900  100.00200 3.92500   1.000 53.54138  ?  616  LEU   A O   1 
ATOM   4837  C  CB  . LEU   A 1 616  ? -22.82400  100.97500 6.19500   1.000 42.63566  ?  616  LEU   A CB  1 
ATOM   4838  C  CG  . LEU   A 1 616  ? -21.71800  100.84900 7.24300   1.000 56.33916  ?  616  LEU   A CG  1 
ATOM   4839  C  CD1 . LEU   A 1 616  ? -21.35700  102.21900 7.80200   1.000 61.04759  ?  616  LEU   A CD1 1 
ATOM   4840  C  CD2 . LEU   A 1 616  ? -22.12700  99.89500  8.35700   1.000 67.29529  ?  616  LEU   A CD2 1 
ATOM   4841  N  N   . ALA   A 1 617  ? -25.94400  100.60800 5.86600   1.000 62.11591  ?  617  ALA   A N   1 
ATOM   4842  C  CA  . ALA   A 1 617  ? -27.17600  101.09300 5.26200   1.000 59.26621  ?  617  ALA   A CA  1 
ATOM   4843  C  C   . ALA   A 1 617  ? -27.18200  102.61400 5.31400   1.000 67.93206  ?  617  ALA   A C   1 
ATOM   4844  O  O   . ALA   A 1 617  ? -27.17700  103.20300 6.40100   1.000 97.25424  ?  617  ALA   A O   1 
ATOM   4845  C  CB  . ALA   A 1 617  ? -28.39800  100.52500 5.98300   1.000 45.91674  ?  617  ALA   A CB  1 
ATOM   4846  N  N   . LYS   A 1 618  ? -27.18500  103.24600 4.14400   1.000 60.18026  ?  618  LYS   A N   1 
ATOM   4847  C  CA  . LYS   A 1 618  ? -27.24200  104.69400 4.04000   1.000 70.20684  ?  618  LYS   A CA  1 
ATOM   4848  C  C   . LYS   A 1 618  ? -28.52300  105.09500 3.32000   1.000 84.22466  ?  618  LYS   A C   1 
ATOM   4849  O  O   . LYS   A 1 618  ? -29.13900  104.29500 2.60900   1.000 79.33148  ?  618  LYS   A O   1 
ATOM   4850  C  CB  . LYS   A 1 618  ? -26.01100  105.24800 3.30900   1.000 62.47471  ?  618  LYS   A CB  1 
ATOM   4851  C  CG  . LYS   A 1 618  ? -24.74400  104.43800 3.54800   1.000 64.85010  ?  618  LYS   A CG  1 
ATOM   4852  C  CD  . LYS   A 1 618  ? -23.51200  105.31900 3.69600   1.000 62.22014  ?  618  LYS   A CD  1 
ATOM   4853  C  CE  . LYS   A 1 618  ? -23.43400  105.93000 5.08800   1.000 79.04966  ?  618  LYS   A CE  1 
ATOM   4854  N  NZ  . LYS   A 1 618  ? -22.09400  106.52200 5.36700   1.000 92.15742  ?  618  LYS   A NZ  1 
ATOM   4855  N  N   . GLU   A 1 619  ? -28.92600  106.34700 3.51600   1.000 97.16528  ?  619  GLU   A N   1 
ATOM   4856  C  CA  . GLU   A 1 619  ? -30.20000  106.83700 3.01400   1.000 101.65685 ?  619  GLU   A CA  1 
ATOM   4857  C  C   . GLU   A 1 619  ? -29.99000  108.07600 2.15700   1.000 94.93700  ?  619  GLU   A C   1 
ATOM   4858  O  O   . GLU   A 1 619  ? -29.01000  108.80900 2.31800   1.000 84.85181  ?  619  GLU   A O   1 
ATOM   4859  C  CB  . GLU   A 1 619  ? -31.16200  107.17200 4.16200   1.000 97.10443  ?  619  GLU   A CB  1 
ATOM   4860  C  CG  . GLU   A 1 619  ? -30.64900  108.27200 5.07800   1.000 109.63983 ?  619  GLU   A CG  1 
ATOM   4861  C  CD  . GLU   A 1 619  ? -31.75200  109.18700 5.57000   1.000 117.54112 ?  619  GLU   A CD  1 
ATOM   4862  O  OE1 . GLU   A 1 619  ? -32.52500  108.76900 6.45700   1.000 129.13083 ?  619  GLU   A OE1 1 
ATOM   4863  O  OE2 . GLU   A 1 619  ? -31.84900  110.32400 5.06100   1.000 105.49250 -1 619  GLU   A OE2 1 
ATOM   4864  N  N   . GLN   A 1 620  ? -30.92800  108.29900 1.24200   1.000 95.47277  ?  620  GLN   A N   1 
ATOM   4865  C  CA  . GLN   A 1 620  ? -31.00000  109.52200 0.45900   1.000 105.19690 ?  620  GLN   A CA  1 
ATOM   4866  C  C   . GLN   A 1 620  ? -32.19600  110.34000 0.92900   1.000 112.69634 ?  620  GLN   A C   1 
ATOM   4867  O  O   . GLN   A 1 620  ? -33.15900  109.79800 1.47900   1.000 113.73480 ?  620  GLN   A O   1 
ATOM   4868  C  CB  . GLN   A 1 620  ? -31.12000  109.21700 -1.03800  1.000 93.67927  ?  620  GLN   A CB  1 
ATOM   4869  C  CG  . GLN   A 1 620  ? -30.16800  108.13400 -1.52700  1.000 91.77087  ?  620  GLN   A CG  1 
ATOM   4870  C  CD  . GLN   A 1 620  ? -29.31300  108.58300 -2.69700  1.000 89.93360  ?  620  GLN   A CD  1 
ATOM   4871  O  OE1 . GLN   A 1 620  ? -29.06500  109.77500 -2.88100  1.000 87.84800  ?  620  GLN   A OE1 1 
ATOM   4872  N  NE2 . GLN   A 1 620  ? -28.85600  107.62600 -3.49800  1.000 77.66310  ?  620  GLN   A NE2 1 
ATOM   4873  N  N   . ALA   A 1 621  ? -32.12300  111.65700 0.71500   1.000 97.85880  ?  621  ALA   A N   1 
ATOM   4874  C  CA  . ALA   A 1 621  ? -33.18900  112.54100 1.18000   1.000 97.64908  ?  621  ALA   A CA  1 
ATOM   4875  C  C   . ALA   A 1 621  ? -34.52700  112.20000 0.53700   1.000 105.71261 ?  621  ALA   A C   1 
ATOM   4876  O  O   . ALA   A 1 621  ? -35.58200  112.42900 1.14100   1.000 99.18038  ?  621  ALA   A O   1 
ATOM   4877  C  CB  . ALA   A 1 621  ? -32.82300  113.99900 0.90400   1.000 89.13379  ?  621  ALA   A CB  1 
ATOM   4878  N  N   . ASP   A 1 622  ? -34.50500  111.65100 -0.67900  1.000 113.49490 ?  622  ASP   A N   1 
ATOM   4879  C  CA  . ASP   A 1 622  ? -35.73900  111.24900 -1.34200  1.000 112.61014 ?  622  ASP   A CA  1 
ATOM   4880  C  C   . ASP   A 1 622  ? -36.44300  110.11600 -0.60800  1.000 100.92621 ?  622  ASP   A C   1 
ATOM   4881  O  O   . ASP   A 1 622  ? -37.65800  109.95000 -0.76200  1.000 86.94433  ?  622  ASP   A O   1 
ATOM   4882  C  CB  . ASP   A 1 622  ? -35.44100  110.83700 -2.78400  1.000 105.54831 ?  622  ASP   A CB  1 
ATOM   4883  C  CG  . ASP   A 1 622  ? -34.41400  111.73500 -3.44200  1.000 105.99393 ?  622  ASP   A CG  1 
ATOM   4884  O  OD1 . ASP   A 1 622  ? -33.22100  111.63400 -3.08100  1.000 103.33779 ?  622  ASP   A OD1 1 
ATOM   4885  O  OD2 . ASP   A 1 622  ? -34.79700  112.54400 -4.31300  1.000 94.67870  -1 622  ASP   A OD2 1 
ATOM   4886  N  N   . GLY   A 1 623  ? -35.71100  109.33600 0.18500   1.000 105.26210 ?  623  GLY   A N   1 
ATOM   4887  C  CA  . GLY   A 1 623  ? -36.30700  108.26700 0.96000   1.000 116.87023 ?  623  GLY   A CA  1 
ATOM   4888  C  C   . GLY   A 1 623  ? -35.66700  106.91700 0.71400   1.000 105.73882 ?  623  GLY   A C   1 
ATOM   4889  O  O   . GLY   A 1 623  ? -35.60600  106.07700 1.61800   1.000 89.47945  ?  623  GLY   A O   1 
ATOM   4890  N  N   . ARG   A 1 624  ? -35.18500  106.69900 -0.50700  1.000 92.52819  ?  624  ARG   A N   1 
ATOM   4891  C  CA  . ARG   A 1 624  ? -34.60900  105.41100 -0.86700  1.000 89.93866  ?  624  ARG   A CA  1 
ATOM   4892  C  C   . ARG   A 1 624  ? -33.36800  105.12100 -0.03100  1.000 98.54176  ?  624  ARG   A C   1 
ATOM   4893  O  O   . ARG   A 1 624  ? -32.55800  106.01200 0.24000   1.000 83.85147  ?  624  ARG   A O   1 
ATOM   4894  C  CB  . ARG   A 1 624  ? -34.26100  105.38600 -2.35500  1.000 97.28297  ?  624  ARG   A CB  1 
ATOM   4895  N  N   . LYS   A 1 625  ? -33.22700  103.86500 0.38100   1.000 96.06898  ?  625  LYS   A N   1 
ATOM   4896  C  CA  . LYS   A 1 625  ? -32.08900  103.41300 1.16700   1.000 83.17110  ?  625  LYS   A CA  1 
ATOM   4897  C  C   . LYS   A 1 625  ? -31.22000  102.48100 0.33500   1.000 72.63907  ?  625  LYS   A C   1 
ATOM   4898  O  O   . LYS   A 1 625  ? -31.73000  101.59800 -0.36200  1.000 63.13918  ?  625  LYS   A O   1 
ATOM   4899  C  CB  . LYS   A 1 625  ? -32.54700  102.70500 2.44500   1.000 72.43961  ?  625  LYS   A CB  1 
ATOM   4900  C  CG  . LYS   A 1 625  ? -33.13100  103.63800 3.49000   1.000 89.89748  ?  625  LYS   A CG  1 
ATOM   4901  C  CD  . LYS   A 1 625  ? -33.20100  102.96800 4.85200   1.000 89.43679  ?  625  LYS   A CD  1 
ATOM   4902  C  CE  . LYS   A 1 625  ? -32.97700  103.97300 5.97100   1.000 95.91601  ?  625  LYS   A CE  1 
ATOM   4903  N  NZ  . LYS   A 1 625  ? -31.70700  103.70800 6.70500   1.000 85.99422  ?  625  LYS   A NZ  1 
ATOM   4904  N  N   . TYR   A 1 626  ? -29.90800  102.68200 0.41400   1.000 64.17420  ?  626  TYR   A N   1 
ATOM   4905  C  CA  . TYR   A 1 626  ? -28.95200  101.91600 -0.36900  1.000 43.02162  ?  626  TYR   A CA  1 
ATOM   4906  C  C   . TYR   A 1 626  ? -27.89600  101.31600 0.54700   1.000 59.35539  ?  626  TYR   A C   1 
ATOM   4907  O  O   . TYR   A 1 626  ? -27.51800  101.91000 1.56100   1.000 63.09330  ?  626  TYR   A O   1 
ATOM   4908  C  CB  . TYR   A 1 626  ? -28.29000  102.78500 -1.45400  1.000 54.81473  ?  626  TYR   A CB  1 
ATOM   4909  C  CG  . TYR   A 1 626  ? -27.46800  103.95400 -0.94400  1.000 58.94485  ?  626  TYR   A CG  1 
ATOM   4910  C  CD1 . TYR   A 1 626  ? -28.07200  105.05100 -0.34000  1.000 60.49783  ?  626  TYR   A CD1 1 
ATOM   4911  C  CD2 . TYR   A 1 626  ? -26.08800  103.97300 -1.09900  1.000 64.23678  ?  626  TYR   A CD2 1 
ATOM   4912  C  CE1 . TYR   A 1 626  ? -27.32100  106.12200 0.11400   1.000 78.42551  ?  626  TYR   A CE1 1 
ATOM   4913  C  CE2 . TYR   A 1 626  ? -25.33000  105.04000 -0.65300  1.000 64.16028  ?  626  TYR   A CE2 1 
ATOM   4914  C  CZ  . TYR   A 1 626  ? -25.95000  106.11000 -0.04700  1.000 76.25379  ?  626  TYR   A CZ  1 
ATOM   4915  O  OH  . TYR   A 1 626  ? -25.19400  107.17100 0.40000   1.000 87.32545  ?  626  TYR   A OH  1 
ATOM   4916  N  N   . LEU   A 1 627  ? -27.43200  100.12600 0.18200   1.000 57.46566  ?  627  LEU   A N   1 
ATOM   4917  C  CA  . LEU   A 1 627  ? -26.40900  99.41200  0.93200   1.000 44.93658  ?  627  LEU   A CA  1 
ATOM   4918  C  C   . LEU   A 1 627  ? -25.04900  99.65400  0.29200   1.000 47.18564  ?  627  LEU   A C   1 
ATOM   4919  O  O   . LEU   A 1 627  ? -24.90900  99.56500  -0.93200  1.000 48.51177  ?  627  LEU   A O   1 
ATOM   4920  C  CB  . LEU   A 1 627  ? -26.71000  97.91300  0.97200   1.000 43.54710  ?  627  LEU   A CB  1 
ATOM   4921  C  CG  . LEU   A 1 627  ? -28.08500  97.48200  1.48500   1.000 49.25960  ?  627  LEU   A CG  1 
ATOM   4922  C  CD1 . LEU   A 1 627  ? -28.31400  96.01100  1.18400   1.000 37.36982  ?  627  LEU   A CD1 1 
ATOM   4923  C  CD2 . LEU   A 1 627  ? -28.21100  97.75100  2.97400   1.000 54.70862  ?  627  LEU   A CD2 1 
ATOM   4924  N  N   . VAL   A 1 628  ? -24.05200  99.95700  1.12000   1.000 52.73107  ?  628  VAL   A N   1 
ATOM   4925  C  CA  . VAL   A 1 628  ? -22.68500  100.18100 0.66600   1.000 40.63737  ?  628  VAL   A CA  1 
ATOM   4926  C  C   . VAL   A 1 628  ? -21.80200  99.09600  1.26200   1.000 46.34736  ?  628  VAL   A C   1 
ATOM   4927  O  O   . VAL   A 1 628  ? -21.78900  98.90100  2.48300   1.000 59.55262  ?  628  VAL   A O   1 
ATOM   4928  C  CB  . VAL   A 1 628  ? -22.17200  101.57800 1.06100   1.000 37.64281  ?  628  VAL   A CB  1 
ATOM   4929  C  CG1 . VAL   A 1 628  ? -20.85000  101.86600 0.37200   1.000 61.53382  ?  628  VAL   A CG1 1 
ATOM   4930  C  CG2 . VAL   A 1 628  ? -23.19700  102.63700 0.71200   1.000 43.71300  ?  628  VAL   A CG2 1 
ATOM   4931  N  N   . GLY   A 1 629  ? -21.06900  98.39300  0.40300   1.000 47.93101  ?  629  GLY   A N   1 
ATOM   4932  C  CA  . GLY   A 1 629  ? -20.19000  97.33300  0.85500   1.000 50.97022  ?  629  GLY   A CA  1 
ATOM   4933  C  C   . GLY   A 1 629  ? -18.73400  97.74500  0.92700   1.000 50.87327  ?  629  GLY   A C   1 
ATOM   4934  O  O   . GLY   A 1 629  ? -18.05800  97.84900  -0.10100  1.000 52.11060  ?  629  GLY   A O   1 
ATOM   4935  N  N   . TYR   A 1 630  ? -18.23800  97.98300  2.13900   1.000 57.35663  ?  630  TYR   A N   1 
ATOM   4936  C  CA  . TYR   A 1 630  ? -16.84500  98.35100  2.35200   1.000 45.14032  ?  630  TYR   A CA  1 
ATOM   4937  C  C   . TYR   A 1 630  ? -16.01300  97.09100  2.54800   1.000 51.70800  ?  630  TYR   A C   1 
ATOM   4938  O  O   . TYR   A 1 630  ? -16.36500  96.23000  3.36100   1.000 50.71873  ?  630  TYR   A O   1 
ATOM   4939  C  CB  . TYR   A 1 630  ? -16.71100  99.26800  3.56700   1.000 49.89635  ?  630  TYR   A CB  1 
ATOM   4940  C  CG  . TYR   A 1 630  ? -17.62100  100.47400 3.52400   1.000 64.07211  ?  630  TYR   A CG  1 
ATOM   4941  C  CD1 . TYR   A 1 630  ? -18.90000  100.42500 4.06300   1.000 54.99885  ?  630  TYR   A CD1 1 
ATOM   4942  C  CD2 . TYR   A 1 630  ? -17.20100  101.66100 2.94300   1.000 64.79017  ?  630  TYR   A CD2 1 
ATOM   4943  C  CE1 . TYR   A 1 630  ? -19.73600  101.52500 4.02300   1.000 53.82265  ?  630  TYR   A CE1 1 
ATOM   4944  C  CE2 . TYR   A 1 630  ? -18.02700  102.76300 2.89800   1.000 55.70957  ?  630  TYR   A CE2 1 
ATOM   4945  C  CZ  . TYR   A 1 630  ? -19.29300  102.69300 3.44000   1.000 56.68170  ?  630  TYR   A CZ  1 
ATOM   4946  O  OH  . TYR   A 1 630  ? -20.11800  103.79400 3.39600   1.000 62.73236  ?  630  TYR   A OH  1 
ATOM   4947  N  N   . TYR   A 1 631  ? -14.91300  96.98300  1.80600   1.000 56.96603  ?  631  TYR   A N   1 
ATOM   4948  C  CA  . TYR   A 1 631  ? -14.07300  95.79600  1.87300   1.000 61.25044  ?  631  TYR   A CA  1 
ATOM   4949  C  C   . TYR   A 1 631  ? -12.60300  96.18700  1.89200   1.000 53.24823  ?  631  TYR   A C   1 
ATOM   4950  O  O   . TYR   A 1 631  ? -12.19600  97.15400  1.24200   1.000 59.60979  ?  631  TYR   A O   1 
ATOM   4951  C  CB  . TYR   A 1 631  ? -14.35100  94.84100  0.70000   1.000 56.03195  ?  631  TYR   A CB  1 
ATOM   4952  C  CG  . TYR   A 1 631  ? -14.05500  95.40200  -0.67600  1.000 55.96086  ?  631  TYR   A CG  1 
ATOM   4953  C  CD1 . TYR   A 1 631  ? -14.97700  96.20600  -1.33400  1.000 56.32245  ?  631  TYR   A CD1 1 
ATOM   4954  C  CD2 . TYR   A 1 631  ? -12.86300  95.10500  -1.32700  1.000 59.45123  ?  631  TYR   A CD2 1 
ATOM   4955  C  CE1 . TYR   A 1 631  ? -14.71400  96.71400  -2.59500  1.000 64.77957  ?  631  TYR   A CE1 1 
ATOM   4956  C  CE2 . TYR   A 1 631  ? -12.59200  95.60700  -2.58800  1.000 64.09989  ?  631  TYR   A CE2 1 
ATOM   4957  C  CZ  . TYR   A 1 631  ? -13.52100  96.41000  -3.21700  1.000 67.11491  ?  631  TYR   A CZ  1 
ATOM   4958  O  OH  . TYR   A 1 631  ? -13.25700  96.91300  -4.47200  1.000 54.30192  ?  631  TYR   A OH  1 
ATOM   4959  N  N   . VAL   A 1 632  ? -11.81600  95.42800  2.65000   1.000 50.90658  ?  632  VAL   A N   1 
ATOM   4960  C  CA  . VAL   A 1 632  ? -10.36900  95.58700  2.71900   1.000 62.64147  ?  632  VAL   A CA  1 
ATOM   4961  C  C   . VAL   A 1 632  ? -9.74200   94.44200  1.93600   1.000 65.90438  ?  632  VAL   A C   1 
ATOM   4962  O  O   . VAL   A 1 632  ? -10.02000  93.26700  2.20900   1.000 61.05153  ?  632  VAL   A O   1 
ATOM   4963  C  CB  . VAL   A 1 632  ? -9.86500   95.61100  4.17000   1.000 64.38020  ?  632  VAL   A CB  1 
ATOM   4964  C  CG1 . VAL   A 1 632  ? -8.34900   95.52400  4.20700   1.000 58.45470  ?  632  VAL   A CG1 1 
ATOM   4965  C  CG2 . VAL   A 1 632  ? -10.34400  96.87200  4.87300   1.000 67.49691  ?  632  VAL   A CG2 1 
ATOM   4966  N  N   . ALA   A 1 633  ? -8.90300   94.78300  0.96600   1.000 77.51808  ?  633  ALA   A N   1 
ATOM   4967  C  CA  . ALA   A 1 633  ? -8.30900   93.81200  0.06100   1.000 68.59318  ?  633  ALA   A CA  1 
ATOM   4968  C  C   . ALA   A 1 633  ? -6.95900   94.34700  -0.38800  1.000 72.43390  ?  633  ALA   A C   1 
ATOM   4969  O  O   . ALA   A 1 633  ? -6.66700   95.53400  -0.19500  1.000 72.69857  ?  633  ALA   A O   1 
ATOM   4970  C  CB  . ALA   A 1 633  ? -9.22300   93.55100  -1.14600  1.000 71.08459  ?  633  ALA   A CB  1 
ATOM   4971  N  N   . PRO   A 1 634  ? -6.10100   93.49600  -0.96500  1.000 69.15670  ?  634  PRO   A N   1 
ATOM   4972  C  CA  . PRO   A 1 634  ? -4.82900   94.01100  -1.50800  1.000 56.03033  ?  634  PRO   A CA  1 
ATOM   4973  C  C   . PRO   A 1 634  ? -5.01400   95.14900  -2.49800  1.000 61.01260  ?  634  PRO   A C   1 
ATOM   4974  O  O   . PRO   A 1 634  ? -4.40800   96.21600  -2.33600  1.000 52.79471  ?  634  PRO   A O   1 
ATOM   4975  C  CB  . PRO   A 1 634  ? -4.20100   92.76600  -2.15900  1.000 62.60466  ?  634  PRO   A CB  1 
ATOM   4976  C  CG  . PRO   A 1 634  ? -5.30900   91.75000  -2.24600  1.000 71.11151  ?  634  PRO   A CG  1 
ATOM   4977  C  CD  . PRO   A 1 634  ? -6.17800   92.03000  -1.07000  1.000 67.61554  ?  634  PRO   A CD  1 
ATOM   4978  N  N   . GLU   A 1 635  ? -5.84400   94.95400  -3.52100  1.000 58.57272  ?  635  GLU   A N   1 
ATOM   4979  C  CA  . GLU   A 1 635  ? -6.18000   96.02800  -4.44600  1.000 67.23676  ?  635  GLU   A CA  1 
ATOM   4980  C  C   . GLU   A 1 635  ? -7.68800   96.07100  -4.65000  1.000 72.21670  ?  635  GLU   A C   1 
ATOM   4981  O  O   . GLU   A 1 635  ? -8.43000   95.36800  -3.95700  1.000 73.58954  ?  635  GLU   A O   1 
ATOM   4982  C  CB  . GLU   A 1 635  ? -5.45400   95.84400  -5.78000  1.000 68.21130  ?  635  GLU   A CB  1 
ATOM   4983  N  N   . GLU   A 1 636  ? -8.15300   96.88700  -5.59100  1.000 70.62058  ?  636  GLU   A N   1 
ATOM   4984  C  CA  . GLU   A 1 636  ? -9.58400   96.98700  -5.83800  1.000 60.97386  ?  636  GLU   A CA  1 
ATOM   4985  C  C   . GLU   A 1 636  ? -10.09000  95.75000  -6.57300  1.000 69.08166  ?  636  GLU   A C   1 
ATOM   4986  O  O   . GLU   A 1 636  ? -9.34500   95.07200  -7.28600  1.000 66.11773  ?  636  GLU   A O   1 
ATOM   4987  C  CB  . GLU   A 1 636  ? -9.90600   98.24200  -6.64900  1.000 65.99091  ?  636  GLU   A CB  1 
ATOM   4988  C  CG  . GLU   A 1 636  ? -11.31300  98.77800  -6.41900  1.000 73.46217  ?  636  GLU   A CG  1 
ATOM   4989  C  CD  . GLU   A 1 636  ? -11.80400  99.65200  -7.55700  1.000 83.17974  ?  636  GLU   A CD  1 
ATOM   4990  O  OE1 . GLU   A 1 636  ? -11.63200  99.25500  -8.72900  1.000 68.45038  ?  636  GLU   A OE1 1 
ATOM   4991  O  OE2 . GLU   A 1 636  ? -12.36200  100.73500 -7.28000  1.000 72.94407  -1 636  GLU   A OE2 1 
ATOM   4992  N  N   . ILE   A 1 637  ? -11.37300  95.46200  -6.39000  1.000 66.77502  ?  637  ILE   A N   1 
ATOM   4993  C  CA  . ILE   A 1 637  ? -12.04200  94.33900  -7.03200  1.000 57.68392  ?  637  ILE   A CA  1 
ATOM   4994  C  C   . ILE   A 1 637  ? -13.12900  94.90800  -7.93300  1.000 66.36099  ?  637  ILE   A C   1 
ATOM   4995  O  O   . ILE   A 1 637  ? -13.86100  95.80300  -7.50800  1.000 68.66895  ?  637  ILE   A O   1 
ATOM   4996  C  CB  . ILE   A 1 637  ? -12.64600  93.35500  -6.01300  1.000 49.00518  ?  637  ILE   A CB  1 
ATOM   4997  C  CG1 . ILE   A 1 637  ? -11.56300  92.87700  -5.04300  1.000 56.77542  ?  637  ILE   A CG1 1 
ATOM   4998  C  CG2 . ILE   A 1 637  ? -13.28400  92.16800  -6.71600  1.000 54.12102  ?  637  ILE   A CG2 1 
ATOM   4999  C  CD1 . ILE   A 1 637  ? -11.99500  91.73400  -4.15700  1.000 59.44960  ?  637  ILE   A CD1 1 
ATOM   5000  N  N   . PRO   A 1 638  ? -13.25600  94.44300  -9.17900  1.000 61.76452  ?  638  PRO   A N   1 
ATOM   5001  C  CA  . PRO   A 1 638  ? -14.25800  95.01900  -10.08500 1.000 54.84964  ?  638  PRO   A CA  1 
ATOM   5002  C  C   . PRO   A 1 638  ? -15.66700  94.92400  -9.51900  1.000 55.02659  ?  638  PRO   A C   1 
ATOM   5003  O  O   . PRO   A 1 638  ? -16.02200  93.96800  -8.82700  1.000 63.36704  ?  638  PRO   A O   1 
ATOM   5004  C  CB  . PRO   A 1 638  ? -14.11100  94.17500  -11.35600 1.000 65.98513  ?  638  PRO   A CB  1 
ATOM   5005  C  CG  . PRO   A 1 638  ? -12.70400  93.68700  -11.31500 1.000 63.43468  ?  638  PRO   A CG  1 
ATOM   5006  C  CD  . PRO   A 1 638  ? -12.39300  93.46300  -9.86200  1.000 64.46978  ?  638  PRO   A CD  1 
ATOM   5007  N  N   . HIS   A 1 639  ? -16.47100  95.94500  -9.82800  1.000 52.60142  ?  639  HIS   A N   1 
ATOM   5008  C  CA  . HIS   A 1 639  ? -17.83100  96.01900  -9.30100  1.000 49.59444  ?  639  HIS   A CA  1 
ATOM   5009  C  C   . HIS   A 1 639  ? -18.65400  94.81100  -9.72900  1.000 56.95454  ?  639  HIS   A C   1 
ATOM   5010  O  O   . HIS   A 1 639  ? -19.32000  94.17400  -8.90400  1.000 61.11901  ?  639  HIS   A O   1 
ATOM   5011  C  CB  . HIS   A 1 639  ? -18.49700  97.31700  -9.76000  1.000 49.66562  ?  639  HIS   A CB  1 
ATOM   5012  C  CG  . HIS   A 1 639  ? -19.86600  97.52900  -9.19300  1.000 72.53776  ?  639  HIS   A CG  1 
ATOM   5013  N  ND1 . HIS   A 1 639  ? -20.09100  98.26900  -8.05200  1.000 71.81504  ?  639  HIS   A ND1 1 
ATOM   5014  C  CD2 . HIS   A 1 639  ? -21.08100  97.09800  -9.60800  1.000 65.81353  ?  639  HIS   A CD2 1 
ATOM   5015  C  CE1 . HIS   A 1 639  ? -21.38600  98.28600  -7.78900  1.000 77.58766  ?  639  HIS   A CE1 1 
ATOM   5016  N  NE2 . HIS   A 1 639  ? -22.00900  97.58200  -8.71800  1.000 70.47807  ?  639  HIS   A NE2 1 
ATOM   5017  N  N   . GLY   A 1 640  ? -18.62100  94.48200  -11.02200 1.000 58.83717  ?  640  GLY   A N   1 
ATOM   5018  C  CA  . GLY   A 1 640  ? -19.34700  93.31900  -11.49900 1.000 50.95299  ?  640  GLY   A CA  1 
ATOM   5019  C  C   . GLY   A 1 640  ? -18.88600  92.02600  -10.85900 1.000 58.00765  ?  640  GLY   A C   1 
ATOM   5020  O  O   . GLY   A 1 640  ? -19.69500  91.12500  -10.62400 1.000 66.33307  ?  640  GLY   A O   1 
ATOM   5021  N  N   . GLU   A 1 641  ? -17.58800  91.91700  -10.56200 1.000 58.17729  ?  641  GLU   A N   1 
ATOM   5022  C  CA  . GLU   A 1 641  ? -17.07900  90.72000  -9.89800  1.000 62.73077  ?  641  GLU   A CA  1 
ATOM   5023  C  C   . GLU   A 1 641  ? -17.72800  90.52400  -8.53500  1.000 62.64603  ?  641  GLU   A C   1 
ATOM   5024  O  O   . GLU   A 1 641  ? -18.09400  89.40000  -8.16800  1.000 49.56332  ?  641  GLU   A O   1 
ATOM   5025  C  CB  . GLU   A 1 641  ? -15.55900  90.79900  -9.75400  1.000 62.42770  ?  641  GLU   A CB  1 
ATOM   5026  C  CG  . GLU   A 1 641  ? -14.78700  90.24600  -10.93700 1.000 84.06263  ?  641  GLU   A CG  1 
ATOM   5027  C  CD  . GLU   A 1 641  ? -13.49100  89.58100  -10.51700 1.000 90.75252  ?  641  GLU   A CD  1 
ATOM   5028  O  OE1 . GLU   A 1 641  ? -13.15700  89.63500  -9.31400  1.000 78.03344  ?  641  GLU   A OE1 1 
ATOM   5029  O  OE2 . GLU   A 1 641  ? -12.80900  88.99900  -11.38700 1.000 95.99073  -1 641  GLU   A OE2 1 
ATOM   5030  N  N   . LEU   A 1 642  ? -17.87600  91.60500  -7.76800  1.000 58.74330  ?  642  LEU   A N   1 
ATOM   5031  C  CA  . LEU   A 1 642  ? -18.51500  91.49900  -6.46100  1.000 57.11185  ?  642  LEU   A CA  1 
ATOM   5032  C  C   . LEU   A 1 642  ? -20.00600  91.22000  -6.59900  1.000 57.22094  ?  642  LEU   A C   1 
ATOM   5033  O  O   . LEU   A 1 642  ? -20.58200  90.48000  -5.79300  1.000 66.82091  ?  642  LEU   A O   1 
ATOM   5034  C  CB  . LEU   A 1 642  ? -18.26900  92.77400  -5.65500  1.000 58.06164  ?  642  LEU   A CB  1 
ATOM   5035  C  CG  . LEU   A 1 642  ? -16.79700  93.06700  -5.35100  1.000 55.02535  ?  642  LEU   A CG  1 
ATOM   5036  C  CD1 . LEU   A 1 642  ? -16.62800  94.45300  -4.75100  1.000 46.25202  ?  642  LEU   A CD1 1 
ATOM   5037  C  CD2 . LEU   A 1 642  ? -16.21700  92.00700  -4.42600  1.000 40.48523  ?  642  LEU   A CD2 1 
ATOM   5038  N  N   . ARG   A 1 643  ? -20.64800  91.80200  -7.61700  1.000 50.43196  ?  643  ARG   A N   1 
ATOM   5039  C  CA  . ARG   A 1 643  ? -22.05300  91.49600  -7.86900  1.000 47.12466  ?  643  ARG   A CA  1 
ATOM   5040  C  C   . ARG   A 1 643  ? -22.23100  90.04400  -8.29500  1.000 47.06334  ?  643  ARG   A C   1 
ATOM   5041  O  O   . ARG   A 1 643  ? -23.23500  89.40900  -7.95100  1.000 46.52151  ?  643  ARG   A O   1 
ATOM   5042  C  CB  . ARG   A 1 643  ? -22.61800  92.43800  -8.93000  1.000 43.42720  ?  643  ARG   A CB  1 
ATOM   5043  C  CG  . ARG   A 1 643  ? -22.69400  93.89200  -8.50000  1.000 65.18842  ?  643  ARG   A CG  1 
ATOM   5044  C  CD  . ARG   A 1 643  ? -23.62300  94.67200  -9.41400  1.000 73.87953  ?  643  ARG   A CD  1 
ATOM   5045  N  NE  . ARG   A 1 643  ? -24.93900  94.04900  -9.49000  1.000 79.80392  ?  643  ARG   A NE  1 
ATOM   5046  C  CZ  . ARG   A 1 643  ? -25.96400  94.36100  -8.70800  1.000 81.53707  ?  643  ARG   A CZ  1 
ATOM   5047  N  NH1 . ARG   A 1 643  ? -25.86800  95.30700  -7.78700  1.000 72.73648  ?  643  ARG   A NH1 1 
ATOM   5048  N  NH2 . ARG   A 1 643  ? -27.11300  93.70800  -8.85400  1.000 73.20456  ?  643  ARG   A NH2 1 
ATOM   5049  N  N   . GLU   A 1 644  ? -21.26900  89.50200  -9.04500  1.000 44.95619  ?  644  GLU   A N   1 
ATOM   5050  C  CA  . GLU   A 1 644  ? -21.31700  88.08800  -9.40100  1.000 45.41217  ?  644  GLU   A CA  1 
ATOM   5051  C  C   . GLU   A 1 644  ? -21.06800  87.21100  -8.18100  1.000 53.34316  ?  644  GLU   A C   1 
ATOM   5052  O  O   . GLU   A 1 644  ? -21.78800  86.23200  -7.95100  1.000 57.94605  ?  644  GLU   A O   1 
ATOM   5053  C  CB  . GLU   A 1 644  ? -20.29200  87.77800  -10.49400 1.000 64.62608  ?  644  GLU   A CB  1 
ATOM   5054  C  CG  . GLU   A 1 644  ? -20.59100  88.40100  -11.84700 1.000 94.15303  ?  644  GLU   A CG  1 
ATOM   5055  C  CD  . GLU   A 1 644  ? -19.53100  88.07100  -12.88200 1.000 100.04800 ?  644  GLU   A CD  1 
ATOM   5056  O  OE1 . GLU   A 1 644  ? -19.13100  86.89100  -12.96800 1.000 90.68018  ?  644  GLU   A OE1 1 
ATOM   5057  O  OE2 . GLU   A 1 644  ? -19.09100  88.99300  -13.60100 1.000 86.97536  -1 644  GLU   A OE2 1 
ATOM   5058  N  N   . TRP   A 1 645  ? -20.04800  87.55000  -7.38700  1.000 57.21140  ?  645  TRP   A N   1 
ATOM   5059  C  CA  . TRP   A 1 645  ? -19.67600  86.71200  -6.25100  1.000 52.70607  ?  645  TRP   A CA  1 
ATOM   5060  C  C   . TRP   A 1 645  ? -20.82100  86.57800  -5.25600  1.000 53.64624  ?  645  TRP   A C   1 
ATOM   5061  O  O   . TRP   A 1 645  ? -21.08000  85.48400  -4.74000  1.000 51.66268  ?  645  TRP   A O   1 
ATOM   5062  C  CB  . TRP   A 1 645  ? -18.43700  87.28200  -5.56100  1.000 45.69684  ?  645  TRP   A CB  1 
ATOM   5063  C  CG  . TRP   A 1 645  ? -18.05500  86.52000  -4.33500  1.000 49.82081  ?  645  TRP   A CG  1 
ATOM   5064  C  CD1 . TRP   A 1 645  ? -18.28500  86.88000  -3.04000  1.000 46.06892  ?  645  TRP   A CD1 1 
ATOM   5065  C  CD2 . TRP   A 1 645  ? -17.39100  85.25200  -4.28800  1.000 52.77754  ?  645  TRP   A CD2 1 
ATOM   5066  N  NE1 . TRP   A 1 645  ? -17.79700  85.91800  -2.18800  1.000 51.85709  ?  645  TRP   A NE1 1 
ATOM   5067  C  CE2 . TRP   A 1 645  ? -17.24300  84.90800  -2.93100  1.000 52.46043  ?  645  TRP   A CE2 1 
ATOM   5068  C  CE3 . TRP   A 1 645  ? -16.90300  84.37700  -5.26300  1.000 53.30835  ?  645  TRP   A CE3 1 
ATOM   5069  C  CZ2 . TRP   A 1 645  ? -16.62800  83.72700  -2.52400  1.000 53.40717  ?  645  TRP   A CZ2 1 
ATOM   5070  C  CZ3 . TRP   A 1 645  ? -16.29300  83.20600  -4.85700  1.000 58.58595  ?  645  TRP   A CZ3 1 
ATOM   5071  C  CH2 . TRP   A 1 645  ? -16.16000  82.89100  -3.50000  1.000 63.18217  ?  645  TRP   A CH2 1 
ATOM   5072  N  N   . LEU   A 1 646  ? -21.51900  87.67800  -4.97300  1.000 47.77587  ?  646  LEU   A N   1 
ATOM   5073  C  CA  . LEU   A 1 646  ? -22.65400  87.61900  -4.06100  1.000 38.05495  ?  646  LEU   A CA  1 
ATOM   5074  C  C   . LEU   A 1 646  ? -23.89100  87.03200  -4.72700  1.000 54.93148  ?  646  LEU   A C   1 
ATOM   5075  O  O   . LEU   A 1 646  ? -24.72300  86.42100  -4.04700  1.000 55.06205  ?  646  LEU   A O   1 
ATOM   5076  C  CB  . LEU   A 1 646  ? -22.96000  89.01300  -3.51800  1.000 35.13014  ?  646  LEU   A CB  1 
ATOM   5077  C  CG  . LEU   A 1 646  ? -21.83000  89.65100  -2.71100  1.000 38.78886  ?  646  LEU   A CG  1 
ATOM   5078  C  CD1 . LEU   A 1 646  ? -22.16000  91.09300  -2.37700  1.000 39.22777  ?  646  LEU   A CD1 1 
ATOM   5079  C  CD2 . LEU   A 1 646  ? -21.56400  88.85300  -1.44500  1.000 43.00508  ?  646  LEU   A CD2 1 
ATOM   5080  N  N   . GLY   A 1 647  ? -24.02700  87.19800  -6.04200  1.000 54.66737  ?  647  GLY   A N   1 
ATOM   5081  C  CA  . GLY   A 1 647  ? -25.18200  86.68000  -6.75000  1.000 55.40579  ?  647  GLY   A CA  1 
ATOM   5082  C  C   . GLY   A 1 647  ? -25.26400  85.17100  -6.80400  1.000 50.34116  ?  647  GLY   A C   1 
ATOM   5083  O  O   . GLY   A 1 647  ? -26.31300  84.64100  -7.19000  1.000 65.42745  ?  647  GLY   A O   1 
ATOM   5084  N  N   . ASN   A 1 648  ? -24.19100  84.46800  -6.43200  1.000 54.59818  ?  648  ASN   A N   1 
ATOM   5085  C  CA  . ASN   A 1 648  ? -24.21900  83.01200  -6.46400  1.000 57.60363  ?  648  ASN   A CA  1 
ATOM   5086  C  C   . ASN   A 1 648  ? -25.14600  82.43900  -5.40000  1.000 54.25715  ?  648  ASN   A C   1 
ATOM   5087  O  O   . ASN   A 1 648  ? -25.59700  81.29600  -5.53900  1.000 52.48237  ?  648  ASN   A O   1 
ATOM   5088  C  CB  . ASN   A 1 648  ? -22.81300  82.42600  -6.27300  1.000 45.75105  ?  648  ASN   A CB  1 
ATOM   5089  C  CG  . ASN   A 1 648  ? -21.75500  83.06900  -7.17100  1.000 69.67576  ?  648  ASN   A CG  1 
ATOM   5090  O  OD1 . ASN   A 1 648  ? -20.55800  82.97700  -6.88300  1.000 78.38412  ?  648  ASN   A OD1 1 
ATOM   5091  N  ND2 . ASN   A 1 648  ? -22.18300  83.71200  -8.25500  1.000 83.92870  ?  648  ASN   A ND2 1 
ATOM   5092  N  N   . ASP   A 1 649  ? -25.44100  83.20500  -4.34600  1.000 48.84329  ?  649  ASP   A N   1 
ATOM   5093  C  CA  . ASP   A 1 649  ? -26.28500  82.72600  -3.25900  1.000 60.26153  ?  649  ASP   A CA  1 
ATOM   5094  C  C   . ASP   A 1 649  ? -26.86200  83.87500  -2.43800  1.000 59.12615  ?  649  ASP   A C   1 
ATOM   5095  O  O   . ASP   A 1 649  ? -26.97500  83.77200  -1.21200  1.000 64.25116  ?  649  ASP   A O   1 
ATOM   5096  C  CB  . ASP   A 1 649  ? -25.49600  81.77200  -2.35900  1.000 69.26572  ?  649  ASP   A CB  1 
ATOM   5097  C  CG  . ASP   A 1 649  ? -24.08000  82.24500  -2.10300  1.000 57.83080  ?  649  ASP   A CG  1 
ATOM   5098  O  OD1 . ASP   A 1 649  ? -23.77400  83.41500  -2.41400  1.000 61.77538  ?  649  ASP   A OD1 1 
ATOM   5099  O  OD2 . ASP   A 1 649  ? -23.27000  81.44000  -1.59800  1.000 53.15136  -1 649  ASP   A OD2 1 
ATOM   5100  N  N   . LEU   A 1 650  ? -27.23600  84.97200  -3.10300  1.000 56.79439  ?  650  LEU   A N   1 
ATOM   5101  C  CA  . LEU   A 1 650  ? -27.90400  86.08800  -2.44000  1.000 53.30267  ?  650  LEU   A CA  1 
ATOM   5102  C  C   . LEU   A 1 650  ? -28.83800  86.76900  -3.43200  1.000 46.71603  ?  650  LEU   A C   1 
ATOM   5103  O  O   . LEU   A 1 650  ? -28.41500  87.06000  -4.56200  1.000 53.86219  ?  650  LEU   A O   1 
ATOM   5104  C  CB  . LEU   A 1 650  ? -26.91500  87.11100  -1.87600  1.000 55.09368  ?  650  LEU   A CB  1 
ATOM   5105  C  CG  . LEU   A 1 650  ? -26.29300  86.83000  -0.50700  1.000 37.09502  ?  650  LEU   A CG  1 
ATOM   5106  C  CD1 . LEU   A 1 650  ? -25.37900  87.97100  -0.09100  1.000 33.45768  ?  650  LEU   A CD1 1 
ATOM   5107  C  CD2 . LEU   A 1 650  ? -27.37600  86.60000  0.53500   1.000 55.92030  ?  650  LEU   A CD2 1 
ATOM   5108  N  N   . PRO   A 1 651  ? -30.08900  87.02600  -3.05200  1.000 52.76490  ?  651  PRO   A N   1 
ATOM   5109  C  CA  . PRO   A 1 651  ? -30.99800  87.77300  -3.93100  1.000 47.60198  ?  651  PRO   A CA  1 
ATOM   5110  C  C   . PRO   A 1 651  ? -30.48900  89.18200  -4.20400  1.000 42.95727  ?  651  PRO   A C   1 
ATOM   5111  O  O   . PRO   A 1 651  ? -29.53700  89.67100  -3.59100  1.000 59.44226  ?  651  PRO   A O   1 
ATOM   5112  C  CB  . PRO   A 1 651  ? -32.32100  87.79000  -3.15400  1.000 35.04509  ?  651  PRO   A CB  1 
ATOM   5113  C  CG  . PRO   A 1 651  ? -31.96000  87.42800  -1.74700  1.000 52.75483  ?  651  PRO   A CG  1 
ATOM   5114  C  CD  . PRO   A 1 651  ? -30.77200  86.52600  -1.84900  1.000 68.22732  ?  651  PRO   A CD  1 
ATOM   5115  N  N   . ASP   A 1 652  ? -31.16000  89.84700  -5.14800  1.000 60.26372  ?  652  ASP   A N   1 
ATOM   5116  C  CA  . ASP   A 1 652  ? -30.65100  91.11300  -5.66900  1.000 56.09689  ?  652  ASP   A CA  1 
ATOM   5117  C  C   . ASP   A 1 652  ? -30.77400  92.23600  -4.64600  1.000 51.45329  ?  652  ASP   A C   1 
ATOM   5118  O  O   . ASP   A 1 652  ? -29.88000  93.08400  -4.54100  1.000 49.87818  ?  652  ASP   A O   1 
ATOM   5119  C  CB  . ASP   A 1 652  ? -31.38400  91.48000  -6.95900  1.000 54.51053  ?  652  ASP   A CB  1 
ATOM   5120  C  CG  . ASP   A 1 652  ? -30.60700  92.46700  -7.80900  1.000 63.73799  ?  652  ASP   A CG  1 
ATOM   5121  O  OD1 . ASP   A 1 652  ? -29.51700  92.10000  -8.29800  1.000 68.80013  ?  652  ASP   A OD1 1 
ATOM   5122  O  OD2 . ASP   A 1 652  ? -31.08600  93.60600  -7.99300  1.000 72.57411  -1 652  ASP   A OD2 1 
ATOM   5123  N  N   . TYR   A 1 653  ? -31.87000  92.26500  -3.88400  1.000 49.90820  ?  653  TYR   A N   1 
ATOM   5124  C  CA  . TYR   A 1 653  ? -32.04700  93.32700  -2.90000  1.000 51.04551  ?  653  TYR   A CA  1 
ATOM   5125  C  C   . TYR   A 1 653  ? -31.05700  93.23500  -1.74700  1.000 52.69348  ?  653  TYR   A C   1 
ATOM   5126  O  O   . TYR   A 1 653  ? -30.95700  94.18600  -0.96500  1.000 54.71928  ?  653  TYR   A O   1 
ATOM   5127  C  CB  . TYR   A 1 653  ? -33.48100  93.32300  -2.36100  1.000 46.10728  ?  653  TYR   A CB  1 
ATOM   5128  C  CG  . TYR   A 1 653  ? -33.98300  91.97300  -1.89600  1.000 45.07304  ?  653  TYR   A CG  1 
ATOM   5129  C  CD1 . TYR   A 1 653  ? -33.76900  91.53900  -0.59400  1.000 45.51768  ?  653  TYR   A CD1 1 
ATOM   5130  C  CD2 . TYR   A 1 653  ? -34.68800  91.14100  -2.75600  1.000 51.03814  ?  653  TYR   A CD2 1 
ATOM   5131  C  CE1 . TYR   A 1 653  ? -34.23300  90.30700  -0.16500  1.000 57.56118  ?  653  TYR   A CE1 1 
ATOM   5132  C  CE2 . TYR   A 1 653  ? -35.15600  89.90900  -2.33600  1.000 63.42276  ?  653  TYR   A CE2 1 
ATOM   5133  C  CZ  . TYR   A 1 653  ? -34.92600  89.49700  -1.04000  1.000 60.97662  ?  653  TYR   A CZ  1 
ATOM   5134  O  OH  . TYR   A 1 653  ? -35.39100  88.27100  -0.61900  1.000 42.03513  ?  653  TYR   A OH  1 
ATOM   5135  N  N   . MET   A 1 654  ? -30.32700  92.12800  -1.62400  1.000 47.74101  ?  654  MET   A N   1 
ATOM   5136  C  CA  . MET   A 1 654  ? -29.26600  92.00400  -0.63600  1.000 45.33280  ?  654  MET   A CA  1 
ATOM   5137  C  C   . MET   A 1 654  ? -27.87700  92.09300  -1.25100  1.000 52.15664  ?  654  MET   A C   1 
ATOM   5138  O  O   . MET   A 1 654  ? -26.88500  91.90500  -0.54000  1.000 61.78188  ?  654  MET   A O   1 
ATOM   5139  C  CB  . MET   A 1 654  ? -29.41400  90.69400  0.14600   1.000 47.23170  ?  654  MET   A CB  1 
ATOM   5140  C  CG  . MET   A 1 654  ? -30.51200  90.74900  1.19600   1.000 64.03143  ?  654  MET   A CG  1 
ATOM   5141  S  SD  . MET   A 1 654  ? -30.23900  89.64200  2.59200   1.000 69.20384  ?  654  MET   A SD  1 
ATOM   5142  C  CE  . MET   A 1 654  ? -31.02500  88.15200  1.99800   1.000 36.71945  ?  654  MET   A CE  1 
ATOM   5143  N  N   . ILE   A 1 655  ? -27.77900  92.36800  -2.54600  1.000 56.99340  ?  655  ILE   A N   1 
ATOM   5144  C  CA  . ILE   A 1 655  ? -26.50600  92.67200  -3.19100  1.000 40.55398  ?  655  ILE   A CA  1 
ATOM   5145  C  C   . ILE   A 1 655  ? -26.30900  94.18400  -3.12300  1.000 42.85758  ?  655  ILE   A C   1 
ATOM   5146  O  O   . ILE   A 1 655  ? -27.14100  94.92700  -3.66800  1.000 50.48399  ?  655  ILE   A O   1 
ATOM   5147  C  CB  . ILE   A 1 655  ? -26.47500  92.17900  -4.64200  1.000 42.64676  ?  655  ILE   A CB  1 
ATOM   5148  C  CG1 . ILE   A 1 655  ? -26.60600  90.65500  -4.68700  1.000 39.38095  ?  655  ILE   A CG1 1 
ATOM   5149  C  CG2 . ILE   A 1 655  ? -25.19300  92.62500  -5.32900  1.000 42.72337  ?  655  ILE   A CG2 1 
ATOM   5150  C  CD1 . ILE   A 1 655  ? -26.66900  90.08900  -6.08600  1.000 51.71352  ?  655  ILE   A CD1 1 
ATOM   5151  N  N   . PRO   A 1 656  ? -25.25900  94.67300  -2.46200  1.000 46.46266  ?  656  PRO   A N   1 
ATOM   5152  C  CA  . PRO   A 1 656  ? -25.10500  96.12200  -2.28900  1.000 33.15538  ?  656  PRO   A CA  1 
ATOM   5153  C  C   . PRO   A 1 656  ? -25.04600  96.85600  -3.62000  1.000 43.44504  ?  656  PRO   A C   1 
ATOM   5154  O  O   . PRO   A 1 656  ? -24.52700  96.35000  -4.61700  1.000 50.24665  ?  656  PRO   A O   1 
ATOM   5155  C  CB  . PRO   A 1 656  ? -23.78300  96.24800  -1.52400  1.000 31.54703  ?  656  PRO   A CB  1 
ATOM   5156  C  CG  . PRO   A 1 656  ? -23.64200  94.94500  -0.81000  1.000 40.53522  ?  656  PRO   A CG  1 
ATOM   5157  C  CD  . PRO   A 1 656  ? -24.23000  93.91600  -1.73200  1.000 43.69339  ?  656  PRO   A CD  1 
ATOM   5158  N  N   . THR   A 1 657  ? -25.60300  98.06900  -3.62100  1.000 49.52391  ?  657  THR   A N   1 
ATOM   5159  C  CA  . THR   A 1 657  ? -25.58800  98.89700  -4.82000  1.000 49.78791  ?  657  THR   A CA  1 
ATOM   5160  C  C   . THR   A 1 657  ? -24.20800  99.48900  -5.07800  1.000 49.66594  ?  657  THR   A C   1 
ATOM   5161  O  O   . THR   A 1 657  ? -23.81000  99.64900  -6.23800  1.000 47.62038  ?  657  THR   A O   1 
ATOM   5162  C  CB  . THR   A 1 657  ? -26.62600  100.01300 -4.69700  1.000 55.47736  ?  657  THR   A CB  1 
ATOM   5163  O  OG1 . THR   A 1 657  ? -27.88100  99.45800  -4.28000  1.000 50.88675  ?  657  THR   A OG1 1 
ATOM   5164  C  CG2 . THR   A 1 657  ? -26.81100  100.72100 -6.03000  1.000 48.18649  ?  657  THR   A CG2 1 
ATOM   5165  N  N   . TYR   A 1 658  ? -23.46600  99.81400  -4.02100  1.000 57.47772  ?  658  TYR   A N   1 
ATOM   5166  C  CA  . TYR   A 1 658  ? -22.13900  100.39600 -4.14400  1.000 57.35201  ?  658  TYR   A CA  1 
ATOM   5167  C  C   . TYR   A 1 658  ? -21.13900  99.58400  -3.33500  1.000 49.31532  ?  658  TYR   A C   1 
ATOM   5168  O  O   . TYR   A 1 658  ? -21.46200  99.04800  -2.27200  1.000 42.90630  ?  658  TYR   A O   1 
ATOM   5169  C  CB  . TYR   A 1 658  ? -22.11500  101.85700 -3.67200  1.000 58.21923  ?  658  TYR   A CB  1 
ATOM   5170  C  CG  . TYR   A 1 658  ? -23.12300  102.73900 -4.36800  1.000 68.02617  ?  658  TYR   A CG  1 
ATOM   5171  C  CD1 . TYR   A 1 658  ? -22.84300  103.30800 -5.60500  1.000 70.11235  ?  658  TYR   A CD1 1 
ATOM   5172  C  CD2 . TYR   A 1 658  ? -24.35500  103.00500 -3.78900  1.000 67.07607  ?  658  TYR   A CD2 1 
ATOM   5173  C  CE1 . TYR   A 1 658  ? -23.76400  104.11500 -6.24300  1.000 69.93504  ?  658  TYR   A CE1 1 
ATOM   5174  C  CE2 . TYR   A 1 658  ? -25.28100  103.81000 -4.41900  1.000 75.81985  ?  658  TYR   A CE2 1 
ATOM   5175  C  CZ  . TYR   A 1 658  ? -24.98100  104.36100 -5.64500  1.000 74.49392  ?  658  TYR   A CZ  1 
ATOM   5176  O  OH  . TYR   A 1 658  ? -25.90400  105.16500 -6.27200  1.000 70.73091  ?  658  TYR   A OH  1 
ATOM   5177  N  N   . PHE   A 1 659  ? -19.91700  99.50000  -3.85500  1.000 49.21242  ?  659  PHE   A N   1 
ATOM   5178  C  CA  . PHE   A 1 659  ? -18.80900  98.84400  -3.18000  1.000 38.11958  ?  659  PHE   A CA  1 
ATOM   5179  C  C   . PHE   A 1 659  ? -17.65400  99.82600  -3.04600  1.000 45.47935  ?  659  PHE   A C   1 
ATOM   5180  O  O   . PHE   A 1 659  ? -17.32300  100.54100 -3.99700  1.000 55.35689  ?  659  PHE   A O   1 
ATOM   5181  C  CB  . PHE   A 1 659  ? -18.35200  97.59600  -3.94100  1.000 42.79952  ?  659  PHE   A CB  1 
ATOM   5182  C  CG  . PHE   A 1 659  ? -19.38500  96.50600  -3.99900  1.000 49.22108  ?  659  PHE   A CG  1 
ATOM   5183  C  CD1 . PHE   A 1 659  ? -19.50300  95.59000  -2.96700  1.000 47.46324  ?  659  PHE   A CD1 1 
ATOM   5184  C  CD2 . PHE   A 1 659  ? -20.23300  96.39400  -5.08800  1.000 57.89632  ?  659  PHE   A CD2 1 
ATOM   5185  C  CE1 . PHE   A 1 659  ? -20.44900  94.58500  -3.01800  1.000 36.50588  ?  659  PHE   A CE1 1 
ATOM   5186  C  CE2 . PHE   A 1 659  ? -21.18200  95.39000  -5.14400  1.000 52.82445  ?  659  PHE   A CE2 1 
ATOM   5187  C  CZ  . PHE   A 1 659  ? -21.29000  94.48500  -4.10800  1.000 45.37358  ?  659  PHE   A CZ  1 
ATOM   5188  N  N   . VAL   A 1 660  ? -17.04500  99.85800  -1.86500  1.000 56.56442  ?  660  VAL   A N   1 
ATOM   5189  C  CA  . VAL   A 1 660  ? -15.95000  100.77300 -1.56100  1.000 61.71424  ?  660  VAL   A CA  1 
ATOM   5190  C  C   . VAL   A 1 660  ? -14.74000  99.94700  -1.14700  1.000 55.29410  ?  660  VAL   A C   1 
ATOM   5191  O  O   . VAL   A 1 660  ? -14.82000  99.14900  -0.20500  1.000 51.63778  ?  660  VAL   A O   1 
ATOM   5192  C  CB  . VAL   A 1 660  ? -16.33200  101.77500 -0.46000  1.000 51.46487  ?  660  VAL   A CB  1 
ATOM   5193  C  CG1 . VAL   A 1 660  ? -15.11400  102.56500 -0.01200  1.000 46.31530  ?  660  VAL   A CG1 1 
ATOM   5194  C  CG2 . VAL   A 1 660  ? -17.42800  102.70900 -0.95400  1.000 55.11157  ?  660  VAL   A CG2 1 
ATOM   5195  N  N   . HIS   A 1 661  ? -13.62500  100.13800 -1.84800  1.000 61.48264  ?  661  HIS   A N   1 
ATOM   5196  C  CA  . HIS   A 1 661  ? -12.38100  99.45100  -1.53000  1.000 60.48809  ?  661  HIS   A CA  1 
ATOM   5197  C  C   . HIS   A 1 661  ? -11.56900  100.26200 -0.52900  1.000 65.23497  ?  661  HIS   A C   1 
ATOM   5198  O  O   . HIS   A 1 661  ? -11.50900  101.49200 -0.60900  1.000 67.10083  ?  661  HIS   A O   1 
ATOM   5199  C  CB  . HIS   A 1 661  ? -11.55300  99.20700  -2.79100  1.000 60.59183  ?  661  HIS   A CB  1 
ATOM   5200  C  CG  . HIS   A 1 661  ? -10.15600  98.75000  -2.51100  1.000 64.41568  ?  661  HIS   A CG  1 
ATOM   5201  N  ND1 . HIS   A 1 661  ? -9.05700   99.56100  -2.69500  1.000 69.69498  ?  661  HIS   A ND1 1 
ATOM   5202  C  CD2 . HIS   A 1 661  ? -9.67900   97.57000  -2.04700  1.000 77.39934  ?  661  HIS   A CD2 1 
ATOM   5203  C  CE1 . HIS   A 1 661  ? -7.96300   98.89800  -2.36400  1.000 73.85210  ?  661  HIS   A CE1 1 
ATOM   5204  N  NE2 . HIS   A 1 661  ? -8.31300   97.68800  -1.96700  1.000 73.33327  ?  661  HIS   A NE2 1 
ATOM   5205  N  N   . MET   A 1 662  ? -10.94300  99.56000  0.41400   1.000 64.41923  ?  662  MET   A N   1 
ATOM   5206  C  CA  . MET   A 1 662  ? -10.21500  100.19400 1.50100   1.000 59.94698  ?  662  MET   A CA  1 
ATOM   5207  C  C   . MET   A 1 662  ? -8.88100   99.49200  1.70100   1.000 77.81859  ?  662  MET   A C   1 
ATOM   5208  O  O   . MET   A 1 662  ? -8.75000   98.29000  1.45400   1.000 79.22930  ?  662  MET   A O   1 
ATOM   5209  C  CB  . MET   A 1 662  ? -11.01600  100.15100 2.80700   1.000 57.22161  ?  662  MET   A CB  1 
ATOM   5210  C  CG  . MET   A 1 662  ? -12.48500  100.46700 2.62900   1.000 56.93155  ?  662  MET   A CG  1 
ATOM   5211  S  SD  . MET   A 1 662  ? -12.85600  102.19500 2.93400   1.000 76.21212  ?  662  MET   A SD  1 
ATOM   5212  C  CE  . MET   A 1 662  ? -13.16700  102.10800 4.69200   1.000 58.60801  ?  662  MET   A CE  1 
ATOM   5213  N  N   . LYS   A 1 663  ? -7.88900   100.25800 2.15500   1.000 69.97539  ?  663  LYS   A N   1 
ATOM   5214  C  CA  . LYS   A 1 663  ? -6.60600   99.67000  2.52300   1.000 52.40087  ?  663  LYS   A CA  1 
ATOM   5215  C  C   . LYS   A 1 663  ? -6.66500   99.05800  3.91600   1.000 59.57213  ?  663  LYS   A C   1 
ATOM   5216  O  O   . LYS   A 1 663  ? -6.09600   97.98700  4.15400   1.000 55.72559  ?  663  LYS   A O   1 
ATOM   5217  C  CB  . LYS   A 1 663  ? -5.50600   100.72800 2.45600   1.000 73.19356  ?  663  LYS   A CB  1 
ATOM   5218  C  CG  . LYS   A 1 663  ? -5.72200   101.79100 1.39100   1.000 76.93877  ?  663  LYS   A CG  1 
ATOM   5219  C  CD  . LYS   A 1 663  ? -4.93500   101.49200 0.12800   1.000 69.59164  ?  663  LYS   A CD  1 
ATOM   5220  C  CE  . LYS   A 1 663  ? -4.85600   102.72300 -0.76200  1.000 74.43987  ?  663  LYS   A CE  1 
ATOM   5221  N  NZ  . LYS   A 1 663  ? -3.59200   102.76200 -1.55000  1.000 71.11558  ?  663  LYS   A NZ  1 
ATOM   5222  N  N   . ALA   A 1 664  ? -7.34800   99.72700  4.84300   1.000 61.86939  ?  664  ALA   A N   1 
ATOM   5223  C  CA  . ALA   A 1 664  ? -7.51200   99.24500  6.20500   1.000 49.67743  ?  664  ALA   A CA  1 
ATOM   5224  C  C   . ALA   A 1 664  ? -8.71800   99.93800  6.82100   1.000 53.34215  ?  664  ALA   A C   1 
ATOM   5225  O  O   . ALA   A 1 664  ? -8.97600   101.11100 6.53700   1.000 63.63859  ?  664  ALA   A O   1 
ATOM   5226  C  CB  . ALA   A 1 664  ? -6.25800   99.50200  7.04800   1.000 58.03185  ?  664  ALA   A CB  1 
ATOM   5227  N  N   . PHE   A 1 665  ? -9.44900   99.20900  7.66000   1.000 58.07433  ?  665  PHE   A N   1 
ATOM   5228  C  CA  . PHE   A 1 665  ? -10.65300  99.75800  8.27100   1.000 63.06666  ?  665  PHE   A CA  1 
ATOM   5229  C  C   . PHE   A 1 665  ? -10.29200  100.68000 9.43500   1.000 59.91360  ?  665  PHE   A C   1 
ATOM   5230  O  O   . PHE   A 1 665  ? -9.39700   100.36500 10.22400  1.000 54.17120  ?  665  PHE   A O   1 
ATOM   5231  C  CB  . PHE   A 1 665  ? -11.56300  98.63700  8.77000   1.000 68.77437  ?  665  PHE   A CB  1 
ATOM   5232  C  CG  . PHE   A 1 665  ? -12.55100  98.15200  7.74700   1.000 72.76383  ?  665  PHE   A CG  1 
ATOM   5233  C  CD1 . PHE   A 1 665  ? -12.87900  98.93600  6.65300   1.000 66.14432  ?  665  PHE   A CD1 1 
ATOM   5234  C  CD2 . PHE   A 1 665  ? -13.16000  96.91400  7.88500   1.000 65.09286  ?  665  PHE   A CD2 1 
ATOM   5235  C  CE1 . PHE   A 1 665  ? -13.79100  98.49200  5.71300   1.000 65.54404  ?  665  PHE   A CE1 1 
ATOM   5236  C  CE2 . PHE   A 1 665  ? -14.07300  96.46500  6.94900   1.000 53.05565  ?  665  PHE   A CE2 1 
ATOM   5237  C  CZ  . PHE   A 1 665  ? -14.38900  97.25500  5.86200   1.000 61.85449  ?  665  PHE   A CZ  1 
ATOM   5238  N  N   . PRO   A 1 666  ? -10.96200  101.82400 9.55800   1.000 55.22490  ?  666  PRO   A N   1 
ATOM   5239  C  CA  . PRO   A 1 666  ? -10.75900  102.67100 10.73900  1.000 58.60281  ?  666  PRO   A CA  1 
ATOM   5240  C  C   . PRO   A 1 666  ? -11.37200  102.03600 11.97800  1.000 79.12619  ?  666  PRO   A C   1 
ATOM   5241  O  O   . PRO   A 1 666  ? -12.46200  101.46100 11.93000  1.000 72.41951  ?  666  PRO   A O   1 
ATOM   5242  C  CB  . PRO   A 1 666  ? -11.47100  103.97900 10.37200  1.000 67.75605  ?  666  PRO   A CB  1 
ATOM   5243  C  CG  . PRO   A 1 666  ? -11.64200  103.93000 8.88100   1.000 78.93001  ?  666  PRO   A CG  1 
ATOM   5244  C  CD  . PRO   A 1 666  ? -11.80200  102.48200 8.54500   1.000 64.11996  ?  666  PRO   A CD  1 
ATOM   5245  N  N   . LEU   A 1 667  ? -10.66100  102.15100 13.09700  1.000 81.79715  ?  667  LEU   A N   1 
ATOM   5246  C  CA  . LEU   A 1 667  ? -11.08600  101.57200 14.36400  1.000 67.82015  ?  667  LEU   A CA  1 
ATOM   5247  C  C   . LEU   A 1 667  ? -11.29900  102.66900 15.39600  1.000 65.15771  ?  667  LEU   A C   1 
ATOM   5248  O  O   . LEU   A 1 667  ? -10.46400  103.57000 15.53100  1.000 66.32469  ?  667  LEU   A O   1 
ATOM   5249  C  CB  . LEU   A 1 667  ? -10.05700  100.56700 14.89000  1.000 55.56809  ?  667  LEU   A CB  1 
ATOM   5250  C  CG  . LEU   A 1 667  ? -10.18900  99.10900  14.45500  1.000 64.69257  ?  667  LEU   A CG  1 
ATOM   5251  C  CD1 . LEU   A 1 667  ? -9.69200   98.90900  13.03700  1.000 59.67579  ?  667  LEU   A CD1 1 
ATOM   5252  C  CD2 . LEU   A 1 667  ? -9.43500   98.21900  15.41900  1.000 56.40169  ?  667  LEU   A CD2 1 
ATOM   5253  N  N   . THR   A 1 668  ? -12.41000  102.58600 16.12400  1.000 69.41348  ?  668  THR   A N   1 
ATOM   5254  C  CA  . THR   A 1 668  ? -12.60200  103.44900 17.27700  1.000 70.39991  ?  668  THR   A CA  1 
ATOM   5255  C  C   . THR   A 1 668  ? -11.61500  103.07200 18.37600  1.000 81.34198  ?  668  THR   A C   1 
ATOM   5256  O  O   . THR   A 1 668  ? -11.03300  101.98300 18.38100  1.000 89.15288  ?  668  THR   A O   1 
ATOM   5257  C  CB  . THR   A 1 668  ? -14.03100  103.34500 17.81700  1.000 58.19394  ?  668  THR   A CB  1 
ATOM   5258  O  OG1 . THR   A 1 668  ? -14.14300  102.19600 18.66500  1.000 74.04153  ?  668  THR   A OG1 1 
ATOM   5259  C  CG2 . THR   A 1 668  ? -15.02300  103.21500 16.68300  1.000 64.90884  ?  668  THR   A CG2 1 
ATOM   5260  N  N   . ALA   A 1 669  ? -11.43300  103.99200 19.32600  1.000 79.90349  ?  669  ALA   A N   1 
ATOM   5261  C  CA  . ALA   A 1 669  ? -10.55700  103.71600 20.45700  1.000 73.54804  ?  669  ALA   A CA  1 
ATOM   5262  C  C   . ALA   A 1 669  ? -11.04700  102.53700 21.28600  1.000 87.07309  ?  669  ALA   A C   1 
ATOM   5263  O  O   . ALA   A 1 669  ? -10.26500  101.96400 22.05400  1.000 101.69232 ?  669  ALA   A O   1 
ATOM   5264  C  CB  . ALA   A 1 669  ? -10.42600  104.95900 21.33800  1.000 92.00803  ?  669  ALA   A CB  1 
ATOM   5265  N  N   . ASN   A 1 670  ? -12.31700  102.15800 21.14300  1.000 77.25396  ?  670  ASN   A N   1 
ATOM   5266  C  CA  . ASN   A 1 670  ? -12.87000  101.01100 21.84900  1.000 84.30926  ?  670  ASN   A CA  1 
ATOM   5267  C  C   . ASN   A 1 670  ? -12.50700  99.68300  21.19800  1.000 84.51463  ?  670  ASN   A C   1 
ATOM   5268  O  O   . ASN   A 1 670  ? -12.83400  98.63000  21.75800  1.000 68.94407  ?  670  ASN   A O   1 
ATOM   5269  C  CB  . ASN   A 1 670  ? -14.39100  101.13700 21.93400  1.000 81.88749  ?  670  ASN   A CB  1 
ATOM   5270  C  CG  . ASN   A 1 670  ? -14.84000  102.56000 22.18900  1.000 96.67759  ?  670  ASN   A CG  1 
ATOM   5271  O  OD1 . ASN   A 1 670  ? -14.17500  103.31500 22.89900  1.000 87.86331  ?  670  ASN   A OD1 1 
ATOM   5272  N  ND2 . ASN   A 1 670  ? -15.97000  102.93900 21.60200  1.000 92.57270  ?  670  ASN   A ND2 1 
ATOM   5273  N  N   . GLY   A 1 671  ? -11.85300  99.70500  20.03900  1.000 79.64570  ?  671  GLY   A N   1 
ATOM   5274  C  CA  . GLY   A 1 671  ? -11.46000  98.49400  19.35000  1.000 71.37850  ?  671  GLY   A CA  1 
ATOM   5275  C  C   . GLY   A 1 671  ? -12.42900  97.99400  18.30200  1.000 69.35669  ?  671  GLY   A C   1 
ATOM   5276  O  O   . GLY   A 1 671  ? -12.27200  96.86100  17.83200  1.000 69.67758  ?  671  GLY   A O   1 
ATOM   5277  N  N   . LYS   A 1 672  ? -13.42000  98.79300  17.92100  1.000 59.64749  ?  672  LYS   A N   1 
ATOM   5278  C  CA  . LYS   A 1 672  ? -14.42400  98.40300  16.94400  1.000 53.06756  ?  672  LYS   A CA  1 
ATOM   5279  C  C   . LYS   A 1 672  ? -14.28300  99.25000  15.68700  1.000 58.84171  ?  672  LYS   A C   1 
ATOM   5280  O  O   . LYS   A 1 672  ? -13.67300  100.32200 15.70200  1.000 68.72813  ?  672  LYS   A O   1 
ATOM   5281  C  CB  . LYS   A 1 672  ? -15.83500  98.55600  17.52200  1.000 65.33478  ?  672  LYS   A CB  1 
ATOM   5282  C  CG  . LYS   A 1 672  ? -16.02100  97.89900  18.88100  1.000 61.41429  ?  672  LYS   A CG  1 
ATOM   5283  C  CD  . LYS   A 1 672  ? -16.99300  98.68800  19.74700  1.000 50.36312  ?  672  LYS   A CD  1 
ATOM   5284  C  CE  . LYS   A 1 672  ? -18.41500  98.61800  19.21600  1.000 58.03413  ?  672  LYS   A CE  1 
ATOM   5285  N  NZ  . LYS   A 1 672  ? -19.23500  97.62200  19.96000  1.000 61.00860  ?  672  LYS   A NZ  1 
ATOM   5286  N  N   . VAL   A 1 673  ? -14.85700  98.75400  14.58800  1.000 68.86418  ?  673  VAL   A N   1 
ATOM   5287  C  CA  . VAL   A 1 673  ? -14.83600  99.51200  13.34300  1.000 74.51873  ?  673  VAL   A CA  1 
ATOM   5288  C  C   . VAL   A 1 673  ? -15.60300  100.81300 13.53600  1.000 74.91847  ?  673  VAL   A C   1 
ATOM   5289  O  O   . VAL   A 1 673  ? -16.64800  100.84800 14.19900  1.000 68.57665  ?  673  VAL   A O   1 
ATOM   5290  C  CB  . VAL   A 1 673  ? -15.42600  98.67700  12.19500  1.000 66.14439  ?  673  VAL   A CB  1 
ATOM   5291  C  CG1 . VAL   A 1 673  ? -15.08000  99.30300  10.85200  1.000 64.82174  ?  673  VAL   A CG1 1 
ATOM   5292  C  CG2 . VAL   A 1 673  ? -14.91900  97.24700  12.26900  1.000 59.03658  ?  673  VAL   A CG2 1 
ATOM   5293  N  N   . ASP   A 1 674  ? -15.08000  101.89800 12.95800  1.000 65.52973  ?  674  ASP   A N   1 
ATOM   5294  C  CA  . ASP   A 1 674  ? -15.66000  103.21400 13.21500  1.000 67.85081  ?  674  ASP   A CA  1 
ATOM   5295  C  C   . ASP   A 1 674  ? -17.08700  103.31600 12.68700  1.000 83.01007  ?  674  ASP   A C   1 
ATOM   5296  O  O   . ASP   A 1 674  ? -17.94000  103.94500 13.32500  1.000 78.19237  ?  674  ASP   A O   1 
ATOM   5297  C  CB  . ASP   A 1 674  ? -14.78200  104.30700 12.61000  1.000 76.33536  ?  674  ASP   A CB  1 
ATOM   5298  C  CG  . ASP   A 1 674  ? -14.78800  105.57900 13.43700  1.000 83.17122  ?  674  ASP   A CG  1 
ATOM   5299  O  OD1 . ASP   A 1 674  ? -15.85200  105.92700 13.99100  1.000 87.25135  ?  674  ASP   A OD1 1 
ATOM   5300  O  OD2 . ASP   A 1 674  ? -13.72400  106.22300 13.54600  1.000 80.61394  -1 674  ASP   A OD2 1 
ATOM   5301  N  N   . ARG   A 1 675  ? -17.36400  102.71300 11.52700  1.000 81.65713  ?  675  ARG   A N   1 
ATOM   5302  C  CA  . ARG   A 1 675  ? -18.70000  102.69100 10.92200  1.000 69.19442  ?  675  ARG   A CA  1 
ATOM   5303  C  C   . ARG   A 1 675  ? -19.30600  104.08900 10.79700  1.000 76.40295  ?  675  ARG   A C   1 
ATOM   5304  O  O   . ARG   A 1 675  ? -20.53200  104.24200 10.75900  1.000 109.95822 ?  675  ARG   A O   1 
ATOM   5305  C  CB  . ARG   A 1 675  ? -19.64800  101.76900 11.70100  1.000 55.63762  ?  675  ARG   A CB  1 
ATOM   5306  C  CG  . ARG   A 1 675  ? -19.29300  100.29500 11.60500  1.000 76.64889  ?  675  ARG   A CG  1 
ATOM   5307  C  CD  . ARG   A 1 675  ? -20.13000  99.45800  12.55900  1.000 61.65898  ?  675  ARG   A CD  1 
ATOM   5308  N  NE  . ARG   A 1 675  ? -21.55900  99.65700  12.35500  1.000 84.10914  ?  675  ARG   A NE  1 
ATOM   5309  C  CZ  . ARG   A 1 675  ? -22.34000  98.84800  11.65200  1.000 85.97153  ?  675  ARG   A CZ  1 
ATOM   5310  N  NH1 . ARG   A 1 675  ? -21.86400  97.75600  11.07600  1.000 82.88046  ?  675  ARG   A NH1 1 
ATOM   5311  N  NH2 . ARG   A 1 675  ? -23.63100  99.14200  11.52400  1.000 62.55937  ?  675  ARG   A NH2 1 
ATOM   5312  N  N   . ARG   A 1 676  ? -18.45400  105.11200 10.73400  1.000 75.50255  ?  676  ARG   A N   1 
ATOM   5313  C  CA  . ARG   A 1 676  ? -18.87400  106.50100 10.60800  1.000 66.03123  ?  676  ARG   A CA  1 
ATOM   5314  C  C   . ARG   A 1 676  ? -17.75800  107.28500 9.92800   1.000 74.36556  ?  676  ARG   A C   1 
ATOM   5315  O  O   . ARG   A 1 676  ? -18.00000  108.33000 9.31600   1.000 99.49893  ?  676  ARG   A O   1 
ATOM   5316  C  CB  . ARG   A 1 676  ? -19.21500  107.09700 11.97600  1.000 59.63860  ?  676  ARG   A CB  1 
ATOM   5317  N  N   . ALA   A 1 677  ? -16.52900  106.77800 10.03500  1.000 63.06767  ?  677  ALA   A N   1 
ATOM   5318  C  CA  . ALA   A 1 677  ? -15.41400  107.25600 9.23400   1.000 60.91272  ?  677  ALA   A CA  1 
ATOM   5319  C  C   . ALA   A 1 677  ? -15.33600  106.57500 7.87500   1.000 59.50977  ?  677  ALA   A C   1 
ATOM   5320  O  O   . ALA   A 1 677  ? -14.61300  107.06100 6.99700   1.000 74.49281  ?  677  ALA   A O   1 
ATOM   5321  C  CB  . ALA   A 1 677  ? -14.09200  107.05100 9.98100   1.000 84.08778  ?  677  ALA   A CB  1 
ATOM   5322  N  N   . LEU   A 1 678  ? -16.05700  105.47000 7.68500   1.000 72.97529  ?  678  LEU   A N   1 
ATOM   5323  C  CA  . LEU   A 1 678  ? -16.08100  104.79400 6.39400   1.000 64.95411  ?  678  LEU   A CA  1 
ATOM   5324  C  C   . LEU   A 1 678  ? -16.53700  105.77000 5.31200   1.000 60.78133  ?  678  LEU   A C   1 
ATOM   5325  O  O   . LEU   A 1 678  ? -17.54900  106.46100 5.49700   1.000 68.43773  ?  678  LEU   A O   1 
ATOM   5326  C  CB  . LEU   A 1 678  ? -17.01100  103.58100 6.44400   1.000 66.05194  ?  678  LEU   A CB  1 
ATOM   5327  C  CG  . LEU   A 1 678  ? -16.76500  102.59600 7.59000   1.000 64.88374  ?  678  LEU   A CG  1 
ATOM   5328  C  CD1 . LEU   A 1 678  ? -17.67000  101.37600 7.47600   1.000 55.64713  ?  678  LEU   A CD1 1 
ATOM   5329  C  CD2 . LEU   A 1 678  ? -15.30200  102.18000 7.65400   1.000 58.17307  ?  678  LEU   A CD2 1 
ATOM   5330  N  N   . PRO   A 1 679  ? -15.82000  105.86800 4.19200   1.000 56.52664  ?  679  PRO   A N   1 
ATOM   5331  C  CA  . PRO   A 1 679  ? -16.14000  106.88900 3.18700   1.000 48.95959  ?  679  PRO   A CA  1 
ATOM   5332  C  C   . PRO   A 1 679  ? -17.58400  106.80100 2.71400   1.000 60.95514  ?  679  PRO   A C   1 
ATOM   5333  O  O   . PRO   A 1 679  ? -18.20800  105.73900 2.73500   1.000 68.97696  ?  679  PRO   A O   1 
ATOM   5334  C  CB  . PRO   A 1 679  ? -15.16200  106.57900 2.04900   1.000 44.04394  ?  679  PRO   A CB  1 
ATOM   5335  C  CG  . PRO   A 1 679  ? -14.00400  105.93400 2.72000   1.000 68.11877  ?  679  PRO   A CG  1 
ATOM   5336  C  CD  . PRO   A 1 679  ? -14.55300  105.17500 3.89900   1.000 60.70269  ?  679  PRO   A CD  1 
ATOM   5337  N  N   . ASP   A 1 680  ? -18.11500  107.94400 2.30200   1.000 57.13052  ?  680  ASP   A N   1 
ATOM   5338  C  CA  . ASP   A 1 680  ? -19.43600  108.00900 1.70500   1.000 59.33805  ?  680  ASP   A CA  1 
ATOM   5339  C  C   . ASP   A 1 680  ? -19.31500  108.01400 0.18800   1.000 80.26507  ?  680  ASP   A C   1 
ATOM   5340  O  O   . ASP   A 1 680  ? -18.23700  108.20400 -0.38000  1.000 60.26707  ?  680  ASP   A O   1 
ATOM   5341  C  CB  . ASP   A 1 680  ? -20.19600  109.24700 2.19000   1.000 55.62088  ?  680  ASP   A CB  1 
ATOM   5342  C  CG  . ASP   A 1 680  ? -21.58000  108.90800 2.69700   1.000 91.40043  ?  680  ASP   A CG  1 
ATOM   5343  O  OD1 . ASP   A 1 680  ? -22.30400  108.16800 1.99700   1.000 81.31672  ?  680  ASP   A OD1 1 
ATOM   5344  O  OD2 . ASP   A 1 680  ? -21.93900  109.36800 3.80200   1.000 87.62047  -1 680  ASP   A OD2 1 
ATOM   5345  N  N   . VAL   A 1 681  ? -20.44900  107.79400 -0.47000  1.000 83.20930  ?  681  VAL   A N   1 
ATOM   5346  C  CA  . VAL   A 1 681  ? -20.47700  107.66900 -1.92000  1.000 82.00086  ?  681  VAL   A CA  1 
ATOM   5347  C  C   . VAL   A 1 681  ? -21.25900  108.83100 -2.51400  1.000 102.62268 ?  681  VAL   A C   1 
ATOM   5348  O  O   . VAL   A 1 681  ? -20.70100  109.90400 -2.77400  1.000 105.48936 ?  681  VAL   A O   1 
ATOM   5349  C  CB  . VAL   A 1 681  ? -21.08800  106.32300 -2.34600  1.000 78.43369  ?  681  VAL   A CB  1 
ATOM   5350  C  CG1 . VAL   A 1 681  ? -20.74000  106.02100 -3.79000  1.000 76.67507  ?  681  VAL   A CG1 1 
ATOM   5351  C  CG2 . VAL   A 1 681  ? -20.61900  105.21000 -1.42600  1.000 66.30515  ?  681  VAL   A CG2 1 
ATOM   5352  N  N   . GLN   A 1 682  ? -22.55100  108.62100 -2.74000  1.000 112.82495 ?  682  GLN   A N   1 
ATOM   5353  C  CA  . GLN   A 1 682  ? -23.41500  109.67000 -3.26600  1.000 98.85955  ?  682  GLN   A CA  1 
ATOM   5354  C  C   . GLN   A 1 682  ? -24.85800  109.44900 -2.81600  1.000 95.86664  ?  682  GLN   A C   1 
ATOM   5355  O  O   . GLN   A 1 682  ? -25.27900  108.31500 -2.58800  1.000 86.34466  ?  682  GLN   A O   1 
ATOM   5356  C  CB  . GLN   A 1 682  ? -23.32400  109.72800 -4.79600  1.000 78.07867  ?  682  GLN   A CB  1 
ATOM   5357  C  CG  . GLN   A 1 682  ? -23.65600  108.42200 -5.51500  1.000 93.49535  ?  682  GLN   A CG  1 
ATOM   5358  C  CD  . GLN   A 1 682  ? -25.15000  108.20400 -5.69300  1.000 92.02842  ?  682  GLN   A CD  1 
ATOM   5359  O  OE1 . GLN   A 1 682  ? -25.79900  108.87800 -6.49400  1.000 81.86886  ?  682  GLN   A OE1 1 
ATOM   5360  N  NE2 . GLN   A 1 682  ? -25.70200  107.26000 -4.94100  1.000 93.78511  ?  682  GLN   A NE2 1 
ATOM   5361  N  N   . GLU   A 1 686  ? -28.34600  110.39300 -6.46600  1.000 90.78160  ?  686  GLU   A N   1 
ATOM   5362  C  CA  . GLU   A 1 686  ? -29.28100  109.29200 -6.66700  1.000 91.08259  ?  686  GLU   A CA  1 
ATOM   5363  C  C   . GLU   A 1 686  ? -28.93200  108.51200 -7.93100  1.000 87.70167  ?  686  GLU   A C   1 
ATOM   5364  O  O   . GLU   A 1 686  ? -29.61700  108.62000 -8.94900  1.000 86.15978  ?  686  GLU   A O   1 
ATOM   5365  C  CB  . GLU   A 1 686  ? -30.72000  109.81300 -6.74400  1.000 76.44160  ?  686  GLU   A CB  1 
ATOM   5366  C  CG  . GLU   A 1 686  ? -31.79200  108.72800 -6.67000  1.000 72.09803  ?  686  GLU   A CG  1 
ATOM   5367  C  CD  . GLU   A 1 686  ? -32.55500  108.74000 -5.35600  1.000 92.64155  ?  686  GLU   A CD  1 
ATOM   5368  O  OE1 . GLU   A 1 686  ? -32.13200  109.45600 -4.42400  1.000 93.86756  ?  686  GLU   A OE1 1 
ATOM   5369  O  OE2 . GLU   A 1 686  ? -33.58300  108.03600 -5.25800  1.000 83.46168  ?  686  GLU   A OE2 1 
ATOM   5370  N  N   . LEU   A 1 687  ? -27.85500  107.73600 -7.86600  1.000 82.57033  ?  687  LEU   A N   1 
ATOM   5371  C  CA  . LEU   A 1 687  ? -27.46000  106.87700 -8.97100  1.000 96.24336  ?  687  LEU   A CA  1 
ATOM   5372  C  C   . LEU   A 1 687  ? -28.08900  105.49800 -8.80500  1.000 101.20744 ?  687  LEU   A C   1 
ATOM   5373  O  O   . LEU   A 1 687  ? -28.32600  105.03200 -7.68700  1.000 95.42295  ?  687  LEU   A O   1 
ATOM   5374  C  CB  . LEU   A 1 687  ? -25.93600  106.75500 -9.05000  1.000 99.45566  ?  687  LEU   A CB  1 
ATOM   5375  C  CG  . LEU   A 1 687  ? -25.34600  106.08300 -10.29400 1.000 89.91322  ?  687  LEU   A CG  1 
ATOM   5376  C  CD1 . LEU   A 1 687  ? -25.43900  107.00400 -11.50200 1.000 104.66615 ?  687  LEU   A CD1 1 
ATOM   5377  C  CD2 . LEU   A 1 687  ? -23.90700  105.64400 -10.05300 1.000 68.90778  ?  687  LEU   A CD2 1 
ATOM   5378  N  N   . LEU   A 1 688  ? -28.36700  104.85000 -9.93600  1.000 86.47692  ?  688  LEU   A N   1 
ATOM   5379  C  CA  . LEU   A 1 688  ? -28.98600  103.53300 -9.94900  1.000 68.47746  ?  688  LEU   A CA  1 
ATOM   5380  C  C   . LEU   A 1 688  ? -27.96000  102.41100 -10.05500 1.000 73.57225  ?  688  LEU   A C   1 
ATOM   5381  O  O   . LEU   A 1 688  ? -28.32400  101.27200 -10.36600 1.000 77.70440  ?  688  LEU   A O   1 
ATOM   5382  C  CB  . LEU   A 1 688  ? -29.99600  103.43600 -11.09300 1.000 75.43452  ?  688  LEU   A CB  1 
ATOM   5383  C  CG  . LEU   A 1 688  ? -31.06200  104.53100 -11.14600 1.000 60.39385  ?  688  LEU   A CG  1 
ATOM   5384  C  CD1 . LEU   A 1 688  ? -30.69100  105.61000 -12.15400 1.000 56.54390  ?  688  LEU   A CD1 1 
ATOM   5385  C  CD2 . LEU   A 1 688  ? -32.41800  103.93500 -11.46600 1.000 67.88966  ?  688  LEU   A CD2 1 
ATOM   5386  N  N   . GLY   A 1 689  ? -26.69100  102.70900 -9.80100  1.000 74.21049  ?  689  GLY   A N   1 
ATOM   5387  C  CA  . GLY   A 1 689  ? -25.63100  101.72800 -9.88100  1.000 72.10482  ?  689  GLY   A CA  1 
ATOM   5388  C  C   . GLY   A 1 689  ? -24.89400  101.78600 -11.20800 1.000 71.43944  ?  689  GLY   A C   1 
ATOM   5389  O  O   . GLY   A 1 689  ? -25.24000  102.53400 -12.12600 1.000 82.30641  ?  689  GLY   A O   1 
ATOM   5390  N  N   . GLU   A 1 690  ? -23.84800  100.96500 -11.29800 1.000 67.68661  ?  690  GLU   A N   1 
ATOM   5391  C  CA  . GLU   A 1 690  ? -23.04900  100.92200 -12.51500 1.000 59.77057  ?  690  GLU   A CA  1 
ATOM   5392  C  C   . GLU   A 1 690  ? -23.63800  99.97300  -13.54900 1.000 59.09046  ?  690  GLU   A C   1 
ATOM   5393  O  O   . GLU   A 1 690  ? -23.42400  100.16300 -14.75100 1.000 76.85429  ?  690  GLU   A O   1 
ATOM   5394  C  CB  . GLU   A 1 690  ? -21.61100  100.52100 -12.18300 1.000 70.25939  ?  690  GLU   A CB  1 
ATOM   5395  C  CG  . GLU   A 1 690  ? -20.99200  101.35500 -11.07300 1.000 80.89811  ?  690  GLU   A CG  1 
ATOM   5396  C  CD  . GLU   A 1 690  ? -19.47800  101.27100 -11.04500 1.000 90.04283  ?  690  GLU   A CD  1 
ATOM   5397  O  OE1 . GLU   A 1 690  ? -18.92300  100.26900 -11.54400 1.000 69.76787  ?  690  GLU   A OE1 1 
ATOM   5398  O  OE2 . GLU   A 1 690  ? -18.84400  102.21500 -10.53000 1.000 104.17234 -1 690  GLU   A OE2 1 
ATOM   5399  N  N   . ASP   A 1 691  ? -24.38300  98.96000  -13.10800 1.000 62.84854  ?  691  ASP   A N   1 
ATOM   5400  C  CA  . ASP   A 1 691  ? -25.00400  98.00800  -14.02100 1.000 68.00834  ?  691  ASP   A CA  1 
ATOM   5401  C  C   . ASP   A 1 691  ? -26.26000  98.55400  -14.68600 1.000 71.04130  ?  691  ASP   A C   1 
ATOM   5402  O  O   . ASP   A 1 691  ? -26.85800  97.85200  -15.50900 1.000 71.95158  ?  691  ASP   A O   1 
ATOM   5403  C  CB  . ASP   A 1 691  ? -25.33700  96.70900  -13.28100 1.000 78.18471  ?  691  ASP   A CB  1 
ATOM   5404  C  CG  . ASP   A 1 691  ? -24.09700  95.94400  -12.85500 1.000 103.82368 ?  691  ASP   A CG  1 
ATOM   5405  O  OD1 . ASP   A 1 691  ? -22.99300  96.52800  -12.89000 1.000 100.65073 ?  691  ASP   A OD1 1 
ATOM   5406  O  OD2 . ASP   A 1 691  ? -24.22500  94.75500  -12.49400 1.000 110.85841 -1 691  ASP   A OD2 1 
ATOM   5407  N  N   . TYR   A 1 692  ? -26.67200  99.77500  -14.35700 1.000 70.55518  ?  692  TYR   A N   1 
ATOM   5408  C  CA  . TYR   A 1 692  ? -27.87600  100.35800 -14.93500 1.000 61.52208  ?  692  TYR   A CA  1 
ATOM   5409  C  C   . TYR   A 1 692  ? -27.55800  100.94200 -16.30600 1.000 50.39154  ?  692  TYR   A C   1 
ATOM   5410  O  O   . TYR   A 1 692  ? -26.69300  101.81600 -16.43100 1.000 59.69823  ?  692  TYR   A O   1 
ATOM   5411  C  CB  . TYR   A 1 692  ? -28.44700  101.43200 -14.00900 1.000 55.32253  ?  692  TYR   A CB  1 
ATOM   5412  C  CG  . TYR   A 1 692  ? -29.61600  102.19500 -14.59700 1.000 53.56098  ?  692  TYR   A CG  1 
ATOM   5413  C  CD1 . TYR   A 1 692  ? -30.91600  101.72500 -14.46300 1.000 62.82034  ?  692  TYR   A CD1 1 
ATOM   5414  C  CD2 . TYR   A 1 692  ? -29.41900  103.38800 -15.28200 1.000 53.05110  ?  692  TYR   A CD2 1 
ATOM   5415  C  CE1 . TYR   A 1 692  ? -31.98700  102.42000 -14.99900 1.000 72.86928  ?  692  TYR   A CE1 1 
ATOM   5416  C  CE2 . TYR   A 1 692  ? -30.48200  104.08800 -15.82200 1.000 55.38578  ?  692  TYR   A CE2 1 
ATOM   5417  C  CZ  . TYR   A 1 692  ? -31.76300  103.60000 -15.67700 1.000 68.33806  ?  692  TYR   A CZ  1 
ATOM   5418  O  OH  . TYR   A 1 692  ? -32.82300  104.29600 -16.21200 1.000 63.88875  ?  692  TYR   A OH  1 
ATOM   5419  N  N   . VAL   A 1 693  ? -28.25500  100.45900 -17.33000 1.000 50.45370  ?  693  VAL   A N   1 
ATOM   5420  C  CA  . VAL   A 1 693  ? -28.17500  101.00500 -18.67900 1.000 45.35092  ?  693  VAL   A CA  1 
ATOM   5421  C  C   . VAL   A 1 693  ? -29.56300  101.50900 -19.04300 1.000 46.18384  ?  693  VAL   A C   1 
ATOM   5422  O  O   . VAL   A 1 693  ? -30.52400  100.73000 -19.06900 1.000 49.91547  ?  693  VAL   A O   1 
ATOM   5423  C  CB  . VAL   A 1 693  ? -27.67800  99.96300  -19.69300 1.000 45.83528  ?  693  VAL   A CB  1 
ATOM   5424  C  CG1 . VAL   A 1 693  ? -27.43700  100.61200 -21.04800 1.000 49.34930  ?  693  VAL   A CG1 1 
ATOM   5425  C  CG2 . VAL   A 1 693  ? -26.41300  99.28600  -19.18300 1.000 40.32786  ?  693  VAL   A CG2 1 
ATOM   5426  N  N   . ALA   A 1 694  ? -29.67200  102.80600 -19.30900 1.000 41.35799  ?  694  ALA   A N   1 
ATOM   5427  C  CA  . ALA   A 1 694  ? -30.97000  103.41400 -19.54600 1.000 43.83651  ?  694  ALA   A CA  1 
ATOM   5428  C  C   . ALA   A 1 694  ? -31.51300  103.03500 -20.92300 1.000 54.62086  ?  694  ALA   A C   1 
ATOM   5429  O  O   . ALA   A 1 694  ? -30.74500  102.75100 -21.84600 1.000 53.98593  ?  694  ALA   A O   1 
ATOM   5430  C  CB  . ALA   A 1 694  ? -30.87300  104.93100 -19.43200 1.000 48.55503  ?  694  ALA   A CB  1 
ATOM   5431  N  N   . PRO   A 1 695  ? -32.83800  103.01600 -21.07800 1.000 50.40645  ?  695  PRO   A N   1 
ATOM   5432  C  CA  . PRO   A 1 695  ? -33.42100  102.74900 -22.39900 1.000 43.10169  ?  695  PRO   A CA  1 
ATOM   5433  C  C   . PRO   A 1 695  ? -32.97700  103.78000 -23.42600 1.000 47.88558  ?  695  PRO   A C   1 
ATOM   5434  O  O   . PRO   A 1 695  ? -32.89600  104.97700 -23.14100 1.000 56.76055  ?  695  PRO   A O   1 
ATOM   5435  C  CB  . PRO   A 1 695  ? -34.93000  102.82400 -22.14100 1.000 45.46491  ?  695  PRO   A CB  1 
ATOM   5436  C  CG  . PRO   A 1 695  ? -35.07500  102.49200 -20.69400 1.000 41.59596  ?  695  PRO   A CG  1 
ATOM   5437  C  CD  . PRO   A 1 695  ? -33.86500  103.07700 -20.02300 1.000 38.89551  ?  695  PRO   A CD  1 
ATOM   5438  N  N   . THR   A 1 696  ? -32.68500  103.29700 -24.63400 1.000 50.45852  ?  696  THR   A N   1 
ATOM   5439  C  CA  . THR   A 1 696  ? -32.21500  104.14900 -25.71600 1.000 48.54682  ?  696  THR   A CA  1 
ATOM   5440  C  C   . THR   A 1 696  ? -33.23000  104.33800 -26.83200 1.000 44.64627  ?  696  THR   A C   1 
ATOM   5441  O  O   . THR   A 1 696  ? -33.08200  105.27300 -27.62500 1.000 60.97835  ?  696  THR   A O   1 
ATOM   5442  C  CB  . THR   A 1 696  ? -30.92100  103.58000 -26.31500 1.000 56.03329  ?  696  THR   A CB  1 
ATOM   5443  O  OG1 . THR   A 1 696  ? -31.14600  102.23300 -26.75100 1.000 48.77571  ?  696  THR   A OG1 1 
ATOM   5444  C  CG2 . THR   A 1 696  ? -29.80900  103.58800 -25.27600 1.000 56.57542  ?  696  THR   A CG2 1 
ATOM   5445  N  N   . ASP   A 1 697  ? -34.24700  103.48900 -26.91300 1.000 47.99943  ?  697  ASP   A N   1 
ATOM   5446  C  CA  . ASP   A 1 697  ? -35.27500  103.55500 -27.94100 1.000 40.50759  ?  697  ASP   A CA  1 
ATOM   5447  C  C   . ASP   A 1 697  ? -36.63600  103.75600 -27.28100 1.000 55.63797  ?  697  ASP   A C   1 
ATOM   5448  O  O   . ASP   A 1 697  ? -36.75700  103.79200 -26.05400 1.000 61.05297  ?  697  ASP   A O   1 
ATOM   5449  C  CB  . ASP   A 1 697  ? -35.26400  102.28600 -28.79900 1.000 48.97459  ?  697  ASP   A CB  1 
ATOM   5450  C  CG  . ASP   A 1 697  ? -33.86200  101.85200 -29.18000 1.000 78.01265  ?  697  ASP   A CG  1 
ATOM   5451  O  OD1 . ASP   A 1 697  ? -33.03700  102.72700 -29.52000 1.000 101.02693 ?  697  ASP   A OD1 1 
ATOM   5452  O  OD2 . ASP   A 1 697  ? -33.58200  100.63400 -29.13100 1.000 72.57141  -1 697  ASP   A OD2 1 
ATOM   5453  N  N   . GLU   A 1 698  ? -37.67300  103.88400 -28.11000 1.000 52.41679  ?  698  GLU   A N   1 
ATOM   5454  C  CA  . GLU   A 1 698  ? -39.02100  103.99500 -27.56500 1.000 51.33465  ?  698  GLU   A CA  1 
ATOM   5455  C  C   . GLU   A 1 698  ? -39.55000  102.64800 -27.09100 1.000 54.61763  ?  698  GLU   A C   1 
ATOM   5456  O  O   . GLU   A 1 698  ? -40.32400  102.59600 -26.12900 1.000 50.39644  ?  698  GLU   A O   1 
ATOM   5457  C  CB  . GLU   A 1 698  ? -39.97100  104.60700 -28.60000 1.000 55.60480  ?  698  GLU   A CB  1 
ATOM   5458  C  CG  . GLU   A 1 698  ? -40.27400  103.73200 -29.81200 1.000 55.34444  ?  698  GLU   A CG  1 
ATOM   5459  C  CD  . GLU   A 1 698  ? -39.32200  103.97000 -30.96800 1.000 66.78079  ?  698  GLU   A CD  1 
ATOM   5460  O  OE1 . GLU   A 1 698  ? -38.10100  104.07900 -30.73100 1.000 61.56940  ?  698  GLU   A OE1 1 
ATOM   5461  O  OE2 . GLU   A 1 698  ? -39.80200  104.05600 -32.11900 1.000 87.86722  -1 698  GLU   A OE2 1 
ATOM   5462  N  N   . LEU   A 1 699  ? -39.13700  101.55500 -27.73900 1.000 55.67525  ?  699  LEU   A N   1 
ATOM   5463  C  CA  . LEU   A 1 699  ? -39.58800  100.23200 -27.32100 1.000 53.11754  ?  699  LEU   A CA  1 
ATOM   5464  C  C   . LEU   A 1 699  ? -38.91300  99.79500  -26.02800 1.000 47.88653  ?  699  LEU   A C   1 
ATOM   5465  O  O   . LEU   A 1 699  ? -39.53300  99.10700  -25.20800 1.000 49.05958  ?  699  LEU   A O   1 
ATOM   5466  C  CB  . LEU   A 1 699  ? -39.32100  99.21200  -28.42700 1.000 44.54338  ?  699  LEU   A CB  1 
ATOM   5467  C  CG  . LEU   A 1 699  ? -40.04700  97.86900  -28.31000 1.000 38.53770  ?  699  LEU   A CG  1 
ATOM   5468  C  CD1 . LEU   A 1 699  ? -41.29700  97.86600  -29.17200 1.000 52.45473  ?  699  LEU   A CD1 1 
ATOM   5469  C  CD2 . LEU   A 1 699  ? -39.13200  96.71500  -28.68100 1.000 49.15270  ?  699  LEU   A CD2 1 
ATOM   5470  N  N   . GLU   A 1 700  ? -37.65100  100.18000 -25.82700 1.000 43.35580  ?  700  GLU   A N   1 
ATOM   5471  C  CA  . GLU   A 1 700  ? -36.95800  99.81400  -24.59700 1.000 55.28960  ?  700  GLU   A CA  1 
ATOM   5472  C  C   . GLU   A 1 700  ? -37.56900  100.50000 -23.38200 1.000 59.08031  ?  700  GLU   A C   1 
ATOM   5473  O  O   . GLU   A 1 700  ? -37.59500  99.91600  -22.29300 1.000 59.15713  ?  700  GLU   A O   1 
ATOM   5474  C  CB  . GLU   A 1 700  ? -35.47100  100.14600 -24.71300 1.000 58.02334  ?  700  GLU   A CB  1 
ATOM   5475  C  CG  . GLU   A 1 700  ? -34.72900  99.29100  -25.72700 1.000 49.92970  ?  700  GLU   A CG  1 
ATOM   5476  C  CD  . GLU   A 1 700  ? -33.23800  99.56000  -25.74100 1.000 50.79849  ?  700  GLU   A CD  1 
ATOM   5477  O  OE1 . GLU   A 1 700  ? -32.81400  100.59600 -25.18600 1.000 52.72458  ?  700  GLU   A OE1 1 
ATOM   5478  O  OE2 . GLU   A 1 700  ? -32.48900  98.73500  -26.30400 1.000 57.91080  -1 700  GLU   A OE2 1 
ATOM   5479  N  N   . GLN   A 1 701  ? -38.06100  101.73100 -23.54200 1.000 61.16234  ?  701  GLN   A N   1 
ATOM   5480  C  CA  . GLN   A 1 701  ? -38.76300  102.39300 -22.44700 1.000 54.52225  ?  701  GLN   A CA  1 
ATOM   5481  C  C   . GLN   A 1 701  ? -40.15600  101.81000 -22.26000 1.000 49.01653  ?  701  GLN   A C   1 
ATOM   5482  O  O   . GLN   A 1 701  ? -40.62000  101.64600 -21.12500 1.000 64.06625  ?  701  GLN   A O   1 
ATOM   5483  C  CB  . GLN   A 1 701  ? -38.84300  103.89800 -22.70400 1.000 42.93753  ?  701  GLN   A CB  1 
ATOM   5484  C  CG  . GLN   A 1 701  ? -39.56700  104.67600 -21.61800 1.000 53.75451  ?  701  GLN   A CG  1 
ATOM   5485  C  CD  . GLN   A 1 701  ? -38.70700  105.77300 -21.02700 1.000 62.75332  ?  701  GLN   A CD  1 
ATOM   5486  O  OE1 . GLN   A 1 701  ? -37.49700  105.81400 -21.24900 1.000 67.51529  ?  701  GLN   A OE1 1 
ATOM   5487  N  NE2 . GLN   A 1 701  ? -39.32900  106.67400 -20.27500 1.000 62.02439  ?  701  GLN   A NE2 1 
ATOM   5488  N  N   . GLN   A 1 702  ? -40.83300  101.49800 -23.36700 1.000 34.99001  ?  702  GLN   A N   1 
ATOM   5489  C  CA  . GLN   A 1 702  ? -42.13200  100.83500 -23.29800 1.000 42.17307  ?  702  GLN   A CA  1 
ATOM   5490  C  C   . GLN   A 1 702  ? -42.03400  99.51100  -22.55200 1.000 45.79352  ?  702  GLN   A C   1 
ATOM   5491  O  O   . GLN   A 1 702  ? -42.87800  99.20400  -21.70100 1.000 47.34364  ?  702  GLN   A O   1 
ATOM   5492  C  CB  . GLN   A 1 702  ? -42.66500  100.61500 -24.71200 1.000 50.92457  ?  702  GLN   A CB  1 
ATOM   5493  C  CG  . GLN   A 1 702  ? -44.16600  100.70400 -24.86600 1.000 42.01108  ?  702  GLN   A CG  1 
ATOM   5494  C  CD  . GLN   A 1 702  ? -44.57100  100.70800 -26.32300 1.000 77.70179  ?  702  GLN   A CD  1 
ATOM   5495  O  OE1 . GLN   A 1 702  ? -45.76100  100.71300 -26.65000 1.000 99.54480  ?  702  GLN   A OE1 1 
ATOM   5496  N  NE2 . GLN   A 1 702  ? -43.58200  100.70600 -27.21000 1.000 73.19141  ?  702  GLN   A NE2 1 
ATOM   5497  N  N   . LEU   A 1 703  ? -41.00800  98.71400  -22.85900 1.000 49.69972  ?  703  LEU   A N   1 
ATOM   5498  C  CA  . LEU   A 1 703  ? -40.79400  97.45800  -22.14900 1.000 37.87748  ?  703  LEU   A CA  1 
ATOM   5499  C  C   . LEU   A 1 703  ? -40.39500  97.70200  -20.69900 1.000 42.72352  ?  703  LEU   A C   1 
ATOM   5500  O  O   . LEU   A 1 703  ? -40.82700  96.97200  -19.80000 1.000 49.53133  ?  703  LEU   A O   1 
ATOM   5501  C  CB  . LEU   A 1 703  ? -39.72600  96.63100  -22.86300 1.000 37.21479  ?  703  LEU   A CB  1 
ATOM   5502  C  CG  . LEU   A 1 703  ? -40.12500  95.93400  -24.16200 1.000 39.36918  ?  703  LEU   A CG  1 
ATOM   5503  C  CD1 . LEU   A 1 703  ? -38.88800  95.56900  -24.96400 1.000 40.56569  ?  703  LEU   A CD1 1 
ATOM   5504  C  CD2 . LEU   A 1 703  ? -40.94600  94.69300  -23.85800 1.000 35.16397  ?  703  LEU   A CD2 1 
ATOM   5505  N  N   . ALA   A 1 704  ? -39.56600  98.72100  -20.45400 1.000 41.30992  ?  704  ALA   A N   1 
ATOM   5506  C  CA  . ALA   A 1 704  ? -39.12100  99.00100  -19.09300 1.000 40.15528  ?  704  ALA   A CA  1 
ATOM   5507  C  C   . ALA   A 1 704  ? -40.28700  99.39700  -18.19800 1.000 49.65262  ?  704  ALA   A C   1 
ATOM   5508  O  O   . ALA   A 1 704  ? -40.31300  99.05400  -17.01100 1.000 57.83132  ?  704  ALA   A O   1 
ATOM   5509  C  CB  . ALA   A 1 704  ? -38.05600  100.09700 -19.10400 1.000 28.74255  ?  704  ALA   A CB  1 
ATOM   5510  N  N   . GLN   A 1 705  ? -41.26300  100.12100 -18.74800 1.000 47.28468  ?  705  GLN   A N   1 
ATOM   5511  C  CA  . GLN   A 1 705  ? -42.43500  100.48500 -17.96100 1.000 49.05210  ?  705  GLN   A CA  1 
ATOM   5512  C  C   . GLN   A 1 705  ? -43.30800  99.26800  -17.68400 1.000 53.47925  ?  705  GLN   A C   1 
ATOM   5513  O  O   . GLN   A 1 705  ? -43.84400  99.12000  -16.57900 1.000 63.39516  ?  705  GLN   A O   1 
ATOM   5514  C  CB  . GLN   A 1 705  ? -43.22800  101.57600 -18.67800 1.000 49.41247  ?  705  GLN   A CB  1 
ATOM   5515  C  CG  . GLN   A 1 705  ? -42.50700  102.91400 -18.72600 1.000 63.15359  ?  705  GLN   A CG  1 
ATOM   5516  C  CD  . GLN   A 1 705  ? -43.08000  103.85300 -19.76800 1.000 73.99577  ?  705  GLN   A CD  1 
ATOM   5517  O  OE1 . GLN   A 1 705  ? -44.00700  103.50000 -20.49800 1.000 71.36947  ?  705  GLN   A OE1 1 
ATOM   5518  N  NE2 . GLN   A 1 705  ? -42.52400  105.05800 -19.84700 1.000 65.10012  ?  705  GLN   A NE2 1 
ATOM   5519  N  N   . VAL   A 1 706  ? -43.45900  98.38300  -18.67200 1.000 48.63242  ?  706  VAL   A N   1 
ATOM   5520  C  CA  . VAL   A 1 706  ? -44.17000  97.12900  -18.43900 1.000 40.86465  ?  706  VAL   A CA  1 
ATOM   5521  C  C   . VAL   A 1 706  ? -43.42700  96.28700  -17.41000 1.000 46.94837  ?  706  VAL   A C   1 
ATOM   5522  O  O   . VAL   A 1 706  ? -44.03800  95.69200  -16.51300 1.000 49.54454  ?  706  VAL   A O   1 
ATOM   5523  C  CB  . VAL   A 1 706  ? -44.36400  96.36800  -19.76300 1.000 30.19131  ?  706  VAL   A CB  1 
ATOM   5524  C  CG1 . VAL   A 1 706  ? -44.91900  94.98000  -19.49900 1.000 47.71789  ?  706  VAL   A CG1 1 
ATOM   5525  C  CG2 . VAL   A 1 706  ? -45.28700  97.14500  -20.68800 1.000 37.63861  ?  706  VAL   A CG2 1 
ATOM   5526  N  N   . TRP   A 1 707  ? -42.09700  96.23100  -17.51800 1.000 48.74209  ?  707  TRP   A N   1 
ATOM   5527  C  CA  . TRP   A 1 707  ? -41.30100  95.52500  -16.51800 1.000 48.86245  ?  707  TRP   A CA  1 
ATOM   5528  C  C   . TRP   A 1 707  ? -41.44500  96.16500  -15.14400 1.000 46.10005  ?  707  TRP   A C   1 
ATOM   5529  O  O   . TRP   A 1 707  ? -41.46800  95.46700  -14.12400 1.000 48.11992  ?  707  TRP   A O   1 
ATOM   5530  C  CB  . TRP   A 1 707  ? -39.83200  95.49400  -16.93800 1.000 42.99983  ?  707  TRP   A CB  1 
ATOM   5531  C  CG  . TRP   A 1 707  ? -39.50400  94.40900  -17.91100 1.000 41.25356  ?  707  TRP   A CG  1 
ATOM   5532  C  CD1 . TRP   A 1 707  ? -40.27900  93.96900  -18.94400 1.000 41.28622  ?  707  TRP   A CD1 1 
ATOM   5533  C  CD2 . TRP   A 1 707  ? -38.31800  93.60900  -17.92800 1.000 35.73081  ?  707  TRP   A CD2 1 
ATOM   5534  N  NE1 . TRP   A 1 707  ? -39.64300  92.94900  -19.61000 1.000 41.22042  ?  707  TRP   A NE1 1 
ATOM   5535  C  CE2 . TRP   A 1 707  ? -38.43700  92.70900  -19.00500 1.000 48.76186  ?  707  TRP   A CE2 1 
ATOM   5536  C  CE3 . TRP   A 1 707  ? -37.16500  93.56900  -17.13900 1.000 40.90762  ?  707  TRP   A CE3 1 
ATOM   5537  C  CZ2 . TRP   A 1 707  ? -37.44600  91.78000  -19.31400 1.000 43.14679  ?  707  TRP   A CZ2 1 
ATOM   5538  C  CZ3 . TRP   A 1 707  ? -36.18400  92.64600  -17.44600 1.000 44.22684  ?  707  TRP   A CZ3 1 
ATOM   5539  C  CH2 . TRP   A 1 707  ? -36.33000  91.76500  -18.52400 1.000 43.88346  ?  707  TRP   A CH2 1 
ATOM   5540  N  N   . SER   A 1 708  ? -41.53800  97.49600  -15.09700 1.000 49.77103  ?  708  SER   A N   1 
ATOM   5541  C  CA  . SER   A 1 708  ? -41.71900  98.17700  -13.82000 1.000 39.25958  ?  708  SER   A CA  1 
ATOM   5542  C  C   . SER   A 1 708  ? -43.08500  97.87000  -13.22200 1.000 44.93409  ?  708  SER   A C   1 
ATOM   5543  O  O   . SER   A 1 708  ? -43.21400  97.71100  -12.00300 1.000 44.19140  ?  708  SER   A O   1 
ATOM   5544  C  CB  . SER   A 1 708  ? -41.53600  99.68300  -13.99900 1.000 44.49149  ?  708  SER   A CB  1 
ATOM   5545  O  OG  . SER   A 1 708  ? -40.22100  99.98800  -14.43200 1.000 69.29890  ?  708  SER   A OG  1 
ATOM   5546  N  N   . HIS   A 1 709  ? -44.11500  97.77900  -14.06500 1.000 53.02200  ?  709  HIS   A N   1 
ATOM   5547  C  CA  . HIS   A 1 709  ? -45.45700  97.49500  -13.57100 1.000 50.11046  ?  709  HIS   A CA  1 
ATOM   5548  C  C   . HIS   A 1 709  ? -45.54300  96.08900  -12.99000 1.000 52.57698  ?  709  HIS   A C   1 
ATOM   5549  O  O   . HIS   A 1 709  ? -46.10100  95.88600  -11.90600 1.000 67.49985  ?  709  HIS   A O   1 
ATOM   5550  C  CB  . HIS   A 1 709  ? -46.47400  97.67800  -14.69900 1.000 45.01446  ?  709  HIS   A CB  1 
ATOM   5551  C  CG  . HIS   A 1 709  ? -47.89400  97.45400  -14.28000 1.000 68.35767  ?  709  HIS   A CG  1 
ATOM   5552  N  ND1 . HIS   A 1 709  ? -48.78700  98.48800  -14.09700 1.000 81.17872  ?  709  HIS   A ND1 1 
ATOM   5553  C  CD2 . HIS   A 1 709  ? -48.57600  96.31600  -14.01000 1.000 71.03301  ?  709  HIS   A CD2 1 
ATOM   5554  C  CE1 . HIS   A 1 709  ? -49.95800  97.99600  -13.73300 1.000 89.72376  ?  709  HIS   A CE1 1 
ATOM   5555  N  NE2 . HIS   A 1 709  ? -49.85700  96.68100  -13.67200 1.000 72.82915  ?  709  HIS   A NE2 1 
ATOM   5556  N  N   . VAL   A 1 710  ? -44.98700  95.10400  -13.69700 1.000 47.85684  ?  710  VAL   A N   1 
ATOM   5557  C  CA  . VAL   A 1 710  ? -45.13000  93.71400  -13.27500 1.000 47.50738  ?  710  VAL   A CA  1 
ATOM   5558  C  C   . VAL   A 1 710  ? -44.24000  93.42200  -12.07200 1.000 42.94305  ?  710  VAL   A C   1 
ATOM   5559  O  O   . VAL   A 1 710  ? -44.69700  92.88200  -11.05800 1.000 62.79605  ?  710  VAL   A O   1 
ATOM   5560  C  CB  . VAL   A 1 710  ? -44.82500  92.76500  -14.44800 1.000 37.49359  ?  710  VAL   A CB  1 
ATOM   5561  C  CG1 . VAL   A 1 710  ? -44.98800  91.32000  -14.01400 1.000 59.81505  ?  710  VAL   A CG1 1 
ATOM   5562  C  CG2 . VAL   A 1 710  ? -45.73400  93.07400  -15.62600 1.000 38.02143  ?  710  VAL   A CG2 1 
ATOM   5563  N  N   . LEU   A 1 711  ? -42.95800  93.77500  -12.16300 1.000 42.38696  ?  711  LEU   A N   1 
ATOM   5564  C  CA  . LEU   A 1 711  ? -42.01300  93.45400  -11.10000 1.000 46.21177  ?  711  LEU   A CA  1 
ATOM   5565  C  C   . LEU   A 1 711  ? -42.01700  94.46800  -9.96300  1.000 39.72953  ?  711  LEU   A C   1 
ATOM   5566  O  O   . LEU   A 1 711  ? -41.41000  94.20100  -8.92100  1.000 47.56820  ?  711  LEU   A O   1 
ATOM   5567  C  CB  . LEU   A 1 711  ? -40.59900  93.32900  -11.67300 1.000 44.77137  ?  711  LEU   A CB  1 
ATOM   5568  C  CG  . LEU   A 1 711  ? -40.39500  92.22800  -12.71700 1.000 35.51931  ?  711  LEU   A CG  1 
ATOM   5569  C  CD1 . LEU   A 1 711  ? -38.94100  92.15100  -13.14700 1.000 32.61588  ?  711  LEU   A CD1 1 
ATOM   5570  C  CD2 . LEU   A 1 711  ? -40.86500  90.88700  -12.17800 1.000 53.65482  ?  711  LEU   A CD2 1 
ATOM   5571  N  N   . GLY   A 1 712  ? -42.67200  95.61400  -10.13500 1.000 42.69496  ?  712  GLY   A N   1 
ATOM   5572  C  CA  . GLY   A 1 712  ? -42.79400  96.57200  -9.05300  1.000 35.41369  ?  712  GLY   A CA  1 
ATOM   5573  C  C   . GLY   A 1 712  ? -41.54300  97.35300  -8.72800  1.000 44.27877  ?  712  GLY   A C   1 
ATOM   5574  O  O   . GLY   A 1 712  ? -41.43900  97.90300  -7.62900  1.000 68.27389  ?  712  GLY   A O   1 
ATOM   5575  N  N   . ILE   A 1 713  ? -40.59400  97.42800  -9.64900  1.000 49.75253  ?  713  ILE   A N   1 
ATOM   5576  C  CA  . ILE   A 1 713  ? -39.32600  98.12600  -9.44300  1.000 51.45271  ?  713  ILE   A CA  1 
ATOM   5577  C  C   . ILE   A 1 713  ? -39.31100  99.35700  -10.33800 1.000 56.57468  ?  713  ILE   A C   1 
ATOM   5578  O  O   . ILE   A 1 713  ? -39.62300  99.24400  -11.52900 1.000 65.20233  ?  713  ILE   A O   1 
ATOM   5579  C  CB  . ILE   A 1 713  ? -38.11900  97.21800  -9.74900  1.000 48.34878  ?  713  ILE   A CB  1 
ATOM   5580  C  CG1 . ILE   A 1 713  ? -38.08000  96.03700  -8.77700  1.000 55.98491  ?  713  ILE   A CG1 1 
ATOM   5581  C  CG2 . ILE   A 1 713  ? -36.81900  98.01200  -9.70400  1.000 47.53480  ?  713  ILE   A CG2 1 
ATOM   5582  C  CD1 . ILE   A 1 713  ? -37.32800  94.83700  -9.31000  1.000 54.30990  ?  713  ILE   A CD1 1 
ATOM   5583  N  N   . PRO   A 1 714  ? -38.96800  100.53300 -9.82100  1.000 53.22919  ?  714  PRO   A N   1 
ATOM   5584  C  CA  . PRO   A 1 714  ? -38.92600  101.72800 -10.66600 1.000 42.98687  ?  714  PRO   A CA  1 
ATOM   5585  C  C   . PRO   A 1 714  ? -37.61400  101.84700 -11.42600 1.000 52.50731  ?  714  PRO   A C   1 
ATOM   5586  O  O   . PRO   A 1 714  ? -36.55200  101.43000 -10.95600 1.000 54.22741  ?  714  PRO   A O   1 
ATOM   5587  C  CB  . PRO   A 1 714  ? -39.07900  102.86900 -9.65600  1.000 38.01689  ?  714  PRO   A CB  1 
ATOM   5588  C  CG  . PRO   A 1 714  ? -38.42900  102.33500 -8.42200  1.000 62.17954  ?  714  PRO   A CG  1 
ATOM   5589  C  CD  . PRO   A 1 714  ? -38.70600  100.84800 -8.40500  1.000 66.64769  ?  714  PRO   A CD  1 
ATOM   5590  N  N   . GLN   A 1 715  ? -37.70900  102.43200 -12.62000 1.000 46.41566  ?  715  GLN   A N   1 
ATOM   5591  C  CA  . GLN   A 1 715  ? -36.56200  102.71200 -13.48500 1.000 45.52051  ?  715  GLN   A CA  1 
ATOM   5592  C  C   . GLN   A 1 715  ? -35.74200  101.44500 -13.74400 1.000 54.78831  ?  715  GLN   A C   1 
ATOM   5593  O  O   . GLN   A 1 715  ? -34.64100  101.25300 -13.22700 1.000 66.64388  ?  715  GLN   A O   1 
ATOM   5594  C  CB  . GLN   A 1 715  ? -35.69100  103.82300 -12.89000 1.000 51.92739  ?  715  GLN   A CB  1 
ATOM   5595  C  CG  . GLN   A 1 715  ? -36.18200  105.23200 -13.18400 1.000 57.99984  ?  715  GLN   A CG  1 
ATOM   5596  C  CD  . GLN   A 1 715  ? -35.44100  106.28300 -12.38100 1.000 68.61723  ?  715  GLN   A CD  1 
ATOM   5597  O  OE1 . GLN   A 1 715  ? -35.50300  106.29700 -11.15200 1.000 82.90932  ?  715  GLN   A OE1 1 
ATOM   5598  N  NE2 . GLN   A 1 715  ? -34.73000  107.16700 -13.07300 1.000 70.28073  ?  715  GLN   A NE2 1 
ATOM   5599  N  N   . MET   A 1 716  ? -36.32100  100.58400 -14.57500 1.000 56.23418  ?  716  MET   A N   1 
ATOM   5600  C  CA  . MET   A 1 716  ? -35.67100  99.33500  -14.93600 1.000 52.79521  ?  716  MET   A CA  1 
ATOM   5601  C  C   . MET   A 1 716  ? -34.45200  99.59200  -15.81800 1.000 55.41897  ?  716  MET   A C   1 
ATOM   5602  O  O   . MET   A 1 716  ? -34.29200  100.66000 -16.41500 1.000 60.35118  ?  716  MET   A O   1 
ATOM   5603  C  CB  . MET   A 1 716  ? -36.65000  98.41200  -15.65700 1.000 60.32352  ?  716  MET   A CB  1 
ATOM   5604  C  CG  . MET   A 1 716  ? -37.62100  97.70100  -14.73900 1.000 62.79307  ?  716  MET   A CG  1 
ATOM   5605  S  SD  . MET   A 1 716  ? -36.82800  96.38300  -13.80300 1.000 52.26010  ?  716  MET   A SD  1 
ATOM   5606  C  CE  . MET   A 1 716  ? -38.25100  95.68000  -12.98100 1.000 56.76071  ?  716  MET   A CE  1 
ATOM   5607  N  N   . GLY   A 1 717  ? -33.58800  98.58400  -15.89600 1.000 55.10196  ?  717  GLY   A N   1 
ATOM   5608  C  CA  . GLY   A 1 717  ? -32.36900  98.65500  -16.67700 1.000 41.56905  ?  717  GLY   A CA  1 
ATOM   5609  C  C   . GLY   A 1 717  ? -32.45600  97.78200  -17.91500 1.000 46.67026  ?  717  GLY   A C   1 
ATOM   5610  O  O   . GLY   A 1 717  ? -33.14100  96.75600  -17.92300 1.000 46.26494  ?  717  GLY   A O   1 
ATOM   5611  N  N   . ILE   A 1 718  ? -31.74800  98.19900  -18.96500 1.000 50.70091  ?  718  ILE   A N   1 
ATOM   5612  C  CA  . ILE   A 1 718  ? -31.76000  97.45600  -20.22000 1.000 50.71373  ?  718  ILE   A CA  1 
ATOM   5613  C  C   . ILE   A 1 718  ? -31.08800  96.09800  -20.05300 1.000 53.81630  ?  718  ILE   A C   1 
ATOM   5614  O  O   . ILE   A 1 718  ? -31.42200  95.13800  -20.76000 1.000 55.01671  ?  718  ILE   A O   1 
ATOM   5615  C  CB  . ILE   A 1 718  ? -31.10600  98.31300  -21.32300 1.000 44.86442  ?  718  ILE   A CB  1 
ATOM   5616  C  CG1 . ILE   A 1 718  ? -31.98300  99.52900  -21.62300 1.000 59.90129  ?  718  ILE   A CG1 1 
ATOM   5617  C  CG2 . ILE   A 1 718  ? -30.88000  97.52400  -22.59200 1.000 48.90619  ?  718  ILE   A CG2 1 
ATOM   5618  C  CD1 . ILE   A 1 718  ? -33.46500  99.20800  -21.68900 1.000 50.48021  ?  718  ILE   A CD1 1 
ATOM   5619  N  N   . ASP   A 1 719  ? -30.16400  95.97700  -19.10300 1.000 42.17074  ?  719  ASP   A N   1 
ATOM   5620  C  CA  . ASP   A 1 719  ? -29.44900  94.73200  -18.84300 1.000 45.23337  ?  719  ASP   A CA  1 
ATOM   5621  C  C   . ASP   A 1 719  ? -29.83900  94.12800  -17.49900 1.000 48.43083  ?  719  ASP   A C   1 
ATOM   5622  O  O   . ASP   A 1 719  ? -29.00800  93.55500  -16.79100 1.000 41.68974  ?  719  ASP   A O   1 
ATOM   5623  C  CB  . ASP   A 1 719  ? -27.94300  94.95600  -18.91100 1.000 46.90037  ?  719  ASP   A CB  1 
ATOM   5624  C  CG  . ASP   A 1 719  ? -27.48200  95.34000  -20.29400 1.000 61.10359  ?  719  ASP   A CG  1 
ATOM   5625  O  OD1 . ASP   A 1 719  ? -28.03300  94.79700  -21.27600 1.000 63.20289  ?  719  ASP   A OD1 1 
ATOM   5626  O  OD2 . ASP   A 1 719  ? -26.57300  96.18900  -20.40500 1.000 76.56580  -1 719  ASP   A OD2 1 
ATOM   5627  N  N   . ASP   A 1 720  ? -31.10900  94.25000  -17.13200 1.000 52.33873  ?  720  ASP   A N   1 
ATOM   5628  C  CA  . ASP   A 1 720  ? -31.62100  93.67900  -15.89600 1.000 43.48729  ?  720  ASP   A CA  1 
ATOM   5629  C  C   . ASP   A 1 720  ? -32.34100  92.37500  -16.20800 1.000 44.19963  ?  720  ASP   A C   1 
ATOM   5630  O  O   . ASP   A 1 720  ? -33.12800  92.30500  -17.15700 1.000 51.59732  ?  720  ASP   A O   1 
ATOM   5631  C  CB  . ASP   A 1 720  ? -32.55800  94.65700  -15.18700 1.000 41.79053  ?  720  ASP   A CB  1 
ATOM   5632  C  CG  . ASP   A 1 720  ? -31.81900  95.84100  -14.59100 1.000 40.87524  ?  720  ASP   A CG  1 
ATOM   5633  O  OD1 . ASP   A 1 720  ? -30.57200  95.86900  -14.67200 1.000 58.91237  ?  720  ASP   A OD1 1 
ATOM   5634  O  OD2 . ASP   A 1 720  ? -32.48300  96.74300  -14.04100 1.000 46.07774  -1 720  ASP   A OD2 1 
ATOM   5635  N  N   . HIS   A 1 721  ? -32.06100  91.34600  -15.41400 1.000 33.77267  ?  721  HIS   A N   1 
ATOM   5636  C  CA  . HIS   A 1 721  ? -32.60700  90.01500  -15.63900 1.000 27.93285  ?  721  HIS   A CA  1 
ATOM   5637  C  C   . HIS   A 1 721  ? -33.97100  89.89200  -14.96900 1.000 45.70265  ?  721  HIS   A C   1 
ATOM   5638  O  O   . HIS   A 1 721  ? -34.11500  90.20000  -13.78200 1.000 43.95081  ?  721  HIS   A O   1 
ATOM   5639  C  CB  . HIS   A 1 721  ? -31.64400  88.95700  -15.09900 1.000 21.04608  ?  721  HIS   A CB  1 
ATOM   5640  C  CG  . HIS   A 1 721  ? -31.98900  87.55700  -15.49500 1.000 33.79739  ?  721  HIS   A CG  1 
ATOM   5641  N  ND1 . HIS   A 1 721  ? -31.28500  86.86200  -16.45300 1.000 33.60618  ?  721  HIS   A ND1 1 
ATOM   5642  C  CD2 . HIS   A 1 721  ? -32.95400  86.71700  -15.05300 1.000 41.15551  ?  721  HIS   A CD2 1 
ATOM   5643  C  CE1 . HIS   A 1 721  ? -31.80300  85.65500  -16.58700 1.000 35.33102  ?  721  HIS   A CE1 1 
ATOM   5644  N  NE2 . HIS   A 1 721  ? -32.81900  85.54200  -15.75200 1.000 36.63929  ?  721  HIS   A NE2 1 
ATOM   5645  N  N   . PHE   A 1 722  ? -34.96400  89.43100  -15.73500 1.000 38.07597  ?  722  PHE   A N   1 
ATOM   5646  C  CA  . PHE   A 1 722  ? -36.33400  89.35800  -15.23200 1.000 31.72203  ?  722  PHE   A CA  1 
ATOM   5647  C  C   . PHE   A 1 722  ? -36.43900  88.43100  -14.02600 1.000 37.83565  ?  722  PHE   A C   1 
ATOM   5648  O  O   . PHE   A 1 722  ? -37.08000  88.77300  -13.02500 1.000 41.20485  ?  722  PHE   A O   1 
ATOM   5649  C  CB  . PHE   A 1 722  ? -37.26700  88.89300  -16.35100 1.000 42.02162  ?  722  PHE   A CB  1 
ATOM   5650  C  CG  . PHE   A 1 722  ? -38.72700  89.08000  -16.04900 1.000 31.82433  ?  722  PHE   A CG  1 
ATOM   5651  C  CD1 . PHE   A 1 722  ? -39.33100  90.31200  -16.23600 1.000 25.34826  ?  722  PHE   A CD1 1 
ATOM   5652  C  CD2 . PHE   A 1 722  ? -39.50100  88.02100  -15.60200 1.000 34.24151  ?  722  PHE   A CD2 1 
ATOM   5653  C  CE1 . PHE   A 1 722  ? -40.67400  90.49000  -15.97000 1.000 38.87470  ?  722  PHE   A CE1 1 
ATOM   5654  C  CE2 . PHE   A 1 722  ? -40.84700  88.19100  -15.33400 1.000 26.44041  ?  722  PHE   A CE2 1 
ATOM   5655  C  CZ  . PHE   A 1 722  ? -41.43400  89.42700  -15.51800 1.000 38.33151  ?  722  PHE   A CZ  1 
ATOM   5656  N  N   . LEU   A 1 723  ? -35.81300  87.25400  -14.10000 1.000 39.08041  ?  723  LEU   A N   1 
ATOM   5657  C  CA  . LEU   A 1 723  ? -35.92700  86.27000  -13.03000 1.000 39.40093  ?  723  LEU   A CA  1 
ATOM   5658  C  C   . LEU   A 1 723  ? -35.10900  86.64200  -11.80000 1.000 38.98487  ?  723  LEU   A C   1 
ATOM   5659  O  O   . LEU   A 1 723  ? -35.50500  86.30400  -10.67900 1.000 44.88932  ?  723  LEU   A O   1 
ATOM   5660  C  CB  . LEU   A 1 723  ? -35.50400  84.89100  -13.53900 1.000 34.81154  ?  723  LEU   A CB  1 
ATOM   5661  C  CG  . LEU   A 1 723  ? -36.28100  84.36200  -14.74500 1.000 38.27636  ?  723  LEU   A CG  1 
ATOM   5662  C  CD1 . LEU   A 1 723  ? -35.80000  82.97100  -15.11700 1.000 38.12580  ?  723  LEU   A CD1 1 
ATOM   5663  C  CD2 . LEU   A 1 723  ? -37.78000  84.36700  -14.47500 1.000 29.07573  ?  723  LEU   A CD2 1 
ATOM   5664  N  N   . GLU   A 1 724  ? -33.97800  87.32000  -11.97300 1.000 38.05190  ?  724  GLU   A N   1 
ATOM   5665  C  CA  . GLU   A 1 724  ? -33.13100  87.66400  -10.83900 1.000 48.71529  ?  724  GLU   A CA  1 
ATOM   5666  C  C   . GLU   A 1 724  ? -33.55600  88.95700  -10.15000 1.000 42.50760  ?  724  GLU   A C   1 
ATOM   5667  O  O   . GLU   A 1 724  ? -32.95500  89.33100  -9.13700  1.000 53.05570  ?  724  GLU   A O   1 
ATOM   5668  C  CB  . GLU   A 1 724  ? -31.66200  87.74900  -11.27800 1.000 42.09600  ?  724  GLU   A CB  1 
ATOM   5669  C  CG  . GLU   A 1 724  ? -31.16400  89.13200  -11.64900 1.000 46.14247  ?  724  GLU   A CG  1 
ATOM   5670  C  CD  . GLU   A 1 724  ? -29.69800  89.12100  -12.03300 1.000 40.89110  ?  724  GLU   A CD  1 
ATOM   5671  O  OE1 . GLU   A 1 724  ? -29.19100  88.03800  -12.39500 1.000 28.71132  ?  724  GLU   A OE1 1 
ATOM   5672  O  OE2 . GLU   A 1 724  ? -29.05400  90.18900  -11.96500 1.000 59.82640  -1 724  GLU   A OE2 1 
ATOM   5673  N  N   . ARG   A 1 725  ? -34.58600  89.63600  -10.65600 1.000 42.95304  ?  725  ARG   A N   1 
ATOM   5674  C  CA  . ARG   A 1 725  ? -35.13300  90.82100  -10.00800 1.000 47.33898  ?  725  ARG   A CA  1 
ATOM   5675  C  C   . ARG   A 1 725  ? -36.57500  90.59800  -9.56200  1.000 45.70512  ?  725  ARG   A C   1 
ATOM   5676  O  O   . ARG   A 1 725  ? -37.35300  91.54800  -9.44800  1.000 56.52676  ?  725  ARG   A O   1 
ATOM   5677  C  CB  . ARG   A 1 725  ? -35.03100  92.03900  -10.92500 1.000 43.92993  ?  725  ARG   A CB  1 
ATOM   5678  C  CG  . ARG   A 1 725  ? -33.61100  92.36600  -11.35400 1.000 35.90929  ?  725  ARG   A CG  1 
ATOM   5679  C  CD  . ARG   A 1 725  ? -33.44000  93.85300  -11.60700 1.000 46.17745  ?  725  ARG   A CD  1 
ATOM   5680  N  NE  . ARG   A 1 725  ? -33.72400  94.63700  -10.41100 1.000 59.31558  ?  725  ARG   A NE  1 
ATOM   5681  C  CZ  . ARG   A 1 725  ? -33.55700  95.94900  -10.31600 1.000 44.34099  ?  725  ARG   A CZ  1 
ATOM   5682  N  NH1 . ARG   A 1 725  ? -33.10300  96.66300  -11.33300 1.000 39.71190  ?  725  ARG   A NH1 1 
ATOM   5683  N  NH2 . ARG   A 1 725  ? -33.85200  96.56000  -9.17200  1.000 43.23052  ?  725  ARG   A NH2 1 
ATOM   5684  N  N   . GLY   A 1 726  ? -36.94600  89.34300  -9.30900  1.000 37.55395  ?  726  GLY   A N   1 
ATOM   5685  C  CA  . GLY   A 1 726  ? -38.23200  89.01300  -8.72400  1.000 35.13942  ?  726  GLY   A CA  1 
ATOM   5686  C  C   . GLY   A 1 726  ? -39.20700  88.29700  -9.63400  1.000 46.74333  ?  726  GLY   A C   1 
ATOM   5687  O  O   . GLY   A 1 726  ? -40.33000  88.01300  -9.19900  1.000 51.39860  ?  726  GLY   A O   1 
ATOM   5688  N  N   . GLY   A 1 727  ? -38.82600  87.98400  -10.86900 1.000 42.07226  ?  727  GLY   A N   1 
ATOM   5689  C  CA  . GLY   A 1 727  ? -39.77500  87.40800  -11.80900 1.000 31.89053  ?  727  GLY   A CA  1 
ATOM   5690  C  C   . GLY   A 1 727  ? -40.09100  85.96100  -11.47400 1.000 37.07935  ?  727  GLY   A C   1 
ATOM   5691  O  O   . GLY   A 1 727  ? -39.19100  85.15700  -11.20400 1.000 35.62255  ?  727  GLY   A O   1 
ATOM   5692  N  N   . ASP   A 1 728  ? -41.38100  85.62400  -11.49000 1.000 48.78226  ?  728  ASP   A N   1 
ATOM   5693  C  CA  . ASP   A 1 728  ? -41.88800  84.27500  -11.30300 1.000 41.64305  ?  728  ASP   A CA  1 
ATOM   5694  C  C   . ASP   A 1 728  ? -42.46700  83.77700  -12.62900 1.000 52.56917  ?  728  ASP   A C   1 
ATOM   5695  O  O   . ASP   A 1 728  ? -42.17900  84.33800  -13.69500 1.000 52.74177  ?  728  ASP   A O   1 
ATOM   5696  C  CB  . ASP   A 1 728  ? -42.92400  84.26900  -10.17400 1.000 34.03390  ?  728  ASP   A CB  1 
ATOM   5697  C  CG  . ASP   A 1 728  ? -42.40700  84.90100  -8.89900  1.000 70.93745  ?  728  ASP   A CG  1 
ATOM   5698  O  OD1 . ASP   A 1 728  ? -41.34200  84.47400  -8.40700  1.000 91.97997  ?  728  ASP   A OD1 1 
ATOM   5699  O  OD2 . ASP   A 1 728  ? -43.06800  85.83200  -8.39100  1.000 86.25487  -1 728  ASP   A OD2 1 
HETATM 5700  O  O   . 4HH   A 1 729  ? -45.45900  83.65200  -15.12800 1.000 57.94722  ?  729  4HH   A O   1 
HETATM 5701  C  C   . 4HH   A 1 729  ? -45.22100  83.22000  -13.99400 1.000 51.13857  ?  729  4HH   A C   1 
HETATM 5702  C  CA  . 4HH   A 1 729  ? -44.02900  82.30600  -13.74600 1.000 52.87634  ?  729  4HH   A CA  1 
HETATM 5703  N  N   . 4HH   A 1 729  ? -43.28600  82.72700  -12.56400 1.000 53.44786  ?  729  4HH   A N   1 
HETATM 5704  C  CB  . 4HH   A 1 729  ? -44.49300  80.85800  -13.59800 1.000 59.34527  ?  729  4HH   A CB  1 
HETATM 5705  O  OG  . 4HH   A 1 729  ? -43.44200  79.95300  -13.87200 1.000 47.22093  ?  729  4HH   A OG  1 
HETATM 5706  C  CJ  . 4HH   A 1 729  ? -44.49000  77.05400  -12.90200 1.000 53.26119  ?  729  4HH   A CJ  1 
HETATM 5707  C  CK  . 4HH   A 1 729  ? -45.95600  76.83800  -12.57300 1.000 40.47492  ?  729  4HH   A CK  1 
HETATM 5708  C  CL1 . 4HH   A 1 729  ? -46.05400  76.31900  -11.14000 1.000 31.40882  ?  729  4HH   A CL1 1 
HETATM 5709  C  CL2 . 4HH   A 1 729  ? -46.55100  75.80500  -13.52600 1.000 43.97110  ?  729  4HH   A CL2 1 
HETATM 5710  C  CL3 . 4HH   A 1 729  ? -47.99600  78.15800  -11.91000 1.000 36.03595  ?  729  4HH   A CL3 1 
HETATM 5711  C  CM  . 4HH   A 1 729  ? -46.69700  78.17200  -12.72200 1.000 43.89006  ?  729  4HH   A CM  1 
HETATM 5712  O  OM  . 4HH   A 1 729  ? -46.99900  78.38600  -14.07200 1.000 76.08949  ?  729  4HH   A OM  1 
HETATM 5713  N  NN  . 4HH   A 1 729  ? -48.04300  78.82000  -10.60800 1.000 44.52097  ?  729  4HH   A NN  1 
HETATM 5714  O  ON  . 4HH   A 1 729  ? -48.95400  77.61900  -12.34600 1.000 28.88630  ?  729  4HH   A ON  1 
HETATM 5715  P  P   . 4HH   A 1 729  ? -42.84200  79.07000  -12.61900 1.000 44.83428  ?  729  4HH   A P   1 
HETATM 5716  O  O1P . 4HH   A 1 729  ? -41.68000  78.28600  -13.09300 1.000 55.04695  ?  729  4HH   A O1P 1 
HETATM 5717  O  O2P . 4HH   A 1 729  ? -42.37500  80.08000  -11.41500 1.000 38.40340  ?  729  4HH   A O2P 1 
HETATM 5718  O  O3P . 4HH   A 1 729  ? -44.01000  78.06600  -12.05500 1.000 34.58177  ?  729  4HH   A O3P 1 
HETATM 5719  C  CO  . 4HH   A 1 729  ? -49.28000  78.79500  -9.82700  1.000 58.44937  ?  729  4HH   A CO  1 
HETATM 5720  C  CP  . 4HH   A 1 729  ? -49.47500  77.35400  -9.31300  1.000 45.07695  ?  729  4HH   A CP  1 
HETATM 5721  C  CQ  . 4HH   A 1 729  ? -50.87000  77.09200  -8.71500  1.000 53.05277  ?  729  4HH   A CQ  1 
HETATM 5722  C  CS  . 4HH   A 1 729  ? -52.29500  75.77700  -7.06000  1.000 48.70090  ?  729  4HH   A CS  1 
HETATM 5723  C  CT  . 4HH   A 1 729  ? -52.03000  74.90800  -5.83000  1.000 63.49087  ?  729  4HH   A CT  1 
HETATM 5724  N  NR  . 4HH   A 1 729  ? -50.99800  76.07500  -7.67300  1.000 55.97335  ?  729  4HH   A NR  1 
HETATM 5725  O  OR  . 4HH   A 1 729  ? -51.81900  77.69600  -9.09100  1.000 72.25621  ?  729  4HH   A OR  1 
HETATM 5726  S  SU  . 4HH   A 1 729  ? -50.33000  75.13200  -5.24900  1.000 107.38233 ?  729  4HH   A SU  1 
ATOM   5727  N  N   . ILE   A 1 730  ? -45.98100  83.52300  -12.93800 1.000 47.24301  ?  730  ILE   A N   1 
ATOM   5728  C  CA  . ILE   A 1 730  ? -47.12400  84.42100  -13.07000 1.000 58.57296  ?  730  ILE   A CA  1 
ATOM   5729  C  C   . ILE   A 1 730  ? -46.67500  85.80300  -13.51800 1.000 47.76347  ?  730  ILE   A C   1 
ATOM   5730  O  O   . ILE   A 1 730  ? -47.41900  86.51200  -14.20600 1.000 53.76501  ?  730  ILE   A O   1 
ATOM   5731  C  CB  . ILE   A 1 730  ? -47.90700  84.48500  -11.74500 1.000 44.53605  ?  730  ILE   A CB  1 
ATOM   5732  C  CG1 . ILE   A 1 730  ? -46.93600  84.54300  -10.56200 1.000 64.72232  ?  730  ILE   A CG1 1 
ATOM   5733  C  CG2 . ILE   A 1 730  ? -48.85600  83.29900  -11.62900 1.000 43.84562  ?  730  ILE   A CG2 1 
ATOM   5734  C  CD1 . ILE   A 1 730  ? -47.58400  84.93300  -9.25200  1.000 65.27402  ?  730  ILE   A CD1 1 
ATOM   5735  N  N   . LYS   A 1 731  ? -45.46100  86.21200  -13.14100 1.000 45.41775  ?  731  LYS   A N   1 
ATOM   5736  C  CA  . LYS   A 1 731  ? -44.94100  87.49600  -13.60000 1.000 44.76502  ?  731  LYS   A CA  1 
ATOM   5737  C  C   . LYS   A 1 731  ? -44.63700  87.46600  -15.09300 1.000 44.12698  ?  731  LYS   A C   1 
ATOM   5738  O  O   . LYS   A 1 731  ? -44.83300  88.46700  -15.79100 1.000 44.47859  ?  731  LYS   A O   1 
ATOM   5739  C  CB  . LYS   A 1 731  ? -43.69200  87.87100  -12.80400 1.000 41.28732  ?  731  LYS   A CB  1 
ATOM   5740  C  CG  . LYS   A 1 731  ? -43.90600  87.98400  -11.30200 1.000 48.84305  ?  731  LYS   A CG  1 
ATOM   5741  C  CD  . LYS   A 1 731  ? -44.20500  89.41500  -10.88600 1.000 38.47736  ?  731  LYS   A CD  1 
ATOM   5742  C  CE  . LYS   A 1 731  ? -44.07700  89.58900  -9.37900  1.000 49.30990  ?  731  LYS   A CE  1 
ATOM   5743  N  NZ  . LYS   A 1 731  ? -45.05700  88.75900  -8.62400  1.000 60.06445  ?  731  LYS   A NZ  1 
ATOM   5744  N  N   . VAL   A 1 732  ? -44.15200  86.32900  -15.59800 1.000 43.39499  ?  732  VAL   A N   1 
ATOM   5745  C  CA  . VAL   A 1 732  ? -43.91900  86.20000  -17.03300 1.000 46.02287  ?  732  VAL   A CA  1 
ATOM   5746  C  C   . VAL   A 1 732  ? -45.23900  86.25300  -17.79100 1.000 39.50719  ?  732  VAL   A C   1 
ATOM   5747  O  O   . VAL   A 1 732  ? -45.35500  86.93500  -18.81700 1.000 52.34281  ?  732  VAL   A O   1 
ATOM   5748  C  CB  . VAL   A 1 732  ? -43.14000  84.90700  -17.34000 1.000 52.71012  ?  732  VAL   A CB  1 
ATOM   5749  C  CG1 . VAL   A 1 732  ? -43.08100  84.66000  -18.84200 1.000 33.54486  ?  732  VAL   A CG1 1 
ATOM   5750  C  CG2 . VAL   A 1 732  ? -41.73500  84.98200  -16.76300 1.000 32.89238  ?  732  VAL   A CG2 1 
ATOM   5751  N  N   . MET   A 1 733  ? -46.25600  85.54600  -17.29400 1.000 45.06657  ?  733  MET   A N   1 
ATOM   5752  C  CA  . MET   A 1 733  ? -47.55800  85.57400  -17.95100 1.000 45.33984  ?  733  MET   A CA  1 
ATOM   5753  C  C   . MET   A 1 733  ? -48.19200  86.95700  -17.86500 1.000 46.87202  ?  733  MET   A C   1 
ATOM   5754  O  O   . MET   A 1 733  ? -48.88700  87.37800  -18.79700 1.000 45.37017  ?  733  MET   A O   1 
ATOM   5755  C  CB  . MET   A 1 733  ? -48.47900  84.51900  -17.33900 1.000 46.32262  ?  733  MET   A CB  1 
ATOM   5756  C  CG  . MET   A 1 733  ? -49.48900  83.94600  -18.32000 1.000 60.43164  ?  733  MET   A CG  1 
ATOM   5757  S  SD  . MET   A 1 733  ? -48.71000  82.95900  -19.61500 1.000 82.26564  ?  733  MET   A SD  1 
ATOM   5758  C  CE  . MET   A 1 733  ? -48.63700  81.35000  -18.82900 1.000 57.44802  ?  733  MET   A CE  1 
ATOM   5759  N  N   . GLN   A 1 734  ? -47.96400  87.67500  -16.76200 1.000 53.74537  ?  734  GLN   A N   1 
ATOM   5760  C  CA  . GLN   A 1 734  ? -48.39900  89.06600  -16.68300 1.000 42.56372  ?  734  GLN   A CA  1 
ATOM   5761  C  C   . GLN   A 1 734  ? -47.69000  89.91200  -17.73100 1.000 43.32917  ?  734  GLN   A C   1 
ATOM   5762  O  O   . GLN   A 1 734  ? -48.33400  90.64400  -18.49100 1.000 56.54579  ?  734  GLN   A O   1 
ATOM   5763  C  CB  . GLN   A 1 734  ? -48.14500  89.62200  -15.28100 1.000 40.15880  ?  734  GLN   A CB  1 
ATOM   5764  C  CG  . GLN   A 1 734  ? -49.13300  89.14800  -14.22800 1.000 41.27041  ?  734  GLN   A CG  1 
ATOM   5765  C  CD  . GLN   A 1 734  ? -48.69300  89.50500  -12.82100 1.000 48.98595  ?  734  GLN   A CD  1 
ATOM   5766  O  OE1 . GLN   A 1 734  ? -47.97000  90.48000  -12.61100 1.000 42.91698  ?  734  GLN   A OE1 1 
ATOM   5767  N  NE2 . GLN   A 1 734  ? -49.12100  88.70900  -11.84800 1.000 61.37618  ?  734  GLN   A NE2 1 
ATOM   5768  N  N   . LEU   A 1 735  ? -46.35800  89.81400  -17.78800 1.000 51.36260  ?  735  LEU   A N   1 
ATOM   5769  C  CA  . LEU   A 1 735  ? -45.58500  90.53400  -18.79600 1.000 55.68616  ?  735  LEU   A CA  1 
ATOM   5770  C  C   . LEU   A 1 735  ? -46.12800  90.27700  -20.19600 1.000 50.29619  ?  735  LEU   A C   1 
ATOM   5771  O  O   . LEU   A 1 735  ? -46.31000  91.21000  -20.98600 1.000 52.05324  ?  735  LEU   A O   1 
ATOM   5772  C  CB  . LEU   A 1 735  ? -44.11300  90.12600  -18.71200 1.000 39.25705  ?  735  LEU   A CB  1 
ATOM   5773  C  CG  . LEU   A 1 735  ? -43.24500  90.47800  -19.92200 1.000 32.40766  ?  735  LEU   A CG  1 
ATOM   5774  C  CD1 . LEU   A 1 735  ? -42.93900  91.96500  -19.96200 1.000 43.08851  ?  735  LEU   A CD1 1 
ATOM   5775  C  CD2 . LEU   A 1 735  ? -41.96600  89.66200  -19.92000 1.000 33.10786  ?  735  LEU   A CD2 1 
ATOM   5776  N  N   . ILE   A 1 736  ? -46.40100  89.01000  -20.51300 1.000 41.23075  ?  736  ILE   A N   1 
ATOM   5777  C  CA  . ILE   A 1 736  ? -46.94500  88.66300  -21.82300 1.000 41.07769  ?  736  ILE   A CA  1 
ATOM   5778  C  C   . ILE   A 1 736  ? -48.29200  89.34300  -22.04200 1.000 47.79737  ?  736  ILE   A C   1 
ATOM   5779  O  O   . ILE   A 1 736  ? -48.57100  89.86700  -23.12900 1.000 47.37868  ?  736  ILE   A O   1 
ATOM   5780  C  CB  . ILE   A 1 736  ? -47.04700  87.13200  -21.96200 1.000 33.33991  ?  736  ILE   A CB  1 
ATOM   5781  C  CG1 . ILE   A 1 736  ? -45.65600  86.52000  -22.14400 1.000 40.88741  ?  736  ILE   A CG1 1 
ATOM   5782  C  CG2 . ILE   A 1 736  ? -47.96200  86.75000  -23.11600 1.000 44.89485  ?  736  ILE   A CG2 1 
ATOM   5783  C  CD1 . ILE   A 1 736  ? -45.65700  85.00900  -22.19000 1.000 40.99164  ?  736  ILE   A CD1 1 
ATOM   5784  N  N   . HIS   A 1 737  ? -49.14300  89.36100  -21.01300 1.000 42.62262  ?  737  HIS   A N   1 
ATOM   5785  C  CA  . HIS   A 1 737  ? -50.47200  89.94500  -21.16600 1.000 45.95485  ?  737  HIS   A CA  1 
ATOM   5786  C  C   . HIS   A 1 737  ? -50.40800  91.46600  -21.24700 1.000 49.42833  ?  737  HIS   A C   1 
ATOM   5787  O  O   . HIS   A 1 737  ? -51.18700  92.08600  -21.98100 1.000 65.38797  ?  737  HIS   A O   1 
ATOM   5788  C  CB  . HIS   A 1 737  ? -51.37700  89.49600  -20.01900 1.000 51.16379  ?  737  HIS   A CB  1 
ATOM   5789  C  CG  . HIS   A 1 737  ? -51.70200  88.03400  -20.04600 1.000 79.33700  ?  737  HIS   A CG  1 
ATOM   5790  N  ND1 . HIS   A 1 737  ? -52.17700  87.35500  -18.94400 1.000 75.47922  ?  737  HIS   A ND1 1 
ATOM   5791  C  CD2 . HIS   A 1 737  ? -51.62200  87.12100  -21.04400 1.000 77.15890  ?  737  HIS   A CD2 1 
ATOM   5792  C  CE1 . HIS   A 1 737  ? -52.37400  86.08700  -19.26200 1.000 64.85547  ?  737  HIS   A CE1 1 
ATOM   5793  N  NE2 . HIS   A 1 737  ? -52.04500  85.91900  -20.53000 1.000 72.73475  ?  737  HIS   A NE2 1 
ATOM   5794  N  N   . GLN   A 1 738  ? -49.49000  92.08800  -20.50200 1.000 40.93112  ?  738  GLN   A N   1 
ATOM   5795  C  CA  . GLN   A 1 738  ? -49.30300  93.52900  -20.63300 1.000 48.94218  ?  738  GLN   A CA  1 
ATOM   5796  C  C   . GLN   A 1 738  ? -48.69100  93.88900  -21.98100 1.000 54.71658  ?  738  GLN   A C   1 
ATOM   5797  O  O   . GLN   A 1 738  ? -48.90000  95.00200  -22.47800 1.000 59.90216  ?  738  GLN   A O   1 
ATOM   5798  C  CB  . GLN   A 1 738  ? -48.42800  94.05800  -19.49500 1.000 44.68725  ?  738  GLN   A CB  1 
ATOM   5799  C  CG  . GLN   A 1 738  ? -48.87700  93.62700  -18.10900 1.000 54.10447  ?  738  GLN   A CG  1 
ATOM   5800  C  CD  . GLN   A 1 738  ? -49.43600  94.76500  -17.28400 1.000 67.64449  ?  738  GLN   A CD  1 
ATOM   5801  O  OE1 . GLN   A 1 738  ? -49.43700  95.91800  -17.71400 1.000 66.12928  ?  738  GLN   A OE1 1 
ATOM   5802  N  NE2 . GLN   A 1 738  ? -49.91600  94.44500  -16.08700 1.000 79.55892  ?  738  GLN   A NE2 1 
ATOM   5803  N  N   . LEU   A 1 739  ? -47.93600  92.96700  -22.58400 1.000 53.96075  ?  739  LEU   A N   1 
ATOM   5804  C  CA  . LEU   A 1 739  ? -47.39600  93.19600  -23.92000 1.000 50.73347  ?  739  LEU   A CA  1 
ATOM   5805  C  C   . LEU   A 1 739  ? -48.44900  92.99500  -25.00100 1.000 54.15513  ?  739  LEU   A C   1 
ATOM   5806  O  O   . LEU   A 1 739  ? -48.34800  93.59600  -26.07600 1.000 59.45603  ?  739  LEU   A O   1 
ATOM   5807  C  CB  . LEU   A 1 739  ? -46.19900  92.27800  -24.17400 1.000 46.36207  ?  739  LEU   A CB  1 
ATOM   5808  C  CG  . LEU   A 1 739  ? -44.92700  92.59000  -23.38100 1.000 48.66696  ?  739  LEU   A CG  1 
ATOM   5809  C  CD1 . LEU   A 1 739  ? -43.83300  91.57800  -23.68600 1.000 48.50739  ?  739  LEU   A CD1 1 
ATOM   5810  C  CD2 . LEU   A 1 739  ? -44.45300  94.00500  -23.66100 1.000 57.00077  ?  739  LEU   A CD2 1 
ATOM   5811  N  N   . LYS   A 1 740  ? -49.45600  92.15500  -24.74300 1.000 52.87095  ?  740  LYS   A N   1 
ATOM   5812  C  CA  . LYS   A 1 740  ? -50.56700  92.02900  -25.68100 1.000 48.75894  ?  740  LYS   A CA  1 
ATOM   5813  C  C   . LYS   A 1 740  ? -51.36400  93.32400  -25.76000 1.000 55.64699  ?  740  LYS   A C   1 
ATOM   5814  O  O   . LYS   A 1 740  ? -51.78700  93.73400  -26.84800 1.000 65.40484  ?  740  LYS   A O   1 
ATOM   5815  C  CB  . LYS   A 1 740  ? -51.47700  90.87000  -25.27700 1.000 43.60765  ?  740  LYS   A CB  1 
ATOM   5816  C  CG  . LYS   A 1 740  ? -50.90600  89.49000  -25.55000 1.000 54.62223  ?  740  LYS   A CG  1 
ATOM   5817  C  CD  . LYS   A 1 740  ? -51.96600  88.42000  -25.33100 1.000 57.99032  ?  740  LYS   A CD  1 
ATOM   5818  C  CE  . LYS   A 1 740  ? -51.41800  87.02100  -25.55700 1.000 58.94587  ?  740  LYS   A CE  1 
ATOM   5819  N  NZ  . LYS   A 1 740  ? -52.47200  85.98500  -25.36500 1.000 71.85788  ?  740  LYS   A NZ  1 
ATOM   5820  N  N   . ASN   A 1 741  ? -51.58300  93.97700  -24.61600 1.000 56.18970  ?  741  ASN   A N   1 
ATOM   5821  C  CA  . ASN   A 1 741  ? -52.24800  95.27400  -24.61700 1.000 55.81261  ?  741  ASN   A CA  1 
ATOM   5822  C  C   . ASN   A 1 741  ? -51.46500  96.30000  -25.42700 1.000 66.89864  ?  741  ASN   A C   1 
ATOM   5823  O  O   . ASN   A 1 741  ? -52.05900  97.20600  -26.02200 1.000 84.21726  ?  741  ASN   A O   1 
ATOM   5824  C  CB  . ASN   A 1 741  ? -52.44300  95.75800  -23.17900 1.000 55.89106  ?  741  ASN   A CB  1 
ATOM   5825  C  CG  . ASN   A 1 741  ? -53.12700  97.10900  -23.10300 1.000 79.41258  ?  741  ASN   A CG  1 
ATOM   5826  O  OD1 . ASN   A 1 741  ? -52.47600  98.15200  -23.17200 1.000 85.01892  ?  741  ASN   A OD1 1 
ATOM   5827  N  ND2 . ASN   A 1 741  ? -54.44600  97.09800  -22.95300 1.000 83.99921  ?  741  ASN   A ND2 1 
ATOM   5828  N  N   . ILE   A 1 742  ? -50.13800  96.17300  -25.46400 1.000 72.09494  ?  742  ILE   A N   1 
ATOM   5829  C  CA  . ILE   A 1 742  ? -49.32900  97.05700  -26.29600 1.000 55.77297  ?  742  ILE   A CA  1 
ATOM   5830  C  C   . ILE   A 1 742  ? -49.45600  96.66900  -27.76400 1.000 64.13654  ?  742  ILE   A C   1 
ATOM   5831  O  O   . ILE   A 1 742  ? -49.57400  97.53300  -28.64200 1.000 89.34735  ?  742  ILE   A O   1 
ATOM   5832  C  CB  . ILE   A 1 742  ? -47.86400  97.04100  -25.81900 1.000 58.58723  ?  742  ILE   A CB  1 
ATOM   5833  C  CG1 . ILE   A 1 742  ? -47.68300  97.96700  -24.61400 1.000 71.44351  ?  742  ILE   A CG1 1 
ATOM   5834  C  CG2 . ILE   A 1 742  ? -46.91700  97.41800  -26.94800 1.000 80.33312  ?  742  ILE   A CG2 1 
ATOM   5835  C  CD1 . ILE   A 1 742  ? -48.20000  99.36600  -24.84900 1.000 83.18394  ?  742  ILE   A CD1 1 
ATOM   5836  N  N   . GLY   A 1 743  ? -49.44700  95.37100  -28.05300 1.000 65.34560  ?  743  GLY   A N   1 
ATOM   5837  C  CA  . GLY   A 1 743  ? -49.61400  94.90100  -29.41300 1.000 61.83616  ?  743  GLY   A CA  1 
ATOM   5838  C  C   . GLY   A 1 743  ? -48.53100  93.94200  -29.85800 1.000 62.53724  ?  743  GLY   A C   1 
ATOM   5839  O  O   . GLY   A 1 743  ? -48.47700  93.55800  -31.03000 1.000 65.22243  ?  743  GLY   A O   1 
ATOM   5840  N  N   . LEU   A 1 744  ? -47.66400  93.54400  -28.93200 1.000 59.69235  ?  744  LEU   A N   1 
ATOM   5841  C  CA  . LEU   A 1 744  ? -46.55800  92.64600  -29.22200 1.000 55.93855  ?  744  LEU   A CA  1 
ATOM   5842  C  C   . LEU   A 1 744  ? -46.80300  91.28700  -28.57900 1.000 53.21513  ?  744  LEU   A C   1 
ATOM   5843  O  O   . LEU   A 1 744  ? -47.37800  91.18800  -27.49100 1.000 48.22627  ?  744  LEU   A O   1 
ATOM   5844  C  CB  . LEU   A 1 744  ? -45.23400  93.23000  -28.72400 1.000 55.56728  ?  744  LEU   A CB  1 
ATOM   5845  C  CG  . LEU   A 1 744  ? -44.97600  94.68600  -29.11300 1.000 50.04524  ?  744  LEU   A CG  1 
ATOM   5846  C  CD1 . LEU   A 1 744  ? -43.66300  95.17000  -28.52300 1.000 40.57127  ?  744  LEU   A CD1 1 
ATOM   5847  C  CD2 . LEU   A 1 744  ? -44.98800  94.85500  -30.62600 1.000 66.45491  ?  744  LEU   A CD2 1 
ATOM   5848  N  N   . SER   A 1 745  ? -46.35200  90.23900  -29.26200 1.000 51.27119  ?  745  SER   A N   1 
ATOM   5849  C  CA  . SER   A 1 745  ? -46.59300  88.86200  -28.85200 1.000 52.50573  ?  745  SER   A CA  1 
ATOM   5850  C  C   . SER   A 1 745  ? -45.27600  88.22500  -28.43100 1.000 54.04236  ?  745  SER   A C   1 
ATOM   5851  O  O   . SER   A 1 745  ? -44.33300  88.15500  -29.22800 1.000 58.07418  ?  745  SER   A O   1 
ATOM   5852  C  CB  . SER   A 1 745  ? -47.23600  88.06600  -29.98700 1.000 50.38103  ?  745  SER   A CB  1 
ATOM   5853  O  OG  . SER   A 1 745  ? -48.19200  88.85300  -30.67600 1.000 60.17463  ?  745  SER   A OG  1 
ATOM   5854  N  N   . LEU   A 1 746  ? -45.21500  87.76100  -27.18700 1.000 46.40527  ?  746  LEU   A N   1 
ATOM   5855  C  CA  . LEU   A 1 746  ? -44.04800  87.06900  -26.65800 1.000 43.37114  ?  746  LEU   A CA  1 
ATOM   5856  C  C   . LEU   A 1 746  ? -44.48100  85.71000  -26.13100 1.000 48.58708  ?  746  LEU   A C   1 
ATOM   5857  O  O   . LEU   A 1 746  ? -45.48500  85.60900  -25.41900 1.000 59.41127  ?  746  LEU   A O   1 
ATOM   5858  C  CB  . LEU   A 1 746  ? -43.38000  87.88000  -25.54400 1.000 39.14144  ?  746  LEU   A CB  1 
ATOM   5859  C  CG  . LEU   A 1 746  ? -42.00600  87.38300  -25.09600 1.000 40.78513  ?  746  LEU   A CG  1 
ATOM   5860  C  CD1 . LEU   A 1 746  ? -40.97600  87.60200  -26.19500 1.000 42.10344  ?  746  LEU   A CD1 1 
ATOM   5861  C  CD2 . LEU   A 1 746  ? -41.58200  88.06600  -23.80600 1.000 51.12095  ?  746  LEU   A CD2 1 
ATOM   5862  N  N   . ARG   A 1 747  ? -43.73200  84.67200  -26.48400 1.000 47.14139  ?  747  ARG   A N   1 
ATOM   5863  C  CA  . ARG   A 1 747  ? -44.02000  83.33200  -26.00000 1.000 46.74057  ?  747  ARG   A CA  1 
ATOM   5864  C  C   . ARG   A 1 747  ? -43.33600  83.09500  -24.65900 1.000 54.23429  ?  747  ARG   A C   1 
ATOM   5865  O  O   . ARG   A 1 747  ? -42.28800  83.67600  -24.36100 1.000 61.56618  ?  747  ARG   A O   1 
ATOM   5866  C  CB  . ARG   A 1 747  ? -43.57300  82.27500  -27.01100 1.000 50.14101  ?  747  ARG   A CB  1 
ATOM   5867  C  CG  . ARG   A 1 747  ? -44.19300  82.43400  -28.39000 1.000 61.30017  ?  747  ARG   A CG  1 
ATOM   5868  C  CD  . ARG   A 1 747  ? -44.08000  81.14800  -29.19400 1.000 63.27118  ?  747  ARG   A CD  1 
ATOM   5869  N  NE  . ARG   A 1 747  ? -42.72700  80.60600  -29.17700 1.000 51.60441  ?  747  ARG   A NE  1 
ATOM   5870  C  CZ  . ARG   A 1 747  ? -41.79000  80.89600  -30.06900 1.000 63.61547  ?  747  ARG   A CZ  1 
ATOM   5871  N  NH1 . ARG   A 1 747  ? -42.02300  81.72700  -31.07100 1.000 59.98241  ?  747  ARG   A NH1 1 
ATOM   5872  N  NH2 . ARG   A 1 747  ? -40.58800  80.34000  -29.95200 1.000 76.67697  ?  747  ARG   A NH2 1 
ATOM   5873  N  N   . TYR   A 1 748  ? -43.94900  82.22600  -23.84900 1.000 56.96100  ?  748  TYR   A N   1 
ATOM   5874  C  CA  . TYR   A 1 748  ? -43.43300  81.93800  -22.51400 1.000 46.16501  ?  748  TYR   A CA  1 
ATOM   5875  C  C   . TYR   A 1 748  ? -41.98800  81.45200  -22.55600 1.000 53.80943  ?  748  TYR   A C   1 
ATOM   5876  O  O   . TYR   A 1 748  ? -41.21800  81.71700  -21.62500 1.000 56.05282  ?  748  TYR   A O   1 
ATOM   5877  C  CB  . TYR   A 1 748  ? -44.33300  80.90300  -21.83100 1.000 39.18109  ?  748  TYR   A CB  1 
ATOM   5878  C  CG  . TYR   A 1 748  ? -44.02200  80.64800  -20.37500 1.000 31.72336  ?  748  TYR   A CG  1 
ATOM   5879  C  CD1 . TYR   A 1 748  ? -44.60700  81.41400  -19.37500 1.000 27.98245  ?  748  TYR   A CD1 1 
ATOM   5880  C  CD2 . TYR   A 1 748  ? -43.15700  79.62900  -19.99700 1.000 48.78907  ?  748  TYR   A CD2 1 
ATOM   5881  C  CE1 . TYR   A 1 748  ? -44.33000  81.17900  -18.04000 1.000 37.44845  ?  748  TYR   A CE1 1 
ATOM   5882  C  CE2 . TYR   A 1 748  ? -42.87500  79.38600  -18.66500 1.000 47.62087  ?  748  TYR   A CE2 1 
ATOM   5883  C  CZ  . TYR   A 1 748  ? -43.46300  80.16400  -17.69200 1.000 49.64468  ?  748  TYR   A CZ  1 
ATOM   5884  O  OH  . TYR   A 1 748  ? -43.18200  79.92200  -16.36800 1.000 61.97152  ?  748  TYR   A OH  1 
ATOM   5885  N  N   . ASP   A 1 749  ? -41.60000  80.75100  -23.62400 1.000 51.71719  ?  749  ASP   A N   1 
ATOM   5886  C  CA  . ASP   A 1 749  ? -40.22500  80.28600  -23.76400 1.000 46.82444  ?  749  ASP   A CA  1 
ATOM   5887  C  C   . ASP   A 1 749  ? -39.26600  81.40600  -24.14900 1.000 55.13312  ?  749  ASP   A C   1 
ATOM   5888  O  O   . ASP   A 1 749  ? -38.11000  81.40000  -23.71100 1.000 55.79633  ?  749  ASP   A O   1 
ATOM   5889  C  CB  . ASP   A 1 749  ? -40.15200  79.17000  -24.80700 1.000 35.66456  ?  749  ASP   A CB  1 
ATOM   5890  C  CG  . ASP   A 1 749  ? -40.96900  79.47900  -26.04200 1.000 66.00799  ?  749  ASP   A CG  1 
ATOM   5891  O  OD1 . ASP   A 1 749  ? -42.20800  79.56900  -25.91700 1.000 76.00734  ?  749  ASP   A OD1 1 
ATOM   5892  O  OD2 . ASP   A 1 749  ? -40.37600  79.65200  -27.12800 1.000 57.63008  -1 749  ASP   A OD2 1 
ATOM   5893  N  N   . GLN   A 1 750  ? -39.71700  82.36400  -24.96400 1.000 52.24446  ?  750  GLN   A N   1 
ATOM   5894  C  CA  . GLN   A 1 750  ? -38.84700  83.43600  -25.43600 1.000 55.30272  ?  750  GLN   A CA  1 
ATOM   5895  C  C   . GLN   A 1 750  ? -38.38500  84.37000  -24.32400 1.000 53.34615  ?  750  GLN   A C   1 
ATOM   5896  O  O   . GLN   A 1 750  ? -37.43300  85.12900  -24.53600 1.000 46.85732  ?  750  GLN   A O   1 
ATOM   5897  C  CB  . GLN   A 1 750  ? -39.55700  84.23700  -26.53000 1.000 55.29758  ?  750  GLN   A CB  1 
ATOM   5898  C  CG  . GLN   A 1 750  ? -39.98200  83.39200  -27.71700 1.000 47.64218  ?  750  GLN   A CG  1 
ATOM   5899  C  CD  . GLN   A 1 750  ? -40.52400  84.21600  -28.86600 1.000 48.63190  ?  750  GLN   A CD  1 
ATOM   5900  O  OE1 . GLN   A 1 750  ? -41.47200  84.98500  -28.70300 1.000 57.79206  ?  750  GLN   A OE1 1 
ATOM   5901  N  NE2 . GLN   A 1 750  ? -39.92200  84.06100  -30.03900 1.000 46.21435  ?  750  GLN   A NE2 1 
ATOM   5902  N  N   . LEU   A 1 751  ? -39.02700  84.33600  -23.15300 1.000 53.00793  ?  751  LEU   A N   1 
ATOM   5903  C  CA  . LEU   A 1 751  ? -38.55600  85.14600  -22.03400 1.000 52.03198  ?  751  LEU   A CA  1 
ATOM   5904  C  C   . LEU   A 1 751  ? -37.27900  84.56600  -21.43700 1.000 53.22537  ?  751  LEU   A C   1 
ATOM   5905  O  O   . LEU   A 1 751  ? -36.35800  85.31100  -21.08600 1.000 49.90020  ?  751  LEU   A O   1 
ATOM   5906  C  CB  . LEU   A 1 751  ? -39.65300  85.25900  -20.97100 1.000 33.98137  ?  751  LEU   A CB  1 
ATOM   5907  C  CG  . LEU   A 1 751  ? -39.53400  86.35500  -19.90600 1.000 35.05157  ?  751  LEU   A CG  1 
ATOM   5908  C  CD1 . LEU   A 1 751  ? -38.65000  85.92900  -18.73800 1.000 42.13288  ?  751  LEU   A CD1 1 
ATOM   5909  C  CD2 . LEU   A 1 751  ? -39.01100  87.63800  -20.53000 1.000 29.41159  ?  751  LEU   A CD2 1 
ATOM   5910  N  N   . PHE   A 1 752  ? -37.20500  83.23900  -21.31100 1.000 54.30348  ?  752  PHE   A N   1 
ATOM   5911  C  CA  . PHE   A 1 752  ? -36.00900  82.61700  -20.75500 1.000 47.10232  ?  752  PHE   A CA  1 
ATOM   5912  C  C   . PHE   A 1 752  ? -34.84100  82.64500  -21.72900 1.000 44.54150  ?  752  PHE   A C   1 
ATOM   5913  O  O   . PHE   A 1 752  ? -33.68900  82.52000  -21.29900 1.000 46.86272  ?  752  PHE   A O   1 
ATOM   5914  C  CB  . PHE   A 1 752  ? -36.31700  81.18300  -20.32800 1.000 39.73258  ?  752  PHE   A CB  1 
ATOM   5915  C  CG  . PHE   A 1 752  ? -37.42400  81.08300  -19.31800 1.000 51.60333  ?  752  PHE   A CG  1 
ATOM   5916  C  CD1 . PHE   A 1 752  ? -37.16200  81.22500  -17.96500 1.000 46.78905  ?  752  PHE   A CD1 1 
ATOM   5917  C  CD2 . PHE   A 1 752  ? -38.73000  80.86000  -19.72300 1.000 47.79376  ?  752  PHE   A CD2 1 
ATOM   5918  C  CE1 . PHE   A 1 752  ? -38.18200  81.14000  -17.03300 1.000 37.46711  ?  752  PHE   A CE1 1 
ATOM   5919  C  CE2 . PHE   A 1 752  ? -39.75200  80.77300  -18.79600 1.000 44.11667  ?  752  PHE   A CE2 1 
ATOM   5920  C  CZ  . PHE   A 1 752  ? -39.47800  80.91400  -17.45000 1.000 42.63644  ?  752  PHE   A CZ  1 
ATOM   5921  N  N   . THR   A 1 753  ? -35.10800  82.80700  -23.02400 1.000 46.30525  ?  753  THR   A N   1 
ATOM   5922  C  CA  . THR   A 1 753  ? -34.04800  83.00000  -24.00300 1.000 49.64733  ?  753  THR   A CA  1 
ATOM   5923  C  C   . THR   A 1 753  ? -33.71100  84.46900  -24.22000 1.000 53.43695  ?  753  THR   A C   1 
ATOM   5924  O  O   . THR   A 1 753  ? -32.66000  84.77200  -24.79600 1.000 62.55962  ?  753  THR   A O   1 
ATOM   5925  C  CB  . THR   A 1 753  ? -34.43400  82.36600  -25.34400 1.000 41.21082  ?  753  THR   A CB  1 
ATOM   5926  O  OG1 . THR   A 1 753  ? -35.64700  82.95800  -25.82400 1.000 57.24775  ?  753  THR   A OG1 1 
ATOM   5927  C  CG2 . THR   A 1 753  ? -34.63600  80.86900  -25.18500 1.000 41.59063  ?  753  THR   A CG2 1 
ATOM   5928  N  N   . HIS   A 1 754  ? -34.57600  85.38000  -23.77900 1.000 52.23134  ?  754  HIS   A N   1 
ATOM   5929  C  CA  . HIS   A 1 754  ? -34.33300  86.82100  -23.85100 1.000 52.52843  ?  754  HIS   A CA  1 
ATOM   5930  C  C   . HIS   A 1 754  ? -34.72100  87.44300  -22.51500 1.000 51.87681  ?  754  HIS   A C   1 
ATOM   5931  O  O   . HIS   A 1 754  ? -35.72200  88.16300  -22.41300 1.000 41.22374  ?  754  HIS   A O   1 
ATOM   5932  C  CB  . HIS   A 1 754  ? -35.11100  87.45200  -25.00600 1.000 45.55876  ?  754  HIS   A CB  1 
ATOM   5933  C  CG  . HIS   A 1 754  ? -34.77300  86.87300  -26.34500 1.000 56.46772  ?  754  HIS   A CG  1 
ATOM   5934  N  ND1 . HIS   A 1 754  ? -35.14200  85.59800  -26.71800 1.000 49.33719  ?  754  HIS   A ND1 1 
ATOM   5935  C  CD2 . HIS   A 1 754  ? -34.09200  87.39000  -27.39400 1.000 63.56616  ?  754  HIS   A CD2 1 
ATOM   5936  C  CE1 . HIS   A 1 754  ? -34.70600  85.35700  -27.94100 1.000 57.15912  ?  754  HIS   A CE1 1 
ATOM   5937  N  NE2 . HIS   A 1 754  ? -34.06500  86.42800  -28.37400 1.000 59.21377  ?  754  HIS   A NE2 1 
ATOM   5938  N  N   . PRO   A 1 755  ? -33.94400  87.18200  -21.46300 1.000 46.41988  ?  755  PRO   A N   1 
ATOM   5939  C  CA  . PRO   A 1 755  ? -34.33400  87.60300  -20.11400 1.000 36.59895  ?  755  PRO   A CA  1 
ATOM   5940  C  C   . PRO   A 1 755  ? -34.00400  89.04600  -19.77000 1.000 37.26697  ?  755  PRO   A C   1 
ATOM   5941  O  O   . PRO   A 1 755  ? -34.10100  89.41600  -18.59600 1.000 38.56320  ?  755  PRO   A O   1 
ATOM   5942  C  CB  . PRO   A 1 755  ? -33.53200  86.64000  -19.23000 1.000 30.53773  ?  755  PRO   A CB  1 
ATOM   5943  C  CG  . PRO   A 1 755  ? -32.28400  86.40800  -20.00300 1.000 49.39642  ?  755  PRO   A CG  1 
ATOM   5944  C  CD  . PRO   A 1 755  ? -32.67800  86.42600  -21.46000 1.000 41.03730  ?  755  PRO   A CD  1 
ATOM   5945  N  N   . THR   A 1 756  ? -33.61100  89.86700  -20.73900 1.000 30.59262  ?  756  THR   A N   1 
ATOM   5946  C  CA  . THR   A 1 756  ? -33.36500  91.28200  -20.51000 1.000 38.64226  ?  756  THR   A CA  1 
ATOM   5947  C  C   . THR   A 1 756  ? -34.15000  92.09600  -21.52800 1.000 42.20402  ?  756  THR   A C   1 
ATOM   5948  O  O   . THR   A 1 756  ? -34.62900  91.57300  -22.53700 1.000 54.84405  ?  756  THR   A O   1 
ATOM   5949  C  CB  . THR   A 1 756  ? -31.87300  91.63300  -20.60400 1.000 50.86991  ?  756  THR   A CB  1 
ATOM   5950  O  OG1 . THR   A 1 756  ? -31.41600  91.43400  -21.94700 1.000 54.09511  ?  756  THR   A OG1 1 
ATOM   5951  C  CG2 . THR   A 1 756  ? -31.05800  90.76000  -19.66300 1.000 34.93018  ?  756  THR   A CG2 1 
ATOM   5952  N  N   . ILE   A 1 757  ? -34.27900  93.39400  -21.24700 1.000 38.97950  ?  757  ILE   A N   1 
ATOM   5953  C  CA  . ILE   A 1 757  ? -34.96100  94.28500  -22.18100 1.000 40.74172  ?  757  ILE   A CA  1 
ATOM   5954  C  C   . ILE   A 1 757  ? -34.14700  94.45000  -23.45700 1.000 48.90647  ?  757  ILE   A C   1 
ATOM   5955  O  O   . ILE   A 1 757  ? -34.71200  94.63300  -24.54300 1.000 49.48616  ?  757  ILE   A O   1 
ATOM   5956  C  CB  . ILE   A 1 757  ? -35.24400  95.63900  -21.50600 1.000 34.13637  ?  757  ILE   A CB  1 
ATOM   5957  C  CG1 . ILE   A 1 757  ? -36.10200  95.43400  -20.25900 1.000 42.69174  ?  757  ILE   A CG1 1 
ATOM   5958  C  CG2 . ILE   A 1 757  ? -35.93300  96.59100  -22.47000 1.000 46.20814  ?  757  ILE   A CG2 1 
ATOM   5959  C  CD1 . ILE   A 1 757  ? -36.32100  96.69200  -19.46200 1.000 43.69622  ?  757  ILE   A CD1 1 
ATOM   5960  N  N   . ARG   A 1 758  ? -32.81800  94.37900  -23.35200 1.000 41.25370  ?  758  ARG   A N   1 
ATOM   5961  C  CA  . ARG   A 1 758  ? -31.96100  94.49000  -24.52800 1.000 43.89250  ?  758  ARG   A CA  1 
ATOM   5962  C  C   . ARG   A 1 758  ? -32.28300  93.40200  -25.54500 1.000 54.93321  ?  758  ARG   A C   1 
ATOM   5963  O  O   . ARG   A 1 758  ? -32.51100  93.68500  -26.72600 1.000 65.05274  ?  758  ARG   A O   1 
ATOM   5964  C  CB  . ARG   A 1 758  ? -30.49400  94.41700  -24.10400 1.000 55.13032  ?  758  ARG   A CB  1 
ATOM   5965  C  CG  . ARG   A 1 758  ? -29.49300  94.78200  -25.18400 1.000 48.20774  ?  758  ARG   A CG  1 
ATOM   5966  C  CD  . ARG   A 1 758  ? -28.10600  94.94400  -24.58200 1.000 46.58866  ?  758  ARG   A CD  1 
ATOM   5967  N  NE  . ARG   A 1 758  ? -27.71900  96.34500  -24.45700 1.000 76.13267  ?  758  ARG   A NE  1 
ATOM   5968  C  CZ  . ARG   A 1 758  ? -26.76100  96.79000  -23.65300 1.000 72.62828  ?  758  ARG   A CZ  1 
ATOM   5969  N  NH1 . ARG   A 1 758  ? -26.10400  95.97800  -22.84500 1.000 77.26093  ?  758  ARG   A NH1 1 
ATOM   5970  N  NH2 . ARG   A 1 758  ? -26.45600  98.08400  -23.66000 1.000 67.61098  ?  758  ARG   A NH2 1 
ATOM   5971  N  N   . GLN   A 1 759  ? -32.31100  92.14500  -25.09700 1.000 50.38422  ?  759  GLN   A N   1 
ATOM   5972  C  CA  . GLN   A 1 759  ? -32.64600  91.04700  -25.99600 1.000 50.61008  ?  759  GLN   A CA  1 
ATOM   5973  C  C   . GLN   A 1 759  ? -34.12500  91.06700  -26.36000 1.000 45.19388  ?  759  GLN   A C   1 
ATOM   5974  O  O   . GLN   A 1 759  ? -34.49700  90.72700  -27.48900 1.000 52.53334  ?  759  GLN   A O   1 
ATOM   5975  C  CB  . GLN   A 1 759  ? -32.27400  89.71500  -25.34800 1.000 60.53508  ?  759  GLN   A CB  1 
ATOM   5976  C  CG  . GLN   A 1 759  ? -30.94300  89.73800  -24.61900 1.000 43.92151  ?  759  GLN   A CG  1 
ATOM   5977  C  CD  . GLN   A 1 759  ? -30.74000  88.51600  -23.74700 1.000 52.02237  ?  759  GLN   A CD  1 
ATOM   5978  O  OE1 . GLN   A 1 759  ? -30.45700  88.63100  -22.55500 1.000 51.22596  ?  759  GLN   A OE1 1 
ATOM   5979  N  NE2 . GLN   A 1 759  ? -30.88200  87.33600  -24.34000 1.000 64.69643  ?  759  GLN   A NE2 1 
ATOM   5980  N  N   . LEU   A 1 760  ? -34.98100  91.46000  -25.41300 1.000 43.45345  ?  760  LEU   A N   1 
ATOM   5981  C  CA  . LEU   A 1 760  ? -36.41100  91.52100  -25.68900 1.000 47.94305  ?  760  LEU   A CA  1 
ATOM   5982  C  C   . LEU   A 1 760  ? -36.71200  92.53100  -26.78800 1.000 56.39971  ?  760  LEU   A C   1 
ATOM   5983  O  O   . LEU   A 1 760  ? -37.57700  92.29400  -27.64000 1.000 54.89873  ?  760  LEU   A O   1 
ATOM   5984  C  CB  . LEU   A 1 760  ? -37.17500  91.86700  -24.41100 1.000 35.73543  ?  760  LEU   A CB  1 
ATOM   5985  C  CG  . LEU   A 1 760  ? -38.47100  91.09500  -24.16000 1.000 35.73798  ?  760  LEU   A CG  1 
ATOM   5986  C  CD1 . LEU   A 1 760  ? -38.21900  89.59700  -24.22300 1.000 30.36712  ?  760  LEU   A CD1 1 
ATOM   5987  C  CD2 . LEU   A 1 760  ? -39.06600  91.48100  -22.81700 1.000 35.22791  ?  760  LEU   A CD2 1 
ATOM   5988  N  N   . LYS   A 1 761  ? -36.00000  93.66000  -26.79200 1.000 50.23242  ?  761  LYS   A N   1 
ATOM   5989  C  CA  . LYS   A 1 761  ? -36.17100  94.63600  -27.86200 1.000 46.13007  ?  761  LYS   A CA  1 
ATOM   5990  C  C   . LYS   A 1 761  ? -35.77500  94.04200  -29.20700 1.000 57.09451  ?  761  LYS   A C   1 
ATOM   5991  O  O   . LYS   A 1 761  ? -36.51800  94.15100  -30.18700 1.000 62.51802  ?  761  LYS   A O   1 
ATOM   5992  C  CB  . LYS   A 1 761  ? -35.35800  95.89600  -27.56600 1.000 49.76279  ?  761  LYS   A CB  1 
ATOM   5993  C  CG  . LYS   A 1 761  ? -35.53800  96.99800  -28.59900 1.000 39.42330  ?  761  LYS   A CG  1 
ATOM   5994  C  CD  . LYS   A 1 761  ? -34.26300  97.23800  -29.38700 1.000 55.53760  ?  761  LYS   A CD  1 
ATOM   5995  C  CE  . LYS   A 1 761  ? -34.48800  98.24100  -30.50600 1.000 65.80812  ?  761  LYS   A CE  1 
ATOM   5996  N  NZ  . LYS   A 1 761  ? -33.20400  98.72300  -31.08800 1.000 75.95765  ?  761  LYS   A NZ  1 
ATOM   5997  N  N   . ARG   A 1 762  ? -34.60700  93.39000  -29.26700 1.000 48.03417  ?  762  ARG   A N   1 
ATOM   5998  C  CA  . ARG   A 1 762  ? -34.15900  92.78400  -30.51800 1.000 46.32270  ?  762  ARG   A CA  1 
ATOM   5999  C  C   . ARG   A 1 762  ? -35.16800  91.77200  -31.04600 1.000 55.69003  ?  762  ARG   A C   1 
ATOM   6000  O  O   . ARG   A 1 762  ? -35.31500  91.61800  -32.26400 1.000 53.21695  ?  762  ARG   A O   1 
ATOM   6001  C  CB  . ARG   A 1 762  ? -32.79200  92.12100  -30.32700 1.000 42.67367  ?  762  ARG   A CB  1 
ATOM   6002  C  CG  . ARG   A 1 762  ? -31.72300  93.04900  -29.76800 1.000 61.43374  ?  762  ARG   A CG  1 
ATOM   6003  C  CD  . ARG   A 1 762  ? -30.31600  92.46800  -29.89000 1.000 66.43574  ?  762  ARG   A CD  1 
ATOM   6004  N  NE  . ARG   A 1 762  ? -29.60000  93.00800  -31.04100 1.000 73.35960  ?  762  ARG   A NE  1 
ATOM   6005  C  CZ  . ARG   A 1 762  ? -29.12100  92.28200  -32.04300 1.000 86.23907  ?  762  ARG   A CZ  1 
ATOM   6006  N  NH1 . ARG   A 1 762  ? -29.21900  90.96200  -32.05000 1.000 93.60591  ?  762  ARG   A NH1 1 
ATOM   6007  N  NH2 . ARG   A 1 762  ? -28.52200  92.89500  -33.06000 1.000 74.33674  ?  762  ARG   A NH2 1 
ATOM   6008  N  N   . LEU   A 1 763  ? -35.88000  91.08700  -30.15000 1.000 56.52573  ?  763  LEU   A N   1 
ATOM   6009  C  CA  . LEU   A 1 763  ? -36.88500  90.12200  -30.58200 1.000 48.35446  ?  763  LEU   A CA  1 
ATOM   6010  C  C   . LEU   A 1 763  ? -38.13000  90.82200  -31.11300 1.000 50.42792  ?  763  LEU   A C   1 
ATOM   6011  O  O   . LEU   A 1 763  ? -38.70700  90.39700  -32.12100 1.000 63.04479  ?  763  LEU   A O   1 
ATOM   6012  C  CB  . LEU   A 1 763  ? -37.24100  89.19300  -29.42000 1.000 49.55775  ?  763  LEU   A CB  1 
ATOM   6013  C  CG  . LEU   A 1 763  ? -37.62700  87.73800  -29.70000 1.000 53.76282  ?  763  LEU   A CG  1 
ATOM   6014  C  CD1 . LEU   A 1 763  ? -37.68500  86.97200  -28.39300 1.000 47.48817  ?  763  LEU   A CD1 1 
ATOM   6015  C  CD2 . LEU   A 1 763  ? -38.95700  87.62800  -30.42500 1.000 71.09576  ?  763  LEU   A CD2 1 
ATOM   6016  N  N   . LEU   A 1 764  ? -38.55200  91.90300  -30.45700 1.000 48.53902  ?  764  LEU   A N   1 
ATOM   6017  C  CA  . LEU   A 1 764  ? -39.82900  92.54100  -30.74500 1.000 50.45635  ?  764  LEU   A CA  1 
ATOM   6018  C  C   . LEU   A 1 764  ? -39.71300  93.79000  -31.61200 1.000 62.51610  ?  764  LEU   A C   1 
ATOM   6019  O  O   . LEU   A 1 764  ? -40.74000  94.27700  -32.09600 1.000 71.29427  ?  764  LEU   A O   1 
ATOM   6020  C  CB  . LEU   A 1 764  ? -40.53800  92.90000  -29.43400 1.000 34.18650  ?  764  LEU   A CB  1 
ATOM   6021  C  CG  . LEU   A 1 764  ? -40.69900  91.74900  -28.43900 1.000 32.82123  ?  764  LEU   A CG  1 
ATOM   6022  C  CD1 . LEU   A 1 764  ? -40.94700  92.28600  -27.04000 1.000 28.91630  ?  764  LEU   A CD1 1 
ATOM   6023  C  CD2 . LEU   A 1 764  ? -41.82300  90.81600  -28.86700 1.000 40.68018  ?  764  LEU   A CD2 1 
ATOM   6024  N  N   . THR   A 1 765  ? -38.50500  94.32400  -31.81900 1.000 61.88865  ?  765  THR   A N   1 
ATOM   6025  C  CA  . THR   A 1 765  ? -38.36700  95.52000  -32.64600 1.000 52.47450  ?  765  THR   A CA  1 
ATOM   6026  C  C   . THR   A 1 765  ? -38.73100  95.25800  -34.10100 1.000 67.01147  ?  765  THR   A C   1 
ATOM   6027  O  O   . THR   A 1 765  ? -39.05500  96.20400  -34.82700 1.000 80.33432  ?  765  THR   A O   1 
ATOM   6028  C  CB  . THR   A 1 765  ? -36.94200  96.08000  -32.56200 1.000 52.71513  ?  765  THR   A CB  1 
ATOM   6029  O  OG1 . THR   A 1 765  ? -36.88500  97.35300  -33.21800 1.000 56.95355  ?  765  THR   A OG1 1 
ATOM   6030  C  CG2 . THR   A 1 765  ? -35.94600  95.13200  -33.22000 1.000 57.89430  ?  765  THR   A CG2 1 
ATOM   6031  N  N   . GLU   A 1 766  ? -38.69000  94.00200  -34.53900 1.000 72.39219  ?  766  GLU   A N   1 
ATOM   6032  C  CA  . GLU   A 1 766  ? -39.10300  93.62400  -35.88100 1.000 82.44296  ?  766  GLU   A CA  1 
ATOM   6033  C  C   . GLU   A 1 766  ? -40.58900  93.30200  -35.96400 1.000 90.67215  ?  766  GLU   A C   1 
ATOM   6034  O  O   . GLU   A 1 766  ? -41.07300  92.94300  -37.04200 1.000 96.84274  ?  766  GLU   A O   1 
ATOM   6035  C  CB  . GLU   A 1 766  ? -38.28500  92.42000  -36.36000 1.000 66.64571  ?  766  GLU   A CB  1 
ATOM   6036  C  CG  . GLU   A 1 766  ? -38.63400  91.12000  -35.65100 1.000 86.83157  ?  766  GLU   A CG  1 
ATOM   6037  C  CD  . GLU   A 1 766  ? -37.42800  90.22600  -35.44100 1.000 85.35602  ?  766  GLU   A CD  1 
ATOM   6038  O  OE1 . GLU   A 1 766  ? -36.31800  90.76200  -35.23400 1.000 86.60502  ?  766  GLU   A OE1 1 
ATOM   6039  O  OE2 . GLU   A 1 766  ? -37.58800  88.98800  -35.48300 1.000 95.16358  -1 766  GLU   A OE2 1 
ATOM   6040  N  N   . GLN   A 1 767  ? -41.31600  93.42000  -34.85700 1.000 87.87624  ?  767  GLN   A N   1 
ATOM   6041  C  CA  . GLN   A 1 767  ? -42.74000  93.12600  -34.81000 1.000 83.41561  ?  767  GLN   A CA  1 
ATOM   6042  C  C   . GLN   A 1 767  ? -43.54900  94.40600  -34.96300 1.000 80.49476  ?  767  GLN   A C   1 
ATOM   6043  O  O   . GLN   A 1 767  ? -43.16100  95.46400  -34.45700 1.000 80.26539  ?  767  GLN   A O   1 
ATOM   6044  C  CB  . GLN   A 1 767  ? -43.11200  92.43300  -33.49800 1.000 71.29399  ?  767  GLN   A CB  1 
ATOM   6045  C  CG  . GLN   A 1 767  ? -43.49200  90.97200  -33.65000 1.000 81.44996  ?  767  GLN   A CG  1 
ATOM   6046  C  CD  . GLN   A 1 767  ? -43.80200  90.31200  -32.32000 1.000 82.85445  ?  767  GLN   A CD  1 
ATOM   6047  O  OE1 . GLN   A 1 767  ? -44.26900  90.96100  -31.38400 1.000 74.72504  ?  767  GLN   A OE1 1 
ATOM   6048  N  NE2 . GLN   A 1 767  ? -43.53500  89.01400  -32.22900 1.000 99.43232  ?  767  GLN   A NE2 1 
ATOM   6049  N  N   . LYS   A 1 768  ? -44.67300  94.30000  -35.66200 1.000 87.02223  ?  768  LYS   A N   1 
ATOM   6050  C  CA  . LYS   A 1 768  ? -45.60400  95.40400  -35.84000 1.000 79.33793  ?  768  LYS   A CA  1 
ATOM   6051  C  C   . LYS   A 1 768  ? -46.75800  95.26200  -34.85700 1.000 85.16126  ?  768  LYS   A C   1 
ATOM   6052  O  O   . LYS   A 1 768  ? -47.23800  94.15300  -34.60400 1.000 89.53706  ?  768  LYS   A O   1 
ATOM   6053  C  CB  . LYS   A 1 768  ? -46.12900  95.44000  -37.27800 1.000 83.92282  ?  768  LYS   A CB  1 
ATOM   6054  C  CG  . LYS   A 1 768  ? -46.46600  94.06600  -37.84000 1.000 94.73059  ?  768  LYS   A CG  1 
ATOM   6055  C  CD  . LYS   A 1 768  ? -46.89600  94.13100  -39.29900 1.000 92.20247  ?  768  LYS   A CD  1 
ATOM   6056  C  CE  . LYS   A 1 768  ? -45.77500  94.64200  -40.19000 1.000 94.72646  ?  768  LYS   A CE  1 
ATOM   6057  N  NZ  . LYS   A 1 768  ? -45.81500  94.01600  -41.54300 1.000 54.49190  ?  768  LYS   A NZ  1 
ATOM   6058  N  N   . GLN   A 1 769  ? -47.19500  96.38900  -34.29700 1.000 77.44309  ?  769  GLN   A N   1 
ATOM   6059  C  CA  . GLN   A 1 769  ? -48.25500  96.37100  -33.29500 1.000 76.54071  ?  769  GLN   A CA  1 
ATOM   6060  C  C   . GLN   A 1 769  ? -49.56900  95.91900  -33.92400 1.000 79.06743  ?  769  GLN   A C   1 
ATOM   6061  O  O   . GLN   A 1 769  ? -50.10100  96.58400  -34.81800 1.000 84.46021  ?  769  GLN   A O   1 
ATOM   6062  C  CB  . GLN   A 1 769  ? -48.41300  97.75000  -32.65900 1.000 76.91690  ?  769  GLN   A CB  1 
ATOM   6063  C  CG  . GLN   A 1 769  ? -47.35000  98.09300  -31.62500 1.000 82.80332  ?  769  GLN   A CG  1 
ATOM   6064  C  CD  . GLN   A 1 769  ? -47.70800  99.32200  -30.80900 1.000 94.10527  ?  769  GLN   A CD  1 
ATOM   6065  O  OE1 . GLN   A 1 769  ? -48.84600  99.79100  -30.83900 1.000 103.42159 ?  769  GLN   A OE1 1 
ATOM   6066  N  NE2 . GLN   A 1 769  ? -46.73500  99.85100  -30.07500 1.000 81.31081  ?  769  GLN   A NE2 1 
ATOM   6067  N  N   . VAL   A 1 770  ? -50.08900  94.78900  -33.45100 1.000 75.73594  ?  770  VAL   A N   1 
ATOM   6068  C  CA  . VAL   A 1 770  ? -51.35500  94.23200  -33.91500 1.000 73.38266  ?  770  VAL   A CA  1 
ATOM   6069  C  C   . VAL   A 1 770  ? -52.42800  94.52600  -32.87800 1.000 78.60887  ?  770  VAL   A C   1 
ATOM   6070  O  O   . VAL   A 1 770  ? -52.20000  94.38000  -31.67000 1.000 88.05724  ?  770  VAL   A O   1 
ATOM   6071  C  CB  . VAL   A 1 770  ? -51.23000  92.71700  -34.17600 1.000 68.84739  ?  770  VAL   A CB  1 
ATOM   6072  C  CG1 . VAL   A 1 770  ? -52.60100  92.08200  -34.36300 1.000 72.19814  ?  770  VAL   A CG1 1 
ATOM   6073  C  CG2 . VAL   A 1 770  ? -50.35200  92.46200  -35.39200 1.000 75.44211  ?  770  VAL   A CG2 1 
ATOM   6074  N  N   . ASN   A 1 771  A -53.59900  94.95100  -33.34500 1.000 84.78326  ?  770  ASN   A N   1 
ATOM   6075  C  CA  . ASN   A 1 771  A -54.72600  95.24400  -32.47500 1.000 89.06929  ?  770  ASN   A CA  1 
ATOM   6076  C  C   . ASN   A 1 771  A -55.65600  94.04000  -32.38200 1.000 81.06680  ?  770  ASN   A C   1 
ATOM   6077  O  O   . ASN   A 1 771  A -55.82500  93.28500  -33.34300 1.000 83.29218  ?  770  ASN   A O   1 
ATOM   6078  C  CB  . ASN   A 1 771  A -55.49800  96.46700  -32.97300 1.000 77.31006  ?  770  ASN   A CB  1 
ATOM   6079  C  CG  . ASN   A 1 771  A -54.74800  97.76000  -32.73300 1.000 81.99405  ?  770  ASN   A CG  1 
ATOM   6080  O  OD1 . ASN   A 1 771  A -54.89500  98.38900  -31.68600 1.000 83.92171  ?  770  ASN   A OD1 1 
ATOM   6081  N  ND2 . ASN   A 1 771  A -53.92800  98.15800  -33.69800 1.000 81.76103  ?  770  ASN   A ND2 1 
ATOM   6082  N  N   . GLY   A 1 772  B -56.25600  93.87000  -31.20900 1.000 70.64332  ?  770  GLY   A N   1 
ATOM   6083  C  CA  . GLY   A 1 772  B -57.11900  92.74100  -30.94100 1.000 76.81592  ?  770  GLY   A CA  1 
ATOM   6084  C  C   . GLY   A 1 772  B -56.45600  91.56600  -30.26000 1.000 72.70514  ?  770  GLY   A C   1 
ATOM   6085  O  O   . GLY   A 1 772  B -57.10200  90.52400  -30.09900 1.000 71.43425  ?  770  GLY   A O   1 
ATOM   6086  N  N   . LEU   A 1 773  ? -55.19000  91.69600  -29.85400 1.000 89.66702  ?  771  LEU   A N   1 
ATOM   6087  C  CA  . LEU   A 1 773  ? -54.49800  90.59600  -29.19400 1.000 86.10048  ?  771  LEU   A CA  1 
ATOM   6088  C  C   . LEU   A 1 773  ? -55.07400  90.28700  -27.81900 1.000 90.91427  ?  771  LEU   A C   1 
ATOM   6089  O  O   . LEU   A 1 773  ? -54.87800  89.17600  -27.31500 1.000 92.28064  ?  771  LEU   A O   1 
ATOM   6090  C  CB  . LEU   A 1 773  ? -53.00600  90.90800  -29.06900 1.000 65.22350  ?  771  LEU   A CB  1 
ATOM   6091  C  CG  . LEU   A 1 773  ? -52.19100  90.91600  -30.36300 1.000 59.76936  ?  771  LEU   A CG  1 
ATOM   6092  C  CD1 . LEU   A 1 773  ? -50.71900  91.15200  -30.06200 1.000 58.07159  ?  771  LEU   A CD1 1 
ATOM   6093  C  CD2 . LEU   A 1 773  ? -52.38400  89.61400  -31.12500 1.000 64.24647  ?  771  LEU   A CD2 1 
ATOM   6094  N  N   . LEU   A 1 774  ? -55.77700  91.23700  -27.20500 1.000 87.80018  ?  772  LEU   A N   1 
ATOM   6095  C  CA  . LEU   A 1 774  ? -56.34700  91.06400  -25.86900 1.000 82.27603  ?  772  LEU   A CA  1 
ATOM   6096  C  C   . LEU   A 1 774  ? -57.82500  91.43800  -25.93700 1.000 78.52033  ?  772  LEU   A C   1 
ATOM   6097  O  O   . LEU   A 1 774  ? -58.17300  92.62200  -25.95800 1.000 75.19690  ?  772  LEU   A O   1 
ATOM   6098  C  CB  . LEU   A 1 774  ? -55.60100  91.91300  -24.84200 1.000 82.24149  ?  772  LEU   A CB  1 
ATOM   6099  C  CG  . LEU   A 1 774  ? -55.44700  91.32300  -23.43800 1.000 81.40473  ?  772  LEU   A CG  1 
ATOM   6100  C  CD1 . LEU   A 1 774  ? -54.61100  90.05300  -23.47900 1.000 79.15550  ?  772  LEU   A CD1 1 
ATOM   6101  C  CD2 . LEU   A 1 774  ? -54.83000  92.33900  -22.49000 1.000 59.27990  ?  772  LEU   A CD2 1 
ATOM   6102  N  N   . GLU   A 1 775  ? -58.69100  90.42700  -25.97500 1.000 83.64284  ?  773  GLU   A N   1 
ATOM   6103  C  CA  . GLU   A 1 775  ? -60.12600  90.67300  -26.03000 1.000 76.68971  ?  773  GLU   A CA  1 
ATOM   6104  C  C   . GLU   A 1 775  ? -60.74500  90.55100  -24.64300 1.000 87.14942  ?  773  GLU   A C   1 
ATOM   6105  O  O   . GLU   A 1 775  ? -60.36700  89.66500  -23.86800 1.000 94.17252  ?  773  GLU   A O   1 
ATOM   6106  C  CB  . GLU   A 1 775  ? -60.81700  89.69300  -26.98300 1.000 84.16972  ?  773  GLU   A CB  1 
ATOM   6107  C  CG  . GLU   A 1 775  ? -60.60100  88.21700  -26.66000 1.000 91.89547  ?  773  GLU   A CG  1 
ATOM   6108  C  CD  . GLU   A 1 775  ? -59.28000  87.68600  -27.18400 1.000 105.70899 ?  773  GLU   A CD  1 
ATOM   6109  O  OE1 . GLU   A 1 775  ? -58.86100  88.10900  -28.28300 1.000 98.24943  ?  773  GLU   A OE1 1 
ATOM   6110  O  OE2 . GLU   A 1 775  ? -58.65700  86.84900  -26.49600 1.000 85.35760  -1 773  GLU   A OE2 1 
ATOM   6111  N  N   . PRO   A 1 776  ? -61.68300  91.43000  -24.30000 1.000 77.73930  ?  774  PRO   A N   1 
ATOM   6112  C  CA  . PRO   A 1 776  ? -62.33400  91.34500  -22.98800 1.000 57.90787  ?  774  PRO   A CA  1 
ATOM   6113  C  C   . PRO   A 1 776  ? -63.22800  90.11700  -22.89800 1.000 68.60207  ?  774  PRO   A C   1 
ATOM   6114  O  O   . PRO   A 1 776  ? -63.53700  89.45200  -23.88800 1.000 73.75473  ?  774  PRO   A O   1 
ATOM   6115  C  CB  . PRO   A 1 776  ? -63.15300  92.63800  -22.90300 1.000 49.05706  ?  774  PRO   A CB  1 
ATOM   6116  C  CG  . PRO   A 1 776  ? -62.58300  93.53600  -23.96300 1.000 58.46852  ?  774  PRO   A CG  1 
ATOM   6117  C  CD  . PRO   A 1 776  ? -62.11100  92.62200  -25.04900 1.000 71.14487  ?  774  PRO   A CD  1 
ATOM   6118  N  N   . LEU   A 1 777  ? -63.64800  89.82400  -21.67200 1.000 63.90202  ?  775  LEU   A N   1 
ATOM   6119  C  CA  . LEU   A 1 777  ? -64.51700  88.68700  -21.40300 1.000 70.74781  ?  775  LEU   A CA  1 
ATOM   6120  C  C   . LEU   A 1 777  ? -65.97000  89.14400  -21.46400 1.000 70.05766  ?  775  LEU   A C   1 
ATOM   6121  O  O   . LEU   A 1 777  ? -66.37700  90.03900  -20.71500 1.000 71.17279  ?  775  LEU   A O   1 
ATOM   6122  C  CB  . LEU   A 1 777  ? -64.19000  88.07300  -20.04300 1.000 60.08488  ?  775  LEU   A CB  1 
ATOM   6123  C  CG  . LEU   A 1 777  ? -64.90500  86.76700  -19.69400 1.000 70.18833  ?  775  LEU   A CG  1 
ATOM   6124  C  CD1 . LEU   A 1 777  ? -64.86100  85.80300  -20.86700 1.000 64.02124  ?  775  LEU   A CD1 1 
ATOM   6125  C  CD2 . LEU   A 1 777  ? -64.27700  86.13400  -18.46400 1.000 61.24490  ?  775  LEU   A CD2 1 
ATOM   6126  N  N   . ARG   A 1 778  ? -66.74600  88.53900  -22.36000 1.000 66.53152  ?  776  ARG   A N   1 
ATOM   6127  C  CA  . ARG   A 1 778  ? -68.14700  88.91300  -22.50600 1.000 71.35038  ?  776  ARG   A CA  1 
ATOM   6128  C  C   . ARG   A 1 778  ? -68.95400  88.40800  -21.31700 1.000 72.70811  ?  776  ARG   A C   1 
ATOM   6129  O  O   . ARG   A 1 778  ? -68.92400  87.21700  -20.99300 1.000 74.31950  ?  776  ARG   A O   1 
ATOM   6130  C  CB  . ARG   A 1 778  ? -68.72000  88.34900  -23.80500 1.000 68.53397  ?  776  ARG   A CB  1 
ATOM   6131  C  CG  . ARG   A 1 778  ? -70.21300  88.59200  -23.96700 1.000 75.80549  ?  776  ARG   A CG  1 
ATOM   6132  C  CD  . ARG   A 1 778  ? -70.94900  87.31900  -24.35800 1.000 84.78939  ?  776  ARG   A CD  1 
ATOM   6133  N  NE  . ARG   A 1 778  ? -72.38100  87.41800  -24.09700 1.000 87.30518  ?  776  ARG   A NE  1 
ATOM   6134  C  CZ  . ARG   A 1 778  ? -73.24300  86.42200  -24.25400 1.000 93.01696  ?  776  ARG   A CZ  1 
ATOM   6135  N  NH1 . ARG   A 1 778  ? -72.85500  85.23300  -24.68600 1.000 101.02370 ?  776  ARG   A NH1 1 
ATOM   6136  N  NH2 . ARG   A 1 778  ? -74.52600  86.62300  -23.96900 1.000 76.77459  ?  776  ARG   A NH2 1 
ATOM   6137  N  N   . GLU   A 1 779  ? -69.68000  89.31500  -20.66800 1.000 69.11365  ?  777  GLU   A N   1 
ATOM   6138  C  CA  . GLU   A 1 779  ? -70.52700  88.94300  -19.54300 1.000 70.46316  ?  777  GLU   A CA  1 
ATOM   6139  C  C   . GLU   A 1 779  ? -71.79700  88.27800  -20.05500 1.000 76.18993  ?  777  GLU   A C   1 
ATOM   6140  O  O   . GLU   A 1 779  ? -72.54700  88.87400  -20.83700 1.000 64.56850  ?  777  GLU   A O   1 
ATOM   6141  C  CB  . GLU   A 1 779  ? -70.85800  90.16200  -18.68600 1.000 58.47069  ?  777  GLU   A CB  1 
ATOM   6142  C  CG  . GLU   A 1 779  ? -69.93000  90.32100  -17.49700 1.000 75.75944  ?  777  GLU   A CG  1 
ATOM   6143  C  CD  . GLU   A 1 779  ? -69.75400  89.02300  -16.72800 1.000 75.84074  ?  777  GLU   A CD  1 
ATOM   6144  O  OE1 . GLU   A 1 779  ? -70.77300  88.39700  -16.36300 1.000 77.41087  ?  777  GLU   A OE1 1 
ATOM   6145  O  OE2 . GLU   A 1 779  ? -68.59300  88.61800  -16.50300 1.000 64.48479  -1 777  GLU   A OE2 1 
ATOM   6146  N  N   . LEU   A 1 780  ? -72.03300  87.04500  -19.61500 1.000 73.78031  ?  778  LEU   A N   1 
ATOM   6147  C  CA  . LEU   A 1 780  ? -73.19800  86.29600  -20.06100 1.000 76.26473  ?  778  LEU   A CA  1 
ATOM   6148  C  C   . LEU   A 1 780  ? -74.48300  86.95700  -19.58100 1.000 79.33595  ?  778  LEU   A C   1 
ATOM   6149  O  O   . LEU   A 1 780  ? -74.56600  87.44900  -18.45200 1.000 82.85246  ?  778  LEU   A O   1 
ATOM   6150  C  CB  . LEU   A 1 780  ? -73.12900  84.85700  -19.55000 1.000 59.15374  ?  778  LEU   A CB  1 
ATOM   6151  C  CG  . LEU   A 1 780  ? -72.87400  83.77100  -20.59700 1.000 62.22369  ?  778  LEU   A CG  1 
ATOM   6152  C  CD1 . LEU   A 1 780  ? -71.51700  83.96200  -21.25700 1.000 67.43879  ?  778  LEU   A CD1 1 
ATOM   6153  C  CD2 . LEU   A 1 780  ? -72.98600  82.38800  -19.97300 1.000 49.15715  ?  778  LEU   A CD2 1 
ATOM   6154  N  N   . ASP   A 1 781  ? -75.48800  86.97200  -20.45200 1.000 75.40592  ?  779  ASP   A N   1 
ATOM   6155  C  CA  . ASP   A 1 781  ? -76.79100  87.49400  -20.07800 1.000 82.59423  ?  779  ASP   A CA  1 
ATOM   6156  C  C   . ASP   A 1 781  ? -77.49100  86.53400  -19.12100 1.000 81.45152  ?  779  ASP   A C   1 
ATOM   6157  O  O   . ASP   A 1 781  ? -77.12700  85.36100  -18.99600 1.000 84.97123  ?  779  ASP   A O   1 
ATOM   6158  C  CB  . ASP   A 1 781  ? -77.64900  87.73400  -21.32100 1.000 82.01341  ?  779  ASP   A CB  1 
ATOM   6159  C  CG  . ASP   A 1 781  ? -77.17800  88.92700  -22.13000 1.000 100.45884 ?  779  ASP   A CG  1 
ATOM   6160  O  OD1 . ASP   A 1 781  ? -76.85400  89.96800  -21.51900 1.000 95.38305  ?  779  ASP   A OD1 1 
ATOM   6161  O  OD2 . ASP   A 1 781  ? -77.12500  88.82300  -23.37400 1.000 91.35034  -1 779  ASP   A OD2 1 
ATOM   6162  N  N   . GLU   A 1 782  ? -78.51000  87.05100  -18.43700 1.000 78.13335  ?  780  GLU   A N   1 
ATOM   6163  C  CA  . GLU   A 1 782  ? -79.18500  86.27900  -17.40100 1.000 65.84923  ?  780  GLU   A CA  1 
ATOM   6164  C  C   . GLU   A 1 782  ? -79.86200  85.04800  -17.98700 1.000 68.10895  ?  780  GLU   A C   1 
ATOM   6165  O  O   . GLU   A 1 782  ? -80.57500  85.13000  -18.99200 1.000 72.14493  ?  780  GLU   A O   1 
ATOM   6166  C  CB  . GLU   A 1 782  ? -80.20800  87.15000  -16.67400 1.000 61.38725  ?  780  GLU   A CB  1 
ATOM   6167  C  CG  . GLU   A 1 782  ? -79.78400  87.53200  -15.26900 1.000 81.42073  ?  780  GLU   A CG  1 
ATOM   6168  C  CD  . GLU   A 1 782  ? -80.63900  88.63200  -14.67700 1.000 96.85733  ?  780  GLU   A CD  1 
ATOM   6169  O  OE1 . GLU   A 1 782  ? -81.81900  88.75000  -15.06900 1.000 102.53515 ?  780  GLU   A OE1 1 
ATOM   6170  O  OE2 . GLU   A 1 782  ? -80.12500  89.38500  -13.82300 1.000 97.57338  -1 780  GLU   A OE2 1 
ATOM   6171  N  N   . GLN   A 1 783  ? -79.62400  83.90200  -17.35400 1.000 66.70985  ?  781  GLN   A N   1 
ATOM   6172  C  CA  . GLN   A 1 783  ? -80.20800  82.63400  -17.76100 1.000 74.72924  ?  781  GLN   A CA  1 
ATOM   6173  C  C   . GLN   A 1 783  ? -80.60900  81.85800  -16.51500 1.000 60.73593  ?  781  GLN   A C   1 
ATOM   6174  O  O   . GLN   A 1 783  ? -80.15500  82.14900  -15.40600 1.000 59.49269  ?  781  GLN   A O   1 
ATOM   6175  C  CB  . GLN   A 1 783  ? -79.23100  81.80500  -18.60900 1.000 67.25274  ?  781  GLN   A CB  1 
ATOM   6176  C  CG  . GLN   A 1 783  ? -78.76400  82.49600  -19.87900 1.000 78.24076  ?  781  GLN   A CG  1 
ATOM   6177  C  CD  . GLN   A 1 783  ? -77.41500  81.99700  -20.35100 1.000 74.97932  ?  781  GLN   A CD  1 
ATOM   6178  O  OE1 . GLN   A 1 783  ? -77.10100  80.81300  -20.23200 1.000 70.34028  ?  781  GLN   A OE1 1 
ATOM   6179  N  NE2 . GLN   A 1 783  ? -76.60200  82.90300  -20.88200 1.000 73.30027  ?  781  GLN   A NE2 1 
ATOM   6180  N  N   . ALA   A 1 784  ? -81.47800  80.86600  -16.70900 1.000 55.29905  ?  782  ALA   A N   1 
ATOM   6181  C  CA  . ALA   A 1 784  ? -81.85400  79.99100  -15.60300 1.000 59.40234  ?  782  ALA   A CA  1 
ATOM   6182  C  C   . ALA   A 1 784  ? -80.66100  79.16200  -15.14600 1.000 66.01132  ?  782  ALA   A C   1 
ATOM   6183  O  O   . ALA   A 1 784  ? -80.24300  79.23200  -13.98500 1.000 72.73330  ?  782  ALA   A O   1 
ATOM   6184  C  CB  . ALA   A 1 784  ? -83.01600  79.08900  -16.01800 1.000 59.14402  ?  782  ALA   A CB  1 
ATOM   6185  N  N   . GLU   A 1 785  ? -80.09600  78.37800  -16.05600 1.000 66.11403  ?  783  GLU   A N   1 
ATOM   6186  C  CA  . GLU   A 1 785  ? -78.92100  77.56400  -15.79600 1.000 62.80218  ?  783  GLU   A CA  1 
ATOM   6187  C  C   . GLU   A 1 785  ? -77.72500  78.12900  -16.55100 1.000 68.79619  ?  783  GLU   A C   1 
ATOM   6188  O  O   . GLU   A 1 785  ? -77.87000  78.90400  -17.50100 1.000 66.80004  ?  783  GLU   A O   1 
ATOM   6189  C  CB  . GLU   A 1 785  ? -79.16500  76.11100  -16.21300 1.000 48.00815  ?  783  GLU   A CB  1 
ATOM   6190  C  CG  . GLU   A 1 785  ? -80.45400  75.52200  -15.67000 1.000 55.02392  ?  783  GLU   A CG  1 
ATOM   6191  C  CD  . GLU   A 1 785  ? -80.86900  74.26700  -16.40900 1.000 66.03024  ?  783  GLU   A CD  1 
ATOM   6192  O  OE1 . GLU   A 1 785  ? -80.94000  74.30800  -17.65500 1.000 72.87278  ?  783  GLU   A OE1 1 
ATOM   6193  O  OE2 . GLU   A 1 785  ? -81.11400  73.23800  -15.74500 1.000 63.28675  -1 783  GLU   A OE2 1 
ATOM   6194  N  N   . TYR   A 1 786  ? -76.53300  77.73100  -16.11500 1.000 61.94171  ?  784  TYR   A N   1 
ATOM   6195  C  CA  . TYR   A 1 786  ? -75.29300  78.12000  -16.76800 1.000 47.91156  ?  784  TYR   A CA  1 
ATOM   6196  C  C   . TYR   A 1 786  ? -74.40200  76.89900  -16.92500 1.000 59.41910  ?  784  TYR   A C   1 
ATOM   6197  O  O   . TYR   A 1 786  ? -74.33300  76.04800  -16.03200 1.000 71.94462  ?  784  TYR   A O   1 
ATOM   6198  C  CB  . TYR   A 1 786  ? -74.56000  79.21000  -15.97900 1.000 51.85283  ?  784  TYR   A CB  1 
ATOM   6199  C  CG  . TYR   A 1 786  ? -75.34500  80.49300  -15.84300 1.000 49.26006  ?  784  TYR   A CG  1 
ATOM   6200  C  CD1 . TYR   A 1 786  ? -75.33900  81.44400  -16.85500 1.000 57.50332  ?  784  TYR   A CD1 1 
ATOM   6201  C  CD2 . TYR   A 1 786  ? -76.09200  80.75600  -14.70300 1.000 61.51901  ?  784  TYR   A CD2 1 
ATOM   6202  C  CE1 . TYR   A 1 786  ? -76.05500  82.62000  -16.73600 1.000 63.98375  ?  784  TYR   A CE1 1 
ATOM   6203  C  CE2 . TYR   A 1 786  ? -76.81200  81.92900  -14.57400 1.000 70.90002  ?  784  TYR   A CE2 1 
ATOM   6204  C  CZ  . TYR   A 1 786  ? -76.79000  82.85700  -15.59400 1.000 62.88898  ?  784  TYR   A CZ  1 
ATOM   6205  O  OH  . TYR   A 1 786  ? -77.50500  84.02700  -15.47100 1.000 73.99215  ?  784  TYR   A OH  1 
ATOM   6206  N  N   . GLU   A 1 787  ? -73.72700  76.81400  -18.06500 1.000 56.88615  ?  785  GLU   A N   1 
ATOM   6207  C  CA  . GLU   A 1 787  ? -72.87000  75.67100  -18.33700 1.000 54.24044  ?  785  GLU   A CA  1 
ATOM   6208  C  C   . GLU   A 1 787  ? -71.60800  75.73400  -17.48700 1.000 56.99314  ?  785  GLU   A C   1 
ATOM   6209  O  O   . GLU   A 1 787  ? -71.04700  76.80800  -17.25200 1.000 37.85673  ?  785  GLU   A O   1 
ATOM   6210  C  CB  . GLU   A 1 787  ? -72.51200  75.62600  -19.81700 1.000 50.50930  ?  785  GLU   A CB  1 
ATOM   6211  C  CG  . GLU   A 1 787  ? -72.16200  76.97700  -20.38800 1.000 66.75097  ?  785  GLU   A CG  1 
ATOM   6212  C  CD  . GLU   A 1 787  ? -71.68200  76.88300  -21.81200 1.000 84.39111  ?  785  GLU   A CD  1 
ATOM   6213  O  OE1 . GLU   A 1 787  ? -72.33200  76.17900  -22.61300 1.000 86.82098  ?  785  GLU   A OE1 1 
ATOM   6214  O  OE2 . GLU   A 1 787  ? -70.64200  77.50000  -22.12600 1.000 93.03715  -1 785  GLU   A OE2 1 
ATOM   6215  N  N   . THR   A 1 788  ? -71.17100  74.57400  -17.01900 1.000 51.25360  ?  786  THR   A N   1 
ATOM   6216  C  CA  . THR   A 1 788  ? -69.99100  74.47600  -16.17600 1.000 33.19035  ?  786  THR   A CA  1 
ATOM   6217  C  C   . THR   A 1 788  ? -68.73000  74.37100  -17.02600 1.000 44.02912  ?  786  THR   A C   1 
ATOM   6218  O  O   . THR   A 1 788  ? -68.78000  74.09200  -18.22600 1.000 58.02273  ?  786  THR   A O   1 
ATOM   6219  C  CB  . THR   A 1 788  ? -70.09700  73.25900  -15.26000 1.000 45.65990  ?  786  THR   A CB  1 
ATOM   6220  O  OG1 . THR   A 1 788  ? -70.50800  72.12500  -16.03400 1.000 53.78164  ?  786  THR   A OG1 1 
ATOM   6221  C  CG2 . THR   A 1 788  ? -71.11400  73.50700  -14.15800 1.000 47.96056  ?  786  THR   A CG2 1 
ATOM   6222  N  N   . SER   A 1 789  ? -67.58800  74.59500  -16.38400 1.000 56.12254  ?  787  SER   A N   1 
ATOM   6223  C  CA  . SER   A 1 789  ? -66.30300  74.45200  -17.04800 1.000 43.43544  ?  787  SER   A CA  1 
ATOM   6224  C  C   . SER   A 1 789  ? -65.83000  73.00200  -16.97900 1.000 47.32236  ?  787  SER   A C   1 
ATOM   6225  O  O   . SER   A 1 789  ? -66.36500  72.18100  -16.23200 1.000 45.69765  ?  787  SER   A O   1 
ATOM   6226  C  CB  . SER   A 1 789  ? -65.26500  75.38300  -16.42200 1.000 35.51924  ?  787  SER   A CB  1 
ATOM   6227  O  OG  . SER   A 1 789  ? -64.89000  74.93400  -15.13300 1.000 36.78293  ?  787  SER   A OG  1 
ATOM   6228  N  N   . ALA   A 1 790  ? -64.79900  72.69400  -17.77300 1.000 47.18237  ?  788  ALA   A N   1 
ATOM   6229  C  CA  . ALA   A 1 790  ? -64.29400  71.32600  -17.83200 1.000 43.37639  ?  788  ALA   A CA  1 
ATOM   6230  C  C   . ALA   A 1 790  ? -63.78200  70.86200  -16.47400 1.000 51.91101  ?  788  ALA   A C   1 
ATOM   6231  O  O   . ALA   A 1 790  ? -64.01900  69.71700  -16.07200 1.000 48.30337  ?  788  ALA   A O   1 
ATOM   6232  C  CB  . ALA   A 1 790  ? -63.19100  71.21600  -18.88300 1.000 58.61652  ?  788  ALA   A CB  1 
ATOM   6233  N  N   . VAL   A 1 791  ? -63.08100  71.73900  -15.75100 1.000 41.63552  ?  789  VAL   A N   1 
ATOM   6234  C  CA  . VAL   A 1 791  ? -62.57600  71.36000  -14.43600 1.000 42.74191  ?  789  VAL   A CA  1 
ATOM   6235  C  C   . VAL   A 1 791  ? -63.71300  71.30800  -13.42000 1.000 46.39962  ?  789  VAL   A C   1 
ATOM   6236  O  O   . VAL   A 1 791  ? -63.68100  70.49800  -12.48500 1.000 55.80883  ?  789  VAL   A O   1 
ATOM   6237  C  CB  . VAL   A 1 791  ? -61.44800  72.31500  -13.99700 1.000 34.29033  ?  789  VAL   A CB  1 
ATOM   6238  C  CG1 . VAL   A 1 791  ? -61.98000  73.72200  -13.74500 1.000 37.16147  ?  789  VAL   A CG1 1 
ATOM   6239  C  CG2 . VAL   A 1 791  ? -60.73200  71.77000  -12.77000 1.000 22.30679  ?  789  VAL   A CG2 1 
ATOM   6240  N  N   . GLU   A 1 792  ? -64.73700  72.15000  -13.58700 1.000 49.44627  ?  790  GLU   A N   1 
ATOM   6241  C  CA  . GLU   A 1 792  ? -65.91500  72.04900  -12.73100 1.000 44.48156  ?  790  GLU   A CA  1 
ATOM   6242  C  C   . GLU   A 1 792  ? -66.65600  70.74200  -12.97700 1.000 48.97839  ?  790  GLU   A C   1 
ATOM   6243  O  O   . GLU   A 1 792  ? -67.13800  70.10700  -12.03100 1.000 48.94498  ?  790  GLU   A O   1 
ATOM   6244  C  CB  . GLU   A 1 792  ? -66.84400  73.24100  -12.95900 1.000 30.70912  ?  790  GLU   A CB  1 
ATOM   6245  C  CG  . GLU   A 1 792  ? -66.39700  74.52000  -12.27300 1.000 48.15352  ?  790  GLU   A CG  1 
ATOM   6246  C  CD  . GLU   A 1 792  ? -67.45100  75.60800  -12.32600 1.000 48.98325  ?  790  GLU   A CD  1 
ATOM   6247  O  OE1 . GLU   A 1 792  ? -68.38800  75.49500  -13.14500 1.000 48.36255  ?  790  GLU   A OE1 1 
ATOM   6248  O  OE2 . GLU   A 1 792  ? -67.34500  76.57800  -11.54600 1.000 56.96752  -1 790  GLU   A OE2 1 
ATOM   6249  N  N   . LYS   A 1 793  ? -66.75900  70.32700  -14.24200 1.000 45.54874  ?  791  LYS   A N   1 
ATOM   6250  C  CA  . LYS   A 1 793  ? -67.35600  69.03100  -14.54300 1.000 51.41006  ?  791  LYS   A CA  1 
ATOM   6251  C  C   . LYS   A 1 793  ? -66.54200  67.90200  -13.92700 1.000 51.89384  ?  791  LYS   A C   1 
ATOM   6252  O  O   . LYS   A 1 793  ? -67.10500  66.94000  -13.39100 1.000 56.87740  ?  791  LYS   A O   1 
ATOM   6253  C  CB  . LYS   A 1 793  ? -67.47600  68.84000  -16.05600 1.000 58.29680  ?  791  LYS   A CB  1 
ATOM   6254  C  CG  . LYS   A 1 793  ? -68.37500  69.84900  -16.75900 1.000 59.32062  ?  791  LYS   A CG  1 
ATOM   6255  C  CD  . LYS   A 1 793  ? -68.40100  69.60700  -18.26300 1.000 44.56879  ?  791  LYS   A CD  1 
ATOM   6256  C  CE  . LYS   A 1 793  ? -68.78800  70.86400  -19.03000 1.000 46.41548  ?  791  LYS   A CE  1 
ATOM   6257  N  NZ  . LYS   A 1 793  ? -70.17600  71.31300  -18.73400 1.000 63.15970  ?  791  LYS   A NZ  1 
ATOM   6258  N  N   . ARG   A 1 794  ? -65.21100  68.01100  -13.98000 1.000 52.02389  ?  792  ARG   A N   1 
ATOM   6259  C  CA  . ARG   A 1 794  ? -64.36300  66.94400  -13.46000 1.000 52.94311  ?  792  ARG   A CA  1 
ATOM   6260  C  C   . ARG   A 1 794  ? -64.48300  66.82900  -11.94400 1.000 52.68615  ?  792  ARG   A C   1 
ATOM   6261  O  O   . ARG   A 1 794  ? -64.57600  65.71900  -11.40900 1.000 48.28472  ?  792  ARG   A O   1 
ATOM   6262  C  CB  . ARG   A 1 794  ? -62.91000  67.18000  -13.87600 1.000 48.68895  ?  792  ARG   A CB  1 
ATOM   6263  C  CG  . ARG   A 1 794  ? -62.19100  65.91000  -14.29800 1.000 56.56668  ?  792  ARG   A CG  1 
ATOM   6264  C  CD  . ARG   A 1 794  ? -60.80400  66.18500  -14.86200 1.000 65.01882  ?  792  ARG   A CD  1 
ATOM   6265  N  NE  . ARG   A 1 794  ? -59.87700  66.68400  -13.85200 1.000 67.29809  ?  792  ARG   A NE  1 
ATOM   6266  C  CZ  . ARG   A 1 794  ? -59.32500  67.88900  -13.87200 1.000 73.97435  ?  792  ARG   A CZ  1 
ATOM   6267  N  NH1 . ARG   A 1 794  ? -59.57300  68.74700  -14.84800 1.000 72.72984  ?  792  ARG   A NH1 1 
ATOM   6268  N  NH2 . ARG   A 1 794  ? -58.49400  68.23700  -12.89300 1.000 59.32075  ?  792  ARG   A NH2 1 
ATOM   6269  N  N   . MET   A 1 795  ? -64.48700  67.96300  -11.23700 1.000 48.70403  ?  793  MET   A N   1 
ATOM   6270  C  CA  . MET   A 1 795  ? -64.70200  67.93000  -9.79300  1.000 47.93148  ?  793  MET   A CA  1 
ATOM   6271  C  C   . MET   A 1 795  ? -66.06800  67.34900  -9.45600  1.000 51.62415  ?  793  MET   A C   1 
ATOM   6272  O  O   . MET   A 1 795  ? -66.21300  66.60300  -8.48000  1.000 54.16320  ?  793  MET   A O   1 
ATOM   6273  C  CB  . MET   A 1 795  ? -64.55700  69.33400  -9.20500  1.000 39.32611  ?  793  MET   A CB  1 
ATOM   6274  C  CG  . MET   A 1 795  ? -63.14400  69.88800  -9.25500  1.000 42.06619  ?  793  MET   A CG  1 
ATOM   6275  S  SD  . MET   A 1 795  ? -62.00800  68.95400  -8.21400  1.000 59.17575  ?  793  MET   A SD  1 
ATOM   6276  C  CE  . MET   A 1 795  ? -60.76300  68.47100  -9.40700  1.000 44.68536  ?  793  MET   A CE  1 
ATOM   6277  N  N   . TYR   A 1 796  ? -67.08500  67.68500  -10.25400 1.000 49.53684  ?  794  TYR   A N   1 
ATOM   6278  C  CA  . TYR   A 1 796  ? -68.40500  67.09300  -10.06600 1.000 49.34462  ?  794  TYR   A CA  1 
ATOM   6279  C  C   . TYR   A 1 796  ? -68.35400  65.58400  -10.26200 1.000 50.45579  ?  794  TYR   A C   1 
ATOM   6280  O  O   . TYR   A 1 796  ? -68.94200  64.82800  -9.48200  1.000 50.45516  ?  794  TYR   A O   1 
ATOM   6281  C  CB  . TYR   A 1 796  ? -69.40100  67.73100  -11.03500 1.000 48.53390  ?  794  TYR   A CB  1 
ATOM   6282  C  CG  . TYR   A 1 796  ? -70.85800  67.45400  -10.72700 1.000 55.05135  ?  794  TYR   A CG  1 
ATOM   6283  C  CD1 . TYR   A 1 796  ? -71.48900  66.31400  -11.21200 1.000 53.84932  ?  794  TYR   A CD1 1 
ATOM   6284  C  CD2 . TYR   A 1 796  ? -71.60700  68.34300  -9.96700  1.000 52.51405  ?  794  TYR   A CD2 1 
ATOM   6285  C  CE1 . TYR   A 1 796  ? -72.82200  66.06300  -10.93800 1.000 52.49959  ?  794  TYR   A CE1 1 
ATOM   6286  C  CE2 . TYR   A 1 796  ? -72.93900  68.10100  -9.68900  1.000 60.01870  ?  794  TYR   A CE2 1 
ATOM   6287  C  CZ  . TYR   A 1 796  ? -73.54200  66.96000  -10.17600 1.000 65.61128  ?  794  TYR   A CZ  1 
ATOM   6288  O  OH  . TYR   A 1 796  ? -74.86900  66.71500  -9.90000  1.000 64.64922  ?  794  TYR   A OH  1 
ATOM   6289  N  N   . ILE   A 1 797  ? -67.63800  65.13000  -11.29300 1.000 49.86315  ?  795  ILE   A N   1 
ATOM   6290  C  CA  . ILE   A 1 797  ? -67.54000  63.70100  -11.57700 1.000 54.16372  ?  795  ILE   A CA  1 
ATOM   6291  C  C   . ILE   A 1 797  ? -66.84900  62.97000  -10.43200 1.000 60.44217  ?  795  ILE   A C   1 
ATOM   6292  O  O   . ILE   A 1 797  ? -67.23600  61.85400  -10.06400 1.000 67.49696  ?  795  ILE   A O   1 
ATOM   6293  C  CB  . ILE   A 1 797  ? -66.81700  63.48400  -12.92000 1.000 46.42224  ?  795  ILE   A CB  1 
ATOM   6294  C  CG1 . ILE   A 1 797  ? -67.79200  63.70800  -14.07800 1.000 47.95776  ?  795  ILE   A CG1 1 
ATOM   6295  C  CG2 . ILE   A 1 797  ? -66.19100  62.09900  -12.99200 1.000 58.26400  ?  795  ILE   A CG2 1 
ATOM   6296  C  CD1 . ILE   A 1 797  ? -67.17300  64.37500  -15.28200 1.000 56.99786  ?  795  ILE   A CD1 1 
ATOM   6297  N  N   . ILE   A 1 798  ? -65.83000  63.59400  -9.83800  1.000 49.53343  ?  796  ILE   A N   1 
ATOM   6298  C  CA  . ILE   A 1 798  ? -65.10600  62.95600  -8.74200  1.000 46.95251  ?  796  ILE   A CA  1 
ATOM   6299  C  C   . ILE   A 1 798  ? -65.99800  62.83400  -7.51200  1.000 45.45139  ?  796  ILE   A C   1 
ATOM   6300  O  O   . ILE   A 1 798  ? -66.07000  61.77400  -6.87900  1.000 46.26034  ?  796  ILE   A O   1 
ATOM   6301  C  CB  . ILE   A 1 798  ? -63.81600  63.73200  -8.42400  1.000 47.51447  ?  796  ILE   A CB  1 
ATOM   6302  C  CG1 . ILE   A 1 798  ? -62.85200  63.68100  -9.60900  1.000 49.90618  ?  796  ILE   A CG1 1 
ATOM   6303  C  CG2 . ILE   A 1 798  ? -63.15300  63.16700  -7.18100  1.000 57.67576  ?  796  ILE   A CG2 1 
ATOM   6304  C  CD1 . ILE   A 1 798  ? -61.55700  64.42600  -9.37000  1.000 45.86499  ?  796  ILE   A CD1 1 
ATOM   6305  N  N   . GLN   A 1 799  ? -66.68900  63.92000  -7.15500  1.000 48.50526  ?  797  GLN   A N   1 
ATOM   6306  C  CA  . GLN   A 1 799  ? -67.50600  63.91200  -5.94600  1.000 49.18450  ?  797  GLN   A CA  1 
ATOM   6307  C  C   . GLN   A 1 799  ? -68.65600  62.91800  -6.04800  1.000 44.19328  ?  797  GLN   A C   1 
ATOM   6308  O  O   . GLN   A 1 799  ? -69.08800  62.36500  -5.03100  1.000 56.84213  ?  797  GLN   A O   1 
ATOM   6309  C  CB  . GLN   A 1 799  ? -68.04100  65.31700  -5.66300  1.000 47.15525  ?  797  GLN   A CB  1 
ATOM   6310  C  CG  . GLN   A 1 799  ? -68.77400  65.45000  -4.33500  1.000 49.51787  ?  797  GLN   A CG  1 
ATOM   6311  C  CD  . GLN   A 1 799  ? -67.86800  65.20900  -3.14100  1.000 56.00445  ?  797  GLN   A CD  1 
ATOM   6312  O  OE1 . GLN   A 1 799  ? -66.74500  65.70900  -3.08800  1.000 63.55381  ?  797  GLN   A OE1 1 
ATOM   6313  N  NE2 . GLN   A 1 799  ? -68.35400  64.43500  -2.17800  1.000 58.61072  ?  797  GLN   A NE2 1 
ATOM   6314  N  N   . GLN   A 1 800  ? -69.15600  62.66700  -7.25900  1.000 48.09864  ?  798  GLN   A N   1 
ATOM   6315  C  CA  . GLN   A 1 800  ? -70.29000  61.76500  -7.41400  1.000 49.83241  ?  798  GLN   A CA  1 
ATOM   6316  C  C   . GLN   A 1 800  ? -69.90500  60.29800  -7.28200  1.000 47.87923  ?  798  GLN   A C   1 
ATOM   6317  O  O   . GLN   A 1 800  ? -70.78900  59.46400  -7.05800  1.000 70.92650  ?  798  GLN   A O   1 
ATOM   6318  C  CB  . GLN   A 1 800  ? -70.97700  61.99400  -8.76100  1.000 40.46262  ?  798  GLN   A CB  1 
ATOM   6319  C  CG  . GLN   A 1 800  ? -71.56700  63.38500  -8.92800  1.000 41.80059  ?  798  GLN   A CG  1 
ATOM   6320  C  CD  . GLN   A 1 800  ? -72.46400  63.79100  -7.77700  1.000 41.89003  ?  798  GLN   A CD  1 
ATOM   6321  O  OE1 . GLN   A 1 800  ? -73.32500  63.02500  -7.34400  1.000 52.91529  ?  798  GLN   A OE1 1 
ATOM   6322  N  NE2 . GLN   A 1 800  ? -72.26500  65.00300  -7.27200  1.000 36.00823  ?  798  GLN   A NE2 1 
ATOM   6323  N  N   . GLN   A 1 801  ? -68.62100  59.95700  -7.42200  1.000 42.09462  ?  799  GLN   A N   1 
ATOM   6324  C  CA  . GLN   A 1 801  ? -68.19100  58.58900  -7.14800  1.000 57.80741  ?  799  GLN   A CA  1 
ATOM   6325  C  C   . GLN   A 1 801  ? -68.54000  58.19600  -5.71700  1.000 78.19524  ?  799  GLN   A C   1 
ATOM   6326  O  O   . GLN   A 1 801  ? -69.28500  57.23700  -5.48400  1.000 88.74261  ?  799  GLN   A O   1 
ATOM   6327  C  CB  . GLN   A 1 801  ? -66.69000  58.44200  -7.39600  1.000 59.25020  ?  799  GLN   A CB  1 
ATOM   6328  C  CG  . GLN   A 1 801  ? -66.17700  57.03000  -7.16400  1.000 76.49014  ?  799  GLN   A CG  1 
ATOM   6329  C  CD  . GLN   A 1 801  ? -64.75600  56.99600  -6.63600  1.000 90.83212  ?  799  GLN   A CD  1 
ATOM   6330  O  OE1 . GLN   A 1 801  ? -64.17700  55.92500  -6.45700  1.000 86.29649  ?  799  GLN   A OE1 1 
ATOM   6331  N  NE2 . GLN   A 1 801  ? -64.18500  58.17000  -6.38600  1.000 98.49555  ?  799  GLN   A NE2 1 
ATOM   6332  N  N   . ASP   A 1 802  ? -68.01000  58.93500  -4.74400  1.000 59.69483  ?  800  ASP   A N   1 
ATOM   6333  C  CA  . ASP   A 1 802  ? -68.38300  58.80200  -3.33700  1.000 56.75880  ?  800  ASP   A CA  1 
ATOM   6334  C  C   . ASP   A 1 802  ? -68.96700  60.14100  -2.89700  1.000 53.32057  ?  800  ASP   A C   1 
ATOM   6335  O  O   . ASP   A 1 802  ? -68.22500  61.09800  -2.64800  1.000 55.65860  ?  800  ASP   A O   1 
ATOM   6336  C  CB  . ASP   A 1 802  ? -67.18600  58.41000  -2.47600  1.000 60.29571  ?  800  ASP   A CB  1 
ATOM   6337  C  CG  . ASP   A 1 802  ? -67.57000  58.19200  -1.02500  1.000 66.00471  ?  800  ASP   A CG  1 
ATOM   6338  O  OD1 . ASP   A 1 802  ? -68.74000  57.84000  -0.77500  1.000 74.71070  ?  800  ASP   A OD1 1 
ATOM   6339  O  OD2 . ASP   A 1 802  ? -66.70700  58.38300  -0.13700  1.000 72.16567  -1 800  ASP   A OD2 1 
ATOM   6340  N  N   . VAL   A 1 803  ? -70.29800  60.20200  -2.78500  1.000 49.97762  ?  801  VAL   A N   1 
ATOM   6341  C  CA  . VAL   A 1 803  ? -71.00300  61.45200  -2.52600  1.000 51.32977  ?  801  VAL   A CA  1 
ATOM   6342  C  C   . VAL   A 1 803  ? -70.85600  61.80900  -1.05600  1.000 53.09311  ?  801  VAL   A C   1 
ATOM   6343  O  O   . VAL   A 1 803  ? -71.43000  62.79500  -0.57300  1.000 58.21667  ?  801  VAL   A O   1 
ATOM   6344  C  CB  . VAL   A 1 803  ? -72.48800  61.36200  -2.92500  1.000 39.98205  ?  801  VAL   A CB  1 
ATOM   6345  C  CG1 . VAL   A 1 803  ? -72.80900  62.37200  -4.02800  1.000 36.90911  ?  801  VAL   A CG1 1 
ATOM   6346  C  CG2 . VAL   A 1 803  ? -72.84500  59.94700  -3.37300  1.000 38.68987  ?  801  VAL   A CG2 1 
ATOM   6347  N  N   . GLU   A 1 804  ? -70.07500  61.01200  -0.32900  1.000 52.21770  ?  802  GLU   A N   1 
ATOM   6348  C  CA  . GLU   A 1 804  ? -69.79900  61.26000  1.08000   1.000 52.30798  ?  802  GLU   A CA  1 
ATOM   6349  C  C   . GLU   A 1 804  ? -68.30600  61.44900  1.32900   1.000 55.09616  ?  802  GLU   A C   1 
ATOM   6350  O  O   . GLU   A 1 804  ? -67.81800  61.19100  2.42900   1.000 66.90325  ?  802  GLU   A O   1 
ATOM   6351  C  CB  . GLU   A 1 804  ? -70.35700  60.12900  1.94300   1.000 48.23517  ?  802  GLU   A CB  1 
ATOM   6352  C  CG  . GLU   A 1 804  ? -71.87800  60.12000  2.05100   1.000 59.79075  ?  802  GLU   A CG  1 
ATOM   6353  C  CD  . GLU   A 1 804  ? -72.41600  61.24000  2.92800   1.000 71.47632  ?  802  GLU   A CD  1 
ATOM   6354  O  OE1 . GLU   A 1 804  ? -72.09500  61.26600  4.13600   1.000 79.82603  ?  802  GLU   A OE1 1 
ATOM   6355  O  OE2 . GLU   A 1 804  ? -73.16100  62.09700  2.40800   1.000 65.71245  -1 802  GLU   A OE2 1 
ATOM   6356  N  N   . SER   A 1 805  ? -67.56900  61.90700  0.31900   1.000 48.00057  ?  803  SER   A N   1 
ATOM   6357  C  CA  . SER   A 1 805  ? -66.12100  62.04100  0.40500   1.000 40.31576  ?  803  SER   A CA  1 
ATOM   6358  C  C   . SER   A 1 805  ? -65.73400  63.45800  0.80700   1.000 47.93397  ?  803  SER   A C   1 
ATOM   6359  O  O   . SER   A 1 805  ? -66.36600  64.43200  0.38800   1.000 50.29383  ?  803  SER   A O   1 
ATOM   6360  C  CB  . SER   A 1 805  ? -65.46000  61.68400  -0.92800  1.000 36.37332  ?  803  SER   A CB  1 
ATOM   6361  O  OG  . SER   A 1 805  ? -64.05000  61.82500  -0.85900  1.000 30.80062  ?  803  SER   A OG  1 
ATOM   6362  N  N   . ILE   A 1 806  ? -64.68900  63.56300  1.62600   1.000 46.57501  ?  804  ILE   A N   1 
ATOM   6363  C  CA  . ILE   A 1 806  ? -64.10900  64.84200  2.01000   1.000 40.40910  ?  804  ILE   A CA  1 
ATOM   6364  C  C   . ILE   A 1 806  ? -62.73100  65.03400  1.39500   1.000 37.83103  ?  804  ILE   A C   1 
ATOM   6365  O  O   . ILE   A 1 806  ? -61.98600  65.92600  1.81400   1.000 52.65074  ?  804  ILE   A O   1 
ATOM   6366  C  CB  . ILE   A 1 806  ? -64.05200  65.00000  3.54100   1.000 43.97948  ?  804  ILE   A CB  1 
ATOM   6367  C  CG1 . ILE   A 1 806  ? -63.03200  64.03300  4.16400   1.000 31.02142  ?  804  ILE   A CG1 1 
ATOM   6368  C  CG2 . ILE   A 1 806  ? -65.43700  64.81100  4.14400   1.000 37.25614  ?  804  ILE   A CG2 1 
ATOM   6369  C  CD1 . ILE   A 1 806  ? -63.56500  62.63800  4.46100   1.000 48.49008  ?  804  ILE   A CD1 1 
ATOM   6370  N  N   . ALA   A 1 807  ? -62.37800  64.22000  0.39600   1.000 29.94933  ?  805  ALA   A N   1 
ATOM   6371  C  CA  . ALA   A 1 807  ? -61.03200  64.25900  -0.16500  1.000 30.65127  ?  805  ALA   A CA  1 
ATOM   6372  C  C   . ALA   A 1 807  ? -60.73200  65.60700  -0.81000  1.000 35.65177  ?  805  ALA   A C   1 
ATOM   6373  O  O   . ALA   A 1 807  ? -59.63500  66.15200  -0.64300  1.000 54.09161  ?  805  ALA   A O   1 
ATOM   6374  C  CB  . ALA   A 1 807  ? -60.85600  63.12900  -1.17800  1.000 42.06534  ?  805  ALA   A CB  1 
ATOM   6375  N  N   . TYR   A 1 808  ? -61.69200  66.16000  -1.55100  1.000 40.58674  ?  806  TYR   A N   1 
ATOM   6376  C  CA  . TYR   A 1 808  ? -61.52700  67.45800  -2.19200  1.000 48.38731  ?  806  TYR   A CA  1 
ATOM   6377  C  C   . TYR   A 1 808  ? -62.20100  68.57900  -1.40700  1.000 47.80552  ?  806  TYR   A C   1 
ATOM   6378  O  O   . TYR   A 1 808  ? -62.62200  69.58500  -1.99000  1.000 38.51529  ?  806  TYR   A O   1 
ATOM   6379  C  CB  . TYR   A 1 808  ? -62.04000  67.40500  -3.63100  1.000 41.93849  ?  806  TYR   A CB  1 
ATOM   6380  C  CG  . TYR   A 1 808  ? -61.12800  66.61200  -4.54200  1.000 44.44378  ?  806  TYR   A CG  1 
ATOM   6381  C  CD1 . TYR   A 1 808  ? -61.26900  65.23600  -4.67400  1.000 49.30389  ?  806  TYR   A CD1 1 
ATOM   6382  C  CD2 . TYR   A 1 808  ? -60.10900  67.23600  -5.25200  1.000 45.65213  ?  806  TYR   A CD2 1 
ATOM   6383  C  CE1 . TYR   A 1 808  ? -60.42800  64.50500  -5.49500  1.000 56.08368  ?  806  TYR   A CE1 1 
ATOM   6384  C  CE2 . TYR   A 1 808  ? -59.26300  66.51400  -6.07800  1.000 56.25184  ?  806  TYR   A CE2 1 
ATOM   6385  C  CZ  . TYR   A 1 808  ? -59.42900  65.14800  -6.19600  1.000 63.64206  ?  806  TYR   A CZ  1 
ATOM   6386  O  OH  . TYR   A 1 808  ? -58.59300  64.42200  -7.01500  1.000 66.94328  ?  806  TYR   A OH  1 
ATOM   6387  N  N   . ASN   A 1 809  ? -62.31100  68.41700  -0.09000  1.000 42.53333  ?  807  ASN   A N   1 
ATOM   6388  C  CA  . ASN   A 1 809  ? -62.73400  69.49400  0.79200   1.000 49.15483  ?  807  ASN   A CA  1 
ATOM   6389  C  C   . ASN   A 1 809  ? -61.52000  70.30500  1.21900   1.000 38.81479  ?  807  ASN   A C   1 
ATOM   6390  O  O   . ASN   A 1 809  ? -60.47500  69.74700  1.56500   1.000 49.28792  ?  807  ASN   A O   1 
ATOM   6391  C  CB  . ASN   A 1 809  ? -63.45700  68.94600  2.02400   1.000 40.67439  ?  807  ASN   A CB  1 
ATOM   6392  C  CG  . ASN   A 1 809  ? -64.88200  68.52900  1.72700   1.000 45.44195  ?  807  ASN   A CG  1 
ATOM   6393  O  OD1 . ASN   A 1 809  ? -65.19200  68.06600  0.62900   1.000 66.72831  ?  807  ASN   A OD1 1 
ATOM   6394  N  ND2 . ASN   A 1 809  ? -65.76100  68.69900  2.70800   1.000 37.15760  ?  807  ASN   A ND2 1 
ATOM   6395  N  N   . VAL   A 1 810  ? -61.66500  71.62500  1.19200   1.000 41.97982  ?  808  VAL   A N   1 
ATOM   6396  C  CA  . VAL   A 1 810  ? -60.57300  72.55100  1.46600   1.000 36.97253  ?  808  VAL   A CA  1 
ATOM   6397  C  C   . VAL   A 1 810  ? -60.81300  73.15300  2.84400   1.000 52.09827  ?  808  VAL   A C   1 
ATOM   6398  O  O   . VAL   A 1 810  ? -61.76300  73.92100  3.03800   1.000 55.38778  ?  808  VAL   A O   1 
ATOM   6399  C  CB  . VAL   A 1 810  ? -60.47600  73.64200  0.39200   1.000 34.43404  ?  808  VAL   A CB  1 
ATOM   6400  C  CG1 . VAL   A 1 810  ? -59.18500  74.41300  0.54100   1.000 43.95620  ?  808  VAL   A CG1 1 
ATOM   6401  C  CG2 . VAL   A 1 810  ? -60.58600  73.02900  -0.99500  1.000 41.85768  ?  808  VAL   A CG2 1 
ATOM   6402  N  N   . VAL   A 1 811  ? -59.95100  72.81400  3.80100   1.000 48.85234  ?  809  VAL   A N   1 
ATOM   6403  C  CA  . VAL   A 1 811  ? -60.07700  73.26800  5.18200   1.000 38.83543  ?  809  VAL   A CA  1 
ATOM   6404  C  C   . VAL   A 1 811  ? -58.89600  74.17100  5.50900   1.000 39.20342  ?  809  VAL   A C   1 
ATOM   6405  O  O   . VAL   A 1 811  ? -57.73900  73.80400  5.26800   1.000 43.17462  ?  809  VAL   A O   1 
ATOM   6406  C  CB  . VAL   A 1 811  ? -60.14500  72.08500  6.16300   1.000 42.56008  ?  809  VAL   A CB  1 
ATOM   6407  C  CG1 . VAL   A 1 811  ? -60.65200  72.55200  7.52100   1.000 39.67444  ?  809  VAL   A CG1 1 
ATOM   6408  C  CG2 . VAL   A 1 811  ? -61.02000  70.97400  5.60600   1.000 46.35289  ?  809  VAL   A CG2 1 
ATOM   6409  N  N   . TYR   A 1 812  ? -59.18800  75.34600  6.06300   1.000 40.57910  ?  810  TYR   A N   1 
ATOM   6410  C  CA  . TYR   A 1 812  ? -58.16900  76.28200  6.51700   1.000 33.77902  ?  810  TYR   A CA  1 
ATOM   6411  C  C   . TYR   A 1 812  ? -58.57000  76.83000  7.87700   1.000 41.66131  ?  810  TYR   A C   1 
ATOM   6412  O  O   . TYR   A 1 812  ? -59.75800  77.03500  8.14400   1.000 46.19452  ?  810  TYR   A O   1 
ATOM   6413  C  CB  . TYR   A 1 812  ? -57.97600  77.44000  5.52800   1.000 30.60172  ?  810  TYR   A CB  1 
ATOM   6414  C  CG  . TYR   A 1 812  ? -57.09500  77.12000  4.34000   1.000 47.94423  ?  810  TYR   A CG  1 
ATOM   6415  C  CD1 . TYR   A 1 812  ? -55.71600  77.27400  4.41300   1.000 52.48335  ?  810  TYR   A CD1 1 
ATOM   6416  C  CD2 . TYR   A 1 812  ? -57.64000  76.67700  3.14300   1.000 34.15037  ?  810  TYR   A CD2 1 
ATOM   6417  C  CE1 . TYR   A 1 812  ? -54.90500  76.98900  3.32800   1.000 37.84266  ?  810  TYR   A CE1 1 
ATOM   6418  C  CE2 . TYR   A 1 812  ? -56.83600  76.39100  2.05500   1.000 47.02421  ?  810  TYR   A CE2 1 
ATOM   6419  C  CZ  . TYR   A 1 812  ? -55.47100  76.54700  2.15300   1.000 34.23926  ?  810  TYR   A CZ  1 
ATOM   6420  O  OH  . TYR   A 1 812  ? -54.67100  76.26000  1.06900   1.000 57.88300  ?  810  TYR   A OH  1 
ATOM   6421  N  N   . THR   A 1 813  ? -57.57800  77.06400  8.73500   1.000 42.91042  ?  811  THR   A N   1 
ATOM   6422  C  CA  . THR   A 1 813  ? -57.80600  77.63300  10.05600  1.000 30.03358  ?  811  THR   A CA  1 
ATOM   6423  C  C   . THR   A 1 813  ? -56.91100  78.84700  10.25100  1.000 39.95834  ?  811  THR   A C   1 
ATOM   6424  O  O   . THR   A 1 813  ? -55.76200  78.86200  9.80100   1.000 45.52464  ?  811  THR   A O   1 
ATOM   6425  C  CB  . THR   A 1 813  ? -57.53200  76.61800  11.17500  1.000 33.93566  ?  811  THR   A CB  1 
ATOM   6426  O  OG1 . THR   A 1 813  ? -56.13200  76.31500  11.21800  1.000 55.28292  ?  811  THR   A OG1 1 
ATOM   6427  C  CG2 . THR   A 1 813  ? -58.32000  75.33900  10.94600  1.000 36.74140  ?  811  THR   A CG2 1 
ATOM   6428  N  N   . ILE   A 1 814  ? -57.45000  79.86600  10.91800  1.000 49.71384  ?  812  ILE   A N   1 
ATOM   6429  C  CA  . ILE   A 1 814  ? -56.70400  81.06300  11.28500  1.000 41.30324  ?  812  ILE   A CA  1 
ATOM   6430  C  C   . ILE   A 1 814  ? -56.94300  81.32800  12.76400  1.000 44.34708  ?  812  ILE   A C   1 
ATOM   6431  O  O   . ILE   A 1 814  ? -58.09500  81.39000  13.20700  1.000 44.29275  ?  812  ILE   A O   1 
ATOM   6432  C  CB  . ILE   A 1 814  ? -57.12000  82.29100  10.45300  1.000 37.81158  ?  812  ILE   A CB  1 
ATOM   6433  C  CG1 . ILE   A 1 814  ? -57.52900  81.88200  9.03700   1.000 47.46130  ?  812  ILE   A CG1 1 
ATOM   6434  C  CG2 . ILE   A 1 814  ? -55.98500  83.30100  10.39900  1.000 48.51926  ?  812  ILE   A CG2 1 
ATOM   6435  C  CD1 . ILE   A 1 814  ? -58.24400  82.97700  8.27700   1.000 58.76776  ?  812  ILE   A CD1 1 
ATOM   6436  N  N   . ASN   A 1 815  ? -55.86200  81.48500  13.52200  1.000 54.72729  ?  813  ASN   A N   1 
ATOM   6437  C  CA  . ASN   A 1 815  ? -55.95200  81.77800  14.94800  1.000 46.69325  ?  813  ASN   A CA  1 
ATOM   6438  C  C   . ASN   A 1 815  ? -55.94700  83.29100  15.15000  1.000 47.34334  ?  813  ASN   A C   1 
ATOM   6439  O  O   . ASN   A 1 815  ? -54.95700  83.96000  14.83900  1.000 60.02506  ?  813  ASN   A O   1 
ATOM   6440  C  CB  . ASN   A 1 815  ? -54.79700  81.12700  15.71000  1.000 29.17661  ?  813  ASN   A CB  1 
ATOM   6441  C  CG  . ASN   A 1 815  ? -54.78200  79.61300  15.57400  1.000 46.89194  ?  813  ASN   A CG  1 
ATOM   6442  O  OD1 . ASN   A 1 815  ? -55.82900  78.97700  15.44600  1.000 58.85091  ?  813  ASN   A OD1 1 
ATOM   6443  N  ND2 . ASN   A 1 815  ? -53.59000  79.02900  15.60500  1.000 34.08774  ?  813  ASN   A ND2 1 
ATOM   6444  N  N   . PHE   A 1 816  ? -57.06400  83.82900  15.66700  1.000 50.59547  ?  814  PHE   A N   1 
ATOM   6445  C  CA  . PHE   A 1 816  ? -57.21200  85.24300  15.93900  1.000 50.26608  ?  814  PHE   A CA  1 
ATOM   6446  C  C   . PHE   A 1 816  ? -57.02800  85.52900  17.42600  1.000 63.91070  ?  814  PHE   A C   1 
ATOM   6447  O  O   . PHE   A 1 816  ? -57.24500  84.65400  18.26500  1.000 58.50650  ?  814  PHE   A O   1 
ATOM   6448  C  CB  . PHE   A 1 816  ? -58.59500  85.74800  15.51000  1.000 48.08674  ?  814  PHE   A CB  1 
ATOM   6449  C  CG  . PHE   A 1 816  ? -58.76000  85.89100  14.02700  1.000 43.83796  ?  814  PHE   A CG  1 
ATOM   6450  C  CD1 . PHE   A 1 816  ? -58.14000  86.92400  13.34500  1.000 49.98621  ?  814  PHE   A CD1 1 
ATOM   6451  C  CD2 . PHE   A 1 816  ? -59.55500  85.00700  13.32000  1.000 45.75693  ?  814  PHE   A CD2 1 
ATOM   6452  C  CE1 . PHE   A 1 816  ? -58.29800  87.06200  11.98100  1.000 59.97787  ?  814  PHE   A CE1 1 
ATOM   6453  C  CE2 . PHE   A 1 816  ? -59.71800  85.14200  11.95700  1.000 53.77297  ?  814  PHE   A CE2 1 
ATOM   6454  C  CZ  . PHE   A 1 816  ? -59.08900  86.16900  11.28600  1.000 65.38061  ?  814  PHE   A CZ  1 
ATOM   6455  N  N   . PRO   A 1 817  ? -56.62700  86.75000  17.78200  1.000 69.82915  ?  815  PRO   A N   1 
ATOM   6456  C  CA  . PRO   A 1 817  ? -56.68400  87.15200  19.18800  1.000 49.56762  ?  815  PRO   A CA  1 
ATOM   6457  C  C   . PRO   A 1 817  ? -58.13100  87.28200  19.63700  1.000 64.10441  ?  815  PRO   A C   1 
ATOM   6458  O  O   . PRO   A 1 817  ? -59.04800  87.49300  18.83800  1.000 61.99891  ?  815  PRO   A O   1 
ATOM   6459  C  CB  . PRO   A 1 817  ? -55.96800  88.50400  19.19300  1.000 38.13063  ?  815  PRO   A CB  1 
ATOM   6460  C  CG  . PRO   A 1 817  ? -56.16200  89.03200  17.80900  1.000 61.28947  ?  815  PRO   A CG  1 
ATOM   6461  C  CD  . PRO   A 1 817  ? -56.10000  87.82700  16.92000  1.000 73.75182  ?  815  PRO   A CD  1 
ATOM   6462  N  N   . LEU   A 1 818  ? -58.33500  87.16500  20.95300  1.000 64.83737  ?  816  LEU   A N   1 
ATOM   6463  C  CA  . LEU   A 1 818  ? -59.69100  87.24400  21.48000  1.000 58.83663  ?  816  LEU   A CA  1 
ATOM   6464  C  C   . LEU   A 1 818  ? -60.29700  88.63600  21.36700  1.000 57.38058  ?  816  LEU   A C   1 
ATOM   6465  O  O   . LEU   A 1 818  ? -61.48700  88.80000  21.66600  1.000 59.17377  ?  816  LEU   A O   1 
ATOM   6466  C  CB  . LEU   A 1 818  ? -59.74500  86.80800  22.94600  1.000 48.53192  ?  816  LEU   A CB  1 
ATOM   6467  C  CG  . LEU   A 1 818  ? -59.52700  85.32200  23.20100  1.000 54.27328  ?  816  LEU   A CG  1 
ATOM   6468  C  CD1 . LEU   A 1 818  ? -58.10700  85.16100  23.66100  1.000 66.43553  ?  816  LEU   A CD1 1 
ATOM   6469  C  CD2 . LEU   A 1 818  ? -60.49100  84.78400  24.24300  1.000 59.20186  ?  816  LEU   A CD2 1 
ATOM   6470  N  N   . THR   A 1 819  ? -59.51700  89.63500  20.95600  1.000 64.64222  ?  817  THR   A N   1 
ATOM   6471  C  CA  . THR   A 1 819  ? -60.05300  90.97600  20.77600  1.000 43.86611  ?  817  THR   A CA  1 
ATOM   6472  C  C   . THR   A 1 819  ? -60.94600  91.07600  19.54700  1.000 60.84395  ?  817  THR   A C   1 
ATOM   6473  O  O   . THR   A 1 819  ? -61.76600  91.99600  19.46500  1.000 86.82913  ?  817  THR   A O   1 
ATOM   6474  C  CB  . THR   A 1 819  ? -58.91300  91.99000  20.66600  1.000 63.53211  ?  817  THR   A CB  1 
ATOM   6475  O  OG1 . THR   A 1 819  ? -58.49100  92.08900  19.30100  1.000 83.91569  ?  817  THR   A OG1 1 
ATOM   6476  C  CG2 . THR   A 1 819  ? -57.73100  91.55200  21.51600  1.000 47.79512  ?  817  THR   A CG2 1 
ATOM   6477  N  N   . VAL   A 1 820  ? -60.80700  90.15300  18.59500  1.000 50.16715  ?  818  VAL   A N   1 
ATOM   6478  C  CA  . VAL   A 1 820  ? -61.58300  90.21700  17.36300  1.000 52.88081  ?  818  VAL   A CA  1 
ATOM   6479  C  C   . VAL   A 1 820  ? -63.02500  89.82200  17.64500  1.000 47.99850  ?  818  VAL   A C   1 
ATOM   6480  O  O   . VAL   A 1 820  ? -63.29400  88.79600  18.28300  1.000 58.53561  ?  818  VAL   A O   1 
ATOM   6481  C  CB  . VAL   A 1 820  ? -60.95600  89.31900  16.28700  1.000 53.68697  ?  818  VAL   A CB  1 
ATOM   6482  C  CG1 . VAL   A 1 820  ? -61.93700  89.08100  15.14800  1.000 54.46270  ?  818  VAL   A CG1 1 
ATOM   6483  C  CG2 . VAL   A 1 820  ? -59.67400  89.94700  15.76400  1.000 56.47009  ?  818  VAL   A CG2 1 
ATOM   6484  N  N   . ASP   A 1 821  ? -63.96300  90.64200  17.17500  1.000 49.35758  ?  819  ASP   A N   1 
ATOM   6485  C  CA  . ASP   A 1 821  ? -65.37800  90.32300  17.30700  1.000 65.77435  ?  819  ASP   A CA  1 
ATOM   6486  C  C   . ASP   A 1 821  ? -65.71300  89.12300  16.42900  1.000 56.85827  ?  819  ASP   A C   1 
ATOM   6487  O  O   . ASP   A 1 821  ? -65.52500  89.16600  15.20800  1.000 63.87350  ?  819  ASP   A O   1 
ATOM   6488  C  CB  . ASP   A 1 821  ? -66.22900  91.53100  16.92400  1.000 68.92026  ?  819  ASP   A CB  1 
ATOM   6489  C  CG  . ASP   A 1 821  ? -67.65200  91.43800  17.44800  1.000 76.21094  ?  819  ASP   A CG  1 
ATOM   6490  O  OD1 . ASP   A 1 821  ? -68.22600  90.32800  17.44700  1.000 76.70913  ?  819  ASP   A OD1 1 
ATOM   6491  O  OD2 . ASP   A 1 821  ? -68.19700  92.48200  17.86700  1.000 74.07851  -1 819  ASP   A OD2 1 
ATOM   6492  N  N   . THR   A 1 822  ? -66.20700  88.05200  17.05500  1.000 54.38901  ?  820  THR   A N   1 
ATOM   6493  C  CA  . THR   A 1 822  ? -66.56800  86.84800  16.31300  1.000 53.73374  ?  820  THR   A CA  1 
ATOM   6494  C  C   . THR   A 1 822  ? -67.65900  87.12400  15.28200  1.000 55.27734  ?  820  THR   A C   1 
ATOM   6495  O  O   . THR   A 1 822  ? -67.70800  86.46100  14.23900  1.000 68.67254  ?  820  THR   A O   1 
ATOM   6496  C  CB  . THR   A 1 822  ? -67.00700  85.74800  17.28900  1.000 65.37461  ?  820  THR   A CB  1 
ATOM   6497  O  OG1 . THR   A 1 822  ? -65.94000  85.45700  18.20300  1.000 62.84835  ?  820  THR   A OG1 1 
ATOM   6498  C  CG2 . THR   A 1 822  ? -67.37300  84.47700  16.54500  1.000 50.71708  ?  820  THR   A CG2 1 
ATOM   6499  N  N   . GLU   A 1 823  ? -68.52000  88.11500  15.53400  1.000 60.10546  ?  821  GLU   A N   1 
ATOM   6500  C  CA  . GLU   A 1 823  ? -69.59400  88.42300  14.59300  1.000 67.64832  ?  821  GLU   A CA  1 
ATOM   6501  C  C   . GLU   A 1 823  ? -69.09400  89.23400  13.40100  1.000 65.64583  ?  821  GLU   A C   1 
ATOM   6502  O  O   . GLU   A 1 823  ? -69.56700  89.03500  12.27600  1.000 72.18346  ?  821  GLU   A O   1 
ATOM   6503  C  CB  . GLU   A 1 823  ? -70.72500  89.15800  15.31200  1.000 53.70251  ?  821  GLU   A CB  1 
ATOM   6504  C  CG  . GLU   A 1 823  ? -71.25300  88.39200  16.51300  1.000 75.71557  ?  821  GLU   A CG  1 
ATOM   6505  C  CD  . GLU   A 1 823  ? -71.56000  86.94300  16.18300  1.000 65.88467  ?  821  GLU   A CD  1 
ATOM   6506  O  OE1 . GLU   A 1 823  ? -72.29300  86.70100  15.20200  1.000 60.60819  ?  821  GLU   A OE1 1 
ATOM   6507  O  OE2 . GLU   A 1 823  ? -71.06000  86.04500  16.89400  1.000 59.35506  -1 821  GLU   A OE2 1 
ATOM   6508  N  N   . GLN   A 1 824  ? -68.14200  90.14900  13.61800  1.000 58.57323  ?  822  GLN   A N   1 
ATOM   6509  C  CA  . GLN   A 1 824  ? -67.53200  90.85400  12.49300  1.000 63.18116  ?  822  GLN   A CA  1 
ATOM   6510  C  C   . GLN   A 1 824  ? -66.94400  89.88200  11.47900  1.000 62.73430  ?  822  GLN   A C   1 
ATOM   6511  O  O   . GLN   A 1 824  ? -66.90600  90.18200  10.28100  1.000 62.81207  ?  822  GLN   A O   1 
ATOM   6512  C  CB  . GLN   A 1 824  ? -66.45100  91.81600  12.98600  1.000 60.56212  ?  822  GLN   A CB  1 
ATOM   6513  C  CG  . GLN   A 1 824  ? -66.92900  93.24500  13.17700  1.000 77.10781  ?  822  GLN   A CG  1 
ATOM   6514  C  CD  . GLN   A 1 824  ? -65.89500  94.26300  12.73800  1.000 97.71557  ?  822  GLN   A CD  1 
ATOM   6515  O  OE1 . GLN   A 1 824  ? -64.69300  94.05700  12.90700  1.000 92.47205  ?  822  GLN   A OE1 1 
ATOM   6516  N  NE2 . GLN   A 1 824  ? -66.35800  95.36400  12.15800  1.000 97.23868  ?  822  GLN   A NE2 1 
ATOM   6517  N  N   . ILE   A 1 825  ? -66.48700  88.71700  11.93800  1.000 52.96479  ?  823  ILE   A N   1 
ATOM   6518  C  CA  . ILE   A 1 825  ? -66.01600  87.68800  11.01700  1.000 55.45216  ?  823  ILE   A CA  1 
ATOM   6519  C  C   . ILE   A 1 825  ? -67.18600  87.10500  10.23600  1.000 63.71314  ?  823  ILE   A C   1 
ATOM   6520  O  O   . ILE   A 1 825  ? -67.15500  87.03900  9.00100   1.000 69.84031  ?  823  ILE   A O   1 
ATOM   6521  C  CB  . ILE   A 1 825  ? -65.25100  86.59600  11.78200  1.000 50.33690  ?  823  ILE   A CB  1 
ATOM   6522  C  CG1 . ILE   A 1 825  ? -64.15800  87.22200  12.64600  1.000 46.24367  ?  823  ILE   A CG1 1 
ATOM   6523  C  CG2 . ILE   A 1 825  ? -64.65500  85.59400  10.81000  1.000 39.10003  ?  823  ILE   A CG2 1 
ATOM   6524  C  CD1 . ILE   A 1 825  ? -63.37000  86.21400  13.44400  1.000 45.68140  ?  823  ILE   A CD1 1 
ATOM   6525  N  N   . ARG   A 1 826  ? -68.22900  86.66400  10.94600  1.000 45.81003  ?  824  ARG   A N   1 
ATOM   6526  C  CA  . ARG   A 1 826  ? -69.42600  86.15300  10.28600  1.000 47.12949  ?  824  ARG   A CA  1 
ATOM   6527  C  C   . ARG   A 1 826  ? -69.99200  87.17600  9.31200   1.000 60.56022  ?  824  ARG   A C   1 
ATOM   6528  O  O   . ARG   A 1 826  ? -70.32500  86.84800  8.16800   1.000 69.32815  ?  824  ARG   A O   1 
ATOM   6529  C  CB  . ARG   A 1 826  ? -70.48300  85.77600  11.32600  1.000 53.67356  ?  824  ARG   A CB  1 
ATOM   6530  C  CG  . ARG   A 1 826  ? -71.90300  85.78500  10.76600  1.000 68.61458  ?  824  ARG   A CG  1 
ATOM   6531  C  CD  . ARG   A 1 826  ? -72.96500  85.60700  11.84400  1.000 68.62784  ?  824  ARG   A CD  1 
ATOM   6532  N  NE  . ARG   A 1 826  ? -72.95500  86.68200  12.83000  1.000 86.02328  ?  824  ARG   A NE  1 
ATOM   6533  C  CZ  . ARG   A 1 826  ? -73.67200  87.79500  12.74200  1.000 79.06062  ?  824  ARG   A CZ  1 
ATOM   6534  N  NH1 . ARG   A 1 826  ? -74.46900  88.02600  11.71200  1.000 74.84556  ?  824  ARG   A NH1 1 
ATOM   6535  N  NH2 . ARG   A 1 826  ? -73.58600  88.70000  13.71300  1.000 68.79359  ?  824  ARG   A NH2 1 
ATOM   6536  N  N   . VAL   A 1 827  ? -70.10600  88.43100  9.75600   1.000 58.06438  ?  825  VAL   A N   1 
ATOM   6537  C  CA  . VAL   A 1 827  ? -70.62000  89.49200  8.89400   1.000 70.06018  ?  825  VAL   A CA  1 
ATOM   6538  C  C   . VAL   A 1 827  ? -69.80500  89.57100  7.61000   1.000 62.95639  ?  825  VAL   A C   1 
ATOM   6539  O  O   . VAL   A 1 827  ? -70.35100  89.50200  6.50200   1.000 60.67635  ?  825  VAL   A O   1 
ATOM   6540  C  CB  . VAL   A 1 827  ? -70.62800  90.83400  9.64900   1.000 55.81549  ?  825  VAL   A CB  1 
ATOM   6541  C  CG1 . VAL   A 1 827  ? -70.84900  91.98800  8.68700   1.000 63.30127  ?  825  VAL   A CG1 1 
ATOM   6542  C  CG2 . VAL   A 1 827  ? -71.70500  90.82400  10.71900  1.000 57.37150  ?  825  VAL   A CG2 1 
ATOM   6543  N  N   . ALA   A 1 828  ? -68.47900  89.68500  7.74200   1.000 47.45376  ?  826  ALA   A N   1 
ATOM   6544  C  CA  . ALA   A 1 828  ? -67.62200  89.81000  6.56600   1.000 53.20330  ?  826  ALA   A CA  1 
ATOM   6545  C  C   . ALA   A 1 828  ? -67.69900  88.57200  5.67900   1.000 55.32753  ?  826  ALA   A C   1 
ATOM   6546  O  O   . ALA   A 1 828  ? -67.74100  88.68500  4.44800   1.000 59.32256  ?  826  ALA   A O   1 
ATOM   6547  C  CB  . ALA   A 1 828  ? -66.18100  90.07300  6.99700   1.000 52.18088  ?  826  ALA   A CB  1 
ATOM   6548  N  N   . LEU   A 1 829  ? -67.71000  87.38100  6.28400   1.000 49.01334  ?  827  LEU   A N   1 
ATOM   6549  C  CA  . LEU   A 1 829  ? -67.85600  86.15800  5.49900   1.000 46.46446  ?  827  LEU   A CA  1 
ATOM   6550  C  C   . LEU   A 1 829  ? -69.18000  86.14100  4.74800   1.000 54.94732  ?  827  LEU   A C   1 
ATOM   6551  O  O   . LEU   A 1 829  ? -69.25300  85.65800  3.61100   1.000 57.46000  ?  827  LEU   A O   1 
ATOM   6552  C  CB  . LEU   A 1 829  ? -67.73900  84.93200  6.40300   1.000 50.42896  ?  827  LEU   A CB  1 
ATOM   6553  C  CG  . LEU   A 1 829  ? -66.34800  84.60500  6.94300   1.000 40.09114  ?  827  LEU   A CG  1 
ATOM   6554  C  CD1 . LEU   A 1 829  ? -66.41500  83.43200  7.90500   1.000 35.13288  ?  827  LEU   A CD1 1 
ATOM   6555  C  CD2 . LEU   A 1 829  ? -65.39400  84.30800  5.79800   1.000 32.37089  ?  827  LEU   A CD2 1 
ATOM   6556  N  N   . GLU   A 1 830  ? -70.24000  86.66500  5.36700   1.000 63.87961  ?  828  GLU   A N   1 
ATOM   6557  C  CA  . GLU   A 1 830  ? -71.52700  86.74500  4.68400   1.000 60.91313  ?  828  GLU   A CA  1 
ATOM   6558  C  C   . GLU   A 1 830  ? -71.50900  87.78700  3.57200   1.000 56.39255  ?  828  GLU   A C   1 
ATOM   6559  O  O   . GLU   A 1 830  ? -72.25700  87.65900  2.59600   1.000 55.17077  ?  828  GLU   A O   1 
ATOM   6560  C  CB  . GLU   A 1 830  ? -72.63500  87.04400  5.69500   1.000 57.34796  ?  828  GLU   A CB  1 
ATOM   6561  C  CG  . GLU   A 1 830  ? -73.01100  85.84300  6.55400   1.000 68.71202  ?  828  GLU   A CG  1 
ATOM   6562  C  CD  . GLU   A 1 830  ? -73.77500  86.22600  7.80700   1.000 63.61789  ?  828  GLU   A CD  1 
ATOM   6563  O  OE1 . GLU   A 1 830  ? -73.64700  87.38500  8.25400   1.000 59.26544  ?  828  GLU   A OE1 1 
ATOM   6564  O  OE2 . GLU   A 1 830  ? -74.50200  85.36600  8.34600   1.000 63.58561  -1 828  GLU   A OE2 1 
ATOM   6565  N  N   . GLN   A 1 831  ? -70.66600  88.81700  3.69500   1.000 62.76274  ?  829  GLN   A N   1 
ATOM   6566  C  CA  . GLN   A 1 831  ? -70.49600  89.75700  2.59100   1.000 54.34909  ?  829  GLN   A CA  1 
ATOM   6567  C  C   . GLN   A 1 831  ? -69.82500  89.08400  1.40200   1.000 58.01704  ?  829  GLN   A C   1 
ATOM   6568  O  O   . GLN   A 1 831  ? -70.20600  89.32100  0.25000   1.000 65.75442  ?  829  GLN   A O   1 
ATOM   6569  C  CB  . GLN   A 1 831  ? -69.68100  90.97100  3.04100   1.000 56.07170  ?  829  GLN   A CB  1 
ATOM   6570  C  CG  . GLN   A 1 831  ? -70.19300  91.62400  4.31000   1.000 73.33973  ?  829  GLN   A CG  1 
ATOM   6571  C  CD  . GLN   A 1 831  ? -69.69300  93.04400  4.49200   1.000 85.39444  ?  829  GLN   A CD  1 
ATOM   6572  O  OE1 . GLN   A 1 831  ? -68.74100  93.29000  5.23500   1.000 66.17317  ?  829  GLN   A OE1 1 
ATOM   6573  N  NE2 . GLN   A 1 831  ? -70.34100  93.98900  3.82000   1.000 90.04359  ?  829  GLN   A NE2 1 
ATOM   6574  N  N   . LEU   A 1 832  ? -68.82600  88.23700  1.66500   1.000 52.61481  ?  830  LEU   A N   1 
ATOM   6575  C  CA  . LEU   A 1 832  ? -68.14000  87.54100  0.58300   1.000 42.99371  ?  830  LEU   A CA  1 
ATOM   6576  C  C   . LEU   A 1 832  ? -69.06500  86.57200  -0.14100  1.000 52.04215  ?  830  LEU   A C   1 
ATOM   6577  O  O   . LEU   A 1 832  ? -68.90300  86.34900  -1.34600  1.000 63.37084  ?  830  LEU   A O   1 
ATOM   6578  C  CB  . LEU   A 1 832  ? -66.91400  86.80500  1.12400   1.000 34.79975  ?  830  LEU   A CB  1 
ATOM   6579  C  CG  . LEU   A 1 832  ? -65.75900  87.68800  1.60200   1.000 41.65251  ?  830  LEU   A CG  1 
ATOM   6580  C  CD1 . LEU   A 1 832  ? -64.52400  86.85000  1.89800   1.000 36.35148  ?  830  LEU   A CD1 1 
ATOM   6581  C  CD2 . LEU   A 1 832  ? -65.44700  88.75900  0.57200   1.000 44.15149  ?  830  LEU   A CD2 1 
ATOM   6582  N  N   . VAL   A 1 833  ? -70.03400  85.98700  0.56800   1.000 44.68345  ?  831  VAL   A N   1 
ATOM   6583  C  CA  . VAL   A 1 833  ? -71.01500  85.12900  -0.09100  1.000 47.46592  ?  831  VAL   A CA  1 
ATOM   6584  C  C   . VAL   A 1 833  ? -71.80400  85.92600  -1.12200  1.000 51.39767  ?  831  VAL   A C   1 
ATOM   6585  O  O   . VAL   A 1 833  ? -72.14000  85.41800  -2.19800  1.000 50.51520  ?  831  VAL   A O   1 
ATOM   6586  C  CB  . VAL   A 1 833  ? -71.94100  84.47300  0.95200   1.000 36.25775  ?  831  VAL   A CB  1 
ATOM   6587  C  CG1 . VAL   A 1 833  ? -72.97000  83.58700  0.26900   1.000 39.68756  ?  831  VAL   A CG1 1 
ATOM   6588  C  CG2 . VAL   A 1 833  ? -71.12800  83.66800  1.94800   1.000 41.89810  ?  831  VAL   A CG2 1 
ATOM   6589  N  N   . LEU   A 1 834  ? -72.09700  87.19100  -0.81600  1.000 48.84172  ?  832  LEU   A N   1 
ATOM   6590  C  CA  . LEU   A 1 834  ? -72.82000  88.04000  -1.75500  1.000 52.61533  ?  832  LEU   A CA  1 
ATOM   6591  C  C   . LEU   A 1 834  ? -71.91100  88.52900  -2.87700  1.000 57.31808  ?  832  LEU   A C   1 
ATOM   6592  O  O   . LEU   A 1 834  ? -72.32000  88.55300  -4.04400  1.000 62.33933  ?  832  LEU   A O   1 
ATOM   6593  C  CB  . LEU   A 1 834  ? -73.44100  89.22500  -1.01000  1.000 62.15948  ?  832  LEU   A CB  1 
ATOM   6594  C  CG  . LEU   A 1 834  ? -74.65500  89.95000  -1.60500  1.000 73.26333  ?  832  LEU   A CG  1 
ATOM   6595  C  CD1 . LEU   A 1 834  ? -74.29500  90.81400  -2.81400  1.000 77.03561  ?  832  LEU   A CD1 1 
ATOM   6596  C  CD2 . LEU   A 1 834  ? -75.75400  88.95300  -1.95900  1.000 45.69293  ?  832  LEU   A CD2 1 
ATOM   6597  N  N   . ARG   A 1 835  ? -70.67700  88.91300  -2.54200  1.000 54.21763  ?  833  ARG   A N   1 
ATOM   6598  C  CA  . ARG   A 1 835  ? -69.78100  89.51300  -3.52800  1.000 47.02976  ?  833  ARG   A CA  1 
ATOM   6599  C  C   . ARG   A 1 835  ? -69.40400  88.52800  -4.62800  1.000 51.67863  ?  833  ARG   A C   1 
ATOM   6600  O  O   . ARG   A 1 835  ? -69.26300  88.91700  -5.79400  1.000 47.85052  ?  833  ARG   A O   1 
ATOM   6601  C  CB  . ARG   A 1 835  ? -68.52800  90.04100  -2.83000  1.000 35.24409  ?  833  ARG   A CB  1 
ATOM   6602  C  CG  . ARG   A 1 835  ? -67.50200  90.68100  -3.75200  1.000 47.77046  ?  833  ARG   A CG  1 
ATOM   6603  C  CD  . ARG   A 1 835  ? -66.21700  90.96100  -2.99400  1.000 50.15280  ?  833  ARG   A CD  1 
ATOM   6604  N  NE  . ARG   A 1 835  ? -65.74700  92.32900  -3.17300  1.000 54.16550  ?  833  ARG   A NE  1 
ATOM   6605  C  CZ  . ARG   A 1 835  ? -64.72200  92.67500  -3.94000  1.000 63.93042  ?  833  ARG   A CZ  1 
ATOM   6606  N  NH1 . ARG   A 1 835  ? -64.03700  91.77600  -4.62700  1.000 71.47331  ?  833  ARG   A NH1 1 
ATOM   6607  N  NH2 . ARG   A 1 835  ? -64.37100  93.95500  -4.01200  1.000 76.89831  ?  833  ARG   A NH2 1 
ATOM   6608  N  N   . HIS   A 1 836  ? -69.23700  87.25400  -4.28500  1.000 39.88272  ?  834  HIS   A N   1 
ATOM   6609  C  CA  . HIS   A 1 836  ? -68.72900  86.25000  -5.21300  1.000 43.12767  ?  834  HIS   A CA  1 
ATOM   6610  C  C   . HIS   A 1 836  ? -69.82800  85.24600  -5.53100  1.000 41.44224  ?  834  HIS   A C   1 
ATOM   6611  O  O   . HIS   A 1 836  ? -70.38000  84.61400  -4.62300  1.000 51.84918  ?  834  HIS   A O   1 
ATOM   6612  C  CB  . HIS   A 1 836  ? -67.50300  85.55300  -4.62700  1.000 50.41166  ?  834  HIS   A CB  1 
ATOM   6613  C  CG  . HIS   A 1 836  ? -66.41500  86.49800  -4.22200  1.000 40.38246  ?  834  HIS   A CG  1 
ATOM   6614  N  ND1 . HIS   A 1 836  ? -65.53800  87.05400  -5.12900  1.000 43.51483  ?  834  HIS   A ND1 1 
ATOM   6615  C  CD2 . HIS   A 1 836  ? -66.07100  86.99700  -3.01200  1.000 36.76591  ?  834  HIS   A CD2 1 
ATOM   6616  C  CE1 . HIS   A 1 836  ? -64.69600  87.84900  -4.49300  1.000 42.99234  ?  834  HIS   A CE1 1 
ATOM   6617  N  NE2 . HIS   A 1 836  ? -64.99700  87.83100  -3.20700  1.000 44.95967  ?  834  HIS   A NE2 1 
ATOM   6618  N  N   . GLU   A 1 837  ? -70.13800  85.09700  -6.82100  1.000 28.02655  ?  835  GLU   A N   1 
ATOM   6619  C  CA  . GLU   A 1 837  ? -71.19600  84.18400  -7.23600  1.000 30.85580  ?  835  GLU   A CA  1 
ATOM   6620  C  C   . GLU   A 1 837  ? -70.83100  82.72400  -7.01300  1.000 31.92162  ?  835  GLU   A C   1 
ATOM   6621  O  O   . GLU   A 1 837  ? -71.73100  81.88000  -6.94500  1.000 34.95568  ?  835  GLU   A O   1 
ATOM   6622  C  CB  . GLU   A 1 837  ? -71.54200  84.40900  -8.70800  1.000 38.15339  ?  835  GLU   A CB  1 
ATOM   6623  C  CG  . GLU   A 1 837  ? -72.16900  85.76000  -8.99400  1.000 57.71025  ?  835  GLU   A CG  1 
ATOM   6624  C  CD  . GLU   A 1 837  ? -72.86800  85.80300  -10.33700 1.000 62.89833  ?  835  GLU   A CD  1 
ATOM   6625  O  OE1 . GLU   A 1 837  ? -72.57800  84.93600  -11.18800 1.000 55.88730  ?  835  GLU   A OE1 1 
ATOM   6626  O  OE2 . GLU   A 1 837  ? -73.71500  86.69900  -10.53800 1.000 87.52111  -1 835  GLU   A OE2 1 
ATOM   6627  N  N   . GLY   A 1 838  ? -69.54000  82.40400  -6.90900  1.000 34.93573  ?  836  GLY   A N   1 
ATOM   6628  C  CA  . GLY   A 1 838  ? -69.15400  81.03100  -6.62700  1.000 33.86157  ?  836  GLY   A CA  1 
ATOM   6629  C  C   . GLY   A 1 838  ? -69.66300  80.55700  -5.28100  1.000 38.08544  ?  836  GLY   A C   1 
ATOM   6630  O  O   . GLY   A 1 838  ? -70.08800  79.40800  -5.13400  1.000 36.53917  ?  836  GLY   A O   1 
ATOM   6631  N  N   . LEU   A 1 839  ? -69.63700  81.44000  -4.28100  1.000 40.29919  ?  837  LEU   A N   1 
ATOM   6632  C  CA  . LEU   A 1 839  ? -70.22400  81.15500  -2.97900  1.000 35.18130  ?  837  LEU   A CA  1 
ATOM   6633  C  C   . LEU   A 1 839  ? -71.74400  81.10900  -3.01700  1.000 39.00704  ?  837  LEU   A C   1 
ATOM   6634  O  O   . LEU   A 1 839  ? -72.36300  80.80800  -1.99100  1.000 47.70416  ?  837  LEU   A O   1 
ATOM   6635  C  CB  . LEU   A 1 839  ? -69.75800  82.19800  -1.96300  1.000 29.53433  ?  837  LEU   A CB  1 
ATOM   6636  C  CG  . LEU   A 1 839  ? -68.31900  82.02400  -1.47700  1.000 32.56985  ?  837  LEU   A CG  1 
ATOM   6637  C  CD1 . LEU   A 1 839  ? -67.72600  83.35300  -1.04500  1.000 31.54289  ?  837  LEU   A CD1 1 
ATOM   6638  C  CD2 . LEU   A 1 839  ? -68.27700  81.02400  -0.33400  1.000 38.52580  ?  837  LEU   A CD2 1 
ATOM   6639  N  N   . ARG   A 1 840  ? -72.35800  81.40700  -4.16400  1.000 46.11779  ?  838  ARG   A N   1 
ATOM   6640  C  CA  . ARG   A 1 840  ? -73.79700  81.26500  -4.34800  1.000 42.03111  ?  838  ARG   A CA  1 
ATOM   6641  C  C   . ARG   A 1 840  ? -74.11900  80.41400  -5.57100  1.000 44.19002  ?  838  ARG   A C   1 
ATOM   6642  O  O   . ARG   A 1 840  ? -75.21700  80.52300  -6.12500  1.000 55.70443  ?  838  ARG   A O   1 
ATOM   6643  C  CB  . ARG   A 1 840  ? -74.46800  82.63600  -4.46100  1.000 42.71629  ?  838  ARG   A CB  1 
ATOM   6644  C  CG  . ARG   A 1 840  ? -74.49000  83.41900  -3.15900  1.000 45.30793  ?  838  ARG   A CG  1 
ATOM   6645  C  CD  . ARG   A 1 840  ? -75.05500  84.81900  -3.34900  1.000 52.83071  ?  838  ARG   A CD  1 
ATOM   6646  N  NE  . ARG   A 1 840  ? -74.18200  85.66200  -4.15800  1.000 49.95292  ?  838  ARG   A NE  1 
ATOM   6647  C  CZ  . ARG   A 1 840  ? -74.40800  85.97700  -5.42600  1.000 51.05876  ?  838  ARG   A CZ  1 
ATOM   6648  N  NH1 . ARG   A 1 840  ? -75.48500  85.54700  -6.06400  1.000 50.26877  ?  838  ARG   A NH1 1 
ATOM   6649  N  NH2 . ARG   A 1 840  ? -73.53500  86.74800  -6.06900  1.000 50.68600  ?  838  ARG   A NH2 1 
ATOM   6650  N  N   . SER   A 1 841  ? -73.18500  79.57100  -6.00000  1.000 43.45886  ?  839  SER   A N   1 
ATOM   6651  C  CA  . SER   A 1 841  ? -73.36000  78.73000  -7.17400  1.000 46.55978  ?  839  SER   A CA  1 
ATOM   6652  C  C   . SER   A 1 841  ? -73.70700  77.30700  -6.75600  1.000 49.91790  ?  839  SER   A C   1 
ATOM   6653  O  O   . SER   A 1 841  ? -73.11600  76.76200  -5.81900  1.000 64.34837  ?  839  SER   A O   1 
ATOM   6654  C  CB  . SER   A 1 841  ? -72.09300  78.72500  -8.03100  1.000 50.69235  ?  839  SER   A CB  1 
ATOM   6655  O  OG  . SER   A 1 841  ? -71.84300  80.00400  -8.58700  1.000 53.53061  ?  839  SER   A OG  1 
ATOM   6656  N  N   . THR   A 1 842  ? -74.67000  76.71200  -7.45600  1.000 45.12127  ?  840  THR   A N   1 
ATOM   6657  C  CA  . THR   A 1 842  ? -75.09300  75.34100  -7.21300  1.000 44.72979  ?  840  THR   A CA  1 
ATOM   6658  C  C   . THR   A 1 842  ? -74.99500  74.55000  -8.50900  1.000 42.04535  ?  840  THR   A C   1 
ATOM   6659  O  O   . THR   A 1 842  ? -75.33600  75.05500  -9.58300  1.000 48.88405  ?  840  THR   A O   1 
ATOM   6660  C  CB  . THR   A 1 842  ? -76.52500  75.28000  -6.66200  1.000 45.95146  ?  840  THR   A CB  1 
ATOM   6661  O  OG1 . THR   A 1 842  ? -77.42700  75.90000  -7.58700  1.000 59.64090  ?  840  THR   A OG1 1 
ATOM   6662  C  CG2 . THR   A 1 842  ? -76.60900  75.99600  -5.32400  1.000 45.48890  ?  840  THR   A CG2 1 
ATOM   6663  N  N   . TYR   A 1 843  ? -74.53300  73.30700  -8.40300  1.000 45.70597  ?  841  TYR   A N   1 
ATOM   6664  C  CA  . TYR   A 1 843  ? -74.21200  72.47700  -9.55700  1.000 38.19289  ?  841  TYR   A CA  1 
ATOM   6665  C  C   . TYR   A 1 843  ? -75.19300  71.31400  -9.63200  1.000 48.80946  ?  841  TYR   A C   1 
ATOM   6666  O  O   . TYR   A 1 843  ? -75.27400  70.50300  -8.70300  1.000 52.87824  ?  841  TYR   A O   1 
ATOM   6667  C  CB  . TYR   A 1 843  ? -72.77200  71.96900  -9.47400  1.000 39.93373  ?  841  TYR   A CB  1 
ATOM   6668  C  CG  . TYR   A 1 843  ? -71.74100  73.07700  -9.46000  1.000 44.77889  ?  841  TYR   A CG  1 
ATOM   6669  C  CD1 . TYR   A 1 843  ? -71.48600  73.80300  -8.30200  1.000 42.43913  ?  841  TYR   A CD1 1 
ATOM   6670  C  CD2 . TYR   A 1 843  ? -71.02200  73.39700  -10.60300 1.000 43.94247  ?  841  TYR   A CD2 1 
ATOM   6671  C  CE1 . TYR   A 1 843  ? -70.54900  74.81800  -8.28600  1.000 45.96767  ?  841  TYR   A CE1 1 
ATOM   6672  C  CE2 . TYR   A 1 843  ? -70.08100  74.40900  -10.59600 1.000 45.90237  ?  841  TYR   A CE2 1 
ATOM   6673  C  CZ  . TYR   A 1 843  ? -69.84800  75.11500  -9.43500  1.000 45.69111  ?  841  TYR   A CZ  1 
ATOM   6674  O  OH  . TYR   A 1 843  ? -68.91200  76.12300  -9.42400  1.000 44.57078  ?  841  TYR   A OH  1 
ATOM   6675  N  N   . HIS   A 1 844  ? -75.92900  71.23500  -10.73700 1.000 49.24775  ?  842  HIS   A N   1 
ATOM   6676  C  CA  . HIS   A 1 844  ? -76.92100  70.19500  -10.96000 1.000 43.93766  ?  842  HIS   A CA  1 
ATOM   6677  C  C   . HIS   A 1 844  ? -76.65900  69.55600  -12.31700 1.000 52.25613  ?  842  HIS   A C   1 
ATOM   6678  O  O   . HIS   A 1 844  ? -75.75300  69.96000  -13.05200 1.000 60.19874  ?  842  HIS   A O   1 
ATOM   6679  C  CB  . HIS   A 1 844  ? -78.34000  70.76900  -10.87800 1.000 35.54219  ?  842  HIS   A CB  1 
ATOM   6680  C  CG  . HIS   A 1 844  ? -78.47500  71.88200  -9.88800  1.000 45.82209  ?  842  HIS   A CG  1 
ATOM   6681  N  ND1 . HIS   A 1 844  ? -78.92800  71.68600  -8.60100  1.000 53.87338  ?  842  HIS   A ND1 1 
ATOM   6682  C  CD2 . HIS   A 1 844  ? -78.19600  73.20300  -9.99100  1.000 43.36290  ?  842  HIS   A CD2 1 
ATOM   6683  C  CE1 . HIS   A 1 844  ? -78.93200  72.84000  -7.95800  1.000 57.51902  ?  842  HIS   A CE1 1 
ATOM   6684  N  NE2 . HIS   A 1 844  ? -78.49400  73.77700  -8.77900  1.000 51.91164  ?  842  HIS   A NE2 1 
ATOM   6685  N  N   . MET   A 1 845  ? -77.46000  68.55100  -12.65600 1.000 51.49550  ?  843  MET   A N   1 
ATOM   6686  C  CA  . MET   A 1 845  ? -77.27100  67.79200  -13.88500 1.000 64.66681  ?  843  MET   A CA  1 
ATOM   6687  C  C   . MET   A 1 845  ? -78.54500  67.84500  -14.71600 1.000 77.49449  ?  843  MET   A C   1 
ATOM   6688  O  O   . MET   A 1 845  ? -79.59700  67.36500  -14.28100 1.000 74.04602  ?  843  MET   A O   1 
ATOM   6689  C  CB  . MET   A 1 845  ? -76.87700  66.34700  -13.57500 1.000 46.77618  ?  843  MET   A CB  1 
ATOM   6690  C  CG  . MET   A 1 845  ? -75.87100  65.77400  -14.55500 1.000 61.40674  ?  843  MET   A CG  1 
ATOM   6691  S  SD  . MET   A 1 845  ? -75.24100  64.16100  -14.06200 1.000 91.68372  ?  843  MET   A SD  1 
ATOM   6692  C  CE  . MET   A 1 845  ? -74.44300  63.65000  -15.58100 1.000 65.90746  ?  843  MET   A CE  1 
ATOM   6693  N  N   . ARG   A 1 846  ? -78.44600  68.43300  -15.90900 1.000 80.44894  ?  844  ARG   A N   1 
ATOM   6694  C  CA  . ARG   A 1 846  ? -79.55200  68.51100  -16.86200 1.000 61.44312  ?  844  ARG   A CA  1 
ATOM   6695  C  C   . ARG   A 1 846  ? -79.32000  67.43800  -17.92000 1.000 49.22260  ?  844  ARG   A C   1 
ATOM   6696  O  O   . ARG   A 1 846  ? -78.51200  67.61600  -18.83500 1.000 53.94620  ?  844  ARG   A O   1 
ATOM   6697  C  CB  . ARG   A 1 846  ? -79.63900  69.90500  -17.47600 1.000 62.98210  ?  844  ARG   A CB  1 
ATOM   6698  C  CG  . ARG   A 1 846  ? -80.65700  70.03800  -18.59500 1.000 62.32200  ?  844  ARG   A CG  1 
ATOM   6699  C  CD  . ARG   A 1 846  ? -81.62900  71.17500  -18.32400 1.000 68.94558  ?  844  ARG   A CD  1 
ATOM   6700  N  NE  . ARG   A 1 846  ? -82.59500  70.83500  -17.28500 1.000 75.18096  ?  844  ARG   A NE  1 
ATOM   6701  C  CZ  . ARG   A 1 846  ? -83.57000  71.63600  -16.87800 1.000 78.71196  ?  844  ARG   A CZ  1 
ATOM   6702  N  NH1 . ARG   A 1 846  ? -83.72400  72.85000  -17.38300 1.000 82.69829  ?  844  ARG   A NH1 1 
ATOM   6703  N  NH2 . ARG   A 1 846  ? -84.41500  71.20800  -15.94400 1.000 89.96547  ?  844  ARG   A NH2 1 
ATOM   6704  N  N   . GLY   A 1 847  ? -80.03000  66.32000  -17.79000 1.000 47.09563  ?  845  GLY   A N   1 
ATOM   6705  C  CA  . GLY   A 1 847  ? -79.76600  65.16300  -18.62200 1.000 53.83947  ?  845  GLY   A CA  1 
ATOM   6706  C  C   . GLY   A 1 847  ? -78.41200  64.55300  -18.32100 1.000 67.58890  ?  845  GLY   A C   1 
ATOM   6707  O  O   . GLY   A 1 847  ? -78.17200  64.07800  -17.20700 1.000 74.41906  ?  845  GLY   A O   1 
ATOM   6708  N  N   . ASP   A 1 848  ? -77.51400  64.56200  -19.30600 1.000 64.70869  ?  846  ASP   A N   1 
ATOM   6709  C  CA  . ASP   A 1 848  ? -76.14300  64.11000  -19.11500 1.000 56.55786  ?  846  ASP   A CA  1 
ATOM   6710  C  C   . ASP   A 1 848  ? -75.15800  65.27100  -19.03400 1.000 60.68960  ?  846  ASP   A C   1 
ATOM   6711  O  O   . ASP   A 1 848  ? -73.94700  65.05800  -19.15700 1.000 68.70843  ?  846  ASP   A O   1 
ATOM   6712  C  CB  . ASP   A 1 848  ? -75.73800  63.15100  -20.23600 1.000 60.11157  ?  846  ASP   A CB  1 
ATOM   6713  C  CG  . ASP   A 1 848  ? -76.44900  61.81600  -20.14400 1.000 74.72048  ?  846  ASP   A CG  1 
ATOM   6714  O  OD1 . ASP   A 1 848  ? -77.67300  61.81400  -19.90300 1.000 78.46667  ?  846  ASP   A OD1 1 
ATOM   6715  O  OD2 . ASP   A 1 848  ? -75.78800  60.77100  -20.32200 1.000 80.14287  -1 846  ASP   A OD2 1 
ATOM   6716  N  N   . GLU   A 1 849  ? -75.65000  66.48900  -18.82300 1.000 58.69660  ?  847  GLU   A N   1 
ATOM   6717  C  CA  . GLU   A 1 849  ? -74.81600  67.68300  -18.79400 1.000 66.33322  ?  847  GLU   A CA  1 
ATOM   6718  C  C   . GLU   A 1 849  ? -74.81900  68.29400  -17.40000 1.000 72.47006  ?  847  GLU   A C   1 
ATOM   6719  O  O   . GLU   A 1 849  ? -75.88500  68.53300  -16.82200 1.000 68.35297  ?  847  GLU   A O   1 
ATOM   6720  C  CB  . GLU   A 1 849  ? -75.29400  68.71100  -19.82100 1.000 52.85499  ?  847  GLU   A CB  1 
ATOM   6721  C  CG  . GLU   A 1 849  ? -74.83400  70.12800  -19.52700 1.000 77.40704  ?  847  GLU   A CG  1 
ATOM   6722  C  CD  . GLU   A 1 849  ? -74.50200  70.90700  -20.78100 1.000 104.26340 ?  847  GLU   A CD  1 
ATOM   6723  O  OE1 . GLU   A 1 849  ? -73.78400  70.36200  -21.64700 1.000 114.43720 ?  847  GLU   A OE1 1 
ATOM   6724  O  OE2 . GLU   A 1 849  ? -74.95800  72.06300  -20.90300 1.000 111.86832 -1 847  GLU   A OE2 1 
ATOM   6725  N  N   . ILE   A 1 850  ? -73.62500  68.54500  -16.87200 1.000 63.69708  ?  848  ILE   A N   1 
ATOM   6726  C  CA  . ILE   A 1 850  ? -73.46700  69.20900  -15.58300 1.000 53.20772  ?  848  ILE   A CA  1 
ATOM   6727  C  C   . ILE   A 1 850  ? -73.63200  70.71000  -15.79200 1.000 55.37902  ?  848  ILE   A C   1 
ATOM   6728  O  O   . ILE   A 1 850  ? -72.93000  71.31300  -16.61200 1.000 71.10835  ?  848  ILE   A O   1 
ATOM   6729  C  CB  . ILE   A 1 850  ? -72.10200  68.88200  -14.96200 1.000 52.03225  ?  848  ILE   A CB  1 
ATOM   6730  C  CG1 . ILE   A 1 850  ? -71.88900  67.36600  -14.93300 1.000 53.97094  ?  848  ILE   A CG1 1 
ATOM   6731  C  CG2 . ILE   A 1 850  ? -71.99300  69.48000  -13.56700 1.000 57.26351  ?  848  ILE   A CG2 1 
ATOM   6732  C  CD1 . ILE   A 1 850  ? -70.45000  66.95000  -14.72800 1.000 35.52282  ?  848  ILE   A CD1 1 
ATOM   6733  N  N   . VAL   A 1 851  ? -74.56100  71.31500  -15.05500 1.000 44.33639  ?  849  VAL   A N   1 
ATOM   6734  C  CA  . VAL   A 1 851  ? -74.87600  72.72900  -15.20000 1.000 49.66831  ?  849  VAL   A CA  1 
ATOM   6735  C  C   . VAL   A 1 851  ? -74.66000  73.42500  -13.86000 1.000 51.97354  ?  849  VAL   A C   1 
ATOM   6736  O  O   . VAL   A 1 851  ? -74.42900  72.78900  -12.83100 1.000 58.53526  ?  849  VAL   A O   1 
ATOM   6737  C  CB  . VAL   A 1 851  ? -76.31300  72.95900  -15.70900 1.000 59.69997  ?  849  VAL   A CB  1 
ATOM   6738  C  CG1 . VAL   A 1 851  ? -76.63300  72.00300  -16.84900 1.000 63.79004  ?  849  VAL   A CG1 1 
ATOM   6739  C  CG2 . VAL   A 1 851  ? -77.31500  72.80600  -14.57300 1.000 62.59394  ?  849  VAL   A CG2 1 
ATOM   6740  N  N   . LYS   A 1 852  ? -74.74100  74.75400  -13.88800 1.000 45.39332  ?  850  LYS   A N   1 
ATOM   6741  C  CA  . LYS   A 1 852  ? -74.58200  75.57900  -12.70000 1.000 48.05786  ?  850  LYS   A CA  1 
ATOM   6742  C  C   . LYS   A 1 852  ? -75.75200  76.54800  -12.59400 1.000 50.85788  ?  850  LYS   A C   1 
ATOM   6743  O  O   . LYS   A 1 852  ? -76.30100  76.99300  -13.60600 1.000 47.06105  ?  850  LYS   A O   1 
ATOM   6744  C  CB  . LYS   A 1 852  ? -73.25500  76.35800  -12.72500 1.000 39.49664  ?  850  LYS   A CB  1 
ATOM   6745  C  CG  . LYS   A 1 852  ? -72.88600  76.98600  -11.39100 1.000 44.24934  ?  850  LYS   A CG  1 
ATOM   6746  C  CD  . LYS   A 1 852  ? -72.00000  78.20900  -11.55900 1.000 45.52695  ?  850  LYS   A CD  1 
ATOM   6747  C  CE  . LYS   A 1 852  ? -70.56300  77.85100  -11.88800 1.000 47.19746  ?  850  LYS   A CE  1 
ATOM   6748  N  NZ  . LYS   A 1 852  ? -69.69100  79.05900  -11.82000 1.000 39.32391  ?  850  LYS   A NZ  1 
ATOM   6749  N  N   . ARG   A 1 853  ? -76.13300  76.86900  -11.35700 1.000 50.41471  ?  851  ARG   A N   1 
ATOM   6750  C  CA  . ARG   A 1 853  ? -77.22300  77.80400  -11.08800 1.000 49.86607  ?  851  ARG   A CA  1 
ATOM   6751  C  C   . ARG   A 1 853  ? -76.80400  78.74600  -9.97000  1.000 45.81240  ?  851  ARG   A C   1 
ATOM   6752  O  O   . ARG   A 1 853  ? -76.44400  78.29300  -8.87900  1.000 57.86345  ?  851  ARG   A O   1 
ATOM   6753  C  CB  . ARG   A 1 853  ? -78.51200  77.06800  -10.70800 1.000 38.95785  ?  851  ARG   A CB  1 
ATOM   6754  C  CG  . ARG   A 1 853  ? -79.07700  76.18000  -11.80200 1.000 44.88860  ?  851  ARG   A CG  1 
ATOM   6755  C  CD  . ARG   A 1 853  ? -80.32300  75.45600  -11.32400 1.000 42.96790  ?  851  ARG   A CD  1 
ATOM   6756  N  NE  . ARG   A 1 853  ? -80.64600  74.31000  -12.16500 1.000 47.76283  ?  851  ARG   A NE  1 
ATOM   6757  C  CZ  . ARG   A 1 853  ? -81.41700  73.30000  -11.78400 1.000 47.88183  ?  851  ARG   A CZ  1 
ATOM   6758  N  NH1 . ARG   A 1 853  ? -81.96000  73.26300  -10.57800 1.000 47.15357  ?  851  ARG   A NH1 1 
ATOM   6759  N  NH2 . ARG   A 1 853  ? -81.64200  72.29900  -12.63100 1.000 35.60389  ?  851  ARG   A NH2 1 
ATOM   6760  N  N   . ILE   A 1 854  ? -76.86200  80.04700  -10.23600 1.000 37.11065  ?  852  ILE   A N   1 
ATOM   6761  C  CA  . ILE   A 1 854  ? -76.49100  81.06600  -9.26000  1.000 48.51978  ?  852  ILE   A CA  1 
ATOM   6762  C  C   . ILE   A 1 854  ? -77.73500  81.48600  -8.48900  1.000 54.09234  ?  852  ILE   A C   1 
ATOM   6763  O  O   . ILE   A 1 854  ? -78.80600  81.69400  -9.07000  1.000 64.73136  ?  852  ILE   A O   1 
ATOM   6764  C  CB  . ILE   A 1 854  ? -75.81800  82.27300  -9.94600  1.000 53.40378  ?  852  ILE   A CB  1 
ATOM   6765  C  CG1 . ILE   A 1 854  ? -74.33700  81.98900  -10.21800 1.000 44.57435  ?  852  ILE   A CG1 1 
ATOM   6766  C  CG2 . ILE   A 1 854  ? -75.95700  83.53300  -9.10200  1.000 44.11719  ?  852  ILE   A CG2 1 
ATOM   6767  C  CD1 . ILE   A 1 854  ? -74.08800  81.01800  -11.34200 1.000 44.62963  ?  852  ILE   A CD1 1 
ATOM   6768  N  N   . VAL   A 1 855  ? -77.59400  81.60300  -7.17200  1.000 65.98303  ?  853  VAL   A N   1 
ATOM   6769  C  CA  . VAL   A 1 855  ? -78.69700  81.95200  -6.28100  1.000 47.63805  ?  853  VAL   A CA  1 
ATOM   6770  C  C   . VAL   A 1 855  ? -78.46200  83.36100  -5.74700  1.000 52.10919  ?  853  VAL   A C   1 
ATOM   6771  O  O   . VAL   A 1 855  ? -77.31900  83.71300  -5.42500  1.000 63.30201  ?  853  VAL   A O   1 
ATOM   6772  C  CB  . VAL   A 1 855  ? -78.82900  80.91500  -5.15200  1.000 41.85082  ?  853  VAL   A CB  1 
ATOM   6773  C  CG1 . VAL   A 1 855  ? -79.64600  81.45600  -3.99400  1.000 64.20590  ?  853  VAL   A CG1 1 
ATOM   6774  C  CG2 . VAL   A 1 855  ? -79.45300  79.63500  -5.69000  1.000 40.88687  ?  853  VAL   A CG2 1 
ATOM   6775  N  N   . PRO   A 1 856  ? -79.49700  84.20500  -5.65300  1.000 56.52212  ?  854  PRO   A N   1 
ATOM   6776  C  CA  . PRO   A 1 856  ? -79.26600  85.59300  -5.20900  1.000 51.33849  ?  854  PRO   A CA  1 
ATOM   6777  C  C   . PRO   A 1 856  ? -78.72500  85.71400  -3.79300  1.000 60.59909  ?  854  PRO   A C   1 
ATOM   6778  O  O   . PRO   A 1 856  ? -77.83900  86.54400  -3.54900  1.000 55.95940  ?  854  PRO   A O   1 
ATOM   6779  C  CB  . PRO   A 1 856  ? -80.65600  86.23400  -5.34300  1.000 48.59181  ?  854  PRO   A CB  1 
ATOM   6780  C  CG  . PRO   A 1 856  ? -81.61700  85.08300  -5.34000  1.000 53.34403  ?  854  PRO   A CG  1 
ATOM   6781  C  CD  . PRO   A 1 856  ? -80.89900  83.97800  -6.04300  1.000 60.53230  ?  854  PRO   A CD  1 
ATOM   6782  N  N   . ARG   A 1 857  ? -79.23000  84.92300  -2.84800  1.000 55.83853  ?  855  ARG   A N   1 
ATOM   6783  C  CA  . ARG   A 1 857  ? -78.80000  85.01700  -1.45900  1.000 54.02035  ?  855  ARG   A CA  1 
ATOM   6784  C  C   . ARG   A 1 857  ? -78.64900  83.62300  -0.86900  1.000 62.05466  ?  855  ARG   A C   1 
ATOM   6785  O  O   . ARG   A 1 857  ? -79.47900  82.74400  -1.11300  1.000 53.92493  ?  855  ARG   A O   1 
ATOM   6786  C  CB  . ARG   A 1 857  ? -79.79100  85.83700  -0.62100  1.000 40.15192  ?  855  ARG   A CB  1 
ATOM   6787  N  N   . ALA   A 1 858  ? -77.58800  83.43100  -0.08400  1.000 47.91718  ?  856  ALA   A N   1 
ATOM   6788  C  CA  . ALA   A 1 858  ? -77.29500  82.14900  0.53900   1.000 50.73216  ?  856  ALA   A CA  1 
ATOM   6789  C  C   . ALA   A 1 858  ? -77.00300  82.34800  2.02000   1.000 79.81324  ?  856  ALA   A C   1 
ATOM   6790  O  O   . ALA   A 1 858  ? -76.43700  83.36800  2.42700   1.000 73.73998  ?  856  ALA   A O   1 
ATOM   6791  C  CB  . ALA   A 1 858  ? -76.10900  81.45200  -0.14100  1.000 48.45938  ?  856  ALA   A CB  1 
ATOM   6792  N  N   . GLU   A 1 859  ? -77.38800  81.35700  2.82300   1.000 56.68068  ?  857  GLU   A N   1 
ATOM   6793  C  CA  . GLU   A 1 859  ? -77.25500  81.41600  4.27300   1.000 42.50856  ?  857  GLU   A CA  1 
ATOM   6794  C  C   . GLU   A 1 859  ? -75.99700  80.67000  4.70100   1.000 49.79443  ?  857  GLU   A C   1 
ATOM   6795  O  O   . GLU   A 1 859  ? -75.88000  79.46000  4.47600   1.000 40.95883  ?  857  GLU   A O   1 
ATOM   6796  C  CB  . GLU   A 1 859  ? -78.48900  80.82400  4.95600   1.000 47.17772  ?  857  GLU   A CB  1 
ATOM   6797  N  N   . LEU   A 1 860  ? -75.07100  81.39000  5.33200   1.000 51.12565  ?  858  LEU   A N   1 
ATOM   6798  C  CA  . LEU   A 1 860  ? -73.79700  80.81900  5.74900   1.000 44.43721  ?  858  LEU   A CA  1 
ATOM   6799  C  C   . LEU   A 1 860  ? -73.93500  80.09100  7.08200   1.000 42.66155  ?  858  LEU   A C   1 
ATOM   6800  O  O   . LEU   A 1 860  ? -74.68100  80.51800  7.96700   1.000 44.89281  ?  858  LEU   A O   1 
ATOM   6801  C  CB  . LEU   A 1 860  ? -72.74300  81.92000  5.86600   1.000 43.40595  ?  858  LEU   A CB  1 
ATOM   6802  C  CG  . LEU   A 1 860  ? -71.32700  81.52800  6.29000   1.000 51.14667  ?  858  LEU   A CG  1 
ATOM   6803  C  CD1 . LEU   A 1 860  ? -70.56700  80.92000  5.12500   1.000 38.72866  ?  858  LEU   A CD1 1 
ATOM   6804  C  CD2 . LEU   A 1 860  ? -70.58700  82.73100  6.85500   1.000 47.59769  ?  858  LEU   A CD2 1 
ATOM   6805  N  N   . SER   A 1 861  ? -73.20200  78.98800  7.22000   1.000 46.42184  ?  859  SER   A N   1 
ATOM   6806  C  CA  . SER   A 1 861  ? -73.18100  78.20500  8.45300   1.000 32.16915  ?  859  SER   A CA  1 
ATOM   6807  C  C   . SER   A 1 861  ? -72.00600  78.66800  9.30700   1.000 50.76876  ?  859  SER   A C   1 
ATOM   6808  O  O   . SER   A 1 861  ? -70.84700  78.37700  8.99200   1.000 53.34334  ?  859  SER   A O   1 
ATOM   6809  C  CB  . SER   A 1 861  ? -73.08200  76.71400  8.14000   1.000 23.35016  ?  859  SER   A CB  1 
ATOM   6810  O  OG  . SER   A 1 861  ? -72.85700  75.95600  9.31500   1.000 61.80935  ?  859  SER   A OG  1 
ATOM   6811  N  N   . PHE   A 1 862  ? -72.30100  79.38400  10.39000  1.000 46.01773  ?  860  PHE   A N   1 
ATOM   6812  C  CA  . PHE   A 1 862  ? -71.28500  79.91800  11.29600  1.000 37.39746  ?  860  PHE   A CA  1 
ATOM   6813  C  C   . PHE   A 1 862  ? -71.52300  79.31800  12.67900  1.000 44.78460  ?  860  PHE   A C   1 
ATOM   6814  O  O   . PHE   A 1 862  ? -72.31600  79.84000  13.46700  1.000 62.49549  ?  860  PHE   A O   1 
ATOM   6815  C  CB  . PHE   A 1 862  ? -71.32800  81.44200  11.32800  1.000 30.51715  ?  860  PHE   A CB  1 
ATOM   6816  C  CG  . PHE   A 1 862  ? -70.03200  82.07500  11.73600  1.000 45.19061  ?  860  PHE   A CG  1 
ATOM   6817  C  CD1 . PHE   A 1 862  ? -69.03000  82.28800  10.80400  1.000 46.63043  ?  860  PHE   A CD1 1 
ATOM   6818  C  CD2 . PHE   A 1 862  ? -69.81300  82.45900  13.04800  1.000 45.31528  ?  860  PHE   A CD2 1 
ATOM   6819  C  CE1 . PHE   A 1 862  ? -67.83400  82.87000  11.17100  1.000 46.48306  ?  860  PHE   A CE1 1 
ATOM   6820  C  CE2 . PHE   A 1 862  ? -68.61700  83.04300  13.42200  1.000 47.03299  ?  860  PHE   A CE2 1 
ATOM   6821  C  CZ  . PHE   A 1 862  ? -67.62700  83.24800  12.48100  1.000 55.62243  ?  860  PHE   A CZ  1 
ATOM   6822  N  N   . VAL   A 1 863  ? -70.82900  78.22300  12.97300  1.000 45.37387  ?  861  VAL   A N   1 
ATOM   6823  C  CA  . VAL   A 1 863  ? -70.97900  77.51300  14.23900  1.000 44.65938  ?  861  VAL   A CA  1 
ATOM   6824  C  C   . VAL   A 1 863  ? -69.98600  78.08200  15.24500  1.000 55.59673  ?  861  VAL   A C   1 
ATOM   6825  O  O   . VAL   A 1 863  ? -68.77500  78.07800  15.00500  1.000 57.69840  ?  861  VAL   A O   1 
ATOM   6826  C  CB  . VAL   A 1 863  ? -70.76800  76.00300  14.05500  1.000 47.10725  ?  861  VAL   A CB  1 
ATOM   6827  C  CG1 . VAL   A 1 863  ? -70.83000  75.29000  15.39900  1.000 50.30275  ?  861  VAL   A CG1 1 
ATOM   6828  C  CG2 . VAL   A 1 863  ? -71.79900  75.43500  13.09200  1.000 66.77933  ?  861  VAL   A CG2 1 
ATOM   6829  N  N   . ARG   A 1 864  ? -70.49500  78.56100  16.37600  1.000 43.11262  ?  862  ARG   A N   1 
ATOM   6830  C  CA  . ARG   A 1 864  ? -69.66000  79.07400  17.45400  1.000 40.19709  ?  862  ARG   A CA  1 
ATOM   6831  C  C   . ARG   A 1 864  ? -69.53800  78.02300  18.55000  1.000 55.77756  ?  862  ARG   A C   1 
ATOM   6832  O  O   . ARG   A 1 864  ? -70.54800  77.49100  19.02300  1.000 56.60890  ?  862  ARG   A O   1 
ATOM   6833  C  CB  . ARG   A 1 864  ? -70.23600  80.37600  18.01500  1.000 39.47587  ?  862  ARG   A CB  1 
ATOM   6834  C  CG  . ARG   A 1 864  ? -69.78700  81.61100  17.25200  1.000 60.26335  ?  862  ARG   A CG  1 
ATOM   6835  C  CD  . ARG   A 1 864  ? -70.90500  82.62600  17.10100  1.000 54.71976  ?  862  ARG   A CD  1 
ATOM   6836  N  NE  . ARG   A 1 864  ? -72.07200  82.04800  16.44600  1.000 68.65554  ?  862  ARG   A NE  1 
ATOM   6837  C  CZ  . ARG   A 1 864  ? -72.93300  82.73500  15.70900  1.000 72.74444  ?  862  ARG   A CZ  1 
ATOM   6838  N  NH1 . ARG   A 1 864  ? -72.76900  84.02700  15.47800  1.000 50.60852  ?  862  ARG   A NH1 1 
ATOM   6839  N  NH2 . ARG   A 1 864  ? -73.98100  82.10800  15.18200  1.000 78.87525  ?  862  ARG   A NH2 1 
ATOM   6840  N  N   . GLN   A 1 865  ? -68.30100  77.72200  18.94300  1.000 51.65715  ?  863  GLN   A N   1 
ATOM   6841  C  CA  . GLN   A 1 865  ? -68.02700  76.67700  19.91800  1.000 45.42468  ?  863  GLN   A CA  1 
ATOM   6842  C  C   . GLN   A 1 865  ? -66.98000  77.16200  20.91000  1.000 56.44725  ?  863  GLN   A C   1 
ATOM   6843  O  O   . GLN   A 1 865  ? -66.31900  78.18500  20.70800  1.000 57.73845  ?  863  GLN   A O   1 
ATOM   6844  C  CB  . GLN   A 1 865  ? -67.55200  75.38400  19.24000  1.000 32.97955  ?  863  GLN   A CB  1 
ATOM   6845  C  CG  . GLN   A 1 865  ? -68.63000  74.64400  18.46800  1.000 45.48253  ?  863  GLN   A CG  1 
ATOM   6846  C  CD  . GLN   A 1 865  ? -68.06800  73.51800  17.62200  1.000 54.66785  ?  863  GLN   A CD  1 
ATOM   6847  O  OE1 . GLN   A 1 865  ? -67.31200  73.75300  16.67800  1.000 50.76198  ?  863  GLN   A OE1 1 
ATOM   6848  N  NE2 . GLN   A 1 865  ? -68.43300  72.28600  17.95700  1.000 55.24206  ?  863  GLN   A NE2 1 
ATOM   6849  N  N   . THR   A 1 866  ? -66.83500  76.40300  21.99400  1.000 40.79723  ?  864  THR   A N   1 
ATOM   6850  C  CA  . THR   A 1 866  ? -65.84100  76.65300  23.03000  1.000 35.00304  ?  864  THR   A CA  1 
ATOM   6851  C  C   . THR   A 1 866  ? -64.99800  75.39800  23.20000  1.000 48.54982  ?  864  THR   A C   1 
ATOM   6852  O  O   . THR   A 1 866  ? -65.54100  74.29300  23.30400  1.000 45.20046  ?  864  THR   A O   1 
ATOM   6853  C  CB  . THR   A 1 866  ? -66.51000  77.03400  24.35600  1.000 43.11788  ?  864  THR   A CB  1 
ATOM   6854  O  OG1 . THR   A 1 866  ? -67.12700  78.32100  24.23200  1.000 56.55802  ?  864  THR   A OG1 1 
ATOM   6855  C  CG2 . THR   A 1 866  ? -65.49300  77.06500  25.48700  1.000 59.10407  ?  864  THR   A CG2 1 
ATOM   6856  N  N   . GLY   A 1 867  ? -63.67700  75.56200  23.22200  1.000 39.07496  ?  865  GLY   A N   1 
ATOM   6857  C  CA  . GLY   A 1 867  ? -62.80000  74.41500  23.31200  1.000 46.53778  ?  865  GLY   A CA  1 
ATOM   6858  C  C   . GLY   A 1 867  ? -61.50700  74.73700  24.03000  1.000 52.87724  ?  865  GLY   A C   1 
ATOM   6859  O  O   . GLY   A 1 867  ? -61.24100  75.88300  24.39800  1.000 53.91350  ?  865  GLY   A O   1 
ATOM   6860  N  N   . GLU   A 1 868  ? -60.70600  73.69700  24.23300  1.000 43.90570  ?  866  GLU   A N   1 
ATOM   6861  C  CA  . GLU   A 1 868  ? -59.37800  73.80100  24.81600  1.000 43.34705  ?  866  GLU   A CA  1 
ATOM   6862  C  C   . GLU   A 1 868  ? -58.33000  73.41800  23.77700  1.000 53.35562  ?  866  GLU   A C   1 
ATOM   6863  O  O   . GLU   A 1 868  ? -58.64800  72.94200  22.68400  1.000 55.86309  ?  866  GLU   A O   1 
ATOM   6864  C  CB  . GLU   A 1 868  ? -59.25400  72.90900  26.05700  1.000 44.81690  ?  866  GLU   A CB  1 
ATOM   6865  C  CG  . GLU   A 1 868  ? -59.45900  71.43000  25.78100  1.000 52.08950  ?  866  GLU   A CG  1 
ATOM   6866  C  CD  . GLU   A 1 868  ? -59.29400  70.57700  27.02300  1.000 66.61853  ?  866  GLU   A CD  1 
ATOM   6867  O  OE1 . GLU   A 1 868  ? -58.70800  71.07100  28.01000  1.000 53.60587  ?  866  GLU   A OE1 1 
ATOM   6868  O  OE2 . GLU   A 1 868  ? -59.75200  69.41500  27.01400  1.000 79.07964  -1 866  GLU   A OE2 1 
ATOM   6869  N  N   . GLU   A 1 869  ? -57.06200  73.62600  24.14300  1.000 46.24820  ?  867  GLU   A N   1 
ATOM   6870  C  CA  . GLU   A 1 869  ? -55.96500  73.36700  23.21400  1.000 46.61607  ?  867  GLU   A CA  1 
ATOM   6871  C  C   . GLU   A 1 869  ? -55.94800  71.91500  22.75500  1.000 51.07204  ?  867  GLU   A C   1 
ATOM   6872  O  O   . GLU   A 1 869  ? -55.64600  71.62700  21.59100  1.000 70.84786  ?  867  GLU   A O   1 
ATOM   6873  C  CB  . GLU   A 1 869  ? -54.63200  73.73500  23.86300  1.000 51.44033  ?  867  GLU   A CB  1 
ATOM   6874  C  CG  . GLU   A 1 869  ? -54.19600  75.16900  23.62500  1.000 68.73862  ?  867  GLU   A CG  1 
ATOM   6875  C  CD  . GLU   A 1 869  ? -53.29500  75.30400  22.41500  1.000 67.44270  ?  867  GLU   A CD  1 
ATOM   6876  O  OE1 . GLU   A 1 869  ? -53.19500  74.33300  21.63500  1.000 51.98182  ?  867  GLU   A OE1 1 
ATOM   6877  O  OE2 . GLU   A 1 869  ? -52.67900  76.37800  22.24800  1.000 69.92232  -1 867  GLU   A OE2 1 
ATOM   6878  N  N   . GLU   A 1 870  ? -56.27100  70.98400  23.65300  1.000 43.74590  ?  868  GLU   A N   1 
ATOM   6879  C  CA  . GLU   A 1 870  ? -56.25900  69.56100  23.33700  1.000 48.37016  ?  868  GLU   A CA  1 
ATOM   6880  C  C   . GLU   A 1 870  ? -57.61200  69.05800  22.84900  1.000 57.50967  ?  868  GLU   A C   1 
ATOM   6881  O  O   . GLU   A 1 870  ? -57.98100  67.90900  23.12400  1.000 63.48302  ?  868  GLU   A O   1 
ATOM   6882  C  CB  . GLU   A 1 870  ? -55.79000  68.76600  24.55600  1.000 53.11680  ?  868  GLU   A CB  1 
ATOM   6883  C  CG  . GLU   A 1 870  ? -54.54800  69.35400  25.21500  1.000 58.66647  ?  868  GLU   A CG  1 
ATOM   6884  C  CD  . GLU   A 1 870  ? -53.89000  68.40400  26.19600  1.000 54.22109  ?  868  GLU   A CD  1 
ATOM   6885  O  OE1 . GLU   A 1 870  ? -54.41800  67.29100  26.39300  1.000 58.87532  ?  868  GLU   A OE1 1 
ATOM   6886  O  OE2 . GLU   A 1 870  ? -52.84000  68.77100  26.76600  1.000 47.57974  -1 868  GLU   A OE2 1 
ATOM   6887  N  N   . SER   A 1 871  ? -58.36000  69.89100  22.12400  1.000 62.34384  ?  869  SER   A N   1 
ATOM   6888  C  CA  . SER   A 1 871  ? -59.68100  69.51300  21.64000  1.000 54.96352  ?  869  SER   A CA  1 
ATOM   6889  C  C   . SER   A 1 871  ? -60.03500  70.27400  20.37000  1.000 41.52902  ?  869  SER   A C   1 
ATOM   6890  O  O   . SER   A 1 871  ? -61.00300  69.92700  19.68500  1.000 53.84566  ?  869  SER   A O   1 
ATOM   6891  C  CB  . SER   A 1 871  ? -60.74100  69.77300  22.71200  1.000 50.52492  ?  869  SER   A CB  1 
ATOM   6892  O  OG  . SER   A 1 871  ? -60.97100  71.16300  22.86600  1.000 53.11997  ?  869  SER   A OG  1 
ATOM   6893  N  N   . VAL   A 1 872  ? -59.25900  71.31700  20.05600  1.000 32.50354  ?  870  VAL   A N   1 
ATOM   6894  C  CA  . VAL   A 1 872  ? -59.55700  72.15900  18.89900  1.000 36.38129  ?  870  VAL   A CA  1 
ATOM   6895  C  C   . VAL   A 1 872  ? -59.62600  71.32300  17.62700  1.000 38.69501  ?  870  VAL   A C   1 
ATOM   6896  O  O   . VAL   A 1 872  ? -60.54200  71.48200  16.80900  1.000 47.06620  ?  870  VAL   A O   1 
ATOM   6897  C  CB  . VAL   A 1 872  ? -58.51500  73.28800  18.77900  1.000 40.07664  ?  870  VAL   A CB  1 
ATOM   6898  C  CG1 . VAL   A 1 872  ? -58.56800  73.92400  17.39800  1.000 34.45416  ?  870  VAL   A CG1 1 
ATOM   6899  C  CG2 . VAL   A 1 872  ? -58.74600  74.33800  19.85000  1.000 36.72995  ?  870  VAL   A CG2 1 
ATOM   6900  N  N   . GLN   A 1 873  ? -58.67100  70.41000  17.44800  1.000 38.21518  ?  871  GLN   A N   1 
ATOM   6901  C  CA  . GLN   A 1 873  ? -58.63600  69.60500  16.23200  1.000 43.25817  ?  871  GLN   A CA  1 
ATOM   6902  C  C   . GLN   A 1 873  ? -59.82600  68.65500  16.15800  1.000 44.54519  ?  871  GLN   A C   1 
ATOM   6903  O  O   . GLN   A 1 873  ? -60.45300  68.51700  15.10100  1.000 47.41987  ?  871  GLN   A O   1 
ATOM   6904  C  CB  . GLN   A 1 873  ? -57.32400  68.82800  16.16400  1.000 45.61920  ?  871  GLN   A CB  1 
ATOM   6905  C  CG  . GLN   A 1 873  ? -56.09100  69.68700  16.36400  1.000 34.39055  ?  871  GLN   A CG  1 
ATOM   6906  C  CD  . GLN   A 1 873  ? -54.82000  68.87000  16.38600  1.000 44.91734  ?  871  GLN   A CD  1 
ATOM   6907  O  OE1 . GLN   A 1 873  ? -54.32600  68.50000  17.45100  1.000 52.23273  ?  871  GLN   A OE1 1 
ATOM   6908  N  NE2 . GLN   A 1 873  ? -54.28500  68.57400  15.20800  1.000 46.08457  ?  871  GLN   A NE2 1 
ATOM   6909  N  N   . SER   A 1 874  ? -60.15200  67.99200  17.27000  1.000 38.11920  ?  872  SER   A N   1 
ATOM   6910  C  CA  . SER   A 1 874  ? -61.26800  67.05400  17.26300  1.000 46.47156  ?  872  SER   A CA  1 
ATOM   6911  C  C   . SER   A 1 874  ? -62.60700  67.77600  17.19900  1.000 44.49779  ?  872  SER   A C   1 
ATOM   6912  O  O   . SER   A 1 874  ? -63.57800  67.22900  16.66600  1.000 53.19292  ?  872  SER   A O   1 
ATOM   6913  C  CB  . SER   A 1 874  ? -61.20100  66.15700  18.49500  1.000 51.95541  ?  872  SER   A CB  1 
ATOM   6914  O  OG  . SER   A 1 874  ? -59.87000  65.73400  18.73900  1.000 84.71399  ?  872  SER   A OG  1 
ATOM   6915  N  N   . LEU   A 1 875  ? -62.68200  68.99200  17.74500  1.000 39.20291  ?  873  LEU   A N   1 
ATOM   6916  C  CA  . LEU   A 1 875  ? -63.85100  69.83200  17.51200  1.000 30.00841  ?  873  LEU   A CA  1 
ATOM   6917  C  C   . LEU   A 1 875  ? -63.95400  70.23500  16.04900  1.000 40.75495  ?  873  LEU   A C   1 
ATOM   6918  O  O   . LEU   A 1 875  ? -65.06200  70.39700  15.52600  1.000 58.06821  ?  873  LEU   A O   1 
ATOM   6919  C  CB  . LEU   A 1 875  ? -63.79400  71.07700  18.39700  1.000 39.78337  ?  873  LEU   A CB  1 
ATOM   6920  C  CG  . LEU   A 1 875  ? -64.34200  70.97000  19.82000  1.000 39.47359  ?  873  LEU   A CG  1 
ATOM   6921  C  CD1 . LEU   A 1 875  ? -64.01200  72.22500  20.60700  1.000 41.93717  ?  873  LEU   A CD1 1 
ATOM   6922  C  CD2 . LEU   A 1 875  ? -65.83900  70.75000  19.78400  1.000 41.87838  ?  873  LEU   A CD2 1 
ATOM   6923  N  N   . LEU   A 1 876  ? -62.81300  70.39700  15.37900  1.000 43.11625  ?  874  LEU   A N   1 
ATOM   6924  C  CA  . LEU   A 1 876  ? -62.80100  70.76600  13.96900  1.000 36.32722  ?  874  LEU   A CA  1 
ATOM   6925  C  C   . LEU   A 1 876  ? -63.07400  69.56800  13.06900  1.000 46.02151  ?  874  LEU   A C   1 
ATOM   6926  O  O   . LEU   A 1 876  ? -63.74400  69.70300  12.03900  1.000 53.61964  ?  874  LEU   A O   1 
ATOM   6927  C  CB  . LEU   A 1 876  ? -61.45300  71.39100  13.60800  1.000 35.33687  ?  874  LEU   A CB  1 
ATOM   6928  C  CG  . LEU   A 1 876  ? -61.31100  71.81300  12.14700  1.000 43.45168  ?  874  LEU   A CG  1 
ATOM   6929  C  CD1 . LEU   A 1 876  ? -62.13300  73.05500  11.89600  1.000 46.31405  ?  874  LEU   A CD1 1 
ATOM   6930  C  CD2 . LEU   A 1 876  ? -59.86000  72.04100  11.77300  1.000 48.60774  ?  874  LEU   A CD2 1 
ATOM   6931  N  N   . ALA   A 1 877  ? -62.56500  68.39300  13.44700  1.000 46.25491  ?  875  ALA   A N   1 
ATOM   6932  C  CA  . ALA   A 1 877  ? -62.64500  67.22500  12.57600  1.000 37.41721  ?  875  ALA   A CA  1 
ATOM   6933  C  C   . ALA   A 1 877  ? -64.08400  66.81100  12.30300  1.000 39.40732  ?  875  ALA   A C   1 
ATOM   6934  O  O   . ALA   A 1 877  ? -64.38500  66.28500  11.22500  1.000 54.34826  ?  875  ALA   A O   1 
ATOM   6935  C  CB  . ALA   A 1 877  ? -61.86800  66.06200  13.19300  1.000 37.42868  ?  875  ALA   A CB  1 
ATOM   6936  N  N   . GLU   A 1 878  ? -64.98400  67.03400  13.25800  1.000 36.51374  ?  876  GLU   A N   1 
ATOM   6937  C  CA  . GLU   A 1 878  ? -66.37800  66.65800  13.06700  1.000 41.04447  ?  876  GLU   A CA  1 
ATOM   6938  C  C   . GLU   A 1 878  ? -67.13200  67.63600  12.17800  1.000 45.63775  ?  876  GLU   A C   1 
ATOM   6939  O  O   . GLU   A 1 878  ? -68.18200  67.27500  11.63600  1.000 56.64416  ?  876  GLU   A O   1 
ATOM   6940  C  CB  . GLU   A 1 878  ? -67.07900  66.54500  14.42000  1.000 50.25524  ?  876  GLU   A CB  1 
ATOM   6941  C  CG  . GLU   A 1 878  ? -67.11400  67.84600  15.19400  1.000 69.25943  ?  876  GLU   A CG  1 
ATOM   6942  C  CD  . GLU   A 1 878  ? -67.89600  67.72500  16.47900  1.000 91.04394  ?  876  GLU   A CD  1 
ATOM   6943  O  OE1 . GLU   A 1 878  ? -67.88000  66.63000  17.08000  1.000 83.37016  ?  876  GLU   A OE1 1 
ATOM   6944  O  OE2 . GLU   A 1 878  ? -68.53300  68.72100  16.88300  1.000 95.75895  -1 876  GLU   A OE2 1 
ATOM   6945  N  N   . GLN   A 1 879  ? -66.62700  68.85900  12.02000  1.000 43.78624  ?  877  GLN   A N   1 
ATOM   6946  C  CA  . GLN   A 1 879  ? -67.25700  69.84300  11.15000  1.000 46.65270  ?  877  GLN   A CA  1 
ATOM   6947  C  C   . GLN   A 1 879  ? -66.87800  69.66200  9.68700   1.000 48.45886  ?  877  GLN   A C   1 
ATOM   6948  O  O   . GLN   A 1 879  ? -67.43900  70.35000  8.82600   1.000 51.58078  ?  877  GLN   A O   1 
ATOM   6949  C  CB  . GLN   A 1 879  ? -66.88500  71.25700  11.60100  1.000 41.65868  ?  877  GLN   A CB  1 
ATOM   6950  C  CG  . GLN   A 1 879  ? -67.08100  71.51900  13.08800  1.000 47.40744  ?  877  GLN   A CG  1 
ATOM   6951  C  CD  . GLN   A 1 879  ? -68.46100  72.05300  13.42200  1.000 54.47240  ?  877  GLN   A CD  1 
ATOM   6952  O  OE1 . GLN   A 1 879  ? -69.41800  71.85400  12.67300  1.000 69.04111  ?  877  GLN   A OE1 1 
ATOM   6953  N  NE2 . GLN   A 1 879  ? -68.56700  72.74400  14.55100  1.000 68.28259  ?  877  GLN   A NE2 1 
ATOM   6954  N  N   . ILE   A 1 880  ? -65.94100  68.76500  9.38700   1.000 39.34910  ?  878  ILE   A N   1 
ATOM   6955  C  CA  . ILE   A 1 880  ? -65.53000  68.49400  8.01000   1.000 38.22826  ?  878  ILE   A CA  1 
ATOM   6956  C  C   . ILE   A 1 880  ? -66.44900  67.38500  7.50700   1.000 42.88650  ?  878  ILE   A C   1 
ATOM   6957  O  O   . ILE   A 1 880  ? -66.14700  66.19500  7.60700   1.000 36.60377  ?  878  ILE   A O   1 
ATOM   6958  C  CB  . ILE   A 1 880  ? -64.05300  68.12300  7.91600   1.000 28.36296  ?  878  ILE   A CB  1 
ATOM   6959  C  CG1 . ILE   A 1 880  ? -63.19500  69.24000  8.51400   1.000 40.22094  ?  878  ILE   A CG1 1 
ATOM   6960  C  CG2 . ILE   A 1 880  ? -63.65900  67.86300  6.47000   1.000 32.84366  ?  878  ILE   A CG2 1 
ATOM   6961  C  CD1 . ILE   A 1 880  ? -61.76900  68.83400  8.79600   1.000 41.31802  ?  878  ILE   A CD1 1 
ATOM   6962  N  N   . LYS   A 1 881  ? -67.59400  67.78700  6.97400   1.000 53.79053  ?  879  LYS   A N   1 
ATOM   6963  C  CA  . LYS   A 1 881  ? -68.61700  66.89400  6.45900   1.000 53.04905  ?  879  LYS   A CA  1 
ATOM   6964  C  C   . LYS   A 1 881  ? -68.74400  67.05400  4.94800   1.000 44.22091  ?  879  LYS   A C   1 
ATOM   6965  O  O   . LYS   A 1 881  ? -68.33600  68.07600  4.38600   1.000 40.10510  ?  879  LYS   A O   1 
ATOM   6966  C  CB  . LYS   A 1 881  ? -69.96600  67.18200  7.13400   1.000 46.74491  ?  879  LYS   A CB  1 
ATOM   6967  C  CG  . LYS   A 1 881  ? -70.06800  66.67100  8.56500   1.000 32.74061  ?  879  LYS   A CG  1 
ATOM   6968  C  CD  . LYS   A 1 881  ? -71.01300  67.53200  9.38900   1.000 44.52448  ?  879  LYS   A CD  1 
ATOM   6969  C  CE  . LYS   A 1 881  ? -71.29400  66.92000  10.75500  1.000 67.02441  ?  879  LYS   A CE  1 
ATOM   6970  N  NZ  . LYS   A 1 881  ? -72.31400  65.83600  10.68800  1.000 80.15630  ?  879  LYS   A NZ  1 
ATOM   6971  N  N   . PRO   A 1 882  ? -69.29100  66.05300  4.25500   1.000 38.85294  ?  880  PRO   A N   1 
ATOM   6972  C  CA  . PRO   A 1 882  ? -69.41400  66.14800  2.79500   1.000 33.69168  ?  880  PRO   A CA  1 
ATOM   6973  C  C   . PRO   A 1 882  ? -70.30600  67.30500  2.36700   1.000 35.50163  ?  880  PRO   A C   1 
ATOM   6974  O  O   . PRO   A 1 882  ? -71.11500  67.82900  3.13600   1.000 40.34321  ?  880  PRO   A O   1 
ATOM   6975  C  CB  . PRO   A 1 882  ? -70.03100  64.80000  2.40200   1.000 34.19151  ?  880  PRO   A CB  1 
ATOM   6976  C  CG  . PRO   A 1 882  ? -69.66100  63.88100  3.51200   1.000 41.08270  ?  880  PRO   A CG  1 
ATOM   6977  C  CD  . PRO   A 1 882  ? -69.67800  64.72100  4.75200   1.000 45.98003  ?  880  PRO   A CD  1 
ATOM   6978  N  N   . PHE   A 1 883  ? -70.14200  67.70100  1.10800   1.000 46.84268  ?  881  PHE   A N   1 
ATOM   6979  C  CA  . PHE   A 1 883  ? -70.92200  68.76900  0.50100   1.000 32.46050  ?  881  PHE   A CA  1 
ATOM   6980  C  C   . PHE   A 1 883  ? -71.86000  68.20300  -0.55500  1.000 32.49193  ?  881  PHE   A C   1 
ATOM   6981  O  O   . PHE   A 1 883  ? -71.51100  67.25700  -1.26800  1.000 43.52007  ?  881  PHE   A O   1 
ATOM   6982  C  CB  . PHE   A 1 883  ? -70.01700  69.82000  -0.14700  1.000 29.61161  ?  881  PHE   A CB  1 
ATOM   6983  C  CG  . PHE   A 1 883  ? -69.56000  70.89700  0.79100   1.000 43.32267  ?  881  PHE   A CG  1 
ATOM   6984  C  CD1 . PHE   A 1 883  ? -70.42700  71.90100  1.18700   1.000 46.94407  ?  881  PHE   A CD1 1 
ATOM   6985  C  CD2 . PHE   A 1 883  ? -68.25600  70.92100  1.25900   1.000 43.16913  ?  881  PHE   A CD2 1 
ATOM   6986  C  CE1 . PHE   A 1 883  ? -70.00900  72.90200  2.04300   1.000 41.17007  ?  881  PHE   A CE1 1 
ATOM   6987  C  CE2 . PHE   A 1 883  ? -67.83100  71.91900  2.11600   1.000 47.71743  ?  881  PHE   A CE2 1 
ATOM   6988  C  CZ  . PHE   A 1 883  ? -68.70900  72.91100  2.50800   1.000 49.78171  ?  881  PHE   A CZ  1 
ATOM   6989  N  N   . ASP   A 1 884  ? -73.05100  68.78900  -0.65100  1.000 45.48381  ?  882  ASP   A N   1 
ATOM   6990  C  CA  . ASP   A 1 884  ? -73.95900  68.54700  -1.76500  1.000 50.65714  ?  882  ASP   A CA  1 
ATOM   6991  C  C   . ASP   A 1 884  ? -73.76600  69.68700  -2.75500  1.000 50.36936  ?  882  ASP   A C   1 
ATOM   6992  O  O   . ASP   A 1 884  ? -74.14300  70.83100  -2.47700  1.000 47.94317  ?  882  ASP   A O   1 
ATOM   6993  C  CB  . ASP   A 1 884  ? -75.40900  68.46000  -1.29700  1.000 58.91874  ?  882  ASP   A CB  1 
ATOM   6994  C  CG  . ASP   A 1 884  ? -76.35900  68.06300  -2.41300  1.000 65.76068  ?  882  ASP   A CG  1 
ATOM   6995  O  OD1 . ASP   A 1 884  ? -75.88800  67.81600  -3.54400  1.000 64.88772  ?  882  ASP   A OD1 1 
ATOM   6996  O  OD2 . ASP   A 1 884  ? -77.58000  67.99300  -2.15900  1.000 74.86684  -1 882  ASP   A OD2 1 
ATOM   6997  N  N   . LEU   A 1 885  ? -73.18000  69.37100  -3.91200  1.000 41.35382  ?  883  LEU   A N   1 
ATOM   6998  C  CA  . LEU   A 1 885  ? -72.81000  70.40700  -4.86900  1.000 39.74028  ?  883  LEU   A CA  1 
ATOM   6999  C  C   . LEU   A 1 885  ? -74.02500  71.10000  -5.46400  1.000 49.29061  ?  883  LEU   A C   1 
ATOM   7000  O  O   . LEU   A 1 885  ? -73.86600  72.05000  -6.23900  1.000 63.67032  ?  883  LEU   A O   1 
ATOM   7001  C  CB  . LEU   A 1 885  ? -71.94500  69.80800  -5.97900  1.000 38.04172  ?  883  LEU   A CB  1 
ATOM   7002  C  CG  . LEU   A 1 885  ? -70.64500  69.14900  -5.50400  1.000 40.02617  ?  883  LEU   A CG  1 
ATOM   7003  C  CD1 . LEU   A 1 885  ? -69.76900  68.75000  -6.68200  1.000 53.80483  ?  883  LEU   A CD1 1 
ATOM   7004  C  CD2 . LEU   A 1 885  ? -69.88800  70.07000  -4.55900  1.000 40.11121  ?  883  LEU   A CD2 1 
ATOM   7005  N  N   . ALA   A 1 886  ? -75.22700  70.65900  -5.11700  1.000 50.58600  ?  884  ALA   A N   1 
ATOM   7006  C  CA  . ALA   A 1 886  ? -76.44700  71.31300  -5.55500  1.000 47.70752  ?  884  ALA   A CA  1 
ATOM   7007  C  C   . ALA   A 1 886  ? -76.96300  72.32400  -4.54300  1.000 39.91475  ?  884  ALA   A C   1 
ATOM   7008  O  O   . ALA   A 1 886  ? -77.98300  72.96900  -4.80100  1.000 55.37576  ?  884  ALA   A O   1 
ATOM   7009  C  CB  . ALA   A 1 886  ? -77.52100  70.26300  -5.84800  1.000 36.88594  ?  884  ALA   A CB  1 
ATOM   7010  N  N   . LYS   A 1 887  ? -76.28400  72.48800  -3.40900  1.000 40.81305  ?  885  LYS   A N   1 
ATOM   7011  C  CA  . LYS   A 1 887  ? -76.72100  73.39200  -2.35200  1.000 37.31029  ?  885  LYS   A CA  1 
ATOM   7012  C  C   . LYS   A 1 887  ? -75.60700  74.37500  -2.01900  1.000 44.67298  ?  885  LYS   A C   1 
ATOM   7013  O  O   . LYS   A 1 887  ? -74.44500  73.98000  -1.87700  1.000 54.39317  ?  885  LYS   A O   1 
ATOM   7014  C  CB  . LYS   A 1 887  ? -77.13900  72.61100  -1.10200  1.000 39.49263  ?  885  LYS   A CB  1 
ATOM   7015  C  CG  . LYS   A 1 887  ? -78.46100  71.87400  -1.25000  1.000 59.21015  ?  885  LYS   A CG  1 
ATOM   7016  C  CD  . LYS   A 1 887  ? -78.78100  71.03900  -0.02100  1.000 55.38307  ?  885  LYS   A CD  1 
ATOM   7017  C  CE  . LYS   A 1 887  ? -80.16100  70.41000  -0.14000  1.000 52.37601  ?  885  LYS   A CE  1 
ATOM   7018  N  NZ  . LYS   A 1 887  ? -80.39100  69.34600  0.87600   1.000 68.44492  ?  885  LYS   A NZ  1 
ATOM   7019  N  N   . ALA   A 1 888  ? -75.97000  75.65500  -1.90800  1.000 40.30721  ?  886  ALA   A N   1 
ATOM   7020  C  CA  . ALA   A 1 888  ? -75.11100  76.76500  -1.53300  1.000 33.67481  ?  886  ALA   A CA  1 
ATOM   7021  C  C   . ALA   A 1 888  ? -75.19200  76.99800  -0.02900  1.000 47.62368  ?  886  ALA   A C   1 
ATOM   7022  O  O   . ALA   A 1 888  ? -76.16000  76.58100  0.61700   1.000 71.73219  ?  886  ALA   A O   1 
ATOM   7023  C  CB  . ALA   A 1 888  ? -75.52700  78.01900  -2.29800  1.000 35.52457  ?  886  ALA   A CB  1 
ATOM   7024  N  N   . PRO   A 1 889  ? -74.20700  77.68800  0.57700   1.000 59.24051  ?  887  PRO   A N   1 
ATOM   7025  C  CA  . PRO   A 1 889  ? -73.10300  78.47100  0.00100   1.000 45.56381  ?  887  PRO   A CA  1 
ATOM   7026  C  C   . PRO   A 1 889  ? -71.84600  77.68500  -0.36300  1.000 45.11685  ?  887  PRO   A C   1 
ATOM   7027  O  O   . PRO   A 1 889  ? -70.89100  78.29600  -0.83400  1.000 74.23516  ?  887  PRO   A O   1 
ATOM   7028  C  CB  . PRO   A 1 889  ? -72.79600  79.49600  1.11300   1.000 42.36237  ?  887  PRO   A CB  1 
ATOM   7029  C  CG  . PRO   A 1 889  ? -73.57700  79.04800  2.35500   1.000 39.82709  ?  887  PRO   A CG  1 
ATOM   7030  C  CD  . PRO   A 1 889  ? -74.12000  77.68400  2.04300   1.000 62.78738  ?  887  PRO   A CD  1 
ATOM   7031  N  N   . LEU   A 1 890  ? -71.80300  76.36500  -0.16600  1.000 32.57643  ?  888  LEU   A N   1 
ATOM   7032  C  CA  . LEU   A 1 890  ? -70.61400  75.55400  -0.45800  1.000 50.55668  ?  888  LEU   A CA  1 
ATOM   7033  C  C   . LEU   A 1 890  ? -69.39800  75.99800  0.35400   1.000 50.32284  ?  888  LEU   A C   1 
ATOM   7034  O  O   . LEU   A 1 890  ? -68.25600  75.84800  -0.08900  1.000 24.52900  ?  888  LEU   A O   1 
ATOM   7035  C  CB  . LEU   A 1 890  ? -70.27300  75.56000  -1.95300  1.000 29.28138  ?  888  LEU   A CB  1 
ATOM   7036  C  CG  . LEU   A 1 890  ? -70.90500  74.49100  -2.84400  1.000 27.74770  ?  888  LEU   A CG  1 
ATOM   7037  C  CD1 . LEU   A 1 890  ? -70.19700  74.45600  -4.18600  1.000 31.28446  ?  888  LEU   A CD1 1 
ATOM   7038  C  CD2 . LEU   A 1 890  ? -70.85800  73.12600  -2.17800  1.000 31.29829  ?  888  LEU   A CD2 1 
ATOM   7039  N  N   . LEU   A 1 891  ? -69.63100  76.54800  1.54500   1.000 52.79132  ?  889  LEU   A N   1 
ATOM   7040  C  CA  . LEU   A 1 891  ? -68.53800  76.93000  2.43700   1.000 38.30257  ?  889  LEU   A CA  1 
ATOM   7041  C  C   . LEU   A 1 891  ? -69.11000  77.06800  3.84100   1.000 52.85764  ?  889  LEU   A C   1 
ATOM   7042  O  O   . LEU   A 1 891  ? -69.90000  77.98100  4.09800   1.000 56.07148  ?  889  LEU   A O   1 
ATOM   7043  C  CB  . LEU   A 1 891  ? -67.87900  78.22800  1.97900   1.000 35.99164  ?  889  LEU   A CB  1 
ATOM   7044  C  CG  . LEU   A 1 891  ? -66.74200  78.75700  2.86000   1.000 35.49064  ?  889  LEU   A CG  1 
ATOM   7045  C  CD1 . LEU   A 1 891  ? -65.52100  79.09500  2.02200   1.000 45.94519  ?  889  LEU   A CD1 1 
ATOM   7046  C  CD2 . LEU   A 1 891  ? -67.19200  79.97400  3.65100   1.000 27.47510  ?  889  LEU   A CD2 1 
ATOM   7047  N  N   . ARG   A 1 892  ? -68.71900  76.16600  4.73500   1.000 50.42777  ?  890  ARG   A N   1 
ATOM   7048  C  CA  . ARG   A 1 892  ? -69.13200  76.21300  6.13000   1.000 34.43376  ?  890  ARG   A CA  1 
ATOM   7049  C  C   . ARG   A 1 892  ? -67.98600  76.75300  6.97400   1.000 45.49513  ?  890  ARG   A C   1 
ATOM   7050  O  O   . ARG   A 1 892  ? -66.81800  76.46100  6.70600   1.000 49.44803  ?  890  ARG   A O   1 
ATOM   7051  C  CB  . ARG   A 1 892  ? -69.54700  74.82600  6.62200   1.000 24.79993  ?  890  ARG   A CB  1 
ATOM   7052  C  CG  . ARG   A 1 892  ? -70.45300  74.08600  5.65400   1.000 25.29985  ?  890  ARG   A CG  1 
ATOM   7053  C  CD  . ARG   A 1 892  ? -70.93200  72.76800  6.23300   1.000 37.18434  ?  890  ARG   A CD  1 
ATOM   7054  N  NE  . ARG   A 1 892  ? -71.67200  71.98300  5.25300   1.000 44.32371  ?  890  ARG   A NE  1 
ATOM   7055  C  CZ  . ARG   A 1 892  ? -71.19400  70.91000  4.63800   1.000 54.03245  ?  890  ARG   A CZ  1 
ATOM   7056  N  NH1 . ARG   A 1 892  ? -69.98400  70.44400  4.90100   1.000 54.28673  ?  890  ARG   A NH1 1 
ATOM   7057  N  NH2 . ARG   A 1 892  ? -71.95100  70.28500  3.74000   1.000 50.03255  ?  890  ARG   A NH2 1 
ATOM   7058  N  N   . ALA   A 1 893  ? -68.32300  77.54600  7.99000   1.000 45.70507  ?  891  ALA   A N   1 
ATOM   7059  C  CA  . ALA   A 1 893  ? -67.31900  78.24100  8.78300   1.000 41.79863  ?  891  ALA   A CA  1 
ATOM   7060  C  C   . ALA   A 1 893  ? -67.69100  78.17100  10.25900  1.000 42.06165  ?  891  ALA   A C   1 
ATOM   7061  O  O   . ALA   A 1 893  ? -68.66200  77.51600  10.64900  1.000 49.23294  ?  891  ALA   A O   1 
ATOM   7062  C  CB  . ALA   A 1 893  ? -67.16400  79.69500  8.32100   1.000 32.83960  ?  891  ALA   A CB  1 
ATOM   7063  N  N   . GLY   A 1 894  ? -66.90500  78.85500  11.07700  1.000 45.83490  ?  892  GLY   A N   1 
ATOM   7064  C  CA  . GLY   A 1 894  ? -67.13000  78.88800  12.50800  1.000 49.46673  ?  892  GLY   A CA  1 
ATOM   7065  C  C   . GLY   A 1 894  ? -65.89300  79.34800  13.24200  1.000 54.79657  ?  892  GLY   A C   1 
ATOM   7066  O  O   . GLY   A 1 894  ? -64.81100  79.48700  12.67000  1.000 50.82791  ?  892  GLY   A O   1 
ATOM   7067  N  N   . VAL   A 1 895  ? -66.06900  79.58600  14.54100  1.000 46.42065  ?  893  VAL   A N   1 
ATOM   7068  C  CA  . VAL   A 1 895  ? -65.00100  80.07800  15.40500  1.000 43.86816  ?  893  VAL   A CA  1 
ATOM   7069  C  C   . VAL   A 1 895  ? -64.97100  79.23800  16.67400  1.000 48.76548  ?  893  VAL   A C   1 
ATOM   7070  O  O   . VAL   A 1 895  ? -65.97600  79.15500  17.39200  1.000 55.04996  ?  893  VAL   A O   1 
ATOM   7071  C  CB  . VAL   A 1 895  ? -65.17400  81.56700  15.74900  1.000 44.34791  ?  893  VAL   A CB  1 
ATOM   7072  C  CG1 . VAL   A 1 895  ? -64.27600  81.94900  16.91600  1.000 47.12758  ?  893  VAL   A CG1 1 
ATOM   7073  C  CG2 . VAL   A 1 895  ? -64.86100  82.43000  14.53600  1.000 40.41320  ?  893  VAL   A CG2 1 
ATOM   7074  N  N   . ILE   A 1 896  ? -63.82400  78.62400  16.95200  1.000 34.58246  ?  894  ILE   A N   1 
ATOM   7075  C  CA  . ILE   A 1 896  ? -63.60000  77.86800  18.17700  1.000 41.91157  ?  894  ILE   A CA  1 
ATOM   7076  C  C   . ILE   A 1 896  ? -62.81900  78.76500  19.12600  1.000 50.55520  ?  894  ILE   A C   1 
ATOM   7077  O  O   . ILE   A 1 896  ? -61.66500  79.11500  18.85600  1.000 40.54536  ?  894  ILE   A O   1 
ATOM   7078  C  CB  . ILE   A 1 896  ? -62.84900  76.55600  17.90600  1.000 34.08513  ?  894  ILE   A CB  1 
ATOM   7079  C  CG1 . ILE   A 1 896  ? -63.53700  75.76500  16.79400  1.000 40.71618  ?  894  ILE   A CG1 1 
ATOM   7080  C  CG2 . ILE   A 1 896  ? -62.75900  75.72200  19.17200  1.000 38.33294  ?  894  ILE   A CG2 1 
ATOM   7081  C  CD1 . ILE   A 1 896  ? -62.76100  74.54300  16.35400  1.000 36.24161  ?  894  ILE   A CD1 1 
ATOM   7082  N  N   . GLU   A 1 897  ? -63.43800  79.14100  20.24200  1.000 48.60013  ?  895  GLU   A N   1 
ATOM   7083  C  CA  . GLU   A 1 897  ? -62.83600  80.06500  21.19500  1.000 44.97299  ?  895  GLU   A CA  1 
ATOM   7084  C  C   . GLU   A 1 897  ? -62.24600  79.28400  22.36300  1.000 53.11940  ?  895  GLU   A C   1 
ATOM   7085  O  O   . GLU   A 1 897  ? -62.96600  78.56200  23.06200  1.000 45.05737  ?  895  GLU   A O   1 
ATOM   7086  C  CB  . GLU   A 1 897  ? -63.86300  81.07900  21.69600  1.000 41.48861  ?  895  GLU   A CB  1 
ATOM   7087  C  CG  . GLU   A 1 897  ? -63.30200  82.07700  22.69600  1.000 46.82213  ?  895  GLU   A CG  1 
ATOM   7088  C  CD  . GLU   A 1 897  ? -64.32300  83.11200  23.12700  1.000 67.39100  ?  895  GLU   A CD  1 
ATOM   7089  O  OE1 . GLU   A 1 897  ? -65.43600  83.12400  22.56000  1.000 79.56156  ?  895  GLU   A OE1 1 
ATOM   7090  O  OE2 . GLU   A 1 897  ? -64.01200  83.91300  24.03300  1.000 62.55280  -1 895  GLU   A OE2 1 
ATOM   7091  N  N   . THR   A 1 898  ? -60.94000  79.43100  22.56800  1.000 42.84390  ?  896  THR   A N   1 
ATOM   7092  C  CA  . THR   A 1 898  ? -60.25800  78.88600  23.72800  1.000 40.48248  ?  896  THR   A CA  1 
ATOM   7093  C  C   . THR   A 1 898  ? -59.96000  80.01900  24.70700  1.000 48.28948  ?  896  THR   A C   1 
ATOM   7094  O  O   . THR   A 1 898  ? -60.40400  81.15800  24.53000  1.000 52.67083  ?  896  THR   A O   1 
ATOM   7095  C  CB  . THR   A 1 898  ? -58.98100  78.15200  23.31100  1.000 44.40264  ?  896  THR   A CB  1 
ATOM   7096  O  OG1 . THR   A 1 898  ? -57.94100  79.10400  23.05600  1.000 56.87526  ?  896  THR   A OG1 1 
ATOM   7097  C  CG2 . THR   A 1 898  ? -59.22600  77.33100  22.05600  1.000 43.03130  ?  896  THR   A CG2 1 
ATOM   7098  N  N   . ALA   A 1 899  ? -59.19600  79.71300  25.75300  1.000 47.60532  ?  897  ALA   A N   1 
ATOM   7099  C  CA  . ALA   A 1 899  ? -58.84800  80.72500  26.74000  1.000 49.75741  ?  897  ALA   A CA  1 
ATOM   7100  C  C   . ALA   A 1 899  ? -57.78100  81.69300  26.24700  1.000 53.12259  ?  897  ALA   A C   1 
ATOM   7101  O  O   . ALA   A 1 899  ? -57.56400  82.72700  26.88600  1.000 59.52301  ?  897  ALA   A O   1 
ATOM   7102  C  CB  . ALA   A 1 899  ? -58.38000  80.05900  28.03600  1.000 47.47415  ?  897  ALA   A CB  1 
ATOM   7103  N  N   . ASP   A 1 900  ? -57.11900  81.39400  25.12900  1.000 59.87052  ?  898  ASP   A N   1 
ATOM   7104  C  CA  . ASP   A 1 900  ? -56.02600  82.22100  24.64200  1.000 54.12780  ?  898  ASP   A CA  1 
ATOM   7105  C  C   . ASP   A 1 900  ? -56.13300  82.59600  23.17000  1.000 59.38703  ?  898  ASP   A C   1 
ATOM   7106  O  O   . ASP   A 1 900  ? -55.34000  83.42800  22.71400  1.000 76.52742  ?  898  ASP   A O   1 
ATOM   7107  C  CB  . ASP   A 1 900  ? -54.68100  81.51900  24.88500  1.000 54.05503  ?  898  ASP   A CB  1 
ATOM   7108  C  CG  . ASP   A 1 900  ? -54.72600  80.04200  24.54300  1.000 84.14683  ?  898  ASP   A CG  1 
ATOM   7109  O  OD1 . ASP   A 1 900  ? -55.47700  79.30100  25.21400  1.000 85.57081  ?  898  ASP   A OD1 1 
ATOM   7110  O  OD2 . ASP   A 1 900  ? -54.02500  79.62500  23.59600  1.000 89.56231  -1 898  ASP   A OD2 1 
ATOM   7111  N  N   . LYS   A 1 901  ? -57.08600  82.04400  22.42100  1.000 47.19099  ?  899  LYS   A N   1 
ATOM   7112  C  CA  . LYS   A 1 901  ? -57.18300  82.34700  20.99800  1.000 54.43998  ?  899  LYS   A CA  1 
ATOM   7113  C  C   . LYS   A 1 901  ? -58.60600  82.09500  20.51500  1.000 56.55926  ?  899  LYS   A C   1 
ATOM   7114  O  O   . LYS   A 1 901  ? -59.42000  81.47300  21.20200  1.000 59.51415  ?  899  LYS   A O   1 
ATOM   7115  C  CB  . LYS   A 1 901  ? -56.17900  81.51900  20.19200  1.000 53.78591  ?  899  LYS   A CB  1 
ATOM   7116  C  CG  . LYS   A 1 901  ? -56.39100  80.02200  20.31100  1.000 41.21219  ?  899  LYS   A CG  1 
ATOM   7117  C  CD  . LYS   A 1 901  ? -55.10100  79.25800  20.06800  1.000 47.89245  ?  899  LYS   A CD  1 
ATOM   7118  C  CE  . LYS   A 1 901  ? -55.37100  77.93800  19.36300  1.000 45.72563  ?  899  LYS   A CE  1 
ATOM   7119  N  NZ  . LYS   A 1 901  ? -54.55600  76.81700  19.91000  1.000 61.01881  ?  899  LYS   A NZ  1 
ATOM   7120  N  N   . LYS   A 1 902  ? -58.89300  82.59900  19.31300  1.000 48.32758  ?  900  LYS   A N   1 
ATOM   7121  C  CA  . LYS   A 1 902  ? -60.15100  82.35700  18.61000  1.000 48.63931  ?  900  LYS   A CA  1 
ATOM   7122  C  C   . LYS   A 1 902  ? -59.81800  81.76300  17.24600  1.000 50.70035  ?  900  LYS   A C   1 
ATOM   7123  O  O   . LYS   A 1 902  ? -59.32500  82.47000  16.36100  1.000 48.36723  ?  900  LYS   A O   1 
ATOM   7124  C  CB  . LYS   A 1 902  ? -60.96600  83.64200  18.46000  1.000 40.39097  ?  900  LYS   A CB  1 
ATOM   7125  C  CG  . LYS   A 1 902  ? -61.60100  84.14600  19.74400  1.000 54.26005  ?  900  LYS   A CG  1 
ATOM   7126  C  CD  . LYS   A 1 902  ? -62.53400  85.31400  19.46100  1.000 57.45662  ?  900  LYS   A CD  1 
ATOM   7127  C  CE  . LYS   A 1 902  ? -63.32600  85.71500  20.69400  1.000 69.80195  ?  900  LYS   A CE  1 
ATOM   7128  N  NZ  . LYS   A 1 902  ? -64.37200  86.72800  20.37500  1.000 75.21861  ?  900  LYS   A NZ  1 
ATOM   7129  N  N   . VAL   A 1 903  ? -60.09300  80.47200  17.07600  1.000 53.05039  ?  901  VAL   A N   1 
ATOM   7130  C  CA  . VAL   A 1 903  ? -59.70200  79.73900  15.87500  1.000 35.09595  ?  901  VAL   A CA  1 
ATOM   7131  C  C   . VAL   A 1 903  ? -60.83800  79.85300  14.86400  1.000 32.69802  ?  901  VAL   A C   1 
ATOM   7132  O  O   . VAL   A 1 903  ? -61.86600  79.18500  14.98500  1.000 34.68662  ?  901  VAL   A O   1 
ATOM   7133  C  CB  . VAL   A 1 903  ? -59.37400  78.27800  16.18800  1.000 38.46402  ?  901  VAL   A CB  1 
ATOM   7134  C  CG1 . VAL   A 1 903  ? -58.82500  77.58000  14.95200  1.000 35.60694  ?  901  VAL   A CG1 1 
ATOM   7135  C  CG2 . VAL   A 1 903  ? -58.39100  78.19200  17.34100  1.000 53.84942  ?  901  VAL   A CG2 1 
ATOM   7136  N  N   . LEU   A 1 904  ? -60.65100  80.70100  13.85700  1.000 34.86398  ?  902  LEU   A N   1 
ATOM   7137  C  CA  . LEU   A 1 904  ? -61.57900  80.75300  12.73700  1.000 38.20201  ?  902  LEU   A CA  1 
ATOM   7138  C  C   . LEU   A 1 904  ? -61.29000  79.60100  11.78600  1.000 39.38743  ?  902  LEU   A C   1 
ATOM   7139  O  O   . LEU   A 1 904  ? -60.14500  79.39900  11.37100  1.000 37.87884  ?  902  LEU   A O   1 
ATOM   7140  C  CB  . LEU   A 1 904  ? -61.47000  82.08300  11.99300  1.000 36.67323  ?  902  LEU   A CB  1 
ATOM   7141  C  CG  . LEU   A 1 904  ? -62.15700  82.08900  10.62200  1.000 39.53396  ?  902  LEU   A CG  1 
ATOM   7142  C  CD1 . LEU   A 1 904  ? -63.67100  81.94000  10.75900  1.000 33.82207  ?  902  LEU   A CD1 1 
ATOM   7143  C  CD2 . LEU   A 1 904  ? -61.80100  83.33500  9.82300   1.000 27.14643  ?  902  LEU   A CD2 1 
ATOM   7144  N  N   . TRP   A 1 905  ? -62.32800  78.84500  11.44300  1.000 44.79258  ?  903  TRP   A N   1 
ATOM   7145  C  CA  . TRP   A 1 905  ? -62.20300  77.73100  10.52000  1.000 30.21231  ?  903  TRP   A CA  1 
ATOM   7146  C  C   . TRP   A 1 905  ? -63.22500  77.88300  9.40600   1.000 40.21701  ?  903  TRP   A C   1 
ATOM   7147  O  O   . TRP   A 1 905  ? -64.30000  78.45200  9.60500   1.000 55.10500  ?  903  TRP   A O   1 
ATOM   7148  C  CB  . TRP   A 1 905  ? -62.40400  76.38400  11.23100  1.000 28.25431  ?  903  TRP   A CB  1 
ATOM   7149  C  CG  . TRP   A 1 905  ? -63.83300  76.08800  11.60500  1.000 40.94629  ?  903  TRP   A CG  1 
ATOM   7150  C  CD1 . TRP   A 1 905  ? -64.45100  76.39000  12.78300  1.000 43.52461  ?  903  TRP   A CD1 1 
ATOM   7151  C  CD2 . TRP   A 1 905  ? -64.81600  75.42300  10.79800  1.000 40.52934  ?  903  TRP   A CD2 1 
ATOM   7152  N  NE1 . TRP   A 1 905  ? -65.75600  75.96000  12.75800  1.000 56.18497  ?  903  TRP   A NE1 1 
ATOM   7153  C  CE2 . TRP   A 1 905  ? -66.00500  75.36500  11.55000  1.000 40.91507  ?  903  TRP   A CE2 1 
ATOM   7154  C  CE3 . TRP   A 1 905  ? -64.80500  74.87600  9.51100   1.000 45.30905  ?  903  TRP   A CE3 1 
ATOM   7155  C  CZ2 . TRP   A 1 905  ? -67.17200  74.78200  11.05800  1.000 51.64365  ?  903  TRP   A CZ2 1 
ATOM   7156  C  CZ3 . TRP   A 1 905  ? -65.96500  74.29900  9.02400   1.000 51.72591  ?  903  TRP   A CZ3 1 
ATOM   7157  C  CH2 . TRP   A 1 905  ? -67.13200  74.25700  9.79600   1.000 58.38338  ?  903  TRP   A CH2 1 
ATOM   7158  N  N   . PHE   A 1 906  ? -62.87500  77.38200  8.22500   1.000 34.26285  ?  904  PHE   A N   1 
ATOM   7159  C  CA  . PHE   A 1 906  ? -63.84800  77.26200  7.15200   1.000 37.64570  ?  904  PHE   A CA  1 
ATOM   7160  C  C   . PHE   A 1 906  ? -63.50200  76.04600  6.30800   1.000 49.50855  ?  904  PHE   A C   1 
ATOM   7161  O  O   . PHE   A 1 906  ? -62.33600  75.65800  6.19400   1.000 40.20839  ?  904  PHE   A O   1 
ATOM   7162  C  CB  . PHE   A 1 906  ? -63.92900  78.52800  6.28500   1.000 36.80582  ?  904  PHE   A CB  1 
ATOM   7163  C  CG  . PHE   A 1 906  ? -62.69600  78.80300  5.47300   1.000 44.34567  ?  904  PHE   A CG  1 
ATOM   7164  C  CD1 . PHE   A 1 906  ? -62.50700  78.19900  4.23900   1.000 56.95003  ?  904  PHE   A CD1 1 
ATOM   7165  C  CD2 . PHE   A 1 906  ? -61.74500  79.69500  5.92800   1.000 36.14212  ?  904  PHE   A CD2 1 
ATOM   7166  C  CE1 . PHE   A 1 906  ? -61.38000  78.45900  3.49200   1.000 51.05628  ?  904  PHE   A CE1 1 
ATOM   7167  C  CE2 . PHE   A 1 906  ? -60.62100  79.96200  5.18200   1.000 46.34957  ?  904  PHE   A CE2 1 
ATOM   7168  C  CZ  . PHE   A 1 906  ? -60.43600  79.34600  3.96100   1.000 44.54176  ?  904  PHE   A CZ  1 
ATOM   7169  N  N   . ASP   A 1 907  ? -64.53700  75.44400  5.72600   1.000 39.47053  ?  905  ASP   A N   1 
ATOM   7170  C  CA  . ASP   A 1 907  ? -64.39800  74.27600  4.86800   1.000 41.05437  ?  905  ASP   A CA  1 
ATOM   7171  C  C   . ASP   A 1 907  ? -65.12400  74.55600  3.56300   1.000 53.62721  ?  905  ASP   A C   1 
ATOM   7172  O  O   . ASP   A 1 907  ? -66.32300  74.85300  3.57000   1.000 44.46913  ?  905  ASP   A O   1 
ATOM   7173  C  CB  . ASP   A 1 907  ? -64.95700  73.02100  5.54700   1.000 45.51504  ?  905  ASP   A CB  1 
ATOM   7174  C  CG  . ASP   A 1 907  ? -64.91700  71.79900  4.64500   1.000 52.39680  ?  905  ASP   A CG  1 
ATOM   7175  O  OD1 . ASP   A 1 907  ? -63.82700  71.47100  4.13100   1.000 69.68753  ?  905  ASP   A OD1 1 
ATOM   7176  O  OD2 . ASP   A 1 907  ? -65.97300  71.16000  4.45900   1.000 60.12470  -1 905  ASP   A OD2 1 
ATOM   7177  N  N   . SER   A 1 908  ? -64.39900  74.47600  2.45400   1.000 45.61309  ?  906  SER   A N   1 
ATOM   7178  C  CA  . SER   A 1 908  ? -64.94900  74.70200  1.12600   1.000 48.92138  ?  906  SER   A CA  1 
ATOM   7179  C  C   . SER   A 1 908  ? -64.72900  73.46000  0.26800   1.000 50.90802  ?  906  SER   A C   1 
ATOM   7180  O  O   . SER   A 1 908  ? -64.17900  72.45300  0.71900   1.000 51.97642  ?  906  SER   A O   1 
ATOM   7181  C  CB  . SER   A 1 908  ? -64.31800  75.93800  0.47800   1.000 46.29624  ?  906  SER   A CB  1 
ATOM   7182  O  OG  . SER   A 1 908  ? -64.99200  76.29000  -0.71800  1.000 39.23569  ?  906  SER   A OG  1 
ATOM   7183  N  N   . HIS   A 1 909  ? -65.17000  73.54100  -0.98200  1.000 48.43908  ?  907  HIS   A N   1 
ATOM   7184  C  CA  . HIS   A 1 909  ? -64.99400  72.47000  -1.94800  1.000 46.33384  ?  907  HIS   A CA  1 
ATOM   7185  C  C   . HIS   A 1 909  ? -64.05500  72.93400  -3.05300  1.000 50.20078  ?  907  HIS   A C   1 
ATOM   7186  O  O   . HIS   A 1 909  ? -64.05500  74.10800  -3.43500  1.000 45.69742  ?  907  HIS   A O   1 
ATOM   7187  C  CB  . HIS   A 1 909  ? -66.33800  72.04100  -2.54400  1.000 33.73688  ?  907  HIS   A CB  1 
ATOM   7188  C  CG  . HIS   A 1 909  ? -66.30300  70.70800  -3.22400  1.000 34.09547  ?  907  HIS   A CG  1 
ATOM   7189  N  ND1 . HIS   A 1 909  ? -65.77000  70.52700  -4.48200  1.000 37.65496  ?  907  HIS   A ND1 1 
ATOM   7190  C  CD2 . HIS   A 1 909  ? -66.74100  69.49200  -2.82300  1.000 33.64970  ?  907  HIS   A CD2 1 
ATOM   7191  C  CE1 . HIS   A 1 909  ? -65.87800  69.25600  -4.82500  1.000 37.44717  ?  907  HIS   A CE1 1 
ATOM   7192  N  NE2 . HIS   A 1 909  ? -66.46400  68.60600  -3.83600  1.000 39.65622  ?  907  HIS   A NE2 1 
ATOM   7193  N  N   . HIS   A 1 910  ? -63.25200  72.00300  -3.56800  1.000 44.10584  ?  908  HIS   A N   1 
ATOM   7194  C  CA  . HIS   A 1 910  ? -62.28100  72.38100  -4.58700  1.000 42.23848  ?  908  HIS   A CA  1 
ATOM   7195  C  C   . HIS   A 1 910  ? -62.92800  72.76000  -5.91100  1.000 53.01344  ?  908  HIS   A C   1 
ATOM   7196  O  O   . HIS   A 1 910  ? -62.21300  73.16000  -6.83600  1.000 60.31352  ?  908  HIS   A O   1 
ATOM   7197  C  CB  . HIS   A 1 910  ? -61.26800  71.25700  -4.80300  1.000 47.82540  ?  908  HIS   A CB  1 
ATOM   7198  C  CG  . HIS   A 1 910  ? -59.89400  71.75000  -5.13000  1.000 53.23576  ?  908  HIS   A CG  1 
ATOM   7199  N  ND1 . HIS   A 1 910  ? -59.55300  73.08400  -5.07000  1.000 60.26149  ?  908  HIS   A ND1 1 
ATOM   7200  C  CD2 . HIS   A 1 910  ? -58.77600  71.09300  -5.51900  1.000 54.61325  ?  908  HIS   A CD2 1 
ATOM   7201  C  CE1 . HIS   A 1 910  ? -58.28400  73.22800  -5.40900  1.000 61.64796  ?  908  HIS   A CE1 1 
ATOM   7202  N  NE2 . HIS   A 1 910  ? -57.79000  72.03500  -5.68700  1.000 67.61012  ?  908  HIS   A NE2 1 
ATOM   7203  N  N   . ILE   A 1 911  ? -64.25400  72.64100  -6.02800  1.000 47.97194  ?  909  ILE   A N   1 
ATOM   7204  C  CA  . ILE   A 1 911  ? -64.96600  73.20800  -7.17100  1.000 44.77739  ?  909  ILE   A CA  1 
ATOM   7205  C  C   . ILE   A 1 911  ? -65.10200  74.71700  -7.05600  1.000 41.49421  ?  909  ILE   A C   1 
ATOM   7206  O  O   . ILE   A 1 911  ? -65.52400  75.37100  -8.01900  1.000 33.36974  ?  909  ILE   A O   1 
ATOM   7207  C  CB  . ILE   A 1 911  ? -66.34900  72.54200  -7.30800  1.000 37.65225  ?  909  ILE   A CB  1 
ATOM   7208  C  CG1 . ILE   A 1 911  ? -66.85900  72.63100  -8.74700  1.000 47.49994  ?  909  ILE   A CG1 1 
ATOM   7209  C  CG2 . ILE   A 1 911  ? -67.34800  73.17400  -6.34800  1.000 38.90939  ?  909  ILE   A CG2 1 
ATOM   7210  C  CD1 . ILE   A 1 911  ? -68.09900  71.80200  -9.00000  1.000 50.23398  ?  909  ILE   A CD1 1 
ATOM   7211  N  N   . LEU   A 1 912  ? -64.73500  75.29100  -5.91000  1.000 33.27931  ?  910  LEU   A N   1 
ATOM   7212  C  CA  . LEU   A 1 912  ? -64.88500  76.72100  -5.67900  1.000 44.94026  ?  910  LEU   A CA  1 
ATOM   7213  C  C   . LEU   A 1 912  ? -63.57100  77.36800  -5.25700  1.000 48.48192  ?  910  LEU   A C   1 
ATOM   7214  O  O   . LEU   A 1 912  ? -63.19400  78.41600  -5.79000  1.000 55.73845  ?  910  LEU   A O   1 
ATOM   7215  C  CB  . LEU   A 1 912  ? -65.96300  76.97200  -4.62000  1.000 25.54917  ?  910  LEU   A CB  1 
ATOM   7216  C  CG  . LEU   A 1 912  ? -66.00200  78.36200  -3.98000  1.000 38.22358  ?  910  LEU   A CG  1 
ATOM   7217  C  CD1 . LEU   A 1 912  ? -66.25700  79.44300  -5.01900  1.000 42.13563  ?  910  LEU   A CD1 1 
ATOM   7218  C  CD2 . LEU   A 1 912  ? -67.05300  78.41200  -2.88100  1.000 47.79009  ?  910  LEU   A CD2 1 
ATOM   7219  N  N   . LEU   A 1 913  ? -62.86600  76.76200  -4.30800  1.000 38.11362  ?  911  LEU   A N   1 
ATOM   7220  C  CA  . LEU   A 1 913  ? -61.69900  77.38200  -3.68500  1.000 40.96295  ?  911  LEU   A CA  1 
ATOM   7221  C  C   . LEU   A 1 913  ? -60.43100  76.68000  -4.16300  1.000 44.19033  ?  911  LEU   A C   1 
ATOM   7222  O  O   . LEU   A 1 913  ? -60.09200  75.59400  -3.68400  1.000 54.98191  ?  911  LEU   A O   1 
ATOM   7223  C  CB  . LEU   A 1 913  ? -61.81500  77.33200  -2.16500  1.000 37.44045  ?  911  LEU   A CB  1 
ATOM   7224  C  CG  . LEU   A 1 913  ? -61.20300  78.52200  -1.43100  1.000 45.20874  ?  911  LEU   A CG  1 
ATOM   7225  C  CD1 . LEU   A 1 913  ? -61.95600  79.79900  -1.77300  1.000 40.73447  ?  911  LEU   A CD1 1 
ATOM   7226  C  CD2 . LEU   A 1 913  ? -61.20600  78.27600  0.06200   1.000 42.92545  ?  911  LEU   A CD2 1 
ATOM   7227  N  N   . ASP   A 1 914  ? -59.73100  77.30600  -5.10000  1.000 42.20701  ?  912  ASP   A N   1 
ATOM   7228  C  CA  . ASP   A 1 914  ? -58.43600  76.82800  -5.54900  1.000 43.45424  ?  912  ASP   A CA  1 
ATOM   7229  C  C   . ASP   A 1 914  ? -57.34600  77.64800  -4.85000  1.000 54.82786  ?  912  ASP   A C   1 
ATOM   7230  O  O   . ASP   A 1 914  ? -57.61400  78.34000  -3.86100  1.000 49.02040  ?  912  ASP   A O   1 
ATOM   7231  C  CB  . ASP   A 1 914  ? -58.36700  76.88500  -7.08300  1.000 33.88631  ?  912  ASP   A CB  1 
ATOM   7232  C  CG  . ASP   A 1 914  ? -58.20000  78.29500  -7.61300  1.000 46.71828  ?  912  ASP   A CG  1 
ATOM   7233  O  OD1 . ASP   A 1 914  ? -58.74700  79.23600  -7.00600  1.000 55.62308  ?  912  ASP   A OD1 1 
ATOM   7234  O  OD2 . ASP   A 1 914  ? -57.51300  78.46100  -8.64300  1.000 61.00972  -1 912  ASP   A OD2 1 
ATOM   7235  N  N   . GLY   A 1 915  ? -56.11200  77.57500  -5.35300  1.000 47.89454  ?  913  GLY   A N   1 
ATOM   7236  C  CA  . GLY   A 1 915  ? -55.02000  78.28300  -4.70200  1.000 46.70928  ?  913  GLY   A CA  1 
ATOM   7237  C  C   . GLY   A 1 915  ? -55.20400  79.78900  -4.71200  1.000 51.13474  ?  913  GLY   A C   1 
ATOM   7238  O  O   . GLY   A 1 915  ? -55.12900  80.44400  -3.67000  1.000 52.95692  ?  913  GLY   A O   1 
ATOM   7239  N  N   . LEU   A 1 916  ? -55.44100  80.36000  -5.89600  1.000 49.57002  ?  914  LEU   A N   1 
ATOM   7240  C  CA  . LEU   A 1 916  ? -55.59200  81.80900  -5.99500  1.000 45.82619  ?  914  LEU   A CA  1 
ATOM   7241  C  C   . LEU   A 1 916  ? -56.83200  82.30200  -5.26200  1.000 47.28321  ?  914  LEU   A C   1 
ATOM   7242  O  O   . LEU   A 1 916  ? -56.81900  83.40500  -4.70300  1.000 51.89234  ?  914  LEU   A O   1 
ATOM   7243  C  CB  . LEU   A 1 916  ? -55.63800  82.23600  -7.46100  1.000 48.05538  ?  914  LEU   A CB  1 
ATOM   7244  C  CG  . LEU   A 1 916  ? -54.38000  82.91300  -8.00400  1.000 52.34315  ?  914  LEU   A CG  1 
ATOM   7245  C  CD1 . LEU   A 1 916  ? -54.14100  84.23800  -7.29300  1.000 51.81437  ?  914  LEU   A CD1 1 
ATOM   7246  C  CD2 . LEU   A 1 916  ? -53.16800  81.99700  -7.87100  1.000 68.40046  ?  914  LEU   A CD2 1 
ATOM   7247  N  N   . SER   A 1 917  ? -57.90700  81.50900  -5.25000  1.000 48.32745  ?  915  SER   A N   1 
ATOM   7248  C  CA  . SER   A 1 917  ? -59.11800  81.92000  -4.54700  1.000 42.59710  ?  915  SER   A CA  1 
ATOM   7249  C  C   . SER   A 1 917  ? -58.87100  82.06300  -3.05200  1.000 46.21614  ?  915  SER   A C   1 
ATOM   7250  O  O   . SER   A 1 917  ? -59.45900  82.93800  -2.40500  1.000 55.36287  ?  915  SER   A O   1 
ATOM   7251  C  CB  . SER   A 1 917  ? -60.24500  80.91900  -4.80300  1.000 46.98780  ?  915  SER   A CB  1 
ATOM   7252  O  OG  . SER   A 1 917  ? -60.57700  80.86200  -6.18100  1.000 51.64068  ?  915  SER   A OG  1 
ATOM   7253  N  N   . LYS   A 1 918  ? -58.00700  81.21800  -2.48800  1.000 45.20309  ?  916  LYS   A N   1 
ATOM   7254  C  CA  . LYS   A 1 918  ? -57.67100  81.33800  -1.07300  1.000 39.19182  ?  916  LYS   A CA  1 
ATOM   7255  C  C   . LYS   A 1 918  ? -56.91600  82.63300  -0.79600  1.000 41.09849  ?  916  LYS   A C   1 
ATOM   7256  O  O   . LYS   A 1 918  ? -57.12100  83.26600  0.24600   1.000 53.92674  ?  916  LYS   A O   1 
ATOM   7257  C  CB  . LYS   A 1 918  ? -56.85800  80.12000  -0.63100  1.000 33.24387  ?  916  LYS   A CB  1 
ATOM   7258  C  CG  . LYS   A 1 918  ? -56.42300  80.13200  0.82500   1.000 33.97571  ?  916  LYS   A CG  1 
ATOM   7259  C  CD  . LYS   A 1 918  ? -54.93300  80.40700  0.94400   1.000 51.45147  ?  916  LYS   A CD  1 
ATOM   7260  C  CE  . LYS   A 1 918  ? -54.12800  79.47200  0.05200   1.000 61.06754  ?  916  LYS   A CE  1 
ATOM   7261  N  NZ  . LYS   A 1 918  ? -52.67600  79.80700  0.05500   1.000 56.60800  ?  916  LYS   A NZ  1 
ATOM   7262  N  N   . SER   A 1 919  ? -56.04700  83.04800  -1.72000  1.000 35.24211  ?  917  SER   A N   1 
ATOM   7263  C  CA  . SER   A 1 919  ? -55.31600  84.29800  -1.53500  1.000 49.18395  ?  917  SER   A CA  1 
ATOM   7264  C  C   . SER   A 1 919  ? -56.24000  85.50200  -1.66800  1.000 49.53600  ?  917  SER   A C   1 
ATOM   7265  O  O   . SER   A 1 919  ? -56.07600  86.50000  -0.95700  1.000 60.80470  ?  917  SER   A O   1 
ATOM   7266  C  CB  . SER   A 1 919  ? -54.16700  84.38900  -2.54000  1.000 59.43656  ?  917  SER   A CB  1 
ATOM   7267  O  OG  . SER   A 1 919  ? -53.28800  83.28400  -2.41500  1.000 56.78286  ?  917  SER   A OG  1 
ATOM   7268  N  N   . ILE   A 1 920  ? -57.21700  85.42800  -2.57500  1.000 47.86868  ?  918  ILE   A N   1 
ATOM   7269  C  CA  . ILE   A 1 920  ? -58.16600  86.52400  -2.73600  1.000 50.54100  ?  918  ILE   A CA  1 
ATOM   7270  C  C   . ILE   A 1 920  ? -59.09200  86.60900  -1.53000  1.000 44.82585  ?  918  ILE   A C   1 
ATOM   7271  O  O   . ILE   A 1 920  ? -59.40000  87.70300  -1.04100  1.000 52.63177  ?  918  ILE   A O   1 
ATOM   7272  C  CB  . ILE   A 1 920  ? -58.95800  86.35500  -4.04400  1.000 39.93369  ?  918  ILE   A CB  1 
ATOM   7273  C  CG1 . ILE   A 1 920  ? -58.00500  86.28900  -5.23800  1.000 45.13351  ?  918  ILE   A CG1 1 
ATOM   7274  C  CG2 . ILE   A 1 920  ? -59.94800  87.49500  -4.21600  1.000 48.38538  ?  918  ILE   A CG2 1 
ATOM   7275  C  CD1 . ILE   A 1 920  ? -58.66900  85.85700  -6.52600  1.000 37.95094  ?  918  ILE   A CD1 1 
ATOM   7276  N  N   . LEU   A 1 921  ? -59.54800  85.45800  -1.03100  1.000 48.75622  ?  919  LEU   A N   1 
ATOM   7277  C  CA  . LEU   A 1 921  ? -60.44900  85.45100  0.11800   1.000 50.30968  ?  919  LEU   A CA  1 
ATOM   7278  C  C   . LEU   A 1 921  ? -59.75700  85.99400  1.36300   1.000 46.83129  ?  919  LEU   A C   1 
ATOM   7279  O  O   . LEU   A 1 921  ? -60.37000  86.71900  2.15600   1.000 45.96893  ?  919  LEU   A O   1 
ATOM   7280  C  CB  . LEU   A 1 921  ? -60.97000  84.03200  0.35500   1.000 30.71103  ?  919  LEU   A CB  1 
ATOM   7281  C  CG  . LEU   A 1 921  ? -62.19400  83.84000  1.25300   1.000 36.83045  ?  919  LEU   A CG  1 
ATOM   7282  C  CD1 . LEU   A 1 921  ? -63.00000  82.64300  0.77800   1.000 30.34134  ?  919  LEU   A CD1 1 
ATOM   7283  C  CD2 . LEU   A 1 921  ? -61.78700  83.65700  2.70700   1.000 40.39109  ?  919  LEU   A CD2 1 
ATOM   7284  N  N   . ALA   A 1 922  ? -58.47900  85.66000  1.54900   1.000 41.33641  ?  920  ALA   A N   1 
ATOM   7285  C  CA  . ALA   A 1 922  ? -57.74100  86.18500  2.69300   1.000 50.55056  ?  920  ALA   A CA  1 
ATOM   7286  C  C   . ALA   A 1 922  ? -57.50400  87.68300  2.55500   1.000 50.05293  ?  920  ALA   A C   1 
ATOM   7287  O  O   . ALA   A 1 922  ? -57.55800  88.41900  3.54800   1.000 55.75106  ?  920  ALA   A O   1 
ATOM   7288  C  CB  . ALA   A 1 922  ? -56.41500  85.44200  2.85100   1.000 49.17341  ?  920  ALA   A CB  1 
ATOM   7289  N  N   . ARG   A 1 923  ? -57.23900  88.15200  1.33400   1.000 39.18157  ?  921  ARG   A N   1 
ATOM   7290  C  CA  . ARG   A 1 923  ? -57.03200  89.58100  1.11600   1.000 35.33644  ?  921  ARG   A CA  1 
ATOM   7291  C  C   . ARG   A 1 923  ? -58.29500  90.36900  1.43500   1.000 39.53917  ?  921  ARG   A C   1 
ATOM   7292  O  O   . ARG   A 1 923  ? -58.24600  91.39600  2.12100   1.000 50.96969  ?  921  ARG   A O   1 
ATOM   7293  C  CB  . ARG   A 1 923  ? -56.59700  89.83900  -0.32700  1.000 34.79147  ?  921  ARG   A CB  1 
ATOM   7294  C  CG  . ARG   A 1 923  ? -56.32700  91.30700  -0.62700  1.000 54.09784  ?  921  ARG   A CG  1 
ATOM   7295  C  CD  . ARG   A 1 923  ? -56.27500  91.59700  -2.12200  1.000 45.17688  ?  921  ARG   A CD  1 
ATOM   7296  N  NE  . ARG   A 1 923  ? -55.77700  90.46600  -2.89500  1.000 52.40788  ?  921  ARG   A NE  1 
ATOM   7297  C  CZ  . ARG   A 1 923  ? -56.43600  89.89700  -3.89600  1.000 71.02457  ?  921  ARG   A CZ  1 
ATOM   7298  N  NH1 . ARG   A 1 923  ? -57.61200  90.35400  -4.29700  1.000 65.57449  ?  921  ARG   A NH1 1 
ATOM   7299  N  NH2 . ARG   A 1 923  ? -55.89800  88.85100  -4.51600  1.000 63.93041  ?  921  ARG   A NH2 1 
ATOM   7300  N  N   . GLU   A 1 924  ? -59.44100  89.89700  0.94200   1.000 42.65956  ?  922  GLU   A N   1 
ATOM   7301  C  CA  . GLU   A 1 924  ? -60.68000  90.64200  1.12500   1.000 52.82678  ?  922  GLU   A CA  1 
ATOM   7302  C  C   . GLU   A 1 924  ? -61.20000  90.52900  2.55100   1.000 58.78852  ?  922  GLU   A C   1 
ATOM   7303  O  O   . GLU   A 1 924  ? -61.82900  91.46700  3.05300   1.000 71.63025  ?  922  GLU   A O   1 
ATOM   7304  C  CB  . GLU   A 1 924  ? -61.72700  90.16200  0.12100   1.000 44.11223  ?  922  GLU   A CB  1 
ATOM   7305  C  CG  . GLU   A 1 924  ? -61.31700  90.38300  -1.32800  1.000 33.90329  ?  922  GLU   A CG  1 
ATOM   7306  C  CD  . GLU   A 1 924  ? -62.42200  90.05200  -2.31100  1.000 47.64804  ?  922  GLU   A CD  1 
ATOM   7307  O  OE1 . GLU   A 1 924  ? -63.48500  89.56800  -1.87100  1.000 54.15712  ?  922  GLU   A OE1 1 
ATOM   7308  O  OE2 . GLU   A 1 924  ? -62.22900  90.27800  -3.52400  1.000 49.86168  -1 922  GLU   A OE2 1 
ATOM   7309  N  N   . LEU   A 1 925  ? -60.94700  89.40300  3.22100   1.000 44.22381  ?  923  LEU   A N   1 
ATOM   7310  C  CA  . LEU   A 1 925  ? -61.33900  89.28900  4.62200   1.000 47.33433  ?  923  LEU   A CA  1 
ATOM   7311  C  C   . LEU   A 1 925  ? -60.49600  90.20200  5.50300   1.000 45.88737  ?  923  LEU   A C   1 
ATOM   7312  O  O   . LEU   A 1 925  ? -61.02000  90.84200  6.42200   1.000 56.97948  ?  923  LEU   A O   1 
ATOM   7313  C  CB  . LEU   A 1 925  ? -61.23000  87.83700  5.08800   1.000 48.25725  ?  923  LEU   A CB  1 
ATOM   7314  C  CG  . LEU   A 1 925  ? -61.58400  87.58400  6.55600   1.000 38.52319  ?  923  LEU   A CG  1 
ATOM   7315  C  CD1 . LEU   A 1 925  ? -62.96600  88.12900  6.88200   1.000 50.72087  ?  923  LEU   A CD1 1 
ATOM   7316  C  CD2 . LEU   A 1 925  ? -61.50400  86.10300  6.88100   1.000 29.78449  ?  923  LEU   A CD2 1 
ATOM   7317  N  N   . GLN   A 1 926  ? -59.19000  90.28400  5.23300   1.000 48.59294  ?  924  GLN   A N   1 
ATOM   7318  C  CA  . GLN   A 1 926  ? -58.33400  91.19100  5.99000   1.000 52.36682  ?  924  GLN   A CA  1 
ATOM   7319  C  C   . GLN   A 1 926  ? -58.72300  92.64500  5.75700   1.000 53.25364  ?  924  GLN   A C   1 
ATOM   7320  O  O   . GLN   A 1 926  ? -58.53400  93.49000  6.64000   1.000 60.14778  ?  924  GLN   A O   1 
ATOM   7321  C  CB  . GLN   A 1 926  ? -56.86900  90.96400  5.61800   1.000 46.50324  ?  924  GLN   A CB  1 
ATOM   7322  C  CG  . GLN   A 1 926  ? -55.87700  91.68200  6.51800   1.000 51.30203  ?  924  GLN   A CG  1 
ATOM   7323  C  CD  . GLN   A 1 926  ? -54.44500  91.51600  6.05200   1.000 53.38085  ?  924  GLN   A CD  1 
ATOM   7324  O  OE1 . GLN   A 1 926  ? -53.61400  90.93900  6.75200   1.000 58.62094  ?  924  GLN   A OE1 1 
ATOM   7325  N  NE2 . GLN   A 1 926  ? -54.14900  92.02800  4.86200   1.000 38.73452  ?  924  GLN   A NE2 1 
ATOM   7326  N  N   . ALA   A 1 927  ? -59.26600  92.95600  4.57900   1.000 51.59298  ?  925  ALA   A N   1 
ATOM   7327  C  CA  . ALA   A 1 927  ? -59.74300  94.30700  4.31200   1.000 53.45169  ?  925  ALA   A CA  1 
ATOM   7328  C  C   . ALA   A 1 927  ? -61.06800  94.57100  5.01500   1.000 63.85437  ?  925  ALA   A C   1 
ATOM   7329  O  O   . ALA   A 1 927  ? -61.22900  95.59400  5.68900   1.000 79.20511  ?  925  ALA   A O   1 
ATOM   7330  C  CB  . ALA   A 1 927  ? -59.88100  94.52600  2.80500   1.000 53.96715  ?  925  ALA   A CB  1 
ATOM   7331  N  N   . LEU   A 1 928  ? -62.02900  93.65300  4.86800   1.000 57.83831  ?  926  LEU   A N   1 
ATOM   7332  C  CA  . LEU   A 1 928  ? -63.32100  93.81600  5.52700   1.000 44.84302  ?  926  LEU   A CA  1 
ATOM   7333  C  C   . LEU   A 1 928  ? -63.17100  93.83300  7.04400   1.000 61.18608  ?  926  LEU   A C   1 
ATOM   7334  O  O   . LEU   A 1 928  ? -63.84000  94.61400  7.73200   1.000 68.79738  ?  926  LEU   A O   1 
ATOM   7335  C  CB  . LEU   A 1 928  ? -64.27300  92.70100  5.09100   1.000 49.22576  ?  926  LEU   A CB  1 
ATOM   7336  C  CG  . LEU   A 1 928  ? -64.76700  92.72800  3.64300   1.000 41.32713  ?  926  LEU   A CG  1 
ATOM   7337  C  CD1 . LEU   A 1 928  ? -65.19500  91.33800  3.20900   1.000 39.70395  ?  926  LEU   A CD1 1 
ATOM   7338  C  CD2 . LEU   A 1 928  ? -65.91700  93.71100  3.48300   1.000 62.55241  ?  926  LEU   A CD2 1 
ATOM   7339  N  N   . LEU   A 1 929  ? -62.29700  92.97700  7.58600   1.000 52.91782  ?  927  LEU   A N   1 
ATOM   7340  C  CA  . LEU   A 1 929  ? -62.05300  92.97800  9.02500   1.000 51.64249  ?  927  LEU   A CA  1 
ATOM   7341  C  C   . LEU   A 1 929  ? -61.39600  94.27400  9.47800   1.000 56.60332  ?  927  LEU   A C   1 
ATOM   7342  O  O   . LEU   A 1 929  ? -61.61900  94.72100  10.60800  1.000 82.37894  ?  927  LEU   A O   1 
ATOM   7343  C  CB  . LEU   A 1 929  ? -61.18900  91.78300  9.42000   1.000 46.29603  ?  927  LEU   A CB  1 
ATOM   7344  C  CG  . LEU   A 1 929  ? -61.93100  90.50900  9.82400   1.000 51.84590  ?  927  LEU   A CG  1 
ATOM   7345  C  CD1 . LEU   A 1 929  ? -60.94700  89.36800  10.00600  1.000 59.45758  ?  927  LEU   A CD1 1 
ATOM   7346  C  CD2 . LEU   A 1 929  ? -62.72800  90.74200  11.09900  1.000 67.93313  ?  927  LEU   A CD2 1 
ATOM   7347  N  N   . GLY   A 1 930  ? -60.58800  94.88200  8.61900   1.000 56.99205  ?  928  GLY   A N   1 
ATOM   7348  C  CA  . GLY   A 1 930  ? -60.05300  96.20400  8.84900   1.000 67.00235  ?  928  GLY   A CA  1 
ATOM   7349  C  C   . GLY   A 1 930  ? -61.02000  97.33800  8.57500   1.000 71.36283  ?  928  GLY   A C   1 
ATOM   7350  O  O   . GLY   A 1 930  ? -60.59600  98.49700  8.54900   1.000 70.03000  ?  928  GLY   A O   1 
ATOM   7351  N  N   . GLN   A 1 931  ? -62.30500  97.04000  8.38100   1.000 68.14438  ?  929  GLN   A N   1 
ATOM   7352  C  CA  . GLN   A 1 931  ? -63.32900  98.04800  8.08700   1.000 74.26703  ?  929  GLN   A CA  1 
ATOM   7353  C  C   . GLN   A 1 931  ? -62.94100  98.89900  6.87700   1.000 71.58582  ?  929  GLN   A C   1 
ATOM   7354  O  O   . GLN   A 1 931  ? -63.02200  100.12900 6.88800   1.000 92.27407  ?  929  GLN   A O   1 
ATOM   7355  C  CB  . GLN   A 1 931  ? -63.61700  98.91900  9.31300   1.000 65.86771  ?  929  GLN   A CB  1 
ATOM   7356  C  CG  . GLN   A 1 931  ? -64.62700  98.29600  10.26700  1.000 73.53205  ?  929  GLN   A CG  1 
ATOM   7357  C  CD  . GLN   A 1 931  ? -64.22500  98.42200  11.72200  1.000 96.68578  ?  929  GLN   A CD  1 
ATOM   7358  O  OE1 . GLN   A 1 931  ? -63.23800  97.82900  12.15900  1.000 96.71508  ?  929  GLN   A OE1 1 
ATOM   7359  N  NE2 . GLN   A 1 931  ? -64.99400  99.19100  12.48300  1.000 83.00259  ?  929  GLN   A NE2 1 
ATOM   7360  N  N   . GLN   A 1 932  ? -62.51800  98.21900  5.81700   1.000 66.72854  ?  930  GLN   A N   1 
ATOM   7361  C  CA  . GLN   A 1 932  ? -62.16600  98.85700  4.56000   1.000 72.44483  ?  930  GLN   A CA  1 
ATOM   7362  C  C   . GLN   A 1 932  ? -63.21100  98.53400  3.50000   1.000 69.36640  ?  930  GLN   A C   1 
ATOM   7363  O  O   . GLN   A 1 932  ? -63.93500  97.53900  3.58800   1.000 74.34919  ?  930  GLN   A O   1 
ATOM   7364  C  CB  . GLN   A 1 932  ? -60.77700  98.41300  4.08700   1.000 57.27015  ?  930  GLN   A CB  1 
ATOM   7365  C  CG  . GLN   A 1 932  ? -59.69800  98.52000  5.15100   1.000 72.24115  ?  930  GLN   A CG  1 
ATOM   7366  C  CD  . GLN   A 1 932  ? -58.29900  98.50500  4.56600   1.000 98.67855  ?  930  GLN   A CD  1 
ATOM   7367  O  OE1 . GLN   A 1 932  ? -58.03400  99.14600  3.54900   1.000 99.32952  ?  930  GLN   A OE1 1 
ATOM   7368  N  NE2 . GLN   A 1 932  ? -57.39600  97.77200  5.20700   1.000 102.75666 ?  930  GLN   A NE2 1 
ATOM   7369  N  N   . VAL   A 1 933  ? -63.28200  99.40000  2.49200   1.000 51.97570  ?  931  VAL   A N   1 
ATOM   7370  C  CA  . VAL   A 1 933  ? -64.25300  99.22300  1.42000   1.000 71.84670  ?  931  VAL   A CA  1 
ATOM   7371  C  C   . VAL   A 1 933  ? -63.74900  98.18300  0.42600   1.000 89.34364  ?  931  VAL   A C   1 
ATOM   7372  O  O   . VAL   A 1 933  ? -62.55000  97.91100  0.31400   1.000 90.23624  ?  931  VAL   A O   1 
ATOM   7373  C  CB  . VAL   A 1 933  ? -64.55400  100.56200 0.72300   1.000 76.17790  ?  931  VAL   A CB  1 
ATOM   7374  C  CG1 . VAL   A 1 933  ? -65.57600  101.35600 1.52000   1.000 63.73787  ?  931  VAL   A CG1 1 
ATOM   7375  C  CG2 . VAL   A 1 933  ? -63.27300  101.36300 0.54700   1.000 76.37498  ?  931  VAL   A CG2 1 
ATOM   7376  N  N   . LEU   A 1 934  ? -64.68900  97.59600  -0.31100  1.000 77.13887  ?  932  LEU   A N   1 
ATOM   7377  C  CA  . LEU   A 1 934  ? -64.39100  96.56800  -1.30500  1.000 74.17673  ?  932  LEU   A CA  1 
ATOM   7378  C  C   . LEU   A 1 934  ? -65.12200  96.92300  -2.59300  1.000 86.10261  ?  932  LEU   A C   1 
ATOM   7379  O  O   . LEU   A 1 934  ? -66.34800  96.78100  -2.67300  1.000 100.57357 ?  932  LEU   A O   1 
ATOM   7380  C  CB  . LEU   A 1 934  ? -64.80700  95.18400  -0.80800  1.000 86.83113  ?  932  LEU   A CB  1 
ATOM   7381  C  CG  . LEU   A 1 934  ? -63.69900  94.18100  -0.47800  1.000 66.21101  ?  932  LEU   A CG  1 
ATOM   7382  C  CD1 . LEU   A 1 934  ? -62.80700  94.70500  0.63200   1.000 67.02378  ?  932  LEU   A CD1 1 
ATOM   7383  C  CD2 . LEU   A 1 934  ? -64.30100  92.84000  -0.09300  1.000 71.15168  ?  932  LEU   A CD2 1 
ATOM   7384  N  N   . SER   A 1 935  ? -64.37800  97.38300  -3.59300  1.000 84.59524  ?  933  SER   A N   1 
ATOM   7385  C  CA  . SER   A 1 935  ? -64.98200  97.72200  -4.87600  1.000 80.21157  ?  933  SER   A CA  1 
ATOM   7386  C  C   . SER   A 1 935  ? -65.58200  96.46900  -5.50800  1.000 81.26529  ?  933  SER   A C   1 
ATOM   7387  O  O   . SER   A 1 935  ? -64.88900  95.44900  -5.62500  1.000 95.53089  ?  933  SER   A O   1 
ATOM   7388  C  CB  . SER   A 1 935  ? -63.94400  98.34200  -5.80900  1.000 64.55264  ?  933  SER   A CB  1 
ATOM   7389  O  OG  . SER   A 1 935  ? -62.87000  97.44800  -6.04100  1.000 87.68272  ?  933  SER   A OG  1 
ATOM   7390  N  N   . PRO   A 1 936  ? -66.84700  96.50400  -5.93100  1.000 87.78944  ?  934  PRO   A N   1 
ATOM   7391  C  CA  . PRO   A 1 936  ? -67.51100  95.27400  -6.38400  1.000 95.66031  ?  934  PRO   A CA  1 
ATOM   7392  C  C   . PRO   A 1 936  ? -66.80000  94.62500  -7.56200  1.000 81.65308  ?  934  PRO   A C   1 
ATOM   7393  O  O   . PRO   A 1 936  ? -66.08700  95.27700  -8.32900  1.000 71.75234  ?  934  PRO   A O   1 
ATOM   7394  C  CB  . PRO   A 1 936  ? -68.91800  95.75000  -6.77200  1.000 84.08564  ?  934  PRO   A CB  1 
ATOM   7395  C  CG  . PRO   A 1 936  ? -68.79600  97.23300  -6.95100  1.000 89.08804  ?  934  PRO   A CG  1 
ATOM   7396  C  CD  . PRO   A 1 936  ? -67.74200  97.67100  -5.98400  1.000 95.08596  ?  934  PRO   A CD  1 
ATOM   7397  N  N   . VAL   A 1 937  ? -67.00400  93.31000  -7.69200  1.000 74.85106  ?  935  VAL   A N   1 
ATOM   7398  C  CA  . VAL   A 1 937  ? -66.33300  92.54100  -8.73500  1.000 71.60750  ?  935  VAL   A CA  1 
ATOM   7399  C  C   . VAL   A 1 937  ? -66.90000  92.91000  -10.10500 1.000 75.94995  ?  935  VAL   A C   1 
ATOM   7400  O  O   . VAL   A 1 937  ? -67.97100  93.51500  -10.23200 1.000 88.75277  ?  935  VAL   A O   1 
ATOM   7401  C  CB  . VAL   A 1 937  ? -66.46400  91.03300  -8.45900  1.000 52.16667  ?  935  VAL   A CB  1 
ATOM   7402  C  CG1 . VAL   A 1 937  ? -67.77500  90.49100  -9.01600  1.000 70.94553  ?  935  VAL   A CG1 1 
ATOM   7403  C  CG2 . VAL   A 1 937  ? -65.26500  90.27100  -9.01200  1.000 71.50531  ?  935  VAL   A CG2 1 
ATOM   7404  N  N   . GLU   A 1 938  ? -66.15900  92.53900  -11.14900 1.000 61.33682  ?  936  GLU   A N   1 
ATOM   7405  C  CA  . GLU   A 1 938  ? -66.51300  92.88600  -12.51800 1.000 49.70594  ?  936  GLU   A CA  1 
ATOM   7406  C  C   . GLU   A 1 938  ? -66.81100  91.69100  -13.41000 1.000 65.30639  ?  936  GLU   A C   1 
ATOM   7407  O  O   . GLU   A 1 938  ? -67.60800  91.82600  -14.34200 1.000 75.83184  ?  936  GLU   A O   1 
ATOM   7408  C  CB  . GLU   A 1 938  ? -65.39200  93.71600  -13.16300 1.000 50.25785  ?  936  GLU   A CB  1 
ATOM   7409  C  CG  . GLU   A 1 938  ? -65.55300  95.21600  -12.97900 1.000 71.71335  ?  936  GLU   A CG  1 
ATOM   7410  C  CD  . GLU   A 1 938  ? -66.30300  95.86300  -14.12800 1.000 98.93606  ?  936  GLU   A CD  1 
ATOM   7411  O  OE1 . GLU   A 1 938  ? -65.68800  96.06800  -15.19600 1.000 89.59825  ?  936  GLU   A OE1 1 
ATOM   7412  O  OE2 . GLU   A 1 938  ? -67.50700  96.15600  -13.96800 1.000 103.03419 -1 936  GLU   A OE2 1 
ATOM   7413  N  N   . LYS   A 1 939  ? -66.20500  90.53300  -13.16100 1.000 50.44185  ?  937  LYS   A N   1 
ATOM   7414  C  CA  . LYS   A 1 939  ? -66.41000  89.35900  -13.99500 1.000 47.52292  ?  937  LYS   A CA  1 
ATOM   7415  C  C   . LYS   A 1 939  ? -66.91700  88.19100  -13.16000 1.000 53.26050  ?  937  LYS   A C   1 
ATOM   7416  O  O   . LYS   A 1 939  ? -66.75500  88.15300  -11.93700 1.000 63.84680  ?  937  LYS   A O   1 
ATOM   7417  C  CB  . LYS   A 1 939  ? -65.12200  88.96000  -14.72400 1.000 55.69798  ?  937  LYS   A CB  1 
ATOM   7418  C  CG  . LYS   A 1 939  ? -64.72300  89.92200  -15.82800 1.000 70.67334  ?  937  LYS   A CG  1 
ATOM   7419  C  CD  . LYS   A 1 939  ? -65.91200  90.25400  -16.71600 1.000 72.57046  ?  937  LYS   A CD  1 
ATOM   7420  C  CE  . LYS   A 1 939  ? -65.48800  91.07700  -17.91900 1.000 72.80321  ?  937  LYS   A CE  1 
ATOM   7421  N  NZ  . LYS   A 1 939  ? -64.68200  92.26800  -17.53700 1.000 71.78207  ?  937  LYS   A NZ  1 
ATOM   7422  N  N   . THR   A 1 940  ? -67.53700  87.23200  -13.84500 1.000 49.36160  ?  938  THR   A N   1 
ATOM   7423  C  CA  . THR   A 1 940  ? -68.08600  86.03800  -13.22100 1.000 59.97734  ?  938  THR   A CA  1 
ATOM   7424  C  C   . THR   A 1 940  ? -67.49600  84.79500  -13.87300 1.000 41.52060  ?  938  THR   A C   1 
ATOM   7425  O  O   . THR   A 1 940  ? -67.06800  84.82400  -15.03100 1.000 45.53411  ?  938  THR   A O   1 
ATOM   7426  C  CB  . THR   A 1 940  ? -69.61800  85.99900  -13.32900 1.000 58.34665  ?  938  THR   A CB  1 
ATOM   7427  O  OG1 . THR   A 1 940  ? -70.00500  86.01400  -14.70900 1.000 67.97735  ?  938  THR   A OG1 1 
ATOM   7428  C  CG2 . THR   A 1 940  ? -70.23200  87.19500  -12.62400 1.000 36.63854  ?  938  THR   A CG2 1 
ATOM   7429  N  N   . TYR   A 1 941  ? -67.48200  83.69600  -13.11300 1.000 33.40837  ?  939  TYR   A N   1 
ATOM   7430  C  CA  . TYR   A 1 941  ? -66.93200  82.44600  -13.62600 1.000 31.45017  ?  939  TYR   A CA  1 
ATOM   7431  C  C   . TYR   A 1 941  ? -67.75400  81.90800  -14.79000 1.000 50.24836  ?  939  TYR   A C   1 
ATOM   7432  O  O   . TYR   A 1 941  ? -67.20700  81.24500  -15.68000 1.000 56.54161  ?  939  TYR   A O   1 
ATOM   7433  C  CB  . TYR   A 1 941  ? -66.85400  81.40800  -12.50400 1.000 40.78138  ?  939  TYR   A CB  1 
ATOM   7434  C  CG  . TYR   A 1 941  ? -66.02900  80.18200  -12.83500 1.000 38.01226  ?  939  TYR   A CG  1 
ATOM   7435  C  CD1 . TYR   A 1 941  ? -66.57400  79.12300  -13.55100 1.000 46.49102  ?  939  TYR   A CD1 1 
ATOM   7436  C  CD2 . TYR   A 1 941  ? -64.70900  80.07800  -12.41900 1.000 43.43165  ?  939  TYR   A CD2 1 
ATOM   7437  C  CE1 . TYR   A 1 941  ? -65.82300  78.00300  -13.85400 1.000 47.17721  ?  939  TYR   A CE1 1 
ATOM   7438  C  CE2 . TYR   A 1 941  ? -63.95000  78.96000  -12.71600 1.000 47.94065  ?  939  TYR   A CE2 1 
ATOM   7439  C  CZ  . TYR   A 1 941  ? -64.51300  77.92400  -13.43200 1.000 52.23147  ?  939  TYR   A CZ  1 
ATOM   7440  O  OH  . TYR   A 1 941  ? -63.76400  76.80900  -13.73000 1.000 46.86736  ?  939  TYR   A OH  1 
ATOM   7441  N  N   . LYS   A 1 942  ? -69.06300  82.17800  -14.79900 1.000 54.42167  ?  940  LYS   A N   1 
ATOM   7442  C  CA  . LYS   A 1 942  ? -69.91000  81.72900  -15.90000 1.000 47.76978  ?  940  LYS   A CA  1 
ATOM   7443  C  C   . LYS   A 1 942  ? -69.40700  82.26400  -17.23400 1.000 54.38295  ?  940  LYS   A C   1 
ATOM   7444  O  O   . LYS   A 1 942  ? -69.48200  81.57400  -18.25900 1.000 55.18674  ?  940  LYS   A O   1 
ATOM   7445  C  CB  . LYS   A 1 942  ? -71.35200  82.17400  -15.66600 1.000 45.26559  ?  940  LYS   A CB  1 
ATOM   7446  C  CG  . LYS   A 1 942  ? -71.71300  82.36900  -14.20600 1.000 65.19126  ?  940  LYS   A CG  1 
ATOM   7447  C  CD  . LYS   A 1 942  ? -73.07200  83.03500  -14.06600 1.000 55.84212  ?  940  LYS   A CD  1 
ATOM   7448  C  CE  . LYS   A 1 942  ? -73.06300  84.44600  -14.62300 1.000 42.22548  ?  940  LYS   A CE  1 
ATOM   7449  N  NZ  . LYS   A 1 942  ? -74.40000  85.08700  -14.49400 1.000 64.46625  ?  940  LYS   A NZ  1 
ATOM   7450  N  N   . SER   A 1 943  ? -68.89100  83.49400  -17.23900 1.000 45.32822  ?  941  SER   A N   1 
ATOM   7451  C  CA  . SER   A 1 943  ? -68.35400  84.07400  -18.46400 1.000 39.12792  ?  941  SER   A CA  1 
ATOM   7452  C  C   . SER   A 1 943  ? -67.09600  83.34000  -18.91000 1.000 57.27766  ?  941  SER   A C   1 
ATOM   7453  O  O   . SER   A 1 943  ? -66.94600  83.00500  -20.09100 1.000 79.83550  ?  941  SER   A O   1 
ATOM   7454  C  CB  . SER   A 1 943  ? -68.06000  85.55800  -18.25100 1.000 49.95772  ?  941  SER   A CB  1 
ATOM   7455  O  OG  . SER   A 1 943  ? -68.78600  86.06300  -17.14500 1.000 61.86238  ?  941  SER   A OG  1 
ATOM   7456  N  N   . PHE   A 1 944  ? -66.17800  83.08600  -17.97500 1.000 52.11746  ?  942  PHE   A N   1 
ATOM   7457  C  CA  . PHE   A 1 944  ? -64.94300  82.39100  -18.32200 1.000 54.07781  ?  942  PHE   A CA  1 
ATOM   7458  C  C   . PHE   A 1 944  ? -65.22400  80.97500  -18.80600 1.000 50.70614  ?  942  PHE   A C   1 
ATOM   7459  O  O   . PHE   A 1 944  ? -64.55300  80.47900  -19.71900 1.000 54.37919  ?  942  PHE   A O   1 
ATOM   7460  C  CB  . PHE   A 1 944  ? -63.99300  82.36700  -17.12400 1.000 47.77639  ?  942  PHE   A CB  1 
ATOM   7461  C  CG  . PHE   A 1 944  ? -62.77500  81.51400  -17.33800 1.000 52.57771  ?  942  PHE   A CG  1 
ATOM   7462  C  CD1 . PHE   A 1 944  ? -61.70200  81.99000  -18.07300 1.000 50.57171  ?  942  PHE   A CD1 1 
ATOM   7463  C  CD2 . PHE   A 1 944  ? -62.70400  80.23500  -16.81000 1.000 47.50336  ?  942  PHE   A CD2 1 
ATOM   7464  C  CE1 . PHE   A 1 944  ? -60.58200  81.20800  -18.27500 1.000 58.20651  ?  942  PHE   A CE1 1 
ATOM   7465  C  CE2 . PHE   A 1 944  ? -61.58800  79.44800  -17.01000 1.000 33.54135  ?  942  PHE   A CE2 1 
ATOM   7466  C  CZ  . PHE   A 1 944  ? -60.52500  79.93500  -17.74200 1.000 52.11673  ?  942  PHE   A CZ  1 
ATOM   7467  N  N   . ALA   A 1 945  ? -66.21100  80.30700  -18.20500 1.000 32.08459  ?  943  ALA   A N   1 
ATOM   7468  C  CA  . ALA   A 1 945  ? -66.54600  78.95000  -18.62400 1.000 44.79741  ?  943  ALA   A CA  1 
ATOM   7469  C  C   . ALA   A 1 945  ? -66.99200  78.92400  -20.08000 1.000 52.10971  ?  943  ALA   A C   1 
ATOM   7470  O  O   . ALA   A 1 945  ? -66.55000  78.07400  -20.86200 1.000 57.02529  ?  943  ALA   A O   1 
ATOM   7471  C  CB  . ALA   A 1 945  ? -67.62600  78.36800  -17.71300 1.000 45.74988  ?  943  ALA   A CB  1 
ATOM   7472  N  N   . ARG   A 1 946  ? -67.86600  79.85800  -20.46700 1.000 54.28320  ?  944  ARG   A N   1 
ATOM   7473  C  CA  . ARG   A 1 946  ? -68.30100  79.92600  -21.85900 1.000 68.25826  ?  944  ARG   A CA  1 
ATOM   7474  C  C   . ARG   A 1 946  ? -67.13600  80.24800  -22.78500 1.000 57.75045  ?  944  ARG   A C   1 
ATOM   7475  O  O   . ARG   A 1 946  ? -67.01100  79.65900  -23.86500 1.000 61.99312  ?  944  ARG   A O   1 
ATOM   7476  C  CB  . ARG   A 1 946  ? -69.40800  80.96900  -22.02000 1.000 56.39249  ?  944  ARG   A CB  1 
ATOM   7477  C  CG  . ARG   A 1 946  ? -69.98300  81.02600  -23.42900 1.000 58.40421  ?  944  ARG   A CG  1 
ATOM   7478  C  CD  . ARG   A 1 946  ? -70.93400  79.86200  -23.68500 1.000 73.32263  ?  944  ARG   A CD  1 
ATOM   7479  N  NE  . ARG   A 1 946  ? -70.83300  79.32400  -25.03800 1.000 88.40239  ?  944  ARG   A NE  1 
ATOM   7480  C  CZ  . ARG   A 1 946  ? -70.42400  78.09700  -25.33300 1.000 96.59695  ?  944  ARG   A CZ  1 
ATOM   7481  N  NH1 . ARG   A 1 946  ? -70.07300  77.23700  -24.38900 1.000 86.90507  ?  944  ARG   A NH1 1 
ATOM   7482  N  NH2 . ARG   A 1 946  ? -70.37300  77.71800  -26.60700 1.000 104.25782 ?  944  ARG   A NH2 1 
ATOM   7483  N  N   . TRP   A 1 947  ? -66.27500  81.18300  -22.37600 1.000 43.88889  ?  945  TRP   A N   1 
ATOM   7484  C  CA  . TRP   A 1 947  ? -65.10600  81.53200  -23.17700 1.000 47.95349  ?  945  TRP   A CA  1 
ATOM   7485  C  C   . TRP   A 1 947  ? -64.23500  80.30900  -23.44000 1.000 59.24971  ?  945  TRP   A C   1 
ATOM   7486  O  O   . TRP   A 1 947  ? -63.78900  80.08200  -24.57100 1.000 63.19324  ?  945  TRP   A O   1 
ATOM   7487  C  CB  . TRP   A 1 947  ? -64.30500  82.62800  -22.47000 1.000 41.02674  ?  945  TRP   A CB  1 
ATOM   7488  C  CG  . TRP   A 1 947  ? -62.99400  82.94900  -23.12500 1.000 51.05899  ?  945  TRP   A CG  1 
ATOM   7489  C  CD1 . TRP   A 1 947  ? -62.74600  83.94600  -24.02300 1.000 67.13774  ?  945  TRP   A CD1 1 
ATOM   7490  C  CD2 . TRP   A 1 947  ? -61.74700  82.27100  -22.92600 1.000 61.16165  ?  945  TRP   A CD2 1 
ATOM   7491  N  NE1 . TRP   A 1 947  ? -61.42400  83.92900  -24.39800 1.000 74.08965  ?  945  TRP   A NE1 1 
ATOM   7492  C  CE2 . TRP   A 1 947  ? -60.79000  82.90900  -23.73800 1.000 64.12333  ?  945  TRP   A CE2 1 
ATOM   7493  C  CE3 . TRP   A 1 947  ? -61.34800  81.18700  -22.13900 1.000 47.24408  ?  945  TRP   A CE3 1 
ATOM   7494  C  CZ2 . TRP   A 1 947  ? -59.46300  82.49700  -23.78900 1.000 57.77370  ?  945  TRP   A CZ2 1 
ATOM   7495  C  CZ3 . TRP   A 1 947  ? -60.03400  80.77700  -22.19400 1.000 69.53459  ?  945  TRP   A CZ3 1 
ATOM   7496  C  CH2 . TRP   A 1 947  ? -59.10600  81.43200  -23.01100 1.000 76.99319  ?  945  TRP   A CH2 1 
ATOM   7497  N  N   . GLN   A 1 948  ? -63.99000  79.50300  -22.40500 1.000 50.32216  ?  946  GLN   A N   1 
ATOM   7498  C  CA  . GLN   A 1 948  ? -63.10000  78.35600  -22.55300 1.000 45.28182  ?  946  GLN   A CA  1 
ATOM   7499  C  C   . GLN   A 1 948  ? -63.77500  77.21500  -23.30200 1.000 52.36958  ?  946  GLN   A C   1 
ATOM   7500  O  O   . GLN   A 1 948  ? -63.13900  76.55300  -24.13000 1.000 66.84911  ?  946  GLN   A O   1 
ATOM   7501  C  CB  . GLN   A 1 948  ? -62.62300  77.88200  -21.18200 1.000 66.97101  ?  946  GLN   A CB  1 
ATOM   7502  C  CG  . GLN   A 1 948  ? -61.16300  77.46400  -21.15300 1.000 64.34374  ?  946  GLN   A CG  1 
ATOM   7503  C  CD  . GLN   A 1 948  ? -60.78800  76.75200  -19.87200 1.000 51.74825  ?  946  GLN   A CD  1 
ATOM   7504  O  OE1 . GLN   A 1 948  ? -61.58100  75.99000  -19.31900 1.000 53.65194  ?  946  GLN   A OE1 1 
ATOM   7505  N  NE2 . GLN   A 1 948  ? -59.57500  76.99800  -19.39100 1.000 52.97607  ?  946  GLN   A NE2 1 
ATOM   7506  N  N   . ASN   A 1 949  ? -65.05700  76.96900  -23.01900 1.000 58.03271  ?  947  ASN   A N   1 
ATOM   7507  C  CA  . ASN   A 1 949  ? -65.78800  75.93500  -23.74200 1.000 58.21057  ?  947  ASN   A CA  1 
ATOM   7508  C  C   . ASN   A 1 949  ? -65.82500  76.22600  -25.23600 1.000 52.95954  ?  947  ASN   A C   1 
ATOM   7509  O  O   . ASN   A 1 949  ? -65.87800  75.29600  -26.04900 1.000 48.28886  ?  947  ASN   A O   1 
ATOM   7510  C  CB  . ASN   A 1 949  ? -67.20500  75.80800  -23.17800 1.000 67.40458  ?  947  ASN   A CB  1 
ATOM   7511  C  CG  . ASN   A 1 949  ? -67.23300  75.16300  -21.80100 1.000 63.38863  ?  947  ASN   A CG  1 
ATOM   7512  O  OD1 . ASN   A 1 949  ? -67.85800  74.12000  -21.60500 1.000 57.01250  ?  947  ASN   A OD1 1 
ATOM   7513  N  ND2 . ASN   A 1 949  ? -66.54800  75.77600  -20.84300 1.000 77.15682  ?  947  ASN   A ND2 1 
ATOM   7514  N  N   . GLU   A 1 950  ? -65.78900  77.50600  -25.61600 1.000 50.53463  ?  948  GLU   A N   1 
ATOM   7515  C  CA  . GLU   A 1 950  ? -65.70600  77.86300  -27.02700 1.000 61.45734  ?  948  GLU   A CA  1 
ATOM   7516  C  C   . GLU   A 1 950  ? -64.28400  77.70700  -27.55100 1.000 69.12776  ?  948  GLU   A C   1 
ATOM   7517  O  O   . GLU   A 1 950  ? -64.08400  77.26100  -28.68600 1.000 64.85368  ?  948  GLU   A O   1 
ATOM   7518  C  CB  . GLU   A 1 950  ? -66.19500  79.29600  -27.23900 1.000 69.17765  ?  948  GLU   A CB  1 
ATOM   7519  C  CG  . GLU   A 1 950  ? -66.45400  79.65600  -28.69400 1.000 93.20471  ?  948  GLU   A CG  1 
ATOM   7520  C  CD  . GLU   A 1 950  ? -67.84100  79.25600  -29.15800 1.000 101.07561 ?  948  GLU   A CD  1 
ATOM   7521  O  OE1 . GLU   A 1 950  ? -68.07300  78.04900  -29.37900 1.000 99.15358  ?  948  GLU   A OE1 1 
ATOM   7522  O  OE2 . GLU   A 1 950  ? -68.70300  80.15000  -29.29800 1.000 100.57819 -1 948  GLU   A OE2 1 
ATOM   7523  N  N   . TRP   A 1 951  ? -63.28700  78.07000  -26.73800 1.000 50.78581  ?  949  TRP   A N   1 
ATOM   7524  C  CA  . TRP   A 1 951  ? -61.89400  77.88700  -27.12800 1.000 46.78125  ?  949  TRP   A CA  1 
ATOM   7525  C  C   . TRP   A 1 951  ? -61.55500  76.41900  -27.35100 1.000 47.50492  ?  949  TRP   A C   1 
ATOM   7526  O  O   . TRP   A 1 951  ? -60.60300  76.11500  -28.08100 1.000 64.89519  ?  949  TRP   A O   1 
ATOM   7527  C  CB  . TRP   A 1 951  ? -60.97100  78.48800  -26.06400 1.000 48.02971  ?  949  TRP   A CB  1 
ATOM   7528  C  CG  . TRP   A 1 951  ? -59.50500  78.39300  -26.38600 1.000 53.56774  ?  949  TRP   A CG  1 
ATOM   7529  C  CD1 . TRP   A 1 951  ? -58.78900  79.21600  -27.20700 1.000 52.05682  ?  949  TRP   A CD1 1 
ATOM   7530  C  CD2 . TRP   A 1 951  ? -58.57600  77.42600  -25.88000 1.000 56.02346  ?  949  TRP   A CD2 1 
ATOM   7531  N  NE1 . TRP   A 1 951  ? -57.47500  78.81800  -27.24900 1.000 59.47306  ?  949  TRP   A NE1 1 
ATOM   7532  C  CE2 . TRP   A 1 951  ? -57.31800  77.72100  -26.44300 1.000 61.44393  ?  949  TRP   A CE2 1 
ATOM   7533  C  CE3 . TRP   A 1 951  ? -58.68600  76.33800  -25.00900 1.000 50.36037  ?  949  TRP   A CE3 1 
ATOM   7534  C  CZ2 . TRP   A 1 951  ? -56.17900  76.96700  -26.16300 1.000 59.38786  ?  949  TRP   A CZ2 1 
ATOM   7535  C  CZ3 . TRP   A 1 951  ? -57.55500  75.59100  -24.73300 1.000 50.61580  ?  949  TRP   A CZ3 1 
ATOM   7536  C  CH2 . TRP   A 1 951  ? -56.31800  75.90900  -25.30800 1.000 53.60575  ?  949  TRP   A CH2 1 
ATOM   7537  N  N   . PHE   A 1 952  ? -62.31600  75.50200  -26.74900 1.000 42.00974  ?  950  PHE   A N   1 
ATOM   7538  C  CA  . PHE   A 1 952  ? -62.06800  74.08100  -26.95300 1.000 63.27617  ?  950  PHE   A CA  1 
ATOM   7539  C  C   . PHE   A 1 952  ? -62.39300  73.64100  -28.37300 1.000 58.17976  ?  950  PHE   A C   1 
ATOM   7540  O  O   . PHE   A 1 952  ? -61.97500  72.55400  -28.78500 1.000 54.25436  ?  950  PHE   A O   1 
ATOM   7541  C  CB  . PHE   A 1 952  ? -62.87600  73.25500  -25.95200 1.000 74.74898  ?  950  PHE   A CB  1 
ATOM   7542  C  CG  . PHE   A 1 952  ? -62.40500  73.39100  -24.53000 1.000 51.47355  ?  950  PHE   A CG  1 
ATOM   7543  C  CD1 . PHE   A 1 952  ? -61.14300  73.89200  -24.24100 1.000 56.70088  ?  950  PHE   A CD1 1 
ATOM   7544  C  CD2 . PHE   A 1 952  ? -63.22300  73.01000  -23.48000 1.000 39.66889  ?  950  PHE   A CD2 1 
ATOM   7545  C  CE1 . PHE   A 1 952  ? -60.71000  74.01200  -22.93100 1.000 58.10743  ?  950  PHE   A CE1 1 
ATOM   7546  C  CE2 . PHE   A 1 952  ? -62.79600  73.12800  -22.17000 1.000 65.01073  ?  950  PHE   A CE2 1 
ATOM   7547  C  CZ  . PHE   A 1 952  ? -61.54000  73.63000  -21.89500 1.000 69.90494  ?  950  PHE   A CZ  1 
ATOM   7548  N  N   . ALA   A 1 953  ? -63.12500  74.45600  -29.12700 1.000 67.04381  ?  951  ALA   A N   1 
ATOM   7549  C  CA  . ALA   A 1 953  ? -63.42300  74.17400  -30.52100 1.000 75.03839  ?  951  ALA   A CA  1 
ATOM   7550  C  C   . ALA   A 1 953  ? -62.54800  74.97600  -31.47200 1.000 70.87535  ?  951  ALA   A C   1 
ATOM   7551  O  O   . ALA   A 1 953  ? -62.85200  75.04900  -32.66700 1.000 63.81767  ?  951  ALA   A O   1 
ATOM   7552  C  CB  . ALA   A 1 953  ? -64.90100  74.44400  -30.80900 1.000 72.83895  ?  951  ALA   A CB  1 
ATOM   7553  N  N   . SER   A 1 954  ? -61.47300  75.57600  -30.97100 1.000 61.19540  ?  952  SER   A N   1 
ATOM   7554  C  CA  . SER   A 1 954  ? -60.60100  76.40400  -31.79200 1.000 66.89430  ?  952  SER   A CA  1 
ATOM   7555  C  C   . SER   A 1 954  ? -59.61800  75.52000  -32.55500 1.000 81.32518  ?  952  SER   A C   1 
ATOM   7556  O  O   . SER   A 1 954  ? -59.71000  74.28900  -32.55400 1.000 72.17925  ?  952  SER   A O   1 
ATOM   7557  C  CB  . SER   A 1 954  ? -59.87400  77.43100  -30.92600 1.000 63.66679  ?  952  SER   A CB  1 
ATOM   7558  O  OG  . SER   A 1 954  ? -58.99500  76.80300  -30.00500 1.000 60.00349  ?  952  SER   A OG  1 
ATOM   7559  N  N   . ASP   A 1 955  ? -58.65900  76.15700  -33.22300 1.000 84.58409  ?  953  ASP   A N   1 
ATOM   7560  C  CA  . ASP   A 1 955  ? -57.56000  75.44700  -33.86100 1.000 75.40767  ?  953  ASP   A CA  1 
ATOM   7561  C  C   . ASP   A 1 955  ? -56.36100  75.29100  -32.94400 1.000 66.80844  ?  953  ASP   A C   1 
ATOM   7562  O  O   . ASP   A 1 955  ? -55.62100  74.30800  -33.06200 1.000 66.07272  ?  953  ASP   A O   1 
ATOM   7563  C  CB  . ASP   A 1 955  ? -57.12900  76.18300  -35.12600 1.000 71.55146  ?  953  ASP   A CB  1 
ATOM   7564  C  CG  . ASP   A 1 955  ? -58.26300  76.37100  -36.08700 1.000 95.19633  ?  953  ASP   A CG  1 
ATOM   7565  O  OD1 . ASP   A 1 955  ? -59.42900  76.40900  -35.63600 1.000 107.99961 ?  953  ASP   A OD1 1 
ATOM   7566  O  OD2 . ASP   A 1 955  ? -57.98500  76.45900  -37.29700 1.000 101.80563 -1 953  ASP   A OD2 1 
ATOM   7567  N  N   . GLU   A 1 956  ? -56.15000  76.25300  -32.04500 1.000 62.78213  ?  954  GLU   A N   1 
ATOM   7568  C  CA  . GLU   A 1 956  ? -55.08400  76.14000  -31.05800 1.000 54.03347  ?  954  GLU   A CA  1 
ATOM   7569  C  C   . GLU   A 1 956  ? -55.30100  74.93500  -30.15100 1.000 60.64331  ?  954  GLU   A C   1 
ATOM   7570  O  O   . GLU   A 1 956  ? -54.35000  74.21600  -29.82200 1.000 65.25935  ?  954  GLU   A O   1 
ATOM   7571  C  CB  . GLU   A 1 956  ? -55.01400  77.43000  -30.24400 1.000 40.21454  ?  954  GLU   A CB  1 
ATOM   7572  C  CG  . GLU   A 1 956  ? -53.83600  77.54300  -29.31000 1.000 61.62908  ?  954  GLU   A CG  1 
ATOM   7573  C  CD  . GLU   A 1 956  ? -53.71600  78.93500  -28.72100 1.000 80.52169  ?  954  GLU   A CD  1 
ATOM   7574  O  OE1 . GLU   A 1 956  ? -54.40100  79.85300  -29.22100 1.000 57.10622  ?  954  GLU   A OE1 1 
ATOM   7575  O  OE2 . GLU   A 1 956  ? -52.94000  79.11200  -27.75900 1.000 89.68518  -1 954  GLU   A OE2 1 
ATOM   7576  N  N   . TYR   A 1 957  ? -56.55300  74.69700  -29.74200 1.000 53.01694  ?  955  TYR   A N   1 
ATOM   7577  C  CA  . TYR   A 1 957  ? -56.85700  73.54900  -28.89300 1.000 51.57956  ?  955  TYR   A CA  1 
ATOM   7578  C  C   . TYR   A 1 957  ? -56.48300  72.23900  -29.57700 1.000 58.71353  ?  955  TYR   A C   1 
ATOM   7579  O  O   . TYR   A 1 957  ? -55.95800  71.32200  -28.93500 1.000 58.87414  ?  955  TYR   A O   1 
ATOM   7580  C  CB  . TYR   A 1 957  ? -58.34000  73.55900  -28.51600 1.000 48.49883  ?  955  TYR   A CB  1 
ATOM   7581  C  CG  . TYR   A 1 957  ? -58.76900  72.39400  -27.64800 1.000 49.21508  ?  955  TYR   A CG  1 
ATOM   7582  C  CD1 . TYR   A 1 957  ? -58.69900  72.47200  -26.26300 1.000 41.09932  ?  955  TYR   A CD1 1 
ATOM   7583  C  CD2 . TYR   A 1 957  ? -59.24600  71.21800  -28.21400 1.000 66.76562  ?  955  TYR   A CD2 1 
ATOM   7584  C  CE1 . TYR   A 1 957  ? -59.08700  71.41000  -25.46900 1.000 62.10117  ?  955  TYR   A CE1 1 
ATOM   7585  C  CE2 . TYR   A 1 957  ? -59.63500  70.15300  -27.42900 1.000 64.43660  ?  955  TYR   A CE2 1 
ATOM   7586  C  CZ  . TYR   A 1 957  ? -59.55500  70.25300  -26.05800 1.000 63.30813  ?  955  TYR   A CZ  1 
ATOM   7587  O  OH  . TYR   A 1 957  ? -59.94500  69.19000  -25.27700 1.000 65.45054  ?  955  TYR   A OH  1 
ATOM   7588  N  N   . GLU   A 1 958  ? -56.75300  72.13000  -30.88100 1.000 61.25097  ?  956  GLU   A N   1 
ATOM   7589  C  CA  . GLU   A 1 958  ? -56.37500  70.92600  -31.61300 1.000 59.09864  ?  956  GLU   A CA  1 
ATOM   7590  C  C   . GLU   A 1 958  ? -54.86200  70.78200  -31.71100 1.000 50.29018  ?  956  GLU   A C   1 
ATOM   7591  O  O   . GLU   A 1 958  ? -54.34900  69.65700  -31.71300 1.000 47.54467  ?  956  GLU   A O   1 
ATOM   7592  C  CB  . GLU   A 1 958  ? -57.00600  70.93900  -33.00500 1.000 49.42353  ?  956  GLU   A CB  1 
ATOM   7593  C  CG  . GLU   A 1 958  ? -58.51100  70.72100  -33.00100 1.000 58.74929  ?  956  GLU   A CG  1 
ATOM   7594  C  CD  . GLU   A 1 958  ? -58.89400  69.30300  -32.62000 1.000 76.39198  ?  956  GLU   A CD  1 
ATOM   7595  O  OE1 . GLU   A 1 958  ? -58.20000  68.36200  -33.05800 1.000 73.60663  ?  956  GLU   A OE1 1 
ATOM   7596  O  OE2 . GLU   A 1 958  ? -59.88600  69.12900  -31.87900 1.000 72.33788  -1 956  GLU   A OE2 1 
ATOM   7597  N  N   . GLN   A 1 959  ? -54.13500  71.89900  -31.79300 1.000 41.39635  ?  957  GLN   A N   1 
ATOM   7598  C  CA  . GLN   A 1 959  ? -52.67800  71.82900  -31.77000 1.000 44.92190  ?  957  GLN   A CA  1 
ATOM   7599  C  C   . GLN   A 1 959  ? -52.17500  71.33300  -30.42100 1.000 59.00427  ?  957  GLN   A C   1 
ATOM   7600  O  O   . GLN   A 1 959  ? -51.25400  70.51000  -30.35700 1.000 59.51456  ?  957  GLN   A O   1 
ATOM   7601  C  CB  . GLN   A 1 959  ? -52.07500  73.19900  -32.08400 1.000 47.85964  ?  957  GLN   A CB  1 
ATOM   7602  C  CG  . GLN   A 1 959  ? -52.45000  73.76300  -33.44200 1.000 66.01417  ?  957  GLN   A CG  1 
ATOM   7603  C  CD  . GLN   A 1 959  ? -51.81900  75.11900  -33.69800 1.000 79.69521  ?  957  GLN   A CD  1 
ATOM   7604  O  OE1 . GLN   A 1 959  ? -50.69300  75.38300  -33.27500 1.000 84.57649  ?  957  GLN   A OE1 1 
ATOM   7605  N  NE2 . GLN   A 1 959  ? -52.54700  75.98900  -34.38800 1.000 79.24489  ?  957  GLN   A NE2 1 
ATOM   7606  N  N   . GLN   A 1 960  ? -52.77300  71.82200  -29.33200 1.000 57.89034  ?  958  GLN   A N   1 
ATOM   7607  C  CA  . GLN   A 1 960  ? -52.29800  71.45800  -28.00200 1.000 41.91540  ?  958  GLN   A CA  1 
ATOM   7608  C  C   . GLN   A 1 960  ? -52.62100  70.00700  -27.67400 1.000 41.19821  ?  958  GLN   A C   1 
ATOM   7609  O  O   . GLN   A 1 960  ? -51.81000  69.31200  -27.05200 1.000 62.45094  ?  958  GLN   A O   1 
ATOM   7610  C  CB  . GLN   A 1 960  ? -52.89900  72.39500  -26.95600 1.000 39.81036  ?  958  GLN   A CB  1 
ATOM   7611  C  CG  . GLN   A 1 960  ? -52.49800  73.85200  -27.12000 1.000 49.27615  ?  958  GLN   A CG  1 
ATOM   7612  C  CD  . GLN   A 1 960  ? -52.84800  74.68900  -25.90600 1.000 44.38032  ?  958  GLN   A CD  1 
ATOM   7613  O  OE1 . GLN   A 1 960  ? -53.41600  74.18900  -24.93500 1.000 47.67461  ?  958  GLN   A OE1 1 
ATOM   7614  N  NE2 . GLN   A 1 960  ? -52.50400  75.97100  -25.95100 1.000 50.38530  ?  958  GLN   A NE2 1 
ATOM   7615  N  N   . ILE   A 1 961  ? -53.79800  69.52800  -28.08300 1.000 31.27673  ?  959  ILE   A N   1 
ATOM   7616  C  CA  . ILE   A 1 961  ? -54.13900  68.13600  -27.82600 1.000 43.53218  ?  959  ILE   A CA  1 
ATOM   7617  C  C   . ILE   A 1 961  ? -53.26600  67.20000  -28.64900 1.000 50.97113  ?  959  ILE   A C   1 
ATOM   7618  O  O   . ILE   A 1 961  ? -53.08800  66.03400  -28.27800 1.000 52.58351  ?  959  ILE   A O   1 
ATOM   7619  C  CB  . ILE   A 1 961  ? -55.63800  67.88700  -28.08700 1.000 42.95744  ?  959  ILE   A CB  1 
ATOM   7620  C  CG1 . ILE   A 1 961  ? -56.10600  66.63800  -27.33700 1.000 41.80768  ?  959  ILE   A CG1 1 
ATOM   7621  C  CG2 . ILE   A 1 961  ? -55.91400  67.74800  -29.57700 1.000 49.53755  ?  959  ILE   A CG2 1 
ATOM   7622  C  CD1 . ILE   A 1 961  ? -57.59700  66.59600  -27.09500 1.000 58.29927  ?  959  ILE   A CD1 1 
ATOM   7623  N  N   . ALA   A 1 962  ? -52.69900  67.68700  -29.75600 1.000 55.39179  ?  960  ALA   A N   1 
ATOM   7624  C  CA  . ALA   A 1 962  ? -51.75900  66.87600  -30.51800 1.000 47.18323  ?  960  ALA   A CA  1 
ATOM   7625  C  C   . ALA   A 1 962  ? -50.42200  66.75600  -29.80100 1.000 56.72070  ?  960  ALA   A C   1 
ATOM   7626  O  O   . ALA   A 1 962  ? -49.71800  65.75400  -29.97100 1.000 65.51162  ?  960  ALA   A O   1 
ATOM   7627  C  CB  . ALA   A 1 962  ? -51.56300  67.46500  -31.91400 1.000 40.83358  ?  960  ALA   A CB  1 
ATOM   7628  N  N   . TYR   A 1 963  ? -50.05700  67.76300  -29.00200 1.000 51.79620  ?  961  TYR   A N   1 
ATOM   7629  C  CA  . TYR   A 1 963  ? -48.81900  67.68300  -28.23500 1.000 45.11658  ?  961  TYR   A CA  1 
ATOM   7630  C  C   . TYR   A 1 963  ? -48.85800  66.51600  -27.25800 1.000 51.86326  ?  961  TYR   A C   1 
ATOM   7631  O  O   . TYR   A 1 963  ? -47.89000  65.75600  -27.15000 1.000 68.13402  ?  961  TYR   A O   1 
ATOM   7632  C  CB  . TYR   A 1 963  ? -48.56500  68.99600  -27.49100 1.000 40.44997  ?  961  TYR   A CB  1 
ATOM   7633  C  CG  . TYR   A 1 963  ? -47.42200  68.92000  -26.50100 1.000 41.20315  ?  961  TYR   A CG  1 
ATOM   7634  C  CD1 . TYR   A 1 963  ? -46.10400  68.86000  -26.93600 1.000 46.31759  ?  961  TYR   A CD1 1 
ATOM   7635  C  CD2 . TYR   A 1 963  ? -47.66000  68.90800  -25.13200 1.000 40.68522  ?  961  TYR   A CD2 1 
ATOM   7636  C  CE1 . TYR   A 1 963  ? -45.05500  68.78900  -26.03600 1.000 58.56978  ?  961  TYR   A CE1 1 
ATOM   7637  C  CE2 . TYR   A 1 963  ? -46.61700  68.83700  -24.22400 1.000 54.03638  ?  961  TYR   A CE2 1 
ATOM   7638  C  CZ  . TYR   A 1 963  ? -45.31500  68.77800  -24.68200 1.000 63.38223  ?  961  TYR   A CZ  1 
ATOM   7639  O  OH  . TYR   A 1 963  ? -44.27000  68.70800  -23.78700 1.000 55.01053  ?  961  TYR   A OH  1 
ATOM   7640  N  N   . TRP   A 1 964  ? -49.97400  66.34900  -26.54900 1.000 47.98446  ?  962  TRP   A N   1 
ATOM   7641  C  CA  . TRP   A 1 964  ? -50.08800  65.24600  -25.60300 1.000 54.98175  ?  962  TRP   A CA  1 
ATOM   7642  C  C   . TRP   A 1 964  ? -50.29500  63.90900  -26.30300 1.000 59.74316  ?  962  TRP   A C   1 
ATOM   7643  O  O   . TRP   A 1 964  ? -49.84600  62.87500  -25.79600 1.000 65.37538  ?  962  TRP   A O   1 
ATOM   7644  C  CB  . TRP   A 1 964  ? -51.23100  65.51600  -24.62400 1.000 51.52752  ?  962  TRP   A CB  1 
ATOM   7645  C  CG  . TRP   A 1 964  ? -51.09800  66.82700  -23.91600 1.000 44.99698  ?  962  TRP   A CG  1 
ATOM   7646  C  CD1 . TRP   A 1 964  ? -51.85400  67.94400  -24.11200 1.000 44.47035  ?  962  TRP   A CD1 1 
ATOM   7647  C  CD2 . TRP   A 1 964  ? -50.13700  67.16400  -22.90800 1.000 48.57754  ?  962  TRP   A CD2 1 
ATOM   7648  N  NE1 . TRP   A 1 964  ? -51.43100  68.95400  -23.28200 1.000 39.63350  ?  962  TRP   A NE1 1 
ATOM   7649  C  CE2 . TRP   A 1 964  ? -50.37700  68.50000  -22.53400 1.000 39.62097  ?  962  TRP   A CE2 1 
ATOM   7650  C  CE3 . TRP   A 1 964  ? -49.09900  66.46400  -22.28400 1.000 46.58862  ?  962  TRP   A CE3 1 
ATOM   7651  C  CZ2 . TRP   A 1 964  ? -49.61800  69.15200  -21.56300 1.000 44.16402  ?  962  TRP   A CZ2 1 
ATOM   7652  C  CZ3 . TRP   A 1 964  ? -48.34700  67.11200  -21.32100 1.000 42.78220  ?  962  TRP   A CZ3 1 
ATOM   7653  C  CH2 . TRP   A 1 964  ? -48.61000  68.44300  -20.97000 1.000 37.86769  ?  962  TRP   A CH2 1 
ATOM   7654  N  N   . LYS   A 1 965  ? -50.96200  63.90400  -27.46000 1.000 64.21171  ?  963  LYS   A N   1 
ATOM   7655  C  CA  . LYS   A 1 965  ? -51.16800  62.65200  -28.18100 1.000 64.60594  ?  963  LYS   A CA  1 
ATOM   7656  C  C   . LYS   A 1 965  ? -49.87300  62.14200  -28.79800 1.000 63.85303  ?  963  LYS   A C   1 
ATOM   7657  O  O   . LYS   A 1 965  ? -49.66400  60.92700  -28.87800 1.000 82.27701  ?  963  LYS   A O   1 
ATOM   7658  C  CB  . LYS   A 1 965  ? -52.23800  62.83500  -29.25700 1.000 62.59289  ?  963  LYS   A CB  1 
ATOM   7659  C  CG  . LYS   A 1 965  ? -52.58100  61.56700  -30.02900 1.000 66.51600  ?  963  LYS   A CG  1 
ATOM   7660  C  CD  . LYS   A 1 965  ? -54.07600  61.50200  -30.31200 1.000 76.48896  ?  963  LYS   A CD  1 
ATOM   7661  C  CE  . LYS   A 1 965  ? -54.42800  60.41700  -31.32400 1.000 69.24900  ?  963  LYS   A CE  1 
ATOM   7662  N  NZ  . LYS   A 1 965  ? -54.42400  59.03700  -30.76400 1.000 69.81389  ?  963  LYS   A NZ  1 
ATOM   7663  N  N   . THR   A 1 966  ? -48.99600  63.04300  -29.23700 1.000 54.82012  ?  964  THR   A N   1 
ATOM   7664  C  CA  . THR   A 1 966  ? -47.71600  62.66100  -29.81700 1.000 65.19076  ?  964  THR   A CA  1 
ATOM   7665  C  C   . THR   A 1 966  ? -46.61900  62.51600  -28.76900 1.000 64.01684  ?  964  THR   A C   1 
ATOM   7666  O  O   . THR   A 1 966  ? -45.48900  62.15600  -29.11800 1.000 73.14816  ?  964  THR   A O   1 
ATOM   7667  C  CB  . THR   A 1 966  ? -47.28600  63.68300  -30.87500 1.000 50.92871  ?  964  THR   A CB  1 
ATOM   7668  O  OG1 . THR   A 1 966  ? -48.44600  64.29100  -31.45600 1.000 75.83658  ?  964  THR   A OG1 1 
ATOM   7669  C  CG2 . THR   A 1 966  ? -46.49500  62.99800  -31.97800 1.000 56.07523  ?  964  THR   A CG2 1 
ATOM   7670  N  N   . LEU   A 1 967  ? -46.92700  62.77900  -27.49700 1.000 60.55540  ?  965  LEU   A N   1 
ATOM   7671  C  CA  . LEU   A 1 967  ? -45.96700  62.67400  -26.40500 1.000 60.46333  ?  965  LEU   A CA  1 
ATOM   7672  C  C   . LEU   A 1 967  ? -46.31700  61.54400  -25.44500 1.000 56.64430  ?  965  LEU   A C   1 
ATOM   7673  O  O   . LEU   A 1 967  ? -45.49600  60.65400  -25.21000 1.000 55.07682  ?  965  LEU   A O   1 
ATOM   7674  C  CB  . LEU   A 1 967  ? -45.89300  64.00900  -25.65300 1.000 50.89692  ?  965  LEU   A CB  1 
ATOM   7675  C  CG  . LEU   A 1 967  ? -45.20900  64.02900  -24.28600 1.000 51.67873  ?  965  LEU   A CG  1 
ATOM   7676  C  CD1 . LEU   A 1 967  ? -43.70400  64.15500  -24.44700 1.000 51.11978  ?  965  LEU   A CD1 1 
ATOM   7677  C  CD2 . LEU   A 1 967  ? -45.77200  65.15200  -23.42500 1.000 35.92451  ?  965  LEU   A CD2 1 
ATOM   7678  N  N   . LEU   A 1 968  ? -47.52600  61.55400  -24.88500 1.000 63.90451  ?  966  LEU   A N   1 
ATOM   7679  C  CA  . LEU   A 1 968  ? -47.94200  60.57400  -23.89000 1.000 57.28964  ?  966  LEU   A CA  1 
ATOM   7680  C  C   . LEU   A 1 968  ? -48.41000  59.26100  -24.50000 1.000 63.17367  ?  966  LEU   A C   1 
ATOM   7681  O  O   . LEU   A 1 968  ? -48.98900  58.43700  -23.78400 1.000 76.46704  ?  966  LEU   A O   1 
ATOM   7682  C  CB  . LEU   A 1 968  ? -49.05400  61.15100  -23.01700 1.000 38.25634  ?  966  LEU   A CB  1 
ATOM   7683  C  CG  . LEU   A 1 968  ? -48.71200  62.43500  -22.27100 1.000 52.45062  ?  966  LEU   A CG  1 
ATOM   7684  C  CD1 . LEU   A 1 968  ? -49.94900  62.91200  -21.56800 1.000 56.07745  ?  966  LEU   A CD1 1 
ATOM   7685  C  CD2 . LEU   A 1 968  ? -47.57900  62.20300  -21.28400 1.000 57.36957  ?  966  LEU   A CD2 1 
ATOM   7686  N  N   . GLN   A 1 969  ? -48.19300  59.04600  -25.79200 1.000 52.98313  ?  967  GLN   A N   1 
ATOM   7687  C  CA  . GLN   A 1 969  ? -48.47400  57.76100  -26.41200 1.000 66.44665  ?  967  GLN   A CA  1 
ATOM   7688  C  C   . GLN   A 1 969  ? -47.17300  57.00000  -26.61900 1.000 67.41610  ?  967  GLN   A C   1 
ATOM   7689  O  O   . GLN   A 1 969  ? -46.13100  57.59400  -26.90900 1.000 70.48844  ?  967  GLN   A O   1 
ATOM   7690  C  CB  . GLN   A 1 969  ? -49.21200  57.92600  -27.74200 1.000 90.92099  ?  967  GLN   A CB  1 
ATOM   7691  C  CG  . GLN   A 1 969  ? -50.68800  58.25200  -27.57900 1.000 81.43814  ?  967  GLN   A CG  1 
ATOM   7692  C  CD  . GLN   A 1 969  ? -51.56300  57.51100  -28.57000 1.000 87.24251  ?  967  GLN   A CD  1 
ATOM   7693  O  OE1 . GLN   A 1 969  ? -52.27900  58.12200  -29.36400 1.000 89.37835  ?  967  GLN   A OE1 1 
ATOM   7694  N  NE2 . GLN   A 1 969  ? -51.51600  56.18500  -28.52200 1.000 83.67844  ?  967  GLN   A NE2 1 
ATOM   7695  N  N   . GLY   A 1 970  ? -47.25000  55.68800  -26.47000 1.000 71.62130  ?  968  GLY   A N   1 
ATOM   7696  C  CA  . GLY   A 1 970  ? -46.10000  54.81200  -26.41800 1.000 63.69529  ?  968  GLY   A CA  1 
ATOM   7697  C  C   . GLY   A 1 970  ? -45.97100  54.18400  -25.04700 1.000 77.74732  ?  968  GLY   A C   1 
ATOM   7698  O  O   . GLY   A 1 970  ? -46.83800  54.32900  -24.17900 1.000 86.16647  ?  968  GLY   A O   1 
ATOM   7699  N  N   . GLU   A 1 971  ? -44.86700  53.46800  -24.85300 1.000 79.86853  ?  969  GLU   A N   1 
ATOM   7700  C  CA  . GLU   A 1 971  ? -44.56900  52.86600  -23.55600 1.000 81.79685  ?  969  GLU   A CA  1 
ATOM   7701  C  C   . GLU   A 1 971  ? -44.04600  53.96800  -22.64200 1.000 81.73646  ?  969  GLU   A C   1 
ATOM   7702  O  O   . GLU   A 1 971  ? -42.87400  54.34500  -22.70600 1.000 81.05953  ?  969  GLU   A O   1 
ATOM   7703  C  CB  . GLU   A 1 971  ? -43.56700  51.73000  -23.70700 1.000 81.99802  ?  969  GLU   A CB  1 
ATOM   7704  C  CG  . GLU   A 1 971  ? -43.58300  50.73400  -22.56000 1.000 81.27991  ?  969  GLU   A CG  1 
ATOM   7705  C  CD  . GLU   A 1 971  ? -44.22100  49.40700  -22.93600 1.000 92.42882  ?  969  GLU   A CD  1 
ATOM   7706  O  OE1 . GLU   A 1 971  ? -45.39000  49.39900  -23.37900 1.000 95.54944  ?  969  GLU   A OE1 1 
ATOM   7707  O  OE2 . GLU   A 1 971  ? -43.54500  48.36800  -22.78700 1.000 90.08600  -1 969  GLU   A OE2 1 
ATOM   7708  N  N   . LEU   A 1 972  ? -44.92900  54.50200  -21.80100 1.000 76.95228  ?  970  LEU   A N   1 
ATOM   7709  C  CA  . LEU   A 1 972  ? -44.56300  55.58100  -20.90400 1.000 62.74106  ?  970  LEU   A CA  1 
ATOM   7710  C  C   . LEU   A 1 972  ? -43.65000  55.05900  -19.79800 1.000 64.95411  ?  970  LEU   A C   1 
ATOM   7711  O  O   . LEU   A 1 972  ? -43.60600  53.85400  -19.53600 1.000 82.25770  ?  970  LEU   A O   1 
ATOM   7712  C  CB  . LEU   A 1 972  ? -45.81600  56.21200  -20.30400 1.000 67.14645  ?  970  LEU   A CB  1 
ATOM   7713  C  CG  . LEU   A 1 972  ? -46.90500  56.60400  -21.30500 1.000 70.55293  ?  970  LEU   A CG  1 
ATOM   7714  C  CD1 . LEU   A 1 972  ? -48.14900  55.73900  -21.12700 1.000 70.03554  ?  970  LEU   A CD1 1 
ATOM   7715  C  CD2 . LEU   A 1 972  ? -47.24100  58.08200  -21.17700 1.000 59.37670  ?  970  LEU   A CD2 1 
ATOM   7716  N  N   . PRO   A 1 973  ? -42.89800  55.94400  -19.14400 1.000 57.32321  ?  971  PRO   A N   1 
ATOM   7717  C  CA  . PRO   A 1 973  ? -42.05700  55.50400  -18.02600 1.000 61.50602  ?  971  PRO   A CA  1 
ATOM   7718  C  C   . PRO   A 1 973  ? -42.89500  54.93300  -16.89200 1.000 70.66202  ?  971  PRO   A C   1 
ATOM   7719  O  O   . PRO   A 1 973  ? -44.08200  55.23100  -16.74000 1.000 67.21862  ?  971  PRO   A O   1 
ATOM   7720  C  CB  . PRO   A 1 973  ? -41.33400  56.78500  -17.59800 1.000 64.85582  ?  971  PRO   A CB  1 
ATOM   7721  C  CG  . PRO   A 1 973  ? -41.34100  57.63800  -18.81300 1.000 64.13076  ?  971  PRO   A CG  1 
ATOM   7722  C  CD  . PRO   A 1 973  ? -42.63500  57.34600  -19.51300 1.000 60.38999  ?  971  PRO   A CD  1 
ATOM   7723  N  N   . ALA   A 1 974  ? -42.25300  54.08900  -16.09000 1.000 67.63639  ?  972  ALA   A N   1 
ATOM   7724  C  CA  . ALA   A 1 974  ? -42.90000  53.41000  -14.97400 1.000 63.45527  ?  972  ALA   A CA  1 
ATOM   7725  C  C   . ALA   A 1 974  ? -42.11200  53.70600  -13.70600 1.000 61.20315  ?  972  ALA   A C   1 
ATOM   7726  O  O   . ALA   A 1 974  ? -40.96000  53.28000  -13.57400 1.000 70.66524  ?  972  ALA   A O   1 
ATOM   7727  C  CB  . ALA   A 1 974  ? -42.99000  51.90400  -15.22400 1.000 61.72153  ?  972  ALA   A CB  1 
ATOM   7728  N  N   . VAL   A 1 975  ? -42.73100  54.43000  -12.77800 1.000 45.60142  ?  973  VAL   A N   1 
ATOM   7729  C  CA  . VAL   A 1 975  ? -42.10100  54.81000  -11.52000 1.000 46.78228  ?  973  VAL   A CA  1 
ATOM   7730  C  C   . VAL   A 1 975  ? -42.64500  53.87900  -10.44200 1.000 59.50948  ?  973  VAL   A C   1 
ATOM   7731  O  O   . VAL   A 1 975  ? -43.74100  54.09000  -9.91400  1.000 68.10088  ?  973  VAL   A O   1 
ATOM   7732  C  CB  . VAL   A 1 975  ? -42.35300  56.28200  -11.18100 1.000 39.61994  ?  973  VAL   A CB  1 
ATOM   7733  C  CG1 . VAL   A 1 975  ? -41.67300  56.64300  -9.87300  1.000 47.82985  ?  973  VAL   A CG1 1 
ATOM   7734  C  CG2 . VAL   A 1 975  ? -41.85700  57.17600  -12.30400 1.000 34.08486  ?  973  VAL   A CG2 1 
ATOM   7735  N  N   . GLN   A 1 976  ? -41.87500  52.84100  -10.11700 1.000 67.66924  ?  974  GLN   A N   1 
ATOM   7736  C  CA  . GLN   A 1 976  ? -42.20700  51.90900  -9.03900  1.000 63.11437  ?  974  GLN   A CA  1 
ATOM   7737  C  C   . GLN   A 1 976  ? -41.46000  52.37300  -7.79200  1.000 56.44574  ?  974  GLN   A C   1 
ATOM   7738  O  O   . GLN   A 1 976  ? -40.36400  51.89700  -7.48500  1.000 56.27207  ?  974  GLN   A O   1 
ATOM   7739  C  CB  . GLN   A 1 976  ? -41.83100  50.47900  -9.40400  1.000 59.68209  ?  974  GLN   A CB  1 
ATOM   7740  C  CG  . GLN   A 1 976  ? -41.92000  50.15400  -10.88000 1.000 78.37372  ?  974  GLN   A CG  1 
ATOM   7741  C  CD  . GLN   A 1 976  ? -41.47900  48.73500  -11.18700 1.000 85.71333  ?  974  GLN   A CD  1 
ATOM   7742  O  OE1 . GLN   A 1 976  ? -42.06200  47.76900  -10.69200 1.000 77.10460  ?  974  GLN   A OE1 1 
ATOM   7743  N  NE2 . GLN   A 1 976  ? -40.44000  48.60200  -12.00200 1.000 86.00984  ?  974  GLN   A NE2 1 
ATOM   7744  N  N   . LEU   A 1 977  ? -42.05800  53.31900  -7.07300  1.000 47.29060  ?  975  LEU   A N   1 
ATOM   7745  C  CA  . LEU   A 1 977  ? -41.46200  53.78900  -5.83500  1.000 52.56274  ?  975  LEU   A CA  1 
ATOM   7746  C  C   . LEU   A 1 977  ? -41.43400  52.65900  -4.80600  1.000 53.36756  ?  975  LEU   A C   1 
ATOM   7747  O  O   . LEU   A 1 977  ? -42.26100  51.74500  -4.85200  1.000 46.51267  ?  975  LEU   A O   1 
ATOM   7748  C  CB  . LEU   A 1 977  ? -42.23700  54.98400  -5.28400  1.000 42.04845  ?  975  LEU   A CB  1 
ATOM   7749  C  CG  . LEU   A 1 977  ? -41.95500  56.32500  -5.96100  1.000 48.08011  ?  975  LEU   A CG  1 
ATOM   7750  C  CD1 . LEU   A 1 977  ? -42.40200  57.47500  -5.07100  1.000 37.77466  ?  975  LEU   A CD1 1 
ATOM   7751  C  CD2 . LEU   A 1 977  ? -40.48000  56.46000  -6.32400  1.000 45.38744  ?  975  LEU   A CD2 1 
ATOM   7752  N  N   . PRO   A 1 978  ? -40.47500  52.68700  -3.87700  1.000 57.24284  ?  976  PRO   A N   1 
ATOM   7753  C  CA  . PRO   A 1 978  ? -40.41000  51.62500  -2.86600  1.000 43.84865  ?  976  PRO   A CA  1 
ATOM   7754  C  C   . PRO   A 1 978  ? -41.56600  51.70200  -1.88500  1.000 45.11209  ?  976  PRO   A C   1 
ATOM   7755  O  O   . PRO   A 1 978  ? -41.37700  52.10200  -0.73500  1.000 64.58642  ?  976  PRO   A O   1 
ATOM   7756  C  CB  . PRO   A 1 978  ? -39.06400  51.88200  -2.17600  1.000 31.05228  ?  976  PRO   A CB  1 
ATOM   7757  C  CG  . PRO   A 1 978  ? -38.81400  53.33900  -2.37900  1.000 35.94801  ?  976  PRO   A CG  1 
ATOM   7758  C  CD  . PRO   A 1 978  ? -39.37600  53.65800  -3.73400  1.000 53.84022  ?  976  PRO   A CD  1 
ATOM   7759  N  N   . THR   A 1 979  ? -42.76200  51.33100  -2.32600  1.000 42.08606  ?  977  THR   A N   1 
ATOM   7760  C  CA  . THR   A 1 979  ? -43.95100  51.37000  -1.48900  1.000 48.07931  ?  977  THR   A CA  1 
ATOM   7761  C  C   . THR   A 1 979  ? -44.25400  49.98400  -0.93100  1.000 46.65401  ?  977  THR   A C   1 
ATOM   7762  O  O   . THR   A 1 979  ? -43.60600  48.99000  -1.26800  1.000 47.11674  ?  977  THR   A O   1 
ATOM   7763  C  CB  . THR   A 1 979  ? -45.15900  51.89100  -2.27800  1.000 47.81305  ?  977  THR   A CB  1 
ATOM   7764  O  OG1 . THR   A 1 979  ? -45.75300  50.81400  -3.01400  1.000 39.83315  ?  977  THR   A OG1 1 
ATOM   7765  C  CG2 . THR   A 1 979  ? -44.73200  52.97900  -3.24900  1.000 54.90987  ?  977  THR   A CG2 1 
ATOM   7766  N  N   . LYS   A 1 980  ? -45.25800  49.93100  -0.06000  1.000 60.17116  ?  978  LYS   A N   1 
ATOM   7767  C  CA  . LYS   A 1 980  ? -45.77100  48.66100  0.42400   1.000 49.91984  ?  978  LYS   A CA  1 
ATOM   7768  C  C   . LYS   A 1 980  ? -46.72700  48.06500  -0.60600  1.000 56.33257  ?  978  LYS   A C   1 
ATOM   7769  O  O   . LYS   A 1 980  ? -46.95500  48.62700  -1.68100  1.000 66.65653  ?  978  LYS   A O   1 
ATOM   7770  C  CB  . LYS   A 1 980  ? -46.45800  48.84000  1.77600   1.000 35.11880  ?  978  LYS   A CB  1 
ATOM   7771  C  CG  . LYS   A 1 980  ? -45.51600  49.20600  2.90900   1.000 56.10313  ?  978  LYS   A CG  1 
ATOM   7772  C  CD  . LYS   A 1 980  ? -46.22500  49.14500  4.25000   1.000 52.91038  ?  978  LYS   A CD  1 
ATOM   7773  C  CE  . LYS   A 1 980  ? -47.48600  49.99100  4.24400   1.000 44.68689  ?  978  LYS   A CE  1 
ATOM   7774  N  NZ  . LYS   A 1 980  ? -48.07900  50.12000  5.60400   1.000 44.82442  ?  978  LYS   A NZ  1 
ATOM   7775  N  N   . LYS   A 1 981  ? -47.29500  46.90800  -0.27000  1.000 63.87922  ?  979  LYS   A N   1 
ATOM   7776  C  CA  . LYS   A 1 981  ? -48.20400  46.22500  -1.17900  1.000 61.68344  ?  979  LYS   A CA  1 
ATOM   7777  C  C   . LYS   A 1 981  ? -49.40200  47.11100  -1.49600  1.000 51.60485  ?  979  LYS   A C   1 
ATOM   7778  O  O   . LYS   A 1 981  ? -50.06100  47.63700  -0.59300  1.000 53.09611  ?  979  LYS   A O   1 
ATOM   7779  C  CB  . LYS   A 1 981  ? -48.66500  44.90100  -0.57100  1.000 70.69009  ?  979  LYS   A CB  1 
ATOM   7780  N  N   . ARG   A 1 982  ? -49.67100  47.28300  -2.78100  1.000 52.52973  ?  980  ARG   A N   1 
ATOM   7781  C  CA  . ARG   A 1 982  ? -50.74500  48.17100  -3.20400  1.000 59.05554  ?  980  ARG   A CA  1 
ATOM   7782  C  C   . ARG   A 1 982  ? -52.09000  47.52800  -2.89100  1.000 56.48066  ?  980  ARG   A C   1 
ATOM   7783  O  O   . ARG   A 1 982  ? -52.31700  46.36800  -3.26400  1.000 52.93923  ?  980  ARG   A O   1 
ATOM   7784  C  CB  . ARG   A 1 982  ? -50.63300  48.46700  -4.69700  1.000 81.41480  ?  980  ARG   A CB  1 
ATOM   7785  C  CG  . ARG   A 1 982  ? -49.23600  48.86400  -5.14300  1.000 68.97606  ?  980  ARG   A CG  1 
ATOM   7786  C  CD  . ARG   A 1 982  ? -49.26500  49.47900  -6.52800  1.000 63.74535  ?  980  ARG   A CD  1 
ATOM   7787  N  NE  . ARG   A 1 982  ? -50.12000  50.65900  -6.56300  1.000 75.27099  ?  980  ARG   A NE  1 
ATOM   7788  C  CZ  . ARG   A 1 982  ? -49.68800  51.90200  -6.39900  1.000 64.95136  ?  980  ARG   A CZ  1 
ATOM   7789  N  NH1 . ARG   A 1 982  ? -48.40400  52.16900  -6.22300  1.000 63.33963  ?  980  ARG   A NH1 1 
ATOM   7790  N  NH2 . ARG   A 1 982  ? -50.56600  52.90000  -6.41100  1.000 48.01001  ?  980  ARG   A NH2 1 
ATOM   7791  N  N   . PRO   A 1 983  ? -52.98800  48.22300  -2.19400  1.000 73.61858  ?  981  PRO   A N   1 
ATOM   7792  C  CA  . PRO   A 1 983  ? -54.28900  47.63400  -1.89700  1.000 66.81334  ?  981  PRO   A CA  1 
ATOM   7793  C  C   . PRO   A 1 983  ? -55.05700  47.36800  -3.17500  1.000 75.04916  ?  981  PRO   A C   1 
ATOM   7794  O  O   . PRO   A 1 983  ? -54.81900  48.01400  -4.21700  1.000 78.86189  ?  981  PRO   A O   1 
ATOM   7795  C  CB  . PRO   A 1 983  ? -54.97600  48.70700  -1.04000  1.000 49.75789  ?  981  PRO   A CB  1 
ATOM   7796  C  CG  . PRO   A 1 983  ? -53.84600  49.47800  -0.44300  1.000 57.97759  ?  981  PRO   A CG  1 
ATOM   7797  C  CD  . PRO   A 1 983  ? -52.78200  49.49800  -1.49700  1.000 69.66507  ?  981  PRO   A CD  1 
ATOM   7798  N  N   . PRO   A 1 984  ? -55.98100  46.40600  -3.15200  1.000 78.25522  ?  982  PRO   A N   1 
ATOM   7799  C  CA  . PRO   A 1 984  ? -56.69200  46.06300  -4.39400  1.000 72.56288  ?  982  PRO   A CA  1 
ATOM   7800  C  C   . PRO   A 1 984  ? -57.51900  47.20800  -4.94500  1.000 79.58414  ?  982  PRO   A C   1 
ATOM   7801  O  O   . PRO   A 1 984  ? -57.63100  47.36100  -6.16800  1.000 83.87272  ?  982  PRO   A O   1 
ATOM   7802  C  CB  . PRO   A 1 984  ? -57.59300  44.88300  -3.97400  1.000 70.49678  ?  982  PRO   A CB  1 
ATOM   7803  C  CG  . PRO   A 1 984  ? -57.81900  45.12000  -2.51100  1.000 91.32765  ?  982  PRO   A CG  1 
ATOM   7804  C  CD  . PRO   A 1 984  ? -56.52400  45.68200  -1.99900  1.000 85.23668  ?  982  PRO   A CD  1 
ATOM   7805  N  N   . GLN   A 1 985  ? -58.07500  48.03700  -4.06400  1.000 80.59379  ?  983  GLN   A N   1 
ATOM   7806  C  CA  . GLN   A 1 985  ? -58.89800  49.16100  -4.48100  1.000 94.49579  ?  983  GLN   A CA  1 
ATOM   7807  C  C   . GLN   A 1 985  ? -58.07900  50.44100  -4.53400  1.000 92.36306  ?  983  GLN   A C   1 
ATOM   7808  O  O   . GLN   A 1 985  ? -56.85700  50.40900  -4.71500  1.000 84.23589  ?  983  GLN   A O   1 
ATOM   7809  C  CB  . GLN   A 1 985  ? -60.07100  49.33700  -3.51900  1.000 81.53311  ?  983  GLN   A CB  1 
ATOM   7810  C  CG  . GLN   A 1 985  ? -60.87200  48.07100  -3.28500  1.000 101.83918 ?  983  GLN   A CG  1 
ATOM   7811  C  CD  . GLN   A 1 985  ? -62.18800  48.08000  -4.02900  1.000 101.62373 ?  983  GLN   A CD  1 
ATOM   7812  O  OE1 . GLN   A 1 985  ? -62.71500  49.14100  -4.36000  1.000 102.20408 ?  983  GLN   A OE1 1 
ATOM   7813  N  NE2 . GLN   A 1 985  ? -62.72600  46.89700  -4.30100  1.000 90.36040  ?  983  GLN   A NE2 1 
ATOM   7814  N  N   . LEU   A 1 986  ? -58.75400  51.57100  -4.36900  1.000 93.51961  ?  984  LEU   A N   1 
ATOM   7815  C  CA  . LEU   A 1 986  ? -58.12000  52.87700  -4.26900  1.000 80.11039  ?  984  LEU   A CA  1 
ATOM   7816  C  C   . LEU   A 1 986  ? -58.27400  53.37600  -2.84000  1.000 82.69143  ?  984  LEU   A C   1 
ATOM   7817  O  O   . LEU   A 1 986  ? -59.37900  53.35200  -2.28500  1.000 78.85024  ?  984  LEU   A O   1 
ATOM   7818  C  CB  . LEU   A 1 986  ? -58.73800  53.86800  -5.26000  1.000 73.31800  ?  984  LEU   A CB  1 
ATOM   7819  C  CG  . LEU   A 1 986  ? -60.25500  54.09800  -5.23000  1.000 85.28176  ?  984  LEU   A CG  1 
ATOM   7820  C  CD1 . LEU   A 1 986  ? -60.59400  55.45600  -5.82000  1.000 73.39336  ?  984  LEU   A CD1 1 
ATOM   7821  C  CD2 . LEU   A 1 986  ? -61.00900  53.00000  -5.97200  1.000 69.36657  ?  984  LEU   A CD2 1 
ATOM   7822  N  N   . THR   A 1 987  ? -57.16700  53.80100  -2.24000  1.000 64.23269  ?  985  THR   A N   1 
ATOM   7823  C  CA  . THR   A 1 987  ? -57.16700  54.31600  -0.87800  1.000 56.20759  ?  985  THR   A CA  1 
ATOM   7824  C  C   . THR   A 1 987  ? -56.81500  55.79400  -0.89900  1.000 60.37285  ?  985  THR   A C   1 
ATOM   7825  O  O   . THR   A 1 987  ? -55.77400  56.18400  -1.44100  1.000 76.36426  ?  985  THR   A O   1 
ATOM   7826  C  CB  . THR   A 1 987  ? -56.17700  53.55500  0.00800   1.000 63.30003  ?  985  THR   A CB  1 
ATOM   7827  O  OG1 . THR   A 1 987  ? -54.87100  54.13400  -0.10800  1.000 81.42900  ?  985  THR   A OG1 1 
ATOM   7828  C  CG2 . THR   A 1 987  ? -56.10700  52.11100  -0.41900  1.000 65.05683  ?  985  THR   A CG2 1 
ATOM   7829  N  N   . PHE   A 1 988  ? -57.69000  56.61400  -0.32600  1.000 52.72927  ?  986  PHE   A N   1 
ATOM   7830  C  CA  . PHE   A 1 988  ? -57.43100  58.03900  -0.19100  1.000 44.07614  ?  986  PHE   A CA  1 
ATOM   7831  C  C   . PHE   A 1 988  ? -57.08600  58.41800  1.24300   1.000 45.63649  ?  986  PHE   A C   1 
ATOM   7832  O  O   . PHE   A 1 988  ? -57.04300  59.60700  1.56900   1.000 55.87985  ?  986  PHE   A O   1 
ATOM   7833  C  CB  . PHE   A 1 988  ? -58.62800  58.85300  -0.69700  1.000 52.72750  ?  986  PHE   A CB  1 
ATOM   7834  C  CG  . PHE   A 1 988  ? -58.77900  58.85600  -2.20300  1.000 69.77441  ?  986  PHE   A CG  1 
ATOM   7835  C  CD1 . PHE   A 1 988  ? -58.27100  57.82300  -2.97800  1.000 66.41978  ?  986  PHE   A CD1 1 
ATOM   7836  C  CD2 . PHE   A 1 988  ? -59.42300  59.90300  -2.84300  1.000 76.33811  ?  986  PHE   A CD2 1 
ATOM   7837  C  CE1 . PHE   A 1 988  ? -58.41000  57.83100  -4.35300  1.000 80.35940  ?  986  PHE   A CE1 1 
ATOM   7838  C  CE2 . PHE   A 1 988  ? -59.56400  59.91800  -4.22100  1.000 69.92521  ?  986  PHE   A CE2 1 
ATOM   7839  C  CZ  . PHE   A 1 988  ? -59.05600  58.88000  -4.97500  1.000 92.84147  ?  986  PHE   A CZ  1 
ATOM   7840  N  N   . ASP   A 1 989  ? -56.83600  57.43200  2.10500   1.000 37.90754  ?  987  ASP   A N   1 
ATOM   7841  C  CA  . ASP   A 1 989  ? -56.35700  57.69600  3.45600   1.000 39.31407  ?  987  ASP   A CA  1 
ATOM   7842  C  C   . ASP   A 1 989  ? -54.89400  58.11500  3.41200   1.000 44.66069  ?  987  ASP   A C   1 
ATOM   7843  O  O   . ASP   A 1 989  ? -54.07100  57.45900  2.76600   1.000 47.23814  ?  987  ASP   A O   1 
ATOM   7844  C  CB  . ASP   A 1 989  ? -56.52100  56.45200  4.32800   1.000 50.59742  ?  987  ASP   A CB  1 
ATOM   7845  C  CG  . ASP   A 1 989  ? -57.97200  56.09400  4.57100   1.000 60.91860  ?  987  ASP   A CG  1 
ATOM   7846  O  OD1 . ASP   A 1 989  ? -58.66900  56.87300  5.25400   1.000 84.06142  ?  987  ASP   A OD1 1 
ATOM   7847  O  OD2 . ASP   A 1 989  ? -58.41700  55.04000  4.06900   1.000 66.40500  -1 987  ASP   A OD2 1 
ATOM   7848  N  N   . GLY   A 1 990  ? -54.56100  59.20100  4.10700   1.000 40.43921  ?  988  GLY   A N   1 
ATOM   7849  C  CA  . GLY   A 1 990  ? -53.21700  59.73000  4.03200   1.000 38.64866  ?  988  GLY   A CA  1 
ATOM   7850  C  C   . GLY   A 1 990  ? -52.79700  60.44700  5.29700   1.000 38.42868  ?  988  GLY   A C   1 
ATOM   7851  O  O   . GLY   A 1 990  ? -53.56900  60.59400  6.24600   1.000 29.90643  ?  988  GLY   A O   1 
ATOM   7852  N  N   . ALA   A 1 991  ? -51.54000  60.89200  5.29500   1.000 38.05710  ?  989  ALA   A N   1 
ATOM   7853  C  CA  . ALA   A 1 991  ? -50.95800  61.65700  6.38700   1.000 37.34573  ?  989  ALA   A CA  1 
ATOM   7854  C  C   . ALA   A 1 991  ? -50.00000  62.68500  5.79500   1.000 35.71143  ?  989  ALA   A C   1 
ATOM   7855  O  O   . ALA   A 1 991  ? -49.82200  62.76700  4.57600   1.000 39.08822  ?  989  ALA   A O   1 
ATOM   7856  C  CB  . ALA   A 1 991  ? -50.25500  60.74000  7.39400   1.000 30.35237  ?  989  ALA   A CB  1 
ATOM   7857  N  N   . ILE   A 1 992  ? -49.37200  63.47100  6.66800   1.000 36.38931  ?  990  ILE   A N   1 
ATOM   7858  C  CA  . ILE   A 1 992  ? -48.54200  64.59900  6.25900   1.000 35.87817  ?  990  ILE   A CA  1 
ATOM   7859  C  C   . ILE   A 1 992  ? -47.23700  64.58000  7.04400   1.000 43.77314  ?  990  ILE   A C   1 
ATOM   7860  O  O   . ILE   A 1 992  ? -47.23700  64.37100  8.26200   1.000 45.56518  ?  990  ILE   A O   1 
ATOM   7861  C  CB  . ILE   A 1 992  ? -49.27500  65.94300  6.46800   1.000 34.10860  ?  990  ILE   A CB  1 
ATOM   7862  C  CG1 . ILE   A 1 992  ? -50.48400  66.05300  5.54000   1.000 36.70715  ?  990  ILE   A CG1 1 
ATOM   7863  C  CG2 . ILE   A 1 992  ? -48.33300  67.11900  6.24700   1.000 36.44190  ?  990  ILE   A CG2 1 
ATOM   7864  C  CD1 . ILE   A 1 992  ? -50.13600  66.44100  4.12500   1.000 50.84692  ?  990  ILE   A CD1 1 
ATOM   7865  N  N   . GLN   A 1 993  ? -46.12600  64.79000  6.33900   1.000 38.98605  ?  991  GLN   A N   1 
ATOM   7866  C  CA  . GLN   A 1 993  ? -44.83500  65.07500  6.94900   1.000 31.11830  ?  991  GLN   A CA  1 
ATOM   7867  C  C   . GLN   A 1 993  ? -44.27000  66.32700  6.29400   1.000 30.00474  ?  991  GLN   A C   1 
ATOM   7868  O  O   . GLN   A 1 993  ? -44.56500  66.61800  5.13200   1.000 47.35628  ?  991  GLN   A O   1 
ATOM   7869  C  CB  . GLN   A 1 993  ? -43.85400  63.90800  6.79300   1.000 41.93659  ?  991  GLN   A CB  1 
ATOM   7870  C  CG  . GLN   A 1 993  ? -42.79400  63.83700  7.88000   1.000 44.34586  ?  991  GLN   A CG  1 
ATOM   7871  C  CD  . GLN   A 1 993  ? -43.24700  63.02700  9.07700   1.000 53.83094  ?  991  GLN   A CD  1 
ATOM   7872  O  OE1 . GLN   A 1 993  ? -43.61300  61.85800  8.94500   1.000 56.91674  ?  991  GLN   A OE1 1 
ATOM   7873  N  NE2 . GLN   A 1 993  ? -43.23200  63.64400  10.25300  1.000 67.76715  ?  991  GLN   A NE2 1 
ATOM   7874  N  N   . MET   A 1 994  ? -43.45500  67.07100  7.04000   1.000 22.23211  ?  992  MET   A N   1 
ATOM   7875  C  CA  . MET   A 1 994  ? -43.00300  68.38000  6.59000   1.000 36.80035  ?  992  MET   A CA  1 
ATOM   7876  C  C   . MET   A 1 994  ? -41.49200  68.51000  6.72800   1.000 38.43041  ?  992  MET   A C   1 
ATOM   7877  O  O   . MET   A 1 994  ? -40.90100  68.02500  7.69700   1.000 35.73009  ?  992  MET   A O   1 
ATOM   7878  C  CB  . MET   A 1 994  ? -43.70600  69.49600  7.37700   1.000 30.78712  ?  992  MET   A CB  1 
ATOM   7879  C  CG  . MET   A 1 994  ? -43.78600  70.82700  6.64600   1.000 48.57966  ?  992  MET   A CG  1 
ATOM   7880  S  SD  . MET   A 1 994  ? -42.50900  71.99500  7.15200   1.000 81.48361  ?  992  MET   A SD  1 
ATOM   7881  C  CE  . MET   A 1 994  ? -42.84400  72.11200  8.90800   1.000 54.55235  ?  992  MET   A CE  1 
ATOM   7882  N  N   . TYR   A 1 995  ? -40.87500  69.16400  5.74400   1.000 32.19793  ?  993  TYR   A N   1 
ATOM   7883  C  CA  . TYR   A 1 995  ? -39.44900  69.46700  5.74900   1.000 25.94392  ?  993  TYR   A CA  1 
ATOM   7884  C  C   . TYR   A 1 995  ? -39.27400  70.95700  5.49900   1.000 31.52194  ?  993  TYR   A C   1 
ATOM   7885  O  O   . TYR   A 1 995  ? -39.81500  71.49400  4.52600   1.000 24.70100  ?  993  TYR   A O   1 
ATOM   7886  C  CB  . TYR   A 1 995  ? -38.69600  68.64000  4.69300   1.000 27.19675  ?  993  TYR   A CB  1 
ATOM   7887  C  CG  . TYR   A 1 995  ? -37.32400  69.17300  4.31500   1.000 33.84105  ?  993  TYR   A CG  1 
ATOM   7888  C  CD1 . TYR   A 1 995  ? -36.37200  69.46700  5.28500   1.000 38.39210  ?  993  TYR   A CD1 1 
ATOM   7889  C  CD2 . TYR   A 1 995  ? -36.97500  69.36000  2.98200   1.000 32.55184  ?  993  TYR   A CD2 1 
ATOM   7890  C  CE1 . TYR   A 1 995  ? -35.12000  69.95200  4.93900   1.000 39.76280  ?  993  TYR   A CE1 1 
ATOM   7891  C  CE2 . TYR   A 1 995  ? -35.72400  69.84000  2.62600   1.000 32.44002  ?  993  TYR   A CE2 1 
ATOM   7892  C  CZ  . TYR   A 1 995  ? -34.80200  70.13500  3.60900   1.000 36.26246  ?  993  TYR   A CZ  1 
ATOM   7893  O  OH  . TYR   A 1 995  ? -33.55900  70.61400  3.26100   1.000 29.46576  ?  993  TYR   A OH  1 
ATOM   7894  N  N   . ARG   A 1 996  ? -38.52900  71.62000  6.37900   1.000 32.81691  ?  994  ARG   A N   1 
ATOM   7895  C  CA  . ARG   A 1 996  ? -38.32700  73.06200  6.32500   1.000 25.43053  ?  994  ARG   A CA  1 
ATOM   7896  C  C   . ARG   A 1 996  ? -36.92200  73.35900  5.81600   1.000 40.10840  ?  994  ARG   A C   1 
ATOM   7897  O  O   . ARG   A 1 996  ? -35.93300  72.95200  6.43500   1.000 46.54228  ?  994  ARG   A O   1 
ATOM   7898  C  CB  . ARG   A 1 996  ? -38.55200  73.69200  7.70000   1.000 23.69194  ?  994  ARG   A CB  1 
ATOM   7899  C  CG  . ARG   A 1 996  ? -38.01200  75.11200  7.86400   1.000 28.54106  ?  994  ARG   A CG  1 
ATOM   7900  C  CD  . ARG   A 1 996  ? -38.57200  76.07600  6.82800   1.000 45.46987  ?  994  ARG   A CD  1 
ATOM   7901  N  NE  . ARG   A 1 996  ? -38.13400  77.44500  7.07100   1.000 59.26138  ?  994  ARG   A NE  1 
ATOM   7902  C  CZ  . ARG   A 1 996  ? -38.95100  78.46600  7.29000   1.000 41.46309  ?  994  ARG   A CZ  1 
ATOM   7903  N  NH1 . ARG   A 1 996  ? -40.26500  78.31900  7.25400   1.000 51.87692  ?  994  ARG   A NH1 1 
ATOM   7904  N  NH2 . ARG   A 1 996  ? -38.43700  79.66700  7.54300   1.000 50.14031  ?  994  ARG   A NH2 1 
ATOM   7905  N  N   . VAL   A 1 997  ? -36.84300  74.06300  4.69100   1.000 42.94237  ?  995  VAL   A N   1 
ATOM   7906  C  CA  . VAL   A 1 997  ? -35.58000  74.56900  4.16700   1.000 35.39160  ?  995  VAL   A CA  1 
ATOM   7907  C  C   . VAL   A 1 997  ? -35.34100  75.94200  4.78400   1.000 43.78633  ?  995  VAL   A C   1 
ATOM   7908  O  O   . VAL   A 1 997  ? -36.18700  76.83600  4.66900   1.000 42.58000  ?  995  VAL   A O   1 
ATOM   7909  C  CB  . VAL   A 1 997  ? -35.60600  74.64600  2.63300   1.000 37.16478  ?  995  VAL   A CB  1 
ATOM   7910  C  CG1 . VAL   A 1 997  ? -34.23200  74.99600  2.09300   1.000 32.48382  ?  995  VAL   A CG1 1 
ATOM   7911  C  CG2 . VAL   A 1 997  ? -36.10300  73.33600  2.04000   1.000 29.34360  ?  995  VAL   A CG2 1 
ATOM   7912  N  N   . ASN   A 1 998  ? -34.19200  76.11000  5.44400   1.000 38.15446  ?  996  ASN   A N   1 
ATOM   7913  C  CA  . ASN   A 1 998  ? -33.90300  77.35700  6.13700   1.000 30.90648  ?  996  ASN   A CA  1 
ATOM   7914  C  C   . ASN   A 1 998  ? -33.81200  78.51600  5.14300   1.000 40.80470  ?  996  ASN   A C   1 
ATOM   7915  O  O   . ASN   A 1 998  ? -33.63400  78.30300  3.94000   1.000 49.88660  ?  996  ASN   A O   1 
ATOM   7916  C  CB  . ASN   A 1 998  ? -32.60900  77.22900  6.94900   1.000 28.29837  ?  996  ASN   A CB  1 
ATOM   7917  C  CG  . ASN   A 1 998  ? -31.41000  76.83000  6.10200   1.000 50.88121  ?  996  ASN   A CG  1 
ATOM   7918  O  OD1 . ASN   A 1 998  ? -31.20900  77.33400  4.99800   1.000 59.64595  ?  996  ASN   A OD1 1 
ATOM   7919  N  ND2 . ASN   A 1 998  ? -30.59900  75.92000  6.62900   1.000 70.69895  ?  996  ASN   A ND2 1 
ATOM   7920  N  N   . PRO   A 1 999  ? -33.95200  79.75700  5.62100   1.000 39.89877  ?  997  PRO   A N   1 
ATOM   7921  C  CA  . PRO   A 1 999  ? -33.86000  80.90400  4.70100   1.000 41.66437  ?  997  PRO   A CA  1 
ATOM   7922  C  C   . PRO   A 1 999  ? -32.53200  81.00400  3.97000   1.000 48.20599  ?  997  PRO   A C   1 
ATOM   7923  O  O   . PRO   A 1 999  ? -32.49100  81.56100  2.86600   1.000 51.24393  ?  997  PRO   A O   1 
ATOM   7924  C  CB  . PRO   A 1 999  ? -34.08700  82.10800  5.62400   1.000 36.30100  ?  997  PRO   A CB  1 
ATOM   7925  C  CG  . PRO   A 1 999  ? -34.89100  81.56500  6.75300   1.000 48.14904  ?  997  PRO   A CG  1 
ATOM   7926  C  CD  . PRO   A 1 999  ? -34.39000  80.16700  6.96800   1.000 47.21538  ?  997  PRO   A CD  1 
ATOM   7927  N  N   . GLU   A 1 1000 ? -31.44500  80.48100  4.54200   1.000 47.99181  ?  998  GLU   A N   1 
ATOM   7928  C  CA  . GLU   A 1 1000 ? -30.15000  80.56000  3.87200   1.000 40.83950  ?  998  GLU   A CA  1 
ATOM   7929  C  C   . GLU   A 1 1000 ? -30.12700  79.70100  2.61300   1.000 38.34971  ?  998  GLU   A C   1 
ATOM   7930  O  O   . GLU   A 1 1000 ? -29.79000  80.18600  1.52500   1.000 31.85514  ?  998  GLU   A O   1 
ATOM   7931  C  CB  . GLU   A 1 1000 ? -29.03300  80.13800  4.82600   1.000 43.31613  ?  998  GLU   A CB  1 
ATOM   7932  C  CG  . GLU   A 1 1000 ? -27.64200  80.28900  4.23000   1.000 64.76378  ?  998  GLU   A CG  1 
ATOM   7933  C  CD  . GLU   A 1 1000 ? -26.57800  79.56200  5.02800   1.000 79.76294  ?  998  GLU   A CD  1 
ATOM   7934  O  OE1 . GLU   A 1 1000 ? -26.93700  78.67300  5.82800   1.000 77.89017  ?  998  GLU   A OE1 1 
ATOM   7935  O  OE2 . GLU   A 1 1000 ? -25.38200  79.88000  4.85400   1.000 74.78788  -1 998  GLU   A OE2 1 
ATOM   7936  N  N   . ILE   A 1 1001 ? -30.47000  78.41700  2.74200   1.000 37.00065  ?  999  ILE   A N   1 
ATOM   7937  C  CA  . ILE   A 1 1001 ? -30.49600  77.53600  1.57800   1.000 35.66720  ?  999  ILE   A CA  1 
ATOM   7938  C  C   . ILE   A 1 1001 ? -31.56000  77.99600  0.59200   1.000 40.76285  ?  999  ILE   A C   1 
ATOM   7939  O  O   . ILE   A 1 1001 ? -31.36800  77.93000  -0.62900  1.000 37.39709  ?  999  ILE   A O   1 
ATOM   7940  C  CB  . ILE   A 1 1001 ? -30.71500  76.07400  2.01300   1.000 36.59039  ?  999  ILE   A CB  1 
ATOM   7941  C  CG1 . ILE   A 1 1001 ? -29.55100  75.59300  2.88000   1.000 43.77486  ?  999  ILE   A CG1 1 
ATOM   7942  C  CG2 . ILE   A 1 1001 ? -30.85500  75.16700  0.80200   1.000 36.54813  ?  999  ILE   A CG2 1 
ATOM   7943  C  CD1 . ILE   A 1 1001 ? -28.22300  75.54800  2.14700   1.000 61.97056  ?  999  ILE   A CD1 1 
ATOM   7944  N  N   . THR   A 1 1002 ? -32.69300  78.48500  1.10600   1.000 42.67276  ?  1000 THR   A N   1 
ATOM   7945  C  CA  . THR   A 1 1002 ? -33.75100  78.99100  0.23700   1.000 35.97985  ?  1000 THR   A CA  1 
ATOM   7946  C  C   . THR   A 1 1002 ? -33.23400  80.09600  -0.67600  1.000 36.53825  ?  1000 THR   A C   1 
ATOM   7947  O  O   . THR   A 1 1002 ? -33.62700  80.18200  -1.84500  1.000 48.22759  ?  1000 THR   A O   1 
ATOM   7948  C  CB  . THR   A 1 1002 ? -34.92500  79.49500  1.07700   1.000 36.86255  ?  1000 THR   A CB  1 
ATOM   7949  O  OG1 . THR   A 1 1002 ? -35.39100  78.44100  1.92900   1.000 41.99988  ?  1000 THR   A OG1 1 
ATOM   7950  C  CG2 . THR   A 1 1002 ? -36.06500  79.95000  0.18300   1.000 42.42623  ?  1000 THR   A CG2 1 
ATOM   7951  N  N   . ARG   A 1 1003 ? -32.34000  80.94700  -0.16400  1.000 24.67226  ?  1001 ARG   A N   1 
ATOM   7952  C  CA  . ARG   A 1 1003 ? -31.74700  81.97800  -1.00800  1.000 38.78486  ?  1001 ARG   A CA  1 
ATOM   7953  C  C   . ARG   A 1 1003 ? -30.80100  81.37300  -2.03700  1.000 41.93286  ?  1001 ARG   A C   1 
ATOM   7954  O  O   . ARG   A 1 1003 ? -30.80500  81.77900  -3.20500  1.000 32.60528  ?  1001 ARG   A O   1 
ATOM   7955  C  CB  . ARG   A 1 1003 ? -31.01100  83.00400  -0.15100  1.000 41.43826  ?  1001 ARG   A CB  1 
ATOM   7956  C  CG  . ARG   A 1 1003 ? -31.90400  83.80800  0.76600   1.000 44.80221  ?  1001 ARG   A CG  1 
ATOM   7957  C  CD  . ARG   A 1 1003 ? -31.06200  84.60900  1.73100   1.000 53.99946  ?  1001 ARG   A CD  1 
ATOM   7958  N  NE  . ARG   A 1 1003 ? -31.79100  84.95900  2.94300   1.000 62.81655  ?  1001 ARG   A NE  1 
ATOM   7959  C  CZ  . ARG   A 1 1003 ? -31.21200  85.34800  4.07100   1.000 68.01351  ?  1001 ARG   A CZ  1 
ATOM   7960  N  NH1 . ARG   A 1 1003 ? -29.89700  85.44700  4.17300   1.000 61.89111  ?  1001 ARG   A NH1 1 
ATOM   7961  N  NH2 . ARG   A 1 1003 ? -31.97100  85.63900  5.12300   1.000 65.94856  ?  1001 ARG   A NH2 1 
ATOM   7962  N  N   . LYS   A 1 1004 ? -29.97800  80.40600  -1.62000  1.000 46.97592  ?  1002 LYS   A N   1 
ATOM   7963  C  CA  . LYS   A 1 1004 ? -29.04400  79.78600  -2.55300  1.000 36.06441  ?  1002 LYS   A CA  1 
ATOM   7964  C  C   . LYS   A 1 1004 ? -29.78500  79.05400  -3.66200  1.000 40.70188  ?  1002 LYS   A C   1 
ATOM   7965  O  O   . LYS   A 1 1004 ? -29.35400  79.06800  -4.82000  1.000 39.10121  ?  1002 LYS   A O   1 
ATOM   7966  C  CB  . LYS   A 1 1004 ? -28.10700  78.83200  -1.81100  1.000 42.20784  ?  1002 LYS   A CB  1 
ATOM   7967  C  CG  . LYS   A 1 1004 ? -26.82800  78.51900  -2.57100  1.000 38.82026  ?  1002 LYS   A CG  1 
ATOM   7968  C  CD  . LYS   A 1 1004 ? -25.90400  77.61300  -1.77800  1.000 41.62051  ?  1002 LYS   A CD  1 
ATOM   7969  C  CE  . LYS   A 1 1004 ? -24.47000  77.74100  -2.26700  1.000 61.22046  ?  1002 LYS   A CE  1 
ATOM   7970  N  NZ  . LYS   A 1 1004 ? -24.38000  77.67900  -3.75200  1.000 73.73845  ?  1002 LYS   A NZ  1 
ATOM   7971  N  N   . LEU   A 1 1005 ? -30.90900  78.41600  -3.32800  1.000 30.48933  ?  1003 LEU   A N   1 
ATOM   7972  C  CA  . LEU   A 1 1005 ? -31.72000  77.76600  -4.35100  1.000 25.20433  ?  1003 LEU   A CA  1 
ATOM   7973  C  C   . LEU   A 1 1005 ? -32.28500  78.78400  -5.33400  1.000 31.39221  ?  1003 LEU   A C   1 
ATOM   7974  O  O   . LEU   A 1 1005 ? -32.27300  78.55700  -6.54900  1.000 37.42211  ?  1003 LEU   A O   1 
ATOM   7975  C  CB  . LEU   A 1 1005 ? -32.84800  76.96800  -3.69700  1.000 31.48962  ?  1003 LEU   A CB  1 
ATOM   7976  C  CG  . LEU   A 1 1005 ? -32.45000  75.84200  -2.73900  1.000 33.10248  ?  1003 LEU   A CG  1 
ATOM   7977  C  CD1 . LEU   A 1 1005 ? -33.65300  75.39300  -1.92800  1.000 24.04811  ?  1003 LEU   A CD1 1 
ATOM   7978  C  CD2 . LEU   A 1 1005 ? -31.84400  74.66800  -3.49100  1.000 33.12555  ?  1003 LEU   A CD2 1 
ATOM   7979  N  N   . LYS   A 1 1006 ? -32.77800  79.91700  -4.82700  1.000 24.05781  ?  1004 LYS   A N   1 
ATOM   7980  C  CA  . LYS   A 1 1006 ? -33.35100  80.93400  -5.70500  1.000 32.35050  ?  1004 LYS   A CA  1 
ATOM   7981  C  C   . LYS   A 1 1006 ? -32.27100  81.62800  -6.52400  1.000 34.76341  ?  1004 LYS   A C   1 
ATOM   7982  O  O   . LYS   A 1 1006 ? -32.42800  81.82900  -7.73400  1.000 39.95817  ?  1004 LYS   A O   1 
ATOM   7983  C  CB  . LYS   A 1 1006 ? -34.14100  81.95800  -4.89000  1.000 38.52192  ?  1004 LYS   A CB  1 
ATOM   7984  C  CG  . LYS   A 1 1006 ? -35.39300  81.41400  -4.22500  1.000 54.48948  ?  1004 LYS   A CG  1 
ATOM   7985  C  CD  . LYS   A 1 1006 ? -36.30500  82.54800  -3.78000  1.000 50.87154  ?  1004 LYS   A CD  1 
ATOM   7986  C  CE  . LYS   A 1 1006 ? -37.17100  82.13400  -2.60100  1.000 50.77638  ?  1004 LYS   A CE  1 
ATOM   7987  N  NZ  . LYS   A 1 1006 ? -38.20200  83.16000  -2.27900  1.000 36.48935  ?  1004 LYS   A NZ  1 
ATOM   7988  N  N   . ALA   A 1 1007 ? -31.16800  82.01400  -5.87800  1.000 40.53229  ?  1005 ALA   A N   1 
ATOM   7989  C  CA  . ALA   A 1 1007 ? -30.09500  82.69400  -6.59600  1.000 37.69154  ?  1005 ALA   A CA  1 
ATOM   7990  C  C   . ALA   A 1 1007 ? -29.48600  81.78900  -7.65800  1.000 41.42130  ?  1005 ALA   A C   1 
ATOM   7991  O  O   . ALA   A 1 1007 ? -29.13900  82.24800  -8.75200  1.000 53.75281  ?  1005 ALA   A O   1 
ATOM   7992  C  CB  . ALA   A 1 1007 ? -29.02400  83.16900  -5.61700  1.000 31.90569  ?  1005 ALA   A CB  1 
ATOM   7993  N  N   . THR   A 1 1008 ? -29.35200  80.49800  -7.35200  1.000 35.39717  ?  1006 THR   A N   1 
ATOM   7994  C  CA  . THR   A 1 1008 ? -28.85500  79.54900  -8.34100  1.000 37.13558  ?  1006 THR   A CA  1 
ATOM   7995  C  C   . THR   A 1 1008 ? -29.79300  79.46300  -9.53800  1.000 39.40430  ?  1006 THR   A C   1 
ATOM   7996  O  O   . THR   A 1 1008 ? -29.35100  79.50200  -10.69200 1.000 45.05628  ?  1006 THR   A O   1 
ATOM   7997  C  CB  . THR   A 1 1008 ? -28.67700  78.17200  -7.70100  1.000 44.53618  ?  1006 THR   A CB  1 
ATOM   7998  O  OG1 . THR   A 1 1008 ? -27.47800  78.15400  -6.91600  1.000 44.54349  ?  1006 THR   A OG1 1 
ATOM   7999  C  CG2 . THR   A 1 1008 ? -28.60900  77.10100  -8.76500  1.000 31.61298  ?  1006 THR   A CG2 1 
ATOM   8000  N  N   . ALA   A 1 1009 ? -31.09900  79.34900  -9.27900  1.000 32.96599  ?  1007 ALA   A N   1 
ATOM   8001  C  CA  . ALA   A 1 1009 ? -32.06200  79.23700  -10.36900 1.000 38.09880  ?  1007 ALA   A CA  1 
ATOM   8002  C  C   . ALA   A 1 1009 ? -32.03900  80.47500  -11.25700 1.000 44.64917  ?  1007 ALA   A C   1 
ATOM   8003  O  O   . ALA   A 1 1009 ? -32.06600  80.36400  -12.48800 1.000 48.84763  ?  1007 ALA   A O   1 
ATOM   8004  C  CB  . ALA   A 1 1009 ? -33.46500  79.00300  -9.80900  1.000 27.89316  ?  1007 ALA   A CB  1 
ATOM   8005  N  N   . ALA   A 1 1010 ? -31.97500  81.66200  -10.65200 1.000 37.00171  ?  1008 ALA   A N   1 
ATOM   8006  C  CA  . ALA   A 1 1010 ? -31.96500  82.89000  -11.44000 1.000 39.79283  ?  1008 ALA   A CA  1 
ATOM   8007  C  C   . ALA   A 1 1010 ? -30.68300  83.01900  -12.25100 1.000 42.66994  ?  1008 ALA   A C   1 
ATOM   8008  O  O   . ALA   A 1 1010 ? -30.70700  83.51200  -13.38500 1.000 58.35601  ?  1008 ALA   A O   1 
ATOM   8009  C  CB  . ALA   A 1 1010 ? -32.14800  84.10100  -10.52700 1.000 37.99366  ?  1008 ALA   A CB  1 
ATOM   8010  N  N   . LYS   A 1 1011 ? -29.55400  82.57800  -11.69000 1.000 45.76940  ?  1009 LYS   A N   1 
ATOM   8011  C  CA  . LYS   A 1 1011 ? -28.27900  82.70800  -12.38800 1.000 41.06681  ?  1009 LYS   A CA  1 
ATOM   8012  C  C   . LYS   A 1 1011 ? -28.25700  81.90100  -13.68000 1.000 38.18069  ?  1009 LYS   A C   1 
ATOM   8013  O  O   . LYS   A 1 1011 ? -27.56000  82.27100  -14.63200 1.000 50.92543  ?  1009 LYS   A O   1 
ATOM   8014  C  CB  . LYS   A 1 1011 ? -27.13300  82.28000  -11.46700 1.000 38.42093  ?  1009 LYS   A CB  1 
ATOM   8015  C  CG  . LYS   A 1 1011 ? -25.76500  82.25800  -12.13700 1.000 64.78111  ?  1009 LYS   A CG  1 
ATOM   8016  C  CD  . LYS   A 1 1011 ? -24.63000  82.18000  -11.12700 1.000 70.33707  ?  1009 LYS   A CD  1 
ATOM   8017  C  CE  . LYS   A 1 1011 ? -23.28000  82.20600  -11.82900 1.000 64.98627  ?  1009 LYS   A CE  1 
ATOM   8018  N  NZ  . LYS   A 1 1011 ? -22.43400  81.04100  -11.45000 1.000 68.58727  ?  1009 LYS   A NZ  1 
ATOM   8019  N  N   . HIS   A 1 1012 ? -29.02500  80.81800  -13.74800 1.000 35.88800  ?  1010 HIS   A N   1 
ATOM   8020  C  CA  . HIS   A 1 1012 ? -28.98900  79.90500  -14.88100 1.000 43.12928  ?  1010 HIS   A CA  1 
ATOM   8021  C  C   . HIS   A 1 1012 ? -30.32200  79.87800  -15.62400 1.000 42.17957  ?  1010 HIS   A C   1 
ATOM   8022  O  O   . HIS   A 1 1012 ? -30.75500  78.83600  -16.11900 1.000 55.02282  ?  1010 HIS   A O   1 
ATOM   8023  C  CB  . HIS   A 1 1012 ? -28.58500  78.50600  -14.42500 1.000 29.47804  ?  1010 HIS   A CB  1 
ATOM   8024  C  CG  . HIS   A 1 1012 ? -27.25200  78.45900  -13.74300 1.000 43.83748  ?  1010 HIS   A CG  1 
ATOM   8025  N  ND1 . HIS   A 1 1012 ? -27.11400  78.51300  -12.37300 1.000 46.20362  ?  1010 HIS   A ND1 1 
ATOM   8026  C  CD2 . HIS   A 1 1012 ? -25.99700  78.37900  -14.24500 1.000 43.48615  ?  1010 HIS   A CD2 1 
ATOM   8027  C  CE1 . HIS   A 1 1012 ? -25.83100  78.46000  -12.05900 1.000 39.56679  ?  1010 HIS   A CE1 1 
ATOM   8028  N  NE2 . HIS   A 1 1012 ? -25.13200  78.37800  -13.17700 1.000 36.94408  ?  1010 HIS   A NE2 1 
ATOM   8029  N  N   . ASP   A 1 1013 ? -30.98100  81.03700  -15.71400 1.000 34.29818  ?  1011 ASP   A N   1 
ATOM   8030  C  CA  . ASP   A 1 1013 ? -32.20400  81.20200  -16.50800 1.000 42.19669  ?  1011 ASP   A CA  1 
ATOM   8031  C  C   . ASP   A 1 1013 ? -33.29000  80.21000  -16.09600 1.000 37.64809  ?  1011 ASP   A C   1 
ATOM   8032  O  O   . ASP   A 1 1013 ? -34.00000  79.65800  -16.93800 1.000 38.10167  ?  1011 ASP   A O   1 
ATOM   8033  C  CB  . ASP   A 1 1013 ? -31.91400  81.07900  -18.00700 1.000 51.93490  ?  1011 ASP   A CB  1 
ATOM   8034  C  CG  . ASP   A 1 1013 ? -31.00800  82.17800  -18.52200 1.000 53.27947  ?  1011 ASP   A CG  1 
ATOM   8035  O  OD1 . ASP   A 1 1013 ? -30.88800  83.21700  -17.84500 1.000 54.11832  ?  1011 ASP   A OD1 1 
ATOM   8036  O  OD2 . ASP   A 1 1013 ? -30.41900  82.00500  -19.61000 1.000 57.75269  -1 1011 ASP   A OD2 1 
ATOM   8037  N  N   . LEU   A 1 1014 ? -33.42500  79.98200  -14.79300 1.000 36.70418  ?  1012 LEU   A N   1 
ATOM   8038  C  CA  . LEU   A 1 1014 ? -34.39500  79.03200  -14.27200 1.000 40.84859  ?  1012 LEU   A CA  1 
ATOM   8039  C  C   . LEU   A 1 1014 ? -35.23600  79.68700  -13.18700 1.000 37.26276  ?  1012 LEU   A C   1 
ATOM   8040  O  O   . LEU   A 1 1014 ? -34.83800  80.68000  -12.57300 1.000 46.48149  ?  1012 LEU   A O   1 
ATOM   8041  C  CB  . LEU   A 1 1014 ? -33.71100  77.78000  -13.70500 1.000 35.58814  ?  1012 LEU   A CB  1 
ATOM   8042  C  CG  . LEU   A 1 1014 ? -32.96600  76.87400  -14.68200 1.000 33.95356  ?  1012 LEU   A CG  1 
ATOM   8043  C  CD1 . LEU   A 1 1014 ? -31.88300  76.10800  -13.95000 1.000 40.31631  ?  1012 LEU   A CD1 1 
ATOM   8044  C  CD2 . LEU   A 1 1014 ? -33.92900  75.91400  -15.36000 1.000 49.56387  ?  1012 LEU   A CD2 1 
ATOM   8045  N  N   . THR   A 1 1015 ? -36.41300  79.11700  -12.96200 1.000 36.53924  ?  1013 THR   A N   1 
ATOM   8046  C  CA  . THR   A 1 1015 ? -37.23700  79.48700  -11.82500 1.000 27.22625  ?  1013 THR   A CA  1 
ATOM   8047  C  C   . THR   A 1 1015 ? -36.96400  78.53700  -10.66300 1.000 34.37317  ?  1013 THR   A C   1 
ATOM   8048  O  O   . THR   A 1 1015 ? -36.34900  77.48000  -10.82200 1.000 45.91002  ?  1013 THR   A O   1 
ATOM   8049  C  CB  . THR   A 1 1015 ? -38.71900  79.45900  -12.19700 1.000 34.58872  ?  1013 THR   A CB  1 
ATOM   8050  O  OG1 . THR   A 1 1015 ? -39.10900  78.11500  -12.50600 1.000 33.69372  ?  1013 THR   A OG1 1 
ATOM   8051  C  CG2 . THR   A 1 1015 ? -38.98200  80.34300  -13.40400 1.000 40.63595  ?  1013 THR   A CG2 1 
ATOM   8052  N  N   . LEU   A 1 1016 ? -37.42600  78.92800  -9.47400  1.000 31.01805  ?  1014 LEU   A N   1 
ATOM   8053  C  CA  . LEU   A 1 1016 ? -37.29300  78.04200  -8.32300  1.000 33.84992  ?  1014 LEU   A CA  1 
ATOM   8054  C  C   . LEU   A 1 1016 ? -38.07800  76.75500  -8.53800  1.000 45.76073  ?  1014 LEU   A C   1 
ATOM   8055  O  O   . LEU   A 1 1016 ? -37.64700  75.67600  -8.11500  1.000 54.58062  ?  1014 LEU   A O   1 
ATOM   8056  C  CB  . LEU   A 1 1016 ? -37.75800  78.75000  -7.05200  1.000 26.24290  ?  1014 LEU   A CB  1 
ATOM   8057  C  CG  . LEU   A 1 1016 ? -37.54500  77.95600  -5.76300  1.000 31.16618  ?  1014 LEU   A CG  1 
ATOM   8058  C  CD1 . LEU   A 1 1016 ? -36.06300  77.70600  -5.53600  1.000 31.49968  ?  1014 LEU   A CD1 1 
ATOM   8059  C  CD2 . LEU   A 1 1016 ? -38.16100  78.67300  -4.57400  1.000 34.81162  ?  1014 LEU   A CD2 1 
ATOM   8060  N  N   . TYR   A 1 1017 ? -39.23000  76.85100  -9.20600  1.000 37.25005  ?  1015 TYR   A N   1 
ATOM   8061  C  CA  . TYR   A 1 1017 ? -40.02200  75.66300  -9.50600  1.000 32.37522  ?  1015 TYR   A CA  1 
ATOM   8062  C  C   . TYR   A 1 1017 ? -39.24000  74.69200  -10.38300 1.000 35.71775  ?  1015 TYR   A C   1 
ATOM   8063  O  O   . TYR   A 1 1017 ? -39.22600  73.48200  -10.12900 1.000 39.92856  ?  1015 TYR   A O   1 
ATOM   8064  C  CB  . TYR   A 1 1017 ? -41.33300  76.07300  -10.17600 1.000 28.81166  ?  1015 TYR   A CB  1 
ATOM   8065  C  CG  . TYR   A 1 1017 ? -42.13900  74.91900  -10.72600 1.000 30.82550  ?  1015 TYR   A CG  1 
ATOM   8066  C  CD1 . TYR   A 1 1017 ? -42.99400  74.19200  -9.90900  1.000 34.00701  ?  1015 TYR   A CD1 1 
ATOM   8067  C  CD2 . TYR   A 1 1017 ? -42.05100  74.56300  -12.06600 1.000 31.95146  ?  1015 TYR   A CD2 1 
ATOM   8068  C  CE1 . TYR   A 1 1017 ? -43.73400  73.13800  -10.41000 1.000 33.68363  ?  1015 TYR   A CE1 1 
ATOM   8069  C  CE2 . TYR   A 1 1017 ? -42.78600  73.51200  -12.57400 1.000 40.79623  ?  1015 TYR   A CE2 1 
ATOM   8070  C  CZ  . TYR   A 1 1017 ? -43.62500  72.80400  -11.74100 1.000 33.72629  ?  1015 TYR   A CZ  1 
ATOM   8071  O  OH  . TYR   A 1 1017 ? -44.35800  71.75700  -12.24300 1.000 41.81873  ?  1015 TYR   A OH  1 
ATOM   8072  N  N   . MET   A 1 1018 ? -38.57900  75.20700  -11.42300 1.000 30.10880  ?  1016 MET   A N   1 
ATOM   8073  C  CA  . MET   A 1 1018 ? -37.78500  74.34400  -12.29300 1.000 40.44931  ?  1016 MET   A CA  1 
ATOM   8074  C  C   . MET   A 1 1018 ? -36.66300  73.66700  -11.52000 1.000 35.89339  ?  1016 MET   A C   1 
ATOM   8075  O  O   . MET   A 1 1018 ? -36.33900  72.50000  -11.77400 1.000 37.69474  ?  1016 MET   A O   1 
ATOM   8076  C  CB  . MET   A 1 1018 ? -37.21300  75.15000  -13.45800 1.000 32.03442  ?  1016 MET   A CB  1 
ATOM   8077  C  CG  . MET   A 1 1018 ? -38.24700  75.60500  -14.46400 1.000 32.95633  ?  1016 MET   A CG  1 
ATOM   8078  S  SD  . MET   A 1 1018 ? -37.57700  76.79100  -15.64200 1.000 46.65073  ?  1016 MET   A SD  1 
ATOM   8079  C  CE  . MET   A 1 1018 ? -39.07900  77.30000  -16.47300 1.000 49.21502  ?  1016 MET   A CE  1 
ATOM   8080  N  N   . LEU   A 1 1019 ? -36.05900  74.38200  -10.57000 1.000 25.46062  ?  1017 LEU   A N   1 
ATOM   8081  C  CA  . LEU   A 1 1019 ? -34.94900  73.81200  -9.81700  1.000 31.04916  ?  1017 LEU   A CA  1 
ATOM   8082  C  C   . LEU   A 1 1019 ? -35.42900  72.72300  -8.86700  1.000 35.46464  ?  1017 LEU   A C   1 
ATOM   8083  O  O   . LEU   A 1 1019 ? -34.80200  71.66300  -8.76100  1.000 45.34586  ?  1017 LEU   A O   1 
ATOM   8084  C  CB  . LEU   A 1 1019 ? -34.21600  74.91600  -9.05800  1.000 27.73704  ?  1017 LEU   A CB  1 
ATOM   8085  C  CG  . LEU   A 1 1019 ? -32.93800  74.52300  -8.32200  1.000 27.08134  ?  1017 LEU   A CG  1 
ATOM   8086  C  CD1 . LEU   A 1 1019 ? -31.85300  75.54200  -8.60100  1.000 31.56550  ?  1017 LEU   A CD1 1 
ATOM   8087  C  CD2 . LEU   A 1 1019 ? -33.19700  74.41700  -6.83100  1.000 27.01500  ?  1017 LEU   A CD2 1 
ATOM   8088  N  N   . MET   A 1 1020 ? -36.54400  72.96400  -8.17400  1.000 40.84530  ?  1018 MET   A N   1 
ATOM   8089  C  CA  . MET   A 1 1020 ? -37.09600  71.95100  -7.28000  1.000 43.02831  ?  1018 MET   A CA  1 
ATOM   8090  C  C   . MET   A 1 1020 ? -37.63600  70.76100  -8.06300  1.000 38.57816  ?  1018 MET   A C   1 
ATOM   8091  O  O   . MET   A 1 1020 ? -37.52500  69.61400  -7.61300  1.000 34.96526  ?  1018 MET   A O   1 
ATOM   8092  C  CB  . MET   A 1 1020 ? -38.19400  72.56400  -6.41000  1.000 31.92073  ?  1018 MET   A CB  1 
ATOM   8093  C  CG  . MET   A 1 1020 ? -37.75300  73.76400  -5.58000  1.000 33.88002  ?  1018 MET   A CG  1 
ATOM   8094  S  SD  . MET   A 1 1020 ? -36.67800  73.31900  -4.20200  1.000 33.08933  ?  1018 MET   A SD  1 
ATOM   8095  C  CE  . MET   A 1 1020 ? -37.58800  71.93000  -3.52600  1.000 30.00567  ?  1018 MET   A CE  1 
ATOM   8096  N  N   . LEU   A 1 1021 ? -38.22800  71.01500  -9.23400  1.000 34.57322  ?  1019 LEU   A N   1 
ATOM   8097  C  CA  . LEU   A 1 1021 ? -38.73900  69.92900  -10.06500 1.000 33.60313  ?  1019 LEU   A CA  1 
ATOM   8098  C  C   . LEU   A 1 1021 ? -37.62700  68.96600  -10.45800 1.000 38.92700  ?  1019 LEU   A C   1 
ATOM   8099  O  O   . LEU   A 1 1021 ? -37.82800  67.74500  -10.48000 1.000 37.74409  ?  1019 LEU   A O   1 
ATOM   8100  C  CB  . LEU   A 1 1021 ? -39.41600  70.50100  -11.31200 1.000 28.15394  ?  1019 LEU   A CB  1 
ATOM   8101  C  CG  . LEU   A 1 1021 ? -40.05700  69.51600  -12.29200 1.000 29.26322  ?  1019 LEU   A CG  1 
ATOM   8102  C  CD1 . LEU   A 1 1021 ? -41.31200  68.90500  -11.69500 1.000 29.24772  ?  1019 LEU   A CD1 1 
ATOM   8103  C  CD2 . LEU   A 1 1021 ? -40.36500  70.19700  -13.61600 1.000 24.26207  ?  1019 LEU   A CD2 1 
ATOM   8104  N  N   . THR   A 1 1022 ? -36.44300  69.49700  -10.77000 1.000 37.20016  ?  1020 THR   A N   1 
ATOM   8105  C  CA  . THR   A 1 1022 ? -35.31500  68.63700  -11.11300 1.000 37.45233  ?  1020 THR   A CA  1 
ATOM   8106  C  C   . THR   A 1 1022 ? -34.86100  67.82200  -9.90900  1.000 39.87618  ?  1020 THR   A C   1 
ATOM   8107  O  O   . THR   A 1 1022 ? -34.58100  66.62400  -10.03300 1.000 36.60160  ?  1020 THR   A O   1 
ATOM   8108  C  CB  . THR   A 1 1022 ? -34.16200  69.48000  -11.65600 1.000 29.16900  ?  1020 THR   A CB  1 
ATOM   8109  O  OG1 . THR   A 1 1022 ? -34.66200  70.39300  -12.64000 1.000 40.34950  ?  1020 THR   A OG1 1 
ATOM   8110  C  CG2 . THR   A 1 1022 ? -33.10700  68.59000  -12.29400 1.000 37.30767  ?  1020 THR   A CG2 1 
ATOM   8111  N  N   . ILE   A 1 1023 ? -34.78900  68.45700  -8.73700  1.000 36.74607  ?  1021 ILE   A N   1 
ATOM   8112  C  CA  . ILE   A 1 1023 ? -34.40700  67.74500  -7.51900  1.000 29.72690  ?  1021 ILE   A CA  1 
ATOM   8113  C  C   . ILE   A 1 1023 ? -35.41500  66.64700  -7.20700  1.000 36.26886  ?  1021 ILE   A C   1 
ATOM   8114  O  O   . ILE   A 1 1023 ? -35.04400  65.54100  -6.79500  1.000 37.02055  ?  1021 ILE   A O   1 
ATOM   8115  C  CB  . ILE   A 1 1023 ? -34.26500  68.73700  -6.35100  1.000 28.41006  ?  1021 ILE   A CB  1 
ATOM   8116  C  CG1 . ILE   A 1 1023 ? -33.19400  69.78000  -6.66900  1.000 23.05676  ?  1021 ILE   A CG1 1 
ATOM   8117  C  CG2 . ILE   A 1 1023 ? -33.93200  68.00600  -5.06100  1.000 46.92638  ?  1021 ILE   A CG2 1 
ATOM   8118  C  CD1 . ILE   A 1 1023 ? -33.16100  70.93400  -5.69300  1.000 30.91240  ?  1021 ILE   A CD1 1 
ATOM   8119  N  N   . VAL   A 1 1024 ? -36.70400  66.93000  -7.40400  1.000 41.92086  ?  1022 VAL   A N   1 
ATOM   8120  C  CA  . VAL   A 1 1024 ? -37.72300  65.90200  -7.22000  1.000 40.84936  ?  1022 VAL   A CA  1 
ATOM   8121  C  C   . VAL   A 1 1024 ? -37.57400  64.80900  -8.27200  1.000 46.59227  ?  1022 VAL   A C   1 
ATOM   8122  O  O   . VAL   A 1 1024 ? -37.70500  63.61600  -7.97000  1.000 48.27078  ?  1022 VAL   A O   1 
ATOM   8123  C  CB  . VAL   A 1 1024 ? -39.12700  66.53200  -7.24800  1.000 29.99930  ?  1022 VAL   A CB  1 
ATOM   8124  C  CG1 . VAL   A 1 1024 ? -40.19400  65.45100  -7.24900  1.000 42.49427  ?  1022 VAL   A CG1 1 
ATOM   8125  C  CG2 . VAL   A 1 1024 ? -39.31400  67.45700  -6.05800  1.000 29.53197  ?  1022 VAL   A CG2 1 
ATOM   8126  N  N   . SER   A 1 1025 ? -37.29000  65.19300  -9.51900  1.000 35.28817  ?  1023 SER   A N   1 
ATOM   8127  C  CA  . SER   A 1 1025 ? -37.12600  64.20300  -10.57900 1.000 36.02477  ?  1023 SER   A CA  1 
ATOM   8128  C  C   . SER   A 1 1025 ? -35.92200  63.30800  -10.32000 1.000 48.30020  ?  1023 SER   A C   1 
ATOM   8129  O  O   . SER   A 1 1025 ? -35.98900  62.09000  -10.52300 1.000 50.87707  ?  1023 SER   A O   1 
ATOM   8130  C  CB  . SER   A 1 1025 ? -36.99500  64.90100  -11.93200 1.000 36.71374  ?  1023 SER   A CB  1 
ATOM   8131  O  OG  . SER   A 1 1025 ? -38.18200  65.59900  -12.25700 1.000 46.47102  ?  1023 SER   A OG  1 
ATOM   8132  N  N   . ILE   A 1 1026 ? -34.80700  63.89600  -9.87900  1.000 46.99052  ?  1024 ILE   A N   1 
ATOM   8133  C  CA  . ILE   A 1 1026 ? -33.63600  63.10100  -9.52000  1.000 45.42900  ?  1024 ILE   A CA  1 
ATOM   8134  C  C   . ILE   A 1 1026 ? -33.95000  62.20900  -8.32600  1.000 44.21172  ?  1024 ILE   A C   1 
ATOM   8135  O  O   . ILE   A 1 1026 ? -33.55100  61.03900  -8.28000  1.000 47.59988  ?  1024 ILE   A O   1 
ATOM   8136  C  CB  . ILE   A 1 1026 ? -32.43500  64.02300  -9.23900  1.000 32.73870  ?  1024 ILE   A CB  1 
ATOM   8137  C  CG1 . ILE   A 1 1026 ? -32.00500  64.74000  -10.52000 1.000 34.08145  ?  1024 ILE   A CG1 1 
ATOM   8138  C  CG2 . ILE   A 1 1026 ? -31.28200  63.23400  -8.63900  1.000 35.55526  ?  1024 ILE   A CG2 1 
ATOM   8139  C  CD1 . ILE   A 1 1026 ? -31.05900  65.89500  -10.28300 1.000 27.28368  ?  1024 ILE   A CD1 1 
ATOM   8140  N  N   . TRP   A 1 1027 ? -34.67800  62.74900  -7.34800  1.000 34.12022  ?  1025 TRP   A N   1 
ATOM   8141  C  CA  . TRP   A 1 1027 ? -35.05500  61.96900  -6.17400  1.000 34.61876  ?  1025 TRP   A CA  1 
ATOM   8142  C  C   . TRP   A 1 1027 ? -35.92300  60.77700  -6.55800  1.000 42.00892  ?  1025 TRP   A C   1 
ATOM   8143  O  O   . TRP   A 1 1027 ? -35.71400  59.66200  -6.06600  1.000 36.33118  ?  1025 TRP   A O   1 
ATOM   8144  C  CB  . TRP   A 1 1027 ? -35.77100  62.87700  -5.17300  1.000 31.73721  ?  1025 TRP   A CB  1 
ATOM   8145  C  CG  . TRP   A 1 1027 ? -36.24500  62.20400  -3.92900  1.000 36.89614  ?  1025 TRP   A CG  1 
ATOM   8146  C  CD1 . TRP   A 1 1027 ? -35.48200  61.56500  -2.99800  1.000 43.10611  ?  1025 TRP   A CD1 1 
ATOM   8147  C  CD2 . TRP   A 1 1027 ? -37.59500  62.13600  -3.45700  1.000 38.46325  ?  1025 TRP   A CD2 1 
ATOM   8148  N  NE1 . TRP   A 1 1027 ? -36.27500  61.08600  -1.98300  1.000 46.62534  ?  1025 TRP   A NE1 1 
ATOM   8149  C  CE2 . TRP   A 1 1027 ? -37.57700  61.42600  -2.24100  1.000 42.49980  ?  1025 TRP   A CE2 1 
ATOM   8150  C  CE3 . TRP   A 1 1027 ? -38.81900  62.60000  -3.94900  1.000 44.08342  ?  1025 TRP   A CE3 1 
ATOM   8151  C  CZ2 . TRP   A 1 1027 ? -38.73500  61.16800  -1.51100  1.000 41.41878  ?  1025 TRP   A CZ2 1 
ATOM   8152  C  CZ3 . TRP   A 1 1027 ? -39.96800  62.34400  -3.22200  1.000 38.77679  ?  1025 TRP   A CZ3 1 
ATOM   8153  C  CH2 . TRP   A 1 1027 ? -39.91700  61.63500  -2.01600  1.000 37.14868  ?  1025 TRP   A CH2 1 
ATOM   8154  N  N   . LEU   A 1 1028 ? -36.89600  60.98800  -7.44900  1.000 43.66526  ?  1026 LEU   A N   1 
ATOM   8155  C  CA  . LEU   A 1 1028 ? -37.74300  59.88500  -7.89400  1.000 41.63766  ?  1026 LEU   A CA  1 
ATOM   8156  C  C   . LEU   A 1 1028 ? -36.96000  58.89500  -8.74500  1.000 47.02606  ?  1026 LEU   A C   1 
ATOM   8157  O  O   . LEU   A 1 1028 ? -37.13700  57.67800  -8.61200  1.000 42.27288  ?  1026 LEU   A O   1 
ATOM   8158  C  CB  . LEU   A 1 1028 ? -38.94300  60.42200  -8.67200  1.000 40.79542  ?  1026 LEU   A CB  1 
ATOM   8159  C  CG  . LEU   A 1 1028 ? -39.97100  61.23800  -7.88900  1.000 39.66428  ?  1026 LEU   A CG  1 
ATOM   8160  C  CD1 . LEU   A 1 1028 ? -41.06800  61.73000  -8.81700  1.000 24.88213  ?  1026 LEU   A CD1 1 
ATOM   8161  C  CD2 . LEU   A 1 1028 ? -40.55400  60.41600  -6.75100  1.000 42.26566  ?  1026 LEU   A CD2 1 
ATOM   8162  N  N   . SER   A 1 1029 ? -36.09400  59.40000  -9.62800  1.000 43.82673  ?  1027 SER   A N   1 
ATOM   8163  C  CA  . SER   A 1 1029 ? -35.30400  58.52200  -10.48400 1.000 37.37677  ?  1027 SER   A CA  1 
ATOM   8164  C  C   . SER   A 1 1029 ? -34.40100  57.61300  -9.66000  1.000 48.53242  ?  1027 SER   A C   1 
ATOM   8165  O  O   . SER   A 1 1029 ? -34.31700  56.40700  -9.92100  1.000 42.81524  ?  1027 SER   A O   1 
ATOM   8166  C  CB  . SER   A 1 1029 ? -34.47800  59.35600  -11.46300 1.000 35.18176  ?  1027 SER   A CB  1 
ATOM   8167  O  OG  . SER   A 1 1029 ? -33.53500  58.55300  -12.15000 1.000 47.63493  ?  1027 SER   A OG  1 
ATOM   8168  N  N   . LYS   A 1 1030 ? -33.72600  58.17100  -8.65200  1.000 46.64147  ?  1028 LYS   A N   1 
ATOM   8169  C  CA  . LYS   A 1 1030 ? -32.82700  57.36700  -7.83300  1.000 45.25830  ?  1028 LYS   A CA  1 
ATOM   8170  C  C   . LYS   A 1 1030 ? -33.58000  56.31900  -7.02400  1.000 39.75491  ?  1028 LYS   A C   1 
ATOM   8171  O  O   . LYS   A 1 1030 ? -33.04700  55.23100  -6.77700  1.000 65.09660  ?  1028 LYS   A O   1 
ATOM   8172  C  CB  . LYS   A 1 1030 ? -32.00600  58.27200  -6.91700  1.000 44.49270  ?  1028 LYS   A CB  1 
ATOM   8173  C  CG  . LYS   A 1 1030 ? -30.99600  59.11700  -7.66500  1.000 32.03879  ?  1028 LYS   A CG  1 
ATOM   8174  C  CD  . LYS   A 1 1030 ? -30.06400  59.83800  -6.71700  1.000 42.29550  ?  1028 LYS   A CD  1 
ATOM   8175  C  CE  . LYS   A 1 1030 ? -28.76800  60.18900  -7.42000  1.000 57.23128  ?  1028 LYS   A CE  1 
ATOM   8176  N  NZ  . LYS   A 1 1030 ? -28.08000  58.96600  -7.92800  1.000 53.31039  ?  1028 LYS   A NZ  1 
ATOM   8177  N  N   . MET   A 1 1031 ? -34.81000  56.61900  -6.60400  1.000 39.68815  ?  1029 MET   A N   1 
ATOM   8178  C  CA  . MET   A 1 1031 ? -35.63900  55.60900  -5.96000  1.000 37.95956  ?  1029 MET   A CA  1 
ATOM   8179  C  C   . MET   A 1 1031 ? -36.19800  54.60100  -6.95300  1.000 41.70771  ?  1029 MET   A C   1 
ATOM   8180  O  O   . MET   A 1 1031 ? -36.52400  53.47600  -6.55800  1.000 43.20947  ?  1029 MET   A O   1 
ATOM   8181  C  CB  . MET   A 1 1031 ? -36.78800  56.27000  -5.19400  1.000 37.80585  ?  1029 MET   A CB  1 
ATOM   8182  C  CG  . MET   A 1 1031 ? -36.33600  57.08000  -3.99200  1.000 51.31394  ?  1029 MET   A CG  1 
ATOM   8183  S  SD  . MET   A 1 1031 ? -37.69900  57.61700  -2.94200  1.000 46.56749  ?  1029 MET   A SD  1 
ATOM   8184  C  CE  . MET   A 1 1031 ? -38.61800  58.65000  -4.07800  1.000 31.70758  ?  1029 MET   A CE  1 
ATOM   8185  N  N   . ASN   A 1 1032 ? -36.31200  54.97500  -8.22400  1.000 43.20500  ?  1030 ASN   A N   1 
ATOM   8186  C  CA  . ASN   A 1 1032 ? -36.74700  54.06300  -9.27900  1.000 48.11636  ?  1030 ASN   A CA  1 
ATOM   8187  C  C   . ASN   A 1 1032 ? -35.57500  53.33100  -9.91700  1.000 59.38731  ?  1030 ASN   A C   1 
ATOM   8188  O  O   . ASN   A 1 1032 ? -35.53500  53.15900  -11.14000 1.000 64.40602  ?  1030 ASN   A O   1 
ATOM   8189  C  CB  . ASN   A 1 1032 ? -37.54200  54.83300  -10.32800 1.000 52.57133  ?  1030 ASN   A CB  1 
ATOM   8190  C  CG  . ASN   A 1 1032 ? -38.58500  53.97400  -11.01000 1.000 58.22592  ?  1030 ASN   A CG  1 
ATOM   8191  O  OD1 . ASN   A 1 1032 ? -39.17400  53.08800  -10.39100 1.000 73.39421  ?  1030 ASN   A OD1 1 
ATOM   8192  N  ND2 . ASN   A 1 1032 ? -38.81600  54.22900  -12.29300 1.000 45.30385  ?  1030 ASN   A ND2 1 
ATOM   8193  N  N   . SER   A 1 1033 ? -34.60500  52.90400  -9.10400  1.000 60.01116  ?  1031 SER   A N   1 
ATOM   8194  C  CA  . SER   A 1 1033 ? -33.42500  52.17100  -9.57200  1.000 55.21705  ?  1031 SER   A CA  1 
ATOM   8195  C  C   . SER   A 1 1033 ? -32.63800  52.97700  -10.60300 1.000 55.74650  ?  1031 SER   A C   1 
ATOM   8196  O  O   . SER   A 1 1033 ? -32.20300  52.44800  -11.62900 1.000 65.71568  ?  1031 SER   A O   1 
ATOM   8197  C  CB  . SER   A 1 1033 ? -33.81000  50.79900  -10.13000 1.000 39.87039  ?  1031 SER   A CB  1 
ATOM   8198  O  OG  . SER   A 1 1033 ? -34.53700  50.04800  -9.17300  1.000 55.16737  ?  1031 SER   A OG  1 
ATOM   8199  N  N   . ASP   A 1 1034 ? -32.45400  54.26700  -10.32300 1.000 55.52132  ?  1032 ASP   A N   1 
ATOM   8200  C  CA  . ASP   A 1 1034 ? -31.68200  55.16900  -11.18000 1.000 56.60182  ?  1032 ASP   A CA  1 
ATOM   8201  C  C   . ASP   A 1 1034 ? -32.20800  55.15500  -12.61400 1.000 53.00811  ?  1032 ASP   A C   1 
ATOM   8202  O  O   . ASP   A 1 1034 ? -31.46200  54.96700  -13.57800 1.000 53.30931  ?  1032 ASP   A O   1 
ATOM   8203  C  CB  . ASP   A 1 1034 ? -30.19300  54.82400  -11.13000 1.000 40.86350  ?  1032 ASP   A CB  1 
ATOM   8204  C  CG  . ASP   A 1 1034 ? -29.52500  55.31200  -9.85900  1.000 55.80425  ?  1032 ASP   A CG  1 
ATOM   8205  O  OD1 . ASP   A 1 1034 ? -29.33600  56.54000  -9.71800  1.000 56.41506  ?  1032 ASP   A OD1 1 
ATOM   8206  O  OD2 . ASP   A 1 1034 ? -29.20500  54.47000  -8.99500  1.000 74.57043  -1 1032 ASP   A OD2 1 
ATOM   8207  N  N   . SER   A 1 1035 ? -33.51600  55.35800  -12.74700 1.000 50.91445  ?  1033 SER   A N   1 
ATOM   8208  C  CA  . SER   A 1 1035 ? -34.14500  55.37000  -14.05900 1.000 49.55325  ?  1033 SER   A CA  1 
ATOM   8209  C  C   . SER   A 1 1035 ? -33.71300  56.60000  -14.85100 1.000 47.28109  ?  1033 SER   A C   1 
ATOM   8210  O  O   . SER   A 1 1035 ? -33.38200  57.64600  -14.28800 1.000 57.16887  ?  1033 SER   A O   1 
ATOM   8211  C  CB  . SER   A 1 1035 ? -35.66800  55.34800  -13.92400 1.000 46.66061  ?  1033 SER   A CB  1 
ATOM   8212  O  OG  . SER   A 1 1035 ? -36.16000  56.59600  -13.46500 1.000 48.97566  ?  1033 SER   A OG  1 
ATOM   8213  N  N   . ASN   A 1 1036 ? -33.72000  56.46400  -16.17500 1.000 40.41352  ?  1034 ASN   A N   1 
ATOM   8214  C  CA  . ASN   A 1 1036 ? -33.34300  57.55300  -17.06500 1.000 49.91945  ?  1034 ASN   A CA  1 
ATOM   8215  C  C   . ASN   A 1 1036 ? -34.53000  58.40100  -17.50600 1.000 51.10987  ?  1034 ASN   A C   1 
ATOM   8216  O  O   . ASN   A 1 1036 ? -34.33100  59.40300  -18.20000 1.000 60.66051  ?  1034 ASN   A O   1 
ATOM   8217  C  CB  . ASN   A 1 1036 ? -32.61300  57.00400  -18.29500 1.000 50.46298  ?  1034 ASN   A CB  1 
ATOM   8218  C  CG  . ASN   A 1 1036 ? -31.16600  56.65600  -18.00400 1.000 73.88305  ?  1034 ASN   A CG  1 
ATOM   8219  O  OD1 . ASN   A 1 1036 ? -30.30500  57.53500  -17.94300 1.000 80.33927  ?  1034 ASN   A OD1 1 
ATOM   8220  N  ND2 . ASN   A 1 1036 ? -30.88900  55.36900  -17.82400 1.000 81.40484  ?  1034 ASN   A ND2 1 
ATOM   8221  N  N   . GLN   A 1 1037 ? -35.74900  58.03000  -17.12300 1.000 50.69456  ?  1035 GLN   A N   1 
ATOM   8222  C  CA  . GLN   A 1 1037 ? -36.93000  58.82600  -17.42300 1.000 42.95406  ?  1035 GLN   A CA  1 
ATOM   8223  C  C   . GLN   A 1 1037 ? -37.95000  58.63700  -16.31100 1.000 39.14505  ?  1035 GLN   A C   1 
ATOM   8224  O  O   . GLN   A 1 1037 ? -38.11400  57.53100  -15.79000 1.000 47.53242  ?  1035 GLN   A O   1 
ATOM   8225  C  CB  . GLN   A 1 1037 ? -37.54900  58.44700  -18.77200 1.000 46.51141  ?  1035 GLN   A CB  1 
ATOM   8226  C  CG  . GLN   A 1 1037 ? -37.15100  59.36600  -19.91200 1.000 57.62613  ?  1035 GLN   A CG  1 
ATOM   8227  C  CD  . GLN   A 1 1037 ? -38.21400  59.44800  -20.98900 1.000 71.09716  ?  1035 GLN   A CD  1 
ATOM   8228  O  OE1 . GLN   A 1 1037 ? -38.95900  58.49400  -21.21500 1.000 75.88750  ?  1035 GLN   A OE1 1 
ATOM   8229  N  NE2 . GLN   A 1 1037 ? -38.29900  60.59600  -21.65200 1.000 79.82560  ?  1035 GLN   A NE2 1 
ATOM   8230  N  N   . VAL   A 1 1038 ? -38.63300  59.72400  -15.95600 1.000 39.97742  ?  1036 VAL   A N   1 
ATOM   8231  C  CA  . VAL   A 1 1038 ? -39.62600  59.70900  -14.89300 1.000 42.57001  ?  1036 VAL   A CA  1 
ATOM   8232  C  C   . VAL   A 1 1038 ? -40.88500  60.41100  -15.37900 1.000 40.52362  ?  1036 VAL   A C   1 
ATOM   8233  O  O   . VAL   A 1 1038 ? -40.86300  61.20400  -16.32300 1.000 41.19882  ?  1036 VAL   A O   1 
ATOM   8234  C  CB  . VAL   A 1 1038 ? -39.10800  60.37300  -13.60000 1.000 51.27316  ?  1036 VAL   A CB  1 
ATOM   8235  C  CG1 . VAL   A 1 1038 ? -38.25100  59.39700  -12.81300 1.000 56.53065  ?  1036 VAL   A CG1 1 
ATOM   8236  C  CG2 . VAL   A 1 1038 ? -38.32000  61.63100  -13.93400 1.000 50.96859  ?  1036 VAL   A CG2 1 
ATOM   8237  N  N   . ILE   A 1 1039 ? -41.99500  60.10400  -14.71200 1.000 35.15871  ?  1037 ILE   A N   1 
ATOM   8238  C  CA  . ILE   A 1 1039 ? -43.29000  60.70100  -15.00800 1.000 37.37110  ?  1037 ILE   A CA  1 
ATOM   8239  C  C   . ILE   A 1 1039 ? -43.90800  61.16900  -13.69700 1.000 37.54162  ?  1037 ILE   A C   1 
ATOM   8240  O  O   . ILE   A 1 1039 ? -43.98600  60.40300  -12.73100 1.000 43.01422  ?  1037 ILE   A O   1 
ATOM   8241  C  CB  . ILE   A 1 1039 ? -44.22300  59.71500  -15.74400 1.000 37.67304  ?  1037 ILE   A CB  1 
ATOM   8242  C  CG1 . ILE   A 1 1039 ? -45.61300  60.32200  -15.95200 1.000 34.78918  ?  1037 ILE   A CG1 1 
ATOM   8243  C  CG2 . ILE   A 1 1039 ? -44.30200  58.37500  -15.01800 1.000 48.65417  ?  1037 ILE   A CG2 1 
ATOM   8244  C  CD1 . ILE   A 1 1039 ? -45.71000  61.21600  -17.16900 1.000 42.42015  ?  1037 ILE   A CD1 1 
ATOM   8245  N  N   . LEU   A 1 1040 ? -44.32100  62.43200  -13.65600 1.000 40.00989  ?  1038 LEU   A N   1 
ATOM   8246  C  CA  . LEU   A 1 1040 ? -44.97200  62.98800  -12.48100 1.000 33.26414  ?  1038 LEU   A CA  1 
ATOM   8247  C  C   . LEU   A 1 1040 ? -45.99100  64.02100  -12.94000 1.000 39.12971  ?  1038 LEU   A C   1 
ATOM   8248  O  O   . LEU   A 1 1040 ? -46.09100  64.34100  -14.12600 1.000 49.45239  ?  1038 LEU   A O   1 
ATOM   8249  C  CB  . LEU   A 1 1040 ? -43.94900  63.59600  -11.51100 1.000 22.86477  ?  1038 LEU   A CB  1 
ATOM   8250  C  CG  . LEU   A 1 1040 ? -43.08900  64.75000  -12.02700 1.000 35.03728  ?  1038 LEU   A CG  1 
ATOM   8251  C  CD1 . LEU   A 1 1040 ? -43.62300  66.07900  -11.52100 1.000 43.37876  ?  1038 LEU   A CD1 1 
ATOM   8252  C  CD2 . LEU   A 1 1040 ? -41.63300  64.56800  -11.62700 1.000 30.63903  ?  1038 LEU   A CD2 1 
ATOM   8253  N  N   . GLY   A 1 1041 ? -46.75700  64.53800  -11.98400 1.000 34.65060  ?  1039 GLY   A N   1 
ATOM   8254  C  CA  . GLY   A 1 1041 ? -47.76700  65.52400  -12.30600 1.000 26.90672  ?  1039 GLY   A CA  1 
ATOM   8255  C  C   . GLY   A 1 1041 ? -47.57700  66.83400  -11.57500 1.000 34.58593  ?  1039 GLY   A C   1 
ATOM   8256  O  O   . GLY   A 1 1041 ? -46.88100  66.89600  -10.55600 1.000 44.74383  ?  1039 GLY   A O   1 
ATOM   8257  N  N   . THR   A 1 1042 ? -48.19700  67.89300  -12.08700 1.000 36.59484  ?  1040 THR   A N   1 
ATOM   8258  C  CA  . THR   A 1 1042 ? -48.13400  69.19800  -11.44900 1.000 43.40813  ?  1040 THR   A CA  1 
ATOM   8259  C  C   . THR   A 1 1042 ? -49.45100  69.92000  -11.69000 1.000 45.62091  ?  1040 THR   A C   1 
ATOM   8260  O  O   . THR   A 1 1042 ? -50.29300  69.47800  -12.47600 1.000 45.29856  ?  1040 THR   A O   1 
ATOM   8261  C  CB  . THR   A 1 1042 ? -46.95300  70.02400  -11.97100 1.000 31.71747  ?  1040 THR   A CB  1 
ATOM   8262  O  OG1 . THR   A 1 1042 ? -46.70000  71.11700  -11.07900 1.000 49.26041  ?  1040 THR   A OG1 1 
ATOM   8263  C  CG2 . THR   A 1 1042 ? -47.25800  70.57300  -13.35600 1.000 39.64917  ?  1040 THR   A CG2 1 
ATOM   8264  N  N   . VAL   A 1 1043 ? -49.62200  71.04200  -10.99800 1.000 42.33363  ?  1041 VAL   A N   1 
ATOM   8265  C  CA  . VAL   A 1 1043 ? -50.81900  71.86100  -11.12600 1.000 43.85175  ?  1041 VAL   A CA  1 
ATOM   8266  C  C   . VAL   A 1 1043 ? -50.43000  73.23700  -11.64600 1.000 48.64260  ?  1041 VAL   A C   1 
ATOM   8267  O  O   . VAL   A 1 1043 ? -49.34400  73.75300  -11.36000 1.000 38.20314  ?  1041 VAL   A O   1 
ATOM   8268  C  CB  . VAL   A 1 1043 ? -51.58300  71.97600  -9.79000  1.000 31.94188  ?  1041 VAL   A CB  1 
ATOM   8269  C  CG1 . VAL   A 1 1043 ? -52.17000  70.63300  -9.40600  1.000 50.17444  ?  1041 VAL   A CG1 1 
ATOM   8270  C  CG2 . VAL   A 1 1043 ? -50.66600  72.49300  -8.69700  1.000 57.27840  ?  1041 VAL   A CG2 1 
ATOM   8271  N  N   . THR   A 1 1044 ? -51.33500  73.82600  -12.42900 1.000 51.62410  ?  1042 THR   A N   1 
ATOM   8272  C  CA  . THR   A 1 1044 ? -51.17700  75.15800  -12.98900 1.000 36.20348  ?  1042 THR   A CA  1 
ATOM   8273  C  C   . THR   A 1 1044 ? -52.35100  76.02700  -12.56100 1.000 46.50414  ?  1042 THR   A C   1 
ATOM   8274  O  O   . THR   A 1 1044 ? -53.40300  75.52700  -12.15500 1.000 53.25663  ?  1042 THR   A O   1 
ATOM   8275  C  CB  . THR   A 1 1044 ? -51.08100  75.12100  -14.52600 1.000 49.35538  ?  1042 THR   A CB  1 
ATOM   8276  O  OG1 . THR   A 1 1044 ? -52.36300  74.80500  -15.08800 1.000 71.06287  ?  1042 THR   A OG1 1 
ATOM   8277  C  CG2 . THR   A 1 1044 ? -50.06900  74.07800  -14.96900 1.000 42.30592  ?  1042 THR   A CG2 1 
ATOM   8278  N  N   . ASP   A 1 1045 ? -52.15400  77.34300  -12.64700 1.000 50.63384  ?  1043 ASP   A N   1 
ATOM   8279  C  CA  . ASP   A 1 1045 ? -53.18900  78.26600  -12.19400 1.000 43.55356  ?  1043 ASP   A CA  1 
ATOM   8280  C  C   . ASP   A 1 1045 ? -54.47200  78.09500  -13.00000 1.000 48.68204  ?  1043 ASP   A C   1 
ATOM   8281  O  O   . ASP   A 1 1045 ? -55.57500  78.18200  -12.44900 1.000 50.40029  ?  1043 ASP   A O   1 
ATOM   8282  C  CB  . ASP   A 1 1045 ? -52.67300  79.70700  -12.26600 1.000 38.20395  ?  1043 ASP   A CB  1 
ATOM   8283  C  CG  . ASP   A 1 1045 ? -52.35500  80.14600  -13.68100 1.000 71.29040  ?  1043 ASP   A CG  1 
ATOM   8284  O  OD1 . ASP   A 1 1045 ? -52.81700  79.48000  -14.63100 1.000 77.87891  ?  1043 ASP   A OD1 1 
ATOM   8285  O  OD2 . ASP   A 1 1045 ? -51.65700  81.16800  -13.84500 1.000 76.81133  -1 1043 ASP   A OD2 1 
ATOM   8286  N  N   . GLY   A 1 1046 ? -54.34700  77.81700  -14.29700 1.000 52.97698  ?  1044 GLY   A N   1 
ATOM   8287  C  CA  . GLY   A 1 1046 ? -55.50900  77.59800  -15.13400 1.000 37.18859  ?  1044 GLY   A CA  1 
ATOM   8288  C  C   . GLY   A 1 1046 ? -56.29900  78.84100  -15.46400 1.000 50.46989  ?  1044 GLY   A C   1 
ATOM   8289  O  O   . GLY   A 1 1046 ? -57.46500  78.73700  -15.85700 1.000 48.90173  ?  1044 GLY   A O   1 
ATOM   8290  N  N   . ARG   A 1 1047 ? -55.70000  80.01900  -15.32100 1.000 52.56231  ?  1045 ARG   A N   1 
ATOM   8291  C  CA  . ARG   A 1 1047 ? -56.37500  81.28600  -15.58500 1.000 38.74501  ?  1045 ARG   A CA  1 
ATOM   8292  C  C   . ARG   A 1 1047 ? -55.96000  81.74200  -16.98000 1.000 49.82765  ?  1045 ARG   A C   1 
ATOM   8293  O  O   . ARG   A 1 1047 ? -55.01900  82.51800  -17.15200 1.000 49.81011  ?  1045 ARG   A O   1 
ATOM   8294  C  CB  . ARG   A 1 1047 ? -56.03400  82.31000  -14.51000 1.000 48.35002  ?  1045 ARG   A CB  1 
ATOM   8295  C  CG  . ARG   A 1 1047 ? -56.07000  81.72100  -13.10900 1.000 59.70198  ?  1045 ARG   A CG  1 
ATOM   8296  C  CD  . ARG   A 1 1047 ? -56.80800  82.61400  -12.13100 1.000 60.00336  ?  1045 ARG   A CD  1 
ATOM   8297  N  NE  . ARG   A 1 1047 ? -57.36900  81.85300  -11.02000 1.000 43.13527  ?  1045 ARG   A NE  1 
ATOM   8298  C  CZ  . ARG   A 1 1047 ? -58.10400  82.37800  -10.05000 1.000 58.38406  ?  1045 ARG   A CZ  1 
ATOM   8299  N  NH1 . ARG   A 1 1047 ? -58.34700  83.67700  -9.99500  1.000 59.23178  ?  1045 ARG   A NH1 1 
ATOM   8300  N  NH2 . ARG   A 1 1047 ? -58.61500  81.57900  -9.11700  1.000 55.79021  ?  1045 ARG   A NH2 1 
ATOM   8301  N  N   . GLN   A 1 1048 ? -56.68000  81.24300  -17.98500 1.000 52.55065  ?  1046 GLN   A N   1 
ATOM   8302  C  CA  . GLN   A 1 1048 ? -56.31800  81.49700  -19.37400 1.000 46.65066  ?  1046 GLN   A CA  1 
ATOM   8303  C  C   . GLN   A 1 1048 ? -56.67700  82.91700  -19.79800 1.000 68.36842  ?  1046 GLN   A C   1 
ATOM   8304  O  O   . GLN   A 1 1048 ? -55.90600  83.56900  -20.51100 1.000 67.11137  ?  1046 GLN   A O   1 
ATOM   8305  C  CB  . GLN   A 1 1048 ? -57.00400  80.47200  -20.27600 1.000 33.44286  ?  1046 GLN   A CB  1 
ATOM   8306  C  CG  . GLN   A 1 1048 ? -56.25800  80.15300  -21.55700 1.000 55.51076  ?  1046 GLN   A CG  1 
ATOM   8307  C  CD  . GLN   A 1 1048 ? -56.93000  79.04800  -22.34700 1.000 57.64508  ?  1046 GLN   A CD  1 
ATOM   8308  O  OE1 . GLN   A 1 1048 ? -57.80900  78.35200  -21.83600 1.000 40.32660  ?  1046 GLN   A OE1 1 
ATOM   8309  N  NE2 . GLN   A 1 1048 ? -56.52600  78.88500  -23.60200 1.000 57.96981  ?  1046 GLN   A NE2 1 
ATOM   8310  N  N   . HIS   A 1 1049 ? -57.84200  83.41500  -19.36900 1.000 69.03537  ?  1047 HIS   A N   1 
ATOM   8311  C  CA  . HIS   A 1 1049 ? -58.23500  84.78900  -19.66100 1.000 61.59154  ?  1047 HIS   A CA  1 
ATOM   8312  C  C   . HIS   A 1 1049 ? -57.68600  85.71400  -18.58300 1.000 51.57829  ?  1047 HIS   A C   1 
ATOM   8313  O  O   . HIS   A 1 1049 ? -57.93200  85.47900  -17.39400 1.000 58.46723  ?  1047 HIS   A O   1 
ATOM   8314  C  CB  . HIS   A 1 1049 ? -59.74900  84.91800  -19.72600 1.000 63.82289  ?  1047 HIS   A CB  1 
ATOM   8315  C  CG  . HIS   A 1 1049 ? -60.22100  86.05800  -20.57400 1.000 68.20989  ?  1047 HIS   A CG  1 
ATOM   8316  N  ND1 . HIS   A 1 1049 ? -60.85800  85.86900  -21.78200 1.000 71.53433  ?  1047 HIS   A ND1 1 
ATOM   8317  C  CD2 . HIS   A 1 1049 ? -60.14900  87.39800  -20.39300 1.000 58.08697  ?  1047 HIS   A CD2 1 
ATOM   8318  C  CE1 . HIS   A 1 1049 ? -61.16200  87.04200  -22.30700 1.000 83.43913  ?  1047 HIS   A CE1 1 
ATOM   8319  N  NE2 . HIS   A 1 1049 ? -60.74200  87.98700  -21.48500 1.000 78.00929  ?  1047 HIS   A NE2 1 
ATOM   8320  N  N   . PRO   A 1 1050 ? -56.95000  86.76800  -18.95100 1.000 46.22177  ?  1048 PRO   A N   1 
ATOM   8321  C  CA  . PRO   A 1 1050 ? -56.29800  87.60900  -17.93100 1.000 55.73550  ?  1048 PRO   A CA  1 
ATOM   8322  C  C   . PRO   A 1 1050 ? -57.26300  88.30600  -16.98500 1.000 55.08232  ?  1048 PRO   A C   1 
ATOM   8323  O  O   . PRO   A 1 1050 ? -56.81100  88.84600  -15.96800 1.000 62.80938  ?  1048 PRO   A O   1 
ATOM   8324  C  CB  . PRO   A 1 1050 ? -55.51200  88.62900  -18.76600 1.000 56.02129  ?  1048 PRO   A CB  1 
ATOM   8325  C  CG  . PRO   A 1 1050 ? -55.34300  87.98400  -20.10200 1.000 64.90792  ?  1048 PRO   A CG  1 
ATOM   8326  C  CD  . PRO   A 1 1050 ? -56.58400  87.17200  -20.31800 1.000 63.10164  ?  1048 PRO   A CD  1 
ATOM   8327  N  N   . ASP   A 1 1051 ? -58.56100  88.31300  -17.27800 1.000 53.46006  ?  1049 ASP   A N   1 
ATOM   8328  C  CA  . ASP   A 1 1051 ? -59.54500  88.97000  -16.43000 1.000 63.95681  ?  1049 ASP   A CA  1 
ATOM   8329  C  C   . ASP   A 1 1051 ? -60.09700  88.06100  -15.33900 1.000 63.18437  ?  1049 ASP   A C   1 
ATOM   8330  O  O   . ASP   A 1 1051 ? -61.10800  88.40700  -14.72000 1.000 63.98495  ?  1049 ASP   A O   1 
ATOM   8331  C  CB  . ASP   A 1 1051 ? -60.70000  89.50900  -17.27800 1.000 71.75235  ?  1049 ASP   A CB  1 
ATOM   8332  C  CG  . ASP   A 1 1051 ? -60.31800  90.74400  -18.06800 1.000 84.21668  ?  1049 ASP   A CG  1 
ATOM   8333  O  OD1 . ASP   A 1 1051 ? -59.34100  91.42100  -17.68000 1.000 65.86128  ?  1049 ASP   A OD1 1 
ATOM   8334  O  OD2 . ASP   A 1 1051 ? -61.00100  91.04100  -19.07100 1.000 67.43425  -1 1049 ASP   A OD2 1 
ATOM   8335  N  N   . THR   A 1 1052 ? -59.46400  86.91500  -15.08500 1.000 69.46614  ?  1050 THR   A N   1 
ATOM   8336  C  CA  . THR   A 1 1052 ? -59.96300  85.95800  -14.10600 1.000 56.83968  ?  1050 THR   A CA  1 
ATOM   8337  C  C   . THR   A 1 1052 ? -59.03300  85.79900  -12.90700 1.000 59.23311  ?  1050 THR   A C   1 
ATOM   8338  O  O   . THR   A 1 1052 ? -59.12500  84.80000  -12.18900 1.000 71.86236  ?  1050 THR   A O   1 
ATOM   8339  C  CB  . THR   A 1 1052 ? -60.20500  84.59800  -14.76300 1.000 47.08229  ?  1050 THR   A CB  1 
ATOM   8340  O  OG1 . THR   A 1 1052 ? -58.97400  84.09500  -15.29900 1.000 57.92275  ?  1050 THR   A OG1 1 
ATOM   8341  C  CG2 . THR   A 1 1052 ? -61.23000  84.72100  -15.88100 1.000 56.77731  ?  1050 THR   A CG2 1 
ATOM   8342  N  N   . ARG   A 1 1053 ? -58.14500  86.76300  -12.66900 1.000 45.50589  ?  1051 ARG   A N   1 
ATOM   8343  C  CA  . ARG   A 1 1053 ? -57.22000  86.68200  -11.54500 1.000 53.47026  ?  1051 ARG   A CA  1 
ATOM   8344  C  C   . ARG   A 1 1053 ? -57.77600  87.28900  -10.26300 1.000 64.98201  ?  1051 ARG   A C   1 
ATOM   8345  O  O   . ARG   A 1 1053 ? -57.09100  87.25800  -9.23500  1.000 59.97816  ?  1051 ARG   A O   1 
ATOM   8346  C  CB  . ARG   A 1 1053 ? -55.88900  87.35400  -11.89500 1.000 66.36684  ?  1051 ARG   A CB  1 
ATOM   8347  C  CG  . ARG   A 1 1053 ? -55.03800  86.56700  -12.88000 1.000 76.41833  ?  1051 ARG   A CG  1 
ATOM   8348  C  CD  . ARG   A 1 1053 ? -53.55000  86.69300  -12.57100 1.000 68.56042  ?  1051 ARG   A CD  1 
ATOM   8349  N  NE  . ARG   A 1 1053 ? -53.10000  85.71700  -11.58400 1.000 66.27267  ?  1051 ARG   A NE  1 
ATOM   8350  C  CZ  . ARG   A 1 1053 ? -52.81000  84.45200  -11.86100 1.000 68.65021  ?  1051 ARG   A CZ  1 
ATOM   8351  N  NH1 . ARG   A 1 1053 ? -52.94500  83.96500  -13.08400 1.000 68.43871  ?  1051 ARG   A NH1 1 
ATOM   8352  N  NH2 . ARG   A 1 1053 ? -52.37700  83.65600  -10.88800 1.000 60.88556  ?  1051 ARG   A NH2 1 
ATOM   8353  N  N   . GLU   A 1 1054 ? -58.99000  87.83900  -10.29400 1.000 64.58519  ?  1052 GLU   A N   1 
ATOM   8354  C  CA  . GLU   A 1 1054 ? -59.64800  88.34000  -9.09300  1.000 51.32443  ?  1052 GLU   A CA  1 
ATOM   8355  C  C   . GLU   A 1 1054 ? -60.95600  87.61000  -8.81400  1.000 48.96650  ?  1052 GLU   A C   1 
ATOM   8356  O  O   . GLU   A 1 1054 ? -61.74800  88.07100  -7.98300  1.000 49.11882  ?  1052 GLU   A O   1 
ATOM   8357  C  CB  . GLU   A 1 1054 ? -59.90500  89.84700  -9.20600  1.000 38.43679  ?  1052 GLU   A CB  1 
ATOM   8358  C  CG  . GLU   A 1 1054 ? -58.70100  90.67600  -9.64300  1.000 49.82817  ?  1052 GLU   A CG  1 
ATOM   8359  C  CD  . GLU   A 1 1054 ? -57.75800  91.02000  -8.50100  1.000 73.91041  ?  1052 GLU   A CD  1 
ATOM   8360  O  OE1 . GLU   A 1 1054 ? -57.37300  90.11000  -7.73700  1.000 83.43461  ?  1052 GLU   A OE1 1 
ATOM   8361  O  OE2 . GLU   A 1 1054 ? -57.40300  92.21100  -8.36800  1.000 102.61015 -1 1052 GLU   A OE2 1 
ATOM   8362  N  N   . LEU   A 1 1055 ? -61.20000  86.48700  -9.48200  1.000 44.25362  ?  1053 LEU   A N   1 
ATOM   8363  C  CA  . LEU   A 1 1055 ? -62.45000  85.74900  -9.36900  1.000 48.08242  ?  1053 LEU   A CA  1 
ATOM   8364  C  C   . LEU   A 1 1055 ? -62.26700  84.53900  -8.46100  1.000 46.34526  ?  1053 LEU   A C   1 
ATOM   8365  O  O   . LEU   A 1 1055 ? -61.21100  83.90100  -8.46300  1.000 53.33700  ?  1053 LEU   A O   1 
ATOM   8366  C  CB  . LEU   A 1 1055 ? -62.94200  85.29300  -10.74700 1.000 44.66212  ?  1053 LEU   A CB  1 
ATOM   8367  C  CG  . LEU   A 1 1055 ? -63.58900  86.31200  -11.69300 1.000 43.56825  ?  1053 LEU   A CG  1 
ATOM   8368  C  CD1 . LEU   A 1 1055 ? -62.61300  87.39700  -12.12500 1.000 61.52364  ?  1053 LEU   A CD1 1 
ATOM   8369  C  CD2 . LEU   A 1 1055 ? -64.17200  85.60800  -12.91000 1.000 38.59610  ?  1053 LEU   A CD2 1 
ATOM   8370  N  N   . LEU   A 1 1056 ? -63.30600  84.22600  -7.69000  1.000 37.34090  ?  1054 LEU   A N   1 
ATOM   8371  C  CA  . LEU   A 1 1056 ? -63.29500  83.07200  -6.79700  1.000 31.94906  ?  1054 LEU   A CA  1 
ATOM   8372  C  C   . LEU   A 1 1056 ? -63.87400  81.87300  -7.53900  1.000 37.40672  ?  1054 LEU   A C   1 
ATOM   8373  O  O   . LEU   A 1 1056 ? -65.08200  81.81200  -7.79100  1.000 45.16238  ?  1054 LEU   A O   1 
ATOM   8374  C  CB  . LEU   A 1 1056 ? -64.08900  83.36100  -5.52600  1.000 36.02824  ?  1054 LEU   A CB  1 
ATOM   8375  C  CG  . LEU   A 1 1056 ? -63.27600  83.49900  -4.23800  1.000 38.44403  ?  1054 LEU   A CG  1 
ATOM   8376  C  CD1 . LEU   A 1 1056 ? -62.36900  84.71700  -4.30200  1.000 58.02532  ?  1054 LEU   A CD1 1 
ATOM   8377  C  CD2 . LEU   A 1 1056 ? -64.19300  83.56800  -3.02800  1.000 31.97417  ?  1054 LEU   A CD2 1 
ATOM   8378  N  N   . GLY   A 1 1057 ? -63.01700  80.91900  -7.88400  1.000 47.16099  ?  1055 GLY   A N   1 
ATOM   8379  C  CA  . GLY   A 1 1057 ? -63.47300  79.74500  -8.60400  1.000 56.07455  ?  1055 GLY   A CA  1 
ATOM   8380  C  C   . GLY   A 1 1057 ? -62.35700  78.73500  -8.73700  1.000 56.80195  ?  1055 GLY   A C   1 
ATOM   8381  O  O   . GLY   A 1 1057 ? -61.21600  78.97500  -8.33500  1.000 49.70388  ?  1055 GLY   A O   1 
ATOM   8382  N  N   . MET   A 1 1058 ? -62.70800  77.58800  -9.31100  1.000 45.14984  ?  1056 MET   A N   1 
ATOM   8383  C  CA  . MET   A 1 1058 ? -61.75400  76.51300  -9.55900  1.000 38.55202  ?  1056 MET   A CA  1 
ATOM   8384  C  C   . MET   A 1 1058 ? -61.21200  76.65600  -10.97600 1.000 48.36947  ?  1056 MET   A C   1 
ATOM   8385  O  O   . MET   A 1 1058 ? -61.95500  76.50400  -11.95100 1.000 41.01313  ?  1056 MET   A O   1 
ATOM   8386  C  CB  . MET   A 1 1058 ? -62.41100  75.15000  -9.35800  1.000 49.67354  ?  1056 MET   A CB  1 
ATOM   8387  C  CG  . MET   A 1 1058 ? -61.60200  73.97000  -9.88200  1.000 44.57804  ?  1056 MET   A CG  1 
ATOM   8388  S  SD  . MET   A 1 1058 ? -59.96100  73.83700  -9.14400  1.000 63.02283  ?  1056 MET   A SD  1 
ATOM   8389  C  CE  . MET   A 1 1058 ? -59.66600  72.07600  -9.29200  1.000 48.31474  ?  1056 MET   A CE  1 
ATOM   8390  N  N   . PHE   A 1 1059 ? -59.91700  76.95400  -11.08600 1.000 59.10290  ?  1057 PHE   A N   1 
ATOM   8391  C  CA  . PHE   A 1 1059 ? -59.25000  77.07500  -12.37300 1.000 52.71298  ?  1057 PHE   A CA  1 
ATOM   8392  C  C   . PHE   A 1 1059 ? -58.10500  76.09300  -12.56000 1.000 45.33985  ?  1057 PHE   A C   1 
ATOM   8393  O  O   . PHE   A 1 1059 ? -57.67000  75.89400  -13.69900 1.000 49.79598  ?  1057 PHE   A O   1 
ATOM   8394  C  CB  . PHE   A 1 1059 ? -58.70000  78.49900  -12.56700 1.000 44.61170  ?  1057 PHE   A CB  1 
ATOM   8395  C  CG  . PHE   A 1 1059 ? -59.75300  79.57300  -12.57800 1.000 48.68713  ?  1057 PHE   A CG  1 
ATOM   8396  C  CD1 . PHE   A 1 1059 ? -60.32500  80.01600  -11.39600 1.000 62.08660  ?  1057 PHE   A CD1 1 
ATOM   8397  C  CD2 . PHE   A 1 1059 ? -60.15000  80.15900  -13.76800 1.000 53.74000  ?  1057 PHE   A CD2 1 
ATOM   8398  C  CE1 . PHE   A 1 1059 ? -61.28600  81.01000  -11.40400 1.000 58.01176  ?  1057 PHE   A CE1 1 
ATOM   8399  C  CE2 . PHE   A 1 1059 ? -61.11000  81.15400  -13.78100 1.000 47.50095  ?  1057 PHE   A CE2 1 
ATOM   8400  C  CZ  . PHE   A 1 1059 ? -61.67700  81.58000  -12.59800 1.000 52.01718  ?  1057 PHE   A CZ  1 
ATOM   8401  N  N   . VAL   A 1 1060 ? -57.62100  75.46600  -11.48400 1.000 46.18076  ?  1058 VAL   A N   1 
ATOM   8402  C  CA  . VAL   A 1 1060 ? -56.38900  74.68700  -11.54200 1.000 45.58488  ?  1058 VAL   A CA  1 
ATOM   8403  C  C   . VAL   A 1 1060 ? -56.53900  73.51200  -12.49800 1.000 50.94270  ?  1058 VAL   A C   1 
ATOM   8404  O  O   . VAL   A 1 1060 ? -57.50700  72.74400  -12.42300 1.000 52.71421  ?  1058 VAL   A O   1 
ATOM   8405  C  CB  . VAL   A 1 1060 ? -56.00300  74.21700  -10.13200 1.000 37.69385  ?  1058 VAL   A CB  1 
ATOM   8406  C  CG1 . VAL   A 1 1060 ? -54.98800  73.09100  -10.20400 1.000 51.02212  ?  1058 VAL   A CG1 1 
ATOM   8407  C  CG2 . VAL   A 1 1060 ? -55.45400  75.38100  -9.32100  1.000 47.02712  ?  1058 VAL   A CG2 1 
ATOM   8408  N  N   . ASN   A 1 1061 ? -55.57200  73.36700  -13.40200 1.000 43.42620  ?  1059 ASN   A N   1 
ATOM   8409  C  CA  . ASN   A 1 1061 ? -55.50800  72.24600  -14.32700 1.000 52.28931  ?  1059 ASN   A CA  1 
ATOM   8410  C  C   . ASN   A 1 1061 ? -54.28700  71.38700  -14.01800 1.000 40.99082  ?  1059 ASN   A C   1 
ATOM   8411  O  O   . ASN   A 1 1061 ? -53.23600  71.89400  -13.61600 1.000 38.12628  ?  1059 ASN   A O   1 
ATOM   8412  C  CB  . ASN   A 1 1061 ? -55.45100  72.72500  -15.78100 1.000 41.78334  ?  1059 ASN   A CB  1 
ATOM   8413  C  CG  . ASN   A 1 1061 ? -55.71800  71.60800  -16.77400 1.000 64.35413  ?  1059 ASN   A CG  1 
ATOM   8414  O  OD1 . ASN   A 1 1061 ? -56.43500  70.65300  -16.47300 1.000 62.50574  ?  1059 ASN   A OD1 1 
ATOM   8415  N  ND2 . ASN   A 1 1061 ? -55.14100  71.72300  -17.96500 1.000 57.41762  ?  1059 ASN   A ND2 1 
ATOM   8416  N  N   . THR   A 1 1062 ? -54.43700  70.08100  -14.21400 1.000 41.53840  ?  1060 THR   A N   1 
ATOM   8417  C  CA  . THR   A 1 1062 ? -53.39500  69.11100  -13.90500 1.000 38.94674  ?  1060 THR   A CA  1 
ATOM   8418  C  C   . THR   A 1 1062 ? -52.65400  68.72600  -15.17900 1.000 47.60550  ?  1060 THR   A C   1 
ATOM   8419  O  O   . THR   A 1 1062 ? -53.28100  68.40400  -16.19400 1.000 51.13290  ?  1060 THR   A O   1 
ATOM   8420  C  CB  . THR   A 1 1062 ? -53.99700  67.86900  -13.24600 1.000 40.47683  ?  1060 THR   A CB  1 
ATOM   8421  O  OG1 . THR   A 1 1062 ? -54.71000  68.25400  -12.06400 1.000 51.74497  ?  1060 THR   A OG1 1 
ATOM   8422  C  CG2 . THR   A 1 1062 ? -52.90800  66.88400  -12.87500 1.000 43.39800  ?  1060 THR   A CG2 1 
ATOM   8423  N  N   . LEU   A 1 1063 ? -51.32300  68.75400  -15.12200 1.000 44.24072  ?  1061 LEU   A N   1 
ATOM   8424  C  CA  . LEU   A 1 1063 ? -50.49200  68.46100  -16.27600 1.000 34.93822  ?  1061 LEU   A CA  1 
ATOM   8425  C  C   . LEU   A 1 1063 ? -49.58900  67.26700  -16.00000 1.000 36.84655  ?  1061 LEU   A C   1 
ATOM   8426  O  O   . LEU   A 1 1063 ? -48.94300  67.21300  -14.94400 1.000 44.16157  ?  1061 LEU   A O   1 
ATOM   8427  C  CB  . LEU   A 1 1063 ? -49.63200  69.67000  -16.65800 1.000 35.17158  ?  1061 LEU   A CB  1 
ATOM   8428  C  CG  . LEU   A 1 1063 ? -50.35000  70.91200  -17.17500 1.000 43.85556  ?  1061 LEU   A CG  1 
ATOM   8429  C  CD1 . LEU   A 1 1063 ? -49.34500  71.81100  -17.86400 1.000 34.84236  ?  1061 LEU   A CD1 1 
ATOM   8430  C  CD2 . LEU   A 1 1063 ? -51.48400  70.53600  -18.11600 1.000 50.66956  ?  1061 LEU   A CD2 1 
ATOM   8431  N  N   . PRO   A 1 1064 ? -49.51300  66.29900  -16.91500 1.000 44.23149  ?  1062 PRO   A N   1 
ATOM   8432  C  CA  . PRO   A 1 1064 ? -48.54400  65.19900  -16.78200 1.000 41.77474  ?  1062 PRO   A CA  1 
ATOM   8433  C  C   . PRO   A 1 1064 ? -47.17600  65.63300  -17.28800 1.000 27.01403  ?  1062 PRO   A C   1 
ATOM   8434  O  O   . PRO   A 1 1064 ? -47.03400  66.06500  -18.43400 1.000 40.69515  ?  1062 PRO   A O   1 
ATOM   8435  C  CB  . PRO   A 1 1064 ? -49.14500  64.09500  -17.65800 1.000 32.11721  ?  1062 PRO   A CB  1 
ATOM   8436  C  CG  . PRO   A 1 1064 ? -49.91900  64.84100  -18.69300 1.000 42.91609  ?  1062 PRO   A CG  1 
ATOM   8437  C  CD  . PRO   A 1 1064 ? -50.43000  66.10100  -18.05100 1.000 42.94152  ?  1062 PRO   A CD  1 
ATOM   8438  N  N   . LEU   A 1 1065 ? -46.16600  65.51600  -16.43200 1.000 36.79004  ?  1063 LEU   A N   1 
ATOM   8439  C  CA  . LEU   A 1 1065 ? -44.80800  65.94900  -16.74400 1.000 44.67508  ?  1063 LEU   A CA  1 
ATOM   8440  C  C   . LEU   A 1 1065 ? -43.93900  64.72500  -17.00500 1.000 51.33559  ?  1063 LEU   A C   1 
ATOM   8441  O  O   . LEU   A 1 1065 ? -43.59400  63.98900  -16.07300 1.000 49.61246  ?  1063 LEU   A O   1 
ATOM   8442  C  CB  . LEU   A 1 1065 ? -44.23400  66.79700  -15.61100 1.000 41.05216  ?  1063 LEU   A CB  1 
ATOM   8443  C  CG  . LEU   A 1 1065 ? -44.56400  68.29000  -15.65400 1.000 41.89653  ?  1063 LEU   A CG  1 
ATOM   8444  C  CD1 . LEU   A 1 1065 ? -44.13500  68.96900  -14.36600 1.000 42.25897  ?  1063 LEU   A CD1 1 
ATOM   8445  C  CD2 . LEU   A 1 1065 ? -43.88500  68.93900  -16.84800 1.000 49.26293  ?  1063 LEU   A CD2 1 
ATOM   8446  N  N   . LEU   A 1 1066 ? -43.58700  64.51200  -18.27000 1.000 30.35687  ?  1064 LEU   A N   1 
ATOM   8447  C  CA  . LEU   A 1 1066 ? -42.64300  63.46900  -18.65700 1.000 30.91997  ?  1064 LEU   A CA  1 
ATOM   8448  C  C   . LEU   A 1 1066 ? -41.25500  64.09600  -18.74800 1.000 39.33347  ?  1064 LEU   A C   1 
ATOM   8449  O  O   . LEU   A 1 1066 ? -40.99400  64.92200  -19.62900 1.000 45.07595  ?  1064 LEU   A O   1 
ATOM   8450  C  CB  . LEU   A 1 1066 ? -43.06400  62.83100  -19.97900 1.000 29.58974  ?  1064 LEU   A CB  1 
ATOM   8451  C  CG  . LEU   A 1 1066 ? -42.02000  62.05400  -20.78600 1.000 54.22975  ?  1064 LEU   A CG  1 
ATOM   8452  C  CD1 . LEU   A 1 1066 ? -41.39400  60.95200  -19.95400 1.000 52.75938  ?  1064 LEU   A CD1 1 
ATOM   8453  C  CD2 . LEU   A 1 1066 ? -42.64500  61.48100  -22.05100 1.000 35.86271  ?  1064 LEU   A CD2 1 
ATOM   8454  N  N   . LEU   A 1 1067 ? -40.36800  63.71000  -17.83600 1.000 33.02920  ?  1065 LEU   A N   1 
ATOM   8455  C  CA  . LEU   A 1 1067 ? -39.04100  64.29400  -17.73300 1.000 40.67775  ?  1065 LEU   A CA  1 
ATOM   8456  C  C   . LEU   A 1 1067 ? -37.97800  63.20800  -17.82700 1.000 43.81028  ?  1065 LEU   A C   1 
ATOM   8457  O  O   . LEU   A 1 1067 ? -38.23400  62.03000  -17.56500 1.000 50.91054  ?  1065 LEU   A O   1 
ATOM   8458  C  CB  . LEU   A 1 1067 ? -38.88200  65.07500  -16.42300 1.000 33.77845  ?  1065 LEU   A CB  1 
ATOM   8459  C  CG  . LEU   A 1 1067 ? -39.84300  66.25000  -16.23900 1.000 30.92552  ?  1065 LEU   A CG  1 
ATOM   8460  C  CD1 . LEU   A 1 1067 ? -39.82300  66.73700  -14.80400 1.000 47.60284  ?  1065 LEU   A CD1 1 
ATOM   8461  C  CD2 . LEU   A 1 1067 ? -39.49000  67.38000  -17.18900 1.000 37.96473  ?  1065 LEU   A CD2 1 
ATOM   8462  N  N   . SER   A 1 1068 ? -36.77200  63.62500  -18.20700 1.000 37.52652  ?  1066 SER   A N   1 
ATOM   8463  C  CA  . SER   A 1 1068 ? -35.64300  62.72300  -18.38200 1.000 38.35006  ?  1066 SER   A CA  1 
ATOM   8464  C  C   . SER   A 1 1068 ? -34.47700  63.20000  -17.53100 1.000 46.19064  ?  1066 SER   A C   1 
ATOM   8465  O  O   . SER   A 1 1068 ? -34.24900  64.40600  -17.39300 1.000 56.13727  ?  1066 SER   A O   1 
ATOM   8466  C  CB  . SER   A 1 1068 ? -35.21500  62.64100  -19.85200 1.000 36.68158  ?  1066 SER   A CB  1 
ATOM   8467  O  OG  . SER   A 1 1068 ? -36.32100  62.36700  -20.69400 1.000 60.37133  ?  1066 SER   A OG  1 
ATOM   8468  N  N   . ILE   A 1 1069 ? -33.74100  62.24800  -16.96600 1.000 46.72215  ?  1067 ILE   A N   1 
ATOM   8469  C  CA  . ILE   A 1 1069 ? -32.58600  62.53400  -16.12300 1.000 42.38646  ?  1067 ILE   A CA  1 
ATOM   8470  C  C   . ILE   A 1 1069 ? -31.39400  61.76400  -16.66800 1.000 43.80513  ?  1067 ILE   A C   1 
ATOM   8471  O  O   . ILE   A 1 1069 ? -31.46100  60.54000  -16.82700 1.000 54.70495  ?  1067 ILE   A O   1 
ATOM   8472  C  CB  . ILE   A 1 1069 ? -32.84300  62.16000  -14.65200 1.000 36.63475  ?  1067 ILE   A CB  1 
ATOM   8473  C  CG1 . ILE   A 1 1069 ? -34.00800  62.97600  -14.08700 1.000 51.62591  ?  1067 ILE   A CG1 1 
ATOM   8474  C  CG2 . ILE   A 1 1069 ? -31.58400  62.36700  -13.82000 1.000 34.75318  ?  1067 ILE   A CG2 1 
ATOM   8475  C  CD1 . ILE   A 1 1069 ? -33.78100  64.47500  -14.12100 1.000 44.08110  ?  1067 ILE   A CD1 1 
ATOM   8476  N  N   . ASP   A 1 1070 ? -30.31100  62.47900  -16.96000 1.000 37.94788  ?  1068 ASP   A N   1 
ATOM   8477  C  CA  . ASP   A 1 1070 ? -29.04900  61.86900  -17.37000 1.000 43.76702  ?  1068 ASP   A CA  1 
ATOM   8478  C  C   . ASP   A 1 1070 ? -28.12900  61.86900  -16.15400 1.000 43.63469  ?  1068 ASP   A C   1 
ATOM   8479  O  O   . ASP   A 1 1070 ? -27.58100  62.90700  -15.77700 1.000 38.27828  ?  1068 ASP   A O   1 
ATOM   8480  C  CB  . ASP   A 1 1070 ? -28.43100  62.62200  -18.54500 1.000 43.71874  ?  1068 ASP   A CB  1 
ATOM   8481  C  CG  . ASP   A 1 1070 ? -27.27000  61.87200  -19.17900 1.000 50.40698  ?  1068 ASP   A CG  1 
ATOM   8482  O  OD1 . ASP   A 1 1070 ? -26.91500  60.78000  -18.68500 1.000 63.83975  ?  1068 ASP   A OD1 1 
ATOM   8483  O  OD2 . ASP   A 1 1070 ? -26.71500  62.37500  -20.17700 1.000 56.83664  -1 1068 ASP   A OD2 1 
ATOM   8484  N  N   . HIS   A 1 1071 ? -27.96500  60.69500  -15.53700 1.000 43.22197  ?  1069 HIS   A N   1 
ATOM   8485  C  CA  . HIS   A 1 1071 ? -27.09500  60.57600  -14.37400 1.000 48.50979  ?  1069 HIS   A CA  1 
ATOM   8486  C  C   . HIS   A 1 1071 ? -25.62700  60.80100  -14.71600 1.000 51.73070  ?  1069 HIS   A C   1 
ATOM   8487  O  O   . HIS   A 1 1071 ? -24.83100  61.07400  -13.81100 1.000 56.13388  ?  1069 HIS   A O   1 
ATOM   8488  C  CB  . HIS   A 1 1071 ? -27.27500  59.20500  -13.72400 1.000 34.14050  ?  1069 HIS   A CB  1 
ATOM   8489  C  CG  . HIS   A 1 1071 ? -28.67600  58.93400  -13.27300 1.000 35.95629  ?  1069 HIS   A CG  1 
ATOM   8490  N  ND1 . HIS   A 1 1071 ? -29.11000  59.20200  -11.99300 1.000 33.65820  ?  1069 HIS   A ND1 1 
ATOM   8491  C  CD2 . HIS   A 1 1071 ? -29.74300  58.43000  -13.93600 1.000 40.45762  ?  1069 HIS   A CD2 1 
ATOM   8492  C  CE1 . HIS   A 1 1071 ? -30.38400  58.86800  -11.88500 1.000 53.02851  ?  1069 HIS   A CE1 1 
ATOM   8493  N  NE2 . HIS   A 1 1071 ? -30.79200  58.39700  -13.05000 1.000 39.96368  ?  1069 HIS   A NE2 1 
ATOM   8494  N  N   . GLU   A 1 1072 ? -25.25600  60.69900  -15.99100 1.000 38.20630  ?  1070 GLU   A N   1 
ATOM   8495  C  CA  . GLU   A 1 1072 ? -23.88400  60.89900  -16.43800 1.000 46.42677  ?  1070 GLU   A CA  1 
ATOM   8496  C  C   . GLU   A 1 1072 ? -23.55900  62.36100  -16.71700 1.000 52.11057  ?  1070 GLU   A C   1 
ATOM   8497  O  O   . GLU   A 1 1072 ? -22.44600  62.66000  -17.16500 1.000 62.00577  ?  1070 GLU   A O   1 
ATOM   8498  C  CB  . GLU   A 1 1072 ? -23.61700  60.06400  -17.69700 1.000 47.43192  ?  1070 GLU   A CB  1 
ATOM   8499  C  CG  . GLU   A 1 1072 ? -23.81900  58.56400  -17.51400 1.000 62.29406  ?  1070 GLU   A CG  1 
ATOM   8500  C  CD  . GLU   A 1 1072 ? -22.56800  57.85900  -17.02900 1.000 62.51525  ?  1070 GLU   A CD  1 
ATOM   8501  O  OE1 . GLU   A 1 1072 ? -21.47800  58.46400  -17.10600 1.000 58.92815  ?  1070 GLU   A OE1 1 
ATOM   8502  O  OE2 . GLU   A 1 1072 ? -22.67200  56.70200  -16.57100 1.000 64.86386  -1 1070 GLU   A OE2 1 
ATOM   8503  N  N   . GLU   A 1 1073 ? -24.49500  63.27700  -16.47200 1.000 39.22448  ?  1071 GLU   A N   1 
ATOM   8504  C  CA  . GLU   A 1 1073 ? -24.28700  64.69400  -16.72400 1.000 45.04415  ?  1071 GLU   A CA  1 
ATOM   8505  C  C   . GLU   A 1 1073 ? -24.56200  65.48800  -15.45500 1.000 52.40878  ?  1071 GLU   A C   1 
ATOM   8506  O  O   . GLU   A 1 1073 ? -25.04800  64.96000  -14.45100 1.000 55.39150  ?  1071 GLU   A O   1 
ATOM   8507  C  CB  . GLU   A 1 1073 ? -25.16900  65.19700  -17.87600 1.000 49.67023  ?  1071 GLU   A CB  1 
ATOM   8508  C  CG  . GLU   A 1 1073 ? -24.74600  64.69600  -19.25400 1.000 32.20049  ?  1071 GLU   A CG  1 
ATOM   8509  C  CD  . GLU   A 1 1073 ? -23.53500  65.43200  -19.79500 1.000 59.69102  ?  1071 GLU   A CD  1 
ATOM   8510  O  OE1 . GLU   A 1 1073 ? -23.11200  66.41800  -19.15700 1.000 64.21478  ?  1071 GLU   A OE1 1 
ATOM   8511  O  OE2 . GLU   A 1 1073 ? -23.01000  65.03200  -20.85700 1.000 73.30783  -1 1071 GLU   A OE2 1 
ATOM   8512  N  N   . SER   A 1 1074 ? -24.25000  66.77800  -15.51700 1.000 53.15037  ?  1072 SER   A N   1 
ATOM   8513  C  CA  . SER   A 1 1074 ? -24.28700  67.62200  -14.33500 1.000 49.62856  ?  1072 SER   A CA  1 
ATOM   8514  C  C   . SER   A 1 1074 ? -25.72400  67.97900  -13.95600 1.000 57.10585  ?  1072 SER   A C   1 
ATOM   8515  O  O   . SER   A 1 1074 ? -26.67100  67.80600  -14.73100 1.000 62.91740  ?  1072 SER   A O   1 
ATOM   8516  C  CB  . SER   A 1 1074 ? -23.45700  68.88500  -14.56300 1.000 41.13082  ?  1072 SER   A CB  1 
ATOM   8517  O  OG  . SER   A 1 1074 ? -23.18100  69.07200  -15.94200 1.000 59.20387  ?  1072 SER   A OG  1 
ATOM   8518  N  N   . PHE   A 1 1075 ? -25.87400  68.46500  -12.72000 1.000 44.68281  ?  1073 PHE   A N   1 
ATOM   8519  C  CA  . PHE   A 1 1075 ? -27.15000  69.01500  -12.27300 1.000 45.82506  ?  1073 PHE   A CA  1 
ATOM   8520  C  C   . PHE   A 1 1075 ? -27.58400  70.17200  -13.16900 1.000 45.75455  ?  1073 PHE   A C   1 
ATOM   8521  O  O   . PHE   A 1 1075 ? -28.74300  70.24200  -13.59500 1.000 55.18833  ?  1073 PHE   A O   1 
ATOM   8522  C  CB  . PHE   A 1 1075 ? -27.02900  69.46300  -10.81300 1.000 44.75968  ?  1073 PHE   A CB  1 
ATOM   8523  C  CG  . PHE   A 1 1075 ? -28.30700  69.99200  -10.21900 1.000 40.04986  ?  1073 PHE   A CG  1 
ATOM   8524  C  CD1 . PHE   A 1 1075 ? -29.49800  69.30500  -10.37100 1.000 38.28476  ?  1073 PHE   A CD1 1 
ATOM   8525  C  CD2 . PHE   A 1 1075 ? -28.30800  71.16800  -9.48200  1.000 42.12119  ?  1073 PHE   A CD2 1 
ATOM   8526  C  CE1 . PHE   A 1 1075 ? -30.67200  69.78900  -9.81700  1.000 47.85299  ?  1073 PHE   A CE1 1 
ATOM   8527  C  CE2 . PHE   A 1 1075 ? -29.47700  71.65600  -8.92500  1.000 42.22917  ?  1073 PHE   A CE2 1 
ATOM   8528  C  CZ  . PHE   A 1 1075 ? -30.66000  70.96600  -9.09300  1.000 42.60863  ?  1073 PHE   A CZ  1 
ATOM   8529  N  N   . LEU   A 1 1076 ? -26.65400  71.08100  -13.48500 1.000 35.71308  ?  1074 LEU   A N   1 
ATOM   8530  C  CA  . LEU   A 1 1076 ? -26.97300  72.20300  -14.36500 1.000 33.63056  ?  1074 LEU   A CA  1 
ATOM   8531  C  C   . LEU   A 1 1076 ? -27.40800  71.72500  -15.74300 1.000 38.93440  ?  1074 LEU   A C   1 
ATOM   8532  O  O   . LEU   A 1 1076 ? -28.27900  72.33900  -16.37200 1.000 49.23421  ?  1074 LEU   A O   1 
ATOM   8533  C  CB  . LEU   A 1 1076 ? -25.77200  73.14100  -14.48200 1.000 33.54582  ?  1074 LEU   A CB  1 
ATOM   8534  C  CG  . LEU   A 1 1076 ? -25.47900  73.97500  -13.23600 1.000 54.17114  ?  1074 LEU   A CG  1 
ATOM   8535  C  CD1 . LEU   A 1 1076 ? -24.23000  74.82000  -13.41900 1.000 56.00796  ?  1074 LEU   A CD1 1 
ATOM   8536  C  CD2 . LEU   A 1 1076 ? -26.67600  74.85100  -12.90500 1.000 66.31451  ?  1074 LEU   A CD2 1 
ATOM   8537  N  N   . HIS   A 1 1077 ? -26.80500  70.64200  -16.23900 1.000 34.97227  ?  1075 HIS   A N   1 
ATOM   8538  C  CA  . HIS   A 1 1077 ? -27.24000  70.08400  -17.51600 1.000 51.00654  ?  1075 HIS   A CA  1 
ATOM   8539  C  C   . HIS   A 1 1077 ? -28.67200  69.57400  -17.42100 1.000 51.19876  ?  1075 HIS   A C   1 
ATOM   8540  O  O   . HIS   A 1 1077 ? -29.51400  69.88600  -18.27200 1.000 50.05177  ?  1075 HIS   A O   1 
ATOM   8541  C  CB  . HIS   A 1 1077 ? -26.29700  68.96300  -17.95600 1.000 38.11143  ?  1075 HIS   A CB  1 
ATOM   8542  C  CG  . HIS   A 1 1077 ? -26.67600  68.33400  -19.26200 1.000 46.59021  ?  1075 HIS   A CG  1 
ATOM   8543  N  ND1 . HIS   A 1 1077 ? -26.11400  68.71300  -20.46200 1.000 51.10379  ?  1075 HIS   A ND1 1 
ATOM   8544  C  CD2 . HIS   A 1 1077 ? -27.56900  67.35900  -19.55700 1.000 44.89060  ?  1075 HIS   A CD2 1 
ATOM   8545  C  CE1 . HIS   A 1 1077 ? -26.64000  67.99600  -21.43900 1.000 54.86809  ?  1075 HIS   A CE1 1 
ATOM   8546  N  NE2 . HIS   A 1 1077 ? -27.52600  67.16700  -20.91700 1.000 48.41218  ?  1075 HIS   A NE2 1 
ATOM   8547  N  N   . ASN   A 1 1078 ? -28.96900  68.79000  -16.38100 1.000 35.55017  ?  1076 ASN   A N   1 
ATOM   8548  C  CA  . ASN   A 1 1078 ? -30.32400  68.27800  -16.20900 1.000 46.43575  ?  1076 ASN   A CA  1 
ATOM   8549  C  C   . ASN   A 1 1078 ? -31.30700  69.39300  -15.87800 1.000 42.96693  ?  1076 ASN   A C   1 
ATOM   8550  O  O   . ASN   A 1 1078 ? -32.49400  69.28500  -16.20400 1.000 41.88972  ?  1076 ASN   A O   1 
ATOM   8551  C  CB  . ASN   A 1 1078 ? -30.34600  67.20200  -15.12200 1.000 43.08097  ?  1076 ASN   A CB  1 
ATOM   8552  C  CG  . ASN   A 1 1078 ? -29.67400  65.91500  -15.56400 1.000 39.86311  ?  1076 ASN   A CG  1 
ATOM   8553  O  OD1 . ASN   A 1 1078 ? -30.32900  64.99800  -16.06200 1.000 43.08968  ?  1076 ASN   A OD1 1 
ATOM   8554  N  ND2 . ASN   A 1 1078 ? -28.35900  65.84100  -15.38600 1.000 42.19540  ?  1076 ASN   A ND2 1 
ATOM   8555  N  N   . LEU   A 1 1079 ? -30.83700  70.46600  -15.23700 1.000 48.46380  ?  1077 LEU   A N   1 
ATOM   8556  C  CA  . LEU   A 1 1079 ? -31.70100  71.61400  -14.98500 1.000 35.66834  ?  1077 LEU   A CA  1 
ATOM   8557  C  C   . LEU   A 1 1079 ? -32.17200  72.24600  -16.28800 1.000 43.86244  ?  1077 LEU   A C   1 
ATOM   8558  O  O   . LEU   A 1 1079 ? -33.34600  72.60900  -16.42400 1.000 49.01259  ?  1077 LEU   A O   1 
ATOM   8559  C  CB  . LEU   A 1 1079 ? -30.96700  72.64600  -14.13000 1.000 26.55294  ?  1077 LEU   A CB  1 
ATOM   8560  C  CG  . LEU   A 1 1079 ? -30.96300  72.43200  -12.61900 1.000 31.55863  ?  1077 LEU   A CG  1 
ATOM   8561  C  CD1 . LEU   A 1 1079 ? -29.99700  73.39500  -11.95500 1.000 30.19359  ?  1077 LEU   A CD1 1 
ATOM   8562  C  CD2 . LEU   A 1 1079 ? -32.36200  72.61900  -12.07100 1.000 34.85480  ?  1077 LEU   A CD2 1 
ATOM   8563  N  N   . GLN   A 1 1080 ? -31.26700  72.38700  -17.25900 1.000 39.07439  ?  1078 GLN   A N   1 
ATOM   8564  C  CA  . GLN   A 1 1080 ? -31.63900  73.00200  -18.52700 1.000 40.69293  ?  1078 GLN   A CA  1 
ATOM   8565  C  C   . GLN   A 1 1080 ? -32.49200  72.07000  -19.37700 1.000 43.60895  ?  1078 GLN   A C   1 
ATOM   8566  O  O   . GLN   A 1 1080 ? -33.37800  72.53500  -20.10300 1.000 54.99287  ?  1078 GLN   A O   1 
ATOM   8567  C  CB  . GLN   A 1 1080 ? -30.38400  73.42500  -19.29100 1.000 53.42979  ?  1078 GLN   A CB  1 
ATOM   8568  C  CG  . GLN   A 1 1080 ? -29.54600  74.47100  -18.56800 1.000 51.95078  ?  1078 GLN   A CG  1 
ATOM   8569  C  CD  . GLN   A 1 1080 ? -30.28700  75.78200  -18.37400 1.000 66.95528  ?  1078 GLN   A CD  1 
ATOM   8570  O  OE1 . GLN   A 1 1080 ? -30.90800  76.30200  -19.30200 1.000 81.20736  ?  1078 GLN   A OE1 1 
ATOM   8571  N  NE2 . GLN   A 1 1080 ? -30.22600  76.32100  -17.16200 1.000 52.41638  ?  1078 GLN   A NE2 1 
ATOM   8572  N  N   . GLN   A 1 1081 ? -32.24700  70.76100  -19.30100 1.000 41.89335  ?  1079 GLN   A N   1 
ATOM   8573  C  CA  . GLN   A 1 1081 ? -33.05500  69.80900  -20.05100 1.000 43.51355  ?  1079 GLN   A CA  1 
ATOM   8574  C  C   . GLN   A 1 1081 ? -34.43200  69.59800  -19.43600 1.000 44.38363  ?  1079 GLN   A C   1 
ATOM   8575  O  O   . GLN   A 1 1081 ? -35.36300  69.21500  -20.15400 1.000 47.66222  ?  1079 GLN   A O   1 
ATOM   8576  C  CB  . GLN   A 1 1081 ? -32.32300  68.47100  -20.16900 1.000 39.83877  ?  1079 GLN   A CB  1 
ATOM   8577  C  CG  . GLN   A 1 1081 ? -31.71200  68.22400  -21.54100 1.000 35.30146  ?  1079 GLN   A CG  1 
ATOM   8578  C  CD  . GLN   A 1 1081 ? -30.73000  69.30700  -21.95100 1.000 73.35470  ?  1079 GLN   A CD  1 
ATOM   8579  O  OE1 . GLN   A 1 1081 ? -29.73700  69.55400  -21.26600 1.000 67.93841  ?  1079 GLN   A OE1 1 
ATOM   8580  N  NE2 . GLN   A 1 1081 ? -31.00500  69.96100  -23.07400 1.000 84.04611  ?  1079 GLN   A NE2 1 
ATOM   8581  N  N   . VAL   A 1 1082 ? -34.58300  69.83300  -18.13100 1.000 34.65942  ?  1080 VAL   A N   1 
ATOM   8582  C  CA  . VAL   A 1 1082 ? -35.91000  69.81000  -17.52600 1.000 42.41187  ?  1080 VAL   A CA  1 
ATOM   8583  C  C   . VAL   A 1 1082 ? -36.73900  70.98800  -18.02600 1.000 44.76415  ?  1080 VAL   A C   1 
ATOM   8584  O  O   . VAL   A 1 1082 ? -37.93000  70.84400  -18.33100 1.000 36.75833  ?  1080 VAL   A O   1 
ATOM   8585  C  CB  . VAL   A 1 1082 ? -35.79700  69.79800  -15.98900 1.000 33.72933  ?  1080 VAL   A CB  1 
ATOM   8586  C  CG1 . VAL   A 1 1082 ? -37.07200  70.32000  -15.34800 1.000 40.11592  ?  1080 VAL   A CG1 1 
ATOM   8587  C  CG2 . VAL   A 1 1082 ? -35.50300  68.39100  -15.49600 1.000 32.34597  ?  1080 VAL   A CG2 1 
ATOM   8588  N  N   . LYS   A 1 1083 ? -36.11900  72.16700  -18.13100 1.000 37.87902  ?  1081 LYS   A N   1 
ATOM   8589  C  CA  . LYS   A 1 1083 ? -36.81100  73.32200  -18.69400 1.000 39.56899  ?  1081 LYS   A CA  1 
ATOM   8590  C  C   . LYS   A 1 1083 ? -37.27000  73.04600  -20.11900 1.000 42.43270  ?  1081 LYS   A C   1 
ATOM   8591  O  O   . LYS   A 1 1083 ? -38.38400  73.42300  -20.50600 1.000 40.94352  ?  1081 LYS   A O   1 
ATOM   8592  C  CB  . LYS   A 1 1083 ? -35.89900  74.54800  -18.66100 1.000 30.77952  ?  1081 LYS   A CB  1 
ATOM   8593  C  CG  . LYS   A 1 1083 ? -36.50400  75.77400  -19.32100 1.000 39.66238  ?  1081 LYS   A CG  1 
ATOM   8594  C  CD  . LYS   A 1 1083 ? -35.43500  76.71900  -19.84200 1.000 41.77957  ?  1081 LYS   A CD  1 
ATOM   8595  C  CE  . LYS   A 1 1083 ? -34.47500  77.12700  -18.74400 1.000 34.84364  ?  1081 LYS   A CE  1 
ATOM   8596  N  NZ  . LYS   A 1 1083 ? -33.56900  78.22400  -19.18400 1.000 36.20474  ?  1081 LYS   A NZ  1 
ATOM   8597  N  N   . ALA   A 1 1084 ? -36.42800  72.38100  -20.91400 1.000 38.16018  ?  1082 ALA   A N   1 
ATOM   8598  C  CA  . ALA   A 1 1084 ? -36.76900  72.09500  -22.30200 1.000 37.17136  ?  1082 ALA   A CA  1 
ATOM   8599  C  C   . ALA   A 1 1084 ? -37.94300  71.13600  -22.42800 1.000 45.94485  ?  1082 ALA   A C   1 
ATOM   8600  O  O   . ALA   A 1 1084 ? -38.52300  71.02700  -23.51400 1.000 54.64139  ?  1082 ALA   A O   1 
ATOM   8601  C  CB  . ALA   A 1 1084 ? -35.55200  71.52900  -23.03300 1.000 38.80799  ?  1082 ALA   A CB  1 
ATOM   8602  N  N   . LYS   A 1 1085 ? -38.29600  70.43200  -21.35300 1.000 43.15528  ?  1083 LYS   A N   1 
ATOM   8603  C  CA  . LYS   A 1 1085 ? -39.46700  69.56700  -21.35000 1.000 48.57543  ?  1083 LYS   A CA  1 
ATOM   8604  C  C   . LYS   A 1 1085 ? -40.65500  70.17900  -20.62300 1.000 37.77372  ?  1083 LYS   A C   1 
ATOM   8605  O  O   . LYS   A 1 1085 ? -41.79000  69.74500  -20.85000 1.000 48.01330  ?  1083 LYS   A O   1 
ATOM   8606  C  CB  . LYS   A 1 1085 ? -39.12700  68.21200  -20.71500 1.000 43.05594  ?  1083 LYS   A CB  1 
ATOM   8607  C  CG  . LYS   A 1 1085 ? -38.22500  67.32300  -21.56500 1.000 35.26360  ?  1083 LYS   A CG  1 
ATOM   8608  C  CD  . LYS   A 1 1085 ? -38.96600  66.09500  -22.09200 1.000 54.69651  ?  1083 LYS   A CD  1 
ATOM   8609  C  CE  . LYS   A 1 1085 ? -40.12700  66.48000  -22.99800 1.000 51.52845  ?  1083 LYS   A CE  1 
ATOM   8610  N  NZ  . LYS   A 1 1085 ? -40.76800  65.28800  -23.61300 1.000 47.14676  ?  1083 LYS   A NZ  1 
ATOM   8611  N  N   . LEU   A 1 1086 ? -40.42500  71.17200  -19.76500 1.000 38.50188  ?  1084 LEU   A N   1 
ATOM   8612  C  CA  . LEU   A 1 1086 ? -41.52700  71.80900  -19.05600 1.000 38.53751  ?  1084 LEU   A CA  1 
ATOM   8613  C  C   . LEU   A 1 1086 ? -42.15900  72.91400  -19.89200 1.000 40.96249  ?  1084 LEU   A C   1 
ATOM   8614  O  O   . LEU   A 1 1086 ? -43.38900  73.03400  -19.93900 1.000 43.24320  ?  1084 LEU   A O   1 
ATOM   8615  C  CB  . LEU   A 1 1086 ? -41.03800  72.36600  -17.72000 1.000 31.20408  ?  1084 LEU   A CB  1 
ATOM   8616  C  CG  . LEU   A 1 1086 ? -41.99400  73.31800  -16.99800 1.000 29.73694  ?  1084 LEU   A CG  1 
ATOM   8617  C  CD1 . LEU   A 1 1086 ? -43.13900  72.55000  -16.35700 1.000 25.42477  ?  1084 LEU   A CD1 1 
ATOM   8618  C  CD2 . LEU   A 1 1086 ? -41.26200  74.16800  -15.96600 1.000 23.44976  ?  1084 LEU   A CD2 1 
ATOM   8619  N  N   . LEU   A 1 1087 ? -41.33300  73.72300  -20.55500 1.000 37.12274  ?  1085 LEU   A N   1 
ATOM   8620  C  CA  . LEU   A 1 1087 ? -41.85800  74.83900  -21.33700 1.000 30.25174  ?  1085 LEU   A CA  1 
ATOM   8621  C  C   . LEU   A 1 1087 ? -42.81300  74.40900  -22.44700 1.000 37.68305  ?  1085 LEU   A C   1 
ATOM   8622  O  O   . LEU   A 1 1087 ? -43.85000  75.07500  -22.61700 1.000 39.47178  ?  1085 LEU   A O   1 
ATOM   8623  C  CB  . LEU   A 1 1087 ? -40.69800  75.66800  -21.90400 1.000 18.47039  ?  1085 LEU   A CB  1 
ATOM   8624  C  CG  . LEU   A 1 1087 ? -39.79000  76.36100  -20.88400 1.000 25.03634  ?  1085 LEU   A CG  1 
ATOM   8625  C  CD1 . LEU   A 1 1087 ? -38.95600  77.44300  -21.55100 1.000 33.52578  ?  1085 LEU   A CD1 1 
ATOM   8626  C  CD2 . LEU   A 1 1087 ? -40.60200  76.94000  -19.74200 1.000 32.14914  ?  1085 LEU   A CD2 1 
ATOM   8627  N  N   . PRO   A 1 1088 ? -42.55000  73.35200  -23.22600 1.000 40.57196  ?  1086 PRO   A N   1 
ATOM   8628  C  CA  . PRO   A 1 1088 ? -43.56600  72.91400  -24.19600 1.000 37.65650  ?  1086 PRO   A CA  1 
ATOM   8629  C  C   . PRO   A 1 1088 ? -44.85800  72.46300  -23.54200 1.000 43.01538  ?  1086 PRO   A C   1 
ATOM   8630  O  O   . PRO   A 1 1088 ? -45.93500  72.65700  -24.12000 1.000 52.34496  ?  1086 PRO   A O   1 
ATOM   8631  C  CB  . PRO   A 1 1088 ? -42.87300  71.76200  -24.93900 1.000 39.82596  ?  1086 PRO   A CB  1 
ATOM   8632  C  CG  . PRO   A 1 1088 ? -41.78500  71.31500  -24.02600 1.000 60.08559  ?  1086 PRO   A CG  1 
ATOM   8633  C  CD  . PRO   A 1 1088 ? -41.31300  72.56000  -23.35200 1.000 41.39989  ?  1086 PRO   A CD  1 
ATOM   8634  N  N   . ALA   A 1 1089 ? -44.78500  71.86700  -22.34900 1.000 44.38222  ?  1087 ALA   A N   1 
ATOM   8635  C  CA  . ALA   A 1 1089 ? -46.00100  71.48200  -21.64100 1.000 49.99669  ?  1087 ALA   A CA  1 
ATOM   8636  C  C   . ALA   A 1 1089 ? -46.78700  72.70700  -21.19200 1.000 41.02949  ?  1087 ALA   A C   1 
ATOM   8637  O  O   . ALA   A 1 1089 ? -48.02300  72.71300  -21.24500 1.000 49.40394  ?  1087 ALA   A O   1 
ATOM   8638  C  CB  . ALA   A 1 1089 ? -45.65700  70.59400  -20.44600 1.000 33.95032  ?  1087 ALA   A CB  1 
ATOM   8639  N  N   . LEU   A 1 1090 ? -46.08900  73.75500  -20.75200 1.000 42.65011  ?  1088 LEU   A N   1 
ATOM   8640  C  CA  . LEU   A 1 1090 ? -46.76100  74.98700  -20.36300 1.000 34.91967  ?  1088 LEU   A CA  1 
ATOM   8641  C  C   . LEU   A 1 1090 ? -47.29700  75.75600  -21.56300 1.000 42.95420  ?  1088 LEU   A C   1 
ATOM   8642  O  O   . LEU   A 1 1090 ? -48.16700  76.61600  -21.39200 1.000 59.07316  ?  1088 LEU   A O   1 
ATOM   8643  C  CB  . LEU   A 1 1090 ? -45.81300  75.86900  -19.55100 1.000 39.87762  ?  1088 LEU   A CB  1 
ATOM   8644  C  CG  . LEU   A 1 1090 ? -45.40200  75.29300  -18.19600 1.000 33.92246  ?  1088 LEU   A CG  1 
ATOM   8645  C  CD1 . LEU   A 1 1090 ? -44.58200  76.30200  -17.40800 1.000 24.61069  ?  1088 LEU   A CD1 1 
ATOM   8646  C  CD2 . LEU   A 1 1090 ? -46.63100  74.85700  -17.41000 1.000 45.97500  ?  1088 LEU   A CD2 1 
ATOM   8647  N  N   . GLN   A 1 1091 ? -46.79500  75.47600  -22.76700 1.000 45.02290  ?  1089 GLN   A N   1 
ATOM   8648  C  CA  . GLN   A 1 1091 ? -47.38000  76.05600  -23.96800 1.000 50.20109  ?  1089 GLN   A CA  1 
ATOM   8649  C  C   . GLN   A 1 1091 ? -48.65200  75.33300  -24.38900 1.000 47.27051  ?  1089 GLN   A C   1 
ATOM   8650  O  O   . GLN   A 1 1091 ? -49.46100  75.90400  -25.12700 1.000 61.60968  ?  1089 GLN   A O   1 
ATOM   8651  C  CB  . GLN   A 1 1091 ? -46.36800  76.03600  -25.11700 1.000 38.91737  ?  1089 GLN   A CB  1 
ATOM   8652  C  CG  . GLN   A 1 1091 ? -46.54000  77.17200  -26.11800 1.000 48.28699  ?  1089 GLN   A CG  1 
ATOM   8653  C  CD  . GLN   A 1 1091 ? -45.99300  78.49400  -25.60400 1.000 78.53101  ?  1089 GLN   A CD  1 
ATOM   8654  O  OE1 . GLN   A 1 1091 ? -44.92400  78.54100  -24.99500 1.000 75.19204  ?  1089 GLN   A OE1 1 
ATOM   8655  N  NE2 . GLN   A 1 1091 ? -46.72800  79.57400  -25.84600 1.000 59.83761  ?  1089 GLN   A NE2 1 
ATOM   8656  N  N   . ASN   A 1 1092 ? -48.84100  74.09300  -23.93600 1.000 43.35241  ?  1090 ASN   A N   1 
ATOM   8657  C  CA  . ASN   A 1 1092 ? -50.06400  73.34500  -24.19200 1.000 51.38469  ?  1090 ASN   A CA  1 
ATOM   8658  C  C   . ASN   A 1 1092 ? -50.71600  72.95600  -22.87200 1.000 53.05719  ?  1090 ASN   A C   1 
ATOM   8659  O  O   . ASN   A 1 1092 ? -51.14400  71.81000  -22.69400 1.000 47.92912  ?  1090 ASN   A O   1 
ATOM   8660  C  CB  . ASN   A 1 1092 ? -49.77200  72.09800  -25.03000 1.000 42.85184  ?  1090 ASN   A CB  1 
ATOM   8661  C  CG  . ASN   A 1 1092 ? -48.90400  72.39600  -26.23400 1.000 45.91751  ?  1090 ASN   A CG  1 
ATOM   8662  O  OD1 . ASN   A 1 1092 ? -49.38400  72.89000  -27.25400 1.000 59.90896  ?  1090 ASN   A OD1 1 
ATOM   8663  N  ND2 . ASN   A 1 1092 ? -47.61600  72.09100  -26.12400 1.000 48.13240  ?  1090 ASN   A ND2 1 
ATOM   8664  N  N   . GLN   A 1 1093 ? -50.79500  73.90500  -21.94100 1.000 53.91658  ?  1091 GLN   A N   1 
ATOM   8665  C  CA  . GLN   A 1 1093 ? -51.23900  73.63000  -20.58100 1.000 50.45018  ?  1091 GLN   A CA  1 
ATOM   8666  C  C   . GLN   A 1 1093 ? -52.74900  73.71400  -20.40200 1.000 56.32299  ?  1091 GLN   A C   1 
ATOM   8667  O  O   . GLN   A 1 1093 ? -53.25300  73.29500  -19.35500 1.000 56.63024  ?  1091 GLN   A O   1 
ATOM   8668  C  CB  . GLN   A 1 1093 ? -50.57300  74.60300  -19.60300 1.000 52.71840  ?  1091 GLN   A CB  1 
ATOM   8669  C  CG  . GLN   A 1 1093 ? -50.97000  76.05600  -19.80100 1.000 48.43642  ?  1091 GLN   A CG  1 
ATOM   8670  C  CD  . GLN   A 1 1093 ? -50.69200  76.90300  -18.57500 1.000 59.90913  ?  1091 GLN   A CD  1 
ATOM   8671  O  OE1 . GLN   A 1 1093 ? -51.36300  76.76800  -17.55100 1.000 57.30945  ?  1091 GLN   A OE1 1 
ATOM   8672  N  NE2 . GLN   A 1 1093 ? -49.69700  77.77800  -18.67000 1.000 55.33607  ?  1091 GLN   A NE2 1 
ATOM   8673  N  N   . TYR   A 1 1094 ? -53.48000  74.24000  -21.38000 1.000 54.13744  ?  1092 TYR   A N   1 
ATOM   8674  C  CA  . TYR   A 1 1094 ? -54.89900  74.51400  -21.21200 1.000 47.09993  ?  1092 TYR   A CA  1 
ATOM   8675  C  C   . TYR   A 1 1094 ? -55.79300  73.42300  -21.78800 1.000 51.37533  ?  1092 TYR   A C   1 
ATOM   8676  O  O   . TYR   A 1 1094 ? -56.99900  73.64200  -21.94000 1.000 70.10669  ?  1092 TYR   A O   1 
ATOM   8677  C  CB  . TYR   A 1 1094 ? -55.24300  75.87100  -21.82700 1.000 34.58547  ?  1092 TYR   A CB  1 
ATOM   8678  C  CG  . TYR   A 1 1094 ? -54.52000  77.01500  -21.15400 1.000 33.81103  ?  1092 TYR   A CG  1 
ATOM   8679  C  CD1 . TYR   A 1 1094 ? -54.78900  77.34700  -19.83300 1.000 39.35593  ?  1092 TYR   A CD1 1 
ATOM   8680  C  CD2 . TYR   A 1 1094 ? -53.56400  77.75700  -21.83500 1.000 42.08785  ?  1092 TYR   A CD2 1 
ATOM   8681  C  CE1 . TYR   A 1 1094 ? -54.12900  78.38800  -19.20800 1.000 49.82405  ?  1092 TYR   A CE1 1 
ATOM   8682  C  CE2 . TYR   A 1 1094 ? -52.90000  78.80200  -21.21900 1.000 43.07753  ?  1092 TYR   A CE2 1 
ATOM   8683  C  CZ  . TYR   A 1 1094 ? -53.18600  79.11300  -19.90600 1.000 49.87581  ?  1092 TYR   A CZ  1 
ATOM   8684  O  OH  . TYR   A 1 1094 ? -52.52600  80.15100  -19.28800 1.000 45.13861  ?  1092 TYR   A OH  1 
ATOM   8685  N  N   . VAL   A 1 1095 ? -55.24000  72.26000  -22.10100 1.000 46.00200  ?  1093 VAL   A N   1 
ATOM   8686  C  CA  . VAL   A 1 1095 ? -56.07300  71.10400  -22.43900 1.000 55.41188  ?  1093 VAL   A CA  1 
ATOM   8687  C  C   . VAL   A 1 1095 ? -56.48900  70.41100  -21.14500 1.000 53.36463  ?  1093 VAL   A C   1 
ATOM   8688  O  O   . VAL   A 1 1095 ? -55.62300  70.11100  -20.30800 1.000 66.59029  ?  1093 VAL   A O   1 
ATOM   8689  C  CB  . VAL   A 1 1095 ? -55.32300  70.14700  -23.35800 1.000 45.41490  ?  1093 VAL   A CB  1 
ATOM   8690  C  CG1 . VAL   A 1 1095 ? -56.09500  68.84600  -23.50600 1.000 38.61942  ?  1093 VAL   A CG1 1 
ATOM   8691  C  CG2 . VAL   A 1 1095 ? -55.11200  70.78700  -24.71400 1.000 58.00996  ?  1093 VAL   A CG2 1 
ATOM   8692  N  N   . PRO   A 1 1096 ? -57.78100  70.16000  -20.93500 1.000 51.80872  ?  1094 PRO   A N   1 
ATOM   8693  C  CA  . PRO   A 1 1096 ? -58.21300  69.51600  -19.69000 1.000 68.98215  ?  1094 PRO   A CA  1 
ATOM   8694  C  C   . PRO   A 1 1096 ? -57.58200  68.14100  -19.52400 1.000 58.50424  ?  1094 PRO   A C   1 
ATOM   8695  O  O   . PRO   A 1 1096 ? -57.28700  67.44400  -20.49800 1.000 61.28595  ?  1094 PRO   A O   1 
ATOM   8696  C  CB  . PRO   A 1 1096 ? -59.73500  69.42400  -19.84800 1.000 57.79267  ?  1094 PRO   A CB  1 
ATOM   8697  C  CG  . PRO   A 1 1096 ? -60.07900  70.48500  -20.84000 1.000 60.89655  ?  1094 PRO   A CG  1 
ATOM   8698  C  CD  . PRO   A 1 1096 ? -58.92000  70.53700  -21.78900 1.000 55.91587  ?  1094 PRO   A CD  1 
ATOM   8699  N  N   . PHE   A 1 1097 ? -57.37800  67.75700  -18.26100 1.000 46.42649  ?  1095 PHE   A N   1 
ATOM   8700  C  CA  . PHE   A 1 1097 ? -56.62700  66.54000  -17.96500 1.000 51.90984  ?  1095 PHE   A CA  1 
ATOM   8701  C  C   . PHE   A 1 1097 ? -57.36100  65.29400  -18.45000 1.000 50.03245  ?  1095 PHE   A C   1 
ATOM   8702  O  O   . PHE   A 1 1097 ? -56.72700  64.32900  -18.89200 1.000 54.39232  ?  1095 PHE   A O   1 
ATOM   8703  C  CB  . PHE   A 1 1097 ? -56.34500  66.45400  -16.46500 1.000 57.54492  ?  1095 PHE   A CB  1 
ATOM   8704  C  CG  . PHE   A 1 1097 ? -55.48200  65.28700  -16.07500 1.000 61.84713  ?  1095 PHE   A CG  1 
ATOM   8705  C  CD1 . PHE   A 1 1097 ? -54.20300  65.15200  -16.58900 1.000 53.85821  ?  1095 PHE   A CD1 1 
ATOM   8706  C  CD2 . PHE   A 1 1097 ? -55.94500  64.33100  -15.18500 1.000 58.75202  ?  1095 PHE   A CD2 1 
ATOM   8707  C  CE1 . PHE   A 1 1097 ? -53.40500  64.08100  -16.23200 1.000 45.79486  ?  1095 PHE   A CE1 1 
ATOM   8708  C  CE2 . PHE   A 1 1097 ? -55.15100  63.25900  -14.82200 1.000 49.21720  ?  1095 PHE   A CE2 1 
ATOM   8709  C  CZ  . PHE   A 1 1097 ? -53.88000  63.13400  -15.34700 1.000 45.04209  ?  1095 PHE   A CZ  1 
ATOM   8710  N  N   . ASP   A 1 1098 ? -58.69500  65.29400  -18.37500 1.000 58.10520  ?  1096 ASP   A N   1 
ATOM   8711  C  CA  . ASP   A 1 1098 ? -59.45700  64.14700  -18.86200 1.000 58.63953  ?  1096 ASP   A CA  1 
ATOM   8712  C  C   . ASP   A 1 1098 ? -59.26900  63.95700  -20.36300 1.000 59.70411  ?  1096 ASP   A C   1 
ATOM   8713  O  O   . ASP   A 1 1098 ? -59.20300  62.82200  -20.84900 1.000 51.03999  ?  1096 ASP   A O   1 
ATOM   8714  C  CB  . ASP   A 1 1098 ? -60.93900  64.31000  -18.51500 1.000 48.80318  ?  1096 ASP   A CB  1 
ATOM   8715  C  CG  . ASP   A 1 1098 ? -61.42000  65.74100  -18.65900 1.000 67.40108  ?  1096 ASP   A CG  1 
ATOM   8716  O  OD1 . ASP   A 1 1098 ? -60.56800  66.64000  -18.79800 1.000 83.61159  ?  1096 ASP   A OD1 1 
ATOM   8717  O  OD2 . ASP   A 1 1098 ? -62.64800  65.96800  -18.63300 1.000 55.86463  -1 1096 ASP   A OD2 1 
ATOM   8718  N  N   . LYS   A 1 1099 ? -59.17500  65.05800  -21.11400 1.000 53.29856  ?  1097 LYS   A N   1 
ATOM   8719  C  CA  . LYS   A 1 1099 ? -58.88800  64.95400  -22.54000 1.000 52.97548  ?  1097 LYS   A CA  1 
ATOM   8720  C  C   . LYS   A 1 1099 ? -57.44600  64.53400  -22.78500 1.000 66.11931  ?  1097 LYS   A C   1 
ATOM   8721  O  O   . LYS   A 1 1099 ? -57.16000  63.83300  -23.76300 1.000 68.88531  ?  1097 LYS   A O   1 
ATOM   8722  C  CB  . LYS   A 1 1099 ? -59.17600  66.28400  -23.23400 1.000 53.44603  ?  1097 LYS   A CB  1 
ATOM   8723  C  CG  . LYS   A 1 1099 ? -60.55300  66.85900  -22.94000 1.000 69.00199  ?  1097 LYS   A CG  1 
ATOM   8724  C  CD  . LYS   A 1 1099 ? -61.66300  65.93700  -23.42000 1.000 75.98851  ?  1097 LYS   A CD  1 
ATOM   8725  C  CE  . LYS   A 1 1099 ? -63.03300  66.52300  -23.11600 1.000 60.45535  ?  1097 LYS   A CE  1 
ATOM   8726  N  NZ  . LYS   A 1 1099 ? -64.13700  65.66100  -23.62000 1.000 66.48432  ?  1097 LYS   A NZ  1 
ATOM   8727  N  N   . ILE   A 1 1100 ? -56.52800  64.95700  -21.91400 1.000 61.52105  ?  1098 ILE   A N   1 
ATOM   8728  C  CA  . ILE   A 1 1100 ? -55.13300  64.54300  -22.02900 1.000 48.28272  ?  1098 ILE   A CA  1 
ATOM   8729  C  C   . ILE   A 1 1100 ? -55.01400  63.03200  -21.88000 1.000 64.30299  ?  1098 ILE   A C   1 
ATOM   8730  O  O   . ILE   A 1 1100 ? -54.28800  62.37400  -22.63600 1.000 74.01921  ?  1098 ILE   A O   1 
ATOM   8731  C  CB  . ILE   A 1 1100 ? -54.27300  65.28900  -20.99100 1.000 49.51051  ?  1098 ILE   A CB  1 
ATOM   8732  C  CG1 . ILE   A 1 1100 ? -54.07400  66.74700  -21.40600 1.000 47.18990  ?  1098 ILE   A CG1 1 
ATOM   8733  C  CG2 . ILE   A 1 1100 ? -52.93800  64.60300  -20.81000 1.000 46.14016  ?  1098 ILE   A CG2 1 
ATOM   8734  C  CD1 . ILE   A 1 1100 ? -53.28800  67.56400  -20.40500 1.000 32.40421  ?  1098 ILE   A CD1 1 
ATOM   8735  N  N   . LEU   A 1 1101 ? -55.72600  62.45900  -20.90600 1.000 56.89617  ?  1099 LEU   A N   1 
ATOM   8736  C  CA  . LEU   A 1 1101 ? -55.72300  61.00900  -20.73300 1.000 57.44518  ?  1099 LEU   A CA  1 
ATOM   8737  C  C   . LEU   A 1 1101 ? -56.29400  60.30900  -21.95900 1.000 67.21438  ?  1099 LEU   A C   1 
ATOM   8738  O  O   . LEU   A 1 1101 ? -55.72300  59.33100  -22.45500 1.000 70.85759  ?  1099 LEU   A O   1 
ATOM   8739  C  CB  . LEU   A 1 1101 ? -56.52200  60.62800  -19.48600 1.000 43.16030  ?  1099 LEU   A CB  1 
ATOM   8740  C  CG  . LEU   A 1 1101 ? -55.92500  60.93900  -18.11500 1.000 66.83113  ?  1099 LEU   A CG  1 
ATOM   8741  C  CD1 . LEU   A 1 1101 ? -56.96000  60.69900  -17.03700 1.000 47.59170  ?  1099 LEU   A CD1 1 
ATOM   8742  C  CD2 . LEU   A 1 1101 ? -54.70200  60.08300  -17.86300 1.000 68.41669  ?  1099 LEU   A CD2 1 
ATOM   8743  N  N   . GLU   A 1 1102 ? -57.43500  60.79700  -22.45500 1.000 65.56345  ?  1100 GLU   A N   1 
ATOM   8744  C  CA  . GLU   A 1 1102 ? -58.07000  60.18300  -23.61600 1.000 68.66418  ?  1100 GLU   A CA  1 
ATOM   8745  C  C   . GLU   A 1 1102 ? -57.15400  60.21600  -24.83300 1.000 75.43473  ?  1100 GLU   A C   1 
ATOM   8746  O  O   . GLU   A 1 1102 ? -57.03500  59.21900  -25.55600 1.000 81.49698  ?  1100 GLU   A O   1 
ATOM   8747  C  CB  . GLU   A 1 1102 ? -59.39300  60.88900  -23.91400 1.000 58.45902  ?  1100 GLU   A CB  1 
ATOM   8748  C  CG  . GLU   A 1 1102 ? -59.73300  60.98200  -25.39100 1.000 85.81662  ?  1100 GLU   A CG  1 
ATOM   8749  C  CD  . GLU   A 1 1102 ? -60.81200  62.00600  -25.67300 1.000 113.51204 ?  1100 GLU   A CD  1 
ATOM   8750  O  OE1 . GLU   A 1 1102 ? -61.89800  61.91300  -25.06300 1.000 105.99948 ?  1100 GLU   A OE1 1 
ATOM   8751  O  OE2 . GLU   A 1 1102 ? -60.57000  62.91300  -26.49800 1.000 107.18337 -1 1100 GLU   A OE2 1 
ATOM   8752  N  N   . ALA   A 1 1103 ? -56.49400  61.35300  -25.07200 1.000 71.37806  ?  1101 ALA   A N   1 
ATOM   8753  C  CA  . ALA   A 1 1103 ? -55.57300  61.44700  -26.19900 1.000 65.23430  ?  1101 ALA   A CA  1 
ATOM   8754  C  C   . ALA   A 1 1103 ? -54.40600  60.48000  -26.05000 1.000 66.50652  ?  1101 ALA   A C   1 
ATOM   8755  O  O   . ALA   A 1 1103 ? -53.91700  59.93900  -27.04800 1.000 73.85834  ?  1101 ALA   A O   1 
ATOM   8756  C  CB  . ALA   A 1 1103 ? -55.06000  62.88000  -26.33900 1.000 63.99989  ?  1101 ALA   A CB  1 
ATOM   8757  N  N   . ALA   A 1 1104 ? -53.95200  60.24600  -24.81700 1.000 61.86780  ?  1102 ALA   A N   1 
ATOM   8758  C  CA  . ALA   A 1 1104 ? -52.85500  59.32300  -24.56500 1.000 73.60800  ?  1102 ALA   A CA  1 
ATOM   8759  C  C   . ALA   A 1 1104 ? -53.27200  57.86200  -24.65500 1.000 77.87227  ?  1102 ALA   A C   1 
ATOM   8760  O  O   . ALA   A 1 1104 ? -52.39400  56.99400  -24.72100 1.000 65.95555  ?  1102 ALA   A O   1 
ATOM   8761  C  CB  . ALA   A 1 1104 ? -52.24700  59.59400  -23.18800 1.000 61.73649  ?  1102 ALA   A CB  1 
ATOM   8762  N  N   . ARG   A 1 1105 ? -54.57400  57.57600  -24.65800 1.000 77.27119  ?  1103 ARG   A N   1 
ATOM   8763  C  CA  . ARG   A 1 1105 ? -55.09500  56.21100  -24.71100 1.000 73.56728  ?  1103 ARG   A CA  1 
ATOM   8764  C  C   . ARG   A 1 1105 ? -54.48100  55.36300  -23.59600 1.000 87.66909  ?  1103 ARG   A C   1 
ATOM   8765  O  O   . ARG   A 1 1105 ? -53.85000  54.33000  -23.82600 1.000 81.89806  ?  1103 ARG   A O   1 
ATOM   8766  C  CB  . ARG   A 1 1105 ? -54.85000  55.58800  -26.08900 1.000 94.20868  ?  1103 ARG   A CB  1 
ATOM   8767  C  CG  . ARG   A 1 1105 ? -55.33800  56.44000  -27.25900 1.000 83.47756  ?  1103 ARG   A CG  1 
ATOM   8768  C  CD  . ARG   A 1 1105 ? -56.84600  56.33300  -27.44600 1.000 90.31454  ?  1103 ARG   A CD  1 
ATOM   8769  N  NE  . ARG   A 1 1105 ? -57.45400  57.61400  -27.79200 1.000 100.96716 ?  1103 ARG   A NE  1 
ATOM   8770  C  CZ  . ARG   A 1 1105 ? -57.66500  58.04200  -29.03000 1.000 100.45257 ?  1103 ARG   A CZ  1 
ATOM   8771  N  NH1 . ARG   A 1 1105 ? -57.32100  57.31600  -30.08100 1.000 100.91817 ?  1103 ARG   A NH1 1 
ATOM   8772  N  NH2 . ARG   A 1 1105 ? -58.23600  59.22800  -29.21700 1.000 78.32131  ?  1103 ARG   A NH2 1 
ATOM   8773  N  N   . VAL   A 1 1106 ? -54.67400  55.83300  -22.36800 1.000 92.07105  ?  1104 VAL   A N   1 
ATOM   8774  C  CA  . VAL   A 1 1106 ? -54.02100  55.25500  -21.20400 1.000 97.49570  ?  1104 VAL   A CA  1 
ATOM   8775  C  C   . VAL   A 1 1106 ? -54.88800  54.15100  -20.61400 1.000 98.64184  ?  1104 VAL   A C   1 
ATOM   8776  O  O   . VAL   A 1 1106 ? -56.08600  54.04400  -20.89000 1.000 89.87520  ?  1104 VAL   A O   1 
ATOM   8777  C  CB  . VAL   A 1 1106 ? -53.71900  56.33300  -20.14800 1.000 81.00063  ?  1104 VAL   A CB  1 
ATOM   8778  C  CG1 . VAL   A 1 1106 ? -52.49100  57.13500  -20.54000 1.000 75.90702  ?  1104 VAL   A CG1 1 
ATOM   8779  C  CG2 . VAL   A 1 1106 ? -54.92400  57.24000  -19.99000 1.000 65.66685  ?  1104 VAL   A CG2 1 
ATOM   8780  N  N   . LYS   A 1 1107 ? -54.26800  53.32600  -19.77400 1.000 90.72157  ?  1105 LYS   A N   1 
ATOM   8781  C  CA  . LYS   A 1 1107 ? -54.97500  52.27500  -19.06300 1.000 111.83591 ?  1105 LYS   A CA  1 
ATOM   8782  C  C   . LYS   A 1 1107 ? -55.70800  52.86100  -17.85700 1.000 123.26251 ?  1105 LYS   A C   1 
ATOM   8783  O  O   . LYS   A 1 1107 ? -55.70900  54.07200  -17.62000 1.000 123.09935 ?  1105 LYS   A O   1 
ATOM   8784  C  CB  . LYS   A 1 1107 ? -54.00200  51.17800  -18.63800 1.000 74.30954  ?  1105 LYS   A CB  1 
ATOM   8785  N  N   . ARG   A 1 1108 ? -56.34700  51.98900  -17.08300 1.000 114.38121 ?  1106 ARG   A N   1 
ATOM   8786  C  CA  . ARG   A 1 1108 ? -57.01600  52.39200  -15.85100 1.000 95.46256  ?  1106 ARG   A CA  1 
ATOM   8787  C  C   . ARG   A 1 1108 ? -56.82400  51.31400  -14.79000 1.000 117.52148 ?  1106 ARG   A C   1 
ATOM   8788  O  O   . ARG   A 1 1108 ? -57.77800  50.79800  -14.20600 1.000 96.98931  ?  1106 ARG   A O   1 
ATOM   8789  C  CB  . ARG   A 1 1108 ? -58.49600  52.68400  -16.09800 1.000 84.96358  ?  1106 ARG   A CB  1 
ATOM   8790  C  CG  . ARG   A 1 1108 ? -59.15000  53.51800  -15.00300 1.000 94.78580  ?  1106 ARG   A CG  1 
ATOM   8791  C  CD  . ARG   A 1 1108 ? -58.21700  54.62700  -14.53900 1.000 85.16613  ?  1106 ARG   A CD  1 
ATOM   8792  N  NE  . ARG   A 1 1108 ? -58.87300  55.57400  -13.64500 1.000 97.82529  ?  1106 ARG   A NE  1 
ATOM   8793  C  CZ  . ARG   A 1 1108 ? -58.99100  55.41400  -12.33400 1.000 92.93167  ?  1106 ARG   A CZ  1 
ATOM   8794  N  NH1 . ARG   A 1 1108 ? -58.53000  54.33400  -11.72500 1.000 78.62956  ?  1106 ARG   A NH1 1 
ATOM   8795  N  NH2 . ARG   A 1 1108 ? -59.58600  56.36200  -11.61600 1.000 92.01442  ?  1106 ARG   A NH2 1 
ATOM   8796  N  N   . GLU   A 1 1109 ? -55.56400  50.95700  -14.54000 1.000 125.40157 ?  1107 GLU   A N   1 
ATOM   8797  C  CA  . GLU   A 1 1109 ? -55.24400  50.00000  -13.48900 1.000 95.48994  ?  1107 GLU   A CA  1 
ATOM   8798  C  C   . GLU   A 1 1109 ? -55.70300  50.53600  -12.14000 1.000 106.26805 ?  1107 GLU   A C   1 
ATOM   8799  O  O   . GLU   A 1 1109 ? -55.30500  51.63000  -11.72600 1.000 117.77488 ?  1107 GLU   A O   1 
ATOM   8800  C  CB  . GLU   A 1 1109 ? -53.74300  49.71200  -13.47700 1.000 73.95887  ?  1107 GLU   A CB  1 
ATOM   8801  C  CG  . GLU   A 1 1109 ? -53.30200  48.69000  -14.51600 1.000 95.11789  ?  1107 GLU   A CG  1 
ATOM   8802  C  CD  . GLU   A 1 1109 ? -51.79300  48.56800  -14.62300 1.000 108.36509 ?  1107 GLU   A CD  1 
ATOM   8803  O  OE1 . GLU   A 1 1109 ? -51.08100  49.28400  -13.88800 1.000 110.12549 ?  1107 GLU   A OE1 1 
ATOM   8804  O  OE2 . GLU   A 1 1109 ? -51.31800  47.75700  -15.44800 1.000 89.18961  -1 1107 GLU   A OE2 1 
ATOM   8805  N  N   . GLY   A 1 1110 ? -56.55100  49.76100  -11.45900 1.000 106.63124 ?  1108 GLY   A N   1 
ATOM   8806  C  CA  . GLY   A 1 1110 ? -57.16200  50.21200  -10.22100 1.000 95.02477  ?  1108 GLY   A CA  1 
ATOM   8807  C  C   . GLY   A 1 1110 ? -56.19800  50.36900  -9.06400  1.000 86.95752  ?  1108 GLY   A C   1 
ATOM   8808  O  O   . GLY   A 1 1110 ? -56.49900  51.10800  -8.12000  1.000 84.63377  ?  1108 GLY   A O   1 
ATOM   8809  N  N   . ASN   A 1 1111 ? -55.04900  49.69300  -9.11100  1.000 81.17752  ?  1109 ASN   A N   1 
ATOM   8810  C  CA  . ASN   A 1 1111 ? -54.07900  49.80300  -8.02900  1.000 90.57377  ?  1109 ASN   A CA  1 
ATOM   8811  C  C   . ASN   A 1 1111 ? -53.33100  51.13100  -8.03200  1.000 93.35479  ?  1109 ASN   A C   1 
ATOM   8812  O  O   . ASN   A 1 1111 ? -52.64400  51.43300  -7.05100  1.000 83.27719  ?  1109 ASN   A O   1 
ATOM   8813  C  CB  . ASN   A 1 1111 ? -53.07600  48.64700  -8.09600  1.000 73.78808  ?  1109 ASN   A CB  1 
ATOM   8814  C  CG  . ASN   A 1 1111 ? -52.29900  48.62000  -9.39900  1.000 88.44481  ?  1109 ASN   A CG  1 
ATOM   8815  O  OD1 . ASN   A 1 1111 ? -52.88000  48.66800  -10.48300 1.000 104.92479 ?  1109 ASN   A OD1 1 
ATOM   8816  N  ND2 . ASN   A 1 1111 ? -50.97500  48.54900  -9.29800  1.000 81.15833  ?  1109 ASN   A ND2 1 
ATOM   8817  N  N   . ARG   A 1 1112 ? -53.44700  51.92700  -9.09600  1.000 77.82491  ?  1110 ARG   A N   1 
ATOM   8818  C  CA  . ARG   A 1 1112 ? -52.73200  53.19200  -9.20400  1.000 59.13572  ?  1110 ARG   A CA  1 
ATOM   8819  C  C   . ARG   A 1 1112 ? -53.64300  54.23900  -9.83700  1.000 69.60611  ?  1110 ARG   A C   1 
ATOM   8820  O  O   . ARG   A 1 1112 ? -54.79000  53.96300  -10.20000 1.000 58.50773  ?  1110 ARG   A O   1 
ATOM   8821  C  CB  . ARG   A 1 1112 ? -51.43900  53.03500  -10.01300 1.000 54.96890  ?  1110 ARG   A CB  1 
ATOM   8822  C  CG  . ARG   A 1 1112 ? -51.25900  51.67500  -10.66700 1.000 66.18710  ?  1110 ARG   A CG  1 
ATOM   8823  C  CD  . ARG   A 1 1112 ? -49.97100  51.63100  -11.46700 1.000 70.92798  ?  1110 ARG   A CD  1 
ATOM   8824  N  NE  . ARG   A 1 1112 ? -48.90300  52.36600  -10.80100 1.000 55.51552  ?  1110 ARG   A NE  1 
ATOM   8825  C  CZ  . ARG   A 1 1112 ? -47.97700  51.81500  -10.02700 1.000 75.59403  ?  1110 ARG   A CZ  1 
ATOM   8826  N  NH1 . ARG   A 1 1112 ? -47.94200  50.51100  -9.81100  1.000 81.17035  ?  1110 ARG   A NH1 1 
ATOM   8827  N  NH2 . ARG   A 1 1112 ? -47.06100  52.59400  -9.45800  1.000 70.08304  ?  1110 ARG   A NH2 1 
ATOM   8828  N  N   . HIS   A 1 1113 ? -53.11300  55.45300  -9.96600  1.000 74.00591  ?  1111 HIS   A N   1 
ATOM   8829  C  CA  . HIS   A 1 1113 ? -53.78700  56.60700  -10.53900 1.000 56.18664  ?  1111 HIS   A CA  1 
ATOM   8830  C  C   . HIS   A 1 1113 ? -53.42100  56.76400  -12.00800 1.000 56.33273  ?  1111 HIS   A C   1 
ATOM   8831  O  O   . HIS   A 1 1113 ? -52.40100  56.24000  -12.46600 1.000 60.61141  ?  1111 HIS   A O   1 
ATOM   8832  C  CB  . HIS   A 1 1113 ? -53.40900  57.87600  -9.76400  1.000 63.19103  ?  1111 HIS   A CB  1 
ATOM   8833  C  CG  . HIS   A 1 1113 ? -53.89900  57.88700  -8.35000  1.000 74.24818  ?  1111 HIS   A CG  1 
ATOM   8834  N  ND1 . HIS   A 1 1113 ? -55.16400  58.31200  -8.00400  1.000 78.19291  ?  1111 HIS   A ND1 1 
ATOM   8835  C  CD2 . HIS   A 1 1113 ? -53.29500  57.52400  -7.19400  1.000 70.60887  ?  1111 HIS   A CD2 1 
ATOM   8836  C  CE1 . HIS   A 1 1113 ? -55.31800  58.21000  -6.69500  1.000 68.85158  ?  1111 HIS   A CE1 1 
ATOM   8837  N  NE2 . HIS   A 1 1113 ? -54.19800  57.73500  -6.18000  1.000 79.63502  ?  1111 HIS   A NE2 1 
ATOM   8838  N  N   . PRO   A 1 1114 ? -54.24000  57.47500  -12.78500 1.000 65.32464  ?  1112 PRO   A N   1 
ATOM   8839  C  CA  . PRO   A 1 1114 ? -53.96500  57.59500  -14.22300 1.000 51.91296  ?  1112 PRO   A CA  1 
ATOM   8840  C  C   . PRO   A 1 1114 ? -52.68300  58.36700  -14.50700 1.000 62.66360  ?  1112 PRO   A C   1 
ATOM   8841  O  O   . PRO   A 1 1114 ? -52.36200  59.34900  -13.83300 1.000 60.50196  ?  1112 PRO   A O   1 
ATOM   8842  C  CB  . PRO   A 1 1114 ? -55.19300  58.34200  -14.75700 1.000 55.04704  ?  1112 PRO   A CB  1 
ATOM   8843  C  CG  . PRO   A 1 1114 ? -56.25900  58.10600  -13.74100 1.000 62.59019  ?  1112 PRO   A CG  1 
ATOM   8844  C  CD  . PRO   A 1 1114 ? -55.54800  58.05100  -12.42700 1.000 68.90846  ?  1112 PRO   A CD  1 
ATOM   8845  N  N   . LEU   A 1 1115 ? -51.94900  57.89500  -15.51900 1.000 58.95122  ?  1113 LEU   A N   1 
ATOM   8846  C  CA  . LEU   A 1 1115 ? -50.75400  58.54500  -16.05600 1.000 39.82636  ?  1113 LEU   A CA  1 
ATOM   8847  C  C   . LEU   A 1 1115 ? -49.60500  58.62200  -15.05600 1.000 46.57366  ?  1113 LEU   A C   1 
ATOM   8848  O  O   . LEU   A 1 1115 ? -48.49700  58.15900  -15.35000 1.000 51.81210  ?  1113 LEU   A O   1 
ATOM   8849  C  CB  . LEU   A 1 1115 ? -51.09200  59.94500  -16.57500 1.000 52.00971  ?  1113 LEU   A CB  1 
ATOM   8850  C  CG  . LEU   A 1 1115 ? -51.12800  60.07700  -18.10000 1.000 46.36201  ?  1113 LEU   A CG  1 
ATOM   8851  C  CD1 . LEU   A 1 1115 ? -51.49800  61.49200  -18.51300 1.000 51.70486  ?  1113 LEU   A CD1 1 
ATOM   8852  C  CD2 . LEU   A 1 1115 ? -49.79500  59.67300  -18.70400 1.000 38.12649  ?  1113 LEU   A CD2 1 
ATOM   8853  N  N   . PHE   A 1 1116 ? -49.83900  59.21000  -13.88600 1.000 38.12435  ?  1114 PHE   A N   1 
ATOM   8854  C  CA  . PHE   A 1 1116 ? -48.79700  59.35800  -12.88200 1.000 32.35509  ?  1114 PHE   A CA  1 
ATOM   8855  C  C   . PHE   A 1 1116 ? -49.33500  58.96600  -11.51400 1.000 36.94888  ?  1114 PHE   A C   1 
ATOM   8856  O  O   . PHE   A 1 1116 ? -50.54500  58.86200  -11.30100 1.000 59.90513  ?  1114 PHE   A O   1 
ATOM   8857  C  CB  . PHE   A 1 1116 ? -48.25100  60.79300  -12.83900 1.000 47.79960  ?  1114 PHE   A CB  1 
ATOM   8858  C  CG  . PHE   A 1 1116 ? -49.31000  61.84100  -12.64200 1.000 41.99605  ?  1114 PHE   A CG  1 
ATOM   8859  C  CD1 . PHE   A 1 1116 ? -49.72100  62.20200  -11.36900 1.000 32.59943  ?  1114 PHE   A CD1 1 
ATOM   8860  C  CD2 . PHE   A 1 1116 ? -49.88800  62.47100  -13.73000 1.000 39.80744  ?  1114 PHE   A CD2 1 
ATOM   8861  C  CE1 . PHE   A 1 1116 ? -50.69300  63.16500  -11.18600 1.000 32.53038  ?  1114 PHE   A CE1 1 
ATOM   8862  C  CE2 . PHE   A 1 1116 ? -50.86000  63.43600  -13.55400 1.000 47.09466  ?  1114 PHE   A CE2 1 
ATOM   8863  C  CZ  . PHE   A 1 1116 ? -51.26300  63.78300  -12.28000 1.000 35.12862  ?  1114 PHE   A CZ  1 
ATOM   8864  N  N   . ASP   A 1 1117 ? -48.40600  58.75000  -10.58100 1.000 48.91413  ?  1115 ASP   A N   1 
ATOM   8865  C  CA  . ASP   A 1 1117 ? -48.74300  58.43300  -9.20100  1.000 42.72984  ?  1115 ASP   A CA  1 
ATOM   8866  C  C   . ASP   A 1 1117 ? -48.22500  59.44600  -8.19400  1.000 40.86047  ?  1115 ASP   A C   1 
ATOM   8867  O  O   . ASP   A 1 1117 ? -48.71700  59.46500  -7.06100  1.000 38.58223  ?  1115 ASP   A O   1 
ATOM   8868  C  CB  . ASP   A 1 1117 ? -48.20500  57.04300  -8.82300  1.000 29.85789  ?  1115 ASP   A CB  1 
ATOM   8869  C  CG  . ASP   A 1 1117 ? -49.09100  55.92400  -9.32400  1.000 45.64785  ?  1115 ASP   A CG  1 
ATOM   8870  O  OD1 . ASP   A 1 1117 ? -50.30400  55.94800  -9.02700  1.000 57.21825  ?  1115 ASP   A OD1 1 
ATOM   8871  O  OD2 . ASP   A 1 1117 ? -48.57800  55.02500  -10.02200 1.000 59.46772  -1 1115 ASP   A OD2 1 
ATOM   8872  N  N   . VAL   A 1 1118 ? -47.25900  60.28200  -8.56700  1.000 32.41516  ?  1116 VAL   A N   1 
ATOM   8873  C  CA  . VAL   A 1 1118 ? -46.68800  61.29000  -7.68300  1.000 28.37810  ?  1116 VAL   A CA  1 
ATOM   8874  C  C   . VAL   A 1 1118 ? -46.93800  62.66400  -8.29000  1.000 31.26198  ?  1116 VAL   A C   1 
ATOM   8875  O  O   . VAL   A 1 1118 ? -46.76900  62.85800  -9.49900  1.000 35.23959  ?  1116 VAL   A O   1 
ATOM   8876  C  CB  . VAL   A 1 1118 ? -45.18000  61.05500  -7.45600  1.000 34.59173  ?  1116 VAL   A CB  1 
ATOM   8877  C  CG1 . VAL   A 1 1118 ? -44.59400  62.13900  -6.56300  1.000 28.24428  ?  1116 VAL   A CG1 1 
ATOM   8878  C  CG2 . VAL   A 1 1118 ? -44.94500  59.67900  -6.85200  1.000 32.05215  ?  1116 VAL   A CG2 1 
ATOM   8879  N  N   . MET   A 1 1119 ? -47.34300  63.61300  -7.45000  1.000 30.75650  ?  1117 MET   A N   1 
ATOM   8880  C  CA  . MET   A 1 1119 ? -47.61900  64.97800  -7.87500  1.000 33.49018  ?  1117 MET   A CA  1 
ATOM   8881  C  C   . MET   A 1 1119 ? -46.70700  65.95000  -7.13800  1.000 28.80427  ?  1117 MET   A C   1 
ATOM   8882  O  O   . MET   A 1 1119 ? -46.47700  65.80800  -5.93200  1.000 28.84376  ?  1117 MET   A O   1 
ATOM   8883  C  CB  . MET   A 1 1119 ? -49.08500  65.34800  -7.62900  1.000 36.94185  ?  1117 MET   A CB  1 
ATOM   8884  C  CG  . MET   A 1 1119 ? -49.36500  66.83800  -7.71900  1.000 22.98429  ?  1117 MET   A CG  1 
ATOM   8885  S  SD  . MET   A 1 1119 ? -50.92800  67.21300  -8.52000  1.000 62.82505  ?  1117 MET   A SD  1 
ATOM   8886  C  CE  . MET   A 1 1119 ? -50.62400  66.54700  -10.14900 1.000 42.13016  ?  1117 MET   A CE  1 
ATOM   8887  N  N   . PHE   A 1 1120 ? -46.19100  66.93500  -7.87000  1.000 26.90556  ?  1118 PHE   A N   1 
ATOM   8888  C  CA  . PHE   A 1 1120 ? -45.33600  67.97800  -7.31700  1.000 25.93783  ?  1118 PHE   A CA  1 
ATOM   8889  C  C   . PHE   A 1 1120 ? -45.98400  69.33100  -7.57300  1.000 35.73870  ?  1118 PHE   A C   1 
ATOM   8890  O  O   . PHE   A 1 1120 ? -46.19900  69.71100  -8.72900  1.000 39.60333  ?  1118 PHE   A O   1 
ATOM   8891  C  CB  . PHE   A 1 1120 ? -43.93700  67.92400  -7.93200  1.000 23.69147  ?  1118 PHE   A CB  1 
ATOM   8892  C  CG  . PHE   A 1 1120 ? -43.06900  69.09000  -7.56400  1.000 26.89307  ?  1118 PHE   A CG  1 
ATOM   8893  C  CD1 . PHE   A 1 1120 ? -42.53900  69.20200  -6.29000  1.000 39.24291  ?  1118 PHE   A CD1 1 
ATOM   8894  C  CD2 . PHE   A 1 1120 ? -42.77600  70.07200  -8.49500  1.000 34.36506  ?  1118 PHE   A CD2 1 
ATOM   8895  C  CE1 . PHE   A 1 1120 ? -41.73700  70.27500  -5.94800  1.000 33.59407  ?  1118 PHE   A CE1 1 
ATOM   8896  C  CE2 . PHE   A 1 1120 ? -41.97400  71.14600  -8.16100  1.000 34.98290  ?  1118 PHE   A CE2 1 
ATOM   8897  C  CZ  . PHE   A 1 1120 ? -41.45400  71.24700  -6.88600  1.000 37.40648  ?  1118 PHE   A CZ  1 
ATOM   8898  N  N   . MET   A 1 1121 ? -46.28800  70.05400  -6.49800  1.000 31.17502  ?  1119 MET   A N   1 
ATOM   8899  C  CA  . MET   A 1 1121 ? -46.95300  71.34600  -6.57400  1.000 28.53842  ?  1119 MET   A CA  1 
ATOM   8900  C  C   . MET   A 1 1121 ? -46.10200  72.40800  -5.89400  1.000 40.57763  ?  1119 MET   A C   1 
ATOM   8901  O  O   . MET   A 1 1121 ? -45.31200  72.11000  -4.99300  1.000 48.47977  ?  1119 MET   A O   1 
ATOM   8902  C  CB  . MET   A 1 1121 ? -48.33000  71.30400  -5.90600  1.000 31.74003  ?  1119 MET   A CB  1 
ATOM   8903  C  CG  . MET   A 1 1121 ? -49.08200  70.00000  -6.09700  1.000 41.26910  ?  1119 MET   A CG  1 
ATOM   8904  S  SD  . MET   A 1 1121 ? -50.53500  69.90000  -5.03600  1.000 48.56137  ?  1119 MET   A SD  1 
ATOM   8905  C  CE  . MET   A 1 1121 ? -51.02200  71.61600  -5.00800  1.000 38.45250  ?  1119 MET   A CE  1 
ATOM   8906  N  N   . MET   A 1 1122 ? -46.27900  73.65600  -6.32100  1.000 54.58442  ?  1120 MET   A N   1 
ATOM   8907  C  CA  . MET   A 1 1122 ? -45.60300  74.78000  -5.68700  1.000 39.52313  ?  1120 MET   A CA  1 
ATOM   8908  C  C   . MET   A 1 1122 ? -46.51000  75.99900  -5.70900  1.000 43.94077  ?  1120 MET   A C   1 
ATOM   8909  O  O   . MET   A 1 1122 ? -46.99300  76.39900  -6.77300  1.000 50.03592  ?  1120 MET   A O   1 
ATOM   8910  C  CB  . MET   A 1 1122 ? -44.27300  75.10000  -6.37700  1.000 35.58290  ?  1120 MET   A CB  1 
ATOM   8911  C  CG  . MET   A 1 1122 ? -43.50100  76.21500  -5.69500  1.000 41.77168  ?  1120 MET   A CG  1 
ATOM   8912  S  SD  . MET   A 1 1122 ? -41.78800  76.30900  -6.23400  1.000 48.87303  ?  1120 MET   A SD  1 
ATOM   8913  C  CE  . MET   A 1 1122 ? -41.26700  74.62600  -5.94100  1.000 41.73177  ?  1120 MET   A CE  1 
ATOM   8914  N  N   . GLN   A 1 1123 ? -46.73700  76.57900  -4.53400  1.000 59.27368  ?  1121 GLN   A N   1 
ATOM   8915  C  CA  . GLN   A 1 1123 ? -47.50000  77.80900  -4.38200  1.000 58.90486  ?  1121 GLN   A CA  1 
ATOM   8916  C  C   . GLN   A 1 1123 ? -46.56300  78.92600  -3.94400  1.000 65.10511  ?  1121 GLN   A C   1 
ATOM   8917  O  O   . GLN   A 1 1123 ? -45.64100  78.70100  -3.15400  1.000 59.63901  ?  1121 GLN   A O   1 
ATOM   8918  C  CB  . GLN   A 1 1123 ? -48.62600  77.64000  -3.35600  1.000 59.09206  ?  1121 GLN   A CB  1 
ATOM   8919  C  CG  . GLN   A 1 1123 ? -49.58800  78.81800  -3.27300  1.000 72.51062  ?  1121 GLN   A CG  1 
ATOM   8920  C  CD  . GLN   A 1 1123 ? -50.79400  78.65900  -4.18100  1.000 83.34163  ?  1121 GLN   A CD  1 
ATOM   8921  O  OE1 . GLN   A 1 1123 ? -51.35500  77.57000  -4.30000  1.000 69.39117  ?  1121 GLN   A OE1 1 
ATOM   8922  N  NE2 . GLN   A 1 1123 ? -51.19900  79.74700  -4.82600  1.000 75.63658  ?  1121 GLN   A NE2 1 
ATOM   8923  N  N   . GLY   A 1 1124 ? -46.80300  80.12900  -4.45500  1.000 62.07424  ?  1122 GLY   A N   1 
ATOM   8924  C  CA  . GLY   A 1 1124 ? -45.97700  81.26800  -4.12200  1.000 60.23752  ?  1122 GLY   A CA  1 
ATOM   8925  C  C   . GLY   A 1 1124 ? -46.14300  81.70400  -2.67500  1.000 64.54339  ?  1122 GLY   A C   1 
ATOM   8926  O  O   . GLY   A 1 1124 ? -46.90000  81.13300  -1.88900  1.000 79.77734  ?  1122 GLY   A O   1 
ATOM   8927  N  N   . ALA   A 1 1125 ? -45.40200  82.75400  -2.32400  1.000 57.70894  ?  1123 ALA   A N   1 
ATOM   8928  C  CA  . ALA   A 1 1125 ? -45.44500  83.29600  -0.97800  1.000 54.82439  ?  1123 ALA   A CA  1 
ATOM   8929  C  C   . ALA   A 1 1125 ? -46.79700  83.95400  -0.70700  1.000 56.65746  ?  1123 ALA   A C   1 
ATOM   8930  O  O   . ALA   A 1 1125 ? -47.48900  84.38000  -1.63500  1.000 60.93857  ?  1123 ALA   A O   1 
ATOM   8931  C  CB  . ALA   A 1 1125 ? -44.31800  84.30600  -0.77800  1.000 55.80825  ?  1123 ALA   A CB  1 
ATOM   8932  N  N   . PRO   A 1 1126 ? -47.20200  84.03600  0.56200   1.000 48.87940  ?  1124 PRO   A N   1 
ATOM   8933  C  CA  . PRO   A 1 1126 ? -48.47200  84.70000  0.88300   1.000 50.92367  ?  1124 PRO   A CA  1 
ATOM   8934  C  C   . PRO   A 1 1126 ? -48.42300  86.18300  0.55300   1.000 48.52482  ?  1124 PRO   A C   1 
ATOM   8935  O  O   . PRO   A 1 1126 ? -47.42500  86.86400  0.80400   1.000 59.51200  ?  1124 PRO   A O   1 
ATOM   8936  C  CB  . PRO   A 1 1126 ? -48.62400  84.46800  2.39200   1.000 54.62823  ?  1124 PRO   A CB  1 
ATOM   8937  C  CG  . PRO   A 1 1126 ? -47.76100  83.28700  2.68800   1.000 46.10490  ?  1124 PRO   A CG  1 
ATOM   8938  C  CD  . PRO   A 1 1126 ? -46.60100  83.40300  1.74700   1.000 64.85639  ?  1124 PRO   A CD  1 
ATOM   8939  N  N   . GLU   A 1 1127 ? -49.52000  86.68200  -0.01700  1.000 45.12168  ?  1125 GLU   A N   1 
ATOM   8940  C  CA  . GLU   A 1 1127 ? -49.61300  88.08700  -0.39400  1.000 60.41888  ?  1125 GLU   A CA  1 
ATOM   8941  C  C   . GLU   A 1 1127 ? -50.13700  88.96800  0.73200   1.000 45.95592  ?  1125 GLU   A C   1 
ATOM   8942  O  O   . GLU   A 1 1127 ? -49.81500  90.16100  0.77500   1.000 57.74669  ?  1125 GLU   A O   1 
ATOM   8943  C  CB  . GLU   A 1 1127 ? -50.50200  88.24100  -1.63100  1.000 58.48433  ?  1125 GLU   A CB  1 
ATOM   8944  C  CG  . GLU   A 1 1127 ? -49.78100  87.95600  -2.93900  1.000 57.56003  ?  1125 GLU   A CG  1 
ATOM   8945  C  CD  . GLU   A 1 1127 ? -50.66300  87.26700  -3.96100  1.000 93.04850  ?  1125 GLU   A CD  1 
ATOM   8946  O  OE1 . GLU   A 1 1127 ? -51.90000  87.42500  -3.88400  1.000 93.90141  ?  1125 GLU   A OE1 1 
ATOM   8947  O  OE2 . GLU   A 1 1127 ? -50.11900  86.56400  -4.83800  1.000 108.12371 -1 1125 GLU   A OE2 1 
ATOM   8948  N  N   . THR   A 1 1128 ? -50.93100  88.41300  1.64100   1.000 43.00240  ?  1126 THR   A N   1 
ATOM   8949  C  CA  . THR   A 1 1128 ? -51.43100  89.13600  2.79800   1.000 43.35918  ?  1126 THR   A CA  1 
ATOM   8950  C  C   . THR   A 1 1128 ? -50.89400  88.49900  4.07300   1.000 52.16481  ?  1126 THR   A C   1 
ATOM   8951  O  O   . THR   A 1 1128 ? -50.43500  87.35400  4.07400   1.000 59.99433  ?  1126 THR   A O   1 
ATOM   8952  C  CB  . THR   A 1 1128 ? -52.96600  89.15400  2.82700   1.000 44.10780  ?  1126 THR   A CB  1 
ATOM   8953  O  OG1 . THR   A 1 1128 ? -53.47200  87.89400  2.36600   1.000 43.06169  ?  1126 THR   A OG1 1 
ATOM   8954  C  CG2 . THR   A 1 1128 ? -53.50100  90.26500  1.94300   1.000 51.85089  ?  1126 THR   A CG2 1 
ATOM   8955  N  N   . GLU   A 1 1129 ? -50.94400  89.26100  5.16800   1.000 46.20918  ?  1127 GLU   A N   1 
ATOM   8956  C  CA  . GLU   A 1 1129 ? -50.55300  88.69600  6.45400   1.000 46.02230  ?  1127 GLU   A CA  1 
ATOM   8957  C  C   . GLU   A 1 1129 ? -51.59500  87.70300  6.94900   1.000 58.81218  ?  1127 GLU   A C   1 
ATOM   8958  O  O   . GLU   A 1 1129 ? -51.25000  86.68800  7.56600   1.000 57.17540  ?  1127 GLU   A O   1 
ATOM   8959  C  CB  . GLU   A 1 1129 ? -50.33500  89.80200  7.48500   1.000 44.15837  ?  1127 GLU   A CB  1 
ATOM   8960  C  CG  . GLU   A 1 1129 ? -49.57800  89.32700  8.71600   1.000 57.06953  ?  1127 GLU   A CG  1 
ATOM   8961  C  CD  . GLU   A 1 1129 ? -49.62800  90.31700  9.86100   1.000 84.70704  ?  1127 GLU   A CD  1 
ATOM   8962  O  OE1 . GLU   A 1 1129 ? -50.13300  91.44100  9.65800   1.000 76.23620  ?  1127 GLU   A OE1 1 
ATOM   8963  O  OE2 . GLU   A 1 1129 ? -49.16600  89.96600  10.96800  1.000 99.39697  -1 1127 GLU   A OE2 1 
ATOM   8964  N  N   . LEU   A 1 1130 ? -52.87500  87.97700  6.68400   1.000 45.33904  ?  1128 LEU   A N   1 
ATOM   8965  C  CA  . LEU   A 1 1130 ? -53.92100  87.01800  7.01300   1.000 41.18133  ?  1128 LEU   A CA  1 
ATOM   8966  C  C   . LEU   A 1 1130 ? -53.73900  85.70700  6.26400   1.000 55.15067  ?  1128 LEU   A C   1 
ATOM   8967  O  O   . LEU   A 1 1130 ? -54.21200  84.66700  6.73100   1.000 69.07515  ?  1128 LEU   A O   1 
ATOM   8968  C  CB  . LEU   A 1 1130 ? -55.29800  87.61600  6.71200   1.000 38.31154  ?  1128 LEU   A CB  1 
ATOM   8969  C  CG  . LEU   A 1 1130 ? -56.51900  86.82900  7.19600   1.000 44.36604  ?  1128 LEU   A CG  1 
ATOM   8970  C  CD1 . LEU   A 1 1130 ? -56.43400  86.57000  8.69200   1.000 42.82272  ?  1128 LEU   A CD1 1 
ATOM   8971  C  CD2 . LEU   A 1 1130 ? -57.80300  87.56600  6.85300   1.000 50.45306  ?  1128 LEU   A CD2 1 
ATOM   8972  N  N   . GLU   A 1 1131 ? -53.05300  85.73100  5.11900   1.000 51.57136  ?  1129 GLU   A N   1 
ATOM   8973  C  CA  . GLU   A 1 1131 ? -52.77400  84.49800  4.39200   1.000 54.91276  ?  1129 GLU   A CA  1 
ATOM   8974  C  C   . GLU   A 1 1131 ? -51.57500  83.76500  4.98300   1.000 54.61667  ?  1129 GLU   A C   1 
ATOM   8975  O  O   . GLU   A 1 1131 ? -51.56900  82.53000  5.04100   1.000 62.27663  ?  1129 GLU   A O   1 
ATOM   8976  C  CB  . GLU   A 1 1131 ? -52.54000  84.80200  2.91100   1.000 45.44068  ?  1129 GLU   A CB  1 
ATOM   8977  C  CG  . GLU   A 1 1131 ? -52.47600  83.56900  2.02400   1.000 47.02950  ?  1129 GLU   A CG  1 
ATOM   8978  C  CD  . GLU   A 1 1131 ? -52.21600  83.90800  0.56800   1.000 59.25556  ?  1129 GLU   A CD  1 
ATOM   8979  O  OE1 . GLU   A 1 1131 ? -52.21800  85.11000  0.22600   1.000 56.94593  ?  1129 GLU   A OE1 1 
ATOM   8980  O  OE2 . GLU   A 1 1131 ? -52.00700  82.97300  -0.23300  1.000 58.02900  -1 1129 GLU   A OE2 1 
ATOM   8981  N  N   . SER   A 1 1132 ? -50.55700  84.50500  5.43000   1.000 50.47250  ?  1130 SER   A N   1 
ATOM   8982  C  CA  . SER   A 1 1132 ? -49.39200  83.87300  6.03800   1.000 45.85612  ?  1130 SER   A CA  1 
ATOM   8983  C  C   . SER   A 1 1132 ? -49.72700  83.20800  7.36300   1.000 57.37271  ?  1130 SER   A C   1 
ATOM   8984  O  O   . SER   A 1 1132 ? -48.96300  82.35400  7.82500   1.000 58.93359  ?  1130 SER   A O   1 
ATOM   8985  C  CB  . SER   A 1 1132 ? -48.27600  84.89800  6.24700   1.000 55.96517  ?  1130 SER   A CB  1 
ATOM   8986  O  OG  . SER   A 1 1132 ? -48.47700  85.63200  7.44300   1.000 67.56241  ?  1130 SER   A OG  1 
ATOM   8987  N  N   . ASN   A 1 1133 ? -50.84500  83.58000  7.98300   1.000 56.90604  ?  1131 ASN   A N   1 
ATOM   8988  C  CA  . ASN   A 1 1133 ? -51.28400  82.98800  9.23700   1.000 60.00539  ?  1131 ASN   A CA  1 
ATOM   8989  C  C   . ASN   A 1 1133 ? -52.39300  81.96200  9.04400   1.000 50.91892  ?  1131 ASN   A C   1 
ATOM   8990  O  O   . ASN   A 1 1133 ? -53.01800  81.54600  10.02600  1.000 62.18241  ?  1131 ASN   A O   1 
ATOM   8991  C  CB  . ASN   A 1 1133 ? -51.73500  84.08500  10.20400  1.000 51.95210  ?  1131 ASN   A CB  1 
ATOM   8992  C  CG  . ASN   A 1 1133 ? -50.58800  84.97800  10.64500  1.000 51.02397  ?  1131 ASN   A CG  1 
ATOM   8993  O  OD1 . ASN   A 1 1133 ? -49.45700  84.51900  10.80700  1.000 57.88487  ?  1131 ASN   A OD1 1 
ATOM   8994  N  ND2 . ASN   A 1 1133 ? -50.87500  86.26000  10.83800  1.000 68.46151  ?  1131 ASN   A ND2 1 
ATOM   8995  N  N   . MET   A 1 1134 ? -52.65300  81.54800  7.80800   1.000 39.67486  ?  1132 MET   A N   1 
ATOM   8996  C  CA  . MET   A 1 1134 ? -53.59700  80.47600  7.53600   1.000 51.40485  ?  1132 MET   A CA  1 
ATOM   8997  C  C   . MET   A 1 1134 ? -52.88900  79.13000  7.58700   1.000 56.02567  ?  1132 MET   A C   1 
ATOM   8998  O  O   . MET   A 1 1134 ? -51.68000  79.03000  7.36100   1.000 73.29446  ?  1132 MET   A O   1 
ATOM   8999  C  CB  . MET   A 1 1134 ? -54.26100  80.65800  6.17200   1.000 52.04785  ?  1132 MET   A CB  1 
ATOM   9000  C  CG  . MET   A 1 1134 ? -55.21900  81.82600  6.10300   1.000 49.32556  ?  1132 MET   A CG  1 
ATOM   9001  S  SD  . MET   A 1 1134 ? -56.01200  81.96500  4.49500   1.000 48.73999  ?  1132 MET   A SD  1 
ATOM   9002  C  CE  . MET   A 1 1134 ? -57.68100  81.52000  4.93500   1.000 48.28980  ?  1132 MET   A CE  1 
ATOM   9003  N  N   . HIS   A 1 1135 ? -53.65900  78.08700  7.88500   1.000 54.13910  ?  1133 HIS   A N   1 
ATOM   9004  C  CA  . HIS   A 1 1135 ? -53.13000  76.73600  8.02700   1.000 49.87689  ?  1133 HIS   A CA  1 
ATOM   9005  C  C   . HIS   A 1 1135 ? -54.00500  75.77800  7.23600   1.000 41.14024  ?  1133 HIS   A C   1 
ATOM   9006  O  O   . HIS   A 1 1135 ? -55.19400  75.63200  7.53500   1.000 41.46209  ?  1133 HIS   A O   1 
ATOM   9007  C  CB  . HIS   A 1 1135 ? -53.06800  76.32200  9.50000   1.000 40.00641  ?  1133 HIS   A CB  1 
ATOM   9008  C  CG  . HIS   A 1 1135 ? -52.01300  77.03900  10.28400  1.000 56.41966  ?  1133 HIS   A CG  1 
ATOM   9009  N  ND1 . HIS   A 1 1135 ? -50.98300  77.73200  9.68500   1.000 74.11278  ?  1133 HIS   A ND1 1 
ATOM   9010  C  CD2 . HIS   A 1 1135 ? -51.83000  77.17200  11.61900  1.000 53.19975  ?  1133 HIS   A CD2 1 
ATOM   9011  C  CE1 . HIS   A 1 1135 ? -50.21000  78.26000  10.61700  1.000 76.57647  ?  1133 HIS   A CE1 1 
ATOM   9012  N  NE2 . HIS   A 1 1135 ? -50.70100  77.93500  11.79900  1.000 68.53562  ?  1133 HIS   A NE2 1 
ATOM   9013  N  N   . HIS   A 1 1136 ? -53.42100  75.12900  6.23200   1.000 39.82197  ?  1134 HIS   A N   1 
ATOM   9014  C  CA  . HIS   A 1 1136 ? -54.14600  74.13400  5.45800   1.000 36.20831  ?  1134 HIS   A CA  1 
ATOM   9015  C  C   . HIS   A 1 1136 ? -54.22400  72.82700  6.23300   1.000 43.85799  ?  1134 HIS   A C   1 
ATOM   9016  O  O   . HIS   A 1 1136 ? -53.24100  72.38500  6.83500   1.000 53.26448  ?  1134 HIS   A O   1 
ATOM   9017  C  CB  . HIS   A 1 1136 ? -53.47300  73.90100  4.10500   1.000 37.93851  ?  1134 HIS   A CB  1 
ATOM   9018  C  CG  . HIS   A 1 1136 ? -54.33300  73.16500  3.12400   1.000 55.47719  ?  1134 HIS   A CG  1 
ATOM   9019  N  ND1 . HIS   A 1 1136 ? -53.81600  72.32000  2.16600   1.000 54.76433  ?  1134 HIS   A ND1 1 
ATOM   9020  C  CD2 . HIS   A 1 1136 ? -55.67700  73.15200  2.95100   1.000 62.16224  ?  1134 HIS   A CD2 1 
ATOM   9021  C  CE1 . HIS   A 1 1136 ? -54.80400  71.81500  1.44800   1.000 60.85520  ?  1134 HIS   A CE1 1 
ATOM   9022  N  NE2 . HIS   A 1 1136 ? -55.94300  72.30400  1.90300   1.000 60.10312  ?  1134 HIS   A NE2 1 
ATOM   9023  N  N   . ILE   A 1 1137 ? -55.40100  72.20900  6.21600   1.000 41.65118  ?  1135 ILE   A N   1 
ATOM   9024  C  CA  . ILE   A 1 1137 ? -55.66500  70.98900  6.96700   1.000 45.33794  ?  1135 ILE   A CA  1 
ATOM   9025  C  C   . ILE   A 1 1137 ? -55.78100  69.83000  5.98900   1.000 53.30634  ?  1135 ILE   A C   1 
ATOM   9026  O  O   . ILE   A 1 1137 ? -56.40000  69.96000  4.92500   1.000 50.06794  ?  1135 ILE   A O   1 
ATOM   9027  C  CB  . ILE   A 1 1137 ? -56.94300  71.11300  7.81800   1.000 50.75087  ?  1135 ILE   A CB  1 
ATOM   9028  C  CG1 . ILE   A 1 1137 ? -57.10000  72.54100  8.33800   1.000 46.99456  ?  1135 ILE   A CG1 1 
ATOM   9029  C  CG2 . ILE   A 1 1137 ? -56.89200  70.14600  8.97900   1.000 48.41390  ?  1135 ILE   A CG2 1 
ATOM   9030  C  CD1 . ILE   A 1 1137 ? -56.01600  72.96100  9.29400   1.000 42.55735  ?  1135 ILE   A CD1 1 
ATOM   9031  N  N   . ASN   A 1 1138 ? -55.19300  68.69100  6.35500   1.000 44.81670  ?  1136 ASN   A N   1 
ATOM   9032  C  CA  . ASN   A 1 1138 ? -55.22100  67.51500  5.49500   1.000 59.09187  ?  1136 ASN   A CA  1 
ATOM   9033  C  C   . ASN   A 1 1138 ? -56.43200  66.62800  5.75600   1.000 57.67703  ?  1136 ASN   A C   1 
ATOM   9034  O  O   . ASN   A 1 1138 ? -56.97200  66.03300  4.81600   1.000 74.49772  ?  1136 ASN   A O   1 
ATOM   9035  C  CB  . ASN   A 1 1138 ? -53.93900  66.70000  5.67200   1.000 36.65884  ?  1136 ASN   A CB  1 
ATOM   9036  C  CG  . ASN   A 1 1138 ? -53.91000  65.46400  4.79400   1.000 45.28002  ?  1136 ASN   A CG  1 
ATOM   9037  O  OD1 . ASN   A 1 1138 ? -54.07400  64.34300  5.27400   1.000 54.35485  ?  1136 ASN   A OD1 1 
ATOM   9038  N  ND2 . ASN   A 1 1138 ? -53.71100  65.66600  3.49700   1.000 59.06783  ?  1136 ASN   A ND2 1 
ATOM   9039  N  N   . ALA   A 1 1139 ? -56.86100  66.52300  7.01400   1.000 29.94703  ?  1137 ALA   A N   1 
ATOM   9040  C  CA  . ALA   A 1 1139 ? -57.99900  65.69800  7.42100   1.000 42.99967  ?  1137 ALA   A CA  1 
ATOM   9041  C  C   . ALA   A 1 1139 ? -57.79300  64.22000  7.10300   1.000 45.20304  ?  1137 ALA   A C   1 
ATOM   9042  O  O   . ALA   A 1 1139 ? -58.76400  63.46500  6.98500   1.000 34.87193  ?  1137 ALA   A O   1 
ATOM   9043  C  CB  . ALA   A 1 1139 ? -59.30600  66.19600  6.79200   1.000 31.11442  ?  1137 ALA   A CB  1 
ATOM   9044  N  N   . GLY   A 1 1140 ? -56.54200  63.79100  6.96900   1.000 39.74642  ?  1138 GLY   A N   1 
ATOM   9045  C  CA  . GLY   A 1 1140 ? -56.23800  62.38700  6.74500   1.000 32.94047  ?  1138 GLY   A CA  1 
ATOM   9046  C  C   . GLY   A 1 1140 ? -56.55600  61.88300  5.35300   1.000 38.69314  ?  1138 GLY   A C   1 
ATOM   9047  O  O   . GLY   A 1 1140 ? -56.98700  60.73300  5.20000   1.000 46.68934  ?  1138 GLY   A O   1 
ATOM   9048  N  N   . ILE   A 1 1141 ? -56.35000  62.71300  4.33300   1.000 43.77592  ?  1139 ILE   A N   1 
ATOM   9049  C  CA  . ILE   A 1 1141 ? -56.66300  62.36700  2.95100   1.000 53.65620  ?  1139 ILE   A CA  1 
ATOM   9050  C  C   . ILE   A 1 1141 ? -55.41000  62.53300  2.10100   1.000 48.55680  ?  1139 ILE   A C   1 
ATOM   9051  O  O   . ILE   A 1 1141 ? -54.64900  63.49100  2.27900   1.000 44.35854  ?  1139 ILE   A O   1 
ATOM   9052  C  CB  . ILE   A 1 1141 ? -57.82600  63.22300  2.39800   1.000 49.90034  ?  1139 ILE   A CB  1 
ATOM   9053  C  CG1 . ILE   A 1 1141 ? -59.15900  62.47600  2.52700   1.000 34.65611  ?  1139 ILE   A CG1 1 
ATOM   9054  C  CG2 . ILE   A 1 1141 ? -57.58400  63.62300  0.94500   1.000 45.51791  ?  1139 ILE   A CG2 1 
ATOM   9055  C  CD1 . ILE   A 1 1141 ? -59.62300  62.24600  3.95200   1.000 35.70900  ?  1139 ILE   A CD1 1 
ATOM   9056  N  N   . SER   A 1 1142 ? -55.19000  61.58500  1.18900   1.000 40.10926  ?  1140 SER   A N   1 
ATOM   9057  C  CA  . SER   A 1 1142 ? -54.10400  61.65100  0.21200   1.000 43.39598  ?  1140 SER   A CA  1 
ATOM   9058  C  C   . SER   A 1 1142 ? -54.70900  61.38700  -1.16400  1.000 53.60419  ?  1140 SER   A C   1 
ATOM   9059  O  O   . SER   A 1 1142 ? -55.03700  60.24300  -1.49400  1.000 49.28269  ?  1140 SER   A O   1 
ATOM   9060  C  CB  . SER   A 1 1142 ? -53.00100  60.65000  0.53900   1.000 49.48819  ?  1140 SER   A CB  1 
ATOM   9061  O  OG  . SER   A 1 1142 ? -51.87300  60.84200  -0.29600  1.000 53.31061  ?  1140 SER   A OG  1 
ATOM   9062  N  N   . LYS   A 1 1143 ? -54.85500  62.44800  -1.96400  1.000 46.81506  ?  1141 LYS   A N   1 
ATOM   9063  C  CA  . LYS   A 1 1143 ? -55.48900  62.31200  -3.27200  1.000 41.17661  ?  1141 LYS   A CA  1 
ATOM   9064  C  C   . LYS   A 1 1143 ? -54.66300  61.44400  -4.21200  1.000 42.11358  ?  1141 LYS   A C   1 
ATOM   9065  O  O   . LYS   A 1 1143 ? -55.21900  60.78300  -5.09700  1.000 56.58160  ?  1141 LYS   A O   1 
ATOM   9066  C  CB  . LYS   A 1 1143 ? -55.72000  63.69100  -3.89100  1.000 42.76457  ?  1141 LYS   A CB  1 
ATOM   9067  C  CG  . LYS   A 1 1143 ? -56.53200  64.64300  -3.02300  1.000 44.08130  ?  1141 LYS   A CG  1 
ATOM   9068  C  CD  . LYS   A 1 1143 ? -56.44300  66.06600  -3.55200  1.000 41.84935  ?  1141 LYS   A CD  1 
ATOM   9069  C  CE  . LYS   A 1 1143 ? -56.49200  67.09100  -2.42500  1.000 49.47563  ?  1141 LYS   A CE  1 
ATOM   9070  N  NZ  . LYS   A 1 1143 ? -57.88100  67.49500  -2.06700  1.000 28.96211  ?  1141 LYS   A NZ  1 
ATOM   9071  N  N   . PHE   A 1 1144 ? -53.34500  61.43300  -4.04400  1.000 45.40813  ?  1142 PHE   A N   1 
ATOM   9072  C  CA  . PHE   A 1 1144 ? -52.45600  60.60200  -4.83900  1.000 42.86008  ?  1142 PHE   A CA  1 
ATOM   9073  C  C   . PHE   A 1 1144 ? -51.60400  59.75800  -3.90200  1.000 44.48404  ?  1142 PHE   A C   1 
ATOM   9074  O  O   . PHE   A 1 1144 ? -51.66400  59.90000  -2.67700  1.000 49.10073  ?  1142 PHE   A O   1 
ATOM   9075  C  CB  . PHE   A 1 1144 ? -51.56500  61.44900  -5.75900  1.000 38.76499  ?  1142 PHE   A CB  1 
ATOM   9076  C  CG  . PHE   A 1 1144 ? -52.32200  62.45700  -6.58000  1.000 46.75584  ?  1142 PHE   A CG  1 
ATOM   9077  C  CD1 . PHE   A 1 1144 ? -52.83700  62.11700  -7.81900  1.000 40.25159  ?  1142 PHE   A CD1 1 
ATOM   9078  C  CD2 . PHE   A 1 1144 ? -52.51100  63.74900  -6.11200  1.000 47.87155  ?  1142 PHE   A CD2 1 
ATOM   9079  C  CE1 . PHE   A 1 1144 ? -53.53000  63.04400  -8.57500  1.000 49.22853  ?  1142 PHE   A CE1 1 
ATOM   9080  C  CE2 . PHE   A 1 1144 ? -53.20300  64.68000  -6.86300  1.000 41.45052  ?  1142 PHE   A CE2 1 
ATOM   9081  C  CZ  . PHE   A 1 1144 ? -53.71300  64.32700  -8.09700  1.000 47.20200  ?  1142 PHE   A CZ  1 
ATOM   9082  N  N   . ASP   A 1 1145 ? -50.80600  58.86500  -4.49200  1.000 43.01380  ?  1143 ASP   A N   1 
ATOM   9083  C  CA  . ASP   A 1 1145 ? -49.91100  58.03300  -3.69400  1.000 37.06712  ?  1143 ASP   A CA  1 
ATOM   9084  C  C   . ASP   A 1 1145 ? -48.95200  58.89200  -2.88100  1.000 35.16685  ?  1143 ASP   A C   1 
ATOM   9085  O  O   . ASP   A 1 1145 ? -48.74000  58.65100  -1.68700  1.000 44.02673  ?  1143 ASP   A O   1 
ATOM   9086  C  CB  . ASP   A 1 1145 ? -49.13700  57.07300  -4.59900  1.000 39.77258  ?  1143 ASP   A CB  1 
ATOM   9087  C  CG  . ASP   A 1 1145 ? -50.02900  56.03400  -5.24800  1.000 56.39550  ?  1143 ASP   A CG  1 
ATOM   9088  O  OD1 . ASP   A 1 1145 ? -51.24000  56.00500  -4.94200  1.000 57.12160  ?  1143 ASP   A OD1 1 
ATOM   9089  O  OD2 . ASP   A 1 1145 ? -49.51400  55.24300  -6.06600  1.000 54.40576  -1 1143 ASP   A OD2 1 
ATOM   9090  N  N   . LEU   A 1 1146 ? -48.36800  59.90700  -3.51300  1.000 32.13118  ?  1144 LEU   A N   1 
ATOM   9091  C  CA  . LEU   A 1 1146 ? -47.45500  60.81800  -2.83800  1.000 30.77802  ?  1144 LEU   A CA  1 
ATOM   9092  C  C   . LEU   A 1 1146 ? -47.56100  62.18400  -3.49400  1.000 32.72037  ?  1144 LEU   A C   1 
ATOM   9093  O  O   . LEU   A 1 1146 ? -47.51100  62.28800  -4.72300  1.000 33.29895  ?  1144 LEU   A O   1 
ATOM   9094  C  CB  . LEU   A 1 1146 ? -46.01200  60.30900  -2.90100  1.000 40.10558  ?  1144 LEU   A CB  1 
ATOM   9095  C  CG  . LEU   A 1 1146 ? -44.96300  61.19100  -2.22000  1.000 28.29228  ?  1144 LEU   A CG  1 
ATOM   9096  C  CD1 . LEU   A 1 1146 ? -45.15600  61.19100  -0.71300  1.000 31.81313  ?  1144 LEU   A CD1 1 
ATOM   9097  C  CD2 . LEU   A 1 1146 ? -43.55800  60.74400  -2.58700  1.000 23.56510  ?  1144 LEU   A CD2 1 
ATOM   9098  N  N   . THR   A 1 1147 ? -47.71100  63.22300  -2.67700  1.000 40.74060  ?  1145 THR   A N   1 
ATOM   9099  C  CA  . THR   A 1 1147 ? -47.78300  64.59500  -3.15900  1.000 40.14856  ?  1145 THR   A CA  1 
ATOM   9100  C  C   . THR   A 1 1147 ? -46.74600  65.42700  -2.42100  1.000 29.33262  ?  1145 THR   A C   1 
ATOM   9101  O  O   . THR   A 1 1147 ? -46.63100  65.33500  -1.19500  1.000 32.29050  ?  1145 THR   A O   1 
ATOM   9102  C  CB  . THR   A 1 1147 ? -49.18200  65.19000  -2.95800  1.000 46.16041  ?  1145 THR   A CB  1 
ATOM   9103  O  OG1 . THR   A 1 1147 ? -50.16700  64.29300  -3.48800  1.000 52.93549  ?  1145 THR   A OG1 1 
ATOM   9104  C  CG2 . THR   A 1 1147 ? -49.29700  66.53300  -3.66700  1.000 28.19077  ?  1145 THR   A CG2 1 
ATOM   9105  N  N   . LEU   A 1 1148 ? -45.98700  66.22500  -3.16900  1.000 25.62483  ?  1146 LEU   A N   1 
ATOM   9106  C  CA  . LEU   A 1 1148 ? -45.00100  67.14100  -2.60800  1.000 27.14556  ?  1146 LEU   A CA  1 
ATOM   9107  C  C   . LEU   A 1 1148 ? -45.40400  68.56300  -2.96300  1.000 33.78191  ?  1146 LEU   A C   1 
ATOM   9108  O  O   . LEU   A 1 1148 ? -45.46700  68.91700  -4.14500  1.000 40.99792  ?  1146 LEU   A O   1 
ATOM   9109  C  CB  . LEU   A 1 1148 ? -43.59400  66.83900  -3.13000  1.000 20.53664  ?  1146 LEU   A CB  1 
ATOM   9110  C  CG  . LEU   A 1 1148 ? -42.70800  65.92800  -2.27900  1.000 27.78865  ?  1146 LEU   A CG  1 
ATOM   9111  C  CD1 . LEU   A 1 1148 ? -43.28900  64.52600  -2.19700  1.000 43.04101  ?  1146 LEU   A CD1 1 
ATOM   9112  C  CD2 . LEU   A 1 1148 ? -41.28900  65.89400  -2.82800  1.000 26.42485  ?  1146 LEU   A CD2 1 
ATOM   9113  N  N   . GLU   A 1 1149 ? -45.67800  69.37200  -1.94400  1.000 29.54718  ?  1147 GLU   A N   1 
ATOM   9114  C  CA  . GLU   A 1 1149 ? -46.03800  70.77100  -2.12500  1.000 30.84569  ?  1147 GLU   A CA  1 
ATOM   9115  C  C   . GLU   A 1 1149 ? -44.99300  71.63200  -1.43400  1.000 33.08564  ?  1147 GLU   A C   1 
ATOM   9116  O  O   . GLU   A 1 1149 ? -44.73600  71.46000  -0.23800  1.000 42.04638  ?  1147 GLU   A O   1 
ATOM   9117  C  CB  . GLU   A 1 1149 ? -47.43200  71.06400  -1.56700  1.000 44.42796  ?  1147 GLU   A CB  1 
ATOM   9118  C  CG  . GLU   A 1 1149 ? -47.91200  72.48000  -1.83800  1.000 47.59664  ?  1147 GLU   A CG  1 
ATOM   9119  C  CD  . GLU   A 1 1149 ? -49.29900  72.74400  -1.28900  1.000 54.89256  ?  1147 GLU   A CD  1 
ATOM   9120  O  OE1 . GLU   A 1 1149 ? -49.79800  71.90700  -0.50700  1.000 57.34337  ?  1147 GLU   A OE1 1 
ATOM   9121  O  OE2 . GLU   A 1 1149 ? -49.88900  73.78700  -1.64100  1.000 54.40229  -1 1147 GLU   A OE2 1 
ATOM   9122  N  N   . VAL   A 1 1150 ? -44.39300  72.54800  -2.18600  1.000 31.90889  ?  1148 VAL   A N   1 
ATOM   9123  C  CA  . VAL   A 1 1150 ? -43.39000  73.46700  -1.66300  1.000 34.20828  ?  1148 VAL   A CA  1 
ATOM   9124  C  C   . VAL   A 1 1150 ? -44.05400  74.81900  -1.45100  1.000 34.13534  ?  1148 VAL   A C   1 
ATOM   9125  O  O   . VAL   A 1 1150 ? -44.53700  75.44100  -2.40500  1.000 42.79994  ?  1148 VAL   A O   1 
ATOM   9126  C  CB  . VAL   A 1 1150 ? -42.18600  73.58100  -2.61000  1.000 32.14368  ?  1148 VAL   A CB  1 
ATOM   9127  C  CG1 . VAL   A 1 1150 ? -41.15300  74.54700  -2.04500  1.000 25.35354  ?  1148 VAL   A CG1 1 
ATOM   9128  C  CG2 . VAL   A 1 1150 ? -41.57600  72.20900  -2.85000  1.000 26.32394  ?  1148 VAL   A CG2 1 
ATOM   9129  N  N   . LEU   A 1 1151 ? -44.07900  75.27600  -0.20100  1.000 34.06522  ?  1149 LEU   A N   1 
ATOM   9130  C  CA  . LEU   A 1 1151 ? -44.72400  76.52700  0.17700   1.000 38.57710  ?  1149 LEU   A CA  1 
ATOM   9131  C  C   . LEU   A 1 1151 ? -43.67000  77.48300  0.71600   1.000 39.44390  ?  1149 LEU   A C   1 
ATOM   9132  O  O   . LEU   A 1 1151 ? -42.93200  77.13700  1.64400   1.000 34.20991  ?  1149 LEU   A O   1 
ATOM   9133  C  CB  . LEU   A 1 1151 ? -45.81400  76.28000  1.22200   1.000 30.49339  ?  1149 LEU   A CB  1 
ATOM   9134  C  CG  . LEU   A 1 1151 ? -46.97500  75.38900  0.77700   1.000 36.56241  ?  1149 LEU   A CG  1 
ATOM   9135  C  CD1 . LEU   A 1 1151 ? -47.68600  74.79700  1.98100   1.000 34.27940  ?  1149 LEU   A CD1 1 
ATOM   9136  C  CD2 . LEU   A 1 1151 ? -47.94900  76.17600  -0.08500  1.000 52.05260  ?  1149 LEU   A CD2 1 
ATOM   9137  N  N   . GLU   A 1 1152 ? -43.60100  78.68000  0.13500   1.000 38.40854  ?  1150 GLU   A N   1 
ATOM   9138  C  CA  . GLU   A 1 1152 ? -42.65200  79.69800  0.57500   1.000 40.12464  ?  1150 GLU   A CA  1 
ATOM   9139  C  C   . GLU   A 1 1152 ? -43.24000  80.42700  1.77600   1.000 43.07904  ?  1150 GLU   A C   1 
ATOM   9140  O  O   . GLU   A 1 1152 ? -44.17000  81.22600  1.63000   1.000 54.55918  ?  1150 GLU   A O   1 
ATOM   9141  C  CB  . GLU   A 1 1152 ? -42.34200  80.67300  -0.55700  1.000 40.57507  ?  1150 GLU   A CB  1 
ATOM   9142  C  CG  . GLU   A 1 1152 ? -42.08900  80.01300  -1.90100  1.000 53.42489  ?  1150 GLU   A CG  1 
ATOM   9143  C  CD  . GLU   A 1 1152 ? -41.52300  80.97700  -2.92500  1.000 66.50629  ?  1150 GLU   A CD  1 
ATOM   9144  O  OE1 . GLU   A 1 1152 ? -40.80900  81.92200  -2.52500  1.000 53.55471  ?  1150 GLU   A OE1 1 
ATOM   9145  O  OE2 . GLU   A 1 1152 ? -41.79300  80.79200  -4.13100  1.000 82.27819  -1 1150 GLU   A OE2 1 
ATOM   9146  N  N   . ARG   A 1 1153 ? -42.69900  80.15600  2.96300   1.000 41.47582  ?  1151 ARG   A N   1 
ATOM   9147  C  CA  . ARG   A 1 1153 ? -43.21000  80.72600  4.20300   1.000 44.98742  ?  1151 ARG   A CA  1 
ATOM   9148  C  C   . ARG   A 1 1153 ? -42.04800  81.17200  5.07700   1.000 53.71286  ?  1151 ARG   A C   1 
ATOM   9149  O  O   . ARG   A 1 1153 ? -41.11100  80.40000  5.30600   1.000 57.96030  ?  1151 ARG   A O   1 
ATOM   9150  C  CB  . ARG   A 1 1153 ? -44.07700  79.71300  4.96200   1.000 44.40402  ?  1151 ARG   A CB  1 
ATOM   9151  C  CG  . ARG   A 1 1153 ? -45.57400  80.01100  4.96200   1.000 51.11989  ?  1151 ARG   A CG  1 
ATOM   9152  C  CD  . ARG   A 1 1153 ? -46.19400  79.82900  3.58600   1.000 47.02172  ?  1151 ARG   A CD  1 
ATOM   9153  N  NE  . ARG   A 1 1153 ? -47.64000  79.65600  3.65800   1.000 55.21437  ?  1151 ARG   A NE  1 
ATOM   9154  C  CZ  . ARG   A 1 1153 ? -48.44500  79.61600  2.60400   1.000 71.60646  ?  1151 ARG   A CZ  1 
ATOM   9155  N  NH1 . ARG   A 1 1153 ? -47.98100  79.76700  1.37400   1.000 56.62306  ?  1151 ARG   A NH1 1 
ATOM   9156  N  NH2 . ARG   A 1 1153 ? -49.74800  79.42200  2.79000   1.000 80.92327  ?  1151 ARG   A NH2 1 
ATOM   9157  N  N   . GLU   A 1 1154 ? -42.11800  82.41500  5.56100   1.000 54.58544  ?  1152 GLU   A N   1 
ATOM   9158  C  CA  . GLU   A 1 1154 ? -41.14200  82.96900  6.50300   1.000 48.46505  ?  1152 GLU   A CA  1 
ATOM   9159  C  C   . GLU   A 1 1154 ? -39.72300  82.92500  5.93500   1.000 49.48925  ?  1152 GLU   A C   1 
ATOM   9160  O  O   . GLU   A 1 1154 ? -38.78200  82.46100  6.58300   1.000 50.57287  ?  1152 GLU   A O   1 
ATOM   9161  C  CB  . GLU   A 1 1154 ? -41.21500  82.25100  7.85400   1.000 59.73186  ?  1152 GLU   A CB  1 
ATOM   9162  C  CG  . GLU   A 1 1154 ? -42.55000  82.40900  8.56200   1.000 59.85024  ?  1152 GLU   A CG  1 
ATOM   9163  C  CD  . GLU   A 1 1154 ? -42.39300  82.75300  10.03000  1.000 78.60138  ?  1152 GLU   A CD  1 
ATOM   9164  O  OE1 . GLU   A 1 1154 ? -41.49500  82.18300  10.68500  1.000 92.90910  ?  1152 GLU   A OE1 1 
ATOM   9165  O  OE2 . GLU   A 1 1154 ? -43.16200  83.60400  10.52600  1.000 90.88271  -1 1152 GLU   A OE2 1 
ATOM   9166  N  N   . ASN   A 1 1155 ? -39.57800  83.41600  4.70500   1.000 50.15762  ?  1153 ASN   A N   1 
ATOM   9167  C  CA  . ASN   A 1 1155 ? -38.31000  83.49200  3.98200   1.000 52.21118  ?  1153 ASN   A CA  1 
ATOM   9168  C  C   . ASN   A 1 1155 ? -37.67200  82.12700  3.75100   1.000 52.53780  ?  1153 ASN   A C   1 
ATOM   9169  O  O   . ASN   A 1 1155 ? -36.53700  82.05500  3.26200   1.000 55.36717  ?  1153 ASN   A O   1 
ATOM   9170  C  CB  . ASN   A 1 1155 ? -37.31500  84.41900  4.69200   1.000 47.15310  ?  1153 ASN   A CB  1 
ATOM   9171  C  CG  . ASN   A 1 1155 ? -37.70700  85.87800  4.58700   1.000 66.65044  ?  1153 ASN   A CG  1 
ATOM   9172  O  OD1 . ASN   A 1 1155 ? -38.08300  86.35400  3.51500   1.000 74.84403  ?  1153 ASN   A OD1 1 
ATOM   9173  N  ND2 . ASN   A 1 1155 ? -37.62900  86.59500  5.70200   1.000 74.40234  ?  1153 ASN   A ND2 1 
ATOM   9174  N  N   . GLY   A 1 1156 ? -38.36800  81.04300  4.08300   1.000 53.94689  ?  1154 GLY   A N   1 
ATOM   9175  C  CA  . GLY   A 1 1156 ? -37.86300  79.70500  3.84900   1.000 48.43279  ?  1154 GLY   A CA  1 
ATOM   9176  C  C   . GLY   A 1 1156 ? -38.79600  78.89400  2.97500   1.000 50.13633  ?  1154 GLY   A C   1 
ATOM   9177  O  O   . GLY   A 1 1156 ? -39.68200  79.45200  2.32100   1.000 47.84349  ?  1154 GLY   A O   1 
ATOM   9178  N  N   . LEU   A 1 1157 ? -38.61100  77.57600  2.95400   1.000 40.21255  ?  1155 LEU   A N   1 
ATOM   9179  C  CA  . LEU   A 1 1157 ? -39.43800  76.68100  2.15400   1.000 34.27048  ?  1155 LEU   A CA  1 
ATOM   9180  C  C   . LEU   A 1 1157 ? -39.98800  75.58400  3.05000   1.000 36.40367  ?  1155 LEU   A C   1 
ATOM   9181  O  O   . LEU   A 1 1157 ? -39.21900  74.85800  3.68800   1.000 40.70570  ?  1155 LEU   A O   1 
ATOM   9182  C  CB  . LEU   A 1 1157 ? -38.64200  76.07500  0.99400   1.000 27.90197  ?  1155 LEU   A CB  1 
ATOM   9183  C  CG  . LEU   A 1 1157 ? -38.26100  77.02500  -0.14200  1.000 39.60638  ?  1155 LEU   A CG  1 
ATOM   9184  C  CD1 . LEU   A 1 1157 ? -37.45800  76.29100  -1.20400  1.000 41.09795  ?  1155 LEU   A CD1 1 
ATOM   9185  C  CD2 . LEU   A 1 1157 ? -39.50200  77.66000  -0.74700  1.000 34.13626  ?  1155 LEU   A CD2 1 
ATOM   9186  N  N   . ASN   A 1 1158 ? -41.31300  75.46800  3.09800   1.000 38.38452  ?  1156 ASN   A N   1 
ATOM   9187  C  CA  . ASN   A 1 1158 ? -41.98700  74.39200  3.81700   1.000 35.95449  ?  1156 ASN   A CA  1 
ATOM   9188  C  C   . ASN   A 1 1158 ? -42.46200  73.37000  2.79100   1.000 34.98367  ?  1156 ASN   A C   1 
ATOM   9189  O  O   . ASN   A 1 1158 ? -43.43400  73.61100  2.06800   1.000 36.63820  ?  1156 ASN   A O   1 
ATOM   9190  C  CB  . ASN   A 1 1158 ? -43.15300  74.92800  4.64600   1.000 31.31073  ?  1156 ASN   A CB  1 
ATOM   9191  C  CG  . ASN   A 1 1158 ? -42.69700  75.80900  5.79500   1.000 44.67835  ?  1156 ASN   A CG  1 
ATOM   9192  O  OD1 . ASN   A 1 1158 ? -41.59400  76.35500  5.77500   1.000 54.20308  ?  1156 ASN   A OD1 1 
ATOM   9193  N  ND2 . ASN   A 1 1158 ? -43.54700  75.95200  6.80600   1.000 31.03031  ?  1156 ASN   A ND2 1 
ATOM   9194  N  N   . ILE   A 1 1159 ? -41.77100  72.23800  2.72400   1.000 35.04600  ?  1157 ILE   A N   1 
ATOM   9195  C  CA  . ILE   A 1 1159 ? -42.06800  71.18200  1.76400   1.000 32.95096  ?  1157 ILE   A CA  1 
ATOM   9196  C  C   . ILE   A 1 1159 ? -42.94300  70.15200  2.46800   1.000 40.47996  ?  1157 ILE   A C   1 
ATOM   9197  O  O   . ILE   A 1 1159 ? -42.50000  69.48100  3.40600   1.000 41.88946  ?  1157 ILE   A O   1 
ATOM   9198  C  CB  . ILE   A 1 1159 ? -40.78600  70.55100  1.20900   1.000 31.39892  ?  1157 ILE   A CB  1 
ATOM   9199  C  CG1 . ILE   A 1 1159 ? -39.82100  71.64800  0.75500   1.000 28.64628  ?  1157 ILE   A CG1 1 
ATOM   9200  C  CG2 . ILE   A 1 1159 ? -41.11000  69.61500  0.05700   1.000 26.93260  ?  1157 ILE   A CG2 1 
ATOM   9201  C  CD1 . ILE   A 1 1159 ? -38.52500  71.13100  0.18200   1.000 27.88022  ?  1157 ILE   A CD1 1 
ATOM   9202  N  N   . VAL   A 1 1160 ? -44.18600  70.02400  2.01300   1.000 36.71077  ?  1158 VAL   A N   1 
ATOM   9203  C  CA  . VAL   A 1 1160 ? -45.18100  69.16400  2.64500   1.000 29.43189  ?  1158 VAL   A CA  1 
ATOM   9204  C  C   . VAL   A 1 1160 ? -45.26300  67.85200  1.87900   1.000 33.49534  ?  1158 VAL   A C   1 
ATOM   9205  O  O   . VAL   A 1 1160 ? -45.42300  67.84700  0.65200   1.000 37.77616  ?  1158 VAL   A O   1 
ATOM   9206  C  CB  . VAL   A 1 1160 ? -46.55100  69.85900  2.70300   1.000 24.97074  ?  1158 VAL   A CB  1 
ATOM   9207  C  CG1 . VAL   A 1 1160 ? -47.65800  68.83900  2.88200   1.000 40.06260  ?  1158 VAL   A CG1 1 
ATOM   9208  C  CG2 . VAL   A 1 1160 ? -46.57400  70.87200  3.83300   1.000 37.08755  ?  1158 VAL   A CG2 1 
ATOM   9209  N  N   . PHE   A 1 1161 ? -45.16000  66.73900  2.60400   1.000 22.40963  ?  1159 PHE   A N   1 
ATOM   9210  C  CA  . PHE   A 1 1161 ? -45.20300  65.39500  2.02900   1.000 21.29003  ?  1159 PHE   A CA  1 
ATOM   9211  C  C   . PHE   A 1 1161 ? -46.54300  64.76200  2.38800   1.000 36.64380  ?  1159 PHE   A C   1 
ATOM   9212  O  O   . PHE   A 1 1161 ? -46.73600  64.29500  3.51500   1.000 42.87250  ?  1159 PHE   A O   1 
ATOM   9213  C  CB  . PHE   A 1 1161 ? -44.04000  64.54700  2.53600   1.000 29.06846  ?  1159 PHE   A CB  1 
ATOM   9214  C  CG  . PHE   A 1 1161 ? -42.70100  64.94500  1.97700   1.000 35.57534  ?  1159 PHE   A CG  1 
ATOM   9215  C  CD1 . PHE   A 1 1161 ? -42.08800  66.12200  2.37400   1.000 36.22766  ?  1159 PHE   A CD1 1 
ATOM   9216  C  CD2 . PHE   A 1 1161 ? -42.04800  64.13000  1.06700   1.000 25.65613  ?  1159 PHE   A CD2 1 
ATOM   9217  C  CE1 . PHE   A 1 1161 ? -40.85600  66.48500  1.86500   1.000 37.48534  ?  1159 PHE   A CE1 1 
ATOM   9218  C  CE2 . PHE   A 1 1161 ? -40.81600  64.48700  0.55400   1.000 27.24986  ?  1159 PHE   A CE2 1 
ATOM   9219  C  CZ  . PHE   A 1 1161 ? -40.21800  65.66600  0.95500   1.000 34.71149  ?  1159 PHE   A CZ  1 
ATOM   9220  N  N   . GLU   A 1 1162 ? -47.46600  64.75200  1.43100   1.000 39.23741  ?  1160 GLU   A N   1 
ATOM   9221  C  CA  . GLU   A 1 1162 ? -48.75400  64.08600  1.58100   1.000 32.56682  ?  1160 GLU   A CA  1 
ATOM   9222  C  C   . GLU   A 1 1162 ? -48.64600  62.69600  0.97000   1.000 37.48404  ?  1160 GLU   A C   1 
ATOM   9223  O  O   . GLU   A 1 1162 ? -48.35300  62.56200  -0.22300  1.000 46.33819  ?  1160 GLU   A O   1 
ATOM   9224  C  CB  . GLU   A 1 1162 ? -49.86900  64.88700  0.91100   1.000 44.88840  ?  1160 GLU   A CB  1 
ATOM   9225  C  CG  . GLU   A 1 1162 ? -51.20100  64.16100  0.85000   1.000 56.25187  ?  1160 GLU   A CG  1 
ATOM   9226  C  CD  . GLU   A 1 1162 ? -52.27200  64.97000  0.14700   1.000 62.61738  ?  1160 GLU   A CD  1 
ATOM   9227  O  OE1 . GLU   A 1 1162 ? -52.51300  66.12500  0.55800   1.000 52.53740  ?  1160 GLU   A OE1 1 
ATOM   9228  O  OE2 . GLU   A 1 1162 ? -52.86500  64.45200  -0.82300  1.000 62.48711  -1 1160 GLU   A OE2 1 
ATOM   9229  N  N   . TYR   A 1 1163 ? -48.87900  61.66700  1.78000   1.000 28.23736  ?  1161 TYR   A N   1 
ATOM   9230  C  CA  . TYR   A 1 1163 ? -48.61800  60.30300  1.35200   1.000 42.88508  ?  1161 TYR   A CA  1 
ATOM   9231  C  C   . TYR   A 1 1163 ? -49.76500  59.38800  1.74300   1.000 44.66764  ?  1161 TYR   A C   1 
ATOM   9232  O  O   . TYR   A 1 1163 ? -50.43400  59.59500  2.75700   1.000 30.42939  ?  1161 TYR   A O   1 
ATOM   9233  C  CB  . TYR   A 1 1163 ? -47.31300  59.77100  1.95000   1.000 32.60959  ?  1161 TYR   A CB  1 
ATOM   9234  C  CG  . TYR   A 1 1163 ? -47.27500  59.75800  3.46500   1.000 38.72746  ?  1161 TYR   A CG  1 
ATOM   9235  C  CD1 . TYR   A 1 1163 ? -46.89400  60.88700  4.18000   1.000 40.89569  ?  1161 TYR   A CD1 1 
ATOM   9236  C  CD2 . TYR   A 1 1163 ? -47.59600  58.61000  4.18000   1.000 34.82145  ?  1161 TYR   A CD2 1 
ATOM   9237  C  CE1 . TYR   A 1 1163 ? -46.84800  60.87800  5.56400   1.000 35.15076  ?  1161 TYR   A CE1 1 
ATOM   9238  C  CE2 . TYR   A 1 1163 ? -47.55100  58.59100  5.56400   1.000 32.92187  ?  1161 TYR   A CE2 1 
ATOM   9239  C  CZ  . TYR   A 1 1163 ? -47.17600  59.72700  6.25000   1.000 38.26478  ?  1161 TYR   A CZ  1 
ATOM   9240  O  OH  . TYR   A 1 1163 ? -47.13000  59.71500  7.62600   1.000 34.20717  ?  1161 TYR   A OH  1 
ATOM   9241  N  N   . ASN   A 1 1164 ? -49.97000  58.36200  0.92200   1.000 36.71025  ?  1162 ASN   A N   1 
ATOM   9242  C  CA  . ASN   A 1 1164 ? -50.95100  57.32500  1.20700   1.000 31.82564  ?  1162 ASN   A CA  1 
ATOM   9243  C  C   . ASN   A 1 1164 ? -50.46600  56.46500  2.37000   1.000 41.87445  ?  1162 ASN   A C   1 
ATOM   9244  O  O   . ASN   A 1 1164 ? -49.38600  55.86800  2.30000   1.000 55.53066  ?  1162 ASN   A O   1 
ATOM   9245  C  CB  . ASN   A 1 1164 ? -51.17000  56.47600  -0.04100  1.000 43.11555  ?  1162 ASN   A CB  1 
ATOM   9246  C  CG  . ASN   A 1 1164 ? -52.43700  55.66500  0.02100   1.000 41.21885  ?  1162 ASN   A CG  1 
ATOM   9247  O  OD1 . ASN   A 1 1164 ? -52.80200  55.13300  1.06900   1.000 52.80068  ?  1162 ASN   A OD1 1 
ATOM   9248  N  ND2 . ASN   A 1 1164 ? -53.12700  55.56500  -1.10900  1.000 42.78168  ?  1162 ASN   A ND2 1 
ATOM   9249  N  N   . THR   A 1 1165 ? -51.26300  56.39700  3.43800   1.000 44.33121  ?  1163 THR   A N   1 
ATOM   9250  C  CA  . THR   A 1 1165 ? -50.85900  55.63700  4.61600   1.000 42.83342  ?  1163 THR   A CA  1 
ATOM   9251  C  C   . THR   A 1 1165 ? -50.87800  54.13200  4.37800   1.000 45.26754  ?  1163 THR   A C   1 
ATOM   9252  O  O   . THR   A 1 1165 ? -50.23100  53.39200  5.12700   1.000 52.90838  ?  1163 THR   A O   1 
ATOM   9253  C  CB  . THR   A 1 1165 ? -51.75700  55.98600  5.80400   1.000 45.77330  ?  1163 THR   A CB  1 
ATOM   9254  O  OG1 . THR   A 1 1165 ? -53.11600  56.10300  5.36300   1.000 49.39941  ?  1163 THR   A OG1 1 
ATOM   9255  C  CG2 . THR   A 1 1165 ? -51.31400  57.29600  6.43600   1.000 41.08027  ?  1163 THR   A CG2 1 
ATOM   9256  N  N   . HIS   A 1 1166 ? -51.60200  53.66200  3.36200   1.000 43.76869  ?  1164 HIS   A N   1 
ATOM   9257  C  CA  . HIS   A 1 1166 ? -51.59300  52.24200  3.03500   1.000 41.57640  ?  1164 HIS   A CA  1 
ATOM   9258  C  C   . HIS   A 1 1166 ? -50.34900  51.83000  2.26100   1.000 43.37789  ?  1164 HIS   A C   1 
ATOM   9259  O  O   . HIS   A 1 1166 ? -50.00100  50.64500  2.26500   1.000 48.94915  ?  1164 HIS   A O   1 
ATOM   9260  C  CB  . HIS   A 1 1166 ? -52.83700  51.87200  2.22500   1.000 37.59625  ?  1164 HIS   A CB  1 
ATOM   9261  C  CG  . HIS   A 1 1166 ? -54.12300  52.09500  2.95600   1.000 55.51284  ?  1164 HIS   A CG  1 
ATOM   9262  N  ND1 . HIS   A 1 1166 ? -54.95400  51.06200  3.33400   1.000 53.10216  ?  1164 HIS   A ND1 1 
ATOM   9263  C  CD2 . HIS   A 1 1166 ? -54.72100  53.23300  3.38200   1.000 64.62187  ?  1164 HIS   A CD2 1 
ATOM   9264  C  CE1 . HIS   A 1 1166 ? -56.00900  51.55500  3.95800   1.000 58.29009  ?  1164 HIS   A CE1 1 
ATOM   9265  N  NE2 . HIS   A 1 1166 ? -55.89200  52.87000  4.00100   1.000 51.18651  ?  1164 HIS   A NE2 1 
ATOM   9266  N  N   . LEU   A 1 1167 ? -49.67600  52.77600  1.60300   1.000 43.48662  ?  1165 LEU   A N   1 
ATOM   9267  C  CA  . LEU   A 1 1167 ? -48.48800  52.48500  0.81300   1.000 42.99735  ?  1165 LEU   A CA  1 
ATOM   9268  C  C   . LEU   A 1 1167 ? -47.18700  52.88500  1.49800   1.000 38.21010  ?  1165 LEU   A C   1 
ATOM   9269  O  O   . LEU   A 1 1167 ? -46.13100  52.35400  1.13800   1.000 44.74979  ?  1165 LEU   A O   1 
ATOM   9270  C  CB  . LEU   A 1 1167 ? -48.57400  53.19400  -0.54500  1.000 47.28282  ?  1165 LEU   A CB  1 
ATOM   9271  C  CG  . LEU   A 1 1167 ? -49.72800  52.74700  -1.44300  1.000 47.88026  ?  1165 LEU   A CG  1 
ATOM   9272  C  CD1 . LEU   A 1 1167 ? -50.07600  53.82100  -2.46200  1.000 60.25901  ?  1165 LEU   A CD1 1 
ATOM   9273  C  CD2 . LEU   A 1 1167 ? -49.39400  51.43400  -2.14100  1.000 60.09387  ?  1165 LEU   A CD2 1 
ATOM   9274  N  N   . PHE   A 1 1168 ? -47.23300  53.80600  2.46100   1.000 40.08264  ?  1166 PHE   A N   1 
ATOM   9275  C  CA  . PHE   A 1 1168 ? -46.04900  54.28400  3.16300   1.000 39.91692  ?  1166 PHE   A CA  1 
ATOM   9276  C  C   . PHE   A 1 1168 ? -46.30800  54.29100  4.66200   1.000 42.78882  ?  1166 PHE   A C   1 
ATOM   9277  O  O   . PHE   A 1 1168 ? -47.41000  54.61900  5.10800   1.000 36.95542  ?  1166 PHE   A O   1 
ATOM   9278  C  CB  . PHE   A 1 1168 ? -45.65700  55.70300  2.70300   1.000 29.91653  ?  1166 PHE   A CB  1 
ATOM   9279  C  CG  . PHE   A 1 1168 ? -45.40600  55.82000  1.22500   1.000 38.88832  ?  1166 PHE   A CG  1 
ATOM   9280  C  CD1 . PHE   A 1 1168 ? -44.19800  55.41400  0.67800   1.000 42.11789  ?  1166 PHE   A CD1 1 
ATOM   9281  C  CD2 . PHE   A 1 1168 ? -46.37400  56.34300  0.38300   1.000 45.19124  ?  1166 PHE   A CD2 1 
ATOM   9282  C  CE1 . PHE   A 1 1168 ? -43.96500  55.51900  -0.68100  1.000 38.85871  ?  1166 PHE   A CE1 1 
ATOM   9283  C  CE2 . PHE   A 1 1168 ? -46.14600  56.45200  -0.97800  1.000 42.44814  ?  1166 PHE   A CE2 1 
ATOM   9284  C  CZ  . PHE   A 1 1168 ? -44.94000  56.04000  -1.50900  1.000 35.46983  ?  1166 PHE   A CZ  1 
ATOM   9285  N  N   . ASP   A 1 1169 ? -45.28900  53.93000  5.43400   1.000 56.62772  ?  1167 ASP   A N   1 
ATOM   9286  C  CA  . ASP   A 1 1169 ? -45.31600  54.04500  6.88500   1.000 43.17436  ?  1167 ASP   A CA  1 
ATOM   9287  C  C   . ASP   A 1 1169 ? -44.70700  55.38200  7.29900   1.000 51.07185  ?  1167 ASP   A C   1 
ATOM   9288  O  O   . ASP   A 1 1169 ? -44.13600  56.11700  6.48500   1.000 57.12494  ?  1167 ASP   A O   1 
ATOM   9289  C  CB  . ASP   A 1 1169 ? -44.55500  52.88500  7.54600   1.000 57.36822  ?  1167 ASP   A CB  1 
ATOM   9290  C  CG  . ASP   A 1 1169 ? -44.91400  51.53600  6.95400   1.000 80.58917  ?  1167 ASP   A CG  1 
ATOM   9291  O  OD1 . ASP   A 1 1169 ? -44.67300  51.36500  5.72500   1.000 79.70770  ?  1167 ASP   A OD1 1 
ATOM   9292  O  OD2 . ASP   A 1 1169 ? -45.42700  50.67700  7.71400   1.000 100.99811 -1 1167 ASP   A OD2 1 
ATOM   9293  N  N   . GLU   A 1 1170 ? -44.83600  55.69700  8.58900   1.000 41.17934  ?  1168 GLU   A N   1 
ATOM   9294  C  CA  . GLU   A 1 1170 ? -44.20500  56.90700  9.10000   1.000 60.39634  ?  1168 GLU   A CA  1 
ATOM   9295  C  C   . GLU   A 1 1170 ? -42.68600  56.82100  8.98500   1.000 63.66332  ?  1168 GLU   A C   1 
ATOM   9296  O  O   . GLU   A 1 1170 ? -42.03000  57.81400  8.65800   1.000 55.59435  ?  1168 GLU   A O   1 
ATOM   9297  C  CB  . GLU   A 1 1170 ? -44.62700  57.15500  10.54800  1.000 48.35708  ?  1168 GLU   A CB  1 
ATOM   9298  C  CG  . GLU   A 1 1170 ? -44.41700  58.59700  10.99500  1.000 83.85504  ?  1168 GLU   A CG  1 
ATOM   9299  C  CD  . GLU   A 1 1170 ? -44.52600  58.77600  12.49800  1.000 100.49353 ?  1168 GLU   A CD  1 
ATOM   9300  O  OE1 . GLU   A 1 1170 ? -45.48800  58.25200  13.09900  1.000 93.78415  ?  1168 GLU   A OE1 1 
ATOM   9301  O  OE2 . GLU   A 1 1170 ? -43.63800  59.43500  13.08000  1.000 80.61908  -1 1168 GLU   A OE2 1 
ATOM   9302  N  N   . GLY   A 1 1171 ? -42.11000  55.64200  9.23200   1.000 50.40803  ?  1169 GLY   A N   1 
ATOM   9303  C  CA  . GLY   A 1 1171 ? -40.66600  55.49800  9.10800   1.000 59.27460  ?  1169 GLY   A CA  1 
ATOM   9304  C  C   . GLY   A 1 1171 ? -40.19700  55.54500  7.66700   1.000 58.01212  ?  1169 GLY   A C   1 
ATOM   9305  O  O   . GLY   A 1 1171 ? -39.10600  56.04600  7.37400   1.000 48.79430  ?  1169 GLY   A O   1 
ATOM   9306  N  N   . MET   A 1 1172 ? -41.00900  55.01800  6.74800   1.000 53.34813  ?  1170 MET   A N   1 
ATOM   9307  C  CA  . MET   A 1 1172 ? -40.66200  55.08500  5.33300   1.000 43.54064  ?  1170 MET   A CA  1 
ATOM   9308  C  C   . MET   A 1 1172 ? -40.62200  56.52600  4.85000   1.000 45.43929  ?  1170 MET   A C   1 
ATOM   9309  O  O   . MET   A 1 1172 ? -39.71200  56.92000  4.11100   1.000 47.10910  ?  1170 MET   A O   1 
ATOM   9310  C  CB  . MET   A 1 1172 ? -41.66000  54.28200  4.50400   1.000 40.20364  ?  1170 MET   A CB  1 
ATOM   9311  C  CG  . MET   A 1 1172 ? -41.77500  52.82600  4.90900   1.000 49.74016  ?  1170 MET   A CG  1 
ATOM   9312  S  SD  . MET   A 1 1172 ? -42.61500  51.86000  3.63300   1.000 50.15875  ?  1170 MET   A SD  1 
ATOM   9313  C  CE  . MET   A 1 1172 ? -42.05100  52.66900  2.14800   1.000 60.23619  ?  1170 MET   A CE  1 
ATOM   9314  N  N   . ILE   A 1 1173 ? -41.60700  57.32700  5.25600   1.000 41.51884  ?  1171 ILE   A N   1 
ATOM   9315  C  CA  . ILE   A 1 1173 ? -41.64000  58.73000  4.86600   1.000 38.64382  ?  1171 ILE   A CA  1 
ATOM   9316  C  C   . ILE   A 1 1173 ? -40.49700  59.49200  5.52000   1.000 40.91692  ?  1171 ILE   A C   1 
ATOM   9317  O  O   . ILE   A 1 1173 ? -39.83200  60.31100  4.87400   1.000 45.99797  ?  1171 ILE   A O   1 
ATOM   9318  C  CB  . ILE   A 1 1173 ? -43.00500  59.34400  5.21900   1.000 38.36663  ?  1171 ILE   A CB  1 
ATOM   9319  C  CG1 . ILE   A 1 1173 ? -44.11800  58.63600  4.45300   1.000 40.86192  ?  1171 ILE   A CG1 1 
ATOM   9320  C  CG2 . ILE   A 1 1173 ? -43.01300  60.82800  4.89800   1.000 40.00727  ?  1171 ILE   A CG2 1 
ATOM   9321  C  CD1 . ILE   A 1 1173 ? -44.07900  58.91600  2.97800   1.000 36.30809  ?  1171 ILE   A CD1 1 
ATOM   9322  N  N   . LEU   A 1 1174 ? -40.24900  59.23600  6.80900   1.000 48.75956  ?  1172 LEU   A N   1 
ATOM   9323  C  CA  . LEU   A 1 1174 ? -39.16400  59.91800  7.50900   1.000 46.80433  ?  1172 LEU   A CA  1 
ATOM   9324  C  C   . LEU   A 1 1174 ? -37.82100  59.68300  6.83300   1.000 38.35401  ?  1172 LEU   A C   1 
ATOM   9325  O  O   . LEU   A 1 1174 ? -36.96000  60.57000  6.84300   1.000 49.45761  ?  1172 LEU   A O   1 
ATOM   9326  C  CB  . LEU   A 1 1174 ? -39.11400  59.46500  8.96800   1.000 41.99088  ?  1172 LEU   A CB  1 
ATOM   9327  C  CG  . LEU   A 1 1174 ? -40.19100  60.04800  9.88600   1.000 54.90882  ?  1172 LEU   A CG  1 
ATOM   9328  C  CD1 . LEU   A 1 1174 ? -40.40600  59.16400  11.10500  1.000 64.05427  ?  1172 LEU   A CD1 1 
ATOM   9329  C  CD2 . LEU   A 1 1174 ? -39.82400  61.46200  10.30800  1.000 60.78886  ?  1172 LEU   A CD2 1 
ATOM   9330  N  N   . ARG   A 1 1175 ? -37.62000  58.50300  6.24000   1.000 34.50651  ?  1173 ARG   A N   1 
ATOM   9331  C  CA  . ARG   A 1 1175 ? -36.40200  58.27100  5.47100   1.000 38.64269  ?  1173 ARG   A CA  1 
ATOM   9332  C  C   . ARG   A 1 1175 ? -36.40600  59.08000  4.18200   1.000 38.25753  ?  1173 ARG   A C   1 
ATOM   9333  O  O   . ARG   A 1 1175 ? -35.36800  59.61000  3.77200   1.000 46.93542  ?  1173 ARG   A O   1 
ATOM   9334  C  CB  . ARG   A 1 1175 ? -36.24000  56.78300  5.15900   1.000 52.42381  ?  1173 ARG   A CB  1 
ATOM   9335  C  CG  . ARG   A 1 1175 ? -36.06600  55.89200  6.37800   1.000 72.57657  ?  1173 ARG   A CG  1 
ATOM   9336  C  CD  . ARG   A 1 1175 ? -35.44800  54.55300  5.99800   1.000 54.56634  ?  1173 ARG   A CD  1 
ATOM   9337  N  NE  . ARG   A 1 1175 ? -36.14200  53.92400  4.88100   1.000 57.43264  ?  1173 ARG   A NE  1 
ATOM   9338  C  CZ  . ARG   A 1 1175 ? -37.15700  53.08000  5.01000   1.000 68.71183  ?  1173 ARG   A CZ  1 
ATOM   9339  N  NH1 . ARG   A 1 1175 ? -37.62500  52.73800  6.19900   1.000 54.97164  ?  1173 ARG   A NH1 1 
ATOM   9340  N  NH2 . ARG   A 1 1175 ? -37.71700  52.56800  3.91700   1.000 64.65990  ?  1173 ARG   A NH2 1 
ATOM   9341  N  N   . MET   A 1 1176 ? -37.56800  59.19600  3.53600   1.000 36.16435  ?  1174 MET   A N   1 
ATOM   9342  C  CA  . MET   A 1 1176 ? -37.62900  59.85300  2.23600   1.000 27.30934  ?  1174 MET   A CA  1 
ATOM   9343  C  C   . MET   A 1 1176 ? -37.46200  61.36300  2.35700   1.000 35.65394  ?  1174 MET   A C   1 
ATOM   9344  O  O   . MET   A 1 1176 ? -36.79800  61.98500  1.51900   1.000 37.66756  ?  1174 MET   A O   1 
ATOM   9345  C  CB  . MET   A 1 1176 ? -38.94200  59.50000  1.54200   1.000 26.95514  ?  1174 MET   A CB  1 
ATOM   9346  C  CG  . MET   A 1 1176 ? -38.91900  58.13900  0.85400   1.000 38.36163  ?  1174 MET   A CG  1 
ATOM   9347  S  SD  . MET   A 1 1176 ? -40.55900  57.40800  0.71900   1.000 37.08925  ?  1174 MET   A SD  1 
ATOM   9348  C  CE  . MET   A 1 1176 ? -41.54500  58.89100  0.55800   1.000 36.31280  ?  1174 MET   A CE  1 
ATOM   9349  N  N   . VAL   A 1 1177 ? -38.04900  61.97600  3.38900   1.000 39.90961  ?  1175 VAL   A N   1 
ATOM   9350  C  CA  . VAL   A 1 1177 ? -37.85300  63.41200  3.56600   1.000 52.34969  ?  1175 VAL   A CA  1 
ATOM   9351  C  C   . VAL   A 1 1177 ? -36.40800  63.70500  3.94700   1.000 49.82111  ?  1175 VAL   A C   1 
ATOM   9352  O  O   . VAL   A 1 1177 ? -35.88700  64.78700  3.65000   1.000 54.70467  ?  1175 VAL   A O   1 
ATOM   9353  C  CB  . VAL   A 1 1177 ? -38.84400  63.98500  4.60100   1.000 29.63246  ?  1175 VAL   A CB  1 
ATOM   9354  C  CG1 . VAL   A 1 1177 ? -40.24000  63.43400  4.36200   1.000 39.63644  ?  1175 VAL   A CG1 1 
ATOM   9355  C  CG2 . VAL   A 1 1177 ? -38.38100  63.70700  6.02600   1.000 54.61786  ?  1175 VAL   A CG2 1 
ATOM   9356  N  N   . ALA   A 1 1178 ? -35.73200  62.75100  4.59200   1.000 47.86211  ?  1176 ALA   A N   1 
ATOM   9357  C  CA  . ALA   A 1 1178 ? -34.31700  62.92000  4.89600   1.000 43.86413  ?  1176 ALA   A CA  1 
ATOM   9358  C  C   . ALA   A 1 1178 ? -33.45000  62.68800  3.66900   1.000 41.90430  ?  1176 ALA   A C   1 
ATOM   9359  O  O   . ALA   A 1 1178 ? -32.36100  63.26400  3.56500   1.000 48.09261  ?  1176 ALA   A O   1 
ATOM   9360  C  CB  . ALA   A 1 1178 ? -33.90300  61.97400  6.02300   1.000 44.32033  ?  1176 ALA   A CB  1 
ATOM   9361  N  N   . GLN   A 1 1179 ? -33.91300  61.85400  2.73600   1.000 40.36446  ?  1177 GLN   A N   1 
ATOM   9362  C  CA  . GLN   A 1 1179 ? -33.18200  61.66100  1.49000   1.000 33.23105  ?  1177 GLN   A CA  1 
ATOM   9363  C  C   . GLN   A 1 1179 ? -33.35200  62.84900  0.55600   1.000 41.34314  ?  1177 GLN   A C   1 
ATOM   9364  O  O   . GLN   A 1 1179 ? -32.42000  63.19600  -0.17800  1.000 45.74288  ?  1177 GLN   A O   1 
ATOM   9365  C  CB  . GLN   A 1 1179 ? -33.64000  60.37300  0.80700   1.000 39.23652  ?  1177 GLN   A CB  1 
ATOM   9366  C  CG  . GLN   A 1 1179 ? -33.24500  59.10700  1.54700   1.000 45.64247  ?  1177 GLN   A CG  1 
ATOM   9367  C  CD  . GLN   A 1 1179 ? -33.98100  57.88300  1.04000   1.000 42.07789  ?  1177 GLN   A CD  1 
ATOM   9368  O  OE1 . GLN   A 1 1179 ? -34.79900  57.97300  0.12400   1.000 42.12534  ?  1177 GLN   A OE1 1 
ATOM   9369  N  NE2 . GLN   A 1 1179 ? -33.69800  56.73100  1.63700   1.000 50.86626  ?  1177 GLN   A NE2 1 
ATOM   9370  N  N   . PHE   A 1 1180 ? -34.52700  63.48200  0.56800   1.000 49.57569  ?  1178 PHE   A N   1 
ATOM   9371  C  CA  . PHE   A 1 1180 ? -34.73300  64.66600  -0.25800  1.000 47.29870  ?  1178 PHE   A CA  1 
ATOM   9372  C  C   . PHE   A 1 1180 ? -33.84900  65.81600  0.20600   1.000 43.65011  ?  1178 PHE   A C   1 
ATOM   9373  O  O   . PHE   A 1 1180 ? -33.25300  66.52200  -0.61700  1.000 37.89005  ?  1178 PHE   A O   1 
ATOM   9374  C  CB  . PHE   A 1 1180 ? -36.20500  65.07700  -0.23500  1.000 36.43453  ?  1178 PHE   A CB  1 
ATOM   9375  C  CG  . PHE   A 1 1180 ? -36.53600  66.19300  -1.18100  1.000 33.52407  ?  1178 PHE   A CG  1 
ATOM   9376  C  CD1 . PHE   A 1 1180 ? -36.73400  65.93800  -2.52800  1.000 32.80115  ?  1178 PHE   A CD1 1 
ATOM   9377  C  CD2 . PHE   A 1 1180 ? -36.65200  67.49600  -0.72600  1.000 30.25868  ?  1178 PHE   A CD2 1 
ATOM   9378  C  CE1 . PHE   A 1 1180 ? -37.03800  66.96200  -3.40400  1.000 34.58501  ?  1178 PHE   A CE1 1 
ATOM   9379  C  CE2 . PHE   A 1 1180 ? -36.95600  68.52400  -1.59800  1.000 31.58263  ?  1178 PHE   A CE2 1 
ATOM   9380  C  CZ  . PHE   A 1 1180 ? -37.15000  68.25600  -2.93900  1.000 41.81656  ?  1178 PHE   A CZ  1 
ATOM   9381  N  N   . GLU   A 1 1181 ? -33.75200  66.01600  1.52200   1.000 34.34319  ?  1179 GLU   A N   1 
ATOM   9382  C  CA  . GLU   A 1 1181 ? -32.83400  67.01600  2.05600   1.000 33.90728  ?  1179 GLU   A CA  1 
ATOM   9383  C  C   . GLU   A 1 1181 ? -31.39600  66.69000  1.67800   1.000 43.50793  ?  1179 GLU   A C   1 
ATOM   9384  O  O   . GLU   A 1 1181 ? -30.60900  67.59000  1.36000   1.000 38.28725  ?  1179 GLU   A O   1 
ATOM   9385  C  CB  . GLU   A 1 1181 ? -32.98500  67.10400  3.57500   1.000 35.44883  ?  1179 GLU   A CB  1 
ATOM   9386  C  CG  . GLU   A 1 1181 ? -31.99200  68.03800  4.24900   1.000 43.54896  ?  1179 GLU   A CG  1 
ATOM   9387  C  CD  . GLU   A 1 1181 ? -32.15200  68.07100  5.75500   1.000 47.06141  ?  1179 GLU   A CD  1 
ATOM   9388  O  OE1 . GLU   A 1 1181 ? -32.39800  67.00200  6.35300   1.000 50.10656  ?  1179 GLU   A OE1 1 
ATOM   9389  O  OE2 . GLU   A 1 1181 ? -32.03900  69.16900  6.34100   1.000 53.60465  -1 1179 GLU   A OE2 1 
ATOM   9390  N  N   . HIS   A 1 1182 ? -31.03800  65.40500  1.69900   1.000 36.77657  ?  1180 HIS   A N   1 
ATOM   9391  C  CA  . HIS   A 1 1182 ? -29.68200  65.00000  1.34800   1.000 25.64479  ?  1180 HIS   A CA  1 
ATOM   9392  C  C   . HIS   A 1 1182 ? -29.35900  65.37300  -0.09300  1.000 34.85144  ?  1180 HIS   A C   1 
ATOM   9393  O  O   . HIS   A 1 1182 ? -28.28100  65.90400  -0.38300  1.000 47.35734  ?  1180 HIS   A O   1 
ATOM   9394  C  CB  . HIS   A 1 1182 ? -29.51700  63.49700  1.57300   1.000 40.83266  ?  1180 HIS   A CB  1 
ATOM   9395  C  CG  . HIS   A 1 1182 ? -28.09100  63.04500  1.63200   1.000 50.78015  ?  1180 HIS   A CG  1 
ATOM   9396  N  ND1 . HIS   A 1 1182 ? -27.10700  63.76900  2.26800   1.000 49.91698  ?  1180 HIS   A ND1 1 
ATOM   9397  C  CD2 . HIS   A 1 1182 ? -27.48700  61.93600  1.14400   1.000 46.90840  ?  1180 HIS   A CD2 1 
ATOM   9398  C  CE1 . HIS   A 1 1182 ? -25.95600  63.13000  2.16400   1.000 50.35101  ?  1180 HIS   A CE1 1 
ATOM   9399  N  NE2 . HIS   A 1 1182 ? -26.15900  62.01400  1.48700   1.000 50.02041  ?  1180 HIS   A NE2 1 
ATOM   9400  N  N   . LEU   A 1 1183 ? -30.29100  65.10900  -1.01100  1.000 37.19772  ?  1181 LEU   A N   1 
ATOM   9401  C  CA  . LEU   A 1 1183 ? -30.07200  65.46500  -2.40900  1.000 35.90823  ?  1181 LEU   A CA  1 
ATOM   9402  C  C   . LEU   A 1 1183 ? -30.11300  66.97300  -2.61100  1.000 48.36402  ?  1181 LEU   A C   1 
ATOM   9403  O  O   . LEU   A 1 1183 ? -29.32600  67.52000  -3.39200  1.000 53.49683  ?  1181 LEU   A O   1 
ATOM   9404  C  CB  . LEU   A 1 1183 ? -31.11200  64.78200  -3.29400  1.000 32.54089  ?  1181 LEU   A CB  1 
ATOM   9405  C  CG  . LEU   A 1 1183 ? -30.84000  63.32700  -3.67200  1.000 37.50193  ?  1181 LEU   A CG  1 
ATOM   9406  C  CD1 . LEU   A 1 1183 ? -32.05200  62.73500  -4.35500  1.000 53.17042  ?  1181 LEU   A CD1 1 
ATOM   9407  C  CD2 . LEU   A 1 1183 ? -29.63000  63.24100  -4.57900  1.000 35.61714  ?  1181 LEU   A CD2 1 
ATOM   9408  N  N   . LEU   A 1 1184 ? -31.02500  67.66000  -1.91900  1.000 40.69276  ?  1182 LEU   A N   1 
ATOM   9409  C  CA  . LEU   A 1 1184 ? -31.15600  69.10400  -2.09100  1.000 42.61000  ?  1182 LEU   A CA  1 
ATOM   9410  C  C   . LEU   A 1 1184 ? -29.87400  69.82200  -1.68700  1.000 38.66555  ?  1182 LEU   A C   1 
ATOM   9411  O  O   . LEU   A 1 1184 ? -29.39400  70.71100  -2.40100  1.000 41.45907  ?  1182 LEU   A O   1 
ATOM   9412  C  CB  . LEU   A 1 1184 ? -32.34900  69.61800  -1.28400  1.000 43.81053  ?  1182 LEU   A CB  1 
ATOM   9413  C  CG  . LEU   A 1 1184 ? -32.68700  71.10600  -1.40100  1.000 35.28535  ?  1182 LEU   A CG  1 
ATOM   9414  C  CD1 . LEU   A 1 1184 ? -34.19100  71.29600  -1.45600  1.000 32.52298  ?  1182 LEU   A CD1 1 
ATOM   9415  C  CD2 . LEU   A 1 1184 ? -32.09900  71.88500  -0.23600  1.000 29.98508  ?  1182 LEU   A CD2 1 
ATOM   9416  N  N   . LEU   A 1 1185 ? -29.30100  69.44600  -0.54300  1.000 39.43443  ?  1183 LEU   A N   1 
ATOM   9417  C  CA  . LEU   A 1 1185 ? -28.05100  70.06100  -0.11200  1.000 37.27157  ?  1183 LEU   A CA  1 
ATOM   9418  C  C   . LEU   A 1 1185 ? -26.88900  69.62300  -0.99600  1.000 45.81892  ?  1183 LEU   A C   1 
ATOM   9419  O  O   . LEU   A 1 1185 ? -25.97700  70.41200  -1.26900  1.000 53.01498  ?  1183 LEU   A O   1 
ATOM   9420  C  CB  . LEU   A 1 1185 ? -27.78200  69.72100  1.35300   1.000 23.57928  ?  1183 LEU   A CB  1 
ATOM   9421  C  CG  . LEU   A 1 1185 ? -28.89100  70.13400  2.32500   1.000 23.41299  ?  1183 LEU   A CG  1 
ATOM   9422  C  CD1 . LEU   A 1 1185 ? -28.57600  69.67400  3.73900   1.000 44.00807  ?  1183 LEU   A CD1 1 
ATOM   9423  C  CD2 . LEU   A 1 1185 ? -29.12100  71.63800  2.28600   1.000 35.70397  ?  1183 LEU   A CD2 1 
ATOM   9424  N  N   . GLN   A 1 1186 ? -26.90700  68.37000  -1.45900  1.000 44.17720  ?  1184 GLN   A N   1 
ATOM   9425  C  CA  . GLN   A 1 1186 ? -25.86700  67.90500  -2.37200  1.000 45.81393  ?  1184 GLN   A CA  1 
ATOM   9426  C  C   . GLN   A 1 1186 ? -25.92600  68.64600  -3.70100  1.000 50.37629  ?  1184 GLN   A C   1 
ATOM   9427  O  O   . GLN   A 1 1186 ? -24.88600  68.95100  -4.29800  1.000 61.37803  ?  1184 GLN   A O   1 
ATOM   9428  C  CB  . GLN   A 1 1186 ? -25.99900  66.40000  -2.60600  1.000 31.87815  ?  1184 GLN   A CB  1 
ATOM   9429  C  CG  . GLN   A 1 1186 ? -25.21700  65.53500  -1.64000  1.000 32.08697  ?  1184 GLN   A CG  1 
ATOM   9430  C  CD  . GLN   A 1 1186 ? -25.39400  64.05700  -1.92300  1.000 42.17083  ?  1184 GLN   A CD  1 
ATOM   9431  O  OE1 . GLN   A 1 1186 ? -24.57400  63.43800  -2.60200  1.000 52.66557  ?  1184 GLN   A OE1 1 
ATOM   9432  N  NE2 . GLN   A 1 1186 ? -26.47400  63.48300  -1.40500  1.000 40.49669  ?  1184 GLN   A NE2 1 
ATOM   9433  N  N   . ALA   A 1 1187 ? -27.13400  68.94200  -4.18200  1.000 44.33864  ?  1185 ALA   A N   1 
ATOM   9434  C  CA  . ALA   A 1 1187 ? -27.28800  69.54300  -5.50100  1.000 45.97282  ?  1185 ALA   A CA  1 
ATOM   9435  C  C   . ALA   A 1 1187 ? -26.93000  71.02300  -5.48700  1.000 45.19797  ?  1185 ALA   A C   1 
ATOM   9436  O  O   . ALA   A 1 1187 ? -26.16000  71.49100  -6.33300  1.000 48.98931  ?  1185 ALA   A O   1 
ATOM   9437  C  CB  . ALA   A 1 1187 ? -28.71800  69.34500  -6.00600  1.000 38.40185  ?  1185 ALA   A CB  1 
ATOM   9438  N  N   . VAL   A 1 1188 ? -27.48200  71.77600  -4.53300  1.000 45.32387  ?  1186 VAL   A N   1 
ATOM   9439  C  CA  . VAL   A 1 1188 ? -27.23200  73.21000  -4.47600  1.000 52.65538  ?  1186 VAL   A CA  1 
ATOM   9440  C  C   . VAL   A 1 1188 ? -25.75900  73.50700  -4.22800  1.000 57.75771  ?  1186 VAL   A C   1 
ATOM   9441  O  O   . VAL   A 1 1188 ? -25.28400  74.60000  -4.55500  1.000 61.41192  ?  1186 VAL   A O   1 
ATOM   9442  C  CB  . VAL   A 1 1188 ? -28.13200  73.86000  -3.40100  1.000 42.69776  ?  1186 VAL   A CB  1 
ATOM   9443  C  CG1 . VAL   A 1 1188 ? -27.63200  73.52400  -2.00300  1.000 45.42381  ?  1186 VAL   A CG1 1 
ATOM   9444  C  CG2 . VAL   A 1 1188 ? -28.22100  75.36300  -3.61300  1.000 43.96543  ?  1186 VAL   A CG2 1 
ATOM   9445  N  N   . HIS   A 1 1189 ? -25.01600  72.55000  -3.67100  1.000 53.81775  ?  1187 HIS   A N   1 
ATOM   9446  C  CA  . HIS   A 1 1189 ? -23.57600  72.67800  -3.49700  1.000 47.83766  ?  1187 HIS   A CA  1 
ATOM   9447  C  C   . HIS   A 1 1189 ? -22.78300  71.84300  -4.49200  1.000 51.41526  ?  1187 HIS   A C   1 
ATOM   9448  O  O   . HIS   A 1 1189 ? -21.55200  71.79800  -4.39800  1.000 65.08619  ?  1187 HIS   A O   1 
ATOM   9449  C  CB  . HIS   A 1 1189 ? -23.17900  72.29500  -2.06700  1.000 31.76016  ?  1187 HIS   A CB  1 
ATOM   9450  C  CG  . HIS   A 1 1189 ? -23.80700  73.15300  -1.01400  1.000 56.67627  ?  1187 HIS   A CG  1 
ATOM   9451  N  ND1 . HIS   A 1 1189 ? -23.64200  74.52100  -0.97200  1.000 67.84747  ?  1187 HIS   A ND1 1 
ATOM   9452  C  CD2 . HIS   A 1 1189 ? -24.59700  72.83700  0.04100   1.000 55.71318  ?  1187 HIS   A CD2 1 
ATOM   9453  C  CE1 . HIS   A 1 1189 ? -24.30600  75.01100  0.06000   1.000 74.34584  ?  1187 HIS   A CE1 1 
ATOM   9454  N  NE2 . HIS   A 1 1189 ? -24.89300  74.01100  0.69100   1.000 45.55894  ?  1187 HIS   A NE2 1 
ATOM   9455  N  N   . GLY   A 1 1190 ? -23.44900  71.18200  -5.43700  1.000 41.81414  ?  1188 GLY   A N   1 
ATOM   9456  C  CA  . GLY   A 1 1190 ? -22.77000  70.39100  -6.44600  1.000 49.01545  ?  1188 GLY   A CA  1 
ATOM   9457  C  C   . GLY   A 1 1190 ? -23.38300  70.55600  -7.82100  1.000 47.77146  ?  1188 GLY   A C   1 
ATOM   9458  O  O   . GLY   A 1 1190 ? -23.95500  69.61200  -8.37500  1.000 47.21109  ?  1188 GLY   A O   1 
ATOM   9459  N  N   . LEU   A 1 1191 ? -23.25800  71.75600  -8.38900  1.000 42.75782  ?  1189 LEU   A N   1 
ATOM   9460  C  CA  . LEU   A 1 1191 ? -23.94800  72.07400  -9.63500  1.000 33.37064  ?  1189 LEU   A CA  1 
ATOM   9461  C  C   . LEU   A 1 1191 ? -23.23900  71.48900  -10.84900 1.000 46.02860  ?  1189 LEU   A C   1 
ATOM   9462  O  O   . LEU   A 1 1191 ? -23.89300  70.97000  -11.76100 1.000 48.98359  ?  1189 LEU   A O   1 
ATOM   9463  C  CB  . LEU   A 1 1191 ? -24.08500  73.58700  -9.77100  1.000 37.25603  ?  1189 LEU   A CB  1 
ATOM   9464  C  CG  . LEU   A 1 1191 ? -24.97800  74.17800  -8.68300  1.000 61.62842  ?  1189 LEU   A CG  1 
ATOM   9465  C  CD1 . LEU   A 1 1191 ? -24.26900  75.27800  -7.90300  1.000 46.78720  ?  1189 LEU   A CD1 1 
ATOM   9466  C  CD2 . LEU   A 1 1191 ? -26.24600  74.68600  -9.31700  1.000 55.12795  ?  1189 LEU   A CD2 1 
ATOM   9467  N  N   . ASP   A 1 1192 ? -21.91200  71.57500  -10.88700 1.000 57.60485  ?  1190 ASP   A N   1 
ATOM   9468  C  CA  . ASP   A 1 1192 ? -21.13900  70.96200  -11.95800 1.000 38.02395  ?  1190 ASP   A CA  1 
ATOM   9469  C  C   . ASP   A 1 1192 ? -20.89200  69.47600  -11.72800 1.000 53.30103  ?  1190 ASP   A C   1 
ATOM   9470  O  O   . ASP   A 1 1192 ? -20.24800  68.83400  -12.56400 1.000 54.65922  ?  1190 ASP   A O   1 
ATOM   9471  C  CB  . ASP   A 1 1192 ? -19.80500  71.69500  -12.12700 1.000 42.85570  ?  1190 ASP   A CB  1 
ATOM   9472  C  CG  . ASP   A 1 1192 ? -19.03900  71.82400  -10.82200 1.000 86.37398  ?  1190 ASP   A CG  1 
ATOM   9473  O  OD1 . ASP   A 1 1192 ? -19.56600  71.39900  -9.77100  1.000 68.42805  ?  1190 ASP   A OD1 1 
ATOM   9474  O  OD2 . ASP   A 1 1192 ? -17.90600  72.35100  -10.84800 1.000 87.06283  -1 1190 ASP   A OD2 1 
ATOM   9475  N  N   . GLN   A 1 1193 ? -21.38600  68.92100  -10.62400 1.000 51.98861  ?  1191 GLN   A N   1 
ATOM   9476  C  CA  . GLN   A 1 1193 ? -21.21800  67.50800  -10.32400 1.000 45.57355  ?  1191 GLN   A CA  1 
ATOM   9477  C  C   . GLN   A 1 1193 ? -22.25900  66.66900  -11.05400 1.000 46.29239  ?  1191 GLN   A C   1 
ATOM   9478  O  O   . GLN   A 1 1193 ? -23.36800  67.12800  -11.34300 1.000 59.73018  ?  1191 GLN   A O   1 
ATOM   9479  C  CB  . GLN   A 1 1193 ? -21.32300  67.26700  -8.81800  1.000 55.43851  ?  1191 GLN   A CB  1 
ATOM   9480  C  CG  . GLN   A 1 1193 ? -19.98900  67.14800  -8.10200  1.000 74.97739  ?  1191 GLN   A CG  1 
ATOM   9481  C  CD  . GLN   A 1 1193 ? -19.44400  65.73400  -8.12200  1.000 89.78205  ?  1191 GLN   A CD  1 
ATOM   9482  O  OE1 . GLN   A 1 1193 ? -19.16900  65.17500  -9.18400  1.000 90.75749  ?  1191 GLN   A OE1 1 
ATOM   9483  N  NE2 . GLN   A 1 1193 ? -19.29600  65.14300  -6.94200  1.000 81.89698  ?  1191 GLN   A NE2 1 
ATOM   9484  N  N   . GLN   A 1 1194 ? -21.89400  65.42400  -11.34400 1.000 45.85852  ?  1192 GLN   A N   1 
ATOM   9485  C  CA  . GLN   A 1 1194 ? -22.78900  64.51400  -12.04100 1.000 49.48048  ?  1192 GLN   A CA  1 
ATOM   9486  C  C   . GLN   A 1 1194 ? -23.84300  63.95500  -11.09200 1.000 54.80726  ?  1192 GLN   A C   1 
ATOM   9487  O  O   . GLN   A 1 1194 ? -23.59200  63.74600  -9.90200  1.000 57.30038  ?  1192 GLN   A O   1 
ATOM   9488  C  CB  . GLN   A 1 1194 ? -22.00100  63.37200  -12.68100 1.000 50.20124  ?  1192 GLN   A CB  1 
ATOM   9489  C  CG  . GLN   A 1 1194 ? -21.22200  63.78400  -13.91800 1.000 49.75019  ?  1192 GLN   A CG  1 
ATOM   9490  C  CD  . GLN   A 1 1194 ? -20.27000  62.70700  -14.39500 1.000 55.73252  ?  1192 GLN   A CD  1 
ATOM   9491  O  OE1 . GLN   A 1 1194 ? -19.60500  62.05100  -13.59200 1.000 62.43964  ?  1192 GLN   A OE1 1 
ATOM   9492  N  NE2 . GLN   A 1 1194 ? -20.20100  62.51700  -15.70700 1.000 49.61774  ?  1192 GLN   A NE2 1 
ATOM   9493  N  N   . VAL   A 1 1195 ? -25.03700  63.71400  -11.64100 1.000 44.17942  ?  1193 VAL   A N   1 
ATOM   9494  C  CA  . VAL   A 1 1195 ? -26.15300  63.22400  -10.83500 1.000 44.94424  ?  1193 VAL   A CA  1 
ATOM   9495  C  C   . VAL   A 1 1195 ? -25.85700  61.83400  -10.28900 1.000 52.68091  ?  1193 VAL   A C   1 
ATOM   9496  O  O   . VAL   A 1 1195 ? -26.32500  61.47100  -9.20100  1.000 46.95224  ?  1193 VAL   A O   1 
ATOM   9497  C  CB  . VAL   A 1 1195 ? -27.45200  63.25900  -11.66900 1.000 43.29470  ?  1193 VAL   A CB  1 
ATOM   9498  C  CG1 . VAL   A 1 1195 ? -28.58700  62.53900  -10.95800 1.000 43.62227  ?  1193 VAL   A CG1 1 
ATOM   9499  C  CG2 . VAL   A 1 1195 ? -27.84500  64.69700  -11.95800 1.000 37.04397  ?  1193 VAL   A CG2 1 
ATOM   9500  N  N   . LYS   A 1 1196 ? -25.06500  61.04100  -11.01600 1.000 48.92825  ?  1194 LYS   A N   1 
ATOM   9501  C  CA  . LYS   A 1 1196 ? -24.66000  59.73300  -10.51100 1.000 50.70552  ?  1194 LYS   A CA  1 
ATOM   9502  C  C   . LYS   A 1 1196 ? -23.90400  59.85000  -9.19300  1.000 45.97503  ?  1194 LYS   A C   1 
ATOM   9503  O  O   . LYS   A 1 1196 ? -24.03000  58.97900  -8.32600  1.000 40.00660  ?  1194 LYS   A O   1 
ATOM   9504  C  CB  . LYS   A 1 1196 ? -23.79300  59.01400  -11.54700 1.000 39.25794  ?  1194 LYS   A CB  1 
ATOM   9505  C  CG  . LYS   A 1 1196 ? -22.53100  59.78100  -11.91100 1.000 46.31987  ?  1194 LYS   A CG  1 
ATOM   9506  C  CD  . LYS   A 1 1196 ? -21.42300  58.86900  -12.40100 1.000 60.64611  ?  1194 LYS   A CD  1 
ATOM   9507  C  CE  . LYS   A 1 1196 ? -21.72000  58.33500  -13.78500 1.000 58.42757  ?  1194 LYS   A CE  1 
ATOM   9508  N  NZ  . LYS   A 1 1196 ? -20.48800  58.28100  -14.62100 1.000 59.72671  ?  1194 LYS   A NZ  1 
ATOM   9509  N  N   . ARG   A 1 1197 ? -23.12400  60.91900  -9.02300  1.000 44.97500  ?  1195 ARG   A N   1 
ATOM   9510  C  CA  . ARG   A 1 1197 ? -22.29900  61.09500  -7.83600  1.000 54.66313  ?  1195 ARG   A CA  1 
ATOM   9511  C  C   . ARG   A 1 1197 ? -23.09300  61.56500  -6.62500  1.000 44.17362  ?  1195 ARG   A C   1 
ATOM   9512  O  O   . ARG   A 1 1197 ? -22.56000  61.55200  -5.51100  1.000 42.25404  ?  1195 ARG   A O   1 
ATOM   9513  C  CB  . ARG   A 1 1197 ? -21.16500  62.07900  -8.13600  1.000 54.15789  ?  1195 ARG   A CB  1 
ATOM   9514  C  CG  . ARG   A 1 1197 ? -20.21000  61.59500  -9.22000  1.000 57.44853  ?  1195 ARG   A CG  1 
ATOM   9515  C  CD  . ARG   A 1 1197 ? -19.22400  60.56800  -8.67700  1.000 80.63129  ?  1195 ARG   A CD  1 
ATOM   9516  N  NE  . ARG   A 1 1197 ? -18.88300  59.54600  -9.66000  1.000 84.27118  ?  1195 ARG   A NE  1 
ATOM   9517  C  CZ  . ARG   A 1 1197 ? -19.28500  58.28300  -9.59700  1.000 89.97256  ?  1195 ARG   A CZ  1 
ATOM   9518  N  NH1 . ARG   A 1 1197 ? -20.03000  57.84400  -8.59500  1.000 61.39820  ?  1195 ARG   A NH1 1 
ATOM   9519  N  NH2 . ARG   A 1 1197 ? -18.92500  57.43800  -10.55900 1.000 87.92439  ?  1195 ARG   A NH2 1 
ATOM   9520  N  N   . PHE   A 1 1198 ? -24.34000  61.98300  -6.81400  1.000 44.73502  ?  1196 PHE   A N   1 
ATOM   9521  C  CA  . PHE   A 1 1198 ? -25.22600  62.24700  -5.69200  1.000 45.63831  ?  1196 PHE   A CA  1 
ATOM   9522  C  C   . PHE   A 1 1198 ? -25.72300  60.92700  -5.12100  1.000 41.29002  ?  1196 PHE   A C   1 
ATOM   9523  O  O   . PHE   A 1 1198 ? -26.05600  60.00100  -5.86500  1.000 50.10682  ?  1196 PHE   A O   1 
ATOM   9524  C  CB  . PHE   A 1 1198 ? -26.41000  63.10800  -6.13100  1.000 44.89469  ?  1196 PHE   A CB  1 
ATOM   9525  C  CG  . PHE   A 1 1198 ? -26.02000  64.44500  -6.69400  1.000 46.17185  ?  1196 PHE   A CG  1 
ATOM   9526  C  CD1 . PHE   A 1 1198 ? -24.85200  65.07200  -6.28900  1.000 51.93828  ?  1196 PHE   A CD1 1 
ATOM   9527  C  CD2 . PHE   A 1 1198 ? -26.82500  65.07600  -7.62800  1.000 42.73673  ?  1196 PHE   A CD2 1 
ATOM   9528  C  CE1 . PHE   A 1 1198 ? -24.49500  66.30300  -6.80700  1.000 41.43384  ?  1196 PHE   A CE1 1 
ATOM   9529  C  CE2 . PHE   A 1 1198 ? -26.47300  66.30600  -8.14800  1.000 42.03260  ?  1196 PHE   A CE2 1 
ATOM   9530  C  CZ  . PHE   A 1 1198 ? -25.30700  66.91900  -7.73700  1.000 36.93496  ?  1196 PHE   A CZ  1 
ATOM   9531  N  N   . GLU   A 1 1199 ? -25.76600  60.83300  -3.79600  1.000 43.19468  ?  1197 GLU   A N   1 
ATOM   9532  C  CA  . GLU   A 1 1199 ? -26.18300  59.61000  -3.12800  1.000 60.32692  ?  1197 GLU   A CA  1 
ATOM   9533  C  C   . GLU   A 1 1199 ? -27.49100  59.83500  -2.38100  1.000 49.38911  ?  1197 GLU   A C   1 
ATOM   9534  O  O   . GLU   A 1 1199 ? -27.69100  60.87700  -1.74900  1.000 49.47514  ?  1197 GLU   A O   1 
ATOM   9535  C  CB  . GLU   A 1 1199 ? -25.10000  59.10200  -2.16900  1.000 60.29376  ?  1197 GLU   A CB  1 
ATOM   9536  C  CG  . GLU   A 1 1199 ? -24.83600  59.98200  -0.96200  1.000 68.62354  ?  1197 GLU   A CG  1 
ATOM   9537  C  CD  . GLU   A 1 1199 ? -23.68500  59.47100  -0.12100  1.000 87.14090  ?  1197 GLU   A CD  1 
ATOM   9538  O  OE1 . GLU   A 1 1199 ? -22.59700  59.23500  -0.68700  1.000 87.56492  ?  1197 GLU   A OE1 1 
ATOM   9539  O  OE2 . GLU   A 1 1199 ? -23.87200  59.29200  1.10100   1.000 95.41237  -1 1197 GLU   A OE2 1 
ATOM   9540  N  N   . LEU   A 1 1200 ? -28.38600  58.85000  -2.47100  1.000 51.98704  ?  1198 LEU   A N   1 
ATOM   9541  C  CA  . LEU   A 1 1200 ? -29.67900  58.95700  -1.80800  1.000 45.52191  ?  1198 LEU   A CA  1 
ATOM   9542  C  C   . LEU   A 1 1200 ? -29.58000  58.59300  -0.33400  1.000 45.01339  ?  1198 LEU   A C   1 
ATOM   9543  O  O   . LEU   A 1 1200 ? -30.17600  59.26400  0.51500   1.000 59.16897  ?  1198 LEU   A O   1 
ATOM   9544  C  CB  . LEU   A 1 1200 ? -30.70200  58.06000  -2.50400  1.000 40.37626  ?  1198 LEU   A CB  1 
ATOM   9545  C  CG  . LEU   A 1 1200 ? -32.16600  58.27100  -2.11900  1.000 52.32892  ?  1198 LEU   A CG  1 
ATOM   9546  C  CD1 . LEU   A 1 1200 ? -32.70000  59.54500  -2.75100  1.000 56.02973  ?  1198 LEU   A CD1 1 
ATOM   9547  C  CD2 . LEU   A 1 1200 ? -33.00700  57.07100  -2.52200  1.000 44.21666  ?  1198 LEU   A CD2 1 
ATOM   9548  N  N   . VAL   A 1 1201 ? -28.83000  57.53700  -0.01300  1.000 57.45276  ?  1199 VAL   A N   1 
ATOM   9549  C  CA  . VAL   A 1 1201 ? -28.76400  57.05900  1.36000   1.000 60.86394  ?  1199 VAL   A CA  1 
ATOM   9550  C  C   . VAL   A 1 1201 ? -28.04000  58.08400  2.22300   1.000 45.88722  ?  1199 VAL   A C   1 
ATOM   9551  O  O   . VAL   A 1 1201 ? -27.07300  58.72700  1.78900   1.000 47.25744  ?  1199 VAL   A O   1 
ATOM   9552  C  CB  . VAL   A 1 1201 ? -28.09300  55.67300  1.41500   1.000 49.34043  ?  1199 VAL   A CB  1 
ATOM   9553  C  CG1 . VAL   A 1 1201 ? -26.57200  55.78200  1.39900   1.000 55.01402  ?  1199 VAL   A CG1 1 
ATOM   9554  C  CG2 . VAL   A 1 1201 ? -28.57500  54.89100  2.62600   1.000 52.87709  ?  1199 VAL   A CG2 1 
ATOM   9555  N  N   . THR   A 1 1202 ? -28.53500  58.27400  3.43900   1.000 45.37764  ?  1200 THR   A N   1 
ATOM   9556  C  CA  . THR   A 1 1202 ? -27.95300  59.23800  4.35800   1.000 51.38997  ?  1200 THR   A CA  1 
ATOM   9557  C  C   . THR   A 1 1202 ? -26.96800  58.54300  5.29100   1.000 63.78394  ?  1200 THR   A C   1 
ATOM   9558  O  O   . THR   A 1 1202 ? -26.99900  57.32300  5.47000   1.000 72.45292  ?  1200 THR   A O   1 
ATOM   9559  C  CB  . THR   A 1 1202 ? -29.04200  59.93900  5.17100   1.000 49.88072  ?  1200 THR   A CB  1 
ATOM   9560  O  OG1 . THR   A 1 1202 ? -29.50200  59.06700  6.21100   1.000 56.76301  ?  1200 THR   A OG1 1 
ATOM   9561  C  CG2 . THR   A 1 1202 ? -30.21700  60.30400  4.27600   1.000 54.25155  ?  1200 THR   A CG2 1 
ATOM   9562  N  N   . GLU   A 1 1203 ? -26.07800  59.34300  5.88500   1.000 61.61248  ?  1201 GLU   A N   1 
ATOM   9563  C  CA  . GLU   A 1 1203 ? -25.09400  58.78300  6.80400   1.000 52.80667  ?  1201 GLU   A CA  1 
ATOM   9564  C  C   . GLU   A 1 1203 ? -25.76200  58.14700  8.01500   1.000 60.12502  ?  1201 GLU   A C   1 
ATOM   9565  O  O   . GLU   A 1 1203 ? -25.24600  57.16800  8.56600   1.000 72.02587  ?  1201 GLU   A O   1 
ATOM   9566  C  CB  . GLU   A 1 1203 ? -24.10500  59.86300  7.24200   1.000 40.46400  ?  1201 GLU   A CB  1 
ATOM   9567  C  CG  . GLU   A 1 1203 ? -22.64400  59.45600  7.09500   1.000 78.31731  ?  1201 GLU   A CG  1 
ATOM   9568  C  CD  . GLU   A 1 1203 ? -22.22700  59.28100  5.64300   1.000 79.10327  ?  1201 GLU   A CD  1 
ATOM   9569  O  OE1 . GLU   A 1 1203 ? -22.82500  59.94000  4.76600   1.000 75.82461  ?  1201 GLU   A OE1 1 
ATOM   9570  O  OE2 . GLU   A 1 1203 ? -21.30400  58.48100  5.37900   1.000 56.17121  -1 1201 GLU   A OE2 1 
ATOM   9571  N  N   . ASP   A 1 1204 ? -26.90900  58.68200  8.44000   1.000 44.65332  ?  1202 ASP   A N   1 
ATOM   9572  C  CA  . ASP   A 1 1204 ? -27.66400  58.04100  9.51000   1.000 48.94388  ?  1202 ASP   A CA  1 
ATOM   9573  C  C   . ASP   A 1 1204 ? -28.27400  56.72400  9.04800   1.000 61.38345  ?  1202 ASP   A C   1 
ATOM   9574  O  O   . ASP   A 1 1204 ? -28.37300  55.77800  9.83700   1.000 66.54062  ?  1202 ASP   A O   1 
ATOM   9575  C  CB  . ASP   A 1 1204 ? -28.75200  58.98400  10.02600  1.000 62.38501  ?  1202 ASP   A CB  1 
ATOM   9576  C  CG  . ASP   A 1 1204 ? -28.18700  60.27200  10.59400  1.000 84.92741  ?  1202 ASP   A CG  1 
ATOM   9577  O  OD1 . ASP   A 1 1204 ? -27.77900  61.14700  9.80000   1.000 81.50739  ?  1202 ASP   A OD1 1 
ATOM   9578  O  OD2 . ASP   A 1 1204 ? -28.14800  60.40900  11.83500  1.000 80.47801  -1 1202 ASP   A OD2 1 
ATOM   9579  N  N   . GLU   A 1 1205 ? -28.68600  56.64200  7.78000   1.000 59.79815  ?  1203 GLU   A N   1 
ATOM   9580  C  CA  . GLU   A 1 1205 ? -29.16900  55.37500  7.24400   1.000 51.08281  ?  1203 GLU   A CA  1 
ATOM   9581  C  C   . GLU   A 1 1205 ? -28.02500  54.39900  7.00600   1.000 61.54428  ?  1203 GLU   A C   1 
ATOM   9582  O  O   . GLU   A 1 1205 ? -28.21000  53.18400  7.14100   1.000 65.81881  ?  1203 GLU   A O   1 
ATOM   9583  C  CB  . GLU   A 1 1205 ? -29.94300  55.60800  5.94600   1.000 51.01517  ?  1203 GLU   A CB  1 
ATOM   9584  C  CG  . GLU   A 1 1205 ? -31.24200  56.37500  6.11700   1.000 60.38808  ?  1203 GLU   A CG  1 
ATOM   9585  C  CD  . GLU   A 1 1205 ? -31.94000  56.63700  4.79600   1.000 62.98155  ?  1203 GLU   A CD  1 
ATOM   9586  O  OE1 . GLU   A 1 1205 ? -31.42800  56.18500  3.75000   1.000 53.72669  ?  1203 GLU   A OE1 1 
ATOM   9587  O  OE2 . GLU   A 1 1205 ? -33.00000  57.29700  4.80400   1.000 66.81604  -1 1203 GLU   A OE2 1 
ATOM   9588  N  N   . LYS   A 1 1206 ? -26.84300  54.90800  6.64800   1.000 53.65850  ?  1204 LYS   A N   1 
ATOM   9589  C  CA  . LYS   A 1 1206 ? -25.67800  54.04400  6.48400   1.000 47.57986  ?  1204 LYS   A CA  1 
ATOM   9590  C  C   . LYS   A 1 1206 ? -25.27200  53.40700  7.80600   1.000 58.95971  ?  1204 LYS   A C   1 
ATOM   9591  O  O   . LYS   A 1 1206 ? -24.85700  52.24300  7.83900   1.000 64.08205  ?  1204 LYS   A O   1 
ATOM   9592  C  CB  . LYS   A 1 1206 ? -24.51100  54.83900  5.90100   1.000 37.57960  ?  1204 LYS   A CB  1 
ATOM   9593  C  CG  . LYS   A 1 1206 ? -24.55700  55.02800  4.39800   1.000 41.93096  ?  1204 LYS   A CG  1 
ATOM   9594  C  CD  . LYS   A 1 1206 ? -23.61500  56.14200  3.96800   1.000 59.62211  ?  1204 LYS   A CD  1 
ATOM   9595  C  CE  . LYS   A 1 1206 ? -23.06200  55.90300  2.57400   1.000 65.10594  ?  1204 LYS   A CE  1 
ATOM   9596  N  NZ  . LYS   A 1 1206 ? -22.13800  54.73500  2.54700   1.000 70.48036  ?  1204 LYS   A NZ  1 
ATOM   9597  N  N   . ARG   A 1 1207 ? -25.38100  54.15600  8.90500   1.000 59.57726  ?  1205 ARG   A N   1 
ATOM   9598  C  CA  . ARG   A 1 1207 ? -24.97300  53.63000  10.20100  1.000 60.18437  ?  1205 ARG   A CA  1 
ATOM   9599  C  C   . ARG   A 1 1207 ? -26.07500  52.80700  10.85200  1.000 58.13704  ?  1205 ARG   A C   1 
ATOM   9600  O  O   . ARG   A 1 1207 ? -25.78100  51.90700  11.64600  1.000 70.53843  ?  1205 ARG   A O   1 
ATOM   9601  C  CB  . ARG   A 1 1207 ? -24.53700  54.77700  11.11600  1.000 58.52338  ?  1205 ARG   A CB  1 
ATOM   9602  C  CG  . ARG   A 1 1207 ? -23.56400  54.38000  12.22700  1.000 61.08701  ?  1205 ARG   A CG  1 
ATOM   9603  C  CD  . ARG   A 1 1207 ? -22.47800  53.40900  11.74500  1.000 87.32185  ?  1205 ARG   A CD  1 
ATOM   9604  N  NE  . ARG   A 1 1207 ? -21.90200  53.77500  10.45400  1.000 101.13261 ?  1205 ARG   A NE  1 
ATOM   9605  C  CZ  . ARG   A 1 1207 ? -21.09700  52.99500  9.74400   1.000 85.40100  ?  1205 ARG   A CZ  1 
ATOM   9606  N  NH1 . ARG   A 1 1207 ? -20.70500  51.81400  10.19400  1.000 65.48927  ?  1205 ARG   A NH1 1 
ATOM   9607  N  NH2 . ARG   A 1 1207 ? -20.67900  53.40900  8.55100   1.000 74.01522  ?  1205 ARG   A NH2 1 
ATOM   9608  N  N   . ASP   A 1 1208 ? -27.33800  53.09300  10.53100  1.000 58.18433  ?  1206 ASP   A N   1 
ATOM   9609  C  CA  . ASP   A 1 1208 ? -28.42000  52.23200  10.99400  1.000 56.61394  ?  1206 ASP   A CA  1 
ATOM   9610  C  C   . ASP   A 1 1208 ? -28.39400  50.89000  10.27500  1.000 64.84215  ?  1206 ASP   A C   1 
ATOM   9611  O  O   . ASP   A 1 1208 ? -28.67800  49.85000  10.88100  1.000 60.36937  ?  1206 ASP   A O   1 
ATOM   9612  C  CB  . ASP   A 1 1208 ? -29.76700  52.93100  10.80500  1.000 55.00158  ?  1206 ASP   A CB  1 
ATOM   9613  C  CG  . ASP   A 1 1208 ? -30.92100  51.95300  10.67600  1.000 78.37373  ?  1206 ASP   A CG  1 
ATOM   9614  O  OD1 . ASP   A 1 1208 ? -31.00700  51.02300  11.50600  1.000 91.29048  ?  1206 ASP   A OD1 1 
ATOM   9615  O  OD2 . ASP   A 1 1208 ? -31.72800  52.10300  9.73500   1.000 81.80543  -1 1206 ASP   A OD2 1 
ATOM   9616  N  N   . LEU   A 1 1209 ? -28.04400  50.89000  8.98600   1.000 62.04668  ?  1207 LEU   A N   1 
ATOM   9617  C  CA  . LEU   A 1 1209 ? -27.93800  49.63200  8.25600   1.000 53.17948  ?  1207 LEU   A CA  1 
ATOM   9618  C  C   . LEU   A 1 1209 ? -26.77900  48.78900  8.77200   1.000 61.27176  ?  1207 LEU   A C   1 
ATOM   9619  O  O   . LEU   A 1 1209 ? -26.87200  47.55900  8.81200   1.000 62.07169  ?  1207 LEU   A O   1 
ATOM   9620  C  CB  . LEU   A 1 1209 ? -27.78800  49.89800  6.75800   1.000 62.32353  ?  1207 LEU   A CB  1 
ATOM   9621  C  CG  . LEU   A 1 1209 ? -29.09000  50.09700  5.97900   1.000 61.46428  ?  1207 LEU   A CG  1 
ATOM   9622  C  CD1 . LEU   A 1 1209 ? -28.80900  50.33400  4.50300   1.000 54.57447  ?  1207 LEU   A CD1 1 
ATOM   9623  C  CD2 . LEU   A 1 1209 ? -30.00900  48.89900  6.16500   1.000 52.32193  ?  1207 LEU   A CD2 1 
ATOM   9624  N  N   . PHE   A 1 1210 ? -25.68000  49.42800  9.17700   1.000 57.72142  ?  1208 PHE   A N   1 
ATOM   9625  C  CA  . PHE   A 1 1210 ? -24.56500  48.67700  9.74600   1.000 56.91329  ?  1208 PHE   A CA  1 
ATOM   9626  C  C   . PHE   A 1 1210 ? -24.96400  48.01700  11.06100  1.000 61.78672  ?  1208 PHE   A C   1 
ATOM   9627  O  O   . PHE   A 1 1210 ? -24.73400  46.81900  11.26600  1.000 76.98572  ?  1208 PHE   A O   1 
ATOM   9628  C  CB  . PHE   A 1 1210 ? -23.35900  49.59600  9.94800   1.000 53.39762  ?  1208 PHE   A CB  1 
ATOM   9629  C  CG  . PHE   A 1 1210 ? -22.24900  48.97500  10.75200  1.000 60.92098  ?  1208 PHE   A CG  1 
ATOM   9630  C  CD1 . PHE   A 1 1210 ? -21.27600  48.20600  10.13500  1.000 57.86297  ?  1208 PHE   A CD1 1 
ATOM   9631  C  CD2 . PHE   A 1 1210 ? -22.17500  49.16500  12.12400  1.000 60.46966  ?  1208 PHE   A CD2 1 
ATOM   9632  C  CE1 . PHE   A 1 1210 ? -20.25400  47.63500  10.87200  1.000 60.05411  ?  1208 PHE   A CE1 1 
ATOM   9633  C  CE2 . PHE   A 1 1210 ? -21.15900  48.59500  12.86500  1.000 58.77649  ?  1208 PHE   A CE2 1 
ATOM   9634  C  CZ  . PHE   A 1 1210 ? -20.19600  47.83000  12.23800  1.000 55.76866  ?  1208 PHE   A CZ  1 
ATOM   9635  N  N   . LEU   A 1 1211 ? -25.57000  48.78900  11.96600  1.000 51.95479  ?  1209 LEU   A N   1 
ATOM   9636  C  CA  . LEU   A 1 1211 ? -25.90000  48.26700  13.28900  1.000 59.67314  ?  1209 LEU   A CA  1 
ATOM   9637  C  C   . LEU   A 1 1211 ? -26.98200  47.19600  13.21800  1.000 67.42966  ?  1209 LEU   A C   1 
ATOM   9638  O  O   . LEU   A 1 1211 ? -26.95700  46.23100  13.99100  1.000 79.09598  ?  1209 LEU   A O   1 
ATOM   9639  C  CB  . LEU   A 1 1211 ? -26.33400  49.41200  14.20500  1.000 71.80138  ?  1209 LEU   A CB  1 
ATOM   9640  C  CG  . LEU   A 1 1211 ? -25.25100  50.41700  14.60300  1.000 74.17945  ?  1209 LEU   A CG  1 
ATOM   9641  C  CD1 . LEU   A 1 1211 ? -25.87800  51.68400  15.15900  1.000 61.96764  ?  1209 LEU   A CD1 1 
ATOM   9642  C  CD2 . LEU   A 1 1211 ? -24.29800  49.80300  15.61900  1.000 82.09788  ?  1209 LEU   A CD2 1 
ATOM   9643  N  N   . ARG   A 1 1212 ? -27.94000  47.34400  12.30300  1.000 61.06854  ?  1210 ARG   A N   1 
ATOM   9644  C  CA  . ARG   A 1 1212 ? -29.04100  46.39700  12.19100  1.000 57.13329  ?  1210 ARG   A CA  1 
ATOM   9645  C  C   . ARG   A 1 1212 ? -28.73900  45.22200  11.27200  1.000 62.97580  ?  1210 ARG   A C   1 
ATOM   9646  O  O   . ARG   A 1 1212 ? -29.51800  44.26300  11.24900  1.000 66.46592  ?  1210 ARG   A O   1 
ATOM   9647  C  CB  . ARG   A 1 1212 ? -30.30900  47.10200  11.69200  1.000 46.00233  ?  1210 ARG   A CB  1 
ATOM   9648  C  CG  . ARG   A 1 1212 ? -30.83000  48.20000  12.60600  1.000 53.40188  ?  1210 ARG   A CG  1 
ATOM   9649  C  CD  . ARG   A 1 1212 ? -32.32500  48.05100  12.86200  1.000 72.44374  ?  1210 ARG   A CD  1 
ATOM   9650  N  NE  . ARG   A 1 1212 ? -33.00500  49.34000  12.93300  1.000 90.43404  ?  1210 ARG   A NE  1 
ATOM   9651  C  CZ  . ARG   A 1 1212 ? -33.89500  49.76700  12.04600  1.000 92.96274  ?  1210 ARG   A CZ  1 
ATOM   9652  N  NH1 . ARG   A 1 1212 ? -34.25800  49.01900  11.01600  1.000 80.41950  ?  1210 ARG   A NH1 1 
ATOM   9653  N  NH2 . ARG   A 1 1212 ? -34.44000  50.97000  12.20100  1.000 90.53233  ?  1210 ARG   A NH2 1 
ATOM   9654  N  N   . VAL   A 1 1213 ? -27.64300  45.26700  10.51300  1.000 64.77120  ?  1211 VAL   A N   1 
ATOM   9655  C  CA  . VAL   A 1 1213 ? -27.36700  44.23400  9.51900   1.000 60.80324  ?  1211 VAL   A CA  1 
ATOM   9656  C  C   . VAL   A 1 1213 ? -25.92400  43.75000  9.61900   1.000 62.81022  ?  1211 VAL   A C   1 
ATOM   9657  O  O   . VAL   A 1 1213 ? -25.67500  42.57600  9.91500   1.000 70.12435  ?  1211 VAL   A O   1 
ATOM   9658  C  CB  . VAL   A 1 1213 ? -27.67500  44.74200  8.09700   1.000 57.44842  ?  1211 VAL   A CB  1 
ATOM   9659  C  CG1 . VAL   A 1 1213 ? -27.29800  43.70600  7.06100   1.000 48.24816  ?  1211 VAL   A CG1 1 
ATOM   9660  C  CG2 . VAL   A 1 1213 ? -29.14200  45.12500  7.96200   1.000 61.63519  ?  1211 VAL   A CG2 1 
ATOM   9661  N  N   . ASN   A 1 1214 ? -24.96400  44.64600  9.38000   1.000 54.25812  ?  1212 ASN   A N   1 
ATOM   9662  C  CA  . ASN   A 1 1214 ? -23.57400  44.26600  9.14700   1.000 44.79292  ?  1212 ASN   A CA  1 
ATOM   9663  C  C   . ASN   A 1 1214 ? -22.68900  44.39700  10.38500  1.000 57.50877  ?  1212 ASN   A C   1 
ATOM   9664  O  O   . ASN   A 1 1214 ? -21.48100  44.62200  10.25300  1.000 57.75019  ?  1212 ASN   A O   1 
ATOM   9665  C  CB  . ASN   A 1 1214 ? -22.98600  45.08900  8.00100   1.000 42.04138  ?  1212 ASN   A CB  1 
ATOM   9666  C  CG  . ASN   A 1 1214 ? -23.53200  44.67900  6.65000   1.000 52.28406  ?  1212 ASN   A CG  1 
ATOM   9667  O  OD1 . ASN   A 1 1214 ? -24.00100  43.55500  6.47000   1.000 56.14294  ?  1212 ASN   A OD1 1 
ATOM   9668  N  ND2 . ASN   A 1 1214 ? -23.46800  45.59000  5.68700   1.000 50.76077  ?  1212 ASN   A ND2 1 
ATOM   9669  N  N   . ASP   A 1 1215 ? -23.25000  44.25100  11.58500  1.000 69.57437  ?  1213 ASP   A N   1 
ATOM   9670  C  CA  . ASP   A 1 1215 ? -22.44400  44.21400  12.80600  1.000 68.94335  ?  1213 ASP   A CA  1 
ATOM   9671  C  C   . ASP   A 1 1215 ? -22.40200  42.76600  13.28600  1.000 62.00475  ?  1213 ASP   A C   1 
ATOM   9672  O  O   . ASP   A 1 1215 ? -23.13300  42.35100  14.18600  1.000 68.90824  ?  1213 ASP   A O   1 
ATOM   9673  C  CB  . ASP   A 1 1215 ? -23.00600  45.15600  13.86600  1.000 71.05901  ?  1213 ASP   A CB  1 
ATOM   9674  C  CG  . ASP   A 1 1215 ? -21.99300  45.48200  14.94700  1.000 76.80620  ?  1213 ASP   A CG  1 
ATOM   9675  O  OD1 . ASP   A 1 1215 ? -20.81400  45.10000  14.79200  1.000 74.15704  ?  1213 ASP   A OD1 1 
ATOM   9676  O  OD2 . ASP   A 1 1215 ? -22.37400  46.12000  15.95100  1.000 82.20027  -1 1213 ASP   A OD2 1 
ATOM   9677  N  N   . THR   A 1 1216 ? -21.51700  41.98400  12.66100  1.000 53.39210  ?  1214 THR   A N   1 
ATOM   9678  C  CA  . THR   A 1 1216 ? -21.51000  40.53600  12.82600  1.000 65.28292  ?  1214 THR   A CA  1 
ATOM   9679  C  C   . THR   A 1 1216 ? -20.14000  39.97000  13.18400  1.000 69.13449  ?  1214 THR   A C   1 
ATOM   9680  O  O   . THR   A 1 1216 ? -19.97800  38.74500  13.19300  1.000 71.84596  ?  1214 THR   A O   1 
ATOM   9681  C  CB  . THR   A 1 1216 ? -22.01800  39.85500  11.54800  1.000 72.50845  ?  1214 THR   A CB  1 
ATOM   9682  O  OG1 . THR   A 1 1216 ? -21.21900  40.27200  10.43300  1.000 49.87354  ?  1214 THR   A OG1 1 
ATOM   9683  C  CG2 . THR   A 1 1216 ? -23.47600  40.21200  11.28600  1.000 56.68022  ?  1214 THR   A CG2 1 
ATOM   9684  N  N   . ALA   A 1 1217 ? -19.15600  40.81500  13.48000  1.000 71.87211  ?  1215 ALA   A N   1 
ATOM   9685  C  CA  . ALA   A 1 1217 ? -17.81100  40.32500  13.75400  1.000 56.39252  ?  1215 ALA   A CA  1 
ATOM   9686  C  C   . ALA   A 1 1217 ? -17.77300  39.52500  15.05100  1.000 68.72742  ?  1215 ALA   A C   1 
ATOM   9687  O  O   . ALA   A 1 1217 ? -18.36800  39.91400  16.06000  1.000 60.47678  ?  1215 ALA   A O   1 
ATOM   9688  C  CB  . ALA   A 1 1217 ? -16.82600  41.49100  13.83000  1.000 45.81726  ?  1215 ALA   A CB  1 
ATOM   9689  N  N   . LYS   A 1 1218 ? -17.06600  38.39600  15.01600  1.000 70.69931  ?  1216 LYS   A N   1 
ATOM   9690  C  CA  . LYS   A 1 1218 ? -16.91200  37.54900  16.19700  1.000 68.84331  ?  1216 LYS   A CA  1 
ATOM   9691  C  C   . LYS   A 1 1218 ? -15.63800  36.73300  16.04800  1.000 67.09725  ?  1216 LYS   A C   1 
ATOM   9692  O  O   . LYS   A 1 1218 ? -15.50900  35.95900  15.09500  1.000 73.94375  ?  1216 LYS   A O   1 
ATOM   9693  C  CB  . LYS   A 1 1218 ? -18.12300  36.63300  16.38200  1.000 55.77169  ?  1216 LYS   A CB  1 
ATOM   9694  C  CG  . LYS   A 1 1218 ? -17.97300  35.64200  17.52500  1.000 55.58110  ?  1216 LYS   A CG  1 
ATOM   9695  C  CD  . LYS   A 1 1218 ? -19.31900  35.11200  17.98700  1.000 49.36105  ?  1216 LYS   A CD  1 
ATOM   9696  C  CE  . LYS   A 1 1218 ? -19.15900  34.18300  19.17900  1.000 62.63916  ?  1216 LYS   A CE  1 
ATOM   9697  N  NZ  . LYS   A 1 1218 ? -20.46900  33.84000  19.79700  1.000 71.86944  ?  1216 LYS   A NZ  1 
ATOM   9698  N  N   . ALA   A 1 1219 ? -14.70900  36.90100  16.98600  1.000 66.51307  ?  1217 ALA   A N   1 
ATOM   9699  C  CA  . ALA   A 1 1219 ? -13.44900  36.17000  16.94300  1.000 68.24782  ?  1217 ALA   A CA  1 
ATOM   9700  C  C   . ALA   A 1 1219 ? -13.69600  34.67600  17.11300  1.000 76.14600  ?  1217 ALA   A C   1 
ATOM   9701  O  O   . ALA   A 1 1219 ? -14.26300  34.23900  18.12000  1.000 77.15235  ?  1217 ALA   A O   1 
ATOM   9702  C  CB  . ALA   A 1 1219 ? -12.50900  36.68400  18.03100  1.000 68.94576  ?  1217 ALA   A CB  1 
ATOM   9703  N  N   . TYR   A 1 1220 ? -13.27300  33.89400  16.12200  1.000 72.85057  ?  1218 TYR   A N   1 
ATOM   9704  C  CA  . TYR   A 1 1220 ? -13.45600  32.45400  16.12900  1.000 71.37932  ?  1218 TYR   A CA  1 
ATOM   9705  C  C   . TYR   A 1 1220 ? -12.10600  31.74700  16.14400  1.000 75.97091  ?  1218 TYR   A C   1 
ATOM   9706  O  O   . TYR   A 1 1220 ? -11.12000  32.27300  15.61600  1.000 72.50913  ?  1218 TYR   A O   1 
ATOM   9707  C  CB  . TYR   A 1 1220 ? -14.26700  31.99500  14.90900  1.000 63.11846  ?  1218 TYR   A CB  1 
ATOM   9708  C  CG  . TYR   A 1 1220 ? -15.76000  32.15100  15.08600  1.000 63.26895  ?  1218 TYR   A CG  1 
ATOM   9709  C  CD1 . TYR   A 1 1220 ? -16.35700  31.93500  16.32100  1.000 61.88983  ?  1218 TYR   A CD1 1 
ATOM   9710  C  CD2 . TYR   A 1 1220 ? -16.57300  32.52100  14.02100  1.000 57.47288  ?  1218 TYR   A CD2 1 
ATOM   9711  C  CE1 . TYR   A 1 1220 ? -17.72100  32.07600  16.49200  1.000 68.88598  ?  1218 TYR   A CE1 1 
ATOM   9712  C  CE2 . TYR   A 1 1220 ? -17.94000  32.66400  14.18200  1.000 54.81991  ?  1218 TYR   A CE2 1 
ATOM   9713  C  CZ  . TYR   A 1 1220 ? -18.50800  32.44100  15.42000  1.000 57.35948  ?  1218 TYR   A CZ  1 
ATOM   9714  O  OH  . TYR   A 1 1220 ? -19.86700  32.58300  15.58900  1.000 44.31735  ?  1218 TYR   A OH  1 
ATOM   9715  N  N   . PRO   A 1 1221 ? -12.02800  30.56400  16.75500  1.000 77.73038  ?  1219 PRO   A N   1 
ATOM   9716  C  CA  . PRO   A 1 1221 ? -10.74600  29.85200  16.82900  1.000 58.47750  ?  1219 PRO   A CA  1 
ATOM   9717  C  C   . PRO   A 1 1221 ? -10.17900  29.55800  15.44900  1.000 65.37069  ?  1219 PRO   A C   1 
ATOM   9718  O  O   . PRO   A 1 1221 ? -10.91000  29.32300  14.48500  1.000 89.76121  ?  1219 PRO   A O   1 
ATOM   9719  C  CB  . PRO   A 1 1221 ? -11.10100  28.56000  17.57300  1.000 66.35973  ?  1219 PRO   A CB  1 
ATOM   9720  C  CG  . PRO   A 1 1221 ? -12.31700  28.90700  18.36600  1.000 72.82921  ?  1219 PRO   A CG  1 
ATOM   9721  C  CD  . PRO   A 1 1221 ? -13.08500  29.88400  17.52600  1.000 75.73282  ?  1219 PRO   A CD  1 
ATOM   9722  N  N   . ASN   A 1 1222 ? -8.84800   29.57700  15.36500  1.000 60.67683  ?  1220 ASN   A N   1 
ATOM   9723  C  CA  . ASN   A 1 1222 ? -8.13600   29.34200  14.11700  1.000 65.70601  ?  1220 ASN   A CA  1 
ATOM   9724  C  C   . ASN   A 1 1222 ? -7.62100   27.91200  14.00200  1.000 82.61002  ?  1220 ASN   A C   1 
ATOM   9725  O  O   . ASN   A 1 1222 ? -6.74700   27.64000  13.17200  1.000 81.53572  ?  1220 ASN   A O   1 
ATOM   9726  C  CB  . ASN   A 1 1222 ? -6.98000   30.33300  13.97600  1.000 72.34836  ?  1220 ASN   A CB  1 
ATOM   9727  C  CG  . ASN   A 1 1222 ? -7.38600   31.75200  14.32100  1.000 99.02760  ?  1220 ASN   A CG  1 
ATOM   9728  O  OD1 . ASN   A 1 1222 ? -8.11400   32.40200  13.57000  1.000 99.59738  ?  1220 ASN   A OD1 1 
ATOM   9729  N  ND2 . ASN   A 1 1222 ? -6.91000   32.24300  15.45900  1.000 97.07608  ?  1220 ASN   A ND2 1 
ATOM   9730  N  N   . LYS   A 1 1223 ? -8.13900   26.99600  14.81800  1.000 82.15303  ?  1221 LYS   A N   1 
ATOM   9731  C  CA  . LYS   A 1 1223 ? -7.73900   25.59400  14.75400  1.000 72.20410  ?  1221 LYS   A CA  1 
ATOM   9732  C  C   . LYS   A 1 1223 ? -8.41900   24.95600  13.54800  1.000 69.77554  ?  1221 LYS   A C   1 
ATOM   9733  O  O   . LYS   A 1 1223 ? -9.64600   24.81700  13.51900  1.000 75.10189  ?  1221 LYS   A O   1 
ATOM   9734  C  CB  . LYS   A 1 1223 ? -8.10300   24.86900  16.04700  1.000 83.75067  ?  1221 LYS   A CB  1 
ATOM   9735  C  CG  . LYS   A 1 1223 ? -7.43100   23.50800  16.21000  1.000 77.82432  ?  1221 LYS   A CG  1 
ATOM   9736  C  CD  . LYS   A 1 1223 ? -7.99100   22.74700  17.40600  1.000 66.88599  ?  1221 LYS   A CD  1 
ATOM   9737  C  CE  . LYS   A 1 1223 ? -7.19800   23.02400  18.67500  1.000 57.39048  ?  1221 LYS   A CE  1 
ATOM   9738  N  NZ  . LYS   A 1 1223 ? -8.06100   22.96100  19.89000  1.000 65.44009  ?  1221 LYS   A NZ  1 
ATOM   9739  N  N   . LEU   A 1 1224 ? -7.62200   24.57300  12.55300  1.000 62.64828  ?  1222 LEU   A N   1 
ATOM   9740  C  CA  . LEU   A 1 1224 ? -8.16600   24.06800  11.30200  1.000 68.48054  ?  1222 LEU   A CA  1 
ATOM   9741  C  C   . LEU   A 1 1224 ? -8.90500   22.74900  11.52600  1.000 81.01916  ?  1222 LEU   A C   1 
ATOM   9742  O  O   . LEU   A 1 1224 ? -8.65400   22.01900  12.48900  1.000 88.18613  ?  1222 LEU   A O   1 
ATOM   9743  C  CB  . LEU   A 1 1224 ? -7.05000   23.89500  10.27500  1.000 57.74396  ?  1222 LEU   A CB  1 
ATOM   9744  C  CG  . LEU   A 1 1224 ? -6.21200   25.15200  10.01900  1.000 54.03565  ?  1222 LEU   A CG  1 
ATOM   9745  C  CD1 . LEU   A 1 1224 ? -5.16200   24.91200  8.94600   1.000 51.78520  ?  1222 LEU   A CD1 1 
ATOM   9746  C  CD2 . LEU   A 1 1224 ? -7.10200   26.32700  9.64600   1.000 66.18420  ?  1222 LEU   A CD2 1 
ATOM   9747  N  N   . ILE   A 1 1225 ? -9.82700   22.44900  10.60500  1.000 80.43730  ?  1223 ILE   A N   1 
ATOM   9748  C  CA  . ILE   A 1 1225 ? -10.76500  21.34400  10.79900  1.000 67.79205  ?  1223 ILE   A CA  1 
ATOM   9749  C  C   . ILE   A 1 1225 ? -10.04000  20.00700  10.88600  1.000 67.27078  ?  1223 ILE   A C   1 
ATOM   9750  O  O   . ILE   A 1 1225 ? -10.51500  19.07700  11.55000  1.000 73.69544  ?  1223 ILE   A O   1 
ATOM   9751  C  CB  . ILE   A 1 1225 ? -11.82400  21.34900  9.67500   1.000 64.76523  ?  1223 ILE   A CB  1 
ATOM   9752  C  CG1 . ILE   A 1 1225 ? -13.00900  20.45300  10.03900  1.000 57.98919  ?  1223 ILE   A CG1 1 
ATOM   9753  C  CG2 . ILE   A 1 1225 ? -11.21400  20.93200  8.34100   1.000 64.24553  ?  1223 ILE   A CG2 1 
ATOM   9754  C  CD1 . ILE   A 1 1225 ? -14.01600  21.12100  10.94700  1.000 56.81399  ?  1223 ILE   A CD1 1 
ATOM   9755  N  N   . MET   A 1 1226 ? -8.88200   19.88400  10.23400  1.000 71.99629  ?  1224 MET   A N   1 
ATOM   9756  C  CA  . MET   A 1 1226 ? -8.11100   18.64800  10.31900  1.000 62.34295  ?  1224 MET   A CA  1 
ATOM   9757  C  C   . MET   A 1 1226 ? -7.57800   18.43700  11.72800  1.000 69.81675  ?  1224 MET   A C   1 
ATOM   9758  O  O   . MET   A 1 1226 ? -7.66500   17.33400  12.28000  1.000 73.64297  ?  1224 MET   A O   1 
ATOM   9759  C  CB  . MET   A 1 1226 ? -6.96000   18.68400  9.32100   1.000 56.58525  ?  1224 MET   A CB  1 
ATOM   9760  C  CG  . MET   A 1 1226 ? -7.34300   19.25200  7.98400   1.000 64.98881  ?  1224 MET   A CG  1 
ATOM   9761  S  SD  . MET   A 1 1226 ? -5.92000   19.98900  7.16700   1.000 82.68711  ?  1224 MET   A SD  1 
ATOM   9762  C  CE  . MET   A 1 1226 ? -5.85800   21.58600  7.95400   1.000 69.22102  ?  1224 MET   A CE  1 
ATOM   9763  N  N   . SER   A 1 1227 ? -7.01100   19.49000  12.32100  1.000 66.40268  ?  1225 SER   A N   1 
ATOM   9764  C  CA  . SER   A 1 1227 ? -6.49000   19.40000  13.67700  1.000 61.27342  ?  1225 SER   A CA  1 
ATOM   9765  C  C   . SER   A 1 1227 ? -7.58200   19.09200  14.69100  1.000 69.13714  ?  1225 SER   A C   1 
ATOM   9766  O  O   . SER   A 1 1227 ? -7.28600   18.54100  15.75600  1.000 76.44331  ?  1225 SER   A O   1 
ATOM   9767  C  CB  . SER   A 1 1227 ? -5.78400   20.70500  14.04700  1.000 80.96532  ?  1225 SER   A CB  1 
ATOM   9768  O  OG  . SER   A 1 1227 ? -4.92500   21.12900  13.00200  1.000 73.59480  ?  1225 SER   A OG  1 
ATOM   9769  N  N   . MET   A 1 1228 ? -8.83700   19.43200  14.38500  1.000 70.33492  ?  1226 MET   A N   1 
ATOM   9770  C  CA  . MET   A 1 1228 ? -9.93000   19.09900  15.29300  1.000 74.19589  ?  1226 MET   A CA  1 
ATOM   9771  C  C   . MET   A 1 1228 ? -10.22200  17.60400  15.27400  1.000 81.38191  ?  1226 MET   A C   1 
ATOM   9772  O  O   . MET   A 1 1228 ? -10.50600  17.00900  16.32000  1.000 80.40968  ?  1226 MET   A O   1 
ATOM   9773  C  CB  . MET   A 1 1228 ? -11.18000  19.89900  14.92500  1.000 73.48531  ?  1226 MET   A CB  1 
ATOM   9774  C  CG  . MET   A 1 1228 ? -10.90200  21.35500  14.59500  1.000 72.28227  ?  1226 MET   A CG  1 
ATOM   9775  S  SD  . MET   A 1 1228 ? -12.39700  22.32900  14.33500  1.000 68.14261  ?  1226 MET   A SD  1 
ATOM   9776  C  CE  . MET   A 1 1228 ? -12.72700  22.89400  16.00200  1.000 47.39401  ?  1226 MET   A CE  1 
ATOM   9777  N  N   . LEU   A 1 1229 ? -10.15700  16.98100  14.09300  1.000 68.23996  ?  1227 LEU   A N   1 
ATOM   9778  C  CA  . LEU   A 1 1229 ? -10.34500  15.53600  14.00900  1.000 68.09510  ?  1227 LEU   A CA  1 
ATOM   9779  C  C   . LEU   A 1 1229 ? -9.24400   14.79400  14.75800  1.000 83.85386  ?  1227 LEU   A C   1 
ATOM   9780  O  O   . LEU   A 1 1229 ? -9.50900   13.79200  15.43100  1.000 80.80839  ?  1227 LEU   A O   1 
ATOM   9781  C  CB  . LEU   A 1 1229 ? -10.39400  15.09600  12.54600  1.000 54.50454  ?  1227 LEU   A CB  1 
ATOM   9782  C  CG  . LEU   A 1 1229 ? -10.55000  13.59500  12.28900  1.000 54.11595  ?  1227 LEU   A CG  1 
ATOM   9783  C  CD1 . LEU   A 1 1229 ? -11.87000  13.08400  12.84600  1.000 57.09755  ?  1227 LEU   A CD1 1 
ATOM   9784  C  CD2 . LEU   A 1 1229 ? -10.43300  13.28700  10.80300  1.000 53.00008  ?  1227 LEU   A CD2 1 
ATOM   9785  N  N   . GLU   A 1 1230 ? -8.00000   15.27000  14.64900  1.000 80.23565  ?  1228 GLU   A N   1 
ATOM   9786  C  CA  . GLU   A 1 1230 ? -6.91200   14.70400  15.44100  1.000 68.60700  ?  1228 GLU   A CA  1 
ATOM   9787  C  C   . GLU   A 1 1230 ? -7.18200   14.87000  16.93000  1.000 71.31217  ?  1228 GLU   A C   1 
ATOM   9788  O  O   . GLU   A 1 1230 ? -7.16100   13.89900  17.69400  1.000 81.05518  ?  1228 GLU   A O   1 
ATOM   9789  C  CB  . GLU   A 1 1230 ? -5.58500   15.37100  15.07200  1.000 57.08141  ?  1228 GLU   A CB  1 
ATOM   9790  C  CG  . GLU   A 1 1230 ? -5.08900   15.09100  13.67300  1.000 63.37935  ?  1228 GLU   A CG  1 
ATOM   9791  C  CD  . GLU   A 1 1230 ? -3.75900   15.76900  13.38900  1.000 81.93135  ?  1228 GLU   A CD  1 
ATOM   9792  O  OE1 . GLU   A 1 1230 ? -3.32100   16.58900  14.22400  1.000 82.24517  ?  1228 GLU   A OE1 1 
ATOM   9793  O  OE2 . GLU   A 1 1230 ? -3.15100   15.48200  12.33600  1.000 63.01066  -1 1228 GLU   A OE2 1 
ATOM   9794  N  N   . ASP   A 1 1231 ? -7.43000   16.11100  17.35700  1.000 60.10785  ?  1229 ASP   A N   1 
ATOM   9795  C  CA  . ASP   A 1 1231 ? -7.66600   16.38800  18.77000  1.000 75.85896  ?  1229 ASP   A CA  1 
ATOM   9796  C  C   . ASP   A 1 1231 ? -8.83700   15.57600  19.30800  1.000 79.45355  ?  1229 ASP   A C   1 
ATOM   9797  O  O   . ASP   A 1 1231 ? -8.77400   15.05000  20.42500  1.000 80.89999  ?  1229 ASP   A O   1 
ATOM   9798  C  CB  . ASP   A 1 1231 ? -7.91400   17.88400  18.97600  1.000 89.78387  ?  1229 ASP   A CB  1 
ATOM   9799  C  CG  . ASP   A 1 1231 ? -6.63300   18.70100  18.96300  1.000 85.39055  ?  1229 ASP   A CG  1 
ATOM   9800  O  OD1 . ASP   A 1 1231 ? -5.75900   18.43800  18.11100  1.000 94.47032  ?  1229 ASP   A OD1 1 
ATOM   9801  O  OD2 . ASP   A 1 1231 ? -6.50700   19.61900  19.80200  1.000 68.39228  -1 1229 ASP   A OD2 1 
ATOM   9802  N  N   . TRP   A 1 1232 ? -9.91300   15.45300  18.52600  1.000 81.04619  ?  1230 TRP   A N   1 
ATOM   9803  C  CA  . TRP   A 1 1232 ? -11.09000  14.74600  19.02000  1.000 86.68928  ?  1230 TRP   A CA  1 
ATOM   9804  C  C   . TRP   A 1 1232 ? -10.87400  13.23900  19.02400  1.000 78.40742  ?  1230 TRP   A C   1 
ATOM   9805  O  O   . TRP   A 1 1232 ? -11.36200  12.54000  19.92100  1.000 63.72728  ?  1230 TRP   A O   1 
ATOM   9806  C  CB  . TRP   A 1 1232 ? -12.32500  15.10800  18.19300  1.000 83.31722  ?  1230 TRP   A CB  1 
ATOM   9807  C  CG  . TRP   A 1 1232 ? -12.85600  16.51600  18.38800  1.000 88.50572  ?  1230 TRP   A CG  1 
ATOM   9808  C  CD1 . TRP   A 1 1232 ? -13.41700  17.31000  17.42900  1.000 85.35291  ?  1230 TRP   A CD1 1 
ATOM   9809  C  CD2 . TRP   A 1 1232 ? -12.88700  17.28300  19.60700  1.000 94.78856  ?  1230 TRP   A CD2 1 
ATOM   9810  N  NE1 . TRP   A 1 1232 ? -13.79200  18.51600  17.96800  1.000 96.65309  ?  1230 TRP   A NE1 1 
ATOM   9811  C  CE2 . TRP   A 1 1232 ? -13.47700  18.52600  19.30100  1.000 98.30522  ?  1230 TRP   A CE2 1 
ATOM   9812  C  CE3 . TRP   A 1 1232 ? -12.47100  17.04200  20.92300  1.000 93.06618  ?  1230 TRP   A CE3 1 
ATOM   9813  C  CZ2 . TRP   A 1 1232 ? -13.66100  19.52100  20.26000  1.000 95.65072  ?  1230 TRP   A CZ2 1 
ATOM   9814  C  CZ3 . TRP   A 1 1232 ? -12.65700  18.03100  21.87000  1.000 94.71610  ?  1230 TRP   A CZ3 1 
ATOM   9815  C  CH2 . TRP   A 1 1232 ? -13.24500  19.25400  21.53500  1.000 86.59753  ?  1230 TRP   A CH2 1 
ATOM   9816  N  N   . ALA   A 1 1233 ? -10.15300  12.71500  18.03000  1.000 84.10398  ?  1231 ALA   A N   1 
ATOM   9817  C  CA  . ALA   A 1 1233 ? -9.91700   11.27500  17.97900  1.000 71.39682  ?  1231 ALA   A CA  1 
ATOM   9818  C  C   . ALA   A 1 1233 ? -9.07400   10.81300  19.15900  1.000 73.02194  ?  1231 ALA   A C   1 
ATOM   9819  O  O   . ALA   A 1 1233 ? -9.31800   9.74100   19.72300  1.000 82.40386  ?  1231 ALA   A O   1 
ATOM   9820  C  CB  . ALA   A 1 1233 ? -9.24900   10.89400  16.65800  1.000 65.01467  ?  1231 ALA   A CB  1 
ATOM   9821  N  N   . ALA   A 1 1234 ? -8.08200   11.61300  19.55500  1.000 78.30205  ?  1232 ALA   A N   1 
ATOM   9822  C  CA  . ALA   A 1 1234 ? -7.25400   11.24600  20.69800  1.000 74.78279  ?  1232 ALA   A CA  1 
ATOM   9823  C  C   . ALA   A 1 1234 ? -8.05300   11.23200  21.99500  1.000 81.80431  ?  1232 ALA   A C   1 
ATOM   9824  O  O   . ALA   A 1 1234 ? -7.73300   10.46200  22.90800  1.000 108.20858 ?  1232 ALA   A O   1 
ATOM   9825  C  CB  . ALA   A 1 1234 ? -6.06500   12.19900  20.81500  1.000 78.78264  ?  1232 ALA   A CB  1 
ATOM   9826  N  N   . ALA   A 1 1235 ? -9.09100   12.06400  22.09600  1.000 73.84661  ?  1233 ALA   A N   1 
ATOM   9827  C  CA  . ALA   A 1 1235 ? -9.89800   12.11000  23.31100  1.000 81.26484  ?  1233 ALA   A CA  1 
ATOM   9828  C  C   . ALA   A 1 1235 ? -10.92600  10.98400  23.34000  1.000 82.42749  ?  1233 ALA   A C   1 
ATOM   9829  O  O   . ALA   A 1 1235 ? -10.98000  10.20700  24.30000  1.000 94.35339  ?  1233 ALA   A O   1 
ATOM   9830  C  CB  . ALA   A 1 1235 ? -10.58700  13.47000  23.43300  1.000 85.55416  ?  1233 ALA   A CB  1 
ATOM   9831  N  N   . THR   A 1 1236 ? -11.75300  10.88200  22.29800  1.000 91.67140  ?  1234 THR   A N   1 
ATOM   9832  C  CA  . THR   A 1 1236 ? -12.77200  9.84200   22.18000  1.000 93.58923  ?  1234 THR   A CA  1 
ATOM   9833  C  C   . THR   A 1 1236 ? -12.43600  8.97700   20.97000  1.000 96.23195  ?  1234 THR   A C   1 
ATOM   9834  O  O   . THR   A 1 1236 ? -13.01000  9.15900   19.88500  1.000 92.37872  ?  1234 THR   A O   1 
ATOM   9835  C  CB  . THR   A 1 1236 ? -14.17000  10.44800  22.05800  1.000 74.94567  ?  1234 THR   A CB  1 
ATOM   9836  O  OG1 . THR   A 1 1236 ? -14.14700  11.51500  21.10100  1.000 80.20469  ?  1234 THR   A OG1 1 
ATOM   9837  C  CG2 . THR   A 1 1236 ? -14.63400  10.98800  23.40000  1.000 70.26535  ?  1234 THR   A CG2 1 
ATOM   9838  N  N   . PRO   A 1 1237 ? -11.51600  8.01900   21.11900  1.000 87.93052  ?  1235 PRO   A N   1 
ATOM   9839  C  CA  . PRO   A 1 1237 ? -11.10000  7.22900   19.95000  1.000 80.44992  ?  1235 PRO   A CA  1 
ATOM   9840  C  C   . PRO   A 1 1237 ? -12.14000  6.22600   19.49800  1.000 78.19206  ?  1235 PRO   A C   1 
ATOM   9841  O  O   . PRO   A 1 1237 ? -12.24800  5.96600   18.29400  1.000 79.25542  ?  1235 PRO   A O   1 
ATOM   9842  C  CB  . PRO   A 1 1237 ? -9.82200   6.53600   20.43900  1.000 73.07315  ?  1235 PRO   A CB  1 
ATOM   9843  C  CG  . PRO   A 1 1237 ? -10.02300  6.40300   21.91100  1.000 88.92663  ?  1235 PRO   A CG  1 
ATOM   9844  C  CD  . PRO   A 1 1237 ? -10.80200  7.61900   22.34500  1.000 74.50469  ?  1235 PRO   A CD  1 
ATOM   9845  N  N   . ASP   A 1 1238 ? -12.91200  5.65600   20.42200  1.000 79.79274  ?  1236 ASP   A N   1 
ATOM   9846  C  CA  . ASP   A 1 1238 ? -13.88700  4.62600   20.09900  1.000 90.44482  ?  1236 ASP   A CA  1 
ATOM   9847  C  C   . ASP   A 1 1238 ? -15.31400  5.16200   20.06900  1.000 85.99416  ?  1236 ASP   A C   1 
ATOM   9848  O  O   . ASP   A 1 1238 ? -16.26500  4.38600   20.21000  1.000 86.02735  ?  1236 ASP   A O   1 
ATOM   9849  C  CB  . ASP   A 1 1238 ? -13.76800  3.46800   21.09000  1.000 94.72547  ?  1236 ASP   A CB  1 
ATOM   9850  C  CG  . ASP   A 1 1238 ? -12.38100  2.85300   21.10000  1.000 90.51219  ?  1236 ASP   A CG  1 
ATOM   9851  O  OD1 . ASP   A 1 1238 ? -11.82500  2.62100   20.00500  1.000 86.68760  ?  1236 ASP   A OD1 1 
ATOM   9852  O  OD2 . ASP   A 1 1238 ? -11.84100  2.61300   22.20100  1.000 87.21901  -1 1236 ASP   A OD2 1 
ATOM   9853  N  N   . LYS   A 1 1239 ? -15.48200  6.46900   19.89100  1.000 84.97565  ?  1237 LYS   A N   1 
ATOM   9854  C  CA  . LYS   A 1 1239 ? -16.80100  7.05600   19.70800  1.000 72.13720  ?  1237 LYS   A CA  1 
ATOM   9855  C  C   . LYS   A 1 1239 ? -17.16100  7.03700   18.22900  1.000 77.49188  ?  1237 LYS   A C   1 
ATOM   9856  O  O   . LYS   A 1 1239 ? -16.29800  7.21700   17.36500  1.000 74.98767  ?  1237 LYS   A O   1 
ATOM   9857  C  CB  . LYS   A 1 1239 ? -16.84400  8.48900   20.24100  1.000 64.53187  ?  1237 LYS   A CB  1 
ATOM   9858  C  CG  . LYS   A 1 1239 ? -18.24600  9.08100   20.29500  1.000 70.83211  ?  1237 LYS   A CG  1 
ATOM   9859  C  CD  . LYS   A 1 1239 ? -18.23600  10.57300  20.00400  1.000 64.74557  ?  1237 LYS   A CD  1 
ATOM   9860  C  CE  . LYS   A 1 1239 ? -19.64400  11.14700  20.00800  1.000 61.06728  ?  1237 LYS   A CE  1 
ATOM   9861  N  NZ  . LYS   A 1 1239 ? -20.26900  11.07000  21.35600  1.000 69.82094  ?  1237 LYS   A NZ  1 
ATOM   9862  N  N   . THR   A 1 1240 ? -18.44200  6.81500   17.94300  1.000 72.99331  ?  1238 THR   A N   1 
ATOM   9863  C  CA  . THR   A 1 1240 ? -18.90200  6.71100   16.56300  1.000 70.85174  ?  1238 THR   A CA  1 
ATOM   9864  C  C   . THR   A 1 1240 ? -18.74900  8.05300   15.85500  1.000 74.27540  ?  1238 THR   A C   1 
ATOM   9865  O  O   . THR   A 1 1240 ? -19.29000  9.06800   16.30700  1.000 65.71550  ?  1238 THR   A O   1 
ATOM   9866  C  CB  . THR   A 1 1240 ? -20.35600  6.24900   16.52000  1.000 61.32165  ?  1238 THR   A CB  1 
ATOM   9867  O  OG1 . THR   A 1 1240 ? -20.52900  5.11900   17.38400  1.000 68.14284  ?  1238 THR   A OG1 1 
ATOM   9868  C  CG2 . THR   A 1 1240 ? -20.74000  5.85300   15.10300  1.000 55.50050  ?  1238 THR   A CG2 1 
ATOM   9869  N  N   . ALA   A 1 1241 ? -18.01200  8.05500   14.74700  1.000 61.57869  ?  1239 ALA   A N   1 
ATOM   9870  C  CA  . ALA   A 1 1241 ? -17.82600  9.24200   13.92000  1.000 48.30871  ?  1239 ALA   A CA  1 
ATOM   9871  C  C   . ALA   A 1 1241 ? -18.57600  9.17900   12.59900  1.000 58.81769  ?  1239 ALA   A C   1 
ATOM   9872  O  O   . ALA   A 1 1241 ? -19.20200  10.16400  12.20600  1.000 62.73101  ?  1239 ALA   A O   1 
ATOM   9873  C  CB  . ALA   A 1 1241 ? -16.33600  9.46700   13.64100  1.000 47.01688  ?  1239 ALA   A CB  1 
ATOM   9874  N  N   . LEU   A 1 1242 ? -18.52800  8.04700   11.90000  1.000 61.28417  ?  1240 LEU   A N   1 
ATOM   9875  C  CA  . LEU   A 1 1242 ? -19.23000  7.87600   10.63800  1.000 59.41252  ?  1240 LEU   A CA  1 
ATOM   9876  C  C   . LEU   A 1 1242 ? -20.18400  6.69300   10.72100  1.000 60.85177  ?  1240 LEU   A C   1 
ATOM   9877  O  O   . LEU   A 1 1242 ? -19.92100  5.70800   11.41800  1.000 63.73874  ?  1240 LEU   A O   1 
ATOM   9878  C  CB  . LEU   A 1 1242 ? -18.25900  7.65800   9.47100   1.000 38.43321  ?  1240 LEU   A CB  1 
ATOM   9879  C  CG  . LEU   A 1 1242 ? -17.30400  8.79100   9.09400   1.000 56.98872  ?  1240 LEU   A CG  1 
ATOM   9880  C  CD1 . LEU   A 1 1242 ? -16.84500  8.60900   7.65700   1.000 44.98356  ?  1240 LEU   A CD1 1 
ATOM   9881  C  CD2 . LEU   A 1 1242 ? -17.95100  10.15500  9.29000   1.000 53.37483  ?  1240 LEU   A CD2 1 
ATOM   9882  N  N   . VAL   A 1 1243 ? -21.29900  6.80200   9.99800   1.000 57.49026  ?  1241 VAL   A N   1 
ATOM   9883  C  CA  . VAL   A 1 1243 ? -22.27900  5.72600   9.89600   1.000 46.11288  ?  1241 VAL   A CA  1 
ATOM   9884  C  C   . VAL   A 1 1243 ? -22.73700  5.60900   8.44900   1.000 45.31540  ?  1241 VAL   A C   1 
ATOM   9885  O  O   . VAL   A 1 1243 ? -23.52900  6.42800   7.97000   1.000 62.46791  ?  1241 VAL   A O   1 
ATOM   9886  C  CB  . VAL   A 1 1243 ? -23.48400  5.96100   10.82800  1.000 48.39896  ?  1241 VAL   A CB  1 
ATOM   9887  C  CG1 . VAL   A 1 1243 ? -24.53700  4.88100   10.61400  1.000 46.07611  ?  1241 VAL   A CG1 1 
ATOM   9888  C  CG2 . VAL   A 1 1243 ? -23.05000  6.00200   12.28600  1.000 41.65595  ?  1241 VAL   A CG2 1 
ATOM   9889  N  N   . PHE   A 1 1244 ? -22.24300  4.59800   7.74000   1.000 47.43705  ?  1242 PHE   A N   1 
ATOM   9890  C  CA  . PHE   A 1 1244 ? -22.66800  4.31100   6.37600   1.000 42.46284  ?  1242 PHE   A CA  1 
ATOM   9891  C  C   . PHE   A 1 1244 ? -23.44800  3.00500   6.37800   1.000 47.53216  ?  1242 PHE   A C   1 
ATOM   9892  O  O   . PHE   A 1 1244 ? -22.92300  1.96600   6.79500   1.000 59.14978  ?  1242 PHE   A O   1 
ATOM   9893  C  CB  . PHE   A 1 1244 ? -21.47400  4.22900   5.42500   1.000 35.16524  ?  1242 PHE   A CB  1 
ATOM   9894  C  CG  . PHE   A 1 1244 ? -21.85900  4.04500   3.98400   1.000 43.51996  ?  1242 PHE   A CG  1 
ATOM   9895  C  CD1 . PHE   A 1 1244 ? -22.79000  4.88200   3.39200   1.000 49.80789  ?  1242 PHE   A CD1 1 
ATOM   9896  C  CD2 . PHE   A 1 1244 ? -21.28200  3.04600   3.21800   1.000 45.39441  ?  1242 PHE   A CD2 1 
ATOM   9897  C  CE1 . PHE   A 1 1244 ? -23.14600  4.72100   2.06600   1.000 56.75096  ?  1242 PHE   A CE1 1 
ATOM   9898  C  CE2 . PHE   A 1 1244 ? -21.63300  2.88000   1.89000   1.000 41.26946  ?  1242 PHE   A CE2 1 
ATOM   9899  C  CZ  . PHE   A 1 1244 ? -22.56600  3.71800   1.31400   1.000 46.45721  ?  1242 PHE   A CZ  1 
ATOM   9900  N  N   . ARG   A 1 1245 ? -24.69600  3.06400   5.90900   1.000 60.37754  ?  1243 ARG   A N   1 
ATOM   9901  C  CA  . ARG   A 1 1245 ? -25.60700  1.92600   5.94200   1.000 64.77329  ?  1243 ARG   A CA  1 
ATOM   9902  C  C   . ARG   A 1 1245 ? -25.72800  1.38200   7.36000   1.000 60.55466  ?  1243 ARG   A C   1 
ATOM   9903  O  O   . ARG   A 1 1245 ? -26.22600  2.07600   8.25200   1.000 71.71357  ?  1243 ARG   A O   1 
ATOM   9904  C  CB  . ARG   A 1 1245 ? -25.15200  0.84000   4.96300   1.000 50.59461  ?  1243 ARG   A CB  1 
ATOM   9905  C  CG  . ARG   A 1 1245 ? -25.66500  1.06800   3.54900   1.000 39.61840  ?  1243 ARG   A CG  1 
ATOM   9906  C  CD  . ARG   A 1 1245 ? -24.66100  0.65500   2.48900   1.000 47.34119  ?  1243 ARG   A CD  1 
ATOM   9907  N  NE  . ARG   A 1 1245 ? -25.09700  1.08100   1.16400   1.000 54.48371  ?  1243 ARG   A NE  1 
ATOM   9908  C  CZ  . ARG   A 1 1245 ? -24.40500  0.89700   0.04900   1.000 62.10710  ?  1243 ARG   A CZ  1 
ATOM   9909  N  NH1 . ARG   A 1 1245 ? -23.23100  0.28800   0.05700   1.000 60.69147  ?  1243 ARG   A NH1 1 
ATOM   9910  N  NH2 . ARG   A 1 1245 ? -24.90300  1.33700   -1.10400  1.000 67.54455  ?  1243 ARG   A NH2 1 
ATOM   9911  N  N   . GLU   A 1 1246 ? -25.27400  0.15000   7.58500   1.000 53.45271  ?  1244 GLU   A N   1 
ATOM   9912  C  CA  . GLU   A 1 1246 ? -25.34500  -0.46800  8.90300   1.000 68.12583  ?  1244 GLU   A CA  1 
ATOM   9913  C  C   . GLU   A 1 1246 ? -23.95700  -0.77000  9.45800   1.000 72.88113  ?  1244 GLU   A C   1 
ATOM   9914  O  O   . GLU   A 1 1246 ? -23.77300  -1.73700  10.20000  1.000 73.22232  ?  1244 GLU   A O   1 
ATOM   9915  C  CB  . GLU   A 1 1246 ? -26.20100  -1.73300  8.86200   1.000 75.02904  ?  1244 GLU   A CB  1 
ATOM   9916  C  CG  . GLU   A 1 1246 ? -27.67200  -1.47700  8.54900   1.000 86.22362  ?  1244 GLU   A CG  1 
ATOM   9917  C  CD  . GLU   A 1 1246 ? -28.37900  -0.68000  9.63400   1.000 90.78923  ?  1244 GLU   A CD  1 
ATOM   9918  O  OE1 . GLU   A 1 1246 ? -27.92500  -0.71300  10.79800  1.000 81.44735  ?  1244 GLU   A OE1 1 
ATOM   9919  O  OE2 . GLU   A 1 1246 ? -29.39300  -0.01900  9.32200   1.000 83.96771  -1 1244 GLU   A OE2 1 
ATOM   9920  N  N   . GLN   A 1 1247 ? -22.97300  0.05400   9.10700   1.000 63.02784  ?  1245 GLN   A N   1 
ATOM   9921  C  CA  . GLN   A 1 1247 ? -21.62400  -0.05300  9.64000   1.000 52.88617  ?  1245 GLN   A CA  1 
ATOM   9922  C  C   . GLN   A 1 1247 ? -21.21200  1.27700   10.25400  1.000 51.03836  ?  1245 GLN   A C   1 
ATOM   9923  O  O   . GLN   A 1 1247 ? -21.60100  2.34800   9.77700   1.000 39.78130  ?  1245 GLN   A O   1 
ATOM   9924  C  CB  . GLN   A 1 1247 ? -20.62500  -0.47100  8.55400   1.000 58.67465  ?  1245 GLN   A CB  1 
ATOM   9925  C  CG  . GLN   A 1 1247 ? -20.69200  -1.95000  8.20700   1.000 61.90370  ?  1245 GLN   A CG  1 
ATOM   9926  C  CD  . GLN   A 1 1247 ? -19.95900  -2.28700  6.92300   1.000 86.98439  ?  1245 GLN   A CD  1 
ATOM   9927  O  OE1 . GLN   A 1 1247 ? -18.79600  -1.92700  6.74100   1.000 87.96967  ?  1245 GLN   A OE1 1 
ATOM   9928  N  NE2 . GLN   A 1 1247 ? -20.64400  -2.98100  6.02100   1.000 88.26294  ?  1245 GLN   A NE2 1 
ATOM   9929  N  N   . ARG   A 1 1248 ? -20.42200  1.20000   11.32100  1.000 52.13293  ?  1246 ARG   A N   1 
ATOM   9930  C  CA  . ARG   A 1 1248 ? -20.01900  2.37000   12.08900  1.000 53.04790  ?  1246 ARG   A CA  1 
ATOM   9931  C  C   . ARG   A 1 1248 ? -18.50100  2.45000   12.14300  1.000 63.94535  ?  1246 ARG   A C   1 
ATOM   9932  O  O   . ARG   A 1 1248 ? -17.83100  1.45700   12.44600  1.000 63.52521  ?  1246 ARG   A O   1 
ATOM   9933  C  CB  . ARG   A 1 1248 ? -20.59200  2.31700   13.50700  1.000 54.65208  ?  1246 ARG   A CB  1 
ATOM   9934  C  CG  . ARG   A 1 1248 ? -22.07000  1.97600   13.56800  1.000 67.12809  ?  1246 ARG   A CG  1 
ATOM   9935  C  CD  . ARG   A 1 1248 ? -22.43800  1.49000   14.95400  1.000 77.56463  ?  1246 ARG   A CD  1 
ATOM   9936  N  NE  . ARG   A 1 1248 ? -21.44300  0.54900   15.45500  1.000 93.36695  ?  1246 ARG   A NE  1 
ATOM   9937  C  CZ  . ARG   A 1 1248 ? -21.49800  -0.04500  16.63800  1.000 98.38064  ?  1246 ARG   A CZ  1 
ATOM   9938  N  NH1 . ARG   A 1 1248 ? -22.50200  0.17100   17.47400  1.000 85.63138  ?  1246 ARG   A NH1 1 
ATOM   9939  N  NH2 . ARG   A 1 1248 ? -20.52300  -0.87700  16.99300  1.000 79.45648  ?  1246 ARG   A NH2 1 
ATOM   9940  N  N   . VAL   A 1 1249 ? -17.96600  3.63300   11.85500  1.000 59.38039  ?  1247 VAL   A N   1 
ATOM   9941  C  CA  . VAL   A 1 1249 ? -16.53600  3.90600   11.93900  1.000 45.21824  ?  1247 VAL   A CA  1 
ATOM   9942  C  C   . VAL   A 1 1249 ? -16.30000  4.82500   13.12900  1.000 49.07380  ?  1247 VAL   A C   1 
ATOM   9943  O  O   . VAL   A 1 1249 ? -17.01800  5.81700   13.30400  1.000 70.93352  ?  1247 VAL   A O   1 
ATOM   9944  C  CB  . VAL   A 1 1249 ? -16.00500  4.54000   10.64200  1.000 46.57540  ?  1247 VAL   A CB  1 
ATOM   9945  C  CG1 . VAL   A 1 1249 ? -14.50200  4.75100   10.72900  1.000 42.03065  ?  1247 VAL   A CG1 1 
ATOM   9946  C  CG2 . VAL   A 1 1249 ? -16.36200  3.67600   9.44000   1.000 38.23125  ?  1247 VAL   A CG2 1 
ATOM   9947  N  N   . THR   A 1 1250 ? -15.30200  4.49900   13.94300  1.000 51.11223  ?  1248 THR   A N   1 
ATOM   9948  C  CA  . THR   A 1 1250 ? -14.95600  5.32800   15.08600  1.000 60.89917  ?  1248 THR   A CA  1 
ATOM   9949  C  C   . THR   A 1 1250 ? -13.96300  6.41300   14.67100  1.000 60.99654  ?  1248 THR   A C   1 
ATOM   9950  O  O   . THR   A 1 1250 ? -13.37300  6.37100   13.58900  1.000 56.45207  ?  1248 THR   A O   1 
ATOM   9951  C  CB  . THR   A 1 1250 ? -14.38400  4.47700   16.22300  1.000 66.10534  ?  1248 THR   A CB  1 
ATOM   9952  O  OG1 . THR   A 1 1250 ? -13.01800  4.14900   15.94200  1.000 74.51901  ?  1248 THR   A OG1 1 
ATOM   9953  C  CG2 . THR   A 1 1250 ? -15.18000  3.19200   16.36700  1.000 59.39794  ?  1248 THR   A CG2 1 
ATOM   9954  N  N   . TYR   A 1 1251 ? -13.79600  7.40500   15.55100  1.000 61.70326  ?  1249 TYR   A N   1 
ATOM   9955  C  CA  . TYR   A 1 1251 ? -12.85800  8.49200   15.28100  1.000 69.94008  ?  1249 TYR   A CA  1 
ATOM   9956  C  C   . TYR   A 1 1251 ? -11.45200  7.95700   15.03400  1.000 62.33438  ?  1249 TYR   A C   1 
ATOM   9957  O  O   . TYR   A 1 1251 ? -10.77800  8.36400   14.07900  1.000 53.04241  ?  1249 TYR   A O   1 
ATOM   9958  C  CB  . TYR   A 1 1251 ? -12.85500  9.48400   16.44300  1.000 72.77968  ?  1249 TYR   A CB  1 
ATOM   9959  C  CG  . TYR   A 1 1251 ? -13.96200  10.51200  16.39300  1.000 75.54402  ?  1249 TYR   A CG  1 
ATOM   9960  C  CD1 . TYR   A 1 1251 ? -13.79600  11.70300  15.69800  1.000 70.49279  ?  1249 TYR   A CD1 1 
ATOM   9961  C  CD2 . TYR   A 1 1251 ? -15.16800  10.29900  17.04900  1.000 71.37092  ?  1249 TYR   A CD2 1 
ATOM   9962  C  CE1 . TYR   A 1 1251 ? -14.79900  12.64800  15.65200  1.000 73.93114  ?  1249 TYR   A CE1 1 
ATOM   9963  C  CE2 . TYR   A 1 1251 ? -16.17800  11.23900  17.00800  1.000 77.68937  ?  1249 TYR   A CE2 1 
ATOM   9964  C  CZ  . TYR   A 1 1251 ? -15.98800  12.41200  16.30800  1.000 72.24482  ?  1249 TYR   A CZ  1 
ATOM   9965  O  OH  . TYR   A 1 1251 ? -16.98800  13.35300  16.26200  1.000 57.22009  ?  1249 TYR   A OH  1 
ATOM   9966  N  N   . ARG   A 1 1252 ? -10.99600  7.03300   15.88500  1.000 60.02466  ?  1250 ARG   A N   1 
ATOM   9967  C  CA  . ARG   A 1 1252 ? -9.66000   6.46700   15.72800  1.000 59.44467  ?  1250 ARG   A CA  1 
ATOM   9968  C  C   . ARG   A 1 1252 ? -9.52700   5.72600   14.40400  1.000 59.95135  ?  1250 ARG   A C   1 
ATOM   9969  O  O   . ARG   A 1 1252 ? -8.54600   5.91000   13.67200  1.000 51.28968  ?  1250 ARG   A O   1 
ATOM   9970  C  CB  . ARG   A 1 1252 ? -9.34100   5.53500   16.89600  1.000 53.07751  ?  1250 ARG   A CB  1 
ATOM   9971  C  CG  . ARG   A 1 1252 ? -8.01900   4.81300   16.72200  1.000 72.23183  ?  1250 ARG   A CG  1 
ATOM   9972  C  CD  . ARG   A 1 1252 ? -7.39700   4.40900   18.04500  1.000 83.22595  ?  1250 ARG   A CD  1 
ATOM   9973  N  NE  . ARG   A 1 1252 ? -5.94500   4.37200   17.93600  1.000 105.43461 ?  1250 ARG   A NE  1 
ATOM   9974  C  CZ  . ARG   A 1 1252 ? -5.11800   5.14800   18.62600  1.000 111.22450 ?  1250 ARG   A CZ  1 
ATOM   9975  N  NH1 . ARG   A 1 1252 ? -5.56400   6.01800   19.52000  1.000 114.05852 ?  1250 ARG   A NH1 1 
ATOM   9976  N  NH2 . ARG   A 1 1252 ? -3.80900   5.03900   18.42300  1.000 100.38843 ?  1250 ARG   A NH2 1 
ATOM   9977  N  N   . GLU   A 1 1253 ? -10.50100  4.86800   14.08800  1.000 48.23879  ?  1251 GLU   A N   1 
ATOM   9978  C  CA  . GLU   A 1 1253 ? -10.48300  4.16600   12.80900  1.000 52.41679  ?  1251 GLU   A CA  1 
ATOM   9979  C  C   . GLU   A 1 1253 ? -10.47500  5.14700   11.64400  1.000 60.50640  ?  1251 GLU   A C   1 
ATOM   9980  O  O   . GLU   A 1 1253 ? -9.73300   4.96300   10.67200  1.000 66.17535  ?  1251 GLU   A O   1 
ATOM   9981  C  CB  . GLU   A 1 1253 ? -11.68500  3.23000   12.70700  1.000 55.81076  ?  1251 GLU   A CB  1 
ATOM   9982  C  CG  . GLU   A 1 1253 ? -11.74200  2.15900   13.78100  1.000 67.02585  ?  1251 GLU   A CG  1 
ATOM   9983  C  CD  . GLU   A 1 1253 ? -13.02600  1.35800   13.72400  1.000 70.99572  ?  1251 GLU   A CD  1 
ATOM   9984  O  OE1 . GLU   A 1 1253 ? -13.74000  1.46100   12.70600  1.000 74.36211  ?  1251 GLU   A OE1 1 
ATOM   9985  O  OE2 . GLU   A 1 1253 ? -13.32500  0.63300   14.69600  1.000 73.07614  -1 1251 GLU   A OE2 1 
ATOM   9986  N  N   . LEU   A 1 1254 ? -11.29600  6.19600   11.72600  1.000 58.70896  ?  1252 LEU   A N   1 
ATOM   9987  C  CA  . LEU   A 1 1254 ? -11.31000  7.21100   10.67800  1.000 52.18397  ?  1252 LEU   A CA  1 
ATOM   9988  C  C   . LEU   A 1 1254 ? -9.97500   7.94100   10.61000  1.000 61.12727  ?  1252 LEU   A C   1 
ATOM   9989  O  O   . LEU   A 1 1254 ? -9.38100   8.07300   9.53400   1.000 63.78768  ?  1252 LEU   A O   1 
ATOM   9990  C  CB  . LEU   A 1 1254 ? -12.45100  8.19800   10.91900  1.000 40.09044  ?  1252 LEU   A CB  1 
ATOM   9991  C  CG  . LEU   A 1 1254 ? -12.55200  9.34600   9.91300   1.000 40.05346  ?  1252 LEU   A CG  1 
ATOM   9992  C  CD1 . LEU   A 1 1254 ? -12.78000  8.81000   8.50700   1.000 39.01391  ?  1252 LEU   A CD1 1 
ATOM   9993  C  CD2 . LEU   A 1 1254 ? -13.65200  10.31900  10.31000  1.000 39.12527  ?  1252 LEU   A CD2 1 
ATOM   9994  N  N   . ASN   A 1 1255 ? -9.48300   8.41200   11.75900  1.000 44.49637  ?  1253 ASN   A N   1 
ATOM   9995  C  CA  . ASN   A 1 1255 ? -8.23700   9.17100   11.78000  1.000 55.36887  ?  1253 ASN   A CA  1 
ATOM   9996  C  C   . ASN   A 1 1255 ? -7.07500   8.33700   11.25200  1.000 66.15550  ?  1253 ASN   A C   1 
ATOM   9997  O  O   . ASN   A 1 1255 ? -6.30700   8.79500   10.39800  1.000 63.75814  ?  1253 ASN   A O   1 
ATOM   9998  C  CB  . ASN   A 1 1255 ? -7.95400   9.66500   13.20100  1.000 57.24391  ?  1253 ASN   A CB  1 
ATOM   9999  C  CG  . ASN   A 1 1255 ? -7.01400   10.85400  13.23100  1.000 70.10910  ?  1253 ASN   A CG  1 
ATOM   10000 O  OD1 . ASN   A 1 1255 ? -6.61300   11.37300  12.18900  1.000 82.10379  ?  1253 ASN   A OD1 1 
ATOM   10001 N  ND2 . ASN   A 1 1255 ? -6.66700   11.30100  14.43200  1.000 71.28631  ?  1253 ASN   A ND2 1 
ATOM   10002 N  N   . GLU   A 1 1256 ? -6.94500   7.09600   11.73100  1.000 62.14896  ?  1254 GLU   A N   1 
ATOM   10003 C  CA  . GLU   A 1 1256 ? -5.83900   6.24600   11.29700  1.000 59.24463  ?  1254 GLU   A CA  1 
ATOM   10004 C  C   . GLU   A 1 1256 ? -5.92500   5.93100   9.80800   1.000 58.73375  ?  1254 GLU   A C   1 
ATOM   10005 O  O   . GLU   A 1 1256 ? -4.91500   5.98100   9.09700   1.000 62.75363  ?  1254 GLU   A O   1 
ATOM   10006 C  CB  . GLU   A 1 1256 ? -5.81200   4.95600   12.11600  1.000 69.94747  ?  1254 GLU   A CB  1 
ATOM   10007 C  CG  . GLU   A 1 1256 ? -5.35200   5.14000   13.55200  1.000 76.23176  ?  1254 GLU   A CG  1 
ATOM   10008 C  CD  . GLU   A 1 1256 ? -5.25300   3.82700   14.30300  1.000 83.61412  ?  1254 GLU   A CD  1 
ATOM   10009 O  OE1 . GLU   A 1 1256 ? -5.93400   2.85800   13.90500  1.000 82.71157  ?  1254 GLU   A OE1 1 
ATOM   10010 O  OE2 . GLU   A 1 1256 ? -4.48800   3.76200   15.28800  1.000 93.39941  -1 1254 GLU   A OE2 1 
ATOM   10011 N  N   . ARG   A 1 1257 ? -7.12200   5.59700   9.31700   1.000 57.00875  ?  1255 ARG   A N   1 
ATOM   10012 C  CA  . ARG   A 1 1257 ? -7.28200   5.33400   7.89000   1.000 71.24762  ?  1255 ARG   A CA  1 
ATOM   10013 C  C   . ARG   A 1 1257 ? -6.97700   6.58000   7.06900   1.000 70.98033  ?  1255 ARG   A C   1 
ATOM   10014 O  O   . ARG   A 1 1257 ? -6.38700   6.49300   5.98600   1.000 62.42168  ?  1255 ARG   A O   1 
ATOM   10015 C  CB  . ARG   A 1 1257 ? -8.69900   4.83500   7.60400   1.000 61.56929  ?  1255 ARG   A CB  1 
ATOM   10016 C  CG  . ARG   A 1 1257 ? -8.89700   4.28500   6.19900   1.000 70.71735  ?  1255 ARG   A CG  1 
ATOM   10017 C  CD  . ARG   A 1 1257 ? -8.20400   2.94400   6.04300   1.000 79.03334  ?  1255 ARG   A CD  1 
ATOM   10018 N  NE  . ARG   A 1 1257 ? -8.16800   2.49700   4.65600   1.000 82.42686  ?  1255 ARG   A NE  1 
ATOM   10019 C  CZ  . ARG   A 1 1257 ? -7.51600   1.42200   4.23700   1.000 83.96269  ?  1255 ARG   A CZ  1 
ATOM   10020 N  NH1 . ARG   A 1 1257 ? -6.83400   0.65800   5.07500   1.000 77.59956  ?  1255 ARG   A NH1 1 
ATOM   10021 N  NH2 . ARG   A 1 1257 ? -7.54500   1.10700   2.94600   1.000 83.36327  ?  1255 ARG   A NH2 1 
ATOM   10022 N  N   . VAL   A 1 1258 ? -7.37000   7.75100   7.57500   1.000 73.93927  ?  1256 VAL   A N   1 
ATOM   10023 C  CA  . VAL   A 1 1258 ? -7.07500   9.00300   6.88700   1.000 83.66575  ?  1256 VAL   A CA  1 
ATOM   10024 C  C   . VAL   A 1 1258 ? -5.57600   9.28100   6.90100   1.000 74.03939  ?  1256 VAL   A C   1 
ATOM   10025 O  O   . VAL   A 1 1258 ? -5.00700   9.73700   5.90100   1.000 72.26007  ?  1256 VAL   A O   1 
ATOM   10026 C  CB  . VAL   A 1 1258 ? -7.88200   10.15300  7.52100   1.000 70.08330  ?  1256 VAL   A CB  1 
ATOM   10027 C  CG1 . VAL   A 1 1258 ? -7.32700   11.49900  7.10800   1.000 59.84876  ?  1256 VAL   A CG1 1 
ATOM   10028 C  CG2 . VAL   A 1 1258 ? -9.34700   10.05100  7.12400   1.000 58.38410  ?  1256 VAL   A CG2 1 
ATOM   10029 N  N   . ASN   A 1 1259 ? -4.91100   8.99500   8.02500   1.000 60.56877  ?  1257 ASN   A N   1 
ATOM   10030 C  CA  . ASN   A 1 1259 ? -3.46900   9.21300   8.11700   1.000 56.83774  ?  1257 ASN   A CA  1 
ATOM   10031 C  C   . ASN   A 1 1259 ? -2.71900   8.43000   7.04700   1.000 58.70878  ?  1257 ASN   A C   1 
ATOM   10032 O  O   . ASN   A 1 1259 ? -1.81600   8.96700   6.39500   1.000 69.74318  ?  1257 ASN   A O   1 
ATOM   10033 C  CB  . ASN   A 1 1259 ? -2.96200   8.82300   9.50600   1.000 49.72742  ?  1257 ASN   A CB  1 
ATOM   10034 C  CG  . ASN   A 1 1259 ? -3.53600   9.69300   10.60300  1.000 60.89455  ?  1257 ASN   A CG  1 
ATOM   10035 O  OD1 . ASN   A 1 1259 ? -3.98500   10.80900  10.35300  1.000 66.37166  ?  1257 ASN   A OD1 1 
ATOM   10036 N  ND2 . ASN   A 1 1259 ? -3.52700   9.18400   11.83000  1.000 57.68040  ?  1257 ASN   A ND2 1 
ATOM   10037 N  N   . GLN   A 1 1260 ? -3.08500   7.16200   6.84800   1.000 54.20810  ?  1258 GLN   A N   1 
ATOM   10038 C  CA  . GLN   A 1 1260 ? -2.37500   6.31800   5.89100   1.000 57.95290  ?  1258 GLN   A CA  1 
ATOM   10039 C  C   . GLN   A 1 1260 ? -2.46600   6.88300   4.47900   1.000 66.77819  ?  1258 GLN   A C   1 
ATOM   10040 O  O   . GLN   A 1 1260 ? -1.45500   6.99000   3.77500   1.000 80.05297  ?  1258 GLN   A O   1 
ATOM   10041 C  CB  . GLN   A 1 1260 ? -2.93300   4.89700   5.94000   1.000 79.05449  ?  1258 GLN   A CB  1 
ATOM   10042 C  CG  . GLN   A 1 1260 ? -2.88700   4.26900   7.32000   1.000 86.41423  ?  1258 GLN   A CG  1 
ATOM   10043 C  CD  . GLN   A 1 1260 ? -3.56700   2.91800   7.36200   1.000 81.42712  ?  1258 GLN   A CD  1 
ATOM   10044 O  OE1 . GLN   A 1 1260 ? -3.96900   2.38200   6.32900   1.000 72.72420  ?  1258 GLN   A OE1 1 
ATOM   10045 N  NE2 . GLN   A 1 1260 ? -3.70100   2.36100   8.55900   1.000 76.24140  ?  1258 GLN   A NE2 1 
ATOM   10046 N  N   . LEU   A 1 1261 ? -3.67500   7.24800   4.04500   1.000 75.89278  ?  1259 LEU   A N   1 
ATOM   10047 C  CA  . LEU   A 1 1261 ? -3.83300   7.83100   2.71800   1.000 75.89981  ?  1259 LEU   A CA  1 
ATOM   10048 C  C   . LEU   A 1 1261 ? -3.12500   9.17600   2.61400   1.000 71.76798  ?  1259 LEU   A C   1 
ATOM   10049 O  O   . LEU   A 1 1261 ? -2.70000   9.57200   1.52300   1.000 62.57668  ?  1259 LEU   A O   1 
ATOM   10050 C  CB  . LEU   A 1 1261 ? -5.31800   7.97500   2.38100   1.000 71.00775  ?  1259 LEU   A CB  1 
ATOM   10051 C  CG  . LEU   A 1 1261 ? -5.66500   8.44900   0.96900   1.000 60.02093  ?  1259 LEU   A CG  1 
ATOM   10052 C  CD1 . LEU   A 1 1261 ? -4.96700   7.58900   -0.07000  1.000 55.96643  ?  1259 LEU   A CD1 1 
ATOM   10053 C  CD2 . LEU   A 1 1261 ? -7.16900   8.43300   0.75600   1.000 68.21735  ?  1259 LEU   A CD2 1 
ATOM   10054 N  N   . ALA   A 1 1262 ? -2.98300   9.88500   3.73600   1.000 69.16161  ?  1260 ALA   A N   1 
ATOM   10055 C  CA  . ALA   A 1 1262 ? -2.23400   11.13700  3.73100   1.000 73.61138  ?  1260 ALA   A CA  1 
ATOM   10056 C  C   . ALA   A 1 1262 ? -0.76100   10.88900  3.43400   1.000 79.24685  ?  1260 ALA   A C   1 
ATOM   10057 O  O   . ALA   A 1 1262 ? -0.17800   11.53700  2.55600   1.000 70.23071  ?  1260 ALA   A O   1 
ATOM   10058 C  CB  . ALA   A 1 1262 ? -2.40600   11.85700  5.07000   1.000 54.13769  ?  1260 ALA   A CB  1 
ATOM   10059 N  N   . HIS   A 1 1263 ? -0.14200   9.94900   4.15600   1.000 76.14388  ?  1261 HIS   A N   1 
ATOM   10060 C  CA  . HIS   A 1 1263 ? 1.25800    9.61900   3.90400   1.000 49.33965  ?  1261 HIS   A CA  1 
ATOM   10061 C  C   . HIS   A 1 1263 ? 1.46200    9.15400   2.46900   1.000 47.34734  ?  1261 HIS   A C   1 
ATOM   10062 O  O   . HIS   A 1 1263 ? 2.44200    9.53400   1.81800   1.000 70.40300  ?  1261 HIS   A O   1 
ATOM   10063 C  CB  . HIS   A 1 1263 ? 1.73500    8.54300   4.87900   1.000 40.95542  ?  1261 HIS   A CB  1 
ATOM   10064 C  CG  . HIS   A 1 1263 ? 1.51200    8.88400   6.32000   1.000 45.50500  ?  1261 HIS   A CG  1 
ATOM   10065 N  ND1 . HIS   A 1 1263 ? 2.00800    10.03100  6.90000   1.000 52.27712  ?  1261 HIS   A ND1 1 
ATOM   10066 C  CD2 . HIS   A 1 1263 ? 0.85800    8.21900   7.30000   1.000 59.61625  ?  1261 HIS   A CD2 1 
ATOM   10067 C  CE1 . HIS   A 1 1263 ? 1.65900    10.06300  8.17400   1.000 65.02416  ?  1261 HIS   A CE1 1 
ATOM   10068 N  NE2 . HIS   A 1 1263 ? 0.96000    8.97500   8.44200   1.000 54.54494  ?  1261 HIS   A NE2 1 
ATOM   10069 N  N   . THR   A 1 1264 ? 0.54200    8.33200   1.95700   1.000 42.24337  ?  1262 THR   A N   1 
ATOM   10070 C  CA  . THR   A 1 1264 ? 0.64500    7.87900   0.57500   1.000 69.82205  ?  1262 THR   A CA  1 
ATOM   10071 C  C   . THR   A 1 1264 ? 0.49100    9.03700   -0.40200  1.000 74.14468  ?  1262 THR   A C   1 
ATOM   10072 O  O   . THR   A 1 1264 ? 0.98900    8.96800   -1.53300  1.000 62.75635  ?  1262 THR   A O   1 
ATOM   10073 C  CB  . THR   A 1 1264 ? -0.40500   6.80500   0.29200   1.000 75.86233  ?  1262 THR   A CB  1 
ATOM   10074 O  OG1 . THR   A 1 1264 ? -0.53000   5.94500   1.43100   1.000 74.24133  ?  1262 THR   A OG1 1 
ATOM   10075 C  CG2 . THR   A 1 1264 ? -0.00000   5.97100   -0.91500  1.000 63.32967  ?  1262 THR   A CG2 1 
ATOM   10076 N  N   . LEU   A 1 1265 ? -0.19100   10.10700  0.01300   1.000 75.46652  ?  1263 LEU   A N   1 
ATOM   10077 C  CA  . LEU   A 1 1265 ? -0.31500   11.28500  -0.83700  1.000 86.11393  ?  1263 LEU   A CA  1 
ATOM   10078 C  C   . LEU   A 1 1265 ? 0.92800    12.16400  -0.76400  1.000 80.99535  ?  1263 LEU   A C   1 
ATOM   10079 O  O   . LEU   A 1 1265 ? 1.37300    12.69500  -1.78800  1.000 71.83621  ?  1263 LEU   A O   1 
ATOM   10080 C  CB  . LEU   A 1 1265 ? -1.55900   12.08700  -0.45100  1.000 78.11620  ?  1263 LEU   A CB  1 
ATOM   10081 C  CG  . LEU   A 1 1265 ? -2.87000   11.64400  -1.10200  1.000 70.65183  ?  1263 LEU   A CG  1 
ATOM   10082 C  CD1 . LEU   A 1 1265 ? -3.98900   12.62400  -0.78300  1.000 69.51414  ?  1263 LEU   A CD1 1 
ATOM   10083 C  CD2 . LEU   A 1 1265 ? -2.69000   11.50200  -2.60400  1.000 59.33320  ?  1263 LEU   A CD2 1 
ATOM   10084 N  N   . ARG   A 1 1266 ? 1.49900    12.32400  0.43400   1.000 74.37261  ?  1264 ARG   A N   1 
ATOM   10085 C  CA  . ARG   A 1 1266 ? 2.69000    13.15500  0.59000   1.000 67.79220  ?  1264 ARG   A CA  1 
ATOM   10086 C  C   . ARG   A 1 1266 ? 3.83400    12.65300  -0.28200  1.000 70.58088  ?  1264 ARG   A C   1 
ATOM   10087 O  O   . ARG   A 1 1266 ? 4.56600    13.45000  -0.88100  1.000 71.32617  ?  1264 ARG   A O   1 
ATOM   10088 C  CB  . ARG   A 1 1266 ? 3.11600    13.18900  2.05800   1.000 44.04787  ?  1264 ARG   A CB  1 
ATOM   10089 C  CG  . ARG   A 1 1266 ? 2.06100    13.73300  3.00200   1.000 47.81096  ?  1264 ARG   A CG  1 
ATOM   10090 C  CD  . ARG   A 1 1266 ? 2.49900    13.57800  4.44500   1.000 58.32314  ?  1264 ARG   A CD  1 
ATOM   10091 N  NE  . ARG   A 1 1266 ? 3.78600    14.21900  4.68600   1.000 73.53759  ?  1264 ARG   A NE  1 
ATOM   10092 C  CZ  . ARG   A 1 1266 ? 3.93300    15.45300  5.14600   1.000 78.71840  ?  1264 ARG   A CZ  1 
ATOM   10093 N  NH1 . ARG   A 1 1266 ? 2.88800    16.20800  5.44700   1.000 86.03892  ?  1264 ARG   A NH1 1 
ATOM   10094 N  NH2 . ARG   A 1 1266 ? 5.15900    15.94300  5.31100   1.000 68.92035  ?  1264 ARG   A NH2 1 
ATOM   10095 N  N   . GLU   A 1 1267 ? 3.99900    11.33100  -0.37100  1.000 65.95286  ?  1265 GLU   A N   1 
ATOM   10096 C  CA  . GLU   A 1 1267 ? 5.03900    10.74100  -1.20300  1.000 82.50136  ?  1265 GLU   A CA  1 
ATOM   10097 C  C   . GLU   A 1 1267 ? 4.74400    10.86600  -2.69100  1.000 80.23380  ?  1265 GLU   A C   1 
ATOM   10098 O  O   . GLU   A 1 1267 ? 5.60500    10.52000  -3.50700  1.000 87.95891  ?  1265 GLU   A O   1 
ATOM   10099 C  CB  . GLU   A 1 1267 ? 5.22600    9.27200   -0.82700  1.000 95.90545  ?  1265 GLU   A CB  1 
ATOM   10100 C  CG  . GLU   A 1 1267 ? 5.49900    9.05100   0.65100   1.000 91.54139  ?  1265 GLU   A CG  1 
ATOM   10101 C  CD  . GLU   A 1 1267 ? 5.30800    7.60700   1.06600   1.000 102.77165 ?  1265 GLU   A CD  1 
ATOM   10102 O  OE1 . GLU   A 1 1267 ? 4.84100    6.80400   0.23100   1.000 74.63155  ?  1265 GLU   A OE1 1 
ATOM   10103 O  OE2 . GLU   A 1 1267 ? 5.62400    7.27500   2.22800   1.000 95.20355  -1 1265 GLU   A OE2 1 
ATOM   10104 N  N   . LYS   A 1 1268 ? 3.55700    11.34000  -3.06200  1.000 78.05802  ?  1266 LYS   A N   1 
ATOM   10105 C  CA  . LYS   A 1 1268 ? 3.22500    11.63100  -4.44800  1.000 86.99879  ?  1266 LYS   A CA  1 
ATOM   10106 C  C   . LYS   A 1 1268 ? 3.39600    13.10400  -4.79400  1.000 84.26189  ?  1266 LYS   A C   1 
ATOM   10107 O  O   . LYS   A 1 1268 ? 3.11300    13.49900  -5.93000  1.000 73.41389  ?  1266 LYS   A O   1 
ATOM   10108 C  CB  . LYS   A 1 1268 ? 1.79000    11.19000  -4.75200  1.000 79.44690  ?  1266 LYS   A CB  1 
ATOM   10109 C  CG  . LYS   A 1 1268 ? 1.59800    9.68500   -4.70900  1.000 67.16956  ?  1266 LYS   A CG  1 
ATOM   10110 C  CD  . LYS   A 1 1268 ? 2.57000    9.01100   -5.66400  1.000 84.58965  ?  1266 LYS   A CD  1 
ATOM   10111 C  CE  . LYS   A 1 1268 ? 2.15600    7.58600   -5.99000  1.000 80.83879  ?  1266 LYS   A CE  1 
ATOM   10112 N  NZ  . LYS   A 1 1268 ? 2.85500    7.07500   -7.20300  1.000 60.33381  ?  1266 LYS   A NZ  1 
ATOM   10113 N  N   . GLY   A 1 1269 ? 3.85000    13.92400  -3.84700  1.000 73.96234  ?  1267 GLY   A N   1 
ATOM   10114 C  CA  . GLY   A 1 1269 ? 4.06400    15.33500  -4.10200  1.000 77.43595  ?  1267 GLY   A CA  1 
ATOM   10115 C  C   . GLY   A 1 1269 ? 2.87900    16.21900  -3.77200  1.000 97.53648  ?  1267 GLY   A C   1 
ATOM   10116 O  O   . GLY   A 1 1269 ? 2.54000    17.12000  -4.54300  1.000 96.67936  ?  1267 GLY   A O   1 
ATOM   10117 N  N   . VAL   A 1 1270 ? 2.23900    15.97600  -2.63100  1.000 101.09855 ?  1268 VAL   A N   1 
ATOM   10118 C  CA  . VAL   A 1 1270 ? 1.13400    16.81000  -2.17000  1.000 89.73769  ?  1268 VAL   A CA  1 
ATOM   10119 C  C   . VAL   A 1 1270 ? 1.72200    17.88300  -1.26000  1.000 88.46084  ?  1268 VAL   A C   1 
ATOM   10120 O  O   . VAL   A 1 1270 ? 2.04600    17.63300  -0.09700  1.000 56.29018  ?  1268 VAL   A O   1 
ATOM   10121 C  CB  . VAL   A 1 1270 ? 0.05000    15.99500  -1.46400  1.000 80.93892  ?  1268 VAL   A CB  1 
ATOM   10122 C  CG1 . VAL   A 1 1270 ? -0.96800   16.93000  -0.82600  1.000 72.40031  ?  1268 VAL   A CG1 1 
ATOM   10123 C  CG2 . VAL   A 1 1270 ? -0.63600   15.07500  -2.45600  1.000 75.02235  ?  1268 VAL   A CG2 1 
ATOM   10124 N  N   . GLN   A 1 1271 ? 1.86900    19.08500  -1.80500  1.000 97.15724  ?  1269 GLN   A N   1 
ATOM   10125 C  CA  . GLN   A 1 1271 ? 2.32100    20.29900  -1.15600  1.000 89.40919  ?  1269 GLN   A CA  1 
ATOM   10126 C  C   . GLN   A 1 1271 ? 1.14900    21.26200  -0.98700  1.000 84.33693  ?  1269 GLN   A C   1 
ATOM   10127 O  O   . GLN   A 1 1271 ? 0.15500    21.16400  -1.71500  1.000 77.96219  ?  1269 GLN   A O   1 
ATOM   10128 C  CB  . GLN   A 1 1271 ? 3.43400    20.96300  -1.97600  1.000 85.63331  ?  1269 GLN   A CB  1 
ATOM   10129 C  CG  . GLN   A 1 1271 ? 3.31400    20.70400  -3.47300  1.000 90.24451  ?  1269 GLN   A CG  1 
ATOM   10130 C  CD  . GLN   A 1 1271 ? 4.60600    20.20000  -4.09800  1.000 90.68094  ?  1269 GLN   A CD  1 
ATOM   10131 O  OE1 . GLN   A 1 1271 ? 5.69200    20.70400  -3.80900  1.000 72.10542  ?  1269 GLN   A OE1 1 
ATOM   10132 N  NE2 . GLN   A 1 1271 ? 4.49000    19.19900  -4.96400  1.000 87.67956  ?  1269 GLN   A NE2 1 
ATOM   10133 N  N   . PRO   A 1 1272 ? 1.21300    22.17500  -0.01700  1.000 72.28082  ?  1270 PRO   A N   1 
ATOM   10134 C  CA  . PRO   A 1 1272 ? 0.09300    23.09700  0.19900   1.000 65.28234  ?  1270 PRO   A CA  1 
ATOM   10135 C  C   . PRO   A 1 1272 ? -0.28300   23.84900  -1.07200  1.000 55.22982  ?  1270 PRO   A C   1 
ATOM   10136 O  O   . PRO   A 1 1272 ? 0.56500    24.16100  -1.91200  1.000 47.30492  ?  1270 PRO   A O   1 
ATOM   10137 C  CB  . PRO   A 1 1272 ? 0.61900    24.03600  1.28700   1.000 50.65452  ?  1270 PRO   A CB  1 
ATOM   10138 C  CG  . PRO   A 1 1272 ? 1.54500    23.17300  2.07400   1.000 46.04899  ?  1270 PRO   A CG  1 
ATOM   10139 C  CD  . PRO   A 1 1272 ? 2.18800    22.22800  1.08500   1.000 68.29424  ?  1270 PRO   A CD  1 
ATOM   10140 N  N   . ASP   A 1 1273 ? -1.58600   24.10100  -1.21200  1.000 62.63732  ?  1271 ASP   A N   1 
ATOM   10141 C  CA  . ASP   A 1 1273 ? -2.20600   24.73200  -2.37300  1.000 67.89648  ?  1271 ASP   A CA  1 
ATOM   10142 C  C   . ASP   A 1 1273 ? -2.06600   23.91200  -3.64900  1.000 68.88003  ?  1271 ASP   A C   1 
ATOM   10143 O  O   . ASP   A 1 1273 ? -2.24900   24.45100  -4.74700  1.000 64.99468  ?  1271 ASP   A O   1 
ATOM   10144 C  CB  . ASP   A 1 1273 ? -1.67000   26.14800  -2.60700  1.000 80.76282  ?  1271 ASP   A CB  1 
ATOM   10145 C  CG  . ASP   A 1 1273 ? -2.29400   27.16100  -1.68000  1.000 75.60716  ?  1271 ASP   A CG  1 
ATOM   10146 O  OD1 . ASP   A 1 1273 ? -2.93900   26.75300  -0.69000  1.000 75.29089  ?  1271 ASP   A OD1 1 
ATOM   10147 O  OD2 . ASP   A 1 1273 ? -2.14000   28.36800  -1.95200  1.000 70.15679  -1 1271 ASP   A OD2 1 
ATOM   10148 N  N   . ASP   A 1 1274 ? -1.74900   22.62500  -3.53800  1.000 71.67048  ?  1272 ASP   A N   1 
ATOM   10149 C  CA  . ASP   A 1 1274 ? -1.86800   21.69700  -4.65600  1.000 63.23655  ?  1272 ASP   A CA  1 
ATOM   10150 C  C   . ASP   A 1 1274 ? -3.24800   21.05600  -4.64400  1.000 61.00317  ?  1272 ASP   A C   1 
ATOM   10151 O  O   . ASP   A 1 1274 ? -3.83700   20.82300  -3.58400  1.000 57.62854  ?  1272 ASP   A O   1 
ATOM   10152 C  CB  . ASP   A 1 1274 ? -0.79700   20.60500  -4.59900  1.000 78.09301  ?  1272 ASP   A CB  1 
ATOM   10153 C  CG  . ASP   A 1 1274 ? 0.23800    20.74300  -5.69700  1.000 85.41738  ?  1272 ASP   A CG  1 
ATOM   10154 O  OD1 . ASP   A 1 1274 ? 0.12500    21.68400  -6.51100  1.000 83.32736  ?  1272 ASP   A OD1 1 
ATOM   10155 O  OD2 . ASP   A 1 1274 ? 1.16900    19.90900  -5.74100  1.000 86.48819  -1 1272 ASP   A OD2 1 
ATOM   10156 N  N   . LEU   A 1 1275 ? -3.75600   20.75600  -5.83400  1.000 64.07100  ?  1273 LEU   A N   1 
ATOM   10157 C  CA  . LEU   A 1 1275 ? -5.11100   20.25000  -6.00800  1.000 69.08864  ?  1273 LEU   A CA  1 
ATOM   10158 C  C   . LEU   A 1 1275 ? -5.06600   18.81300  -6.50700  1.000 75.29765  ?  1273 LEU   A C   1 
ATOM   10159 O  O   . LEU   A 1 1275 ? -4.30500   18.49600  -7.42600  1.000 90.33597  ?  1273 LEU   A O   1 
ATOM   10160 C  CB  . LEU   A 1 1275 ? -5.89200   21.12600  -6.99200  1.000 51.27452  ?  1273 LEU   A CB  1 
ATOM   10161 C  CG  . LEU   A 1 1275 ? -5.74500   22.64100  -6.81900  1.000 65.77618  ?  1273 LEU   A CG  1 
ATOM   10162 C  CD1 . LEU   A 1 1275 ? -6.53200   23.38900  -7.89000  1.000 57.04862  ?  1273 LEU   A CD1 1 
ATOM   10163 C  CD2 . LEU   A 1 1275 ? -6.16600   23.08600  -5.42100  1.000 61.27933  ?  1273 LEU   A CD2 1 
ATOM   10164 N  N   . VAL   A 1 1276 ? -5.87200   17.94500  -5.89900  1.000 64.73232  ?  1274 VAL   A N   1 
ATOM   10165 C  CA  . VAL   A 1 1276 ? -6.08200   16.58900  -6.39000  1.000 67.68381  ?  1274 VAL   A CA  1 
ATOM   10166 C  C   . VAL   A 1 1276 ? -7.57900   16.36400  -6.52300  1.000 53.29499  ?  1274 VAL   A C   1 
ATOM   10167 O  O   . VAL   A 1 1276 ? -8.34100   16.63700  -5.58800  1.000 49.93847  ?  1274 VAL   A O   1 
ATOM   10168 C  CB  . VAL   A 1 1276 ? -5.44700   15.52700  -5.47200  1.000 71.30562  ?  1274 VAL   A CB  1 
ATOM   10169 C  CG1 . VAL   A 1 1276 ? -5.79600   15.80600  -4.04300  1.000 44.39219  ?  1274 VAL   A CG1 1 
ATOM   10170 C  CG2 . VAL   A 1 1276 ? -5.93800   14.14300  -5.84300  1.000 76.60791  ?  1274 VAL   A CG2 1 
ATOM   10171 N  N   . MET   A 1 1277 ? -7.99400   15.87600  -7.68500  1.000 58.45920  ?  1275 MET   A N   1 
ATOM   10172 C  CA  . MET   A 1 1277 ? -9.39300   15.66800  -8.00200  1.000 51.62005  ?  1275 MET   A CA  1 
ATOM   10173 C  C   . MET   A 1 1277 ? -9.90900   14.39500  -7.33900  1.000 61.02813  ?  1275 MET   A C   1 
ATOM   10174 O  O   . MET   A 1 1277 ? -9.15300   13.46700  -7.03900  1.000 69.47715  ?  1275 MET   A O   1 
ATOM   10175 C  CB  . MET   A 1 1277 ? -9.56800   15.59200  -9.51600  1.000 54.56171  ?  1275 MET   A CB  1 
ATOM   10176 C  CG  . MET   A 1 1277 ? -8.57400   16.46800  -10.26800 1.000 62.70582  ?  1275 MET   A CG  1 
ATOM   10177 S  SD  . MET   A 1 1277 ? -8.66800   16.25900  -12.05200 1.000 106.66926 ?  1275 MET   A SD  1 
ATOM   10178 C  CE  . MET   A 1 1277 ? -10.43900  16.31100  -12.28900 1.000 74.35496  ?  1275 MET   A CE  1 
ATOM   10179 N  N   . LEU   A 1 1278 ? -11.21900  14.36300  -7.11000  1.000 59.71534  ?  1276 LEU   A N   1 
ATOM   10180 C  CA  . LEU   A 1 1278 ? -11.87500  13.23700  -6.46100  1.000 42.97857  ?  1276 LEU   A CA  1 
ATOM   10181 C  C   . LEU   A 1 1278 ? -13.01200  12.73900  -7.33800  1.000 56.16463  ?  1276 LEU   A C   1 
ATOM   10182 O  O   . LEU   A 1 1278 ? -13.86000  13.52800  -7.76900  1.000 63.11090  ?  1276 LEU   A O   1 
ATOM   10183 C  CB  . LEU   A 1 1278 ? -12.40500  13.62500  -5.07700  1.000 31.28560  ?  1276 LEU   A CB  1 
ATOM   10184 C  CG  . LEU   A 1 1278 ? -11.50900  13.32000  -3.87300  1.000 49.30259  ?  1276 LEU   A CG  1 
ATOM   10185 C  CD1 . LEU   A 1 1278 ? -10.19700  14.08700  -3.94200  1.000 47.34577  ?  1276 LEU   A CD1 1 
ATOM   10186 C  CD2 . LEU   A 1 1278 ? -12.24200  13.62600  -2.57800  1.000 39.16617  ?  1276 LEU   A CD2 1 
ATOM   10187 N  N   . MET   A 1 1279 ? -13.02800  11.43100  -7.59800  1.000 55.78012  ?  1277 MET   A N   1 
ATOM   10188 C  CA  . MET   A 1 1279 ? -14.08600  10.77300  -8.36600  1.000 58.83356  ?  1277 MET   A CA  1 
ATOM   10189 C  C   . MET   A 1 1279 ? -14.59900  9.60600   -7.52700  1.000 54.29400  ?  1277 MET   A C   1 
ATOM   10190 O  O   . MET   A 1 1279 ? -14.13000  8.47400   -7.66900  1.000 63.25613  ?  1277 MET   A O   1 
ATOM   10191 C  CB  . MET   A 1 1279 ? -13.57800  10.31600  -9.72900  1.000 49.86817  ?  1277 MET   A CB  1 
ATOM   10192 C  CG  . MET   A 1 1279 ? -14.14300  11.11000  -10.89400 1.000 71.07921  ?  1277 MET   A CG  1 
ATOM   10193 S  SD  . MET   A 1 1279 ? -13.44000  10.62600  -12.48200 1.000 84.50804  ?  1277 MET   A SD  1 
ATOM   10194 C  CE  . MET   A 1 1279 ? -11.77900  11.26900  -12.32600 1.000 64.28589  ?  1277 MET   A CE  1 
ATOM   10195 N  N   . ALA   A 1 1280 ? -15.56200  9.88600   -6.65300  1.000 52.66363  ?  1278 ALA   A N   1 
ATOM   10196 C  CA  . ALA   A 1 1280 ? -16.10400  8.87100   -5.76300  1.000 59.68284  ?  1278 ALA   A CA  1 
ATOM   10197 C  C   . ALA   A 1 1280 ? -17.56900  9.17000   -5.49200  1.000 61.60822  ?  1278 ALA   A C   1 
ATOM   10198 O  O   . ALA   A 1 1280 ? -18.03800  10.29900  -5.66200  1.000 60.45167  ?  1278 ALA   A O   1 
ATOM   10199 C  CB  . ALA   A 1 1280 ? -15.32400  8.80100   -4.44400  1.000 40.90308  ?  1278 ALA   A CB  1 
ATOM   10200 N  N   . GLU   A 1 1281 ? -18.29000  8.13800   -5.07000  1.000 59.13716  ?  1279 GLU   A N   1 
ATOM   10201 C  CA  . GLU   A 1 1281 ? -19.67600  8.27100   -4.65700  1.000 53.28589  ?  1279 GLU   A CA  1 
ATOM   10202 C  C   . GLU   A 1 1281 ? -19.76700  8.22600   -3.13600  1.000 52.41553  ?  1279 GLU   A C   1 
ATOM   10203 O  O   . GLU   A 1 1281 ? -18.78500  7.96600   -2.43600  1.000 58.01878  ?  1279 GLU   A O   1 
ATOM   10204 C  CB  . GLU   A 1 1281 ? -20.53700  7.17600   -5.29500  1.000 54.08436  ?  1279 GLU   A CB  1 
ATOM   10205 C  CG  . GLU   A 1 1281 ? -20.44600  7.15100   -6.81400  1.000 71.69523  ?  1279 GLU   A CG  1 
ATOM   10206 C  CD  . GLU   A 1 1281 ? -21.69100  6.59000   -7.47300  1.000 82.72349  ?  1279 GLU   A CD  1 
ATOM   10207 O  OE1 . GLU   A 1 1281 ? -21.96900  5.38400   -7.30600  1.000 78.96540  ?  1279 GLU   A OE1 1 
ATOM   10208 O  OE2 . GLU   A 1 1281 ? -22.39600  7.36300   -8.15600  1.000 87.41898  -1 1279 GLU   A OE2 1 
ATOM   10209 N  N   . ARG   A 1 1282 ? -20.96900  8.50000   -2.62600  1.000 46.34238  ?  1280 ARG   A N   1 
ATOM   10210 C  CA  . ARG   A 1 1282 ? -21.19800  8.56800   -1.18700  1.000 52.06015  ?  1280 ARG   A CA  1 
ATOM   10211 C  C   . ARG   A 1 1282 ? -20.77200  7.27400   -0.50500  1.000 57.73250  ?  1280 ARG   A C   1 
ATOM   10212 O  O   . ARG   A 1 1282 ? -21.37900  6.22000   -0.72000  1.000 65.79949  ?  1280 ARG   A O   1 
ATOM   10213 C  CB  . ARG   A 1 1282 ? -22.67000  8.87000   -0.89800  1.000 62.33531  ?  1280 ARG   A CB  1 
ATOM   10214 C  CG  . ARG   A 1 1282 ? -22.89100  10.05500  0.02800   1.000 60.51572  ?  1280 ARG   A CG  1 
ATOM   10215 C  CD  . ARG   A 1 1282 ? -23.96200  10.97700  -0.52400  1.000 51.36867  ?  1280 ARG   A CD  1 
ATOM   10216 N  NE  . ARG   A 1 1282 ? -25.21300  10.27000  -0.76700  1.000 58.02695  ?  1280 ARG   A NE  1 
ATOM   10217 C  CZ  . ARG   A 1 1282 ? -26.16100  10.69100  -1.59200  1.000 64.71853  ?  1280 ARG   A CZ  1 
ATOM   10218 N  NH1 . ARG   A 1 1282 ? -26.02600  11.80800  -2.28800  1.000 54.43243  ?  1280 ARG   A NH1 1 
ATOM   10219 N  NH2 . ARG   A 1 1282 ? -27.27000  9.96800   -1.72900  1.000 63.03349  ?  1280 ARG   A NH2 1 
ATOM   10220 N  N   . SER   A 1 1283 ? -19.72500  7.34400   0.30900   1.000 63.98017  ?  1281 SER   A N   1 
ATOM   10221 C  CA  . SER   A 1 1283 ? -19.15700  6.16100   0.94300   1.000 60.28570  ?  1281 SER   A CA  1 
ATOM   10222 C  C   . SER   A 1 1283 ? -18.33100  6.60900   2.14300   1.000 53.84789  ?  1281 SER   A C   1 
ATOM   10223 O  O   . SER   A 1 1283 ? -18.32000  7.78900   2.50700   1.000 62.98952  ?  1281 SER   A O   1 
ATOM   10224 C  CB  . SER   A 1 1283 ? -18.31200  5.36300   -0.05300  1.000 63.48241  ?  1281 SER   A CB  1 
ATOM   10225 O  OG  . SER   A 1 1283 ? -17.19200  6.12000   -0.47800  1.000 68.62228  ?  1281 SER   A OG  1 
ATOM   10226 N  N   . VAL   A 1 1284 ? -17.63900  5.65600   2.76600   1.000 56.21356  ?  1282 VAL   A N   1 
ATOM   10227 C  CA  . VAL   A 1 1284 ? -16.67700  6.01300   3.79900   1.000 62.26279  ?  1282 VAL   A CA  1 
ATOM   10228 C  C   . VAL   A 1 1284 ? -15.34100  6.37500   3.16700   1.000 59.06591  ?  1282 VAL   A C   1 
ATOM   10229 O  O   . VAL   A 1 1284 ? -14.56400  7.14500   3.74400   1.000 67.28244  ?  1282 VAL   A O   1 
ATOM   10230 C  CB  . VAL   A 1 1284 ? -16.52900  4.87000   4.81700   1.000 65.81611  ?  1282 VAL   A CB  1 
ATOM   10231 C  CG1 . VAL   A 1 1284 ? -15.80100  5.35300   6.06600   1.000 46.14236  ?  1282 VAL   A CG1 1 
ATOM   10232 C  CG2 . VAL   A 1 1284 ? -17.89100  4.29700   5.17300   1.000 39.01663  ?  1282 VAL   A CG2 1 
ATOM   10233 N  N   . GLU   A 1 1285 ? -15.05600  5.84400   1.97500   1.000 57.17182  ?  1283 GLU   A N   1 
ATOM   10234 C  CA  . GLU   A 1 1285 ? -13.80700  6.17400   1.29900   1.000 70.26715  ?  1283 GLU   A CA  1 
ATOM   10235 C  C   . GLU   A 1 1285 ? -13.78000  7.63700   0.87700   1.000 70.13063  ?  1283 GLU   A C   1 
ATOM   10236 O  O   . GLU   A 1 1285 ? -12.73100  8.28700   0.94700   1.000 72.50951  ?  1283 GLU   A O   1 
ATOM   10237 C  CB  . GLU   A 1 1285 ? -13.60200  5.26200   0.08800   1.000 74.12176  ?  1283 GLU   A CB  1 
ATOM   10238 C  CG  . GLU   A 1 1285 ? -13.72700  3.77800   0.39400   1.000 77.99760  ?  1283 GLU   A CG  1 
ATOM   10239 C  CD  . GLU   A 1 1285 ? -15.11500  3.24200   0.10700   1.000 86.32279  ?  1283 GLU   A CD  1 
ATOM   10240 O  OE1 . GLU   A 1 1285 ? -15.52300  3.24700   -1.07400  1.000 69.57123  ?  1283 GLU   A OE1 1 
ATOM   10241 O  OE2 . GLU   A 1 1285 ? -15.80100  2.82300   1.06300   1.000 89.19567  -1 1283 GLU   A OE2 1 
ATOM   10242 N  N   . MET   A 1 1286 ? -14.92200  8.17000   0.43300   1.000 67.13350  ?  1284 MET   A N   1 
ATOM   10243 C  CA  . MET   A 1 1286 ? -14.99600  9.58500   0.08300   1.000 57.26200  ?  1284 MET   A CA  1 
ATOM   10244 C  C   . MET   A 1 1286 ? -14.63900  10.46000  1.27800   1.000 54.95901  ?  1284 MET   A C   1 
ATOM   10245 O  O   . MET   A 1 1286 ? -13.86700  11.41800  1.15600   1.000 56.00783  ?  1284 MET   A O   1 
ATOM   10246 C  CB  . MET   A 1 1286 ? -16.39300  9.92900   -0.43700  1.000 63.61838  ?  1284 MET   A CB  1 
ATOM   10247 C  CG  . MET   A 1 1286 ? -16.66300  11.42700  -0.52300  1.000 73.22503  ?  1284 MET   A CG  1 
ATOM   10248 S  SD  . MET   A 1 1286 ? -18.40700  11.85300  -0.72000  1.000 65.96356  ?  1284 MET   A SD  1 
ATOM   10249 C  CE  . MET   A 1 1286 ? -18.58900  11.78600  -2.50100  1.000 43.98672  ?  1284 MET   A CE  1 
ATOM   10250 N  N   . MET   A 1 1287 ? -15.19300  10.13900  2.44900   1.000 54.57818  ?  1285 MET   A N   1 
ATOM   10251 C  CA  . MET   A 1 1287 ? -14.85500  10.88800  3.65400   1.000 59.00160  ?  1285 MET   A CA  1 
ATOM   10252 C  C   . MET   A 1 1287 ? -13.40000  10.66700  4.04700   1.000 62.60351  ?  1285 MET   A C   1 
ATOM   10253 O  O   . MET   A 1 1287 ? -12.70600  11.61300  4.43800   1.000 59.67403  ?  1285 MET   A O   1 
ATOM   10254 C  CB  . MET   A 1 1287 ? -15.78700  10.48800  4.79500   1.000 55.90790  ?  1285 MET   A CB  1 
ATOM   10255 C  CG  . MET   A 1 1287 ? -17.25100  10.77700  4.52300   1.000 65.73813  ?  1285 MET   A CG  1 
ATOM   10256 S  SD  . MET   A 1 1287 ? -17.55200  12.53800  4.30400   1.000 59.08488  ?  1285 MET   A SD  1 
ATOM   10257 C  CE  . MET   A 1 1287 ? -16.91700  13.16400  5.85800   1.000 36.65992  ?  1285 MET   A CE  1 
ATOM   10258 N  N   . VAL   A 1 1288 ? -12.92600  9.42300   3.95600   1.000 75.78850  ?  1286 VAL   A N   1 
ATOM   10259 C  CA  . VAL   A 1 1288 ? -11.52100  9.13900   4.23400   1.000 75.38683  ?  1286 VAL   A CA  1 
ATOM   10260 C  C   . VAL   A 1 1288 ? -10.62600  9.89000   3.25800   1.000 59.72540  ?  1286 VAL   A C   1 
ATOM   10261 O  O   . VAL   A 1 1288 ? -9.58200   10.43200  3.64100   1.000 55.52522  ?  1286 VAL   A O   1 
ATOM   10262 C  CB  . VAL   A 1 1288 ? -11.26200  7.62100   4.19100   1.000 65.37995  ?  1286 VAL   A CB  1 
ATOM   10263 C  CG1 . VAL   A 1 1288 ? -9.77800   7.33200   4.01900   1.000 70.74426  ?  1286 VAL   A CG1 1 
ATOM   10264 C  CG2 . VAL   A 1 1288 ? -11.78500  6.96300   5.45600   1.000 55.63658  ?  1286 VAL   A CG2 1 
ATOM   10265 N  N   . ALA   A 1 1289 ? -11.02300  9.94500   1.98700   1.000 56.13619  ?  1287 ALA   A N   1 
ATOM   10266 C  CA  . ALA   A 1 1289 ? -10.24300  10.68300  1.00000   1.000 61.41508  ?  1287 ALA   A CA  1 
ATOM   10267 C  C   . ALA   A 1 1289 ? -10.16400  12.16200  1.36300   1.000 73.20198  ?  1287 ALA   A C   1 
ATOM   10268 O  O   . ALA   A 1 1289 ? -9.07600   12.69400  1.60800   1.000 80.30140  ?  1287 ALA   A O   1 
ATOM   10269 C  CB  . ALA   A 1 1289 ? -10.84500  10.49100  -0.39300  1.000 52.01944  ?  1287 ALA   A CB  1 
ATOM   10270 N  N   . ILE   A 1 1290 ? -11.32400  12.82800  1.44100   1.000 69.30752  ?  1288 ILE   A N   1 
ATOM   10271 C  CA  . ILE   A 1 1290 ? -11.38000  14.27900  1.64800   1.000 56.16886  ?  1288 ILE   A CA  1 
ATOM   10272 C  C   . ILE   A 1 1290 ? -10.49900  14.70300  2.81800   1.000 55.98184  ?  1288 ILE   A C   1 
ATOM   10273 O  O   . ILE   A 1 1290 ? -9.66700   15.61000  2.69500   1.000 65.77013  ?  1288 ILE   A O   1 
ATOM   10274 C  CB  . ILE   A 1 1290 ? -12.83700  14.73100  1.85300   1.000 51.44604  ?  1288 ILE   A CB  1 
ATOM   10275 C  CG1 . ILE   A 1 1290 ? -13.58200  14.75800  0.51700   1.000 66.57864  ?  1288 ILE   A CG1 1 
ATOM   10276 C  CG2 . ILE   A 1 1290 ? -12.89200  16.09700  2.53000   1.000 57.03448  ?  1288 ILE   A CG2 1 
ATOM   10277 C  CD1 . ILE   A 1 1290 ? -15.08800  14.86200  0.65500   1.000 59.22531  ?  1288 ILE   A CD1 1 
ATOM   10278 N  N   . PHE   A 1 1291 ? -10.66800  14.05400  3.97200   1.000 48.49706  ?  1289 PHE   A N   1 
ATOM   10279 C  CA  . PHE   A 1 1291 ? -9.86100   14.41400  5.13400   1.000 51.13880  ?  1289 PHE   A CA  1 
ATOM   10280 C  C   . PHE   A 1 1291 ? -8.38200   14.12000  4.91000   1.000 65.85008  ?  1289 PHE   A C   1 
ATOM   10281 O  O   . PHE   A 1 1291 ? -7.52100   14.82100  5.45500   1.000 73.83756  ?  1289 PHE   A O   1 
ATOM   10282 C  CB  . PHE   A 1 1291 ? -10.36600  13.68000  6.37600   1.000 45.88905  ?  1289 PHE   A CB  1 
ATOM   10283 C  CG  . PHE   A 1 1291 ? -11.27000  14.50700  7.24600   1.000 51.11296  ?  1289 PHE   A CG  1 
ATOM   10284 C  CD1 . PHE   A 1 1291 ? -10.75600  15.54400  8.00800   1.000 66.39372  ?  1289 PHE   A CD1 1 
ATOM   10285 C  CD2 . PHE   A 1 1291 ? -12.62800  14.24100  7.31500   1.000 42.85006  ?  1289 PHE   A CD2 1 
ATOM   10286 C  CE1 . PHE   A 1 1291 ? -11.57900  16.30600  8.81500   1.000 68.71943  ?  1289 PHE   A CE1 1 
ATOM   10287 C  CE2 . PHE   A 1 1291 ? -13.45700  14.99900  8.12300   1.000 51.16175  ?  1289 PHE   A CE2 1 
ATOM   10288 C  CZ  . PHE   A 1 1291 ? -12.93200  16.03300  8.87300   1.000 66.66208  ?  1289 PHE   A CZ  1 
ATOM   10289 N  N   . ALA   A 1 1292 ? -8.06500   13.09500  4.11400   1.000 71.15502  ?  1290 ALA   A N   1 
ATOM   10290 C  CA  . ALA   A 1 1292 ? -6.66500   12.76600  3.85800   1.000 64.80970  ?  1290 ALA   A CA  1 
ATOM   10291 C  C   . ALA   A 1 1292 ? -6.01600   13.79500  2.94400   1.000 69.25572  ?  1290 ALA   A C   1 
ATOM   10292 O  O   . ALA   A 1 1292 ? -4.82400   14.09500  3.08800   1.000 70.24337  ?  1290 ALA   A O   1 
ATOM   10293 C  CB  . ALA   A 1 1292 ? -6.55200   11.36700  3.25400   1.000 69.84374  ?  1290 ALA   A CB  1 
ATOM   10294 N  N   . VAL   A 1 1293 ? -6.78000   14.33300  1.98900   1.000 60.83291  ?  1291 VAL   A N   1 
ATOM   10295 C  CA  . VAL   A 1 1293 ? -6.27800   15.41700  1.14900   1.000 56.80110  ?  1291 VAL   A CA  1 
ATOM   10296 C  C   . VAL   A 1 1293 ? -5.80500   16.57400  2.01300   1.000 54.31943  ?  1291 VAL   A C   1 
ATOM   10297 O  O   . VAL   A 1 1293 ? -4.73000   17.14500  1.79400   1.000 65.27581  ?  1291 VAL   A O   1 
ATOM   10298 C  CB  . VAL   A 1 1293 ? -7.36000   15.88800  0.16200   1.000 66.57186  ?  1291 VAL   A CB  1 
ATOM   10299 C  CG1 . VAL   A 1 1293 ? -6.72000   16.74900  -0.89600  1.000 59.81540  ?  1291 VAL   A CG1 1 
ATOM   10300 C  CG2 . VAL   A 1 1293 ? -8.07900   14.71000  -0.46700  1.000 66.77909  ?  1291 VAL   A CG2 1 
ATOM   10301 N  N   . LEU   A 1 1294 ? -6.62100   16.94700  2.99600   1.000 59.39853  ?  1292 LEU   A N   1 
ATOM   10302 C  CA  . LEU   A 1 1294 ? -6.31100   18.09600  3.83100   1.000 75.34022  ?  1292 LEU   A CA  1 
ATOM   10303 C  C   . LEU   A 1 1294 ? -5.13300   17.80500  4.75000   1.000 70.88143  ?  1292 LEU   A C   1 
ATOM   10304 O  O   . LEU   A 1 1294 ? -4.25600   18.65700  4.92900   1.000 88.93828  ?  1292 LEU   A O   1 
ATOM   10305 C  CB  . LEU   A 1 1294 ? -7.55000   18.48800  4.63200   1.000 70.94093  ?  1292 LEU   A CB  1 
ATOM   10306 C  CG  . LEU   A 1 1294 ? -8.87200   18.69700  3.89100   1.000 59.63477  ?  1292 LEU   A CG  1 
ATOM   10307 C  CD1 . LEU   A 1 1294 ? -9.88700   19.34500  4.82300   1.000 45.66523  ?  1292 LEU   A CD1 1 
ATOM   10308 C  CD2 . LEU   A 1 1294 ? -8.66800   19.52900  2.63600   1.000 56.11135  ?  1292 LEU   A CD2 1 
ATOM   10309 N  N   . LYS   A 1 1295 ? -5.08900   16.60100  5.33100   1.000 75.42982  ?  1293 LYS   A N   1 
ATOM   10310 C  CA  . LYS   A 1 1295 ? -3.99100   16.24100  6.22300   1.000 72.26092  ?  1293 LYS   A CA  1 
ATOM   10311 C  C   . LYS   A 1 1295 ? -2.64400   16.29300  5.51200   1.000 71.25995  ?  1293 LYS   A C   1 
ATOM   10312 O  O   . LYS   A 1 1295 ? -1.63200   16.67300  6.11400   1.000 67.48796  ?  1293 LYS   A O   1 
ATOM   10313 C  CB  . LYS   A 1 1295 ? -4.22600   14.84900  6.80900   1.000 61.94781  ?  1293 LYS   A CB  1 
ATOM   10314 C  CG  . LYS   A 1 1295 ? -4.92500   14.85000  8.15100   1.000 44.86152  ?  1293 LYS   A CG  1 
ATOM   10315 C  CD  . LYS   A 1 1295 ? -4.48500   13.65200  8.96500   1.000 55.76931  ?  1293 LYS   A CD  1 
ATOM   10316 C  CE  . LYS   A 1 1295 ? -4.76200   13.84600  10.44000  1.000 52.18224  ?  1293 LYS   A CE  1 
ATOM   10317 N  NZ  . LYS   A 1 1295 ? -6.15000   13.47300  10.82200  1.000 64.68000  ?  1293 LYS   A NZ  1 
ATOM   10318 N  N   . ALA   A 1 1296 ? -2.60800   15.91000  4.23400   1.000 67.87231  ?  1294 ALA   A N   1 
ATOM   10319 C  CA  . ALA   A 1 1296 ? -1.35800   15.96500  3.48400   1.000 65.42549  ?  1294 ALA   A CA  1 
ATOM   10320 C  C   . ALA   A 1 1296 ? -0.96300   17.39800  3.15000   1.000 78.81406  ?  1294 ALA   A C   1 
ATOM   10321 O  O   . ALA   A 1 1296 ? 0.23200    17.70000  3.04400   1.000 85.12416  ?  1294 ALA   A O   1 
ATOM   10322 C  CB  . ALA   A 1 1296 ? -1.47300   15.13500  2.20600   1.000 67.31350  ?  1294 ALA   A CB  1 
ATOM   10323 N  N   . GLY   A 1 1297 ? -1.94000   18.28500  2.97100   1.000 83.14468  ?  1295 GLY   A N   1 
ATOM   10324 C  CA  . GLY   A 1 1297 ? -1.65000   19.68700  2.74600   1.000 78.32848  ?  1295 GLY   A CA  1 
ATOM   10325 C  C   . GLY   A 1 1297 ? -2.40300   20.32000  1.59400   1.000 71.96412  ?  1295 GLY   A C   1 
ATOM   10326 O  O   . GLY   A 1 1297 ? -2.44000   21.54900  1.47300   1.000 72.18051  ?  1295 GLY   A O   1 
ATOM   10327 N  N   . GLY   A 1 1298 ? -3.01400   19.50000  0.74300   1.000 70.16049  ?  1296 GLY   A N   1 
ATOM   10328 C  CA  . GLY   A 1 1298 ? -3.64700   19.97800  -0.46600  1.000 59.74458  ?  1296 GLY   A CA  1 
ATOM   10329 C  C   . GLY   A 1 1298 ? -5.11500   20.31700  -0.28100  1.000 63.62525  ?  1296 GLY   A C   1 
ATOM   10330 O  O   . GLY   A 1 1298 ? -5.63600   20.41000  0.83300   1.000 51.48398  ?  1296 GLY   A O   1 
ATOM   10331 N  N   . ALA   A 1 1299 ? -5.78400   20.51600  -1.41500  1.000 65.03824  ?  1297 ALA   A N   1 
ATOM   10332 C  CA  . ALA   A 1 1299 ? -7.21100   20.78800  -1.47400  1.000 71.16493  ?  1297 ALA   A CA  1 
ATOM   10333 C  C   . ALA   A 1 1299 ? -7.87400   19.76800  -2.39000  1.000 75.46665  ?  1297 ALA   A C   1 
ATOM   10334 O  O   . ALA   A 1 1299 ? -7.24400   19.24300  -3.31300  1.000 72.31294  ?  1297 ALA   A O   1 
ATOM   10335 C  CB  . ALA   A 1 1299 ? -7.48900   22.21000  -1.98200  1.000 63.24841  ?  1297 ALA   A CB  1 
ATOM   10336 N  N   . TYR   A 1 1300 ? -9.14800   19.48200  -2.13100  1.000 55.16634  ?  1298 TYR   A N   1 
ATOM   10337 C  CA  . TYR   A 1 1300 ? -9.86500   18.46200  -2.88200  1.000 57.97600  ?  1298 TYR   A CA  1 
ATOM   10338 C  C   . TYR   A 1 1300 ? -10.80700  19.10500  -3.89300  1.000 55.68629  ?  1298 TYR   A C   1 
ATOM   10339 O  O   . TYR   A 1 1300 ? -11.44800  20.12100  -3.60800  1.000 64.88315  ?  1298 TYR   A O   1 
ATOM   10340 C  CB  . TYR   A 1 1300 ? -10.63000  17.51400  -1.94700  1.000 63.87463  ?  1298 TYR   A CB  1 
ATOM   10341 C  CG  . TYR   A 1 1300 ? -11.94000  18.02100  -1.37400  1.000 69.35893  ?  1298 TYR   A CG  1 
ATOM   10342 C  CD1 . TYR   A 1 1300 ? -11.97200  18.74700  -0.18800  1.000 65.67704  ?  1298 TYR   A CD1 1 
ATOM   10343 C  CD2 . TYR   A 1 1300 ? -13.15000  17.72900  -1.99300  1.000 55.27226  ?  1298 TYR   A CD2 1 
ATOM   10344 C  CE1 . TYR   A 1 1300 ? -13.17200  19.19100  0.34700   1.000 55.20534  ?  1298 TYR   A CE1 1 
ATOM   10345 C  CE2 . TYR   A 1 1300 ? -14.35000  18.16900  -1.46500  1.000 38.47075  ?  1298 TYR   A CE2 1 
ATOM   10346 C  CZ  . TYR   A 1 1300 ? -14.35600  18.90000  -0.29800  1.000 41.18095  ?  1298 TYR   A CZ  1 
ATOM   10347 O  OH  . TYR   A 1 1300 ? -15.55200  19.33700  0.22600   1.000 52.81436  ?  1298 TYR   A OH  1 
ATOM   10348 N  N   . LEU   A 1 1301 ? -10.86900  18.50700  -5.08100  1.000 46.09503  ?  1299 LEU   A N   1 
ATOM   10349 C  CA  . LEU   A 1 1301 ? -11.66000  19.02400  -6.19800  1.000 50.94694  ?  1299 LEU   A CA  1 
ATOM   10350 C  C   . LEU   A 1 1301 ? -12.72800  18.00100  -6.55800  1.000 66.73034  ?  1299 LEU   A C   1 
ATOM   10351 O  O   . LEU   A 1 1301 ? -12.43500  17.00900  -7.24900  1.000 60.14594  ?  1299 LEU   A O   1 
ATOM   10352 C  CB  . LEU   A 1 1301 ? -10.76000  19.31700  -7.39900  1.000 40.59073  ?  1299 LEU   A CB  1 
ATOM   10353 C  CG  . LEU   A 1 1301 ? -11.16300  20.41400  -8.38700  1.000 48.98256  ?  1299 LEU   A CG  1 
ATOM   10354 C  CD1 . LEU   A 1 1301 ? -9.98300   20.75900  -9.27700  1.000 62.16466  ?  1299 LEU   A CD1 1 
ATOM   10355 C  CD2 . LEU   A 1 1301 ? -12.35700  19.99900  -9.23100  1.000 59.93483  ?  1299 LEU   A CD2 1 
ATOM   10356 N  N   . PRO   A 1 1302 ? -13.97300  18.19400  -6.12100  1.000 64.15409  ?  1300 PRO   A N   1 
ATOM   10357 C  CA  . PRO   A 1 1302 ? -15.00700  17.17700  -6.35800  1.000 42.75564  ?  1300 PRO   A CA  1 
ATOM   10358 C  C   . PRO   A 1 1302 ? -15.37100  17.08100  -7.83100  1.000 49.02790  ?  1300 PRO   A C   1 
ATOM   10359 O  O   . PRO   A 1 1302 ? -15.57900  18.09200  -8.50500  1.000 55.86416  ?  1300 PRO   A O   1 
ATOM   10360 C  CB  . PRO   A 1 1302 ? -16.19300  17.67100  -5.52400  1.000 43.88969  ?  1300 PRO   A CB  1 
ATOM   10361 C  CG  . PRO   A 1 1302 ? -15.61700  18.66800  -4.57400  1.000 54.75221  ?  1300 PRO   A CG  1 
ATOM   10362 C  CD  . PRO   A 1 1302 ? -14.47100  19.29800  -5.28900  1.000 62.38046  ?  1300 PRO   A CD  1 
ATOM   10363 N  N   . ILE   A 1 1303 ? -15.45800  15.84700  -8.31800  1.000 57.41082  ?  1301 ILE   A N   1 
ATOM   10364 C  CA  . ILE   A 1 1303 ? -15.81500  15.55400  -9.69800  1.000 63.06040  ?  1301 ILE   A CA  1 
ATOM   10365 C  C   . ILE   A 1 1303 ? -16.82900  14.42000  -9.66700  1.000 65.59210  ?  1301 ILE   A C   1 
ATOM   10366 O  O   . ILE   A 1 1303 ? -16.50000  13.30400  -9.24300  1.000 68.91643  ?  1301 ILE   A O   1 
ATOM   10367 C  CB  . ILE   A 1 1303 ? -14.59600  15.16400  -10.54300 1.000 63.04387  ?  1301 ILE   A CB  1 
ATOM   10368 C  CG1 . ILE   A 1 1303 ? -13.53300  16.26300  -10.51300 1.000 63.18146  ?  1301 ILE   A CG1 1 
ATOM   10369 C  CG2 . ILE   A 1 1303 ? -15.02900  14.88800  -11.95600 1.000 57.42854  ?  1301 ILE   A CG2 1 
ATOM   10370 C  CD1 . ILE   A 1 1303 ? -13.81300  17.40800  -11.45200 1.000 66.69343  ?  1301 ILE   A CD1 1 
ATOM   10371 N  N   . ASP   A 1 1304 ? -18.05200  14.69600  -10.10600 1.000 74.82227  ?  1302 ASP   A N   1 
ATOM   10372 C  CA  . ASP   A 1 1304 ? -19.08400  13.66900  -10.15400 1.000 70.25521  ?  1302 ASP   A CA  1 
ATOM   10373 C  C   . ASP   A 1 1304 ? -18.59400  12.50700  -11.01200 1.000 76.21529  ?  1302 ASP   A C   1 
ATOM   10374 O  O   . ASP   A 1 1304 ? -18.24800  12.71700  -12.18500 1.000 82.06061  ?  1302 ASP   A O   1 
ATOM   10375 C  CB  . ASP   A 1 1304 ? -20.38800  14.24400  -10.70900 1.000 75.10716  ?  1302 ASP   A CB  1 
ATOM   10376 C  CG  . ASP   A 1 1304 ? -21.55700  13.27200  -10.60900 1.000 80.65552  ?  1302 ASP   A CG  1 
ATOM   10377 O  OD1 . ASP   A 1 1304 ? -21.45600  12.13900  -11.12600 1.000 82.63160  ?  1302 ASP   A OD1 1 
ATOM   10378 O  OD2 . ASP   A 1 1304 ? -22.58600  13.64700  -10.01000 1.000 76.63167  -1 1302 ASP   A OD2 1 
ATOM   10379 N  N   . PRO   A 1 1305 ? -18.52600  11.28600  -10.47500 1.000 78.47900  ?  1303 PRO   A N   1 
ATOM   10380 C  CA  . PRO   A 1 1305 ? -17.94600  10.17800  -11.25000 1.000 69.46629  ?  1303 PRO   A CA  1 
ATOM   10381 C  C   . PRO   A 1 1305 ? -18.71800  9.85600   -12.51600 1.000 74.25796  ?  1303 PRO   A C   1 
ATOM   10382 O  O   . PRO   A 1 1305 ? -18.12200  9.38000   -13.49100 1.000 79.93515  ?  1303 PRO   A O   1 
ATOM   10383 C  CB  . PRO   A 1 1305 ? -17.97200  9.00500   -10.26000 1.000 67.01435  ?  1303 PRO   A CB  1 
ATOM   10384 C  CG  . PRO   A 1 1305 ? -18.09400  9.63500   -8.90700  1.000 71.62719  ?  1303 PRO   A CG  1 
ATOM   10385 C  CD  . PRO   A 1 1305 ? -18.91000  10.87100  -9.11600  1.000 71.05006  ?  1303 PRO   A CD  1 
ATOM   10386 N  N   . HIS   A 1 1306 ? -20.02700  10.10000  -12.53400 1.000 73.31349  ?  1304 HIS   A N   1 
ATOM   10387 C  CA  . HIS   A 1 1306 ? -20.85500  9.84700   -13.70300 1.000 73.65163  ?  1304 HIS   A CA  1 
ATOM   10388 C  C   . HIS   A 1 1306 ? -20.93500  11.05100  -14.63400 1.000 82.16587  ?  1304 HIS   A C   1 
ATOM   10389 O  O   . HIS   A 1 1306 ? -21.90700  11.17900  -15.38900 1.000 78.47840  ?  1304 HIS   A O   1 
ATOM   10390 C  CB  . HIS   A 1 1306 ? -22.25600  9.41500   -13.26800 1.000 64.94422  ?  1304 HIS   A CB  1 
ATOM   10391 C  CG  . HIS   A 1 1306 ? -22.26400  8.21600   -12.37200 1.000 71.93646  ?  1304 HIS   A CG  1 
ATOM   10392 N  ND1 . HIS   A 1 1306 ? -21.22000  7.31800   -12.32300 1.000 75.00017  ?  1304 HIS   A ND1 1 
ATOM   10393 C  CD2 . HIS   A 1 1306 ? -23.18500  7.77100   -11.48400 1.000 88.60738  ?  1304 HIS   A CD2 1 
ATOM   10394 C  CE1 . HIS   A 1 1306 ? -21.49800  6.36900   -11.44700 1.000 83.68516  ?  1304 HIS   A CE1 1 
ATOM   10395 N  NE2 . HIS   A 1 1306 ? -22.68500  6.62000   -10.92400 1.000 90.08984  ?  1304 HIS   A NE2 1 
ATOM   10396 N  N   . SER   A 1 1307 ? -19.93900  11.93600  -14.59500 1.000 83.02650  ?  1305 SER   A N   1 
ATOM   10397 C  CA  . SER   A 1 1307 ? -19.91900  13.08900  -15.48200 1.000 90.09162  ?  1305 SER   A CA  1 
ATOM   10398 C  C   . SER   A 1 1307 ? -19.48500  12.66600  -16.88300 1.000 84.72613  ?  1305 SER   A C   1 
ATOM   10399 O  O   . SER   A 1 1307 ? -18.60800  11.80900  -17.02700 1.000 91.39952  ?  1305 SER   A O   1 
ATOM   10400 C  CB  . SER   A 1 1307 ? -18.96600  14.16000  -14.95600 1.000 92.14540  ?  1305 SER   A CB  1 
ATOM   10401 O  OG  . SER   A 1 1307 ? -19.16400  14.39400  -13.57500 1.000 86.71816  ?  1305 SER   A OG  1 
ATOM   10402 N  N   . PRO   A 1 1308 ? -20.10100  13.22500  -17.92500 1.000 78.48579  ?  1306 PRO   A N   1 
ATOM   10403 C  CA  . PRO   A 1 1308 ? -19.59700  13.01000  -19.28500 1.000 91.04524  ?  1306 PRO   A CA  1 
ATOM   10404 C  C   . PRO   A 1 1308 ? -18.10700  13.30800  -19.38000 1.000 88.42530  ?  1306 PRO   A C   1 
ATOM   10405 O  O   . PRO   A 1 1308 ? -17.57200  14.15100  -18.65600 1.000 87.91781  ?  1306 PRO   A O   1 
ATOM   10406 C  CB  . PRO   A 1 1308 ? -20.41900  13.99100  -20.12800 1.000 79.74111  ?  1306 PRO   A CB  1 
ATOM   10407 C  CG  . PRO   A 1 1308 ? -21.65800  14.27800  -19.32100 1.000 93.15126  ?  1306 PRO   A CG  1 
ATOM   10408 C  CD  . PRO   A 1 1308 ? -21.47500  13.75400  -17.92000 1.000 99.19039  ?  1306 PRO   A CD  1 
ATOM   10409 N  N   . ALA   A 1 1309 ? -17.43600  12.59800  -20.29100 1.000 83.61771  ?  1307 ALA   A N   1 
ATOM   10410 C  CA  . ALA   A 1 1309 ? -15.98500  12.70800  -20.39800 1.000 82.85361  ?  1307 ALA   A CA  1 
ATOM   10411 C  C   . ALA   A 1 1309 ? -15.55200  14.10200  -20.83000 1.000 96.71153  ?  1307 ALA   A C   1 
ATOM   10412 O  O   . ALA   A 1 1309 ? -14.43200  14.52700  -20.52000 1.000 90.98230  ?  1307 ALA   A O   1 
ATOM   10413 C  CB  . ALA   A 1 1309 ? -15.44700  11.65800  -21.36900 1.000 89.84830  ?  1307 ALA   A CB  1 
ATOM   10414 N  N   . GLU   A 1 1310 ? -16.41600  14.82600  -21.54400 1.000 90.76484  ?  1308 GLU   A N   1 
ATOM   10415 C  CA  . GLU   A 1 1310 ? -16.07500  16.18500  -21.94900 1.000 86.55696  ?  1308 GLU   A CA  1 
ATOM   10416 C  C   . GLU   A 1 1310 ? -15.97700  17.11800  -20.74900 1.000 91.72896  ?  1308 GLU   A C   1 
ATOM   10417 O  O   . GLU   A 1 1310 ? -15.15300  18.04000  -20.74800 1.000 88.72037  ?  1308 GLU   A O   1 
ATOM   10418 C  CB  . GLU   A 1 1310 ? -17.10500  16.70900  -22.94800 1.000 50.34381  ?  1308 GLU   A CB  1 
ATOM   10419 N  N   . ARG   A 1 1311 ? -16.79600  16.89200  -19.72000 1.000 81.00317  ?  1309 ARG   A N   1 
ATOM   10420 C  CA  . ARG   A 1 1311 ? -16.75000  17.75200  -18.54300 1.000 78.40503  ?  1309 ARG   A CA  1 
ATOM   10421 C  C   . ARG   A 1 1311 ? -15.48500  17.50600  -17.73000 1.000 83.61509  ?  1309 ARG   A C   1 
ATOM   10422 O  O   . ARG   A 1 1311 ? -14.78600  18.45400  -17.35600 1.000 90.93755  ?  1309 ARG   A O   1 
ATOM   10423 C  CB  . ARG   A 1 1311 ? -17.99700  17.54300  -17.68300 1.000 82.06716  ?  1309 ARG   A CB  1 
ATOM   10424 C  CG  . ARG   A 1 1311 ? -17.99100  18.37400  -16.41000 1.000 82.87879  ?  1309 ARG   A CG  1 
ATOM   10425 C  CD  . ARG   A 1 1311 ? -19.38300  18.87200  -16.04100 1.000 88.67124  ?  1309 ARG   A CD  1 
ATOM   10426 N  NE  . ARG   A 1 1311 ? -20.08100  19.48100  -17.16900 1.000 94.74680  ?  1309 ARG   A NE  1 
ATOM   10427 C  CZ  . ARG   A 1 1311 ? -19.75400  20.64100  -17.72300 1.000 88.37153  ?  1309 ARG   A CZ  1 
ATOM   10428 N  NH1 . ARG   A 1 1311 ? -18.70400  21.33400  -17.31300 1.000 84.44576  ?  1309 ARG   A NH1 1 
ATOM   10429 N  NH2 . ARG   A 1 1311 ? -20.49600  21.11600  -18.71900 1.000 84.34645  ?  1309 ARG   A NH2 1 
ATOM   10430 N  N   . ILE   A 1 1312 ? -15.17000  16.23800  -17.45000 1.000 94.19554  ?  1310 ILE   A N   1 
ATOM   10431 C  CA  . ILE   A 1 1312 ? -13.97900  15.93500  -16.66000 1.000 98.04576  ?  1310 ILE   A CA  1 
ATOM   10432 C  C   . ILE   A 1 1312 ? -12.71700  16.35900  -17.39700 1.000 101.88605 ?  1310 ILE   A C   1 
ATOM   10433 O  O   . ILE   A 1 1312 ? -11.73000  16.76200  -16.77000 1.000 98.79165  ?  1310 ILE   A O   1 
ATOM   10434 C  CB  . ILE   A 1 1312 ? -13.94200  14.44000  -16.28300 1.000 91.04186  ?  1310 ILE   A CB  1 
ATOM   10435 C  CG1 . ILE   A 1 1312 ? -14.15200  13.55300  -17.50600 1.000 91.09189  ?  1310 ILE   A CG1 1 
ATOM   10436 C  CG2 . ILE   A 1 1312 ? -15.02000  14.12600  -15.28200 1.000 93.13237  ?  1310 ILE   A CG2 1 
ATOM   10437 C  CD1 . ILE   A 1 1312 ? -14.47300  12.10900  -17.15000 1.000 98.66647  ?  1310 ILE   A CD1 1 
ATOM   10438 N  N   . ALA   A 1 1313 ? -12.72600  16.29000  -18.73100 1.000 99.32563  ?  1311 ALA   A N   1 
ATOM   10439 C  CA  . ALA   A 1 1313 ? -11.58400  16.77300  -19.50000 1.000 96.38314  ?  1311 ALA   A CA  1 
ATOM   10440 C  C   . ALA   A 1 1313 ? -11.41600  18.27900  -19.34800 1.000 101.80660 ?  1311 ALA   A C   1 
ATOM   10441 O  O   . ALA   A 1 1313 ? -10.28700  18.77900  -19.27200 1.000 91.42755  ?  1311 ALA   A O   1 
ATOM   10442 C  CB  . ALA   A 1 1313 ? -11.74400  16.39500  -20.97200 1.000 95.95666  ?  1311 ALA   A CB  1 
ATOM   10443 N  N   . TYR   A 1 1314 ? -12.52700  19.01800  -19.30000 1.000 108.39194 ?  1312 TYR   A N   1 
ATOM   10444 C  CA  . TYR   A 1 1314 ? -12.45300  20.46300  -19.10900 1.000 107.96313 ?  1312 TYR   A CA  1 
ATOM   10445 C  C   . TYR   A 1 1314 ? -11.88300  20.80400  -17.73700 1.000 103.11233 ?  1312 TYR   A C   1 
ATOM   10446 O  O   . TYR   A 1 1314 ? -10.99300  21.65300  -17.61500 1.000 99.13040  ?  1312 TYR   A O   1 
ATOM   10447 C  CB  . TYR   A 1 1314 ? -13.83700  21.08900  -19.29400 1.000 90.89970  ?  1312 TYR   A CB  1 
ATOM   10448 C  CG  . TYR   A 1 1314 ? -13.89500  22.56500  -18.96800 1.000 92.23029  ?  1312 TYR   A CG  1 
ATOM   10449 C  CD1 . TYR   A 1 1314 ? -13.11000  23.48000  -19.65800 1.000 106.41049 ?  1312 TYR   A CD1 1 
ATOM   10450 C  CD2 . TYR   A 1 1314 ? -14.74200  23.04500  -17.97800 1.000 94.81532  ?  1312 TYR   A CD2 1 
ATOM   10451 C  CE1 . TYR   A 1 1314 ? -13.16100  24.83100  -19.36600 1.000 118.17514 ?  1312 TYR   A CE1 1 
ATOM   10452 C  CE2 . TYR   A 1 1314 ? -14.80100  24.39500  -17.67900 1.000 109.15904 ?  1312 TYR   A CE2 1 
ATOM   10453 C  CZ  . TYR   A 1 1314 ? -14.00800  25.28300  -18.37600 1.000 122.23468 ?  1312 TYR   A CZ  1 
ATOM   10454 O  OH  . TYR   A 1 1314 ? -14.06200  26.62600  -18.08300 1.000 126.56239 ?  1312 TYR   A OH  1 
ATOM   10455 N  N   . ILE   A 1 1315 ? -12.38400  20.14400  -16.69000 1.000 97.22501  ?  1313 ILE   A N   1 
ATOM   10456 C  CA  . ILE   A 1 1315 ? -11.85900  20.37700  -15.35100 1.000 91.54801  ?  1313 ILE   A CA  1 
ATOM   10457 C  C   . ILE   A 1 1315 ? -10.46600  19.78300  -15.19400 1.000 92.98114  ?  1313 ILE   A C   1 
ATOM   10458 O  O   . ILE   A 1 1315 ? -9.70500   20.21800  -14.32100 1.000 87.33484  ?  1313 ILE   A O   1 
ATOM   10459 C  CB  . ILE   A 1 1315 ? -12.83100  19.82400  -14.29300 1.000 68.55951  ?  1313 ILE   A CB  1 
ATOM   10460 C  CG1 . ILE   A 1 1315 ? -14.27400  20.04400  -14.75100 1.000 72.10950  ?  1313 ILE   A CG1 1 
ATOM   10461 C  CG2 . ILE   A 1 1315 ? -12.61700  20.52300  -12.96500 1.000 74.77561  ?  1313 ILE   A CG2 1 
ATOM   10462 C  CD1 . ILE   A 1 1315 ? -15.32100  19.66600  -13.72800 1.000 73.13005  ?  1313 ILE   A CD1 1 
ATOM   10463 N  N   . PHE   A 1 1316 ? -10.10700  18.79700  -16.02100 1.000 98.35445  ?  1314 PHE   A N   1 
ATOM   10464 C  CA  . PHE   A 1 1316 ? -8.72000   18.34600  -16.07300 1.000 101.27341 ?  1314 PHE   A CA  1 
ATOM   10465 C  C   . PHE   A 1 1316 ? -7.81000   19.44500  -16.60700 1.000 93.55707  ?  1314 PHE   A C   1 
ATOM   10466 O  O   . PHE   A 1 1316 ? -6.69500   19.63700  -16.10600 1.000 75.14640  ?  1314 PHE   A O   1 
ATOM   10467 C  CB  . PHE   A 1 1316 ? -8.59800   17.09500  -16.94600 1.000 105.65502 ?  1314 PHE   A CB  1 
ATOM   10468 C  CG  . PHE   A 1 1316 ? -8.50200   15.81100  -16.16800 1.000 111.28640 ?  1314 PHE   A CG  1 
ATOM   10469 C  CD1 . PHE   A 1 1316 ? -7.44600   15.59000  -15.29900 1.000 111.08780 ?  1314 PHE   A CD1 1 
ATOM   10470 C  CD2 . PHE   A 1 1316 ? -9.45100   14.81400  -16.32600 1.000 102.79657 ?  1314 PHE   A CD2 1 
ATOM   10471 C  CE1 . PHE   A 1 1316 ? -7.35000   14.40800  -14.58900 1.000 102.35955 ?  1314 PHE   A CE1 1 
ATOM   10472 C  CE2 . PHE   A 1 1316 ? -9.36100   13.63000  -15.61900 1.000 101.26305 ?  1314 PHE   A CE2 1 
ATOM   10473 C  CZ  . PHE   A 1 1316 ? -8.30900   13.42700  -14.74900 1.000 98.90535  ?  1314 PHE   A CZ  1 
ATOM   10474 N  N   . ALA   A 1 1317 ? -8.27200   20.17700  -17.62300 1.000 97.76680  ?  1315 ALA   A N   1 
ATOM   10475 C  CA  . ALA   A 1 1317 ? -7.44500   21.19500  -18.26100 1.000 90.24311  ?  1315 ALA   A CA  1 
ATOM   10476 C  C   . ALA   A 1 1317 ? -7.35100   22.45600  -17.41000 1.000 81.05421  ?  1315 ALA   A C   1 
ATOM   10477 O  O   . ALA   A 1 1317 ? -6.25100   22.94100  -17.12600 1.000 83.88904  ?  1315 ALA   A O   1 
ATOM   10478 C  CB  . ALA   A 1 1317 ? -8.00200   21.52900  -19.64500 1.000 82.59585  ?  1315 ALA   A CB  1 
ATOM   10479 N  N   . ASP   A 1 1318 ? -8.49900   23.00200  -17.00300 1.000 84.56537  ?  1316 ASP   A N   1 
ATOM   10480 C  CA  . ASP   A 1 1318 ? -8.50400   24.25500  -16.25400 1.000 76.97300  ?  1316 ASP   A CA  1 
ATOM   10481 C  C   . ASP   A 1 1318 ? -7.75500   24.11200  -14.93600 1.000 74.40471  ?  1316 ASP   A C   1 
ATOM   10482 O  O   . ASP   A 1 1318 ? -6.96600   24.98700  -14.56500 1.000 91.69173  ?  1316 ASP   A O   1 
ATOM   10483 C  CB  . ASP   A 1 1318 ? -9.94500   24.71000  -16.01800 1.000 91.64893  ?  1316 ASP   A CB  1 
ATOM   10484 C  CG  . ASP   A 1 1318 ? -10.04300  26.17100  -15.60800 1.000 95.58932  ?  1316 ASP   A CG  1 
ATOM   10485 O  OD1 . ASP   A 1 1318 ? -9.37700   26.57800  -14.63300 1.000 91.66706  ?  1316 ASP   A OD1 1 
ATOM   10486 O  OD2 . ASP   A 1 1318 ? -10.79400  26.91700  -16.27100 1.000 96.38249  -1 1316 ASP   A OD2 1 
ATOM   10487 N  N   . SER   A 1 1319 ? -7.98300   23.01300  -14.21600 1.000 64.87432  ?  1317 SER   A N   1 
ATOM   10488 C  CA  . SER   A 1 1319 ? -7.24200   22.80100  -12.97900 1.000 82.43580  ?  1317 SER   A CA  1 
ATOM   10489 C  C   . SER   A 1 1319 ? -5.78500   22.45700  -13.26100 1.000 95.10477  ?  1317 SER   A C   1 
ATOM   10490 O  O   . SER   A 1 1319 ? -4.89400   22.86200  -12.50700 1.000 82.64089  ?  1317 SER   A O   1 
ATOM   10491 C  CB  . SER   A 1 1319 ? -7.90000   21.70200  -12.14200 1.000 86.85661  ?  1317 SER   A CB  1 
ATOM   10492 O  OG  . SER   A 1 1319 ? -7.76600   20.42400  -12.74700 1.000 86.07031  ?  1317 SER   A OG  1 
ATOM   10493 N  N   . GLY   A 1 1320 ? -5.52300   21.71400  -14.33500 1.000 95.97400  ?  1318 GLY   A N   1 
ATOM   10494 C  CA  . GLY   A 1 1320 ? -4.19900   21.17500  -14.56700 1.000 86.75684  ?  1318 GLY   A CA  1 
ATOM   10495 C  C   . GLY   A 1 1320 ? -3.69300   20.22600  -13.50000 1.000 100.38285 ?  1318 GLY   A C   1 
ATOM   10496 O  O   . GLY   A 1 1320 ? -2.52200   19.84200  -13.55000 1.000 121.54364 ?  1318 GLY   A O   1 
ATOM   10497 N  N   . ALA   A 1 1321 ? -4.54000   19.83300  -12.54100 1.000 98.59783  ?  1319 ALA   A N   1 
ATOM   10498 C  CA  . ALA   A 1 1321 ? -4.11100   18.94400  -11.46400 1.000 86.60892  ?  1319 ALA   A CA  1 
ATOM   10499 C  C   . ALA   A 1 1321 ? -3.74300   17.56100  -11.99400 1.000 102.42027 ?  1319 ALA   A C   1 
ATOM   10500 O  O   . ALA   A 1 1321 ? -4.35300   17.05300  -12.93800 1.000 93.03224  ?  1319 ALA   A O   1 
ATOM   10501 C  CB  . ALA   A 1 1321 ? -5.20800   18.81300  -10.40700 1.000 70.54396  ?  1319 ALA   A CB  1 
ATOM   10502 N  N   . LYS   A 1 1322 ? -2.74800   16.94100  -11.36000 1.000 109.71654 ?  1320 LYS   A N   1 
ATOM   10503 C  CA  . LYS   A 1 1322 ? -2.22100   15.65400  -11.80200 1.000 107.32402 ?  1320 LYS   A CA  1 
ATOM   10504 C  C   . LYS   A 1 1322 ? -2.83100   14.48000  -11.04500 1.000 96.27265  ?  1320 LYS   A C   1 
ATOM   10505 O  O   . LYS   A 1 1322 ? -3.23600   13.48400  -11.65700 1.000 101.49001 ?  1320 LYS   A O   1 
ATOM   10506 C  CB  . LYS   A 1 1322 ? -0.69200   15.63500  -11.65500 1.000 95.84155  ?  1320 LYS   A CB  1 
ATOM   10507 N  N   . LEU   A 1 1323 ? -2.92700   14.58800  -9.72600  1.000 77.21138  ?  1321 LEU   A N   1 
ATOM   10508 C  CA  . LEU   A 1 1323 ? -3.41300   13.49000  -8.90800  1.000 69.81165  ?  1321 LEU   A CA  1 
ATOM   10509 C  C   . LEU   A 1 1323 ? -4.93400   13.40300  -8.95700  1.000 81.08785  ?  1321 LEU   A C   1 
ATOM   10510 O  O   . LEU   A 1 1323 ? -5.63600   14.41600  -9.03500  1.000 74.83115  ?  1321 LEU   A O   1 
ATOM   10511 C  CB  . LEU   A 1 1323 ? -2.94800   13.65000  -7.46000  1.000 61.07596  ?  1321 LEU   A CB  1 
ATOM   10512 C  CG  . LEU   A 1 1323 ? -1.53200   13.21700  -7.07600  1.000 86.65717  ?  1321 LEU   A CG  1 
ATOM   10513 C  CD1 . LEU   A 1 1323 ? -0.47400   14.11500  -7.70100  1.000 89.65304  ?  1321 LEU   A CD1 1 
ATOM   10514 C  CD2 . LEU   A 1 1323 ? -1.39200   13.19700  -5.56300  1.000 80.53318  ?  1321 LEU   A CD2 1 
ATOM   10515 N  N   . VAL   A 1 1324 ? -5.43800   12.16900  -8.91500  1.000 82.59086  ?  1322 VAL   A N   1 
ATOM   10516 C  CA  . VAL   A 1 1324 ? -6.87100   11.88900  -8.89400  1.000 52.69294  ?  1322 VAL   A CA  1 
ATOM   10517 C  C   . VAL   A 1 1324 ? -7.10700   10.72800  -7.93700  1.000 60.10562  ?  1322 VAL   A C   1 
ATOM   10518 O  O   . VAL   A 1 1324 ? -6.68100   9.60000   -8.21000  1.000 77.95752  ?  1322 VAL   A O   1 
ATOM   10519 C  CB  . VAL   A 1 1324 ? -7.43400   11.55000  -10.28200 1.000 59.28817  ?  1322 VAL   A CB  1 
ATOM   10520 C  CG1 . VAL   A 1 1324 ? -8.90300   11.19600  -10.16400 1.000 60.26138  ?  1322 VAL   A CG1 1 
ATOM   10521 C  CG2 . VAL   A 1 1324 ? -7.24000   12.70700  -11.25200 1.000 79.63620  ?  1322 VAL   A CG2 1 
ATOM   10522 N  N   . LEU   A 1 1325 ? -7.79000   10.99500  -6.82500  1.000 61.67037  ?  1323 LEU   A N   1 
ATOM   10523 C  CA  . LEU   A 1 1325 ? -8.21000   9.95200   -5.88900  1.000 51.60303  ?  1323 LEU   A CA  1 
ATOM   10524 C  C   . LEU   A 1 1325 ? -9.58900   9.46800   -6.31700  1.000 60.27329  ?  1323 LEU   A C   1 
ATOM   10525 O  O   . LEU   A 1 1325 ? -10.60200  10.11100  -6.03100  1.000 86.93248  ?  1323 LEU   A O   1 
ATOM   10526 C  CB  . LEU   A 1 1325 ? -8.22200   10.47800  -4.45800  1.000 34.52844  ?  1323 LEU   A CB  1 
ATOM   10527 C  CG  . LEU   A 1 1325 ? -7.02300   10.12100  -3.57900  1.000 51.97166  ?  1323 LEU   A CG  1 
ATOM   10528 C  CD1 . LEU   A 1 1325 ? -5.72800   10.52000  -4.25900  1.000 62.54433  ?  1323 LEU   A CD1 1 
ATOM   10529 C  CD2 . LEU   A 1 1325 ? -7.14400   10.78200  -2.21300  1.000 50.80980  ?  1323 LEU   A CD2 1 
ATOM   10530 N  N   . ALA   A 1 1326 ? -9.63400   8.32900   -7.00200  1.000 57.94609  ?  1324 ALA   A N   1 
ATOM   10531 C  CA  . ALA   A 1 1326 ? -10.87000  7.80100   -7.55700  1.000 73.04255  ?  1324 ALA   A CA  1 
ATOM   10532 C  C   . ALA   A 1 1326 ? -11.18300  6.43200   -6.96700  1.000 73.13930  ?  1324 ALA   A C   1 
ATOM   10533 O  O   . ALA   A 1 1326 ? -10.31600  5.75500   -6.40800  1.000 75.90716  ?  1324 ALA   A O   1 
ATOM   10534 C  CB  . ALA   A 1 1326 ? -10.79100  7.69800   -9.08600  1.000 57.19408  ?  1324 ALA   A CB  1 
ATOM   10535 N  N   . GLN   A 1 1327 ? -12.44700  6.03700   -7.09300  1.000 74.97897  ?  1325 GLN   A N   1 
ATOM   10536 C  CA  . GLN   A 1 1327 ? -12.85300  4.68600   -6.74500  1.000 79.54484  ?  1325 GLN   A CA  1 
ATOM   10537 C  C   . GLN   A 1 1327 ? -12.56400  3.73800   -7.90600  1.000 89.04940  ?  1325 GLN   A C   1 
ATOM   10538 O  O   . GLN   A 1 1327 ? -12.27100  4.15700   -9.03000  1.000 95.05988  ?  1325 GLN   A O   1 
ATOM   10539 C  CB  . GLN   A 1 1327 ? -14.33600  4.64400   -6.37200  1.000 60.39210  ?  1325 GLN   A CB  1 
ATOM   10540 C  CG  . GLN   A 1 1327 ? -14.62600  5.03200   -4.92700  1.000 68.51434  ?  1325 GLN   A CG  1 
ATOM   10541 C  CD  . GLN   A 1 1327 ? -16.11200  5.07400   -4.61600  1.000 66.35752  ?  1325 GLN   A CD  1 
ATOM   10542 O  OE1 . GLN   A 1 1327 ? -16.93700  5.31600   -5.49800  1.000 55.44641  ?  1325 GLN   A OE1 1 
ATOM   10543 N  NE2 . GLN   A 1 1327 ? -16.46000  4.83700   -3.35600  1.000 45.71984  ?  1325 GLN   A NE2 1 
ATOM   10544 N  N   . SER   A 1 1328 ? -12.64600  2.44000   -7.61700  1.000 79.06801  ?  1326 SER   A N   1 
ATOM   10545 C  CA  . SER   A 1 1328 ? -12.34400  1.41500   -8.61600  1.000 70.67639  ?  1326 SER   A CA  1 
ATOM   10546 C  C   . SER   A 1 1328 ? -13.15200  1.55400   -9.90100  1.000 69.09856  ?  1326 SER   A C   1 
ATOM   10547 O  O   . SER   A 1 1328 ? -12.55000  1.48800   -10.98500 1.000 65.42474  ?  1326 SER   A O   1 
ATOM   10548 C  CB  . SER   A 1 1328 ? -12.54400  0.02700   -7.99200  1.000 83.41311  ?  1326 SER   A CB  1 
ATOM   10549 O  OG  . SER   A 1 1328 ? -12.11300  0.01300   -6.64400  1.000 93.86801  ?  1326 SER   A OG  1 
ATOM   10550 N  N   . PRO   A 1 1329 ? -14.47800  1.74500   -9.87400  1.000 73.24160  ?  1327 PRO   A N   1 
ATOM   10551 C  CA  . PRO   A 1 1329 ? -15.22200  1.84000   -11.14100 1.000 68.91397  ?  1327 PRO   A CA  1 
ATOM   10552 C  C   . PRO   A 1 1329 ? -14.91200  3.08700   -11.95500 1.000 74.87697  ?  1327 PRO   A C   1 
ATOM   10553 O  O   . PRO   A 1 1329 ? -15.40800  3.19800   -13.08400 1.000 66.00824  ?  1327 PRO   A O   1 
ATOM   10554 C  CB  . PRO   A 1 1329 ? -16.69100  1.83100   -10.69100 1.000 47.12822  ?  1327 PRO   A CB  1 
ATOM   10555 C  CG  . PRO   A 1 1329 ? -16.67400  1.27900   -9.30500  1.000 58.24917  ?  1327 PRO   A CG  1 
ATOM   10556 C  CD  . PRO   A 1 1329 ? -15.39300  1.76200   -8.71800  1.000 59.27448  ?  1327 PRO   A CD  1 
ATOM   10557 N  N   . PHE   A 1 1330 ? -14.11500  4.02200   -11.43500 1.000 81.72819  ?  1328 PHE   A N   1 
ATOM   10558 C  CA  . PHE   A 1 1330 ? -13.85300  5.28000   -12.12300 1.000 81.38313  ?  1328 PHE   A CA  1 
ATOM   10559 C  C   . PHE   A 1 1330 ? -12.36700  5.54300   -12.33600 1.000 85.54260  ?  1328 PHE   A C   1 
ATOM   10560 O  O   . PHE   A 1 1330 ? -12.00200  6.64400   -12.76800 1.000 87.38690  ?  1328 PHE   A O   1 
ATOM   10561 C  CB  . PHE   A 1 1330 ? -14.48500  6.44300   -11.35300 1.000 73.34579  ?  1328 PHE   A CB  1 
ATOM   10562 C  CG  . PHE   A 1 1330 ? -15.82400  6.11500   -10.75700 1.000 60.64597  ?  1328 PHE   A CG  1 
ATOM   10563 C  CD1 . PHE   A 1 1330 ? -16.92200  5.88100   -11.56900 1.000 54.74036  ?  1328 PHE   A CD1 1 
ATOM   10564 C  CD2 . PHE   A 1 1330 ? -15.98400  6.04100   -9.38400  1.000 68.88488  ?  1328 PHE   A CD2 1 
ATOM   10565 C  CE1 . PHE   A 1 1330 ? -18.15400  5.57600   -11.02200 1.000 62.72902  ?  1328 PHE   A CE1 1 
ATOM   10566 C  CE2 . PHE   A 1 1330 ? -17.21400  5.73800   -8.82900  1.000 69.64182  ?  1328 PHE   A CE2 1 
ATOM   10567 C  CZ  . PHE   A 1 1330 ? -18.30000  5.50600   -9.65000  1.000 68.25674  ?  1328 PHE   A CZ  1 
ATOM   10568 N  N   . VAL   A 1 1331 ? -11.50100  4.57000   -12.04400 1.000 86.16451  ?  1329 VAL   A N   1 
ATOM   10569 C  CA  . VAL   A 1 1331 ? -10.07400  4.74500   -12.30400 1.000 83.92939  ?  1329 VAL   A CA  1 
ATOM   10570 C  C   . VAL   A 1 1331 ? -9.82000   4.88500   -13.80000 1.000 82.89700  ?  1329 VAL   A C   1 
ATOM   10571 O  O   . VAL   A 1 1331 ? -9.00800   5.71400   -14.23300 1.000 82.60635  ?  1329 VAL   A O   1 
ATOM   10572 C  CB  . VAL   A 1 1331 ? -9.27100   3.58100   -11.69100 1.000 72.27728  ?  1329 VAL   A CB  1 
ATOM   10573 C  CG1 . VAL   A 1 1331 ? -7.95300   3.39200   -12.42200 1.000 76.45173  ?  1329 VAL   A CG1 1 
ATOM   10574 C  CG2 . VAL   A 1 1331 ? -9.02100   3.83400   -10.21000 1.000 72.90855  ?  1329 VAL   A CG2 1 
ATOM   10575 N  N   . GLU   A 1 1332 ? -10.52300  4.09200   -14.61600 1.000 90.28186  ?  1330 GLU   A N   1 
ATOM   10576 C  CA  . GLU   A 1 1332 ? -10.41000  4.21300   -16.06500 1.000 98.64097  ?  1330 GLU   A CA  1 
ATOM   10577 C  C   . GLU   A 1 1332 ? -10.89200  5.56700   -16.57800 1.000 105.42945 ?  1330 GLU   A C   1 
ATOM   10578 O  O   . GLU   A 1 1332 ? -10.44500  6.00000   -17.64500 1.000 108.11634 ?  1330 GLU   A O   1 
ATOM   10579 C  CB  . GLU   A 1 1332 ? -11.18900  3.08500   -16.74700 1.000 83.98836  ?  1330 GLU   A CB  1 
ATOM   10580 N  N   . LYS   A 1 1333 ? -11.79100  6.24100   -15.84800 1.000 99.49223  ?  1331 LYS   A N   1 
ATOM   10581 C  CA  . LYS   A 1 1333 ? -12.23800  7.57200   -16.25300 1.000 90.99706  ?  1331 LYS   A CA  1 
ATOM   10582 C  C   . LYS   A 1 1333 ? -11.15900  8.62800   -16.03500 1.000 92.06094  ?  1331 LYS   A C   1 
ATOM   10583 O  O   . LYS   A 1 1333 ? -11.02600  9.54600   -16.85400 1.000 97.87515  ?  1331 LYS   A O   1 
ATOM   10584 C  CB  . LYS   A 1 1333 ? -13.51800  7.94600   -15.50500 1.000 77.88246  ?  1331 LYS   A CB  1 
ATOM   10585 C  CG  . LYS   A 1 1333 ? -14.68200  7.03000   -15.80500 1.000 78.86208  ?  1331 LYS   A CG  1 
ATOM   10586 C  CD  . LYS   A 1 1333 ? -15.93600  7.49000   -15.10700 1.000 65.71534  ?  1331 LYS   A CD  1 
ATOM   10587 C  CE  . LYS   A 1 1333 ? -17.11100  7.41000   -16.05900 1.000 63.74462  ?  1331 LYS   A CE  1 
ATOM   10588 N  NZ  . LYS   A 1 1333 ? -18.41200  7.32600   -15.34800 1.000 65.74884  ?  1331 LYS   A NZ  1 
ATOM   10589 N  N   . ALA   A 1 1334 ? -10.38700  8.52200   -14.94400 1.000 75.58215  ?  1332 ALA   A N   1 
ATOM   10590 C  CA  . ALA   A 1 1334 ? -9.20600   9.34800   -14.71800 1.000 79.59072  ?  1332 ALA   A CA  1 
ATOM   10591 C  C   . ALA   A 1 1334 ? -8.01000   8.88500   -15.56100 1.000 101.32470 ?  1332 ALA   A C   1 
ATOM   10592 O  O   . ALA   A 1 1334 ? -6.86100   9.06900   -15.14000 1.000 84.19075  ?  1332 ALA   A O   1 
ATOM   10593 C  CB  . ALA   A 1 1334 ? -8.82200   9.34700   -13.23600 1.000 83.08966  ?  1332 ALA   A CB  1 
ATOM   10594 N  N   . SER   A 1 1335 ? -8.24800   8.29000   -16.74000 1.000 121.00448 ?  1333 SER   A N   1 
ATOM   10595 C  CA  . SER   A 1 1335 ? -7.14200   7.81100   -17.57500 1.000 105.27200 ?  1333 SER   A CA  1 
ATOM   10596 C  C   . SER   A 1 1335 ? -6.15000   8.92400   -17.89200 1.000 105.07516 ?  1333 SER   A C   1 
ATOM   10597 O  O   . SER   A 1 1335 ? -4.93700   8.72400   -17.81800 1.000 96.11947  ?  1333 SER   A O   1 
ATOM   10598 C  CB  . SER   A 1 1335 ? -7.69600   7.20800   -18.86800 1.000 86.91918  ?  1333 SER   A CB  1 
ATOM   10599 O  OG  . SER   A 1 1335 ? -8.46700   8.15500   -19.57400 1.000 96.24984  ?  1333 SER   A OG  1 
ATOM   10600 N  N   . MET   A 1 1336 ? -6.64400   10.10300  -18.26300 1.000 109.71152 ?  1334 MET   A N   1 
ATOM   10601 C  CA  . MET   A 1 1336 ? -5.75800   11.19000  -18.68200 1.000 104.32608 ?  1334 MET   A CA  1 
ATOM   10602 C  C   . MET   A 1 1336 ? -5.44200   12.10800  -17.50000 1.000 90.12582  ?  1334 MET   A C   1 
ATOM   10603 O  O   . MET   A 1 1336 ? -5.80300   13.28900  -17.45000 1.000 104.51448 ?  1334 MET   A O   1 
ATOM   10604 C  CB  . MET   A 1 1336 ? -6.37400   11.95700  -19.83600 1.000 93.79539  ?  1334 MET   A CB  1 
ATOM   10605 C  CG  . MET   A 1 1336 ? -5.95500   11.38200  -21.19100 1.000 87.63029  ?  1334 MET   A CG  1 
ATOM   10606 S  SD  . MET   A 1 1336 ? -4.45000   10.34000  -21.36200 1.000 146.25612 ?  1334 MET   A SD  1 
ATOM   10607 C  CE  . MET   A 1 1336 ? -3.03700   11.35700  -20.83700 1.000 80.12206  ?  1334 MET   A CE  1 
ATOM   10608 N  N   . ALA   A 1 1337 ? -4.76300   11.52400  -16.51500 1.000 76.88789  ?  1335 ALA   A N   1 
ATOM   10609 C  CA  . ALA   A 1 1337 ? -4.16600   12.28200  -15.42300 1.000 82.73070  ?  1335 ALA   A CA  1 
ATOM   10610 C  C   . ALA   A 1 1337 ? -2.68000   11.96000  -15.33500 1.000 82.16335  ?  1335 ALA   A C   1 
ATOM   10611 O  O   . ALA   A 1 1337 ? -2.02300   11.74500  -16.35900 1.000 94.84401  ?  1335 ALA   A O   1 
ATOM   10612 C  CB  . ALA   A 1 1337 ? -4.86900   11.96300  -14.10300 1.000 78.31105  ?  1335 ALA   A CB  1 
ATOM   10613 N  N   . GLU   A 1 1338 ? -2.14400   11.92400  -14.12000 1.000 76.29427  ?  1336 GLU   A N   1 
ATOM   10614 C  CA  . GLU   A 1 1338 ? -0.77500   11.47300  -13.91300 1.000 91.77442  ?  1336 GLU   A CA  1 
ATOM   10615 C  C   . GLU   A 1 1338 ? -0.74100   10.39600  -12.83700 1.000 89.73229  ?  1336 GLU   A C   1 
ATOM   10616 O  O   . GLU   A 1 1338 ? -0.38600   9.24400   -13.10900 1.000 102.29226 ?  1336 GLU   A O   1 
ATOM   10617 C  CB  . GLU   A 1 1338 ? 0.13600    12.64200  -13.53000 1.000 99.73606  ?  1336 GLU   A CB  1 
ATOM   10618 C  CG  . GLU   A 1 1338 ? 0.26700    13.70900  -14.60500 1.000 109.93063 ?  1336 GLU   A CG  1 
ATOM   10619 C  CD  . GLU   A 1 1338 ? 1.70400    13.92900  -15.03800 1.000 118.72703 ?  1336 GLU   A CD  1 
ATOM   10620 O  OE1 . GLU   A 1 1338 ? 2.57500    13.12300  -14.64800 1.000 126.19056 ?  1336 GLU   A OE1 1 
ATOM   10621 O  OE2 . GLU   A 1 1338 ? 1.96200    14.90800  -15.77000 1.000 120.16144 -1 1336 GLU   A OE2 1 
ATOM   10622 N  N   . VAL   A 1 1339 ? -1.12300   10.76000  -11.61800 1.000 80.00885  ?  1337 VAL   A N   1 
ATOM   10623 C  CA  . VAL   A 1 1339 ? -1.12300   9.85400   -10.47700 1.000 83.46557  ?  1337 VAL   A CA  1 
ATOM   10624 C  C   . VAL   A 1 1339 ? -2.58000   9.53700   -10.16200 1.000 83.60507  ?  1337 VAL   A C   1 
ATOM   10625 O  O   . VAL   A 1 1339 ? -3.29200   10.35100  -9.56300  1.000 84.34723  ?  1337 VAL   A O   1 
ATOM   10626 C  CB  . VAL   A 1 1339 ? -0.40300   10.46200  -9.26900  1.000 83.61257  ?  1337 VAL   A CB  1 
ATOM   10627 C  CG1 . VAL   A 1 1339 ? 0.01700    9.37500   -8.28900  1.000 78.66523  ?  1337 VAL   A CG1 1 
ATOM   10628 C  CG2 . VAL   A 1 1339 ? 0.79500    11.28200  -9.72700  1.000 67.86105  ?  1337 VAL   A CG2 1 
ATOM   10629 N  N   . VAL   A 1 1340 ? -3.03200   8.35400   -10.56900 1.000 94.23227  ?  1338 VAL   A N   1 
ATOM   10630 C  CA  . VAL   A 1 1340 ? -4.40100   7.90200   -10.34600 1.000 74.12804  ?  1338 VAL   A CA  1 
ATOM   10631 C  C   . VAL   A 1 1340 ? -4.35900   6.77100   -9.33000  1.000 73.54802  ?  1338 VAL   A C   1 
ATOM   10632 O  O   . VAL   A 1 1340 ? -3.68500   5.75700   -9.54800  1.000 88.49533  ?  1338 VAL   A O   1 
ATOM   10633 C  CB  . VAL   A 1 1340 ? -5.06600   7.44300   -11.65200 1.000 64.81155  ?  1338 VAL   A CB  1 
ATOM   10634 C  CG1 . VAL   A 1 1340 ? -6.54100   7.15100   -11.42400 1.000 66.11790  ?  1338 VAL   A CG1 1 
ATOM   10635 C  CG2 . VAL   A 1 1340 ? -4.87600   8.49100   -12.73400 1.000 72.89665  ?  1338 VAL   A CG2 1 
ATOM   10636 N  N   . LEU   A 1 1341 ? -5.07700   6.94000   -8.22300  1.000 71.93735  ?  1339 LEU   A N   1 
ATOM   10637 C  CA  . LEU   A 1 1341 ? -5.07200   5.97500   -7.13200  1.000 78.26605  ?  1339 LEU   A CA  1 
ATOM   10638 C  C   . LEU   A 1 1341 ? -6.47500   5.42400   -6.92600  1.000 78.29727  ?  1339 LEU   A C   1 
ATOM   10639 O  O   . LEU   A 1 1341 ? -7.44500   6.18700   -6.87500  1.000 83.99150  ?  1339 LEU   A O   1 
ATOM   10640 C  CB  . LEU   A 1 1341 ? -4.56000   6.60700   -5.83300  1.000 57.06557  ?  1339 LEU   A CB  1 
ATOM   10641 C  CG  . LEU   A 1 1341 ? -3.20600   7.32600   -5.82500  1.000 65.21642  ?  1339 LEU   A CG  1 
ATOM   10642 C  CD1 . LEU   A 1 1341 ? -2.67700   7.42400   -4.40200  1.000 61.53988  ?  1339 LEU   A CD1 1 
ATOM   10643 C  CD2 . LEU   A 1 1341 ? -2.18300   6.65300   -6.72900  1.000 69.62524  ?  1339 LEU   A CD2 1 
ATOM   10644 N  N   . ASP   A 1 1342 ? -6.57700   4.10200   -6.81100  1.000 78.10156  ?  1340 ASP   A N   1 
ATOM   10645 C  CA  . ASP   A 1 1342 ? -7.83600   3.45500   -6.46500  1.000 71.31740  ?  1340 ASP   A CA  1 
ATOM   10646 C  C   . ASP   A 1 1342 ? -8.02800   3.51400   -4.95400  1.000 80.33978  ?  1340 ASP   A C   1 
ATOM   10647 O  O   . ASP   A 1 1342 ? -7.17400   3.04100   -4.19600  1.000 65.42089  ?  1340 ASP   A O   1 
ATOM   10648 C  CB  . ASP   A 1 1342 ? -7.84600   2.00800   -6.95500  1.000 82.73167  ?  1340 ASP   A CB  1 
ATOM   10649 C  CG  . ASP   A 1 1342 ? -9.06600   1.23600   -6.48000  1.000 83.06672  ?  1340 ASP   A CG  1 
ATOM   10650 O  OD1 . ASP   A 1 1342 ? -10.12100  1.86200   -6.23900  1.000 83.92293  ?  1340 ASP   A OD1 1 
ATOM   10651 O  OD2 . ASP   A 1 1342 ? -8.96700   0.00000   -6.33600  1.000 78.92791  -1 1340 ASP   A OD2 1 
ATOM   10652 N  N   . LEU   A 1 1343 ? -9.14700   4.09000   -4.51800  1.000 83.42087  ?  1341 LEU   A N   1 
ATOM   10653 C  CA  . LEU   A 1 1343 ? -9.43300   4.21900   -3.09600  1.000 69.06508  ?  1341 LEU   A CA  1 
ATOM   10654 C  C   . LEU   A 1 1343 ? -9.90300   2.91700   -2.46100  1.000 69.29406  ?  1341 LEU   A C   1 
ATOM   10655 O  O   . LEU   A 1 1343 ? -10.01500  2.85400   -1.23200  1.000 72.94002  ?  1341 LEU   A O   1 
ATOM   10656 C  CB  . LEU   A 1 1343 ? -10.48100  5.31200   -2.87500  1.000 81.18108  ?  1341 LEU   A CB  1 
ATOM   10657 C  CG  . LEU   A 1 1343 ? -10.03700  6.73000   -3.24100  1.000 68.23057  ?  1341 LEU   A CG  1 
ATOM   10658 C  CD1 . LEU   A 1 1343 ? -11.23300  7.66000   -3.34600  1.000 52.14502  ?  1341 LEU   A CD1 1 
ATOM   10659 C  CD2 . LEU   A 1 1343 ? -9.03700   7.25300   -2.22100  1.000 57.69480  ?  1341 LEU   A CD2 1 
ATOM   10660 N  N   . ASN   A 1 1344 ? -10.17900  1.88600   -3.25700  1.000 70.39006  ?  1342 ASN   A N   1 
ATOM   10661 C  CA  . ASN   A 1 1344 ? -10.60000  0.59000   -2.74400  1.000 75.26785  ?  1342 ASN   A CA  1 
ATOM   10662 C  C   . ASN   A 1 1344 ? -9.48500   -0.44500  -2.79400  1.000 77.63131  ?  1342 ASN   A C   1 
ATOM   10663 O  O   . ASN   A 1 1344 ? -9.74700   -1.63600  -2.59800  1.000 72.78740  ?  1342 ASN   A O   1 
ATOM   10664 C  CB  . ASN   A 1 1344 ? -11.81700  0.08700   -3.51900  1.000 69.46070  ?  1342 ASN   A CB  1 
ATOM   10665 C  CG  . ASN   A 1 1344 ? -12.86700  1.16100   -3.71000  1.000 71.70824  ?  1342 ASN   A CG  1 
ATOM   10666 O  OD1 . ASN   A 1 1344 ? -13.19300  1.53300   -4.83800  1.000 79.03146  ?  1342 ASN   A OD1 1 
ATOM   10667 N  ND2 . ASN   A 1 1344 ? -13.40100  1.67100   -2.60600  1.000 68.83469  ?  1342 ASN   A ND2 1 
ATOM   10668 N  N   . SER   A 1 1345 ? -8.25300   -0.01900  -3.05900  1.000 89.81082  ?  1343 SER   A N   1 
ATOM   10669 C  CA  . SER   A 1 1345 ? -7.08900   -0.89400  -3.08300  1.000 86.62926  ?  1343 SER   A CA  1 
ATOM   10670 C  C   . SER   A 1 1345 ? -6.13100   -0.47300  -1.98000  1.000 65.80182  ?  1343 SER   A C   1 
ATOM   10671 O  O   . SER   A 1 1345 ? -5.81900   0.71500   -1.84500  1.000 71.96351  ?  1343 SER   A O   1 
ATOM   10672 C  CB  . SER   A 1 1345 ? -6.38800   -0.84200  -4.44400  1.000 61.21899  ?  1343 SER   A CB  1 
ATOM   10673 O  OG  . SER   A 1 1345 ? -5.12900   -1.49000  -4.39700  1.000 69.22788  ?  1343 SER   A OG  1 
ATOM   10674 N  N   . ALA   A 1 1346 ? -5.66300   -1.44600  -1.19500  1.000 65.61679  ?  1344 ALA   A N   1 
ATOM   10675 C  CA  . ALA   A 1 1346 ? -4.72700   -1.15400  -0.11600  1.000 68.63080  ?  1344 ALA   A CA  1 
ATOM   10676 C  C   . ALA   A 1 1346 ? -3.36300   -0.70100  -0.62200  1.000 75.05014  ?  1344 ALA   A C   1 
ATOM   10677 O  O   . ALA   A 1 1346 ? -2.53100   -0.28100  0.18900   1.000 66.36385  ?  1344 ALA   A O   1 
ATOM   10678 C  CB  . ALA   A 1 1346 ? -4.56600   -2.37900  0.78700   1.000 53.79679  ?  1344 ALA   A CB  1 
ATOM   10679 N  N   . SER   A 1 1347 ? -3.11300   -0.77800  -1.93200  1.000 65.15219  ?  1345 SER   A N   1 
ATOM   10680 C  CA  . SER   A 1 1347 ? -1.86800   -0.24800  -2.47700  1.000 64.13333  ?  1345 SER   A CA  1 
ATOM   10681 C  C   . SER   A 1 1347 ? -1.83300   1.27200   -2.38400  1.000 79.39527  ?  1345 SER   A C   1 
ATOM   10682 O  O   . SER   A 1 1347 ? -0.78900   1.85800   -2.07700  1.000 86.67630  ?  1345 SER   A O   1 
ATOM   10683 C  CB  . SER   A 1 1347 ? -1.69000   -0.70300  -3.92600  1.000 75.04530  ?  1345 SER   A CB  1 
ATOM   10684 O  OG  . SER   A 1 1347 ? -2.63800   -0.08700  -4.78100  1.000 84.48805  ?  1345 SER   A OG  1 
ATOM   10685 N  N   . SER   A 1 1348 ? -2.96600   1.92600   -2.63500  1.000 72.98034  ?  1346 SER   A N   1 
ATOM   10686 C  CA  . SER   A 1 1348 ? -3.04200   3.37700   -2.53100  1.000 61.97300  ?  1346 SER   A CA  1 
ATOM   10687 C  C   . SER   A 1 1348 ? -3.03100   3.87000   -1.08900  1.000 68.84179  ?  1346 SER   A C   1 
ATOM   10688 O  O   . SER   A 1 1348 ? -3.06600   5.08600   -0.87100  1.000 83.53686  ?  1346 SER   A O   1 
ATOM   10689 C  CB  . SER   A 1 1348 ? -4.29500   3.88100   -3.24800  1.000 74.45269  ?  1346 SER   A CB  1 
ATOM   10690 O  OG  . SER   A 1 1348 ? -4.36000   3.37200   -4.57000  1.000 64.38901  ?  1346 SER   A OG  1 
ATOM   10691 N  N   . TYR   A 1 1349 ? -2.98900   2.97000   -0.11200  1.000 58.49271  ?  1347 TYR   A N   1 
ATOM   10692 C  CA  . TYR   A 1 1349 ? -2.87800   3.31600   1.29700   1.000 52.89883  ?  1347 TYR   A CA  1 
ATOM   10693 C  C   . TYR   A 1 1349 ? -1.52400   2.86500   1.82900   1.000 66.92232  ?  1347 TYR   A C   1 
ATOM   10694 O  O   . TYR   A 1 1349 ? -0.78200   2.12800   1.17300   1.000 68.69504  ?  1347 TYR   A O   1 
ATOM   10695 C  CB  . TYR   A 1 1349 ? -4.01500   2.68100   2.10800   1.000 66.70381  ?  1347 TYR   A CB  1 
ATOM   10696 C  CG  . TYR   A 1 1349 ? -5.39800   3.16000   1.71900   1.000 82.81868  ?  1347 TYR   A CG  1 
ATOM   10697 C  CD1 . TYR   A 1 1349 ? -6.02000   2.69000   0.56900   1.000 64.25213  ?  1347 TYR   A CD1 1 
ATOM   10698 C  CD2 . TYR   A 1 1349 ? -6.08600   4.07600   2.50700   1.000 81.01654  ?  1347 TYR   A CD2 1 
ATOM   10699 C  CE1 . TYR   A 1 1349 ? -7.28100   3.12200   0.21000   1.000 68.48603  ?  1347 TYR   A CE1 1 
ATOM   10700 C  CE2 . TYR   A 1 1349 ? -7.35100   4.51400   2.15500   1.000 76.20562  ?  1347 TYR   A CE2 1 
ATOM   10701 C  CZ  . TYR   A 1 1349 ? -7.94300   4.03200   1.00500   1.000 72.02205  ?  1347 TYR   A CZ  1 
ATOM   10702 O  OH  . TYR   A 1 1349 ? -9.20000   4.46200   0.64800   1.000 60.98177  ?  1347 TYR   A OH  1 
ATOM   10703 N  N   . ALA   A 1 1350 ? -1.20100   3.32200   3.03800   1.000 74.50721  ?  1348 ALA   A N   1 
ATOM   10704 C  CA  . ALA   A 1 1350 ? 0.08000    2.98900   3.64700   1.000 59.07325  ?  1348 ALA   A CA  1 
ATOM   10705 C  C   . ALA   A 1 1350 ? -0.11600   2.37700   5.02600   1.000 62.96897  ?  1348 ALA   A C   1 
ATOM   10706 O  O   . ALA   A 1 1350 ? -1.24700   2.09000   5.43000   1.000 69.07054  ?  1348 ALA   A O   1 
ATOM   10707 C  CB  . ALA   A 1 1350 ? 0.97400    4.22700   3.73700   1.000 56.38812  ?  1348 ALA   A CB  1 
ATOM   10708 N  N   . ALA   A 1 1351 ? 0.98200    2.18400   5.75700   1.000 62.90696  ?  1349 ALA   A N   1 
ATOM   10709 C  CA  . ALA   A 1 1351 ? 0.94300    1.51700   7.05000   1.000 58.44698  ?  1349 ALA   A CA  1 
ATOM   10710 C  C   . ALA   A 1 1351 ? 0.98200    2.47100   8.23400   1.000 60.55691  ?  1349 ALA   A C   1 
ATOM   10711 O  O   . ALA   A 1 1351 ? 0.51600    2.10300   9.31800   1.000 61.81583  ?  1349 ALA   A O   1 
ATOM   10712 C  CB  . ALA   A 1 1351 ? 2.11300    0.53300   7.17300   1.000 45.03732  ?  1349 ALA   A CB  1 
ATOM   10713 N  N   . ASP   A 1 1352 ? 1.51900    3.67400   8.05800   1.000 68.80805  ?  1350 ASP   A N   1 
ATOM   10714 C  CA  . ASP   A 1 1352 ? 1.73600    4.58100   9.17900   1.000 75.71560  ?  1350 ASP   A CA  1 
ATOM   10715 C  C   . ASP   A 1 1352 ? 0.40000    5.12900   9.66600   1.000 79.42163  ?  1350 ASP   A C   1 
ATOM   10716 O  O   . ASP   A 1 1352 ? -0.26000   5.89900   8.96100   1.000 79.21639  ?  1350 ASP   A O   1 
ATOM   10717 C  CB  . ASP   A 1 1352 ? 2.67600    5.70800   8.76400   1.000 74.12517  ?  1350 ASP   A CB  1 
ATOM   10718 C  CG  . ASP   A 1 1352 ? 3.31000    6.40300   9.95200   1.000 88.74123  ?  1350 ASP   A CG  1 
ATOM   10719 O  OD1 . ASP   A 1 1352 ? 3.14300    5.91000   11.08700  1.000 89.18382  ?  1350 ASP   A OD1 1 
ATOM   10720 O  OD2 . ASP   A 1 1352 ? 3.97700    7.44100   9.75100   1.000 86.04048  -1 1350 ASP   A OD2 1 
ATOM   10721 N  N   . THR   A 1 1353 ? -0.00400   4.72800   10.86900  1.000 83.45146  ?  1351 THR   A N   1 
ATOM   10722 C  CA  . THR   A 1 1353 ? -1.17900   5.28900   11.52300  1.000 77.52110  ?  1351 THR   A CA  1 
ATOM   10723 C  C   . THR   A 1 1353 ? -0.86300   6.56800   12.28800  1.000 83.04428  ?  1351 THR   A C   1 
ATOM   10724 O  O   . THR   A 1 1353 ? -1.68600   7.01100   13.09700  1.000 70.48054  ?  1351 THR   A O   1 
ATOM   10725 C  CB  . THR   A 1 1353 ? -1.80200   4.26100   12.47100  1.000 82.70156  ?  1351 THR   A CB  1 
ATOM   10726 O  OG1 . THR   A 1 1353 ? -0.83700   3.86700   13.45500  1.000 74.70544  ?  1351 THR   A OG1 1 
ATOM   10727 C  CG2 . THR   A 1 1353 ? -2.26500   3.03400   11.69800  1.000 58.72562  ?  1351 THR   A CG2 1 
ATOM   10728 N  N   . SER   A 1 1354 ? 0.30600    7.15700   12.05300  1.000 83.46199  ?  1352 SER   A N   1 
ATOM   10729 C  CA  . SER   A 1 1354 ? 0.69500    8.38600   12.72700  1.000 78.46165  ?  1352 SER   A CA  1 
ATOM   10730 C  C   . SER   A 1 1354 ? 0.06200    9.58800   12.04100  1.000 72.14597  ?  1352 SER   A C   1 
ATOM   10731 O  O   . SER   A 1 1354 ? -0.06000   9.62600   10.81400  1.000 71.69787  ?  1352 SER   A O   1 
ATOM   10732 C  CB  . SER   A 1 1354 ? 2.21700    8.53700   12.73200  1.000 89.28419  ?  1352 SER   A CB  1 
ATOM   10733 O  OG  . SER   A 1 1354 ? 2.85000    7.38400   13.25700  1.000 103.33430 ?  1352 SER   A OG  1 
ATOM   10734 N  N   . ASN   A 1 1355 ? -0.34000   10.56700  12.84100  1.000 66.76030  ?  1353 ASN   A N   1 
ATOM   10735 C  CA  . ASN   A 1 1355 ? -0.87300   11.80900  12.30200  1.000 55.29857  ?  1353 ASN   A CA  1 
ATOM   10736 C  C   . ASN   A 1 1355 ? 0.21700    12.53900  11.52600  1.000 58.66889  ?  1353 ASN   A C   1 
ATOM   10737 O  O   . ASN   A 1 1355 ? 1.25600    12.88400  12.11000  1.000 74.56305  ?  1353 ASN   A O   1 
ATOM   10738 C  CB  . ASN   A 1 1355 ? -1.41300   12.70000  13.41900  1.000 52.88393  ?  1353 ASN   A CB  1 
ATOM   10739 C  CG  . ASN   A 1 1355 ? -2.77500   12.25300  13.91700  1.000 74.62011  ?  1353 ASN   A CG  1 
ATOM   10740 O  OD1 . ASN   A 1 1355 ? -3.52000   11.58200  13.20200  1.000 67.96232  ?  1353 ASN   A OD1 1 
ATOM   10741 N  ND2 . ASN   A 1 1355 ? -3.11100   12.63200  15.14600  1.000 53.29504  ?  1353 ASN   A ND2 1 
ATOM   10742 N  N   . PRO   A 1 1356 ? 0.03600    12.78200  10.23100  1.000 66.39277  ?  1354 PRO   A N   1 
ATOM   10743 C  CA  . PRO   A 1 1356 ? 1.06400    13.48000  9.45000   1.000 71.36151  ?  1354 PRO   A CA  1 
ATOM   10744 C  C   . PRO   A 1 1356 ? 1.25300    14.90100  9.95200   1.000 82.32922  ?  1354 PRO   A C   1 
ATOM   10745 O  O   . PRO   A 1 1356 ? 0.38500    15.44000  10.65600  1.000 79.30102  ?  1354 PRO   A O   1 
ATOM   10746 C  CB  . PRO   A 1 1356 ? 0.49900    13.45300  8.02000   1.000 53.89416  ?  1354 PRO   A CB  1 
ATOM   10747 C  CG  . PRO   A 1 1356 ? -0.96800   13.26500  8.19200   1.000 73.02563  ?  1354 PRO   A CG  1 
ATOM   10748 C  CD  . PRO   A 1 1356 ? -1.12400   12.40400  9.40800   1.000 76.30595  ?  1354 PRO   A CD  1 
ATOM   10749 N  N   . PRO   A 1 1357 ? 2.37400    15.53900  9.62400   1.000 90.32928  ?  1355 PRO   A N   1 
ATOM   10750 C  CA  . PRO   A 1 1357 ? 2.66100    16.85500  10.20200  1.000 81.09394  ?  1355 PRO   A CA  1 
ATOM   10751 C  C   . PRO   A 1 1357 ? 1.74700    17.93600  9.65000   1.000 82.07721  ?  1355 PRO   A C   1 
ATOM   10752 O  O   . PRO   A 1 1357 ? 1.24400    17.85000  8.52600   1.000 67.24648  ?  1355 PRO   A O   1 
ATOM   10753 C  CB  . PRO   A 1 1357 ? 4.11800    17.10600  9.79800   1.000 70.62169  ?  1355 PRO   A CB  1 
ATOM   10754 C  CG  . PRO   A 1 1357 ? 4.28000    16.33200  8.53700   1.000 60.40087  ?  1355 PRO   A CG  1 
ATOM   10755 C  CD  . PRO   A 1 1357 ? 3.45000    15.09100  8.72000   1.000 73.14334  ?  1355 PRO   A CD  1 
ATOM   10756 N  N   . LEU   A 1 1358 ? 1.53900    18.96900  10.46400  1.000 82.28959  ?  1356 LEU   A N   1 
ATOM   10757 C  CA  . LEU   A 1 1358 ? 0.76000    20.12500  10.03700  1.000 68.01206  ?  1356 LEU   A CA  1 
ATOM   10758 C  C   . LEU   A 1 1358 ? 1.56600    20.94100  9.03300   1.000 68.64662  ?  1356 LEU   A C   1 
ATOM   10759 O  O   . LEU   A 1 1358 ? 2.65400    21.43100  9.35300   1.000 87.86138  ?  1356 LEU   A O   1 
ATOM   10760 C  CB  . LEU   A 1 1358 ? 0.37800    20.98700  11.23900  1.000 52.35806  ?  1356 LEU   A CB  1 
ATOM   10761 C  CG  . LEU   A 1 1358 ? -0.21200   20.29200  12.46600  1.000 86.87309  ?  1356 LEU   A CG  1 
ATOM   10762 C  CD1 . LEU   A 1 1358 ? 0.86200    20.07800  13.52400  1.000 66.07757  ?  1356 LEU   A CD1 1 
ATOM   10763 C  CD2 . LEU   A 1 1358 ? -1.38700   21.08400  13.02900  1.000 54.55196  ?  1356 LEU   A CD2 1 
ATOM   10764 N  N   . VAL   A 1 1359 ? 1.03300    21.08300  7.81800   1.000 62.18331  ?  1357 VAL   A N   1 
ATOM   10765 C  CA  . VAL   A 1 1359 ? 1.69200    21.83900  6.76200   1.000 58.04349  ?  1357 VAL   A CA  1 
ATOM   10766 C  C   . VAL   A 1 1359 ? 0.80100    22.91500  6.16900   1.000 86.56793  ?  1357 VAL   A C   1 
ATOM   10767 O  O   . VAL   A 1 1359 ? 1.23100    23.62400  5.25900   1.000 89.70207  ?  1357 VAL   A O   1 
ATOM   10768 C  CB  . VAL   A 1 1359 ? 2.21000    20.90500  5.64800   1.000 65.07179  ?  1357 VAL   A CB  1 
ATOM   10769 C  CG1 . VAL   A 1 1359 ? 3.41300    20.13100  6.13400   1.000 73.82841  ?  1357 VAL   A CG1 1 
ATOM   10770 C  CG2 . VAL   A 1 1359 ? 1.11000    19.95400  5.20000   1.000 80.68347  ?  1357 VAL   A CG2 1 
ATOM   10771 N  N   . ASN   A 1 1360 ? -0.42900   23.06100  6.65100   1.000 85.48402  ?  1358 ASN   A N   1 
ATOM   10772 C  CA  . ASN   A 1 1360 ? -1.37400   24.02200  6.10600   1.000 74.46243  ?  1358 ASN   A CA  1 
ATOM   10773 C  C   . ASN   A 1 1360 ? -1.52800   25.21700  7.03700   1.000 77.59271  ?  1358 ASN   A C   1 
ATOM   10774 O  O   . ASN   A 1 1360 ? -1.39800   25.09900  8.25800   1.000 72.35250  ?  1358 ASN   A O   1 
ATOM   10775 C  CB  . ASN   A 1 1360 ? -2.74300   23.38100  5.86800   1.000 73.09023  ?  1358 ASN   A CB  1 
ATOM   10776 C  CG  . ASN   A 1 1360 ? -2.77100   22.51600  4.62900   1.000 71.95013  ?  1358 ASN   A CG  1 
ATOM   10777 O  OD1 . ASN   A 1 1360 ? -3.42000   21.47100  4.60500   1.000 74.63163  ?  1358 ASN   A OD1 1 
ATOM   10778 N  ND2 . ASN   A 1 1360 ? -2.05800   22.94200  3.59200   1.000 65.51837  ?  1358 ASN   A ND2 1 
ATOM   10779 N  N   . GLN   A 1 1361 ? -1.82000   26.36700  6.44300   1.000 75.88621  ?  1359 GLN   A N   1 
ATOM   10780 C  CA  . GLN   A 1 1361 ? -2.02900   27.61900  7.14700   1.000 74.12207  ?  1359 GLN   A CA  1 
ATOM   10781 C  C   . GLN   A 1 1361 ? -3.43300   28.14100  6.86300   1.000 67.16673  ?  1359 GLN   A C   1 
ATOM   10782 O  O   . GLN   A 1 1361 ? -4.03500   27.79900  5.83700   1.000 60.25339  ?  1359 GLN   A O   1 
ATOM   10783 C  CB  . GLN   A 1 1361 ? -0.97300   28.65100  6.72900   1.000 78.41143  ?  1359 GLN   A CB  1 
ATOM   10784 C  CG  . GLN   A 1 1361 ? 0.20900    28.69700  7.68200   1.000 73.06054  ?  1359 GLN   A CG  1 
ATOM   10785 C  CD  . GLN   A 1 1361 ? 1.47000    29.22600  7.03600   1.000 91.41552  ?  1359 GLN   A CD  1 
ATOM   10786 O  OE1 . GLN   A 1 1361 ? 1.66400    29.09400  5.82800   1.000 105.28976 ?  1359 GLN   A OE1 1 
ATOM   10787 N  NE2 . GLN   A 1 1361 ? 2.33800    29.83100  7.84000   1.000 90.20956  ?  1359 GLN   A NE2 1 
ATOM   10788 N  N   . PRO   A 1 1362 ? -3.99500   28.97400  7.76500   1.000 56.27575  ?  1360 PRO   A N   1 
ATOM   10789 C  CA  . PRO   A 1 1362 ? -5.40200   29.38800  7.62600   1.000 48.98569  ?  1360 PRO   A CA  1 
ATOM   10790 C  C   . PRO   A 1 1362 ? -5.75400   30.03100  6.29100   1.000 45.88178  ?  1360 PRO   A C   1 
ATOM   10791 O  O   . PRO   A 1 1362 ? -6.93800   30.18800  5.97600   1.000 64.70880  ?  1360 PRO   A O   1 
ATOM   10792 C  CB  . PRO   A 1 1362 ? -5.58600   30.38600  8.77700   1.000 36.61955  ?  1360 PRO   A CB  1 
ATOM   10793 C  CG  . PRO   A 1 1362 ? -4.60300   29.94500  9.80200   1.000 55.94669  ?  1360 PRO   A CG  1 
ATOM   10794 C  CD  . PRO   A 1 1362 ? -3.41000   29.43100  9.04000   1.000 62.39562  ?  1360 PRO   A CD  1 
ATOM   10795 N  N   . GLY   A 1 1363 ? -4.75100   30.39800  5.49800   1.000 36.58618  ?  1361 GLY   A N   1 
ATOM   10796 C  CA  . GLY   A 1 1363 ? -5.00200   31.00900  4.20800   1.000 36.73299  ?  1361 GLY   A CA  1 
ATOM   10797 C  C   . GLY   A 1 1363 ? -4.71400   30.10100  3.03100   1.000 44.66147  ?  1361 GLY   A C   1 
ATOM   10798 O  O   . GLY   A 1 1363 ? -4.58500   30.57200  1.89700   1.000 38.21074  ?  1361 GLY   A O   1 
ATOM   10799 N  N   . ASP   A 1 1364 ? -4.61300   28.80000  3.28100   1.000 48.44872  ?  1362 ASP   A N   1 
ATOM   10800 C  CA  . ASP   A 1 1364 ? -4.33800   27.82500  2.23800   1.000 51.92518  ?  1362 ASP   A CA  1 
ATOM   10801 C  C   . ASP   A 1 1364 ? -5.63200   27.20500  1.73000   1.000 56.61102  ?  1362 ASP   A C   1 
ATOM   10802 O  O   . ASP   A 1 1364 ? -6.60100   27.04300  2.47700   1.000 62.71025  ?  1362 ASP   A O   1 
ATOM   10803 C  CB  . ASP   A 1 1364 ? -3.39900   26.73000  2.74800   1.000 67.62146  ?  1362 ASP   A CB  1 
ATOM   10804 C  CG  . ASP   A 1 1364 ? -1.96000   27.19100  2.82000   1.000 67.14477  ?  1362 ASP   A CG  1 
ATOM   10805 O  OD1 . ASP   A 1 1364 ? -1.49100   27.82600  1.85300   1.000 60.00204  ?  1362 ASP   A OD1 1 
ATOM   10806 O  OD2 . ASP   A 1 1364 ? -1.30100   26.92400  3.84800   1.000 75.06320  -1 1362 ASP   A OD2 1 
ATOM   10807 N  N   . LEU   A 1 1365 ? -5.63400   26.85300  0.44400   1.000 44.86706  ?  1363 LEU   A N   1 
ATOM   10808 C  CA  . LEU   A 1 1365 ? -6.83300   26.32000  -0.18900  1.000 53.89717  ?  1363 LEU   A CA  1 
ATOM   10809 C  C   . LEU   A 1 1365 ? -7.25000   24.99900  0.44500   1.000 57.59306  ?  1363 LEU   A C   1 
ATOM   10810 O  O   . LEU   A 1 1365 ? -6.42800   24.09700  0.63600   1.000 57.45674  ?  1363 LEU   A O   1 
ATOM   10811 C  CB  . LEU   A 1 1365 ? -6.60100   26.13200  -1.68800  1.000 45.30184  ?  1363 LEU   A CB  1 
ATOM   10812 C  CG  . LEU   A 1 1365 ? -6.54700   27.40800  -2.52900  1.000 43.85379  ?  1363 LEU   A CG  1 
ATOM   10813 C  CD1 . LEU   A 1 1365 ? -6.60400   27.07400  -4.01100  1.000 49.31809  ?  1363 LEU   A CD1 1 
ATOM   10814 C  CD2 . LEU   A 1 1365 ? -7.66900   28.36300  -2.14300  1.000 58.83166  ?  1363 LEU   A CD2 1 
ATOM   10815 N  N   . VAL   A 1 1366 ? -8.54000   24.88900  0.76300   1.000 59.01198  ?  1364 VAL   A N   1 
ATOM   10816 C  CA  . VAL   A 1 1366 ? -9.08700   23.67300  1.33600   1.000 48.69238  ?  1364 VAL   A CA  1 
ATOM   10817 C  C   . VAL   A 1 1366 ? -9.95300   22.89300  0.34600   1.000 53.46649  ?  1364 VAL   A C   1 
ATOM   10818 O  O   . VAL   A 1 1366 ? -10.00400  21.66000  0.43200   1.000 67.46086  ?  1364 VAL   A O   1 
ATOM   10819 C  CB  . VAL   A 1 1366 ? -9.87100   23.98200  2.63100   1.000 45.88214  ?  1364 VAL   A CB  1 
ATOM   10820 C  CG1 . VAL   A 1 1366 ? -11.23800  24.57000  2.31800   1.000 57.49023  ?  1364 VAL   A CG1 1 
ATOM   10821 C  CG2 . VAL   A 1 1366 ? -9.99700   22.74000  3.49100   1.000 50.18700  ?  1364 VAL   A CG2 1 
ATOM   10822 N  N   . TYR   A 1 1367 ? -10.62500  23.56300  -0.59200  1.000 46.11983  ?  1365 TYR   A N   1 
ATOM   10823 C  CA  . TYR   A 1 1367 ? -11.32100  22.87000  -1.67100  1.000 57.57688  ?  1365 TYR   A CA  1 
ATOM   10824 C  C   . TYR   A 1 1367 ? -11.52100  23.83600  -2.83000  1.000 52.47526  ?  1365 TYR   A C   1 
ATOM   10825 O  O   . TYR   A 1 1367 ? -11.40900  25.05500  -2.67400  1.000 55.93509  ?  1365 TYR   A O   1 
ATOM   10826 C  CB  . TYR   A 1 1367 ? -12.66400  22.26800  -1.21400  1.000 56.51546  ?  1365 TYR   A CB  1 
ATOM   10827 C  CG  . TYR   A 1 1367 ? -13.78900  23.25100  -0.93000  1.000 52.82501  ?  1365 TYR   A CG  1 
ATOM   10828 C  CD1 . TYR   A 1 1367 ? -14.59100  23.74400  -1.95700  1.000 41.80085  ?  1365 TYR   A CD1 1 
ATOM   10829 C  CD2 . TYR   A 1 1367 ? -14.07600  23.65100  0.36900   1.000 45.60823  ?  1365 TYR   A CD2 1 
ATOM   10830 C  CE1 . TYR   A 1 1367 ? -15.62200  24.63100  -1.69900  1.000 42.80387  ?  1365 TYR   A CE1 1 
ATOM   10831 C  CE2 . TYR   A 1 1367 ? -15.10900  24.53500  0.63700   1.000 49.88536  ?  1365 TYR   A CE2 1 
ATOM   10832 C  CZ  . TYR   A 1 1367 ? -15.87700  25.02300  -0.40100  1.000 62.58678  ?  1365 TYR   A CZ  1 
ATOM   10833 O  OH  . TYR   A 1 1367 ? -16.90400  25.90400  -0.14500  1.000 47.78114  ?  1365 TYR   A OH  1 
ATOM   10834 N  N   . VAL   A 1 1368 ? -11.81100  23.27000  -4.00000  1.000 43.13356  ?  1366 VAL   A N   1 
ATOM   10835 C  CA  . VAL   A 1 1368 ? -12.04700  24.03400  -5.22100  1.000 49.01217  ?  1366 VAL   A CA  1 
ATOM   10836 C  C   . VAL   A 1 1368 ? -13.34900  23.53100  -5.82900  1.000 67.45446  ?  1366 VAL   A C   1 
ATOM   10837 O  O   . VAL   A 1 1368 ? -13.39000  22.43400  -6.39700  1.000 71.63228  ?  1366 VAL   A O   1 
ATOM   10838 C  CB  . VAL   A 1 1368 ? -10.88900  23.90700  -6.22100  1.000 43.25095  ?  1366 VAL   A CB  1 
ATOM   10839 C  CG1 . VAL   A 1 1368 ? -11.23800  24.59600  -7.53600  1.000 49.57717  ?  1366 VAL   A CG1 1 
ATOM   10840 C  CG2 . VAL   A 1 1368 ? -9.61300   24.49200  -5.62900  1.000 39.20224  ?  1366 VAL   A CG2 1 
ATOM   10841 N  N   . MET   A 1 1369 ? -14.41000  24.32300  -5.70200  1.000 65.75020  ?  1367 MET   A N   1 
ATOM   10842 C  CA  . MET   A 1 1369 ? -15.73800  23.94900  -6.17000  1.000 48.35434  ?  1367 MET   A CA  1 
ATOM   10843 C  C   . MET   A 1 1369 ? -15.98900  24.58900  -7.53000  1.000 56.35693  ?  1367 MET   A C   1 
ATOM   10844 O  O   . MET   A 1 1369 ? -15.91700  25.81500  -7.66500  1.000 71.30804  ?  1367 MET   A O   1 
ATOM   10845 C  CB  . MET   A 1 1369 ? -16.80600  24.39000  -5.16800  1.000 52.03839  ?  1367 MET   A CB  1 
ATOM   10846 C  CG  . MET   A 1 1369 ? -18.19700  23.85800  -5.45700  1.000 64.58513  ?  1367 MET   A CG  1 
ATOM   10847 S  SD  . MET   A 1 1369 ? -18.35600  22.12200  -5.00200  1.000 55.32504  ?  1367 MET   A SD  1 
ATOM   10848 C  CE  . MET   A 1 1369 ? -17.73500  22.16200  -3.32100  1.000 35.31530  ?  1367 MET   A CE  1 
ATOM   10849 N  N   . TYR   A 1 1370 ? -16.28600  23.76400  -8.52900  1.000 49.12794  ?  1368 TYR   A N   1 
ATOM   10850 C  CA  . TYR   A 1 1370 ? -16.57100  24.26100  -9.86600  1.000 53.97613  ?  1368 TYR   A CA  1 
ATOM   10851 C  C   . TYR   A 1 1370 ? -18.05000  24.59100  -10.01700 1.000 63.12464  ?  1368 TYR   A C   1 
ATOM   10852 O  O   . TYR   A 1 1370 ? -18.91400  23.97300  -9.38900  1.000 64.15942  ?  1368 TYR   A O   1 
ATOM   10853 C  CB  . TYR   A 1 1370 ? -16.14700  23.24500  -10.92800 1.000 50.00561  ?  1368 TYR   A CB  1 
ATOM   10854 C  CG  . TYR   A 1 1370 ? -14.79200  23.54400  -11.52100 1.000 63.49502  ?  1368 TYR   A CG  1 
ATOM   10855 C  CD1 . TYR   A 1 1370 ? -13.63500  23.37300  -10.77300 1.000 70.98330  ?  1368 TYR   A CD1 1 
ATOM   10856 C  CD2 . TYR   A 1 1370 ? -14.66900  24.00800  -12.82400 1.000 55.18439  ?  1368 TYR   A CD2 1 
ATOM   10857 C  CE1 . TYR   A 1 1370 ? -12.39300  23.65100  -11.30400 1.000 64.94718  ?  1368 TYR   A CE1 1 
ATOM   10858 C  CE2 . TYR   A 1 1370 ? -13.42800  24.28900  -13.36700 1.000 72.84437  ?  1368 TYR   A CE2 1 
ATOM   10859 C  CZ  . TYR   A 1 1370 ? -12.29400  24.10700  -12.60000 1.000 79.67285  ?  1368 TYR   A CZ  1 
ATOM   10860 O  OH  . TYR   A 1 1370 ? -11.05300  24.38100  -13.12200 1.000 81.44901  ?  1368 TYR   A OH  1 
ATOM   10861 N  N   . THR   A 1 1371 ? -18.33200  25.58100  -10.85900 1.000 55.87589  ?  1369 THR   A N   1 
ATOM   10862 C  CA  . THR   A 1 1371 ? -19.69800  26.04200  -11.07700 1.000 61.86630  ?  1369 THR   A CA  1 
ATOM   10863 C  C   . THR   A 1 1371 ? -20.17800  25.70900  -12.48800 1.000 78.66254  ?  1369 THR   A C   1 
ATOM   10864 O  O   . THR   A 1 1371 ? -20.54000  26.59900  -13.25900 1.000 86.90190  ?  1369 THR   A O   1 
ATOM   10865 C  CB  . THR   A 1 1371 ? -19.82000  27.56000  -10.84900 1.000 75.79073  ?  1369 THR   A CB  1 
ATOM   10866 O  OG1 . THR   A 1 1371 ? -19.08700  28.25800  -11.86300 1.000 73.36591  ?  1369 THR   A OG1 1 
ATOM   10867 C  CG2 . THR   A 1 1371 ? -19.26900  27.93800  -9.48100  1.000 66.70782  ?  1369 THR   A CG2 1 
ATOM   10868 N  N   . GLY   A 1 1376 ? -22.63200  28.12400  -19.90700 1.000 66.89436  ?  1374 GLY   A N   1 
ATOM   10869 C  CA  . GLY   A 1 1376 ? -21.54400  28.84300  -19.27000 1.000 84.27162  ?  1374 GLY   A CA  1 
ATOM   10870 C  C   . GLY   A 1 1376 ? -20.47800  27.91900  -18.71500 1.000 99.65060  ?  1374 GLY   A C   1 
ATOM   10871 O  O   . GLY   A 1 1376 ? -20.72200  27.19900  -17.74600 1.000 107.07347 ?  1374 GLY   A O   1 
ATOM   10872 N  N   . LYS   A 1 1377 ? -19.29800  27.94600  -19.33300 1.000 90.13055  ?  1375 LYS   A N   1 
ATOM   10873 C  CA  . LYS   A 1 1377 ? -18.19200  27.07800  -18.96000 1.000 78.36811  ?  1375 LYS   A CA  1 
ATOM   10874 C  C   . LYS   A 1 1377 ? -17.88000  27.22200  -17.47000 1.000 92.79062  ?  1375 LYS   A C   1 
ATOM   10875 O  O   . LYS   A 1 1377 ? -17.61000  28.34000  -17.00700 1.000 98.61076  ?  1375 LYS   A O   1 
ATOM   10876 C  CB  . LYS   A 1 1377 ? -16.95500  27.41200  -19.79000 1.000 78.10750  ?  1375 LYS   A CB  1 
ATOM   10877 N  N   . PRO   A 1 1378 ? -17.91800  26.13400  -16.69700 1.000 96.80622  ?  1376 PRO   A N   1 
ATOM   10878 C  CA  . PRO   A 1 1378 ? -17.70400  26.24500  -15.24900 1.000 88.18226  ?  1376 PRO   A CA  1 
ATOM   10879 C  C   . PRO   A 1 1378 ? -16.36200  26.87200  -14.90500 1.000 74.21233  ?  1376 PRO   A C   1 
ATOM   10880 O  O   . PRO   A 1 1378 ? -15.40400  26.81600  -15.67800 1.000 85.15242  ?  1376 PRO   A O   1 
ATOM   10881 C  CB  . PRO   A 1 1378 ? -17.77600  24.79000  -14.77200 1.000 82.32776  ?  1376 PRO   A CB  1 
ATOM   10882 C  CG  . PRO   A 1 1378 ? -18.65300  24.12500  -15.76700 1.000 101.14583 ?  1376 PRO   A CG  1 
ATOM   10883 C  CD  . PRO   A 1 1378 ? -18.33700  24.77700  -17.08900 1.000 98.33390  ?  1376 PRO   A CD  1 
ATOM   10884 N  N   . LYS   A 1 1379 ? -16.31000  27.47900  -13.72200 1.000 73.87250  ?  1377 LYS   A N   1 
ATOM   10885 C  CA  . LYS   A 1 1379 ? -15.10900  28.11700  -13.20900 1.000 72.81725  ?  1377 LYS   A CA  1 
ATOM   10886 C  C   . LYS   A 1 1379 ? -14.80300  27.56800  -11.82400 1.000 62.97294  ?  1377 LYS   A C   1 
ATOM   10887 O  O   . LYS   A 1 1379 ? -15.70700  27.18200  -11.07800 1.000 61.66986  ?  1377 LYS   A O   1 
ATOM   10888 C  CB  . LYS   A 1 1379 ? -15.26200  29.64300  -13.15100 1.000 60.49987  ?  1377 LYS   A CB  1 
ATOM   10889 N  N   . GLY   A 1 1380 ? -13.51700  27.53900  -11.48400 1.000 47.49662  ?  1378 GLY   A N   1 
ATOM   10890 C  CA  . GLY   A 1 1380 ? -13.08800  26.96300  -10.22500 1.000 50.63826  ?  1378 GLY   A CA  1 
ATOM   10891 C  C   . GLY   A 1 1380 ? -13.04200  27.94700  -9.07500  1.000 48.73973  ?  1378 GLY   A C   1 
ATOM   10892 O  O   . GLY   A 1 1380 ? -12.17300  28.82200  -9.03200  1.000 59.33775  ?  1378 GLY   A O   1 
ATOM   10893 N  N   . VAL   A 1 1381 ? -13.96600  27.80800  -8.12900  1.000 38.53022  ?  1379 VAL   A N   1 
ATOM   10894 C  CA  . VAL   A 1 1381 ? -14.00800  28.68000  -6.95900  1.000 44.07862  ?  1379 VAL   A CA  1 
ATOM   10895 C  C   . VAL   A 1 1381 ? -13.04200  28.12500  -5.91800  1.000 47.00658  ?  1379 VAL   A C   1 
ATOM   10896 O  O   . VAL   A 1 1381 ? -13.25600  27.04100  -5.37300  1.000 56.40036  ?  1379 VAL   A O   1 
ATOM   10897 C  CB  . VAL   A 1 1381 ? -15.42800  28.79700  -6.39400  1.000 47.33479  ?  1379 VAL   A CB  1 
ATOM   10898 C  CG1 . VAL   A 1 1381 ? -15.42600  29.63600  -5.12200  1.000 35.94433  ?  1379 VAL   A CG1 1 
ATOM   10899 C  CG2 . VAL   A 1 1381 ? -16.36300  29.39500  -7.43600  1.000 52.19856  ?  1379 VAL   A CG2 1 
ATOM   10900 N  N   . MET   A 1 1382 ? -11.97700  28.87200  -5.63900  1.000 36.11521  ?  1380 MET   A N   1 
ATOM   10901 C  CA  . MET   A 1 1382 ? -10.95500  28.45200  -4.68900  1.000 43.41546  ?  1380 MET   A CA  1 
ATOM   10902 C  C   . MET   A 1 1382 ? -11.33200  28.93600  -3.29200  1.000 37.01140  ?  1380 MET   A C   1 
ATOM   10903 O  O   . MET   A 1 1382 ? -11.50200  30.13900  -3.07200  1.000 38.19257  ?  1380 MET   A O   1 
ATOM   10904 C  CB  . MET   A 1 1382 ? -9.59100   28.99900  -5.10500  1.000 39.09343  ?  1380 MET   A CB  1 
ATOM   10905 C  CG  . MET   A 1 1382 ? -9.08500   28.45700  -6.43400  1.000 62.06913  ?  1380 MET   A CG  1 
ATOM   10906 S  SD  . MET   A 1 1382 ? -8.04900   29.63800  -7.31900  1.000 67.66309  ?  1380 MET   A SD  1 
ATOM   10907 C  CE  . MET   A 1 1382 ? -7.15300   30.38100  -5.96000  1.000 48.65631  ?  1380 MET   A CE  1 
ATOM   10908 N  N   . ILE   A 1 1383 ? -11.45500  28.00000  -2.35400  1.000 36.97229  ?  1381 ILE   A N   1 
ATOM   10909 C  CA  . ILE   A 1 1383 ? -11.84100  28.29500  -0.97800  1.000 42.86796  ?  1381 ILE   A CA  1 
ATOM   10910 C  C   . ILE   A 1 1383 ? -10.66200  27.99200  -0.06300  1.000 35.65869  ?  1381 ILE   A C   1 
ATOM   10911 O  O   . ILE   A 1 1383 ? -10.06400  26.91300  -0.14800  1.000 43.39967  ?  1381 ILE   A O   1 
ATOM   10912 C  CB  . ILE   A 1 1383 ? -13.08500  27.49400  -0.55700  1.000 37.46600  ?  1381 ILE   A CB  1 
ATOM   10913 C  CG1 . ILE   A 1 1383 ? -14.35000  28.18200  -1.06300  1.000 38.10314  ?  1381 ILE   A CG1 1 
ATOM   10914 C  CG2 . ILE   A 1 1383 ? -13.14400  27.34900  0.95300   1.000 41.63285  ?  1381 ILE   A CG2 1 
ATOM   10915 C  CD1 . ILE   A 1 1383 ? -14.51400  29.58700  -0.53000  1.000 55.09348  ?  1381 ILE   A CD1 1 
ATOM   10916 N  N   . GLU   A 1 1384 ? -10.33500  28.94000  0.81100   1.000 42.40114  ?  1382 GLU   A N   1 
ATOM   10917 C  CA  . GLU   A 1 1384 ? -9.25500   28.77600  1.76900   1.000 49.74470  ?  1382 GLU   A CA  1 
ATOM   10918 C  C   . GLU   A 1 1384 ? -9.77100   28.13700  3.05500   1.000 50.77296  ?  1382 GLU   A C   1 
ATOM   10919 O  O   . GLU   A 1 1384 ? -10.97100  27.93600  3.24800   1.000 50.87700  ?  1382 GLU   A O   1 
ATOM   10920 C  CB  . GLU   A 1 1384 ? -8.59700   30.12200  2.07500   1.000 56.62435  ?  1382 GLU   A CB  1 
ATOM   10921 C  CG  . GLU   A 1 1384 ? -8.00200   30.82200  0.86600   1.000 63.50265  ?  1382 GLU   A CG  1 
ATOM   10922 C  CD  . GLU   A 1 1384 ? -7.41600   32.17500  1.21600   1.000 77.38153  ?  1382 GLU   A CD  1 
ATOM   10923 O  OE1 . GLU   A 1 1384 ? -7.61300   32.63100  2.36300   1.000 70.65052  ?  1382 GLU   A OE1 1 
ATOM   10924 O  OE2 . GLU   A 1 1384 ? -6.75600   32.78200  0.34500   1.000 71.49042  -1 1382 GLU   A OE2 1 
ATOM   10925 N  N   . HIS   A 1 1385 ? -8.83600   27.82500  3.95300   1.000 46.18460  ?  1383 HIS   A N   1 
ATOM   10926 C  CA  . HIS   A 1 1385 ? -9.19300   27.16600  5.20500   1.000 43.44757  ?  1383 HIS   A CA  1 
ATOM   10927 C  C   . HIS   A 1 1385 ? -9.97800   28.10000  6.11500   1.000 51.21641  ?  1383 HIS   A C   1 
ATOM   10928 O  O   . HIS   A 1 1385 ? -11.14800  27.84100  6.42700   1.000 57.81711  ?  1383 HIS   A O   1 
ATOM   10929 C  CB  . HIS   A 1 1385 ? -7.93500   26.65800  5.91400   1.000 59.89837  ?  1383 HIS   A CB  1 
ATOM   10930 C  CG  . HIS   A 1 1385 ? -7.54000   25.26900  5.52700   1.000 71.41159  ?  1383 HIS   A CG  1 
ATOM   10931 N  ND1 . HIS   A 1 1385 ? -6.68500   25.00300  4.47800   1.000 65.75257  ?  1383 HIS   A ND1 1 
ATOM   10932 C  CD2 . HIS   A 1 1385 ? -7.87600   24.06800  6.05400   1.000 45.40626  ?  1383 HIS   A CD2 1 
ATOM   10933 C  CE1 . HIS   A 1 1385 ? -6.51200   23.69700  4.37800   1.000 57.52988  ?  1383 HIS   A CE1 1 
ATOM   10934 N  NE2 . HIS   A 1 1385 ? -7.22400   23.10800  5.32200   1.000 60.22666  ?  1383 HIS   A NE2 1 
ATOM   10935 N  N   . GLY   A 1 1386 ? -9.34900   29.19800  6.55100   1.000 53.21043  ?  1384 GLY   A N   1 
ATOM   10936 C  CA  . GLY   A 1 1386 ? -9.99900   30.10800  7.48000   1.000 53.53371  ?  1384 GLY   A CA  1 
ATOM   10937 C  C   . GLY   A 1 1386 ? -11.34100  30.61500  6.99100   1.000 55.27327  ?  1384 GLY   A C   1 
ATOM   10938 O  O   . GLY   A 1 1386 ? -12.19900  30.99600  7.79300   1.000 46.74923  ?  1384 GLY   A O   1 
ATOM   10939 N  N   . ALA   A 1 1387 ? -11.54300  30.62800  5.67200   1.000 63.58971  ?  1385 ALA   A N   1 
ATOM   10940 C  CA  . ALA   A 1 1387 ? -12.86000  30.93200  5.12500   1.000 46.37152  ?  1385 ALA   A CA  1 
ATOM   10941 C  C   . ALA   A 1 1387 ? -13.87000  29.86000  5.51900   1.000 57.41745  ?  1385 ALA   A C   1 
ATOM   10942 O  O   . ALA   A 1 1387 ? -14.95000  30.16700  6.03700   1.000 55.36172  ?  1385 ALA   A O   1 
ATOM   10943 C  CB  . ALA   A 1 1387 ? -12.77100  31.06800  3.60400   1.000 30.56449  ?  1385 ALA   A CB  1 
ATOM   10944 N  N   . LEU   A 1 1388 ? -13.52700  28.58900  5.28600   1.000 51.01988  ?  1386 LEU   A N   1 
ATOM   10945 C  CA  . LEU   A 1 1388 ? -14.40100  27.49200  5.69300   1.000 42.22382  ?  1386 LEU   A CA  1 
ATOM   10946 C  C   . LEU   A 1 1388 ? -14.55500  27.43900  7.20800   1.000 46.39341  ?  1386 LEU   A C   1 
ATOM   10947 O  O   . LEU   A 1 1388 ? -15.63000  27.10400  7.72000   1.000 60.82536  ?  1386 LEU   A O   1 
ATOM   10948 C  CB  . LEU   A 1 1388 ? -13.85400  26.16500  5.16700   1.000 54.54353  ?  1386 LEU   A CB  1 
ATOM   10949 C  CG  . LEU   A 1 1388 ? -14.52200  24.89200  5.69400   1.000 52.92328  ?  1386 LEU   A CG  1 
ATOM   10950 C  CD1 . LEU   A 1 1388 ? -15.88300  24.67800  5.04500   1.000 49.85230  ?  1386 LEU   A CD1 1 
ATOM   10951 C  CD2 . LEU   A 1 1388 ? -13.62300  23.67800  5.49900   1.000 48.73388  ?  1386 LEU   A CD2 1 
ATOM   10952 N  N   . LEU   A 1 1389 ? -13.49000  27.76200  7.94300   1.000 50.04997  ?  1387 LEU   A N   1 
ATOM   10953 C  CA  . LEU   A 1 1389 ? -13.56200  27.72800  9.40000   1.000 52.26666  ?  1387 LEU   A CA  1 
ATOM   10954 C  C   . LEU   A 1 1389 ? -14.54600  28.75900  9.93600   1.000 52.52057  ?  1387 LEU   A C   1 
ATOM   10955 O  O   . LEU   A 1 1389 ? -15.15800  28.54400  10.98900  1.000 58.34936  ?  1387 LEU   A O   1 
ATOM   10956 C  CB  . LEU   A 1 1389 ? -12.17300  27.95500  10.00000  1.000 62.05792  ?  1387 LEU   A CB  1 
ATOM   10957 C  CG  . LEU   A 1 1389 ? -11.25900  26.74600  10.22800  1.000 63.54832  ?  1387 LEU   A CG  1 
ATOM   10958 C  CD1 . LEU   A 1 1389 ? -11.82400  25.86000  11.32600  1.000 64.17775  ?  1387 LEU   A CD1 1 
ATOM   10959 C  CD2 . LEU   A 1 1389 ? -11.03200  25.94100  8.95300   1.000 59.97355  ?  1387 LEU   A CD2 1 
ATOM   10960 N  N   . ASN   A 1 1390 ? -14.72000  29.87600  9.22700   1.000 49.06777  ?  1388 ASN   A N   1 
ATOM   10961 C  CA  . ASN   A 1 1390 ? -15.60300  30.93200  9.71100   1.000 48.15728  ?  1388 ASN   A CA  1 
ATOM   10962 C  C   . ASN   A 1 1390 ? -17.07000  30.57800  9.50200   1.000 47.63645  ?  1388 ASN   A C   1 
ATOM   10963 O  O   . ASN   A 1 1390 ? -17.89800  30.81300  10.39000  1.000 47.43665  ?  1388 ASN   A O   1 
ATOM   10964 C  CB  . ASN   A 1 1390 ? -15.26200  32.25500  9.02100   1.000 46.18899  ?  1388 ASN   A CB  1 
ATOM   10965 C  CG  . ASN   A 1 1390 ? -16.02000  33.43200  9.60600   1.000 44.42270  ?  1388 ASN   A CG  1 
ATOM   10966 O  OD1 . ASN   A 1 1390 ? -15.79400  33.82300  10.75200  1.000 50.71535  ?  1388 ASN   A OD1 1 
ATOM   10967 N  ND2 . ASN   A 1 1390 ? -16.91500  34.01100  8.81500   1.000 50.15578  ?  1388 ASN   A ND2 1 
ATOM   10968 N  N   . VAL   A 1 1391 ? -17.41200  30.01200  8.34100   1.000 45.06228  ?  1389 VAL   A N   1 
ATOM   10969 C  CA  . VAL   A 1 1391 ? -18.79400  29.60700  8.10300   1.000 42.10080  ?  1389 VAL   A CA  1 
ATOM   10970 C  C   . VAL   A 1 1391 ? -19.15400  28.40100  8.96300   1.000 52.06158  ?  1389 VAL   A C   1 
ATOM   10971 O  O   . VAL   A 1 1391 ? -20.30500  28.26200  9.39800   1.000 60.05369  ?  1389 VAL   A O   1 
ATOM   10972 C  CB  . VAL   A 1 1391 ? -19.02300  29.33800  6.60100   1.000 44.74589  ?  1389 VAL   A CB  1 
ATOM   10973 C  CG1 . VAL   A 1 1391 ? -18.03400  28.31400  6.07500   1.000 46.69972  ?  1389 VAL   A CG1 1 
ATOM   10974 C  CG2 . VAL   A 1 1391 ? -20.45400  28.88600  6.34100   1.000 51.44823  ?  1389 VAL   A CG2 1 
ATOM   10975 N  N   . LEU   A 1 1392 ? -18.18600  27.52600  9.24300   1.000 46.57666  ?  1390 LEU   A N   1 
ATOM   10976 C  CA  . LEU   A 1 1392 ? -18.44900  26.38800  10.11900  1.000 47.47766  ?  1390 LEU   A CA  1 
ATOM   10977 C  C   . LEU   A 1 1392 ? -18.67100  26.84100  11.55600  1.000 50.55422  ?  1390 LEU   A C   1 
ATOM   10978 O  O   . LEU   A 1 1392 ? -19.62600  26.41000  12.21200  1.000 56.02169  ?  1390 LEU   A O   1 
ATOM   10979 C  CB  . LEU   A 1 1392 ? -17.29700  25.38600  10.04200  1.000 42.99126  ?  1390 LEU   A CB  1 
ATOM   10980 C  CG  . LEU   A 1 1392 ? -17.24000  24.50800  8.79200   1.000 43.61704  ?  1390 LEU   A CG  1 
ATOM   10981 C  CD1 . LEU   A 1 1392 ? -16.01400  23.61400  8.83300   1.000 46.26674  ?  1390 LEU   A CD1 1 
ATOM   10982 C  CD2 . LEU   A 1 1392 ? -18.50900  23.68000  8.66400   1.000 49.20515  ?  1390 LEU   A CD2 1 
ATOM   10983 N  N   . HIS   A 1 1393 ? -17.79300  27.71000  12.06500  1.000 50.04297  ?  1391 HIS   A N   1 
ATOM   10984 C  CA  . HIS   A 1 1393 ? -17.95900  28.21500  13.42500  1.000 60.93451  ?  1391 HIS   A CA  1 
ATOM   10985 C  C   . HIS   A 1 1393 ? -19.25000  29.01000  13.56400  1.000 58.85189  ?  1391 HIS   A C   1 
ATOM   10986 O  O   . HIS   A 1 1393 ? -19.92900  28.93000  14.59400  1.000 58.68775  ?  1391 HIS   A O   1 
ATOM   10987 C  CB  . HIS   A 1 1393 ? -16.76000  29.07600  13.82000  1.000 60.14053  ?  1391 HIS   A CB  1 
ATOM   10988 C  CG  . HIS   A 1 1393 ? -15.55600  28.28900  14.23500  1.000 63.77890  ?  1391 HIS   A CG  1 
ATOM   10989 N  ND1 . HIS   A 1 1393 ? -15.61800  27.26500  15.15500  1.000 71.40719  ?  1391 HIS   A ND1 1 
ATOM   10990 C  CD2 . HIS   A 1 1393 ? -14.25600  28.38700  13.86800  1.000 59.05835  ?  1391 HIS   A CD2 1 
ATOM   10991 C  CE1 . HIS   A 1 1393 ? -14.40900  26.76000  15.33000  1.000 72.93024  ?  1391 HIS   A CE1 1 
ATOM   10992 N  NE2 . HIS   A 1 1393 ? -13.56500  27.42300  14.56100  1.000 66.20449  ?  1391 HIS   A NE2 1 
ATOM   10993 N  N   . GLY   A 1 1394 ? -19.60300  29.78600  12.53800  1.000 52.36450  ?  1392 GLY   A N   1 
ATOM   10994 C  CA  . GLY   A 1 1394 ? -20.82500  30.57000  12.60500  1.000 52.28136  ?  1392 GLY   A CA  1 
ATOM   10995 C  C   . GLY   A 1 1394 ? -22.06900  29.70300  12.59500  1.000 61.25446  ?  1392 GLY   A C   1 
ATOM   10996 O  O   . GLY   A 1 1394 ? -23.00100  29.92300  13.37600  1.000 53.64673  ?  1392 GLY   A O   1 
ATOM   10997 N  N   . MET   A 1 1395 ? -22.10200  28.70500  11.70800  1.000 56.24072  ?  1393 MET   A N   1 
ATOM   10998 C  CA  . MET   A 1 1395 ? -23.22100  27.76800  11.69900  1.000 48.19792  ?  1393 MET   A CA  1 
ATOM   10999 C  C   . MET   A 1 1395 ? -23.25600  26.94300  12.97700  1.000 55.02032  ?  1393 MET   A C   1 
ATOM   11000 O  O   . MET   A 1 1395 ? -24.33700  26.62400  13.48800  1.000 54.74411  ?  1393 MET   A O   1 
ATOM   11001 C  CB  . MET   A 1 1395 ? -23.13800  26.86000  10.47300  1.000 35.54827  ?  1393 MET   A CB  1 
ATOM   11002 C  CG  . MET   A 1 1395 ? -23.62200  27.50900  9.18700   1.000 45.97387  ?  1393 MET   A CG  1 
ATOM   11003 S  SD  . MET   A 1 1395 ? -25.30000  28.14400  9.35700   1.000 54.45981  ?  1393 MET   A SD  1 
ATOM   11004 C  CE  . MET   A 1 1395 ? -26.12300  27.35400  7.97900   1.000 54.65438  ?  1393 MET   A CE  1 
ATOM   11005 N  N   . GLN   A 1 1396 ? -22.08600  26.58800  13.51200  1.000 56.66211  ?  1394 GLN   A N   1 
ATOM   11006 C  CA  . GLN   A 1 1396 ? -22.04600  25.87300  14.78300  1.000 62.06047  ?  1394 GLN   A CA  1 
ATOM   11007 C  C   . GLN   A 1 1396 ? -22.47700  26.76800  15.93700  1.000 68.85175  ?  1394 GLN   A C   1 
ATOM   11008 O  O   . GLN   A 1 1396 ? -23.08400  26.29000  16.90200  1.000 73.07805  ?  1394 GLN   A O   1 
ATOM   11009 C  CB  . GLN   A 1 1396 ? -20.64200  25.31900  15.02700  1.000 61.29979  ?  1394 GLN   A CB  1 
ATOM   11010 C  CG  . GLN   A 1 1396 ? -20.48300  24.52700  16.31800  1.000 61.89765  ?  1394 GLN   A CG  1 
ATOM   11011 C  CD  . GLN   A 1 1396 ? -21.29100  23.24200  16.33000  1.000 66.39650  ?  1394 GLN   A CD  1 
ATOM   11012 O  OE1 . GLN   A 1 1396 ? -21.66400  22.71500  15.28100  1.000 66.86077  ?  1394 GLN   A OE1 1 
ATOM   11013 N  NE2 . GLN   A 1 1396 ? -21.56500  22.73200  17.52400  1.000 69.24268  ?  1394 GLN   A NE2 1 
ATOM   11014 N  N   . ASP   A 1 1397 ? -22.18000  28.06600  15.85900  1.000 68.99211  ?  1395 ASP   A N   1 
ATOM   11015 C  CA  . ASP   A 1 1397 ? -22.60700  28.96900  16.92000  1.000 70.38717  ?  1395 ASP   A CA  1 
ATOM   11016 C  C   . ASP   A 1 1397 ? -24.10200  29.24200  16.83700  1.000 72.72335  ?  1395 ASP   A C   1 
ATOM   11017 O  O   . ASP   A 1 1397 ? -24.73500  29.56300  17.85000  1.000 80.89338  ?  1395 ASP   A O   1 
ATOM   11018 C  CB  . ASP   A 1 1397 ? -21.81100  30.27100  16.84900  1.000 52.30839  ?  1395 ASP   A CB  1 
ATOM   11019 C  CG  . ASP   A 1 1397 ? -22.01500  31.14800  18.06800  1.000 76.72270  ?  1395 ASP   A CG  1 
ATOM   11020 O  OD1 . ASP   A 1 1397 ? -22.38900  30.61400  19.13600  1.000 85.74712  ?  1395 ASP   A OD1 1 
ATOM   11021 O  OD2 . ASP   A 1 1397 ? -21.80400  32.37300  17.95700  1.000 85.57113  -1 1395 ASP   A OD2 1 
ATOM   11022 N  N   . GLU   A 1 1398 ? -24.68400  29.09900  15.64900  1.000 62.58076  ?  1396 GLU   A N   1 
ATOM   11023 C  CA  . GLU   A 1 1398 ? -26.09800  29.37300  15.43900  1.000 71.17681  ?  1396 GLU   A CA  1 
ATOM   11024 C  C   . GLU   A 1 1398 ? -26.95100  28.11300  15.49900  1.000 74.30057  ?  1396 GLU   A C   1 
ATOM   11025 O  O   . GLU   A 1 1398 ? -27.97100  28.08600  16.19400  1.000 77.29498  ?  1396 GLU   A O   1 
ATOM   11026 C  CB  . GLU   A 1 1398 ? -26.29800  30.07800  14.09500  1.000 75.04899  ?  1396 GLU   A CB  1 
ATOM   11027 C  CG  . GLU   A 1 1398 ? -27.51300  30.97700  14.06500  1.000 78.84179  ?  1396 GLU   A CG  1 
ATOM   11028 C  CD  . GLU   A 1 1398 ? -27.22000  32.37700  14.57600  1.000 78.70121  ?  1396 GLU   A CD  1 
ATOM   11029 O  OE1 . GLU   A 1 1398 ? -26.18500  32.95000  14.17500  1.000 73.59474  ?  1396 GLU   A OE1 1 
ATOM   11030 O  OE2 . GLU   A 1 1398 ? -28.02400  32.90500  15.37300  1.000 67.79565  -1 1396 GLU   A OE2 1 
ATOM   11031 N  N   . TYR   A 1 1399 ? -26.54900  27.06000  14.78300  1.000 77.31842  ?  1397 TYR   A N   1 
ATOM   11032 C  CA  . TYR   A 1 1399 ? -27.23700  25.77100  14.78900  1.000 72.23297  ?  1397 TYR   A CA  1 
ATOM   11033 C  C   . TYR   A 1 1399 ? -26.25500  24.73100  15.31700  1.000 76.87875  ?  1397 TYR   A C   1 
ATOM   11034 O  O   . TYR   A 1 1399 ? -25.63500  23.99300  14.53600  1.000 64.90420  ?  1397 TYR   A O   1 
ATOM   11035 C  CB  . TYR   A 1 1399 ? -27.74400  25.40300  13.39600  1.000 60.52123  ?  1397 TYR   A CB  1 
ATOM   11036 C  CG  . TYR   A 1 1399 ? -28.43400  26.53800  12.67500  1.000 57.89946  ?  1397 TYR   A CG  1 
ATOM   11037 C  CD1 . TYR   A 1 1399 ? -29.57200  27.13000  13.20300  1.000 57.10074  ?  1397 TYR   A CD1 1 
ATOM   11038 C  CD2 . TYR   A 1 1399 ? -27.95400  27.00900  11.46000  1.000 61.46453  ?  1397 TYR   A CD2 1 
ATOM   11039 C  CE1 . TYR   A 1 1399 ? -30.20700  28.16300  12.54800  1.000 55.63019  ?  1397 TYR   A CE1 1 
ATOM   11040 C  CE2 . TYR   A 1 1399 ? -28.58600  28.04100  10.79500  1.000 54.83298  ?  1397 TYR   A CE2 1 
ATOM   11041 C  CZ  . TYR   A 1 1399 ? -29.71300  28.61400  11.34500  1.000 59.11240  ?  1397 TYR   A CZ  1 
ATOM   11042 O  OH  . TYR   A 1 1399 ? -30.35200  29.64200  10.69300  1.000 62.67556  ?  1397 TYR   A OH  1 
ATOM   11043 N  N   . PRO   A 1 1400 ? -26.08800  24.64600  16.63600  1.000 76.87095  ?  1398 PRO   A N   1 
ATOM   11044 C  CA  . PRO   A 1 1400 ? -25.01900  23.80500  17.19000  1.000 68.63094  ?  1398 PRO   A CA  1 
ATOM   11045 C  C   . PRO   A 1 1400 ? -25.29200  22.32200  16.99600  1.000 68.70502  ?  1398 PRO   A C   1 
ATOM   11046 O  O   . PRO   A 1 1400 ? -26.41000  21.84200  17.19600  1.000 61.27857  ?  1398 PRO   A O   1 
ATOM   11047 C  CB  . PRO   A 1 1400 ? -25.00900  24.17600  18.67900  1.000 61.81696  ?  1398 PRO   A CB  1 
ATOM   11048 C  CG  . PRO   A 1 1400 ? -25.76100  25.47200  18.77100  1.000 70.70240  ?  1398 PRO   A CG  1 
ATOM   11049 C  CD  . PRO   A 1 1400 ? -26.78400  25.40900  17.68400  1.000 78.12257  ?  1398 PRO   A CD  1 
ATOM   11050 N  N   . LEU   A 1 1401 ? -24.24600  21.60000  16.60000  1.000 69.78235  ?  1399 LEU   A N   1 
ATOM   11051 C  CA  . LEU   A 1 1401 ? -24.25100  20.14300  16.55000  1.000 65.28031  ?  1399 LEU   A CA  1 
ATOM   11052 C  C   . LEU   A 1 1401 ? -23.29800  19.65800  17.63400  1.000 75.97002  ?  1399 LEU   A C   1 
ATOM   11053 O  O   . LEU   A 1 1401 ? -22.08000  19.83900  17.52500  1.000 68.71572  ?  1399 LEU   A O   1 
ATOM   11054 C  CB  . LEU   A 1 1401 ? -23.84200  19.63200  15.17000  1.000 62.28225  ?  1399 LEU   A CB  1 
ATOM   11055 C  CG  . LEU   A 1 1401 ? -24.26800  18.20900  14.79300  1.000 48.46319  ?  1399 LEU   A CG  1 
ATOM   11056 C  CD1 . LEU   A 1 1401 ? -24.24600  18.04100  13.28800  1.000 42.48397  ?  1399 LEU   A CD1 1 
ATOM   11057 C  CD2 . LEU   A 1 1401 ? -23.38100  17.16100  15.44500  1.000 54.08644  ?  1399 LEU   A CD2 1 
ATOM   11058 N  N   . LEU   A 1 1402 ? -23.85200  19.05200  18.67500  1.000 70.61751  ?  1400 LEU   A N   1 
ATOM   11059 C  CA  . LEU   A 1 1402 ? -23.08300  18.59500  19.81600  1.000 68.06535  ?  1400 LEU   A CA  1 
ATOM   11060 C  C   . LEU   A 1 1402 ? -22.78100  17.10500  19.66500  1.000 81.24180  ?  1400 LEU   A C   1 
ATOM   11061 O  O   . LEU   A 1 1402 ? -22.95100  16.52000  18.59000  1.000 91.01271  ?  1400 LEU   A O   1 
ATOM   11062 C  CB  . LEU   A 1 1402 ? -23.84800  18.92000  21.09900  1.000 79.55213  ?  1400 LEU   A CB  1 
ATOM   11063 C  CG  . LEU   A 1 1402 ? -24.34300  20.36800  21.15600  1.000 74.09789  ?  1400 LEU   A CG  1 
ATOM   11064 C  CD1 . LEU   A 1 1402 ? -25.46200  20.52000  22.17300  1.000 79.85528  ?  1400 LEU   A CD1 1 
ATOM   11065 C  CD2 . LEU   A 1 1402 ? -23.19800  21.32300  21.46800  1.000 33.54911  ?  1400 LEU   A CD2 1 
ATOM   11066 N  N   . GLN   A 1 1403 ? -22.33100  16.47500  20.75100  1.000 81.05776  ?  1401 GLN   A N   1 
ATOM   11067 C  CA  . GLN   A 1 1403 ? -21.89900  15.08300  20.67200  1.000 73.64325  ?  1401 GLN   A CA  1 
ATOM   11068 C  C   . GLN   A 1 1403 ? -23.07000  14.14700  20.39100  1.000 81.13328  ?  1401 GLN   A C   1 
ATOM   11069 O  O   . GLN   A 1 1403 ? -22.97500  13.26000  19.53500  1.000 81.96340  ?  1401 GLN   A O   1 
ATOM   11070 C  CB  . GLN   A 1 1403 ? -21.17500  14.68800  21.95900  1.000 85.19845  ?  1401 GLN   A CB  1 
ATOM   11071 C  CG  . GLN   A 1 1403 ? -21.63700  15.44100  23.19500  1.000 87.39503  ?  1401 GLN   A CG  1 
ATOM   11072 C  CD  . GLN   A 1 1403 ? -20.64400  15.33600  24.33600  1.000 90.22255  ?  1401 GLN   A CD  1 
ATOM   11073 O  OE1 . GLN   A 1 1403 ? -19.46800  15.04200  24.12400  1.000 75.61727  ?  1401 GLN   A OE1 1 
ATOM   11074 N  NE2 . GLN   A 1 1403 ? -21.11300  15.57600  25.55400  1.000 98.81033  ?  1401 GLN   A NE2 1 
ATOM   11075 N  N   . ASP   A 1 1404 ? -24.18700  14.33500  21.09100  1.000 71.84098  ?  1402 ASP   A N   1 
ATOM   11076 C  CA  . ASP   A 1 1404 ? -25.35100  13.46800  20.90600  1.000 70.09525  ?  1402 ASP   A CA  1 
ATOM   11077 C  C   . ASP   A 1 1404 ? -26.13600  13.76700  19.61600  1.000 74.64181  ?  1402 ASP   A C   1 
ATOM   11078 O  O   . ASP   A 1 1404 ? -27.25700  13.25000  19.48500  1.000 82.39551  ?  1402 ASP   A O   1 
ATOM   11079 C  CB  . ASP   A 1 1404 ? -26.28100  13.58300  22.11700  1.000 88.54798  ?  1402 ASP   A CB  1 
ATOM   11080 C  CG  . ASP   A 1 1404 ? -25.57000  13.30400  23.42900  1.000 94.96921  ?  1402 ASP   A CG  1 
ATOM   11081 O  OD1 . ASP   A 1 1404 ? -24.33700  13.10200  23.41200  1.000 94.10102  ?  1402 ASP   A OD1 1 
ATOM   11082 O  OD2 . ASP   A 1 1404 ? -26.24700  13.28700  24.47900  1.000 88.62413  -1 1402 ASP   A OD2 1 
ATOM   11083 N  N   . ASP   A 1 1405 ? -25.60100  14.55200  18.68500  1.000 80.14447  ?  1403 ASP   A N   1 
ATOM   11084 C  CA  . ASP   A 1 1405 ? -26.30600  14.97800  17.48400  1.000 69.75606  ?  1403 ASP   A CA  1 
ATOM   11085 C  C   . ASP   A 1 1405 ? -25.59600  14.44300  16.24500  1.000 64.18157  ?  1403 ASP   A C   1 
ATOM   11086 O  O   . ASP   A 1 1405 ? -24.49200  13.89700  16.32200  1.000 68.23880  ?  1403 ASP   A O   1 
ATOM   11087 C  CB  . ASP   A 1 1405 ? -26.40900  16.50800  17.43700  1.000 67.34011  ?  1403 ASP   A CB  1 
ATOM   11088 C  CG  . ASP   A 1 1405 ? -27.16400  17.07300  18.62500  1.000 72.94253  ?  1403 ASP   A CG  1 
ATOM   11089 O  OD1 . ASP   A 1 1405 ? -27.15800  16.43100  19.69500  1.000 75.74141  ?  1403 ASP   A OD1 1 
ATOM   11090 O  OD2 . ASP   A 1 1405 ? -27.77800  18.15000  18.48300  1.000 74.90613  -1 1403 ASP   A OD2 1 
ATOM   11091 N  N   . ALA   A 1 1406 ? -26.24000  14.60800  15.09000  1.000 61.75542  ?  1404 ALA   A N   1 
ATOM   11092 C  CA  . ALA   A 1 1406 ? -25.74200  14.00900  13.85900  1.000 50.87857  ?  1404 ALA   A CA  1 
ATOM   11093 C  C   . ALA   A 1 1406 ? -26.20200  14.81400  12.65100  1.000 56.70081  ?  1404 ALA   A C   1 
ATOM   11094 O  O   . ALA   A 1 1406 ? -27.11700  15.63900  12.73000  1.000 59.90534  ?  1404 ALA   A O   1 
ATOM   11095 C  CB  . ALA   A 1 1406 ? -26.20100  12.55300  13.72700  1.000 55.41399  ?  1404 ALA   A CB  1 
ATOM   11096 N  N   . PHE   A 1 1407 ? -25.54900  14.54400  11.52100  1.000 53.25078  ?  1405 PHE   A N   1 
ATOM   11097 C  CA  . PHE   A 1 1407 ? -25.83900  15.12800  10.21900  1.000 55.49626  ?  1405 PHE   A CA  1 
ATOM   11098 C  C   . PHE   A 1 1407 ? -26.15000  14.00900  9.23000   1.000 55.07686  ?  1405 PHE   A C   1 
ATOM   11099 O  O   . PHE   A 1 1407 ? -25.97200  12.82300  9.52200   1.000 58.57688  ?  1405 PHE   A O   1 
ATOM   11100 C  CB  . PHE   A 1 1407 ? -24.65300  15.96300  9.71100   1.000 50.33643  ?  1405 PHE   A CB  1 
ATOM   11101 C  CG  . PHE   A 1 1407 ? -25.02300  17.35500  9.27300   1.000 54.11383  ?  1405 PHE   A CG  1 
ATOM   11102 C  CD1 . PHE   A 1 1407 ? -25.93600  17.55800  8.25200   1.000 62.57677  ?  1405 PHE   A CD1 1 
ATOM   11103 C  CD2 . PHE   A 1 1407 ? -24.43700  18.46100  9.86900   1.000 50.92816  ?  1405 PHE   A CD2 1 
ATOM   11104 C  CE1 . PHE   A 1 1407 ? -26.27000  18.83900  7.84600   1.000 67.44840  ?  1405 PHE   A CE1 1 
ATOM   11105 C  CE2 . PHE   A 1 1407 ? -24.76600  19.74300  9.46700   1.000 41.03564  ?  1405 PHE   A CE2 1 
ATOM   11106 C  CZ  . PHE   A 1 1407 ? -25.68300  19.93200  8.45400   1.000 56.01866  ?  1405 PHE   A CZ  1 
ATOM   11107 N  N   . LEU   A 1 1408 ? -26.61600  14.39400  8.04300   1.000 43.45186  ?  1406 LEU   A N   1 
ATOM   11108 C  CA  . LEU   A 1 1408 ? -26.87300  13.45200  6.95800   1.000 54.17011  ?  1406 LEU   A CA  1 
ATOM   11109 C  C   . LEU   A 1 1408 ? -26.18400  13.95200  5.70000   1.000 50.53808  ?  1406 LEU   A C   1 
ATOM   11110 O  O   . LEU   A 1 1408 ? -26.45500  15.06800  5.24200   1.000 63.93920  ?  1406 LEU   A O   1 
ATOM   11111 C  CB  . LEU   A 1 1408 ? -28.37500  13.27200  6.70800   1.000 54.66080  ?  1406 LEU   A CB  1 
ATOM   11112 C  CG  . LEU   A 1 1408 ? -28.76400  12.18200  5.69900   1.000 64.38535  ?  1406 LEU   A CG  1 
ATOM   11113 C  CD1 . LEU   A 1 1408 ? -28.09600  10.85100  6.02100   1.000 58.25601  ?  1406 LEU   A CD1 1 
ATOM   11114 C  CD2 . LEU   A 1 1408 ? -30.27200  12.01000  5.64600   1.000 62.44170  ?  1406 LEU   A CD2 1 
ATOM   11115 N  N   . LEU   A 1 1409 ? -25.29700  13.13000  5.14400   1.000 41.60468  ?  1407 LEU   A N   1 
ATOM   11116 C  CA  . LEU   A 1 1409 ? -24.65600  13.44000  3.87100   1.000 45.65452  ?  1407 LEU   A CA  1 
ATOM   11117 C  C   . LEU   A 1 1409 ? -25.62000  13.03800  2.76200   1.000 50.05549  ?  1407 LEU   A C   1 
ATOM   11118 O  O   . LEU   A 1 1409 ? -25.71900  11.86200  2.40000   1.000 56.86349  ?  1407 LEU   A O   1 
ATOM   11119 C  CB  . LEU   A 1 1409 ? -23.31900  12.72000  3.74700   1.000 50.16747  ?  1407 LEU   A CB  1 
ATOM   11120 C  CG  . LEU   A 1 1409 ? -22.19800  13.43700  2.98200   1.000 40.85334  ?  1407 LEU   A CG  1 
ATOM   11121 C  CD1 . LEU   A 1 1409 ? -20.94300  12.58000  2.95400   1.000 46.18157  ?  1407 LEU   A CD1 1 
ATOM   11122 C  CD2 . LEU   A 1 1409 ? -22.61400  13.82100  1.56400   1.000 44.72099  ?  1407 LEU   A CD2 1 
ATOM   11123 N  N   . LYS   A 1 1410 ? -26.34200  14.01900  2.22700   1.000 47.60492  ?  1408 LYS   A N   1 
ATOM   11124 C  CA  . LYS   A 1 1410 ? -27.29900  13.78900  1.15600   1.000 43.76292  ?  1408 LYS   A CA  1 
ATOM   11125 C  C   . LYS   A 1 1410 ? -27.09100  14.69300  -0.04800  1.000 50.30759  ?  1408 LYS   A C   1 
ATOM   11126 O  O   . LYS   A 1 1410 ? -27.61700  14.38400  -1.12400  1.000 49.88481  ?  1408 LYS   A O   1 
ATOM   11127 C  CB  . LYS   A 1 1410 ? -28.73200  13.97600  1.67100   1.000 53.31994  ?  1408 LYS   A CB  1 
ATOM   11128 C  CG  . LYS   A 1 1410 ? -29.01900  15.37400  2.19300   1.000 71.27130  ?  1408 LYS   A CG  1 
ATOM   11129 C  CD  . LYS   A 1 1410 ? -30.32100  15.40300  2.97200   1.000 72.74264  ?  1408 LYS   A CD  1 
ATOM   11130 C  CE  . LYS   A 1 1410 ? -31.47800  14.86600  2.14400   1.000 50.29600  ?  1408 LYS   A CE  1 
ATOM   11131 N  NZ  . LYS   A 1 1410 ? -31.66800  15.60700  0.86500   1.000 51.80716  ?  1408 LYS   A NZ  1 
ATOM   11132 N  N   . THR   A 1 1411 ? -26.35200  15.79000  0.09200   1.000 49.12208  ?  1409 THR   A N   1 
ATOM   11133 C  CA  . THR   A 1 1411 ? -26.05800  16.69000  -1.01100  1.000 41.93194  ?  1409 THR   A CA  1 
ATOM   11134 C  C   . THR   A 1 1411 ? -24.83800  16.19500  -1.77700  1.000 38.76165  ?  1409 THR   A C   1 
ATOM   11135 O  O   . THR   A 1 1411 ? -23.90400  15.63800  -1.19600  1.000 55.60712  ?  1409 THR   A O   1 
ATOM   11136 C  CB  . THR   A 1 1411 ? -25.81000  18.10800  -0.49200  1.000 44.14418  ?  1409 THR   A CB  1 
ATOM   11137 O  OG1 . THR   A 1 1411 ? -26.63200  18.34400  0.66000   1.000 52.02080  ?  1409 THR   A OG1 1 
ATOM   11138 C  CG2 . THR   A 1 1411 ? -26.16200  19.12900  -1.56000  1.000 49.28417  ?  1409 THR   A CG2 1 
ATOM   11139 N  N   . THR   A 1 1412 ? -24.85800  16.39500  -3.09300  1.000 31.81399  ?  1410 THR   A N   1 
ATOM   11140 C  CA  . THR   A 1 1412 ? -23.75300  15.93900  -3.92700  1.000 51.59551  ?  1410 THR   A CA  1 
ATOM   11141 C  C   . THR   A 1 1412 ? -22.49300  16.73700  -3.62100  1.000 54.61823  ?  1410 THR   A C   1 
ATOM   11142 O  O   . THR   A 1 1412 ? -22.55300  17.93900  -3.35000  1.000 62.18382  ?  1410 THR   A O   1 
ATOM   11143 C  CB  . THR   A 1 1412 ? -24.10100  16.06400  -5.41000  1.000 45.74345  ?  1410 THR   A CB  1 
ATOM   11144 O  OG1 . THR   A 1 1412 ? -25.45900  15.65900  -5.62400  1.000 63.42326  ?  1410 THR   A OG1 1 
ATOM   11145 C  CG2 . THR   A 1 1412 ? -23.20800  15.15600  -6.21900  1.000 61.26772  ?  1410 THR   A CG2 1 
ATOM   11146 N  N   . TYR   A 1 1413 ? -21.34100  16.06500  -3.66100  1.000 54.53938  ?  1411 TYR   A N   1 
ATOM   11147 C  CA  . TYR   A 1 1413 ? -20.12600  16.76800  -3.27000  1.000 50.72178  ?  1411 TYR   A CA  1 
ATOM   11148 C  C   . TYR   A 1 1413 ? -19.65900  17.78500  -4.30600  1.000 55.61362  ?  1411 TYR   A C   1 
ATOM   11149 O  O   . TYR   A 1 1413 ? -18.70500  18.51300  -4.02500  1.000 55.48510  ?  1411 TYR   A O   1 
ATOM   11150 C  CB  . TYR   A 1 1413 ? -19.00300  15.77300  -2.92700  1.000 48.84447  ?  1411 TYR   A CB  1 
ATOM   11151 C  CG  . TYR   A 1 1413 ? -18.34000  15.00500  -4.06200  1.000 40.53018  ?  1411 TYR   A CG  1 
ATOM   11152 C  CD1 . TYR   A 1 1413 ? -19.01700  14.69000  -5.23600  1.000 52.51670  ?  1411 TYR   A CD1 1 
ATOM   11153 C  CD2 . TYR   A 1 1413 ? -17.02400  14.57000  -3.93400  1.000 50.63841  ?  1411 TYR   A CD2 1 
ATOM   11154 C  CE1 . TYR   A 1 1413 ? -18.39000  13.97600  -6.25600  1.000 62.47548  ?  1411 TYR   A CE1 1 
ATOM   11155 C  CE2 . TYR   A 1 1413 ? -16.39500  13.86200  -4.94000  1.000 46.82452  ?  1411 TYR   A CE2 1 
ATOM   11156 C  CZ  . TYR   A 1 1413 ? -17.07700  13.56600  -6.09800  1.000 54.35956  ?  1411 TYR   A CZ  1 
ATOM   11157 O  OH  . TYR   A 1 1413 ? -16.43700  12.85800  -7.08900  1.000 49.54037  ?  1411 TYR   A OH  1 
ATOM   11158 N  N   . ILE   A 1 1414 ? -20.31900  17.88400  -5.46300  1.000 47.39397  ?  1412 ILE   A N   1 
ATOM   11159 C  CA  . ILE   A 1 1414 ? -20.06400  18.95700  -6.42100  1.000 57.27603  ?  1412 ILE   A CA  1 
ATOM   11160 C  C   . ILE   A 1 1414 ? -20.92200  20.17000  -6.08000  1.000 55.24247  ?  1412 ILE   A C   1 
ATOM   11161 O  O   . ILE   A 1 1414 ? -21.08500  21.08000  -6.90100  1.000 52.33245  ?  1412 ILE   A O   1 
ATOM   11162 C  CB  . ILE   A 1 1414 ? -20.32900  18.50100  -7.86900  1.000 64.62161  ?  1412 ILE   A CB  1 
ATOM   11163 C  CG1 . ILE   A 1 1414 ? -21.67400  17.78100  -7.96200  1.000 57.45007  ?  1412 ILE   A CG1 1 
ATOM   11164 C  CG2 . ILE   A 1 1414 ? -19.20900  17.61100  -8.37000  1.000 55.92295  ?  1412 ILE   A CG2 1 
ATOM   11165 C  CD1 . ILE   A 1 1414 ? -22.25600  17.77100  -9.36300  1.000 42.04819  ?  1412 ILE   A CD1 1 
ATOM   11166 N  N   . PHE   A 1 1415 ? -21.48800  20.18400  -4.87600  1.000 50.31670  ?  1413 PHE   A N   1 
ATOM   11167 C  CA  . PHE   A 1 1415 ? -22.26800  21.31200  -4.38700  1.000 42.83367  ?  1413 PHE   A CA  1 
ATOM   11168 C  C   . PHE   A 1 1415 ? -21.72700  21.74000  -3.03100  1.000 48.62430  ?  1413 PHE   A C   1 
ATOM   11169 O  O   . PHE   A 1 1415 ? -21.42000  20.89800  -2.18200  1.000 48.65977  ?  1413 PHE   A O   1 
ATOM   11170 C  CB  . PHE   A 1 1415 ? -23.75800  20.95600  -4.28400  1.000 54.20817  ?  1413 PHE   A CB  1 
ATOM   11171 C  CG  . PHE   A 1 1415 ? -24.42300  20.72800  -5.61500  1.000 72.61629  ?  1413 PHE   A CG  1 
ATOM   11172 C  CD1 . PHE   A 1 1415 ? -24.27800  21.64400  -6.64600  1.000 78.48791  ?  1413 PHE   A CD1 1 
ATOM   11173 C  CD2 . PHE   A 1 1415 ? -25.20200  19.60200  -5.83300  1.000 83.00994  ?  1413 PHE   A CD2 1 
ATOM   11174 C  CE1 . PHE   A 1 1415 ? -24.89300  21.43800  -7.86900  1.000 86.16016  ?  1413 PHE   A CE1 1 
ATOM   11175 C  CE2 . PHE   A 1 1415 ? -25.81800  19.39000  -7.05400  1.000 72.65117  ?  1413 PHE   A CE2 1 
ATOM   11176 C  CZ  . PHE   A 1 1415 ? -25.66400  20.30900  -8.07300  1.000 78.00174  ?  1413 PHE   A CZ  1 
ATOM   11177 N  N   . ASP   A 1 1416 ? -21.61100  23.05600  -2.83000  1.000 60.75112  ?  1414 ASP   A N   1 
ATOM   11178 C  CA  . ASP   A 1 1416 ? -20.95700  23.56400  -1.62700  1.000 48.66289  ?  1414 ASP   A CA  1 
ATOM   11179 C  C   . ASP   A 1 1416 ? -21.73600  23.23100  -0.35900  1.000 44.47475  ?  1414 ASP   A C   1 
ATOM   11180 O  O   . ASP   A 1 1416 ? -21.14000  23.14200  0.72000   1.000 58.54726  ?  1414 ASP   A O   1 
ATOM   11181 C  CB  . ASP   A 1 1416 ? -20.74500  25.07500  -1.74400  1.000 45.78620  ?  1414 ASP   A CB  1 
ATOM   11182 C  CG  . ASP   A 1 1416 ? -21.97100  25.79800  -2.25800  1.000 74.21919  ?  1414 ASP   A CG  1 
ATOM   11183 O  OD1 . ASP   A 1 1416 ? -22.60000  25.29100  -3.21200  1.000 83.22534  ?  1414 ASP   A OD1 1 
ATOM   11184 O  OD2 . ASP   A 1 1416 ? -22.30900  26.86700  -1.70900  1.000 75.46362  -1 1414 ASP   A OD2 1 
ATOM   11185 N  N   . ILE   A 1 1417 ? -23.05500  23.04100  -0.46200  1.000 44.92829  ?  1415 ILE   A N   1 
ATOM   11186 C  CA  . ILE   A 1 1417 ? -23.85100  22.69200  0.71400   1.000 65.58910  ?  1415 ILE   A CA  1 
ATOM   11187 C  C   . ILE   A 1 1417 ? -23.36100  21.38700  1.33100   1.000 61.12992  ?  1415 ILE   A C   1 
ATOM   11188 O  O   . ILE   A 1 1417 ? -23.40300  21.21700  2.55700   1.000 53.20292  ?  1415 ILE   A O   1 
ATOM   11189 C  CB  . ILE   A 1 1417 ? -25.35100  22.62000  0.34900   1.000 61.23521  ?  1415 ILE   A CB  1 
ATOM   11190 C  CG1 . ILE   A 1 1417 ? -25.87900  24.00000  -0.05200  1.000 45.24545  ?  1415 ILE   A CG1 1 
ATOM   11191 C  CG2 . ILE   A 1 1417 ? -26.17700  22.06400  1.50400   1.000 51.64054  ?  1415 ILE   A CG2 1 
ATOM   11192 C  CD1 . ILE   A 1 1417 ? -26.14100  24.14700  -1.53400  1.000 44.53943  ?  1415 ILE   A CD1 1 
ATOM   11193 N  N   . SER   A 1 1418 ? -22.87300  20.45700  0.50400   1.000 57.14087  ?  1416 SER   A N   1 
ATOM   11194 C  CA  . SER   A 1 1418 ? -22.34700  19.19800  1.02400   1.000 41.24849  ?  1416 SER   A CA  1 
ATOM   11195 C  C   . SER   A 1 1418 ? -21.19400  19.42000  1.99600   1.000 39.31378  ?  1416 SER   A C   1 
ATOM   11196 O  O   . SER   A 1 1418 ? -21.04800  18.66200  2.96200   1.000 45.17260  ?  1416 SER   A O   1 
ATOM   11197 C  CB  . SER   A 1 1418 ? -21.89100  18.30400  -0.13100  1.000 43.76935  ?  1416 SER   A CB  1 
ATOM   11198 O  OG  . SER   A 1 1418 ? -20.76100  18.85600  -0.78500  1.000 51.49146  ?  1416 SER   A OG  1 
ATOM   11199 N  N   . VAL   A 1 1419 ? -20.37300  20.44800  1.76200   1.000 45.14993  ?  1417 VAL   A N   1 
ATOM   11200 C  CA  . VAL   A 1 1419 ? -19.22500  20.70800  2.62800   1.000 45.21945  ?  1417 VAL   A CA  1 
ATOM   11201 C  C   . VAL   A 1 1419 ? -19.67600  21.01500  4.04900   1.000 39.32405  ?  1417 VAL   A C   1 
ATOM   11202 O  O   . VAL   A 1 1419 ? -18.98500  20.67100  5.01600   1.000 52.64791  ?  1417 VAL   A O   1 
ATOM   11203 C  CB  . VAL   A 1 1419 ? -18.36700  21.85000  2.04400   1.000 43.48731  ?  1417 VAL   A CB  1 
ATOM   11204 C  CG1 . VAL   A 1 1419 ? -17.03500  21.95500  2.77600   1.000 36.86201  ?  1417 VAL   A CG1 1 
ATOM   11205 C  CG2 . VAL   A 1 1419 ? -18.14300  21.63700  0.55800   1.000 44.04249  ?  1417 VAL   A CG2 1 
ATOM   11206 N  N   . ALA   A 1 1420 ? -20.83500  21.65900  4.20600   1.000 44.74216  ?  1418 ALA   A N   1 
ATOM   11207 C  CA  . ALA   A 1 1420 ? -21.36900  21.91300  5.53800   1.000 39.61475  ?  1418 ALA   A CA  1 
ATOM   11208 C  C   . ALA   A 1 1420 ? -21.79200  20.63000  6.24000   1.000 53.82704  ?  1418 ALA   A C   1 
ATOM   11209 O  O   . ALA   A 1 1420 ? -21.92200  20.62300  7.46800   1.000 61.24477  ?  1418 ALA   A O   1 
ATOM   11210 C  CB  . ALA   A 1 1420 ? -22.55200  22.87800  5.45900   1.000 46.73409  ?  1418 ALA   A CB  1 
ATOM   11211 N  N   . GLU   A 1 1421 ? -22.01500  19.55200  5.49000   1.000 55.33767  ?  1419 GLU   A N   1 
ATOM   11212 C  CA  . GLU   A 1 1421 ? -22.31400  18.25000  6.07000   1.000 56.10270  ?  1419 GLU   A CA  1 
ATOM   11213 C  C   . GLU   A 1 1421 ? -21.06500  17.40100  6.24500   1.000 50.95736  ?  1419 GLU   A C   1 
ATOM   11214 O  O   . GLU   A 1 1421 ? -20.98500  16.60900  7.19300   1.000 57.05351  ?  1419 GLU   A O   1 
ATOM   11215 C  CB  . GLU   A 1 1421 ? -23.32300  17.50500  5.19100   1.000 56.48084  ?  1419 GLU   A CB  1 
ATOM   11216 C  CG  . GLU   A 1 1421 ? -24.52000  18.34800  4.77300   1.000 54.47217  ?  1419 GLU   A CG  1 
ATOM   11217 C  CD  . GLU   A 1 1421 ? -25.27100  17.75300  3.59600   1.000 60.77729  ?  1419 GLU   A CD  1 
ATOM   11218 O  OE1 . GLU   A 1 1421 ? -24.74100  16.81600  2.96300   1.000 54.13717  ?  1419 GLU   A OE1 1 
ATOM   11219 O  OE2 . GLU   A 1 1421 ? -26.39100  18.22400  3.30200   1.000 49.73019  -1 1419 GLU   A OE2 1 
ATOM   11220 N  N   . ILE   A 1 1422 ? -20.09000  17.55700  5.34700   1.000 57.87204  ?  1420 ILE   A N   1 
ATOM   11221 C  CA  . ILE   A 1 1422 ? -18.83500  16.81800  5.45100   1.000 41.89122  ?  1420 ILE   A CA  1 
ATOM   11222 C  C   . ILE   A 1 1422 ? -18.07900  17.22500  6.71000   1.000 48.52776  ?  1420 ILE   A C   1 
ATOM   11223 O  O   . ILE   A 1 1422 ? -17.43500  16.39400  7.36300   1.000 51.91678  ?  1420 ILE   A O   1 
ATOM   11224 C  CB  . ILE   A 1 1422 ? -17.99400  17.04100  4.17900   1.000 20.78334  ?  1420 ILE   A CB  1 
ATOM   11225 C  CG1 . ILE   A 1 1422 ? -18.70900  16.45700  2.95900   1.000 32.55013  ?  1420 ILE   A CG1 1 
ATOM   11226 C  CG2 . ILE   A 1 1422 ? -16.60900  16.43600  4.32500   1.000 40.39117  ?  1420 ILE   A CG2 1 
ATOM   11227 C  CD1 . ILE   A 1 1422 ? -18.09900  16.87300  1.63700   1.000 34.18648  ?  1420 ILE   A CD1 1 
ATOM   11228 N  N   . PHE   A 1 1423 ? -18.15800  18.50200  7.08400   1.000 53.22118  ?  1421 PHE   A N   1 
ATOM   11229 C  CA  . PHE   A 1 1423 ? -17.40600  19.02100  8.21600   1.000 48.95531  ?  1421 PHE   A CA  1 
ATOM   11230 C  C   . PHE   A 1 1423 ? -18.27400  19.57500  9.33700   1.000 55.94577  ?  1421 PHE   A C   1 
ATOM   11231 O  O   . PHE   A 1 1423 ? -17.72900  20.02300  10.35100  1.000 55.83554  ?  1421 PHE   A O   1 
ATOM   11232 C  CB  . PHE   A 1 1423 ? -16.43400  20.11500  7.75000   1.000 39.02363  ?  1421 PHE   A CB  1 
ATOM   11233 C  CG  . PHE   A 1 1423 ? -15.46400  19.65700  6.69700   1.000 44.71237  ?  1421 PHE   A CG  1 
ATOM   11234 C  CD1 . PHE   A 1 1423 ? -14.50000  18.70700  6.99000   1.000 56.90327  ?  1421 PHE   A CD1 1 
ATOM   11235 C  CD2 . PHE   A 1 1423 ? -15.50700  20.18500  5.41700   1.000 36.65636  ?  1421 PHE   A CD2 1 
ATOM   11236 C  CE1 . PHE   A 1 1423 ? -13.60400  18.28400  6.02600   1.000 52.67873  ?  1421 PHE   A CE1 1 
ATOM   11237 C  CE2 . PHE   A 1 1423 ? -14.61300  19.76700  4.44700   1.000 46.46287  ?  1421 PHE   A CE2 1 
ATOM   11238 C  CZ  . PHE   A 1 1423 ? -13.66000  18.81500  4.75300   1.000 51.60224  ?  1421 PHE   A CZ  1 
ATOM   11239 N  N   . GLY   A 1 1424 ? -19.60200  19.55900  9.19500   1.000 57.62038  ?  1422 GLY   A N   1 
ATOM   11240 C  CA  . GLY   A 1 1424 ? -20.45700  20.16800  10.20100  1.000 50.82841  ?  1422 GLY   A CA  1 
ATOM   11241 C  C   . GLY   A 1 1424 ? -20.50500  19.41400  11.51300  1.000 54.02096  ?  1422 GLY   A C   1 
ATOM   11242 O  O   . GLY   A 1 1424 ? -20.94800  19.97100  12.52400  1.000 50.93523  ?  1422 GLY   A O   1 
ATOM   11243 N  N   . TRP   A 1 1425 ? -20.06000  18.16300  11.52000  1.000 65.36329  ?  1423 TRP   A N   1 
ATOM   11244 C  CA  . TRP   A 1 1425 ? -20.07000  17.35400  12.72900  1.000 52.43298  ?  1423 TRP   A CA  1 
ATOM   11245 C  C   . TRP   A 1 1425 ? -18.76000  17.41900  13.49800  1.000 65.30450  ?  1423 TRP   A C   1 
ATOM   11246 O  O   . TRP   A 1 1425 ? -18.74500  17.09300  14.69100  1.000 68.34724  ?  1423 TRP   A O   1 
ATOM   11247 C  CB  . TRP   A 1 1425 ? -20.37500  15.89700  12.37800  1.000 47.93496  ?  1423 TRP   A CB  1 
ATOM   11248 C  CG  . TRP   A 1 1425 ? -19.42800  15.33300  11.36600  1.000 56.03734  ?  1423 TRP   A CG  1 
ATOM   11249 C  CD1 . TRP   A 1 1425 ? -19.50800  15.46100  10.01000  1.000 47.64808  ?  1423 TRP   A CD1 1 
ATOM   11250 C  CD2 . TRP   A 1 1425 ? -18.25300  14.55600  11.62800  1.000 50.24782  ?  1423 TRP   A CD2 1 
ATOM   11251 N  NE1 . TRP   A 1 1425 ? -18.45900  14.81000  9.41000   1.000 44.13989  ?  1423 TRP   A NE1 1 
ATOM   11252 C  CE2 . TRP   A 1 1425 ? -17.67300  14.24500  10.38100  1.000 52.32576  ?  1423 TRP   A CE2 1 
ATOM   11253 C  CE3 . TRP   A 1 1425 ? -17.63600  14.09100  12.79400  1.000 46.09330  ?  1423 TRP   A CE3 1 
ATOM   11254 C  CZ2 . TRP   A 1 1425 ? -16.50600  13.49100  10.26800  1.000 58.34267  ?  1423 TRP   A CZ2 1 
ATOM   11255 C  CZ3 . TRP   A 1 1425 ? -16.47700  13.34200  12.67800  1.000 55.84962  ?  1423 TRP   A CZ3 1 
ATOM   11256 C  CH2 . TRP   A 1 1425 ? -15.92500  13.05000  11.42500  1.000 60.04508  ?  1423 TRP   A CH2 1 
ATOM   11257 N  N   . VAL   A 1 1426 ? -17.66600  17.82900  12.84800  1.000 54.16713  ?  1424 VAL   A N   1 
ATOM   11258 C  CA  . VAL   A 1 1426 ? -16.36300  17.83300  13.51800  1.000 49.86952  ?  1424 VAL   A CA  1 
ATOM   11259 C  C   . VAL   A 1 1426 ? -16.32400  18.81100  14.68700  1.000 55.51303  ?  1424 VAL   A C   1 
ATOM   11260 O  O   . VAL   A 1 1426 ? -15.85300  18.42500  15.77000  1.000 60.97198  ?  1424 VAL   A O   1 
ATOM   11261 C  CB  . VAL   A 1 1426 ? -15.24100  18.08000  12.49300  1.000 56.28253  ?  1424 VAL   A CB  1 
ATOM   11262 C  CG1 . VAL   A 1 1426 ? -13.87900  17.79900  13.11400  1.000 62.35204  ?  1424 VAL   A CG1 1 
ATOM   11263 C  CG2 . VAL   A 1 1426 ? -15.46200  17.23200  11.25000  1.000 59.81176  ?  1424 VAL   A CG2 1 
ATOM   11264 N  N   . PRO   A 1 1427 ? -16.77900  20.06100  14.55700  1.000 58.94070  ?  1425 PRO   A N   1 
ATOM   11265 C  CA  . PRO   A 1 1427 ? -16.91900  20.90400  15.75400  1.000 47.10310  ?  1425 PRO   A CA  1 
ATOM   11266 C  C   . PRO   A 1 1427 ? -18.11500  20.45000  16.57800  1.000 73.34581  ?  1425 PRO   A C   1 
ATOM   11267 O  O   . PRO   A 1 1427 ? -19.25200  20.45600  16.10100  1.000 86.81136  ?  1425 PRO   A O   1 
ATOM   11268 C  CB  . PRO   A 1 1427 ? -17.12300  22.31000  15.17800  1.000 56.77151  ?  1425 PRO   A CB  1 
ATOM   11269 C  CG  . PRO   A 1 1427 ? -17.73100  22.07500  13.84700  1.000 68.86289  ?  1425 PRO   A CG  1 
ATOM   11270 C  CD  . PRO   A 1 1427 ? -17.09700  20.81600  13.33000  1.000 67.75838  ?  1425 PRO   A CD  1 
ATOM   11271 N  N   . GLY   A 1 1428 ? -17.85200  20.05300  17.82000  1.000 65.79558  ?  1426 GLY   A N   1 
ATOM   11272 C  CA  . GLY   A 1 1428 ? -18.87500  19.53600  18.70000  1.000 79.75083  ?  1426 GLY   A CA  1 
ATOM   11273 C  C   . GLY   A 1 1428 ? -18.82500  18.03700  18.89100  1.000 79.67275  ?  1426 GLY   A C   1 
ATOM   11274 O  O   . GLY   A 1 1428 ? -19.52000  17.52000  19.77700  1.000 76.47269  ?  1426 GLY   A O   1 
ATOM   11275 N  N   . ARG   A 1 1429 ? -18.03300  17.33500  18.07800  1.000 62.53113  ?  1427 ARG   A N   1 
ATOM   11276 C  CA  . ARG   A 1 1429 ? -17.80400  15.90500  18.22600  1.000 71.83158  ?  1427 ARG   A CA  1 
ATOM   11277 C  C   . ARG   A 1 1429 ? -19.07100  15.07600  18.02300  1.000 79.18140  ?  1427 ARG   A C   1 
ATOM   11278 O  O   . ARG   A 1 1429 ? -19.42800  14.27900  18.88700  1.000 75.17231  ?  1427 ARG   A O   1 
ATOM   11279 C  CB  . ARG   A 1 1429 ? -17.21000  15.61000  19.60800  1.000 92.69911  ?  1427 ARG   A CB  1 
ATOM   11280 C  CG  . ARG   A 1 1429 ? -15.94100  14.78900  19.57800  1.000 90.21353  ?  1427 ARG   A CG  1 
ATOM   11281 C  CD  . ARG   A 1 1429 ? -15.21300  14.81200  20.91500  1.000 86.79190  ?  1427 ARG   A CD  1 
ATOM   11282 N  NE  . ARG   A 1 1429 ? -16.11800  14.70100  22.05400  1.000 75.47139  ?  1427 ARG   A NE  1 
ATOM   11283 C  CZ  . ARG   A 1 1429 ? -16.39500  15.69600  22.88500  1.000 85.63093  ?  1427 ARG   A CZ  1 
ATOM   11284 N  NH1 . ARG   A 1 1429 ? -15.82700  16.88300  22.75500  1.000 97.45503  ?  1427 ARG   A NH1 1 
ATOM   11285 N  NH2 . ARG   A 1 1429 ? -17.26500  15.49500  23.87100  1.000 82.66811  ?  1427 ARG   A NH2 1 
ATOM   11286 N  N   . GLY   A 1 1430 ? -19.74000  15.24100  16.89000  1.000 73.75621  ?  1428 GLY   A N   1 
ATOM   11287 C  CA  . GLY   A 1 1430 ? -20.89700  14.43700  16.54800  1.000 72.54019  ?  1428 GLY   A CA  1 
ATOM   11288 C  C   . GLY   A 1 1430 ? -20.56400  13.29700  15.61300  1.000 73.97591  ?  1428 GLY   A C   1 
ATOM   11289 O  O   . GLY   A 1 1430 ? -19.45800  12.75200  15.63600  1.000 76.74023  ?  1428 GLY   A O   1 
ATOM   11290 N  N   . LYS   A 1 1431 ? -21.52800  12.92900  14.77100  1.000 61.99473  ?  1429 LYS   A N   1 
ATOM   11291 C  CA  . LYS   A 1 1431 ? -21.31400  11.88900  13.77800  1.000 56.09473  ?  1429 LYS   A CA  1 
ATOM   11292 C  C   . LYS   A 1 1431 ? -21.96300  12.31400  12.46900  1.000 47.70690  ?  1429 LYS   A C   1 
ATOM   11293 O  O   . LYS   A 1 1431 ? -22.85200  13.16800  12.43900  1.000 51.66989  ?  1429 LYS   A O   1 
ATOM   11294 C  CB  . LYS   A 1 1431 ? -21.88200  10.53300  14.23100  1.000 57.60121  ?  1429 LYS   A CB  1 
ATOM   11295 C  CG  . LYS   A 1 1431 ? -23.40000  10.47600  14.23600  1.000 63.13864  ?  1429 LYS   A CG  1 
ATOM   11296 C  CD  . LYS   A 1 1431 ? -23.93700  9.05300   14.31600  1.000 57.67846  ?  1429 LYS   A CD  1 
ATOM   11297 C  CE  . LYS   A 1 1431 ? -23.92000  8.52600   15.73800  1.000 62.53076  ?  1429 LYS   A CE  1 
ATOM   11298 N  NZ  . LYS   A 1 1431 ? -24.77300  9.35100   16.63500  1.000 67.89913  ?  1429 LYS   A NZ  1 
ATOM   11299 N  N   . LEU   A 1 1432 ? -21.49800  11.71500  11.37600  1.000 54.28338  ?  1430 LEU   A N   1 
ATOM   11300 C  CA  . LEU   A 1 1432 ? -22.06200  11.95400  10.05100  1.000 53.85222  ?  1430 LEU   A CA  1 
ATOM   11301 C  C   . LEU   A 1 1432 ? -22.64400  10.64800  9.53300   1.000 54.52097  ?  1430 LEU   A C   1 
ATOM   11302 O  O   . LEU   A 1 1432 ? -21.90200  9.70100   9.24900   1.000 54.41102  ?  1430 LEU   A O   1 
ATOM   11303 C  CB  . LEU   A 1 1432 ? -21.01600  12.50100  9.08100   1.000 36.75858  ?  1430 LEU   A CB  1 
ATOM   11304 C  CG  . LEU   A 1 1432 ? -21.54600  12.62100  7.65000   1.000 43.14787  ?  1430 LEU   A CG  1 
ATOM   11305 C  CD1 . LEU   A 1 1432 ? -22.63900  13.68300  7.55200   1.000 49.26551  ?  1430 LEU   A CD1 1 
ATOM   11306 C  CD2 . LEU   A 1 1432 ? -20.42800  12.89600  6.65700   1.000 45.69176  ?  1430 LEU   A CD2 1 
ATOM   11307 N  N   . VAL   A 1 1433 ? -23.96600  10.59400  9.41800   1.000 47.40315  ?  1431 VAL   A N   1 
ATOM   11308 C  CA  . VAL   A 1 1433 ? -24.62800  9.46200   8.78300   1.000 43.41389  ?  1431 VAL   A CA  1 
ATOM   11309 C  C   . VAL   A 1 1433 ? -24.56100  9.67200   7.27700   1.000 50.34464  ?  1431 VAL   A C   1 
ATOM   11310 O  O   . VAL   A 1 1433 ? -25.05400  10.67900  6.75800   1.000 61.70929  ?  1431 VAL   A O   1 
ATOM   11311 C  CB  . VAL   A 1 1433 ? -26.07800  9.32400   9.26500   1.000 41.42600  ?  1431 VAL   A CB  1 
ATOM   11312 C  CG1 . VAL   A 1 1433 ? -26.65300  7.98000   8.84400   1.000 54.35325  ?  1431 VAL   A CG1 1 
ATOM   11313 C  CG2 . VAL   A 1 1433 ? -26.14700  9.49300   10.77100  1.000 35.93220  ?  1431 VAL   A CG2 1 
ATOM   11314 N  N   . ILE   A 1 1434 ? -23.92800  8.73800   6.57500   1.000 58.25061  ?  1432 ILE   A N   1 
ATOM   11315 C  CA  . ILE   A 1 1434 ? -23.74200  8.84200   5.13300   1.000 47.52491  ?  1432 ILE   A CA  1 
ATOM   11316 C  C   . ILE   A 1 1434 ? -24.91100  8.13400   4.45900   1.000 55.90937  ?  1432 ILE   A C   1 
ATOM   11317 O  O   . ILE   A 1 1434 ? -25.02200  6.90700   4.51500   1.000 62.78041  ?  1432 ILE   A O   1 
ATOM   11318 C  CB  . ILE   A 1 1434 ? -22.39900  8.24900   4.69700   1.000 48.74472  ?  1432 ILE   A CB  1 
ATOM   11319 C  CG1 . ILE   A 1 1434 ? -21.25300  8.96800   5.41200   1.000 46.73963  ?  1432 ILE   A CG1 1 
ATOM   11320 C  CG2 . ILE   A 1 1434 ? -22.23700  8.35200   3.18600   1.000 59.25790  ?  1432 ILE   A CG2 1 
ATOM   11321 C  CD1 . ILE   A 1 1434 ? -20.00600  8.12500   5.57700   1.000 54.30753  ?  1432 ILE   A CD1 1 
ATOM   11322 N  N   . LEU   A 1 1435 ? -25.78800  8.91000   3.83000   1.000 62.82621  ?  1433 LEU   A N   1 
ATOM   11323 C  CA  . LEU   A 1 1435 ? -26.91900  8.33400   3.11900   1.000 61.12016  ?  1433 LEU   A CA  1 
ATOM   11324 C  C   . LEU   A 1 1435 ? -26.43000  7.51500   1.93200   1.000 64.12334  ?  1433 LEU   A C   1 
ATOM   11325 O  O   . LEU   A 1 1435 ? -25.44200  7.86500   1.27900   1.000 64.35740  ?  1433 LEU   A O   1 
ATOM   11326 C  CB  . LEU   A 1 1435 ? -27.86900  9.43600   2.64800   1.000 53.63790  ?  1433 LEU   A CB  1 
ATOM   11327 C  CG  . LEU   A 1 1435 ? -29.24800  9.00700   2.14200   1.000 62.09504  ?  1433 LEU   A CG  1 
ATOM   11328 C  CD1 . LEU   A 1 1435 ? -30.09500  8.46900   3.28500   1.000 66.51367  ?  1433 LEU   A CD1 1 
ATOM   11329 C  CD2 . LEU   A 1 1435 ? -29.95000  10.16300  1.44300   1.000 53.87391  ?  1433 LEU   A CD2 1 
ATOM   11330 N  N   . GLU   A 1 1436 ? -27.12000  6.41100   1.66600   1.000 60.84683  ?  1434 GLU   A N   1 
ATOM   11331 C  CA  . GLU   A 1 1436 ? -26.76000  5.55200   0.54900   1.000 71.39668  ?  1434 GLU   A CA  1 
ATOM   11332 C  C   . GLU   A 1 1436 ? -26.80400  6.34700   -0.75600  1.000 65.43976  ?  1434 GLU   A C   1 
ATOM   11333 O  O   . GLU   A 1 1436 ? -27.64500  7.24000   -0.90800  1.000 71.43965  ?  1434 GLU   A O   1 
ATOM   11334 C  CB  . GLU   A 1 1436 ? -27.71100  4.35300   0.48700   1.000 72.21932  ?  1434 GLU   A CB  1 
ATOM   11335 C  CG  . GLU   A 1 1436 ? -27.73000  3.59700   -0.83100  1.000 74.23202  ?  1434 GLU   A CG  1 
ATOM   11336 C  CD  . GLU   A 1 1436 ? -28.56600  2.33600   -0.76100  1.000 86.65323  ?  1434 GLU   A CD  1 
ATOM   11337 O  OE1 . GLU   A 1 1436 ? -28.27600  1.47900   0.10100   1.000 83.42647  ?  1434 GLU   A OE1 1 
ATOM   11338 O  OE2 . GLU   A 1 1436 ? -29.51900  2.20600   -1.55900  1.000 85.10546  -1 1434 GLU   A OE2 1 
ATOM   11339 N  N   . PRO   A 1 1437 ? -25.89400  6.08300   -1.69400  1.000 58.00753  ?  1435 PRO   A N   1 
ATOM   11340 C  CA  . PRO   A 1 1437 ? -25.94300  6.77800   -2.98600  1.000 58.03975  ?  1435 PRO   A CA  1 
ATOM   11341 C  C   . PRO   A 1 1437 ? -27.30100  6.61500   -3.65500  1.000 56.65020  ?  1435 PRO   A C   1 
ATOM   11342 O  O   . PRO   A 1 1437 ? -27.93700  5.56200   -3.56500  1.000 73.71650  ?  1435 PRO   A O   1 
ATOM   11343 C  CB  . PRO   A 1 1437 ? -24.83100  6.10100   -3.79300  1.000 52.36256  ?  1435 PRO   A CB  1 
ATOM   11344 C  CG  . PRO   A 1 1437 ? -23.87100  5.62100   -2.76400  1.000 65.91632  ?  1435 PRO   A CG  1 
ATOM   11345 C  CD  . PRO   A 1 1437 ? -24.70200  5.22500   -1.57300  1.000 64.78051  ?  1435 PRO   A CD  1 
ATOM   11346 N  N   . GLU   A 1 1438 ? -27.74600  7.68400   -4.31400  1.000 65.38943  ?  1436 GLU   A N   1 
ATOM   11347 C  CA  . GLU   A 1 1438 ? -29.01800  7.79800   -5.02300  1.000 75.48660  ?  1436 GLU   A CA  1 
ATOM   11348 C  C   . GLU   A 1 1438 ? -30.22900  7.78200   -4.09700  1.000 60.97439  ?  1436 GLU   A C   1 
ATOM   11349 O  O   . GLU   A 1 1438 ? -31.35800  7.92400   -4.58100  1.000 61.05790  ?  1436 GLU   A O   1 
ATOM   11350 C  CB  . GLU   A 1 1438 ? -29.19400  6.71000   -6.09400  1.000 57.41224  ?  1436 GLU   A CB  1 
ATOM   11351 C  CG  . GLU   A 1 1438 ? -28.46000  7.01500   -7.38300  1.000 56.47765  ?  1436 GLU   A CG  1 
ATOM   11352 C  CD  . GLU   A 1 1438 ? -28.81900  8.38300   -7.93100  1.000 99.33543  ?  1436 GLU   A CD  1 
ATOM   11353 O  OE1 . GLU   A 1 1438 ? -30.01500  8.62000   -8.20600  1.000 87.91916  ?  1436 GLU   A OE1 1 
ATOM   11354 O  OE2 . GLU   A 1 1438 ? -27.91000  9.22800   -8.07000  1.000 110.01397 -1 1436 GLU   A OE2 1 
ATOM   11355 N  N   . ALA   A 1 1439 ? -30.04100  7.63100   -2.78800  1.000 51.25981  ?  1437 ALA   A N   1 
ATOM   11356 C  CA  . ALA   A 1 1439 ? -31.16600  7.62900   -1.86200  1.000 49.98440  ?  1437 ALA   A CA  1 
ATOM   11357 C  C   . ALA   A 1 1439 ? -31.67200  9.02700   -1.53800  1.000 64.58956  ?  1437 ALA   A C   1 
ATOM   11358 O  O   . ALA   A 1 1439 ? -32.66300  9.15400   -0.80900  1.000 65.97483  ?  1437 ALA   A O   1 
ATOM   11359 C  CB  . ALA   A 1 1439 ? -30.78500  6.90700   -0.56700  1.000 64.46860  ?  1437 ALA   A CB  1 
ATOM   11360 N  N   . GLU   A 1 1440 ? -31.02700  10.07500  -2.05700  1.000 69.76694  ?  1438 GLU   A N   1 
ATOM   11361 C  CA  . GLU   A 1 1440 ? -31.50700  11.43200  -1.82000  1.000 63.02073  ?  1438 GLU   A CA  1 
ATOM   11362 C  C   . GLU   A 1 1440 ? -32.85000  11.69000  -2.49000  1.000 63.19729  ?  1438 GLU   A C   1 
ATOM   11363 O  O   . GLU   A 1 1440 ? -33.54300  12.64200  -2.11600  1.000 71.79390  ?  1438 GLU   A O   1 
ATOM   11364 C  CB  . GLU   A 1 1440 ? -30.47700  12.45500  -2.30900  1.000 54.21026  ?  1438 GLU   A CB  1 
ATOM   11365 C  CG  . GLU   A 1 1440 ? -30.32600  12.53800  -3.82500  1.000 55.69877  ?  1438 GLU   A CG  1 
ATOM   11366 C  CD  . GLU   A 1 1440 ? -29.29000  11.57400  -4.37100  1.000 76.92871  ?  1438 GLU   A CD  1 
ATOM   11367 O  OE1 . GLU   A 1 1440 ? -28.65700  10.85900  -3.56500  1.000 80.39405  ?  1438 GLU   A OE1 1 
ATOM   11368 O  OE2 . GLU   A 1 1440 ? -29.10400  11.53500  -5.60600  1.000 76.83787  -1 1438 GLU   A OE2 1 
ATOM   11369 N  N   . LYS   A 1 1441 ? -33.23200  10.86300  -3.45900  1.000 52.02140  ?  1439 LYS   A N   1 
ATOM   11370 C  CA  . LYS   A 1 1441 ? -34.48700  11.00800  -4.18200  1.000 52.63717  ?  1439 LYS   A CA  1 
ATOM   11371 C  C   . LYS   A 1 1441 ? -35.61800  10.19200  -3.57300  1.000 65.19828  ?  1439 LYS   A C   1 
ATOM   11372 O  O   . LYS   A 1 1441 ? -36.76100  10.30400  -4.03000  1.000 71.79497  ?  1439 LYS   A O   1 
ATOM   11373 C  CB  . LYS   A 1 1441 ? -34.28800  10.60100  -5.64300  1.000 57.16835  ?  1439 LYS   A CB  1 
ATOM   11374 C  CG  . LYS   A 1 1441 ? -33.07400  11.23700  -6.29200  1.000 52.73297  ?  1439 LYS   A CG  1 
ATOM   11375 C  CD  . LYS   A 1 1441 ? -32.65100  10.46100  -7.52300  1.000 63.04184  ?  1439 LYS   A CD  1 
ATOM   11376 C  CE  . LYS   A 1 1441 ? -32.24800  11.39500  -8.64900  1.000 61.27890  ?  1439 LYS   A CE  1 
ATOM   11377 N  NZ  . LYS   A 1 1441 ? -31.72500  10.64100  -9.82000  1.000 68.11547  ?  1439 LYS   A NZ  1 
ATOM   11378 N  N   . ASN   A 1 1442 ? -35.32900  9.37500   -2.56400  1.000 74.53119  ?  1440 ASN   A N   1 
ATOM   11379 C  CA  . ASN   A 1 1442 ? -36.33900  8.55800   -1.90000  1.000 64.77890  ?  1440 ASN   A CA  1 
ATOM   11380 C  C   . ASN   A 1 1442 ? -36.59900  9.11900   -0.50900  1.000 57.27616  ?  1440 ASN   A C   1 
ATOM   11381 O  O   . ASN   A 1 1442 ? -35.79200  8.90000   0.40900   1.000 56.28593  ?  1440 ASN   A O   1 
ATOM   11382 C  CB  . ASN   A 1 1442 ? -35.88000  7.09900   -1.81700  1.000 64.00766  ?  1440 ASN   A CB  1 
ATOM   11383 C  CG  . ASN   A 1 1442 ? -36.88400  6.20900   -1.11200  1.000 67.31702  ?  1440 ASN   A CG  1 
ATOM   11384 O  OD1 . ASN   A 1 1442 ? -38.06100  6.54900   -0.99300  1.000 76.92887  ?  1440 ASN   A OD1 1 
ATOM   11385 N  ND2 . ASN   A 1 1442 ? -36.42100  5.05700   -0.64100  1.000 73.52765  ?  1440 ASN   A ND2 1 
ATOM   11386 N  N   . PRO   A 1 1443 ? -37.69700  9.84900   -0.29700  1.000 56.96838  ?  1441 PRO   A N   1 
ATOM   11387 C  CA  . PRO   A 1 1443 ? -37.97400  10.38200  1.04700   1.000 58.65444  ?  1441 PRO   A CA  1 
ATOM   11388 C  C   . PRO   A 1 1443 ? -38.16700  9.30400   2.09700   1.000 63.14513  ?  1441 PRO   A C   1 
ATOM   11389 O  O   . PRO   A 1 1443 ? -38.00300  9.58600   3.29000   1.000 63.53258  ?  1441 PRO   A O   1 
ATOM   11390 C  CB  . PRO   A 1 1443 ? -39.25400  11.20600  0.84300   1.000 43.02583  ?  1441 PRO   A CB  1 
ATOM   11391 C  CG  . PRO   A 1 1443 ? -39.88300  10.63200  -0.38700  1.000 60.48752  ?  1441 PRO   A CG  1 
ATOM   11392 C  CD  . PRO   A 1 1443 ? -38.74400  10.21100  -1.26700  1.000 52.83932  ?  1441 PRO   A CD  1 
ATOM   11393 N  N   . LYS   A 1 1444 ? -38.50900  8.07800   1.69400   1.000 58.83013  ?  1442 LYS   A N   1 
ATOM   11394 C  CA  . LYS   A 1 1444 ? -38.59000  6.98200   2.65200   1.000 64.83758  ?  1442 LYS   A CA  1 
ATOM   11395 C  C   . LYS   A 1 1444 ? -37.21400  6.65500   3.22200   1.000 69.54056  ?  1442 LYS   A C   1 
ATOM   11396 O  O   . LYS   A 1 1444 ? -37.03900  6.57900   4.44300   1.000 53.86876  ?  1442 LYS   A O   1 
ATOM   11397 C  CB  . LYS   A 1 1444 ? -39.20800  5.75000   1.99000   1.000 57.14114  ?  1442 LYS   A CB  1 
ATOM   11398 N  N   . ALA   A 1 1445 ? -36.22100  6.46900   2.34600   1.000 55.29238  ?  1443 ALA   A N   1 
ATOM   11399 C  CA  . ALA   A 1 1445 ? -34.86900  6.17100   2.80700   1.000 61.77827  ?  1443 ALA   A CA  1 
ATOM   11400 C  C   . ALA   A 1 1445 ? -34.28600  7.33100   3.60300   1.000 60.10288  ?  1443 ALA   A C   1 
ATOM   11401 O  O   . ALA   A 1 1445 ? -33.53700  7.11900   4.56400   1.000 49.77172  ?  1443 ALA   A O   1 
ATOM   11402 C  CB  . ALA   A 1 1445 ? -33.97100  5.83300   1.61700   1.000 62.47832  ?  1443 ALA   A CB  1 
ATOM   11403 N  N   . ILE   A 1 1446 ? -34.60900  8.56500   3.21100   1.000 55.80750  ?  1444 ILE   A N   1 
ATOM   11404 C  CA  . ILE   A 1 1446 ? -34.17500  9.72500   3.98500   1.000 49.01307  ?  1444 ILE   A CA  1 
ATOM   11405 C  C   . ILE   A 1 1446 ? -34.75600  9.66000   5.39000   1.000 57.63549  ?  1444 ILE   A C   1 
ATOM   11406 O  O   . ILE   A 1 1446 ? -34.02600  9.73400   6.38600   1.000 64.88634  ?  1444 ILE   A O   1 
ATOM   11407 C  CB  . ILE   A 1 1446 ? -34.57300  11.03100  3.27400   1.000 50.19138  ?  1444 ILE   A CB  1 
ATOM   11408 C  CG1 . ILE   A 1 1446 ? -33.90900  11.12100  1.89800   1.000 51.99016  ?  1444 ILE   A CG1 1 
ATOM   11409 C  CG2 . ILE   A 1 1446 ? -34.20400  12.23600  4.13000   1.000 37.83082  ?  1444 ILE   A CG2 1 
ATOM   11410 C  CD1 . ILE   A 1 1446 ? -34.30700  12.35300  1.11300   1.000 38.70920  ?  1444 ILE   A CD1 1 
ATOM   11411 N  N   . TRP   A 1 1447 ? -36.07900  9.50000   5.48800   1.000 57.86509  ?  1445 TRP   A N   1 
ATOM   11412 C  CA  . TRP   A 1 1447 ? -36.73500  9.46100   6.79100   1.000 63.07985  ?  1445 TRP   A CA  1 
ATOM   11413 C  C   . TRP   A 1 1447 ? -36.21300  8.30200   7.63500   1.000 63.68134  ?  1445 TRP   A C   1 
ATOM   11414 O  O   . TRP   A 1 1447 ? -35.91100  8.47600   8.82100   1.000 53.01423  ?  1445 TRP   A O   1 
ATOM   11415 C  CB  . TRP   A 1 1447 ? -38.25300  9.37500   6.60900   1.000 61.18238  ?  1445 TRP   A CB  1 
ATOM   11416 C  CG  . TRP   A 1 1447 ? -39.04000  9.48800   7.89000   1.000 59.96735  ?  1445 TRP   A CG  1 
ATOM   11417 C  CD1 . TRP   A 1 1447 ? -39.94500  8.58800   8.37700   1.000 66.25591  ?  1445 TRP   A CD1 1 
ATOM   11418 C  CD2 . TRP   A 1 1447 ? -38.98900  10.55800  8.84600   1.000 51.43338  ?  1445 TRP   A CD2 1 
ATOM   11419 N  NE1 . TRP   A 1 1447 ? -40.46100  9.03100   9.57100   1.000 64.54037  ?  1445 TRP   A NE1 1 
ATOM   11420 C  CE2 . TRP   A 1 1447 ? -39.89200  10.23900  9.88000   1.000 59.58862  ?  1445 TRP   A CE2 1 
ATOM   11421 C  CE3 . TRP   A 1 1447 ? -38.27000  11.75600  8.92500   1.000 54.50244  ?  1445 TRP   A CE3 1 
ATOM   11422 C  CZ2 . TRP   A 1 1447 ? -40.09000  11.06900  10.98300  1.000 60.05886  ?  1445 TRP   A CZ2 1 
ATOM   11423 C  CZ3 . TRP   A 1 1447 ? -38.47000  12.58000  10.02000  1.000 56.43621  ?  1445 TRP   A CZ3 1 
ATOM   11424 C  CH2 . TRP   A 1 1447 ? -39.37200  12.23200  11.03400  1.000 57.31490  ?  1445 TRP   A CH2 1 
ATOM   11425 N  N   . GLN   A 1 1448 ? -36.07700  7.11500   7.03000   1.000 61.02403  ?  1446 GLN   A N   1 
ATOM   11426 C  CA  . GLN   A 1 1448 ? -35.52900  5.96300   7.74500   1.000 57.12976  ?  1446 GLN   A CA  1 
ATOM   11427 C  C   . GLN   A 1 1448 ? -34.20600  6.30200   8.42500   1.000 65.87785  ?  1446 GLN   A C   1 
ATOM   11428 O  O   . GLN   A 1 1448 ? -33.91100  5.79900   9.51600   1.000 57.33372  ?  1446 GLN   A O   1 
ATOM   11429 C  CB  . GLN   A 1 1448 ? -35.33300  4.78800   6.78600   1.000 56.84836  ?  1446 GLN   A CB  1 
ATOM   11430 C  CG  . GLN   A 1 1448 ? -36.61400  4.09600   6.35500   1.000 79.96932  ?  1446 GLN   A CG  1 
ATOM   11431 C  CD  . GLN   A 1 1448 ? -36.36900  3.03300   5.30100   1.000 80.02045  ?  1446 GLN   A CD  1 
ATOM   11432 O  OE1 . GLN   A 1 1448 ? -35.22700  2.77700   4.91300   1.000 76.57495  ?  1446 GLN   A OE1 1 
ATOM   11433 N  NE2 . GLN   A 1 1448 ? -37.44100  2.40900   4.83000   1.000 66.75955  ?  1446 GLN   A NE2 1 
ATOM   11434 N  N   . ALA   A 1 1449 ? -33.40200  7.16600   7.80000   1.000 63.99131  ?  1447 ALA   A N   1 
ATOM   11435 C  CA  . ALA   A 1 1449 ? -32.10800  7.51800   8.37400   1.000 56.37566  ?  1447 ALA   A CA  1 
ATOM   11436 C  C   . ALA   A 1 1449 ? -32.26700  8.40100   9.60700   1.000 67.18342  ?  1447 ALA   A C   1 
ATOM   11437 O  O   . ALA   A 1 1449 ? -31.65300  8.14000   10.64800  1.000 77.58404  ?  1447 ALA   A O   1 
ATOM   11438 C  CB  . ALA   A 1 1449 ? -31.23900  8.20500   7.32100   1.000 52.52557  ?  1447 ALA   A CB  1 
ATOM   11439 N  N   . VAL   A 1 1450 ? -33.08700  9.45200   9.51500   1.000 55.14574  ?  1448 VAL   A N   1 
ATOM   11440 C  CA  . VAL   A 1 1450 ? -33.20600  10.38500  10.63600  1.000 68.73233  ?  1448 VAL   A CA  1 
ATOM   11441 C  C   . VAL   A 1 1450 ? -33.85000  9.70300   11.83700  1.000 66.17931  ?  1448 VAL   A C   1 
ATOM   11442 O  O   . VAL   A 1 1450 ? -33.48700  9.97300   12.98900  1.000 59.03127  ?  1448 VAL   A O   1 
ATOM   11443 C  CB  . VAL   A 1 1450 ? -33.97400  11.65400  10.21000  1.000 65.72922  ?  1448 VAL   A CB  1 
ATOM   11444 C  CG1 . VAL   A 1 1450 ? -34.57200  11.48100  8.83700   1.000 51.21774  ?  1448 VAL   A CG1 1 
ATOM   11445 C  CG2 . VAL   A 1 1450 ? -35.05800  12.01300  11.22300  1.000 59.44579  ?  1448 VAL   A CG2 1 
ATOM   11446 N  N   . VAL   A 1 1451 ? -34.79700  8.79300   11.59100  1.000 55.15018  ?  1449 VAL   A N   1 
ATOM   11447 C  CA  . VAL   A 1 1451 ? -35.44600  8.10100   12.70000  1.000 61.67934  ?  1449 VAL   A CA  1 
ATOM   11448 C  C   . VAL   A 1 1451 ? -34.49500  7.09600   13.33700  1.000 54.15077  ?  1449 VAL   A C   1 
ATOM   11449 O  O   . VAL   A 1 1451 ? -34.42400  6.98400   14.56700  1.000 50.74178  ?  1449 VAL   A O   1 
ATOM   11450 C  CB  . VAL   A 1 1451 ? -36.74600  7.42500   12.23100  1.000 61.57361  ?  1449 VAL   A CB  1 
ATOM   11451 C  CG1 . VAL   A 1 1451 ? -37.54200  6.93900   13.42600  1.000 55.73035  ?  1449 VAL   A CG1 1 
ATOM   11452 C  CG2 . VAL   A 1 1451 ? -37.57400  8.38200   11.41200  1.000 62.65508  ?  1449 VAL   A CG2 1 
ATOM   11453 N  N   . GLY   A 1 1452 ? -33.75100  6.35600   12.51900  1.000 51.19919  ?  1450 GLY   A N   1 
ATOM   11454 C  CA  . GLY   A 1 1452 ? -32.87400  5.31900   13.02700  1.000 57.85223  ?  1450 GLY   A CA  1 
ATOM   11455 C  C   . GLY   A 1 1452 ? -31.60400  5.83100   13.67300  1.000 55.12192  ?  1450 GLY   A C   1 
ATOM   11456 O  O   . GLY   A 1 1452 ? -31.21500  5.36400   14.74800  1.000 57.84496  ?  1450 GLY   A O   1 
ATOM   11457 N  N   . ALA   A 1 1453 ? -30.94500  6.79200   13.02900  1.000 56.92926  ?  1451 ALA   A N   1 
ATOM   11458 C  CA  . ALA   A 1 1453 ? -29.67800  7.31500   13.52100  1.000 54.54628  ?  1451 ALA   A CA  1 
ATOM   11459 C  C   . ALA   A 1 1453 ? -29.83600  8.53800   14.41400  1.000 61.55260  ?  1451 ALA   A C   1 
ATOM   11460 O  O   . ALA   A 1 1453 ? -28.85500  8.96000   15.03500  1.000 76.22869  ?  1451 ALA   A O   1 
ATOM   11461 C  CB  . ALA   A 1 1453 ? -28.76000  7.65900   12.34500  1.000 48.32339  ?  1451 ALA   A CB  1 
ATOM   11462 N  N   . GLY   A 1 1454 ? -31.03300  9.10900   14.49900  1.000 64.13949  ?  1452 GLY   A N   1 
ATOM   11463 C  CA  . GLY   A 1 1454 ? -31.23600  10.30400  15.30000  1.000 65.67800  ?  1452 GLY   A CA  1 
ATOM   11464 C  C   . GLY   A 1 1454 ? -30.65200  11.55400  14.68100  1.000 72.93787  ?  1452 GLY   A C   1 
ATOM   11465 O  O   . GLY   A 1 1454 ? -29.98900  12.33500  15.37600  1.000 65.10313  ?  1452 GLY   A O   1 
ATOM   11466 N  N   . ILE   A 1 1455 ? -30.88500  11.76600  13.38800  1.000 62.06983  ?  1453 ILE   A N   1 
ATOM   11467 C  CA  . ILE   A 1 1455 ? -30.29900  12.90100  12.68400  1.000 60.38849  ?  1453 ILE   A CA  1 
ATOM   11468 C  C   . ILE   A 1 1455 ? -30.99200  14.18000  13.13200  1.000 67.65199  ?  1453 ILE   A C   1 
ATOM   11469 O  O   . ILE   A 1 1455 ? -32.21400  14.31900  13.01000  1.000 57.71759  ?  1453 ILE   A O   1 
ATOM   11470 C  CB  . ILE   A 1 1455 ? -30.39800  12.71000  11.16600  1.000 53.45813  ?  1453 ILE   A CB  1 
ATOM   11471 C  CG1 . ILE   A 1 1455 ? -29.48800  11.56200  10.73500  1.000 63.64577  ?  1453 ILE   A CG1 1 
ATOM   11472 C  CG2 . ILE   A 1 1455 ? -30.04200  13.99600  10.43200  1.000 64.12876  ?  1453 ILE   A CG2 1 
ATOM   11473 C  CD1 . ILE   A 1 1455 ? -29.57600  11.23800  9.27200   1.000 57.25685  ?  1453 ILE   A CD1 1 
ATOM   11474 N  N   . THR   A 1 1456 ? -30.20700  15.11900  13.65700  1.000 63.47620  ?  1454 THR   A N   1 
ATOM   11475 C  CA  . THR   A 1 1456 ? -30.73200  16.38500  14.14600  1.000 65.14438  ?  1454 THR   A CA  1 
ATOM   11476 C  C   . THR   A 1 1456 ? -30.50500  17.53900  13.18300  1.000 66.20626  ?  1454 THR   A C   1 
ATOM   11477 O  O   . THR   A 1 1456 ? -31.19700  18.55800  13.28900  1.000 64.57194  ?  1454 THR   A O   1 
ATOM   11478 C  CB  . THR   A 1 1456 ? -30.09300  16.73500  15.49200  1.000 60.56287  ?  1454 THR   A CB  1 
ATOM   11479 O  OG1 . THR   A 1 1456 ? -28.73500  17.13600  15.27600  1.000 61.17383  ?  1454 THR   A OG1 1 
ATOM   11480 C  CG2 . THR   A 1 1456 ? -30.10800  15.52700  16.40200  1.000 62.00728  ?  1454 THR   A CG2 1 
ATOM   11481 N  N   . HIS   A 1 1457 ? -29.55600  17.40800  12.26000  1.000 62.85261  ?  1455 HIS   A N   1 
ATOM   11482 C  CA  . HIS   A 1 1457 ? -29.25800  18.43500  11.26900  1.000 56.36910  ?  1455 HIS   A CA  1 
ATOM   11483 C  C   . HIS   A 1 1457 ? -29.42400  17.83500  9.88200   1.000 51.95055  ?  1455 HIS   A C   1 
ATOM   11484 O  O   . HIS   A 1 1457 ? -28.75700  16.85000  9.54500   1.000 65.94954  ?  1455 HIS   A O   1 
ATOM   11485 C  CB  . HIS   A 1 1457 ? -27.83800  18.97900  11.44500  1.000 53.48074  ?  1455 HIS   A CB  1 
ATOM   11486 C  CG  . HIS   A 1 1457 ? -27.63600  19.75000  12.71200  1.000 55.46481  ?  1455 HIS   A CG  1 
ATOM   11487 N  ND1 . HIS   A 1 1457 ? -27.86000  19.20700  13.95800  1.000 48.54205  ?  1455 HIS   A ND1 1 
ATOM   11488 C  CD2 . HIS   A 1 1457 ? -27.22600  21.02300  12.92400  1.000 50.40241  ?  1455 HIS   A CD2 1 
ATOM   11489 C  CE1 . HIS   A 1 1457 ? -27.60000  20.11200  14.88400  1.000 56.07672  ?  1455 HIS   A CE1 1 
ATOM   11490 N  NE2 . HIS   A 1 1457 ? -27.21300  21.22300  14.28300  1.000 56.98067  ?  1455 HIS   A NE2 1 
ATOM   11491 N  N   . ILE   A 1 1458 ? -30.30500  18.42500  9.07900   1.000 50.79293  ?  1456 ILE   A N   1 
ATOM   11492 C  CA  . ILE   A 1 1458 ? -30.51300  17.98300  7.70600   1.000 48.54639  ?  1456 ILE   A CA  1 
ATOM   11493 C  C   . ILE   A 1 1458 ? -30.62700  19.21000  6.81000   1.000 49.85460  ?  1456 ILE   A C   1 
ATOM   11494 O  O   . ILE   A 1 1458 ? -31.17900  20.24200  7.21100   1.000 43.32266  ?  1456 ILE   A O   1 
ATOM   11495 C  CB  . ILE   A 1 1458 ? -31.75000  17.06500  7.58000   1.000 45.15876  ?  1456 ILE   A CB  1 
ATOM   11496 C  CG1 . ILE   A 1 1458 ? -31.71400  16.29800  6.25600   1.000 39.63961  ?  1456 ILE   A CG1 1 
ATOM   11497 C  CG2 . ILE   A 1 1458 ? -33.04600  17.85700  7.70900   1.000 52.54985  ?  1456 ILE   A CG2 1 
ATOM   11498 C  CD1 . ILE   A 1 1458 ? -32.48100  14.99200  6.28600   1.000 44.21528  ?  1456 ILE   A CD1 1 
ATOM   11499 N  N   . ASN   A 1 1459 ? -30.07000  19.10500  5.60800   1.000 57.79870  ?  1457 ASN   A N   1 
ATOM   11500 C  CA  . ASN   A 1 1459 ? -30.11400  20.16600  4.61200   1.000 50.12530  ?  1457 ASN   A CA  1 
ATOM   11501 C  C   . ASN   A 1 1459 ? -31.01700  19.72700  3.47100   1.000 40.63385  ?  1457 ASN   A C   1 
ATOM   11502 O  O   . ASN   A 1 1459 ? -30.90300  18.59800  2.98200   1.000 55.94466  ?  1457 ASN   A O   1 
ATOM   11503 C  CB  . ASN   A 1 1459 ? -28.71200  20.49200  4.09000   1.000 44.32932  ?  1457 ASN   A CB  1 
ATOM   11504 C  CG  . ASN   A 1 1459 ? -27.84400  21.17200  5.13300   1.000 51.81684  ?  1457 ASN   A CG  1 
ATOM   11505 O  OD1 . ASN   A 1 1459 ? -28.29000  21.44600  6.24800   1.000 50.00698  ?  1457 ASN   A OD1 1 
ATOM   11506 N  ND2 . ASN   A 1 1459 ? -26.59200  21.44100  4.77700   1.000 48.67152  ?  1457 ASN   A ND2 1 
ATOM   11507 N  N   . PHE   A 1 1460 ? -31.91500  20.61300  3.05300   1.000 45.56014  ?  1458 PHE   A N   1 
ATOM   11508 C  CA  . PHE   A 1 1460 ? -32.85200  20.30100  1.98600   1.000 51.36456  ?  1458 PHE   A CA  1 
ATOM   11509 C  C   . PHE   A 1 1460 ? -32.95300  21.47300  1.02500   1.000 54.16682  ?  1458 PHE   A C   1 
ATOM   11510 O  O   . PHE   A 1 1460 ? -32.99800  22.63300  1.44500   1.000 41.83731  ?  1458 PHE   A O   1 
ATOM   11511 C  CB  . PHE   A 1 1460 ? -34.24400  19.96700  2.53700   1.000 43.31589  ?  1458 PHE   A CB  1 
ATOM   11512 C  CG  . PHE   A 1 1460 ? -34.53100  18.49600  2.61200   1.000 52.76600  ?  1458 PHE   A CG  1 
ATOM   11513 C  CD1 . PHE   A 1 1460 ? -34.67900  17.74800  1.45400   1.000 62.76920  ?  1458 PHE   A CD1 1 
ATOM   11514 C  CD2 . PHE   A 1 1460 ? -34.66300  17.86100  3.83600   1.000 53.40463  ?  1458 PHE   A CD2 1 
ATOM   11515 C  CE1 . PHE   A 1 1460 ? -34.94600  16.39300  1.51400   1.000 55.88887  ?  1458 PHE   A CE1 1 
ATOM   11516 C  CE2 . PHE   A 1 1460 ? -34.93200  16.50500  3.90300   1.000 60.46108  ?  1458 PHE   A CE2 1 
ATOM   11517 C  CZ  . PHE   A 1 1460 ? -35.07300  15.77100  2.74100   1.000 64.88902  ?  1458 PHE   A CZ  1 
ATOM   11518 N  N   . VAL   A 1 1461 ? -32.97400  21.16100  -0.26200  1.000 57.78133  ?  1459 VAL   A N   1 
ATOM   11519 C  CA  . VAL   A 1 1461 ? -33.36000  22.14400  -1.27500  1.000 57.22005  ?  1459 VAL   A CA  1 
ATOM   11520 C  C   . VAL   A 1 1461 ? -34.87800  22.29900  -1.24200  1.000 64.97716  ?  1459 VAL   A C   1 
ATOM   11521 O  O   . VAL   A 1 1461 ? -35.59100  21.28400  -1.18600  1.000 66.11951  ?  1459 VAL   A O   1 
ATOM   11522 C  CB  . VAL   A 1 1461 ? -32.87700  21.70800  -2.65500  1.000 46.87486  ?  1459 VAL   A CB  1 
ATOM   11523 C  CG1 . VAL   A 1 1461 ? -33.69100  22.37900  -3.75100  1.000 47.11634  ?  1459 VAL   A CG1 1 
ATOM   11524 C  CG2 . VAL   A 1 1461 ? -31.39900  22.03100  -2.81800  1.000 40.24401  ?  1459 VAL   A CG2 1 
ATOM   11525 N  N   . PRO   A 1 1462 ? -35.40000  23.52900  -1.24100  1.000 58.62002  ?  1460 PRO   A N   1 
ATOM   11526 C  CA  . PRO   A 1 1462 ? -36.85800  23.72100  -1.13500  1.000 55.12357  ?  1460 PRO   A CA  1 
ATOM   11527 C  C   . PRO   A 1 1462 ? -37.68500  22.87500  -2.09200  1.000 56.04284  ?  1460 PRO   A C   1 
ATOM   11528 O  O   . PRO   A 1 1462 ? -38.79800  22.47100  -1.73200  1.000 67.37643  ?  1460 PRO   A O   1 
ATOM   11529 C  CB  . PRO   A 1 1462 ? -37.01900  25.21900  -1.42200  1.000 46.14904  ?  1460 PRO   A CB  1 
ATOM   11530 C  CG  . PRO   A 1 1462 ? -35.75700  25.81800  -0.90400  1.000 45.35443  ?  1460 PRO   A CG  1 
ATOM   11531 C  CD  . PRO   A 1 1462 ? -34.66800  24.80600  -1.17100  1.000 52.03609  ?  1460 PRO   A CD  1 
ATOM   11532 N  N   . SER   A 1 1463 ? -37.18200  22.58600  -3.29500  1.000 54.28399  ?  1461 SER   A N   1 
ATOM   11533 C  CA  . SER   A 1 1463 ? -37.94300  21.75000  -4.21900  1.000 53.88583  ?  1461 SER   A CA  1 
ATOM   11534 C  C   . SER   A 1 1463 ? -38.06000  20.32100  -3.70300  1.000 66.24283  ?  1461 SER   A C   1 
ATOM   11535 O  O   . SER   A 1 1463 ? -39.10500  19.68100  -3.86400  1.000 69.22721  ?  1461 SER   A O   1 
ATOM   11536 C  CB  . SER   A 1 1463 ? -37.29800  21.76000  -5.60500  1.000 66.35024  ?  1461 SER   A CB  1 
ATOM   11537 O  OG  . SER   A 1 1463 ? -36.18500  20.88300  -5.65700  1.000 65.96746  ?  1461 SER   A OG  1 
ATOM   11538 N  N   . MET   A 1 1464 ? -36.99800  19.80500  -3.08500  1.000 71.55730  ?  1462 MET   A N   1 
ATOM   11539 C  CA  . MET   A 1 1464 ? -36.98100  18.44500  -2.56600  1.000 55.91351  ?  1462 MET   A CA  1 
ATOM   11540 C  C   . MET   A 1 1464 ? -37.57200  18.33200  -1.16700  1.000 51.37697  ?  1462 MET   A C   1 
ATOM   11541 O  O   . MET   A 1 1464 ? -37.84200  17.21400  -0.71500  1.000 56.27823  ?  1462 MET   A O   1 
ATOM   11542 C  CB  . MET   A 1 1464 ? -35.54800  17.90200  -2.56100  1.000 49.46338  ?  1462 MET   A CB  1 
ATOM   11543 C  CG  . MET   A 1 1464 ? -34.93600  17.78000  -3.94500  1.000 43.55536  ?  1462 MET   A CG  1 
ATOM   11544 S  SD  . MET   A 1 1464 ? -35.53900  16.33200  -4.82800  1.000 67.60973  ?  1462 MET   A SD  1 
ATOM   11545 C  CE  . MET   A 1 1464 ? -35.30200  16.84500  -6.52800  1.000 65.21732  ?  1462 MET   A CE  1 
ATOM   11546 N  N   . LEU   A 1 1465 ? -37.77300  19.45300  -0.47200  1.000 50.83403  ?  1463 LEU   A N   1 
ATOM   11547 C  CA  . LEU   A 1 1465 ? -38.43800  19.41500  0.82300   1.000 55.08743  ?  1463 LEU   A CA  1 
ATOM   11548 C  C   . LEU   A 1 1465 ? -39.93800  19.18200  0.68600   1.000 61.53424  ?  1463 LEU   A C   1 
ATOM   11549 O  O   . LEU   A 1 1465 ? -40.57500  18.73500  1.64600   1.000 63.20803  ?  1463 LEU   A O   1 
ATOM   11550 C  CB  . LEU   A 1 1465 ? -38.16600  20.71400  1.58700   1.000 41.42298  ?  1463 LEU   A CB  1 
ATOM   11551 C  CG  . LEU   A 1 1465 ? -38.61200  20.79000  3.04800   1.000 37.51297  ?  1463 LEU   A CG  1 
ATOM   11552 C  CD1 . LEU   A 1 1465 ? -38.08300  19.60100  3.83400   1.000 43.06659  ?  1463 LEU   A CD1 1 
ATOM   11553 C  CD2 . LEU   A 1 1465 ? -38.15300  22.09600  3.67600   1.000 42.01957  ?  1463 LEU   A CD2 1 
ATOM   11554 N  N   . ILE   A 1 1466 ? -40.50800  19.46100  -0.48200  1.000 61.15160  ?  1464 ILE   A N   1 
ATOM   11555 C  CA  . ILE   A 1 1466 ? -41.93300  19.25100  -0.73400  1.000 63.08855  ?  1464 ILE   A CA  1 
ATOM   11556 C  C   . ILE   A 1 1466 ? -42.25100  17.75600  -0.74500  1.000 65.42251  ?  1464 ILE   A C   1 
ATOM   11557 O  O   . ILE   A 1 1466 ? -43.19300  17.33900  -0.05500  1.000 69.33904  ?  1464 ILE   A O   1 
ATOM   11558 C  CB  . ILE   A 1 1466 ? -42.37700  19.93100  -2.04000  1.000 55.06168  ?  1464 ILE   A CB  1 
ATOM   11559 C  CG1 . ILE   A 1 1466 ? -42.02200  21.41900  -2.01000  1.000 52.46717  ?  1464 ILE   A CG1 1 
ATOM   11560 C  CG2 . ILE   A 1 1466 ? -43.86800  19.73200  -2.26100  1.000 59.62754  ?  1464 ILE   A CG2 1 
ATOM   11561 C  CD1 . ILE   A 1 1466 ? -42.09500  22.09100  -3.36200  1.000 49.55622  ?  1464 ILE   A CD1 1 
ATOM   11562 N  N   . PRO   A 1 1467 ? -41.52500  16.91000  -1.49000  1.000 62.63658  ?  1465 PRO   A N   1 
ATOM   11563 C  CA  . PRO   A 1 1467 ? -41.77400  15.46300  -1.37100  1.000 61.35263  ?  1465 PRO   A CA  1 
ATOM   11564 C  C   . PRO   A 1 1467 ? -41.44900  14.91300  0.00400   1.000 63.75462  ?  1465 PRO   A C   1 
ATOM   11565 O  O   . PRO   A 1 1467 ? -41.97600  13.85600  0.37300   1.000 76.67340  ?  1465 PRO   A O   1 
ATOM   11566 C  CB  . PRO   A 1 1467 ? -40.86300  14.85400  -2.44700  1.000 47.69319  ?  1465 PRO   A CB  1 
ATOM   11567 C  CG  . PRO   A 1 1467 ? -40.60000  15.96100  -3.39600  1.000 52.42998  ?  1465 PRO   A CG  1 
ATOM   11568 C  CD  . PRO   A 1 1467 ? -40.53200  17.18400  -2.54400  1.000 55.25457  ?  1465 PRO   A CD  1 
ATOM   11569 N  N   . PHE   A 1 1468 ? -40.59500  15.59200  0.77400   1.000 52.69436  ?  1466 PHE   A N   1 
ATOM   11570 C  CA  . PHE   A 1 1468 ? -40.29300  15.14100  2.12600   1.000 51.05810  ?  1466 PHE   A CA  1 
ATOM   11571 C  C   . PHE   A 1 1468 ? -41.33800  15.61400  3.12800   1.000 64.23809  ?  1466 PHE   A C   1 
ATOM   11572 O  O   . PHE   A 1 1468 ? -41.55800  14.94800  4.14600   1.000 70.02757  ?  1466 PHE   A O   1 
ATOM   11573 C  CB  . PHE   A 1 1468 ? -38.90000  15.61800  2.54100   1.000 53.44684  ?  1466 PHE   A CB  1 
ATOM   11574 C  CG  . PHE   A 1 1468 ? -38.39800  14.99100  3.81000   1.000 45.69183  ?  1466 PHE   A CG  1 
ATOM   11575 C  CD1 . PHE   A 1 1468 ? -38.04700  13.65100  3.84300   1.000 44.77432  ?  1466 PHE   A CD1 1 
ATOM   11576 C  CD2 . PHE   A 1 1468 ? -38.27100  15.74000  4.96800   1.000 43.37336  ?  1466 PHE   A CD2 1 
ATOM   11577 C  CE1 . PHE   A 1 1468 ? -37.58500  13.06800  5.00900   1.000 44.95727  ?  1466 PHE   A CE1 1 
ATOM   11578 C  CE2 . PHE   A 1 1468 ? -37.80700  15.16300  6.13700   1.000 57.56196  ?  1466 PHE   A CE2 1 
ATOM   11579 C  CZ  . PHE   A 1 1468 ? -37.46400  13.82500  6.15700   1.000 51.65712  ?  1466 PHE   A CZ  1 
ATOM   11580 N  N   . VAL   A 1 1469 ? -41.98400  16.75400  2.86600   1.000 73.93226  ?  1467 VAL   A N   1 
ATOM   11581 C  CA  . VAL   A 1 1469 ? -43.12200  17.16800  3.68300   1.000 71.09249  ?  1467 VAL   A CA  1 
ATOM   11582 C  C   . VAL   A 1 1469 ? -44.31300  16.25600  3.41900   1.000 79.61779  ?  1467 VAL   A C   1 
ATOM   11583 O  O   . VAL   A 1 1469 ? -44.98200  15.79200  4.35100   1.000 79.17070  ?  1467 VAL   A O   1 
ATOM   11584 C  CB  . VAL   A 1 1469 ? -43.46300  18.64500  3.42400   1.000 64.42295  ?  1467 VAL   A CB  1 
ATOM   11585 C  CG1 . VAL   A 1 1469 ? -44.92600  18.92200  3.74100   1.000 76.83865  ?  1467 VAL   A CG1 1 
ATOM   11586 C  CG2 . VAL   A 1 1469 ? -42.56500  19.53300  4.25900   1.000 51.90808  ?  1467 VAL   A CG2 1 
ATOM   11587 N  N   . GLU   A 1 1470 ? -44.58900  15.97700  2.14700   1.000 69.43759  ?  1468 GLU   A N   1 
ATOM   11588 C  CA  . GLU   A 1 1470 ? -45.40900  14.82800  1.80700   1.000 64.89895  ?  1468 GLU   A CA  1 
ATOM   11589 C  C   . GLU   A 1 1470 ? -44.71100  13.56000  2.30100   1.000 77.29155  ?  1468 GLU   A C   1 
ATOM   11590 O  O   . GLU   A 1 1470 ? -43.57300  13.59700  2.77500   1.000 86.66506  ?  1468 GLU   A O   1 
ATOM   11591 C  CB  . GLU   A 1 1470 ? -45.65800  14.78000  0.30000   1.000 55.85012  ?  1468 GLU   A CB  1 
ATOM   11592 C  CG  . GLU   A 1 1470 ? -46.28300  16.05400  -0.25600  1.000 81.53643  ?  1468 GLU   A CG  1 
ATOM   11593 C  CD  . GLU   A 1 1470 ? -46.28200  16.10000  -1.77300  1.000 94.61633  ?  1468 GLU   A CD  1 
ATOM   11594 O  OE1 . GLU   A 1 1470 ? -45.60700  15.25400  -2.39700  1.000 90.46346  ?  1468 GLU   A OE1 1 
ATOM   11595 O  OE2 . GLU   A 1 1470 ? -46.95600  16.98500  -2.34200  1.000 72.19544  -1 1468 GLU   A OE2 1 
ATOM   11596 N  N   . TYR   A 1 1471 ? -45.40900  12.42600  2.19800   1.000 75.44439  ?  1469 TYR   A N   1 
ATOM   11597 C  CA  . TYR   A 1 1471 ? -44.94600  11.17100  2.79300   1.000 84.79746  ?  1469 TYR   A CA  1 
ATOM   11598 C  C   . TYR   A 1 1471 ? -44.95500  11.28800  4.31700   1.000 75.58270  ?  1469 TYR   A C   1 
ATOM   11599 O  O   . TYR   A 1 1471 ? -45.64600  10.51900  4.99200   1.000 93.32903  ?  1469 TYR   A O   1 
ATOM   11600 C  CB  . TYR   A 1 1471 ? -43.55400  10.78500  2.26200   1.000 78.58517  ?  1469 TYR   A CB  1 
ATOM   11601 C  CG  . TYR   A 1 1471 ? -42.88300  9.61100   2.95100   1.000 75.57102  ?  1469 TYR   A CG  1 
ATOM   11602 C  CD1 . TYR   A 1 1471 ? -42.30900  9.74700   4.21300   1.000 71.60934  ?  1469 TYR   A CD1 1 
ATOM   11603 C  CD2 . TYR   A 1 1471 ? -42.79400  8.37500   2.32400   1.000 71.37966  ?  1469 TYR   A CD2 1 
ATOM   11604 C  CE1 . TYR   A 1 1471 ? -41.69400  8.68000   4.83900   1.000 87.73736  ?  1469 TYR   A CE1 1 
ATOM   11605 C  CE2 . TYR   A 1 1471 ? -42.17700  7.30300   2.93900   1.000 75.93470  ?  1469 TYR   A CE2 1 
ATOM   11606 C  CZ  . TYR   A 1 1471 ? -41.62900  7.46000   4.19500   1.000 91.71375  ?  1469 TYR   A CZ  1 
ATOM   11607 O  OH  . TYR   A 1 1471 ? -41.01400  6.38800   4.80000   1.000 104.28754 ?  1469 TYR   A OH  1 
ATOM   11608 N  N   . LEU   A 1 1472 ? -44.19500  12.24200  4.86900   1.000 60.41647  ?  1470 LEU   A N   1 
ATOM   11609 C  CA  . LEU   A 1 1472 ? -44.26500  12.52800  6.29900   1.000 68.32766  ?  1470 LEU   A CA  1 
ATOM   11610 C  C   . LEU   A 1 1472 ? -45.66500  12.93600  6.74300   1.000 73.10561  ?  1470 LEU   A C   1 
ATOM   11611 O  O   . LEU   A 1 1472 ? -45.96000  12.89700  7.94300   1.000 69.21882  ?  1470 LEU   A O   1 
ATOM   11612 C  CB  . LEU   A 1 1472 ? -43.26700  13.62700  6.67200   1.000 60.81996  ?  1470 LEU   A CB  1 
ATOM   11613 C  CG  . LEU   A 1 1472 ? -41.97900  13.17600  7.36400   1.000 50.95133  ?  1470 LEU   A CG  1 
ATOM   11614 C  CD1 . LEU   A 1 1472 ? -41.13600  12.30000  6.44600   1.000 61.28959  ?  1470 LEU   A CD1 1 
ATOM   11615 C  CD2 . LEU   A 1 1472 ? -41.18600  14.38000  7.85000   1.000 50.61585  ?  1470 LEU   A CD2 1 
ATOM   11616 N  N   . GLU   A 1 1473 ? -46.52700  13.33500  5.81000   1.000 78.13478  ?  1471 GLU   A N   1 
ATOM   11617 C  CA  . GLU   A 1 1473 ? -47.93700  13.59300  6.09300   1.000 82.98881  ?  1471 GLU   A CA  1 
ATOM   11618 C  C   . GLU   A 1 1473 ? -48.62100  12.26800  6.41500   1.000 84.92321  ?  1471 GLU   A C   1 
ATOM   11619 O  O   . GLU   A 1 1473 ? -48.96100  11.49600  5.51600   1.000 75.42716  ?  1471 GLU   A O   1 
ATOM   11620 C  CB  . GLU   A 1 1473 ? -48.59200  14.27700  4.89800   1.000 82.56345  ?  1471 GLU   A CB  1 
ATOM   11621 C  CG  . GLU   A 1 1473 ? -49.23200  15.62300  5.20100   1.000 91.68866  ?  1471 GLU   A CG  1 
ATOM   11622 C  CD  . GLU   A 1 1473 ? -50.55000  15.48400  5.93000   1.000 106.51330 ?  1471 GLU   A CD  1 
ATOM   11623 O  OE1 . GLU   A 1 1473 ? -51.20000  14.43000  5.77200   1.000 104.67744 ?  1471 GLU   A OE1 1 
ATOM   11624 O  OE2 . GLU   A 1 1473 ? -50.93400  16.42000  6.66200   1.000 93.42289  -1 1471 GLU   A OE2 1 
ATOM   11625 N  N   . GLY   A 1 1474 ? -48.82800  11.99700  7.70200   1.000 86.57053  ?  1472 GLY   A N   1 
ATOM   11626 C  CA  . GLY   A 1 1474 ? -49.43000  10.74900  8.12700   1.000 90.16695  ?  1472 GLY   A CA  1 
ATOM   11627 C  C   . GLY   A 1 1474 ? -48.51000  9.94200   9.01900   1.000 99.83111  ?  1472 GLY   A C   1 
ATOM   11628 O  O   . GLY   A 1 1474 ? -48.95000  9.36100   10.01600  1.000 98.59071  ?  1472 GLY   A O   1 
ATOM   11629 N  N   . ARG   A 1 1475 ? -47.22500  9.90600   8.67200   1.000 96.60956  ?  1473 ARG   A N   1 
ATOM   11630 C  CA  . ARG   A 1 1475 ? -46.25300  9.18700   9.48100   1.000 89.01777  ?  1473 ARG   A CA  1 
ATOM   11631 C  C   . ARG   A 1 1475 ? -46.14500  9.81500   10.86500  1.000 98.45955  ?  1473 ARG   A C   1 
ATOM   11632 O  O   . ARG   A 1 1475 ? -46.20700  11.03800  11.01800  1.000 97.77896  ?  1473 ARG   A O   1 
ATOM   11633 C  CB  . ARG   A 1 1475 ? -44.88400  9.18700   8.79800   1.000 67.35205  ?  1473 ARG   A CB  1 
ATOM   11634 C  CG  . ARG   A 1 1475 ? -44.88100  8.54000   7.42600   1.000 62.75197  ?  1473 ARG   A CG  1 
ATOM   11635 C  CD  . ARG   A 1 1475 ? -43.92200  7.36600   7.37300   1.000 74.69331  ?  1473 ARG   A CD  1 
ATOM   11636 N  NE  . ARG   A 1 1475 ? -44.27600  6.42600   6.31700   1.000 80.18676  ?  1473 ARG   A NE  1 
ATOM   11637 C  CZ  . ARG   A 1 1475 ? -43.97900  5.13500   6.33800   1.000 87.75907  ?  1473 ARG   A CZ  1 
ATOM   11638 N  NH1 . ARG   A 1 1475 ? -43.34300  4.59000   7.36100   1.000 84.66133  ?  1473 ARG   A NH1 1 
ATOM   11639 N  NH2 . ARG   A 1 1475 ? -44.33500  4.37000   5.30900   1.000 97.43062  ?  1473 ARG   A NH2 1 
ATOM   11640 N  N   . THR   A 1 1476 ? -45.98200  8.96200   11.88000  1.000 94.35091  ?  1474 THR   A N   1 
ATOM   11641 C  CA  . THR   A 1 1476 ? -45.87600  9.41500   13.26100  1.000 97.17208  ?  1474 THR   A CA  1 
ATOM   11642 C  C   . THR   A 1 1476 ? -44.62000  8.88300   13.94600  1.000 85.80194  ?  1474 THR   A C   1 
ATOM   11643 O  O   . THR   A 1 1476 ? -44.53700  8.91200   15.17900  1.000 76.11995  ?  1474 THR   A O   1 
ATOM   11644 C  CB  . THR   A 1 1476 ? -47.11700  9.01400   14.06100  1.000 106.43652 ?  1474 THR   A CB  1 
ATOM   11645 O  OG1 . THR   A 1 1476 ? -46.98200  9.46900   15.41200  1.000 119.25314 ?  1474 THR   A OG1 1 
ATOM   11646 C  CG2 . THR   A 1 1476 ? -47.28900  7.50000   14.05400  1.000 90.81416  ?  1474 THR   A CG2 1 
ATOM   11647 N  N   . GLU   A 1 1477 ? -43.64400  8.39600   13.17800  1.000 75.43665  ?  1475 GLU   A N   1 
ATOM   11648 C  CA  . GLU   A 1 1477 ? -42.40600  7.90700   13.77100  1.000 74.30936  ?  1475 GLU   A CA  1 
ATOM   11649 C  C   . GLU   A 1 1477 ? -41.69700  9.02300   14.53100  1.000 74.80000  ?  1475 GLU   A C   1 
ATOM   11650 O  O   . GLU   A 1 1477 ? -41.62500  10.16500  14.06900  1.000 84.41023  ?  1475 GLU   A O   1 
ATOM   11651 C  CB  . GLU   A 1 1477 ? -41.48300  7.33600   12.69000  1.000 74.71980  ?  1475 GLU   A CB  1 
ATOM   11652 C  CG  . GLU   A 1 1477 ? -41.97200  6.03600   12.04800  1.000 73.32297  ?  1475 GLU   A CG  1 
ATOM   11653 C  CD  . GLU   A 1 1477 ? -42.75700  6.25700   10.76300  1.000 72.29556  ?  1475 GLU   A CD  1 
ATOM   11654 O  OE1 . GLU   A 1 1477 ? -43.88700  6.78600   10.82900  1.000 82.62301  ?  1475 GLU   A OE1 1 
ATOM   11655 O  OE2 . GLU   A 1 1477 ? -42.24000  5.89800   9.68300   1.000 75.66106  -1 1475 GLU   A OE2 1 
ATOM   11656 N  N   . ALA   A 1 1478 ? -41.17900  8.68100   15.71100  1.000 65.99472  ?  1476 ALA   A N   1 
ATOM   11657 C  CA  . ALA   A 1 1478 ? -40.48800  9.65600   16.54400  1.000 75.41269  ?  1476 ALA   A CA  1 
ATOM   11658 C  C   . ALA   A 1 1478 ? -39.27000  10.21100  15.81800  1.000 77.74375  ?  1476 ALA   A C   1 
ATOM   11659 O  O   . ALA   A 1 1478 ? -38.68400  9.56100   14.94800  1.000 69.39289  ?  1476 ALA   A O   1 
ATOM   11660 C  CB  . ALA   A 1 1478 ? -40.06700  9.02300   17.87200  1.000 60.58663  ?  1476 ALA   A CB  1 
ATOM   11661 N  N   . ASN   A 1 1479 ? -38.89100  11.43400  16.17400  1.000 72.58711  ?  1477 ASN   A N   1 
ATOM   11662 C  CA  . ASN   A 1 1479 ? -37.80800  12.11100  15.48200  1.000 69.69965  ?  1477 ASN   A CA  1 
ATOM   11663 C  C   . ASN   A 1 1479 ? -36.93100  12.84100  16.48500  1.000 74.56287  ?  1477 ASN   A C   1 
ATOM   11664 O  O   . ASN   A 1 1479 ? -37.37900  13.23000  17.56700  1.000 69.43363  ?  1477 ASN   A O   1 
ATOM   11665 C  CB  . ASN   A 1 1479 ? -38.33600  13.10000  14.43200  1.000 57.89133  ?  1477 ASN   A CB  1 
ATOM   11666 C  CG  . ASN   A 1 1479 ? -38.95900  14.33800  15.05100  1.000 87.62608  ?  1477 ASN   A CG  1 
ATOM   11667 O  OD1 . ASN   A 1 1479 ? -38.36400  15.41700  15.04100  1.000 85.33598  ?  1477 ASN   A OD1 1 
ATOM   11668 N  ND2 . ASN   A 1 1479 ? -40.16700  14.19200  15.58400  1.000 96.21478  ?  1477 ASN   A ND2 1 
ATOM   11669 N  N   . ARG   A 1 1480 ? -35.66500  13.01100  16.10700  1.000 78.57017  ?  1478 ARG   A N   1 
ATOM   11670 C  CA  . ARG   A 1 1480 ? -34.73300  13.85500  16.83300  1.000 63.79609  ?  1478 ARG   A CA  1 
ATOM   11671 C  C   . ARG   A 1 1480 ? -34.36600  15.10900  16.05200  1.000 65.44882  ?  1478 ARG   A C   1 
ATOM   11672 O  O   . ARG   A 1 1480 ? -33.53300  15.89400  16.52000  1.000 58.66710  ?  1478 ARG   A O   1 
ATOM   11673 C  CB  . ARG   A 1 1480 ? -33.46500  13.06800  17.17900  1.000 53.46133  ?  1478 ARG   A CB  1 
ATOM   11674 C  CG  . ARG   A 1 1480 ? -32.90700  13.44500  18.52600  1.000 66.24473  ?  1478 ARG   A CG  1 
ATOM   11675 C  CD  . ARG   A 1 1480 ? -31.59800  12.76000  18.86900  1.000 72.89300  ?  1478 ARG   A CD  1 
ATOM   11676 N  NE  . ARG   A 1 1480 ? -31.18700  13.18500  20.19900  1.000 91.47964  ?  1478 ARG   A NE  1 
ATOM   11677 C  CZ  . ARG   A 1 1480 ? -30.33900  14.17600  20.44400  1.000 85.02637  ?  1478 ARG   A CZ  1 
ATOM   11678 N  NH1 . ARG   A 1 1480 ? -29.67100  14.77400  19.47200  1.000 85.49800  ?  1478 ARG   A NH1 1 
ATOM   11679 N  NH2 . ARG   A 1 1480 ? -30.16200  14.58200  21.69800  1.000 93.89314  ?  1478 ARG   A NH2 1 
ATOM   11680 N  N   . LEU   A 1 1481 ? -34.97500  15.32200  14.88200  1.000 66.40944  ?  1479 LEU   A N   1 
ATOM   11681 C  CA  . LEU   A 1 1481 ? -34.62500  16.45100  14.02800  1.000 64.41034  ?  1479 LEU   A CA  1 
ATOM   11682 C  C   . LEU   A 1 1481 ? -34.84200  17.77700  14.74300  1.000 65.93099  ?  1479 LEU   A C   1 
ATOM   11683 O  O   . LEU   A 1 1481 ? -35.81500  17.95800  15.48200  1.000 60.41514  ?  1479 LEU   A O   1 
ATOM   11684 C  CB  . LEU   A 1 1481 ? -35.44500  16.41500  12.74100  1.000 37.65990  ?  1479 LEU   A CB  1 
ATOM   11685 C  CG  . LEU   A 1 1481 ? -34.65800  16.13900  11.46100  1.000 62.95819  ?  1479 LEU   A CG  1 
ATOM   11686 C  CD1 . LEU   A 1 1481 ? -35.58700  16.13200  10.25900  1.000 51.56641  ?  1479 LEU   A CD1 1 
ATOM   11687 C  CD2 . LEU   A 1 1481 ? -33.55400  17.17100  11.28900  1.000 72.26596  ?  1479 LEU   A CD2 1 
ATOM   11688 N  N   . ARG   A 1 1482 ? -33.93000  18.71400  14.49400  1.000 59.04864  ?  1480 ARG   A N   1 
ATOM   11689 C  CA  . ARG   A 1 1482 ? -33.91100  19.98100  15.20900  1.000 67.54037  ?  1480 ARG   A CA  1 
ATOM   11690 C  C   . ARG   A 1 1482 ? -33.86000  21.13600  14.21900  1.000 69.65750  ?  1480 ARG   A C   1 
ATOM   11691 O  O   . ARG   A 1 1482 ? -34.48100  22.18100  14.44000  1.000 85.43730  ?  1480 ARG   A O   1 
ATOM   11692 C  CB  . ARG   A 1 1482 ? -32.71900  20.04500  16.17000  1.000 51.87914  ?  1480 ARG   A CB  1 
ATOM   11693 C  CG  . ARG   A 1 1482 ? -32.89300  21.08500  17.27900  1.000 59.65071  ?  1480 ARG   A CG  1 
ATOM   11694 C  CD  . ARG   A 1 1482 ? -31.75000  21.02100  18.27600  1.000 71.27507  ?  1480 ARG   A CD  1 
ATOM   11695 N  NE  . ARG   A 1 1482 ? -31.30100  19.64200  18.39700  1.000 71.73969  ?  1480 ARG   A NE  1 
ATOM   11696 C  CZ  . ARG   A 1 1482 ? -30.39800  19.20100  19.26200  1.000 75.93707  ?  1480 ARG   A CZ  1 
ATOM   11697 N  NH1 . ARG   A 1 1482 ? -29.76000  20.02100  20.08600  1.000 75.45095  ?  1480 ARG   A NH1 1 
ATOM   11698 N  NH2 . ARG   A 1 1482 ? -30.13300  17.89900  19.30700  1.000 76.37223  ?  1480 ARG   A NH2 1 
ATOM   11699 N  N   . TYR   A 1 1483 ? -33.14600  20.94000  13.11200  1.000 55.21827  ?  1481 TYR   A N   1 
ATOM   11700 C  CA  . TYR   A 1 1483 ? -32.94700  21.98500  12.12200  1.000 51.11957  ?  1481 TYR   A CA  1 
ATOM   11701 C  C   . TYR   A 1 1483 ? -33.10200  21.41300  10.72100  1.000 58.12714  ?  1481 TYR   A C   1 
ATOM   11702 O  O   . TYR   A 1 1483 ? -32.43900  20.43200  10.37000  1.000 55.24595  ?  1481 TYR   A O   1 
ATOM   11703 C  CB  . TYR   A 1 1483 ? -31.56200  22.62400  12.27000  1.000 45.56997  ?  1481 TYR   A CB  1 
ATOM   11704 C  CG  . TYR   A 1 1483 ? -31.22300  23.06600  13.67700  1.000 62.23336  ?  1481 TYR   A CG  1 
ATOM   11705 C  CD1 . TYR   A 1 1483 ? -31.79700  24.20500  14.22700  1.000 60.66386  ?  1481 TYR   A CD1 1 
ATOM   11706 C  CD2 . TYR   A 1 1483 ? -30.31600  22.35100  14.45100  1.000 64.49359  ?  1481 TYR   A CD2 1 
ATOM   11707 C  CE1 . TYR   A 1 1483 ? -31.48400  24.61600  15.51300  1.000 64.27235  ?  1481 TYR   A CE1 1 
ATOM   11708 C  CE2 . TYR   A 1 1483 ? -29.99700  22.75400  15.73600  1.000 66.85601  ?  1481 TYR   A CE2 1 
ATOM   11709 C  CZ  . TYR   A 1 1483 ? -30.58300  23.88600  16.26300  1.000 66.91615  ?  1481 TYR   A CZ  1 
ATOM   11710 O  OH  . TYR   A 1 1483 ? -30.26600  24.28800  17.54300  1.000 64.36409  ?  1481 TYR   A OH  1 
ATOM   11711 N  N   . ILE   A 1 1484 ? -33.97600  22.02600  9.93100   1.000 54.95825  ?  1482 ILE   A N   1 
ATOM   11712 C  CA  . ILE   A 1 1484 ? -34.05800  21.78200  8.49600   1.000 54.19277  ?  1482 ILE   A CA  1 
ATOM   11713 C  C   . ILE   A 1 1484 ? -33.55300  23.04700  7.81200   1.000 48.06351  ?  1482 ILE   A C   1 
ATOM   11714 O  O   . ILE   A 1 1484 ? -34.29500  24.02500  7.65600   1.000 53.07162  ?  1482 ILE   A O   1 
ATOM   11715 C  CB  . ILE   A 1 1484 ? -35.47900  21.41400  8.04900   1.000 50.62945  ?  1482 ILE   A CB  1 
ATOM   11716 C  CG1 . ILE   A 1 1484 ? -35.85400  20.03000  8.57400   1.000 55.24115  ?  1482 ILE   A CG1 1 
ATOM   11717 C  CG2 . ILE   A 1 1484 ? -35.58900  21.42300  6.53200   1.000 46.13579  ?  1482 ILE   A CG2 1 
ATOM   11718 C  CD1 . ILE   A 1 1484 ? -37.08200  19.43200  7.92000   1.000 66.55199  ?  1482 ILE   A CD1 1 
ATOM   11719 N  N   . LEU   A 1 1485 ? -32.28300  23.04600  7.42100   1.000 46.40382  ?  1483 LEU   A N   1 
ATOM   11720 C  CA  . LEU   A 1 1485 ? -31.66500  24.21200  6.80300   1.000 48.99772  ?  1483 LEU   A CA  1 
ATOM   11721 C  C   . LEU   A 1 1485 ? -31.91900  24.17900  5.30000   1.000 54.85356  ?  1483 LEU   A C   1 
ATOM   11722 O  O   . LEU   A 1 1485 ? -31.49600  23.24100  4.61400   1.000 52.77274  ?  1483 LEU   A O   1 
ATOM   11723 C  CB  . LEU   A 1 1485 ? -30.16500  24.25500  7.09800   1.000 48.16792  ?  1483 LEU   A CB  1 
ATOM   11724 C  CG  . LEU   A 1 1485 ? -29.72600  24.37300  8.56500   1.000 47.47642  ?  1483 LEU   A CG  1 
ATOM   11725 C  CD1 . LEU   A 1 1485 ? -30.74800  25.13900  9.40000   1.000 54.63596  ?  1483 LEU   A CD1 1 
ATOM   11726 C  CD2 . LEU   A 1 1485 ? -29.43200  23.00700  9.17200   1.000 43.95620  ?  1483 LEU   A CD2 1 
ATOM   11727 N  N   . ALA   A 1 1486 ? -32.60500  25.19900  4.79400   1.000 54.65620  ?  1484 ALA   A N   1 
ATOM   11728 C  CA  . ALA   A 1 1486 ? -32.99900  25.26500  3.39400   1.000 34.37183  ?  1484 ALA   A CA  1 
ATOM   11729 C  C   . ALA   A 1 1486 ? -32.11700  26.24100  2.62800   1.000 39.72746  ?  1484 ALA   A C   1 
ATOM   11730 O  O   . ALA   A 1 1486 ? -31.83700  27.34800  3.10000   1.000 54.53575  ?  1484 ALA   A O   1 
ATOM   11731 C  CB  . ALA   A 1 1486 ? -34.46500  25.68300  3.26000   1.000 42.96898  ?  1484 ALA   A CB  1 
ATOM   11732 N  N   . CYS   A 1 1487 ? -31.69600  25.82600  1.43700   1.000 45.82079  ?  1485 CYS   A N   1 
ATOM   11733 C  CA  . CYS   A 1 1487 ? -30.86500  26.64800  0.56900   1.000 45.60971  ?  1485 CYS   A CA  1 
ATOM   11734 C  C   . CYS   A 1 1487 ? -30.83500  26.01300  -0.81300  1.000 46.71109  ?  1485 CYS   A C   1 
ATOM   11735 O  O   . CYS   A 1 1487 ? -31.06200  24.80900  -0.96800  1.000 51.48996  ?  1485 CYS   A O   1 
ATOM   11736 C  CB  . CYS   A 1 1487 ? -29.44300  26.79900  1.11700   1.000 45.85421  ?  1485 CYS   A CB  1 
ATOM   11737 S  SG  . CYS   A 1 1487 ? -28.33600  27.72600  0.03800   1.000 69.35320  ?  1485 CYS   A SG  1 
ATOM   11738 N  N   . GLY   A 1 1488 ? -30.54700  26.84400  -1.81600  1.000 39.47641  ?  1486 GLY   A N   1 
ATOM   11739 C  CA  . GLY   A 1 1488 ? -30.44000  26.41700  -3.20100  1.000 50.43365  ?  1486 GLY   A CA  1 
ATOM   11740 C  C   . GLY   A 1 1488 ? -31.42600  27.10500  -4.12400  1.000 48.48011  ?  1486 GLY   A C   1 
ATOM   11741 O  O   . GLY   A 1 1488 ? -31.15900  27.23400  -5.32300  1.000 57.75147  ?  1486 GLY   A O   1 
ATOM   11742 N  N   . GLU   A 1 1489 ? -32.55900  27.54700  -3.58700  1.000 50.26053  ?  1487 GLU   A N   1 
ATOM   11743 C  CA  . GLU   A 1 1489 ? -33.58400  28.21300  -4.37900  1.000 49.94487  ?  1487 GLU   A CA  1 
ATOM   11744 C  C   . GLU   A 1 1489 ? -34.51100  28.96100  -3.43300  1.000 53.56244  ?  1487 GLU   A C   1 
ATOM   11745 O  O   . GLU   A 1 1489 ? -34.42400  28.82600  -2.21000  1.000 53.61652  ?  1487 GLU   A O   1 
ATOM   11746 C  CB  . GLU   A 1 1489 ? -34.36000  27.21200  -5.24300  1.000 47.18720  ?  1487 GLU   A CB  1 
ATOM   11747 C  CG  . GLU   A 1 1489 ? -34.81700  25.97700  -4.48800  1.000 59.76113  ?  1487 GLU   A CG  1 
ATOM   11748 C  CD  . GLU   A 1 1489 ? -35.50900  24.96100  -5.37400  1.000 66.82235  ?  1487 GLU   A CD  1 
ATOM   11749 O  OE1 . GLU   A 1 1489 ? -34.93500  24.57900  -6.41600  1.000 69.23943  ?  1487 GLU   A OE1 1 
ATOM   11750 O  OE2 . GLU   A 1 1489 ? -36.63400  24.54900  -5.02700  1.000 73.54529  -1 1487 GLU   A OE2 1 
ATOM   11751 N  N   . ALA   A 1 1490 ? -35.39900  29.76100  -4.01700  1.000 53.42347  ?  1488 ALA   A N   1 
ATOM   11752 C  CA  . ALA   A 1 1490 ? -36.34100  30.53600  -3.22300  1.000 49.62744  ?  1488 ALA   A CA  1 
ATOM   11753 C  C   . ALA   A 1 1490 ? -37.32300  29.61400  -2.51600  1.000 52.04274  ?  1488 ALA   A C   1 
ATOM   11754 O  O   . ALA   A 1 1490 ? -37.83400  28.65400  -3.10100  1.000 61.64293  ?  1488 ALA   A O   1 
ATOM   11755 C  CB  . ALA   A 1 1490 ? -37.09300  31.52800  -4.10900  1.000 50.57889  ?  1488 ALA   A CB  1 
ATOM   11756 N  N   . MET   A 1 1491 ? -37.58200  29.90300  -1.25100  1.000 42.21669  ?  1489 MET   A N   1 
ATOM   11757 C  CA  . MET   A 1 1491 ? -38.49400  29.06400  -0.48400  1.000 50.80836  ?  1489 MET   A CA  1 
ATOM   11758 C  C   . MET   A 1 1491 ? -39.93700  29.46600  -0.76600  1.000 68.87352  ?  1489 MET   A C   1 
ATOM   11759 O  O   . MET   A 1 1491 ? -40.26900  30.65300  -0.68600  1.000 74.76743  ?  1489 MET   A O   1 
ATOM   11760 C  CB  . MET   A 1 1491 ? -38.21100  29.18200  1.00700   1.000 50.49416  ?  1489 MET   A CB  1 
ATOM   11761 C  CG  . MET   A 1 1491 ? -39.41000  28.82900  1.86500   1.000 54.47335  ?  1489 MET   A CG  1 
ATOM   11762 S  SD  . MET   A 1 1491 ? -38.95800  28.05300  3.41900   1.000 66.43438  ?  1489 MET   A SD  1 
ATOM   11763 C  CE  . MET   A 1 1491 ? -38.29000  26.49700  2.84200   1.000 56.16725  ?  1489 MET   A CE  1 
ATOM   11764 N  N   . PRO   A 1 1492 ? -40.81100  28.51900  -1.09900  1.000 71.83303  ?  1490 PRO   A N   1 
ATOM   11765 C  CA  . PRO   A 1 1492 ? -42.22700  28.86000  -1.27100  1.000 69.18097  ?  1490 PRO   A CA  1 
ATOM   11766 C  C   . PRO   A 1 1492 ? -42.83600  29.30900  0.05000   1.000 76.81261  ?  1490 PRO   A C   1 
ATOM   11767 O  O   . PRO   A 1 1492 ? -42.59000  28.71300  1.10200   1.000 86.70455  ?  1490 PRO   A O   1 
ATOM   11768 C  CB  . PRO   A 1 1492 ? -42.85300  27.55000  -1.76400  1.000 82.68390  ?  1490 PRO   A CB  1 
ATOM   11769 C  CG  . PRO   A 1 1492 ? -41.69900  26.71300  -2.25000  1.000 92.04233  ?  1490 PRO   A CG  1 
ATOM   11770 C  CD  . PRO   A 1 1492 ? -40.53400  27.10200  -1.39700  1.000 72.14482  ?  1490 PRO   A CD  1 
ATOM   11771 N  N   . ASP   A 1 1493 ? -43.63500  30.37800  -0.01000  1.000 75.57936  ?  1491 ASP   A N   1 
ATOM   11772 C  CA  . ASP   A 1 1493 ? -44.30700  30.86200  1.19000   1.000 72.72146  ?  1491 ASP   A CA  1 
ATOM   11773 C  C   . ASP   A 1 1493 ? -45.27400  29.83300  1.76000   1.000 73.14705  ?  1491 ASP   A C   1 
ATOM   11774 O  O   . ASP   A 1 1493 ? -45.59200  29.89000  2.95300   1.000 59.20690  ?  1491 ASP   A O   1 
ATOM   11775 C  CB  . ASP   A 1 1493 ? -45.05700  32.16400  0.89700   1.000 68.19640  ?  1491 ASP   A CB  1 
ATOM   11776 C  CG  . ASP   A 1 1493 ? -44.60800  32.81900  -0.39100  1.000 84.08893  ?  1491 ASP   A CG  1 
ATOM   11777 O  OD1 . ASP   A 1 1493 ? -43.45500  32.58200  -0.80900  1.000 101.05941 ?  1491 ASP   A OD1 1 
ATOM   11778 O  OD2 . ASP   A 1 1493 ? -45.40900  33.57100  -0.98500  1.000 88.42099  -1 1491 ASP   A OD2 1 
ATOM   11779 N  N   . GLU   A 1 1494 ? -45.74400  28.89500  0.93300   1.000 70.73357  ?  1492 GLU   A N   1 
ATOM   11780 C  CA  . GLU   A 1 1494 ? -46.67300  27.86600  1.38000   1.000 63.55627  ?  1492 GLU   A CA  1 
ATOM   11781 C  C   . GLU   A 1 1494 ? -45.98400  26.71000  2.09400   1.000 70.05176  ?  1492 GLU   A C   1 
ATOM   11782 O  O   . GLU   A 1 1494 ? -46.65600  25.94500  2.79400   1.000 79.53990  ?  1492 GLU   A O   1 
ATOM   11783 C  CB  . GLU   A 1 1494 ? -47.46800  27.31600  0.19100   1.000 65.86901  ?  1492 GLU   A CB  1 
ATOM   11784 C  CG  . GLU   A 1 1494 ? -46.61600  26.67900  -0.90400  1.000 66.23466  ?  1492 GLU   A CG  1 
ATOM   11785 C  CD  . GLU   A 1 1494 ? -46.30300  27.63400  -2.04300  1.000 74.85196  ?  1492 GLU   A CD  1 
ATOM   11786 O  OE1 . GLU   A 1 1494 ? -46.12000  28.84100  -1.77800  1.000 74.09486  ?  1492 GLU   A OE1 1 
ATOM   11787 O  OE2 . GLU   A 1 1494 ? -46.24600  27.17700  -3.20500  1.000 59.04831  -1 1492 GLU   A OE2 1 
ATOM   11788 N  N   . LEU   A 1 1495 ? -44.66800  26.56400  1.93600   1.000 69.61561  ?  1493 LEU   A N   1 
ATOM   11789 C  CA  . LEU   A 1 1495 ? -43.97400  25.42400  2.52200   1.000 64.48507  ?  1493 LEU   A CA  1 
ATOM   11790 C  C   . LEU   A 1 1495 ? -43.74800  25.59400  4.01800   1.000 57.24675  ?  1493 LEU   A C   1 
ATOM   11791 O  O   . LEU   A 1 1495 ? -43.64300  24.59600  4.73900   1.000 65.78971  ?  1493 LEU   A O   1 
ATOM   11792 C  CB  . LEU   A 1 1495 ? -42.64100  25.20300  1.80500   1.000 72.78649  ?  1493 LEU   A CB  1 
ATOM   11793 C  CG  . LEU   A 1 1495 ? -42.01100  23.81300  1.90200   1.000 72.86466  ?  1493 LEU   A CG  1 
ATOM   11794 C  CD1 . LEU   A 1 1495 ? -43.08400  22.73800  1.98700   1.000 64.31237  ?  1493 LEU   A CD1 1 
ATOM   11795 C  CD2 . LEU   A 1 1495 ? -41.11800  23.58000  0.69500   1.000 67.30294  ?  1493 LEU   A CD2 1 
ATOM   11796 N  N   . VAL   A 1 1496 ? -43.67800  26.83800  4.50200   1.000 57.49198  ?  1494 VAL   A N   1 
ATOM   11797 C  CA  . VAL   A 1 1496 ? -43.43200  27.06800  5.92700   1.000 64.14161  ?  1494 VAL   A CA  1 
ATOM   11798 C  C   . VAL   A 1 1496 ? -44.50100  26.42400  6.80500   1.000 64.95119  ?  1494 VAL   A C   1 
ATOM   11799 O  O   . VAL   A 1 1496 ? -44.14000  25.71900  7.76200   1.000 49.86711  ?  1494 VAL   A O   1 
ATOM   11800 C  CB  . VAL   A 1 1496 ? -43.26500  28.57300  6.19900   1.000 60.82141  ?  1494 VAL   A CB  1 
ATOM   11801 C  CG1 . VAL   A 1 1496 ? -42.78500  28.80600  7.62300   1.000 62.29944  ?  1494 VAL   A CG1 1 
ATOM   11802 C  CG2 . VAL   A 1 1496 ? -42.31200  29.19300  5.19100   1.000 52.79287  ?  1494 VAL   A CG2 1 
ATOM   11803 N  N   . PRO   A 1 1497 ? -45.80500  26.61000  6.55600   1.000 82.54205  ?  1495 PRO   A N   1 
ATOM   11804 C  CA  . PRO   A 1 1497 ? -46.79100  25.88100  7.36900   1.000 85.18169  ?  1495 PRO   A CA  1 
ATOM   11805 C  C   . PRO   A 1 1497 ? -46.80600  24.38500  7.10100   1.000 81.70582  ?  1495 PRO   A C   1 
ATOM   11806 O  O   . PRO   A 1 1497 ? -47.05500  23.60700  8.03100   1.000 73.85385  ?  1495 PRO   A O   1 
ATOM   11807 C  CB  . PRO   A 1 1497 ? -48.12200  26.54100  6.98200   1.000 66.64440  ?  1495 PRO   A CB  1 
ATOM   11808 C  CG  . PRO   A 1 1497 ? -47.89000  27.06900  5.62000   1.000 56.75189  ?  1495 PRO   A CG  1 
ATOM   11809 C  CD  . PRO   A 1 1497 ? -46.46500  27.52800  5.60700   1.000 68.03165  ?  1495 PRO   A CD  1 
ATOM   11810 N  N   . LYS   A 1 1498 ? -46.54900  23.95700  5.86200   1.000 60.00170  ?  1496 LYS   A N   1 
ATOM   11811 C  CA  . LYS   A 1 1498 ? -46.52700  22.52700  5.56600   1.000 58.20002  ?  1496 LYS   A CA  1 
ATOM   11812 C  C   . LYS   A 1 1498 ? -45.40400  21.82100  6.31800   1.000 69.11515  ?  1496 LYS   A C   1 
ATOM   11813 O  O   . LYS   A 1 1498 ? -45.57100  20.68100  6.76700   1.000 64.35780  ?  1496 LYS   A O   1 
ATOM   11814 C  CB  . LYS   A 1 1498 ? -46.39000  22.29700  4.05900   1.000 52.27952  ?  1496 LYS   A CB  1 
ATOM   11815 C  CG  . LYS   A 1 1498 ? -47.65600  22.59200  3.27000   1.000 66.20376  ?  1496 LYS   A CG  1 
ATOM   11816 C  CD  . LYS   A 1 1498 ? -47.63000  21.94000  1.89300   1.000 47.42132  ?  1496 LYS   A CD  1 
ATOM   11817 C  CE  . LYS   A 1 1498 ? -46.67600  22.65100  0.94800   1.000 63.04194  ?  1496 LYS   A CE  1 
ATOM   11818 N  NZ  . LYS   A 1 1498 ? -46.67700  22.02800  -0.40600  1.000 63.00651  ?  1496 LYS   A NZ  1 
ATOM   11819 N  N   . VAL   A 1 1499 ? -44.25300  22.48100  6.46500   1.000 72.79877  ?  1497 VAL   A N   1 
ATOM   11820 C  CA  . VAL   A 1 1499 ? -43.14200  21.88600  7.20500   1.000 67.69034  ?  1497 VAL   A CA  1 
ATOM   11821 C  C   . VAL   A 1 1499 ? -43.49700  21.75100  8.68100   1.000 65.50866  ?  1497 VAL   A C   1 
ATOM   11822 O  O   . VAL   A 1 1499 ? -43.40000  20.66400  9.26300   1.000 60.71590  ?  1497 VAL   A O   1 
ATOM   11823 C  CB  . VAL   A 1 1499 ? -41.85700  22.71300  7.01300   1.000 57.03757  ?  1497 VAL   A CB  1 
ATOM   11824 C  CG1 . VAL   A 1 1499 ? -40.77500  22.23800  7.97200   1.000 51.91985  ?  1497 VAL   A CG1 1 
ATOM   11825 C  CG2 . VAL   A 1 1499 ? -41.36800  22.61900  5.57800   1.000 60.73074  ?  1497 VAL   A CG2 1 
ATOM   11826 N  N   . TYR   A 1 1500 ? -43.91300  22.85400  9.30800   1.000 54.09689  ?  1498 TYR   A N   1 
ATOM   11827 C  CA  . TYR   A 1 1500 ? -44.21800  22.83100  10.73400  1.000 60.62039  ?  1498 TYR   A CA  1 
ATOM   11828 C  C   . TYR   A 1 1500 ? -45.41100  21.94300  11.06200  1.000 72.90550  ?  1498 TYR   A C   1 
ATOM   11829 O  O   . TYR   A 1 1500 ? -45.56600  21.53600  12.21900  1.000 72.81776  ?  1498 TYR   A O   1 
ATOM   11830 C  CB  . TYR   A 1 1500 ? -44.47000  24.25100  11.24200  1.000 71.22579  ?  1498 TYR   A CB  1 
ATOM   11831 C  CG  . TYR   A 1 1500 ? -43.20700  25.04700  11.48900  1.000 76.41481  ?  1498 TYR   A CG  1 
ATOM   11832 C  CD1 . TYR   A 1 1500 ? -42.50600  24.91800  12.68100  1.000 86.17107  ?  1498 TYR   A CD1 1 
ATOM   11833 C  CD2 . TYR   A 1 1500 ? -42.71500  25.92600  10.53200  1.000 75.38988  ?  1498 TYR   A CD2 1 
ATOM   11834 C  CE1 . TYR   A 1 1500 ? -41.35300  25.64100  12.91400  1.000 78.11276  ?  1498 TYR   A CE1 1 
ATOM   11835 C  CE2 . TYR   A 1 1500 ? -41.56000  26.65400  10.75700  1.000 79.38527  ?  1498 TYR   A CE2 1 
ATOM   11836 C  CZ  . TYR   A 1 1500 ? -40.88400  26.50700  11.95100  1.000 70.04558  ?  1498 TYR   A CZ  1 
ATOM   11837 O  OH  . TYR   A 1 1500 ? -39.73400  27.22300  12.19100  1.000 62.55188  ?  1498 TYR   A OH  1 
ATOM   11838 N  N   . GLU   A 1 1501 ? -46.25600  21.63000  10.07800  1.000 61.71779  ?  1499 GLU   A N   1 
ATOM   11839 C  CA  . GLU   A 1 1501 ? -47.38000  20.73800  10.34000  1.000 70.50907  ?  1499 GLU   A CA  1 
ATOM   11840 C  C   . GLU   A 1 1501 ? -46.92200  19.28800  10.44000  1.000 72.53174  ?  1499 GLU   A C   1 
ATOM   11841 O  O   . GLU   A 1 1501 ? -47.25500  18.58900  11.40400  1.000 66.29699  ?  1499 GLU   A O   1 
ATOM   11842 C  CB  . GLU   A 1 1501 ? -48.44300  20.88400  9.25000   1.000 77.01005  ?  1499 GLU   A CB  1 
ATOM   11843 C  CG  . GLU   A 1 1501 ? -49.73300  20.14500  9.56700   1.000 83.55248  ?  1499 GLU   A CG  1 
ATOM   11844 C  CD  . GLU   A 1 1501 ? -50.38900  19.55300  8.33700   1.000 110.20072 ?  1499 GLU   A CD  1 
ATOM   11845 O  OE1 . GLU   A 1 1501 ? -49.95600  19.88200  7.21200   1.000 103.11413 ?  1499 GLU   A OE1 1 
ATOM   11846 O  OE2 . GLU   A 1 1501 ? -51.33500  18.75200  8.49600   1.000 118.63202 -1 1499 GLU   A OE2 1 
ATOM   11847 N  N   . VAL   A 1 1502 ? -46.15300  18.82000  9.45300   1.000 78.95072  ?  1500 VAL   A N   1 
ATOM   11848 C  CA  . VAL   A 1 1502 ? -45.73500  17.42200  9.44000   1.000 64.87203  ?  1500 VAL   A CA  1 
ATOM   11849 C  C   . VAL   A 1 1502 ? -44.66000  17.16300  10.48600  1.000 63.66826  ?  1500 VAL   A C   1 
ATOM   11850 O  O   . VAL   A 1 1502 ? -44.54300  16.04400  11.00200  1.000 65.10532  ?  1500 VAL   A O   1 
ATOM   11851 C  CB  . VAL   A 1 1502 ? -45.25900  17.01700  8.03100   1.000 70.38838  ?  1500 VAL   A CB  1 
ATOM   11852 C  CG1 . VAL   A 1 1502 ? -46.36000  17.25500  7.00600   1.000 75.62924  ?  1500 VAL   A CG1 1 
ATOM   11853 C  CG2 . VAL   A 1 1502 ? -43.99100  17.77200  7.64400   1.000 66.89824  ?  1500 VAL   A CG2 1 
ATOM   11854 N  N   . LEU   A 1 1503 ? -43.86600  18.17500  10.82500  1.000 63.85422  ?  1501 LEU   A N   1 
ATOM   11855 C  CA  . LEU   A 1 1503 ? -42.74500  18.01600  11.75100  1.000 71.03594  ?  1501 LEU   A CA  1 
ATOM   11856 C  C   . LEU   A 1 1503 ? -42.69100  19.20600  12.69400  1.000 65.97561  ?  1501 LEU   A C   1 
ATOM   11857 O  O   . LEU   A 1 1503 ? -41.87600  20.12000  12.52400  1.000 66.26305  ?  1501 LEU   A O   1 
ATOM   11858 C  CB  . LEU   A 1 1503 ? -41.42400  17.86500  10.99200  1.000 61.43369  ?  1501 LEU   A CB  1 
ATOM   11859 C  CG  . LEU   A 1 1503 ? -40.40700  16.90400  11.60500  1.000 55.54907  ?  1501 LEU   A CG  1 
ATOM   11860 C  CD1 . LEU   A 1 1503 ? -40.88300  15.46300  11.46800  1.000 71.64670  ?  1501 LEU   A CD1 1 
ATOM   11861 C  CD2 . LEU   A 1 1503 ? -39.04000  17.08600  10.96900  1.000 67.78597  ?  1501 LEU   A CD2 1 
ATOM   11862 N  N   . PRO   A 1 1504 ? -43.55200  19.23100  13.71000  1.000 74.90449  ?  1502 PRO   A N   1 
ATOM   11863 C  CA  . PRO   A 1 1504 ? -43.42300  20.25400  14.75300  1.000 55.78008  ?  1502 PRO   A CA  1 
ATOM   11864 C  C   . PRO   A 1 1504 ? -42.10800  20.08800  15.50200  1.000 65.03641  ?  1502 PRO   A C   1 
ATOM   11865 O  O   . PRO   A 1 1504 ? -41.41200  19.07500  15.38300  1.000 77.12445  ?  1502 PRO   A O   1 
ATOM   11866 C  CB  . PRO   A 1 1504 ? -44.63100  20.00200  15.66200  1.000 60.18185  ?  1502 PRO   A CB  1 
ATOM   11867 C  CG  . PRO   A 1 1504 ? -45.58800  19.19400  14.82100  1.000 62.45556  ?  1502 PRO   A CG  1 
ATOM   11868 C  CD  . PRO   A 1 1504 ? -44.72400  18.36600  13.92300  1.000 62.99194  ?  1502 PRO   A CD  1 
ATOM   11869 N  N   . GLU   A 1 1505 ? -41.75700  21.13100  16.26100  1.000 70.07290  ?  1503 GLU   A N   1 
ATOM   11870 C  CA  . GLU   A 1 1505 ? -40.52700  21.19900  17.04900  1.000 87.94297  ?  1503 GLU   A CA  1 
ATOM   11871 C  C   . GLU   A 1 1505 ? -39.30500  21.31500  16.13500  1.000 82.82094  ?  1503 GLU   A C   1 
ATOM   11872 O  O   . GLU   A 1 1505 ? -38.19800  21.59400  16.60100  1.000 81.28224  ?  1503 GLU   A O   1 
ATOM   11873 C  CB  . GLU   A 1 1505 ? -40.42100  19.99300  18.00200  1.000 79.99215  ?  1503 GLU   A CB  1 
ATOM   11874 C  CG  . GLU   A 1 1505 ? -39.83500  20.28400  19.37600  1.000 82.31103  ?  1503 GLU   A CG  1 
ATOM   11875 C  CD  . GLU   A 1 1505 ? -38.41100  20.76500  19.31600  1.000 104.08739 ?  1503 GLU   A CD  1 
ATOM   11876 O  OE1 . GLU   A 1 1505 ? -37.50300  19.92400  19.15100  1.000 115.55834 ?  1503 GLU   A OE1 1 
ATOM   11877 O  OE2 . GLU   A 1 1505 ? -38.20800  21.99200  19.39200  1.000 94.59230  -1 1503 GLU   A OE2 1 
ATOM   11878 N  N   . VAL   A 1 1506 ? -39.46900  21.14800  14.83800  1.000 64.03116  ?  1504 VAL   A N   1 
ATOM   11879 C  CA  . VAL   A 1 1506 ? -38.34100  21.42500  13.96100  1.000 64.28067  ?  1504 VAL   A CA  1 
ATOM   11880 C  C   . VAL   A 1 1506 ? -38.23900  22.93200  13.76300  1.000 75.01922  ?  1504 VAL   A C   1 
ATOM   11881 O  O   . VAL   A 1 1506 ? -39.21900  23.66800  13.92800  1.000 77.66849  ?  1504 VAL   A O   1 
ATOM   11882 C  CB  . VAL   A 1 1506 ? -38.47700  20.67500  12.62300  1.000 55.25624  ?  1504 VAL   A CB  1 
ATOM   11883 C  CG1 . VAL   A 1 1506 ? -39.21100  21.53100  11.62400  1.000 61.01688  ?  1504 VAL   A CG1 1 
ATOM   11884 C  CG2 . VAL   A 1 1506 ? -37.10200  20.27400  12.10600  1.000 54.78532  ?  1504 VAL   A CG2 1 
ATOM   11885 N  N   . LYS   A 1 1507 ? -37.03900  23.40800  13.44400  1.000 57.90788  ?  1505 LYS   A N   1 
ATOM   11886 C  CA  . LYS   A 1 1507 ? -36.79600  24.83100  13.22000  1.000 61.56072  ?  1505 LYS   A CA  1 
ATOM   11887 C  C   . LYS   A 1 1507 ? -36.40500  25.02500  11.76000  1.000 69.68570  ?  1505 LYS   A C   1 
ATOM   11888 O  O   . LYS   A 1 1507 ? -35.25200  24.79900  11.38300  1.000 71.42049  ?  1505 LYS   A O   1 
ATOM   11889 C  CB  . LYS   A 1 1507 ? -35.71800  25.36300  14.15900  1.000 61.07905  ?  1505 LYS   A CB  1 
ATOM   11890 C  CG  . LYS   A 1 1507 ? -35.98500  25.09500  15.62800  1.000 61.00109  ?  1505 LYS   A CG  1 
ATOM   11891 C  CD  . LYS   A 1 1507 ? -37.20600  25.85400  16.12500  1.000 73.07665  ?  1505 LYS   A CD  1 
ATOM   11892 C  CE  . LYS   A 1 1507 ? -36.97500  27.35700  16.08700  1.000 78.41648  ?  1505 LYS   A CE  1 
ATOM   11893 N  NZ  . LYS   A 1 1507 ? -38.11000  28.12300  16.67500  1.000 66.25951  ?  1505 LYS   A NZ  1 
ATOM   11894 N  N   . LEU   A 1 1508 ? -37.36500  25.44300  10.94100  1.000 74.52411  ?  1506 LEU   A N   1 
ATOM   11895 C  CA  . LEU   A 1 1508 ? -37.09100  25.68600  9.53200   1.000 56.31158  ?  1506 LEU   A CA  1 
ATOM   11896 C  C   . LEU   A 1 1508 ? -36.33000  26.99500  9.37100   1.000 62.63037  ?  1506 LEU   A C   1 
ATOM   11897 O  O   . LEU   A 1 1508 ? -36.74900  28.03700  9.88300   1.000 65.88387  ?  1506 LEU   A O   1 
ATOM   11898 C  CB  . LEU   A 1 1508 ? -38.39600  25.71900  8.73800   1.000 54.58812  ?  1506 LEU   A CB  1 
ATOM   11899 C  CG  . LEU   A 1 1508 ? -38.27300  25.76700  7.21500   1.000 54.06342  ?  1506 LEU   A CG  1 
ATOM   11900 C  CD1 . LEU   A 1 1508 ? -37.49800  24.56500  6.70000   1.000 51.08037  ?  1506 LEU   A CD1 1 
ATOM   11901 C  CD2 . LEU   A 1 1508 ? -39.64600  25.84200  6.56100   1.000 54.58983  ?  1506 LEU   A CD2 1 
ATOM   11902 N  N   . GLU   A 1 1509 ? -35.19800  26.93500  8.67300   1.000 56.48394  ?  1507 GLU   A N   1 
ATOM   11903 C  CA  . GLU   A 1 1509 ? -34.33200  28.08800  8.47400   1.000 42.83581  ?  1507 GLU   A CA  1 
ATOM   11904 C  C   . GLU   A 1 1509 ? -33.98400  28.19200  6.99800   1.000 56.20013  ?  1507 GLU   A C   1 
ATOM   11905 O  O   . GLU   A 1 1509 ? -33.57300  27.20100  6.38400   1.000 53.75465  ?  1507 GLU   A O   1 
ATOM   11906 C  CB  . GLU   A 1 1509 ? -33.05400  27.97000  9.31200   1.000 40.15080  ?  1507 GLU   A CB  1 
ATOM   11907 C  CG  . GLU   A 1 1509 ? -33.29000  27.55900  10.75900  1.000 44.89725  ?  1507 GLU   A CG  1 
ATOM   11908 C  CD  . GLU   A 1 1509 ? -33.39500  28.74300  11.69700  1.000 58.03002  ?  1507 GLU   A CD  1 
ATOM   11909 O  OE1 . GLU   A 1 1509 ? -32.72500  29.76500  11.43900  1.000 64.24987  ?  1507 GLU   A OE1 1 
ATOM   11910 O  OE2 . GLU   A 1 1509 ? -34.14300  28.65000  12.69300  1.000 57.52850  -1 1507 GLU   A OE2 1 
ATOM   11911 N  N   . ASN   A 1 1510 ? -34.15200  29.38300  6.43200   1.000 60.69703  ?  1508 ASN   A N   1 
ATOM   11912 C  CA  . ASN   A 1 1510 ? -33.80800  29.64300  5.04100   1.000 46.39872  ?  1508 ASN   A CA  1 
ATOM   11913 C  C   . ASN   A 1 1510 ? -32.42200  30.27400  4.99700   1.000 46.76763  ?  1508 ASN   A C   1 
ATOM   11914 O  O   . ASN   A 1 1510 ? -32.20600  31.34800  5.57000   1.000 50.54815  ?  1508 ASN   A O   1 
ATOM   11915 C  CB  . ASN   A 1 1510 ? -34.84100  30.55500  4.37900   1.000 39.84441  ?  1508 ASN   A CB  1 
ATOM   11916 C  CG  . ASN   A 1 1510 ? -34.87000  30.40200  2.87000   1.000 45.16525  ?  1508 ASN   A CG  1 
ATOM   11917 O  OD1 . ASN   A 1 1510 ? -34.66600  29.30800  2.34100   1.000 53.81726  ?  1508 ASN   A OD1 1 
ATOM   11918 N  ND2 . ASN   A 1 1510 ? -35.12300  31.50000  2.16900   1.000 48.46879  ?  1508 ASN   A ND2 1 
ATOM   11919 N  N   . ILE   A 1 1511 ? -31.48900  29.60400  4.32700   1.000 48.18005  ?  1509 ILE   A N   1 
ATOM   11920 C  CA  . ILE   A 1 1511 ? -30.10500  30.05000  4.24800   1.000 39.47353  ?  1509 ILE   A CA  1 
ATOM   11921 C  C   . ILE   A 1 1511 ? -29.79300  30.44000  2.81000   1.000 45.06597  ?  1509 ILE   A C   1 
ATOM   11922 O  O   . ILE   A 1 1511 ? -30.34000  29.87400  1.85600   1.000 46.36997  ?  1509 ILE   A O   1 
ATOM   11923 C  CB  . ILE   A 1 1511 ? -29.12700  28.96400  4.74400   1.000 43.15051  ?  1509 ILE   A CB  1 
ATOM   11924 C  CG1 . ILE   A 1 1511 ? -29.71400  28.20800  5.93800   1.000 46.77296  ?  1509 ILE   A CG1 1 
ATOM   11925 C  CG2 . ILE   A 1 1511 ? -27.81200  29.59200  5.14800   1.000 47.58657  ?  1509 ILE   A CG2 1 
ATOM   11926 C  CD1 . ILE   A 1 1511 ? -29.57100  28.93400  7.26100   1.000 56.01895  ?  1509 ILE   A CD1 1 
ATOM   11927 N  N   . TYR   A 1 1512 ? -28.90300  31.42000  2.65900   1.000 39.38778  ?  1510 TYR   A N   1 
ATOM   11928 C  CA  . TYR   A 1 1512 ? -28.47100  31.89200  1.35200   1.000 41.21391  ?  1510 TYR   A CA  1 
ATOM   11929 C  C   . TYR   A 1 1512 ? -26.96100  32.08200  1.36000   1.000 45.83187  ?  1510 TYR   A C   1 
ATOM   11930 O  O   . TYR   A 1 1512 ? -26.37200  32.44900  2.38000   1.000 41.44029  ?  1510 TYR   A O   1 
ATOM   11931 C  CB  . TYR   A 1 1512 ? -29.16400  33.20900  0.96400   1.000 34.75465  ?  1510 TYR   A CB  1 
ATOM   11932 C  CG  . TYR   A 1 1512 ? -28.53200  33.92300  -0.21400  1.000 37.16976  ?  1510 TYR   A CG  1 
ATOM   11933 C  CD1 . TYR   A 1 1512 ? -28.82000  33.54300  -1.52000  1.000 32.14225  ?  1510 TYR   A CD1 1 
ATOM   11934 C  CD2 . TYR   A 1 1512 ? -27.64700  34.97900  -0.02000  1.000 39.89297  ?  1510 TYR   A CD2 1 
ATOM   11935 C  CE1 . TYR   A 1 1512 ? -28.24300  34.19300  -2.59900  1.000 33.56289  ?  1510 TYR   A CE1 1 
ATOM   11936 C  CE2 . TYR   A 1 1512 ? -27.06500  35.63300  -1.09200  1.000 38.18250  ?  1510 TYR   A CE2 1 
ATOM   11937 C  CZ  . TYR   A 1 1512 ? -27.36700  35.23800  -2.37900  1.000 43.57700  ?  1510 TYR   A CZ  1 
ATOM   11938 O  OH  . TYR   A 1 1512 ? -26.79000  35.88800  -3.44700  1.000 32.14778  ?  1510 TYR   A OH  1 
ATOM   11939 N  N   . GLY   A 1 1513 ? -26.34200  31.83000  0.20900   1.000 32.37736  ?  1511 GLY   A N   1 
ATOM   11940 C  CA  . GLY   A 1 1513 ? -24.92000  32.01300  0.06000   1.000 37.81968  ?  1511 GLY   A CA  1 
ATOM   11941 C  C   . GLY   A 1 1513 ? -24.39500  31.48700  -1.25900  1.000 45.76282  ?  1511 GLY   A C   1 
ATOM   11942 O  O   . GLY   A 1 1513 ? -24.64100  30.33900  -1.64300  1.000 58.18070  ?  1511 GLY   A O   1 
ATOM   11943 N  N   . PRO   A 1 1514 ? -23.66000  32.32600  -1.98300  1.000 48.96477  ?  1512 PRO   A N   1 
ATOM   11944 C  CA  . PRO   A 1 1514 ? -23.01900  31.86800  -3.21700  1.000 49.26370  ?  1512 PRO   A CA  1 
ATOM   11945 C  C   . PRO   A 1 1514 ? -21.81400  30.99300  -2.91200  1.000 55.43846  ?  1512 PRO   A C   1 
ATOM   11946 O  O   . PRO   A 1 1514 ? -21.28400  30.97600  -1.79900  1.000 56.11028  ?  1512 PRO   A O   1 
ATOM   11947 C  CB  . PRO   A 1 1514 ? -22.59800  33.17200  -3.89900  1.000 42.52760  ?  1512 PRO   A CB  1 
ATOM   11948 C  CG  . PRO   A 1 1514 ? -22.35200  34.10200  -2.76100  1.000 40.95641  ?  1512 PRO   A CG  1 
ATOM   11949 C  CD  . PRO   A 1 1514 ? -23.37500  33.74400  -1.70800  1.000 49.30993  ?  1512 PRO   A CD  1 
ATOM   11950 N  N   . THR   A 1 1515 ? -21.38300  30.25300  -3.93600  1.000 54.91974  ?  1513 THR   A N   1 
ATOM   11951 C  CA  . THR   A 1 1515 ? -20.20700  29.40300  -3.78100  1.000 60.52925  ?  1513 THR   A CA  1 
ATOM   11952 C  C   . THR   A 1 1515 ? -18.95300  30.23200  -3.53400  1.000 60.45689  ?  1513 THR   A C   1 
ATOM   11953 O  O   . THR   A 1 1515 ? -18.02600  29.77200  -2.85600  1.000 54.59542  ?  1513 THR   A O   1 
ATOM   11954 C  CB  . THR   A 1 1515 ? -20.02900  28.52300  -5.01700  1.000 46.34448  ?  1513 THR   A CB  1 
ATOM   11955 O  OG1 . THR   A 1 1515 ? -21.30500  28.02600  -5.43800  1.000 67.12403  ?  1513 THR   A OG1 1 
ATOM   11956 C  CG2 . THR   A 1 1515 ? -19.12000  27.34800  -4.70200  1.000 50.19467  ?  1513 THR   A CG2 1 
ATOM   11957 N  N   . GLU   A 1 1516 ? -18.91300  31.45600  -4.06100  1.000 47.58991  ?  1514 GLU   A N   1 
ATOM   11958 C  CA  . GLU   A 1 1516 ? -17.78200  32.35500  -3.87300  1.000 43.14262  ?  1514 GLU   A CA  1 
ATOM   11959 C  C   . GLU   A 1 1516 ? -17.72200  32.95100  -2.47200  1.000 37.08381  ?  1514 GLU   A C   1 
ATOM   11960 O  O   . GLU   A 1 1516 ? -16.82000  33.75100  -2.19700  1.000 26.12866  ?  1514 GLU   A O   1 
ATOM   11961 C  CB  . GLU   A 1 1516 ? -17.83200  33.47400  -4.91700  1.000 32.57898  ?  1514 GLU   A CB  1 
ATOM   11962 C  CG  . GLU   A 1 1516 ? -17.66100  33.00500  -6.36100  1.000 42.14616  ?  1514 GLU   A CG  1 
ATOM   11963 C  CD  . GLU   A 1 1516 ? -18.94300  32.46100  -6.97400  1.000 51.12272  ?  1514 GLU   A CD  1 
ATOM   11964 O  OE1 . GLU   A 1 1516 ? -19.85900  32.07200  -6.21800  1.000 45.20373  ?  1514 GLU   A OE1 1 
ATOM   11965 O  OE2 . GLU   A 1 1516 ? -19.03600  32.42700  -8.21900  1.000 46.42357  -1 1514 GLU   A OE2 1 
ATOM   11966 N  N   . ALA   A 1 1517 ? -18.65600  32.59600  -1.59300  1.000 35.46333  ?  1515 ALA   A N   1 
ATOM   11967 C  CA  . ALA   A 1 1517 ? -18.58400  32.97800  -0.18900  1.000 47.29132  ?  1515 ALA   A CA  1 
ATOM   11968 C  C   . ALA   A 1 1517 ? -18.64000  31.72200  0.67000   1.000 62.14235  ?  1515 ALA   A C   1 
ATOM   11969 O  O   . ALA   A 1 1517 ? -19.49800  31.60100  1.55200   1.000 53.28336  ?  1515 ALA   A O   1 
ATOM   11970 C  CB  . ALA   A 1 1517 ? -19.71500  33.94100  0.17600   1.000 53.47399  ?  1515 ALA   A CB  1 
ATOM   11971 N  N   . THR   A 1 1518 ? -17.71700  30.79200  0.41400   1.000 64.44086  ?  1516 THR   A N   1 
ATOM   11972 C  CA  . THR   A 1 1518 ? -17.72100  29.44400  0.97900   1.000 65.94651  ?  1516 THR   A CA  1 
ATOM   11973 C  C   . THR   A 1 1518 ? -19.02000  28.71800  0.66000   1.000 77.30538  ?  1516 THR   A C   1 
ATOM   11974 O  O   . THR   A 1 1518 ? -19.21000  28.23700  -0.46300  1.000 75.84542  ?  1516 THR   A O   1 
ATOM   11975 C  CB  . THR   A 1 1518 ? -17.48700  29.46000  2.49400   1.000 68.44355  ?  1516 THR   A CB  1 
ATOM   11976 O  OG1 . THR   A 1 1518 ? -18.55800  30.15600  3.14700   1.000 74.19918  ?  1516 THR   A OG1 1 
ATOM   11977 C  CG2 . THR   A 1 1518 ? -16.16300  30.12600  2.81600   1.000 39.61719  ?  1516 THR   A CG2 1 
ATOM   11978 N  N   . ILE   A 1 1519 ? -19.92100  28.62700  1.63700   1.000 44.77624  ?  1517 ILE   A N   1 
ATOM   11979 C  CA  . ILE   A 1 1519 ? -21.13400  27.82800  1.52100   1.000 55.85166  ?  1517 ILE   A CA  1 
ATOM   11980 C  C   . ILE   A 1 1519 ? -22.38300  28.68200  1.69700   1.000 61.19667  ?  1517 ILE   A C   1 
ATOM   11981 O  O   . ILE   A 1 1519 ? -23.31900  28.60700  0.89500   1.000 38.72703  ?  1517 ILE   A O   1 
ATOM   11982 C  CB  . ILE   A 1 1519 ? -21.12700  26.65500  2.52600   1.000 59.41470  ?  1517 ILE   A CB  1 
ATOM   11983 C  CG1 . ILE   A 1 1519 ? -19.87800  25.79900  2.31400   1.000 50.30895  ?  1517 ILE   A CG1 1 
ATOM   11984 C  CG2 . ILE   A 1 1519 ? -22.36800  25.80600  2.35700   1.000 58.14213  ?  1517 ILE   A CG2 1 
ATOM   11985 C  CD1 . ILE   A 1 1519 ? -19.33000  25.16900  3.57300   1.000 30.18921  ?  1517 ILE   A CD1 1 
ATOM   11986 N  N   . TYR   A 1 1520 ? -22.41500  29.50200  2.74300   1.000 60.30717  ?  1518 TYR   A N   1 
ATOM   11987 C  CA  . TYR   A 1 1520 ? -23.55800  30.34600  3.04600   1.000 46.56996  ?  1518 TYR   A CA  1 
ATOM   11988 C  C   . TYR   A 1 1520 ? -23.08300  31.77200  3.28700   1.000 44.56936  ?  1518 TYR   A C   1 
ATOM   11989 O  O   . TYR   A 1 1520 ? -21.89000  32.08000  3.16800   1.000 56.80002  ?  1518 TYR   A O   1 
ATOM   11990 C  CB  . TYR   A 1 1520 ? -24.33500  29.81200  4.25900   1.000 43.90568  ?  1518 TYR   A CB  1 
ATOM   11991 C  CG  . TYR   A 1 1520 ? -24.76000  28.36600  4.13100   1.000 52.11713  ?  1518 TYR   A CG  1 
ATOM   11992 C  CD1 . TYR   A 1 1520 ? -25.60400  27.95500  3.10500   1.000 54.51836  ?  1518 TYR   A CD1 1 
ATOM   11993 C  CD2 . TYR   A 1 1520 ? -24.32900  27.41300  5.04500   1.000 51.89355  ?  1518 TYR   A CD2 1 
ATOM   11994 C  CE1 . TYR   A 1 1520 ? -26.00000  26.63100  2.99100   1.000 55.43422  ?  1518 TYR   A CE1 1 
ATOM   11995 C  CE2 . TYR   A 1 1520 ? -24.72200  26.08900  4.93900   1.000 49.82404  ?  1518 TYR   A CE2 1 
ATOM   11996 C  CZ  . TYR   A 1 1520 ? -25.55400  25.70500  3.91100   1.000 54.50851  ?  1518 TYR   A CZ  1 
ATOM   11997 O  OH  . TYR   A 1 1520 ? -25.94100  24.38900  3.80700   1.000 62.00288  ?  1518 TYR   A OH  1 
ATOM   11998 N  N   . ALA   A 1 1521 ? -24.02000  32.64400  3.64300   1.000 51.89401  ?  1519 ALA   A N   1 
ATOM   11999 C  CA  . ALA   A 1 1521 ? -23.70700  34.04700  3.88800   1.000 38.54562  ?  1519 ALA   A CA  1 
ATOM   12000 C  C   . ALA   A 1 1521 ? -24.78800  34.71700  4.73200   1.000 38.53867  ?  1519 ALA   A C   1 
ATOM   12001 O  O   . ALA   A 1 1521 ? -24.47900  35.54400  5.59600   1.000 52.01014  ?  1519 ALA   A O   1 
ATOM   12002 C  CB  . ALA   A 1 1521 ? -23.52600  34.80000  2.56600   1.000 29.79637  ?  1519 ALA   A CB  1 
ATOM   12003 N  N   . SER   A 1 1522 ? -26.05400  34.37400  4.49500   1.000 38.01732  ?  1520 SER   A N   1 
ATOM   12004 C  CA  . SER   A 1 1522 ? -27.16700  34.95400  5.23500   1.000 42.36142  ?  1520 SER   A CA  1 
ATOM   12005 C  C   . SER   A 1 1522 ? -28.12500  33.85300  5.66900   1.000 46.82141  ?  1520 SER   A C   1 
ATOM   12006 O  O   . SER   A 1 1522 ? -28.14800  32.75900  5.10000   1.000 53.10948  ?  1520 SER   A O   1 
ATOM   12007 C  CB  . SER   A 1 1522 ? -27.92500  36.00100  4.40700   1.000 38.80090  ?  1520 SER   A CB  1 
ATOM   12008 O  OG  . SER   A 1 1522 ? -28.75300  35.38400  3.43700   1.000 52.57334  ?  1520 SER   A OG  1 
ATOM   12009 N  N   . ARG   A 1 1523 ? -28.92800  34.16200  6.68400   1.000 55.72841  ?  1521 ARG   A N   1 
ATOM   12010 C  CA  . ARG   A 1 1523 ? -29.86500  33.20000  7.24400   1.000 43.91769  ?  1521 ARG   A CA  1 
ATOM   12011 C  C   . ARG   A 1 1523 ? -31.06700  33.94400  7.80500   1.000 51.65792  ?  1521 ARG   A C   1 
ATOM   12012 O  O   . ARG   A 1 1523 ? -30.94400  35.06900  8.29700   1.000 54.41918  ?  1521 ARG   A O   1 
ATOM   12013 C  CB  . ARG   A 1 1523 ? -29.21300  32.35900  8.34600   1.000 46.67200  ?  1521 ARG   A CB  1 
ATOM   12014 C  CG  . ARG   A 1 1523 ? -28.81600  33.17700  9.56100   1.000 55.18698  ?  1521 ARG   A CG  1 
ATOM   12015 C  CD  . ARG   A 1 1523 ? -28.69400  32.32600  10.80400  1.000 62.42656  ?  1521 ARG   A CD  1 
ATOM   12016 N  NE  . ARG   A 1 1523 ? -28.72900  33.13900  12.01300  1.000 79.43415  ?  1521 ARG   A NE  1 
ATOM   12017 C  CZ  . ARG   A 1 1523 ? -29.84000  33.49400  12.64500  1.000 69.64266  ?  1521 ARG   A CZ  1 
ATOM   12018 N  NH1 . ARG   A 1 1523 ? -31.03300  33.14400  12.19500  1.000 61.91644  ?  1521 ARG   A NH1 1 
ATOM   12019 N  NH2 . ARG   A 1 1523 ? -29.75000  34.21800  13.75800  1.000 85.03757  ?  1521 ARG   A NH2 1 
ATOM   12020 N  N   . TYR   A 1 1524 ? -32.23100  33.30300  7.72900   1.000 56.03636  ?  1522 TYR   A N   1 
ATOM   12021 C  CA  . TYR   A 1 1524 ? -33.45400  33.85200  8.30300   1.000 52.97169  ?  1522 TYR   A CA  1 
ATOM   12022 C  C   . TYR   A 1 1524 ? -34.23100  32.72100  8.95700   1.000 52.84921  ?  1522 TYR   A C   1 
ATOM   12023 O  O   . TYR   A 1 1524 ? -34.53700  31.71800  8.30400   1.000 48.51690  ?  1522 TYR   A O   1 
ATOM   12024 C  CB  . TYR   A 1 1524 ? -34.30500  34.55800  7.24300   1.000 43.10938  ?  1522 TYR   A CB  1 
ATOM   12025 C  CG  . TYR   A 1 1524 ? -35.58100  35.14500  7.79700   1.000 54.35036  ?  1522 TYR   A CG  1 
ATOM   12026 C  CD1 . TYR   A 1 1524 ? -35.55100  36.22200  8.67300   1.000 71.43697  ?  1522 TYR   A CD1 1 
ATOM   12027 C  CD2 . TYR   A 1 1524 ? -36.81400  34.62200  7.44600   1.000 56.77330  ?  1522 TYR   A CD2 1 
ATOM   12028 C  CE1 . TYR   A 1 1524 ? -36.71800  36.75800  9.18500   1.000 76.47747  ?  1522 TYR   A CE1 1 
ATOM   12029 C  CE2 . TYR   A 1 1524 ? -37.98600  35.14800  7.95300   1.000 64.34098  ?  1522 TYR   A CE2 1 
ATOM   12030 C  CZ  . TYR   A 1 1524 ? -37.93200  36.21700  8.81900   1.000 67.20108  ?  1522 TYR   A CZ  1 
ATOM   12031 O  OH  . TYR   A 1 1524 ? -39.10000  36.74100  9.32100   1.000 86.39803  ?  1522 TYR   A OH  1 
ATOM   12032 N  N   . SER   A 1 1525 ? -34.54600  32.88500  10.24100  1.000 59.42934  ?  1523 SER   A N   1 
ATOM   12033 C  CA  . SER   A 1 1525 ? -35.21000  31.85200  11.02800  1.000 50.81034  ?  1523 SER   A CA  1 
ATOM   12034 C  C   . SER   A 1 1525 ? -36.71900  31.99200  10.86800  1.000 59.99727  ?  1523 SER   A C   1 
ATOM   12035 O  O   . SER   A 1 1525 ? -37.31500  32.96500  11.34300  1.000 62.10672  ?  1523 SER   A O   1 
ATOM   12036 C  CB  . SER   A 1 1525 ? -34.80800  31.95300  12.49700  1.000 42.56742  ?  1523 SER   A CB  1 
ATOM   12037 O  OG  . SER   A 1 1525 ? -33.40400  31.84600  12.64900  1.000 57.73683  ?  1523 SER   A OG  1 
ATOM   12038 N  N   . LEU   A 1 1526 ? -37.33700  31.02000  10.20600  1.000 66.66439  ?  1524 LEU   A N   1 
ATOM   12039 C  CA  . LEU   A 1 1526 ? -38.78400  30.99900  10.07500  1.000 56.38205  ?  1524 LEU   A CA  1 
ATOM   12040 C  C   . LEU   A 1 1526 ? -39.42200  30.48900  11.36100  1.000 62.25037  ?  1524 LEU   A C   1 
ATOM   12041 O  O   . LEU   A 1 1526 ? -38.88300  29.61200  12.04200  1.000 81.88528  ?  1524 LEU   A O   1 
ATOM   12042 C  CB  . LEU   A 1 1526 ? -39.20700  30.11700  8.90300   1.000 41.99779  ?  1524 LEU   A CB  1 
ATOM   12043 C  CG  . LEU   A 1 1526 ? -38.42200  30.28800  7.60400   1.000 52.95731  ?  1524 LEU   A CG  1 
ATOM   12044 C  CD1 . LEU   A 1 1526 ? -38.99200  29.37700  6.55800   1.000 51.25302  ?  1524 LEU   A CD1 1 
ATOM   12045 C  CD2 . LEU   A 1 1526 ? -38.47100  31.71800  7.12400   1.000 68.63163  ?  1524 LEU   A CD2 1 
ATOM   12046 N  N   . ALA   A 1 1527 ? -40.58100  31.04800  11.69000  1.000 60.65522  ?  1525 ALA   A N   1 
ATOM   12047 C  CA  . ALA   A 1 1527 ? -41.31700  30.66800  12.88300  1.000 70.92111  ?  1525 ALA   A CA  1 
ATOM   12048 C  C   . ALA   A 1 1527 ? -42.68200  30.11300  12.49700  1.000 80.70068  ?  1525 ALA   A C   1 
ATOM   12049 O  O   . ALA   A 1 1527 ? -43.14800  30.27600  11.36600  1.000 72.19934  ?  1525 ALA   A O   1 
ATOM   12050 C  CB  . ALA   A 1 1527 ? -41.48200  31.85500  13.84000  1.000 55.00683  ?  1525 ALA   A CB  1 
ATOM   12051 N  N   . LYS   A 1 1528 ? -43.32300  29.45200  13.46400  1.000 76.05900  ?  1526 LYS   A N   1 
ATOM   12052 C  CA  . LYS   A 1 1528 ? -44.63000  28.84700  13.23900  1.000 69.14760  ?  1526 LYS   A CA  1 
ATOM   12053 C  C   . LYS   A 1 1528 ? -45.72500  29.87500  12.98600  1.000 91.52945  ?  1526 LYS   A C   1 
ATOM   12054 O  O   . LYS   A 1 1528 ? -46.83700  29.48400  12.61000  1.000 80.53226  ?  1526 LYS   A O   1 
ATOM   12055 C  CB  . LYS   A 1 1528 ? -45.01300  27.96800  14.43100  1.000 66.17457  ?  1526 LYS   A CB  1 
ATOM   12056 N  N   . GLY   A 1 1529 ? -45.44400  31.16600  13.18500  1.000 94.59850  ?  1527 GLY   A N   1 
ATOM   12057 C  CA  . GLY   A 1 1529 ? -46.41900  32.18800  12.83700  1.000 88.45985  ?  1527 GLY   A CA  1 
ATOM   12058 C  C   . GLY   A 1 1529 ? -46.85800  32.11000  11.38600  1.000 106.97835 ?  1527 GLY   A C   1 
ATOM   12059 O  O   . GLY   A 1 1529 ? -48.02700  32.34100  11.07100  1.000 124.89798 ?  1527 GLY   A O   1 
ATOM   12060 N  N   . SER   A 1 1530 ? -45.92300  31.79400  10.48600  1.000 97.80504  ?  1528 SER   A N   1 
ATOM   12061 C  CA  . SER   A 1 1530 ? -46.20500  31.54800  9.06800   1.000 100.21286 ?  1528 SER   A CA  1 
ATOM   12062 C  C   . SER   A 1 1530 ? -46.93500  32.73600  8.43200   1.000 112.78301 ?  1528 SER   A C   1 
ATOM   12063 O  O   . SER   A 1 1530 ? -48.06700  32.62800  7.95300   1.000 128.17027 ?  1528 SER   A O   1 
ATOM   12064 C  CB  . SER   A 1 1530 ? -46.99900  30.24900  8.88800   1.000 96.64995  ?  1528 SER   A CB  1 
ATOM   12065 O  OG  . SER   A 1 1530 ? -46.33700  29.14500  9.48500   1.000 78.88588  ?  1528 SER   A OG  1 
ATOM   12066 N  N   . GLN   A 1 1531 ? -46.24400  33.88000  8.42100   1.000 106.60765 ?  1529 GLN   A N   1 
ATOM   12067 C  CA  . GLN   A 1 1531 ? -46.81300  35.14800  7.98500   1.000 110.11679 ?  1529 GLN   A CA  1 
ATOM   12068 C  C   . GLN   A 1 1531 ? -45.88200  35.90600  7.04600   1.000 107.21166 ?  1529 GLN   A C   1 
ATOM   12069 O  O   . GLN   A 1 1531 ? -46.19100  37.04000  6.65900   1.000 114.37408 ?  1529 GLN   A O   1 
ATOM   12070 C  CB  . GLN   A 1 1531 ? -47.14800  36.02100  9.20500   1.000 116.66070 ?  1529 GLN   A CB  1 
ATOM   12071 C  CG  . GLN   A 1 1531 ? -45.93500  36.61000  9.95300   1.000 118.16934 ?  1529 GLN   A CG  1 
ATOM   12072 C  CD  . GLN   A 1 1531 ? -45.09000  35.57800  10.69900  1.000 116.01660 ?  1529 GLN   A CD  1 
ATOM   12073 O  OE1 . GLN   A 1 1531 ? -45.20500  34.37500  10.47500  1.000 114.68828 ?  1529 GLN   A OE1 1 
ATOM   12074 N  NE2 . GLN   A 1 1531 ? -44.22700  36.05900  11.59000  1.000 95.47959  ?  1529 GLN   A NE2 1 
ATOM   12075 N  N   . GLU   A 1 1532 ? -44.75100  35.31000  6.67400   1.000 93.37774  ?  1530 GLU   A N   1 
ATOM   12076 C  CA  . GLU   A 1 1532 ? -43.72600  35.97600  5.88000   1.000 86.18851  ?  1530 GLU   A CA  1 
ATOM   12077 C  C   . GLU   A 1 1532 ? -43.93500  35.61500  4.41500   1.000 82.71585  ?  1530 GLU   A C   1 
ATOM   12078 O  O   . GLU   A 1 1532 ? -43.65100  34.48800  3.99700   1.000 99.40776  ?  1530 GLU   A O   1 
ATOM   12079 C  CB  . GLU   A 1 1532 ? -42.33100  35.57700  6.35700   1.000 79.12074  ?  1530 GLU   A CB  1 
ATOM   12080 C  CG  . GLU   A 1 1532 ? -42.13000  35.68000  7.86700   1.000 79.67107  ?  1530 GLU   A CG  1 
ATOM   12081 C  CD  . GLU   A 1 1532 ? -42.06600  37.11300  8.37300   1.000 99.01943  ?  1530 GLU   A CD  1 
ATOM   12082 O  OE1 . GLU   A 1 1532 ? -42.77900  37.97700  7.81200   1.000 105.41043 ?  1530 GLU   A OE1 1 
ATOM   12083 O  OE2 . GLU   A 1 1532 ? -41.31100  37.37700  9.32900   1.000 109.27477 -1 1530 GLU   A OE2 1 
ATOM   12084 N  N   . SER   A 1 1533 ? -44.44300  36.56900  3.64400   1.000 74.17240  ?  1531 SER   A N   1 
ATOM   12085 C  CA  . SER   A 1 1533 ? -44.60100  36.41200  2.20500   1.000 67.23986  ?  1531 SER   A CA  1 
ATOM   12086 C  C   . SER   A 1 1533 ? -43.28500  36.65400  1.46300   1.000 95.27943  ?  1531 SER   A C   1 
ATOM   12087 O  O   . SER   A 1 1533 ? -42.98000  35.90800  0.52300   1.000 115.70274 ?  1531 SER   A O   1 
ATOM   12088 C  CB  . SER   A 1 1533 ? -45.69400  37.34800  1.68000   1.000 102.15404 ?  1531 SER   A CB  1 
ATOM   12089 O  OG  . SER   A 1 1533 ? -45.15700  38.39100  0.88600   1.000 84.22545  ?  1531 SER   A OG  1 
ATOM   12090 N  N   . PRO   A 1 1534 ? -42.47800  37.66700  1.82100   1.000 97.01667  ?  1532 PRO   A N   1 
ATOM   12091 C  CA  . PRO   A 1 1534 ? -41.19000  37.82300  1.12200   1.000 80.59834  ?  1532 PRO   A CA  1 
ATOM   12092 C  C   . PRO   A 1 1534 ? -40.27500  36.62600  1.26900   1.000 81.89507  ?  1532 PRO   A C   1 
ATOM   12093 O  O   . PRO   A 1 1534 ? -39.49100  36.34700  0.35300   1.000 109.39369 ?  1532 PRO   A O   1 
ATOM   12094 C  CB  . PRO   A 1 1534 ? -40.58400  39.07700  1.77300   1.000 76.89960  ?  1532 PRO   A CB  1 
ATOM   12095 C  CG  . PRO   A 1 1534 ? -41.32900  39.26500  3.04000   1.000 89.09333  ?  1532 PRO   A CG  1 
ATOM   12096 C  CD  . PRO   A 1 1534 ? -42.71000  38.79000  2.75100   1.000 92.73614  ?  1532 PRO   A CD  1 
ATOM   12097 N  N   . VAL   A 1 1535 ? -40.36900  35.90700  2.38500   1.000 74.98465  ?  1533 VAL   A N   1 
ATOM   12098 C  CA  . VAL   A 1 1535 ? -39.45000  34.82300  2.72800   1.000 73.80285  ?  1533 VAL   A CA  1 
ATOM   12099 C  C   . VAL   A 1 1535 ? -38.02500  35.34400  2.60000   1.000 67.58034  ?  1533 VAL   A C   1 
ATOM   12100 O  O   . VAL   A 1 1535 ? -37.34400  35.05300  1.60500   1.000 53.00517  ?  1533 VAL   A O   1 
ATOM   12101 C  CB  . VAL   A 1 1535 ? -39.67700  33.58500  1.84800   1.000 66.44303  ?  1533 VAL   A CB  1 
ATOM   12102 C  CG1 . VAL   A 1 1535 ? -38.95400  32.39100  2.44400   1.000 65.17561  ?  1533 VAL   A CG1 1 
ATOM   12103 C  CG2 . VAL   A 1 1535 ? -41.16100  33.30600  1.70800   1.000 64.62905  ?  1533 VAL   A CG2 1 
ATOM   12104 N  N   . PRO   A 1 1536 ? -37.54100  36.12100  3.56400   1.000 62.98823  ?  1534 PRO   A N   1 
ATOM   12105 C  CA  . PRO   A 1 1536 ? -36.23400  36.76400  3.40600   1.000 60.69203  ?  1534 PRO   A CA  1 
ATOM   12106 C  C   . PRO   A 1 1536 ? -35.09900  35.75400  3.40000   1.000 54.04648  ?  1534 PRO   A C   1 
ATOM   12107 O  O   . PRO   A 1 1536 ? -35.17700  34.68600  4.01100   1.000 63.27965  ?  1534 PRO   A O   1 
ATOM   12108 C  CB  . PRO   A 1 1536 ? -36.13900  37.68600  4.62800   1.000 63.35520  ?  1534 PRO   A CB  1 
ATOM   12109 C  CG  . PRO   A 1 1536 ? -37.53800  37.80500  5.14900   1.000 72.73909  ?  1534 PRO   A CG  1 
ATOM   12110 C  CD  . PRO   A 1 1536 ? -38.21600  36.52200  4.80900   1.000 53.05109  ?  1534 PRO   A CD  1 
ATOM   12111 N  N   . ILE   A 1 1537 ? -34.02900  36.10800  2.68500   1.000 46.96884  ?  1535 ILE   A N   1 
ATOM   12112 C  CA  . ILE   A 1 1537 ? -32.80300  35.32600  2.78000   1.000 41.15899  ?  1535 ILE   A CA  1 
ATOM   12113 C  C   . ILE   A 1 1537 ? -32.05800  35.63100  4.07200   1.000 39.11577  ?  1535 ILE   A C   1 
ATOM   12114 O  O   . ILE   A 1 1537 ? -31.19800  34.84200  4.48500   1.000 53.89797  ?  1535 ILE   A O   1 
ATOM   12115 C  CB  . ILE   A 1 1537 ? -31.89700  35.55500  1.55900   1.000 35.27833  ?  1535 ILE   A CB  1 
ATOM   12116 C  CG1 . ILE   A 1 1537 ? -31.40100  36.99900  1.51200   1.000 43.86007  ?  1535 ILE   A CG1 1 
ATOM   12117 C  CG2 . ILE   A 1 1537 ? -32.63400  35.20100  0.27500   1.000 36.64259  ?  1535 ILE   A CG2 1 
ATOM   12118 C  CD1 . ILE   A 1 1537 ? -30.56900  37.30900  0.29000   1.000 34.72010  ?  1535 ILE   A CD1 1 
ATOM   12119 N  N   . GLY   A 1 1538 ? -32.36400  36.74700  4.72100   1.000 34.08117  ?  1536 GLY   A N   1 
ATOM   12120 C  CA  . GLY   A 1 1538 ? -31.93100  37.00900  6.07800   1.000 42.21962  ?  1536 GLY   A CA  1 
ATOM   12121 C  C   . GLY   A 1 1538 ? -30.85500  38.07600  6.16200   1.000 48.79321  ?  1536 GLY   A C   1 
ATOM   12122 O  O   . GLY   A 1 1538 ? -30.60400  38.83800  5.22500   1.000 47.64263  ?  1536 GLY   A O   1 
ATOM   12123 N  N   . LYS   A 1 1539 ? -30.22500  38.12700  7.33500   1.000 52.80029  ?  1537 LYS   A N   1 
ATOM   12124 C  CA  . LYS   A 1 1539 ? -29.11000  38.99800  7.66500   1.000 52.67454  ?  1537 LYS   A CA  1 
ATOM   12125 C  C   . LYS   A 1 1539 ? -27.80300  38.21800  7.63300   1.000 59.92113  ?  1537 LYS   A C   1 
ATOM   12126 O  O   . LYS   A 1 1539 ? -27.79900  36.98900  7.74700   1.000 55.80418  ?  1537 LYS   A O   1 
ATOM   12127 C  CB  . LYS   A 1 1539 ? -29.31800  39.62400  9.05000   1.000 39.22702  ?  1537 LYS   A CB  1 
ATOM   12128 C  CG  . LYS   A 1 1539 ? -30.48200  40.59900  9.12000   1.000 50.89515  ?  1537 LYS   A CG  1 
ATOM   12129 C  CD  . LYS   A 1 1539 ? -30.57100  41.26200  10.48300  1.000 57.94197  ?  1537 LYS   A CD  1 
ATOM   12130 C  CE  . LYS   A 1 1539 ? -31.86300  42.04800  10.62000  1.000 66.55985  ?  1537 LYS   A CE  1 
ATOM   12131 N  NZ  . LYS   A 1 1539 ? -31.90400  42.85000  11.87400  1.000 71.24929  ?  1537 LYS   A NZ  1 
ATOM   12132 N  N   . PRO   A 1 1540 ? -26.66700  38.90000  7.46700   1.000 51.13157  ?  1538 PRO   A N   1 
ATOM   12133 C  CA  . PRO   A 1 1540 ? -25.39200  38.18400  7.33400   1.000 55.49147  ?  1538 PRO   A CA  1 
ATOM   12134 C  C   . PRO   A 1 1540 ? -25.03700  37.37700  8.57400   1.000 57.84497  ?  1538 PRO   A C   1 
ATOM   12135 O  O   . PRO   A 1 1540 ? -25.46200  37.67900  9.69200   1.000 61.14356  ?  1538 PRO   A O   1 
ATOM   12136 C  CB  . PRO   A 1 1540 ? -24.37500  39.30800  7.09100   1.000 45.94693  ?  1538 PRO   A CB  1 
ATOM   12137 C  CG  . PRO   A 1 1540 ? -25.05800  40.56000  7.52400   1.000 56.32141  ?  1538 PRO   A CG  1 
ATOM   12138 C  CD  . PRO   A 1 1540 ? -26.50400  40.34200  7.23500   1.000 54.60598  ?  1538 PRO   A CD  1 
ATOM   12139 N  N   . LEU   A 1 1541 ? -24.24300  36.33800  8.35200   1.000 62.47365  ?  1539 LEU   A N   1 
ATOM   12140 C  CA  . LEU   A 1 1541 ? -23.78700  35.43200  9.39800   1.000 62.66248  ?  1539 LEU   A CA  1 
ATOM   12141 C  C   . LEU   A 1 1541 ? -22.59300  36.06100  10.11800  1.000 66.07721  ?  1539 LEU   A C   1 
ATOM   12142 O  O   . LEU   A 1 1541 ? -22.13900  37.15100  9.75700   1.000 63.73234  ?  1539 LEU   A O   1 
ATOM   12143 C  CB  . LEU   A 1 1541 ? -23.46600  34.07600  8.77200   1.000 40.76602  ?  1539 LEU   A CB  1 
ATOM   12144 C  CG  . LEU   A 1 1541 ? -24.66300  33.15800  8.51900   1.000 54.88415  ?  1539 LEU   A CG  1 
ATOM   12145 C  CD1 . LEU   A 1 1541 ? -24.33600  32.13500  7.44600   1.000 45.65984  ?  1539 LEU   A CD1 1 
ATOM   12146 C  CD2 . LEU   A 1 1541 ? -25.07000  32.46400  9.80900   1.000 52.43705  ?  1539 LEU   A CD2 1 
ATOM   12147 N  N   . PRO   A 1 1542 ? -22.08000  35.41600  11.17300  1.000 68.73346  ?  1540 PRO   A N   1 
ATOM   12148 C  CA  . PRO   A 1 1542 ? -20.89100  35.94600  11.85600  1.000 55.73533  ?  1540 PRO   A CA  1 
ATOM   12149 C  C   . PRO   A 1 1542 ? -19.73800  36.23600  10.90300  1.000 54.02110  ?  1540 PRO   A C   1 
ATOM   12150 O  O   . PRO   A 1 1542 ? -19.41000  35.43400  10.02600  1.000 53.33328  ?  1540 PRO   A O   1 
ATOM   12151 C  CB  . PRO   A 1 1542 ? -20.53500  34.83200  12.84200  1.000 57.77871  ?  1540 PRO   A CB  1 
ATOM   12152 C  CG  . PRO   A 1 1542 ? -21.84700  34.25300  13.20200  1.000 70.49029  ?  1540 PRO   A CG  1 
ATOM   12153 C  CD  . PRO   A 1 1542 ? -22.70400  34.33300  11.95900  1.000 62.30937  ?  1540 PRO   A CD  1 
ATOM   12154 N  N   . ASN   A 1 1543 ? -19.12400  37.40800  11.09600  1.000 62.26514  ?  1541 ASN   A N   1 
ATOM   12155 C  CA  . ASN   A 1 1543 ? -18.00700  37.89100  10.27500  1.000 60.59259  ?  1541 ASN   A CA  1 
ATOM   12156 C  C   . ASN   A 1 1543 ? -18.35200  37.90500  8.78800   1.000 54.33473  ?  1541 ASN   A C   1 
ATOM   12157 O  O   . ASN   A 1 1543 ? -17.47600  37.78600  7.92800   1.000 48.03046  ?  1541 ASN   A O   1 
ATOM   12158 C  CB  . ASN   A 1 1543 ? -16.73400  37.08600  10.53600  1.000 55.31601  ?  1541 ASN   A CB  1 
ATOM   12159 C  CG  . ASN   A 1 1543 ? -15.86000  37.72200  11.59700  1.000 66.73899  ?  1541 ASN   A CG  1 
ATOM   12160 O  OD1 . ASN   A 1 1543 ? -15.59700  37.12900  12.64000  1.000 72.06997  ?  1541 ASN   A OD1 1 
ATOM   12161 N  ND2 . ASN   A 1 1543 ? -15.41400  38.94700  11.33800  1.000 76.30180  ?  1541 ASN   A ND2 1 
ATOM   12162 N  N   . TYR   A 1 1544 ? -19.63600  38.05800  8.48300   1.000 52.44150  ?  1542 TYR   A N   1 
ATOM   12163 C  CA  . TYR   A 1 1544 ? -20.11500  38.31200  7.13500   1.000 50.59301  ?  1542 TYR   A CA  1 
ATOM   12164 C  C   . TYR   A 1 1544 ? -20.66500  39.73000  7.06000   1.000 46.48504  ?  1542 TYR   A C   1 
ATOM   12165 O  O   . TYR   A 1 1544 ? -21.22700  40.24600  8.03100   1.000 48.19869  ?  1542 TYR   A O   1 
ATOM   12166 C  CB  . TYR   A 1 1544 ? -21.21000  37.31900  6.73000   1.000 56.44734  ?  1542 TYR   A CB  1 
ATOM   12167 C  CG  . TYR   A 1 1544 ? -20.73100  36.01600  6.12200   1.000 51.43524  ?  1542 TYR   A CG  1 
ATOM   12168 C  CD1 . TYR   A 1 1544 ? -20.40000  35.93600  4.77500   1.000 52.45605  ?  1542 TYR   A CD1 1 
ATOM   12169 C  CD2 . TYR   A 1 1544 ? -20.64700  34.85900  6.88600   1.000 51.97425  ?  1542 TYR   A CD2 1 
ATOM   12170 C  CE1 . TYR   A 1 1544 ? -19.98000  34.74400  4.21100   1.000 50.76404  ?  1542 TYR   A CE1 1 
ATOM   12171 C  CE2 . TYR   A 1 1544 ? -20.22800  33.66300  6.33100   1.000 47.64083  ?  1542 TYR   A CE2 1 
ATOM   12172 C  CZ  . TYR   A 1 1544 ? -19.89700  33.61200  4.99400   1.000 49.27553  ?  1542 TYR   A CZ  1 
ATOM   12173 O  OH  . TYR   A 1 1544 ? -19.48400  32.42200  4.44000   1.000 44.14669  ?  1542 TYR   A OH  1 
ATOM   12174 N  N   . ARG   A 1 1545 ? -20.49800  40.36100  5.90100   1.000 40.40751  ?  1543 ARG   A N   1 
ATOM   12175 C  CA  . ARG   A 1 1545 ? -21.05700  41.68300  5.65700   1.000 36.92304  ?  1543 ARG   A CA  1 
ATOM   12176 C  C   . ARG   A 1 1545 ? -21.62000  41.72300  4.24600   1.000 45.98783  ?  1543 ARG   A C   1 
ATOM   12177 O  O   . ARG   A 1 1545 ? -20.92600  41.37000  3.28800   1.000 49.35279  ?  1543 ARG   A O   1 
ATOM   12178 C  CB  . ARG   A 1 1545 ? -20.00700  42.78400  5.85200   1.000 39.94093  ?  1543 ARG   A CB  1 
ATOM   12179 C  CG  . ARG   A 1 1545 ? -19.68600  43.07100  7.31100   1.000 43.87546  ?  1543 ARG   A CG  1 
ATOM   12180 C  CD  . ARG   A 1 1545 ? -18.63700  44.15900  7.44900   1.000 47.90941  ?  1543 ARG   A CD  1 
ATOM   12181 N  NE  . ARG   A 1 1545 ? -17.41800  43.83600  6.71800   1.000 50.69107  ?  1543 ARG   A NE  1 
ATOM   12182 C  CZ  . ARG   A 1 1545 ? -16.49100  42.99000  7.14600   1.000 47.90153  ?  1543 ARG   A CZ  1 
ATOM   12183 N  NH1 . ARG   A 1 1545 ? -16.62500  42.33700  8.29000   1.000 43.51966  ?  1543 ARG   A NH1 1 
ATOM   12184 N  NH2 . ARG   A 1 1545 ? -15.40200  42.79300  6.40800   1.000 48.72687  ?  1543 ARG   A NH2 1 
ATOM   12185 N  N   . MET   A 1 1546 ? -22.87700  42.14100  4.12400   1.000 52.70204  ?  1544 MET   A N   1 
ATOM   12186 C  CA  . MET   A 1 1546 ? -23.56900  42.17900  2.84500   1.000 59.25720  ?  1544 MET   A CA  1 
ATOM   12187 C  C   . MET   A 1 1546 ? -23.90900  43.61600  2.47600   1.000 61.26224  ?  1544 MET   A C   1 
ATOM   12188 O  O   . MET   A 1 1546 ? -24.21000  44.44300  3.34100   1.000 53.46855  ?  1544 MET   A O   1 
ATOM   12189 C  CB  . MET   A 1 1546 ? -24.84400  41.33000  2.88100   1.000 52.83239  ?  1544 MET   A CB  1 
ATOM   12190 C  CG  . MET   A 1 1546 ? -24.64800  39.97200  3.53300   1.000 58.52084  ?  1544 MET   A CG  1 
ATOM   12191 S  SD  . MET   A 1 1546 ? -25.82300  38.73300  2.96100   1.000 65.16800  ?  1544 MET   A SD  1 
ATOM   12192 C  CE  . MET   A 1 1546 ? -25.19300  38.43300  1.31400   1.000 32.85186  ?  1544 MET   A CE  1 
ATOM   12193 N  N   . TYR   A 1 1547 ? -23.85600  43.90600  1.17700   1.000 49.05869  ?  1545 TYR   A N   1 
ATOM   12194 C  CA  . TYR   A 1 1547 ? -24.13700  45.23700  0.66200   1.000 30.95340  ?  1545 TYR   A CA  1 
ATOM   12195 C  C   . TYR   A 1 1547 ? -24.98600  45.12700  -0.59400  1.000 41.35680  ?  1545 TYR   A C   1 
ATOM   12196 O  O   . TYR   A 1 1547 ? -24.74300  44.26600  -1.44300  1.000 44.99739  ?  1545 TYR   A O   1 
ATOM   12197 C  CB  . TYR   A 1 1547 ? -22.84900  46.00800  0.33800   1.000 39.41059  ?  1545 TYR   A CB  1 
ATOM   12198 C  CG  . TYR   A 1 1547 ? -21.87800  46.13700  1.49000   1.000 42.54827  ?  1545 TYR   A CG  1 
ATOM   12199 C  CD1 . TYR   A 1 1547 ? -22.15400  46.97000  2.56500   1.000 40.35329  ?  1545 TYR   A CD1 1 
ATOM   12200 C  CD2 . TYR   A 1 1547 ? -20.67700  45.44000  1.49200   1.000 44.52821  ?  1545 TYR   A CD2 1 
ATOM   12201 C  CE1 . TYR   A 1 1547 ? -21.26600  47.09600  3.61700   1.000 49.10778  ?  1545 TYR   A CE1 1 
ATOM   12202 C  CE2 . TYR   A 1 1547 ? -19.78300  45.55900  2.53800   1.000 45.90650  ?  1545 TYR   A CE2 1 
ATOM   12203 C  CZ  . TYR   A 1 1547 ? -20.08200  46.38900  3.59800   1.000 51.08195  ?  1545 TYR   A CZ  1 
ATOM   12204 O  OH  . TYR   A 1 1547 ? -19.19500  46.51200  4.64300   1.000 50.36843  ?  1545 TYR   A OH  1 
ATOM   12205 N  N   . ILE   A 1 1548 ? -25.97700  46.00600  -0.70800  1.000 45.38950  ?  1546 ILE   A N   1 
ATOM   12206 C  CA  . ILE   A 1 1548 ? -26.80600  46.12400  -1.90200  1.000 38.70538  ?  1546 ILE   A CA  1 
ATOM   12207 C  C   . ILE   A 1 1548 ? -26.46600  47.45300  -2.56200  1.000 31.02371  ?  1546 ILE   A C   1 
ATOM   12208 O  O   . ILE   A 1 1548 ? -26.66500  48.51900  -1.96700  1.000 29.09518  ?  1546 ILE   A O   1 
ATOM   12209 C  CB  . ILE   A 1 1548 ? -28.30200  46.02800  -1.56400  1.000 38.99281  ?  1546 ILE   A CB  1 
ATOM   12210 C  CG1 . ILE   A 1 1548 ? -28.66000  44.60200  -1.14100  1.000 30.50475  ?  1546 ILE   A CG1 1 
ATOM   12211 C  CG2 . ILE   A 1 1548 ? -29.15300  46.47200  -2.74300  1.000 35.87853  ?  1546 ILE   A CG2 1 
ATOM   12212 C  CD1 . ILE   A 1 1548 ? -30.01700  44.48600  -0.48700  1.000 35.47394  ?  1546 ILE   A CD1 1 
ATOM   12213 N  N   . ILE   A 1 1549 ? -25.94200  47.39200  -3.78600  1.000 38.59849  ?  1547 ILE   A N   1 
ATOM   12214 C  CA  . ILE   A 1 1549 ? -25.43300  48.57100  -4.47300  1.000 40.67402  ?  1547 ILE   A CA  1 
ATOM   12215 C  C   . ILE   A 1 1549 ? -26.20700  48.78600  -5.76700  1.000 37.33610  ?  1547 ILE   A C   1 
ATOM   12216 O  O   . ILE   A 1 1549 ? -26.90600  47.89800  -6.26300  1.000 32.38896  ?  1547 ILE   A O   1 
ATOM   12217 C  CB  . ILE   A 1 1549 ? -23.92300  48.46600  -4.76500  1.000 45.79429  ?  1547 ILE   A CB  1 
ATOM   12218 C  CG1 . ILE   A 1 1549 ? -23.65300  47.31000  -5.72900  1.000 35.21419  ?  1547 ILE   A CG1 1 
ATOM   12219 C  CG2 . ILE   A 1 1549 ? -23.14400  48.28400  -3.47200  1.000 30.77641  ?  1547 ILE   A CG2 1 
ATOM   12220 C  CD1 . ILE   A 1 1549 ? -22.30100  47.37800  -6.39700  1.000 45.19669  ?  1547 ILE   A CD1 1 
ATOM   12221 N  N   . ASN   A 1 1550 ? -26.06100  49.98700  -6.31800  1.000 45.62152  ?  1548 ASN   A N   1 
ATOM   12222 C  CA  . ASN   A 1 1550 ? -26.73800  50.38500  -7.53900  1.000 47.63835  ?  1548 ASN   A CA  1 
ATOM   12223 C  C   . ASN   A 1 1550 ? -25.78800  50.24500  -8.72800  1.000 58.01639  ?  1548 ASN   A C   1 
ATOM   12224 O  O   . ASN   A 1 1550 ? -24.68500  49.70100  -8.61500  1.000 76.67049  ?  1548 ASN   A O   1 
ATOM   12225 C  CB  . ASN   A 1 1550 ? -27.27200  51.81300  -7.40000  1.000 39.92028  ?  1548 ASN   A CB  1 
ATOM   12226 C  CG  . ASN   A 1 1550 ? -26.16500  52.85200  -7.33800  1.000 52.65626  ?  1548 ASN   A CG  1 
ATOM   12227 O  OD1 . ASN   A 1 1550 ? -25.02100  52.54200  -7.00200  1.000 58.29248  ?  1548 ASN   A OD1 1 
ATOM   12228 N  ND2 . ASN   A 1 1550 ? -26.50400  54.09500  -7.66000  1.000 33.09678  ?  1548 ASN   A ND2 1 
ATOM   12229 N  N   . ARG   A 1 1551 ? -26.21600  50.75200  -9.88600  1.000 53.16863  ?  1549 ARG   A N   1 
ATOM   12230 C  CA  . ARG   A 1 1551 ? -25.41300  50.66600  -11.09900 1.000 56.58234  ?  1549 ARG   A CA  1 
ATOM   12231 C  C   . ARG   A 1 1551 ? -24.20200  51.58800  -11.07900 1.000 54.56031  ?  1549 ARG   A C   1 
ATOM   12232 O  O   . ARG   A 1 1551 ? -23.38400  51.52500  -12.00300 1.000 57.91374  ?  1549 ARG   A O   1 
ATOM   12233 C  CB  . ARG   A 1 1551 ? -26.29100  50.97200  -12.31400 1.000 46.55487  ?  1549 ARG   A CB  1 
ATOM   12234 C  CG  . ARG   A 1 1551 ? -27.52200  51.80100  -11.98100 1.000 73.48000  ?  1549 ARG   A CG  1 
ATOM   12235 C  CD  . ARG   A 1 1551 ? -28.66200  51.52000  -12.94700 1.000 100.20546 ?  1549 ARG   A CD  1 
ATOM   12236 N  NE  . ARG   A 1 1551 ? -28.32100  51.87100  -14.32100 1.000 91.26640  ?  1549 ARG   A NE  1 
ATOM   12237 C  CZ  . ARG   A 1 1551 ? -29.13300  51.71500  -15.35700 1.000 94.98307  ?  1549 ARG   A CZ  1 
ATOM   12238 N  NH1 . ARG   A 1 1551 ? -30.34700  51.21000  -15.21400 1.000 92.02161  ?  1549 ARG   A NH1 1 
ATOM   12239 N  NH2 . ARG   A 1 1551 ? -28.71600  52.07500  -16.56800 1.000 99.56006  ?  1549 ARG   A NH2 1 
ATOM   12240 N  N   . HIS   A 1 1552 ? -24.06100  52.43200  -10.05700 1.000 48.48059  ?  1550 HIS   A N   1 
ATOM   12241 C  CA  . HIS   A 1 1552 ? -22.92200  53.33000  -9.94500  1.000 51.88119  ?  1550 HIS   A CA  1 
ATOM   12242 C  C   . HIS   A 1 1552 ? -22.07400  53.06000  -8.71000  1.000 60.07632  ?  1550 HIS   A C   1 
ATOM   12243 O  O   . HIS   A 1 1552 ? -21.12800  53.81300  -8.44900  1.000 64.57022  ?  1550 HIS   A O   1 
ATOM   12244 C  CB  . HIS   A 1 1552 ? -23.39600  54.79000  -9.94200  1.000 57.81981  ?  1550 HIS   A CB  1 
ATOM   12245 C  CG  . HIS   A 1 1552 ? -24.35900  55.11100  -11.04300 1.000 57.66873  ?  1550 HIS   A CG  1 
ATOM   12246 N  ND1 . HIS   A 1 1552 ? -23.97100  55.23700  -12.35900 1.000 62.86402  ?  1550 HIS   A ND1 1 
ATOM   12247 C  CD2 . HIS   A 1 1552 ? -25.69600  55.32500  -11.02300 1.000 54.37635  ?  1550 HIS   A CD2 1 
ATOM   12248 C  CE1 . HIS   A 1 1552 ? -25.02700  55.51700  -13.10300 1.000 64.86134  ?  1550 HIS   A CE1 1 
ATOM   12249 N  NE2 . HIS   A 1 1552 ? -26.08600  55.57600  -12.31600 1.000 57.90315  ?  1550 HIS   A NE2 1 
ATOM   12250 N  N   . GLY   A 1 1553 ? -22.38300  52.01600  -7.94500  1.000 51.07023  ?  1551 GLY   A N   1 
ATOM   12251 C  CA  . GLY   A 1 1553 ? -21.56700  51.62000  -6.81800  1.000 54.08805  ?  1551 GLY   A CA  1 
ATOM   12252 C  C   . GLY   A 1 1553 ? -21.96700  52.19900  -5.48100  1.000 60.52652  ?  1551 GLY   A C   1 
ATOM   12253 O  O   . GLY   A 1 1553 ? -21.17600  52.12200  -4.53300  1.000 59.47443  ?  1551 GLY   A O   1 
ATOM   12254 N  N   . GLN   A 1 1554 ? -23.16200  52.76800  -5.36700  1.000 58.07476  ?  1552 GLN   A N   1 
ATOM   12255 C  CA  . GLN   A 1 1554 ? -23.61600  53.38900  -4.13200  1.000 50.01204  ?  1552 GLN   A CA  1 
ATOM   12256 C  C   . GLN   A 1 1554 ? -24.54100  52.44800  -3.37200  1.000 45.36249  ?  1552 GLN   A C   1 
ATOM   12257 O  O   . GLN   A 1 1554 ? -25.31000  51.68900  -3.96600  1.000 54.70170  ?  1552 GLN   A O   1 
ATOM   12258 C  CB  . GLN   A 1 1554 ? -24.33700  54.70700  -4.42200  1.000 44.20647  ?  1552 GLN   A CB  1 
ATOM   12259 C  CG  . GLN   A 1 1554 ? -23.52700  55.67300  -5.26500  1.000 50.07358  ?  1552 GLN   A CG  1 
ATOM   12260 C  CD  . GLN   A 1 1554 ? -24.25800  56.97100  -5.53100  1.000 47.75148  ?  1552 GLN   A CD  1 
ATOM   12261 O  OE1 . GLN   A 1 1554 ? -25.48500  57.03500  -5.44800  1.000 52.54699  ?  1552 GLN   A OE1 1 
ATOM   12262 N  NE2 . GLN   A 1 1554 ? -23.50600  58.01800  -5.84800  1.000 60.89331  ?  1552 GLN   A NE2 1 
ATOM   12263 N  N   . LEU   A 1 1555 ? -24.45800  52.50800  -2.04500  1.000 40.25274  ?  1553 LEU   A N   1 
ATOM   12264 C  CA  . LEU   A 1 1555 ? -25.30800  51.67600  -1.20300  1.000 44.41469  ?  1553 LEU   A CA  1 
ATOM   12265 C  C   . LEU   A 1 1555 ? -26.76900  52.07700  -1.37100  1.000 41.94805  ?  1553 LEU   A C   1 
ATOM   12266 O  O   . LEU   A 1 1555 ? -27.11700  53.25700  -1.26100  1.000 46.89374  ?  1553 LEU   A O   1 
ATOM   12267 C  CB  . LEU   A 1 1555 ? -24.88500  51.80000  0.26000   1.000 49.87205  ?  1553 LEU   A CB  1 
ATOM   12268 C  CG  . LEU   A 1 1555 ? -25.52000  50.81100  1.23900   1.000 60.03191  ?  1553 LEU   A CG  1 
ATOM   12269 C  CD1 . LEU   A 1 1555 ? -25.14300  49.38300  0.87400   1.000 55.99029  ?  1553 LEU   A CD1 1 
ATOM   12270 C  CD2 . LEU   A 1 1555 ? -25.11100  51.12900  2.67000   1.000 57.05528  ?  1553 LEU   A CD2 1 
ATOM   12271 N  N   . GLN   A 1 1556 ? -27.62300  51.09300  -1.64600  1.000 44.14049  ?  1554 GLN   A N   1 
ATOM   12272 C  CA  . GLN   A 1 1556 ? -29.04000  51.37400  -1.82800  1.000 46.37176  ?  1554 GLN   A CA  1 
ATOM   12273 C  C   . GLN   A 1 1556 ? -29.74400  51.44700  -0.47400  1.000 52.02655  ?  1554 GLN   A C   1 
ATOM   12274 O  O   . GLN   A 1 1556 ? -29.41900  50.68100  0.43700   1.000 50.10891  ?  1554 GLN   A O   1 
ATOM   12275 C  CB  . GLN   A 1 1556 ? -29.69900  50.30100  -2.69500  1.000 39.67752  ?  1554 GLN   A CB  1 
ATOM   12276 C  CG  . GLN   A 1 1556 ? -29.21000  50.25900  -4.13600  1.000 53.65404  ?  1554 GLN   A CG  1 
ATOM   12277 C  CD  . GLN   A 1 1556 ? -29.82800  51.34000  -5.00600  1.000 52.94217  ?  1554 GLN   A CD  1 
ATOM   12278 O  OE1 . GLN   A 1 1556 ? -29.81100  52.52200  -4.66100  1.000 60.93629  ?  1554 GLN   A OE1 1 
ATOM   12279 N  NE2 . GLN   A 1 1556 ? -30.38000  50.93400  -6.14400  1.000 58.34586  ?  1554 GLN   A NE2 1 
ATOM   12280 N  N   . PRO   A 1 1557 ? -30.70100  52.35200  -0.31600  1.000 56.06866  ?  1555 PRO   A N   1 
ATOM   12281 C  CA  . PRO   A 1 1557 ? -31.45200  52.44600  0.93900   1.000 51.64198  ?  1555 PRO   A CA  1 
ATOM   12282 C  C   . PRO   A 1 1557 ? -32.46400  51.30900  1.05400   1.000 45.52048  ?  1555 PRO   A C   1 
ATOM   12283 O  O   . PRO   A 1 1557 ? -32.58900  50.45800  0.17500   1.000 50.40427  ?  1555 PRO   A O   1 
ATOM   12284 C  CB  . PRO   A 1 1557 ? -32.13800  53.80900  0.83100   1.000 52.20732  ?  1555 PRO   A CB  1 
ATOM   12285 C  CG  . PRO   A 1 1557 ? -32.29700  54.02300  -0.63300  1.000 40.64579  ?  1555 PRO   A CG  1 
ATOM   12286 C  CD  . PRO   A 1 1557 ? -31.09200  53.39800  -1.27700  1.000 50.10589  ?  1555 PRO   A CD  1 
ATOM   12287 N  N   . ILE   A 1 1558 ? -33.19300  51.31200  2.17300   1.000 37.71892  ?  1556 ILE   A N   1 
ATOM   12288 C  CA  . ILE   A 1 1558 ? -34.19100  50.27800  2.42300   1.000 43.89955  ?  1556 ILE   A CA  1 
ATOM   12289 C  C   . ILE   A 1 1558 ? -35.28100  50.34500  1.36500   1.000 39.32621  ?  1556 ILE   A C   1 
ATOM   12290 O  O   . ILE   A 1 1558 ? -35.77700  51.42600  1.02300   1.000 52.93924  ?  1556 ILE   A O   1 
ATOM   12291 C  CB  . ILE   A 1 1558 ? -34.77500  50.43400  3.83500   1.000 49.65537  ?  1556 ILE   A CB  1 
ATOM   12292 C  CG1 . ILE   A 1 1558 ? -33.69200  50.20200  4.89000   1.000 44.51670  ?  1556 ILE   A CG1 1 
ATOM   12293 C  CG2 . ILE   A 1 1558 ? -35.94300  49.48200  4.04600   1.000 43.82897  ?  1556 ILE   A CG2 1 
ATOM   12294 C  CD1 . ILE   A 1 1558 ? -34.19100  50.33200  6.30800   1.000 45.37564  ?  1556 ILE   A CD1 1 
ATOM   12295 N  N   . GLY   A 1 1559 ? -35.65800  49.18100  0.83500   1.000 32.93326  ?  1557 GLY   A N   1 
ATOM   12296 C  CA  . GLY   A 1 1559 ? -36.71200  49.06700  -0.14700  1.000 34.49225  ?  1557 GLY   A CA  1 
ATOM   12297 C  C   . GLY   A 1 1559 ? -36.26200  49.21600  -1.58600  1.000 37.24845  ?  1557 GLY   A C   1 
ATOM   12298 O  O   . GLY   A 1 1559 ? -36.88700  48.63900  -2.48300  1.000 34.57368  ?  1557 GLY   A O   1 
ATOM   12299 N  N   . VAL   A 1 1560 ? -35.20000  49.97100  -1.83000  1.000 40.87129  ?  1558 VAL   A N   1 
ATOM   12300 C  CA  . VAL   A 1 1560 ? -34.71700  50.18300  -3.19600  1.000 39.33485  ?  1558 VAL   A CA  1 
ATOM   12301 C  C   . VAL   A 1 1560 ? -33.88300  48.97600  -3.61600  1.000 51.55279  ?  1558 VAL   A C   1 
ATOM   12302 O  O   . VAL   A 1 1560 ? -32.96900  48.57700  -2.87600  1.000 47.71224  ?  1558 VAL   A O   1 
ATOM   12303 C  CB  . VAL   A 1 1560 ? -33.90700  51.47300  -3.28400  1.000 36.23245  ?  1558 VAL   A CB  1 
ATOM   12304 C  CG1 . VAL   A 1 1560 ? -33.35000  51.65700  -4.68600  1.000 43.35017  ?  1558 VAL   A CG1 1 
ATOM   12305 C  CG2 . VAL   A 1 1560 ? -34.77300  52.66200  -2.89800  1.000 43.90272  ?  1558 VAL   A CG2 1 
ATOM   12306 N  N   . PRO   A 1 1561 ? -34.16000  48.37400  -4.76900  1.000 53.04341  ?  1559 PRO   A N   1 
ATOM   12307 C  CA  . PRO   A 1 1561 ? -33.43500  47.16700  -5.17100  1.000 44.27018  ?  1559 PRO   A CA  1 
ATOM   12308 C  C   . PRO   A 1 1561 ? -32.06500  47.48000  -5.75600  1.000 45.12328  ?  1559 PRO   A C   1 
ATOM   12309 O  O   . PRO   A 1 1561 ? -31.79300  48.57600  -6.24900  1.000 36.29499  ?  1559 PRO   A O   1 
ATOM   12310 C  CB  . PRO   A 1 1561 ? -34.35100  46.54600  -6.23000  1.000 38.06011  ?  1559 PRO   A CB  1 
ATOM   12311 C  CG  . PRO   A 1 1561 ? -35.04400  47.71500  -6.83300  1.000 49.13953  ?  1559 PRO   A CG  1 
ATOM   12312 C  CD  . PRO   A 1 1561 ? -35.23400  48.71500  -5.71800  1.000 53.90544  ?  1559 PRO   A CD  1 
ATOM   12313 N  N   . GLY   A 1 1562 ? -31.20300  46.47400  -5.69400  1.000 53.18003  ?  1560 GLY   A N   1 
ATOM   12314 C  CA  . GLY   A 1 1562 ? -29.86800  46.58900  -6.23800  1.000 38.06060  ?  1560 GLY   A CA  1 
ATOM   12315 C  C   . GLY   A 1 1562 ? -29.19500  45.23600  -6.26700  1.000 36.90762  ?  1560 GLY   A C   1 
ATOM   12316 O  O   . GLY   A 1 1562 ? -29.82500  44.20400  -6.03100  1.000 50.98474  ?  1560 GLY   A O   1 
ATOM   12317 N  N   . GLU   A 1 1563 ? -27.89700  45.25200  -6.55900  1.000 37.89969  ?  1561 GLU   A N   1 
ATOM   12318 C  CA  . GLU   A 1 1563 ? -27.11200  44.02500  -6.63800  1.000 44.20594  ?  1561 GLU   A CA  1 
ATOM   12319 C  C   . GLU   A 1 1563 ? -26.54700  43.69000  -5.26400  1.000 46.29884  ?  1561 GLU   A C   1 
ATOM   12320 O  O   . GLU   A 1 1563 ? -25.86000  44.51400  -4.65100  1.000 45.37332  ?  1561 GLU   A O   1 
ATOM   12321 C  CB  . GLU   A 1 1563 ? -25.98000  44.15500  -7.65600  1.000 51.59464  ?  1561 GLU   A CB  1 
ATOM   12322 C  CG  . GLU   A 1 1563 ? -25.15000  42.88200  -7.80600  1.000 54.38143  ?  1561 GLU   A CG  1 
ATOM   12323 C  CD  . GLU   A 1 1563 ? -24.05000  43.01000  -8.84300  1.000 59.76692  ?  1561 GLU   A CD  1 
ATOM   12324 O  OE1 . GLU   A 1 1563 ? -23.68700  44.15400  -9.18600  1.000 70.87954  ?  1561 GLU   A OE1 1 
ATOM   12325 O  OE2 . GLU   A 1 1563 ? -23.55100  41.96700  -9.31800  1.000 54.79122  -1 1561 GLU   A OE2 1 
ATOM   12326 N  N   . LEU   A 1 1564 ? -26.82900  42.48100  -4.79000  1.000 47.22906  ?  1562 LEU   A N   1 
ATOM   12327 C  CA  . LEU   A 1 1564 ? -26.27300  42.03100  -3.52400  1.000 41.57151  ?  1562 LEU   A CA  1 
ATOM   12328 C  C   . LEU   A 1 1564 ? -24.78300  41.75800  -3.67300  1.000 43.73946  ?  1562 LEU   A C   1 
ATOM   12329 O  O   . LEU   A 1 1564 ? -24.33200  41.20900  -4.68200  1.000 47.38341  ?  1562 LEU   A O   1 
ATOM   12330 C  CB  . LEU   A 1 1564 ? -27.00300  40.77800  -3.03900  1.000 31.34873  ?  1562 LEU   A CB  1 
ATOM   12331 C  CG  . LEU   A 1 1564 ? -26.69700  40.30300  -1.61900  1.000 33.80014  ?  1562 LEU   A CG  1 
ATOM   12332 C  CD1 . LEU   A 1 1564 ? -26.75100  41.46300  -0.63500  1.000 39.13213  ?  1562 LEU   A CD1 1 
ATOM   12333 C  CD2 . LEU   A 1 1564 ? -27.67300  39.20800  -1.21400  1.000 22.93727  ?  1562 LEU   A CD2 1 
ATOM   12334 N  N   . CYS   A 1 1565 ? -24.01400  42.16400  -2.66600  1.000 40.65207  ?  1563 CYS   A N   1 
ATOM   12335 C  CA  . CYS   A 1 1565 ? -22.57300  41.96800  -2.65800  1.000 38.28235  ?  1563 CYS   A CA  1 
ATOM   12336 C  C   . CYS   A 1 1565 ? -22.14900  41.47000  -1.28700  1.000 51.08509  ?  1563 CYS   A C   1 
ATOM   12337 O  O   . CYS   A 1 1565 ? -22.73800  41.83800  -0.26800  1.000 51.77502  ?  1563 CYS   A O   1 
ATOM   12338 C  CB  . CYS   A 1 1565 ? -21.82700  43.26200  -3.01600  1.000 41.79433  ?  1563 CYS   A CB  1 
ATOM   12339 S  SG  . CYS   A 1 1565 ? -22.24300  43.92600  -4.64600  1.000 44.16005  ?  1563 CYS   A SG  1 
ATOM   12340 N  N   . ILE   A 1 1566 ? -21.12000  40.62400  -1.26900  1.000 46.91574  ?  1564 ILE   A N   1 
ATOM   12341 C  CA  . ILE   A 1 1566 ? -20.68200  39.96400  -0.04700  1.000 44.39094  ?  1564 ILE   A CA  1 
ATOM   12342 C  C   . ILE   A 1 1566 ? -19.27700  40.42600  0.30100   1.000 42.66521  ?  1564 ILE   A C   1 
ATOM   12343 O  O   . ILE   A 1 1566 ? -18.47200  40.76100  -0.57300  1.000 45.84402  ?  1564 ILE   A O   1 
ATOM   12344 C  CB  . ILE   A 1 1566 ? -20.71900  38.42700  -0.17300  1.000 45.37054  ?  1564 ILE   A CB  1 
ATOM   12345 C  CG1 . ILE   A 1 1566 ? -21.64400  38.00900  -1.31700  1.000 46.19627  ?  1564 ILE   A CG1 1 
ATOM   12346 C  CG2 . ILE   A 1 1566 ? -21.13100  37.80500  1.15700   1.000 41.55368  ?  1564 ILE   A CG2 1 
ATOM   12347 C  CD1 . ILE   A 1 1566 ? -22.78200  37.11500  -0.89100  1.000 44.53220  ?  1564 ILE   A CD1 1 
ATOM   12348 N  N   . ALA   A 1 1567 ? -18.98700  40.42500  1.59900   1.000 39.43149  ?  1565 ALA   A N   1 
ATOM   12349 C  CA  . ALA   A 1 1567 ? -17.67600  40.78700  2.10800   1.000 49.17237  ?  1565 ALA   A CA  1 
ATOM   12350 C  C   . ALA   A 1 1567 ? -17.48500  40.12900  3.46600   1.000 52.09923  ?  1565 ALA   A C   1 
ATOM   12351 O  O   . ALA   A 1 1567 ? -18.45100  39.88100  4.19100   1.000 57.47042  ?  1565 ALA   A O   1 
ATOM   12352 C  CB  . ALA   A 1 1567 ? -17.51600  42.30600  2.22400   1.000 44.97060  ?  1565 ALA   A CB  1 
ATOM   12353 N  N   . GLY   A 1 1568 ? -16.23500  39.83700  3.79900   1.000 44.99153  ?  1566 GLY   A N   1 
ATOM   12354 C  CA  . GLY   A 1 1568 ? -15.89600  39.28400  5.08900   1.000 48.51519  ?  1566 GLY   A CA  1 
ATOM   12355 C  C   . GLY   A 1 1568 ? -14.76300  38.28600  4.97900   1.000 67.65242  ?  1566 GLY   A C   1 
ATOM   12356 O  O   . GLY   A 1 1568 ? -14.04800  38.22300  3.97800   1.000 37.44162  ?  1566 GLY   A O   1 
ATOM   12357 N  N   . ALA   A 1 1569 ? -14.61400  37.48800  6.04000   1.000 53.22909  ?  1567 ALA   A N   1 
ATOM   12358 C  CA  . ALA   A 1 1569 ? -13.50900  36.53700  6.12800   1.000 48.13980  ?  1567 ALA   A CA  1 
ATOM   12359 C  C   . ALA   A 1 1569 ? -13.73300  35.31700  5.23800   1.000 49.36792  ?  1567 ALA   A C   1 
ATOM   12360 O  O   . ALA   A 1 1569 ? -12.78900  34.82900  4.60600   1.000 73.63878  ?  1567 ALA   A O   1 
ATOM   12361 C  CB  . ALA   A 1 1569 ? -13.30500  36.11300  7.58400   1.000 62.07207  ?  1567 ALA   A CB  1 
ATOM   12362 N  N   . SER   A 1 1570 ? -14.96900  34.81900  5.16100   1.000 56.12145  ?  1568 SER   A N   1 
ATOM   12363 C  CA  . SER   A 1 1570 ? -15.29200  33.62500  4.38100   1.000 48.82380  ?  1568 SER   A CA  1 
ATOM   12364 C  C   . SER   A 1 1570 ? -15.47800  33.92100  2.89500   1.000 47.39574  ?  1568 SER   A C   1 
ATOM   12365 O  O   . SER   A 1 1570 ? -16.28100  33.27300  2.21900   1.000 57.71908  ?  1568 SER   A O   1 
ATOM   12366 C  CB  . SER   A 1 1570 ? -16.53600  32.96900  4.96500   1.000 35.66862  ?  1568 SER   A CB  1 
ATOM   12367 O  OG  . SER   A 1 1570 ? -16.71600  33.37200  6.31300   1.000 56.17809  ?  1568 SER   A OG  1 
ATOM   12368 N  N   . LEU   A 1 1571 ? -14.74000  34.88600  2.35200   1.000 33.31502  ?  1569 LEU   A N   1 
ATOM   12369 C  CA  . LEU   A 1 1571 ? -14.78300  35.17800  0.92400   1.000 39.31053  ?  1569 LEU   A CA  1 
ATOM   12370 C  C   . LEU   A 1 1571 ? -13.74800  34.33600  0.18800   1.000 47.26084  ?  1569 LEU   A C   1 
ATOM   12371 O  O   . LEU   A 1 1571 ? -12.68900  34.00700  0.72700   1.000 53.43321  ?  1569 LEU   A O   1 
ATOM   12372 C  CB  . LEU   A 1 1571 ? -14.53300  36.66400  0.66800   1.000 49.22087  ?  1569 LEU   A CB  1 
ATOM   12373 C  CG  . LEU   A 1 1571 ? -15.38200  37.32400  -0.42200  1.000 47.36033  ?  1569 LEU   A CG  1 
ATOM   12374 C  CD1 . LEU   A 1 1571 ? -16.84700  37.38500  -0.00600  1.000 43.36516  ?  1569 LEU   A CD1 1 
ATOM   12375 C  CD2 . LEU   A 1 1571 ? -14.85200  38.71100  -0.74300  1.000 54.52650  ?  1569 LEU   A CD2 1 
ATOM   12376 N  N   . ALA   A 1 1572 ? -14.06400  33.99400  -1.05700  1.000 47.72278  ?  1570 ALA   A N   1 
ATOM   12377 C  CA  . ALA   A 1 1572 ? -13.19700  33.11400  -1.82800  1.000 44.23724  ?  1570 ALA   A CA  1 
ATOM   12378 C  C   . ALA   A 1 1572 ? -11.93500  33.84400  -2.27100  1.000 58.73802  ?  1570 ALA   A C   1 
ATOM   12379 O  O   . ALA   A 1 1572 ? -11.91700  35.06800  -2.42600  1.000 66.31140  ?  1570 ALA   A O   1 
ATOM   12380 C  CB  . ALA   A 1 1572 ? -13.93700  32.56200  -3.04700  1.000 42.07529  ?  1570 ALA   A CB  1 
ATOM   12381 N  N   . ARG   A 1 1573 ? -10.86400  33.07100  -2.46900  1.000 66.32354  ?  1571 ARG   A N   1 
ATOM   12382 C  CA  . ARG   A 1 1573 ? -9.61100   33.65500  -2.92900  1.000 52.41739  ?  1571 ARG   A CA  1 
ATOM   12383 C  C   . ARG   A 1 1573 ? -9.70700   34.10600  -4.38200  1.000 47.57728  ?  1571 ARG   A C   1 
ATOM   12384 O  O   . ARG   A 1 1573 ? -9.01000   35.04400  -4.78500  1.000 57.46913  ?  1571 ARG   A O   1 
ATOM   12385 C  CB  . ARG   A 1 1573 ? -8.46900   32.65400  -2.75100  1.000 56.52799  ?  1571 ARG   A CB  1 
ATOM   12386 C  CG  . ARG   A 1 1573 ? -7.10200   33.29500  -2.57900  1.000 70.09939  ?  1571 ARG   A CG  1 
ATOM   12387 C  CD  . ARG   A 1 1573 ? -5.98600   32.30600  -2.87600  1.000 59.08003  ?  1571 ARG   A CD  1 
ATOM   12388 N  NE  . ARG   A 1 1573 ? -5.41300   31.71900  -1.67100  1.000 58.20700  ?  1571 ARG   A NE  1 
ATOM   12389 C  CZ  . ARG   A 1 1573 ? -4.50000   30.75800  -1.67400  1.000 52.05227  ?  1571 ARG   A CZ  1 
ATOM   12390 N  NH1 . ARG   A 1 1573 ? -4.05400   30.23400  -2.80500  1.000 36.87185  ?  1571 ARG   A NH1 1 
ATOM   12391 N  NH2 . ARG   A 1 1573 ? -4.02400   30.31000  -0.51500  1.000 42.93406  ?  1571 ARG   A NH2 1 
ATOM   12392 N  N   . GLY   A 1 1574 ? -10.55500  33.46700  -5.16900  1.000 45.24760  ?  1572 GLY   A N   1 
ATOM   12393 C  CA  . GLY   A 1 1574 ? -10.75200  33.85900  -6.55100  1.000 38.76543  ?  1572 GLY   A CA  1 
ATOM   12394 C  C   . GLY   A 1 1574 ? -11.01700  32.64600  -7.42100  1.000 47.83712  ?  1572 GLY   A C   1 
ATOM   12395 O  O   . GLY   A 1 1574 ? -11.02000  31.50800  -6.96100  1.000 49.29829  ?  1572 GLY   A O   1 
ATOM   12396 N  N   . TYR   A 1 1575 ? -11.24500  32.92300  -8.70300  1.000 48.86377  ?  1573 TYR   A N   1 
ATOM   12397 C  CA  . TYR   A 1 1575 ? -11.46000  31.86700  -9.68100  1.000 44.62793  ?  1573 TYR   A CA  1 
ATOM   12398 C  C   . TYR   A 1 1575 ? -10.12700  31.31200  -10.16500 1.000 67.59930  ?  1573 TYR   A C   1 
ATOM   12399 O  O   . TYR   A 1 1575 ? -9.16500   32.05800  -10.37300 1.000 65.42165  ?  1573 TYR   A O   1 
ATOM   12400 C  CB  . TYR   A 1 1575 ? -12.27400  32.38500  -10.86700 1.000 51.43437  ?  1573 TYR   A CB  1 
ATOM   12401 C  CG  . TYR   A 1 1575 ? -13.65500  32.88000  -10.49800 1.000 59.08364  ?  1573 TYR   A CG  1 
ATOM   12402 C  CD1 . TYR   A 1 1575 ? -14.70000  31.99000  -10.28500 1.000 63.78035  ?  1573 TYR   A CD1 1 
ATOM   12403 C  CD2 . TYR   A 1 1575 ? -13.91500  34.23800  -10.37000 1.000 63.23031  ?  1573 TYR   A CD2 1 
ATOM   12404 C  CE1 . TYR   A 1 1575 ? -15.96400  32.43900  -9.94800  1.000 60.57598  ?  1573 TYR   A CE1 1 
ATOM   12405 C  CE2 . TYR   A 1 1575 ? -15.17600  34.69700  -10.03400 1.000 58.90456  ?  1573 TYR   A CE2 1 
ATOM   12406 C  CZ  . TYR   A 1 1575 ? -16.19600  33.79300  -9.82500  1.000 61.73539  ?  1573 TYR   A CZ  1 
ATOM   12407 O  OH  . TYR   A 1 1575 ? -17.45200  34.24400  -9.49100  1.000 55.49540  ?  1573 TYR   A OH  1 
ATOM   12408 N  N   . LEU   A 1 1576 ? -10.07600  29.99500  -10.34700 1.000 73.15825  ?  1574 LEU   A N   1 
ATOM   12409 C  CA  . LEU   A 1 1576 ? -8.84700   29.32500  -10.74700 1.000 57.03167  ?  1574 LEU   A CA  1 
ATOM   12410 C  C   . LEU   A 1 1576 ? -8.56700   29.56500  -12.22600 1.000 75.98102  ?  1574 LEU   A C   1 
ATOM   12411 O  O   . LEU   A 1 1576 ? -9.42800   29.31800  -13.07700 1.000 75.60711  ?  1574 LEU   A O   1 
ATOM   12412 C  CB  . LEU   A 1 1576 ? -8.94500   27.82700  -10.46100 1.000 63.05341  ?  1574 LEU   A CB  1 
ATOM   12413 C  CG  . LEU   A 1 1576 ? -7.70100   26.98400  -10.74400 1.000 71.79880  ?  1574 LEU   A CG  1 
ATOM   12414 C  CD1 . LEU   A 1 1576 ? -6.58800   27.31100  -9.76100  1.000 72.54829  ?  1574 LEU   A CD1 1 
ATOM   12415 C  CD2 . LEU   A 1 1576 ? -8.04200   25.50500  -10.70100 1.000 65.29539  ?  1574 LEU   A CD2 1 
ATOM   12416 N  N   . ASN   A 1 1577 ? -7.35800   30.04800  -12.52400 1.000 70.99128  ?  1575 ASN   A N   1 
ATOM   12417 C  CA  . ASN   A 1 1577 ? -6.91600   30.30600  -13.89700 1.000 70.27358  ?  1575 ASN   A CA  1 
ATOM   12418 C  C   . ASN   A 1 1577 ? -7.85900   31.26500  -14.61900 1.000 84.39397  ?  1575 ASN   A C   1 
ATOM   12419 O  O   . ASN   A 1 1577 ? -8.10700   31.13600  -15.81900 1.000 92.45398  ?  1575 ASN   A O   1 
ATOM   12420 C  CB  . ASN   A 1 1577 ? -6.76100   29.00300  -14.68500 1.000 80.08121  ?  1575 ASN   A CB  1 
ATOM   12421 C  CG  . ASN   A 1 1577 ? -5.64700   28.12700  -14.15100 1.000 77.45624  ?  1575 ASN   A CG  1 
ATOM   12422 O  OD1 . ASN   A 1 1577 ? -5.17000   28.32000  -13.03200 1.000 82.14161  ?  1575 ASN   A OD1 1 
ATOM   12423 N  ND2 . ASN   A 1 1577 ? -5.22700   27.15300  -14.95000 1.000 72.88807  ?  1575 ASN   A ND2 1 
ATOM   12424 N  N   . ASN   A 1 1578 ? -8.39300   32.23900  -13.88000 1.000 79.70274  ?  1576 ASN   A N   1 
ATOM   12425 C  CA  . ASN   A 1 1578 ? -9.27700   33.25700  -14.45000 1.000 74.20668  ?  1576 ASN   A CA  1 
ATOM   12426 C  C   . ASN   A 1 1578 ? -9.15100   34.53600  -13.63200 1.000 80.45299  ?  1576 ASN   A C   1 
ATOM   12427 O  O   . ASN   A 1 1578 ? -10.04500  34.89200  -12.85600 1.000 76.55916  ?  1576 ASN   A O   1 
ATOM   12428 C  CB  . ASN   A 1 1578 ? -10.72200  32.76100  -14.48700 1.000 54.47451  ?  1576 ASN   A CB  1 
ATOM   12429 C  CG  . ASN   A 1 1578 ? -11.51500  33.36000  -15.63200 1.000 73.61205  ?  1576 ASN   A CG  1 
ATOM   12430 O  OD1 . ASN   A 1 1578 ? -11.21900  34.45900  -16.10200 1.000 77.62289  ?  1576 ASN   A OD1 1 
ATOM   12431 N  ND2 . ASN   A 1 1578 ? -12.52900  32.63500  -16.09200 1.000 70.97656  ?  1576 ASN   A ND2 1 
ATOM   12432 N  N   . PRO   A 1 1579 ? -8.03400   35.25600  -13.78000 1.000 84.70211  ?  1577 PRO   A N   1 
ATOM   12433 C  CA  . PRO   A 1 1579 ? -7.89100   36.52400  -13.04800 1.000 68.15658  ?  1577 PRO   A CA  1 
ATOM   12434 C  C   . PRO   A 1 1579 ? -8.81100   37.61400  -13.56600 1.000 59.59063  ?  1577 PRO   A C   1 
ATOM   12435 O  O   . PRO   A 1 1579 ? -9.16000   38.52600  -12.80600 1.000 59.63368  ?  1577 PRO   A O   1 
ATOM   12436 C  CB  . PRO   A 1 1579 ? -6.41300   36.89100  -13.25300 1.000 59.33540  ?  1577 PRO   A CB  1 
ATOM   12437 C  CG  . PRO   A 1 1579 ? -5.75700   35.64100  -13.77800 1.000 66.09375  ?  1577 PRO   A CG  1 
ATOM   12438 C  CD  . PRO   A 1 1579 ? -6.82100   34.93000  -14.54600 1.000 69.97767  ?  1577 PRO   A CD  1 
ATOM   12439 N  N   . ALA   A 1 1580 ? -9.20900   37.55100  -14.83800 1.000 63.24468  ?  1578 ALA   A N   1 
ATOM   12440 C  CA  . ALA   A 1 1580 ? -10.13300  38.54200  -15.38000 1.000 69.22253  ?  1578 ALA   A CA  1 
ATOM   12441 C  C   . ALA   A 1 1580 ? -11.48800  38.45700  -14.69000 1.000 75.94655  ?  1578 ALA   A C   1 
ATOM   12442 O  O   . ALA   A 1 1580 ? -12.05500  39.47500  -14.27700 1.000 85.89348  ?  1578 ALA   A O   1 
ATOM   12443 C  CB  . ALA   A 1 1580 ? -10.28100  38.35100  -16.89000 1.000 58.48328  ?  1578 ALA   A CB  1 
ATOM   12444 N  N   . LEU   A 1 1581 ? -12.02600  37.24200  -14.55800 1.000 68.02578  ?  1579 LEU   A N   1 
ATOM   12445 C  CA  . LEU   A 1 1581 ? -13.28200  37.07000  -13.83900 1.000 65.06748  ?  1579 LEU   A CA  1 
ATOM   12446 C  C   . LEU   A 1 1581 ? -13.11000  37.34200  -12.35100 1.000 71.99855  ?  1579 LEU   A C   1 
ATOM   12447 O  O   . LEU   A 1 1581 ? -14.04100  37.82900  -11.69900 1.000 89.31941  ?  1579 LEU   A O   1 
ATOM   12448 C  CB  . LEU   A 1 1581 ? -13.82900  35.66100  -14.06600 1.000 57.60684  ?  1579 LEU   A CB  1 
ATOM   12449 C  CG  . LEU   A 1 1581 ? -15.32200  35.47400  -13.80400 1.000 51.98458  ?  1579 LEU   A CG  1 
ATOM   12450 C  CD1 . LEU   A 1 1581 ? -16.13800  36.35900  -14.73600 1.000 55.59934  ?  1579 LEU   A CD1 1 
ATOM   12451 C  CD2 . LEU   A 1 1581 ? -15.71200  34.01400  -13.96600 1.000 71.06287  ?  1579 LEU   A CD2 1 
ATOM   12452 N  N   . THR   A 1 1582 ? -11.93200  37.03900  -11.80000 1.000 59.14934  ?  1580 THR   A N   1 
ATOM   12453 C  CA  . THR   A 1 1582 ? -11.67000  37.34900  -10.39900 1.000 66.47030  ?  1580 THR   A CA  1 
ATOM   12454 C  C   . THR   A 1 1582 ? -11.65200  38.85500  -10.16700 1.000 73.87876  ?  1580 THR   A C   1 
ATOM   12455 O  O   . THR   A 1 1582 ? -12.11800  39.33400  -9.12600  1.000 73.40679  ?  1580 THR   A O   1 
ATOM   12456 C  CB  . THR   A 1 1582 ? -10.35000  36.71700  -9.95900  1.000 56.14198  ?  1580 THR   A CB  1 
ATOM   12457 O  OG1 . THR   A 1 1582 ? -10.38000  35.31100  -10.23300 1.000 57.53009  ?  1580 THR   A OG1 1 
ATOM   12458 C  CG2 . THR   A 1 1582 ? -10.12300  36.93100  -8.46900  1.000 46.32126  ?  1580 THR   A CG2 1 
ATOM   12459 N  N   . GLU   A 1 1583 ? -11.12800  39.62000  -11.12700 1.000 78.23334  ?  1581 GLU   A N   1 
ATOM   12460 C  CA  . GLU   A 1 1583 ? -11.14700  41.07400  -11.02100 1.000 71.69878  ?  1581 GLU   A CA  1 
ATOM   12461 C  C   . GLU   A 1 1583 ? -12.51400  41.67000  -11.32500 1.000 66.96815  ?  1581 GLU   A C   1 
ATOM   12462 O  O   . GLU   A 1 1583 ? -12.79400  42.79200  -10.89000 1.000 68.51739  ?  1581 GLU   A O   1 
ATOM   12463 C  CB  . GLU   A 1 1583 ? -10.10600  41.69300  -11.95700 1.000 77.40490  ?  1581 GLU   A CB  1 
ATOM   12464 C  CG  . GLU   A 1 1583 ? -8.75800   41.96500  -11.30700 1.000 83.28393  ?  1581 GLU   A CG  1 
ATOM   12465 C  CD  . GLU   A 1 1583 ? -7.93700   42.98000  -12.08100 1.000 108.85938 ?  1581 GLU   A CD  1 
ATOM   12466 O  OE1 . GLU   A 1 1583 ? -8.52100   43.70900  -12.91100 1.000 95.56115  ?  1581 GLU   A OE1 1 
ATOM   12467 O  OE2 . GLU   A 1 1583 ? -6.70900   43.04900  -11.86100 1.000 113.98995 -1 1581 GLU   A OE2 1 
ATOM   12468 N  N   . GLU   A 1 1584 ? -13.36800  40.95600  -12.06300 1.000 65.21902  ?  1582 GLU   A N   1 
ATOM   12469 C  CA  . GLU   A 1 1584 ? -14.69600  41.48000  -12.36600 1.000 64.56388  ?  1582 GLU   A CA  1 
ATOM   12470 C  C   . GLU   A 1 1584 ? -15.66000  41.27900  -11.20500 1.000 63.05170  ?  1582 GLU   A C   1 
ATOM   12471 O  O   . GLU   A 1 1584 ? -16.44200  42.18000  -10.88100 1.000 76.91208  ?  1582 GLU   A O   1 
ATOM   12472 C  CB  . GLU   A 1 1584 ? -15.25600  40.81900  -13.62600 1.000 50.86411  ?  1582 GLU   A CB  1 
ATOM   12473 C  CG  . GLU   A 1 1584 ? -14.72800  41.38800  -14.92900 1.000 65.85069  ?  1582 GLU   A CG  1 
ATOM   12474 C  CD  . GLU   A 1 1584 ? -15.47800  40.85300  -16.13400 1.000 91.22335  ?  1582 GLU   A CD  1 
ATOM   12475 O  OE1 . GLU   A 1 1584 ? -16.71700  40.71500  -16.05100 1.000 85.67874  ?  1582 GLU   A OE1 1 
ATOM   12476 O  OE2 . GLU   A 1 1584 ? -14.82800  40.56300  -17.16100 1.000 105.04181 -1 1582 GLU   A OE2 1 
ATOM   12477 N  N   . LYS   A 1 1585 ? -15.62300  40.10800  -10.57100 1.000 53.66227  ?  1583 LYS   A N   1 
ATOM   12478 C  CA  . LYS   A 1 1585 ? -16.59000  39.77000  -9.53800  1.000 44.87859  ?  1583 LYS   A CA  1 
ATOM   12479 C  C   . LYS   A 1 1585 ? -16.07800  40.00800  -8.12500  1.000 51.94167  ?  1583 LYS   A C   1 
ATOM   12480 O  O   . LYS   A 1 1585 ? -16.89200  40.10700  -7.20200  1.000 53.38024  ?  1583 LYS   A O   1 
ATOM   12481 C  CB  . LYS   A 1 1585 ? -17.02200  38.30600  -9.68500  1.000 48.11214  ?  1583 LYS   A CB  1 
ATOM   12482 C  CG  . LYS   A 1 1585 ? -17.42800  37.92600  -11.10500 1.000 55.08793  ?  1583 LYS   A CG  1 
ATOM   12483 C  CD  . LYS   A 1 1585 ? -18.79900  38.47400  -11.48200 1.000 68.15366  ?  1583 LYS   A CD  1 
ATOM   12484 C  CE  . LYS   A 1 1585 ? -19.91100  37.70100  -10.78600 1.000 73.60512  ?  1583 LYS   A CE  1 
ATOM   12485 N  NZ  . LYS   A 1 1585 ? -21.24500  37.91700  -11.42000 1.000 61.48074  ?  1583 LYS   A NZ  1 
ATOM   12486 N  N   . PHE   A 1 1586 ? -14.76400  40.10100  -7.93000  1.000 55.75189  ?  1584 PHE   A N   1 
ATOM   12487 C  CA  . PHE   A 1 1586 ? -14.16600  40.41500  -6.63100  1.000 58.15949  ?  1584 PHE   A CA  1 
ATOM   12488 C  C   . PHE   A 1 1586 ? -13.46100  41.76000  -6.77900  1.000 67.65322  ?  1584 PHE   A C   1 
ATOM   12489 O  O   . PHE   A 1 1586 ? -12.30600  41.82400  -7.20600  1.000 70.73270  ?  1584 PHE   A O   1 
ATOM   12490 C  CB  . PHE   A 1 1586 ? -13.19500  39.32200  -6.17000  1.000 62.83477  ?  1584 PHE   A CB  1 
ATOM   12491 C  CG  . PHE   A 1 1586 ? -13.84100  37.98500  -5.93500  1.000 42.67223  ?  1584 PHE   A CG  1 
ATOM   12492 C  CD1 . PHE   A 1 1586 ? -14.03100  37.09700  -6.98100  1.000 49.15323  ?  1584 PHE   A CD1 1 
ATOM   12493 C  CD2 . PHE   A 1 1586 ? -14.24000  37.60900  -4.66300  1.000 39.88746  ?  1584 PHE   A CD2 1 
ATOM   12494 C  CE1 . PHE   A 1 1586 ? -14.61900  35.86500  -6.76600  1.000 48.08180  ?  1584 PHE   A CE1 1 
ATOM   12495 C  CE2 . PHE   A 1 1586 ? -14.82800  36.37700  -4.44100  1.000 41.65082  ?  1584 PHE   A CE2 1 
ATOM   12496 C  CZ  . PHE   A 1 1586 ? -15.01700  35.50500  -5.49300  1.000 47.17102  ?  1584 PHE   A CZ  1 
ATOM   12497 N  N   . THR   A 1 1587 ? -14.16000  42.83700  -6.42000  1.000 72.22686  ?  1585 THR   A N   1 
ATOM   12498 C  CA  . THR   A 1 1587 ? -13.64500  44.17800  -6.63000  1.000 55.38942  ?  1585 THR   A CA  1 
ATOM   12499 C  C   . THR   A 1 1587 ? -13.45200  44.90200  -5.30400  1.000 55.11921  ?  1585 THR   A C   1 
ATOM   12500 O  O   . THR   A 1 1587 ? -14.23800  44.71000  -4.37000  1.000 55.55824  ?  1585 THR   A O   1 
ATOM   12501 C  CB  . THR   A 1 1587 ? -14.59300  45.00000  -7.51500  1.000 56.07956  ?  1585 THR   A CB  1 
ATOM   12502 O  OG1 . THR   A 1 1587 ? -15.79300  45.29400  -6.78700  1.000 72.56698  ?  1585 THR   A OG1 1 
ATOM   12503 C  CG2 . THR   A 1 1587 ? -14.95100  44.22800  -8.77400  1.000 49.73582  ?  1585 THR   A CG2 1 
ATOM   12504 N  N   . PRO   A 1 1588 ? -12.41600  45.72900  -5.18600  1.000 58.70303  ?  1586 PRO   A N   1 
ATOM   12505 C  CA  . PRO   A 1 1588 ? -12.29700  46.59200  -4.00600  1.000 60.43347  ?  1586 PRO   A CA  1 
ATOM   12506 C  C   . PRO   A 1 1588 ? -13.35100  47.68500  -4.02900  1.000 61.35919  ?  1586 PRO   A C   1 
ATOM   12507 O  O   . PRO   A 1 1588 ? -13.71800  48.20300  -5.08600  1.000 68.78051  ?  1586 PRO   A O   1 
ATOM   12508 C  CB  . PRO   A 1 1588 ? -10.88500  47.17800  -4.13000  1.000 45.17873  ?  1586 PRO   A CB  1 
ATOM   12509 C  CG  . PRO   A 1 1588 ? -10.17300  46.28800  -5.10600  1.000 57.13678  ?  1586 PRO   A CG  1 
ATOM   12510 C  CD  . PRO   A 1 1588 ? -11.23100  45.81700  -6.05100  1.000 62.93510  ?  1586 PRO   A CD  1 
ATOM   12511 N  N   . HIS   A 1 1589 ? -13.83500  48.03800  -2.84300  1.000 52.51783  ?  1587 HIS   A N   1 
ATOM   12512 C  CA  . HIS   A 1 1589 ? -14.91000  49.00800  -2.72300  1.000 58.25639  ?  1587 HIS   A CA  1 
ATOM   12513 C  C   . HIS   A 1 1589 ? -14.66800  49.90300  -1.51700  1.000 75.29159  ?  1587 HIS   A C   1 
ATOM   12514 O  O   . HIS   A 1 1589 ? -14.11700  49.45200  -0.50600  1.000 69.03068  ?  1587 HIS   A O   1 
ATOM   12515 C  CB  . HIS   A 1 1589 ? -16.27300  48.31400  -2.58500  1.000 63.95171  ?  1587 HIS   A CB  1 
ATOM   12516 C  CG  . HIS   A 1 1589 ? -17.42200  49.14600  -3.05700  1.000 63.27685  ?  1587 HIS   A CG  1 
ATOM   12517 N  ND1 . HIS   A 1 1589 ? -18.24400  49.83800  -2.19500  1.000 52.66408  ?  1587 HIS   A ND1 1 
ATOM   12518 C  CD2 . HIS   A 1 1589 ? -17.87900  49.40600  -4.30500  1.000 58.30453  ?  1587 HIS   A CD2 1 
ATOM   12519 C  CE1 . HIS   A 1 1589 ? -19.16300  50.48300  -2.89100  1.000 68.99265  ?  1587 HIS   A CE1 1 
ATOM   12520 N  NE2 . HIS   A 1 1589 ? -18.96400  50.23800  -4.17300  1.000 67.46877  ?  1587 HIS   A NE2 1 
ATOM   12521 N  N   . PRO   A 1 1590 ? -15.06400  51.17600  -1.59900  1.000 79.57249  ?  1588 PRO   A N   1 
ATOM   12522 C  CA  . PRO   A 1 1590 ? -14.91100  52.06800  -0.43900  1.000 55.22866  ?  1588 PRO   A CA  1 
ATOM   12523 C  C   . PRO   A 1 1590 ? -15.74400  51.65500  0.75900   1.000 59.57205  ?  1588 PRO   A C   1 
ATOM   12524 O  O   . PRO   A 1 1590 ? -15.45100  52.09700  1.87700   1.000 69.97361  ?  1588 PRO   A O   1 
ATOM   12525 C  CB  . PRO   A 1 1590 ? -15.35900  53.43300  -0.98200  1.000 54.59964  ?  1588 PRO   A CB  1 
ATOM   12526 C  CG  . PRO   A 1 1590 ? -15.19600  53.32500  -2.46400  1.000 64.69041  ?  1588 PRO   A CG  1 
ATOM   12527 C  CD  . PRO   A 1 1590 ? -15.52000  51.90200  -2.79600  1.000 64.88141  ?  1588 PRO   A CD  1 
ATOM   12528 N  N   . LEU   A 1 1591 ? -16.77900  50.83200  0.56700   1.000 63.68188  ?  1589 LEU   A N   1 
ATOM   12529 C  CA  . LEU   A 1 1591 ? -17.55800  50.35100  1.70300   1.000 73.66438  ?  1589 LEU   A CA  1 
ATOM   12530 C  C   . LEU   A 1 1591 ? -16.71500  49.46800  2.61400   1.000 78.18624  ?  1589 LEU   A C   1 
ATOM   12531 O  O   . LEU   A 1 1591 ? -16.88200  49.49000  3.83900   1.000 70.34133  ?  1589 LEU   A O   1 
ATOM   12532 C  CB  . LEU   A 1 1591 ? -18.79200  49.59300  1.21200   1.000 58.20478  ?  1589 LEU   A CB  1 
ATOM   12533 C  CG  . LEU   A 1 1591 ? -20.00900  50.44000  0.84000   1.000 54.95979  ?  1589 LEU   A CG  1 
ATOM   12534 C  CD1 . LEU   A 1 1591 ? -20.97400  49.64400  -0.02100  1.000 41.75201  ?  1589 LEU   A CD1 1 
ATOM   12535 C  CD2 . LEU   A 1 1591 ? -20.70700  50.94300  2.09500   1.000 63.37188  ?  1589 LEU   A CD2 1 
ATOM   12536 N  N   . GLU   A 1 1592 ? -15.80400  48.68900  2.03500   1.000 81.65283  ?  1590 GLU   A N   1 
ATOM   12537 C  CA  . GLU   A 1 1592 ? -14.91100  47.82800  2.79600   1.000 74.01481  ?  1590 GLU   A CA  1 
ATOM   12538 C  C   . GLU   A 1 1592 ? -13.53900  48.45100  3.00900   1.000 71.70045  ?  1590 GLU   A C   1 
ATOM   12539 O  O   . GLU   A 1 1592 ? -12.64400  47.78000  3.53300   1.000 77.72587  ?  1590 GLU   A O   1 
ATOM   12540 C  CB  . GLU   A 1 1592 ? -14.77000  46.47100  2.10300   1.000 54.67869  ?  1590 GLU   A CB  1 
ATOM   12541 C  CG  . GLU   A 1 1592 ? -15.93000  45.52800  2.36200   1.000 47.92296  ?  1590 GLU   A CG  1 
ATOM   12542 C  CD  . GLU   A 1 1592 ? -16.03200  45.11700  3.82100   1.000 58.17162  ?  1590 GLU   A CD  1 
ATOM   12543 O  OE1 . GLU   A 1 1592 ? -14.97900  44.99000  4.48100   1.000 62.17392  ?  1590 GLU   A OE1 1 
ATOM   12544 O  OE2 . GLU   A 1 1592 ? -17.16500  44.92400  4.30900   1.000 62.03288  -1 1590 GLU   A OE2 1 
ATOM   12545 N  N   . LYS   A 1 1593 ? -13.35600  49.71300  2.61900   1.000 75.65423  ?  1591 LYS   A N   1 
ATOM   12546 C  CA  . LYS   A 1 1593 ? -12.09800  50.43700  2.80200   1.000 72.86306  ?  1591 LYS   A CA  1 
ATOM   12547 C  C   . LYS   A 1 1593 ? -10.95000  49.73400  2.07300   1.000 66.62567  ?  1591 LYS   A C   1 
ATOM   12548 O  O   . LYS   A 1 1593 ? -9.95400   49.31900  2.67000   1.000 88.29215  ?  1591 LYS   A O   1 
ATOM   12549 C  CB  . LYS   A 1 1593 ? -11.77900  50.61600  4.29300   1.000 59.19682  ?  1591 LYS   A CB  1 
ATOM   12550 C  CG  . LYS   A 1 1593 ? -12.91200  51.20400  5.13100   1.000 61.04462  ?  1591 LYS   A CG  1 
ATOM   12551 C  CD  . LYS   A 1 1593 ? -12.75700  52.70900  5.32200   1.000 81.68130  ?  1591 LYS   A CD  1 
ATOM   12552 C  CE  . LYS   A 1 1593 ? -13.24800  53.49000  4.11200   1.000 84.44906  ?  1591 LYS   A CE  1 
ATOM   12553 N  NZ  . LYS   A 1 1593 ? -12.68000  54.86500  4.07100   1.000 68.81809  ?  1591 LYS   A NZ  1 
ATOM   12554 N  N   . GLY   A 1 1594 ? -11.10900  49.60600  0.75500   1.000 57.48850  ?  1592 GLY   A N   1 
ATOM   12555 C  CA  . GLY   A 1 1594 ? -10.12500  48.94800  -0.07600  1.000 69.05662  ?  1592 GLY   A CA  1 
ATOM   12556 C  C   . GLY   A 1 1594 ? -10.21100  47.43800  -0.11200  1.000 74.14943  ?  1592 GLY   A C   1 
ATOM   12557 O  O   . GLY   A 1 1594 ? -9.65600   46.82400  -1.03200  1.000 64.17608  ?  1592 GLY   A O   1 
ATOM   12558 N  N   . GLU   A 1 1595 ? -10.87900  46.81600  0.85600   1.000 78.21346  ?  1593 GLU   A N   1 
ATOM   12559 C  CA  . GLU   A 1 1595 ? -11.07000  45.37500  0.82600   1.000 75.93064  ?  1593 GLU   A CA  1 
ATOM   12560 C  C   . GLU   A 1 1595 ? -12.06100  45.00000  -0.27400  1.000 72.05284  ?  1593 GLU   A C   1 
ATOM   12561 O  O   . GLU   A 1 1595 ? -12.80300  45.83800  -0.79500  1.000 76.07951  ?  1593 GLU   A O   1 
ATOM   12562 C  CB  . GLU   A 1 1595 ? -11.56400  44.86500  2.18100   1.000 75.74842  ?  1593 GLU   A CB  1 
ATOM   12563 C  CG  . GLU   A 1 1595 ? -10.73200  45.31600  3.37700   1.000 80.49196  ?  1593 GLU   A CG  1 
ATOM   12564 C  CD  . GLU   A 1 1595 ? -9.65700   44.32000  3.77000   1.000 95.20247  ?  1593 GLU   A CD  1 
ATOM   12565 O  OE1 . GLU   A 1 1595 ? -9.17600   43.57600  2.89000   1.000 95.76494  ?  1593 GLU   A OE1 1 
ATOM   12566 O  OE2 . GLU   A 1 1595 ? -9.29600   44.28000  4.96500   1.000 86.75905  -1 1593 GLU   A OE2 1 
ATOM   12567 N  N   . ARG   A 1 1596 ? -12.07400  43.71700  -0.62000  1.000 72.72349  ?  1594 ARG   A N   1 
ATOM   12568 C  CA  . ARG   A 1 1596 ? -12.85000  43.26700  -1.76300  1.000 60.61308  ?  1594 ARG   A CA  1 
ATOM   12569 C  C   . ARG   A 1 1596 ? -14.30500  43.00100  -1.38800  1.000 57.01610  ?  1594 ARG   A C   1 
ATOM   12570 O  O   . ARG   A 1 1596 ? -14.66100  42.83100  -0.21800  1.000 58.44143  ?  1594 ARG   A O   1 
ATOM   12571 C  CB  . ARG   A 1 1596 ? -12.25200  41.99600  -2.36100  1.000 52.93856  ?  1594 ARG   A CB  1 
ATOM   12572 C  CG  . ARG   A 1 1596 ? -10.99300  42.19200  -3.18000  1.000 64.09233  ?  1594 ARG   A CG  1 
ATOM   12573 C  CD  . ARG   A 1 1596 ? -10.51300  40.83900  -3.66100  1.000 57.06831  ?  1594 ARG   A CD  1 
ATOM   12574 N  NE  . ARG   A 1 1596 ? -10.55000  39.87200  -2.57100  1.000 69.92368  ?  1594 ARG   A NE  1 
ATOM   12575 C  CZ  . ARG   A 1 1596 ? -10.62500  38.55800  -2.72900  1.000 56.84253  ?  1594 ARG   A CZ  1 
ATOM   12576 N  NH1 . ARG   A 1 1596 ? -10.66900  38.00800  -3.93200  1.000 42.04325  ?  1594 ARG   A NH1 1 
ATOM   12577 N  NH2 . ARG   A 1 1596 ? -10.66700  37.77700  -1.65300  1.000 48.91505  ?  1594 ARG   A NH2 1 
ATOM   12578 N  N   . ILE   A 1 1597 ? -15.14600  42.95800  -2.42000  1.000 52.28127  ?  1595 ILE   A N   1 
ATOM   12579 C  CA  . ILE   A 1 1597 ? -16.53500  42.53300  -2.31200  1.000 51.78640  ?  1595 ILE   A CA  1 
ATOM   12580 C  C   . ILE   A 1 1597 ? -16.84600  41.64700  -3.51100  1.000 54.10369  ?  1595 ILE   A C   1 
ATOM   12581 O  O   . ILE   A 1 1597 ? -16.31600  41.85000  -4.60800  1.000 44.09425  ?  1595 ILE   A O   1 
ATOM   12582 C  CB  . ILE   A 1 1597 ? -17.51600  43.72600  -2.25200  1.000 47.36986  ?  1595 ILE   A CB  1 
ATOM   12583 C  CG1 . ILE   A 1 1597 ? -17.24000  44.69900  -3.40100  1.000 53.66620  ?  1595 ILE   A CG1 1 
ATOM   12584 C  CG2 . ILE   A 1 1597 ? -17.43000  44.43100  -0.90600  1.000 44.52855  ?  1595 ILE   A CG2 1 
ATOM   12585 C  CD1 . ILE   A 1 1597 ? -18.48900  45.26400  -4.04000  1.000 55.37910  ?  1595 ILE   A CD1 1 
ATOM   12586 N  N   . TYR   A 1 1598 ? -17.70900  40.65600  -3.30200  1.000 42.46788  ?  1596 TYR   A N   1 
ATOM   12587 C  CA  . TYR   A 1 1598 ? -18.11100  39.74800  -4.36900  1.000 46.67783  ?  1596 TYR   A CA  1 
ATOM   12588 C  C   . TYR   A 1 1598 ? -19.44800  40.19500  -4.94700  1.000 45.80863  ?  1596 TYR   A C   1 
ATOM   12589 O  O   . TYR   A 1 1598 ? -20.44300  40.28900  -4.22100  1.000 45.60446  ?  1596 TYR   A O   1 
ATOM   12590 C  CB  . TYR   A 1 1598 ? -18.20500  38.30300  -3.88000  1.000 43.70840  ?  1596 TYR   A CB  1 
ATOM   12591 C  CG  . TYR   A 1 1598 ? -18.86900  37.39800  -4.89600  1.000 39.04435  ?  1596 TYR   A CG  1 
ATOM   12592 C  CD1 . TYR   A 1 1598 ? -18.27600  37.15600  -6.12900  1.000 31.26110  ?  1596 TYR   A CD1 1 
ATOM   12593 C  CD2 . TYR   A 1 1598 ? -20.09500  36.80100  -4.63100  1.000 39.82717  ?  1596 TYR   A CD2 1 
ATOM   12594 C  CE1 . TYR   A 1 1598 ? -18.88200  36.33900  -7.06700  1.000 36.35243  ?  1596 TYR   A CE1 1 
ATOM   12595 C  CE2 . TYR   A 1 1598 ? -20.70800  35.98200  -5.56100  1.000 41.80346  ?  1596 TYR   A CE2 1 
ATOM   12596 C  CZ  . TYR   A 1 1598 ? -20.09700  35.75400  -6.77700  1.000 41.48992  ?  1596 TYR   A CZ  1 
ATOM   12597 O  OH  . TYR   A 1 1598 ? -20.70400  34.94000  -7.70700  1.000 57.95791  ?  1596 TYR   A OH  1 
ATOM   12598 N  N   . ARG   A 1 1599 ? -19.47000  40.45700  -6.25300  1.000 38.53331  ?  1597 ARG   A N   1 
ATOM   12599 C  CA  . ARG   A 1 1599 ? -20.70100  40.81000  -6.95400  1.000 42.63429  ?  1597 ARG   A CA  1 
ATOM   12600 C  C   . ARG   A 1 1599 ? -21.49500  39.53600  -7.21100  1.000 44.93477  ?  1597 ARG   A C   1 
ATOM   12601 O  O   . ARG   A 1 1599 ? -21.11300  38.72200  -8.05800  1.000 49.90717  ?  1597 ARG   A O   1 
ATOM   12602 C  CB  . ARG   A 1 1599 ? -20.39000  41.52600  -8.26500  1.000 61.10515  ?  1597 ARG   A CB  1 
ATOM   12603 C  CG  . ARG   A 1 1599 ? -19.25100  42.53400  -8.19700  1.000 60.99266  ?  1597 ARG   A CG  1 
ATOM   12604 C  CD  . ARG   A 1 1599 ? -19.57500  43.69800  -7.27900  1.000 63.79615  ?  1597 ARG   A CD  1 
ATOM   12605 N  NE  . ARG   A 1 1599 ? -18.66800  44.82000  -7.49000  1.000 69.82880  ?  1597 ARG   A NE  1 
ATOM   12606 C  CZ  . ARG   A 1 1599 ? -18.93000  45.85600  -8.27600  1.000 70.14338  ?  1597 ARG   A CZ  1 
ATOM   12607 N  NH1 . ARG   A 1 1599 ? -20.07300  45.95000  -8.93700  1.000 70.03378  ?  1597 ARG   A NH1 1 
ATOM   12608 N  NH2 . ARG   A 1 1599 ? -18.02400  46.82100  -8.40200  1.000 62.57407  ?  1597 ARG   A NH2 1 
ATOM   12609 N  N   . THR   A 1 1600 ? -22.60200  39.35800  -6.48600  1.000 44.63859  ?  1598 THR   A N   1 
ATOM   12610 C  CA  . THR   A 1 1600 ? -23.39200  38.14000  -6.64400  1.000 36.76543  ?  1598 THR   A CA  1 
ATOM   12611 C  C   . THR   A 1 1600 ? -24.06300  38.06800  -8.00800  1.000 34.04967  ?  1598 THR   A C   1 
ATOM   12612 O  O   . THR   A 1 1600 ? -24.22400  36.97400  -8.56000  1.000 52.81537  ?  1598 THR   A O   1 
ATOM   12613 C  CB  . THR   A 1 1600 ? -24.45400  38.04200  -5.54800  1.000 48.99214  ?  1598 THR   A CB  1 
ATOM   12614 O  OG1 . THR   A 1 1600 ? -25.27700  39.21600  -5.56500  1.000 54.37299  ?  1598 THR   A OG1 1 
ATOM   12615 C  CG2 . THR   A 1 1600 ? -23.80300  37.90300  -4.19100  1.000 35.26090  ?  1598 THR   A CG2 1 
ATOM   12616 N  N   . GLY   A 1 1601 ? -24.45100  39.20900  -8.56800  1.000 39.87408  ?  1599 GLY   A N   1 
ATOM   12617 C  CA  . GLY   A 1 1601 ? -25.28900  39.20700  -9.74600  1.000 52.57185  ?  1599 GLY   A CA  1 
ATOM   12618 C  C   . GLY   A 1 1601 ? -26.75000  38.95100  -9.46300  1.000 49.84760  ?  1599 GLY   A C   1 
ATOM   12619 O  O   . GLY   A 1 1601 ? -27.53100  38.79000  -10.40700 1.000 58.80480  ?  1599 GLY   A O   1 
ATOM   12620 N  N   . ASP   A 1 1602 ? -27.14000  38.90600  -8.19300  1.000 41.10911  ?  1600 ASP   A N   1 
ATOM   12621 C  CA  . ASP   A 1 1602 ? -28.51800  38.68300  -7.78500  1.000 56.88982  ?  1600 ASP   A CA  1 
ATOM   12622 C  C   . ASP   A 1 1602 ? -29.11300  39.99400  -7.29300  1.000 65.12955  ?  1600 ASP   A C   1 
ATOM   12623 O  O   . ASP   A 1 1602 ? -28.47000  40.72300  -6.52900  1.000 50.30429  ?  1600 ASP   A O   1 
ATOM   12624 C  CB  . ASP   A 1 1602 ? -28.59600  37.62500  -6.68300  1.000 54.93224  ?  1600 ASP   A CB  1 
ATOM   12625 C  CG  . ASP   A 1 1602 ? -28.02800  36.29000  -7.11600  1.000 58.34975  ?  1600 ASP   A CG  1 
ATOM   12626 O  OD1 . ASP   A 1 1602 ? -28.22400  35.90900  -8.28900  1.000 54.05912  ?  1600 ASP   A OD1 1 
ATOM   12627 O  OD2 . ASP   A 1 1602 ? -27.38300  35.62100  -6.28100  1.000 51.27324  -1 1600 ASP   A OD2 1 
ATOM   12628 N  N   . LEU   A 1 1603 ? -30.33300  40.29000  -7.73000  1.000 59.65546  ?  1601 LEU   A N   1 
ATOM   12629 C  CA  . LEU   A 1 1603 ? -31.02600  41.48100  -7.26600  1.000 49.34927  ?  1601 LEU   A CA  1 
ATOM   12630 C  C   . LEU   A 1 1603 ? -31.59200  41.24400  -5.87300  1.000 50.88509  ?  1601 LEU   A C   1 
ATOM   12631 O  O   . LEU   A 1 1603 ? -32.10800  40.16300  -5.57200  1.000 54.98345  ?  1601 LEU   A O   1 
ATOM   12632 C  CB  . LEU   A 1 1603 ? -32.14800  41.86700  -8.22800  1.000 49.44612  ?  1601 LEU   A CB  1 
ATOM   12633 C  CG  . LEU   A 1 1603 ? -32.53600  43.34600  -8.20500  1.000 41.63893  ?  1601 LEU   A CG  1 
ATOM   12634 C  CD1 . LEU   A 1 1603 ? -31.49000  44.18000  -8.93400  1.000 50.53411  ?  1601 LEU   A CD1 1 
ATOM   12635 C  CD2 . LEU   A 1 1603 ? -33.91400  43.55500  -8.80500  1.000 43.70669  ?  1601 LEU   A CD2 1 
ATOM   12636 N  N   . ALA   A 1 1604 ? -31.49500  42.26200  -5.02200  1.000 49.67808  ?  1602 ALA   A N   1 
ATOM   12637 C  CA  . ALA   A 1 1604 ? -31.93300  42.13500  -3.64200  1.000 47.20502  ?  1602 ALA   A CA  1 
ATOM   12638 C  C   . ALA   A 1 1604 ? -32.35300  43.49900  -3.11400  1.000 53.07345  ?  1602 ALA   A C   1 
ATOM   12639 O  O   . ALA   A 1 1604 ? -31.93000  44.54100  -3.62000  1.000 55.01075  ?  1602 ALA   A O   1 
ATOM   12640 C  CB  . ALA   A 1 1604 ? -30.83400  41.53100  -2.76200  1.000 42.74184  ?  1602 ALA   A CB  1 
ATOM   12641 N  N   . ARG   A 1 1605 ? -33.19000  43.47600  -2.08000  1.000 51.51488  ?  1603 ARG   A N   1 
ATOM   12642 C  CA  . ARG   A 1 1605 ? -33.68900  44.69000  -1.45500  1.000 59.14683  ?  1603 ARG   A CA  1 
ATOM   12643 C  C   . ARG   A 1 1605 ? -33.52000  44.59300  0.05400   1.000 51.59581  ?  1603 ARG   A C   1 
ATOM   12644 O  O   . ARG   A 1 1605 ? -33.61500  43.50900  0.64000   1.000 45.54977  ?  1603 ARG   A O   1 
ATOM   12645 C  CB  . ARG   A 1 1605 ? -35.16700  44.94200  -1.81400  1.000 47.71131  ?  1603 ARG   A CB  1 
ATOM   12646 C  CG  . ARG   A 1 1605 ? -36.16800  44.53700  -0.73800  1.000 57.95228  ?  1603 ARG   A CG  1 
ATOM   12647 C  CD  . ARG   A 1 1605 ? -37.50200  44.13400  -1.34300  1.000 72.93849  ?  1603 ARG   A CD  1 
ATOM   12648 N  NE  . ARG   A 1 1605 ? -38.04900  45.16500  -2.21600  1.000 77.25528  ?  1603 ARG   A NE  1 
ATOM   12649 C  CZ  . ARG   A 1 1605 ? -39.09800  44.99200  -3.00800  1.000 62.51160  ?  1603 ARG   A CZ  1 
ATOM   12650 N  NH1 . ARG   A 1 1605 ? -39.73900  43.83500  -3.06500  1.000 46.25948  ?  1603 ARG   A NH1 1 
ATOM   12651 N  NH2 . ARG   A 1 1605 ? -39.51200  46.00400  -3.76500  1.000 71.49926  ?  1603 ARG   A NH2 1 
ATOM   12652 N  N   . TYR   A 1 1606 ? -33.24300  45.73500  0.67300   1.000 46.75079  ?  1604 TYR   A N   1 
ATOM   12653 C  CA  . TYR   A 1 1606 ? -33.20600  45.81100  2.12400   1.000 39.74216  ?  1604 TYR   A CA  1 
ATOM   12654 C  C   . TYR   A 1 1606 ? -34.61500  45.98700  2.66800   1.000 51.61509  ?  1604 TYR   A C   1 
ATOM   12655 O  O   . TYR   A 1 1606 ? -35.43500  46.70900  2.09500   1.000 58.33969  ?  1604 TYR   A O   1 
ATOM   12656 C  CB  . TYR   A 1 1606 ? -32.32800  46.97000  2.59100   1.000 48.80581  ?  1604 TYR   A CB  1 
ATOM   12657 C  CG  . TYR   A 1 1606 ? -30.84400  46.68900  2.58100   1.000 48.86218  ?  1604 TYR   A CG  1 
ATOM   12658 C  CD1 . TYR   A 1 1606 ? -30.29600  45.69800  3.38600   1.000 51.39505  ?  1604 TYR   A CD1 1 
ATOM   12659 C  CD2 . TYR   A 1 1606 ? -29.98800  47.43800  1.78900   1.000 48.30055  ?  1604 TYR   A CD2 1 
ATOM   12660 C  CE1 . TYR   A 1 1606 ? -28.93500  45.45200  3.38500   1.000 56.26921  ?  1604 TYR   A CE1 1 
ATOM   12661 C  CE2 . TYR   A 1 1606 ? -28.63200  47.20100  1.78100   1.000 40.08222  ?  1604 TYR   A CE2 1 
ATOM   12662 C  CZ  . TYR   A 1 1606 ? -28.11000  46.20900  2.57800   1.000 46.41275  ?  1604 TYR   A CZ  1 
ATOM   12663 O  OH  . TYR   A 1 1606 ? -26.75500  45.98000  2.56400   1.000 47.93915  ?  1604 TYR   A OH  1 
ATOM   12664 N  N   . ARG   A 1 1607 ? -34.88800  45.31600  3.77800   1.000 59.52314  ?  1605 ARG   A N   1 
ATOM   12665 C  CA  . ARG   A 1 1607 ? -36.15200  45.40700  4.48800   1.000 57.19344  ?  1605 ARG   A CA  1 
ATOM   12666 C  C   . ARG   A 1 1607 ? -35.94100  46.20800  5.77000   1.000 67.07276  ?  1605 ARG   A C   1 
ATOM   12667 O  O   . ARG   A 1 1607 ? -34.82000  46.30600  6.27900   1.000 62.02669  ?  1605 ARG   A O   1 
ATOM   12668 C  CB  . ARG   A 1 1607 ? -36.68600  43.99800  4.78400   1.000 55.11185  ?  1605 ARG   A CB  1 
ATOM   12669 C  CG  . ARG   A 1 1607 ? -37.68800  43.88200  5.91500   1.000 71.12675  ?  1605 ARG   A CG  1 
ATOM   12670 C  CD  . ARG   A 1 1607 ? -37.68800  42.48600  6.51500   1.000 67.30081  ?  1605 ARG   A CD  1 
ATOM   12671 N  NE  . ARG   A 1 1607 ? -38.70100  41.62700  5.91700   1.000 57.17965  ?  1605 ARG   A NE  1 
ATOM   12672 C  CZ  . ARG   A 1 1607 ? -39.16300  40.51900  6.48100   1.000 65.17182  ?  1605 ARG   A CZ  1 
ATOM   12673 N  NH1 . ARG   A 1 1607 ? -38.67900  40.07500  7.63000   1.000 55.86113  ?  1605 ARG   A NH1 1 
ATOM   12674 N  NH2 . ARG   A 1 1607 ? -40.14700  39.84900  5.88900   1.000 70.86591  ?  1605 ARG   A NH2 1 
ATOM   12675 N  N   . GLU   A 1 1608 ? -37.02700  46.80700  6.27900   1.000 69.97177  ?  1606 GLU   A N   1 
ATOM   12676 C  CA  . GLU   A 1 1608 ? -36.94000  47.61600  7.49300   1.000 61.77674  ?  1606 GLU   A CA  1 
ATOM   12677 C  C   . GLU   A 1 1608 ? -36.32000  46.83300  8.64400   1.000 73.25182  ?  1606 GLU   A C   1 
ATOM   12678 O  O   . GLU   A 1 1608 ? -35.48200  47.36100  9.38400   1.000 80.40199  ?  1606 GLU   A O   1 
ATOM   12679 C  CB  . GLU   A 1 1608 ? -38.32800  48.12700  7.88700   1.000 63.67061  ?  1606 GLU   A CB  1 
ATOM   12680 C  CG  . GLU   A 1 1608 ? -38.89400  49.20100  6.96800   1.000 69.83273  ?  1606 GLU   A CG  1 
ATOM   12681 C  CD  . GLU   A 1 1608 ? -39.24300  50.47700  7.71400   1.000 78.77218  ?  1606 GLU   A CD  1 
ATOM   12682 O  OE1 . GLU   A 1 1608 ? -38.43700  50.90900  8.56600   1.000 81.72919  ?  1606 GLU   A OE1 1 
ATOM   12683 O  OE2 . GLU   A 1 1608 ? -40.32200  51.04800  7.45300   1.000 79.07034  -1 1606 GLU   A OE2 1 
ATOM   12684 N  N   . ASP   A 1 1609 ? -36.71700  45.56900  8.81000   1.000 74.75925  ?  1607 ASP   A N   1 
ATOM   12685 C  CA  . ASP   A 1 1609 ? -36.03800  44.70400  9.77000   1.000 66.74303  ?  1607 ASP   A CA  1 
ATOM   12686 C  C   . ASP   A 1 1609 ? -34.53200  44.69600  9.54700   1.000 69.16432  ?  1607 ASP   A C   1 
ATOM   12687 O  O   . ASP   A 1 1609 ? -33.75800  44.64400  10.51100  1.000 79.11741  ?  1607 ASP   A O   1 
ATOM   12688 C  CB  . ASP   A 1 1609 ? -36.59100  43.28200  9.66900   1.000 56.83900  ?  1607 ASP   A CB  1 
ATOM   12689 C  CG  . ASP   A 1 1609 ? -38.08500  43.22400  9.90000   1.000 92.66087  ?  1607 ASP   A CG  1 
ATOM   12690 O  OD1 . ASP   A 1 1609 ? -38.82300  44.03900  9.29700   1.000 94.83150  ?  1607 ASP   A OD1 1 
ATOM   12691 O  OD2 . ASP   A 1 1609 ? -38.52000  42.37000  10.70200  1.000 96.46951  -1 1607 ASP   A OD2 1 
ATOM   12692 N  N   . GLY   A 1 1610 ? -34.09300  44.76300  8.29200   1.000 67.09063  ?  1608 GLY   A N   1 
ATOM   12693 C  CA  . GLY   A 1 1610 ? -32.70700  44.50200  7.93500   1.000 59.43660  ?  1608 GLY   A CA  1 
ATOM   12694 C  C   . GLY   A 1 1610 ? -32.50300  43.23600  7.12500   1.000 62.72108  ?  1608 GLY   A C   1 
ATOM   12695 O  O   . GLY   A 1 1610 ? -31.46000  43.09600  6.47000   1.000 54.96355  ?  1608 GLY   A O   1 
ATOM   12696 N  N   . ASN   A 1 1611 ? -33.46400  42.31400  7.13100   1.000 59.69117  ?  1609 ASN   A N   1 
ATOM   12697 C  CA  . ASN   A 1 1611 ? -33.32100  41.07800  6.37400   1.000 68.05993  ?  1609 ASN   A CA  1 
ATOM   12698 C  C   . ASN   A 1 1611 ? -33.39500  41.35500  4.87800   1.000 51.59933  ?  1609 ASN   A C   1 
ATOM   12699 O  O   . ASN   A 1 1611 ? -34.22500  42.13900  4.41200   1.000 49.57345  ?  1609 ASN   A O   1 
ATOM   12700 C  CB  . ASN   A 1 1611 ? -34.40300  40.08000  6.78000   1.000 57.84270  ?  1609 ASN   A CB  1 
ATOM   12701 C  CG  . ASN   A 1 1611 ? -34.34300  39.72600  8.25400   1.000 50.36312  ?  1609 ASN   A CG  1 
ATOM   12702 O  OD1 . ASN   A 1 1611 ? -33.36700  39.14200  8.72600   1.000 49.77141  ?  1609 ASN   A OD1 1 
ATOM   12703 N  ND2 . ASN   A 1 1611 ? -35.39000  40.07800  8.98800   1.000 64.21519  ?  1609 ASN   A ND2 1 
ATOM   12704 N  N   . ILE   A 1 1612 ? -32.52800  40.70200  4.13200   1.000 48.81531  ?  1610 ILE   A N   1 
ATOM   12705 C  CA  . ILE   A 1 1612 ? -32.43600  40.89400  2.69100   1.000 45.22399  ?  1610 ILE   A CA  1 
ATOM   12706 C  C   . ILE   A 1 1612 ? -33.43200  39.97000  2.00500   1.000 46.42834  ?  1610 ILE   A C   1 
ATOM   12707 O  O   . ILE   A 1 1612 ? -33.73100  38.87400  2.48900   1.000 44.59407  ?  1610 ILE   A O   1 
ATOM   12708 C  CB  . ILE   A 1 1612 ? -30.99000  40.65100  2.21200   1.000 32.59233  ?  1610 ILE   A CB  1 
ATOM   12709 C  CG1 . ILE   A 1 1612 ? -30.01800  41.47600  3.05700   1.000 38.46990  ?  1610 ILE   A CG1 1 
ATOM   12710 C  CG2 . ILE   A 1 1612 ? -30.83600  41.00300  0.74600   1.000 21.81309  ?  1610 ILE   A CG2 1 
ATOM   12711 C  CD1 . ILE   A 1 1612 ? -28.59100  41.44400  2.56300   1.000 47.99783  ?  1610 ILE   A CD1 1 
ATOM   12712 N  N   . GLU   A 1 1613 ? -33.97000  40.42500  0.87600   1.000 41.53035  ?  1611 GLU   A N   1 
ATOM   12713 C  CA  . GLU   A 1 1613 ? -34.94200  39.66800  0.10100   1.000 49.43474  ?  1611 GLU   A CA  1 
ATOM   12714 C  C   . GLU   A 1 1613 ? -34.37300  39.39400  -1.28300  1.000 44.20966  ?  1611 GLU   A C   1 
ATOM   12715 O  O   . GLU   A 1 1613 ? -33.89100  40.31400  -1.95200  1.000 43.03524  ?  1611 GLU   A O   1 
ATOM   12716 C  CB  . GLU   A 1 1613 ? -36.26900  40.42600  -0.00500  1.000 44.48094  ?  1611 GLU   A CB  1 
ATOM   12717 C  CG  . GLU   A 1 1613 ? -36.83300  40.86900  1.33700   1.000 48.99159  ?  1611 GLU   A CG  1 
ATOM   12718 C  CD  . GLU   A 1 1613 ? -38.20000  41.51400  1.21800   1.000 60.20706  ?  1611 GLU   A CD  1 
ATOM   12719 O  OE1 . GLU   A 1 1613 ? -38.75200  41.54300  0.09800   1.000 62.98591  ?  1611 GLU   A OE1 1 
ATOM   12720 O  OE2 . GLU   A 1 1613 ? -38.72600  41.98900  2.24600   1.000 62.30637  -1 1611 GLU   A OE2 1 
ATOM   12721 N  N   . TYR   A 1 1614 ? -34.42500  38.13300  -1.70600  1.000 44.43959  ?  1612 TYR   A N   1 
ATOM   12722 C  CA  . TYR   A 1 1614 ? -33.91500  37.73800  -3.01400  1.000 43.14414  ?  1612 TYR   A CA  1 
ATOM   12723 C  C   . TYR   A 1 1614 ? -34.91600  38.13600  -4.09200  1.000 51.49521  ?  1612 TYR   A C   1 
ATOM   12724 O  O   . TYR   A 1 1614 ? -36.08900  37.75000  -4.03100  1.000 65.55286  ?  1612 TYR   A O   1 
ATOM   12725 C  CB  . TYR   A 1 1614 ? -33.64700  36.23400  -3.04300  1.000 37.44670  ?  1612 TYR   A CB  1 
ATOM   12726 C  CG  . TYR   A 1 1614 ? -33.10200  35.71500  -4.35700  1.000 43.19263  ?  1612 TYR   A CG  1 
ATOM   12727 C  CD1 . TYR   A 1 1614 ? -31.83100  36.06300  -4.79000  1.000 52.55035  ?  1612 TYR   A CD1 1 
ATOM   12728 C  CD2 . TYR   A 1 1614 ? -33.85400  34.86200  -5.15500  1.000 53.74592  ?  1612 TYR   A CD2 1 
ATOM   12729 C  CE1 . TYR   A 1 1614 ? -31.32800  35.58800  -5.98600  1.000 55.20044  ?  1612 TYR   A CE1 1 
ATOM   12730 C  CE2 . TYR   A 1 1614 ? -33.35900  34.38100  -6.35300  1.000 48.48101  ?  1612 TYR   A CE2 1 
ATOM   12731 C  CZ  . TYR   A 1 1614 ? -32.09600  34.74700  -6.76300  1.000 58.45960  ?  1612 TYR   A CZ  1 
ATOM   12732 O  OH  . TYR   A 1 1614 ? -31.59700  34.27200  -7.95500  1.000 72.98185  ?  1612 TYR   A OH  1 
ATOM   12733 N  N   . LEU   A 1 1615 ? -34.45900  38.91200  -5.07400  1.000 39.02699  ?  1613 LEU   A N   1 
ATOM   12734 C  CA  . LEU   A 1 1615 ? -35.31600  39.40300  -6.14400  1.000 51.86888  ?  1613 LEU   A CA  1 
ATOM   12735 C  C   . LEU   A 1 1615 ? -35.00100  38.78200  -7.49700  1.000 57.87004  ?  1613 LEU   A C   1 
ATOM   12736 O  O   . LEU   A 1 1615 ? -35.60200  39.18000  -8.50100  1.000 67.53283  ?  1613 LEU   A O   1 
ATOM   12737 C  CB  . LEU   A 1 1615 ? -35.21800  40.93100  -6.24300  1.000 51.77369  ?  1613 LEU   A CB  1 
ATOM   12738 C  CG  . LEU   A 1 1615 ? -36.22400  41.77000  -5.44800  1.000 46.93322  ?  1613 LEU   A CG  1 
ATOM   12739 C  CD1 . LEU   A 1 1615 ? -36.15900  41.46900  -3.95900  1.000 45.22183  ?  1613 LEU   A CD1 1 
ATOM   12740 C  CD2 . LEU   A 1 1615 ? -35.99300  43.25100  -5.70100  1.000 67.91288  ?  1613 LEU   A CD2 1 
ATOM   12741 N  N   . GLY   A 1 1616 ? -34.08100  37.82300  -7.55400  1.000 52.23700  ?  1614 GLY   A N   1 
ATOM   12742 C  CA  . GLY   A 1 1616 ? -33.73500  37.15200  -8.79300  1.000 56.15828  ?  1614 GLY   A CA  1 
ATOM   12743 C  C   . GLY   A 1 1616 ? -32.41800  37.64400  -9.36200  1.000 58.51132  ?  1614 GLY   A C   1 
ATOM   12744 O  O   . GLY   A 1 1616 ? -31.77000  38.55900  -8.84300  1.000 65.17631  ?  1614 GLY   A O   1 
ATOM   12745 N  N   . ARG   A 1 1617 ? -32.01900  37.00700  -10.46100 1.000 60.08984  ?  1615 ARG   A N   1 
ATOM   12746 C  CA  . ARG   A 1 1617 ? -30.79500  37.38600  -11.15100 1.000 63.56016  ?  1615 ARG   A CA  1 
ATOM   12747 C  C   . ARG   A 1 1617 ? -31.03900  38.59900  -12.03600 1.000 67.06786  ?  1615 ARG   A C   1 
ATOM   12748 O  O   . ARG   A 1 1617 ? -32.08100  38.71400  -12.68800 1.000 73.52153  ?  1615 ARG   A O   1 
ATOM   12749 C  CB  . ARG   A 1 1617 ? -30.26100  36.22500  -11.99000 1.000 58.41133  ?  1615 ARG   A CB  1 
ATOM   12750 C  CG  . ARG   A 1 1617 ? -29.78000  35.04300  -11.17100 1.000 59.92318  ?  1615 ARG   A CG  1 
ATOM   12751 C  CD  . ARG   A 1 1617 ? -28.63400  34.32200  -11.86100 1.000 64.55450  ?  1615 ARG   A CD  1 
ATOM   12752 N  NE  . ARG   A 1 1617 ? -27.44100  35.15600  -11.95500 1.000 58.67429  ?  1615 ARG   A NE  1 
ATOM   12753 C  CZ  . ARG   A 1 1617 ? -26.53700  35.28200  -10.99200 1.000 55.80864  ?  1615 ARG   A CZ  1 
ATOM   12754 N  NH1 . ARG   A 1 1617 ? -26.66400  34.65100  -9.83700  1.000 58.00905  ?  1615 ARG   A NH1 1 
ATOM   12755 N  NH2 . ARG   A 1 1617 ? -25.47900  36.06300  -11.19400 1.000 59.69056  ?  1615 ARG   A NH2 1 
ATOM   12756 N  N   . MET   A 1 1618 ? -30.06000  39.50600  -12.06100 1.000 72.16829  ?  1616 MET   A N   1 
ATOM   12757 C  CA  . MET   A 1 1618 ? -30.22900  40.75900  -12.78800 1.000 71.07585  ?  1616 MET   A CA  1 
ATOM   12758 C  C   . MET   A 1 1618 ? -30.34700  40.53700  -14.29000 1.000 71.82555  ?  1616 MET   A C   1 
ATOM   12759 O  O   . MET   A 1 1618 ? -31.07000  41.27600  -14.96800 1.000 88.08383  ?  1616 MET   A O   1 
ATOM   12760 C  CB  . MET   A 1 1618 ? -29.06500  41.70000  -12.48400 1.000 69.51493  ?  1616 MET   A CB  1 
ATOM   12761 C  CG  . MET   A 1 1618 ? -28.74200  41.83100  -11.00400 1.000 58.63090  ?  1616 MET   A CG  1 
ATOM   12762 S  SD  . MET   A 1 1618 ? -27.39100  42.98500  -10.69500 1.000 69.53928  ?  1616 MET   A SD  1 
ATOM   12763 C  CE  . MET   A 1 1618 ? -26.52200  42.92400  -12.26100 1.000 66.61234  ?  1616 MET   A CE  1 
ATOM   12764 N  N   . ASP   A 1 1619 ? -29.65000  39.53900  -14.83100 1.000 77.30116  ?  1617 ASP   A N   1 
ATOM   12765 C  CA  . ASP   A 1 1619 ? -29.74800  39.25500  -16.25600 1.000 68.80217  ?  1617 ASP   A CA  1 
ATOM   12766 C  C   . ASP   A 1 1619 ? -30.97900  38.42700  -16.60800 1.000 73.88816  ?  1617 ASP   A C   1 
ATOM   12767 O  O   . ASP   A 1 1619 ? -31.29400  38.28700  -17.79500 1.000 87.08802  ?  1617 ASP   A O   1 
ATOM   12768 C  CB  . ASP   A 1 1619 ? -28.46900  38.55800  -16.73700 1.000 63.65155  ?  1617 ASP   A CB  1 
ATOM   12769 C  CG  . ASP   A 1 1619 ? -28.16900  37.28300  -15.97100 1.000 81.74452  ?  1617 ASP   A CG  1 
ATOM   12770 O  OD1 . ASP   A 1 1619 ? -28.73800  37.10200  -14.87300 1.000 95.19906  ?  1617 ASP   A OD1 1 
ATOM   12771 O  OD2 . ASP   A 1 1619 ? -27.37800  36.45500  -16.47500 1.000 80.05433  -1 1617 ASP   A OD2 1 
ATOM   12772 N  N   . HIS   A 1 1620 ? -31.68300  37.89000  -15.61200 1.000 70.06109  ?  1618 HIS   A N   1 
ATOM   12773 C  CA  . HIS   A 1 1620 ? -32.93800  37.18400  -15.84100 1.000 69.37318  ?  1618 HIS   A CA  1 
ATOM   12774 C  C   . HIS   A 1 1620 ? -34.07600  37.89500  -15.12100 1.000 79.52451  ?  1618 HIS   A C   1 
ATOM   12775 O  O   . HIS   A 1 1620 ? -34.71700  37.30500  -14.24600 1.000 67.06138  ?  1618 HIS   A O   1 
ATOM   12776 C  CB  . HIS   A 1 1620 ? -32.87000  35.73200  -15.34700 1.000 81.68964  ?  1618 HIS   A CB  1 
ATOM   12777 C  CG  . HIS   A 1 1620 ? -31.73400  34.93100  -15.90700 1.000 95.16850  ?  1618 HIS   A CG  1 
ATOM   12778 N  ND1 . HIS   A 1 1620 ? -30.43900  35.39900  -15.95800 1.000 101.01876 ?  1618 HIS   A ND1 1 
ATOM   12779 C  CD2 . HIS   A 1 1620 ? -31.69500  33.67000  -16.39900 1.000 98.56284  ?  1618 HIS   A CD2 1 
ATOM   12780 C  CE1 . HIS   A 1 1620 ? -29.65700  34.47100  -16.47900 1.000 90.88701  ?  1618 HIS   A CE1 1 
ATOM   12781 N  NE2 . HIS   A 1 1620 ? -30.39400  33.41100  -16.75400 1.000 99.66466  ?  1618 HIS   A NE2 1 
ATOM   12782 N  N   . GLN   A 1 1621 ? -34.33100  39.15500  -15.46000 1.000 82.47275  ?  1619 GLN   A N   1 
ATOM   12783 C  CA  . GLN   A 1 1621 ? -35.38500  39.93600  -14.82700 1.000 69.31829  ?  1619 GLN   A CA  1 
ATOM   12784 C  C   . GLN   A 1 1621 ? -36.50800  40.17200  -15.82800 1.000 68.89811  ?  1619 GLN   A C   1 
ATOM   12785 O  O   . GLN   A 1 1621 ? -36.25500  40.59200  -16.96200 1.000 63.68209  ?  1619 GLN   A O   1 
ATOM   12786 C  CB  . GLN   A 1 1621 ? -34.85000  41.27300  -14.30700 1.000 62.54767  ?  1619 GLN   A CB  1 
ATOM   12787 C  CG  . GLN   A 1 1621 ? -35.48700  41.73800  -13.00300 1.000 58.30784  ?  1619 GLN   A CG  1 
ATOM   12788 C  CD  . GLN   A 1 1621 ? -34.79300  41.16800  -11.78000 1.000 69.20549  ?  1619 GLN   A CD  1 
ATOM   12789 O  OE1 . GLN   A 1 1621 ? -33.58200  40.94800  -11.78900 1.000 74.76195  ?  1619 GLN   A OE1 1 
ATOM   12790 N  NE2 . GLN   A 1 1621 ? -35.55800  40.92500  -10.72200 1.000 62.37421  ?  1619 GLN   A NE2 1 
ATOM   12791 N  N   . VAL   A 1 1622 ? -37.74200  39.90600  -15.40400 1.000 68.01007  ?  1620 VAL   A N   1 
ATOM   12792 C  CA  . VAL   A 1 1622 ? -38.91700  40.01400  -16.26200 1.000 81.60840  ?  1620 VAL   A CA  1 
ATOM   12793 C  C   . VAL   A 1 1622 ? -39.61100  41.33900  -15.98300 1.000 79.26251  ?  1620 VAL   A C   1 
ATOM   12794 O  O   . VAL   A 1 1622 ? -39.91500  41.66000  -14.82600 1.000 80.24961  ?  1620 VAL   A O   1 
ATOM   12795 C  CB  . VAL   A 1 1622 ? -39.87100  38.82700  -16.04900 1.000 81.31613  ?  1620 VAL   A CB  1 
ATOM   12796 C  CG1 . VAL   A 1 1622 ? -41.24400  39.13700  -16.61300 1.000 69.69681  ?  1620 VAL   A CG1 1 
ATOM   12797 C  CG2 . VAL   A 1 1622 ? -39.30900  37.59300  -16.71700 1.000 65.69991  ?  1620 VAL   A CG2 1 
ATOM   12798 N  N   . LYS   A 1 1623 ? -39.85900  42.11000  -17.04100 1.000 78.39223  ?  1621 LYS   A N   1 
ATOM   12799 C  CA  . LYS   A 1 1623 ? -40.47700  43.42600  -16.93400 1.000 85.18815  ?  1621 LYS   A CA  1 
ATOM   12800 C  C   . LYS   A 1 1623 ? -41.58500  43.53600  -17.97100 1.000 89.76376  ?  1621 LYS   A C   1 
ATOM   12801 O  O   . LYS   A 1 1623 ? -41.33300  43.37800  -19.17000 1.000 94.99736  ?  1621 LYS   A O   1 
ATOM   12802 C  CB  . LYS   A 1 1623 ? -39.44400  44.54100  -17.13500 1.000 79.17867  ?  1621 LYS   A CB  1 
ATOM   12803 C  CG  . LYS   A 1 1623 ? -38.15800  44.35400  -16.34200 1.000 73.04374  ?  1621 LYS   A CG  1 
ATOM   12804 C  CD  . LYS   A 1 1623 ? -37.17400  45.48200  -16.59600 1.000 57.18794  ?  1621 LYS   A CD  1 
ATOM   12805 C  CE  . LYS   A 1 1623 ? -37.65300  46.78000  -15.97200 1.000 75.79220  ?  1621 LYS   A CE  1 
ATOM   12806 N  NZ  . LYS   A 1 1623 ? -36.75700  47.92400  -16.29500 1.000 77.12019  ?  1621 LYS   A NZ  1 
ATOM   12807 N  N   . ILE   A 1 1624 ? -42.80400  43.80700  -17.51200 1.000 91.76421  ?  1622 ILE   A N   1 
ATOM   12808 C  CA  . ILE   A 1 1624 ? -43.95300  44.01100  -18.38600 1.000 90.56959  ?  1622 ILE   A CA  1 
ATOM   12809 C  C   . ILE   A 1 1624 ? -44.31500  45.48800  -18.32900 1.000 78.97163  ?  1622 ILE   A C   1 
ATOM   12810 O  O   . ILE   A 1 1624 ? -44.74800  45.99100  -17.28400 1.000 78.78486  ?  1622 ILE   A O   1 
ATOM   12811 C  CB  . ILE   A 1 1624 ? -45.14500  43.13000  -17.98900 1.000 87.23134  ?  1622 ILE   A CB  1 
ATOM   12812 C  CG1 . ILE   A 1 1624 ? -44.82200  41.65400  -18.23400 1.000 80.51435  ?  1622 ILE   A CG1 1 
ATOM   12813 C  CG2 . ILE   A 1 1624 ? -46.39600  43.55000  -18.74700 1.000 75.32416  ?  1622 ILE   A CG2 1 
ATOM   12814 C  CD1 . ILE   A 1 1624 ? -44.23300  41.37500  -19.60100 1.000 75.25294  ?  1622 ILE   A CD1 1 
ATOM   12815 N  N   . ARG   A 1 1625 ? -44.13700  46.18100  -19.45600 1.000 87.71863  ?  1623 ARG   A N   1 
ATOM   12816 C  CA  . ARG   A 1 1625 ? -44.40700  47.61500  -19.56300 1.000 90.31765  ?  1623 ARG   A CA  1 
ATOM   12817 C  C   . ARG   A 1 1625 ? -43.62200  48.40100  -18.51200 1.000 90.77655  ?  1623 ARG   A C   1 
ATOM   12818 O  O   . ARG   A 1 1625 ? -44.16300  49.24900  -17.79800 1.000 96.20772  ?  1623 ARG   A O   1 
ATOM   12819 C  CB  . ARG   A 1 1625 ? -45.91000  47.90100  -19.47100 1.000 78.66754  ?  1623 ARG   A CB  1 
ATOM   12820 C  CG  . ARG   A 1 1625 ? -46.69000  47.41700  -20.68800 1.000 72.20584  ?  1623 ARG   A CG  1 
ATOM   12821 C  CD  . ARG   A 1 1625 ? -48.18200  47.72400  -20.59800 1.000 73.00996  ?  1623 ARG   A CD  1 
ATOM   12822 N  NE  . ARG   A 1 1625 ? -48.93900  46.65200  -19.96200 1.000 62.70938  ?  1623 ARG   A NE  1 
ATOM   12823 C  CZ  . ARG   A 1 1625 ? -49.69700  46.80300  -18.88400 1.000 76.57520  ?  1623 ARG   A CZ  1 
ATOM   12824 N  NH1 . ARG   A 1 1625 ? -49.83200  47.97800  -18.29200 1.000 63.64004  ?  1623 ARG   A NH1 1 
ATOM   12825 N  NH2 . ARG   A 1 1625 ? -50.34400  45.74900  -18.39300 1.000 68.25890  ?  1623 ARG   A NH2 1 
ATOM   12826 N  N   . GLY   A 1 1626 ? -42.32800  48.10200  -18.41800 1.000 81.62228  ?  1624 GLY   A N   1 
ATOM   12827 C  CA  . GLY   A 1 1626 ? -41.44700  48.79600  -17.50000 1.000 86.98945  ?  1624 GLY   A CA  1 
ATOM   12828 C  C   . GLY   A 1 1626 ? -41.46500  48.24900  -16.08800 1.000 89.28970  ?  1624 GLY   A C   1 
ATOM   12829 O  O   . GLY   A 1 1626 ? -40.42700  48.20000  -15.42200 1.000 99.56527  ?  1624 GLY   A O   1 
ATOM   12830 N  N   . TYR   A 1 1627 ? -42.63800  47.83500  -15.61800 1.000 87.90918  ?  1625 TYR   A N   1 
ATOM   12831 C  CA  . TYR   A 1 1627 ? -42.76800  47.34700  -14.25200 1.000 94.16834  ?  1625 TYR   A CA  1 
ATOM   12832 C  C   . TYR   A 1 1627 ? -42.14700  45.96200  -14.10600 1.000 88.87889  ?  1625 TYR   A C   1 
ATOM   12833 O  O   . TYR   A 1 1627 ? -42.32700  45.09000  -14.96000 1.000 86.98272  ?  1625 TYR   A O   1 
ATOM   12834 C  CB  . TYR   A 1 1627 ? -44.23900  47.29800  -13.84400 1.000 82.46645  ?  1625 TYR   A CB  1 
ATOM   12835 C  CG  . TYR   A 1 1627 ? -44.93600  48.63900  -13.79800 1.000 77.36519  ?  1625 TYR   A CG  1 
ATOM   12836 C  CD1 . TYR   A 1 1627 ? -44.76300  49.49400  -12.71800 1.000 77.39738  ?  1625 TYR   A CD1 1 
ATOM   12837 C  CD2 . TYR   A 1 1627 ? -45.78200  49.04200  -14.82400 1.000 70.04460  ?  1625 TYR   A CD2 1 
ATOM   12838 C  CE1 . TYR   A 1 1627 ? -45.40200  50.71800  -12.66500 1.000 82.29598  ?  1625 TYR   A CE1 1 
ATOM   12839 C  CE2 . TYR   A 1 1627 ? -46.42700  50.26600  -14.77900 1.000 77.16839  ?  1625 TYR   A CE2 1 
ATOM   12840 C  CZ  . TYR   A 1 1627 ? -46.23300  51.09900  -13.69600 1.000 81.15593  ?  1625 TYR   A CZ  1 
ATOM   12841 O  OH  . TYR   A 1 1627 ? -46.87000  52.31700  -13.64300 1.000 78.17709  ?  1625 TYR   A OH  1 
ATOM   12842 N  N   . ARG   A 1 1628 ? -41.41800  45.76200  -13.01000 1.000 74.35452  ?  1626 ARG   A N   1 
ATOM   12843 C  CA  . ARG   A 1 1628 ? -40.82500  44.46100  -12.73200 1.000 68.72278  ?  1626 ARG   A CA  1 
ATOM   12844 C  C   . ARG   A 1 1628 ? -41.90000  43.46500  -12.31600 1.000 69.15906  ?  1626 ARG   A C   1 
ATOM   12845 O  O   . ARG   A 1 1628 ? -42.85600  43.81300  -11.61700 1.000 70.11771  ?  1626 ARG   A O   1 
ATOM   12846 C  CB  . ARG   A 1 1628 ? -39.76700  44.57700  -11.63400 1.000 75.95450  ?  1626 ARG   A CB  1 
ATOM   12847 C  CG  . ARG   A 1 1628 ? -39.15700  43.24100  -11.23100 1.000 84.01161  ?  1626 ARG   A CG  1 
ATOM   12848 C  CD  . ARG   A 1 1628 ? -38.43200  43.31100  -9.89800  1.000 67.88214  ?  1626 ARG   A CD  1 
ATOM   12849 N  NE  . ARG   A 1 1628 ? -38.32100  41.99000  -9.28900  1.000 77.68499  ?  1626 ARG   A NE  1 
ATOM   12850 C  CZ  . ARG   A 1 1628 ? -39.08400  41.55500  -8.29400  1.000 86.75565  ?  1626 ARG   A CZ  1 
ATOM   12851 N  NH1 . ARG   A 1 1628 ? -39.99900  42.33100  -7.73400  1.000 84.35193  ?  1626 ARG   A NH1 1 
ATOM   12852 N  NH2 . ARG   A 1 1628 ? -38.92300  40.31300  -7.84800  1.000 75.47236  ?  1626 ARG   A NH2 1 
ATOM   12853 N  N   . ILE   A 1 1629 ? -41.73700  42.21600  -12.74400 1.000 69.40161  ?  1627 ILE   A N   1 
ATOM   12854 C  CA  . ILE   A 1 1629 ? -42.69700  41.15200  -12.47900 1.000 72.93493  ?  1627 ILE   A CA  1 
ATOM   12855 C  C   . ILE   A 1 1629 ? -42.10700  40.20600  -11.44400 1.000 77.68133  ?  1627 ILE   A C   1 
ATOM   12856 O  O   . ILE   A 1 1629 ? -40.98900  39.70300  -11.61800 1.000 91.57844  ?  1627 ILE   A O   1 
ATOM   12857 C  CB  . ILE   A 1 1629 ? -43.06200  40.38800  -13.76400 1.000 64.90055  ?  1627 ILE   A CB  1 
ATOM   12858 C  CG1 . ILE   A 1 1629 ? -43.46100  41.35900  -14.88000 1.000 73.30965  ?  1627 ILE   A CG1 1 
ATOM   12859 C  CG2 . ILE   A 1 1629 ? -44.15500  39.36400  -13.48000 1.000 68.27853  ?  1627 ILE   A CG2 1 
ATOM   12860 C  CD1 . ILE   A 1 1629 ? -44.55500  42.32600  -14.50600 1.000 73.83999  ?  1627 ILE   A CD1 1 
ATOM   12861 N  N   . GLU   A 1 1630 ? -42.85700  39.96200  -10.37100 1.000 79.74067  ?  1628 GLU   A N   1 
ATOM   12862 C  CA  . GLU   A 1 1630 ? -42.50600  38.95700  -9.36800  1.000 74.77306  ?  1628 GLU   A CA  1 
ATOM   12863 C  C   . GLU   A 1 1630 ? -43.37300  37.73300  -9.64900  1.000 74.64790  ?  1628 GLU   A C   1 
ATOM   12864 O  O   . GLU   A 1 1630 ? -44.49700  37.61900  -9.16000  1.000 75.54211  ?  1628 GLU   A O   1 
ATOM   12865 C  CB  . GLU   A 1 1630 ? -42.71400  39.49400  -7.95600  1.000 73.03913  ?  1628 GLU   A CB  1 
ATOM   12866 N  N   . LEU   A 1 1631 ? -42.84000  36.81100  -10.45600 1.000 70.07976  ?  1629 LEU   A N   1 
ATOM   12867 C  CA  . LEU   A 1 1631 ? -43.62300  35.66100  -10.89800 1.000 63.40234  ?  1629 LEU   A CA  1 
ATOM   12868 C  C   . LEU   A 1 1631 ? -44.01000  34.73800  -9.75000  1.000 73.34020  ?  1629 LEU   A C   1 
ATOM   12869 O  O   . LEU   A 1 1631 ? -44.96600  33.96600  -9.88800  1.000 67.53586  ?  1629 LEU   A O   1 
ATOM   12870 C  CB  . LEU   A 1 1631 ? -42.85100  34.88200  -11.96500 1.000 62.71984  ?  1629 LEU   A CB  1 
ATOM   12871 C  CG  . LEU   A 1 1631 ? -42.68600  35.63300  -13.29200 1.000 69.86960  ?  1629 LEU   A CG  1 
ATOM   12872 C  CD1 . LEU   A 1 1631 ? -41.24500  36.03400  -13.53500 1.000 54.10275  ?  1629 LEU   A CD1 1 
ATOM   12873 C  CD2 . LEU   A 1 1631 ? -43.20100  34.80600  -14.45500 1.000 76.18144  ?  1629 LEU   A CD2 1 
ATOM   12874 N  N   . ASP   A 1 1632 ? -43.29700  34.79700  -8.62200  1.000 91.80143  ?  1630 ASP   A N   1 
ATOM   12875 C  CA  . ASP   A 1 1632 ? -43.68300  33.99300  -7.46700  1.000 85.34393  ?  1630 ASP   A CA  1 
ATOM   12876 C  C   . ASP   A 1 1632 ? -45.01200  34.46400  -6.89000  1.000 77.64118  ?  1630 ASP   A C   1 
ATOM   12877 O  O   . ASP   A 1 1632 ? -45.84200  33.64500  -6.47800  1.000 84.34568  ?  1630 ASP   A O   1 
ATOM   12878 C  CB  . ASP   A 1 1632 ? -42.58700  34.04000  -6.40200  1.000 62.03560  ?  1630 ASP   A CB  1 
ATOM   12879 N  N   . GLU   A 1 1633 ? -45.23400  35.78100  -6.86100  1.000 69.06525  ?  1631 GLU   A N   1 
ATOM   12880 C  CA  . GLU   A 1 1633 ? -46.48900  36.31300  -6.34300  1.000 79.68574  ?  1631 GLU   A CA  1 
ATOM   12881 C  C   . GLU   A 1 1633 ? -47.66300  35.96500  -7.25000  1.000 81.74900  ?  1631 GLU   A C   1 
ATOM   12882 O  O   . GLU   A 1 1633 ? -48.80000  35.86000  -6.77700  1.000 86.85045  ?  1631 GLU   A O   1 
ATOM   12883 C  CB  . GLU   A 1 1633 ? -46.37300  37.82800  -6.16700  1.000 89.53700  ?  1631 GLU   A CB  1 
ATOM   12884 C  CG  . GLU   A 1 1633 ? -47.31400  38.42100  -5.13200  1.000 85.85956  ?  1631 GLU   A CG  1 
ATOM   12885 C  CD  . GLU   A 1 1633 ? -46.95700  39.85400  -4.78600  1.000 108.38358 ?  1631 GLU   A CD  1 
ATOM   12886 O  OE1 . GLU   A 1 1633 ? -45.81700  40.27000  -5.08400  1.000 98.73732  ?  1631 GLU   A OE1 1 
ATOM   12887 O  OE2 . GLU   A 1 1633 ? -47.81400  40.56400  -4.22000  1.000 122.57873 -1 1631 GLU   A OE2 1 
ATOM   12888 N  N   . ILE   A 1 1634 ? -47.41000  35.77800  -8.54700  1.000 74.96220  ?  1632 ILE   A N   1 
ATOM   12889 C  CA  . ILE   A 1 1634 ? -48.46800  35.36300  -9.46400  1.000 78.29620  ?  1632 ILE   A CA  1 
ATOM   12890 C  C   . ILE   A 1 1634 ? -48.88800  33.92700  -9.17400  1.000 92.44895  ?  1632 ILE   A C   1 
ATOM   12891 O  O   . ILE   A 1 1634 ? -50.08200  33.61900  -9.07700  1.000 90.12652  ?  1632 ILE   A O   1 
ATOM   12892 C  CB  . ILE   A 1 1634 ? -48.00600  35.53000  -10.92300 1.000 77.67788  ?  1632 ILE   A CB  1 
ATOM   12893 C  CG1 . ILE   A 1 1634 ? -47.90200  37.01200  -11.28500 1.000 76.44153  ?  1632 ILE   A CG1 1 
ATOM   12894 C  CG2 . ILE   A 1 1634 ? -48.94600  34.79800  -11.87300 1.000 83.69966  ?  1632 ILE   A CG2 1 
ATOM   12895 C  CD1 . ILE   A 1 1634 ? -47.23300  37.26400  -12.61900 1.000 76.44853  ?  1632 ILE   A CD1 1 
ATOM   12896 N  N   . ARG   A 1 1635 ? -47.91100  33.02700  -9.03100  1.000 94.50685  ?  1633 ARG   A N   1 
ATOM   12897 C  CA  . ARG   A 1 1635 ? -48.22400  31.62000  -8.79800  1.000 94.06756  ?  1633 ARG   A CA  1 
ATOM   12898 C  C   . ARG   A 1 1635 ? -48.92800  31.42000  -7.46200  1.000 90.99416  ?  1633 ARG   A C   1 
ATOM   12899 O  O   . ARG   A 1 1635 ? -49.87300  30.62900  -7.36400  1.000 87.96442  ?  1633 ARG   A O   1 
ATOM   12900 C  CB  . ARG   A 1 1635 ? -46.94800  30.78000  -8.86400  1.000 88.73926  ?  1633 ARG   A CB  1 
ATOM   12901 C  CG  . ARG   A 1 1635 ? -47.12500  29.34900  -8.37800  1.000 95.30227  ?  1633 ARG   A CG  1 
ATOM   12902 C  CD  . ARG   A 1 1635 ? -45.82100  28.57300  -8.43200  1.000 84.76743  ?  1633 ARG   A CD  1 
ATOM   12903 N  NE  . ARG   A 1 1635 ? -45.90400  27.31500  -7.70000  1.000 84.26633  ?  1633 ARG   A NE  1 
ATOM   12904 C  CZ  . ARG   A 1 1635 ? -45.55600  27.16500  -6.42900  1.000 80.05152  ?  1633 ARG   A CZ  1 
ATOM   12905 N  NH1 . ARG   A 1 1635 ? -45.08700  28.17600  -5.71600  1.000 65.42395  ?  1633 ARG   A NH1 1 
ATOM   12906 N  NH2 . ARG   A 1 1635 ? -45.68200  25.97000  -5.85900  1.000 70.02505  ?  1633 ARG   A NH2 1 
ATOM   12907 N  N   . SER   A 1 1636 ? -48.48200  32.12800  -6.42000  1.000 83.17093  ?  1634 SER   A N   1 
ATOM   12908 C  CA  . SER   A 1 1636 ? -49.11600  31.98600  -5.11200  1.000 86.89387  ?  1634 SER   A CA  1 
ATOM   12909 C  C   . SER   A 1 1636 ? -50.57200  32.43000  -5.15900  1.000 82.07614  ?  1634 SER   A C   1 
ATOM   12910 O  O   . SER   A 1 1636 ? -51.44800  31.77200  -4.58700  1.000 71.87705  ?  1634 SER   A O   1 
ATOM   12911 C  CB  . SER   A 1 1636 ? -48.34400  32.78200  -4.05900  1.000 71.59930  ?  1634 SER   A CB  1 
ATOM   12912 O  OG  . SER   A 1 1636 ? -48.68500  34.15600  -4.10100  1.000 94.81288  ?  1634 SER   A OG  1 
ATOM   12913 N  N   . LYS   A 1 1637 ? -50.85300  33.54200  -5.84400  1.000 84.99714  ?  1635 LYS   A N   1 
ATOM   12914 C  CA  . LYS   A 1 1637 ? -52.23400  33.97600  -6.02200  1.000 96.35832  ?  1635 LYS   A CA  1 
ATOM   12915 C  C   . LYS   A 1 1637 ? -53.02300  33.02600  -6.91400  1.000 95.75538  ?  1635 LYS   A C   1 
ATOM   12916 O  O   . LYS   A 1 1637 ? -54.25800  33.03200  -6.86600  1.000 85.09734  ?  1635 LYS   A O   1 
ATOM   12917 C  CB  . LYS   A 1 1637 ? -52.27600  35.39400  -6.59700  1.000 88.60118  ?  1635 LYS   A CB  1 
ATOM   12918 C  CG  . LYS   A 1 1637 ? -51.74800  36.46100  -5.65000  1.000 77.42672  ?  1635 LYS   A CG  1 
ATOM   12919 C  CD  . LYS   A 1 1637 ? -52.52200  36.46300  -4.34300  1.000 84.22225  ?  1635 LYS   A CD  1 
ATOM   12920 C  CE  . LYS   A 1 1637 ? -51.83600  37.31900  -3.29300  1.000 87.27252  ?  1635 LYS   A CE  1 
ATOM   12921 N  NZ  . LYS   A 1 1637 ? -52.44500  37.12400  -1.94800  1.000 74.21850  ?  1635 LYS   A NZ  1 
ATOM   12922 N  N   . LEU   A 1 1638 ? -52.34100  32.21800  -7.72500  1.000 87.13086  ?  1636 LEU   A N   1 
ATOM   12923 C  CA  . LEU   A 1 1638 ? -52.99700  31.18000  -8.50900  1.000 78.73029  ?  1636 LEU   A CA  1 
ATOM   12924 C  C   . LEU   A 1 1638 ? -53.11000  29.86400  -7.75100  1.000 94.20826  ?  1636 LEU   A C   1 
ATOM   12925 O  O   . LEU   A 1 1638 ? -53.95500  29.03300  -8.09900  1.000 96.67382  ?  1636 LEU   A O   1 
ATOM   12926 C  CB  . LEU   A 1 1638 ? -52.24000  30.96400  -9.82700  1.000 73.35488  ?  1636 LEU   A CB  1 
ATOM   12927 C  CG  . LEU   A 1 1638 ? -53.00800  30.53500  -11.08300 1.000 72.07425  ?  1636 LEU   A CG  1 
ATOM   12928 C  CD1 . LEU   A 1 1638 ? -52.24800  30.96300  -12.32700 1.000 72.55675  ?  1636 LEU   A CD1 1 
ATOM   12929 C  CD2 . LEU   A 1 1638 ? -53.25200  29.03300  -11.11600 1.000 76.96695  ?  1636 LEU   A CD2 1 
ATOM   12930 N  N   . ILE   A 1 1639 ? -52.29800  29.66900  -6.71100  1.000 96.36970  ?  1637 ILE   A N   1 
ATOM   12931 C  CA  . ILE   A 1 1639 ? -52.31200  28.41800  -5.96000  1.000 93.89084  ?  1637 ILE   A CA  1 
ATOM   12932 C  C   . ILE   A 1 1639 ? -53.22100  28.45600  -4.73500  1.000 96.72065  ?  1637 ILE   A C   1 
ATOM   12933 O  O   . ILE   A 1 1639 ? -53.56600  27.39000  -4.20300  1.000 100.59758 ?  1637 ILE   A O   1 
ATOM   12934 C  CB  . ILE   A 1 1639 ? -50.88500  28.02800  -5.53200  1.000 68.97879  ?  1637 ILE   A CB  1 
ATOM   12935 N  N   . GLN   A 1 1640 ? -53.62200  29.64300  -4.27300  1.000 94.41796  ?  1638 GLN   A N   1 
ATOM   12936 C  CA  . GLN   A 1 1640 ? -54.48000  29.73800  -3.09500  1.000 91.75326  ?  1638 GLN   A CA  1 
ATOM   12937 C  C   . GLN   A 1 1640 ? -55.88700  29.20500  -3.33500  1.000 101.21787 ?  1638 GLN   A C   1 
ATOM   12938 O  O   . GLN   A 1 1640 ? -56.61800  28.98100  -2.36200  1.000 77.64007  ?  1638 GLN   A O   1 
ATOM   12939 C  CB  . GLN   A 1 1640 ? -54.56200  31.18800  -2.61000  1.000 71.02873  ?  1638 GLN   A CB  1 
ATOM   12940 C  CG  . GLN   A 1 1640 ? -53.26700  31.72400  -2.02600  1.000 79.32434  ?  1638 GLN   A CG  1 
ATOM   12941 C  CD  . GLN   A 1 1640 ? -53.44900  33.05900  -1.33400  1.000 90.19119  ?  1638 GLN   A CD  1 
ATOM   12942 O  OE1 . GLN   A 1 1640 ? -52.79500  34.04400  -1.67700  1.000 87.16045  ?  1638 GLN   A OE1 1 
ATOM   12943 N  NE2 . GLN   A 1 1640 ? -54.33600  33.09700  -0.34600  1.000 85.57013  ?  1638 GLN   A NE2 1 
ATOM   12944 N  N   . GLU   A 1 1641 ? -56.28300  28.99500  -4.58800  1.000 103.27673 ?  1639 GLU   A N   1 
ATOM   12945 C  CA  . GLU   A 1 1641 ? -57.60700  28.47400  -4.88900  1.000 92.77992  ?  1639 GLU   A CA  1 
ATOM   12946 C  C   . GLU   A 1 1641 ? -57.70500  27.00700  -4.47000  1.000 103.66803 ?  1639 GLU   A C   1 
ATOM   12947 O  O   . GLU   A 1 1641 ? -56.76900  26.42000  -3.91900  1.000 116.54799 ?  1639 GLU   A O   1 
ATOM   12948 C  CB  . GLU   A 1 1641 ? -57.91600  28.64000  -6.37500  1.000 78.82096  ?  1639 GLU   A CB  1 
ATOM   12949 N  N   . GLU   A 1 1642 ? -58.86600  26.40400  -4.73500  1.000 107.77082 ?  1640 GLU   A N   1 
ATOM   12950 C  CA  . GLU   A 1 1642 ? -59.04900  24.99300  -4.40900  1.000 99.17036  ?  1640 GLU   A CA  1 
ATOM   12951 C  C   . GLU   A 1 1642 ? -58.29100  24.10000  -5.38500  1.000 111.11266 ?  1640 GLU   A C   1 
ATOM   12952 O  O   . GLU   A 1 1642 ? -57.65900  23.12000  -4.97500  1.000 122.23861 ?  1640 GLU   A O   1 
ATOM   12953 C  CB  . GLU   A 1 1642 ? -60.53700  24.64300  -4.40100  1.000 85.70832  ?  1640 GLU   A CB  1 
ATOM   12954 N  N   . THR   A 1 1643 ? -58.33900  24.42600  -6.67800  1.000 109.06638 ?  1641 THR   A N   1 
ATOM   12955 C  CA  . THR   A 1 1643 ? -57.63700  23.65800  -7.70600  1.000 116.94190 ?  1641 THR   A CA  1 
ATOM   12956 C  C   . THR   A 1 1643 ? -56.17200  24.08800  -7.71400  1.000 116.60073 ?  1641 THR   A C   1 
ATOM   12957 O  O   . THR   A 1 1643 ? -55.73300  24.93200  -8.50100  1.000 93.88692  ?  1641 THR   A O   1 
ATOM   12958 C  CB  . THR   A 1 1643 ? -58.28900  23.85500  -9.06900  1.000 106.68089 ?  1641 THR   A CB  1 
ATOM   12959 O  OG1 . THR   A 1 1643 ? -59.69800  23.61900  -8.96600  1.000 87.32013  ?  1641 THR   A OG1 1 
ATOM   12960 C  CG2 . THR   A 1 1643 ? -57.69600  22.89000  -10.08900 1.000 95.05227  ?  1641 THR   A CG2 1 
ATOM   12961 N  N   . ILE   A 1 1644 ? -55.40100  23.48800  -6.80900  1.000 111.40932 ?  1642 ILE   A N   1 
ATOM   12962 C  CA  . ILE   A 1 1644 ? -53.97900  23.78500  -6.69700  1.000 108.30830 ?  1642 ILE   A CA  1 
ATOM   12963 C  C   . ILE   A 1 1644 ? -53.20800  22.85500  -7.62300  1.000 115.22963 ?  1642 ILE   A C   1 
ATOM   12964 O  O   . ILE   A 1 1644 ? -52.44400  21.99600  -7.16900  1.000 101.13746 ?  1642 ILE   A O   1 
ATOM   12965 C  CB  . ILE   A 1 1644 ? -53.48900  23.65500  -5.24400  1.000 110.09432 ?  1642 ILE   A CB  1 
ATOM   12966 C  CG1 . ILE   A 1 1644 ? -54.52800  24.23700  -4.28600  1.000 93.40331  ?  1642 ILE   A CG1 1 
ATOM   12967 C  CG2 . ILE   A 1 1644 ? -52.15700  24.37200  -5.06500  1.000 95.54940  ?  1642 ILE   A CG2 1 
ATOM   12968 C  CD1 . ILE   A 1 1644 ? -54.38600  23.75800  -2.85900  1.000 73.26415  ?  1642 ILE   A CD1 1 
ATOM   12969 N  N   . GLN   A 1 1645 ? -53.41500  23.01500  -8.93300  1.000 118.47393 ?  1643 GLN   A N   1 
ATOM   12970 C  CA  . GLN   A 1 1645 ? -52.60200  22.29900  -9.91000  1.000 109.81474 ?  1643 GLN   A CA  1 
ATOM   12971 C  C   . GLN   A 1 1645 ? -51.13500  22.69500  -9.81300  1.000 110.89311 ?  1643 GLN   A C   1 
ATOM   12972 O  O   . GLN   A 1 1645 ? -50.27200  21.98100  -10.33900 1.000 91.54716  ?  1643 GLN   A O   1 
ATOM   12973 C  CB  . GLN   A 1 1645 ? -53.13400  22.56500  -11.32200 1.000 91.70135  ?  1643 GLN   A CB  1 
ATOM   12974 C  CG  . GLN   A 1 1645 ? -52.51500  21.70400  -12.41500 1.000 79.83427  ?  1643 GLN   A CG  1 
ATOM   12975 C  CD  . GLN   A 1 1645 ? -52.28100  22.47700  -13.69900 1.000 86.15374  ?  1643 GLN   A CD  1 
ATOM   12976 O  OE1 . GLN   A 1 1645 ? -52.26200  23.70800  -13.70200 1.000 84.93389  ?  1643 GLN   A OE1 1 
ATOM   12977 N  NE2 . GLN   A 1 1645 ? -52.09900  21.75600  -14.80000 1.000 77.82379  ?  1643 GLN   A NE2 1 
ATOM   12978 N  N   . ASP   A 1 1646 ? -50.87300  23.78600  -9.08700  1.000 115.42778 ?  1644 ASP   A N   1 
ATOM   12979 C  CA  . ASP   A 1 1646 ? -49.48700  24.31000  -8.93800  1.000 117.74564 ?  1644 ASP   A CA  1 
ATOM   12980 C  C   . ASP   A 1 1646 ? -48.91400  24.57500  -10.32800 1.000 119.42282 ?  1644 ASP   A C   1 
ATOM   12981 O  O   . ASP   A 1 1646 ? -47.88900  23.95300  -10.67100 1.000 128.77708 ?  1644 ASP   A O   1 
ATOM   12982 C  CB  . ASP   A 1 1646 ? -48.60600  23.40800  -8.08700  1.000 117.00586 ?  1644 ASP   A CB  1 
ATOM   12983 C  CG  . ASP   A 1 1646 ? -48.66100  23.66400  -6.58900  1.000 118.93378 ?  1644 ASP   A CG  1 
ATOM   12984 O  OD1 . ASP   A 1 1646 ? -47.99400  24.61300  -6.13400  1.000 118.93399 ?  1644 ASP   A OD1 1 
ATOM   12985 O  OD2 . ASP   A 1 1646 ? -49.36700  22.90700  -5.89200  1.000 117.57099 -1 1644 ASP   A OD2 1 
ATOM   12986 N  N   . ALA   A 1 1647 ? -49.56400  25.44300  -11.10500 1.000 106.39528 ?  1645 ALA   A N   1 
ATOM   12987 C  CA  . ALA   A 1 1647 ? -48.98600  25.82700  -12.41000 1.000 101.99870 ?  1645 ALA   A CA  1 
ATOM   12988 C  C   . ALA   A 1 1647 ? -47.99100  26.95700  -12.15600 1.000 104.79275 ?  1645 ALA   A C   1 
ATOM   12989 O  O   . ALA   A 1 1647 ? -48.26400  27.81500  -11.29800 1.000 99.86883  ?  1645 ALA   A O   1 
ATOM   12990 C  CB  . ALA   A 1 1647 ? -50.06800  26.24100  -13.37400 1.000 72.35285  ?  1645 ALA   A CB  1 
ATOM   12991 N  N   . VAL   A 1 1648 ? -46.85500  26.93000  -12.85100 1.000 105.35866 ?  1646 VAL   A N   1 
ATOM   12992 C  CA  . VAL   A 1 1648 ? -45.81000  27.97300  -12.63600 1.000 105.14718 ?  1646 VAL   A CA  1 
ATOM   12993 C  C   . VAL   A 1 1648 ? -45.86500  28.93400  -13.82700 1.000 111.67136 ?  1646 VAL   A C   1 
ATOM   12994 O  O   . VAL   A 1 1648 ? -46.17800  28.47500  -14.94600 1.000 102.86151 ?  1646 VAL   A O   1 
ATOM   12995 C  CB  . VAL   A 1 1648 ? -44.39700  27.39500  -12.44400 1.000 97.29594  ?  1646 VAL   A CB  1 
ATOM   12996 C  CG1 . VAL   A 1 1648 ? -43.41000  28.45300  -11.96500 1.000 73.47836  ?  1646 VAL   A CG1 1 
ATOM   12997 C  CG2 . VAL   A 1 1648 ? -44.40600  26.21100  -11.48500 1.000 91.36748  ?  1646 VAL   A CG2 1 
ATOM   12998 N  N   . VAL   A 1 1649 ? -45.59100  30.21200  -13.57900 1.000 104.09018 ?  1647 VAL   A N   1 
ATOM   12999 C  CA  . VAL   A 1 1649 ? -45.68200  31.22800  -14.65900 1.000 92.88399  ?  1647 VAL   A CA  1 
ATOM   13000 C  C   . VAL   A 1 1649 ? -44.26100  31.59200  -15.09000 1.000 80.31079  ?  1647 VAL   A C   1 
ATOM   13001 O  O   . VAL   A 1 1649 ? -43.38000  31.67700  -14.21700 1.000 83.65332  ?  1647 VAL   A O   1 
ATOM   13002 C  CB  . VAL   A 1 1649 ? -46.46800  32.43600  -14.12300 1.000 97.01212  ?  1647 VAL   A CB  1 
ATOM   13003 C  CG1 . VAL   A 1 1649 ? -45.99100  32.85900  -12.74200 1.000 91.30043  ?  1647 VAL   A CG1 1 
ATOM   13004 C  CG2 . VAL   A 1 1649 ? -46.49500  33.60700  -15.09700 1.000 95.12219  ?  1647 VAL   A CG2 1 
ATOM   13005 N  N   . VAL   A 1 1650 ? -44.05400  31.74100  -16.39200 1.000 79.75568  ?  1648 VAL   A N   1 
ATOM   13006 C  CA  . VAL   A 1 1650 ? -42.72100  32.14400  -16.91300 1.000 74.37967  ?  1648 VAL   A CA  1 
ATOM   13007 C  C   . VAL   A 1 1650 ? -42.95300  33.09600  -18.09200 1.000 89.75883  ?  1648 VAL   A C   1 
ATOM   13008 O  O   . VAL   A 1 1650 ? -44.08100  33.12700  -18.62100 1.000 97.53299  ?  1648 VAL   A O   1 
ATOM   13009 C  CB  . VAL   A 1 1650 ? -41.88600  30.91900  -17.31900 1.000 77.47698  ?  1648 VAL   A CB  1 
ATOM   13010 C  CG1 . VAL   A 1 1650 ? -42.21600  30.43200  -18.72400 1.000 68.22241  ?  1648 VAL   A CG1 1 
ATOM   13011 C  CG2 . VAL   A 1 1650 ? -40.39100  31.16800  -17.15900 1.000 68.04772  ?  1648 VAL   A CG2 1 
ATOM   13012 N  N   . ALA   A 1 1651 ? -41.92800  33.84000  -18.48100 1.000 75.00154  ?  1649 ALA   A N   1 
ATOM   13013 C  CA  . ALA   A 1 1651 ? -42.06300  34.81300  -19.55400 1.000 79.92449  ?  1649 ALA   A CA  1 
ATOM   13014 C  C   . ALA   A 1 1651 ? -41.47800  34.28400  -20.85500 1.000 91.12926  ?  1649 ALA   A C   1 
ATOM   13015 O  O   . ALA   A 1 1651 ? -40.39200  33.69700  -20.87300 1.000 96.11315  ?  1649 ALA   A O   1 
ATOM   13016 C  CB  . ALA   A 1 1651 ? -41.38500  36.13300  -19.18800 1.000 76.87329  ?  1649 ALA   A CB  1 
ATOM   13017 N  N   . ARG   A 1 1652 ? -42.21000  34.50000  -21.94000 1.000 97.34678  ?  1650 ARG   A N   1 
ATOM   13018 C  CA  . ARG   A 1 1652 ? -41.75400  34.24600  -23.29700 1.000 94.37211  ?  1650 ARG   A CA  1 
ATOM   13019 C  C   . ARG   A 1 1652 ? -41.77100  35.56100  -24.07200 1.000 99.97279  ?  1650 ARG   A C   1 
ATOM   13020 O  O   . ARG   A 1 1652 ? -42.11600  36.61800  -23.53700 1.000 111.67120 ?  1650 ARG   A O   1 
ATOM   13021 C  CB  . ARG   A 1 1652 ? -42.62100  33.18200  -23.97500 1.000 94.75501  ?  1650 ARG   A CB  1 
ATOM   13022 N  N   . ASN   A 1 1653 ? -41.39600  35.49400  -25.34700 1.000 97.62447  ?  1651 ASN   A N   1 
ATOM   13023 C  CA  . ASN   A 1 1653 ? -41.28600  36.68300  -26.17900 1.000 102.99038 ?  1651 ASN   A CA  1 
ATOM   13024 C  C   . ASN   A 1 1653 ? -41.99100  36.45500  -27.50700 1.000 114.51671 ?  1651 ASN   A C   1 
ATOM   13025 O  O   . ASN   A 1 1653 ? -41.85600  35.39100  -28.11900 1.000 112.23341 ?  1651 ASN   A O   1 
ATOM   13026 C  CB  . ASN   A 1 1653 ? -39.81900  37.05500  -26.41900 1.000 102.64130 ?  1651 ASN   A CB  1 
ATOM   13027 C  CG  . ASN   A 1 1653 ? -38.97000  36.90700  -25.17100 1.000 100.63361 ?  1651 ASN   A CG  1 
ATOM   13028 O  OD1 . ASN   A 1 1653 ? -39.12900  37.65300  -24.20500 1.000 98.71498  ?  1651 ASN   A OD1 1 
ATOM   13029 N  ND2 . ASN   A 1 1653 ? -38.06000  35.94000  -25.18800 1.000 98.95141  ?  1651 ASN   A ND2 1 
ATOM   13030 N  N   . ASP   A 1 1654 ? -42.73900  37.46200  -27.94900 1.000 112.41038 ?  1652 ASP   A N   1 
ATOM   13031 C  CA  . ASP   A 1 1654 ? -43.46300  37.38800  -29.21100 1.000 106.59699 ?  1652 ASP   A CA  1 
ATOM   13032 C  C   . ASP   A 1 1654 ? -42.88100  38.36100  -30.23100 1.000 98.28155  ?  1652 ASP   A C   1 
ATOM   13033 O  O   . ASP   A 1 1654 ? -43.59200  39.20700  -30.77400 1.000 88.31638  ?  1652 ASP   A O   1 
ATOM   13034 C  CB  . ASP   A 1 1654 ? -44.94200  37.66800  -28.99100 1.000 80.76217  ?  1652 ASP   A CB  1 
ATOM   13035 N  N   . ALA   A 1 1659 ? -42.27900  40.26100  -25.81700 1.000 73.52461  ?  1657 ALA   A N   1 
ATOM   13036 C  CA  . ALA   A 1 1659 ? -42.29800  39.94900  -24.39200 1.000 98.42897  ?  1657 ALA   A CA  1 
ATOM   13037 C  C   . ALA   A 1 1659 ? -43.72800  39.79900  -23.88000 1.000 102.92891 ?  1657 ALA   A C   1 
ATOM   13038 O  O   . ALA   A 1 1659 ? -44.54400  40.70900  -24.01800 1.000 97.53945  ?  1657 ALA   A O   1 
ATOM   13039 C  CB  . ALA   A 1 1659 ? -41.56600  41.02400  -23.60600 1.000 76.90716  ?  1657 ALA   A CB  1 
ATOM   13040 N  N   . TYR   A 1 1660 ? -44.02500  38.64500  -23.28700 1.000 94.96041  ?  1658 TYR   A N   1 
ATOM   13041 C  CA  . TYR   A 1 1660 ? -45.35100  38.39000  -22.74100 1.000 90.01627  ?  1658 TYR   A CA  1 
ATOM   13042 C  C   . TYR   A 1 1660 ? -45.24000  37.33900  -21.64800 1.000 90.79281  ?  1658 TYR   A C   1 
ATOM   13043 O  O   . TYR   A 1 1660 ? -44.30400  36.53600  -21.62400 1.000 92.95287  ?  1658 TYR   A O   1 
ATOM   13044 C  CB  . TYR   A 1 1660 ? -46.33500  37.94200  -23.83000 1.000 108.57026 ?  1658 TYR   A CB  1 
ATOM   13045 C  CG  . TYR   A 1 1660 ? -46.05000  36.57400  -24.41500 1.000 114.43217 ?  1658 TYR   A CG  1 
ATOM   13046 C  CD1 . TYR   A 1 1660 ? -45.12600  36.41200  -25.44000 1.000 106.87267 ?  1658 TYR   A CD1 1 
ATOM   13047 C  CD2 . TYR   A 1 1660 ? -46.71600  35.44500  -23.95000 1.000 116.19702 ?  1658 TYR   A CD2 1 
ATOM   13048 C  CE1 . TYR   A 1 1660 ? -44.86700  35.16300  -25.97900 1.000 121.06390 ?  1658 TYR   A CE1 1 
ATOM   13049 C  CE2 . TYR   A 1 1660 ? -46.46300  34.19300  -24.48300 1.000 122.17766 ?  1658 TYR   A CE2 1 
ATOM   13050 C  CZ  . TYR   A 1 1660 ? -45.53900  34.05800  -25.49700 1.000 127.01312 ?  1658 TYR   A CZ  1 
ATOM   13051 O  OH  . TYR   A 1 1660 ? -45.28400  32.81400  -26.03000 1.000 113.80758 ?  1658 TYR   A OH  1 
ATOM   13052 N  N   . LEU   A 1 1661 ? -46.21100  37.35800  -20.74000 1.000 88.54801  ?  1659 LEU   A N   1 
ATOM   13053 C  CA  . LEU   A 1 1661 ? -46.28200  36.40300  -19.64200 1.000 88.11335  ?  1659 LEU   A CA  1 
ATOM   13054 C  C   . LEU   A 1 1661 ? -47.27500  35.30200  -19.98500 1.000 107.18869 ?  1659 LEU   A C   1 
ATOM   13055 O  O   . LEU   A 1 1661 ? -48.38500  35.58300  -20.44900 1.000 111.11761 ?  1659 LEU   A O   1 
ATOM   13056 C  CB  . LEU   A 1 1661 ? -46.69100  37.09400  -18.34100 1.000 84.53348  ?  1659 LEU   A CB  1 
ATOM   13057 C  CG  . LEU   A 1 1661 ? -45.60100  37.88900  -17.62400 1.000 82.00427  ?  1659 LEU   A CG  1 
ATOM   13058 C  CD1 . LEU   A 1 1661 ? -46.17300  38.56600  -16.39200 1.000 68.26596  ?  1659 LEU   A CD1 1 
ATOM   13059 C  CD2 . LEU   A 1 1661 ? -44.44200  36.97900  -17.25000 1.000 85.79989  ?  1659 LEU   A CD2 1 
ATOM   13060 N  N   . CYS   A 1 1662 ? -46.87500  34.05400  -19.75000 1.000 111.05688 ?  1660 CYS   A N   1 
ATOM   13061 C  CA  . CYS   A 1 1662 ? -47.71600  32.90600  -20.05200 1.000 108.12652 ?  1660 CYS   A CA  1 
ATOM   13062 C  C   . CYS   A 1 1662 ? -47.66800  31.91700  -18.89700 1.000 99.28650  ?  1660 CYS   A C   1 
ATOM   13063 O  O   . CYS   A 1 1662 ? -46.70000  31.87500  -18.13400 1.000 75.33589  ?  1660 CYS   A O   1 
ATOM   13064 C  CB  . CYS   A 1 1662 ? -47.28500  32.21600  -21.35400 1.000 102.20409 ?  1660 CYS   A CB  1 
ATOM   13065 S  SG  . CYS   A 1 1662 ? -48.37900  30.87700  -21.88200 1.000 110.09239 ?  1660 CYS   A SG  1 
ATOM   13066 N  N   . ALA   A 1 1663 ? -48.72700  31.12300  -18.77800 1.000 99.68167  ?  1661 ALA   A N   1 
ATOM   13067 C  CA  . ALA   A 1 1663 ? -48.81700  30.11100  -17.73200 1.000 92.26461  ?  1661 ALA   A CA  1 
ATOM   13068 C  C   . ALA   A 1 1663 ? -49.57200  28.88400  -18.23000 1.000 91.50166  ?  1661 ALA   A C   1 
ATOM   13069 O  O   . ALA   A 1 1663 ? -50.66800  28.58300  -17.75700 1.000 113.52368 ?  1661 ALA   A O   1 
ATOM   13070 C  CB  . ALA   A 1 1663 ? -49.48900  30.68400  -16.49500 1.000 85.86142  ?  1661 ALA   A CB  1 
ATOM   13071 N  N   . GLN   A 1 1669 ? -58.20500  20.78800  -12.65300 1.000 92.70228  ?  1667 GLN   A N   1 
ATOM   13072 C  CA  . GLN   A 1 1669 ? -59.53400  20.21900  -12.45700 1.000 96.89491  ?  1667 GLN   A CA  1 
ATOM   13073 C  C   . GLN   A 1 1669 ? -60.61500  21.29000  -12.53100 1.000 110.27115 ?  1667 GLN   A C   1 
ATOM   13074 O  O   . GLN   A 1 1669 ? -61.45000  21.40300  -11.63100 1.000 110.29872 ?  1667 GLN   A O   1 
ATOM   13075 C  CB  . GLN   A 1 1669 ? -59.61200  19.49000  -11.11600 1.000 86.97997  ?  1667 GLN   A CB  1 
ATOM   13076 N  N   . GLU   A 1 1670 ? -60.59400  22.07200  -13.60700 1.000 121.34689 ?  1668 GLU   A N   1 
ATOM   13077 C  CA  . GLU   A 1 1670 ? -61.57000  23.13100  -13.82200 1.000 119.65676 ?  1668 GLU   A CA  1 
ATOM   13078 C  C   . GLU   A 1 1670 ? -61.41900  23.64800  -15.24500 1.000 117.04164 ?  1668 GLU   A C   1 
ATOM   13079 O  O   . GLU   A 1 1670 ? -60.32100  23.63300  -15.80900 1.000 101.38528 ?  1668 GLU   A O   1 
ATOM   13080 C  CB  . GLU   A 1 1670 ? -61.39200  24.27600  -12.81300 1.000 121.95943 ?  1668 GLU   A CB  1 
ATOM   13081 C  CG  . GLU   A 1 1670 ? -62.46800  25.34800  -12.89000 1.000 117.43388 ?  1668 GLU   A CG  1 
ATOM   13082 C  CD  . GLU   A 1 1670 ? -63.86400  24.76200  -12.97700 1.000 142.10320 ?  1668 GLU   A CD  1 
ATOM   13083 O  OE1 . GLU   A 1 1670 ? -64.21700  23.92500  -12.11800 1.000 152.88496 ?  1668 GLU   A OE1 1 
ATOM   13084 O  OE2 . GLU   A 1 1670 ? -64.60200  25.12700  -13.91600 1.000 158.64849 -1 1668 GLU   A OE2 1 
ATOM   13085 N  N   . TRP   A 1 1671 ? -62.54000  24.09800  -15.81800 1.000 123.80911 ?  1669 TRP   A N   1 
ATOM   13086 C  CA  . TRP   A 1 1671 ? -62.56500  24.70000  -17.14500 1.000 125.05042 ?  1669 TRP   A CA  1 
ATOM   13087 C  C   . TRP   A 1 1671 ? -62.32200  26.20600  -17.11000 1.000 124.84797 ?  1669 TRP   A C   1 
ATOM   13088 O  O   . TRP   A 1 1671 ? -62.82600  26.93200  -17.97900 1.000 124.99932 ?  1669 TRP   A O   1 
ATOM   13089 C  CB  . TRP   A 1 1671 ? -63.89400  24.39200  -17.83500 1.000 119.68458 ?  1669 TRP   A CB  1 
ATOM   13090 N  N   . THR   A 1 1672 ? -61.56400  26.69500  -16.12500 1.000 129.46964 ?  1670 THR   A N   1 
ATOM   13091 C  CA  . THR   A 1 1672 ? -61.20500  28.10700  -16.03600 1.000 120.35675 ?  1670 THR   A CA  1 
ATOM   13092 C  C   . THR   A 1 1672 ? -60.57600  28.61600  -17.33100 1.000 118.89054 ?  1670 THR   A C   1 
ATOM   13093 O  O   . THR   A 1 1672 ? -59.46900  28.20300  -17.69400 1.000 118.38707 ?  1670 THR   A O   1 
ATOM   13094 C  CB  . THR   A 1 1672 ? -60.24300  28.33300  -14.86400 1.000 108.75231 ?  1670 THR   A CB  1 
ATOM   13095 O  OG1 . THR   A 1 1672 ? -59.73200  27.07300  -14.40600 1.000 83.18165  ?  1670 THR   A OG1 1 
ATOM   13096 C  CG2 . THR   A 1 1672 ? -60.95700  29.02800  -13.71800 1.000 84.72562  ?  1670 THR   A CG2 1 
ATOM   13097 N  N   . VAL   A 1 1673 ? -61.27800  29.49800  -18.04200 1.000 115.22412 ?  1671 VAL   A N   1 
ATOM   13098 C  CA  . VAL   A 1 1673 ? -60.75300  30.14800  -19.24000 1.000 118.51534 ?  1671 VAL   A CA  1 
ATOM   13099 C  C   . VAL   A 1 1673 ? -61.06800  31.63900  -19.13400 1.000 112.36170 ?  1671 VAL   A C   1 
ATOM   13100 O  O   . VAL   A 1 1673 ? -62.23800  32.03800  -19.11800 1.000 121.75105 ?  1671 VAL   A O   1 
ATOM   13101 C  CB  . VAL   A 1 1673 ? -61.30600  29.53000  -20.54100 1.000 117.59148 ?  1671 VAL   A CB  1 
ATOM   13102 C  CG1 . VAL   A 1 1673 ? -60.88600  28.07100  -20.63700 1.000 100.88751 ?  1671 VAL   A CG1 1 
ATOM   13103 C  CG2 . VAL   A 1 1673 ? -62.83100  29.63800  -20.64500 1.000 110.14020 ?  1671 VAL   A CG2 1 
ATOM   13104 N  N   . GLY   A 1 1674 ? -60.02900  32.46000  -19.00300 1.000 102.40586 ?  1672 GLY   A N   1 
ATOM   13105 C  CA  . GLY   A 1 1674 ? -60.20500  33.88900  -18.80900 1.000 95.11277  ?  1672 GLY   A CA  1 
ATOM   13106 C  C   . GLY   A 1 1674 ? -60.89100  34.28500  -17.51200 1.000 111.25196 ?  1672 GLY   A C   1 
ATOM   13107 O  O   . GLY   A 1 1674 ? -60.83200  35.45400  -17.11400 1.000 106.50643 ?  1672 GLY   A O   1 
ATOM   13108 N  N   . GLN   A 1 1675 ? -61.57000  33.33600  -16.85600 1.000 117.80379 ?  1673 GLN   A N   1 
ATOM   13109 C  CA  . GLN   A 1 1675 ? -62.08400  33.58100  -15.51100 1.000 107.87174 ?  1673 GLN   A CA  1 
ATOM   13110 C  C   . GLN   A 1 1675 ? -60.95400  33.65400  -14.49200 1.000 118.46055 ?  1673 GLN   A C   1 
ATOM   13111 O  O   . GLN   A 1 1675 ? -61.06400  34.38100  -13.49700 1.000 120.58414 ?  1673 GLN   A O   1 
ATOM   13112 C  CB  . GLN   A 1 1675 ? -63.07900  32.48900  -15.11500 1.000 87.33850  ?  1673 GLN   A CB  1 
ATOM   13113 N  N   . LEU   A 1 1676 ? -59.86400  32.90900  -14.71800 1.000 109.47265 ?  1674 LEU   A N   1 
ATOM   13114 C  CA  . LEU   A 1 1676 ? -58.68800  33.03900  -13.86500 1.000 83.65830  ?  1674 LEU   A CA  1 
ATOM   13115 C  C   . LEU   A 1 1676 ? -58.14100  34.46000  -13.88200 1.000 96.20087  ?  1674 LEU   A C   1 
ATOM   13116 O  O   . LEU   A 1 1676 ? -57.48600  34.88100  -12.92300 1.000 103.34305 ?  1674 LEU   A O   1 
ATOM   13117 C  CB  . LEU   A 1 1676 ? -57.60900  32.04800  -14.30000 1.000 71.23534  ?  1674 LEU   A CB  1 
ATOM   13118 N  N   . ARG   A 1 1677 ? -58.38600  35.20700  -14.96400 1.000 97.82360  ?  1675 ARG   A N   1 
ATOM   13119 C  CA  . ARG   A 1 1677 ? -58.03400  36.62400  -14.97600 1.000 96.32548  ?  1675 ARG   A CA  1 
ATOM   13120 C  C   . ARG   A 1 1677 ? -58.82600  37.38900  -13.92600 1.000 100.92609 ?  1675 ARG   A C   1 
ATOM   13121 O  O   . ARG   A 1 1677 ? -58.27700  38.25600  -13.23600 1.000 103.48965 ?  1675 ARG   A O   1 
ATOM   13122 C  CB  . ARG   A 1 1677 ? -58.27600  37.22600  -16.36000 1.000 83.41340  ?  1675 ARG   A CB  1 
ATOM   13123 C  CG  . ARG   A 1 1677 ? -57.57000  36.49800  -17.48000 1.000 92.87627  ?  1675 ARG   A CG  1 
ATOM   13124 C  CD  . ARG   A 1 1677 ? -57.54800  37.28900  -18.77900 1.000 98.52854  ?  1675 ARG   A CD  1 
ATOM   13125 N  NE  . ARG   A 1 1677 ? -56.96100  38.61400  -18.61500 1.000 95.74841  ?  1675 ARG   A NE  1 
ATOM   13126 C  CZ  . ARG   A 1 1677 ? -57.65900  39.74100  -18.60500 1.000 101.29214 ?  1675 ARG   A CZ  1 
ATOM   13127 N  NH1 . ARG   A 1 1677 ? -58.97200  39.74100  -18.77000 1.000 100.79503 ?  1675 ARG   A NH1 1 
ATOM   13128 N  NH2 . ARG   A 1 1677 ? -57.02500  40.89600  -18.42700 1.000 104.38962 ?  1675 ARG   A NH2 1 
ATOM   13129 N  N   . GLU   A 1 1678 ? -60.12200  37.08800  -13.79700 1.000 103.33160 ?  1676 GLU   A N   1 
ATOM   13130 C  CA  . GLU   A 1 1678 ? -60.92900  37.72000  -12.75900 1.000 103.21213 ?  1676 GLU   A CA  1 
ATOM   13131 C  C   . GLU   A 1 1678 ? -60.42500  37.36200  -11.36700 1.000 98.68064  ?  1676 GLU   A C   1 
ATOM   13132 O  O   . GLU   A 1 1678 ? -60.49200  38.19000  -10.45100 1.000 84.65991  ?  1676 GLU   A O   1 
ATOM   13133 C  CB  . GLU   A 1 1678 ? -62.39500  37.31500  -12.91400 1.000 73.14233  ?  1676 GLU   A CB  1 
ATOM   13134 N  N   . LEU   A 1 1679 ? -59.92300  36.13700  -11.18800 1.000 97.04904  ?  1677 LEU   A N   1 
ATOM   13135 C  CA  . LEU   A 1 1679 ? -59.31100  35.77000  -9.91600  1.000 94.59550  ?  1677 LEU   A CA  1 
ATOM   13136 C  C   . LEU   A 1 1679 ? -58.01000  36.53000  -9.69700  1.000 92.98213  ?  1677 LEU   A C   1 
ATOM   13137 O  O   . LEU   A 1 1679 ? -57.74500  37.01200  -8.59000  1.000 94.42336  ?  1677 LEU   A O   1 
ATOM   13138 C  CB  . LEU   A 1 1679 ? -59.07200  34.25900  -9.86700  1.000 90.69746  ?  1677 LEU   A CB  1 
ATOM   13139 C  CG  . LEU   A 1 1679 ? -58.28400  33.69600  -8.68200  1.000 97.14961  ?  1677 LEU   A CG  1 
ATOM   13140 C  CD1 . LEU   A 1 1679 ? -58.86700  34.16900  -7.35800  1.000 88.19877  ?  1677 LEU   A CD1 1 
ATOM   13141 C  CD2 . LEU   A 1 1679 ? -58.25700  32.17600  -8.74100  1.000 67.64416  ?  1677 LEU   A CD2 1 
ATOM   13142 N  N   . LEU   A 1 1680 ? -57.19100  36.65300  -10.73800 1.000 93.61054  ?  1678 LEU   A N   1 
ATOM   13143 C  CA  . LEU   A 1 1680 ? -55.93600  37.38900  -10.66400 1.000 91.31138  ?  1678 LEU   A CA  1 
ATOM   13144 C  C   . LEU   A 1 1680 ? -56.12000  38.89100  -10.84600 1.000 87.20299  ?  1678 LEU   A C   1 
ATOM   13145 O  O   . LEU   A 1 1680 ? -55.12300  39.61400  -10.94000 1.000 86.27240  ?  1678 LEU   A O   1 
ATOM   13146 C  CB  . LEU   A 1 1680 ? -54.95100  36.85200  -11.70600 1.000 86.76982  ?  1678 LEU   A CB  1 
ATOM   13147 C  CG  . LEU   A 1 1680 ? -53.93500  35.80700  -11.23100 1.000 81.88260  ?  1678 LEU   A CG  1 
ATOM   13148 C  CD1 . LEU   A 1 1680 ? -54.58600  34.74100  -10.36000 1.000 85.85172  ?  1678 LEU   A CD1 1 
ATOM   13149 C  CD2 . LEU   A 1 1680 ? -53.23600  35.16700  -12.41900 1.000 84.27123  ?  1678 LEU   A CD2 1 
ATOM   13150 N  N   . ARG   A 1 1681 ? -57.36100  39.37300  -10.90000 1.000 93.34920  ?  1679 ARG   A N   1 
ATOM   13151 C  CA  . ARG   A 1 1681 ? -57.62300  40.80000  -11.03800 1.000 85.60230  ?  1679 ARG   A CA  1 
ATOM   13152 C  C   . ARG   A 1 1681 ? -57.85000  41.47500  -9.69100  1.000 89.31916  ?  1679 ARG   A C   1 
ATOM   13153 O  O   . ARG   A 1 1681 ? -57.43900  42.62500  -9.49900  1.000 84.94176  ?  1679 ARG   A O   1 
ATOM   13154 C  CB  . ARG   A 1 1681 ? -58.83300  41.02800  -11.95100 1.000 90.99188  ?  1679 ARG   A CB  1 
ATOM   13155 C  CG  . ARG   A 1 1681 ? -59.06200  42.48000  -12.33600 1.000 95.30999  ?  1679 ARG   A CG  1 
ATOM   13156 C  CD  . ARG   A 1 1681 ? -60.15400  42.62700  -13.39100 1.000 92.84135  ?  1679 ARG   A CD  1 
ATOM   13157 N  NE  . ARG   A 1 1681 ? -59.61300  43.02100  -14.68700 1.000 108.52184 ?  1679 ARG   A NE  1 
ATOM   13158 C  CZ  . ARG   A 1 1681 ? -59.66700  42.28000  -15.78500 1.000 111.73169 ?  1679 ARG   A CZ  1 
ATOM   13159 N  NH1 . ARG   A 1 1681 ? -60.26900  41.10200  -15.79600 1.000 99.62202  ?  1679 ARG   A NH1 1 
ATOM   13160 N  NH2 . ARG   A 1 1681 ? -59.10900  42.73600  -16.90300 1.000 100.05603 ?  1679 ARG   A NH2 1 
ATOM   13161 N  N   . ARG   A 1 1682 ? -58.48900  40.77900  -8.75100  1.000 86.09430  ?  1680 ARG   A N   1 
ATOM   13162 C  CA  . ARG   A 1 1682 ? -58.77200  41.33000  -7.43100  1.000 80.38397  ?  1680 ARG   A CA  1 
ATOM   13163 C  C   . ARG   A 1 1682 ? -57.60000  41.20900  -6.46600  1.000 91.73810  ?  1680 ARG   A C   1 
ATOM   13164 O  O   . ARG   A 1 1682 ? -57.74500  41.57000  -5.29300  1.000 98.62476  ?  1680 ARG   A O   1 
ATOM   13165 C  CB  . ARG   A 1 1682 ? -60.00500  40.64700  -6.83200  1.000 67.90311  ?  1680 ARG   A CB  1 
ATOM   13166 N  N   . GLU   A 1 1683 ? -56.45200  40.71200  -6.92300  1.000 91.20940  ?  1681 GLU   A N   1 
ATOM   13167 C  CA  . GLU   A 1 1683 ? -55.26600  40.59700  -6.07700  1.000 85.30504  ?  1681 GLU   A CA  1 
ATOM   13168 C  C   . GLU   A 1 1683 ? -53.98300  41.06900  -6.74000  1.000 82.87855  ?  1681 GLU   A C   1 
ATOM   13169 O  O   . GLU   A 1 1683 ? -53.05200  41.45300  -6.02300  1.000 78.72032  ?  1681 GLU   A O   1 
ATOM   13170 C  CB  . GLU   A 1 1683 ? -55.07300  39.14600  -5.61700  1.000 98.85709  ?  1681 GLU   A CB  1 
ATOM   13171 C  CG  . GLU   A 1 1683 ? -56.11900  38.64400  -4.63200  1.000 96.30301  ?  1681 GLU   A CG  1 
ATOM   13172 C  CD  . GLU   A 1 1683 ? -55.58400  38.53900  -3.21600  1.000 104.00115 ?  1681 GLU   A CD  1 
ATOM   13173 O  OE1 . GLU   A 1 1683 ? -55.32400  39.59000  -2.59300  1.000 112.20460 ?  1681 GLU   A OE1 1 
ATOM   13174 O  OE2 . GLU   A 1 1683 ? -55.41500  37.40100  -2.72900  1.000 99.35370  ?  1681 GLU   A OE2 1 
ATOM   13175 N  N   . LEU   A 1 1684 ? -53.88700  41.06200  -8.06700  1.000 83.67913  ?  1682 LEU   A N   1 
ATOM   13176 C  CA  . LEU   A 1 1684 ? -52.67800  41.41400  -8.78400  1.000 88.32526  ?  1682 LEU   A CA  1 
ATOM   13177 C  C   . LEU   A 1 1684 ? -52.95400  42.53900  -9.77400  1.000 87.46350  ?  1682 LEU   A C   1 
ATOM   13178 O  O   . LEU   A 1 1684 ? -54.07200  42.66200  -10.28300 1.000 74.75848  ?  1682 LEU   A O   1 
ATOM   13179 C  CB  . LEU   A 1 1684 ? -52.11400  40.19900  -9.53200  1.000 82.24138  ?  1682 LEU   A CB  1 
ATOM   13180 C  CG  . LEU   A 1 1684 ? -51.49300  39.12100  -8.64200  1.000 82.35012  ?  1682 LEU   A CG  1 
ATOM   13181 C  CD1 . LEU   A 1 1684 ? -51.54000  37.77400  -9.32700  1.000 72.77388  ?  1682 LEU   A CD1 1 
ATOM   13182 C  CD2 . LEU   A 1 1684 ? -50.06000  39.47800  -8.28100  1.000 85.29823  ?  1682 LEU   A CD2 1 
ATOM   13183 N  N   . PRO   A 1 1685 ? -51.96100  43.37800  -10.05800 1.000 97.11727  ?  1683 PRO   A N   1 
ATOM   13184 C  CA  . PRO   A 1 1685 ? -52.15700  44.44400  -11.04500 1.000 86.03743  ?  1683 PRO   A CA  1 
ATOM   13185 C  C   . PRO   A 1 1685 ? -52.17800  43.88500  -12.45900 1.000 84.13585  ?  1683 PRO   A C   1 
ATOM   13186 O  O   . PRO   A 1 1685 ? -51.70300  42.78100  -12.73000 1.000 97.90445  ?  1683 PRO   A O   1 
ATOM   13187 C  CB  . PRO   A 1 1685 ? -50.94600  45.36100  -10.83400 1.000 71.40274  ?  1683 PRO   A CB  1 
ATOM   13188 C  CG  . PRO   A 1 1685 ? -50.29700  44.89500  -9.55700  1.000 74.57372  ?  1683 PRO   A CG  1 
ATOM   13189 C  CD  . PRO   A 1 1685 ? -50.63200  43.44800  -9.43500  1.000 84.91161  ?  1683 PRO   A CD  1 
ATOM   13190 N  N   . GLU   A 1 1686 ? -52.73600  44.68100  -13.37400 1.000 79.10409  ?  1684 GLU   A N   1 
ATOM   13191 C  CA  . GLU   A 1 1686 ? -52.93400  44.21100  -14.74200 1.000 83.27933  ?  1684 GLU   A CA  1 
ATOM   13192 C  C   . GLU   A 1 1686 ? -51.60900  43.91900  -15.44100 1.000 82.48904  ?  1684 GLU   A C   1 
ATOM   13193 O  O   . GLU   A 1 1686 ? -51.55700  43.07100  -16.33900 1.000 81.35698  ?  1684 GLU   A O   1 
ATOM   13194 C  CB  . GLU   A 1 1686 ? -53.74300  45.23500  -15.53800 1.000 94.02914  ?  1684 GLU   A CB  1 
ATOM   13195 C  CG  . GLU   A 1 1686 ? -55.18600  45.39600  -15.06400 1.000 88.93366  ?  1684 GLU   A CG  1 
ATOM   13196 C  CD  . GLU   A 1 1686 ? -56.04700  44.17300  -15.33700 1.000 102.31978 ?  1684 GLU   A CD  1 
ATOM   13197 O  OE1 . GLU   A 1 1686 ? -55.94600  43.60500  -16.44300 1.000 101.78271 ?  1684 GLU   A OE1 1 
ATOM   13198 O  OE2 . GLU   A 1 1686 ? -56.83000  43.78400  -14.44400 1.000 98.58448  -1 1684 GLU   A OE2 1 
ATOM   13199 N  N   . TYR   A 1 1687 ? -50.52500  44.59400  -15.04600 1.000 87.44341  ?  1685 TYR   A N   1 
ATOM   13200 C  CA  . TYR   A 1 1687 ? -49.22500  44.29300  -15.63500 1.000 76.47315  ?  1685 TYR   A CA  1 
ATOM   13201 C  C   . TYR   A 1 1687 ? -48.61700  43.00600  -15.09500 1.000 73.87653  ?  1685 TYR   A C   1 
ATOM   13202 O  O   . TYR   A 1 1687 ? -47.64000  42.51700  -15.67000 1.000 80.70209  ?  1685 TYR   A O   1 
ATOM   13203 C  CB  . TYR   A 1 1687 ? -48.25800  45.46300  -15.42600 1.000 62.07496  ?  1685 TYR   A CB  1 
ATOM   13204 C  CG  . TYR   A 1 1687 ? -47.91300  45.78800  -13.98800 1.000 84.07359  ?  1685 TYR   A CG  1 
ATOM   13205 C  CD1 . TYR   A 1 1687 ? -46.84200  45.16900  -13.35200 1.000 92.12648  ?  1685 TYR   A CD1 1 
ATOM   13206 C  CD2 . TYR   A 1 1687 ? -48.63900  46.73700  -13.27600 1.000 93.09190  ?  1685 TYR   A CD2 1 
ATOM   13207 C  CE1 . TYR   A 1 1687 ? -46.51600  45.47100  -12.04000 1.000 92.05125  ?  1685 TYR   A CE1 1 
ATOM   13208 C  CE2 . TYR   A 1 1687 ? -48.31800  47.04900  -11.96600 1.000 92.34559  ?  1685 TYR   A CE2 1 
ATOM   13209 C  CZ  . TYR   A 1 1687 ? -47.25700  46.41200  -11.35200 1.000 93.18274  ?  1685 TYR   A CZ  1 
ATOM   13210 O  OH  . TYR   A 1 1687 ? -46.93700  46.71800  -10.04800 1.000 78.64602  ?  1685 TYR   A OH  1 
ATOM   13211 N  N   . MET   A 1 1688 ? -49.16700  42.44500  -14.01800 1.000 75.59503  ?  1686 MET   A N   1 
ATOM   13212 C  CA  . MET   A 1 1688 ? -48.74600  41.14600  -13.50800 1.000 76.76883  ?  1686 MET   A CA  1 
ATOM   13213 C  C   . MET   A 1 1688 ? -49.85300  40.10100  -13.63300 1.000 79.09034  ?  1686 MET   A C   1 
ATOM   13214 O  O   . MET   A 1 1688 ? -49.97200  39.20600  -12.79200 1.000 97.41611  ?  1686 MET   A O   1 
ATOM   13215 C  CB  . MET   A 1 1688 ? -48.25400  41.26500  -12.06400 1.000 75.48724  ?  1686 MET   A CB  1 
ATOM   13216 C  CG  . MET   A 1 1688 ? -46.74800  41.51900  -11.98100 1.000 84.04260  ?  1686 MET   A CG  1 
ATOM   13217 S  SD  . MET   A 1 1688 ? -45.97100  41.81500  -10.37500 1.000 119.18522 ?  1686 MET   A SD  1 
ATOM   13218 C  CE  . MET   A 1 1688 ? -47.29500  41.43900  -9.24000  1.000 86.76253  ?  1686 MET   A CE  1 
ATOM   13219 N  N   . ILE   A 1 1689 ? -50.66500  40.20500  -14.67500 1.000 81.84449  ?  1687 ILE   A N   1 
ATOM   13220 C  CA  . ILE   A 1 1689 ? -51.61500  39.16200  -15.06000 1.000 86.20221  ?  1687 ILE   A CA  1 
ATOM   13221 C  C   . ILE   A 1 1689 ? -51.07900  38.48400  -16.31300 1.000 90.03588  ?  1687 ILE   A C   1 
ATOM   13222 O  O   . ILE   A 1 1689 ? -50.74100  39.17800  -17.27900 1.000 72.93009  ?  1687 ILE   A O   1 
ATOM   13223 C  CB  . ILE   A 1 1689 ? -53.02700  39.72200  -15.31700 1.000 84.53363  ?  1687 ILE   A CB  1 
ATOM   13224 C  CG1 . ILE   A 1 1689 ? -53.40700  40.74300  -14.25300 1.000 88.81307  ?  1687 ILE   A CG1 1 
ATOM   13225 C  CG2 . ILE   A 1 1689 ? -54.05400  38.60600  -15.29100 1.000 84.80791  ?  1687 ILE   A CG2 1 
ATOM   13226 C  CD1 . ILE   A 1 1689 ? -54.84400  41.18900  -14.36200 1.000 80.26630  ?  1687 ILE   A CD1 1 
ATOM   13227 N  N   . PRO   A 1 1690 ? -50.96900  37.15600  -16.33800 1.000 102.11011 ?  1688 PRO   A N   1 
ATOM   13228 C  CA  . PRO   A 1 1690 ? -50.48800  36.47400  -17.54900 1.000 80.77267  ?  1688 PRO   A CA  1 
ATOM   13229 C  C   . PRO   A 1 1690 ? -51.48200  36.67400  -18.68400 1.000 94.48185  ?  1688 PRO   A C   1 
ATOM   13230 O  O   . PRO   A 1 1690 ? -52.67900  36.43000  -18.51700 1.000 96.04312  ?  1688 PRO   A O   1 
ATOM   13231 C  CB  . PRO   A 1 1690 ? -50.40400  35.00300  -17.11900 1.000 89.31873  ?  1688 PRO   A CB  1 
ATOM   13232 C  CG  . PRO   A 1 1690 ? -50.48000  35.02000  -15.60700 1.000 95.04329  ?  1688 PRO   A CG  1 
ATOM   13233 C  CD  . PRO   A 1 1690 ? -51.31000  36.20900  -15.26400 1.000 97.00429  ?  1688 PRO   A CD  1 
ATOM   13234 N  N   . ALA   A 1 1691 ? -50.99100  37.14300  -19.83500 1.000 104.05926 ?  1689 ALA   A N   1 
ATOM   13235 C  CA  . ALA   A 1 1691 ? -51.88900  37.33800  -20.96900 1.000 101.87013 ?  1689 ALA   A CA  1 
ATOM   13236 C  C   . ALA   A 1 1691 ? -52.44600  36.00300  -21.44400 1.000 113.39998 ?  1689 ALA   A C   1 
ATOM   13237 O  O   . ALA   A 1 1691 ? -53.66500  35.80300  -21.49300 1.000 116.57111 ?  1689 ALA   A O   1 
ATOM   13238 C  CB  . ALA   A 1 1691 ? -51.17500  38.06500  -22.10600 1.000 89.27782  ?  1689 ALA   A CB  1 
ATOM   13239 N  N   . HIS   A 1 1692 ? -51.56100  35.07000  -21.78700 1.000 114.06435 ?  1690 HIS   A N   1 
ATOM   13240 C  CA  . HIS   A 1 1692 ? -51.93900  33.73200  -22.22200 1.000 106.38184 ?  1690 HIS   A CA  1 
ATOM   13241 C  C   . HIS   A 1 1692 ? -51.81500  32.76900  -21.04900 1.000 109.48726 ?  1690 HIS   A C   1 
ATOM   13242 O  O   . HIS   A 1 1692 ? -50.82400  32.80700  -20.31400 1.000 106.49908 ?  1690 HIS   A O   1 
ATOM   13243 C  CB  . HIS   A 1 1692 ? -51.05700  33.27100  -23.38400 1.000 92.99563  ?  1690 HIS   A CB  1 
ATOM   13244 C  CG  . HIS   A 1 1692 ? -51.09000  34.18600  -24.56800 1.000 111.26112 ?  1690 HIS   A CG  1 
ATOM   13245 N  ND1 . HIS   A 1 1692 ? -52.25000  34.77900  -25.01700 1.000 109.55774 ?  1690 HIS   A ND1 1 
ATOM   13246 C  CD2 . HIS   A 1 1692 ? -50.10500  34.61300  -25.39300 1.000 120.44376 ?  1690 HIS   A CD2 1 
ATOM   13247 C  CE1 . HIS   A 1 1692 ? -51.97900  35.52900  -26.07100 1.000 111.72011 ?  1690 HIS   A CE1 1 
ATOM   13248 N  NE2 . HIS   A 1 1692 ? -50.68400  35.44600  -26.31900 1.000 105.13821 ?  1690 HIS   A NE2 1 
ATOM   13249 N  N   . PHE   A 1 1693 ? -52.82100  31.91900  -20.86800 1.000 110.09018 ?  1691 PHE   A N   1 
ATOM   13250 C  CA  . PHE   A 1 1693 ? -52.82100  30.96500  -19.76100 1.000 92.28206  ?  1691 PHE   A CA  1 
ATOM   13251 C  C   . PHE   A 1 1693 ? -52.58600  29.55800  -20.28300 1.000 87.66500  ?  1691 PHE   A C   1 
ATOM   13252 O  O   . PHE   A 1 1693 ? -53.29600  29.09800  -21.17600 1.000 98.62527  ?  1691 PHE   A O   1 
ATOM   13253 C  CB  . PHE   A 1 1693 ? -54.13900  31.01100  -18.98200 1.000 87.72334  ?  1691 PHE   A CB  1 
ATOM   13254 C  CG  . PHE   A 1 1693 ? -54.36500  32.29200  -18.23300 1.000 94.99499  ?  1691 PHE   A CG  1 
ATOM   13255 C  CD1 . PHE   A 1 1693 ? -54.68300  33.45400  -18.91300 1.000 102.63538 ?  1691 PHE   A CD1 1 
ATOM   13256 C  CD2 . PHE   A 1 1693 ? -54.27600  32.33100  -16.84900 1.000 93.21874  ?  1691 PHE   A CD2 1 
ATOM   13257 C  CE1 . PHE   A 1 1693 ? -54.88900  34.63000  -18.24000 1.000 114.33982 ?  1691 PHE   A CE1 1 
ATOM   13258 C  CE2 . PHE   A 1 1693 ? -54.49200  33.51000  -16.16200 1.000 98.61187  ?  1691 PHE   A CE2 1 
ATOM   13259 C  CZ  . PHE   A 1 1693 ? -54.80100  34.66100  -16.86000 1.000 111.30935 ?  1691 PHE   A CZ  1 
ATOM   13260 N  N   . ALA   A 1 1726 ? -72.31400  36.99700  -24.35100 1.000 88.91122  ?  1724 ALA   A N   1 
ATOM   13261 C  CA  . ALA   A 1 1726 ? -73.41200  37.79300  -23.81700 1.000 98.02971  ?  1724 ALA   A CA  1 
ATOM   13262 C  C   . ALA   A 1 1726 ? -74.58100  36.90500  -23.41100 1.000 101.20697 ?  1724 ALA   A C   1 
ATOM   13263 O  O   . ALA   A 1 1726 ? -75.16700  36.21700  -24.24800 1.000 90.00919  ?  1724 ALA   A O   1 
ATOM   13264 C  CB  . ALA   A 1 1726 ? -73.86300  38.82900  -24.83700 1.000 74.70499  ?  1724 ALA   A CB  1 
ATOM   13265 N  N   . ALA   A 1 1727 ? -74.91900  36.91900  -22.12300 1.000 108.08365 ?  1725 ALA   A N   1 
ATOM   13266 C  CA  . ALA   A 1 1727 ? -76.04700  36.15000  -21.59500 1.000 100.67893 ?  1725 ALA   A CA  1 
ATOM   13267 C  C   . ALA   A 1 1727 ? -76.77600  36.96300  -20.53300 1.000 96.51830  ?  1725 ALA   A C   1 
ATOM   13268 O  O   . ALA   A 1 1727 ? -76.75900  36.62100  -19.34400 1.000 93.84065  ?  1725 ALA   A O   1 
ATOM   13269 C  CB  . ALA   A 1 1727 ? -75.57000  34.80900  -21.03200 1.000 93.21217  ?  1725 ALA   A CB  1 
ATOM   13270 N  N   . PRO   A 1 1728 ? -77.43700  38.05400  -20.93000 1.000 92.75278  ?  1726 PRO   A N   1 
ATOM   13271 C  CA  . PRO   A 1 1728 ? -78.25100  38.80600  -19.96300 1.000 92.86613  ?  1726 PRO   A CA  1 
ATOM   13272 C  C   . PRO   A 1 1728 ? -79.44300  37.97400  -19.51200 1.000 90.95540  ?  1726 PRO   A C   1 
ATOM   13273 O  O   . PRO   A 1 1728 ? -80.14600  37.37600  -20.33000 1.000 87.47489  ?  1726 PRO   A O   1 
ATOM   13274 C  CB  . PRO   A 1 1728 ? -78.68900  40.04800  -20.75100 1.000 79.78053  ?  1726 PRO   A CB  1 
ATOM   13275 C  CG  . PRO   A 1 1728 ? -77.74500  40.12600  -21.91400 1.000 71.64288  ?  1726 PRO   A CG  1 
ATOM   13276 C  CD  . PRO   A 1 1728 ? -77.43200  38.70300  -22.25100 1.000 93.84126  ?  1726 PRO   A CD  1 
ATOM   13277 N  N   . ARG   A 1 1729 ? -79.67000  37.94600  -18.20000 1.000 88.44394  ?  1727 ARG   A N   1 
ATOM   13278 C  CA  . ARG   A 1 1729 ? -80.61700  37.01700  -17.59400 1.000 92.39495  ?  1727 ARG   A CA  1 
ATOM   13279 C  C   . ARG   A 1 1729 ? -81.96000  37.65900  -17.26000 1.000 106.59360 ?  1727 ARG   A C   1 
ATOM   13280 O  O   . ARG   A 1 1729 ? -83.00700  37.13800  -17.65400 1.000 110.53377 ?  1727 ARG   A O   1 
ATOM   13281 C  CB  . ARG   A 1 1729 ? -79.98800  36.39800  -16.34000 1.000 91.90028  ?  1727 ARG   A CB  1 
ATOM   13282 C  CG  . ARG   A 1 1729 ? -78.59800  35.83100  -16.60500 1.000 90.38044  ?  1727 ARG   A CG  1 
ATOM   13283 C  CD  . ARG   A 1 1729 ? -78.05600  35.00900  -15.44500 1.000 80.91079  ?  1727 ARG   A CD  1 
ATOM   13284 N  NE  . ARG   A 1 1729 ? -77.52000  35.83200  -14.36900 1.000 98.73615  ?  1727 ARG   A NE  1 
ATOM   13285 C  CZ  . ARG   A 1 1729 ? -76.65700  35.40000  -13.45800 1.000 112.80969 ?  1727 ARG   A CZ  1 
ATOM   13286 N  NH1 . ARG   A 1 1729 ? -76.19100  34.16100  -13.48200 1.000 115.56262 ?  1727 ARG   A NH1 1 
ATOM   13287 N  NH2 . ARG   A 1 1729 ? -76.24800  36.23100  -12.50400 1.000 105.49110 ?  1727 ARG   A NH2 1 
ATOM   13288 N  N   . THR   A 1 1730 ? -81.95700  38.77800  -16.54400 1.000 105.33110 ?  1728 THR   A N   1 
ATOM   13289 C  CA  . THR   A 1 1730 ? -83.18100  39.46900  -16.16400 1.000 99.27039  ?  1728 THR   A CA  1 
ATOM   13290 C  C   . THR   A 1 1730 ? -83.33000  40.76100  -16.95700 1.000 104.58212 ?  1728 THR   A C   1 
ATOM   13291 O  O   . THR   A 1 1730 ? -82.44500  41.16100  -17.71900 1.000 93.38577  ?  1728 THR   A O   1 
ATOM   13292 C  CB  . THR   A 1 1730 ? -83.19900  39.76400  -14.65900 1.000 85.58902  ?  1728 THR   A CB  1 
ATOM   13293 O  OG1 . THR   A 1 1730 ? -84.34400  40.56500  -14.33900 1.000 88.49159  ?  1728 THR   A OG1 1 
ATOM   13294 C  CG2 . THR   A 1 1730 ? -81.93700  40.50300  -14.24500 1.000 69.81100  ?  1728 THR   A CG2 1 
ATOM   13295 N  N   . GLU   A 1 1731 ? -84.48100  41.41500  -16.77100 1.000 100.27620 ?  1729 GLU   A N   1 
ATOM   13296 C  CA  . GLU   A 1 1731 ? -84.71700  42.69300  -17.43500 1.000 93.00390  ?  1729 GLU   A CA  1 
ATOM   13297 C  C   . GLU   A 1 1731 ? -83.74000  43.75900  -16.96000 1.000 84.17842  ?  1729 GLU   A C   1 
ATOM   13298 O  O   . GLU   A 1 1731 ? -83.34600  44.63200  -17.74100 1.000 68.05535  ?  1729 GLU   A O   1 
ATOM   13299 C  CB  . GLU   A 1 1731 ? -86.15500  43.15700  -17.20100 1.000 87.27172  ?  1729 GLU   A CB  1 
ATOM   13300 C  CG  . GLU   A 1 1731 ? -87.20600  42.30300  -17.88100 1.000 94.41730  ?  1729 GLU   A CG  1 
ATOM   13301 C  CD  . GLU   A 1 1731 ? -88.27900  43.13700  -18.55100 1.000 105.82517 ?  1729 GLU   A CD  1 
ATOM   13302 O  OE1 . GLU   A 1 1731 ? -88.03500  44.34000  -18.78500 1.000 113.24232 ?  1729 GLU   A OE1 1 
ATOM   13303 O  OE2 . GLU   A 1 1731 ? -89.36400  42.59300  -18.84300 1.000 103.82098 -1 1729 GLU   A OE2 1 
ATOM   13304 N  N   . LEU   A 1 1732 ? -83.34200  43.70500  -15.68700 1.000 83.26151  ?  1730 LEU   A N   1 
ATOM   13305 C  CA  . LEU   A 1 1732 ? -82.37400  44.66700  -15.17100 1.000 85.02535  ?  1730 LEU   A CA  1 
ATOM   13306 C  C   . LEU   A 1 1732 ? -81.02100  44.50000  -15.85300 1.000 93.70561  ?  1730 LEU   A C   1 
ATOM   13307 O  O   . LEU   A 1 1732 ? -80.44900  45.47100  -16.36300 1.000 87.46530  ?  1730 LEU   A O   1 
ATOM   13308 C  CB  . LEU   A 1 1732 ? -82.24800  44.51200  -13.65500 1.000 63.25922  ?  1730 LEU   A CB  1 
ATOM   13309 C  CG  . LEU   A 1 1732 ? -81.28100  45.43500  -12.91200 1.000 61.94421  ?  1730 LEU   A CG  1 
ATOM   13310 C  CD1 . LEU   A 1 1732 ? -81.43100  46.87900  -13.36900 1.000 49.33899  ?  1730 LEU   A CD1 1 
ATOM   13311 C  CD2 . LEU   A 1 1732 ? -81.51300  45.32400  -11.41500 1.000 56.90150  ?  1730 LEU   A CD2 1 
ATOM   13312 N  N   . GLU   A 1 1733 ? -80.49700  43.27100  -15.88100 1.000 94.69081  ?  1731 GLU   A N   1 
ATOM   13313 C  CA  . GLU   A 1 1733 ? -79.22600  43.02600  -16.55500 1.000 84.02545  ?  1731 GLU   A CA  1 
ATOM   13314 C  C   . GLU   A 1 1733 ? -79.32500  43.28800  -18.05100 1.000 76.97576  ?  1731 GLU   A C   1 
ATOM   13315 O  O   . GLU   A 1 1733 ? -78.35700  43.75200  -18.66500 1.000 83.73166  ?  1731 GLU   A O   1 
ATOM   13316 C  CB  . GLU   A 1 1733 ? -78.75700  41.59400  -16.29600 1.000 89.69502  ?  1731 GLU   A CB  1 
ATOM   13317 C  CG  . GLU   A 1 1733 ? -78.45000  41.29400  -14.83700 1.000 102.54842 ?  1731 GLU   A CG  1 
ATOM   13318 C  CD  . GLU   A 1 1733 ? -77.98000  39.86900  -14.62100 1.000 99.67467  ?  1731 GLU   A CD  1 
ATOM   13319 O  OE1 . GLU   A 1 1733 ? -77.78200  39.14900  -15.62200 1.000 97.19318  ?  1731 GLU   A OE1 1 
ATOM   13320 O  OE2 . GLU   A 1 1733 ? -77.80800  39.47000  -13.45000 1.000 95.58034  -1 1731 GLU   A OE2 1 
ATOM   13321 N  N   . ALA   A 1 1734 ? -80.47900  42.99500  -18.65700 1.000 78.23487  ?  1732 ALA   A N   1 
ATOM   13322 C  CA  . ALA   A 1 1734 ? -80.66900  43.31400  -20.06700 1.000 85.54285  ?  1732 ALA   A CA  1 
ATOM   13323 C  C   . ALA   A 1 1734 ? -80.61300  44.81700  -20.29800 1.000 78.44370  ?  1732 ALA   A C   1 
ATOM   13324 O  O   . ALA   A 1 1734 ? -79.97600  45.28500  -21.25000 1.000 74.69341  ?  1732 ALA   A O   1 
ATOM   13325 C  CB  . ALA   A 1 1734 ? -81.99700  42.74300  -20.56200 1.000 86.21570  ?  1732 ALA   A CB  1 
ATOM   13326 N  N   . THR   A 1 1735 ? -81.27200  45.59000  -19.43300 1.000 76.53101  ?  1733 THR   A N   1 
ATOM   13327 C  CA  . THR   A 1 1735 ? -81.18500  47.04300  -19.51900 1.000 77.94877  ?  1733 THR   A CA  1 
ATOM   13328 C  C   . THR   A 1 1735 ? -79.74900  47.51000  -19.31800 1.000 78.33695  ?  1733 THR   A C   1 
ATOM   13329 O  O   . THR   A 1 1735 ? -79.20800  48.26200  -20.13700 1.000 74.66071  ?  1733 THR   A O   1 
ATOM   13330 C  CB  . THR   A 1 1735 ? -82.11200  47.68300  -18.48400 1.000 76.16065  ?  1733 THR   A CB  1 
ATOM   13331 O  OG1 . THR   A 1 1735 ? -83.28600  46.87600  -18.32700 1.000 76.56906  ?  1733 THR   A OG1 1 
ATOM   13332 C  CG2 . THR   A 1 1735 ? -82.53400  49.07400  -18.92900 1.000 85.49218  ?  1733 THR   A CG2 1 
ATOM   13333 N  N   . LEU   A 1 1736 ? -79.10800  47.04300  -18.23900 1.000 77.99078  ?  1734 LEU   A N   1 
ATOM   13334 C  CA  . LEU   A 1 1736 ? -77.74600  47.46200  -17.91400 1.000 62.37220  ?  1734 LEU   A CA  1 
ATOM   13335 C  C   . LEU   A 1 1736 ? -76.79300  47.26400  -19.08700 1.000 67.00812  ?  1734 LEU   A C   1 
ATOM   13336 O  O   . LEU   A 1 1736 ? -75.87600  48.06800  -19.29300 1.000 61.02338  ?  1734 LEU   A O   1 
ATOM   13337 C  CB  . LEU   A 1 1736 ? -77.24600  46.69500  -16.68900 1.000 52.01852  ?  1734 LEU   A CB  1 
ATOM   13338 C  CG  . LEU   A 1 1736 ? -77.88000  47.04400  -15.34000 1.000 63.39338  ?  1734 LEU   A CG  1 
ATOM   13339 C  CD1 . LEU   A 1 1736 ? -77.50000  46.02600  -14.27500 1.000 58.83734  ?  1734 LEU   A CD1 1 
ATOM   13340 C  CD2 . LEU   A 1 1736 ? -77.47200  48.43800  -14.90800 1.000 60.05691  ?  1734 LEU   A CD2 1 
ATOM   13341 N  N   . ALA   A 1 1737 ? -76.99400  46.20100  -19.87000 1.000 70.66589  ?  1735 ALA   A N   1 
ATOM   13342 C  CA  . ALA   A 1 1737 ? -76.13700  45.96600  -21.02800 1.000 71.77448  ?  1735 ALA   A CA  1 
ATOM   13343 C  C   . ALA   A 1 1737 ? -76.32000  47.04900  -22.08400 1.000 70.82701  ?  1735 ALA   A C   1 
ATOM   13344 O  O   . ALA   A 1 1737 ? -75.36000  47.42700  -22.76700 1.000 67.68509  ?  1735 ALA   A O   1 
ATOM   13345 C  CB  . ALA   A 1 1737 ? -76.42000  44.58700  -21.62100 1.000 72.34343  ?  1735 ALA   A CB  1 
ATOM   13346 N  N   . HIS   A 1 1738 ? -77.54400  47.56300  -22.23200 1.000 68.91131  ?  1736 HIS   A N   1 
ATOM   13347 C  CA  . HIS   A 1 1738 ? -77.79700  48.59800  -23.22800 1.000 70.36114  ?  1736 HIS   A CA  1 
ATOM   13348 C  C   . HIS   A 1 1738 ? -77.16700  49.92400  -22.81800 1.000 66.07647  ?  1736 HIS   A C   1 
ATOM   13349 O  O   . HIS   A 1 1738 ? -76.53400  50.60100  -23.63800 1.000 65.81646  ?  1736 HIS   A O   1 
ATOM   13350 C  CB  . HIS   A 1 1738 ? -79.30200  48.76100  -23.44900 1.000 65.35386  ?  1736 HIS   A CB  1 
ATOM   13351 C  CG  . HIS   A 1 1738 ? -79.65200  49.78200  -24.48800 1.000 72.28231  ?  1736 HIS   A CG  1 
ATOM   13352 N  ND1 . HIS   A 1 1738 ? -80.69300  50.67200  -24.33600 1.000 63.57218  ?  1736 HIS   A ND1 1 
ATOM   13353 C  CD2 . HIS   A 1 1738 ? -79.10100  50.05200  -25.69500 1.000 87.34626  ?  1736 HIS   A CD2 1 
ATOM   13354 C  CE1 . HIS   A 1 1738 ? -80.76600  51.44800  -25.40200 1.000 69.18042  ?  1736 HIS   A CE1 1 
ATOM   13355 N  NE2 . HIS   A 1 1738 ? -79.81200  51.09200  -26.24300 1.000 76.36859  ?  1736 HIS   A NE2 1 
ATOM   13356 N  N   . ILE   A 1 1739 ? -77.32900  50.31400  -21.55000 1.000 59.39151  ?  1737 ILE   A N   1 
ATOM   13357 C  CA  . ILE   A 1 1739 ? -76.76900  51.58200  -21.09000 1.000 68.97259  ?  1737 ILE   A CA  1 
ATOM   13358 C  C   . ILE   A 1 1739 ? -75.24700  51.53200  -21.10100 1.000 65.66063  ?  1737 ILE   A C   1 
ATOM   13359 O  O   . ILE   A 1 1739 ? -74.58500  52.49500  -21.50600 1.000 66.47707  ?  1737 ILE   A O   1 
ATOM   13360 C  CB  . ILE   A 1 1739 ? -77.31400  51.94400  -19.69600 1.000 59.85385  ?  1737 ILE   A CB  1 
ATOM   13361 C  CG1 . ILE   A 1 1739 ? -78.80200  52.28300  -19.77300 1.000 49.75411  ?  1737 ILE   A CG1 1 
ATOM   13362 C  CG2 . ILE   A 1 1739 ? -76.55400  53.12100  -19.11000 1.000 63.16229  ?  1737 ILE   A CG2 1 
ATOM   13363 C  CD1 . ILE   A 1 1739 ? -79.69800  51.17700  -19.29700 1.000 53.77394  ?  1737 ILE   A CD1 1 
ATOM   13364 N  N   . TRP   A 1 1740 ? -74.66700  50.41500  -20.65500 1.000 72.48309  ?  1738 TRP   A N   1 
ATOM   13365 C  CA  . TRP   A 1 1740 ? -73.21900  50.25400  -20.74000 1.000 67.90740  ?  1738 TRP   A CA  1 
ATOM   13366 C  C   . TRP   A 1 1740 ? -72.74400  50.37400  -22.18200 1.000 78.18572  ?  1738 TRP   A C   1 
ATOM   13367 O  O   . TRP   A 1 1740 ? -71.84300  51.16300  -22.48800 1.000 80.72413  ?  1738 TRP   A O   1 
ATOM   13368 C  CB  . TRP   A 1 1740 ? -72.79700  48.90600  -20.15100 1.000 64.94521  ?  1738 TRP   A CB  1 
ATOM   13369 C  CG  . TRP   A 1 1740 ? -72.76000  48.86100  -18.65300 1.000 70.33185  ?  1738 TRP   A CG  1 
ATOM   13370 C  CD1 . TRP   A 1 1740 ? -73.56600  49.54100  -17.78600 1.000 67.64576  ?  1738 TRP   A CD1 1 
ATOM   13371 C  CD2 . TRP   A 1 1740 ? -71.85700  48.09700  -17.84500 1.000 86.79282  ?  1738 TRP   A CD2 1 
ATOM   13372 N  NE1 . TRP   A 1 1740 ? -73.22400  49.24100  -16.48900 1.000 59.06837  ?  1738 TRP   A NE1 1 
ATOM   13373 C  CE2 . TRP   A 1 1740 ? -72.17700  48.35700  -16.49800 1.000 87.05460  ?  1738 TRP   A CE2 1 
ATOM   13374 C  CE3 . TRP   A 1 1740 ? -70.81000  47.21500  -18.13100 1.000 94.94020  ?  1738 TRP   A CE3 1 
ATOM   13375 C  CZ2 . TRP   A 1 1740 ? -71.48900  47.76700  -15.44000 1.000 87.09546  ?  1738 TRP   A CZ2 1 
ATOM   13376 C  CZ3 . TRP   A 1 1740 ? -70.12800  46.63100  -17.07900 1.000 86.21799  ?  1738 TRP   A CZ3 1 
ATOM   13377 C  CH2 . TRP   A 1 1740 ? -70.47000  46.91000  -15.75100 1.000 79.97589  ?  1738 TRP   A CH2 1 
ATOM   13378 N  N   . GLY   A 1 1741 ? -73.35700  49.60800  -23.08600 1.000 70.69473  ?  1739 GLY   A N   1 
ATOM   13379 C  CA  . GLY   A 1 1741 ? -72.92700  49.62700  -24.47500 1.000 70.34252  ?  1739 GLY   A CA  1 
ATOM   13380 C  C   . GLY   A 1 1741 ? -73.04900  50.99600  -25.11700 1.000 67.78174  ?  1739 GLY   A C   1 
ATOM   13381 O  O   . GLY   A 1 1741 ? -72.16200  51.42400  -25.85900 1.000 71.81418  ?  1739 GLY   A O   1 
ATOM   13382 N  N   . GLU   A 1 1742 ? -74.14800  51.70300  -24.84100 1.000 70.21072  ?  1740 GLU   A N   1 
ATOM   13383 C  CA  . GLU   A 1 1742 ? -74.33700  53.02800  -25.42400 1.000 71.70228  ?  1740 GLU   A CA  1 
ATOM   13384 C  C   . GLU   A 1 1742 ? -73.31900  54.03100  -24.89700 1.000 81.17777  ?  1740 GLU   A C   1 
ATOM   13385 O  O   . GLU   A 1 1742 ? -72.89800  54.92900  -25.63500 1.000 86.47810  ?  1740 GLU   A O   1 
ATOM   13386 C  CB  . GLU   A 1 1742 ? -75.75500  53.52800  -25.15500 1.000 72.80723  ?  1740 GLU   A CB  1 
ATOM   13387 C  CG  . GLU   A 1 1742 ? -76.69700  53.39300  -26.33700 1.000 74.40217  ?  1740 GLU   A CG  1 
ATOM   13388 C  CD  . GLU   A 1 1742 ? -78.05200  54.01800  -26.07000 1.000 92.36617  ?  1740 GLU   A CD  1 
ATOM   13389 O  OE1 . GLU   A 1 1742 ? -78.31200  54.39700  -24.90900 1.000 89.88112  ?  1740 GLU   A OE1 1 
ATOM   13390 O  OE2 . GLU   A 1 1742 ? -78.85400  54.13400  -27.02000 1.000 98.04347  -1 1740 GLU   A OE2 1 
ATOM   13391 N  N   . VAL   A 1 1743 ? -72.91500  53.90000  -23.63400 1.000 82.14288  ?  1741 VAL   A N   1 
ATOM   13392 C  CA  . VAL   A 1 1743 ? -71.94400  54.82800  -23.06500 1.000 86.00508  ?  1741 VAL   A CA  1 
ATOM   13393 C  C   . VAL   A 1 1743 ? -70.52400  54.41200  -23.42800 1.000 83.57637  ?  1741 VAL   A C   1 
ATOM   13394 O  O   . VAL   A 1 1743 ? -69.72000  55.23100  -23.88900 1.000 73.92826  ?  1741 VAL   A O   1 
ATOM   13395 C  CB  . VAL   A 1 1743 ? -72.13400  54.92900  -21.54000 1.000 72.42037  ?  1741 VAL   A CB  1 
ATOM   13396 C  CG1 . VAL   A 1 1743 ? -71.00400  55.73100  -20.91600 1.000 69.94476  ?  1741 VAL   A CG1 1 
ATOM   13397 C  CG2 . VAL   A 1 1743 ? -73.47900  55.56000  -21.21300 1.000 65.10442  ?  1741 VAL   A CG2 1 
ATOM   13398 N  N   . LEU   A 1 1744 ? -70.19600  53.13300  -23.23600 1.000 87.09737  ?  1742 LEU   A N   1 
ATOM   13399 C  CA  . LEU   A 1 1744 ? -68.84500  52.66000  -23.51200 1.000 92.23441  ?  1742 LEU   A CA  1 
ATOM   13400 C  C   . LEU   A 1 1744 ? -68.55500  52.55900  -25.00400 1.000 105.36375 ?  1742 LEU   A C   1 
ATOM   13401 O  O   . LEU   A 1 1744 ? -67.38500  52.60600  -25.39900 1.000 129.86662 ?  1742 LEU   A O   1 
ATOM   13402 C  CB  . LEU   A 1 1744 ? -68.61800  51.30100  -22.84800 1.000 80.62708  ?  1742 LEU   A CB  1 
ATOM   13403 C  CG  . LEU   A 1 1744 ? -68.94000  51.22500  -21.35300 1.000 80.53100  ?  1742 LEU   A CG  1 
ATOM   13404 C  CD1 . LEU   A 1 1744 ? -68.68500  49.82800  -20.80600 1.000 68.04630  ?  1742 LEU   A CD1 1 
ATOM   13405 C  CD2 . LEU   A 1 1744 ? -68.15100  52.26800  -20.58100 1.000 78.39170  ?  1742 LEU   A CD2 1 
ATOM   13406 N  N   . GLY   A 1 1745 ? -69.58400  52.42700  -25.83700 1.000 89.20507  ?  1743 GLY   A N   1 
ATOM   13407 C  CA  . GLY   A 1 1745 ? -69.39500  52.25000  -27.26100 1.000 102.48520 ?  1743 GLY   A CA  1 
ATOM   13408 C  C   . GLY   A 1 1745 ? -69.17600  50.82100  -27.70300 1.000 102.58262 ?  1743 GLY   A C   1 
ATOM   13409 O  O   . GLY   A 1 1745 ? -68.76300  50.60100  -28.84800 1.000 92.26336  ?  1743 GLY   A O   1 
ATOM   13410 N  N   . ILE   A 1 1746 ? -69.44100  49.84600  -26.83800 1.000 99.40002  ?  1744 ILE   A N   1 
ATOM   13411 C  CA  . ILE   A 1 1746 ? -69.22000  48.43500  -27.13100 1.000 106.45227 ?  1744 ILE   A CA  1 
ATOM   13412 C  C   . ILE   A 1 1746 ? -70.55500  47.78500  -27.46100 1.000 98.97107  ?  1744 ILE   A C   1 
ATOM   13413 O  O   . ILE   A 1 1746 ? -71.58300  48.10200  -26.85000 1.000 92.39868  ?  1744 ILE   A O   1 
ATOM   13414 C  CB  . ILE   A 1 1746 ? -68.52900  47.73300  -25.94500 1.000 90.05589  ?  1744 ILE   A CB  1 
ATOM   13415 C  CG1 . ILE   A 1 1746 ? -67.15000  48.34900  -25.69900 1.000 74.30573  ?  1744 ILE   A CG1 1 
ATOM   13416 C  CG2 . ILE   A 1 1746 ? -68.41000  46.23500  -26.18600 1.000 102.93886 ?  1744 ILE   A CG2 1 
ATOM   13417 C  CD1 . ILE   A 1 1746 ? -66.30200  48.47000  -26.95200 1.000 79.47791  ?  1744 ILE   A CD1 1 
ATOM   13418 N  N   . GLU   A 1 1747 ? -70.54700  46.88200  -28.43700 1.000 103.32826 ?  1745 GLU   A N   1 
ATOM   13419 C  CA  . GLU   A 1 1747 ? -71.74400  46.16900  -28.85500 1.000 100.91885 ?  1745 GLU   A CA  1 
ATOM   13420 C  C   . GLU   A 1 1747 ? -71.83000  44.82200  -28.14900 1.000 100.79513 ?  1745 GLU   A C   1 
ATOM   13421 O  O   . GLU   A 1 1747 ? -70.81500  44.14900  -27.94600 1.000 104.62342 ?  1745 GLU   A O   1 
ATOM   13422 C  CB  . GLU   A 1 1747 ? -71.75700  45.96300  -30.37100 1.000 74.06707  ?  1745 GLU   A CB  1 
ATOM   13423 N  N   . ARG   A 1 1748 ? -73.05300  44.44200  -27.77500 1.000 93.17656  ?  1746 ARG   A N   1 
ATOM   13424 C  CA  . ARG   A 1 1748 ? -73.34000  43.14300  -27.16300 1.000 110.14627 ?  1746 ARG   A CA  1 
ATOM   13425 C  C   . ARG   A 1 1748 ? -72.50400  42.91900  -25.90400 1.000 110.95573 ?  1746 ARG   A C   1 
ATOM   13426 O  O   . ARG   A 1 1748 ? -71.80900  41.91200  -25.75900 1.000 109.18658 ?  1746 ARG   A O   1 
ATOM   13427 C  CB  . ARG   A 1 1748 ? -73.13200  42.00700  -28.16700 1.000 103.48591 ?  1746 ARG   A CB  1 
ATOM   13428 N  N   . ILE   A 1 1749 ? -72.57700  43.87700  -24.98200 1.000 106.55253 ?  1747 ILE   A N   1 
ATOM   13429 C  CA  . ILE   A 1 1749 ? -71.91500  43.72300  -23.69200 1.000 89.75619  ?  1747 ILE   A CA  1 
ATOM   13430 C  C   . ILE   A 1 1749 ? -72.62500  42.63000  -22.90700 1.000 94.64418  ?  1747 ILE   A C   1 
ATOM   13431 O  O   . ILE   A 1 1749 ? -73.83100  42.71300  -22.64900 1.000 95.54128  ?  1747 ILE   A O   1 
ATOM   13432 C  CB  . ILE   A 1 1749 ? -71.90100  45.04400  -22.91300 1.000 97.95093  ?  1747 ILE   A CB  1 
ATOM   13433 C  CG1 . ILE   A 1 1749 ? -70.81300  45.97100  -23.45700 1.000 96.01134  ?  1747 ILE   A CG1 1 
ATOM   13434 C  CG2 . ILE   A 1 1749 ? -71.69400  44.78500  -21.42500 1.000 74.57013  ?  1747 ILE   A CG2 1 
ATOM   13435 C  CD1 . ILE   A 1 1749 ? -70.75800  47.31500  -22.76500 1.000 80.12852  ?  1747 ILE   A CD1 1 
ATOM   13436 N  N   . GLY   A 1 1750 ? -71.88400  41.59400  -22.53800 1.000 94.72962  ?  1748 GLY   A N   1 
ATOM   13437 C  CA  . GLY   A 1 1750 ? -72.42500  40.56500  -21.68400 1.000 94.63886  ?  1748 GLY   A CA  1 
ATOM   13438 C  C   . GLY   A 1 1750 ? -72.09400  40.80500  -20.22600 1.000 89.52198  ?  1748 GLY   A C   1 
ATOM   13439 O  O   . GLY   A 1 1750 ? -71.21800  41.59800  -19.88900 1.000 90.91116  ?  1748 GLY   A O   1 
ATOM   13440 N  N   . ILE   A 1 1751 ? -72.82800  40.11600  -19.35100 1.000 72.47914  ?  1749 ILE   A N   1 
ATOM   13441 C  CA  . ILE   A 1 1751 ? -72.48000  40.15900  -17.94200 1.000 70.70985  ?  1749 ILE   A CA  1 
ATOM   13442 C  C   . ILE   A 1 1751 ? -71.11600  39.49900  -17.75300 1.000 99.37107  ?  1749 ILE   A C   1 
ATOM   13443 O  O   . ILE   A 1 1751 ? -70.62400  38.76200  -18.61700 1.000 111.83314 ?  1749 ILE   A O   1 
ATOM   13444 C  CB  . ILE   A 1 1751 ? -73.55400  39.47800  -17.07900 1.000 82.32757  ?  1749 ILE   A CB  1 
ATOM   13445 C  CG1 . ILE   A 1 1751 ? -73.71500  38.01500  -17.48400 1.000 85.07571  ?  1749 ILE   A CG1 1 
ATOM   13446 C  CG2 . ILE   A 1 1751 ? -74.88700  40.19200  -17.22800 1.000 65.21953  ?  1749 ILE   A CG2 1 
ATOM   13447 C  CD1 . ILE   A 1 1751 ? -74.87000  37.32500  -16.79400 1.000 79.50705  ?  1749 ILE   A CD1 1 
ATOM   13448 N  N   . ARG   A 1 1752 ? -70.49000  39.79000  -16.61100 1.000 95.34825  ?  1750 ARG   A N   1 
ATOM   13449 C  CA  . ARG   A 1 1752 ? -69.15000  39.30200  -16.28300 1.000 94.88620  ?  1750 ARG   A CA  1 
ATOM   13450 C  C   . ARG   A 1 1752 ? -68.08200  39.89400  -17.20000 1.000 83.05261  ?  1750 ARG   A C   1 
ATOM   13451 O  O   . ARG   A 1 1752 ? -67.03700  39.28100  -17.42700 1.000 91.02275  ?  1750 ARG   A O   1 
ATOM   13452 C  CB  . ARG   A 1 1752 ? -69.08900  37.77000  -16.30300 1.000 93.55357  ?  1750 ARG   A CB  1 
ATOM   13453 C  CG  . ARG   A 1 1752 ? -69.91700  37.12800  -15.20700 1.000 87.45874  ?  1750 ARG   A CG  1 
ATOM   13454 C  CD  . ARG   A 1 1752 ? -70.56900  35.83200  -15.65500 1.000 77.18388  ?  1750 ARG   A CD  1 
ATOM   13455 N  NE  . ARG   A 1 1752 ? -71.45200  35.31400  -14.61700 1.000 90.04386  ?  1750 ARG   A NE  1 
ATOM   13456 C  CZ  . ARG   A 1 1752 ? -72.16300  34.19900  -14.71500 1.000 94.11150  ?  1750 ARG   A CZ  1 
ATOM   13457 N  NH1 . ARG   A 1 1752 ? -72.15400  33.46800  -15.81700 1.000 90.09115  ?  1750 ARG   A NH1 1 
ATOM   13458 N  NH2 . ARG   A 1 1752 ? -72.89600  33.80500  -13.67700 1.000 94.47820  ?  1750 ARG   A NH2 1 
ATOM   13459 N  N   . ASP   A 1 1753 ? -68.33300  41.08800  -17.73100 1.000 93.26108  ?  1751 ASP   A N   1 
ATOM   13460 C  CA  . ASP   A 1 1753 ? -67.35000  41.84500  -18.49500 1.000 83.55810  ?  1751 ASP   A CA  1 
ATOM   13461 C  C   . ASP   A 1 1753 ? -66.91000  43.04500  -17.67000 1.000 78.00992  ?  1751 ASP   A C   1 
ATOM   13462 O  O   . ASP   A 1 1753 ? -67.75100  43.80600  -17.17900 1.000 83.17558  ?  1751 ASP   A O   1 
ATOM   13463 C  CB  . ASP   A 1 1753 ? -67.92200  42.30500  -19.83800 1.000 89.57686  ?  1751 ASP   A CB  1 
ATOM   13464 C  CG  . ASP   A 1 1753 ? -68.33700  41.14700  -20.72600 1.000 100.33626 ?  1751 ASP   A CG  1 
ATOM   13465 O  OD1 . ASP   A 1 1753 ? -68.18400  39.98200  -20.30200 1.000 92.80635  ?  1751 ASP   A OD1 1 
ATOM   13466 O  OD2 . ASP   A 1 1753 ? -68.82200  41.40400  -21.84800 1.000 91.10156  -1 1751 ASP   A OD2 1 
ATOM   13467 N  N   . ASN   A 1 1754 ? -65.59800  43.21000  -17.51500 1.000 82.07392  ?  1752 ASN   A N   1 
ATOM   13468 C  CA  . ASN   A 1 1754 ? -65.07000  44.27900  -16.67500 1.000 92.42858  ?  1752 ASN   A CA  1 
ATOM   13469 C  C   . ASN   A 1 1754 ? -65.37500  45.63600  -17.30000 1.000 90.58781  ?  1752 ASN   A C   1 
ATOM   13470 O  O   . ASN   A 1 1754 ? -65.02100  45.89300  -18.45500 1.000 88.70389  ?  1752 ASN   A O   1 
ATOM   13471 C  CB  . ASN   A 1 1754 ? -63.56900  44.10200  -16.46900 1.000 85.20324  ?  1752 ASN   A CB  1 
ATOM   13472 C  CG  . ASN   A 1 1754 ? -62.97300  45.18200  -15.58600 1.000 87.61624  ?  1752 ASN   A CG  1 
ATOM   13473 O  OD1 . ASN   A 1 1754 ? -62.61800  46.26200  -16.05900 1.000 92.54612  ?  1752 ASN   A OD1 1 
ATOM   13474 N  ND2 . ASN   A 1 1754 ? -62.86000  44.89400  -14.29500 1.000 83.54532  ?  1752 ASN   A ND2 1 
ATOM   13475 N  N   . PHE   A 1 1755 ? -66.03200  46.50100  -16.52400 1.000 80.40376  ?  1753 PHE   A N   1 
ATOM   13476 C  CA  . PHE   A 1 1755 ? -66.44600  47.80900  -17.02400 1.000 88.59395  ?  1753 PHE   A CA  1 
ATOM   13477 C  C   . PHE   A 1 1755 ? -65.24100  48.67700  -17.36700 1.000 93.21810  ?  1753 PHE   A C   1 
ATOM   13478 O  O   . PHE   A 1 1755 ? -65.20400  49.32000  -18.42300 1.000 83.11757  ?  1753 PHE   A O   1 
ATOM   13479 C  CB  . PHE   A 1 1755 ? -67.34500  48.48100  -15.98200 1.000 75.99219  ?  1753 PHE   A CB  1 
ATOM   13480 C  CG  . PHE   A 1 1755 ? -67.37100  49.98200  -16.05600 1.000 71.46133  ?  1753 PHE   A CG  1 
ATOM   13481 C  CD1 . PHE   A 1 1755 ? -68.12000  50.63600  -17.02100 1.000 76.48233  ?  1753 PHE   A CD1 1 
ATOM   13482 C  CD2 . PHE   A 1 1755 ? -66.67400  50.74000  -15.13000 1.000 80.07243  ?  1753 PHE   A CD2 1 
ATOM   13483 C  CE1 . PHE   A 1 1755 ? -68.15100  52.01900  -17.07300 1.000 81.03707  ?  1753 PHE   A CE1 1 
ATOM   13484 C  CE2 . PHE   A 1 1755 ? -66.70200  52.12100  -15.17700 1.000 85.02555  ?  1753 PHE   A CE2 1 
ATOM   13485 C  CZ  . PHE   A 1 1755 ? -67.44400  52.76100  -16.14800 1.000 78.71508  ?  1753 PHE   A CZ  1 
ATOM   13486 N  N   . PHE   A 1 1756 ? -64.23800  48.70000  -16.48700 1.000 94.57777  ?  1754 PHE   A N   1 
ATOM   13487 C  CA  . PHE   A 1 1756 ? -63.03600  49.48000  -16.76300 1.000 92.32845  ?  1754 PHE   A CA  1 
ATOM   13488 C  C   . PHE   A 1 1756 ? -62.23500  48.88400  -17.91200 1.000 89.23260  ?  1754 PHE   A C   1 
ATOM   13489 O  O   . PHE   A 1 1756 ? -61.54300  49.61600  -18.63000 1.000 75.92284  ?  1754 PHE   A O   1 
ATOM   13490 C  CB  . PHE   A 1 1756 ? -62.17600  49.57900  -15.50400 1.000 73.86024  ?  1754 PHE   A CB  1 
ATOM   13491 C  CG  . PHE   A 1 1756 ? -62.92400  50.07200  -14.30000 1.000 75.24090  ?  1754 PHE   A CG  1 
ATOM   13492 C  CD1 . PHE   A 1 1756 ? -63.09800  51.42900  -14.08500 1.000 90.11908  ?  1754 PHE   A CD1 1 
ATOM   13493 C  CD2 . PHE   A 1 1756 ? -63.46000  49.18000  -13.38800 1.000 78.26802  ?  1754 PHE   A CD2 1 
ATOM   13494 C  CE1 . PHE   A 1 1756 ? -63.78900  51.88700  -12.97900 1.000 80.64503  ?  1754 PHE   A CE1 1 
ATOM   13495 C  CE2 . PHE   A 1 1756 ? -64.15100  49.63100  -12.28000 1.000 83.60813  ?  1754 PHE   A CE2 1 
ATOM   13496 C  CZ  . PHE   A 1 1756 ? -64.31600  50.98700  -12.07500 1.000 76.71921  ?  1754 PHE   A CZ  1 
ATOM   13497 N  N   . GLU   A 1 1757 ? -62.31400  47.56500  -18.10000 1.000 88.54594  ?  1755 GLU   A N   1 
ATOM   13498 C  CA  . GLU   A 1 1757 ? -61.65200  46.94200  -19.24000 1.000 87.99620  ?  1755 GLU   A CA  1 
ATOM   13499 C  C   . GLU   A 1 1757 ? -62.30500  47.37300  -20.54700 1.000 91.36413  ?  1755 GLU   A C   1 
ATOM   13500 O  O   . GLU   A 1 1757 ? -61.61400  47.63100  -21.53900 1.000 93.13511  ?  1755 GLU   A O   1 
ATOM   13501 C  CB  . GLU   A 1 1757 ? -61.68700  45.42200  -19.09400 1.000 72.68661  ?  1755 GLU   A CB  1 
ATOM   13502 C  CG  . GLU   A 1 1757 ? -60.47500  44.70800  -19.65700 1.000 95.01672  ?  1755 GLU   A CG  1 
ATOM   13503 C  CD  . GLU   A 1 1757 ? -60.61200  43.20000  -19.59500 1.000 114.75830 ?  1755 GLU   A CD  1 
ATOM   13504 O  OE1 . GLU   A 1 1757 ? -61.02400  42.67800  -18.53700 1.000 116.09930 ?  1755 GLU   A OE1 1 
ATOM   13505 O  OE2 . GLU   A 1 1757 ? -60.31600  42.53700  -20.61100 1.000 109.59239 -1 1755 GLU   A OE2 1 
ATOM   13506 N  N   . LEU   A 1 1758 ? -63.63500  47.47300  -20.56000 1.000 75.03022  ?  1756 LEU   A N   1 
ATOM   13507 C  CA  . LEU   A 1 1758 ? -64.40800  47.96900  -21.69500 1.000 65.73679  ?  1756 LEU   A CA  1 
ATOM   13508 C  C   . LEU   A 1 1758 ? -64.23300  49.46900  -21.92200 1.000 79.23547  ?  1756 LEU   A C   1 
ATOM   13509 O  O   . LEU   A 1 1758 ? -64.98700  50.05000  -22.71400 1.000 88.55146  ?  1756 LEU   A O   1 
ATOM   13510 C  CB  . LEU   A 1 1758 ? -65.88900  47.64300  -21.49500 1.000 76.15248  ?  1756 LEU   A CB  1 
ATOM   13511 C  CG  . LEU   A 1 1758 ? -66.29700  46.16800  -21.47600 1.000 74.79532  ?  1756 LEU   A CG  1 
ATOM   13512 C  CD1 . LEU   A 1 1758 ? -67.63300  45.99200  -20.77200 1.000 83.84590  ?  1756 LEU   A CD1 1 
ATOM   13513 C  CD2 . LEU   A 1 1758 ? -66.36500  45.61200  -22.88900 1.000 76.19963  ?  1756 LEU   A CD2 1 
ATOM   13514 N  N   . GLY   A 1 1759 ? -63.27100  50.10600  -21.26000 1.000 74.47440  ?  1757 GLY   A N   1 
ATOM   13515 C  CA  . GLY   A 1 1759 ? -63.03200  51.52300  -21.43700 1.000 68.96864  ?  1757 GLY   A CA  1 
ATOM   13516 C  C   . GLY   A 1 1759 ? -63.71200  52.41200  -20.42600 1.000 78.04822  ?  1757 GLY   A C   1 
ATOM   13517 O  O   . GLY   A 1 1759 ? -63.92200  53.59800  -20.70800 1.000 75.25935  ?  1757 GLY   A O   1 
ATOM   13518 N  N   . GLY   A 1 1760 ? -64.05800  51.88500  -19.25500 1.000 74.13624  ?  1758 GLY   A N   1 
ATOM   13519 C  CA  . GLY   A 1 1760 ? -64.81900  52.65500  -18.29500 1.000 73.46270  ?  1758 GLY   A CA  1 
ATOM   13520 C  C   . GLY   A 1 1760 ? -63.95700  53.60200  -17.48300 1.000 73.41809  ?  1758 GLY   A C   1 
ATOM   13521 O  O   . GLY   A 1 1760 ? -62.79000  53.33800  -17.19500 1.000 83.21491  ?  1758 GLY   A O   1 
ATOM   13522 N  N   . ASP   A 1 1761 ? -64.55700  54.73200  -17.11200 1.000 69.08326  ?  1759 ASP   A N   1 
ATOM   13523 C  CA  . ASP   A 1 1761 ? -63.91900  55.70800  -16.24300 1.000 73.28069  ?  1759 ASP   A CA  1 
ATOM   13524 C  C   . ASP   A 1 1761 ? -64.96600  56.29600  -15.30600 1.000 78.64665  ?  1759 ASP   A C   1 
ATOM   13525 O  O   . ASP   A 1 1761 ? -66.16400  56.02200  -15.42400 1.000 68.90184  ?  1759 ASP   A O   1 
ATOM   13526 C  CB  . ASP   A 1 1761 ? -63.20700  56.81100  -17.04800 1.000 59.22813  ?  1759 ASP   A CB  1 
ATOM   13527 C  CG  . ASP   A 1 1761 ? -64.12600  57.52900  -18.03200 1.000 74.54279  ?  1759 ASP   A CG  1 
ATOM   13528 O  OD1 . ASP   A 1 1761 ? -65.35300  57.57600  -17.81200 1.000 86.56445  ?  1759 ASP   A OD1 1 
ATOM   13529 O  OD2 . ASP   A 1 1761 ? -63.60800  58.05400  -19.04100 1.000 90.86346  -1 1759 ASP   A OD2 1 
ATOM   13530 N  N   . SER   A 1 1762 ? -64.50000  57.11900  -14.36300 1.000 81.21571  ?  1760 SER   A N   1 
ATOM   13531 C  CA  . SER   A 1 1762 ? -65.40900  57.78200  -13.43500 1.000 66.41903  ?  1760 SER   A CA  1 
ATOM   13532 C  C   . SER   A 1 1762 ? -66.37500  58.72000  -14.14800 1.000 72.18716  ?  1760 SER   A C   1 
ATOM   13533 O  O   . SER   A 1 1762 ? -67.43700  59.03300  -13.59900 1.000 70.73288  ?  1760 SER   A O   1 
ATOM   13534 C  CB  . SER   A 1 1762 ? -64.61200  58.54600  -12.37400 1.000 73.39302  ?  1760 SER   A CB  1 
ATOM   13535 O  OG  . SER   A 1 1762 ? -63.69000  59.44500  -12.96600 1.000 76.06738  ?  1760 SER   A OG  1 
ATOM   13536 N  N   . ILE   A 1 1763 ? -66.03300  59.17100  -15.35600 1.000 76.76828  ?  1761 ILE   A N   1 
ATOM   13537 C  CA  . ILE   A 1 1763 ? -66.95400  59.98900  -16.13900 1.000 73.02119  ?  1761 ILE   A CA  1 
ATOM   13538 C  C   . ILE   A 1 1763 ? -68.07600  59.12800  -16.70500 1.000 65.31367  ?  1761 ILE   A C   1 
ATOM   13539 O  O   . ILE   A 1 1763 ? -69.26000  59.46600  -16.59400 1.000 50.63033  ?  1761 ILE   A O   1 
ATOM   13540 C  CB  . ILE   A 1 1763 ? -66.19400  60.72400  -17.25800 1.000 54.87830  ?  1761 ILE   A CB  1 
ATOM   13541 C  CG1 . ILE   A 1 1763 ? -64.89900  61.32800  -16.71400 1.000 63.38928  ?  1761 ILE   A CG1 1 
ATOM   13542 C  CG2 . ILE   A 1 1763 ? -67.07100  61.80100  -17.88100 1.000 57.78699  ?  1761 ILE   A CG2 1 
ATOM   13543 C  CD1 . ILE   A 1 1763 ? -63.83000  61.52000  -17.76600 1.000 76.38370  ?  1761 ILE   A CD1 1 
ATOM   13544 N  N   . LYS   A 1 1764 ? -67.71600  57.99900  -17.32300 1.000 67.13227  ?  1762 LYS   A N   1 
ATOM   13545 C  CA  . LYS   A 1 1764 ? -68.71100  57.11100  -17.91300 1.000 61.12033  ?  1762 LYS   A CA  1 
ATOM   13546 C  C   . LYS   A 1 1764 ? -69.60400  56.46300  -16.86500 1.000 63.73030  ?  1762 LYS   A C   1 
ATOM   13547 O  O   . LYS   A 1 1764 ? -70.73100  56.07400  -17.18800 1.000 66.24483  ?  1762 LYS   A O   1 
ATOM   13548 C  CB  . LYS   A 1 1764 ? -68.01800  56.03900  -18.75600 1.000 58.85719  ?  1762 LYS   A CB  1 
ATOM   13549 C  CG  . LYS   A 1 1764 ? -67.42700  56.58000  -20.04900 1.000 54.78813  ?  1762 LYS   A CG  1 
ATOM   13550 C  CD  . LYS   A 1 1764 ? -66.43200  55.61400  -20.66300 1.000 70.85394  ?  1762 LYS   A CD  1 
ATOM   13551 C  CE  . LYS   A 1 1764 ? -65.75300  56.23100  -21.87700 1.000 62.60507  ?  1762 LYS   A CE  1 
ATOM   13552 N  NZ  . LYS   A 1 1764 ? -64.26800  56.11200  -21.81300 1.000 69.16245  ?  1762 LYS   A NZ  1 
ATOM   13553 N  N   . GLY   A 1 1765 ? -69.13000  56.33500  -15.62500 1.000 64.68846  ?  1763 GLY   A N   1 
ATOM   13554 C  CA  . GLY   A 1 1765 ? -69.99900  55.85900  -14.56300 1.000 56.19778  ?  1763 GLY   A CA  1 
ATOM   13555 C  C   . GLY   A 1 1765 ? -71.10500  56.84500  -14.24100 1.000 62.04541  ?  1763 GLY   A C   1 
ATOM   13556 O  O   . GLY   A 1 1765 ? -72.24600  56.45000  -13.98300 1.000 69.98665  ?  1763 GLY   A O   1 
ATOM   13557 N  N   . LEU   A 1 1766 ? -70.78400  58.14200  -14.25300 1.000 66.02256  ?  1764 LEU   A N   1 
ATOM   13558 C  CA  . LEU   A 1 1766 ? -71.80900  59.16000  -14.05100 1.000 57.41802  ?  1764 LEU   A CA  1 
ATOM   13559 C  C   . LEU   A 1 1766 ? -72.82100  59.14600  -15.18700 1.000 50.90505  ?  1764 LEU   A C   1 
ATOM   13560 O  O   . LEU   A 1 1766 ? -74.01600  59.37700  -14.97000 1.000 69.84855  ?  1764 LEU   A O   1 
ATOM   13561 C  CB  . LEU   A 1 1766 ? -71.16400  60.54100  -13.92600 1.000 65.05075  ?  1764 LEU   A CB  1 
ATOM   13562 C  CG  . LEU   A 1 1766 ? -72.06100  61.67600  -13.42500 1.000 60.34399  ?  1764 LEU   A CG  1 
ATOM   13563 C  CD1 . LEU   A 1 1766 ? -72.38800  61.46600  -11.96400 1.000 54.12282  ?  1764 LEU   A CD1 1 
ATOM   13564 C  CD2 . LEU   A 1 1766 ? -71.40100  63.02800  -13.62500 1.000 62.29540  ?  1764 LEU   A CD2 1 
ATOM   13565 N  N   . GLN   A 1 1767 ? -72.36100  58.87600  -16.41000 1.000 60.01784  ?  1765 GLN   A N   1 
ATOM   13566 C  CA  . GLN   A 1 1767 ? -73.28300  58.75600  -17.53300 1.000 60.02779  ?  1765 GLN   A CA  1 
ATOM   13567 C  C   . GLN   A 1 1767 ? -74.15300  57.51300  -17.39100 1.000 58.39370  ?  1765 GLN   A C   1 
ATOM   13568 O  O   . GLN   A 1 1767 ? -75.37700  57.58200  -17.54700 1.000 64.67438  ?  1765 GLN   A O   1 
ATOM   13569 C  CB  . GLN   A 1 1767 ? -72.50800  58.73600  -18.85100 1.000 39.87245  ?  1765 GLN   A CB  1 
ATOM   13570 C  CG  . GLN   A 1 1767 ? -71.72500  60.01400  -19.11300 1.000 57.66021  ?  1765 GLN   A CG  1 
ATOM   13571 C  CD  . GLN   A 1 1767 ? -71.07100  60.04000  -20.48200 1.000 80.69483  ?  1765 GLN   A CD  1 
ATOM   13572 O  OE1 . GLN   A 1 1767 ? -70.82800  58.99800  -21.08900 1.000 72.45277  ?  1765 GLN   A OE1 1 
ATOM   13573 N  NE2 . GLN   A 1 1767 ? -70.78600  61.24000  -20.97600 1.000 77.21701  ?  1765 GLN   A NE2 1 
ATOM   13574 N  N   . ILE   A 1 1768 ? -73.53900  56.36800  -17.07500 1.000 47.84977  ?  1766 ILE   A N   1 
ATOM   13575 C  CA  . ILE   A 1 1768 ? -74.30500  55.13700  -16.89000 1.000 50.42456  ?  1766 ILE   A CA  1 
ATOM   13576 C  C   . ILE   A 1 1768 ? -75.32300  55.30200  -15.76800 1.000 65.51961  ?  1766 ILE   A C   1 
ATOM   13577 O  O   . ILE   A 1 1768 ? -76.45500  54.81000  -15.85700 1.000 70.87697  ?  1766 ILE   A O   1 
ATOM   13578 C  CB  . ILE   A 1 1768 ? -73.35600  53.95100  -16.63000 1.000 46.55353  ?  1766 ILE   A CB  1 
ATOM   13579 C  CG1 . ILE   A 1 1768 ? -72.58200  53.60100  -17.90000 1.000 54.46915  ?  1766 ILE   A CG1 1 
ATOM   13580 C  CG2 . ILE   A 1 1768 ? -74.12600  52.73600  -16.12800 1.000 48.02299  ?  1766 ILE   A CG2 1 
ATOM   13581 C  CD1 . ILE   A 1 1768 ? -71.62400  52.44900  -17.72500 1.000 61.79124  ?  1766 ILE   A CD1 1 
ATOM   13582 N  N   . ALA   A 1 1769 ? -74.94400  56.00800  -14.70100 1.000 61.08051  ?  1767 ALA   A N   1 
ATOM   13583 C  CA  . ALA   A 1 1769 ? -75.89000  56.26600  -13.62000 1.000 57.30781  ?  1767 ALA   A CA  1 
ATOM   13584 C  C   . ALA   A 1 1769 ? -76.99100  57.22000  -14.06500 1.000 59.54284  ?  1767 ALA   A C   1 
ATOM   13585 O  O   . ALA   A 1 1769 ? -78.15100  57.06900  -13.66200 1.000 62.87415  ?  1767 ALA   A O   1 
ATOM   13586 C  CB  . ALA   A 1 1769 ? -75.15500  56.82400  -12.40200 1.000 63.41708  ?  1767 ALA   A CB  1 
ATOM   13587 N  N   . SER   A 1 1770 ? -76.64900  58.20300  -14.90000 1.000 62.93474  ?  1768 SER   A N   1 
ATOM   13588 C  CA  . SER   A 1 1770 ? -77.63800  59.17700  -15.35200 1.000 61.69323  ?  1768 SER   A CA  1 
ATOM   13589 C  C   . SER   A 1 1770 ? -78.68000  58.52600  -16.25400 1.000 67.58295  ?  1768 SER   A C   1 
ATOM   13590 O  O   . SER   A 1 1770 ? -79.88600  58.71400  -16.05700 1.000 73.46301  ?  1768 SER   A O   1 
ATOM   13591 C  CB  . SER   A 1 1770 ? -76.94400  60.32800  -16.07700 1.000 58.68229  ?  1768 SER   A CB  1 
ATOM   13592 O  OG  . SER   A 1 1770 ? -75.77600  60.72600  -15.38400 1.000 80.58207  ?  1768 SER   A OG  1 
ATOM   13593 N  N   . ARG   A 1 1771 ? -78.23000  57.76300  -17.25700 1.000 62.83510  ?  1769 ARG   A N   1 
ATOM   13594 C  CA  . ARG   A 1 1771 ? -79.16700  57.05200  -18.12100 1.000 60.33169  ?  1769 ARG   A CA  1 
ATOM   13595 C  C   . ARG   A 1 1771 ? -80.06000  56.12200  -17.31400 1.000 63.90033  ?  1769 ARG   A C   1 
ATOM   13596 O  O   . ARG   A 1 1771 ? -81.23400  55.93200  -17.65400 1.000 73.13929  ?  1769 ARG   A O   1 
ATOM   13597 C  CB  . ARG   A 1 1771 ? -78.41800  56.24500  -19.18700 1.000 57.56537  ?  1769 ARG   A CB  1 
ATOM   13598 C  CG  . ARG   A 1 1771 ? -77.23900  56.94400  -19.85300 1.000 66.17446  ?  1769 ARG   A CG  1 
ATOM   13599 C  CD  . ARG   A 1 1771 ? -77.66500  57.98300  -20.87200 1.000 74.07238  ?  1769 ARG   A CD  1 
ATOM   13600 N  NE  . ARG   A 1 1771 ? -76.51900  58.67000  -21.45700 1.000 77.99994  ?  1769 ARG   A NE  1 
ATOM   13601 C  CZ  . ARG   A 1 1771 ? -76.06100  58.46000  -22.68400 1.000 75.75030  ?  1769 ARG   A CZ  1 
ATOM   13602 N  NH1 . ARG   A 1 1771 ? -76.65000  57.60600  -23.50500 1.000 65.37770  ?  1769 ARG   A NH1 1 
ATOM   13603 N  NH2 . ARG   A 1 1771 ? -74.98700  59.12600  -23.09800 1.000 92.39995  ?  1769 ARG   A NH2 1 
ATOM   13604 N  N   . LEU   A 1 1772 ? -79.52500  55.54100  -16.23800 1.000 54.87935  ?  1770 LEU   A N   1 
ATOM   13605 C  CA  . LEU   A 1 1772 ? -80.28800  54.61100  -15.41900 1.000 61.16511  ?  1770 LEU   A CA  1 
ATOM   13606 C  C   . LEU   A 1 1772 ? -81.28400  55.30400  -14.49800 1.000 61.45058  ?  1770 LEU   A C   1 
ATOM   13607 O  O   . LEU   A 1 1772 ? -82.24200  54.66100  -14.06100 1.000 64.60346  ?  1770 LEU   A O   1 
ATOM   13608 C  CB  . LEU   A 1 1772 ? -79.33700  53.74000  -14.59600 1.000 52.72416  ?  1770 LEU   A CB  1 
ATOM   13609 C  CG  . LEU   A 1 1772 ? -78.77200  52.51600  -15.31700 1.000 52.91764  ?  1770 LEU   A CG  1 
ATOM   13610 C  CD1 . LEU   A 1 1772 ? -77.55300  52.00100  -14.57800 1.000 46.12818  ?  1770 LEU   A CD1 1 
ATOM   13611 C  CD2 . LEU   A 1 1772 ? -79.83300  51.43200  -15.42900 1.000 40.86391  ?  1770 LEU   A CD2 1 
ATOM   13612 N  N   . GLN   A 1 1773 ? -81.09600  56.59100  -14.19300 1.000 62.27163  ?  1771 GLN   A N   1 
ATOM   13613 C  CA  . GLN   A 1 1773 ? -82.07100  57.26900  -13.34500 1.000 71.80717  ?  1771 GLN   A CA  1 
ATOM   13614 C  C   . GLN   A 1 1773 ? -83.32900  57.64200  -14.11900 1.000 84.21008  ?  1771 GLN   A C   1 
ATOM   13615 O  O   . GLN   A 1 1773 ? -84.43700  57.55200  -13.58000 1.000 75.74199  ?  1771 GLN   A O   1 
ATOM   13616 C  CB  . GLN   A 1 1773 ? -81.45900  58.51500  -12.70600 1.000 67.98803  ?  1771 GLN   A CB  1 
ATOM   13617 C  CG  . GLN   A 1 1773 ? -82.21400  58.96500  -11.46500 1.000 83.21700  ?  1771 GLN   A CG  1 
ATOM   13618 C  CD  . GLN   A 1 1773 ? -82.59100  60.43000  -11.50100 1.000 97.05281  ?  1771 GLN   A CD  1 
ATOM   13619 O  OE1 . GLN   A 1 1773 ? -81.87000  61.25500  -12.06100 1.000 106.43541 ?  1771 GLN   A OE1 1 
ATOM   13620 N  NE2 . GLN   A 1 1773 ? -83.73100  60.76300  -10.90300 1.000 104.65553 ?  1771 GLN   A NE2 1 
ATOM   13621 N  N   . ARG   A 1 1774 ? -83.17700  58.06400  -15.37600 1.000 75.76029  ?  1772 ARG   A N   1 
ATOM   13622 C  CA  . ARG   A 1 1774 ? -84.33200  58.40900  -16.19700 1.000 60.49552  ?  1772 ARG   A CA  1 
ATOM   13623 C  C   . ARG   A 1 1774 ? -85.27500  57.22900  -16.38800 1.000 59.28325  ?  1772 ARG   A C   1 
ATOM   13624 O  O   . ARG   A 1 1774 ? -86.46700  57.43500  -16.64100 1.000 93.54963  ?  1772 ARG   A O   1 
ATOM   13625 C  CB  . ARG   A 1 1774 ? -83.86200  58.95200  -17.54900 1.000 84.73746  ?  1772 ARG   A CB  1 
ATOM   13626 C  CG  . ARG   A 1 1774 ? -82.97900  60.18100  -17.41900 1.000 70.36414  ?  1772 ARG   A CG  1 
ATOM   13627 C  CD  . ARG   A 1 1774 ? -82.86700  60.95700  -18.71900 1.000 79.42936  ?  1772 ARG   A CD  1 
ATOM   13628 N  NE  . ARG   A 1 1774 ? -81.76300  60.50400  -19.55400 1.000 86.41051  ?  1772 ARG   A NE  1 
ATOM   13629 C  CZ  . ARG   A 1 1774 ? -80.49200  60.82600  -19.35300 1.000 80.27357  ?  1772 ARG   A CZ  1 
ATOM   13630 N  NH1 . ARG   A 1 1774 ? -80.11900  61.55800  -18.31600 1.000 83.62313  ?  1772 ARG   A NH1 1 
ATOM   13631 N  NH2 . ARG   A 1 1774 ? -79.57200  60.40400  -20.21400 1.000 73.26883  ?  1772 ARG   A NH2 1 
ATOM   13632 N  N   . ILE   A 1 1775 ? -84.77400  56.00300  -16.26600 1.000 46.42236  ?  1773 ILE   A N   1 
ATOM   13633 C  CA  . ILE   A 1 1775 ? -85.61500  54.81700  -16.24600 1.000 57.20037  ?  1773 ILE   A CA  1 
ATOM   13634 C  C   . ILE   A 1 1775 ? -85.89100  54.35400  -14.81100 1.000 58.48576  ?  1773 ILE   A C   1 
ATOM   13635 O  O   . ILE   A 1 1775 ? -86.26700  53.20300  -14.59500 1.000 60.80003  ?  1773 ILE   A O   1 
ATOM   13636 C  CB  . ILE   A 1 1775 ? -85.01100  53.68900  -17.09600 1.000 58.76013  ?  1773 ILE   A CB  1 
ATOM   13637 C  CG1 . ILE   A 1 1775 ? -83.58800  53.38300  -16.63000 1.000 57.97747  ?  1773 ILE   A CG1 1 
ATOM   13638 C  CG2 . ILE   A 1 1775 ? -85.00300  54.07300  -18.56600 1.000 41.45018  ?  1773 ILE   A CG2 1 
ATOM   13639 C  CD1 . ILE   A 1 1775 ? -82.78500  52.55100  -17.60000 1.000 56.38012  ?  1773 ILE   A CD1 1 
ATOM   13640 N  N   . ASN   A 1 1776 ? -85.69500  55.23700  -13.82700 1.000 51.77336  ?  1774 ASN   A N   1 
ATOM   13641 C  CA  . ASN   A 1 1776 ? -86.02000  55.04200  -12.41200 1.000 58.87144  ?  1774 ASN   A CA  1 
ATOM   13642 C  C   . ASN   A 1 1776 ? -85.16100  53.99200  -11.71600 1.000 67.13471  ?  1774 ASN   A C   1 
ATOM   13643 O  O   . ASN   A 1 1776 ? -85.49500  53.57500  -10.59900 1.000 72.67730  ?  1774 ASN   A O   1 
ATOM   13644 C  CB  . ASN   A 1 1776 ? -87.50300  54.70200  -12.21200 1.000 76.38831  ?  1774 ASN   A CB  1 
ATOM   13645 C  CG  . ASN   A 1 1776 ? -88.38600  55.93800  -12.20900 1.000 86.35810  ?  1774 ASN   A CG  1 
ATOM   13646 O  OD1 . ASN   A 1 1776 ? -88.97900  56.29100  -11.18800 1.000 78.32388  ?  1774 ASN   A OD1 1 
ATOM   13647 N  ND2 . ASN   A 1 1776 ? -88.46300  56.61200  -13.35000 1.000 73.09910  ?  1774 ASN   A ND2 1 
ATOM   13648 N  N   . TRP   A 1 1777 ? -84.06300  53.56000  -12.32800 1.000 76.54425  ?  1775 TRP   A N   1 
ATOM   13649 C  CA  . TRP   A 1 1777 ? -83.08700  52.72300  -11.64600 1.000 59.76422  ?  1775 TRP   A CA  1 
ATOM   13650 C  C   . TRP   A 1 1777 ? -82.08900  53.59800  -10.89500 1.000 69.43615  ?  1775 TRP   A C   1 
ATOM   13651 O  O   . TRP   A 1 1777 ? -81.83800  54.74800  -11.26600 1.000 78.76756  ?  1775 TRP   A O   1 
ATOM   13652 C  CB  . TRP   A 1 1777 ? -82.34600  51.81900  -12.63400 1.000 63.18857  ?  1775 TRP   A CB  1 
ATOM   13653 C  CG  . TRP   A 1 1777 ? -83.15200  50.65500  -13.14300 1.000 62.80118  ?  1775 TRP   A CG  1 
ATOM   13654 C  CD1 . TRP   A 1 1777 ? -83.52000  50.41500  -14.43600 1.000 54.78731  ?  1775 TRP   A CD1 1 
ATOM   13655 C  CD2 . TRP   A 1 1777 ? -83.68100  49.56900  -12.36900 1.000 66.11758  ?  1775 TRP   A CD2 1 
ATOM   13656 N  NE1 . TRP   A 1 1777 ? -84.24400  49.24900  -14.51400 1.000 47.98053  ?  1775 TRP   A NE1 1 
ATOM   13657 C  CE2 . TRP   A 1 1777 ? -84.35800  48.71200  -13.25900 1.000 51.44759  ?  1775 TRP   A CE2 1 
ATOM   13658 C  CE3 . TRP   A 1 1777 ? -83.65000  49.24000  -11.01100 1.000 71.15448  ?  1775 TRP   A CE3 1 
ATOM   13659 C  CZ2 . TRP   A 1 1777 ? -84.99300  47.54500  -12.83600 1.000 46.58429  ?  1775 TRP   A CZ2 1 
ATOM   13660 C  CZ3 . TRP   A 1 1777 ? -84.28700  48.08300  -10.59200 1.000 77.99894  ?  1775 TRP   A CZ3 1 
ATOM   13661 C  CH2 . TRP   A 1 1777 ? -84.94900  47.25100  -11.50100 1.000 74.25327  ?  1775 TRP   A CH2 1 
ATOM   13662 N  N   . THR   A 1 1778 ? -81.51600  53.04100  -9.83000  1.000 63.89247  ?  1776 THR   A N   1 
ATOM   13663 C  CA  . THR   A 1 1778 ? -80.60500  53.77600  -8.95200  1.000 68.99159  ?  1776 THR   A CA  1 
ATOM   13664 C  C   . THR   A 1 1778 ? -79.29500  53.00300  -8.83500  1.000 64.58792  ?  1776 THR   A C   1 
ATOM   13665 O  O   . THR   A 1 1778 ? -79.22700  51.99500  -8.12800  1.000 71.82486  ?  1776 THR   A O   1 
ATOM   13666 C  CB  . THR   A 1 1778 ? -81.23100  53.99900  -7.57700  1.000 72.14371  ?  1776 THR   A CB  1 
ATOM   13667 O  OG1 . THR   A 1 1778 ? -82.37200  54.85800  -7.70000  1.000 87.81694  ?  1776 THR   A OG1 1 
ATOM   13668 C  CG2 . THR   A 1 1778 ? -80.22400  54.63100  -6.63000  1.000 79.78926  ?  1776 THR   A CG2 1 
ATOM   13669 N  N   . MET   A 1 1779 ? -78.25600  53.48300  -9.51300  1.000 61.26856  ?  1777 MET   A N   1 
ATOM   13670 C  CA  . MET   A 1 1779 ? -76.93100  52.88000  -9.46100  1.000 64.90481  ?  1777 MET   A CA  1 
ATOM   13671 C  C   . MET   A 1 1779 ? -75.95700  53.82900  -8.77700  1.000 53.27644  ?  1777 MET   A C   1 
ATOM   13672 O  O   . MET   A 1 1779 ? -75.93900  55.02900  -9.07300  1.000 55.93631  ?  1777 MET   A O   1 
ATOM   13673 C  CB  . MET   A 1 1779 ? -76.42100  52.53200  -10.86300 1.000 63.18466  ?  1777 MET   A CB  1 
ATOM   13674 C  CG  . MET   A 1 1779 ? -74.90100  52.53300  -10.98300 1.000 56.30621  ?  1777 MET   A CG  1 
ATOM   13675 S  SD  . MET   A 1 1779 ? -74.28800  51.81600  -12.51800 1.000 72.74773  ?  1777 MET   A SD  1 
ATOM   13676 C  CE  . MET   A 1 1779 ? -74.54400  50.07400  -12.19900 1.000 69.40804  ?  1777 MET   A CE  1 
ATOM   13677 N  N   . VAL   A 1 1780 ? -75.15200  53.29200  -7.86700  1.000 49.77126  ?  1778 VAL   A N   1 
ATOM   13678 C  CA  . VAL   A 1 1780 ? -74.08900  54.05100  -7.22000  1.000 69.72596  ?  1778 VAL   A CA  1 
ATOM   13679 C  C   . VAL   A 1 1780 ? -72.80900  53.87400  -8.02400  1.000 72.45870  ?  1778 VAL   A C   1 
ATOM   13680 O  O   . VAL   A 1 1780 ? -72.43800  52.75000  -8.38500  1.000 69.41252  ?  1778 VAL   A O   1 
ATOM   13681 C  CB  . VAL   A 1 1780 ? -73.89600  53.59900  -5.76300  1.000 64.05294  ?  1778 VAL   A CB  1 
ATOM   13682 C  CG1 . VAL   A 1 1780 ? -72.77100  54.38900  -5.10800  1.000 61.73498  ?  1778 VAL   A CG1 1 
ATOM   13683 C  CG2 . VAL   A 1 1780 ? -75.19100  53.76100  -4.98600  1.000 45.17282  ?  1778 VAL   A CG2 1 
ATOM   13684 N  N   . ILE   A 1 1781 ? -72.12900  54.98700  -8.30400  1.000 62.92204  ?  1779 ILE   A N   1 
ATOM   13685 C  CA  . ILE   A 1 1781 ? -70.93900  54.94000  -9.14700  1.000 69.38477  ?  1779 ILE   A CA  1 
ATOM   13686 C  C   . ILE   A 1 1781 ? -69.79400  54.22600  -8.44500  1.000 76.62576  ?  1779 ILE   A C   1 
ATOM   13687 O  O   . ILE   A 1 1781 ? -68.99000  53.54300  -9.09200  1.000 74.75903  ?  1779 ILE   A O   1 
ATOM   13688 C  CB  . ILE   A 1 1781 ? -70.54600  56.36600  -9.56100  1.000 61.93155  ?  1779 ILE   A CB  1 
ATOM   13689 C  CG1 . ILE   A 1 1781 ? -71.79100  57.12800  -10.00400 1.000 31.47707  ?  1779 ILE   A CG1 1 
ATOM   13690 C  CG2 . ILE   A 1 1781 ? -69.51400  56.33600  -10.67600 1.000 67.19196  ?  1779 ILE   A CG2 1 
ATOM   13691 C  CD1 . ILE   A 1 1781 ? -71.59600  58.60500  -10.03700 1.000 47.82375  ?  1779 ILE   A CD1 1 
ATOM   13692 N  N   . ASN   A 1 1782 ? -69.69200  54.37100  -7.12100  1.000 82.16609  ?  1780 ASN   A N   1 
ATOM   13693 C  CA  . ASN   A 1 1782 ? -68.66300  53.65900  -6.37000  1.000 88.36210  ?  1780 ASN   A CA  1 
ATOM   13694 C  C   . ASN   A 1 1782 ? -68.81400  52.15000  -6.51200  1.000 86.20490  ?  1780 ASN   A C   1 
ATOM   13695 O  O   . ASN   A 1 1782 ? -67.81200  51.42600  -6.51200  1.000 86.33581  ?  1780 ASN   A O   1 
ATOM   13696 C  CB  . ASN   A 1 1782 ? -68.71600  54.08100  -4.89900  1.000 79.99262  ?  1780 ASN   A CB  1 
ATOM   13697 C  CG  . ASN   A 1 1782 ? -67.71300  53.33700  -4.02500  1.000 89.06405  ?  1780 ASN   A CG  1 
ATOM   13698 O  OD1 . ASN   A 1 1782 ? -67.87300  53.27700  -2.80600  1.000 96.16564  ?  1780 ASN   A OD1 1 
ATOM   13699 N  ND2 . ASN   A 1 1782 ? -66.67800  52.77100  -4.64000  1.000 100.17988 ?  1780 ASN   A ND2 1 
ATOM   13700 N  N   . HIS   A 1 1783 ? -70.04800  51.66000  -6.64600  1.000 69.91924  ?  1781 HIS   A N   1 
ATOM   13701 C  CA  . HIS   A 1 1783 ? -70.25800  50.22300  -6.77900  1.000 66.43056  ?  1781 HIS   A CA  1 
ATOM   13702 C  C   . HIS   A 1 1783 ? -69.64700  49.68000  -8.06400  1.000 66.17428  ?  1781 HIS   A C   1 
ATOM   13703 O  O   . HIS   A 1 1783 ? -69.29100  48.49800  -8.12900  1.000 73.65474  ?  1781 HIS   A O   1 
ATOM   13704 C  CB  . HIS   A 1 1783 ? -71.75000  49.90700  -6.70900  1.000 72.48107  ?  1781 HIS   A CB  1 
ATOM   13705 C  CG  . HIS   A 1 1783 ? -72.35100  50.15000  -5.35900  1.000 80.41138  ?  1781 HIS   A CG  1 
ATOM   13706 N  ND1 . HIS   A 1 1783 ? -73.70200  50.33600  -5.16800  1.000 73.56923  ?  1781 HIS   A ND1 1 
ATOM   13707 C  CD2 . HIS   A 1 1783 ? -71.78200  50.23500  -4.13300  1.000 86.68449  ?  1781 HIS   A CD2 1 
ATOM   13708 C  CE1 . HIS   A 1 1783 ? -73.94200  50.52600  -3.88300  1.000 60.44635  ?  1781 HIS   A CE1 1 
ATOM   13709 N  NE2 . HIS   A 1 1783 ? -72.79400  50.46900  -3.23300  1.000 89.24031  ?  1781 HIS   A NE2 1 
ATOM   13710 N  N   . LEU   A 1 1784 ? -69.51300  50.52200  -9.09300  1.000 59.62425  ?  1782 LEU   A N   1 
ATOM   13711 C  CA  . LEU   A 1 1784 ? -68.81500  50.09800  -10.30300 1.000 66.42912  ?  1782 LEU   A CA  1 
ATOM   13712 C  C   . LEU   A 1 1784 ? -67.36300  49.74400  -10.01400 1.000 85.21943  ?  1782 LEU   A C   1 
ATOM   13713 O  O   . LEU   A 1 1784 ? -66.81000  48.82800  -10.63400 1.000 80.16594  ?  1782 LEU   A O   1 
ATOM   13714 C  CB  . LEU   A 1 1784 ? -68.89000  51.19200  -11.36900 1.000 69.84226  ?  1782 LEU   A CB  1 
ATOM   13715 C  CG  . LEU   A 1 1784 ? -70.08700  51.13500  -12.31500 1.000 69.95586  ?  1782 LEU   A CG  1 
ATOM   13716 C  CD1 . LEU   A 1 1784 ? -70.05700  52.29800  -13.29400 1.000 61.91599  ?  1782 LEU   A CD1 1 
ATOM   13717 C  CD2 . LEU   A 1 1784 ? -70.09100  49.81200  -13.05400 1.000 75.77554  ?  1782 LEU   A CD2 1 
ATOM   13718 N  N   . PHE   A 1 1785 ? -66.73300  50.45700  -9.07800  1.000 96.50025  ?  1783 PHE   A N   1 
ATOM   13719 C  CA  . PHE   A 1 1785 ? -65.36300  50.16300  -8.67900  1.000 76.74928  ?  1783 PHE   A CA  1 
ATOM   13720 C  C   . PHE   A 1 1785 ? -65.27300  48.94100  -7.77600  1.000 83.30508  ?  1783 PHE   A C   1 
ATOM   13721 O  O   . PHE   A 1 1785 ? -64.19200  48.35700  -7.64900  1.000 80.24420  ?  1783 PHE   A O   1 
ATOM   13722 C  CB  . PHE   A 1 1785 ? -64.75300  51.37900  -7.97200  1.000 73.25539  ?  1783 PHE   A CB  1 
ATOM   13723 C  CG  . PHE   A 1 1785 ? -64.50800  52.55600  -8.88200  1.000 84.97118  ?  1783 PHE   A CG  1 
ATOM   13724 C  CD1 . PHE   A 1 1785 ? -65.56800  53.26700  -9.42400  1.000 71.74683  ?  1783 PHE   A CD1 1 
ATOM   13725 C  CD2 . PHE   A 1 1785 ? -63.21600  52.95700  -9.18500  1.000 89.71420  ?  1783 PHE   A CD2 1 
ATOM   13726 C  CE1 . PHE   A 1 1785 ? -65.34500  54.34500  -10.26000 1.000 84.29640  ?  1783 PHE   A CE1 1 
ATOM   13727 C  CE2 . PHE   A 1 1785 ? -62.98700  54.03900  -10.01900 1.000 78.60814  ?  1783 PHE   A CE2 1 
ATOM   13728 C  CZ  . PHE   A 1 1785 ? -64.05300  54.73300  -10.55600 1.000 89.35888  ?  1783 PHE   A CZ  1 
ATOM   13729 N  N   . LEU   A 1 1786 ? -66.38300  48.54500  -7.15200  1.000 82.83112  ?  1784 LEU   A N   1 
ATOM   13730 C  CA  . LEU   A 1 1786 ? -66.43200  47.35600  -6.31200  1.000 85.75033  ?  1784 LEU   A CA  1 
ATOM   13731 C  C   . LEU   A 1 1786 ? -66.99400  46.13800  -7.03200  1.000 80.89456  ?  1784 LEU   A C   1 
ATOM   13732 O  O   . LEU   A 1 1786 ? -66.57000  45.01400  -6.74700  1.000 82.36805  ?  1784 LEU   A O   1 
ATOM   13733 C  CB  . LEU   A 1 1786 ? -67.27900  47.62600  -5.06300  1.000 87.39722  ?  1784 LEU   A CB  1 
ATOM   13734 C  CG  . LEU   A 1 1786 ? -67.17900  49.01600  -4.42700  1.000 84.94637  ?  1784 LEU   A CG  1 
ATOM   13735 C  CD1 . LEU   A 1 1786 ? -68.25900  49.20300  -3.37600  1.000 79.03631  ?  1784 LEU   A CD1 1 
ATOM   13736 C  CD2 . LEU   A 1 1786 ? -65.80900  49.24100  -3.81900  1.000 78.71146  ?  1784 LEU   A CD2 1 
ATOM   13737 N  N   . TYR   A 1 1787 ? -67.93500  46.33100  -7.95500  1.000 86.27074  ?  1785 TYR   A N   1 
ATOM   13738 C  CA  . TYR   A 1 1787 ? -68.58700  45.23900  -8.67900  1.000 84.75786  ?  1785 TYR   A CA  1 
ATOM   13739 C  C   . TYR   A 1 1787 ? -68.49600  45.54600  -10.16900 1.000 81.03861  ?  1785 TYR   A C   1 
ATOM   13740 O  O   . TYR   A 1 1787 ? -69.46900  46.00800  -10.78000 1.000 70.32279  ?  1785 TYR   A O   1 
ATOM   13741 C  CB  . TYR   A 1 1787 ? -70.03600  45.07200  -8.21900  1.000 75.80764  ?  1785 TYR   A CB  1 
ATOM   13742 C  CG  . TYR   A 1 1787 ? -70.21000  45.25600  -6.72300  1.000 75.50960  ?  1785 TYR   A CG  1 
ATOM   13743 C  CD1 . TYR   A 1 1787 ? -69.90800  44.22800  -5.83800  1.000 81.34819  ?  1785 TYR   A CD1 1 
ATOM   13744 C  CD2 . TYR   A 1 1787 ? -70.66200  46.46100  -6.19600  1.000 72.52504  ?  1785 TYR   A CD2 1 
ATOM   13745 C  CE1 . TYR   A 1 1787 ? -70.05800  44.39300  -4.47100  1.000 93.83407  ?  1785 TYR   A CE1 1 
ATOM   13746 C  CE2 . TYR   A 1 1787 ? -70.81400  46.63300  -4.83200  1.000 89.22079  ?  1785 TYR   A CE2 1 
ATOM   13747 C  CZ  . TYR   A 1 1787 ? -70.51100  45.59700  -3.97300  1.000 99.88332  ?  1785 TYR   A CZ  1 
ATOM   13748 O  OH  . TYR   A 1 1787 ? -70.66200  45.76500  -2.61400  1.000 77.81825  ?  1785 TYR   A OH  1 
ATOM   13749 N  N   . PRO   A 1 1788 ? -67.32900  45.31800  -10.78600 1.000 82.29649  ?  1786 PRO   A N   1 
ATOM   13750 C  CA  . PRO   A 1 1788 ? -67.11900  45.79600  -12.16300 1.000 78.92332  ?  1786 PRO   A CA  1 
ATOM   13751 C  C   . PRO   A 1 1788 ? -67.79100  44.93700  -13.22200 1.000 75.92563  ?  1786 PRO   A C   1 
ATOM   13752 O  O   . PRO   A 1 1788 ? -67.57700  45.14100  -14.42300 1.000 71.71797  ?  1786 PRO   A O   1 
ATOM   13753 C  CB  . PRO   A 1 1788 ? -65.59000  45.77300  -12.31700 1.000 74.60501  ?  1786 PRO   A CB  1 
ATOM   13754 C  CG  . PRO   A 1 1788 ? -65.03600  45.59600  -10.93500 1.000 78.17783  ?  1786 PRO   A CG  1 
ATOM   13755 C  CD  . PRO   A 1 1788 ? -66.08000  44.84800  -10.16400 1.000 73.34861  ?  1786 PRO   A CD  1 
ATOM   13756 N  N   . THR   A 1 1789 ? -68.61400  43.97900  -12.79800 1.000 76.84785  ?  1787 THR   A N   1 
ATOM   13757 C  CA  . THR   A 1 1789 ? -69.39900  43.16600  -13.71300 1.000 86.53913  ?  1787 THR   A CA  1 
ATOM   13758 C  C   . THR   A 1 1789 ? -70.88100  43.39200  -13.45500 1.000 88.45231  ?  1787 THR   A C   1 
ATOM   13759 O  O   . THR   A 1 1789 ? -71.29000  43.75300  -12.34600 1.000 93.19220  ?  1787 THR   A O   1 
ATOM   13760 C  CB  . THR   A 1 1789 ? -69.06600  41.66900  -13.58700 1.000 85.82310  ?  1787 THR   A CB  1 
ATOM   13761 O  OG1 . THR   A 1 1789 ? -70.03800  41.01500  -12.76100 1.000 81.31328  ?  1787 THR   A OG1 1 
ATOM   13762 C  CG2 . THR   A 1 1789 ? -67.67800  41.47700  -12.99400 1.000 79.33422  ?  1787 THR   A CG2 1 
ATOM   13763 N  N   . ILE   A 1 1790 ? -71.68300  43.18000  -14.50000 1.000 83.25018  ?  1788 ILE   A N   1 
ATOM   13764 C  CA  . ILE   A 1 1790 ? -73.11600  43.43900  -14.40000 1.000 83.52755  ?  1788 ILE   A CA  1 
ATOM   13765 C  C   . ILE   A 1 1790 ? -73.76800  42.48500  -13.40700 1.000 84.59908  ?  1788 ILE   A C   1 
ATOM   13766 O  O   . ILE   A 1 1790 ? -74.50000  42.91200  -12.50600 1.000 89.20239  ?  1788 ILE   A O   1 
ATOM   13767 C  CB  . ILE   A 1 1790 ? -73.77700  43.34800  -15.78300 1.000 84.42512  ?  1788 ILE   A CB  1 
ATOM   13768 C  CG1 . ILE   A 1 1790 ? -73.22800  44.43500  -16.70900 1.000 76.96295  ?  1788 ILE   A CG1 1 
ATOM   13769 C  CG2 . ILE   A 1 1790 ? -75.27400  43.48100  -15.64100 1.000 72.39214  ?  1788 ILE   A CG2 1 
ATOM   13770 C  CD1 . ILE   A 1 1790 ? -73.85200  44.44100  -18.08700 1.000 56.84798  ?  1788 ILE   A CD1 1 
ATOM   13771 N  N   . GLU   A 1 1791 ? -73.51200  41.18000  -13.55100 1.000 79.81513  ?  1789 GLU   A N   1 
ATOM   13772 C  CA  . GLU   A 1 1791 ? -74.07300  40.21200  -12.61200 1.000 85.98462  ?  1789 GLU   A CA  1 
ATOM   13773 C  C   . GLU   A 1 1791 ? -73.63700  40.48300  -11.18100 1.000 84.81704  ?  1789 GLU   A C   1 
ATOM   13774 O  O   . GLU   A 1 1791 ? -74.30400  40.03400  -10.24200 1.000 79.06168  ?  1789 GLU   A O   1 
ATOM   13775 C  CB  . GLU   A 1 1791 ? -73.67000  38.78900  -13.00000 1.000 89.81149  ?  1789 GLU   A CB  1 
ATOM   13776 C  CG  . GLU   A 1 1791 ? -72.21600  38.45200  -12.70500 1.000 91.03972  ?  1789 GLU   A CG  1 
ATOM   13777 C  CD  . GLU   A 1 1791 ? -72.03900  37.03400  -12.20200 1.000 98.64403  ?  1789 GLU   A CD  1 
ATOM   13778 O  OE1 . GLU   A 1 1791 ? -72.98700  36.49900  -11.58800 1.000 93.35771  ?  1789 GLU   A OE1 1 
ATOM   13779 O  OE2 . GLU   A 1 1791 ? -70.95900  36.44800  -12.42800 1.000 88.70513  -1 1789 GLU   A OE2 1 
ATOM   13780 N  N   . GLN   A 1 1792 ? -72.53200  41.20600  -10.99400 1.000 79.07540  ?  1790 GLN   A N   1 
ATOM   13781 C  CA  . GLN   A 1 1792 ? -72.05800  41.52700  -9.65500  1.000 87.00114  ?  1790 GLN   A CA  1 
ATOM   13782 C  C   . GLN   A 1 1792 ? -72.73600  42.77900  -9.11700  1.000 93.42519  ?  1790 GLN   A C   1 
ATOM   13783 O  O   . GLN   A 1 1792 ? -73.03400  42.86400  -7.92100  1.000 77.66773  ?  1790 GLN   A O   1 
ATOM   13784 C  CB  . GLN   A 1 1792 ? -70.54100  41.70700  -9.67400  1.000 80.69241  ?  1790 GLN   A CB  1 
ATOM   13785 C  CG  . GLN   A 1 1792 ? -69.79200  40.95600  -8.59300  1.000 91.28208  ?  1790 GLN   A CG  1 
ATOM   13786 C  CD  . GLN   A 1 1792 ? -68.28800  41.06700  -8.75800  1.000 86.45770  ?  1790 GLN   A CD  1 
ATOM   13787 O  OE1 . GLN   A 1 1792 ? -67.79700  41.49800  -9.80200  1.000 77.28042  ?  1790 GLN   A OE1 1 
ATOM   13788 N  NE2 . GLN   A 1 1792 ? -67.54800  40.67900  -7.72700  1.000 101.50900 ?  1790 GLN   A NE2 1 
ATOM   13789 N  N   . ILE   A 1 1793 ? -73.00300  43.74800  -9.98700  1.000 87.45042  ?  1791 ILE   A N   1 
ATOM   13790 C  CA  . ILE   A 1 1793 ? -73.52100  45.03000  -9.53500  1.000 81.97050  ?  1791 ILE   A CA  1 
ATOM   13791 C  C   . ILE   A 1 1793 ? -75.04500  45.10100  -9.59600  1.000 84.44511  ?  1791 ILE   A C   1 
ATOM   13792 O  O   . ILE   A 1 1793 ? -75.65300  45.88400  -8.85500  1.000 86.09559  ?  1791 ILE   A O   1 
ATOM   13793 C  CB  . ILE   A 1 1793 ? -72.88100  46.16300  -10.35100 1.000 69.36897  ?  1791 ILE   A CB  1 
ATOM   13794 C  CG1 . ILE   A 1 1793 ? -72.98800  47.47800  -9.58900  1.000 65.07119  ?  1791 ILE   A CG1 1 
ATOM   13795 C  CG2 . ILE   A 1 1793 ? -73.53600  46.28500  -11.71900 1.000 62.77019  ?  1791 ILE   A CG2 1 
ATOM   13796 C  CD1 . ILE   A 1 1793 ? -72.08100  48.54200  -10.12000 1.000 72.24827  ?  1791 ILE   A CD1 1 
ATOM   13797 N  N   . ALA   A 1 1794 ? -75.67900  44.29500  -10.44800 1.000 77.87899  ?  1792 ALA   A N   1 
ATOM   13798 C  CA  . ALA   A 1 1794 ? -77.13300  44.35700  -10.58800 1.000 76.43261  ?  1792 ALA   A CA  1 
ATOM   13799 C  C   . ALA   A 1 1794 ? -77.88100  44.14100  -9.27600  1.000 80.54634  ?  1792 ALA   A C   1 
ATOM   13800 O  O   . ALA   A 1 1794 ? -78.83500  44.89400  -9.01700  1.000 94.07865  ?  1792 ALA   A O   1 
ATOM   13801 C  CB  . ALA   A 1 1794 ? -77.60000  43.35600  -11.65700 1.000 77.28953  ?  1792 ALA   A CB  1 
ATOM   13802 N  N   . PRO   A 1 1795 ? -77.53000  43.16600  -8.40800  1.000 81.00127  ?  1793 PRO   A N   1 
ATOM   13803 C  CA  . PRO   A 1 1795 ? -78.19500  43.10600  -7.09700  1.000 81.26943  ?  1793 PRO   A CA  1 
ATOM   13804 C  C   . PRO   A 1 1795 ? -77.59600  44.06200  -6.07700  1.000 96.68588  ?  1793 PRO   A C   1 
ATOM   13805 O  O   . PRO   A 1 1795 ? -78.33000  44.63100  -5.26300  1.000 89.12115  ?  1793 PRO   A O   1 
ATOM   13806 C  CB  . PRO   A 1 1795 ? -78.00000  41.64500  -6.67600  1.000 89.91885  ?  1793 PRO   A CB  1 
ATOM   13807 C  CG  . PRO   A 1 1795 ? -76.73600  41.24200  -7.32700  1.000 97.43867  ?  1793 PRO   A CG  1 
ATOM   13808 C  CD  . PRO   A 1 1795 ? -76.68600  41.98200  -8.64600  1.000 87.61050  ?  1793 PRO   A CD  1 
ATOM   13809 N  N   . PHE   A 1 1796 ? -76.27400  44.26000  -6.11200  1.000 117.75128 ?  1794 PHE   A N   1 
ATOM   13810 C  CA  . PHE   A 1 1796 ? -75.59500  45.09300  -5.11800  1.000 110.68976 ?  1794 PHE   A CA  1 
ATOM   13811 C  C   . PHE   A 1 1796 ? -75.96300  46.56700  -5.21100  1.000 104.65361 ?  1794 PHE   A C   1 
ATOM   13812 O  O   . PHE   A 1 1796 ? -75.47700  47.35700  -4.39100  1.000 108.15319 ?  1794 PHE   A O   1 
ATOM   13813 C  CB  . PHE   A 1 1796 ? -74.07800  44.93400  -5.24000  1.000 93.32764  ?  1794 PHE   A CB  1 
ATOM   13814 C  CG  . PHE   A 1 1796 ? -73.50900  43.87600  -4.34000  1.000 113.89115 ?  1794 PHE   A CG  1 
ATOM   13815 C  CD1 . PHE   A 1 1796 ? -73.41100  44.09200  -2.97600  1.000 121.44128 ?  1794 PHE   A CD1 1 
ATOM   13816 C  CD2 . PHE   A 1 1796 ? -73.07100  42.66700  -4.85500  1.000 126.73690 ?  1794 PHE   A CD2 1 
ATOM   13817 C  CE1 . PHE   A 1 1796 ? -72.88800  43.12200  -2.14100  1.000 134.37800 ?  1794 PHE   A CE1 1 
ATOM   13818 C  CE2 . PHE   A 1 1796 ? -72.54600  41.69300  -4.02600  1.000 132.32764 ?  1794 PHE   A CE2 1 
ATOM   13819 C  CZ  . PHE   A 1 1796 ? -72.45500  41.92100  -2.66700  1.000 124.98992 ?  1794 PHE   A CZ  1 
ATOM   13820 N  N   . VAL   A 1 1797 ? -76.78600  46.95200  -6.18400  1.000 99.77553  ?  1795 VAL   A N   1 
ATOM   13821 C  CA  . VAL   A 1 1797 ? -77.35700  48.29100  -6.26600  1.000 104.39557 ?  1795 VAL   A CA  1 
ATOM   13822 C  C   . VAL   A 1 1797 ? -78.54200  48.18800  -7.22500  1.000 92.78812  ?  1795 VAL   A C   1 
ATOM   13823 O  O   . VAL   A 1 1797 ? -79.33800  47.24800  -7.11300  1.000 100.57385 ?  1795 VAL   A O   1 
ATOM   13824 C  CB  . VAL   A 1 1797 ? -76.29000  49.33600  -6.67500  1.000 107.48578 ?  1795 VAL   A CB  1 
ATOM   13825 C  CG1 . VAL   A 1 1797 ? -75.71100  49.09000  -8.07800  1.000 103.71973 ?  1795 VAL   A CG1 1 
ATOM   13826 C  CG2 . VAL   A 1 1797 ? -76.78400  50.77600  -6.46400  1.000 89.52810  ?  1795 VAL   A CG2 1 
ATOM   13827 N  N   . THR   A 1 1798 ? -78.66300  49.11800  -8.17300  1.000 88.56030  ?  1796 THR   A N   1 
ATOM   13828 C  CA  . THR   A 1 1798 ? -79.75200  49.14500  -9.15000  1.000 82.97134  ?  1796 THR   A CA  1 
ATOM   13829 C  C   . THR   A 1 1798 ? -81.09400  48.87600  -8.47600  1.000 90.17758  ?  1796 THR   A C   1 
ATOM   13830 O  O   . THR   A 1 1798 ? -81.84800  47.97700  -8.85200  1.000 92.02170  ?  1796 THR   A O   1 
ATOM   13831 C  CB  . THR   A 1 1798 ? -79.50000  48.17000  -10.30200 1.000 88.69141  ?  1796 THR   A CB  1 
ATOM   13832 O  OG1 . THR   A 1 1798 ? -78.88000  46.97600  -9.81200  1.000 110.19058 ?  1796 THR   A OG1 1 
ATOM   13833 C  CG2 . THR   A 1 1798 ? -78.60500  48.81200  -11.35500 1.000 74.34769  ?  1796 THR   A CG2 1 
ATOM   13834 N  N   . SER   A 1 1799 ? -81.36400  49.64900  -7.43000  1.000 88.34922  ?  1797 SER   A N   1 
ATOM   13835 C  CA  . SER   A 1 1799 ? -82.68600  49.67200  -6.83700  1.000 83.22206  ?  1797 SER   A CA  1 
ATOM   13836 C  C   . SER   A 1 1799 ? -83.58300  50.60800  -7.64000  1.000 94.91044  ?  1797 SER   A C   1 
ATOM   13837 O  O   . SER   A 1 1799 ? -83.11500  51.45700  -8.40300  1.000 79.50737  ?  1797 SER   A O   1 
ATOM   13838 C  CB  . SER   A 1 1799 ? -82.61600  50.11900  -5.37600  1.000 51.74780  ?  1797 SER   A CB  1 
ATOM   13839 O  OG  . SER   A 1 1799 ? -81.97200  51.37700  -5.24200  1.000 65.52261  ?  1797 SER   A OG  1 
ATOM   13840 N  N   . GLU   A 1 1800 ? -84.88700  50.44900  -7.45000  1.000 84.92829  ?  1798 GLU   A N   1 
ATOM   13841 C  CA  . GLU   A 1 1800 ? -85.88900  51.22100  -8.16600  1.000 82.52691  ?  1798 GLU   A CA  1 
ATOM   13842 C  C   . GLU   A 1 1800 ? -86.42700  52.33400  -7.27000  1.000 98.63203  ?  1798 GLU   A C   1 
ATOM   13843 O  O   . GLU   A 1 1800 ? -86.48000  52.18800  -6.04400  1.000 100.43293 ?  1798 GLU   A O   1 
ATOM   13844 C  CB  . GLU   A 1 1800 ? -87.01000  50.29600  -8.64800  1.000 71.52090  ?  1798 GLU   A CB  1 
ATOM   13845 C  CG  . GLU   A 1 1800 ? -88.04900  50.96600  -9.50400  1.000 101.62620 ?  1798 GLU   A CG  1 
ATOM   13846 C  CD  . GLU   A 1 1800 ? -89.21500  51.51900  -8.69400  1.000 116.46327 ?  1798 GLU   A CD  1 
ATOM   13847 O  OE1 . GLU   A 1 1800 ? -89.22000  51.32300  -7.44700  1.000 124.86732 ?  1798 GLU   A OE1 1 
ATOM   13848 O  OE2 . GLU   A 1 1800 ? -90.10800  52.14300  -9.31400  1.000 111.78007 ?  1798 GLU   A OE2 1 
ATOM   13849 N  N   . GLN   A 1 1801 ? -86.77300  53.46300  -7.88400  1.000 95.63860  ?  1799 GLN   A N   1 
ATOM   13850 C  CA  . GLN   A 1 1801 ? -87.41700  54.56900  -7.18200  1.000 98.87135  ?  1799 GLN   A CA  1 
ATOM   13851 C  C   . GLN   A 1 1801 ? -88.93000  54.39000  -7.26100  1.000 105.15906 ?  1799 GLN   A C   1 
ATOM   13852 O  O   . GLN   A 1 1801 ? -89.54100  54.67600  -8.29600  1.000 116.49632 ?  1799 GLN   A O   1 
ATOM   13853 C  CB  . GLN   A 1 1801 ? -87.00600  55.90700  -7.78700  1.000 92.77901  ?  1799 GLN   A CB  1 
ATOM   13854 C  CG  . GLN   A 1 1801 ? -86.99900  57.08700  -6.81300  1.000 95.90529  ?  1799 GLN   A CG  1 
ATOM   13855 C  CD  . GLN   A 1 1801 ? -88.33800  57.33300  -6.12300  1.000 103.09248 ?  1799 GLN   A CD  1 
ATOM   13856 O  OE1 . GLN   A 1 1801 ? -89.40900  57.12200  -6.69800  1.000 102.81002 ?  1799 GLN   A OE1 1 
ATOM   13857 N  NE2 . GLN   A 1 1801 ? -88.27500  57.78400  -4.87500  1.000 104.29377 ?  1799 GLN   A NE2 1 
ATOM   13858 N  N   . VAL   A 1 1802 ? -89.54000  53.99900  -6.13900  1.000 108.77623 ?  1800 VAL   A N   1 
ATOM   13859 C  CA  . VAL   A 1 1802 ? -90.94100  53.57900  -6.13200  1.000 97.46508  ?  1800 VAL   A CA  1 
ATOM   13860 C  C   . VAL   A 1 1802 ? -91.84300  54.72300  -6.57900  1.000 97.00775  ?  1800 VAL   A C   1 
ATOM   13861 O  O   . VAL   A 1 1802 ? -91.84400  55.80900  -5.98600  1.000 103.47279 ?  1800 VAL   A O   1 
ATOM   13862 C  CB  . VAL   A 1 1802 ? -91.33400  53.07000  -4.74600  1.000 76.35827  ?  1800 VAL   A CB  1 
ATOM   13863 N  N   . VAL   A 1 1803 ? -92.63500  54.47300  -7.62000  1.000 83.36999  ?  1801 VAL   A N   1 
ATOM   13864 C  CA  . VAL   A 1 1803 ? -93.59000  55.44300  -8.14300  1.000 80.68128  ?  1801 VAL   A CA  1 
ATOM   13865 C  C   . VAL   A 1 1803 ? -94.98000  55.05200  -7.66100  1.000 87.39508  ?  1801 VAL   A C   1 
ATOM   13866 O  O   . VAL   A 1 1803 ? -95.35400  53.87300  -7.70400  1.000 84.10659  ?  1801 VAL   A O   1 
ATOM   13867 C  CB  . VAL   A 1 1803 ? -93.53700  55.51500  -9.68000  1.000 79.85659  ?  1801 VAL   A CB  1 
ATOM   13868 C  CG1 . VAL   A 1 1803 ? -94.30500  56.72900  -10.17500 1.000 68.99268  ?  1801 VAL   A CG1 1 
ATOM   13869 C  CG2 . VAL   A 1 1803 ? -92.09500  55.55700  -10.16600 1.000 87.00817  ?  1801 VAL   A CG2 1 
ATOM   13870 N  N   . ILE   A 1 1804 ? -95.74300  56.03900  -7.19200  1.000 92.11401  ?  1802 ILE   A N   1 
ATOM   13871 C  CA  . ILE   A 1 1804 ? -97.05400  55.82000  -6.59900  1.000 84.03951  ?  1802 ILE   A CA  1 
ATOM   13872 C  C   . ILE   A 1 1804 ? -98.06700  56.68500  -7.34500  1.000 67.00157  ?  1802 ILE   A C   1 
ATOM   13873 O  O   . ILE   A 1 1804 ? -97.70900  57.61200  -8.07500  1.000 59.62342  ?  1802 ILE   A O   1 
ATOM   13874 C  CB  . ILE   A 1 1804 ? -97.06500  56.12700  -5.08200  1.000 78.41318  ?  1802 ILE   A CB  1 
ATOM   13875 C  CG1 . ILE   A 1 1804 ? -95.76800  55.65100  -4.41700  1.000 83.09634  ?  1802 ILE   A CG1 1 
ATOM   13876 C  CG2 . ILE   A 1 1804 ? -98.24200  55.45200  -4.38900  1.000 60.54061  ?  1802 ILE   A CG2 1 
ATOM   13877 C  CD1 . ILE   A 1 1804 ? -94.66700  56.69900  -4.34600  1.000 77.16581  ?  1802 ILE   A CD1 1 
ATOM   13878 N  N   . GLU   A 1 1805 ? -99.35200  56.36000  -7.16700  1.000 72.33799  ?  1803 GLU   A N   1 
ATOM   13879 C  CA  . GLU   A 1 1805 ? -100.42400 57.04200  -7.89800  1.000 62.73124  ?  1803 GLU   A CA  1 
ATOM   13880 C  C   . GLU   A 1 1805 ? -101.68800 57.03000  -7.03200  1.000 60.91165  ?  1803 GLU   A C   1 
ATOM   13881 O  O   . GLU   A 1 1805 ? -102.45800 56.06700  -7.05200  1.000 63.55715  ?  1803 GLU   A O   1 
ATOM   13882 C  CB  . GLU   A 1 1805 ? -100.65900 56.38500  -9.25200  1.000 61.03699  ?  1803 GLU   A CB  1 
ATOM   13883 C  CG  . GLU   A 1 1805 ? -100.49900 54.86400  -9.25700  1.000 72.41466  ?  1803 GLU   A CG  1 
ATOM   13884 C  CD  . GLU   A 1 1805 ? -99.22100  54.39900  -9.94100  1.000 67.53525  ?  1803 GLU   A CD  1 
ATOM   13885 O  OE1 . GLU   A 1 1805 ? -98.16400  55.03500  -9.75000  1.000 71.78260  ?  1803 GLU   A OE1 1 
ATOM   13886 O  OE2 . GLU   A 1 1805 ? -99.27700  53.39300  -10.68000 1.000 75.92414  -1 1803 GLU   A OE2 1 
ATOM   13887 N  N   . ALA   A 1 1806 ? -101.89500 58.12000  -6.28400  1.000 53.17260  ?  1804 ALA   A N   1 
ATOM   13888 C  CA  . ALA   A 1 1806 ? -103.07300 58.25100  -5.43000  1.000 69.58248  ?  1804 ALA   A CA  1 
ATOM   13889 C  C   . ALA   A 1 1806 ? -103.25900 59.67200  -4.90300  1.000 59.16372  ?  1804 ALA   A C   1 
ATOM   13890 O  O   . ALA   A 1 1806 ? -103.49600 60.60100  -5.68300  1.000 53.10939  ?  1804 ALA   A O   1 
ATOM   13891 C  CB  . ALA   A 1 1806 ? -102.99400 57.27300  -4.25400  1.000 74.45958  ?  1804 ALA   A CB  1 
ATOM   13892 N  N   . ALA   A 1 1807 ? -103.16000 59.83100  -3.57700  1.000 55.20327  ?  1805 ALA   A N   1 
ATOM   13893 C  CA  . ALA   A 1 1807 ? -103.42100 61.07100  -2.84400  1.000 36.77224  ?  1805 ALA   A CA  1 
ATOM   13894 C  C   . ALA   A 1 1807 ? -104.90700 61.40900  -2.85500  1.000 52.63190  ?  1805 ALA   A C   1 
ATOM   13895 O  O   . ALA   A 1 1807 ? -105.71500 60.69400  -2.25300  1.000 70.07495  ?  1805 ALA   A O   1 
ATOM   13896 C  CB  . ALA   A 1 1807 ? -102.60000 62.23800  -3.40100  1.000 56.01376  ?  1805 ALA   A CB  1 
ATOM   13897 N  N   . ALA   A 1 1808 ? -105.27600 62.50300  -3.51400  1.000 63.68987  ?  1806 ALA   A N   1 
ATOM   13898 C  CA  . ALA   A 1 1808 ? -106.67400 62.86700  -3.71300  1.000 52.81497  ?  1806 ALA   A CA  1 
ATOM   13899 C  C   . ALA   A 1 1808 ? -107.05200 62.48700  -5.13900  1.000 50.65732  ?  1806 ALA   A C   1 
ATOM   13900 O  O   . ALA   A 1 1808 ? -106.51400 63.04700  -6.09900  1.000 53.60570  ?  1806 ALA   A O   1 
ATOM   13901 C  CB  . ALA   A 1 1808 ? -106.90000 64.35500  -3.45400  1.000 42.50556  ?  1806 ALA   A CB  1 
ATOM   13902 N  N   . GLU   A 1 1809 ? -107.96000 61.52400  -5.27900  1.000 60.51623  ?  1807 GLU   A N   1 
ATOM   13903 C  CA  . GLU   A 1 1809 ? -108.33700 61.00600  -6.58900  1.000 67.50099  ?  1807 GLU   A CA  1 
ATOM   13904 C  C   . GLU   A 1 1809 ? -109.64100 61.59000  -7.11200  1.000 69.36181  ?  1807 GLU   A C   1 
ATOM   13905 O  O   . GLU   A 1 1809 ? -109.71900 61.96500  -8.28600  1.000 79.57674  ?  1807 GLU   A O   1 
ATOM   13906 C  CB  . GLU   A 1 1809 ? -108.44400 59.47800  -6.53800  1.000 71.48337  ?  1807 GLU   A CB  1 
ATOM   13907 C  CG  . GLU   A 1 1809 ? -107.20500 58.79600  -5.98000  1.000 66.78706  ?  1807 GLU   A CG  1 
ATOM   13908 C  CD  . GLU   A 1 1809 ? -107.30000 57.28500  -6.01700  1.000 91.48904  ?  1807 GLU   A CD  1 
ATOM   13909 O  OE1 . GLU   A 1 1809 ? -108.18000 56.76000  -6.73200  1.000 78.33084  ?  1807 GLU   A OE1 1 
ATOM   13910 O  OE2 . GLU   A 1 1809 ? -106.49500 56.62100  -5.32900  1.000 108.54529 -1 1807 GLU   A OE2 1 
ATOM   13911 N  N   . ASN   A 1 1810 ? -110.66800 61.67800  -6.27000  1.000 49.94949  ?  1808 ASN   A N   1 
ATOM   13912 C  CA  . ASN   A 1 1810 ? -111.96600 62.21200  -6.65700  1.000 64.71529  ?  1808 ASN   A CA  1 
ATOM   13913 C  C   . ASN   A 1 1810 ? -112.25900 63.46500  -5.84400  1.000 49.61250  ?  1808 ASN   A C   1 
ATOM   13914 O  O   . ASN   A 1 1810 ? -112.05000 63.48200  -4.62700  1.000 52.38631  ?  1808 ASN   A O   1 
ATOM   13915 C  CB  . ASN   A 1 1810 ? -113.07200 61.17200  -6.45300  1.000 66.69251  ?  1808 ASN   A CB  1 
ATOM   13916 C  CG  . ASN   A 1 1810 ? -112.98600 60.03400  -7.44900  1.000 84.26369  ?  1808 ASN   A CG  1 
ATOM   13917 O  OD1 . ASN   A 1 1810 ? -112.82900 60.26000  -8.65000  1.000 74.73161  ?  1808 ASN   A OD1 1 
ATOM   13918 N  ND2 . ASN   A 1 1810 ? -113.07800 58.80500  -6.95700  1.000 78.31171  ?  1808 ASN   A ND2 1 
ATOM   13919 N  N   . LEU   A 1 1811 ? -112.73800 64.50800  -6.52000  1.000 40.57080  ?  1809 LEU   A N   1 
ATOM   13920 C  CA  . LEU   A 1 1811 ? -113.06300 65.78300  -5.89800  1.000 30.70293  ?  1809 LEU   A CA  1 
ATOM   13921 C  C   . LEU   A 1 1811 ? -114.54700 66.07400  -6.06200  1.000 40.88306  ?  1809 LEU   A C   1 
ATOM   13922 O  O   . LEU   A 1 1811 ? -115.14000 65.75900  -7.09800  1.000 68.66316  ?  1809 LEU   A O   1 
ATOM   13923 C  CB  . LEU   A 1 1811 ? -112.24300 66.92600  -6.51000  1.000 44.47142  ?  1809 LEU   A CB  1 
ATOM   13924 C  CG  . LEU   A 1 1811 ? -111.15300 67.57200  -5.65100  1.000 53.65961  ?  1809 LEU   A CG  1 
ATOM   13925 C  CD1 . LEU   A 1 1811 ? -110.05700 66.57500  -5.31000  1.000 54.89330  ?  1809 LEU   A CD1 1 
ATOM   13926 C  CD2 . LEU   A 1 1811 ? -110.57200 68.79100  -6.35600  1.000 54.53609  ?  1809 LEU   A CD2 1 
ATOM   13927 N  N   . TYR   A 1 1812 ? -115.14100 66.68900  -5.04100  1.000 44.19739  ?  1810 TYR   A N   1 
ATOM   13928 C  CA  . TYR   A 1 1812 ? -116.56100 67.03600  -5.04000  1.000 49.85502  ?  1810 TYR   A CA  1 
ATOM   13929 C  C   . TYR   A 1 1812 ? -116.69400 68.49400  -4.61700  1.000 50.47378  ?  1810 TYR   A C   1 
ATOM   13930 O  O   . TYR   A 1 1812 ? -116.56200 68.81800  -3.43400  1.000 56.12945  ?  1810 TYR   A O   1 
ATOM   13931 C  CB  . TYR   A 1 1812 ? -117.35600 66.11400  -4.11400  1.000 47.44968  ?  1810 TYR   A CB  1 
ATOM   13932 C  CG  . TYR   A 1 1812 ? -117.14800 64.63800  -4.37300  1.000 52.94977  ?  1810 TYR   A CG  1 
ATOM   13933 C  CD1 . TYR   A 1 1812 ? -117.82500 63.98700  -5.39800  1.000 51.16577  ?  1810 TYR   A CD1 1 
ATOM   13934 C  CD2 . TYR   A 1 1812 ? -116.28100 63.89200  -3.58400  1.000 59.49983  ?  1810 TYR   A CD2 1 
ATOM   13935 C  CE1 . TYR   A 1 1812 ? -117.63800 62.63400  -5.63200  1.000 59.62657  ?  1810 TYR   A CE1 1 
ATOM   13936 C  CE2 . TYR   A 1 1812 ? -116.09000 62.54000  -3.81200  1.000 66.06605  ?  1810 TYR   A CE2 1 
ATOM   13937 C  CZ  . TYR   A 1 1812 ? -116.76900 61.91600  -4.83500  1.000 63.34303  ?  1810 TYR   A CZ  1 
ATOM   13938 O  OH  . TYR   A 1 1812 ? -116.57700 60.57400  -5.05900  1.000 56.58099  ?  1810 TYR   A OH  1 
ATOM   13939 N  N   . PHE   A 1 1813 ? -116.95000 69.37100  -5.58400  1.000 45.04035  ?  1811 PHE   A N   1 
ATOM   13940 C  CA  . PHE   A 1 1813 ? -117.14400 70.79300  -5.31900  1.000 48.26666  ?  1811 PHE   A CA  1 
ATOM   13941 C  C   . PHE   A 1 1813 ? -118.47800 70.97700  -4.60700  1.000 54.74240  ?  1811 PHE   A C   1 
ATOM   13942 O  O   . PHE   A 1 1813 ? -119.53500 70.96600  -5.24200  1.000 70.57476  ?  1811 PHE   A O   1 
ATOM   13943 C  CB  . PHE   A 1 1813 ? -117.10200 71.59100  -6.62400  1.000 38.80052  ?  1811 PHE   A CB  1 
ATOM   13944 C  CG  . PHE   A 1 1813 ? -115.71800 71.76500  -7.19200  1.000 52.48519  ?  1811 PHE   A CG  1 
ATOM   13945 C  CD1 . PHE   A 1 1813 ? -114.96900 70.67100  -7.58900  1.000 53.39454  ?  1811 PHE   A CD1 1 
ATOM   13946 C  CD2 . PHE   A 1 1813 ? -115.17600 73.03300  -7.34400  1.000 48.97076  ?  1811 PHE   A CD2 1 
ATOM   13947 C  CE1 . PHE   A 1 1813 ? -113.69900 70.83400  -8.11100  1.000 60.35350  ?  1811 PHE   A CE1 1 
ATOM   13948 C  CE2 . PHE   A 1 1813 ? -113.90500 73.20000  -7.86800  1.000 55.55176  ?  1811 PHE   A CE2 1 
ATOM   13949 C  CZ  . PHE   A 1 1813 ? -113.16900 72.09900  -8.25300  1.000 61.77381  ?  1811 PHE   A CZ  1 
ATOM   13950 N  N   . GLN   A 1 1814 ? -118.43600 71.13900  -3.28800  1.000 71.17312  ?  1812 GLN   A N   1 
ATOM   13951 C  CA  . GLN   A 1 1814 ? -119.64400 71.34200  -2.49300  1.000 70.60903  ?  1812 GLN   A CA  1 
ATOM   13952 C  C   . GLN   A 1 1814 ? -120.47000 72.51000  -3.02600  1.000 87.66645  ?  1812 GLN   A C   1 
ATOM   13953 O  O   . GLN   A 1 1814 ? -121.67500 72.38600  -3.24100  1.000 85.30919  ?  1812 GLN   A O   1 
ATOM   13954 C  CB  . GLN   A 1 1814 ? -119.29900 71.60400  -1.02300  1.000 57.55941  ?  1812 GLN   A CB  1 
ATOM   13955 C  CG  . GLN   A 1 1814 ? -118.27200 70.66500  -0.42800  1.000 61.06657  ?  1812 GLN   A CG  1 
ATOM   13956 C  CD  . GLN   A 1 1814 ? -118.21900 70.75800  1.08500   1.000 78.55847  ?  1812 GLN   A CD  1 
ATOM   13957 O  OE1 . GLN   A 1 1814 ? -118.92500 71.56500  1.69200   1.000 67.89261  ?  1812 GLN   A OE1 1 
ATOM   13958 N  NE2 . GLN   A 1 1814 ? -117.38700 69.92800  1.70300   1.000 58.62253  ?  1812 GLN   A NE2 1 
ATOM   13959 O  OXT . GLN   A 1 1814 ? -119.94300 73.60000  -3.25300  1.000 66.16138  ?  1812 GLN   A OXT 1 
ATOM   13960 N  N   . MET   B 1 1    ? 98.14400   50.74800  -22.30700 1.000 69.88685  ?  1    MET   B N   1 
ATOM   13961 C  CA  . MET   B 1 1    ? 97.06100   50.21400  -23.12600 1.000 92.46174  ?  1    MET   B CA  1 
ATOM   13962 C  C   . MET   B 1 1    ? 96.73000   51.14100  -24.28500 1.000 110.61229 ?  1    MET   B C   1 
ATOM   13963 O  O   . MET   B 1 1    ? 97.02700   50.84000  -25.44200 1.000 123.73439 ?  1    MET   B O   1 
ATOM   13964 C  CB  . MET   B 1 1    ? 95.80900   49.97900  -22.27900 1.000 62.31441  ?  1    MET   B CB  1 
ATOM   13965 C  CG  . MET   B 1 1    ? 94.61500   49.47800  -23.08000 1.000 69.44033  ?  1    MET   B CG  1 
ATOM   13966 S  SD  . MET   B 1 1    ? 93.26400   48.90400  -22.03500 1.000 108.16246 ?  1    MET   B SD  1 
ATOM   13967 C  CE  . MET   B 1 1    ? 94.10200   48.76800  -20.45900 1.000 58.24708  ?  1    MET   B CE  1 
ATOM   13968 N  N   . GLY   B 1 2    ? 96.10600   52.27200  -23.96500 1.000 95.08428  ?  2    GLY   B N   1 
ATOM   13969 C  CA  . GLY   B 1 2    ? 95.73000   53.25100  -24.96600 1.000 80.66641  ?  2    GLY   B CA  1 
ATOM   13970 C  C   . GLY   B 1 2    ? 95.66600   54.66300  -24.42100 1.000 80.69427  ?  2    GLY   B C   1 
ATOM   13971 O  O   . GLY   B 1 2    ? 95.27300   54.87600  -23.27100 1.000 75.68020  ?  2    GLY   B O   1 
ATOM   13972 N  N   . ARG   B 1 3    ? 96.05300   55.63800  -25.24000 1.000 73.07382  ?  3    ARG   B N   1 
ATOM   13973 C  CA  . ARG   B 1 3    ? 96.01100   57.04300  -24.84700 1.000 74.65538  ?  3    ARG   B CA  1 
ATOM   13974 C  C   . ARG   B 1 3    ? 94.68300   57.63000  -25.30900 1.000 78.86861  ?  3    ARG   B C   1 
ATOM   13975 O  O   . ARG   B 1 3    ? 94.42300   57.72800  -26.51200 1.000 74.69600  ?  3    ARG   B O   1 
ATOM   13976 C  CB  . ARG   B 1 3    ? 97.19300   57.81000  -25.43400 1.000 72.79803  ?  3    ARG   B CB  1 
ATOM   13977 C  CG  . ARG   B 1 3    ? 97.97800   58.61500  -24.40500 1.000 72.38957  ?  3    ARG   B CG  1 
ATOM   13978 C  CD  . ARG   B 1 3    ? 99.26900   59.16200  -24.99500 1.000 62.34059  ?  3    ARG   B CD  1 
ATOM   13979 N  NE  . ARG   B 1 3    ? 99.07700   60.43900  -25.67200 1.000 75.38684  ?  3    ARG   B NE  1 
ATOM   13980 C  CZ  . ARG   B 1 3    ? 99.23900   61.62200  -25.09500 1.000 84.05934  ?  3    ARG   B CZ  1 
ATOM   13981 N  NH1 . ARG   B 1 3    ? 99.58300   61.72800  -23.82100 1.000 84.18953  ?  3    ARG   B NH1 1 
ATOM   13982 N  NH2 . ARG   B 1 3    ? 99.05300   62.72700  -25.81300 1.000 64.49569  ?  3    ARG   B NH2 1 
ATOM   13983 N  N   . ILE   B 1 4    ? 93.84200   58.01800  -24.35400 1.000 64.95713  ?  4    ILE   B N   1 
ATOM   13984 C  CA  . ILE   B 1 4    ? 92.50100   58.51300  -24.63800 1.000 44.25469  ?  4    ILE   B CA  1 
ATOM   13985 C  C   . ILE   B 1 4    ? 92.49200   60.02500  -24.48000 1.000 55.77167  ?  4    ILE   B C   1 
ATOM   13986 O  O   . ILE   B 1 4    ? 92.98700   60.55700  -23.47800 1.000 57.53460  ?  4    ILE   B O   1 
ATOM   13987 C  CB  . ILE   B 1 4    ? 91.46000   57.86300  -23.71200 1.000 45.18832  ?  4    ILE   B CB  1 
ATOM   13988 C  CG1 . ILE   B 1 4    ? 91.63000   56.34500  -23.70000 1.000 54.41988  ?  4    ILE   B CG1 1 
ATOM   13989 C  CG2 . ILE   B 1 4    ? 90.05200   58.24100  -24.14800 1.000 52.32605  ?  4    ILE   B CG2 1 
ATOM   13990 C  CD1 . ILE   B 1 4    ? 90.68200   55.64200  -22.76000 1.000 56.33161  ?  4    ILE   B CD1 1 
ATOM   13991 N  N   . LEU   B 1 5    ? 91.93100   60.71800  -25.46600 1.000 61.05884  ?  5    LEU   B N   1 
ATOM   13992 C  CA  . LEU   B 1 5    ? 91.71100   62.16000  -25.39100 1.000 54.90269  ?  5    LEU   B CA  1 
ATOM   13993 C  C   . LEU   B 1 5    ? 90.24800   62.38100  -25.03000 1.000 59.06581  ?  5    LEU   B C   1 
ATOM   13994 O  O   . LEU   B 1 5    ? 89.36000   62.24500  -25.87600 1.000 55.82947  ?  5    LEU   B O   1 
ATOM   13995 C  CB  . LEU   B 1 5    ? 92.06900   62.84300  -26.70600 1.000 42.64329  ?  5    LEU   B CB  1 
ATOM   13996 C  CG  . LEU   B 1 5    ? 91.72000   64.33200  -26.75200 1.000 44.81242  ?  5    LEU   B CG  1 
ATOM   13997 C  CD1 . LEU   B 1 5    ? 92.58800   65.11700  -25.78300 1.000 46.46926  ?  5    LEU   B CD1 1 
ATOM   13998 C  CD2 . LEU   B 1 5    ? 91.84900   64.87800  -28.16000 1.000 55.46821  ?  5    LEU   B CD2 1 
ATOM   13999 N  N   . PHE   B 1 6    ? 89.99500   62.71400  -23.76800 1.000 52.83173  ?  6    PHE   B N   1 
ATOM   14000 C  CA  . PHE   B 1 6    ? 88.63400   62.96400  -23.31400 1.000 48.26338  ?  6    PHE   B CA  1 
ATOM   14001 C  C   . PHE   B 1 6    ? 88.23800   64.39100  -23.66700 1.000 55.52205  ?  6    PHE   B C   1 
ATOM   14002 O  O   . PHE   B 1 6    ? 88.87000   65.35000  -23.20900 1.000 44.79165  ?  6    PHE   B O   1 
ATOM   14003 C  CB  . PHE   B 1 6    ? 88.50900   62.72500  -21.81200 1.000 44.19994  ?  6    PHE   B CB  1 
ATOM   14004 C  CG  . PHE   B 1 6    ? 87.09000   62.65000  -21.33500 1.000 38.37482  ?  6    PHE   B CG  1 
ATOM   14005 C  CD1 . PHE   B 1 6    ? 86.39400   61.45400  -21.38900 1.000 38.46823  ?  6    PHE   B CD1 1 
ATOM   14006 C  CD2 . PHE   B 1 6    ? 86.44800   63.77300  -20.84300 1.000 45.51441  ?  6    PHE   B CD2 1 
ATOM   14007 C  CE1 . PHE   B 1 6    ? 85.08600   61.37900  -20.95500 1.000 45.83180  ?  6    PHE   B CE1 1 
ATOM   14008 C  CE2 . PHE   B 1 6    ? 85.14000   63.70500  -20.40800 1.000 44.10598  ?  6    PHE   B CE2 1 
ATOM   14009 C  CZ  . PHE   B 1 6    ? 84.45800   62.50600  -20.46400 1.000 42.81440  ?  6    PHE   B CZ  1 
ATOM   14010 N  N   . LEU   B 1 7    ? 87.19500   64.53100  -24.47900 1.000 52.06862  ?  7    LEU   B N   1 
ATOM   14011 C  CA  . LEU   B 1 7    ? 86.70900   65.83200  -24.91700 1.000 49.24413  ?  7    LEU   B CA  1 
ATOM   14012 C  C   . LEU   B 1 7    ? 85.44900   66.18700  -24.13800 1.000 48.76262  ?  7    LEU   B C   1 
ATOM   14013 O  O   . LEU   B 1 7    ? 84.45900   65.45000  -24.17800 1.000 51.84031  ?  7    LEU   B O   1 
ATOM   14014 C  CB  . LEU   B 1 7    ? 86.43100   65.83100  -26.41900 1.000 49.97513  ?  7    LEU   B CB  1 
ATOM   14015 C  CG  . LEU   B 1 7    ? 87.67000   65.72600  -27.30700 1.000 44.34075  ?  7    LEU   B CG  1 
ATOM   14016 C  CD1 . LEU   B 1 7    ? 87.28800   65.82700  -28.77200 1.000 44.55990  ?  7    LEU   B CD1 1 
ATOM   14017 C  CD2 . LEU   B 1 7    ? 88.67200   66.80400  -26.93200 1.000 53.84726  ?  7    LEU   B CD2 1 
ATOM   14018 N  N   . THR   B 1 8    ? 85.49300   67.31200  -23.43000 1.000 38.95078  ?  8    THR   B N   1 
ATOM   14019 C  CA  . THR   B 1 8    ? 84.33300   67.80700  -22.70700 1.000 47.07949  ?  8    THR   B CA  1 
ATOM   14020 C  C   . THR   B 1 8    ? 84.42300   69.32100  -22.62100 1.000 55.19209  ?  8    THR   B C   1 
ATOM   14021 O  O   . THR   B 1 8    ? 85.48700   69.90900  -22.81900 1.000 65.06471  ?  8    THR   B O   1 
ATOM   14022 C  CB  . THR   B 1 8    ? 84.23100   67.20000  -21.30500 1.000 45.58047  ?  8    THR   B CB  1 
ATOM   14023 O  OG1 . THR   B 1 8    ? 83.02000   67.64500  -20.68800 1.000 60.92600  ?  8    THR   B OG1 1 
ATOM   14024 C  CG2 . THR   B 1 8    ? 85.41300   67.63100  -20.45300 1.000 51.05182  ?  8    THR   B CG2 1 
ATOM   14025 N  N   . THR   B 1 9    ? 83.28800   69.95100  -22.33100 1.000 47.73457  ?  9    THR   B N   1 
ATOM   14026 C  CA  . THR   B 1 9    ? 83.25600   71.39800  -22.16100 1.000 45.20828  ?  9    THR   B CA  1 
ATOM   14027 C  C   . THR   B 1 9    ? 82.33900   71.76100  -21.00400 1.000 52.17979  ?  9    THR   B C   1 
ATOM   14028 O  O   . THR   B 1 9    ? 82.64800   72.65600  -20.21100 1.000 62.51942  ?  9    THR   B O   1 
ATOM   14029 C  CB  . THR   B 1 9    ? 82.80200   72.09000  -23.45100 1.000 50.78523  ?  9    THR   B CB  1 
ATOM   14030 O  OG1 . THR   B 1 9    ? 83.77200   71.87000  -24.48200 1.000 70.06718  ?  9    THR   B OG1 1 
ATOM   14031 C  CG2 . THR   B 1 9    ? 82.64100   73.58800  -23.23300 1.000 60.44314  ?  9    THR   B CG2 1 
ATOM   14032 N  N   . PHE   B 1 10   ? 81.21800   71.05500  -20.88800 1.000 47.57066  ?  10   PHE   B N   1 
ATOM   14033 C  CA  . PHE   B 1 10   ? 80.22900   71.32900  -19.85600 1.000 51.86073  ?  10   PHE   B CA  1 
ATOM   14034 C  C   . PHE   B 1 10   ? 80.25700   70.31100  -18.72800 1.000 52.10326  ?  10   PHE   B C   1 
ATOM   14035 O  O   . PHE   B 1 10   ? 79.53200   70.47700  -17.74200 1.000 51.56011  ?  10   PHE   B O   1 
ATOM   14036 C  CB  . PHE   B 1 10   ? 78.83200   71.39200  -20.47700 1.000 50.36557  ?  10   PHE   B CB  1 
ATOM   14037 C  CG  . PHE   B 1 10   ? 78.76100   72.24400  -21.71000 1.000 49.91493  ?  10   PHE   B CG  1 
ATOM   14038 C  CD1 . PHE   B 1 10   ? 79.00100   73.60700  -21.64100 1.000 41.39811  ?  10   PHE   B CD1 1 
ATOM   14039 C  CD2 . PHE   B 1 10   ? 78.45800   71.68400  -22.93900 1.000 50.13580  ?  10   PHE   B CD2 1 
ATOM   14040 C  CE1 . PHE   B 1 10   ? 78.94000   74.39500  -22.77500 1.000 47.91575  ?  10   PHE   B CE1 1 
ATOM   14041 C  CE2 . PHE   B 1 10   ? 78.39300   72.46600  -24.07600 1.000 55.08563  ?  10   PHE   B CE2 1 
ATOM   14042 C  CZ  . PHE   B 1 10   ? 78.63400   73.82300  -23.99500 1.000 53.57454  ?  10   PHE   B CZ  1 
ATOM   14043 N  N   . MET   B 1 11   ? 81.06900   69.26700  -18.84600 1.000 53.74575  ?  11   MET   B N   1 
ATOM   14044 C  CA  . MET   B 1 11   ? 81.30700   68.33300  -17.76100 1.000 57.26688  ?  11   MET   B CA  1 
ATOM   14045 C  C   . MET   B 1 11   ? 82.63600   68.67100  -17.09700 1.000 53.63278  ?  11   MET   B C   1 
ATOM   14046 O  O   . MET   B 1 11   ? 83.21700   69.73600  -17.32300 1.000 55.48882  ?  11   MET   B O   1 
ATOM   14047 C  CB  . MET   B 1 11   ? 81.26500   66.89200  -18.27700 1.000 54.84944  ?  11   MET   B CB  1 
ATOM   14048 C  CG  . MET   B 1 11   ? 79.87000   66.41000  -18.62500 1.000 59.44142  ?  11   MET   B CG  1 
ATOM   14049 S  SD  . MET   B 1 11   ? 78.93000   65.95200  -17.15500 1.000 60.64612  ?  11   MET   B SD  1 
ATOM   14050 C  CE  . MET   B 1 11   ? 77.29700   66.54900  -17.58200 1.000 51.50120  ?  11   MET   B CE  1 
ATOM   14051 N  N   . SER   B 1 12   ? 83.12900   67.76000  -16.26800 1.000 60.88380  ?  12   SER   B N   1 
ATOM   14052 C  CA  . SER   B 1 12   ? 84.32200   68.01600  -15.48100 1.000 65.28391  ?  12   SER   B CA  1 
ATOM   14053 C  C   . SER   B 1 12   ? 85.51200   67.23900  -16.02600 1.000 64.88220  ?  12   SER   B C   1 
ATOM   14054 O  O   . SER   B 1 12   ? 85.40600   66.42300  -16.94800 1.000 76.39634  ?  12   SER   B O   1 
ATOM   14055 C  CB  . SER   B 1 12   ? 84.10200   67.65800  -14.00500 1.000 56.95184  ?  12   SER   B CB  1 
ATOM   14056 O  OG  . SER   B 1 12   ? 84.27300   66.26700  -13.78400 1.000 73.74999  ?  12   SER   B OG  1 
ATOM   14057 N  N   . LYS   B 1 13   ? 86.65900   67.53500  -15.42900 1.000 58.47748  ?  13   LYS   B N   1 
ATOM   14058 C  CA  . LYS   B 1 13   ? 87.93400   66.88900  -15.68400 1.000 49.96248  ?  13   LYS   B CA  1 
ATOM   14059 C  C   . LYS   B 1 13   ? 88.11400   65.63500  -14.84000 1.000 52.00129  ?  13   LYS   B C   1 
ATOM   14060 O  O   . LYS   B 1 13   ? 89.10500   64.91900  -15.01200 1.000 64.39907  ?  13   LYS   B O   1 
ATOM   14061 C  CB  . LYS   B 1 13   ? 89.07800   67.87800  -15.40600 1.000 42.44651  ?  13   LYS   B CB  1 
ATOM   14062 C  CG  . LYS   B 1 13   ? 88.74600   69.35400  -15.70100 1.000 60.31991  ?  13   LYS   B CG  1 
ATOM   14063 C  CD  . LYS   B 1 13   ? 88.03700   70.06000  -14.53400 1.000 75.92447  ?  13   LYS   B CD  1 
ATOM   14064 C  CE  . LYS   B 1 13   ? 87.35000   71.34800  -14.99700 1.000 67.69323  ?  13   LYS   B CE  1 
ATOM   14065 N  NZ  . LYS   B 1 13   ? 86.24600   71.77300  -14.08300 1.000 54.23883  ?  13   LYS   B NZ  1 
ATOM   14066 N  N   . GLY   B 1 14   ? 87.18300   65.37100  -13.92600 1.000 48.38696  ?  14   GLY   B N   1 
ATOM   14067 C  CA  . GLY   B 1 14   ? 87.19200   64.17900  -13.10700 1.000 53.48111  ?  14   GLY   B CA  1 
ATOM   14068 C  C   . GLY   B 1 14   ? 85.80100   63.59600  -12.97400 1.000 64.94156  ?  14   GLY   B C   1 
ATOM   14069 O  O   . GLY   B 1 14   ? 85.22300   63.57600  -11.88300 1.000 72.59930  ?  14   GLY   B O   1 
ATOM   14070 N  N   . ASN   B 1 15   ? 85.24700   63.14100  -14.09000 1.000 68.85809  ?  15   ASN   B N   1 
ATOM   14071 C  CA  . ASN   B 1 15   ? 83.95200   62.48300  -14.09600 1.000 58.70673  ?  15   ASN   B CA  1 
ATOM   14072 C  C   . ASN   B 1 15   ? 84.12500   60.99000  -13.85400 1.000 57.86863  ?  15   ASN   B C   1 
ATOM   14073 O  O   . ASN   B 1 15   ? 85.22800   60.44700  -13.92400 1.000 61.11897  ?  15   ASN   B O   1 
ATOM   14074 C  CB  . ASN   B 1 15   ? 83.23500   62.71800  -15.42400 1.000 60.25030  ?  15   ASN   B CB  1 
ATOM   14075 C  CG  . ASN   B 1 15   ? 83.43200   64.12300  -15.94000 1.000 85.09847  ?  15   ASN   B CG  1 
ATOM   14076 O  OD1 . ASN   B 1 15   ? 82.92200   65.08200  -15.36200 1.000 113.98091 ?  15   ASN   B OD1 1 
ATOM   14077 N  ND2 . ASN   B 1 15   ? 84.17400   64.25600  -17.03400 1.000 88.33141  ?  15   ASN   B ND2 1 
ATOM   14078 N  N   . LYS   B 1 16   ? 83.00000   60.33300  -13.55900 1.000 61.71083  ?  16   LYS   B N   1 
ATOM   14079 C  CA  . LYS   B 1 16   ? 82.98700   58.88500  -13.37100 1.000 49.65841  ?  16   LYS   B CA  1 
ATOM   14080 C  C   . LYS   B 1 16   ? 83.68000   58.17800  -14.52700 1.000 56.97438  ?  16   LYS   B C   1 
ATOM   14081 O  O   . LYS   B 1 16   ? 84.41600   57.20600  -14.32100 1.000 67.61967  ?  16   LYS   B O   1 
ATOM   14082 C  CB  . LYS   B 1 16   ? 81.54400   58.38700  -13.23400 1.000 40.22483  ?  16   LYS   B CB  1 
ATOM   14083 C  CG  . LYS   B 1 16   ? 81.20900   57.72900  -11.90200 1.000 52.05002  ?  16   LYS   B CG  1 
ATOM   14084 C  CD  . LYS   B 1 16   ? 79.89200   56.95900  -11.98800 1.000 47.71644  ?  16   LYS   B CD  1 
ATOM   14085 C  CE  . LYS   B 1 16   ? 79.54900   56.26900  -10.67300 1.000 43.45831  ?  16   LYS   B CE  1 
ATOM   14086 N  NZ  . LYS   B 1 16   ? 79.02700   57.22500  -9.65500  1.000 56.29457  ?  16   LYS   B NZ  1 
ATOM   14087 N  N   . VAL   B 1 17   ? 83.47000   58.66900  -15.75000 1.000 57.97758  ?  17   VAL   B N   1 
ATOM   14088 C  CA  . VAL   B 1 17   ? 84.04900   58.02700  -16.92500 1.000 55.01172  ?  17   VAL   B CA  1 
ATOM   14089 C  C   . VAL   B 1 17   ? 85.56500   58.18800  -16.94000 1.000 49.01827  ?  17   VAL   B C   1 
ATOM   14090 O  O   . VAL   B 1 17   ? 86.29800   57.23000  -17.21000 1.000 60.10397  ?  17   VAL   B O   1 
ATOM   14091 C  CB  . VAL   B 1 17   ? 83.39800   58.58200  -18.20500 1.000 44.83003  ?  17   VAL   B CB  1 
ATOM   14092 C  CG1 . VAL   B 1 17   ? 82.03900   57.93900  -18.41800 1.000 57.84753  ?  17   VAL   B CG1 1 
ATOM   14093 C  CG2 . VAL   B 1 17   ? 83.25200   60.09600  -18.11900 1.000 60.75436  ?  17   VAL   B CG2 1 
ATOM   14094 N  N   . VAL   B 1 18   ? 86.06200   59.39100  -16.64300 1.000 50.47625  ?  18   VAL   B N   1 
ATOM   14095 C  CA  . VAL   B 1 18   ? 87.50500   59.61500  -16.64700 1.000 65.54856  ?  18   VAL   B CA  1 
ATOM   14096 C  C   . VAL   B 1 18   ? 88.17300   58.81100  -15.53900 1.000 62.19160  ?  18   VAL   B C   1 
ATOM   14097 O  O   . VAL   B 1 18   ? 89.22400   58.19300  -15.74800 1.000 59.55230  ?  18   VAL   B O   1 
ATOM   14098 C  CB  . VAL   B 1 18   ? 87.81500   61.11900  -16.52400 1.000 46.73180  ?  18   VAL   B CB  1 
ATOM   14099 C  CG1 . VAL   B 1 18   ? 89.31300   61.34600  -16.37300 1.000 53.19770  ?  18   VAL   B CG1 1 
ATOM   14100 C  CG2 . VAL   B 1 18   ? 87.28900   61.86200  -17.73700 1.000 47.76730  ?  18   VAL   B CG2 1 
ATOM   14101 N  N   . ARG   B 1 19   ? 87.57100   58.79800  -14.34800 1.000 52.04051  ?  19   ARG   B N   1 
ATOM   14102 C  CA  . ARG   B 1 19   ? 88.13100   58.02200  -13.24800 1.000 50.48248  ?  19   ARG   B CA  1 
ATOM   14103 C  C   . ARG   B 1 19   ? 88.06000   56.52800  -13.53800 1.000 49.11955  ?  19   ARG   B C   1 
ATOM   14104 O  O   . ARG   B 1 19   ? 88.98100   55.77800  -13.19200 1.000 57.79990  ?  19   ARG   B O   1 
ATOM   14105 C  CB  . ARG   B 1 19   ? 87.40100   58.35800  -11.94800 1.000 54.61194  ?  19   ARG   B CB  1 
ATOM   14106 C  CG  . ARG   B 1 19   ? 87.41100   59.83900  -11.60000 1.000 55.20897  ?  19   ARG   B CG  1 
ATOM   14107 C  CD  . ARG   B 1 19   ? 86.85900   60.07500  -10.20400 1.000 54.73378  ?  19   ARG   B CD  1 
ATOM   14108 N  NE  . ARG   B 1 19   ? 85.51600   59.52900  -10.04800 1.000 70.94731  ?  19   ARG   B NE  1 
ATOM   14109 C  CZ  . ARG   B 1 19   ? 84.40700   60.25600  -10.02900 1.000 73.51777  ?  19   ARG   B CZ  1 
ATOM   14110 N  NH1 . ARG   B 1 19   ? 84.44300   61.57500  -10.13100 1.000 73.49788  ?  19   ARG   B NH1 1 
ATOM   14111 N  NH2 . ARG   B 1 19   ? 83.23300   59.64500  -9.89900  1.000 59.50277  ?  19   ARG   B NH2 1 
ATOM   14112 N  N   . TYR   B 1 20   ? 86.97600   56.07600  -14.17200 1.000 47.17136  ?  20   TYR   B N   1 
ATOM   14113 C  CA  . TYR   B 1 20   ? 86.88700   54.67400  -14.56500 1.000 49.72864  ?  20   TYR   B CA  1 
ATOM   14114 C  C   . TYR   B 1 20   ? 87.88800   54.34900  -15.66500 1.000 50.66640  ?  20   TYR   B C   1 
ATOM   14115 O  O   . TYR   B 1 20   ? 88.50100   53.27400  -15.65700 1.000 49.91956  ?  20   TYR   B O   1 
ATOM   14116 C  CB  . TYR   B 1 20   ? 85.46500   54.34000  -15.01400 1.000 44.42370  ?  20   TYR   B CB  1 
ATOM   14117 C  CG  . TYR   B 1 20   ? 85.34800   53.02500  -15.74800 1.000 40.22571  ?  20   TYR   B CG  1 
ATOM   14118 C  CD1 . TYR   B 1 20   ? 85.32700   51.82100  -15.05700 1.000 33.02443  ?  20   TYR   B CD1 1 
ATOM   14119 C  CD2 . TYR   B 1 20   ? 85.25600   52.98700  -17.13300 1.000 51.20451  ?  20   TYR   B CD2 1 
ATOM   14120 C  CE1 . TYR   B 1 20   ? 85.22200   50.61500  -15.72600 1.000 46.36210  ?  20   TYR   B CE1 1 
ATOM   14121 C  CE2 . TYR   B 1 20   ? 85.14900   51.78800  -17.81100 1.000 49.92505  ?  20   TYR   B CE2 1 
ATOM   14122 C  CZ  . TYR   B 1 20   ? 85.13200   50.60500  -17.10300 1.000 45.71400  ?  20   TYR   B CZ  1 
ATOM   14123 O  OH  . TYR   B 1 20   ? 85.02600   49.40900  -17.77500 1.000 48.63702  ?  20   TYR   B OH  1 
ATOM   14124 N  N   . LEU   B 1 21   ? 88.06200   55.26100  -16.62500 1.000 43.66265  ?  21   LEU   B N   1 
ATOM   14125 C  CA  . LEU   B 1 21   ? 89.08000   55.06700  -17.65100 1.000 48.35533  ?  21   LEU   B CA  1 
ATOM   14126 C  C   . LEU   B 1 21   ? 90.47000   55.01000  -17.03200 1.000 56.66697  ?  21   LEU   B C   1 
ATOM   14127 O  O   . LEU   B 1 21   ? 91.27700   54.13500  -17.36700 1.000 59.36214  ?  21   LEU   B O   1 
ATOM   14128 C  CB  . LEU   B 1 21   ? 88.99900   56.18400  -18.69300 1.000 58.64033  ?  21   LEU   B CB  1 
ATOM   14129 C  CG  . LEU   B 1 21   ? 87.86500   56.08700  -19.71300 1.000 52.48025  ?  21   LEU   B CG  1 
ATOM   14130 C  CD1 . LEU   B 1 21   ? 87.94000   57.22900  -20.71500 1.000 47.37378  ?  21   LEU   B CD1 1 
ATOM   14131 C  CD2 . LEU   B 1 21   ? 87.91500   54.74800  -20.41600 1.000 46.29463  ?  21   LEU   B CD2 1 
ATOM   14132 N  N   . GLU   B 1 22   ? 90.76500   55.93600  -16.11600 1.000 59.22515  ?  22   GLU   B N   1 
ATOM   14133 C  CA  . GLU   B 1 22   ? 92.06100   55.92600  -15.44800 1.000 46.83945  ?  22   GLU   B CA  1 
ATOM   14134 C  C   . GLU   B 1 22   ? 92.22500   54.70700  -14.55200 1.000 53.94863  ?  22   GLU   B C   1 
ATOM   14135 O  O   . GLU   B 1 22   ? 93.35000   54.23200  -14.35600 1.000 69.14475  ?  22   GLU   B O   1 
ATOM   14136 C  CB  . GLU   B 1 22   ? 92.24800   57.21400  -14.64700 1.000 27.62200  ?  22   GLU   B CB  1 
ATOM   14137 C  CG  . GLU   B 1 22   ? 92.83400   58.35000  -15.46900 1.000 52.48447  ?  22   GLU   B CG  1 
ATOM   14138 C  CD  . GLU   B 1 22   ? 92.57100   59.71300  -14.86300 1.000 82.06575  ?  22   GLU   B CD  1 
ATOM   14139 O  OE1 . GLU   B 1 22   ? 92.00200   59.77500  -13.75200 1.000 66.09791  ?  22   GLU   B OE1 1 
ATOM   14140 O  OE2 . GLU   B 1 22   ? 92.92900   60.72500  -15.50400 1.000 76.36508  -1 22   GLU   B OE2 1 
ATOM   14141 N  N   . SER   B 1 23   ? 91.12400   54.18400  -14.00400 1.000 51.42937  ?  23   SER   B N   1 
ATOM   14142 C  CA  . SER   B 1 23   ? 91.21000   52.96700  -13.20600 1.000 50.89422  ?  23   SER   B CA  1 
ATOM   14143 C  C   . SER   B 1 23   ? 91.70100   51.79100  -14.04000 1.000 48.69039  ?  23   SER   B C   1 
ATOM   14144 O  O   . SER   B 1 23   ? 92.35100   50.88300  -13.51100 1.000 58.11437  ?  23   SER   B O   1 
ATOM   14145 C  CB  . SER   B 1 23   ? 89.85100   52.64100  -12.58800 1.000 48.35943  ?  23   SER   B CB  1 
ATOM   14146 O  OG  . SER   B 1 23   ? 88.96600   52.11300  -13.56100 1.000 61.70156  ?  23   SER   B OG  1 
ATOM   14147 N  N   . LEU   B 1 24   ? 91.40800   51.79600  -15.34200 1.000 51.27647  ?  24   LEU   B N   1 
ATOM   14148 C  CA  . LEU   B 1 24   ? 91.79600   50.72100  -16.24800 1.000 64.41543  ?  24   LEU   B CA  1 
ATOM   14149 C  C   . LEU   B 1 24   ? 93.16300   50.94700  -16.88400 1.000 68.30777  ?  24   LEU   B C   1 
ATOM   14150 O  O   . LEU   B 1 24   ? 93.40000   50.47300  -18.00300 1.000 67.98483  ?  24   LEU   B O   1 
ATOM   14151 C  CB  . LEU   B 1 24   ? 90.73500   50.54400  -17.33500 1.000 55.44277  ?  24   LEU   B CB  1 
ATOM   14152 C  CG  . LEU   B 1 24   ? 89.29100   50.24300  -16.92900 1.000 47.74631  ?  24   LEU   B CG  1 
ATOM   14153 C  CD1 . LEU   B 1 24   ? 88.39300   50.30600  -18.15100 1.000 60.39992  ?  24   LEU   B CD1 1 
ATOM   14154 C  CD2 . LEU   B 1 24   ? 89.18100   48.88300  -16.26100 1.000 44.03959  ?  24   LEU   B CD2 1 
ATOM   14155 N  N   . HIS   B 1 25   ? 94.06200   51.67100  -16.21200 1.000 57.81825  ?  25   HIS   B N   1 
ATOM   14156 C  CA  . HIS   B 1 25   ? 95.42800   51.90900  -16.68400 1.000 56.36241  ?  25   HIS   B CA  1 
ATOM   14157 C  C   . HIS   B 1 25   ? 95.47200   52.73000  -17.96900 1.000 51.87212  ?  25   HIS   B C   1 
ATOM   14158 O  O   . HIS   B 1 25   ? 96.39200   52.57700  -18.77500 1.000 66.75971  ?  25   HIS   B O   1 
ATOM   14159 C  CB  . HIS   B 1 25   ? 96.19200   50.59600  -16.88700 1.000 78.47349  ?  25   HIS   B CB  1 
ATOM   14160 C  CG  . HIS   B 1 25   ? 96.28300   49.75400  -15.65600 1.000 90.31797  ?  25   HIS   B CG  1 
ATOM   14161 N  ND1 . HIS   B 1 25   ? 96.88100   50.19600  -14.49600 1.000 69.89676  ?  25   HIS   B ND1 1 
ATOM   14162 C  CD2 . HIS   B 1 25   ? 95.85900   48.49300  -15.40500 1.000 99.97445  ?  25   HIS   B CD2 1 
ATOM   14163 C  CE1 . HIS   B 1 25   ? 96.81500   49.24700  -13.58100 1.000 73.07176  ?  25   HIS   B CE1 1 
ATOM   14164 N  NE2 . HIS   B 1 25   ? 96.20400   48.20100  -14.10700 1.000 94.04113  ?  25   HIS   B NE2 1 
ATOM   14165 N  N   . HIS   B 1 26   ? 94.49700   53.60500  -18.18300 1.000 41.95538  ?  26   HIS   B N   1 
ATOM   14166 C  CA  . HIS   B 1 26   ? 94.50800   54.45800  -19.36100 1.000 52.63778  ?  26   HIS   B CA  1 
ATOM   14167 C  C   . HIS   B 1 26   ? 95.15100   55.80100  -19.04300 1.000 53.57604  ?  26   HIS   B C   1 
ATOM   14168 O  O   . HIS   B 1 26   ? 95.09800   56.28700  -17.91000 1.000 56.49051  ?  26   HIS   B O   1 
ATOM   14169 C  CB  . HIS   B 1 26   ? 93.09100   54.67900  -19.89300 1.000 54.11652  ?  26   HIS   B CB  1 
ATOM   14170 C  CG  . HIS   B 1 26   ? 92.57300   53.55000  -20.72800 1.000 66.33888  ?  26   HIS   B CG  1 
ATOM   14171 N  ND1 . HIS   B 1 26   ? 93.02900   53.29800  -22.00400 1.000 73.81122  ?  26   HIS   B ND1 1 
ATOM   14172 C  CD2 . HIS   B 1 26   ? 91.62600   52.61500  -20.47600 1.000 58.21100  ?  26   HIS   B CD2 1 
ATOM   14173 C  CE1 . HIS   B 1 26   ? 92.39100   52.25300  -22.50000 1.000 66.66443  ?  26   HIS   B CE1 1 
ATOM   14174 N  NE2 . HIS   B 1 26   ? 91.53400   51.82000  -21.59300 1.000 55.98901  ?  26   HIS   B NE2 1 
ATOM   14175 N  N   . GLU   B 1 27   ? 95.77300   56.39300  -20.05800 1.000 42.93239  ?  27   GLU   B N   1 
ATOM   14176 C  CA  . GLU   B 1 27   ? 96.29000   57.75600  -19.97300 1.000 53.66834  ?  27   GLU   B CA  1 
ATOM   14177 C  C   . GLU   B 1 27   ? 95.23300   58.66500  -20.58700 1.000 57.51578  ?  27   GLU   B C   1 
ATOM   14178 O  O   . GLU   B 1 27   ? 95.07500   58.71700  -21.80900 1.000 71.62008  ?  27   GLU   B O   1 
ATOM   14179 C  CB  . GLU   B 1 27   ? 97.63400   57.89500  -20.68000 1.000 67.63163  ?  27   GLU   B CB  1 
ATOM   14180 C  CG  . GLU   B 1 27   ? 98.28800   59.25400  -20.46500 1.000 62.62340  ?  27   GLU   B CG  1 
ATOM   14181 C  CD  . GLU   B 1 27   ? 99.51300   59.47000  -21.33400 1.000 77.48415  ?  27   GLU   B CD  1 
ATOM   14182 O  OE1 . GLU   B 1 27   ? 100.08700  58.47300  -21.81900 1.000 75.14070  ?  27   GLU   B OE1 1 
ATOM   14183 O  OE2 . GLU   B 1 27   ? 99.89700   60.64200  -21.53500 1.000 78.02561  -1 27   GLU   B OE2 1 
ATOM   14184 N  N   . VAL   B 1 28   ? 94.50300   59.37400  -19.73500 1.000 49.37876  ?  28   VAL   B N   1 
ATOM   14185 C  CA  . VAL   B 1 28   ? 93.38800   60.21000  -20.16000 1.000 54.96705  ?  28   VAL   B CA  1 
ATOM   14186 C  C   . VAL   B 1 28   ? 93.86100   61.65700  -20.18200 1.000 51.13405  ?  28   VAL   B C   1 
ATOM   14187 O  O   . VAL   B 1 28   ? 94.06700   62.27200  -19.13000 1.000 39.45799  ?  28   VAL   B O   1 
ATOM   14188 C  CB  . VAL   B 1 28   ? 92.17000   60.03400  -19.24400 1.000 63.38680  ?  28   VAL   B CB  1 
ATOM   14189 C  CG1 . VAL   B 1 28   ? 91.07100   61.01000  -19.63500 1.000 57.74176  ?  28   VAL   B CG1 1 
ATOM   14190 C  CG2 . VAL   B 1 28   ? 91.66600   58.60100  -19.30700 1.000 58.27500  ?  28   VAL   B CG2 1 
ATOM   14191 N  N   . VAL   B 1 29   ? 94.03600   62.20000  -21.38200 1.000 48.12799  ?  29   VAL   B N   1 
ATOM   14192 C  CA  . VAL   B 1 29   ? 94.31400   63.61900  -21.56300 1.000 45.82221  ?  29   VAL   B CA  1 
ATOM   14193 C  C   . VAL   B 1 29   ? 92.97900   64.33400  -21.72300 1.000 49.41588  ?  29   VAL   B C   1 
ATOM   14194 O  O   . VAL   B 1 29   ? 92.20600   64.02600  -22.63600 1.000 49.82051  ?  29   VAL   B O   1 
ATOM   14195 C  CB  . VAL   B 1 29   ? 95.22300   63.86300  -22.77700 1.000 38.98561  ?  29   VAL   B CB  1 
ATOM   14196 C  CG1 . VAL   B 1 29   ? 95.76100   65.29000  -22.76300 1.000 40.33004  ?  29   VAL   B CG1 1 
ATOM   14197 C  CG2 . VAL   B 1 29   ? 96.35900   62.85400  -22.80200 1.000 38.33768  ?  29   VAL   B CG2 1 
ATOM   14198 N  N   . ILE   B 1 30   ? 92.70300   65.27800  -20.83100 1.000 51.91479  ?  30   ILE   B N   1 
ATOM   14199 C  CA  . ILE   B 1 30   ? 91.44000   66.00600  -20.81500 1.000 47.50693  ?  30   ILE   B CA  1 
ATOM   14200 C  C   . ILE   B 1 30   ? 91.62200   67.30900  -21.57600 1.000 50.59390  ?  30   ILE   B C   1 
ATOM   14201 O  O   . ILE   B 1 30   ? 92.60600   68.02900  -21.36600 1.000 56.13237  ?  30   ILE   B O   1 
ATOM   14202 C  CB  . ILE   B 1 30   ? 90.97000   66.26600  -19.37400 1.000 37.61408  ?  30   ILE   B CB  1 
ATOM   14203 C  CG1 . ILE   B 1 30   ? 90.76600   64.93900  -18.64000 1.000 45.79652  ?  30   ILE   B CG1 1 
ATOM   14204 C  CG2 . ILE   B 1 30   ? 89.68900   67.08700  -19.36700 1.000 53.14372  ?  30   ILE   B CG2 1 
ATOM   14205 C  CD1 . ILE   B 1 30   ? 91.42500   64.88200  -17.27900 1.000 49.24638  ?  30   ILE   B CD1 1 
ATOM   14206 N  N   . CYS   B 1 31   ? 90.68000   67.61300  -22.46600 1.000 49.66019  ?  31   CYS   B N   1 
ATOM   14207 C  CA  . CYS   B 1 31   ? 90.70300   68.84700  -23.23700 1.000 52.07170  ?  31   CYS   B CA  1 
ATOM   14208 C  C   . CYS   B 1 31   ? 89.33800   69.51200  -23.14800 1.000 57.12664  ?  31   CYS   B C   1 
ATOM   14209 O  O   . CYS   B 1 31   ? 88.31600   68.87300  -23.42000 1.000 64.02512  ?  31   CYS   B O   1 
ATOM   14210 C  CB  . CYS   B 1 31   ? 91.07600   68.58300  -24.69800 1.000 49.40698  ?  31   CYS   B CB  1 
ATOM   14211 S  SG  . CYS   B 1 31   ? 91.40400   70.08100  -25.64500 1.000 95.03722  ?  31   CYS   B SG  1 
ATOM   14212 N  N   . GLN   B 1 32   ? 89.32300   70.79100  -22.76900 1.000 56.75882  ?  32   GLN   B N   1 
ATOM   14213 C  CA  . GLN   B 1 32   ? 88.08600   71.54300  -22.58700 1.000 53.72047  ?  32   GLN   B CA  1 
ATOM   14214 C  C   . GLN   B 1 32   ? 88.01200   72.76100  -23.50300 1.000 62.23780  ?  32   GLN   B C   1 
ATOM   14215 O  O   . GLN   B 1 32   ? 87.32100   73.73400  -23.19400 1.000 82.04906  ?  32   GLN   B O   1 
ATOM   14216 C  CB  . GLN   B 1 32   ? 87.91900   71.96000  -21.12500 1.000 46.20384  ?  32   GLN   B CB  1 
ATOM   14217 C  CG  . GLN   B 1 32   ? 87.10100   70.97500  -20.30300 1.000 58.54407  ?  32   GLN   B CG  1 
ATOM   14218 C  CD  . GLN   B 1 32   ? 87.32000   71.11800  -18.81000 1.000 60.07318  ?  32   GLN   B CD  1 
ATOM   14219 O  OE1 . GLN   B 1 32   ? 88.17000   71.88700  -18.36300 1.000 51.10577  ?  32   GLN   B OE1 1 
ATOM   14220 N  NE2 . GLN   B 1 32   ? 86.55300   70.36600  -18.02800 1.000 74.04765  ?  32   GLN   B NE2 1 
ATOM   14221 N  N   . GLU   B 1 33   ? 88.70600   72.71600  -24.64000 1.000 64.95107  ?  33   GLU   B N   1 
ATOM   14222 C  CA  . GLU   B 1 33   ? 88.71900   73.81900  -25.59000 1.000 53.70721  ?  33   GLU   B CA  1 
ATOM   14223 C  C   . GLU   B 1 33   ? 88.65500   73.24900  -27.00200 1.000 54.57171  ?  33   GLU   B C   1 
ATOM   14224 O  O   . GLU   B 1 33   ? 88.58600   72.03100  -27.19900 1.000 55.81674  ?  33   GLU   B O   1 
ATOM   14225 C  CB  . GLU   B 1 33   ? 89.96100   74.69800  -25.39800 1.000 68.36510  ?  33   GLU   B CB  1 
ATOM   14226 N  N   . LYS   B 1 34   ? 88.67700   74.14100  -27.99300 1.000 67.40964  ?  34   LYS   B N   1 
ATOM   14227 C  CA  . LYS   B 1 34   ? 88.62500   73.71100  -29.38600 1.000 68.87556  ?  34   LYS   B CA  1 
ATOM   14228 C  C   . LYS   B 1 34   ? 89.87000   72.91400  -29.74900 1.000 61.27889  ?  34   LYS   B C   1 
ATOM   14229 O  O   . LYS   B 1 34   ? 90.99900   73.37000  -29.54300 1.000 66.71014  ?  34   LYS   B O   1 
ATOM   14230 C  CB  . LYS   B 1 34   ? 88.48700   74.91500  -30.32000 1.000 72.94321  ?  34   LYS   B CB  1 
ATOM   14231 C  CG  . LYS   B 1 34   ? 87.09400   75.51600  -30.36900 1.000 76.32041  ?  34   LYS   B CG  1 
ATOM   14232 C  CD  . LYS   B 1 34   ? 86.88000   76.38000  -31.60900 1.000 85.29496  ?  34   LYS   B CD  1 
ATOM   14233 C  CE  . LYS   B 1 34   ? 86.45000   75.54600  -32.81000 1.000 77.94578  ?  34   LYS   B CE  1 
ATOM   14234 N  NZ  . LYS   B 1 34   ? 85.46800   76.27600  -33.66300 1.000 85.38062  ?  34   LYS   B NZ  1 
ATOM   14235 N  N   . VAL   B 1 35   ? 89.65900   71.72300  -30.29500 1.000 58.24709  ?  35   VAL   B N   1 
ATOM   14236 C  CA  . VAL   B 1 35   ? 90.74900   70.86100  -30.73200 1.000 65.52760  ?  35   VAL   B CA  1 
ATOM   14237 C  C   . VAL   B 1 35   ? 90.98600   71.09600  -32.21700 1.000 91.16897  ?  35   VAL   B C   1 
ATOM   14238 O  O   . VAL   B 1 35   ? 90.09100   70.88200  -33.04100 1.000 99.46060  ?  35   VAL   B O   1 
ATOM   14239 C  CB  . VAL   B 1 35   ? 90.44300   69.38300  -30.45100 1.000 55.01957  ?  35   VAL   B CB  1 
ATOM   14240 C  CG1 . VAL   B 1 35   ? 91.42400   68.49200  -31.19400 1.000 60.58767  ?  35   VAL   B CG1 1 
ATOM   14241 C  CG2 . VAL   B 1 35   ? 90.50700   69.11100  -28.96400 1.000 59.04767  ?  35   VAL   B CG2 1 
ATOM   14242 N  N   . HIS   B 1 36   ? 92.18900   71.54400  -32.55600 1.000 84.45435  ?  36   HIS   B N   1 
ATOM   14243 C  CA  . HIS   B 1 36   ? 92.61100   71.70900  -33.93700 1.000 77.17831  ?  36   HIS   B CA  1 
ATOM   14244 C  C   . HIS   B 1 36   ? 93.56800   70.58000  -34.29100 1.000 90.87301  ?  36   HIS   B C   1 
ATOM   14245 O  O   . HIS   B 1 36   ? 94.36500   70.14800  -33.45200 1.000 88.60667  ?  36   HIS   B O   1 
ATOM   14246 C  CB  . HIS   B 1 36   ? 93.27200   73.07400  -34.14200 1.000 79.70256  ?  36   HIS   B CB  1 
ATOM   14247 C  CG  . HIS   B 1 36   ? 92.44500   74.21900  -33.64100 1.000 97.62308  ?  36   HIS   B CG  1 
ATOM   14248 N  ND1 . HIS   B 1 36   ? 91.06700   74.19300  -33.63500 1.000 97.92000  ?  36   HIS   B ND1 1 
ATOM   14249 C  CD2 . HIS   B 1 36   ? 92.80100   75.41500  -33.11600 1.000 102.84617 ?  36   HIS   B CD2 1 
ATOM   14250 C  CE1 . HIS   B 1 36   ? 90.60900   75.32700  -33.13600 1.000 93.41823  ?  36   HIS   B CE1 1 
ATOM   14251 N  NE2 . HIS   B 1 36   ? 91.64100   76.08600  -32.81200 1.000 95.23750  ?  36   HIS   B NE2 1 
ATOM   14252 N  N   . ALA   B 1 37   ? 93.47900   70.10100  -35.53600 1.000 93.92759  ?  37   ALA   B N   1 
ATOM   14253 C  CA  . ALA   B 1 37   ? 94.20500   68.89500  -35.92900 1.000 79.83664  ?  37   ALA   B CA  1 
ATOM   14254 C  C   . ALA   B 1 37   ? 95.70400   69.02100  -35.69400 1.000 85.23226  ?  37   ALA   B C   1 
ATOM   14255 O  O   . ALA   B 1 37   ? 96.38300   68.01200  -35.46600 1.000 103.91848 ?  37   ALA   B O   1 
ATOM   14256 C  CB  . ALA   B 1 37   ? 93.92800   68.57000  -37.39700 1.000 84.04284  ?  37   ALA   B CB  1 
ATOM   14257 N  N   . GLN   B 1 38   ? 96.23700   70.23700  -35.73700 1.000 87.47186  ?  38   GLN   B N   1 
ATOM   14258 C  CA  . GLN   B 1 38   ? 97.66600   70.47100  -35.53800 1.000 95.27562  ?  38   GLN   B CA  1 
ATOM   14259 C  C   . GLN   B 1 38   ? 97.99400   70.71900  -34.06700 1.000 88.76215  ?  38   GLN   B C   1 
ATOM   14260 O  O   . GLN   B 1 38   ? 98.60700   71.72200  -33.70400 1.000 91.51569  ?  38   GLN   B O   1 
ATOM   14261 C  CB  . GLN   B 1 38   ? 98.12300   71.63500  -36.40900 1.000 105.71608 ?  38   GLN   B CB  1 
ATOM   14262 C  CG  . GLN   B 1 38   ? 98.39700   71.27000  -37.86700 1.000 97.67792  ?  38   GLN   B CG  1 
ATOM   14263 C  CD  . GLN   B 1 38   ? 97.20200   70.65400  -38.56800 1.000 103.21453 ?  38   GLN   B CD  1 
ATOM   14264 O  OE1 . GLN   B 1 38   ? 96.11400   71.22600  -38.58600 1.000 114.60336 ?  38   GLN   B OE1 1 
ATOM   14265 N  NE2 . GLN   B 1 38   ? 97.40200   69.47600  -39.14900 1.000 97.32276  ?  38   GLN   B NE2 1 
ATOM   14266 N  N   . SER   B 1 39   ? 97.58400   69.79000  -33.20500 1.000 85.83337  ?  39   SER   B N   1 
ATOM   14267 C  CA  . SER   B 1 39   ? 97.76900   69.91200  -31.76600 1.000 83.08486  ?  39   SER   B CA  1 
ATOM   14268 C  C   . SER   B 1 39   ? 98.49700   68.69000  -31.22500 1.000 81.26399  ?  39   SER   B C   1 
ATOM   14269 O  O   . SER   B 1 39   ? 98.36200   67.58200  -31.75000 1.000 90.24630  ?  39   SER   B O   1 
ATOM   14270 C  CB  . SER   B 1 39   ? 96.42700   70.07400  -31.03800 1.000 78.94544  ?  39   SER   B CB  1 
ATOM   14271 O  OG  . SER   B 1 39   ? 96.55200   69.77000  -29.66000 1.000 69.47528  ?  39   SER   B OG  1 
ATOM   14272 N  N   . ALA   B 1 40   ? 99.27100   68.90900  -30.15800 1.000 64.66307  ?  40   ALA   B N   1 
ATOM   14273 C  CA  . ALA   B 1 40   ? 99.97200   67.80300  -29.51300 1.000 73.60168  ?  40   ALA   B CA  1 
ATOM   14274 C  C   . ALA   B 1 40   ? 99.01700   66.91100  -28.73200 1.000 91.41613  ?  40   ALA   B C   1 
ATOM   14275 O  O   . ALA   B 1 40   ? 99.27000   65.70800  -28.59300 1.000 86.05544  ?  40   ALA   B O   1 
ATOM   14276 C  CB  . ALA   B 1 40   ? 101.07000  68.33900  -28.59400 1.000 74.79008  ?  40   ALA   B CB  1 
ATOM   14277 N  N   . ASN   B 1 41   ? 97.91900   67.47500  -28.22000 1.000 89.19214  ?  41   ASN   B N   1 
ATOM   14278 C  CA  . ASN   B 1 41   ? 96.92300   66.66800  -27.52300 1.000 70.79092  ?  41   ASN   B CA  1 
ATOM   14279 C  C   . ASN   B 1 41   ? 96.24700   65.66700  -28.44800 1.000 69.18811  ?  41   ASN   B C   1 
ATOM   14280 O  O   . ASN   B 1 41   ? 95.59600   64.73500  -27.96400 1.000 78.92312  ?  41   ASN   B O   1 
ATOM   14281 C  CB  . ASN   B 1 41   ? 95.86300   67.56600  -26.88000 1.000 63.96153  ?  41   ASN   B CB  1 
ATOM   14282 C  CG  . ASN   B 1 41   ? 96.44200   68.49500  -25.83500 1.000 76.43772  ?  41   ASN   B CG  1 
ATOM   14283 O  OD1 . ASN   B 1 41   ? 97.57800   68.32200  -25.39400 1.000 93.89927  ?  41   ASN   B OD1 1 
ATOM   14284 N  ND2 . ASN   B 1 41   ? 95.65800   69.48500  -25.42400 1.000 74.25272  ?  41   ASN   B ND2 1 
ATOM   14285 N  N   . LEU   B 1 42   ? 96.38200   65.84000  -29.76100 1.000 60.03922  ?  42   LEU   B N   1 
ATOM   14286 C  CA  . LEU   B 1 42   ? 95.79400   64.94000  -30.74100 1.000 73.67251  ?  42   LEU   B CA  1 
ATOM   14287 C  C   . LEU   B 1 42   ? 96.79300   63.92900  -31.28800 1.000 77.96700  ?  42   LEU   B C   1 
ATOM   14288 O  O   . LEU   B 1 42   ? 96.41900   63.09100  -32.11400 1.000 68.61553  ?  42   LEU   B O   1 
ATOM   14289 C  CB  . LEU   B 1 42   ? 95.19100   65.74900  -31.89400 1.000 68.47662  ?  42   LEU   B CB  1 
ATOM   14290 C  CG  . LEU   B 1 42   ? 93.95900   65.15900  -32.58100 1.000 66.38739  ?  42   LEU   B CG  1 
ATOM   14291 C  CD1 . LEU   B 1 42   ? 92.77500   65.14000  -31.63200 1.000 70.81752  ?  42   LEU   B CD1 1 
ATOM   14292 C  CD2 . LEU   B 1 42   ? 93.62300   65.93600  -33.83900 1.000 62.86387  ?  42   LEU   B CD2 1 
ATOM   14293 N  N   . GLN   B 1 43   ? 98.04700   63.98100  -30.84800 1.000 76.03756  ?  43   GLN   B N   1 
ATOM   14294 C  CA  . GLN   B 1 43   ? 99.08900   63.09200  -31.33600 1.000 69.73559  ?  43   GLN   B CA  1 
ATOM   14295 C  C   . GLN   B 1 43   ? 99.33500   61.96000  -30.34600 1.000 60.65282  ?  43   GLN   B C   1 
ATOM   14296 O  O   . GLN   B 1 43   ? 99.21700   62.13600  -29.13000 1.000 66.82899  ?  43   GLN   B O   1 
ATOM   14297 C  CB  . GLN   B 1 43   ? 100.38400  63.86800  -31.58800 1.000 74.73745  ?  43   GLN   B CB  1 
ATOM   14298 C  CG  . GLN   B 1 43   ? 100.30000  64.79500  -32.79100 1.000 76.34674  ?  43   GLN   B CG  1 
ATOM   14299 C  CD  . GLN   B 1 43   ? 101.24300  65.97900  -32.69600 1.000 90.68221  ?  43   GLN   B CD  1 
ATOM   14300 O  OE1 . GLN   B 1 43   ? 102.36200  65.86300  -32.19600 1.000 78.77993  ?  43   GLN   B OE1 1 
ATOM   14301 N  NE2 . GLN   B 1 43   ? 100.78800  67.13300  -33.17300 1.000 90.11530  ?  43   GLN   B NE2 1 
ATOM   14302 N  N   . GLU   B 1 44   ? 99.67500   60.78800  -30.89000 1.000 62.69856  ?  44   GLU   B N   1 
ATOM   14303 C  CA  . GLU   B 1 44   ? 99.87600   59.56500  -30.10900 1.000 66.85100  ?  44   GLU   B CA  1 
ATOM   14304 C  C   . GLU   B 1 44   ? 98.61800   59.17600  -29.33700 1.000 70.30337  ?  44   GLU   B C   1 
ATOM   14305 O  O   . GLU   B 1 44   ? 98.69500   58.57900  -28.26000 1.000 71.33845  ?  44   GLU   B O   1 
ATOM   14306 C  CB  . GLU   B 1 44   ? 101.07100  59.69600  -29.15800 1.000 86.99409  ?  44   GLU   B CB  1 
ATOM   14307 N  N   . ILE   B 1 45   ? 97.45200   59.50300  -29.88800 1.000 81.64821  ?  45   ILE   B N   1 
ATOM   14308 C  CA  . ILE   B 1 45   ? 96.16400   59.24600  -29.25500 1.000 71.67062  ?  45   ILE   B CA  1 
ATOM   14309 C  C   . ILE   B 1 45   ? 95.49000   58.09400  -29.98500 1.000 68.35195  ?  45   ILE   B C   1 
ATOM   14310 O  O   . ILE   B 1 45   ? 95.39300   58.10500  -31.21800 1.000 66.77619  ?  45   ILE   B O   1 
ATOM   14311 C  CB  . ILE   B 1 45   ? 95.27400   60.50100  -29.26700 1.000 62.57579  ?  45   ILE   B CB  1 
ATOM   14312 C  CG1 . ILE   B 1 45   ? 95.94100   61.63900  -28.49300 1.000 53.02741  ?  45   ILE   B CG1 1 
ATOM   14313 C  CG2 . ILE   B 1 45   ? 93.90900   60.19100  -28.68100 1.000 71.00576  ?  45   ILE   B CG2 1 
ATOM   14314 C  CD1 . ILE   B 1 45   ? 95.93800   61.44500  -26.99200 1.000 55.24599  ?  45   ILE   B CD1 1 
ATOM   14315 N  N   . ASP   B 1 46   ? 95.02500   57.10100  -29.22400 1.000 76.36618  ?  46   ASP   B N   1 
ATOM   14316 C  CA  . ASP   B 1 46   ? 94.38700   55.92200  -29.79700 1.000 77.89409  ?  46   ASP   B CA  1 
ATOM   14317 C  C   . ASP   B 1 46   ? 92.86700   55.94000  -29.68900 1.000 68.64647  ?  46   ASP   B C   1 
ATOM   14318 O  O   . ASP   B 1 46   ? 92.20400   55.20000  -30.42300 1.000 67.13740  ?  46   ASP   B O   1 
ATOM   14319 C  CB  . ASP   B 1 46   ? 94.91600   54.64900  -29.12300 1.000 83.21462  ?  46   ASP   B CB  1 
ATOM   14320 C  CG  . ASP   B 1 46   ? 96.43100   54.57700  -29.11800 1.000 87.98070  ?  46   ASP   B CG  1 
ATOM   14321 O  OD1 . ASP   B 1 46   ? 97.08000   55.60300  -29.41300 1.000 92.33193  ?  46   ASP   B OD1 1 
ATOM   14322 O  OD2 . ASP   B 1 46   ? 96.97400   53.49200  -28.82000 1.000 99.13893  -1 46   ASP   B OD2 1 
ATOM   14323 N  N   . TRP   B 1 47   ? 92.30500   56.75300  -28.79700 1.000 76.49862  ?  47   TRP   B N   1 
ATOM   14324 C  CA  . TRP   B 1 47   ? 90.86300   56.84800  -28.62100 1.000 65.90416  ?  47   TRP   B CA  1 
ATOM   14325 C  C   . TRP   B 1 47   ? 90.47800   58.28400  -28.30700 1.000 62.67654  ?  47   TRP   B C   1 
ATOM   14326 O  O   . TRP   B 1 47   ? 91.19900   58.98600  -27.59200 1.000 62.23414  ?  47   TRP   B O   1 
ATOM   14327 C  CB  . TRP   B 1 47   ? 90.36100   55.93600  -27.49100 1.000 59.81139  ?  47   TRP   B CB  1 
ATOM   14328 C  CG  . TRP   B 1 47   ? 90.29800   54.48200  -27.83800 1.000 60.83929  ?  47   TRP   B CG  1 
ATOM   14329 C  CD1 . TRP   B 1 47   ? 91.16500   53.50700  -27.44100 1.000 74.43550  ?  47   TRP   B CD1 1 
ATOM   14330 C  CD2 . TRP   B 1 47   ? 89.30600   53.83400  -28.64200 1.000 71.44226  ?  47   TRP   B CD2 1 
ATOM   14331 N  NE1 . TRP   B 1 47   ? 90.77700   52.29200  -27.95100 1.000 69.82265  ?  47   TRP   B NE1 1 
ATOM   14332 C  CE2 . TRP   B 1 47   ? 89.63900   52.46500  -28.69300 1.000 64.70749  ?  47   TRP   B CE2 1 
ATOM   14333 C  CE3 . TRP   B 1 47   ? 88.17000   54.27800  -29.32600 1.000 87.45860  ?  47   TRP   B CE3 1 
ATOM   14334 C  CZ2 . TRP   B 1 47   ? 88.87800   51.53800  -29.40100 1.000 74.41668  ?  47   TRP   B CZ2 1 
ATOM   14335 C  CZ3 . TRP   B 1 47   ? 87.41600   53.35500  -30.02900 1.000 86.38195  ?  47   TRP   B CZ3 1 
ATOM   14336 C  CH2 . TRP   B 1 47   ? 87.77300   52.00200  -30.06100 1.000 80.59322  ?  47   TRP   B CH2 1 
ATOM   14337 N  N   . ILE   B 1 48   ? 89.33700   58.71300  -28.83500 1.000 64.65669  ?  48   ILE   B N   1 
ATOM   14338 C  CA  . ILE   B 1 48   ? 88.74500   60.00300  -28.50000 1.000 58.94724  ?  48   ILE   B CA  1 
ATOM   14339 C  C   . ILE   B 1 48   ? 87.35800   59.73700  -27.93300 1.000 58.05175  ?  48   ILE   B C   1 
ATOM   14340 O  O   . ILE   B 1 48   ? 86.51300   59.13100  -28.60300 1.000 61.03803  ?  48   ILE   B O   1 
ATOM   14341 C  CB  . ILE   B 1 48   ? 88.67500   60.94300  -29.71300 1.000 59.26786  ?  48   ILE   B CB  1 
ATOM   14342 C  CG1 . ILE   B 1 48   ? 90.08200   61.36000  -30.14600 1.000 62.31757  ?  48   ILE   B CG1 1 
ATOM   14343 C  CG2 . ILE   B 1 48   ? 87.83800   62.16900  -29.38700 1.000 61.93110  ?  48   ILE   B CG2 1 
ATOM   14344 C  CD1 . ILE   B 1 48   ? 90.09800   62.40000  -31.24500 1.000 56.42881  ?  48   ILE   B CD1 1 
ATOM   14345 N  N   . VAL   B 1 49   ? 87.13000   60.17500  -26.69900 1.000 52.84778  ?  49   VAL   B N   1 
ATOM   14346 C  CA  . VAL   B 1 49   ? 85.84900   60.01300  -26.02300 1.000 46.02399  ?  49   VAL   B CA  1 
ATOM   14347 C  C   . VAL   B 1 49   ? 85.31800   61.40000  -25.69900 1.000 43.97856  ?  49   VAL   B C   1 
ATOM   14348 O  O   . VAL   B 1 49   ? 85.96300   62.16200  -24.96700 1.000 45.27230  ?  49   VAL   B O   1 
ATOM   14349 C  CB  . VAL   B 1 49   ? 85.97600   59.15900  -24.75200 1.000 51.63258  ?  49   VAL   B CB  1 
ATOM   14350 C  CG1 . VAL   B 1 49   ? 84.69800   59.23000  -23.93500 1.000 49.73091  ?  49   VAL   B CG1 1 
ATOM   14351 C  CG2 . VAL   B 1 49   ? 86.29700   57.71700  -25.11500 1.000 47.56179  ?  49   VAL   B CG2 1 
ATOM   14352 N  N   . SER   B 1 50   ? 84.15400   61.73200  -26.24800 1.000 48.71960  ?  50   SER   B N   1 
ATOM   14353 C  CA  . SER   B 1 50   ? 83.53800   63.03500  -26.04800 1.000 44.08509  ?  50   SER   B CA  1 
ATOM   14354 C  C   . SER   B 1 50   ? 82.30100   62.90400  -25.17100 1.000 49.40797  ?  50   SER   B C   1 
ATOM   14355 O  O   . SER   B 1 50   ? 81.56600   61.91300  -25.25100 1.000 46.46062  ?  50   SER   B O   1 
ATOM   14356 C  CB  . SER   B 1 50   ? 83.17100   63.68600  -27.38500 1.000 34.63846  ?  50   SER   B CB  1 
ATOM   14357 O  OG  . SER   B 1 50   ? 82.50100   62.77500  -28.23600 1.000 64.70332  ?  50   SER   B OG  1 
ATOM   14358 N  N   . TYR   B 1 51   ? 82.08200   63.91400  -24.32900 1.000 50.11519  ?  51   TYR   B N   1 
ATOM   14359 C  CA  . TYR   B 1 51   ? 80.95800   63.91400  -23.39700 1.000 39.48996  ?  51   TYR   B CA  1 
ATOM   14360 C  C   . TYR   B 1 51   ? 80.69200   65.37800  -23.04900 1.000 35.27467  ?  51   TYR   B C   1 
ATOM   14361 O  O   . TYR   B 1 51   ? 81.45100   65.97700  -22.28200 1.000 48.66969  ?  51   TYR   B O   1 
ATOM   14362 C  CB  . TYR   B 1 51   ? 81.27100   63.08200  -22.16200 1.000 34.74394  ?  51   TYR   B CB  1 
ATOM   14363 C  CG  . TYR   B 1 51   ? 80.11900   62.90600  -21.19500 1.000 47.65573  ?  51   TYR   B CG  1 
ATOM   14364 C  CD1 . TYR   B 1 51   ? 78.80600   63.12100  -21.59300 1.000 52.11689  ?  51   TYR   B CD1 1 
ATOM   14365 C  CD2 . TYR   B 1 51   ? 80.35000   62.53100  -19.87700 1.000 47.20268  ?  51   TYR   B CD2 1 
ATOM   14366 C  CE1 . TYR   B 1 51   ? 77.75500   62.96400  -20.70500 1.000 50.89880  ?  51   TYR   B CE1 1 
ATOM   14367 C  CE2 . TYR   B 1 51   ? 79.30700   62.37200  -18.98400 1.000 50.29530  ?  51   TYR   B CE2 1 
ATOM   14368 C  CZ  . TYR   B 1 51   ? 78.01300   62.59000  -19.40300 1.000 38.97000  ?  51   TYR   B CZ  1 
ATOM   14369 O  OH  . TYR   B 1 51   ? 76.97200   62.43200  -18.51700 1.000 59.46145  ?  51   TYR   B OH  1 
ATOM   14370 N  N   . ALA   B 1 52   ? 79.62900   65.93700  -23.62800 1.000 38.17406  ?  52   ALA   B N   1 
ATOM   14371 C  CA  . ALA   B 1 52   ? 79.29100   67.35400  -23.47800 1.000 40.28259  ?  52   ALA   B CA  1 
ATOM   14372 C  C   . ALA   B 1 52   ? 80.42200   68.24300  -23.99500 1.000 46.64117  ?  52   ALA   B C   1 
ATOM   14373 O  O   . ALA   B 1 52   ? 80.92200   69.12700  -23.29600 1.000 46.47249  ?  52   ALA   B O   1 
ATOM   14374 C  CB  . ALA   B 1 52   ? 78.93900   67.69400  -22.02700 1.000 33.48748  ?  52   ALA   B CB  1 
ATOM   14375 N  N   . TYR   B 1 53   ? 80.82700   67.99500  -25.23900 1.000 41.49167  ?  53   TYR   B N   1 
ATOM   14376 C  CA  . TYR   B 1 53   ? 81.83000   68.81300  -25.90900 1.000 47.14703  ?  53   TYR   B CA  1 
ATOM   14377 C  C   . TYR   B 1 53   ? 81.11800   69.90200  -26.70300 1.000 41.11841  ?  53   TYR   B C   1 
ATOM   14378 O  O   . TYR   B 1 53   ? 80.35600   69.60500  -27.62900 1.000 50.09608  ?  53   TYR   B O   1 
ATOM   14379 C  CB  . TYR   B 1 53   ? 82.71200   67.95700  -26.81700 1.000 44.59011  ?  53   TYR   B CB  1 
ATOM   14380 C  CG  . TYR   B 1 53   ? 83.87800   68.70800  -27.42100 1.000 55.74621  ?  53   TYR   B CG  1 
ATOM   14381 C  CD1 . TYR   B 1 53   ? 84.62300   69.59900  -26.66000 1.000 57.01634  ?  53   TYR   B CD1 1 
ATOM   14382 C  CD2 . TYR   B 1 53   ? 84.24200   68.51600  -28.74800 1.000 60.01468  ?  53   TYR   B CD2 1 
ATOM   14383 C  CE1 . TYR   B 1 53   ? 85.69100   70.28700  -27.20500 1.000 59.27018  ?  53   TYR   B CE1 1 
ATOM   14384 C  CE2 . TYR   B 1 53   ? 85.31100   69.19900  -29.30200 1.000 64.27113  ?  53   TYR   B CE2 1 
ATOM   14385 C  CZ  . TYR   B 1 53   ? 86.03100   70.08300  -28.52500 1.000 56.71762  ?  53   TYR   B CZ  1 
ATOM   14386 O  OH  . TYR   B 1 53   ? 87.09500   70.76500  -29.07000 1.000 52.01096  ?  53   TYR   B OH  1 
ATOM   14387 N  N   . GLY   B 1 54   ? 81.36700   71.15800  -26.34000 1.000 40.31906  ?  54   GLY   B N   1 
ATOM   14388 C  CA  . GLY   B 1 54   ? 80.61600   72.27100  -26.88900 1.000 55.80864  ?  54   GLY   B CA  1 
ATOM   14389 C  C   . GLY   B 1 54   ? 81.15900   72.84100  -28.18300 1.000 57.07195  ?  54   GLY   B C   1 
ATOM   14390 O  O   . GLY   B 1 54   ? 80.78000   73.94600  -28.58300 1.000 65.39000  ?  54   GLY   B O   1 
ATOM   14391 N  N   . TYR   B 1 55   ? 82.04200   72.10200  -28.84800 1.000 65.18878  ?  55   TYR   B N   1 
ATOM   14392 C  CA  . TYR   B 1 55   ? 82.60400   72.52500  -30.12000 1.000 54.34549  ?  55   TYR   B CA  1 
ATOM   14393 C  C   . TYR   B 1 55   ? 82.47700   71.39500  -31.13100 1.000 46.96364  ?  55   TYR   B C   1 
ATOM   14394 O  O   . TYR   B 1 55   ? 82.32400   70.22400  -30.77100 1.000 46.79351  ?  55   TYR   B O   1 
ATOM   14395 C  CB  . TYR   B 1 55   ? 84.07500   72.94300  -29.98100 1.000 51.78884  ?  55   TYR   B CB  1 
ATOM   14396 C  CG  . TYR   B 1 55   ? 84.32100   74.00500  -28.93200 1.000 57.62818  ?  55   TYR   B CG  1 
ATOM   14397 C  CD1 . TYR   B 1 55   ? 83.88200   75.31000  -29.11700 1.000 64.52505  ?  55   TYR   B CD1 1 
ATOM   14398 C  CD2 . TYR   B 1 55   ? 85.00500   73.70400  -27.76100 1.000 57.28134  ?  55   TYR   B CD2 1 
ATOM   14399 C  CE1 . TYR   B 1 55   ? 84.11200   76.28400  -28.16200 1.000 55.72634  ?  55   TYR   B CE1 1 
ATOM   14400 C  CE2 . TYR   B 1 55   ? 85.23800   74.67100  -26.80100 1.000 55.75534  ?  55   TYR   B CE2 1 
ATOM   14401 C  CZ  . TYR   B 1 55   ? 84.79000   75.95800  -27.00600 1.000 48.80435  ?  55   TYR   B CZ  1 
ATOM   14402 O  OH  . TYR   B 1 55   ? 85.02300   76.92000  -26.05000 1.000 61.35703  ?  55   TYR   B OH  1 
ATOM   14403 N  N   . ILE   B 1 56   ? 82.53800   71.76000  -32.40600 1.000 54.86886  ?  56   ILE   B N   1 
ATOM   14404 C  CA  . ILE   B 1 56   ? 82.46700   70.80100  -33.50100 1.000 62.44260  ?  56   ILE   B CA  1 
ATOM   14405 C  C   . ILE   B 1 56   ? 83.88500   70.49900  -33.96700 1.000 70.55551  ?  56   ILE   B C   1 
ATOM   14406 O  O   . ILE   B 1 56   ? 84.73700   71.39600  -34.03900 1.000 71.18749  ?  56   ILE   B O   1 
ATOM   14407 C  CB  . ILE   B 1 56   ? 81.58400   71.33000  -34.65100 1.000 58.16892  ?  56   ILE   B CB  1 
ATOM   14408 C  CG1 . ILE   B 1 56   ? 81.20900   70.20000  -35.61300 1.000 60.83242  ?  56   ILE   B CG1 1 
ATOM   14409 C  CG2 . ILE   B 1 56   ? 82.25300   72.48600  -35.38900 1.000 65.43071  ?  56   ILE   B CG2 1 
ATOM   14410 C  CD1 . ILE   B 1 56   ? 80.10900   69.30300  -35.09000 1.000 55.69868  ?  56   ILE   B CD1 1 
ATOM   14411 N  N   . LEU   B 1 57   ? 84.15400   69.22700  -34.24900 1.000 70.21485  ?  57   LEU   B N   1 
ATOM   14412 C  CA  . LEU   B 1 57   ? 85.48000   68.79500  -34.66500 1.000 66.00085  ?  57   LEU   B CA  1 
ATOM   14413 C  C   . LEU   B 1 57   ? 85.61100   68.88100  -36.17900 1.000 78.44228  ?  57   LEU   B C   1 
ATOM   14414 O  O   . LEU   B 1 57   ? 84.67000   68.56800  -36.91400 1.000 95.95872  ?  57   LEU   B O   1 
ATOM   14415 C  CB  . LEU   B 1 57   ? 85.75700   67.36500  -34.19600 1.000 49.36147  ?  57   LEU   B CB  1 
ATOM   14416 C  CG  . LEU   B 1 57   ? 85.95100   67.16700  -32.69200 1.000 54.87168  ?  57   LEU   B CG  1 
ATOM   14417 C  CD1 . LEU   B 1 57   ? 86.11100   65.69100  -32.36700 1.000 46.65351  ?  57   LEU   B CD1 1 
ATOM   14418 C  CD2 . LEU   B 1 57   ? 87.15100   67.96300  -32.19700 1.000 53.16391  ?  57   LEU   B CD2 1 
ATOM   14419 N  N   . ASP   B 1 58   ? 86.78500   69.31000  -36.63900 1.000 69.81402  ?  58   ASP   B N   1 
ATOM   14420 C  CA  . ASP   B 1 58   ? 87.02500   69.41600  -38.07100 1.000 79.47006  ?  58   ASP   B CA  1 
ATOM   14421 C  C   . ASP   B 1 58   ? 86.97700   68.03900  -38.72300 1.000 84.16761  ?  58   ASP   B C   1 
ATOM   14422 O  O   . ASP   B 1 58   ? 87.26800   67.01600  -38.09600 1.000 76.54156  ?  58   ASP   B O   1 
ATOM   14423 C  CB  . ASP   B 1 58   ? 88.37400   70.08300  -38.34300 1.000 72.65107  ?  58   ASP   B CB  1 
ATOM   14424 C  CG  . ASP   B 1 58   ? 88.38000   71.55500  -37.98200 1.000 94.70274  ?  58   ASP   B CG  1 
ATOM   14425 O  OD1 . ASP   B 1 58   ? 87.48800   71.98600  -37.22100 1.000 104.80563 ?  58   ASP   B OD1 1 
ATOM   14426 O  OD2 . ASP   B 1 58   ? 89.27200   72.28400  -38.46400 1.000 86.01619  -1 58   ASP   B OD2 1 
ATOM   14427 N  N   . LYS   B 1 59   ? 86.60000   68.02400  -40.00500 1.000 80.04900  ?  59   LYS   B N   1 
ATOM   14428 C  CA  . LYS   B 1 59   ? 86.44200   66.76600  -40.72800 1.000 75.67709  ?  59   LYS   B CA  1 
ATOM   14429 C  C   . LYS   B 1 59   ? 87.74200   65.97900  -40.81700 1.000 86.70771  ?  59   LYS   B C   1 
ATOM   14430 O  O   . LYS   B 1 59   ? 87.70000   64.75600  -40.99700 1.000 74.56125  ?  59   LYS   B O   1 
ATOM   14431 C  CB  . LYS   B 1 59   ? 85.89800   67.03200  -42.13200 1.000 74.78175  ?  59   LYS   B CB  1 
ATOM   14432 N  N   . GLU   B 1 60   ? 88.89200   66.64600  -40.70100 1.000 83.87646  ?  60   GLU   B N   1 
ATOM   14433 C  CA  . GLU   B 1 60   ? 90.16100   65.92700  -40.70300 1.000 68.74339  ?  60   GLU   B CA  1 
ATOM   14434 C  C   . GLU   B 1 60   ? 90.29100   65.04200  -39.47000 1.000 75.97726  ?  60   GLU   B C   1 
ATOM   14435 O  O   . GLU   B 1 60   ? 90.79700   63.91800  -39.55500 1.000 66.87256  ?  60   GLU   B O   1 
ATOM   14436 C  CB  . GLU   B 1 60   ? 91.32600   66.91300  -40.77900 1.000 82.80153  ?  60   GLU   B CB  1 
ATOM   14437 C  CG  . GLU   B 1 60   ? 91.23900   67.89000  -41.93900 1.000 92.76659  ?  60   GLU   B CG  1 
ATOM   14438 C  CD  . GLU   B 1 60   ? 92.52300   68.66900  -42.14000 1.000 104.91694 ?  60   GLU   B CD  1 
ATOM   14439 O  OE1 . GLU   B 1 60   ? 93.57700   68.21800  -41.64400 1.000 99.40318  ?  60   GLU   B OE1 1 
ATOM   14440 O  OE2 . GLU   B 1 60   ? 92.47900   69.73300  -42.79200 1.000 105.93297 -1 60   GLU   B OE2 1 
ATOM   14441 N  N   . ILE   B 1 61   ? 89.82900   65.53100  -38.31700 1.000 83.34485  ?  61   ILE   B N   1 
ATOM   14442 C  CA  . ILE   B 1 61   ? 89.91300   64.74500  -37.09000 1.000 80.18242  ?  61   ILE   B CA  1 
ATOM   14443 C  C   . ILE   B 1 61   ? 88.91700   63.59300  -37.12300 1.000 69.55881  ?  61   ILE   B C   1 
ATOM   14444 O  O   . ILE   B 1 61   ? 89.24300   62.46400  -36.73900 1.000 69.96505  ?  61   ILE   B O   1 
ATOM   14445 C  CB  . ILE   B 1 61   ? 89.69500   65.65000  -35.86400 1.000 59.16762  ?  61   ILE   B CB  1 
ATOM   14446 C  CG1 . ILE   B 1 61   ? 90.71600   66.78800  -35.85800 1.000 53.76129  ?  61   ILE   B CG1 1 
ATOM   14447 C  CG2 . ILE   B 1 61   ? 89.79600   64.84100  -34.58100 1.000 59.75732  ?  61   ILE   B CG2 1 
ATOM   14448 C  CD1 . ILE   B 1 61   ? 90.09900   68.16000  -35.74300 1.000 55.90979  ?  61   ILE   B CD1 1 
ATOM   14449 N  N   . VAL   B 1 62   ? 87.69000   63.85400  -37.58500 1.000 67.26655  ?  62   VAL   B N   1 
ATOM   14450 C  CA  . VAL   B 1 62   ? 86.67900   62.80300  -37.63100 1.000 71.95128  ?  62   VAL   B CA  1 
ATOM   14451 C  C   . VAL   B 1 62   ? 87.02600   61.74000  -38.66300 1.000 73.16734  ?  62   VAL   B C   1 
ATOM   14452 O  O   . VAL   B 1 62   ? 86.50300   60.62100  -38.59500 1.000 75.16671  ?  62   VAL   B O   1 
ATOM   14453 C  CB  . VAL   B 1 62   ? 85.28400   63.39700  -37.90800 1.000 67.15308  ?  62   VAL   B CB  1 
ATOM   14454 C  CG1 . VAL   B 1 62   ? 85.07200   64.66100  -37.08900 1.000 68.61671  ?  62   VAL   B CG1 1 
ATOM   14455 C  CG2 . VAL   B 1 62   ? 85.09400   63.66900  -39.39200 1.000 77.29506  ?  62   VAL   B CG2 1 
ATOM   14456 N  N   . SER   B 1 63   ? 87.90000   62.05700  -39.61800 1.000 78.65282  ?  63   SER   B N   1 
ATOM   14457 C  CA  . SER   B 1 63   ? 88.37500   61.07500  -40.58300 1.000 80.07364  ?  63   SER   B CA  1 
ATOM   14458 C  C   . SER   B 1 63   ? 89.64900   60.38400  -40.11300 1.000 84.44641  ?  63   SER   B C   1 
ATOM   14459 O  O   . SER   B 1 63   ? 89.77800   59.16300  -40.25900 1.000 85.28614  ?  63   SER   B O   1 
ATOM   14460 C  CB  . SER   B 1 63   ? 88.61500   61.74100  -41.93900 1.000 78.32285  ?  63   SER   B CB  1 
ATOM   14461 O  OG  . SER   B 1 63   ? 89.54900   62.80000  -41.82200 1.000 76.07389  ?  63   SER   B OG  1 
ATOM   14462 N  N   . ARG   B 1 64   ? 90.59500   61.14500  -39.55100 1.000 77.70557  ?  64   ARG   B N   1 
ATOM   14463 C  CA  . ARG   B 1 64   ? 91.82100   60.54100  -39.03900 1.000 65.02627  ?  64   ARG   B CA  1 
ATOM   14464 C  C   . ARG   B 1 64   ? 91.51800   59.54900  -37.92600 1.000 72.61594  ?  64   ARG   B C   1 
ATOM   14465 O  O   . ARG   B 1 64   ? 92.09300   58.45500  -37.88200 1.000 82.98468  ?  64   ARG   B O   1 
ATOM   14466 C  CB  . ARG   B 1 64   ? 92.78000   61.62400  -38.53700 1.000 56.48079  ?  64   ARG   B CB  1 
ATOM   14467 C  CG  . ARG   B 1 64   ? 94.24600   61.21700  -38.59700 1.000 77.41055  ?  64   ARG   B CG  1 
ATOM   14468 C  CD  . ARG   B 1 64   ? 95.05600   61.75500  -37.42300 1.000 76.65121  ?  64   ARG   B CD  1 
ATOM   14469 N  NE  . ARG   B 1 64   ? 94.91200   63.19500  -37.24600 1.000 87.84374  ?  64   ARG   B NE  1 
ATOM   14470 C  CZ  . ARG   B 1 64   ? 95.84500   63.98100  -36.72700 1.000 81.65360  ?  64   ARG   B CZ  1 
ATOM   14471 N  NH1 . ARG   B 1 64   ? 97.02700   63.50700  -36.36700 1.000 76.36166  ?  64   ARG   B NH1 1 
ATOM   14472 N  NH2 . ARG   B 1 64   ? 95.59000   65.27700  -36.57300 1.000 65.93777  ?  64   ARG   B NH2 1 
ATOM   14473 N  N   . PHE   B 1 65   ? 90.61200   59.91200  -37.01800 1.000 65.93128  ?  65   PHE   B N   1 
ATOM   14474 C  CA  . PHE   B 1 65   ? 90.22000   59.05600  -35.90800 1.000 72.16922  ?  65   PHE   B CA  1 
ATOM   14475 C  C   . PHE   B 1 65   ? 88.86800   58.38900  -36.14100 1.000 66.44124  ?  65   PHE   B C   1 
ATOM   14476 O  O   . PHE   B 1 65   ? 88.10700   58.18100  -35.19000 1.000 73.86507  ?  65   PHE   B O   1 
ATOM   14477 C  CB  . PHE   B 1 65   ? 90.20100   59.85500  -34.60500 1.000 66.71245  ?  65   PHE   B CB  1 
ATOM   14478 C  CG  . PHE   B 1 65   ? 91.54200   60.39900  -34.20300 1.000 65.32973  ?  65   PHE   B CG  1 
ATOM   14479 C  CD1 . PHE   B 1 65   ? 91.95900   61.64600  -34.63900 1.000 69.33313  ?  65   PHE   B CD1 1 
ATOM   14480 C  CD2 . PHE   B 1 65   ? 92.38200   59.66700  -33.38100 1.000 72.62320  ?  65   PHE   B CD2 1 
ATOM   14481 C  CE1 . PHE   B 1 65   ? 93.19100   62.14900  -34.26800 1.000 67.43887  ?  65   PHE   B CE1 1 
ATOM   14482 C  CE2 . PHE   B 1 65   ? 93.61500   60.16500  -33.00600 1.000 77.96278  ?  65   PHE   B CE2 1 
ATOM   14483 C  CZ  . PHE   B 1 65   ? 94.02000   61.40800  -33.45000 1.000 75.57137  ?  65   PHE   B CZ  1 
ATOM   14484 N  N   . ARG   B 1 66   ? 88.55000   58.05700  -37.39200 1.000 58.85083  ?  66   ARG   B N   1 
ATOM   14485 C  CA  . ARG   B 1 66   ? 87.30400   57.36200  -37.68600 1.000 61.85645  ?  66   ARG   B CA  1 
ATOM   14486 C  C   . ARG   B 1 66   ? 87.29000   56.00300  -36.99800 1.000 61.95171  ?  66   ARG   B C   1 
ATOM   14487 O  O   . ARG   B 1 66   ? 88.27900   55.26400  -37.03100 1.000 75.74123  ?  66   ARG   B O   1 
ATOM   14488 C  CB  . ARG   B 1 66   ? 87.13100   57.19800  -39.19500 1.000 53.90981  ?  66   ARG   B CB  1 
ATOM   14489 N  N   . GLY   B 1 67   ? 86.16400   55.67600  -36.36800 1.000 51.41441  ?  67   GLY   B N   1 
ATOM   14490 C  CA  . GLY   B 1 67   ? 86.07500   54.49100  -35.54300 1.000 49.65336  ?  67   GLY   B CA  1 
ATOM   14491 C  C   . GLY   B 1 67   ? 86.72300   54.62000  -34.18300 1.000 66.43013  ?  67   GLY   B C   1 
ATOM   14492 O  O   . GLY   B 1 67   ? 86.71400   53.65000  -33.41500 1.000 60.76265  ?  67   GLY   B O   1 
ATOM   14493 N  N   . ARG   B 1 68   ? 87.28300   55.78700  -33.86000 1.000 71.15564  ?  68   ARG   B N   1 
ATOM   14494 C  CA  . ARG   B 1 68   ? 87.92900   56.01200  -32.57600 1.000 75.49910  ?  68   ARG   B CA  1 
ATOM   14495 C  C   . ARG   B 1 68   ? 87.39100   57.22200  -31.82300 1.000 76.05792  ?  68   ARG   B C   1 
ATOM   14496 O  O   . ARG   B 1 68   ? 87.81000   57.44500  -30.68100 1.000 77.31545  ?  68   ARG   B O   1 
ATOM   14497 C  CB  . ARG   B 1 68   ? 89.44700   56.17400  -32.76400 1.000 85.95810  ?  68   ARG   B CB  1 
ATOM   14498 C  CG  . ARG   B 1 68   ? 90.10300   55.02500  -33.53000 1.000 84.16381  ?  68   ARG   B CG  1 
ATOM   14499 C  CD  . ARG   B 1 68   ? 91.19500   55.52700  -34.47300 1.000 91.09530  ?  68   ARG   B CD  1 
ATOM   14500 N  NE  . ARG   B 1 68   ? 92.47600   55.72300  -33.80300 1.000 92.51559  ?  68   ARG   B NE  1 
ATOM   14501 C  CZ  . ARG   B 1 68   ? 93.51300   56.35100  -34.34100 1.000 80.68723  ?  68   ARG   B CZ  1 
ATOM   14502 N  NH1 . ARG   B 1 68   ? 93.44500   56.89100  -35.54600 1.000 79.75891  ?  68   ARG   B NH1 1 
ATOM   14503 N  NH2 . ARG   B 1 68   ? 94.64700   56.44100  -33.65100 1.000 70.26665  ?  68   ARG   B NH2 1 
ATOM   14504 N  N   . ILE   B 1 69   ? 86.49400   58.00700  -32.41300 1.000 64.95422  ?  69   ILE   B N   1 
ATOM   14505 C  CA  . ILE   B 1 69   ? 85.87800   59.14400  -31.74200 1.000 67.36187  ?  69   ILE   B CA  1 
ATOM   14506 C  C   . ILE   B 1 69   ? 84.50800   58.70000  -31.25000 1.000 67.07561  ?  69   ILE   B C   1 
ATOM   14507 O  O   . ILE   B 1 69   ? 83.61400   58.40200  -32.05000 1.000 61.94748  ?  69   ILE   B O   1 
ATOM   14508 C  CB  . ILE   B 1 69   ? 85.76400   60.36800  -32.66100 1.000 49.52484  ?  69   ILE   B CB  1 
ATOM   14509 C  CG1 . ILE   B 1 69   ? 87.11300   60.71000  -33.28200 1.000 60.40536  ?  69   ILE   B CG1 1 
ATOM   14510 C  CG2 . ILE   B 1 69   ? 85.24500   61.56400  -31.88600 1.000 42.55125  ?  69   ILE   B CG2 1 
ATOM   14511 C  CD1 . ILE   B 1 69   ? 87.09400   61.97200  -34.10800 1.000 55.42291  ?  69   ILE   B CD1 1 
ATOM   14512 N  N   . ILE   B 1 70   ? 84.33500   58.66200  -29.93500 1.000 72.56577  ?  70   ILE   B N   1 
ATOM   14513 C  CA  . ILE   B 1 70   ? 83.10800   58.18400  -29.31500 1.000 55.83438  ?  70   ILE   B CA  1 
ATOM   14514 C  C   . ILE   B 1 70   ? 82.45000   59.35000  -28.58700 1.000 60.64463  ?  70   ILE   B C   1 
ATOM   14515 O  O   . ILE   B 1 70   ? 83.13500   60.18700  -27.98500 1.000 60.40462  ?  70   ILE   B O   1 
ATOM   14516 C  CB  . ILE   B 1 70   ? 83.38300   57.01200  -28.34500 1.000 41.80448  ?  70   ILE   B CB  1 
ATOM   14517 C  CG1 . ILE   B 1 70   ? 84.28800   55.92700  -28.97200 1.000 66.89109  ?  70   ILE   B CG1 1 
ATOM   14518 C  CG2 . ILE   B 1 70   ? 82.08000   56.43200  -27.81900 1.000 50.44996  ?  70   ILE   B CG2 1 
ATOM   14519 C  CD1 . ILE   B 1 70   ? 83.86100   55.42300  -30.36100 1.000 67.92029  ?  70   ILE   B CD1 1 
ATOM   14520 N  N   . ASN   B 1 71   ? 81.12200   59.40400  -28.63700 1.000 59.62980  ?  71   ASN   B N   1 
ATOM   14521 C  CA  . ASN   B 1 71   ? 80.36500   60.42300  -27.93000 1.000 40.93977  ?  71   ASN   B CA  1 
ATOM   14522 C  C   . ASN   B 1 71   ? 79.36900   59.76700  -26.98700 1.000 45.46686  ?  71   ASN   B C   1 
ATOM   14523 O  O   . ASN   B 1 71   ? 78.82700   58.69400  -27.27300 1.000 42.43858  ?  71   ASN   B O   1 
ATOM   14524 C  CB  . ASN   B 1 71   ? 79.63300   61.35500  -28.89900 1.000 37.22397  ?  71   ASN   B CB  1 
ATOM   14525 C  CG  . ASN   B 1 71   ? 79.05300   62.57000  -28.20600 1.000 50.53835  ?  71   ASN   B CG  1 
ATOM   14526 O  OD1 . ASN   B 1 71   ? 77.85100   62.64100  -27.95100 1.000 71.09168  ?  71   ASN   B OD1 1 
ATOM   14527 N  ND2 . ASN   B 1 71   ? 79.91100   63.53000  -27.88200 1.000 56.65288  ?  71   ASN   B ND2 1 
ATOM   14528 N  N   . LEU   B 1 72   ? 79.14400   60.42000  -25.85300 1.000 56.42996  ?  72   LEU   B N   1 
ATOM   14529 C  CA  . LEU   B 1 72   ? 78.17900   59.98300  -24.84900 1.000 57.95882  ?  72   LEU   B CA  1 
ATOM   14530 C  C   . LEU   B 1 72   ? 77.03000   60.98700  -24.85400 1.000 54.43346  ?  72   LEU   B C   1 
ATOM   14531 O  O   . LEU   B 1 72   ? 77.12900   62.06100  -24.25300 1.000 58.10096  ?  72   LEU   B O   1 
ATOM   14532 C  CB  . LEU   B 1 72   ? 78.82900   59.87300  -23.47200 1.000 54.37787  ?  72   LEU   B CB  1 
ATOM   14533 C  CG  . LEU   B 1 72   ? 79.69500   58.63800  -23.19500 1.000 56.46937  ?  72   LEU   B CG  1 
ATOM   14534 C  CD1 . LEU   B 1 72   ? 81.06100   58.75400  -23.85100 1.000 42.60332  ?  72   LEU   B CD1 1 
ATOM   14535 C  CD2 . LEU   B 1 72   ? 79.83500   58.39900  -21.69900 1.000 41.49475  ?  72   LEU   B CD2 1 
ATOM   14536 N  N   . HIS   B 1 73   ? 75.94300   60.63300  -25.53700 1.000 44.29809  ?  73   HIS   B N   1 
ATOM   14537 C  CA  . HIS   B 1 73   ? 74.79200   61.50900  -25.69200 1.000 56.02572  ?  73   HIS   B CA  1 
ATOM   14538 C  C   . HIS   B 1 73   ? 73.62700   60.99700  -24.85900 1.000 49.97466  ?  73   HIS   B C   1 
ATOM   14539 O  O   . HIS   B 1 73   ? 73.24300   59.82700  -24.99600 1.000 54.83801  ?  73   HIS   B O   1 
ATOM   14540 C  CB  . HIS   B 1 73   ? 74.38400   61.59600  -27.16600 1.000 59.35579  ?  73   HIS   B CB  1 
ATOM   14541 C  CG  . HIS   B 1 73   ? 73.38800   62.67500  -27.45700 1.000 52.34229  ?  73   HIS   B CG  1 
ATOM   14542 N  ND1 . HIS   B 1 73   ? 73.64100   64.00800  -27.21000 1.000 59.13267  ?  73   HIS   B ND1 1 
ATOM   14543 C  CD2 . HIS   B 1 73   ? 72.14100   62.62000  -27.98000 1.000 58.49990  ?  73   HIS   B CD2 1 
ATOM   14544 C  CE1 . HIS   B 1 73   ? 72.59100   64.72600  -27.56500 1.000 70.82995  ?  73   HIS   B CE1 1 
ATOM   14545 N  NE2 . HIS   B 1 73   ? 71.66600   63.90800  -28.03500 1.000 71.94334  ?  73   HIS   B NE2 1 
ATOM   14546 N  N   . PRO   B 1 74   ? 73.04600   61.82400  -23.98900 1.000 37.81398  ?  74   PRO   B N   1 
ATOM   14547 C  CA  . PRO   B 1 74   ? 71.93600   61.36700  -23.13200 1.000 43.88774  ?  74   PRO   B CA  1 
ATOM   14548 C  C   . PRO   B 1 74   ? 70.58300   61.43900  -23.83300 1.000 50.91003  ?  74   PRO   B C   1 
ATOM   14549 O  O   . PRO   B 1 74   ? 69.67900   62.17800  -23.43500 1.000 43.27350  ?  74   PRO   B O   1 
ATOM   14550 C  CB  . PRO   B 1 74   ? 72.03500   62.32300  -21.93800 1.000 35.63118  ?  74   PRO   B CB  1 
ATOM   14551 C  CG  . PRO   B 1 74   ? 72.54700   63.59000  -22.53400 1.000 54.01735  ?  74   PRO   B CG  1 
ATOM   14552 C  CD  . PRO   B 1 74   ? 73.48500   63.19000  -23.64600 1.000 39.54813  ?  74   PRO   B CD  1 
ATOM   14553 N  N   . SER   B 1 75   ? 70.44000   60.65700  -24.89800 1.000 51.96872  ?  75   SER   B N   1 
ATOM   14554 C  CA  . SER   B 1 75   ? 69.18600   60.57500  -25.63100 1.000 47.23071  ?  75   SER   B CA  1 
ATOM   14555 C  C   . SER   B 1 75   ? 69.12400   59.23200  -26.34000 1.000 57.72129  ?  75   SER   B C   1 
ATOM   14556 O  O   . SER   B 1 75   ? 70.11100   58.49700  -26.41300 1.000 68.60983  ?  75   SER   B O   1 
ATOM   14557 C  CB  . SER   B 1 75   ? 69.03600   61.72900  -26.63000 1.000 49.19804  ?  75   SER   B CB  1 
ATOM   14558 O  OG  . SER   B 1 75   ? 69.42400   61.33300  -27.93400 1.000 54.14117  ?  75   SER   B OG  1 
ATOM   14559 N  N   . LEU   B 1 76   ? 67.94100   58.91700  -26.86500 1.000 65.17499  ?  76   LEU   B N   1 
ATOM   14560 C  CA  . LEU   B 1 76   ? 67.73100   57.69100  -27.63100 1.000 50.80804  ?  76   LEU   B CA  1 
ATOM   14561 C  C   . LEU   B 1 76   ? 67.78600   58.06400  -29.10900 1.000 54.79914  ?  76   LEU   B C   1 
ATOM   14562 O  O   . LEU   B 1 76   ? 66.76700   58.23000  -29.77700 1.000 72.54311  ?  76   LEU   B O   1 
ATOM   14563 C  CB  . LEU   B 1 76   ? 66.40300   57.04200  -27.24300 1.000 54.63276  ?  76   LEU   B CB  1 
ATOM   14564 C  CG  . LEU   B 1 76   ? 66.20400   55.53800  -27.47500 1.000 56.14338  ?  76   LEU   B CG  1 
ATOM   14565 C  CD1 . LEU   B 1 76   ? 66.03700   55.18300  -28.95300 1.000 79.45217  ?  76   LEU   B CD1 1 
ATOM   14566 C  CD2 . LEU   B 1 76   ? 67.35100   54.74700  -26.86300 1.000 60.19840  ?  76   LEU   B CD2 1 
ATOM   14567 N  N   . LEU   B 1 77   ? 69.01200   58.21600  -29.61000 1.000 54.58492  ?  77   LEU   B N   1 
ATOM   14568 C  CA  . LEU   B 1 77   ? 69.21800   58.56300  -31.00700 1.000 50.49631  ?  77   LEU   B CA  1 
ATOM   14569 C  C   . LEU   B 1 77   ? 68.47400   57.57300  -31.89900 1.000 65.37684  ?  77   LEU   B C   1 
ATOM   14570 O  O   . LEU   B 1 77   ? 68.46200   56.36900  -31.60800 1.000 66.73830  ?  77   LEU   B O   1 
ATOM   14571 C  CB  . LEU   B 1 77   ? 70.70800   58.56500  -31.35100 1.000 48.82914  ?  77   LEU   B CB  1 
ATOM   14572 C  CG  . LEU   B 1 77   ? 71.53600   59.64300  -30.65100 1.000 53.42613  ?  77   LEU   B CG  1 
ATOM   14573 C  CD1 . LEU   B 1 77   ? 72.95800   59.69000  -31.19400 1.000 46.24051  ?  77   LEU   B CD1 1 
ATOM   14574 C  CD2 . LEU   B 1 77   ? 70.86000   60.99900  -30.77500 1.000 56.68689  ?  77   LEU   B CD2 1 
ATOM   14575 N  N   . PRO   B 1 78   ? 67.85600   58.02800  -32.99600 1.000 60.64080  ?  78   PRO   B N   1 
ATOM   14576 C  CA  . PRO   B 1 78   ? 67.97000   59.34400  -33.65000 1.000 60.56265  ?  78   PRO   B CA  1 
ATOM   14577 C  C   . PRO   B 1 78   ? 67.23700   60.50500  -32.97300 1.000 59.71095  ?  78   PRO   B C   1 
ATOM   14578 O  O   . PRO   B 1 78   ? 67.20400   61.60300  -33.52700 1.000 53.86862  ?  78   PRO   B O   1 
ATOM   14579 C  CB  . PRO   B 1 78   ? 67.36100   59.07000  -35.02600 1.000 53.95499  ?  78   PRO   B CB  1 
ATOM   14580 C  CG  . PRO   B 1 78   ? 66.23600   58.11200  -34.70800 1.000 68.31559  ?  78   PRO   B CG  1 
ATOM   14581 C  CD  . PRO   B 1 78   ? 66.75000   57.24200  -33.57500 1.000 54.52452  ?  78   PRO   B CD  1 
ATOM   14582 N  N   . TRP   B 1 79   ? 66.65200   60.31500  -31.79500 1.000 53.87184  ?  79   TRP   B N   1 
ATOM   14583 C  CA  . TRP   B 1 79   ? 65.80000   61.32500  -31.18200 1.000 52.05923  ?  79   TRP   B CA  1 
ATOM   14584 C  C   . TRP   B 1 79   ? 66.60200   62.30200  -30.33200 1.000 54.43833  ?  79   TRP   B C   1 
ATOM   14585 O  O   . TRP   B 1 79   ? 67.63300   61.95400  -29.75100 1.000 64.71509  ?  79   TRP   B O   1 
ATOM   14586 C  CB  . TRP   B 1 79   ? 64.72000   60.66600  -30.32200 1.000 48.51644  ?  79   TRP   B CB  1 
ATOM   14587 C  CG  . TRP   B 1 79   ? 63.83300   59.74600  -31.09200 1.000 54.53099  ?  79   TRP   B CG  1 
ATOM   14588 C  CD1 . TRP   B 1 79   ? 63.94200   58.38900  -31.18500 1.000 66.61690  ?  79   TRP   B CD1 1 
ATOM   14589 C  CD2 . TRP   B 1 79   ? 62.70400   60.11400  -31.89300 1.000 65.73203  ?  79   TRP   B CD2 1 
ATOM   14590 N  NE1 . TRP   B 1 79   ? 62.94700   57.88900  -31.99000 1.000 67.24506  ?  79   TRP   B NE1 1 
ATOM   14591 C  CE2 . TRP   B 1 79   ? 62.17400   58.92800  -32.43800 1.000 72.78172  ?  79   TRP   B CE2 1 
ATOM   14592 C  CE3 . TRP   B 1 79   ? 62.08900   61.33200  -32.20000 1.000 72.47063  ?  79   TRP   B CE3 1 
ATOM   14593 C  CZ2 . TRP   B 1 79   ? 61.05900   58.92300  -33.27200 1.000 75.65308  ?  79   TRP   B CZ2 1 
ATOM   14594 C  CZ3 . TRP   B 1 79   ? 60.98200   61.32500  -33.02900 1.000 73.76613  ?  79   TRP   B CZ3 1 
ATOM   14595 C  CH2 . TRP   B 1 79   ? 60.47800   60.13000  -33.55500 1.000 69.57694  ?  79   TRP   B CH2 1 
ATOM   14596 N  N   . ASN   B 1 80   ? 66.10500   63.54000  -30.27000 1.000 54.69641  ?  80   ASN   B N   1 
ATOM   14597 C  CA  . ASN   B 1 80   ? 66.62600   64.57200  -29.37100 1.000 55.71034  ?  80   ASN   B CA  1 
ATOM   14598 C  C   . ASN   B 1 80   ? 68.11100   64.83900  -29.61000 1.000 57.31177  ?  80   ASN   B C   1 
ATOM   14599 O  O   . ASN   B 1 80   ? 68.88500   65.03300  -28.67100 1.000 67.87356  ?  80   ASN   B O   1 
ATOM   14600 C  CB  . ASN   B 1 80   ? 66.36800   64.20600  -27.90900 1.000 47.32335  ?  80   ASN   B CB  1 
ATOM   14601 C  CG  . ASN   B 1 80   ? 64.94500   63.75300  -27.67000 1.000 52.74044  ?  80   ASN   B CG  1 
ATOM   14602 O  OD1 . ASN   B 1 80   ? 64.00300   64.53400  -27.80900 1.000 71.75042  ?  80   ASN   B OD1 1 
ATOM   14603 N  ND2 . ASN   B 1 80   ? 64.77900   62.48600  -27.30900 1.000 66.99471  ?  80   ASN   B ND2 1 
ATOM   14604 N  N   . LYS   B 1 81   ? 68.51200   64.84600  -30.87800 1.000 54.27132  ?  81   LYS   B N   1 
ATOM   14605 C  CA  . LYS   B 1 81   ? 69.88100   65.19500  -31.21700 1.000 54.20045  ?  81   LYS   B CA  1 
ATOM   14606 C  C   . LYS   B 1 81   ? 70.15000   66.66300  -30.89700 1.000 55.44561  ?  81   LYS   B C   1 
ATOM   14607 O  O   . LYS   B 1 81   ? 69.24000   67.49600  -30.84500 1.000 58.52806  ?  81   LYS   B O   1 
ATOM   14608 C  CB  . LYS   B 1 81   ? 70.15600   64.92500  -32.69800 1.000 57.32440  ?  81   LYS   B CB  1 
ATOM   14609 C  CG  . LYS   B 1 81   ? 69.94000   63.48100  -33.12300 1.000 63.03106  ?  81   LYS   B CG  1 
ATOM   14610 C  CD  . LYS   B 1 81   ? 70.37600   63.25200  -34.56300 1.000 46.93481  ?  81   LYS   B CD  1 
ATOM   14611 C  CE  . LYS   B 1 81   ? 69.37900   63.83200  -35.55100 1.000 62.96405  ?  81   LYS   B CE  1 
ATOM   14612 N  NZ  . LYS   B 1 81   ? 68.13000   63.02200  -35.61400 1.000 64.07605  ?  81   LYS   B NZ  1 
ATOM   14613 N  N   . GLY   B 1 82   ? 71.42300   66.97300  -30.67100 1.000 45.13690  ?  82   GLY   B N   1 
ATOM   14614 C  CA  . GLY   B 1 82   ? 71.82900   68.34500  -30.43600 1.000 42.02761  ?  82   GLY   B CA  1 
ATOM   14615 C  C   . GLY   B 1 82   ? 71.88900   68.74200  -28.97600 1.000 47.47513  ?  82   GLY   B C   1 
ATOM   14616 O  O   . GLY   B 1 82   ? 72.27900   67.94200  -28.11900 1.000 49.59417  ?  82   GLY   B O   1 
ATOM   14617 N  N   . ARG   B 1 83   ? 71.50200   69.98000  -28.68200 1.000 45.68238  ?  83   ARG   B N   1 
ATOM   14618 C  CA  . ARG   B 1 83   ? 71.63000   70.54700  -27.34600 1.000 42.97903  ?  83   ARG   B CA  1 
ATOM   14619 C  C   . ARG   B 1 83   ? 70.34400   70.34800  -26.55000 1.000 45.53870  ?  83   ARG   B C   1 
ATOM   14620 O  O   . ARG   B 1 83   ? 69.27800   70.08500  -27.10600 1.000 48.85471  ?  83   ARG   B O   1 
ATOM   14621 C  CB  . ARG   B 1 83   ? 71.96800   72.03600  -27.43000 1.000 43.89798  ?  83   ARG   B CB  1 
ATOM   14622 C  CG  . ARG   B 1 83   ? 73.09700   72.35600  -28.39100 1.000 58.06615  ?  83   ARG   B CG  1 
ATOM   14623 C  CD  . ARG   B 1 83   ? 74.44300   71.90200  -27.84800 1.000 54.80553  ?  83   ARG   B CD  1 
ATOM   14624 N  NE  . ARG   B 1 83   ? 75.09900   72.94900  -27.07300 1.000 46.71230  ?  83   ARG   B NE  1 
ATOM   14625 C  CZ  . ARG   B 1 83   ? 75.96800   73.81600  -27.57400 1.000 74.24572  ?  83   ARG   B CZ  1 
ATOM   14626 N  NH1 . ARG   B 1 83   ? 76.32100   73.78500  -28.84900 1.000 71.89345  ?  83   ARG   B NH1 1 
ATOM   14627 N  NH2 . ARG   B 1 83   ? 76.49800   74.73900  -26.77500 1.000 75.75096  ?  83   ARG   B NH2 1 
ATOM   14628 N  N   . ASP   B 1 84   ? 70.46500   70.49300  -25.23100 1.000 43.75895  ?  84   ASP   B N   1 
ATOM   14629 C  CA  . ASP   B 1 84   ? 69.36700   70.30100  -24.28900 1.000 41.20699  ?  84   ASP   B CA  1 
ATOM   14630 C  C   . ASP   B 1 84   ? 68.55600   69.03800  -24.60000 1.000 47.27626  ?  84   ASP   B C   1 
ATOM   14631 O  O   . ASP   B 1 84   ? 67.33700   69.10500  -24.75300 1.000 51.99791  ?  84   ASP   B O   1 
ATOM   14632 C  CB  . ASP   B 1 84   ? 68.45500   71.52000  -24.28300 1.000 37.31819  ?  84   ASP   B CB  1 
ATOM   14633 C  CG  . ASP   B 1 84   ? 69.20400   72.80000  -24.00400 1.000 45.81559  ?  84   ASP   B CG  1 
ATOM   14634 O  OD1 . ASP   B 1 84   ? 70.03000   72.80600  -23.06900 1.000 66.70591  ?  84   ASP   B OD1 1 
ATOM   14635 O  OD2 . ASP   B 1 84   ? 68.97400   73.79400  -24.72400 1.000 56.32373  -1 84   ASP   B OD2 1 
ATOM   14636 N  N   . PRO   B 1 85   ? 69.20700   67.87200  -24.68900 1.000 44.26897  ?  85   PRO   B N   1 
ATOM   14637 C  CA  . PRO   B 1 85   ? 68.50100   66.69400  -25.22100 1.000 44.11434  ?  85   PRO   B CA  1 
ATOM   14638 C  C   . PRO   B 1 85   ? 67.47800   66.09200  -24.27100 1.000 40.77968  ?  85   PRO   B C   1 
ATOM   14639 O  O   . PRO   B 1 85   ? 66.46800   65.55000  -24.73700 1.000 38.71468  ?  85   PRO   B O   1 
ATOM   14640 C  CB  . PRO   B 1 85   ? 69.64200   65.71100  -25.51000 1.000 40.32736  ?  85   PRO   B CB  1 
ATOM   14641 C  CG  . PRO   B 1 85   ? 70.68000   66.06500  -24.50600 1.000 48.88352  ?  85   PRO   B CG  1 
ATOM   14642 C  CD  . PRO   B 1 85   ? 70.59600   67.55500  -24.30700 1.000 51.04794  ?  85   PRO   B CD  1 
ATOM   14643 N  N   . VAL   B 1 86   ? 67.70500   66.15500  -22.95800 1.000 47.12406  ?  86   VAL   B N   1 
ATOM   14644 C  CA  . VAL   B 1 86   ? 66.78500   65.51200  -22.02500 1.000 48.29175  ?  86   VAL   B CA  1 
ATOM   14645 C  C   . VAL   B 1 86   ? 65.47400   66.28400  -21.94500 1.000 48.98301  ?  86   VAL   B C   1 
ATOM   14646 O  O   . VAL   B 1 86   ? 64.39200   65.68800  -21.87300 1.000 51.09996  ?  86   VAL   B O   1 
ATOM   14647 C  CB  . VAL   B 1 86   ? 67.44000   65.36000  -20.64000 1.000 43.21808  ?  86   VAL   B CB  1 
ATOM   14648 C  CG1 . VAL   B 1 86   ? 66.47300   64.70300  -19.66700 1.000 43.23084  ?  86   VAL   B CG1 1 
ATOM   14649 C  CG2 . VAL   B 1 86   ? 68.72200   64.54800  -20.74600 1.000 40.10554  ?  86   VAL   B CG2 1 
ATOM   14650 N  N   . PHE   B 1 87   ? 65.54500   67.61800  -21.96100 1.000 43.97832  ?  87   PHE   B N   1 
ATOM   14651 C  CA  . PHE   B 1 87   ? 64.32800   68.42500  -21.92700 1.000 34.99218  ?  87   PHE   B CA  1 
ATOM   14652 C  C   . PHE   B 1 87   ? 63.46600   68.16800  -23.15700 1.000 47.92642  ?  87   PHE   B C   1 
ATOM   14653 O  O   . PHE   B 1 87   ? 62.26700   67.88900  -23.04100 1.000 58.96856  ?  87   PHE   B O   1 
ATOM   14654 C  CB  . PHE   B 1 87   ? 64.67800   69.91000  -21.81300 1.000 29.29416  ?  87   PHE   B CB  1 
ATOM   14655 C  CG  . PHE   B 1 87   ? 63.53700   70.82600  -22.16000 1.000 45.23973  ?  87   PHE   B CG  1 
ATOM   14656 C  CD1 . PHE   B 1 87   ? 62.50500   71.04400  -21.26100 1.000 57.46771  ?  87   PHE   B CD1 1 
ATOM   14657 C  CD2 . PHE   B 1 87   ? 63.49300   71.46400  -23.38800 1.000 45.97237  ?  87   PHE   B CD2 1 
ATOM   14658 C  CE1 . PHE   B 1 87   ? 61.45200   71.88400  -21.58200 1.000 51.46830  ?  87   PHE   B CE1 1 
ATOM   14659 C  CE2 . PHE   B 1 87   ? 62.44500   72.30300  -23.71400 1.000 50.11229  ?  87   PHE   B CE2 1 
ATOM   14660 C  CZ  . PHE   B 1 87   ? 61.42400   72.51300  -22.81000 1.000 52.10312  ?  87   PHE   B CZ  1 
ATOM   14661 N  N   . TRP   B 1 88   ? 64.06400   68.25200  -24.35000 1.000 48.35788  ?  88   TRP   B N   1 
ATOM   14662 C  CA  . TRP   B 1 88   ? 63.32900   67.99200  -25.58100 1.000 46.45108  ?  88   TRP   B CA  1 
ATOM   14663 C  C   . TRP   B 1 88   ? 62.84700   66.54900  -25.69000 1.000 51.71697  ?  88   TRP   B C   1 
ATOM   14664 O  O   . TRP   B 1 88   ? 61.98200   66.26900  -26.52700 1.000 65.61112  ?  88   TRP   B O   1 
ATOM   14665 C  CB  . TRP   B 1 88   ? 64.18800   68.35400  -26.79600 1.000 41.03713  ?  88   TRP   B CB  1 
ATOM   14666 C  CG  . TRP   B 1 88   ? 64.40800   69.82900  -26.93600 1.000 41.13567  ?  88   TRP   B CG  1 
ATOM   14667 C  CD1 . TRP   B 1 88   ? 65.59100   70.49600  -26.81900 1.000 45.22824  ?  88   TRP   B CD1 1 
ATOM   14668 C  CD2 . TRP   B 1 88   ? 63.41100   70.82300  -27.20000 1.000 45.63992  ?  88   TRP   B CD2 1 
ATOM   14669 N  NE1 . TRP   B 1 88   ? 65.39500   71.84400  -27.00200 1.000 45.53129  ?  88   TRP   B NE1 1 
ATOM   14670 C  CE2 . TRP   B 1 88   ? 64.06500   72.07100  -27.23700 1.000 46.79275  ?  88   TRP   B CE2 1 
ATOM   14671 C  CE3 . TRP   B 1 88   ? 62.02900   70.77900  -27.41300 1.000 43.88167  ?  88   TRP   B CE3 1 
ATOM   14672 C  CZ2 . TRP   B 1 88   ? 63.38600   73.26300  -27.47800 1.000 45.05183  ?  88   TRP   B CZ2 1 
ATOM   14673 C  CZ3 . TRP   B 1 88   ? 61.35700   71.96400  -27.65200 1.000 51.00556  ?  88   TRP   B CZ3 1 
ATOM   14674 C  CH2 . TRP   B 1 88   ? 62.03500   73.18900  -27.68200 1.000 57.36718  ?  88   TRP   B CH2 1 
ATOM   14675 N  N   . SER   B 1 89   ? 63.38100   65.63200  -24.87700 1.000 45.86292  ?  89   SER   B N   1 
ATOM   14676 C  CA  . SER   B 1 89   ? 62.80600   64.29400  -24.79800 1.000 51.14920  ?  89   SER   B CA  1 
ATOM   14677 C  C   . SER   B 1 89   ? 61.49500   64.29300  -24.02400 1.000 61.91405  ?  89   SER   B C   1 
ATOM   14678 O  O   . SER   B 1 89   ? 60.60600   63.48600  -24.32000 1.000 66.63459  ?  89   SER   B O   1 
ATOM   14679 C  CB  . SER   B 1 89   ? 63.79500   63.32200  -24.15000 1.000 50.39687  ?  89   SER   B CB  1 
ATOM   14680 O  OG  . SER   B 1 89   ? 63.85300   63.50100  -22.74400 1.000 60.02841  ?  89   SER   B OG  1 
ATOM   14681 N  N   . VAL   B 1 90   ? 61.35400   65.18200  -23.04400 1.000 48.60349  ?  90   VAL   B N   1 
ATOM   14682 C  CA  . VAL   B 1 90   ? 60.12900   65.26500  -22.25600 1.000 50.61193  ?  90   VAL   B CA  1 
ATOM   14683 C  C   . VAL   B 1 90   ? 59.09300   66.14800  -22.93600 1.000 51.97251  ?  90   VAL   B C   1 
ATOM   14684 O  O   . VAL   B 1 90   ? 57.92400   65.77200  -23.05600 1.000 48.03874  ?  90   VAL   B O   1 
ATOM   14685 C  CB  . VAL   B 1 90   ? 60.45000   65.77600  -20.83700 1.000 40.64042  ?  90   VAL   B CB  1 
ATOM   14686 C  CG1 . VAL   B 1 90   ? 59.18100   65.84700  -19.99600 1.000 51.95047  ?  90   VAL   B CG1 1 
ATOM   14687 C  CG2 . VAL   B 1 90   ? 61.49100   64.88800  -20.17700 1.000 47.29614  ?  90   VAL   B CG2 1 
ATOM   14688 N  N   . TRP   B 1 91   ? 59.51100   67.33200  -23.39400 1.000 48.30201  ?  91   TRP   B N   1 
ATOM   14689 C  CA  . TRP   B 1 91   ? 58.57200   68.27600  -23.99300 1.000 43.80364  ?  91   TRP   B CA  1 
ATOM   14690 C  C   . TRP   B 1 91   ? 57.98000   67.72100  -25.28300 1.000 52.44249  ?  91   TRP   B C   1 
ATOM   14691 O  O   . TRP   B 1 91   ? 56.75700   67.70200  -25.46000 1.000 69.87151  ?  91   TRP   B O   1 
ATOM   14692 C  CB  . TRP   B 1 91   ? 59.26700   69.61500  -24.24600 1.000 34.22549  ?  91   TRP   B CB  1 
ATOM   14693 C  CG  . TRP   B 1 91   ? 58.34200   70.70000  -24.72400 1.000 40.94383  ?  91   TRP   B CG  1 
ATOM   14694 C  CD1 . TRP   B 1 91   ? 58.04000   71.00900  -26.01900 1.000 45.65887  ?  91   TRP   B CD1 1 
ATOM   14695 C  CD2 . TRP   B 1 91   ? 57.60300   71.62000  -23.91000 1.000 42.70578  ?  91   TRP   B CD2 1 
ATOM   14696 N  NE1 . TRP   B 1 91   ? 57.15900   72.06300  -26.06100 1.000 50.71659  ?  91   TRP   B NE1 1 
ATOM   14697 C  CE2 . TRP   B 1 91   ? 56.87500   72.45600  -24.78000 1.000 47.75052  ?  91   TRP   B CE2 1 
ATOM   14698 C  CE3 . TRP   B 1 91   ? 57.48700   71.81800  -22.53100 1.000 43.77341  ?  91   TRP   B CE3 1 
ATOM   14699 C  CZ2 . TRP   B 1 91   ? 56.04200   73.47200  -24.31600 1.000 50.35161  ?  91   TRP   B CZ2 1 
ATOM   14700 C  CZ3 . TRP   B 1 91   ? 56.65900   72.82800  -22.07200 1.000 52.27114  ?  91   TRP   B CZ3 1 
ATOM   14701 C  CH2 . TRP   B 1 91   ? 55.94800   73.64200  -22.96200 1.000 47.35151  ?  91   TRP   B CH2 1 
ATOM   14702 N  N   . ASP   B 1 92   ? 58.83200   67.25700  -26.19500 1.000 53.57354  ?  92   ASP   B N   1 
ATOM   14703 C  CA  . ASP   B 1 92   ? 58.36500   66.69900  -27.45800 1.000 43.21500  ?  92   ASP   B CA  1 
ATOM   14704 C  C   . ASP   B 1 92   ? 57.85000   65.27000  -27.32700 1.000 49.33858  ?  92   ASP   B C   1 
ATOM   14705 O  O   . ASP   B 1 92   ? 57.44500   64.68400  -28.33800 1.000 56.37784  ?  92   ASP   B O   1 
ATOM   14706 C  CB  . ASP   B 1 92   ? 59.48400   66.75600  -28.50100 1.000 39.28009  ?  92   ASP   B CB  1 
ATOM   14707 C  CG  . ASP   B 1 92   ? 59.80000   68.17300  -28.93800 1.000 67.16656  ?  92   ASP   B CG  1 
ATOM   14708 O  OD1 . ASP   B 1 92   ? 59.01700   69.08600  -28.60000 1.000 60.77033  ?  92   ASP   B OD1 1 
ATOM   14709 O  OD2 . ASP   B 1 92   ? 60.83000   68.37300  -29.61500 1.000 70.67172  -1 92   ASP   B OD2 1 
ATOM   14710 N  N   . GLU   B 1 93   ? 57.86000   64.70300  -26.11800 1.000 39.93718  ?  93   GLU   B N   1 
ATOM   14711 C  CA  . GLU   B 1 93   ? 57.30500   63.37300  -25.84800 1.000 57.37341  ?  93   GLU   B CA  1 
ATOM   14712 C  C   . GLU   B 1 93   ? 57.92500   62.30700  -26.75200 1.000 54.72705  ?  93   GLU   B C   1 
ATOM   14713 O  O   . GLU   B 1 93   ? 57.23300   61.43600  -27.28400 1.000 51.82515  ?  93   GLU   B O   1 
ATOM   14714 C  CB  . GLU   B 1 93   ? 55.78000   63.37700  -25.97300 1.000 69.34368  ?  93   GLU   B CB  1 
ATOM   14715 C  CG  . GLU   B 1 93   ? 55.10600   64.51500  -25.22000 1.000 63.73935  ?  93   GLU   B CG  1 
ATOM   14716 C  CD  . GLU   B 1 93   ? 53.66900   64.20400  -24.85700 1.000 67.28543  ?  93   GLU   B CD  1 
ATOM   14717 O  OE1 . GLU   B 1 93   ? 53.36900   63.02500  -24.57600 1.000 75.06321  ?  93   GLU   B OE1 1 
ATOM   14718 O  OE2 . GLU   B 1 93   ? 52.83800   65.13700  -24.85200 1.000 80.57149  -1 93   GLU   B OE2 1 
ATOM   14719 N  N   . THR   B 1 94   ? 59.23700   62.37400  -26.92000 1.000 67.48352  ?  94   THR   B N   1 
ATOM   14720 C  CA  . THR   B 1 94   ? 59.98200   61.41300  -27.72100 1.000 48.45626  ?  94   THR   B CA  1 
ATOM   14721 C  C   . THR   B 1 94   ? 60.36900   60.21400  -26.87000 1.000 54.91576  ?  94   THR   B C   1 
ATOM   14722 O  O   . THR   B 1 94   ? 60.21500   60.22800  -25.64500 1.000 57.30724  ?  94   THR   B O   1 
ATOM   14723 C  CB  . THR   B 1 94   ? 61.22400   62.08400  -28.30300 1.000 46.38860  ?  94   THR   B CB  1 
ATOM   14724 O  OG1 . THR   B 1 94   ? 62.20700   62.24200  -27.27200 1.000 59.37207  ?  94   THR   B OG1 1 
ATOM   14725 C  CG2 . THR   B 1 94   ? 60.87400   63.44700  -28.87500 1.000 53.63700  ?  94   THR   B CG2 1 
ATOM   14726 N  N   . PRO   B 1 95   ? 60.85800   59.13700  -27.48900 1.000 54.79549  ?  95   PRO   B N   1 
ATOM   14727 C  CA  . PRO   B 1 95   ? 61.41900   58.03500  -26.70000 1.000 53.66034  ?  95   PRO   B CA  1 
ATOM   14728 C  C   . PRO   B 1 95   ? 62.55300   58.51600  -25.80500 1.000 65.33160  ?  95   PRO   B C   1 
ATOM   14729 O  O   . PRO   B 1 95   ? 63.26100   59.47600  -26.11900 1.000 70.38383  ?  95   PRO   B O   1 
ATOM   14730 C  CB  . PRO   B 1 95   ? 61.92300   57.05700  -27.76600 1.000 59.71332  ?  95   PRO   B CB  1 
ATOM   14731 C  CG  . PRO   B 1 95   ? 61.03500   57.30400  -28.93100 1.000 63.95028  ?  95   PRO   B CG  1 
ATOM   14732 C  CD  . PRO   B 1 95   ? 60.72700   58.77700  -28.91400 1.000 50.17644  ?  95   PRO   B CD  1 
ATOM   14733 N  N   . LYS   B 1 96   ? 62.71700   57.83600  -24.67400 1.000 53.48136  ?  96   LYS   B N   1 
ATOM   14734 C  CA  . LYS   B 1 96   ? 63.69900   58.20600  -23.66500 1.000 70.38221  ?  96   LYS   B CA  1 
ATOM   14735 C  C   . LYS   B 1 96   ? 64.79300   57.14800  -23.58700 1.000 64.71606  ?  96   LYS   B C   1 
ATOM   14736 O  O   . LYS   B 1 96   ? 64.50900   55.94600  -23.58200 1.000 53.05213  ?  96   LYS   B O   1 
ATOM   14737 C  CB  . LYS   B 1 96   ? 63.03700   58.36600  -22.29200 1.000 39.66144  ?  96   LYS   B CB  1 
ATOM   14738 C  CG  . LYS   B 1 96   ? 61.72200   59.13400  -22.30200 1.000 59.79012  ?  96   LYS   B CG  1 
ATOM   14739 C  CD  . LYS   B 1 96   ? 61.93900   60.63600  -22.23400 1.000 59.72603  ?  96   LYS   B CD  1 
ATOM   14740 C  CE  . LYS   B 1 96   ? 60.63300   61.36700  -21.95000 1.000 55.92384  ?  96   LYS   B CE  1 
ATOM   14741 N  NZ  . LYS   B 1 96   ? 59.63800   61.20000  -23.04700 1.000 56.12854  ?  96   LYS   B NZ  1 
ATOM   14742 N  N   . GLY   B 1 97   ? 66.04100   57.59600  -23.52000 1.000 58.27491  ?  97   GLY   B N   1 
ATOM   14743 C  CA  . GLY   B 1 97   ? 67.14600   56.66300  -23.41200 1.000 58.00977  ?  97   GLY   B CA  1 
ATOM   14744 C  C   . GLY   B 1 97   ? 68.47700   57.38200  -23.41500 1.000 62.38005  ?  97   GLY   B C   1 
ATOM   14745 O  O   . GLY   B 1 97   ? 68.54900   58.60300  -23.26700 1.000 63.19331  ?  97   GLY   B O   1 
ATOM   14746 N  N   . VAL   B 1 98   ? 69.54100   56.59300  -23.57600 1.000 62.57371  ?  98   VAL   B N   1 
ATOM   14747 C  CA  . VAL   B 1 98   ? 70.90500   57.10200  -23.65800 1.000 52.48253  ?  98   VAL   B CA  1 
ATOM   14748 C  C   . VAL   B 1 98   ? 71.63700   56.34300  -24.75500 1.000 52.22179  ?  98   VAL   B C   1 
ATOM   14749 O  O   . VAL   B 1 98   ? 71.36000   55.16800  -25.01400 1.000 53.43366  ?  98   VAL   B O   1 
ATOM   14750 C  CB  . VAL   B 1 98   ? 71.65800   56.98000  -22.31500 1.000 43.04034  ?  98   VAL   B CB  1 
ATOM   14751 C  CG1 . VAL   B 1 98   ? 71.18900   58.05200  -21.34300 1.000 44.38145  ?  98   VAL   B CG1 1 
ATOM   14752 C  CG2 . VAL   B 1 98   ? 71.46100   55.59500  -21.72400 1.000 52.44327  ?  98   VAL   B CG2 1 
ATOM   14753 N  N   . THR   B 1 99   ? 72.58600   57.02000  -25.40000 1.000 50.64642  ?  99   THR   B N   1 
ATOM   14754 C  CA  . THR   B 1 99   ? 73.24000   56.47500  -26.58300 1.000 54.08373  ?  99   THR   B CA  1 
ATOM   14755 C  C   . THR   B 1 99   ? 74.74100   56.71100  -26.52400 1.000 63.54437  ?  99   THR   B C   1 
ATOM   14756 O  O   . THR   B 1 99   ? 75.18900   57.82000  -26.21800 1.000 48.30570  ?  99   THR   B O   1 
ATOM   14757 C  CB  . THR   B 1 99   ? 72.67500   57.10800  -27.86100 1.000 57.69101  ?  99   THR   B CB  1 
ATOM   14758 O  OG1 . THR   B 1 99   ? 71.25000   56.97100  -27.87600 1.000 71.91252  ?  99   THR   B OG1 1 
ATOM   14759 C  CG2 . THR   B 1 99   ? 73.26300   56.44100  -29.09900 1.000 53.29377  ?  99   THR   B CG2 1 
ATOM   14760 N  N   . ILE   B 1 100  ? 75.51000   55.66800  -26.82500 1.000 58.66442  ?  100  ILE   B N   1 
ATOM   14761 C  CA  . ILE   B 1 100  ? 76.93900   55.77900  -27.09600 1.000 54.24131  ?  100  ILE   B CA  1 
ATOM   14762 C  C   . ILE   B 1 100  ? 77.13000   55.52200  -28.58400 1.000 49.13508  ?  100  ILE   B C   1 
ATOM   14763 O  O   . ILE   B 1 100  ? 76.75700   54.45600  -29.09000 1.000 47.00704  ?  100  ILE   B O   1 
ATOM   14764 C  CB  . ILE   B 1 100  ? 77.75800   54.80100  -26.23900 1.000 56.69940  ?  100  ILE   B CB  1 
ATOM   14765 C  CG1 . ILE   B 1 100  ? 78.01900   55.40600  -24.86000 1.000 63.23371  ?  100  ILE   B CG1 1 
ATOM   14766 C  CG2 . ILE   B 1 100  ? 79.06700   54.43500  -26.92500 1.000 62.68102  ?  100  ILE   B CG2 1 
ATOM   14767 C  CD1 . ILE   B 1 100  ? 78.22800   54.37800  -23.77800 1.000 54.69180  ?  100  ILE   B CD1 1 
ATOM   14768 N  N   . HIS   B 1 101  ? 77.68900   56.50300  -29.29100 1.000 50.47366  ?  101  HIS   B N   1 
ATOM   14769 C  CA  . HIS   B 1 101  ? 77.72700   56.47000  -30.74600 1.000 58.42151  ?  101  HIS   B CA  1 
ATOM   14770 C  C   . HIS   B 1 101  ? 79.05600   57.01400  -31.25100 1.000 64.85961  ?  101  HIS   B C   1 
ATOM   14771 O  O   . HIS   B 1 101  ? 79.89300   57.49800  -30.48400 1.000 57.09358  ?  101  HIS   B O   1 
ATOM   14772 C  CB  . HIS   B 1 101  ? 76.56600   57.27200  -31.34600 1.000 53.07787  ?  101  HIS   B CB  1 
ATOM   14773 C  CG  . HIS   B 1 101  ? 76.60400   58.73000  -31.00900 1.000 44.63466  ?  101  HIS   B CG  1 
ATOM   14774 N  ND1 . HIS   B 1 101  ? 77.16600   59.67300  -31.84200 1.000 49.25483  ?  101  HIS   B ND1 1 
ATOM   14775 C  CD2 . HIS   B 1 101  ? 76.15800   59.40600  -29.92400 1.000 54.21824  ?  101  HIS   B CD2 1 
ATOM   14776 C  CE1 . HIS   B 1 101  ? 77.05900   60.86800  -31.28800 1.000 46.98954  ?  101  HIS   B CE1 1 
ATOM   14777 N  NE2 . HIS   B 1 101  ? 76.45100   60.73400  -30.12400 1.000 50.19215  ?  101  HIS   B NE2 1 
ATOM   14778 N  N   . LEU   B 1 102  ? 79.23800   56.92700  -32.56600 1.000 62.25562  ?  102  LEU   B N   1 
ATOM   14779 C  CA  . LEU   B 1 102  ? 80.40200   57.46700  -33.25000 1.000 48.01828  ?  102  LEU   B CA  1 
ATOM   14780 C  C   . LEU   B 1 102  ? 80.11800   58.88400  -33.74000 1.000 50.48223  ?  102  LEU   B C   1 
ATOM   14781 O  O   . LEU   B 1 102  ? 78.96600   59.29500  -33.89500 1.000 65.58254  ?  102  LEU   B O   1 
ATOM   14782 C  CB  . LEU   B 1 102  ? 80.79500   56.57200  -34.42700 1.000 49.37468  ?  102  LEU   B CB  1 
ATOM   14783 C  CG  . LEU   B 1 102  ? 81.25600   55.15200  -34.09100 1.000 52.21841  ?  102  LEU   B CG  1 
ATOM   14784 C  CD1 . LEU   B 1 102  ? 80.95200   54.20500  -35.23900 1.000 51.93205  ?  102  LEU   B CD1 1 
ATOM   14785 C  CD2 . LEU   B 1 102  ? 82.74000   55.14500  -33.77800 1.000 54.19042  ?  102  LEU   B CD2 1 
ATOM   14786 N  N   . ILE   B 1 103  ? 81.19000   59.63200  -33.98700 1.000 33.91519  ?  103  ILE   B N   1 
ATOM   14787 C  CA  . ILE   B 1 103  ? 81.10000   61.02700  -34.40600 1.000 50.91549  ?  103  ILE   B CA  1 
ATOM   14788 C  C   . ILE   B 1 103  ? 81.27500   61.10300  -35.91700 1.000 61.01617  ?  103  ILE   B C   1 
ATOM   14789 O  O   . ILE   B 1 103  ? 82.23300   60.54700  -36.46800 1.000 72.85318  ?  103  ILE   B O   1 
ATOM   14790 C  CB  . ILE   B 1 103  ? 82.14600   61.89200  -33.68100 1.000 44.07625  ?  103  ILE   B CB  1 
ATOM   14791 C  CG1 . ILE   B 1 103  ? 81.68600   62.21400  -32.25600 1.000 49.38884  ?  103  ILE   B CG1 1 
ATOM   14792 C  CG2 . ILE   B 1 103  ? 82.42600   63.17300  -34.45700 1.000 47.34576  ?  103  ILE   B CG2 1 
ATOM   14793 C  CD1 . ILE   B 1 103  ? 80.61100   63.27800  -32.18100 1.000 49.64871  ?  103  ILE   B CD1 1 
ATOM   14794 N  N   . ASP   B 1 104  ? 80.34700   61.78800  -36.58900 1.000 78.96665  ?  104  ASP   B N   1 
ATOM   14795 C  CA  . ASP   B 1 104  ? 80.40200   62.01600  -38.02200 1.000 72.87217  ?  104  ASP   B CA  1 
ATOM   14796 C  C   . ASP   B 1 104  ? 80.81900   63.46100  -38.30200 1.000 75.00919  ?  104  ASP   B C   1 
ATOM   14797 O  O   . ASP   B 1 104  ? 81.44200   64.12200  -37.45500 1.000 61.39023  ?  104  ASP   B O   1 
ATOM   14798 C  CB  . ASP   B 1 104  ? 79.04600   61.68500  -38.65600 1.000 70.48864  ?  104  ASP   B CB  1 
ATOM   14799 C  CG  . ASP   B 1 104  ? 78.74300   60.20500  -38.65800 1.000 92.89069  ?  104  ASP   B CG  1 
ATOM   14800 O  OD1 . ASP   B 1 104  ? 79.44800   59.44900  -37.95300 1.000 109.62319 ?  104  ASP   B OD1 1 
ATOM   14801 O  OD2 . ASP   B 1 104  ? 77.79000   59.79700  -39.35200 1.000 93.93141  -1 104  ASP   B OD2 1 
ATOM   14802 N  N   . GLU   B 1 105  ? 80.47600   63.95200  -39.49200 1.000 84.22230  ?  105  GLU   B N   1 
ATOM   14803 C  CA  . GLU   B 1 105  ? 80.64900   65.35600  -39.84000 1.000 77.40924  ?  105  GLU   B CA  1 
ATOM   14804 C  C   . GLU   B 1 105  ? 79.42000   66.19100  -39.51300 1.000 84.04849  ?  105  GLU   B C   1 
ATOM   14805 O  O   . GLU   B 1 105  ? 79.44600   67.41200  -39.70500 1.000 71.77428  ?  105  GLU   B O   1 
ATOM   14806 C  CB  . GLU   B 1 105  ? 80.98200   65.50200  -41.32800 1.000 78.84031  ?  105  GLU   B CB  1 
ATOM   14807 C  CG  . GLU   B 1 105  ? 82.03000   64.53400  -41.84700 1.000 90.33155  ?  105  GLU   B CG  1 
ATOM   14808 C  CD  . GLU   B 1 105  ? 81.43600   63.47200  -42.75100 1.000 101.55486 ?  105  GLU   B CD  1 
ATOM   14809 O  OE1 . GLU   B 1 105  ? 80.78400   62.54100  -42.23200 1.000 87.44545  ?  105  GLU   B OE1 1 
ATOM   14810 O  OE2 . GLU   B 1 105  ? 81.61000   63.57800  -43.98400 1.000 102.83019 -1 105  GLU   B OE2 1 
ATOM   14811 N  N   . HIS   B 1 106  ? 78.34700   65.56500  -39.04200 1.000 91.70782  ?  106  HIS   B N   1 
ATOM   14812 C  CA  . HIS   B 1 106  ? 77.13100   66.25500  -38.63800 1.000 80.69292  ?  106  HIS   B CA  1 
ATOM   14813 C  C   . HIS   B 1 106  ? 76.84200   65.94700  -37.17000 1.000 82.28025  ?  106  HIS   B C   1 
ATOM   14814 O  O   . HIS   B 1 106  ? 77.56800   65.20000  -36.51000 1.000 76.19523  ?  106  HIS   B O   1 
ATOM   14815 C  CB  . HIS   B 1 106  ? 75.95500   65.86300  -39.53800 1.000 75.29574  ?  106  HIS   B CB  1 
ATOM   14816 C  CG  . HIS   B 1 106  ? 76.32800   65.68000  -40.97700 1.000 81.04976  ?  106  HIS   B CG  1 
ATOM   14817 N  ND1 . HIS   B 1 106  ? 76.61800   66.73800  -41.81300 1.000 71.90543  ?  106  HIS   B ND1 1 
ATOM   14818 C  CD2 . HIS   B 1 106  ? 76.45900   64.56100  -41.72800 1.000 72.83082  ?  106  HIS   B CD2 1 
ATOM   14819 C  CE1 . HIS   B 1 106  ? 76.91200   66.27700  -43.01600 1.000 76.17603  ?  106  HIS   B CE1 1 
ATOM   14820 N  NE2 . HIS   B 1 106  ? 76.82300   64.96000  -42.99100 1.000 77.40300  ?  106  HIS   B NE2 1 
ATOM   14821 N  N   . VAL   B 1 107  ? 75.75900   66.52900  -36.66300 1.000 77.68011  ?  107  VAL   B N   1 
ATOM   14822 C  CA  . VAL   B 1 107  ? 75.47000   66.53500  -35.23200 1.000 48.19548  ?  107  VAL   B CA  1 
ATOM   14823 C  C   . VAL   B 1 107  ? 74.74400   65.24600  -34.86000 1.000 43.31231  ?  107  VAL   B C   1 
ATOM   14824 O  O   . VAL   B 1 107  ? 73.59900   65.02600  -35.26400 1.000 67.50166  ?  107  VAL   B O   1 
ATOM   14825 C  CB  . VAL   B 1 107  ? 74.64400   67.76400  -34.83800 1.000 48.42170  ?  107  VAL   B CB  1 
ATOM   14826 C  CG1 . VAL   B 1 107  ? 74.48800   67.83400  -33.32600 1.000 67.61869  ?  107  VAL   B CG1 1 
ATOM   14827 C  CG2 . VAL   B 1 107  ? 75.29300   69.02800  -35.37600 1.000 57.38150  ?  107  VAL   B CG2 1 
ATOM   14828 N  N   . ASP   B 1 108  ? 75.41900   64.39500  -34.08300 1.000 56.68239  ?  108  ASP   B N   1 
ATOM   14829 C  CA  . ASP   B 1 108  ? 74.81500   63.22100  -33.44500 1.000 58.19647  ?  108  ASP   B CA  1 
ATOM   14830 C  C   . ASP   B 1 108  ? 74.15200   62.28700  -34.45300 1.000 57.25896  ?  108  ASP   B C   1 
ATOM   14831 O  O   . ASP   B 1 108  ? 73.21400   61.55800  -34.11900 1.000 55.18406  ?  108  ASP   B O   1 
ATOM   14832 C  CB  . ASP   B 1 108  ? 73.81500   63.63900  -32.36400 1.000 58.94247  ?  108  ASP   B CB  1 
ATOM   14833 C  CG  . ASP   B 1 108  ? 74.43700   64.54200  -31.31400 1.000 66.76868  ?  108  ASP   B CG  1 
ATOM   14834 O  OD1 . ASP   B 1 108  ? 75.65700   64.42600  -31.07200 1.000 68.35095  ?  108  ASP   B OD1 1 
ATOM   14835 O  OD2 . ASP   B 1 108  ? 73.70600   65.37200  -30.73300 1.000 74.00963  -1 108  ASP   B OD2 1 
ATOM   14836 N  N   . THR   B 1 109  ? 74.63600   62.29500  -35.69000 1.000 58.79790  ?  109  THR   B N   1 
ATOM   14837 C  CA  . THR   B 1 109  ? 74.13000   61.41400  -36.73300 1.000 73.62413  ?  109  THR   B CA  1 
ATOM   14838 C  C   . THR   B 1 109  ? 74.92800   60.12400  -36.85800 1.000 79.81364  ?  109  THR   B C   1 
ATOM   14839 O  O   . THR   B 1 109  ? 74.58000   59.27800  -37.68500 1.000 86.28339  ?  109  THR   B O   1 
ATOM   14840 C  CB  . THR   B 1 109  ? 74.14000   62.13700  -38.08000 1.000 72.91362  ?  109  THR   B CB  1 
ATOM   14841 O  OG1 . THR   B 1 109  ? 73.72900   61.23200  -39.11300 1.000 98.63410  ?  109  THR   B OG1 1 
ATOM   14842 C  CG2 . THR   B 1 109  ? 75.53900   62.63100  -38.38500 1.000 79.00148  ?  109  THR   B CG2 1 
ATOM   14843 N  N   . GLY   B 1 110  ? 75.98500   59.95900  -36.06900 1.000 75.43527  ?  110  GLY   B N   1 
ATOM   14844 C  CA  . GLY   B 1 110  ? 76.86100   58.81600  -36.23300 1.000 73.42740  ?  110  GLY   B CA  1 
ATOM   14845 C  C   . GLY   B 1 110  ? 76.16700   57.50400  -35.92600 1.000 67.45833  ?  110  GLY   B C   1 
ATOM   14846 O  O   . GLY   B 1 110  ? 75.09000   57.44700  -35.33000 1.000 77.95924  ?  110  GLY   B O   1 
ATOM   14847 N  N   . ASP   B 1 111  ? 76.81200   56.42300  -36.36100 1.000 69.36244  ?  111  ASP   B N   1 
ATOM   14848 C  CA  . ASP   B 1 111  ? 76.29300   55.08900  -36.10900 1.000 61.92936  ?  111  ASP   B CA  1 
ATOM   14849 C  C   . ASP   B 1 111  ? 76.39300   54.76100  -34.62500 1.000 54.46392  ?  111  ASP   B C   1 
ATOM   14850 O  O   . ASP   B 1 111  ? 77.22500   55.30900  -33.89700 1.000 57.80392  ?  111  ASP   B O   1 
ATOM   14851 C  CB  . ASP   B 1 111  ? 77.05500   54.05300  -36.93500 1.000 73.97934  ?  111  ASP   B CB  1 
ATOM   14852 C  CG  . ASP   B 1 111  ? 77.27100   54.50200  -38.36600 1.000 79.97047  ?  111  ASP   B CG  1 
ATOM   14853 O  OD1 . ASP   B 1 111  ? 78.26900   55.20800  -38.62400 1.000 77.49274  ?  111  ASP   B OD1 1 
ATOM   14854 O  OD2 . ASP   B 1 111  ? 76.43700   54.15800  -39.23000 1.000 74.63973  -1 111  ASP   B OD2 1 
ATOM   14855 N  N   . ILE   B 1 112  ? 75.53600   53.86100  -34.18000 1.000 54.50902  ?  112  ILE   B N   1 
ATOM   14856 C  CA  . ILE   B 1 112  ? 75.36600   53.59000  -32.76000 1.000 62.28215  ?  112  ILE   B CA  1 
ATOM   14857 C  C   . ILE   B 1 112  ? 76.15600   52.35100  -32.37800 1.000 68.35029  ?  112  ILE   B C   1 
ATOM   14858 O  O   . ILE   B 1 112  ? 76.15100   51.34500  -33.09800 1.000 76.73151  ?  112  ILE   B O   1 
ATOM   14859 C  CB  . ILE   B 1 112  ? 73.87800   53.42700  -32.41500 1.000 61.75209  ?  112  ILE   B CB  1 
ATOM   14860 C  CG1 . ILE   B 1 112  ? 73.10700   54.64100  -32.93100 1.000 69.86434  ?  112  ILE   B CG1 1 
ATOM   14861 C  CG2 . ILE   B 1 112  ? 73.69500   53.22400  -30.91200 1.000 63.49199  ?  112  ILE   B CG2 1 
ATOM   14862 C  CD1 . ILE   B 1 112  ? 71.70300   54.74300  -32.39700 1.000 77.16975  ?  112  ILE   B CD1 1 
ATOM   14863 N  N   . LEU   B 1 113  ? 76.84200   52.42700  -31.24000 1.000 59.15255  ?  113  LEU   B N   1 
ATOM   14864 C  CA  . LEU   B 1 113  ? 77.57700   51.28900  -30.70100 1.000 59.16031  ?  113  LEU   B CA  1 
ATOM   14865 C  C   . LEU   B 1 113  ? 76.73000   50.53900  -29.67500 1.000 52.66506  ?  113  LEU   B C   1 
ATOM   14866 O  O   . LEU   B 1 113  ? 76.45300   49.34700  -29.83800 1.000 67.78056  ?  113  LEU   B O   1 
ATOM   14867 C  CB  . LEU   B 1 113  ? 78.89800   51.76600  -30.08900 1.000 61.01170  ?  113  LEU   B CB  1 
ATOM   14868 C  CG  . LEU   B 1 113  ? 79.77900   52.59100  -31.03200 1.000 61.86702  ?  113  LEU   B CG  1 
ATOM   14869 C  CD1 . LEU   B 1 113  ? 80.88100   53.31300  -30.27000 1.000 61.19720  ?  113  LEU   B CD1 1 
ATOM   14870 C  CD2 . LEU   B 1 113  ? 80.36800   51.70800  -32.12300 1.000 51.34620  ?  113  LEU   B CD2 1 
ATOM   14871 N  N   . VAL   B 1 114  ? 76.30500   51.23200  -28.62100 1.000 47.76148  ?  114  VAL   B N   1 
ATOM   14872 C  CA  . VAL   B 1 114  ? 75.40300   50.67200  -27.62300 1.000 65.37101  ?  114  VAL   B CA  1 
ATOM   14873 C  C   . VAL   B 1 114  ? 74.34100   51.70900  -27.29200 1.000 59.61346  ?  114  VAL   B C   1 
ATOM   14874 O  O   . VAL   B 1 114  ? 74.57900   52.91900  -27.36900 1.000 47.70077  ?  114  VAL   B O   1 
ATOM   14875 C  CB  . VAL   B 1 114  ? 76.14400   50.22500  -26.34300 1.000 73.18257  ?  114  VAL   B CB  1 
ATOM   14876 C  CG1 . VAL   B 1 114  ? 76.76600   48.85400  -26.54100 1.000 75.95067  ?  114  VAL   B CG1 1 
ATOM   14877 C  CG2 . VAL   B 1 114  ? 77.20800   51.24200  -25.96200 1.000 74.93227  ?  114  VAL   B CG2 1 
ATOM   14878 N  N   . GLN   B 1 115  ? 73.16000   51.22400  -26.92100 1.000 55.19519  ?  115  GLN   B N   1 
ATOM   14879 C  CA  . GLN   B 1 115  ? 72.05200   52.10100  -26.58200 1.000 55.92557  ?  115  GLN   B CA  1 
ATOM   14880 C  C   . GLN   B 1 115  ? 71.22300   51.46000  -25.48100 1.000 52.45606  ?  115  GLN   B C   1 
ATOM   14881 O  O   . GLN   B 1 115  ? 71.10100   50.23500  -25.40700 1.000 68.27231  ?  115  GLN   B O   1 
ATOM   14882 C  CB  . GLN   B 1 115  ? 71.18100   52.39900  -27.80500 1.000 65.71978  ?  115  GLN   B CB  1 
ATOM   14883 C  CG  . GLN   B 1 115  ? 70.79500   53.85700  -27.91300 1.000 62.37433  ?  115  GLN   B CG  1 
ATOM   14884 C  CD  . GLN   B 1 115  ? 70.04000   54.17700  -29.18700 1.000 59.98825  ?  115  GLN   B CD  1 
ATOM   14885 O  OE1 . GLN   B 1 115  ? 69.36900   53.31700  -29.75900 1.000 49.07549  ?  115  GLN   B OE1 1 
ATOM   14886 N  NE2 . GLN   B 1 115  ? 70.15200   55.42000  -29.64400 1.000 72.12210  ?  115  GLN   B NE2 1 
ATOM   14887 N  N   . GLU   B 1 116  ? 70.65300   52.30600  -24.62600 1.000 43.52062  ?  116  GLU   B N   1 
ATOM   14888 C  CA  . GLU   B 1 116  ? 69.86700   51.85900  -23.48800 1.000 59.99523  ?  116  GLU   B CA  1 
ATOM   14889 C  C   . GLU   B 1 116  ? 68.64400   52.75300  -23.35400 1.000 59.85237  ?  116  GLU   B C   1 
ATOM   14890 O  O   . GLU   B 1 116  ? 68.68600   53.93900  -23.69100 1.000 64.29442  ?  116  GLU   B O   1 
ATOM   14891 C  CB  . GLU   B 1 116  ? 70.69200   51.88600  -22.19100 1.000 62.55377  ?  116  GLU   B CB  1 
ATOM   14892 C  CG  . GLU   B 1 116  ? 70.03900   51.19200  -21.00600 1.000 69.83618  ?  116  GLU   B CG  1 
ATOM   14893 C  CD  . GLU   B 1 116  ? 70.83500   51.35500  -19.72500 1.000 87.50074  ?  116  GLU   B CD  1 
ATOM   14894 O  OE1 . GLU   B 1 116  ? 71.84700   52.08800  -19.74000 1.000 87.73247  ?  116  GLU   B OE1 1 
ATOM   14895 O  OE2 . GLU   B 1 116  ? 70.45000   50.75200  -18.70100 1.000 82.85029  -1 116  GLU   B OE2 1 
ATOM   14896 N  N   . GLU   B 1 117  ? 67.55200   52.17400  -22.86400 1.000 66.41477  ?  117  GLU   B N   1 
ATOM   14897 C  CA  . GLU   B 1 117  ? 66.29800   52.89400  -22.69300 1.000 65.19783  ?  117  GLU   B CA  1 
ATOM   14898 C  C   . GLU   B 1 117  ? 66.11000   53.26100  -21.22800 1.000 58.31074  ?  117  GLU   B C   1 
ATOM   14899 O  O   . GLU   B 1 117  ? 66.17200   52.39300  -20.35100 1.000 57.74309  ?  117  GLU   B O   1 
ATOM   14900 C  CB  . GLU   B 1 117  ? 65.11600   52.05700  -23.18600 1.000 63.24049  ?  117  GLU   B CB  1 
ATOM   14901 C  CG  . GLU   B 1 117  ? 63.77700   52.76200  -23.07100 1.000 76.89780  ?  117  GLU   B CG  1 
ATOM   14902 C  CD  . GLU   B 1 117  ? 62.92000   52.59100  -24.30800 1.000 79.09375  ?  117  GLU   B CD  1 
ATOM   14903 O  OE1 . GLU   B 1 117  ? 63.31600   51.81700  -25.20500 1.000 79.96839  ?  117  GLU   B OE1 1 
ATOM   14904 O  OE2 . GLU   B 1 117  ? 61.85200   53.23500  -24.38600 1.000 77.87432  -1 117  GLU   B OE2 1 
ATOM   14905 N  N   . ILE   B 1 118  ? 65.88900   54.54600  -20.96900 1.000 56.58848  ?  118  ILE   B N   1 
ATOM   14906 C  CA  . ILE   B 1 118  ? 65.64200   55.04000  -19.62300 1.000 62.25471  ?  118  ILE   B CA  1 
ATOM   14907 C  C   . ILE   B 1 118  ? 64.19600   55.51000  -19.54000 1.000 59.77364  ?  118  ILE   B C   1 
ATOM   14908 O  O   . ILE   B 1 118  ? 63.53700   55.76700  -20.55200 1.000 58.14417  ?  118  ILE   B O   1 
ATOM   14909 C  CB  . ILE   B 1 118  ? 66.61600   56.16900  -19.23100 1.000 49.10174  ?  118  ILE   B CB  1 
ATOM   14910 C  CG1 . ILE   B 1 118  ? 66.28100   57.45500  -19.98900 1.000 60.89551  ?  118  ILE   B CG1 1 
ATOM   14911 C  CG2 . ILE   B 1 118  ? 68.04600   55.75100  -19.51800 1.000 57.75694  ?  118  ILE   B CG2 1 
ATOM   14912 C  CD1 . ILE   B 1 118  ? 67.24100   58.59300  -19.71500 1.000 58.57374  ?  118  ILE   B CD1 1 
ATOM   14913 N  N   . ALA   B 1 119  ? 63.69700   55.61900  -18.31100 1.000 57.32930  ?  119  ALA   B N   1 
ATOM   14914 C  CA  . ALA   B 1 119  ? 62.31100   55.99300  -18.06400 1.000 45.23372  ?  119  ALA   B CA  1 
ATOM   14915 C  C   . ALA   B 1 119  ? 62.25400   57.10500  -17.03000 1.000 54.11535  ?  119  ALA   B C   1 
ATOM   14916 O  O   . ALA   B 1 119  ? 62.93300   57.03800  -16.00000 1.000 56.72301  ?  119  ALA   B O   1 
ATOM   14917 C  CB  . ALA   B 1 119  ? 61.49100   54.78900  -17.59100 1.000 50.37356  ?  119  ALA   B CB  1 
ATOM   14918 N  N   . PHE   B 1 120  ? 61.44100   58.12000  -17.30500 1.000 47.99625  ?  120  PHE   B N   1 
ATOM   14919 C  CA  . PHE   B 1 120  ? 61.23600   59.24000  -16.40100 1.000 53.18990  ?  120  PHE   B CA  1 
ATOM   14920 C  C   . PHE   B 1 120  ? 59.85700   59.14900  -15.76100 1.000 56.77129  ?  120  PHE   B C   1 
ATOM   14921 O  O   . PHE   B 1 120  ? 58.89400   58.68700  -16.38100 1.000 69.75111  ?  120  PHE   B O   1 
ATOM   14922 C  CB  . PHE   B 1 120  ? 61.37900   60.57500  -17.13900 1.000 49.40173  ?  120  PHE   B CB  1 
ATOM   14923 C  CG  . PHE   B 1 120  ? 62.77400   60.85500  -17.62000 1.000 65.73837  ?  120  PHE   B CG  1 
ATOM   14924 C  CD1 . PHE   B 1 120  ? 63.86900   60.54400  -16.83100 1.000 73.42779  ?  120  PHE   B CD1 1 
ATOM   14925 C  CD2 . PHE   B 1 120  ? 62.98900   61.42300  -18.86400 1.000 56.71874  ?  120  PHE   B CD2 1 
ATOM   14926 C  CE1 . PHE   B 1 120  ? 65.15500   60.80100  -17.27300 1.000 50.01418  ?  120  PHE   B CE1 1 
ATOM   14927 C  CE2 . PHE   B 1 120  ? 64.27100   61.68100  -19.31100 1.000 60.03541  ?  120  PHE   B CE2 1 
ATOM   14928 C  CZ  . PHE   B 1 120  ? 65.35500   61.36900  -18.51300 1.000 45.75537  ?  120  PHE   B CZ  1 
ATOM   14929 N  N   . ALA   B 1 121  ? 59.77000   59.59200  -14.51200 1.000 46.03399  ?  121  ALA   B N   1 
ATOM   14930 C  CA  . ALA   B 1 121  ? 58.51300   59.59000  -13.78200 1.000 51.66415  ?  121  ALA   B CA  1 
ATOM   14931 C  C   . ALA   B 1 121  ? 57.74400   60.88300  -14.03500 1.000 61.87431  ?  121  ALA   B C   1 
ATOM   14932 O  O   . ALA   B 1 121  ? 58.29800   61.88700  -14.48700 1.000 65.43076  ?  121  ALA   B O   1 
ATOM   14933 C  CB  . ALA   B 1 121  ? 58.75900   59.40900  -12.28400 1.000 48.45147  ?  121  ALA   B CB  1 
ATOM   14934 N  N   . ASP   B 1 122  ? 56.44300   60.84400  -13.73800 1.000 62.48960  ?  122  ASP   B N   1 
ATOM   14935 C  CA  . ASP   B 1 122  ? 55.61600   62.03500  -13.89800 1.000 62.34515  ?  122  ASP   B CA  1 
ATOM   14936 C  C   . ASP   B 1 122  ? 55.82900   63.03400  -12.76900 1.000 55.54275  ?  122  ASP   B C   1 
ATOM   14937 O  O   . ASP   B 1 122  ? 55.68300   64.24200  -12.98200 1.000 57.33543  ?  122  ASP   B O   1 
ATOM   14938 C  CB  . ASP   B 1 122  ? 54.13700   61.65200  -13.98600 1.000 55.29727  ?  122  ASP   B CB  1 
ATOM   14939 C  CG  . ASP   B 1 122  ? 53.78600   60.98100  -15.29800 1.000 68.22210  ?  122  ASP   B CG  1 
ATOM   14940 O  OD1 . ASP   B 1 122  ? 54.71100   60.52100  -16.00000 1.000 90.38113  ?  122  ASP   B OD1 1 
ATOM   14941 O  OD2 . ASP   B 1 122  ? 52.58400   60.92200  -15.63300 1.000 82.10229  -1 122  ASP   B OD2 1 
ATOM   14942 N  N   . GLU   B 1 123  ? 56.16800   62.55700  -11.57400 1.000 49.78455  ?  123  GLU   B N   1 
ATOM   14943 C  CA  . GLU   B 1 123  ? 56.46100   63.42600  -10.44400 1.000 61.21586  ?  123  GLU   B CA  1 
ATOM   14944 C  C   . GLU   B 1 123  ? 57.93100   63.81500  -10.37400 1.000 63.89027  ?  123  GLU   B C   1 
ATOM   14945 O  O   . GLU   B 1 123  ? 58.34400   64.46600  -9.40800  1.000 68.16504  ?  123  GLU   B O   1 
ATOM   14946 C  CB  . GLU   B 1 123  ? 56.03000   62.75400  -9.13800  1.000 62.78443  ?  123  GLU   B CB  1 
ATOM   14947 C  CG  . GLU   B 1 123  ? 54.55000   62.40000  -9.09000  1.000 81.33530  ?  123  GLU   B CG  1 
ATOM   14948 C  CD  . GLU   B 1 123  ? 53.65000   63.61800  -9.20700  1.000 93.05931  ?  123  GLU   B CD  1 
ATOM   14949 O  OE1 . GLU   B 1 123  ? 53.95700   64.65200  -8.57600  1.000 90.55886  ?  123  GLU   B OE1 1 
ATOM   14950 O  OE2 . GLU   B 1 123  ? 52.63800   63.54200  -9.93500  1.000 90.27965  -1 123  GLU   B OE2 1 
ATOM   14951 N  N   . ASP   B 1 124  ? 58.72500   63.42900  -11.37000 1.000 66.01911  ?  124  ASP   B N   1 
ATOM   14952 C  CA  . ASP   B 1 124  ? 60.12500   63.82100  -11.43100 1.000 60.78914  ?  124  ASP   B CA  1 
ATOM   14953 C  C   . ASP   B 1 124  ? 60.25400   65.20000  -12.06300 1.000 43.74518  ?  124  ASP   B C   1 
ATOM   14954 O  O   . ASP   B 1 124  ? 59.68500   65.46000  -13.12800 1.000 44.10961  ?  124  ASP   B O   1 
ATOM   14955 C  CB  . ASP   B 1 124  ? 60.93300   62.80200  -12.23500 1.000 47.32979  ?  124  ASP   B CB  1 
ATOM   14956 C  CG  . ASP   B 1 124  ? 61.50400   61.69700  -11.37200 1.000 66.36271  ?  124  ASP   B CG  1 
ATOM   14957 O  OD1 . ASP   B 1 124  ? 61.31400   61.74400  -10.13900 1.000 89.01252  ?  124  ASP   B OD1 1 
ATOM   14958 O  OD2 . ASP   B 1 124  ? 62.14800   60.78400  -11.93000 1.000 72.36410  -1 124  ASP   B OD2 1 
ATOM   14959 N  N   . THR   B 1 125  ? 61.00200   66.08300  -11.40800 1.000 45.70107  ?  125  THR   B N   1 
ATOM   14960 C  CA  . THR   B 1 125  ? 61.29400   67.37600  -12.00300 1.000 47.29094  ?  125  THR   B CA  1 
ATOM   14961 C  C   . THR   B 1 125  ? 62.24800   67.20200  -13.18100 1.000 53.51329  ?  125  THR   B C   1 
ATOM   14962 O  O   . THR   B 1 125  ? 62.86800   66.15000  -13.36400 1.000 49.52141  ?  125  THR   B O   1 
ATOM   14963 C  CB  . THR   B 1 125  ? 61.90500   68.32500  -10.97300 1.000 39.79008  ?  125  THR   B CB  1 
ATOM   14964 O  OG1 . THR   B 1 125  ? 63.28900   68.00400  -10.78900 1.000 65.79994  ?  125  THR   B OG1 1 
ATOM   14965 C  CG2 . THR   B 1 125  ? 61.18800   68.19300  -9.64100  1.000 59.05477  ?  125  THR   B CG2 1 
ATOM   14966 N  N   . LEU   B 1 126  ? 62.35800   68.25500  -13.99400 1.000 50.12407  ?  126  LEU   B N   1 
ATOM   14967 C  CA  . LEU   B 1 126  ? 63.27500   68.20100  -15.12800 1.000 45.21635  ?  126  LEU   B CA  1 
ATOM   14968 C  C   . LEU   B 1 126  ? 64.71300   68.02800  -14.66000 1.000 46.29184  ?  126  LEU   B C   1 
ATOM   14969 O  O   . LEU   B 1 126  ? 65.50500   67.33400  -15.30900 1.000 45.38172  ?  126  LEU   B O   1 
ATOM   14970 C  CB  . LEU   B 1 126  ? 63.13100   69.45700  -15.98700 1.000 43.65734  ?  126  LEU   B CB  1 
ATOM   14971 C  CG  . LEU   B 1 126  ? 62.35200   69.28300  -17.29200 1.000 33.58620  ?  126  LEU   B CG  1 
ATOM   14972 C  CD1 . LEU   B 1 126  ? 63.02600   68.25100  -18.18400 1.000 38.43050  ?  126  LEU   B CD1 1 
ATOM   14973 C  CD2 . LEU   B 1 126  ? 60.91700   68.88500  -17.00600 1.000 55.43592  ?  126  LEU   B CD2 1 
ATOM   14974 N  N   . LEU   B 1 127  ? 65.06800   68.64200  -13.52800 1.000 43.67395  ?  127  LEU   B N   1 
ATOM   14975 C  CA  . LEU   B 1 127  ? 66.40700   68.45500  -12.98000 1.000 41.06455  ?  127  LEU   B CA  1 
ATOM   14976 C  C   . LEU   B 1 127  ? 66.62600   67.00900  -12.55700 1.000 37.60102  ?  127  LEU   B C   1 
ATOM   14977 O  O   . LEU   B 1 127  ? 67.70600   66.44700  -12.77600 1.000 51.45502  ?  127  LEU   B O   1 
ATOM   14978 C  CB  . LEU   B 1 127  ? 66.63400   69.40100  -11.80100 1.000 31.28604  ?  127  LEU   B CB  1 
ATOM   14979 C  CG  . LEU   B 1 127  ? 66.50600   70.89400  -12.10300 1.000 41.34549  ?  127  LEU   B CG  1 
ATOM   14980 C  CD1 . LEU   B 1 127  ? 67.09900   71.72200  -10.97300 1.000 39.40608  ?  127  LEU   B CD1 1 
ATOM   14981 C  CD2 . LEU   B 1 127  ? 67.16100   71.24100  -13.43200 1.000 55.35343  ?  127  LEU   B CD2 1 
ATOM   14982 N  N   . ASP   B 1 128  ? 65.61100   66.38900  -11.95000 1.000 40.34786  ?  128  ASP   B N   1 
ATOM   14983 C  CA  . ASP   B 1 128  ? 65.70500   64.97000  -11.62800 1.000 50.47595  ?  128  ASP   B CA  1 
ATOM   14984 C  C   . ASP   B 1 128  ? 65.90900   64.13100  -12.88100 1.000 51.64102  ?  128  ASP   B C   1 
ATOM   14985 O  O   . ASP   B 1 128  ? 66.59400   63.10400  -12.83500 1.000 50.11683  ?  128  ASP   B O   1 
ATOM   14986 C  CB  . ASP   B 1 128  ? 64.45100   64.51400  -10.88100 1.000 49.28160  ?  128  ASP   B CB  1 
ATOM   14987 C  CG  . ASP   B 1 128  ? 64.26600   65.23100  -9.55800  1.000 56.42406  ?  128  ASP   B CG  1 
ATOM   14988 O  OD1 . ASP   B 1 128  ? 65.18600   65.96600  -9.14200  1.000 74.53351  ?  128  ASP   B OD1 1 
ATOM   14989 O  OD2 . ASP   B 1 128  ? 63.19700   65.06000  -8.93500  1.000 57.32383  -1 128  ASP   B OD2 1 
ATOM   14990 N  N   . CYS   B 1 129  ? 65.33500   64.55600  -14.00800 1.000 52.02441  ?  129  CYS   B N   1 
ATOM   14991 C  CA  . CYS   B 1 129  ? 65.50100   63.80600  -15.24800 1.000 57.32602  ?  129  CYS   B CA  1 
ATOM   14992 C  C   . CYS   B 1 129  ? 66.92200   63.93100  -15.78400 1.000 55.40366  ?  129  CYS   B C   1 
ATOM   14993 O  O   . CYS   B 1 129  ? 67.49300   62.94900  -16.27400 1.000 53.38457  ?  129  CYS   B O   1 
ATOM   14994 C  CB  . CYS   B 1 129  ? 64.49000   64.28300  -16.28900 1.000 52.95777  ?  129  CYS   B CB  1 
ATOM   14995 S  SG  . CYS   B 1 129  ? 62.76400   64.04300  -15.81200 1.000 59.74283  ?  129  CYS   B SG  1 
ATOM   14996 N  N   . TYR   B 1 130  ? 67.50800   65.12900  -15.70100 1.000 48.45041  ?  130  TYR   B N   1 
ATOM   14997 C  CA  . TYR   B 1 130  ? 68.86900   65.32100  -16.19500 1.000 35.45390  ?  130  TYR   B CA  1 
ATOM   14998 C  C   . TYR   B 1 130  ? 69.84600   64.41000  -15.46900 1.000 42.11750  ?  130  TYR   B C   1 
ATOM   14999 O  O   . TYR   B 1 130  ? 70.74500   63.83000  -16.09000 1.000 55.09990  ?  130  TYR   B O   1 
ATOM   15000 C  CB  . TYR   B 1 130  ? 69.29600   66.78100  -16.03600 1.000 30.33044  ?  130  TYR   B CB  1 
ATOM   15001 C  CG  . TYR   B 1 130  ? 68.35500   67.77500  -16.67000 1.000 40.73970  ?  130  TYR   B CG  1 
ATOM   15002 C  CD1 . TYR   B 1 130  ? 67.58700   67.42500  -17.76900 1.000 46.78658  ?  130  TYR   B CD1 1 
ATOM   15003 C  CD2 . TYR   B 1 130  ? 68.23100   69.06200  -16.16500 1.000 42.59951  ?  130  TYR   B CD2 1 
ATOM   15004 C  CE1 . TYR   B 1 130  ? 66.72400   68.32100  -18.34900 1.000 52.58298  ?  130  TYR   B CE1 1 
ATOM   15005 C  CE2 . TYR   B 1 130  ? 67.36700   69.97100  -16.74200 1.000 49.83188  ?  130  TYR   B CE2 1 
ATOM   15006 C  CZ  . TYR   B 1 130  ? 66.61700   69.59000  -17.83500 1.000 55.24780  ?  130  TYR   B CZ  1 
ATOM   15007 O  OH  . TYR   B 1 130  ? 65.74800   70.47100  -18.42700 1.000 65.92984  ?  130  TYR   B OH  1 
ATOM   15008 N  N   . ASN   B 1 131  ? 69.68400   64.26900  -14.15200 1.000 39.05651  ?  131  ASN   B N   1 
ATOM   15009 C  CA  . ASN   B 1 131  ? 70.58100   63.41500  -13.38100 1.000 48.06485  ?  131  ASN   B CA  1 
ATOM   15010 C  C   . ASN   B 1 131  ? 70.47000   61.96200  -13.82300 1.000 50.07816  ?  131  ASN   B C   1 
ATOM   15011 O  O   . ASN   B 1 131  ? 71.48200   61.30400  -14.09200 1.000 46.81167  ?  131  ASN   B O   1 
ATOM   15012 C  CB  . ASN   B 1 131  ? 70.28100   63.54700  -11.88800 1.000 37.53780  ?  131  ASN   B CB  1 
ATOM   15013 C  CG  . ASN   B 1 131  ? 70.75400   64.86500  -11.30900 1.000 45.26627  ?  131  ASN   B CG  1 
ATOM   15014 O  OD1 . ASN   B 1 131  ? 69.98000   65.59900  -10.69700 1.000 46.89328  ?  131  ASN   B OD1 1 
ATOM   15015 N  ND2 . ASN   B 1 131  ? 72.03500   65.16800  -11.49200 1.000 60.55068  ?  131  ASN   B ND2 1 
ATOM   15016 N  N   . LYS   B 1 132  ? 69.24000   61.44700  -13.90700 1.000 42.16249  ?  132  LYS   B N   1 
ATOM   15017 C  CA  . LYS   B 1 132  ? 69.04500   60.04100  -14.25000 1.000 41.64765  ?  132  LYS   B CA  1 
ATOM   15018 C  C   . LYS   B 1 132  ? 69.62800   59.71700  -15.61900 1.000 48.54088  ?  132  LYS   B C   1 
ATOM   15019 O  O   . LYS   B 1 132  ? 70.20000   58.63900  -15.81900 1.000 41.24745  ?  132  LYS   B O   1 
ATOM   15020 C  CB  . LYS   B 1 132  ? 67.55700   59.69500  -14.20200 1.000 52.46370  ?  132  LYS   B CB  1 
ATOM   15021 C  CG  . LYS   B 1 132  ? 66.89300   60.01400  -12.87500 1.000 55.11389  ?  132  LYS   B CG  1 
ATOM   15022 C  CD  . LYS   B 1 132  ? 65.38600   59.84500  -12.95300 1.000 54.85892  ?  132  LYS   B CD  1 
ATOM   15023 C  CE  . LYS   B 1 132  ? 64.91700   58.70000  -12.06900 1.000 77.21748  ?  132  LYS   B CE  1 
ATOM   15024 N  NZ  . LYS   B 1 132  ? 63.44500   58.48900  -12.14800 1.000 69.93716  ?  132  LYS   B NZ  1 
ATOM   15025 N  N   . ALA   B 1 133  ? 69.49900   60.64100  -16.57300 1.000 51.78163  ?  133  ALA   B N   1 
ATOM   15026 C  CA  . ALA   B 1 133  ? 70.06700   60.42200  -17.89900 1.000 51.75100  ?  133  ALA   B CA  1 
ATOM   15027 C  C   . ALA   B 1 133  ? 71.59000   60.44200  -17.85300 1.000 56.54977  ?  133  ALA   B C   1 
ATOM   15028 O  O   . ALA   B 1 133  ? 72.25100   59.58400  -18.45200 1.000 54.04360  ?  133  ALA   B O   1 
ATOM   15029 C  CB  . ALA   B 1 133  ? 69.54200   61.47400  -18.87600 1.000 46.22353  ?  133  ALA   B CB  1 
ATOM   15030 N  N   . ASN   B 1 134  ? 72.16700   61.41900  -17.14700 1.000 50.16290  ?  134  ASN   B N   1 
ATOM   15031 C  CA  . ASN   B 1 134  ? 73.61900   61.48200  -17.02600 1.000 41.10311  ?  134  ASN   B CA  1 
ATOM   15032 C  C   . ASN   B 1 134  ? 74.17300   60.27200  -16.28600 1.000 51.69971  ?  134  ASN   B C   1 
ATOM   15033 O  O   . ASN   B 1 134  ? 75.26800   59.79800  -16.60900 1.000 58.38319  ?  134  ASN   B O   1 
ATOM   15034 C  CB  . ASN   B 1 134  ? 74.03500   62.77500  -16.32300 1.000 36.64917  ?  134  ASN   B CB  1 
ATOM   15035 C  CG  . ASN   B 1 134  ? 73.89800   63.99600  -17.21500 1.000 52.95246  ?  134  ASN   B CG  1 
ATOM   15036 O  OD1 . ASN   B 1 134  ? 74.12000   63.92400  -18.42500 1.000 47.79861  ?  134  ASN   B OD1 1 
ATOM   15037 N  ND2 . ASN   B 1 134  ? 73.53400   65.12700  -16.62000 1.000 54.94277  ?  134  ASN   B ND2 1 
ATOM   15038 N  N   . GLN   B 1 135  ? 73.43700   59.75400  -15.30000 1.000 46.61169  ?  135  GLN   B N   1 
ATOM   15039 C  CA  . GLN   B 1 135  ? 73.88600   58.55000  -14.60900 1.000 41.84000  ?  135  GLN   B CA  1 
ATOM   15040 C  C   . GLN   B 1 135  ? 73.82600   57.33300  -15.52300 1.000 45.52395  ?  135  GLN   B C   1 
ATOM   15041 O  O   . GLN   B 1 135  ? 74.70900   56.46900  -15.47300 1.000 61.69673  ?  135  GLN   B O   1 
ATOM   15042 C  CB  . GLN   B 1 135  ? 73.04600   58.30900  -13.35500 1.000 51.60991  ?  135  GLN   B CB  1 
ATOM   15043 C  CG  . GLN   B 1 135  ? 73.54900   59.02300  -12.11500 1.000 71.08528  ?  135  GLN   B CG  1 
ATOM   15044 C  CD  . GLN   B 1 135  ? 72.96000   58.44800  -10.84200 1.000 87.66187  ?  135  GLN   B CD  1 
ATOM   15045 O  OE1 . GLN   B 1 135  ? 72.18700   57.49000  -10.88000 1.000 83.04316  ?  135  GLN   B OE1 1 
ATOM   15046 N  NE2 . GLN   B 1 135  ? 73.32600   59.02900  -9.70600  1.000 79.99469  ?  135  GLN   B NE2 1 
ATOM   15047 N  N   . ALA   B 1 136  ? 72.79300   57.24800  -16.36300 1.000 44.20817  ?  136  ALA   B N   1 
ATOM   15048 C  CA  . ALA   B 1 136  ? 72.65100   56.09000  -17.23900 1.000 41.68933  ?  136  ALA   B CA  1 
ATOM   15049 C  C   . ALA   B 1 136  ? 73.76900   56.03400  -18.27200 1.000 45.02136  ?  136  ALA   B C   1 
ATOM   15050 O  O   . ALA   B 1 136  ? 74.34800   54.96800  -18.50900 1.000 57.47192  ?  136  ALA   B O   1 
ATOM   15051 C  CB  . ALA   B 1 136  ? 71.28700   56.11800  -17.92500 1.000 33.27740  ?  136  ALA   B CB  1 
ATOM   15052 N  N   . ILE   B 1 137  ? 74.09100   57.17100  -18.89300 1.000 47.91942  ?  137  ILE   B N   1 
ATOM   15053 C  CA  . ILE   B 1 137  ? 75.13600   57.17500  -19.91000 1.000 54.32844  ?  137  ILE   B CA  1 
ATOM   15054 C  C   . ILE   B 1 137  ? 76.50300   56.94900  -19.27700 1.000 46.44137  ?  137  ILE   B C   1 
ATOM   15055 O  O   . ILE   B 1 137  ? 77.40800   56.40000  -19.91700 1.000 52.00669  ?  137  ILE   B O   1 
ATOM   15056 C  CB  . ILE   B 1 137  ? 75.08500   58.48200  -20.72600 1.000 45.83421  ?  137  ILE   B CB  1 
ATOM   15057 C  CG1 . ILE   B 1 137  ? 75.96700   58.37000  -21.96900 1.000 38.11221  ?  137  ILE   B CG1 1 
ATOM   15058 C  CG2 . ILE   B 1 137  ? 75.49400   59.67400  -19.87300 1.000 44.85756  ?  137  ILE   B CG2 1 
ATOM   15059 C  CD1 . ILE   B 1 137  ? 75.60900   57.20600  -22.86200 1.000 47.57917  ?  137  ILE   B CD1 1 
ATOM   15060 N  N   . GLU   B 1 138  ? 76.67800   57.34900  -18.01500 1.000 47.16526  ?  138  GLU   B N   1 
ATOM   15061 C  CA  . GLU   B 1 138  ? 77.93000   57.06400  -17.32400 1.000 59.68909  ?  138  GLU   B CA  1 
ATOM   15062 C  C   . GLU   B 1 138  ? 78.04500   55.58300  -16.98500 1.000 59.67499  ?  138  GLU   B C   1 
ATOM   15063 O  O   . GLU   B 1 138  ? 79.10700   54.97800  -17.17100 1.000 55.16292  ?  138  GLU   B O   1 
ATOM   15064 C  CB  . GLU   B 1 138  ? 78.04100   57.92000  -16.06300 1.000 44.41643  ?  138  GLU   B CB  1 
ATOM   15065 C  CG  . GLU   B 1 138  ? 78.33800   59.38700  -16.33700 1.000 49.06372  ?  138  GLU   B CG  1 
ATOM   15066 C  CD  . GLU   B 1 138  ? 78.08200   60.26600  -15.13000 1.000 58.37480  ?  138  GLU   B CD  1 
ATOM   15067 O  OE1 . GLU   B 1 138  ? 77.92900   59.71800  -14.01800 1.000 53.54158  ?  138  GLU   B OE1 1 
ATOM   15068 O  OE2 . GLU   B 1 138  ? 78.02600   61.50400  -15.29400 1.000 56.56311  -1 138  GLU   B OE2 1 
ATOM   15069 N  N   . GLU   B 1 139  ? 76.95800   54.98000  -16.49600 1.000 55.09449  ?  139  GLU   B N   1 
ATOM   15070 C  CA  . GLU   B 1 139  ? 76.99100   53.56000  -16.15800 1.000 57.54065  ?  139  GLU   B CA  1 
ATOM   15071 C  C   . GLU   B 1 139  ? 77.06200   52.69400  -17.41000 1.000 58.25442  ?  139  GLU   B C   1 
ATOM   15072 O  O   . GLU   B 1 139  ? 77.70700   51.63900  -17.40400 1.000 59.70854  ?  139  GLU   B O   1 
ATOM   15073 C  CB  . GLU   B 1 139  ? 75.77000   53.19200  -15.31500 1.000 64.44277  ?  139  GLU   B CB  1 
ATOM   15074 C  CG  . GLU   B 1 139  ? 75.75300   53.83300  -13.93400 1.000 67.01339  ?  139  GLU   B CG  1 
ATOM   15075 C  CD  . GLU   B 1 139  ? 76.88100   53.34000  -13.04700 1.000 93.96886  ?  139  GLU   B CD  1 
ATOM   15076 O  OE1 . GLU   B 1 139  ? 77.20000   52.13400  -13.10300 1.000 101.14619 ?  139  GLU   B OE1 1 
ATOM   15077 O  OE2 . GLU   B 1 139  ? 77.45200   54.16000  -12.29700 1.000 99.55364  -1 139  GLU   B OE2 1 
ATOM   15078 N  N   . LEU   B 1 140  ? 76.40400   53.12000  -18.49200 1.000 52.80298  ?  140  LEU   B N   1 
ATOM   15079 C  CA  . LEU   B 1 140  ? 76.46400   52.36100  -19.73800 1.000 56.53543  ?  140  LEU   B CA  1 
ATOM   15080 C  C   . LEU   B 1 140  ? 77.88300   52.32700  -20.28900 1.000 56.66171  ?  140  LEU   B C   1 
ATOM   15081 O  O   . LEU   B 1 140  ? 78.34800   51.28400  -20.76500 1.000 56.68759  ?  140  LEU   B O   1 
ATOM   15082 C  CB  . LEU   B 1 140  ? 75.50200   52.96000  -20.76400 1.000 57.54800  ?  140  LEU   B CB  1 
ATOM   15083 C  CG  . LEU   B 1 140  ? 75.39000   52.23400  -22.10700 1.000 56.26331  ?  140  LEU   B CG  1 
ATOM   15084 C  CD1 . LEU   B 1 140  ? 74.61300   50.93700  -21.95700 1.000 58.09166  ?  140  LEU   B CD1 1 
ATOM   15085 C  CD2 . LEU   B 1 140  ? 74.75500   53.12700  -23.16300 1.000 43.60572  ?  140  LEU   B CD2 1 
ATOM   15086 N  N   . PHE   B 1 141  ? 78.58500   53.46100  -20.23400 1.000 50.56549  ?  141  PHE   B N   1 
ATOM   15087 C  CA  . PHE   B 1 141  ? 79.98400   53.49700  -20.65000 1.000 43.80652  ?  141  PHE   B CA  1 
ATOM   15088 C  C   . PHE   B 1 141  ? 80.82700   52.55300  -19.80100 1.000 53.43518  ?  141  PHE   B C   1 
ATOM   15089 O  O   . PHE   B 1 141  ? 81.62000   51.76500  -20.32900 1.000 54.17821  ?  141  PHE   B O   1 
ATOM   15090 C  CB  . PHE   B 1 141  ? 80.51200   54.93100  -20.56200 1.000 48.57753  ?  141  PHE   B CB  1 
ATOM   15091 C  CG  . PHE   B 1 141  ? 81.94900   55.08300  -20.97800 1.000 52.09220  ?  141  PHE   B CG  1 
ATOM   15092 C  CD1 . PHE   B 1 141  ? 82.97400   54.92500  -20.05700 1.000 51.96982  ?  141  PHE   B CD1 1 
ATOM   15093 C  CD2 . PHE   B 1 141  ? 82.27500   55.39800  -22.28600 1.000 57.76934  ?  141  PHE   B CD2 1 
ATOM   15094 C  CE1 . PHE   B 1 141  ? 84.29400   55.06600  -20.43500 1.000 58.44474  ?  141  PHE   B CE1 1 
ATOM   15095 C  CE2 . PHE   B 1 141  ? 83.59500   55.54400  -22.67000 1.000 58.15573  ?  141  PHE   B CE2 1 
ATOM   15096 C  CZ  . PHE   B 1 141  ? 84.60600   55.37700  -21.74300 1.000 60.89897  ?  141  PHE   B CZ  1 
ATOM   15097 N  N   . ILE   B 1 142  ? 80.66100   52.61900  -18.47700 1.000 53.03541  ?  142  ILE   B N   1 
ATOM   15098 C  CA  . ILE   B 1 142  ? 81.41000   51.75200  -17.57100 1.000 48.80832  ?  142  ILE   B CA  1 
ATOM   15099 C  C   . ILE   B 1 142  ? 81.11800   50.28300  -17.85700 1.000 58.62927  ?  142  ILE   B C   1 
ATOM   15100 O  O   . ILE   B 1 142  ? 81.96600   49.41300  -17.61900 1.000 55.63274  ?  142  ILE   B O   1 
ATOM   15101 C  CB  . ILE   B 1 142  ? 81.09000   52.13300  -16.10900 1.000 38.41727  ?  142  ILE   B CB  1 
ATOM   15102 C  CG1 . ILE   B 1 142  ? 81.59800   53.54500  -15.80800 1.000 52.81244  ?  142  ILE   B CG1 1 
ATOM   15103 C  CG2 . ILE   B 1 142  ? 81.69800   51.14500  -15.12800 1.000 45.95408  ?  142  ILE   B CG2 1 
ATOM   15104 C  CD1 . ILE   B 1 142  ? 81.29900   54.02400  -14.40300 1.000 49.87857  ?  142  ILE   B CD1 1 
ATOM   15105 N  N   . ARG   B 1 143  ? 79.94000   49.98400  -18.40300 1.000 52.22910  ?  143  ARG   B N   1 
ATOM   15106 C  CA  . ARG   B 1 143  ? 79.54100   48.60500  -18.64500 1.000 40.47440  ?  143  ARG   B CA  1 
ATOM   15107 C  C   . ARG   B 1 143  ? 80.03900   48.05700  -19.97700 1.000 50.47904  ?  143  ARG   B C   1 
ATOM   15108 O  O   . ARG   B 1 143  ? 80.28000   46.84900  -20.08500 1.000 72.49895  ?  143  ARG   B O   1 
ATOM   15109 C  CB  . ARG   B 1 143  ? 78.01500   48.48200  -18.59000 1.000 49.50825  ?  143  ARG   B CB  1 
ATOM   15110 C  CG  . ARG   B 1 143  ? 77.51500   47.06400  -18.37400 1.000 67.44531  ?  143  ARG   B CG  1 
ATOM   15111 C  CD  . ARG   B 1 143  ? 75.99500   46.99900  -18.33300 1.000 57.98298  ?  143  ARG   B CD  1 
ATOM   15112 N  NE  . ARG   B 1 143  ? 75.40600   48.18500  -17.72200 1.000 55.74649  ?  143  ARG   B NE  1 
ATOM   15113 C  CZ  . ARG   B 1 143  ? 74.55100   48.99400  -18.33300 1.000 66.46141  ?  143  ARG   B CZ  1 
ATOM   15114 N  NH1 . ARG   B 1 143  ? 74.12800   48.75200  -19.56300 1.000 67.38898  ?  143  ARG   B NH1 1 
ATOM   15115 N  NH2 . ARG   B 1 143  ? 74.10100   50.06800  -17.68900 1.000 66.10364  ?  143  ARG   B NH2 1 
ATOM   15116 N  N   . GLU   B 1 144  ? 80.20500   48.90700  -20.99200 1.000 51.54600  ?  144  GLU   B N   1 
ATOM   15117 C  CA  . GLU   B 1 144  ? 80.47200   48.44000  -22.34800 1.000 61.16855  ?  144  GLU   B CA  1 
ATOM   15118 C  C   . GLU   B 1 144  ? 81.76000   48.99600  -22.94500 1.000 63.33791  ?  144  GLU   B C   1 
ATOM   15119 O  O   . GLU   B 1 144  ? 82.01900   48.77300  -24.13400 1.000 61.63064  ?  144  GLU   B O   1 
ATOM   15120 C  CB  . GLU   B 1 144  ? 79.29200   48.78800  -23.26400 1.000 63.58477  ?  144  GLU   B CB  1 
ATOM   15121 C  CG  . GLU   B 1 144  ? 77.92900   48.35400  -22.73700 1.000 70.93180  ?  144  GLU   B CG  1 
ATOM   15122 C  CD  . GLU   B 1 144  ? 77.61000   46.90300  -23.04200 1.000 84.25158  ?  144  GLU   B CD  1 
ATOM   15123 O  OE1 . GLU   B 1 144  ? 78.23700   46.33200  -23.96000 1.000 79.12836  ?  144  GLU   B OE1 1 
ATOM   15124 O  OE2 . GLU   B 1 144  ? 76.72800   46.33400  -22.36500 1.000 91.87437  -1 144  GLU   B OE2 1 
ATOM   15125 N  N   . TRP   B 1 145  ? 82.57800   49.70900  -22.16500 1.000 58.61473  ?  145  TRP   B N   1 
ATOM   15126 C  CA  . TRP   B 1 145  ? 83.78400   50.31000  -22.73000 1.000 57.60925  ?  145  TRP   B CA  1 
ATOM   15127 C  C   . TRP   B 1 145  ? 84.78400   49.24900  -23.17300 1.000 59.56372  ?  145  TRP   B C   1 
ATOM   15128 O  O   . TRP   B 1 145  ? 85.38800   49.36900  -24.24600 1.000 57.20752  ?  145  TRP   B O   1 
ATOM   15129 C  CB  . TRP   B 1 145  ? 84.42700   51.26100  -21.72200 1.000 58.16040  ?  145  TRP   B CB  1 
ATOM   15130 C  CG  . TRP   B 1 145  ? 85.80900   51.71300  -22.10700 1.000 58.80155  ?  145  TRP   B CG  1 
ATOM   15131 C  CD1 . TRP   B 1 145  ? 86.97600   51.40500  -21.47100 1.000 53.61526  ?  145  TRP   B CD1 1 
ATOM   15132 C  CD2 . TRP   B 1 145  ? 86.16600   52.54900  -23.21700 1.000 52.49511  ?  145  TRP   B CD2 1 
ATOM   15133 N  NE1 . TRP   B 1 145  ? 88.03600   51.99800  -22.11300 1.000 52.40908  ?  145  TRP   B NE1 1 
ATOM   15134 C  CE2 . TRP   B 1 145  ? 87.56600   52.70800  -23.18600 1.000 60.72993  ?  145  TRP   B CE2 1 
ATOM   15135 C  CE3 . TRP   B 1 145  ? 85.43900   53.17900  -24.23200 1.000 51.21309  ?  145  TRP   B CE3 1 
ATOM   15136 C  CZ2 . TRP   B 1 145  ? 88.25200   53.47300  -24.12800 1.000 65.44569  ?  145  TRP   B CZ2 1 
ATOM   15137 C  CZ3 . TRP   B 1 145  ? 86.12200   53.93700  -25.16700 1.000 51.61588  ?  145  TRP   B CZ3 1 
ATOM   15138 C  CH2 . TRP   B 1 145  ? 87.51400   54.07500  -25.11000 1.000 51.91744  ?  145  TRP   B CH2 1 
ATOM   15139 N  N   . GLU   B 1 146  ? 84.97700   48.20600  -22.36200 1.000 56.61338  ?  146  GLU   B N   1 
ATOM   15140 C  CA  . GLU   B 1 146  ? 85.90400   47.14400  -22.74200 1.000 64.64351  ?  146  GLU   B CA  1 
ATOM   15141 C  C   . GLU   B 1 146  ? 85.41700   46.40300  -23.98100 1.000 66.51744  ?  146  GLU   B C   1 
ATOM   15142 O  O   . GLU   B 1 146  ? 86.21500   46.07000  -24.86500 1.000 76.72108  ?  146  GLU   B O   1 
ATOM   15143 C  CB  . GLU   B 1 146  ? 86.10200   46.17200  -21.58000 1.000 78.35403  ?  146  GLU   B CB  1 
ATOM   15144 C  CG  . GLU   B 1 146  ? 86.90700   46.73700  -20.42100 1.000 76.43077  ?  146  GLU   B CG  1 
ATOM   15145 C  CD  . GLU   B 1 146  ? 87.32700   45.66500  -19.43400 1.000 84.76357  ?  146  GLU   B CD  1 
ATOM   15146 O  OE1 . GLU   B 1 146  ? 87.27900   44.47100  -19.79600 1.000 78.22765  ?  146  GLU   B OE1 1 
ATOM   15147 O  OE2 . GLU   B 1 146  ? 87.70300   46.01700  -18.29600 1.000 86.21105  -1 146  GLU   B OE2 1 
ATOM   15148 N  N   . ASN   B 1 147  ? 84.11200   46.13800  -24.06500 1.000 68.44800  ?  147  ASN   B N   1 
ATOM   15149 C  CA  . ASN   B 1 147  ? 83.55800   45.50000  -25.25400 1.000 67.93534  ?  147  ASN   B CA  1 
ATOM   15150 C  C   . ASN   B 1 147  ? 83.73200   46.36000  -26.49700 1.000 60.52663  ?  147  ASN   B C   1 
ATOM   15151 O  O   . ASN   B 1 147  ? 83.69600   45.83200  -27.61400 1.000 67.38825  ?  147  ASN   B O   1 
ATOM   15152 C  CB  . ASN   B 1 147  ? 82.07700   45.18500  -25.03800 1.000 66.35386  ?  147  ASN   B CB  1 
ATOM   15153 C  CG  . ASN   B 1 147  ? 81.84800   44.23500  -23.88000 1.000 82.35197  ?  147  ASN   B CG  1 
ATOM   15154 O  OD1 . ASN   B 1 147  ? 82.09500   44.57800  -22.72400 1.000 85.84595  ?  147  ASN   B OD1 1 
ATOM   15155 N  ND2 . ASN   B 1 147  ? 81.36500   43.03600  -24.18500 1.000 79.23885  ?  147  ASN   B ND2 1 
ATOM   15156 N  N   . ILE   B 1 148  ? 83.92700   47.66700  -26.32900 1.000 49.27121  ?  148  ILE   B N   1 
ATOM   15157 C  CA  . ILE   B 1 148  ? 84.11900   48.55100  -27.47300 1.000 56.79706  ?  148  ILE   B CA  1 
ATOM   15158 C  C   . ILE   B 1 148  ? 85.57600   48.54900  -27.92400 1.000 66.98099  ?  148  ILE   B C   1 
ATOM   15159 O  O   . ILE   B 1 148  ? 85.86300   48.46400  -29.12300 1.000 81.05317  ?  148  ILE   B O   1 
ATOM   15160 C  CB  . ILE   B 1 148  ? 83.62900   49.97000  -27.12600 1.000 57.46783  ?  148  ILE   B CB  1 
ATOM   15161 C  CG1 . ILE   B 1 148  ? 82.10000   50.00400  -27.06900 1.000 50.91855  ?  148  ILE   B CG1 1 
ATOM   15162 C  CG2 . ILE   B 1 148  ? 84.15500   50.98600  -28.13000 1.000 61.89677  ?  148  ILE   B CG2 1 
ATOM   15163 C  CD1 . ILE   B 1 148  ? 81.54000   51.31500  -26.57400 1.000 44.61533  ?  148  ILE   B CD1 1 
ATOM   15164 N  N   . VAL   B 1 149  ? 86.51700   48.63100  -26.98000 1.000 82.20235  ?  149  VAL   B N   1 
ATOM   15165 C  CA  . VAL   B 1 149  ? 87.92700   48.69300  -27.35500 1.000 88.18339  ?  149  VAL   B CA  1 
ATOM   15166 C  C   . VAL   B 1 149  ? 88.40000   47.36300  -27.92600 1.000 81.01612  ?  149  VAL   B C   1 
ATOM   15167 O  O   . VAL   B 1 149  ? 89.32800   47.32700  -28.74300 1.000 88.58600  ?  149  VAL   B O   1 
ATOM   15168 C  CB  . VAL   B 1 149  ? 88.78400   49.12600  -26.15100 1.000 69.18051  ?  149  VAL   B CB  1 
ATOM   15169 C  CG1 . VAL   B 1 149  ? 88.27700   50.43500  -25.60300 1.000 56.32801  ?  149  VAL   B CG1 1 
ATOM   15170 C  CG2 . VAL   B 1 149  ? 88.78100   48.05500  -25.06800 1.000 47.73475  ?  149  VAL   B CG2 1 
ATOM   15171 N  N   . HIS   B 1 150  ? 87.78300   46.25800  -27.52000 1.000 70.42636  ?  150  HIS   B N   1 
ATOM   15172 C  CA  . HIS   B 1 150  ? 88.13700   44.94200  -28.02800 1.000 81.29705  ?  150  HIS   B CA  1 
ATOM   15173 C  C   . HIS   B 1 150  ? 87.41700   44.60100  -29.32500 1.000 87.59026  ?  150  HIS   B C   1 
ATOM   15174 O  O   . HIS   B 1 150  ? 87.59500   43.49400  -29.84400 1.000 106.03416 ?  150  HIS   B O   1 
ATOM   15175 C  CB  . HIS   B 1 150  ? 87.84000   43.87500  -26.96800 1.000 86.51661  ?  150  HIS   B CB  1 
ATOM   15176 C  CG  . HIS   B 1 150  ? 88.63200   44.04000  -25.70800 1.000 86.03822  ?  150  HIS   B CG  1 
ATOM   15177 N  ND1 . HIS   B 1 150  ? 88.11700   43.75500  -24.46200 1.000 83.84132  ?  150  HIS   B ND1 1 
ATOM   15178 C  CD2 . HIS   B 1 150  ? 89.90400   44.45800  -25.50200 1.000 77.62469  ?  150  HIS   B CD2 1 
ATOM   15179 C  CE1 . HIS   B 1 150  ? 89.03600   43.99300  -23.54300 1.000 81.36482  ?  150  HIS   B CE1 1 
ATOM   15180 N  NE2 . HIS   B 1 150  ? 90.12900   44.42000  -24.14800 1.000 81.64634  ?  150  HIS   B NE2 1 
ATOM   15181 N  N   . GLY   B 1 151  ? 86.61600   45.52100  -29.85900 1.000 84.92846  ?  151  GLY   B N   1 
ATOM   15182 C  CA  . GLY   B 1 151  ? 85.89700   45.26800  -31.09000 1.000 88.39042  ?  151  GLY   B CA  1 
ATOM   15183 C  C   . GLY   B 1 151  ? 84.77400   44.26500  -30.97500 1.000 86.15474  ?  151  GLY   B C   1 
ATOM   15184 O  O   . GLY   B 1 151  ? 84.36600   43.68900  -31.98700 1.000 99.49897  ?  151  GLY   B O   1 
ATOM   15185 N  N   . ARG   B 1 152  ? 84.25500   44.04000  -29.76600 1.000 83.79746  ?  152  ARG   B N   1 
ATOM   15186 C  CA  . ARG   B 1 152  ? 83.20100   43.04900  -29.58300 1.000 86.55933  ?  152  ARG   B CA  1 
ATOM   15187 C  C   . ARG   B 1 152  ? 81.82500   43.59900  -29.94000 1.000 85.83852  ?  152  ARG   B C   1 
ATOM   15188 O  O   . ARG   B 1 152  ? 80.92600   42.82400  -30.28700 1.000 89.01862  ?  152  ARG   B O   1 
ATOM   15189 C  CB  . ARG   B 1 152  ? 83.20700   42.53600  -28.14100 1.000 78.29736  ?  152  ARG   B CB  1 
ATOM   15190 C  CG  . ARG   B 1 152  ? 84.53700   41.93700  -27.71000 1.000 83.81068  ?  152  ARG   B CG  1 
ATOM   15191 C  CD  . ARG   B 1 152  ? 84.35600   40.89000  -26.62200 1.000 82.43952  ?  152  ARG   B CD  1 
ATOM   15192 N  NE  . ARG   B 1 152  ? 84.68000   41.39400  -25.29300 1.000 82.82736  ?  152  ARG   B NE  1 
ATOM   15193 C  CZ  . ARG   B 1 152  ? 85.89900   41.39600  -24.77100 1.000 89.43993  ?  152  ARG   B CZ  1 
ATOM   15194 N  NH1 . ARG   B 1 152  ? 86.94600   40.96700  -25.45800 1.000 91.09907  ?  152  ARG   B NH1 1 
ATOM   15195 N  NH2 . ARG   B 1 152  ? 86.07300   41.83800  -23.52900 1.000 80.95537  ?  152  ARG   B NH2 1 
ATOM   15196 N  N   . ILE   B 1 153  ? 81.64300   44.91300  -29.86600 1.000 81.30129  ?  153  ILE   B N   1 
ATOM   15197 C  CA  . ILE   B 1 153  ? 80.36500   45.54600  -30.17300 1.000 80.10824  ?  153  ILE   B CA  1 
ATOM   15198 C  C   . ILE   B 1 153  ? 80.30800   45.84500  -31.66600 1.000 75.50528  ?  153  ILE   B C   1 
ATOM   15199 O  O   . ILE   B 1 153  ? 81.23600   46.44100  -32.22700 1.000 67.80211  ?  153  ILE   B O   1 
ATOM   15200 C  CB  . ILE   B 1 153  ? 80.17100   46.82400  -29.33900 1.000 73.67758  ?  153  ILE   B CB  1 
ATOM   15201 C  CG1 . ILE   B 1 153  ? 79.67700   46.47800  -27.93100 1.000 56.76060  ?  153  ILE   B CG1 1 
ATOM   15202 C  CG2 . ILE   B 1 153  ? 79.20700   47.78000  -30.02100 1.000 52.22800  ?  153  ILE   B CG2 1 
ATOM   15203 C  CD1 . ILE   B 1 153  ? 78.31300   45.81800  -27.90700 1.000 77.76410  ?  153  ILE   B CD1 1 
ATOM   15204 N  N   . ALA   B 1 154  ? 79.21800   45.42400  -32.31200 1.000 73.95676  ?  154  ALA   B N   1 
ATOM   15205 C  CA  . ALA   B 1 154  ? 79.02600   45.65700  -33.73500 1.000 73.36672  ?  154  ALA   B CA  1 
ATOM   15206 C  C   . ALA   B 1 154  ? 78.19200   46.91000  -33.93700 1.000 76.39750  ?  154  ALA   B C   1 
ATOM   15207 O  O   . ALA   B 1 154  ? 77.05900   46.97400  -33.43400 1.000 79.15592  ?  154  ALA   B O   1 
ATOM   15208 C  CB  . ALA   B 1 154  ? 78.34300   44.46000  -34.38700 1.000 81.27231  ?  154  ALA   B CB  1 
ATOM   15209 N  N   . PRO   B 1 155  ? 78.69200   47.91700  -34.64900 1.000 64.64956  ?  155  PRO   B N   1 
ATOM   15210 C  CA  . PRO   B 1 155  ? 77.91300   49.14700  -34.83300 1.000 72.89052  ?  155  PRO   B CA  1 
ATOM   15211 C  C   . PRO   B 1 155  ? 76.69900   48.92000  -35.72100 1.000 83.66523  ?  155  PRO   B C   1 
ATOM   15212 O  O   . PRO   B 1 155  ? 76.72100   48.11200  -36.65300 1.000 86.58298  ?  155  PRO   B O   1 
ATOM   15213 C  CB  . PRO   B 1 155  ? 78.91000   50.10600  -35.49900 1.000 63.97769  ?  155  PRO   B CB  1 
ATOM   15214 C  CG  . PRO   B 1 155  ? 80.26600   49.49500  -35.27300 1.000 63.84768  ?  155  PRO   B CG  1 
ATOM   15215 C  CD  . PRO   B 1 155  ? 80.03800   48.01900  -35.23500 1.000 47.81570  ?  155  PRO   B CD  1 
ATOM   15216 N  N   . TYR   B 1 156  ? 75.62100   49.64500  -35.41500 1.000 79.31130  ?  156  TYR   B N   1 
ATOM   15217 C  CA  . TYR   B 1 156  ? 74.44600   49.68300  -36.27400 1.000 66.39636  ?  156  TYR   B CA  1 
ATOM   15218 C  C   . TYR   B 1 156  ? 74.04400   51.13000  -36.52600 1.000 77.17647  ?  156  TYR   B C   1 
ATOM   15219 O  O   . TYR   B 1 156  ? 74.30700   52.02000  -35.71100 1.000 84.76745  ?  156  TYR   B O   1 
ATOM   15220 C  CB  . TYR   B 1 156  ? 73.25600   48.87700  -35.69500 1.000 68.87349  ?  156  TYR   B CB  1 
ATOM   15221 C  CG  . TYR   B 1 156  ? 72.77200   49.26300  -34.30800 1.000 84.56292  ?  156  TYR   B CG  1 
ATOM   15222 C  CD1 . TYR   B 1 156  ? 72.10700   50.46600  -34.08700 1.000 85.35459  ?  156  TYR   B CD1 1 
ATOM   15223 C  CD2 . TYR   B 1 156  ? 72.94900   48.40400  -33.22500 1.000 90.51394  ?  156  TYR   B CD2 1 
ATOM   15224 C  CE1 . TYR   B 1 156  ? 71.65600   50.81400  -32.83000 1.000 73.65752  ?  156  TYR   B CE1 1 
ATOM   15225 C  CE2 . TYR   B 1 156  ? 72.49600   48.74400  -31.95900 1.000 73.13806  ?  156  TYR   B CE2 1 
ATOM   15226 C  CZ  . TYR   B 1 156  ? 71.85100   49.95200  -31.77200 1.000 68.91100  ?  156  TYR   B CZ  1 
ATOM   15227 O  OH  . TYR   B 1 156  ? 71.39300   50.31300  -30.52500 1.000 89.27992  ?  156  TYR   B OH  1 
ATOM   15228 N  N   . ARG   B 1 157  ? 73.40900   51.35500  -37.67200 1.000 86.95241  ?  157  ARG   B N   1 
ATOM   15229 C  CA  . ARG   B 1 157  ? 73.01900   52.69100  -38.09000 1.000 74.70197  ?  157  ARG   B CA  1 
ATOM   15230 C  C   . ARG   B 1 157  ? 71.72900   53.11900  -37.39900 1.000 81.98489  ?  157  ARG   B C   1 
ATOM   15231 O  O   . ARG   B 1 157  ? 70.90000   52.28900  -37.01400 1.000 83.55515  ?  157  ARG   B O   1 
ATOM   15232 C  CB  . ARG   B 1 157  ? 72.83800   52.73000  -39.60700 1.000 80.06438  ?  157  ARG   B CB  1 
ATOM   15233 C  CG  . ARG   B 1 157  ? 72.88500   54.11100  -40.23400 1.000 81.45829  ?  157  ARG   B CG  1 
ATOM   15234 C  CD  . ARG   B 1 157  ? 72.36100   54.03400  -41.65400 1.000 83.57089  ?  157  ARG   B CD  1 
ATOM   15235 N  NE  . ARG   B 1 157  ? 72.74200   52.77600  -42.28700 1.000 111.55805 ?  157  ARG   B NE  1 
ATOM   15236 C  CZ  . ARG   B 1 157  ? 72.04900   52.17900  -43.24600 1.000 119.04976 ?  157  ARG   B CZ  1 
ATOM   15237 N  NH1 . ARG   B 1 157  ? 70.92700   52.70100  -43.71400 1.000 96.80353  ?  157  ARG   B NH1 1 
ATOM   15238 N  NH2 . ARG   B 1 157  ? 72.48700   51.02500  -43.74200 1.000 99.07903  ?  157  ARG   B NH2 1 
ATOM   15239 N  N   . GLN   B 1 158  ? 71.56500   54.43100  -37.24500 1.000 84.27005  ?  158  GLN   B N   1 
ATOM   15240 C  CA  . GLN   B 1 158  ? 70.35600   54.97300  -36.64200 1.000 71.40811  ?  158  GLN   B CA  1 
ATOM   15241 C  C   . GLN   B 1 158  ? 69.14700   54.72900  -37.54300 1.000 76.71671  ?  158  GLN   B C   1 
ATOM   15242 O  O   . GLN   B 1 158  ? 69.27400   54.45100  -38.73900 1.000 94.31326  ?  158  GLN   B O   1 
ATOM   15243 C  CB  . GLN   B 1 158  ? 70.50800   56.47300  -36.38200 1.000 62.32596  ?  158  GLN   B CB  1 
ATOM   15244 C  CG  . GLN   B 1 158  ? 71.63700   56.84500  -35.43700 1.000 67.01462  ?  158  GLN   B CG  1 
ATOM   15245 C  CD  . GLN   B 1 158  ? 71.70300   58.33800  -35.17500 1.000 75.53620  ?  158  GLN   B CD  1 
ATOM   15246 O  OE1 . GLN   B 1 158  ? 70.76300   59.07500  -35.47600 1.000 70.57486  ?  158  GLN   B OE1 1 
ATOM   15247 N  NE2 . GLN   B 1 158  ? 72.81800   58.79300  -34.61400 1.000 67.22074  ?  158  GLN   B NE2 1 
ATOM   15248 N  N   . THR   B 1 159  ? 67.95900   54.83900  -36.95200 1.000 86.17370  ?  159  THR   B N   1 
ATOM   15249 C  CA  . THR   B 1 159  ? 66.72100   54.70600  -37.70500 1.000 71.72898  ?  159  THR   B CA  1 
ATOM   15250 C  C   . THR   B 1 159  ? 66.39700   56.01900  -38.42200 1.000 76.02860  ?  159  THR   B C   1 
ATOM   15251 O  O   . THR   B 1 159  ? 67.15100   56.99500  -38.36300 1.000 88.31691  ?  159  THR   B O   1 
ATOM   15252 C  CB  . THR   B 1 159  ? 65.58000   54.27200  -36.78800 1.000 59.24206  ?  159  THR   B CB  1 
ATOM   15253 O  OG1 . THR   B 1 159  ? 65.67100   54.97400  -35.54300 1.000 82.93784  ?  159  THR   B OG1 1 
ATOM   15254 C  CG2 . THR   B 1 159  ? 65.64500   52.77000  -36.52900 1.000 43.61865  ?  159  THR   B CG2 1 
ATOM   15255 N  N   . ALA   B 1 160  ? 65.25300   56.04700  -39.10800 1.000 76.19964  ?  160  ALA   B N   1 
ATOM   15256 C  CA  . ALA   B 1 160  ? 64.97000   57.12700  -40.04600 1.000 94.48742  ?  160  ALA   B CA  1 
ATOM   15257 C  C   . ALA   B 1 160  ? 64.38200   58.36000  -39.37000 1.000 88.61727  ?  160  ALA   B C   1 
ATOM   15258 O  O   . ALA   B 1 160  ? 64.54400   59.47500  -39.88100 1.000 88.34903  ?  160  ALA   B O   1 
ATOM   15259 C  CB  . ALA   B 1 160  ? 64.02300   56.63400  -41.14300 1.000 105.11179 ?  160  ALA   B CB  1 
ATOM   15260 N  N   . GLY   B 1 161  ? 63.70400   58.18300  -38.23800 1.000 66.56336  ?  161  GLY   B N   1 
ATOM   15261 C  CA  . GLY   B 1 161  ? 63.06600   59.28800  -37.55200 1.000 82.62062  ?  161  GLY   B CA  1 
ATOM   15262 C  C   . GLY   B 1 161  ? 64.03500   60.19100  -36.82600 1.000 77.24569  ?  161  GLY   B C   1 
ATOM   15263 O  O   . GLY   B 1 161  ? 65.22000   60.27900  -37.17300 1.000 89.81689  ?  161  GLY   B O   1 
ATOM   15264 N  N   . GLY   B 1 162  ? 63.53000   60.89000  -35.82600 1.000 72.52414  ?  162  GLY   B N   1 
ATOM   15265 C  CA  . GLY   B 1 162  ? 64.38600   61.64100  -34.93300 1.000 67.74258  ?  162  GLY   B CA  1 
ATOM   15266 C  C   . GLY   B 1 162  ? 64.22500   63.14500  -35.09500 1.000 70.24855  ?  162  GLY   B C   1 
ATOM   15267 O  O   . GLY   B 1 162  ? 63.81900   63.65000  -36.15100 1.000 80.16950  ?  162  GLY   B O   1 
ATOM   15268 N  N   . THR   B 1 163  ? 64.55200   63.87100  -34.02600 1.000 67.30479  ?  163  THR   B N   1 
ATOM   15269 C  CA  . THR   B 1 163  ? 64.52700   65.32300  -33.99700 1.000 56.12780  ?  163  THR   B CA  1 
ATOM   15270 C  C   . THR   B 1 163  ? 65.91500   65.85200  -33.65900 1.000 62.65944  ?  163  THR   B C   1 
ATOM   15271 O  O   . THR   B 1 163  ? 66.72900   65.16700  -33.03200 1.000 71.13576  ?  163  THR   B O   1 
ATOM   15272 C  CB  . THR   B 1 163  ? 63.50800   65.85200  -32.97300 1.000 59.52976  ?  163  THR   B CB  1 
ATOM   15273 O  OG1 . THR   B 1 163  ? 64.08500   65.82000  -31.66100 1.000 69.44650  ?  163  THR   B OG1 1 
ATOM   15274 C  CG2 . THR   B 1 163  ? 62.24500   65.00100  -32.98200 1.000 62.03153  ?  163  THR   B CG2 1 
ATOM   15275 N  N   . LEU   B 1 164  ? 66.17500   67.08800  -34.07900 1.000 56.03244  ?  164  LEU   B N   1 
ATOM   15276 C  CA  . LEU   B 1 164  ? 67.44400   67.76100  -33.83800 1.000 39.06055  ?  164  LEU   B CA  1 
ATOM   15277 C  C   . LEU   B 1 164  ? 67.17000   69.14400  -33.27100 1.000 53.89631  ?  164  LEU   B C   1 
ATOM   15278 O  O   . LEU   B 1 164  ? 66.31300   69.86900  -33.78600 1.000 74.42152  ?  164  LEU   B O   1 
ATOM   15279 C  CB  . LEU   B 1 164  ? 68.26400   67.87200  -35.12500 1.000 45.09139  ?  164  LEU   B CB  1 
ATOM   15280 C  CG  . LEU   B 1 164  ? 69.43000   68.86300  -35.10600 1.000 56.74302  ?  164  LEU   B CG  1 
ATOM   15281 C  CD1 . LEU   B 1 164  ? 70.70100   68.21800  -34.57300 1.000 74.15263  ?  164  LEU   B CD1 1 
ATOM   15282 C  CD2 . LEU   B 1 164  ? 69.65200   69.43700  -36.48700 1.000 53.15549  ?  164  LEU   B CD2 1 
ATOM   15283 N  N   . HIS   B 1 165  ? 67.90000   69.51100  -32.22000 1.000 56.13131  ?  165  HIS   B N   1 
ATOM   15284 C  CA  . HIS   B 1 165  ? 67.70800   70.79000  -31.55400 1.000 54.00587  ?  165  HIS   B CA  1 
ATOM   15285 C  C   . HIS   B 1 165  ? 69.04100   71.51000  -31.39800 1.000 48.49358  ?  165  HIS   B C   1 
ATOM   15286 O  O   . HIS   B 1 165  ? 70.11500   70.90700  -31.45700 1.000 55.32163  ?  165  HIS   B O   1 
ATOM   15287 C  CB  . HIS   B 1 165  ? 67.03900   70.61600  -30.18500 1.000 59.63591  ?  165  HIS   B CB  1 
ATOM   15288 C  CG  . HIS   B 1 165  ? 65.60700   70.19000  -30.26800 1.000 55.19031  ?  165  HIS   B CG  1 
ATOM   15289 N  ND1 . HIS   B 1 165  ? 64.58300   71.07400  -30.53200 1.000 52.18513  ?  165  HIS   B ND1 1 
ATOM   15290 C  CD2 . HIS   B 1 165  ? 65.02800   68.97400  -30.12900 1.000 52.87288  ?  165  HIS   B CD2 1 
ATOM   15291 C  CE1 . HIS   B 1 165  ? 63.43500   70.42200  -30.54900 1.000 64.00877  ?  165  HIS   B CE1 1 
ATOM   15292 N  NE2 . HIS   B 1 165  ? 63.67600   69.14600  -30.30700 1.000 66.28224  ?  165  HIS   B NE2 1 
ATOM   15293 N  N   . PHE   B 1 166  ? 68.94800   72.82000  -31.19300 1.000 53.78545  ?  166  PHE   B N   1 
ATOM   15294 C  CA  . PHE   B 1 166  ? 70.09300   73.71000  -31.10300 1.000 48.94964  ?  166  PHE   B CA  1 
ATOM   15295 C  C   . PHE   B 1 166  ? 70.05800   74.45600  -29.77800 1.000 52.36598  ?  166  PHE   B C   1 
ATOM   15296 O  O   . PHE   B 1 166  ? 69.07400   74.41300  -29.03500 1.000 56.04508  ?  166  PHE   B O   1 
ATOM   15297 C  CB  . PHE   B 1 166  ? 70.10600   74.71900  -32.26100 1.000 46.76349  ?  166  PHE   B CB  1 
ATOM   15298 C  CG  . PHE   B 1 166  ? 70.27700   74.09700  -33.61900 1.000 80.17054  ?  166  PHE   B CG  1 
ATOM   15299 C  CD1 . PHE   B 1 166  ? 69.26600   73.33500  -34.18300 1.000 86.29997  ?  166  PHE   B CD1 1 
ATOM   15300 C  CD2 . PHE   B 1 166  ? 71.44200   74.29200  -34.34100 1.000 70.04882  ?  166  PHE   B CD2 1 
ATOM   15301 C  CE1 . PHE   B 1 166  ? 69.42100   72.76500  -35.43000 1.000 72.57791  ?  166  PHE   B CE1 1 
ATOM   15302 C  CE2 . PHE   B 1 166  ? 71.60200   73.72800  -35.59000 1.000 83.51148  ?  166  PHE   B CE2 1 
ATOM   15303 C  CZ  . PHE   B 1 166  ? 70.58900   72.96400  -36.13600 1.000 84.38513  ?  166  PHE   B CZ  1 
ATOM   15304 N  N   . LYS   B 1 167  ? 71.15400   75.14800  -29.48400 1.000 42.90371  ?  167  LYS   B N   1 
ATOM   15305 C  CA  . LYS   B 1 167  ? 71.13900   76.08600  -28.37600 1.000 56.18891  ?  167  LYS   B CA  1 
ATOM   15306 C  C   . LYS   B 1 167  ? 70.21100   77.25300  -28.70700 1.000 68.62672  ?  167  LYS   B C   1 
ATOM   15307 O  O   . LYS   B 1 167  ? 69.90000   77.52100  -29.87100 1.000 86.76000  ?  167  LYS   B O   1 
ATOM   15308 C  CB  . LYS   B 1 167  ? 72.55000   76.58500  -28.07100 1.000 49.27148  ?  167  LYS   B CB  1 
ATOM   15309 C  CG  . LYS   B 1 167  ? 73.28100   77.16000  -29.26900 1.000 67.75688  ?  167  LYS   B CG  1 
ATOM   15310 C  CD  . LYS   B 1 167  ? 74.67400   77.62600  -28.88600 1.000 66.91519  ?  167  LYS   B CD  1 
ATOM   15311 C  CE  . LYS   B 1 167  ? 74.61700   78.64900  -27.76300 1.000 64.87647  ?  167  LYS   B CE  1 
ATOM   15312 N  NZ  . LYS   B 1 167  ? 75.96800   79.14600  -27.39000 1.000 75.13412  ?  167  LYS   B NZ  1 
ATOM   15313 N  N   . ALA   B 1 168  ? 69.75300   77.93400  -27.65900 1.000 61.80852  ?  168  ALA   B N   1 
ATOM   15314 C  CA  . ALA   B 1 168  ? 68.78900   79.02900  -27.73600 1.000 57.72163  ?  168  ALA   B CA  1 
ATOM   15315 C  C   . ALA   B 1 168  ? 67.42300   78.58500  -28.25100 1.000 52.43471  ?  168  ALA   B C   1 
ATOM   15316 O  O   . ALA   B 1 168  ? 66.59800   79.43100  -28.61300 1.000 82.52883  ?  168  ALA   B O   1 
ATOM   15317 C  CB  . ALA   B 1 168  ? 69.31400   80.19300  -28.58800 1.000 46.38166  ?  168  ALA   B CB  1 
ATOM   15318 N  N   . ASP   B 1 169  ? 67.16300   77.27800  -28.30500 1.000 42.36993  ?  169  ASP   B N   1 
ATOM   15319 C  CA  . ASP   B 1 169  ? 65.81600   76.77000  -28.52400 1.000 45.45305  ?  169  ASP   B CA  1 
ATOM   15320 C  C   . ASP   B 1 169  ? 65.02200   76.65900  -27.23200 1.000 51.25816  ?  169  ASP   B C   1 
ATOM   15321 O  O   . ASP   B 1 169  ? 63.82300   76.36800  -27.27700 1.000 54.27437  ?  169  ASP   B O   1 
ATOM   15322 C  CB  . ASP   B 1 169  ? 65.86100   75.39800  -29.20400 1.000 54.38145  ?  169  ASP   B CB  1 
ATOM   15323 C  CG  . ASP   B 1 169  ? 66.23900   75.48400  -30.66700 1.000 51.92490  ?  169  ASP   B CG  1 
ATOM   15324 O  OD1 . ASP   B 1 169  ? 66.42500   76.61200  -31.17000 1.000 37.32194  ?  169  ASP   B OD1 1 
ATOM   15325 O  OD2 . ASP   B 1 169  ? 66.34700   74.41900  -31.31400 1.000 45.68397  -1 169  ASP   B OD2 1 
ATOM   15326 N  N   . ARG   B 1 170  ? 65.66400   76.88900  -26.09200 1.000 56.99806  ?  170  ARG   B N   1 
ATOM   15327 C  CA  . ARG   B 1 170  ? 65.04200   76.75400  -24.78600 1.000 52.37961  ?  170  ARG   B CA  1 
ATOM   15328 C  C   . ARG   B 1 170  ? 64.88800   78.08900  -24.07100 1.000 47.88832  ?  170  ARG   B C   1 
ATOM   15329 O  O   . ARG   B 1 170  ? 64.33000   78.12500  -22.96900 1.000 62.00200  ?  170  ARG   B O   1 
ATOM   15330 C  CB  . ARG   B 1 170  ? 65.87100   75.78800  -23.93500 1.000 49.34206  ?  170  ARG   B CB  1 
ATOM   15331 C  CG  . ARG   B 1 170  ? 65.20700   75.28400  -22.68400 1.000 62.59795  ?  170  ARG   B CG  1 
ATOM   15332 C  CD  . ARG   B 1 170  ? 66.25700   74.79700  -21.72000 1.000 68.25505  ?  170  ARG   B CD  1 
ATOM   15333 N  NE  . ARG   B 1 170  ? 65.64800   73.98800  -20.67700 1.000 50.65891  ?  170  ARG   B NE  1 
ATOM   15334 C  CZ  . ARG   B 1 170  ? 66.29600   73.11800  -19.91800 1.000 65.80121  ?  170  ARG   B CZ  1 
ATOM   15335 N  NH1 . ARG   B 1 170  ? 67.57900   72.85200  -20.10900 1.000 57.53191  ?  170  ARG   B NH1 1 
ATOM   15336 N  NH2 . ARG   B 1 170  ? 65.64200   72.50500  -18.93800 1.000 66.72729  ?  170  ARG   B NH2 1 
ATOM   15337 N  N   . ASP   B 1 171  ? 65.36000   79.18800  -24.67300 1.000 41.44168  ?  171  ASP   B N   1 
ATOM   15338 C  CA  . ASP   B 1 171  ? 65.25300   80.50000  -24.04000 1.000 38.64782  ?  171  ASP   B CA  1 
ATOM   15339 C  C   . ASP   B 1 171  ? 63.83900   80.78400  -23.55400 1.000 45.56078  ?  171  ASP   B C   1 
ATOM   15340 O  O   . ASP   B 1 171  ? 63.65100   81.51600  -22.57600 1.000 61.49853  ?  171  ASP   B O   1 
ATOM   15341 C  CB  . ASP   B 1 171  ? 65.70000   81.59200  -25.01500 1.000 61.21929  ?  171  ASP   B CB  1 
ATOM   15342 C  CG  . ASP   B 1 171  ? 67.13100   81.41000  -25.47900 1.000 68.21622  ?  171  ASP   B CG  1 
ATOM   15343 O  OD1 . ASP   B 1 171  ? 67.84500   80.56700  -24.89600 1.000 46.72991  ?  171  ASP   B OD1 1 
ATOM   15344 O  OD2 . ASP   B 1 171  ? 67.53900   82.10600  -26.43300 1.000 76.17591  -1 171  ASP   B OD2 1 
ATOM   15345 N  N   . PHE   B 1 172  ? 62.83700   80.19900  -24.21000 1.000 49.45335  ?  172  PHE   B N   1 
ATOM   15346 C  CA  . PHE   B 1 172  ? 61.45200   80.38800  -23.79700 1.000 49.03994  ?  172  PHE   B CA  1 
ATOM   15347 C  C   . PHE   B 1 172  ? 61.10100   79.52300  -22.59100 1.000 48.63568  ?  172  PHE   B C   1 
ATOM   15348 O  O   . PHE   B 1 172  ? 60.36500   79.96500  -21.70100 1.000 52.91270  ?  172  PHE   B O   1 
ATOM   15349 C  CB  . PHE   B 1 172  ? 60.52200   80.08000  -24.97100 1.000 47.60647  ?  172  PHE   B CB  1 
ATOM   15350 C  CG  . PHE   B 1 172  ? 59.10100   80.50500  -24.75000 1.000 53.17692  ?  172  PHE   B CG  1 
ATOM   15351 C  CD1 . PHE   B 1 172  ? 58.80900   81.77500  -24.28100 1.000 48.45769  ?  172  PHE   B CD1 1 
ATOM   15352 C  CD2 . PHE   B 1 172  ? 58.05400   79.64300  -25.03400 1.000 45.27560  ?  172  PHE   B CD2 1 
ATOM   15353 C  CE1 . PHE   B 1 172  ? 57.50200   82.17200  -24.08500 1.000 52.49081  ?  172  PHE   B CE1 1 
ATOM   15354 C  CE2 . PHE   B 1 172  ? 56.74300   80.03500  -24.84000 1.000 42.87465  ?  172  PHE   B CE2 1 
ATOM   15355 C  CZ  . PHE   B 1 172  ? 56.46600   81.30200  -24.36500 1.000 60.08834  ?  172  PHE   B CZ  1 
ATOM   15356 N  N   . TYR   B 1 173  ? 61.62200   78.29700  -22.53900 1.000 36.69980  ?  173  TYR   B N   1 
ATOM   15357 C  CA  . TYR   B 1 173  ? 61.30400   77.33800  -21.48100 1.000 42.00767  ?  173  TYR   B CA  1 
ATOM   15358 C  C   . TYR   B 1 173  ? 62.34900   77.34000  -20.37400 1.000 47.17444  ?  173  TYR   B C   1 
ATOM   15359 O  O   . TYR   B 1 173  ? 62.67400   76.29000  -19.81300 1.000 43.21762  ?  173  TYR   B O   1 
ATOM   15360 C  CB  . TYR   B 1 173  ? 61.15200   75.94100  -22.07400 1.000 42.17216  ?  173  TYR   B CB  1 
ATOM   15361 C  CG  . TYR   B 1 173  ? 60.43300   75.91600  -23.40400 1.000 45.98526  ?  173  TYR   B CG  1 
ATOM   15362 C  CD1 . TYR   B 1 173  ? 59.04600   75.97800  -23.46900 1.000 53.72491  ?  173  TYR   B CD1 1 
ATOM   15363 C  CD2 . TYR   B 1 173  ? 61.14100   75.83000  -24.59600 1.000 55.02601  ?  173  TYR   B CD2 1 
ATOM   15364 C  CE1 . TYR   B 1 173  ? 58.38600   75.95900  -24.68500 1.000 59.46930  ?  173  TYR   B CE1 1 
ATOM   15365 C  CE2 . TYR   B 1 173  ? 60.48800   75.81000  -25.81600 1.000 62.90607  ?  173  TYR   B CE2 1 
ATOM   15366 C  CZ  . TYR   B 1 173  ? 59.11200   75.87400  -25.85400 1.000 65.26699  ?  173  TYR   B CZ  1 
ATOM   15367 O  OH  . TYR   B 1 173  ? 58.45900   75.85400  -27.06600 1.000 84.69555  ?  173  TYR   B OH  1 
ATOM   15368 N  N   . LYS   B 1 174  ? 62.89300   78.51000  -20.03600 1.000 49.27021  ?  174  LYS   B N   1 
ATOM   15369 C  CA  . LYS   B 1 174  ? 63.95400   78.58000  -19.04100 1.000 33.12681  ?  174  LYS   B CA  1 
ATOM   15370 C  C   . LYS   B 1 174  ? 63.43200   78.54200  -17.61200 1.000 38.27705  ?  174  LYS   B C   1 
ATOM   15371 O  O   . LYS   B 1 174  ? 64.18900   78.18700  -16.70200 1.000 64.71199  ?  174  LYS   B O   1 
ATOM   15372 C  CB  . LYS   B 1 174  ? 64.79100   79.84600  -19.24300 1.000 33.17856  ?  174  LYS   B CB  1 
ATOM   15373 C  CG  . LYS   B 1 174  ? 64.10400   81.13800  -18.81900 1.000 45.04588  ?  174  LYS   B CG  1 
ATOM   15374 C  CD  . LYS   B 1 174  ? 65.01000   82.34100  -19.05300 1.000 60.19142  ?  174  LYS   B CD  1 
ATOM   15375 C  CE  . LYS   B 1 174  ? 64.28800   83.66000  -18.79600 1.000 74.89438  ?  174  LYS   B CE  1 
ATOM   15376 N  NZ  . LYS   B 1 174  ? 64.06400   83.93400  -17.34700 1.000 58.47798  ?  174  LYS   B NZ  1 
ATOM   15377 N  N   . ASN   B 1 175  ? 62.16900   78.89500  -17.39000 1.000 37.67697  ?  175  ASN   B N   1 
ATOM   15378 C  CA  . ASN   B 1 175  ? 61.59700   78.92100  -16.05100 1.000 38.45485  ?  175  ASN   B CA  1 
ATOM   15379 C  C   . ASN   B 1 175  ? 60.95200   77.59800  -15.65800 1.000 39.82961  ?  175  ASN   B C   1 
ATOM   15380 O  O   . ASN   B 1 175  ? 60.24600   77.54300  -14.64600 1.000 51.82978  ?  175  ASN   B O   1 
ATOM   15381 C  CB  . ASN   B 1 175  ? 60.57300   80.05300  -15.94000 1.000 35.29584  ?  175  ASN   B CB  1 
ATOM   15382 C  CG  . ASN   B 1 175  ? 61.20000   81.42200  -16.11700 1.000 47.49297  ?  175  ASN   B CG  1 
ATOM   15383 O  OD1 . ASN   B 1 175  ? 62.34500   81.64600  -15.72600 1.000 62.20122  ?  175  ASN   B OD1 1 
ATOM   15384 N  ND2 . ASN   B 1 175  ? 60.45200   82.34500  -16.70900 1.000 58.40458  ?  175  ASN   B ND2 1 
ATOM   15385 N  N   . LEU   B 1 176  ? 61.18800   76.53300  -16.42200 1.000 31.03971  ?  176  LEU   B N   1 
ATOM   15386 C  CA  . LEU   B 1 176  ? 60.54100   75.24600  -16.20200 1.000 47.32330  ?  176  LEU   B CA  1 
ATOM   15387 C  C   . LEU   B 1 176  ? 61.53400   74.17400  -15.76000 1.000 49.50538  ?  176  LEU   B C   1 
ATOM   15388 O  O   . LEU   B 1 176  ? 61.29800   72.98100  -15.96200 1.000 50.90088  ?  176  LEU   B O   1 
ATOM   15389 C  CB  . LEU   B 1 176  ? 59.81100   74.80300  -17.46900 1.000 49.90881  ?  176  LEU   B CB  1 
ATOM   15390 C  CG  . LEU   B 1 176  ? 58.99500   75.87700  -18.19200 1.000 42.38802  ?  176  LEU   B CG  1 
ATOM   15391 C  CD1 . LEU   B 1 176  ? 58.50100   75.35800  -19.53100 1.000 26.69527  ?  176  LEU   B CD1 1 
ATOM   15392 C  CD2 . LEU   B 1 176  ? 57.83200   76.34300  -17.33400 1.000 37.42357  ?  176  LEU   B CD2 1 
ATOM   15393 N  N   . ASN   B 1 177  ? 62.64900   74.58700  -15.15300 1.000 55.76132  ?  177  ASN   B N   1 
ATOM   15394 C  CA  . ASN   B 1 177  ? 63.68200   73.62700  -14.77800 1.000 53.07243  ?  177  ASN   B CA  1 
ATOM   15395 C  C   . ASN   B 1 177  ? 63.22500   72.73000  -13.63500 1.000 47.64504  ?  177  ASN   B C   1 
ATOM   15396 O  O   . ASN   B 1 177  ? 63.53800   71.53400  -13.61300 1.000 37.61999  ?  177  ASN   B O   1 
ATOM   15397 C  CB  . ASN   B 1 177  ? 64.96800   74.36100  -14.40000 1.000 49.95165  ?  177  ASN   B CB  1 
ATOM   15398 C  CG  . ASN   B 1 177  ? 65.94500   74.45500  -15.55600 1.000 74.94518  ?  177  ASN   B CG  1 
ATOM   15399 O  OD1 . ASN   B 1 177  ? 65.60400   74.15500  -16.70100 1.000 66.06111  ?  177  ASN   B OD1 1 
ATOM   15400 N  ND2 . ASN   B 1 177  ? 67.17000   74.87300  -15.26200 1.000 77.50875  ?  177  ASN   B ND2 1 
ATOM   15401 N  N   . MET   B 1 178  ? 62.48300   73.28500  -12.68000 1.000 57.77531  ?  178  MET   B N   1 
ATOM   15402 C  CA  . MET   B 1 178  ? 62.05600   72.55500  -11.49600 1.000 54.78384  ?  178  MET   B CA  1 
ATOM   15403 C  C   . MET   B 1 178  ? 60.61300   72.07700  -11.58900 1.000 54.97128  ?  178  MET   B C   1 
ATOM   15404 O  O   . MET   B 1 178  ? 60.09100   71.51300  -10.62200 1.000 50.82089  ?  178  MET   B O   1 
ATOM   15405 C  CB  . MET   B 1 178  ? 62.25300   73.42300  -10.25500 1.000 60.13327  ?  178  MET   B CB  1 
ATOM   15406 C  CG  . MET   B 1 178  ? 63.67200   73.95600  -10.11200 1.000 66.09851  ?  178  MET   B CG  1 
ATOM   15407 S  SD  . MET   B 1 178  ? 64.14700   74.13500  -8.38600  1.000 67.86978  ?  178  MET   B SD  1 
ATOM   15408 C  CE  . MET   B 1 178  ? 63.51500   72.59300  -7.72800  1.000 52.76731  ?  178  MET   B CE  1 
ATOM   15409 N  N   . THR   B 1 179  ? 59.96200   72.28500  -12.72800 1.000 53.50355  ?  179  THR   B N   1 
ATOM   15410 C  CA  . THR   B 1 179  ? 58.59800   71.82000  -12.92500 1.000 59.75454  ?  179  THR   B CA  1 
ATOM   15411 C  C   . THR   B 1 179  ? 58.58700   70.31800  -13.17900 1.000 50.67707  ?  179  THR   B C   1 
ATOM   15412 O  O   . THR   B 1 179  ? 59.44400   69.78800  -13.89300 1.000 40.51608  ?  179  THR   B O   1 
ATOM   15413 C  CB  . THR   B 1 179  ? 57.95000   72.56500  -14.09300 1.000 57.73631  ?  179  THR   B CB  1 
ATOM   15414 O  OG1 . THR   B 1 179  ? 57.82900   73.95500  -13.76300 1.000 52.60173  ?  179  THR   B OG1 1 
ATOM   15415 C  CG2 . THR   B 1 179  ? 56.57300   72.00200  -14.40500 1.000 35.79050  ?  179  THR   B CG2 1 
ATOM   15416 N  N   . THR   B 1 180  ? 57.61700   69.63100  -12.57700 1.000 50.72735  ?  180  THR   B N   1 
ATOM   15417 C  CA  . THR   B 1 180  ? 57.49100   68.19200  -12.75200 1.000 49.34739  ?  180  THR   B CA  1 
ATOM   15418 C  C   . THR   B 1 180  ? 57.14600   67.85300  -14.20100 1.000 42.37131  ?  180  THR   B C   1 
ATOM   15419 O  O   . THR   B 1 180  ? 56.70100   68.70200  -14.97900 1.000 52.67662  ?  180  THR   B O   1 
ATOM   15420 C  CB  . THR   B 1 180  ? 56.41900   67.62900  -11.81900 1.000 53.78801  ?  180  THR   B CB  1 
ATOM   15421 O  OG1 . THR   B 1 180  ? 55.12300   68.03100  -12.28000 1.000 55.90483  ?  180  THR   B OG1 1 
ATOM   15422 C  CG2 . THR   B 1 180  ? 56.62500   68.14400  -10.40600 1.000 56.43699  ?  180  THR   B CG2 1 
ATOM   15423 N  N   . VAL   B 1 181  ? 57.35400   66.58300  -14.55600 1.000 35.35994  ?  181  VAL   B N   1 
ATOM   15424 C  CA  . VAL   B 1 181  ? 57.10600   66.14000  -15.92700 1.000 50.28687  ?  181  VAL   B CA  1 
ATOM   15425 C  C   . VAL   B 1 181  ? 55.63200   66.29400  -16.27500 1.000 53.45552  ?  181  VAL   B C   1 
ATOM   15426 O  O   . VAL   B 1 181  ? 55.27600   66.77400  -17.35900 1.000 53.05607  ?  181  VAL   B O   1 
ATOM   15427 C  CB  . VAL   B 1 181  ? 57.58100   64.68800  -16.11600 1.000 44.37167  ?  181  VAL   B CB  1 
ATOM   15428 C  CG1 . VAL   B 1 181  ? 56.92600   64.06600  -17.34200 1.000 41.26263  ?  181  VAL   B CG1 1 
ATOM   15429 C  CG2 . VAL   B 1 181  ? 59.09100   64.64400  -16.24600 1.000 47.06000  ?  181  VAL   B CG2 1 
ATOM   15430 N  N   . ARG   B 1 182  ? 54.75300   65.89000  -15.35600 1.000 46.57303  ?  182  ARG   B N   1 
ATOM   15431 C  CA  . ARG   B 1 182  ? 53.31900   65.97100  -15.61200 1.000 40.18485  ?  182  ARG   B CA  1 
ATOM   15432 C  C   . ARG   B 1 182  ? 52.88100   67.41500  -15.82700 1.000 51.66419  ?  182  ARG   B C   1 
ATOM   15433 O  O   . ARG   B 1 182  ? 52.14300   67.72000  -16.77200 1.000 50.65622  ?  182  ARG   B O   1 
ATOM   15434 C  CB  . ARG   B 1 182  ? 52.54000   65.34100  -14.45800 1.000 62.12017  ?  182  ARG   B CB  1 
ATOM   15435 C  CG  . ARG   B 1 182  ? 51.04200   65.56300  -14.56600 1.000 79.67341  ?  182  ARG   B CG  1 
ATOM   15436 C  CD  . ARG   B 1 182  ? 50.27000   65.01800  -13.36900 1.000 71.64093  ?  182  ARG   B CD  1 
ATOM   15437 N  NE  . ARG   B 1 182  ? 50.70200   65.58600  -12.09600 1.000 73.07303  ?  182  ARG   B NE  1 
ATOM   15438 C  CZ  . ARG   B 1 182  ? 50.46000   66.82900  -11.70000 1.000 83.27512  ?  182  ARG   B CZ  1 
ATOM   15439 N  NH1 . ARG   B 1 182  ? 49.83800   67.69800  -12.48200 1.000 68.50197  ?  182  ARG   B NH1 1 
ATOM   15440 N  NH2 . ARG   B 1 182  ? 50.85700   67.21300  -10.49000 1.000 85.00930  ?  182  ARG   B NH2 1 
ATOM   15441 N  N   . GLU   B 1 183  ? 53.32900   68.32000  -14.95500 1.000 46.12997  ?  183  GLU   B N   1 
ATOM   15442 C  CA  . GLU   B 1 183  ? 52.94800   69.72100  -15.08200 1.000 45.59449  ?  183  GLU   B CA  1 
ATOM   15443 C  C   . GLU   B 1 183  ? 53.62000   70.39400  -16.27100 1.000 50.35465  ?  183  GLU   B C   1 
ATOM   15444 O  O   . GLU   B 1 183  ? 53.09700   71.39000  -16.78200 1.000 51.57721  ?  183  GLU   B O   1 
ATOM   15445 C  CB  . GLU   B 1 183  ? 53.28000   70.47100  -13.79300 1.000 41.36194  ?  183  GLU   B CB  1 
ATOM   15446 C  CG  . GLU   B 1 183  ? 52.39200   70.08700  -12.61900 1.000 61.57778  ?  183  GLU   B CG  1 
ATOM   15447 C  CD  . GLU   B 1 183  ? 53.01500   70.43100  -11.28100 1.000 79.63594  ?  183  GLU   B CD  1 
ATOM   15448 O  OE1 . GLU   B 1 183  ? 54.24000   70.67500  -11.23900 1.000 65.92777  ?  183  GLU   B OE1 1 
ATOM   15449 O  OE2 . GLU   B 1 183  ? 52.28000   70.45400  -10.27100 1.000 78.98507  -1 183  GLU   B OE2 1 
ATOM   15450 N  N   . LEU   B 1 184  ? 54.76500   69.87400  -16.72100 1.000 50.41191  ?  184  LEU   B N   1 
ATOM   15451 C  CA  . LEU   B 1 184  ? 55.38600   70.40600  -17.92700 1.000 45.14822  ?  184  LEU   B CA  1 
ATOM   15452 C  C   . LEU   B 1 184  ? 54.57600   70.03700  -19.16400 1.000 44.17167  ?  184  LEU   B C   1 
ATOM   15453 O  O   . LEU   B 1 184  ? 54.34000   70.88400  -20.03400 1.000 34.03216  ?  184  LEU   B O   1 
ATOM   15454 C  CB  . LEU   B 1 184  ? 56.82000   69.89400  -18.05200 1.000 39.88873  ?  184  LEU   B CB  1 
ATOM   15455 C  CG  . LEU   B 1 184  ? 57.63100   70.51800  -19.19000 1.000 34.75690  ?  184  LEU   B CG  1 
ATOM   15456 C  CD1 . LEU   B 1 184  ? 58.34100   71.77700  -18.71900 1.000 36.89318  ?  184  LEU   B CD1 1 
ATOM   15457 C  CD2 . LEU   B 1 184  ? 58.61600   69.52400  -19.78600 1.000 38.41594  ?  184  LEU   B CD2 1 
ATOM   15458 N  N   . LEU   B 1 185  ? 54.13700   68.77900  -19.25400 1.000 50.60803  ?  185  LEU   B N   1 
ATOM   15459 C  CA  . LEU   B 1 185  ? 53.30400   68.36500  -20.37800 1.000 40.87189  ?  185  LEU   B CA  1 
ATOM   15460 C  C   . LEU   B 1 185  ? 51.94500   69.05300  -20.34200 1.000 64.35373  ?  185  LEU   B C   1 
ATOM   15461 O  O   . LEU   B 1 185  ? 51.38900   69.38700  -21.39400 1.000 62.63577  ?  185  LEU   B O   1 
ATOM   15462 C  CB  . LEU   B 1 185  ? 53.14500   66.84500  -20.38200 1.000 36.65692  ?  185  LEU   B CB  1 
ATOM   15463 C  CG  . LEU   B 1 185  ? 54.41800   66.07000  -20.72000 1.000 43.80036  ?  185  LEU   B CG  1 
ATOM   15464 C  CD1 . LEU   B 1 185  ? 54.13800   64.58000  -20.81400 1.000 39.17426  ?  185  LEU   B CD1 1 
ATOM   15465 C  CD2 . LEU   B 1 185  ? 55.01500   66.59400  -22.01600 1.000 50.48884  ?  185  LEU   B CD2 1 
ATOM   15466 N  N   . ALA   B 1 186  ? 51.39800   69.27400  -19.14400 1.000 62.20492  ?  186  ALA   B N   1 
ATOM   15467 C  CA  . ALA   B 1 186  ? 50.14800   70.02000  -19.02800 1.000 45.14133  ?  186  ALA   B CA  1 
ATOM   15468 C  C   . ALA   B 1 186  ? 50.29500   71.43000  -19.58700 1.000 48.41849  ?  186  ALA   B C   1 
ATOM   15469 O  O   . ALA   B 1 186  ? 49.39400   71.93300  -20.27000 1.000 58.96933  ?  186  ALA   B O   1 
ATOM   15470 C  CB  . ALA   B 1 186  ? 49.69600   70.06600  -17.56900 1.000 30.57472  ?  186  ALA   B CB  1 
ATOM   15471 N  N   . LEU   B 1 187  ? 51.42600   72.08300  -19.30900 1.000 44.22843  ?  187  LEU   B N   1 
ATOM   15472 C  CA  . LEU   B 1 187  ? 51.68100   73.40000  -19.88200 1.000 39.08676  ?  187  LEU   B CA  1 
ATOM   15473 C  C   . LEU   B 1 187  ? 51.84700   73.32700  -21.39500 1.000 50.97242  ?  187  LEU   B C   1 
ATOM   15474 O  O   . LEU   B 1 187  ? 51.56700   74.30600  -22.09500 1.000 54.11719  ?  187  LEU   B O   1 
ATOM   15475 C  CB  . LEU   B 1 187  ? 52.91900   74.02200  -19.23500 1.000 37.70684  ?  187  LEU   B CB  1 
ATOM   15476 C  CG  . LEU   B 1 187  ? 53.18300   75.50400  -19.50700 1.000 39.49481  ?  187  LEU   B CG  1 
ATOM   15477 C  CD1 . LEU   B 1 187  ? 51.98200   76.34500  -19.11100 1.000 42.84304  ?  187  LEU   B CD1 1 
ATOM   15478 C  CD2 . LEU   B 1 187  ? 54.42300   75.96800  -18.76300 1.000 42.69473  ?  187  LEU   B CD2 1 
ATOM   15479 N  N   . LYS   B 1 188  ? 52.29600   72.18300  -21.91800 1.000 47.04662  ?  188  LYS   B N   1 
ATOM   15480 C  CA  . LYS   B 1 188  ? 52.42300   72.03000  -23.36400 1.000 48.17619  ?  188  LYS   B CA  1 
ATOM   15481 C  C   . LYS   B 1 188  ? 51.05400   71.96600  -24.02800 1.000 51.52809  ?  188  LYS   B C   1 
ATOM   15482 O  O   . LYS   B 1 188  ? 50.81800   72.62000  -25.05100 1.000 69.22304  ?  188  LYS   B O   1 
ATOM   15483 C  CB  . LYS   B 1 188  ? 53.23800   70.77900  -23.69300 1.000 44.11400  ?  188  LYS   B CB  1 
ATOM   15484 C  CG  . LYS   B 1 188  ? 53.45100   70.55900  -25.18200 1.000 37.74011  ?  188  LYS   B CG  1 
ATOM   15485 C  CD  . LYS   B 1 188  ? 53.92600   69.14700  -25.47200 1.000 51.18830  ?  188  LYS   B CD  1 
ATOM   15486 C  CE  . LYS   B 1 188  ? 54.16400   68.93700  -26.96000 1.000 58.51346  ?  188  LYS   B CE  1 
ATOM   15487 N  NZ  . LYS   B 1 188  ? 54.56200   67.53200  -27.26200 1.000 44.01775  ?  188  LYS   B NZ  1 
ATOM   15488 N  N   . ARG   B 1 189  ? 50.13500   71.18200  -23.45800 1.000 56.53384  ?  189  ARG   B N   1 
ATOM   15489 C  CA  . ARG   B 1 189  ? 48.78300   71.09500  -23.99900 1.000 60.22012  ?  189  ARG   B CA  1 
ATOM   15490 C  C   . ARG   B 1 189  ? 48.03800   72.42000  -23.90500 1.000 51.53904  ?  189  ARG   B C   1 
ATOM   15491 O  O   . ARG   B 1 189  ? 47.03800   72.60800  -24.60600 1.000 62.97191  ?  189  ARG   B O   1 
ATOM   15492 C  CB  . ARG   B 1 189  ? 47.98500   70.00900  -23.27000 1.000 42.79286  ?  189  ARG   B CB  1 
ATOM   15493 C  CG  . ARG   B 1 189  ? 48.18000   68.58900  -23.79900 1.000 60.31938  ?  189  ARG   B CG  1 
ATOM   15494 C  CD  . ARG   B 1 189  ? 49.55300   68.03700  -23.45900 1.000 67.44347  ?  189  ARG   B CD  1 
ATOM   15495 N  NE  . ARG   B 1 189  ? 49.64000   66.59300  -23.64200 1.000 93.30987  ?  189  ARG   B NE  1 
ATOM   15496 C  CZ  . ARG   B 1 189  ? 49.44000   65.70200  -22.68000 1.000 101.65399 ?  189  ARG   B CZ  1 
ATOM   15497 N  NH1 . ARG   B 1 189  ? 49.12300   66.07200  -21.44900 1.000 79.29445  ?  189  ARG   B NH1 1 
ATOM   15498 N  NH2 . ARG   B 1 189  ? 49.56100   64.40700  -22.95900 1.000 97.92713  ?  189  ARG   B NH2 1 
ATOM   15499 N  N   . LEU   B 1 190  ? 48.50400   73.34100  -23.06300 1.000 51.25816  ?  190  LEU   B N   1 
ATOM   15500 C  CA  . LEU   B 1 190  ? 47.82400   74.60500  -22.81500 1.000 47.66737  ?  190  LEU   B CA  1 
ATOM   15501 C  C   . LEU   B 1 190  ? 48.54100   75.79000  -23.44600 1.000 48.68803  ?  190  LEU   B C   1 
ATOM   15502 O  O   . LEU   B 1 190  ? 48.22100   76.93900  -23.12300 1.000 65.81872  ?  190  LEU   B O   1 
ATOM   15503 C  CB  . LEU   B 1 190  ? 47.67000   74.83000  -21.30800 1.000 35.59216  ?  190  LEU   B CB  1 
ATOM   15504 C  CG  . LEU   B 1 190  ? 46.49300   74.19000  -20.56100 1.000 62.32185  ?  190  LEU   B CG  1 
ATOM   15505 C  CD1 . LEU   B 1 190  ? 46.33000   72.70300  -20.86400 1.000 58.08729  ?  190  LEU   B CD1 1 
ATOM   15506 C  CD2 . LEU   B 1 190  ? 46.65500   74.40900  -19.06300 1.000 52.05579  ?  190  LEU   B CD2 1 
ATOM   15507 N  N   . CYS   B 1 191  ? 49.50600   75.54400  -24.33600 1.000 64.78036  ?  191  CYS   B N   1 
ATOM   15508 C  CA  . CYS   B 1 191  ? 50.27400   76.63100  -24.92800 1.000 77.74604  ?  191  CYS   B CA  1 
ATOM   15509 C  C   . CYS   B 1 191  ? 50.60500   76.40000  -26.39800 1.000 75.13271  ?  191  CYS   B C   1 
ATOM   15510 O  O   . CYS   B 1 191  ? 51.37100   77.18600  -26.97100 1.000 66.17640  ?  191  CYS   B O   1 
ATOM   15511 C  CB  . CYS   B 1 191  ? 51.57500   76.85900  -24.14600 1.000 62.22254  ?  191  CYS   B CB  1 
ATOM   15512 S  SG  . CYS   B 1 191  ? 51.34100   77.43800  -22.45000 1.000 102.18575 ?  191  CYS   B SG  1 
ATOM   15513 N  N   . ALA   B 1 192  ? 50.06300   75.35900  -27.02800 1.000 82.44312  ?  192  ALA   B N   1 
ATOM   15514 C  CA  . ALA   B 1 192  ? 50.37100   75.05300  -28.41700 1.000 80.29578  ?  192  ALA   B CA  1 
ATOM   15515 C  C   . ALA   B 1 192  ? 49.09400   74.66900  -29.15400 1.000 94.85716  ?  192  ALA   B C   1 
ATOM   15516 O  O   . ALA   B 1 192  ? 48.02500   74.51200  -28.55700 1.000 79.71747  ?  192  ALA   B O   1 
ATOM   15517 C  CB  . ALA   B 1 192  ? 51.42200   73.94200  -28.52800 1.000 75.86748  ?  192  ALA   B CB  1 
ATOM   15518 N  N   . GLU   B 1 193  ? 49.22700   74.51500  -30.47200 1.000 94.07035  ?  193  GLU   B N   1 
ATOM   15519 C  CA  . GLU   B 1 193  ? 48.10800   74.34500  -31.38900 1.000 85.46605  ?  193  GLU   B CA  1 
ATOM   15520 C  C   . GLU   B 1 193  ? 48.41100   73.18900  -32.33700 1.000 99.93143  ?  193  GLU   B C   1 
ATOM   15521 O  O   . GLU   B 1 193  ? 49.48600   73.16500  -32.96500 1.000 111.31242 ?  193  GLU   B O   1 
ATOM   15522 C  CB  . GLU   B 1 193  ? 47.84400   75.65000  -32.16400 1.000 72.62026  ?  193  GLU   B CB  1 
ATOM   15523 C  CG  . GLU   B 1 193  ? 48.94300   76.09200  -33.13800 1.000 98.95335  ?  193  GLU   B CG  1 
ATOM   15524 C  CD  . GLU   B 1 193  ? 50.30700   76.31500  -32.49300 1.000 108.44167 ?  193  GLU   B CD  1 
ATOM   15525 O  OE1 . GLU   B 1 193  ? 50.54000   75.79900  -31.37200 1.000 96.23141  ?  193  GLU   B OE1 1 
ATOM   15526 O  OE2 . GLU   B 1 193  ? 51.14200   77.00500  -33.11300 1.000 116.63705 -1 193  GLU   B OE2 1 
ATOM   15527 N  N   . PRO   B 1 194  ? 47.52600   72.19200  -32.43700 1.000 114.65530 ?  194  PRO   B N   1 
ATOM   15528 C  CA  . PRO   B 1 194  ? 47.84200   71.01900  -33.26200 1.000 117.22208 ?  194  PRO   B CA  1 
ATOM   15529 C  C   . PRO   B 1 194  ? 47.04400   70.92200  -34.55500 1.000 128.78090 ?  194  PRO   B C   1 
ATOM   15530 O  O   . PRO   B 1 194  ? 47.15800   69.92000  -35.26900 1.000 117.95523 ?  194  PRO   B O   1 
ATOM   15531 C  CB  . PRO   B 1 194  ? 47.50400   69.86000  -32.32100 1.000 115.53726 ?  194  PRO   B CB  1 
ATOM   15532 C  CG  . PRO   B 1 194  ? 46.30300   70.37900  -31.56000 1.000 115.78398 ?  194  PRO   B CG  1 
ATOM   15533 C  CD  . PRO   B 1 194  ? 46.42300   71.90400  -31.50300 1.000 109.63589 ?  194  PRO   B CD  1 
ATOM   15534 N  N   . LYS   B 1 195  ? 46.24000   71.94000  -34.86200 1.000 143.74192 ?  195  LYS   B N   1 
ATOM   15535 C  CA  . LYS   B 1 195  ? 45.40200   71.95900  -36.06500 1.000 118.00725 ?  195  LYS   B CA  1 
ATOM   15536 C  C   . LYS   B 1 195  ? 44.47600   70.74600  -36.13200 1.000 101.24346 ?  195  LYS   B C   1 
ATOM   15537 O  O   . LYS   B 1 195  ? 44.65000   69.86400  -36.97400 1.000 105.13802 ?  195  LYS   B O   1 
ATOM   15538 C  CB  . LYS   B 1 195  ? 46.26700   72.02300  -37.32800 1.000 110.29913 ?  195  LYS   B CB  1 
ATOM   15539 C  CG  . LYS   B 1 195  ? 47.30800   73.13100  -37.31300 1.000 111.05567 ?  195  LYS   B CG  1 
ATOM   15540 C  CD  . LYS   B 1 195  ? 48.49400   72.77100  -38.19100 1.000 99.63788  ?  195  LYS   B CD  1 
ATOM   15541 C  CE  . LYS   B 1 195  ? 49.71400   73.61900  -37.86100 1.000 104.91340 ?  195  LYS   B CE  1 
ATOM   15542 N  NZ  . LYS   B 1 195  ? 49.61000   75.00400  -38.39600 1.000 81.61801  ?  195  LYS   B NZ  1 
ATOM   15543 N  N   . GLU   B 1 198  ? 42.26600   72.94500  -37.67300 1.000 94.56816  ?  198  GLU   B N   1 
ATOM   15544 C  CA  . GLU   B 1 198  ? 42.28900   74.39500  -37.82500 1.000 110.22770 ?  198  GLU   B CA  1 
ATOM   15545 C  C   . GLU   B 1 198  ? 41.33000   74.83000  -38.93200 1.000 107.09143 ?  198  GLU   B C   1 
ATOM   15546 O  O   . GLU   B 1 198  ? 41.05600   74.06900  -39.86000 1.000 113.79017 ?  198  GLU   B O   1 
ATOM   15547 C  CB  . GLU   B 1 198  ? 43.71300   74.87800  -38.12300 1.000 114.91958 ?  198  GLU   B CB  1 
ATOM   15548 C  CG  . GLU   B 1 198  ? 44.01500   76.29600  -37.65100 1.000 105.54741 ?  198  GLU   B CG  1 
ATOM   15549 C  CD  . GLU   B 1 198  ? 43.58100   77.35700  -38.64400 1.000 118.90044 ?  198  GLU   B CD  1 
ATOM   15550 O  OE1 . GLU   B 1 198  ? 44.23500   77.49100  -39.69900 1.000 114.76418 ?  198  GLU   B OE1 1 
ATOM   15551 O  OE2 . GLU   B 1 198  ? 42.58100   78.05400  -38.37000 1.000 124.19687 -1 198  GLU   B OE2 1 
ATOM   15552 N  N   . LYS   B 1 199  ? 40.81200   76.05200  -38.82200 1.000 94.99258  ?  199  LYS   B N   1 
ATOM   15553 C  CA  . LYS   B 1 199  ? 39.91700   76.60800  -39.82900 1.000 94.71237  ?  199  LYS   B CA  1 
ATOM   15554 C  C   . LYS   B 1 199  ? 40.14200   78.10900  -39.97000 1.000 98.77095  ?  199  LYS   B C   1 
ATOM   15555 O  O   . LYS   B 1 199  ? 39.89800   78.86600  -39.02200 1.000 92.50369  ?  199  LYS   B O   1 
ATOM   15556 C  CB  . LYS   B 1 199  ? 38.45400   76.32600  -39.47500 1.000 97.05515  ?  199  LYS   B CB  1 
ATOM   15557 C  CG  . LYS   B 1 199  ? 37.92600   74.97200  -39.93500 1.000 102.97121 ?  199  LYS   B CG  1 
ATOM   15558 C  CD  . LYS   B 1 199  ? 37.32700   75.03500  -41.33900 1.000 98.62709  ?  199  LYS   B CD  1 
ATOM   15559 C  CE  . LYS   B 1 199  ? 38.36000   74.75500  -42.42000 1.000 77.47313  ?  199  LYS   B CE  1 
ATOM   15560 N  NZ  . LYS   B 1 199  ? 37.73500   74.67500  -43.76900 1.000 91.04495  ?  199  LYS   B NZ  1 
ATOM   15561 N  N   . PRO   B 1 200  ? 40.60600   78.57500  -41.12500 1.000 95.03944  ?  200  PRO   B N   1 
ATOM   15562 C  CA  . PRO   B 1 200  ? 40.74800   80.01600  -41.33900 1.000 83.78912  ?  200  PRO   B CA  1 
ATOM   15563 C  C   . PRO   B 1 200  ? 39.40400   80.67000  -41.62700 1.000 83.77527  ?  200  PRO   B C   1 
ATOM   15564 O  O   . PRO   B 1 200  ? 38.42100   80.01800  -41.98200 1.000 89.20805  ?  200  PRO   B O   1 
ATOM   15565 C  CB  . PRO   B 1 200  ? 41.67400   80.10200  -42.55600 1.000 69.95436  ?  200  PRO   B CB  1 
ATOM   15566 C  CG  . PRO   B 1 200  ? 41.38400   78.85000  -43.31400 1.000 74.86873  ?  200  PRO   B CG  1 
ATOM   15567 C  CD  . PRO   B 1 200  ? 41.08300   77.79300  -42.28000 1.000 76.36513  ?  200  PRO   B CD  1 
ATOM   15568 N  N   . ILE   B 1 201  ? 39.38000   81.98900  -41.46700 1.000 67.83143  ?  201  ILE   B N   1 
ATOM   15569 C  CA  . ILE   B 1 201  ? 38.17700   82.78500  -41.67300 1.000 50.89002  ?  201  ILE   B CA  1 
ATOM   15570 C  C   . ILE   B 1 201  ? 38.25600   83.42400  -43.05100 1.000 47.00949  ?  201  ILE   B C   1 
ATOM   15571 O  O   . ILE   B 1 201  ? 39.18300   84.19000  -43.33800 1.000 72.34763  ?  201  ILE   B O   1 
ATOM   15572 C  CB  . ILE   B 1 201  ? 38.01300   83.84500  -40.57300 1.000 63.07146  ?  201  ILE   B CB  1 
ATOM   15573 C  CG1 . ILE   B 1 201  ? 37.62500   83.17100  -39.25500 1.000 68.20054  ?  201  ILE   B CG1 1 
ATOM   15574 C  CG2 . ILE   B 1 201  ? 36.98300   84.89000  -40.98200 1.000 55.72881  ?  201  ILE   B CG2 1 
ATOM   15575 C  CD1 . ILE   B 1 201  ? 37.61600   84.10100  -38.07600 1.000 46.25777  ?  201  ILE   B CD1 1 
ATOM   15576 N  N   . ASP   B 1 202  ? 37.28100   83.10800  -43.90500 1.000 56.12128  ?  202  ASP   B N   1 
ATOM   15577 C  CA  . ASP   B 1 202  ? 37.23000   83.61900  -45.27000 1.000 58.58168  ?  202  ASP   B CA  1 
ATOM   15578 C  C   . ASP   B 1 202  ? 35.97900   84.45200  -45.52400 1.000 62.10914  ?  202  ASP   B C   1 
ATOM   15579 O  O   . ASP   B 1 202  ? 35.57000   84.61100  -46.67900 1.000 69.04605  ?  202  ASP   B O   1 
ATOM   15580 C  CB  . ASP   B 1 202  ? 37.30200   82.46600  -46.27400 1.000 61.33382  ?  202  ASP   B CB  1 
ATOM   15581 C  CG  . ASP   B 1 202  ? 36.12700   81.51500  -46.15000 1.000 70.45213  ?  202  ASP   B CG  1 
ATOM   15582 O  OD1 . ASP   B 1 202  ? 35.69700   81.24600  -45.00700 1.000 80.61057  ?  202  ASP   B OD1 1 
ATOM   15583 O  OD2 . ASP   B 1 202  ? 35.62900   81.04200  -47.19300 1.000 65.71313  -1 202  ASP   B OD2 1 
ATOM   15584 N  N   . LYS   B 1 203  ? 35.36300   84.98800  -44.47300 1.000 45.88411  ?  203  LYS   B N   1 
ATOM   15585 C  CA  . LYS   B 1 203  ? 34.09200   85.68800  -44.58300 1.000 46.88705  ?  203  LYS   B CA  1 
ATOM   15586 C  C   . LYS   B 1 203  ? 34.14800   87.01100  -43.83500 1.000 35.66539  ?  203  LYS   B C   1 
ATOM   15587 O  O   . LYS   B 1 203  ? 34.76400   87.10800  -42.77000 1.000 47.62314  ?  203  LYS   B O   1 
ATOM   15588 C  CB  . LYS   B 1 203  ? 32.94100   84.83400  -44.02800 1.000 49.74737  ?  203  LYS   B CB  1 
ATOM   15589 C  CG  . LYS   B 1 203  ? 32.61900   83.59800  -44.85200 1.000 58.14096  ?  203  LYS   B CG  1 
ATOM   15590 C  CD  . LYS   B 1 203  ? 31.83900   83.96400  -46.10200 1.000 55.93554  ?  203  LYS   B CD  1 
ATOM   15591 C  CE  . LYS   B 1 203  ? 31.70200   82.77600  -47.03800 1.000 67.02105  ?  203  LYS   B CE  1 
ATOM   15592 N  NZ  . LYS   B 1 203  ? 32.23600   83.09100  -48.39200 1.000 65.64805  ?  203  LYS   B NZ  1 
ATOM   15593 N  N   . THR   B 1 204  ? 33.50400   88.02800  -44.40300 1.000 33.37509  ?  204  THR   B N   1 
ATOM   15594 C  CA  . THR   B 1 204  ? 33.24100   89.26800  -43.69300 1.000 39.21313  ?  204  THR   B CA  1 
ATOM   15595 C  C   . THR   B 1 204  ? 31.94200   89.11900  -42.90200 1.000 39.53364  ?  204  THR   B C   1 
ATOM   15596 O  O   . THR   B 1 204  ? 31.29100   88.07200  -42.92700 1.000 45.56081  ?  204  THR   B O   1 
ATOM   15597 C  CB  . THR   B 1 204  ? 33.17300   90.44700  -44.66500 1.000 41.25471  ?  204  THR   B CB  1 
ATOM   15598 O  OG1 . THR   B 1 204  ? 32.18000   90.19200  -45.66600 1.000 25.71736  ?  204  THR   B OG1 1 
ATOM   15599 C  CG2 . THR   B 1 204  ? 34.51900   90.65900  -45.33900 1.000 47.29748  ?  204  THR   B CG2 1 
ATOM   15600 N  N   . PHE   B 1 205  ? 31.55100   90.17400  -42.18700 1.000 29.41207  ?  205  PHE   B N   1 
ATOM   15601 C  CA  . PHE   B 1 205  ? 30.33600   90.07400  -41.38500 1.000 39.97852  ?  205  PHE   B CA  1 
ATOM   15602 C  C   . PHE   B 1 205  ? 29.08600   90.18900  -42.24900 1.000 43.81721  ?  205  PHE   B C   1 
ATOM   15603 O  O   . PHE   B 1 205  ? 28.18500   89.34700  -42.16000 1.000 46.54465  ?  205  PHE   B O   1 
ATOM   15604 C  CB  . PHE   B 1 205  ? 30.31800   91.13600  -40.28700 1.000 43.12369  ?  205  PHE   B CB  1 
ATOM   15605 C  CG  . PHE   B 1 205  ? 29.11200   91.04800  -39.39700 1.000 43.13294  ?  205  PHE   B CG  1 
ATOM   15606 C  CD1 . PHE   B 1 205  ? 29.08300   90.15300  -38.34200 1.000 22.55854  ?  205  PHE   B CD1 1 
ATOM   15607 C  CD2 . PHE   B 1 205  ? 27.99900   91.84000  -39.63000 1.000 50.57825  ?  205  PHE   B CD2 1 
ATOM   15608 C  CE1 . PHE   B 1 205  ? 27.97300   90.05800  -37.52700 1.000 41.81726  ?  205  PHE   B CE1 1 
ATOM   15609 C  CE2 . PHE   B 1 205  ? 26.88400   91.75000  -38.81800 1.000 38.35210  ?  205  PHE   B CE2 1 
ATOM   15610 C  CZ  . PHE   B 1 205  ? 26.87200   90.85800  -37.76500 1.000 48.41616  ?  205  PHE   B CZ  1 
ATOM   15611 N  N   . HIS   B 1 206  ? 29.00600   91.23500  -43.07700 1.000 32.60948  ?  206  HIS   B N   1 
ATOM   15612 C  CA  . HIS   B 1 206  ? 27.84100   91.40300  -43.94100 1.000 31.62129  ?  206  HIS   B CA  1 
ATOM   15613 C  C   . HIS   B 1 206  ? 27.64700   90.20100  -44.85300 1.000 30.70082  ?  206  HIS   B C   1 
ATOM   15614 O  O   . HIS   B 1 206  ? 26.51100   89.87200  -45.21300 1.000 46.04632  ?  206  HIS   B O   1 
ATOM   15615 C  CB  . HIS   B 1 206  ? 27.96800   92.68900  -44.75900 1.000 38.48319  ?  206  HIS   B CB  1 
ATOM   15616 C  CG  . HIS   B 1 206  ? 29.34500   92.93900  -45.29200 1.000 39.68253  ?  206  HIS   B CG  1 
ATOM   15617 N  ND1 . HIS   B 1 206  ? 30.37400   93.41000  -44.50400 1.000 43.80695  ?  206  HIS   B ND1 1 
ATOM   15618 C  CD2 . HIS   B 1 206  ? 29.86000   92.80000  -46.53700 1.000 40.69062  ?  206  HIS   B CD2 1 
ATOM   15619 C  CE1 . HIS   B 1 206  ? 31.46400   93.54100  -45.23800 1.000 40.54864  ?  206  HIS   B CE1 1 
ATOM   15620 N  NE2 . HIS   B 1 206  ? 31.17900   93.17800  -46.47500 1.000 33.18742  ?  206  HIS   B NE2 1 
ATOM   15621 N  N   . GLN   B 1 207  ? 28.73800   89.53200  -45.22800 1.000 39.20244  ?  207  GLN   B N   1 
ATOM   15622 C  CA  . GLN   B 1 207  ? 28.63400   88.27000  -45.95100 1.000 37.75128  ?  207  GLN   B CA  1 
ATOM   15623 C  C   . GLN   B 1 207  ? 27.80400   87.26100  -45.16700 1.000 36.33249  ?  207  GLN   B C   1 
ATOM   15624 O  O   . GLN   B 1 207  ? 26.85400   86.67200  -45.69500 1.000 39.61691  ?  207  GLN   B O   1 
ATOM   15625 C  CB  . GLN   B 1 207  ? 30.03400   87.71600  -46.21900 1.000 48.93665  ?  207  GLN   B CB  1 
ATOM   15626 C  CG  . GLN   B 1 207  ? 30.30300   87.34300  -47.66200 1.000 63.26021  ?  207  GLN   B CG  1 
ATOM   15627 C  CD  . GLN   B 1 207  ? 31.77600   87.10200  -47.93700 1.000 63.90442  ?  207  GLN   B CD  1 
ATOM   15628 O  OE1 . GLN   B 1 207  ? 32.62700   87.33100  -47.07700 1.000 57.13432  ?  207  GLN   B OE1 1 
ATOM   15629 N  NE2 . GLN   B 1 207  ? 32.08300   86.64000  -49.14300 1.000 91.39328  ?  207  GLN   B NE2 1 
ATOM   15630 N  N   . LEU   B 1 208  ? 28.15000   87.05500  -43.89500 1.000 34.62305  ?  208  LEU   B N   1 
ATOM   15631 C  CA  . LEU   B 1 208  ? 27.44300   86.06900  -43.08600 1.000 45.97625  ?  208  LEU   B CA  1 
ATOM   15632 C  C   . LEU   B 1 208  ? 26.07500   86.57700  -42.65500 1.000 47.10160  ?  208  LEU   B C   1 
ATOM   15633 O  O   . LEU   B 1 208  ? 25.18000   85.77600  -42.36000 1.000 44.02485  ?  208  LEU   B O   1 
ATOM   15634 C  CB  . LEU   B 1 208  ? 28.28200   85.69800  -41.86500 1.000 39.97996  ?  208  LEU   B CB  1 
ATOM   15635 C  CG  . LEU   B 1 208  ? 29.56800   84.91800  -42.13400 1.000 36.46541  ?  208  LEU   B CG  1 
ATOM   15636 C  CD1 . LEU   B 1 208  ? 30.48000   84.95100  -40.91900 1.000 28.13493  ?  208  LEU   B CD1 1 
ATOM   15637 C  CD2 . LEU   B 1 208  ? 29.23300   83.48700  -42.50900 1.000 43.82422  ?  208  LEU   B CD2 1 
ATOM   15638 N  N   . PHE   B 1 209  ? 25.89100   87.89700  -42.61000 1.000 42.46671  ?  209  PHE   B N   1 
ATOM   15639 C  CA  . PHE   B 1 209  ? 24.59200   88.44500  -42.24000 1.000 38.55414  ?  209  PHE   B CA  1 
ATOM   15640 C  C   . PHE   B 1 209  ? 23.59900   88.31500  -43.38800 1.000 44.00803  ?  209  PHE   B C   1 
ATOM   15641 O  O   . PHE   B 1 209  ? 22.46400   87.86700  -43.19000 1.000 48.01258  ?  209  PHE   B O   1 
ATOM   15642 C  CB  . PHE   B 1 209  ? 24.73300   89.90600  -41.81300 1.000 49.33528  ?  209  PHE   B CB  1 
ATOM   15643 C  CG  . PHE   B 1 209  ? 23.42200   90.58100  -41.52900 1.000 45.68645  ?  209  PHE   B CG  1 
ATOM   15644 C  CD1 . PHE   B 1 209  ? 22.69800   90.26800  -40.38900 1.000 35.51853  ?  209  PHE   B CD1 1 
ATOM   15645 C  CD2 . PHE   B 1 209  ? 22.91400   91.53100  -42.39800 1.000 42.87492  ?  209  PHE   B CD2 1 
ATOM   15646 C  CE1 . PHE   B 1 209  ? 21.49000   90.88900  -40.12400 1.000 38.63047  ?  209  PHE   B CE1 1 
ATOM   15647 C  CE2 . PHE   B 1 209  ? 21.70700   92.15700  -42.13900 1.000 44.37225  ?  209  PHE   B CE2 1 
ATOM   15648 C  CZ  . PHE   B 1 209  ? 20.99500   91.83500  -41.00000 1.000 45.32297  ?  209  PHE   B CZ  1 
ATOM   15649 N  N   . GLU   B 1 210  ? 24.01400   88.70000  -44.59800 1.000 41.71920  ?  210  GLU   B N   1 
ATOM   15650 C  CA  . GLU   B 1 210  ? 23.15300   88.53100  -45.76300 1.000 44.37659  ?  210  GLU   B CA  1 
ATOM   15651 C  C   . GLU   B 1 210  ? 22.78400   87.07000  -45.97000 1.000 43.97858  ?  210  GLU   B C   1 
ATOM   15652 O  O   . GLU   B 1 210  ? 21.69100   86.76900  -46.46300 1.000 55.67558  ?  210  GLU   B O   1 
ATOM   15653 C  CB  . GLU   B 1 210  ? 23.83800   89.09500  -47.00800 1.000 30.69065  ?  210  GLU   B CB  1 
ATOM   15654 C  CG  . GLU   B 1 210  ? 24.01300   90.60300  -46.97800 1.000 29.27300  ?  210  GLU   B CG  1 
ATOM   15655 C  CD  . GLU   B 1 210  ? 24.96800   91.10200  -48.04200 1.000 42.44056  ?  210  GLU   B CD  1 
ATOM   15656 O  OE1 . GLU   B 1 210  ? 25.39300   90.28700  -48.88800 1.000 40.76661  ?  210  GLU   B OE1 1 
ATOM   15657 O  OE2 . GLU   B 1 210  ? 25.29700   92.30800  -48.02900 1.000 48.25591  -1 210  GLU   B OE2 1 
ATOM   15658 N  N   . GLN   B 1 211  ? 23.67800   86.15100  -45.59900 1.000 40.85564  ?  211  GLN   B N   1 
ATOM   15659 C  CA  . GLN   B 1 211  ? 23.33900   84.73300  -45.63700 1.000 43.45269  ?  211  GLN   B CA  1 
ATOM   15660 C  C   . GLN   B 1 211  ? 22.27000   84.40100  -44.60400 1.000 43.46848  ?  211  GLN   B C   1 
ATOM   15661 O  O   . GLN   B 1 211  ? 21.38400   83.57700  -44.86100 1.000 39.83389  ?  211  GLN   B O   1 
ATOM   15662 C  CB  . GLN   B 1 211  ? 24.59600   83.89300  -45.40900 1.000 43.65302  ?  211  GLN   B CB  1 
ATOM   15663 C  CG  . GLN   B 1 211  ? 24.35000   82.39500  -45.34200 1.000 65.59318  ?  211  GLN   B CG  1 
ATOM   15664 C  CD  . GLN   B 1 211  ? 25.63100   81.60200  -45.15800 1.000 66.46621  ?  211  GLN   B CD  1 
ATOM   15665 O  OE1 . GLN   B 1 211  ? 26.72200   82.16900  -45.08400 1.000 52.99058  ?  211  GLN   B OE1 1 
ATOM   15666 N  NE2 . GLN   B 1 211  ? 25.50400   80.28100  -45.08300 1.000 58.13004  ?  211  GLN   B NE2 1 
ATOM   15667 N  N   . GLN   B 1 212  ? 22.33200   85.03800  -43.43200 1.000 42.97236  ?  212  GLN   B N   1 
ATOM   15668 C  CA  . GLN   B 1 212  ? 21.31900   84.80500  -42.40800 1.000 47.09213  ?  212  GLN   B CA  1 
ATOM   15669 C  C   . GLN   B 1 212  ? 19.99800   85.46800  -42.77400 1.000 53.54836  ?  212  GLN   B C   1 
ATOM   15670 O  O   . GLN   B 1 212  ? 18.93000   84.96100  -42.41200 1.000 47.92029  ?  212  GLN   B O   1 
ATOM   15671 C  CB  . GLN   B 1 212  ? 21.81400   85.31100  -41.05300 1.000 43.18593  ?  212  GLN   B CB  1 
ATOM   15672 C  CG  . GLN   B 1 212  ? 20.91900   84.93400  -39.88400 1.000 32.89515  ?  212  GLN   B CG  1 
ATOM   15673 C  CD  . GLN   B 1 212  ? 20.83800   83.43500  -39.67900 1.000 49.98090  ?  212  GLN   B CD  1 
ATOM   15674 O  OE1 . GLN   B 1 212  ? 21.82700   82.71900  -39.84400 1.000 59.43784  ?  212  GLN   B OE1 1 
ATOM   15675 N  NE2 . GLN   B 1 212  ? 19.65400   82.94900  -39.32500 1.000 38.14527  ?  212  GLN   B NE2 1 
ATOM   15676 N  N   . VAL   B 1 213  ? 20.05300   86.59700  -43.48700 1.000 54.31974  ?  213  VAL   B N   1 
ATOM   15677 C  CA  . VAL   B 1 213  ? 18.83600   87.24300  -43.96900 1.000 38.19040  ?  213  VAL   B CA  1 
ATOM   15678 C  C   . VAL   B 1 213  ? 18.05200   86.30400  -44.87500 1.000 38.23335  ?  213  VAL   B C   1 
ATOM   15679 O  O   . VAL   B 1 213  ? 16.81700   86.30600  -44.86800 1.000 43.93844  ?  213  VAL   B O   1 
ATOM   15680 C  CB  . VAL   B 1 213  ? 19.18800   88.56500  -44.68300 1.000 39.92986  ?  213  VAL   B CB  1 
ATOM   15681 C  CG1 . VAL   B 1 213  ? 17.98900   89.10700  -45.43700 1.000 40.19634  ?  213  VAL   B CG1 1 
ATOM   15682 C  CG2 . VAL   B 1 213  ? 19.68700   89.59300  -43.68000 1.000 38.04172  ?  213  VAL   B CG2 1 
ATOM   15683 N  N   . GLU   B 1 214  ? 18.74700   85.46900  -45.64800 1.000 44.79370  ?  214  GLU   B N   1 
ATOM   15684 C  CA  . GLU   B 1 214  ? 18.07600   84.54300  -46.55200 1.000 46.48196  ?  214  GLU   B CA  1 
ATOM   15685 C  C   . GLU   B 1 214  ? 17.53400   83.30600  -45.84100 1.000 41.51494  ?  214  GLU   B C   1 
ATOM   15686 O  O   . GLU   B 1 214  ? 16.64700   82.63700  -46.38500 1.000 57.73864  ?  214  GLU   B O   1 
ATOM   15687 C  CB  . GLU   B 1 214  ? 19.03400   84.13200  -47.67200 1.000 33.97813  ?  214  GLU   B CB  1 
ATOM   15688 C  CG  . GLU   B 1 214  ? 19.60900   85.31000  -48.45600 1.000 47.09359  ?  214  GLU   B CG  1 
ATOM   15689 C  CD  . GLU   B 1 214  ? 18.67300   85.81000  -49.54000 1.000 66.47594  ?  214  GLU   B CD  1 
ATOM   15690 O  OE1 . GLU   B 1 214  ? 18.30100   85.00300  -50.41700 1.000 67.84099  ?  214  GLU   B OE1 1 
ATOM   15691 O  OE2 . GLU   B 1 214  ? 18.30700   87.00500  -49.51400 1.000 61.42508  -1 214  GLU   B OE2 1 
ATOM   15692 N  N   . MET   B 1 215  ? 18.03400   82.98800  -44.64600 1.000 35.84749  ?  215  MET   B N   1 
ATOM   15693 C  CA  . MET   B 1 215  ? 17.53500   81.84100  -43.89600 1.000 53.30193  ?  215  MET   B CA  1 
ATOM   15694 C  C   . MET   B 1 215  ? 16.44700   82.21700  -42.89900 1.000 53.89637  ?  215  MET   B C   1 
ATOM   15695 O  O   . MET   B 1 215  ? 15.59700   81.37900  -42.57400 1.000 60.99125  ?  215  MET   B O   1 
ATOM   15696 C  CB  . MET   B 1 215  ? 18.68000   81.14700  -43.15400 1.000 53.75369  ?  215  MET   B CB  1 
ATOM   15697 C  CG  . MET   B 1 215  ? 19.69800   80.47400  -44.06200 1.000 45.89670  ?  215  MET   B CG  1 
ATOM   15698 S  SD  . MET   B 1 215  ? 19.95000   78.73900  -43.64300 1.000 104.57624 ?  215  MET   B SD  1 
ATOM   15699 C  CE  . MET   B 1 215  ? 18.46500   78.00900  -44.32900 1.000 66.61359  ?  215  MET   B CE  1 
ATOM   15700 N  N   . THR   B 1 216  ? 16.46000   83.45500  -42.40300 1.000 48.29220  ?  216  THR   B N   1 
ATOM   15701 C  CA  . THR   B 1 216  ? 15.43400   83.96700  -41.49300 1.000 30.61644  ?  216  THR   B CA  1 
ATOM   15702 C  C   . THR   B 1 216  ? 14.90300   85.29600  -42.01700 1.000 47.93448  ?  216  THR   B C   1 
ATOM   15703 O  O   . THR   B 1 216  ? 15.03500   86.33500  -41.36100 1.000 45.29538  ?  216  THR   B O   1 
ATOM   15704 C  CB  . THR   B 1 216  ? 15.99400   84.11800  -40.07800 1.000 36.19615  ?  216  THR   B CB  1 
ATOM   15705 O  OG1 . THR   B 1 216  ? 17.31900   84.66500  -40.13800 1.000 52.83676  ?  216  THR   B OG1 1 
ATOM   15706 C  CG2 . THR   B 1 216  ? 16.03200   82.77700  -39.36900 1.000 38.50855  ?  216  THR   B CG2 1 
ATOM   15707 N  N   . PRO   B 1 217  ? 14.27200   85.29900  -43.20700 1.000 46.02093  ?  217  PRO   B N   1 
ATOM   15708 C  CA  . PRO   B 1 217  ? 13.92700   86.57100  -43.86500 1.000 33.19845  ?  217  PRO   B CA  1 
ATOM   15709 C  C   . PRO   B 1 217  ? 12.87300   87.37500  -43.13200 1.000 45.39204  ?  217  PRO   B C   1 
ATOM   15710 O  O   . PRO   B 1 217  ? 13.01400   88.59200  -42.95900 1.000 41.87663  ?  217  PRO   B O   1 
ATOM   15711 C  CB  . PRO   B 1 217  ? 13.41500   86.12100  -45.24100 1.000 23.77118  ?  217  PRO   B CB  1 
ATOM   15712 C  CG  . PRO   B 1 217  ? 13.90300   84.71400  -45.40500 1.000 54.45818  ?  217  PRO   B CG  1 
ATOM   15713 C  CD  . PRO   B 1 217  ? 13.89100   84.14200  -44.03000 1.000 52.00366  ?  217  PRO   B CD  1 
ATOM   15714 N  N   . ASP   B 1 218  ? 11.80600   86.71000  -42.70100 1.000 44.85453  ?  218  ASP   B N   1 
ATOM   15715 C  CA  . ASP   B 1 218  ? 10.69200   87.37300  -42.04400 1.000 42.67806  ?  218  ASP   B CA  1 
ATOM   15716 C  C   . ASP   B 1 218  ? 10.76700   87.27300  -40.52400 1.000 44.37967  ?  218  ASP   B C   1 
ATOM   15717 O  O   . ASP   B 1 218  ? 9.76600    87.52100  -39.84300 1.000 48.96118  ?  218  ASP   B O   1 
ATOM   15718 C  CB  . ASP   B 1 218  ? 9.37000    86.80700  -42.55800 1.000 31.69790  ?  218  ASP   B CB  1 
ATOM   15719 C  CG  . ASP   B 1 218  ? 9.24900    86.90300  -44.06800 1.000 40.59791  ?  218  ASP   B CG  1 
ATOM   15720 O  OD1 . ASP   B 1 218  ? 9.64800    87.94500  -44.63400 1.000 39.91513  ?  218  ASP   B OD1 1 
ATOM   15721 O  OD2 . ASP   B 1 218  ? 8.76400    85.93600  -44.69000 1.000 55.35531  -1 218  ASP   B OD2 1 
ATOM   15722 N  N   . HIS   B 1 219  ? 11.92800   86.91800  -39.98000 1.000 33.53814  ?  219  HIS   B N   1 
ATOM   15723 C  CA  . HIS   B 1 219  ? 12.11100   86.90200  -38.53600 1.000 37.24441  ?  219  HIS   B CA  1 
ATOM   15724 C  C   . HIS   B 1 219  ? 12.37400   88.30800  -38.01200 1.000 41.36675  ?  219  HIS   B C   1 
ATOM   15725 O  O   . HIS   B 1 219  ? 12.95000   89.15300  -38.70300 1.000 43.61444  ?  219  HIS   B O   1 
ATOM   15726 C  CB  . HIS   B 1 219  ? 13.27200   85.98900  -38.14100 1.000 35.29708  ?  219  HIS   B CB  1 
ATOM   15727 C  CG  . HIS   B 1 219  ? 12.88000   84.55800  -37.95100 1.000 36.86533  ?  219  HIS   B CG  1 
ATOM   15728 N  ND1 . HIS   B 1 219  ? 12.59600   83.71600  -39.00500 1.000 40.18675  ?  219  HIS   B ND1 1 
ATOM   15729 C  CD2 . HIS   B 1 219  ? 12.72900   83.81800  -36.82700 1.000 38.33512  ?  219  HIS   B CD2 1 
ATOM   15730 C  CE1 . HIS   B 1 219  ? 12.28600   82.52000  -38.53800 1.000 39.60376  ?  219  HIS   B CE1 1 
ATOM   15731 N  NE2 . HIS   B 1 219  ? 12.36000   82.55500  -37.21900 1.000 48.92458  ?  219  HIS   B NE2 1 
ATOM   15732 N  N   . VAL   B 1 220  ? 11.95300   88.54900  -36.77200 1.000 30.99418  ?  220  VAL   B N   1 
ATOM   15733 C  CA  . VAL   B 1 220  ? 12.20100   89.84000  -36.14000 1.000 38.25254  ?  220  VAL   B CA  1 
ATOM   15734 C  C   . VAL   B 1 220  ? 13.68400   89.95100  -35.81500 1.000 50.31814  ?  220  VAL   B C   1 
ATOM   15735 O  O   . VAL   B 1 220  ? 14.25200   89.09200  -35.13000 1.000 47.20757  ?  220  VAL   B O   1 
ATOM   15736 C  CB  . VAL   B 1 220  ? 11.34300   90.01000  -34.88100 1.000 32.88457  ?  220  VAL   B CB  1 
ATOM   15737 C  CG1 . VAL   B 1 220  ? 11.32500   91.46900  -34.44800 1.000 34.94083  ?  220  VAL   B CG1 1 
ATOM   15738 C  CG2 . VAL   B 1 220  ? 9.93500    89.49900  -35.12600 1.000 39.63008  ?  220  VAL   B CG2 1 
ATOM   15739 N  N   . ALA   B 1 221  ? 14.31900   91.01100  -36.31000 1.000 44.37319  ?  221  ALA   B N   1 
ATOM   15740 C  CA  . ALA   B 1 221  ? 15.73600   91.25200  -36.07100 1.000 27.33610  ?  221  ALA   B CA  1 
ATOM   15741 C  C   . ALA   B 1 221  ? 15.98600   92.34300  -35.04100 1.000 39.41003  ?  221  ALA   B C   1 
ATOM   15742 O  O   . ALA   B 1 221  ? 16.86100   92.19100  -34.18300 1.000 46.18233  ?  221  ALA   B O   1 
ATOM   15743 C  CB  . ALA   B 1 221  ? 16.43600   91.62500  -37.38100 1.000 32.27827  ?  221  ALA   B CB  1 
ATOM   15744 N  N   . VAL   B 1 222  ? 15.24200   93.44500  -35.11200 1.000 37.59204  ?  222  VAL   B N   1 
ATOM   15745 C  CA  . VAL   B 1 222  ? 15.45200   94.60500  -34.25500 1.000 38.19180  ?  222  VAL   B CA  1 
ATOM   15746 C  C   . VAL   B 1 222  ? 14.10100   95.06100  -33.71700 1.000 45.58439  ?  222  VAL   B C   1 
ATOM   15747 O  O   . VAL   B 1 222  ? 13.09000   94.99800  -34.42600 1.000 41.02445  ?  222  VAL   B O   1 
ATOM   15748 C  CB  . VAL   B 1 222  ? 16.15300   95.74800  -35.02200 1.000 37.18838  ?  222  VAL   B CB  1 
ATOM   15749 C  CG1 . VAL   B 1 222  ? 16.83900   96.68000  -34.06700 1.000 22.89759  ?  222  VAL   B CG1 1 
ATOM   15750 C  CG2 . VAL   B 1 222  ? 17.16000   95.20200  -36.02600 1.000 36.87903  ?  222  VAL   B CG2 1 
ATOM   15751 N  N   . VAL   B 1 223  ? 14.08200   95.51300  -32.46200 1.000 48.16061  ?  223  VAL   B N   1 
ATOM   15752 C  CA  . VAL   B 1 223  ? 12.86400   95.99400  -31.80800 1.000 40.72069  ?  223  VAL   B CA  1 
ATOM   15753 C  C   . VAL   B 1 223  ? 13.20200   97.26400  -31.03700 1.000 42.27566  ?  223  VAL   B C   1 
ATOM   15754 O  O   . VAL   B 1 223  ? 14.06900   97.24500  -30.15600 1.000 47.12123  ?  223  VAL   B O   1 
ATOM   15755 C  CB  . VAL   B 1 223  ? 12.25100   94.94700  -30.85900 1.000 34.39723  ?  223  VAL   B CB  1 
ATOM   15756 C  CG1 . VAL   B 1 223  ? 11.07900   95.54600  -30.09800 1.000 40.29103  ?  223  VAL   B CG1 1 
ATOM   15757 C  CG2 . VAL   B 1 223  ? 11.80700   93.71500  -31.62900 1.000 43.58275  ?  223  VAL   B CG2 1 
ATOM   15758 N  N   . ASP   B 1 224  ? 12.51000   98.36000  -31.35300 1.000 44.16958  ?  224  ASP   B N   1 
ATOM   15759 C  CA  . ASP   B 1 224  ? 12.75500   99.65400  -30.71600 1.000 36.15336  ?  224  ASP   B CA  1 
ATOM   15760 C  C   . ASP   B 1 224  ? 11.42000   100.35800 -30.50600 1.000 55.13006  ?  224  ASP   B C   1 
ATOM   15761 O  O   . ASP   B 1 224  ? 10.76100   100.73900 -31.47800 1.000 62.71355  ?  224  ASP   B O   1 
ATOM   15762 C  CB  . ASP   B 1 224  ? 13.69300   100.51400 -31.56400 1.000 34.58948  ?  224  ASP   B CB  1 
ATOM   15763 C  CG  . ASP   B 1 224  ? 13.93700   101.88600 -30.96200 1.000 56.94007  ?  224  ASP   B CG  1 
ATOM   15764 O  OD1 . ASP   B 1 224  ? 13.83100   102.02700 -29.72500 1.000 58.45079  ?  224  ASP   B OD1 1 
ATOM   15765 O  OD2 . ASP   B 1 224  ? 14.22800   102.82800 -31.73100 1.000 56.31659  -1 224  ASP   B OD2 1 
ATOM   15766 N  N   . ARG   B 1 225  ? 11.03400   100.53200 -29.23900 1.000 66.86563  ?  225  ARG   B N   1 
ATOM   15767 C  CA  . ARG   B 1 225  ? 9.83600    101.28400 -28.85600 1.000 52.51446  ?  225  ARG   B CA  1 
ATOM   15768 C  C   . ARG   B 1 225  ? 8.58900    100.73500 -29.54200 1.000 59.45664  ?  225  ARG   B C   1 
ATOM   15769 O  O   . ARG   B 1 225  ? 7.81100    101.46700 -30.15800 1.000 79.73164  ?  225  ARG   B O   1 
ATOM   15770 C  CB  . ARG   B 1 225  ? 10.00600   102.77500 -29.14900 1.000 67.65094  ?  225  ARG   B CB  1 
ATOM   15771 C  CG  . ARG   B 1 225  ? 10.76900   103.52200 -28.08000 1.000 72.31978  ?  225  ARG   B CG  1 
ATOM   15772 C  CD  . ARG   B 1 225  ? 11.61300   104.61000 -28.69700 1.000 79.01834  ?  225  ARG   B CD  1 
ATOM   15773 N  NE  . ARG   B 1 225  ? 12.83000   104.82900 -27.92900 1.000 76.62268  ?  225  ARG   B NE  1 
ATOM   15774 C  CZ  . ARG   B 1 225  ? 13.96300   105.28800 -28.44100 1.000 77.89433  ?  225  ARG   B CZ  1 
ATOM   15775 N  NH1 . ARG   B 1 225  ? 14.07000   105.59000 -29.72500 1.000 70.80620  ?  225  ARG   B NH1 1 
ATOM   15776 N  NH2 . ARG   B 1 225  ? 15.01900   105.43900 -27.64700 1.000 83.90235  ?  225  ARG   B NH2 1 
ATOM   15777 N  N   . GLY   B 1 226  ? 8.40800    99.42200  -29.43500 1.000 52.35409  ?  226  GLY   B N   1 
ATOM   15778 C  CA  . GLY   B 1 226  ? 7.25900    98.76400  -30.01000 1.000 64.30987  ?  226  GLY   B CA  1 
ATOM   15779 C  C   . GLY   B 1 226  ? 7.27300    98.61800  -31.51700 1.000 68.72670  ?  226  GLY   B C   1 
ATOM   15780 O  O   . GLY   B 1 226  ? 6.44900    97.86600  -32.05100 1.000 70.37158  ?  226  GLY   B O   1 
ATOM   15781 N  N   . GLN   B 1 227  ? 8.16300    99.30600  -32.22500 1.000 60.35490  ?  227  GLN   B N   1 
ATOM   15782 C  CA  . GLN   B 1 227  ? 8.32000    99.10900  -33.65900 1.000 48.63672  ?  227  GLN   B CA  1 
ATOM   15783 C  C   . GLN   B 1 227  ? 9.36500    98.03000  -33.91700 1.000 48.54482  ?  227  GLN   B C   1 
ATOM   15784 O  O   . GLN   B 1 227  ? 10.24900   97.79000  -33.09200 1.000 54.98016  ?  227  GLN   B O   1 
ATOM   15785 C  CB  . GLN   B 1 227  ? 8.72200    100.41300 -34.34900 1.000 55.41662  ?  227  GLN   B CB  1 
ATOM   15786 C  CG  . GLN   B 1 227  ? 7.94400    101.62000 -33.86200 1.000 69.98507  ?  227  GLN   B CG  1 
ATOM   15787 C  CD  . GLN   B 1 227  ? 7.52700    102.54300 -34.98600 1.000 92.53394  ?  227  GLN   B CD  1 
ATOM   15788 O  OE1 . GLN   B 1 227  ? 6.67000    102.20000 -35.80100 1.000 92.37637  ?  227  GLN   B OE1 1 
ATOM   15789 N  NE2 . GLN   B 1 227  ? 8.12800    103.72500 -35.03400 1.000 106.35364 ?  227  GLN   B NE2 1 
ATOM   15790 N  N   . SER   B 1 228  ? 9.25600    97.37300  -35.07100 1.000 35.05259  ?  228  SER   B N   1 
ATOM   15791 C  CA  . SER   B 1 228  ? 10.10000   96.22300  -35.36100 1.000 34.32954  ?  228  SER   B CA  1 
ATOM   15792 C  C   . SER   B 1 228  ? 10.61300   96.27900  -36.79400 1.000 49.29515  ?  228  SER   B C   1 
ATOM   15793 O  O   . SER   B 1 228  ? 10.08700   97.00300  -37.64300 1.000 54.99539  ?  228  SER   B O   1 
ATOM   15794 C  CB  . SER   B 1 228  ? 9.34900    94.90700  -35.12900 1.000 28.99496  ?  228  SER   B CB  1 
ATOM   15795 O  OG  . SER   B 1 228  ? 8.91000    94.81000  -33.78800 1.000 41.70233  ?  228  SER   B OG  1 
ATOM   15796 N  N   . LEU   B 1 229  ? 11.65800   95.49000  -37.04600 1.000 48.18889  ?  229  LEU   B N   1 
ATOM   15797 C  CA  . LEU   B 1 229  ? 12.25800   95.34400  -38.36600 1.000 33.13329  ?  229  LEU   B CA  1 
ATOM   15798 C  C   . LEU   B 1 229  ? 12.59300   93.88000  -38.59100 1.000 37.07647  ?  229  LEU   B C   1 
ATOM   15799 O  O   . LEU   B 1 229  ? 13.29400   93.27300  -37.77600 1.000 40.00576  ?  229  LEU   B O   1 
ATOM   15800 C  CB  . LEU   B 1 229  ? 13.53000   96.18900  -38.50400 1.000 31.29223  ?  229  LEU   B CB  1 
ATOM   15801 C  CG  . LEU   B 1 229  ? 13.38900   97.68500  -38.77000 1.000 35.47474  ?  229  LEU   B CG  1 
ATOM   15802 C  CD1 . LEU   B 1 229  ? 14.76100   98.33900  -38.79100 1.000 29.96151  ?  229  LEU   B CD1 1 
ATOM   15803 C  CD2 . LEU   B 1 229  ? 12.66700   97.91400  -40.08300 1.000 45.25260  ?  229  LEU   B CD2 1 
ATOM   15804 N  N   . THR   B 1 230  ? 12.09700   93.31400  -39.68700 1.000 41.07723  ?  230  THR   B N   1 
ATOM   15805 C  CA  . THR   B 1 230  ? 12.48000   91.95600  -40.03100 1.000 36.09576  ?  230  THR   B CA  1 
ATOM   15806 C  C   . THR   B 1 230  ? 13.87800   91.94500  -40.63900 1.000 40.22778  ?  230  THR   B C   1 
ATOM   15807 O  O   . THR   B 1 230  ? 14.40200   92.97600  -41.07200 1.000 41.14771  ?  230  THR   B O   1 
ATOM   15808 C  CB  . THR   B 1 230  ? 11.48200   91.32900  -41.00600 1.000 42.90468  ?  230  THR   B CB  1 
ATOM   15809 O  OG1 . THR   B 1 230  ? 11.52800   92.02600  -42.25600 1.000 46.66039  ?  230  THR   B OG1 1 
ATOM   15810 C  CG2 . THR   B 1 230  ? 10.07200   91.39500  -40.44400 1.000 46.59139  ?  230  THR   B CG2 1 
ATOM   15811 N  N   . TYR   B 1 231  ? 14.48700   90.75600  -40.65800 1.000 41.96375  ?  231  TYR   B N   1 
ATOM   15812 C  CA  . TYR   B 1 231  ? 15.82100   90.61800  -41.23600 1.000 42.44625  ?  231  TYR   B CA  1 
ATOM   15813 C  C   . TYR   B 1 231  ? 15.84600   91.08400  -42.68500 1.000 42.16739  ?  231  TYR   B C   1 
ATOM   15814 O  O   . TYR   B 1 231  ? 16.81600   91.70900  -43.12900 1.000 47.21090  ?  231  TYR   B O   1 
ATOM   15815 C  CB  . TYR   B 1 231  ? 16.29400   89.16800  -41.13500 1.000 37.26680  ?  231  TYR   B CB  1 
ATOM   15816 C  CG  . TYR   B 1 231  ? 16.97000   88.82200  -39.82900 1.000 33.51131  ?  231  TYR   B CG  1 
ATOM   15817 C  CD1 . TYR   B 1 231  ? 16.23200   88.39400  -38.73300 1.000 48.40618  ?  231  TYR   B CD1 1 
ATOM   15818 C  CD2 . TYR   B 1 231  ? 18.34800   88.91500  -39.69400 1.000 32.73391  ?  231  TYR   B CD2 1 
ATOM   15819 C  CE1 . TYR   B 1 231  ? 16.84900   88.07500  -37.53800 1.000 52.20421  ?  231  TYR   B CE1 1 
ATOM   15820 C  CE2 . TYR   B 1 231  ? 18.97300   88.59800  -38.50500 1.000 30.33943  ?  231  TYR   B CE2 1 
ATOM   15821 C  CZ  . TYR   B 1 231  ? 18.21900   88.17900  -37.43000 1.000 39.87403  ?  231  TYR   B CZ  1 
ATOM   15822 O  OH  . TYR   B 1 231  ? 18.83700   87.86400  -36.24200 1.000 35.05667  ?  231  TYR   B OH  1 
ATOM   15823 N  N   . LYS   B 1 232  ? 14.78400   90.78900  -43.43700 1.000 38.74666  ?  232  LYS   B N   1 
ATOM   15824 C  CA  . LYS   B 1 232  ? 14.70100   91.25700  -44.81600 1.000 40.09327  ?  232  LYS   B CA  1 
ATOM   15825 C  C   . LYS   B 1 232  ? 14.57700   92.77500  -44.87400 1.000 39.45172  ?  232  LYS   B C   1 
ATOM   15826 O  O   . LYS   B 1 232  ? 15.17400   93.41900  -45.74400 1.000 51.61046  ?  232  LYS   B O   1 
ATOM   15827 C  CB  . LYS   B 1 232  ? 13.52100   90.58300  -45.51700 1.000 29.85837  ?  232  LYS   B CB  1 
ATOM   15828 C  CG  . LYS   B 1 232  ? 13.26000   91.04400  -46.94100 1.000 44.88763  ?  232  LYS   B CG  1 
ATOM   15829 C  CD  . LYS   B 1 232  ? 12.17300   90.19000  -47.57800 1.000 48.64530  ?  232  LYS   B CD  1 
ATOM   15830 C  CE  . LYS   B 1 232  ? 11.43300   90.93400  -48.67800 1.000 53.96272  ?  232  LYS   B CE  1 
ATOM   15831 N  NZ  . LYS   B 1 232  ? 12.28400   91.19800  -49.86900 1.000 68.33976  ?  232  LYS   B NZ  1 
ATOM   15832 N  N   . GLN   B 1 233  ? 13.82500   93.36500  -43.94300 1.000 34.08560  ?  233  GLN   B N   1 
ATOM   15833 C  CA  . GLN   B 1 233  ? 13.64500   94.81300  -43.94500 1.000 37.85300  ?  233  GLN   B CA  1 
ATOM   15834 C  C   . GLN   B 1 233  ? 14.91300   95.53300  -43.50500 1.000 35.64206  ?  233  GLN   B C   1 
ATOM   15835 O  O   . GLN   B 1 233  ? 15.24400   96.59800  -44.03800 1.000 41.09476  ?  233  GLN   B O   1 
ATOM   15836 C  CB  . GLN   B 1 233  ? 12.47000   95.19200  -43.04800 1.000 33.90602  ?  233  GLN   B CB  1 
ATOM   15837 C  CG  . GLN   B 1 233  ? 11.12000   94.81300  -43.62800 1.000 44.07410  ?  233  GLN   B CG  1 
ATOM   15838 C  CD  . GLN   B 1 233  ? 10.03900   94.74200  -42.57300 1.000 46.40222  ?  233  GLN   B CD  1 
ATOM   15839 O  OE1 . GLN   B 1 233  ? 10.32500   94.72000  -41.37500 1.000 39.09623  ?  233  GLN   B OE1 1 
ATOM   15840 N  NE2 . GLN   B 1 233  ? 8.78600    94.71000  -43.01000 1.000 48.58115  ?  233  GLN   B NE2 1 
ATOM   15841 N  N   . LEU   B 1 234  ? 15.63000   94.97000  -42.53000 1.000 44.29352  ?  234  LEU   B N   1 
ATOM   15842 C  CA  . LEU   B 1 234  ? 16.88600   95.57400  -42.09900 1.000 45.52543  ?  234  LEU   B CA  1 
ATOM   15843 C  C   . LEU   B 1 234  ? 17.92700   95.52400  -43.20900 1.000 48.50486  ?  234  LEU   B C   1 
ATOM   15844 O  O   . LEU   B 1 234  ? 18.66500   96.49400  -43.42300 1.000 42.47379  ?  234  LEU   B O   1 
ATOM   15845 C  CB  . LEU   B 1 234  ? 17.40200   94.87100  -40.84300 1.000 37.86744  ?  234  LEU   B CB  1 
ATOM   15846 C  CG  . LEU   B 1 234  ? 18.77000   95.30800  -40.31500 1.000 37.89079  ?  234  LEU   B CG  1 
ATOM   15847 C  CD1 . LEU   B 1 234  ? 18.79100   96.79900  -40.01600 1.000 25.03492  ?  234  LEU   B CD1 1 
ATOM   15848 C  CD2 . LEU   B 1 234  ? 19.14400   94.50300  -39.07900 1.000 24.88503  ?  234  LEU   B CD2 1 
ATOM   15849 N  N   . ASN   B 1 235  ? 17.99200   94.40500  -43.93300 1.000 38.82866  ?  235  ASN   B N   1 
ATOM   15850 C  CA  . ASN   B 1 235  ? 18.96000   94.27200  -45.01600 1.000 39.08583  ?  235  ASN   B CA  1 
ATOM   15851 C  C   . ASN   B 1 235  ? 18.67900   95.27600  -46.12600 1.000 46.70882  ?  235  ASN   B C   1 
ATOM   15852 O  O   . ASN   B 1 235  ? 19.59100   95.95800  -46.60800 1.000 50.70496  ?  235  ASN   B O   1 
ATOM   15853 C  CB  . ASN   B 1 235  ? 18.93400   92.84400  -45.56200 1.000 46.28806  ?  235  ASN   B CB  1 
ATOM   15854 C  CG  . ASN   B 1 235  ? 20.30200   92.36300  -45.99500 1.000 55.91997  ?  235  ASN   B CG  1 
ATOM   15855 O  OD1 . ASN   B 1 235  ? 21.29500   92.57300  -45.29900 1.000 60.57213  ?  235  ASN   B OD1 1 
ATOM   15856 N  ND2 . ASN   B 1 235  ? 20.36300   91.71600  -47.15300 1.000 50.55791  ?  235  ASN   B ND2 1 
ATOM   15857 N  N   . GLU   B 1 236  ? 17.41300   95.38500  -46.53800 1.000 50.61461  ?  236  GLU   B N   1 
ATOM   15858 C  CA  . GLU   B 1 236  ? 17.06200   96.27600  -47.64000 1.000 34.57324  ?  236  GLU   B CA  1 
ATOM   15859 C  C   . GLU   B 1 236  ? 17.30500   97.73500  -47.27500 1.000 41.75854  ?  236  GLU   B C   1 
ATOM   15860 O  O   . GLU   B 1 236  ? 17.82000   98.50800  -48.09200 1.000 39.25760  ?  236  GLU   B O   1 
ATOM   15861 C  CB  . GLU   B 1 236  ? 15.60400   96.06100  -48.04300 1.000 37.09541  ?  236  GLU   B CB  1 
ATOM   15862 C  CG  . GLU   B 1 236  ? 15.32600   94.69100  -48.64100 1.000 39.97921  ?  236  GLU   B CG  1 
ATOM   15863 C  CD  . GLU   B 1 236  ? 13.85400   94.46500  -48.92700 1.000 48.70496  ?  236  GLU   B CD  1 
ATOM   15864 O  OE1 . GLU   B 1 236  ? 13.01700   95.25100  -48.43300 1.000 52.72310  ?  236  GLU   B OE1 1 
ATOM   15865 O  OE2 . GLU   B 1 236  ? 13.53400   93.49800  -49.65000 1.000 63.67934  -1 236  GLU   B OE2 1 
ATOM   15866 N  N   . ARG   B 1 237  ? 16.94300   98.13100  -46.05200 1.000 39.48169  ?  237  ARG   B N   1 
ATOM   15867 C  CA  . ARG   B 1 237  ? 17.15500   99.51400  -45.63800 1.000 41.65313  ?  237  ARG   B CA  1 
ATOM   15868 C  C   . ARG   B 1 237  ? 18.63700   99.83900  -45.51000 1.000 51.67099  ?  237  ARG   B C   1 
ATOM   15869 O  O   . ARG   B 1 237  ? 19.04800   100.97100 -45.79000 1.000 52.69852  ?  237  ARG   B O   1 
ATOM   15870 C  CB  . ARG   B 1 237  ? 16.43200   99.78700  -44.31900 1.000 37.80895  ?  237  ARG   B CB  1 
ATOM   15871 C  CG  . ARG   B 1 237  ? 16.19800   101.26200 -44.03800 1.000 49.44785  ?  237  ARG   B CG  1 
ATOM   15872 C  CD  . ARG   B 1 237  ? 15.46400   101.93000 -45.19500 1.000 68.20400  ?  237  ARG   B CD  1 
ATOM   15873 N  NE  . ARG   B 1 237  ? 15.04300   103.28900 -44.87500 1.000 69.85043  ?  237  ARG   B NE  1 
ATOM   15874 C  CZ  . ARG   B 1 237  ? 14.47900   104.12200 -45.74000 1.000 60.33515  ?  237  ARG   B CZ  1 
ATOM   15875 N  NH1 . ARG   B 1 237  ? 14.26600   103.77200 -46.99900 1.000 54.78750  ?  237  ARG   B NH1 1 
ATOM   15876 N  NH2 . ARG   B 1 237  ? 14.12200   105.33700 -45.33300 1.000 66.57478  ?  237  ARG   B NH2 1 
ATOM   15877 N  N   . ALA   B 1 238  ? 19.45200   98.86700  -45.09300 1.000 48.88850  ?  238  ALA   B N   1 
ATOM   15878 C  CA  . ALA   B 1 238  ? 20.89100   99.09300  -45.02900 1.000 38.77320  ?  238  ALA   B CA  1 
ATOM   15879 C  C   . ALA   B 1 238  ? 21.49900   99.16100  -46.42300 1.000 49.86560  ?  238  ALA   B C   1 
ATOM   15880 O  O   . ALA   B 1 238  ? 22.38800   99.98100  -46.67900 1.000 56.47964  ?  238  ALA   B O   1 
ATOM   15881 C  CB  . ALA   B 1 238  ? 21.56200   97.99600  -44.20300 1.000 33.41628  ?  238  ALA   B CB  1 
ATOM   15882 N  N   . ASN   B 1 239  ? 21.03000   98.30800  -47.33800 1.000 43.24186  ?  239  ASN   B N   1 
ATOM   15883 C  CA  . ASN   B 1 239  ? 21.55000   98.32000  -48.70100 1.000 43.73088  ?  239  ASN   B CA  1 
ATOM   15884 C  C   . ASN   B 1 239  ? 21.25800   99.64100  -49.40100 1.000 50.97870  ?  239  ASN   B C   1 
ATOM   15885 O  O   . ASN   B 1 239  ? 22.05500   100.09000 -50.23300 1.000 58.75661  ?  239  ASN   B O   1 
ATOM   15886 C  CB  . ASN   B 1 239  ? 20.96300   97.15400  -49.49700 1.000 36.39088  ?  239  ASN   B CB  1 
ATOM   15887 C  CG  . ASN   B 1 239  ? 21.44700   95.80600  -48.99900 1.000 40.61586  ?  239  ASN   B CG  1 
ATOM   15888 O  OD1 . ASN   B 1 239  ? 22.59800   95.65900  -48.59100 1.000 62.75363  ?  239  ASN   B OD1 1 
ATOM   15889 N  ND2 . ASN   B 1 239  ? 20.56600   94.81200  -49.02800 1.000 49.00934  ?  239  ASN   B ND2 1 
ATOM   15890 N  N   . GLN   B 1 240  ? 20.12800   100.27400 -49.08200 1.000 48.71484  ?  240  GLN   B N   1 
ATOM   15891 C  CA  . GLN   B 1 240  ? 19.82500   101.58000 -49.65900 1.000 49.14115  ?  240  GLN   B CA  1 
ATOM   15892 C  C   . GLN   B 1 240  ? 20.83500   102.62200 -49.20000 1.000 48.09565  ?  240  GLN   B C   1 
ATOM   15893 O  O   . GLN   B 1 240  ? 21.41200   103.35000 -50.01700 1.000 59.51223  ?  240  GLN   B O   1 
ATOM   15894 C  CB  . GLN   B 1 240  ? 18.40400   102.00100 -49.28600 1.000 55.68386  ?  240  GLN   B CB  1 
ATOM   15895 C  CG  . GLN   B 1 240  ? 17.32000   101.08700 -49.83300 1.000 57.50208  ?  240  GLN   B CG  1 
ATOM   15896 C  CD  . GLN   B 1 240  ? 15.94700   101.40700 -49.27300 1.000 51.62519  ?  240  GLN   B CD  1 
ATOM   15897 O  OE1 . GLN   B 1 240  ? 15.56300   102.57200 -49.16400 1.000 48.74737  ?  240  GLN   B OE1 1 
ATOM   15898 N  NE2 . GLN   B 1 240  ? 15.20200   100.37100 -48.90800 1.000 41.47488  ?  240  GLN   B NE2 1 
ATOM   15899 N  N   . LEU   B 1 241  ? 21.06600   102.70500 -47.88700 1.000 48.02253  ?  241  LEU   B N   1 
ATOM   15900 C  CA  . LEU   B 1 241  ? 22.05800   103.64000 -47.36900 1.000 51.78163  ?  241  LEU   B CA  1 
ATOM   15901 C  C   . LEU   B 1 241  ? 23.46600   103.26400 -47.81500 1.000 54.05345  ?  241  LEU   B C   1 
ATOM   15902 O  O   . LEU   B 1 241  ? 24.31700   104.14500 -47.98400 1.000 51.52312  ?  241  LEU   B O   1 
ATOM   15903 C  CB  . LEU   B 1 241  ? 21.97700   103.69400 -45.84200 1.000 33.92321  ?  241  LEU   B CB  1 
ATOM   15904 C  CG  . LEU   B 1 241  ? 22.81700   104.75700 -45.12900 1.000 35.68073  ?  241  LEU   B CG  1 
ATOM   15905 C  CD1 . LEU   B 1 241  ? 22.37700   106.15600 -45.53100 1.000 44.02088  ?  241  LEU   B CD1 1 
ATOM   15906 C  CD2 . LEU   B 1 241  ? 22.73500   104.58300 -43.62200 1.000 43.26613  ?  241  LEU   B CD2 1 
ATOM   15907 N  N   . ALA   B 1 242  ? 23.72700   101.97000 -48.02000 1.000 52.36733  ?  242  ALA   B N   1 
ATOM   15908 C  CA  . ALA   B 1 242  ? 25.05800   101.54300 -48.43900 1.000 49.81725  ?  242  ALA   B CA  1 
ATOM   15909 C  C   . ALA   B 1 242  ? 25.31700   101.89100 -49.89900 1.000 45.92939  ?  242  ALA   B C   1 
ATOM   15910 O  O   . ALA   B 1 242  ? 26.42500   102.31000 -50.25300 1.000 48.67388  ?  242  ALA   B O   1 
ATOM   15911 C  CB  . ALA   B 1 242  ? 25.23000   100.04500 -48.20000 1.000 45.46077  ?  242  ALA   B CB  1 
ATOM   15912 N  N   . HIS   B 1 243  ? 24.31300   101.71000 -50.76400 1.000 45.20923  ?  243  HIS   B N   1 
ATOM   15913 C  CA  . HIS   B 1 243  ? 24.43200   102.18600 -52.13900 1.000 48.94920  ?  243  HIS   B CA  1 
ATOM   15914 C  C   . HIS   B 1 243  ? 24.73700   103.67700 -52.17200 1.000 49.61834  ?  243  HIS   B C   1 
ATOM   15915 O  O   . HIS   B 1 243  ? 25.57800   104.13300 -52.95600 1.000 51.02344  ?  243  HIS   B O   1 
ATOM   15916 C  CB  . HIS   B 1 243  ? 23.14900   101.89200 -52.91800 1.000 44.83398  ?  243  HIS   B CB  1 
ATOM   15917 C  CG  . HIS   B 1 243  ? 23.10200   100.52400 -53.52500 1.000 47.70862  ?  243  HIS   B CG  1 
ATOM   15918 N  ND1 . HIS   B 1 243  ? 22.47100   99.46000  -52.91700 1.000 43.40814  ?  243  HIS   B ND1 1 
ATOM   15919 C  CD2 . HIS   B 1 243  ? 23.59500   100.05100 -54.69400 1.000 54.13129  ?  243  HIS   B CD2 1 
ATOM   15920 C  CE1 . HIS   B 1 243  ? 22.58400   98.38800  -53.68300 1.000 40.03808  ?  243  HIS   B CE1 1 
ATOM   15921 N  NE2 . HIS   B 1 243  ? 23.26200   98.72000  -54.76600 1.000 56.88250  ?  243  HIS   B NE2 1 
ATOM   15922 N  N   . HIS   B 1 244  ? 24.06200   104.45100 -51.32100 1.000 33.54607  ?  244  HIS   B N   1 
ATOM   15923 C  CA  . HIS   B 1 244  ? 24.33700   105.88000 -51.23300 1.000 42.45435  ?  244  HIS   B CA  1 
ATOM   15924 C  C   . HIS   B 1 244  ? 25.73600   106.14000 -50.68500 1.000 57.45487  ?  244  HIS   B C   1 
ATOM   15925 O  O   . HIS   B 1 244  ? 26.45300   107.01100 -51.18900 1.000 58.95794  ?  244  HIS   B O   1 
ATOM   15926 C  CB  . HIS   B 1 244  ? 23.28000   106.55600 -50.36100 1.000 38.82015  ?  244  HIS   B CB  1 
ATOM   15927 C  CG  . HIS   B 1 244  ? 23.48600   108.02800 -50.18700 1.000 44.49427  ?  244  HIS   B CG  1 
ATOM   15928 N  ND1 . HIS   B 1 244  ? 22.90700   108.96400 -51.01600 1.000 42.15891  ?  244  HIS   B ND1 1 
ATOM   15929 C  CD2 . HIS   B 1 244  ? 24.20600   108.72600 -49.27700 1.000 57.16203  ?  244  HIS   B CD2 1 
ATOM   15930 C  CE1 . HIS   B 1 244  ? 23.26100   110.17500 -50.62500 1.000 54.65306  ?  244  HIS   B CE1 1 
ATOM   15931 N  NE2 . HIS   B 1 244  ? 24.05100   110.05800 -49.57200 1.000 48.38983  ?  244  HIS   B NE2 1 
ATOM   15932 N  N   . LEU   B 1 245  ? 26.14300   105.38800 -49.65800 1.000 51.32379  ?  245  LEU   B N   1 
ATOM   15933 C  CA  . LEU   B 1 245  ? 27.45200   105.60400 -49.05000 1.000 45.80736  ?  245  LEU   B CA  1 
ATOM   15934 C  C   . LEU   B 1 245  ? 28.57600   105.25400 -50.01700 1.000 43.57246  ?  245  LEU   B C   1 
ATOM   15935 O  O   . LEU   B 1 245  ? 29.54500   106.01000 -50.15600 1.000 42.47793  ?  245  LEU   B O   1 
ATOM   15936 C  CB  . LEU   B 1 245  ? 27.58000   104.78800 -47.76300 1.000 51.96139  ?  245  LEU   B CB  1 
ATOM   15937 C  CG  . LEU   B 1 245  ? 27.00000   105.40900 -46.49200 1.000 43.39280  ?  245  LEU   B CG  1 
ATOM   15938 C  CD1 . LEU   B 1 245  ? 27.26200   104.50600 -45.29900 1.000 31.84715  ?  245  LEU   B CD1 1 
ATOM   15939 C  CD2 . LEU   B 1 245  ? 27.58300   106.79400 -46.25900 1.000 45.61328  ?  245  LEU   B CD2 1 
ATOM   15940 N  N   . ARG   B 1 246  ? 28.46700   104.10700 -50.69300 1.000 49.47856  ?  246  ARG   B N   1 
ATOM   15941 C  CA  . ARG   B 1 246  ? 29.50700   103.71500 -51.63800 1.000 46.47742  ?  246  ARG   B CA  1 
ATOM   15942 C  C   . ARG   B 1 246  ? 29.61500   104.70500 -52.79100 1.000 51.39582  ?  246  ARG   B C   1 
ATOM   15943 O  O   . ARG   B 1 246  ? 30.71800   104.96100 -53.28800 1.000 62.90982  ?  246  ARG   B O   1 
ATOM   15944 C  CB  . ARG   B 1 246  ? 29.23600   102.30300 -52.16200 1.000 29.51721  ?  246  ARG   B CB  1 
ATOM   15945 C  CG  . ARG   B 1 246  ? 30.41900   101.67700 -52.88600 1.000 29.17412  ?  246  ARG   B CG  1 
ATOM   15946 C  CD  . ARG   B 1 246  ? 30.12300   100.25500 -53.35000 1.000 28.73670  ?  246  ARG   B CD  1 
ATOM   15947 N  NE  . ARG   B 1 246  ? 30.20500   99.27900  -52.26800 1.000 26.18530  ?  246  ARG   B NE  1 
ATOM   15948 C  CZ  . ARG   B 1 246  ? 30.17900   97.96500  -52.44300 1.000 28.71020  ?  246  ARG   B CZ  1 
ATOM   15949 N  NH1 . ARG   B 1 246  ? 30.07800   97.43000  -53.64900 1.000 34.93225  ?  246  ARG   B NH1 1 
ATOM   15950 N  NH2 . ARG   B 1 246  ? 30.25900   97.16700  -51.38300 1.000 41.21779  ?  246  ARG   B NH2 1 
ATOM   15951 N  N   . GLY   B 1 247  ? 28.49100   105.28500 -53.21900 1.000 51.60050  ?  247  GLY   B N   1 
ATOM   15952 C  CA  . GLY   B 1 247  ? 28.53800   106.28900 -54.26600 1.000 44.58065  ?  247  GLY   B CA  1 
ATOM   15953 C  C   . GLY   B 1 247  ? 29.19900   107.57900 -53.82800 1.000 46.47030  ?  247  GLY   B C   1 
ATOM   15954 O  O   . GLY   B 1 247  ? 29.73700   108.31600 -54.66000 1.000 71.25889  ?  247  GLY   B O   1 
ATOM   15955 N  N   . LYS   B 1 248  ? 29.16800   107.87600 -52.52900 1.000 41.50124  ?  248  LYS   B N   1 
ATOM   15956 C  CA  . LYS   B 1 248  ? 29.82000   109.07000 -52.00800 1.000 48.66146  ?  248  LYS   B CA  1 
ATOM   15957 C  C   . LYS   B 1 248  ? 31.32700   108.90400 -51.85800 1.000 52.68764  ?  248  LYS   B C   1 
ATOM   15958 O  O   . LYS   B 1 248  ? 32.01600   109.89300 -51.58800 1.000 59.14199  ?  248  LYS   B O   1 
ATOM   15959 C  CB  . LYS   B 1 248  ? 29.20800   109.46000 -50.66000 1.000 48.52133  ?  248  LYS   B CB  1 
ATOM   15960 C  CG  . LYS   B 1 248  ? 27.74200   109.86300 -50.73200 1.000 60.76164  ?  248  LYS   B CG  1 
ATOM   15961 C  CD  . LYS   B 1 248  ? 27.56900   111.34100 -51.04400 1.000 58.61125  ?  248  LYS   B CD  1 
ATOM   15962 C  CE  . LYS   B 1 248  ? 28.08600   112.20400 -49.90400 1.000 59.23696  ?  248  LYS   B CE  1 
ATOM   15963 N  NZ  . LYS   B 1 248  ? 27.59800   113.60900 -49.99800 1.000 61.36564  ?  248  LYS   B NZ  1 
ATOM   15964 N  N   . GLY   B 1 249  ? 31.85200   107.69000 -52.01800 1.000 43.04039  ?  249  GLY   B N   1 
ATOM   15965 C  CA  . GLY   B 1 249  ? 33.28700   107.48600 -52.00700 1.000 56.87318  ?  249  GLY   B CA  1 
ATOM   15966 C  C   . GLY   B 1 249  ? 33.78800   106.45700 -51.01400 1.000 62.17444  ?  249  GLY   B C   1 
ATOM   15967 O  O   . GLY   B 1 249  ? 34.99500   106.21200 -50.93200 1.000 64.20580  ?  249  GLY   B O   1 
ATOM   15968 N  N   . VAL   B 1 250  ? 32.87700   105.84500 -50.25500 1.000 57.79037  ?  250  VAL   B N   1 
ATOM   15969 C  CA  . VAL   B 1 250  ? 33.28300   104.88000 -49.23800 1.000 46.55737  ?  250  VAL   B CA  1 
ATOM   15970 C  C   . VAL   B 1 250  ? 33.94200   103.68400 -49.91000 1.000 47.45480  ?  250  VAL   B C   1 
ATOM   15971 O  O   . VAL   B 1 250  ? 33.30900   102.96100 -50.69000 1.000 45.67234  ?  250  VAL   B O   1 
ATOM   15972 C  CB  . VAL   B 1 250  ? 32.08500   104.45800 -48.38400 1.000 32.17756  ?  250  VAL   B CB  1 
ATOM   15973 C  CG1 . VAL   B 1 250  ? 32.48000   103.32700 -47.44500 1.000 37.03502  ?  250  VAL   B CG1 1 
ATOM   15974 C  CG2 . VAL   B 1 250  ? 31.55300   105.65000 -47.59900 1.000 21.13883  ?  250  VAL   B CG2 1 
ATOM   15975 N  N   . LYS   B 1 251  ? 35.21900   103.47600 -49.61500 1.000 41.95414  ?  251  LYS   B N   1 
ATOM   15976 C  CA  . LYS   B 1 251  ? 36.02200   102.38400 -50.13900 1.000 39.45025  ?  251  LYS   B CA  1 
ATOM   15977 C  C   . LYS   B 1 251  ? 36.53600   101.52700 -48.98700 1.000 32.66389  ?  251  LYS   B C   1 
ATOM   15978 O  O   . LYS   B 1 251  ? 36.49400   101.95300 -47.82600 1.000 34.93785  ?  251  LYS   B O   1 
ATOM   15979 C  CB  . LYS   B 1 251  ? 37.19800   102.92700 -50.96600 1.000 49.27214  ?  251  LYS   B CB  1 
ATOM   15980 C  CG  . LYS   B 1 251  ? 37.04300   102.73100 -52.47200 1.000 54.41798  ?  251  LYS   B CG  1 
ATOM   15981 C  CD  . LYS   B 1 251  ? 36.75500   104.04200 -53.19100 1.000 64.54286  ?  251  LYS   B CD  1 
ATOM   15982 C  CE  . LYS   B 1 251  ? 36.58100   103.82400 -54.68900 1.000 55.71500  ?  251  LYS   B CE  1 
ATOM   15983 N  NZ  . LYS   B 1 251  ? 36.20300   105.07700 -55.40300 1.000 55.02764  ?  251  LYS   B NZ  1 
ATOM   15984 N  N   . PRO   B 1 252  ? 37.00000   100.30500 -49.26300 1.000 29.24824  ?  252  PRO   B N   1 
ATOM   15985 C  CA  . PRO   B 1 252  ? 37.48600   99.43800  -48.18000 1.000 33.35080  ?  252  PRO   B CA  1 
ATOM   15986 C  C   . PRO   B 1 252  ? 38.53700   100.11800 -47.31100 1.000 38.59543  ?  252  PRO   B C   1 
ATOM   15987 O  O   . PRO   B 1 252  ? 39.38000   100.87600 -47.79500 1.000 38.46234  ?  252  PRO   B O   1 
ATOM   15988 C  CB  . PRO   B 1 252  ? 38.06600   98.23700  -48.93200 1.000 33.95546  ?  252  PRO   B CB  1 
ATOM   15989 C  CG  . PRO   B 1 252  ? 37.23000   98.14800  -50.15400 1.000 38.09384  ?  252  PRO   B CG  1 
ATOM   15990 C  CD  . PRO   B 1 252  ? 36.91000   99.57300  -50.54100 1.000 42.18352  ?  252  PRO   B CD  1 
ATOM   15991 N  N   . ASP   B 1 253  ? 38.46100   99.84100  -46.00700 1.000 41.43045  ?  253  ASP   B N   1 
ATOM   15992 C  CA  . ASP   B 1 253  ? 39.29400   100.38600 -44.93500 1.000 38.17853  ?  253  ASP   B CA  1 
ATOM   15993 C  C   . ASP   B 1 253  ? 39.03600   101.86300 -44.66100 1.000 40.45078  ?  253  ASP   B C   1 
ATOM   15994 O  O   . ASP   B 1 253  ? 39.68800   102.42900 -43.77400 1.000 33.65617  ?  253  ASP   B O   1 
ATOM   15995 C  CB  . ASP   B 1 253  ? 40.79600   100.18300 -45.18500 1.000 46.99674  ?  253  ASP   B CB  1 
ATOM   15996 C  CG  . ASP   B 1 253  ? 41.34300   98.95500  -44.48200 1.000 44.52937  ?  253  ASP   B CG  1 
ATOM   15997 O  OD1 . ASP   B 1 253  ? 40.61700   98.36700  -43.65300 1.000 44.99970  ?  253  ASP   B OD1 1 
ATOM   15998 O  OD2 . ASP   B 1 253  ? 42.50000   98.57700  -44.75900 1.000 39.06676  -1 253  ASP   B OD2 1 
ATOM   15999 N  N   . ASP   B 1 254  ? 38.11500   102.50700 -45.37500 1.000 49.77699  ?  254  ASP   B N   1 
ATOM   16000 C  CA  . ASP   B 1 254  ? 37.73000   103.86900 -45.02600 1.000 53.10387  ?  254  ASP   B CA  1 
ATOM   16001 C  C   . ASP   B 1 254  ? 36.89100   103.86700 -43.75600 1.000 50.56681  ?  254  ASP   B C   1 
ATOM   16002 O  O   . ASP   B 1 254  ? 36.07800   102.96700 -43.52900 1.000 56.50130  ?  254  ASP   B O   1 
ATOM   16003 C  CB  . ASP   B 1 254  ? 36.94800   104.53000 -46.16200 1.000 35.47961  ?  254  ASP   B CB  1 
ATOM   16004 C  CG  . ASP   B 1 254  ? 37.84300   104.99700 -47.29000 1.000 64.82928  ?  254  ASP   B CG  1 
ATOM   16005 O  OD1 . ASP   B 1 254  ? 39.06100   105.13800 -47.06400 1.000 75.51746  ?  254  ASP   B OD1 1 
ATOM   16006 O  OD2 . ASP   B 1 254  ? 37.32200   105.23000 -48.40400 1.000 69.27799  -1 254  ASP   B OD2 1 
ATOM   16007 N  N   . GLN   B 1 255  ? 37.09300   104.88400 -42.92600 1.000 37.27621  ?  255  GLN   B N   1 
ATOM   16008 C  CA  . GLN   B 1 255  ? 36.37000   105.02700 -41.67100 1.000 43.35218  ?  255  GLN   B CA  1 
ATOM   16009 C  C   . GLN   B 1 255  ? 35.27500   106.07200 -41.84200 1.000 41.30044  ?  255  GLN   B C   1 
ATOM   16010 O  O   . GLN   B 1 255  ? 35.55500   107.21500 -42.21800 1.000 47.62973  ?  255  GLN   B O   1 
ATOM   16011 C  CB  . GLN   B 1 255  ? 37.31800   105.41900 -40.53800 1.000 36.49135  ?  255  GLN   B CB  1 
ATOM   16012 C  CG  . GLN   B 1 255  ? 38.45700   104.43800 -40.31600 1.000 44.90848  ?  255  GLN   B CG  1 
ATOM   16013 C  CD  . GLN   B 1 255  ? 39.49400   104.95600 -39.33700 1.000 55.86892  ?  255  GLN   B CD  1 
ATOM   16014 O  OE1 . GLN   B 1 255  ? 39.40300   106.08700 -38.85700 1.000 44.67154  ?  255  GLN   B OE1 1 
ATOM   16015 N  NE2 . GLN   B 1 255  ? 40.48900   104.12800 -39.03600 1.000 56.12745  ?  255  GLN   B NE2 1 
ATOM   16016 N  N   . VAL   B 1 256  ? 34.03500   105.67400 -41.58000 1.000 33.53951  ?  256  VAL   B N   1 
ATOM   16017 C  CA  . VAL   B 1 256  ? 32.89900   106.58400 -41.55600 1.000 41.01427  ?  256  VAL   B CA  1 
ATOM   16018 C  C   . VAL   B 1 256  ? 32.28700   106.52700 -40.16400 1.000 37.68196  ?  256  VAL   B C   1 
ATOM   16019 O  O   . VAL   B 1 256  ? 32.18600   105.45200 -39.56100 1.000 34.12145  ?  256  VAL   B O   1 
ATOM   16020 C  CB  . VAL   B 1 256  ? 31.86500   106.24200 -42.65100 1.000 39.03998  ?  256  VAL   B CB  1 
ATOM   16021 C  CG1 . VAL   B 1 256  ? 32.25800   104.96100 -43.36600 1.000 31.77294  ?  256  VAL   B CG1 1 
ATOM   16022 C  CG2 . VAL   B 1 256  ? 30.46000   106.14000 -42.07600 1.000 37.35198  ?  256  VAL   B CG2 1 
ATOM   16023 N  N   . ALA   B 1 257  ? 31.90500   107.68900 -39.64900 1.000 39.11530  ?  257  ALA   B N   1 
ATOM   16024 C  CA  . ALA   B 1 257  ? 31.46800   107.83200 -38.27000 1.000 40.58363  ?  257  ALA   B CA  1 
ATOM   16025 C  C   . ALA   B 1 257  ? 29.94900   107.83200 -38.17100 1.000 38.98252  ?  257  ALA   B C   1 
ATOM   16026 O  O   . ALA   B 1 257  ? 29.24300   108.26700 -39.08400 1.000 42.42048  ?  257  ALA   B O   1 
ATOM   16027 C  CB  . ALA   B 1 257  ? 32.02700   109.11800 -37.65700 1.000 41.51350  ?  257  ALA   B CB  1 
ATOM   16028 N  N   . ILE   B 1 258  ? 29.45800   107.32900 -37.04000 1.000 49.44191  ?  258  ILE   B N   1 
ATOM   16029 C  CA  . ILE   B 1 258  ? 28.03700   107.28100 -36.72500 1.000 43.45841  ?  258  ILE   B CA  1 
ATOM   16030 C  C   . ILE   B 1 258  ? 27.86000   107.88400 -35.34100 1.000 47.56477  ?  258  ILE   B C   1 
ATOM   16031 O  O   . ILE   B 1 258  ? 28.48600   107.42500 -34.37900 1.000 61.45769  ?  258  ILE   B O   1 
ATOM   16032 C  CB  . ILE   B 1 258  ? 27.48900   105.84700 -36.75600 1.000 29.85841  ?  258  ILE   B CB  1 
ATOM   16033 C  CG1 . ILE   B 1 258  ? 28.02400   105.09900 -37.97200 1.000 25.10554  ?  258  ILE   B CG1 1 
ATOM   16034 C  CG2 . ILE   B 1 258  ? 25.97300   105.85900 -36.77100 1.000 48.02581  ?  258  ILE   B CG2 1 
ATOM   16035 C  CD1 . ILE   B 1 258  ? 27.88800   103.60900 -37.85300 1.000 43.94775  ?  258  ILE   B CD1 1 
ATOM   16036 N  N   . MET   B 1 259  ? 27.01900   108.90900 -35.23900 1.000 46.34624  ?  259  MET   B N   1 
ATOM   16037 C  CA  . MET   B 1 259  ? 26.71500   109.55400 -33.96100 1.000 48.17344  ?  259  MET   B CA  1 
ATOM   16038 C  C   . MET   B 1 259  ? 25.20100   109.53600 -33.78800 1.000 53.95445  ?  259  MET   B C   1 
ATOM   16039 O  O   . MET   B 1 259  ? 24.52200   110.54200 -34.00500 1.000 59.57381  ?  259  MET   B O   1 
ATOM   16040 C  CB  . MET   B 1 259  ? 27.26900   110.96900 -33.89900 1.000 39.48479  ?  259  MET   B CB  1 
ATOM   16041 C  CG  . MET   B 1 259  ? 27.30100   111.53900 -32.48900 1.000 43.27240  ?  259  MET   B CG  1 
ATOM   16042 S  SD  . MET   B 1 259  ? 27.26500   113.33800 -32.44100 1.000 65.92137  ?  259  MET   B SD  1 
ATOM   16043 C  CE  . MET   B 1 259  ? 28.06400   113.73100 -33.99000 1.000 39.44748  ?  259  MET   B CE  1 
ATOM   16044 N  N   . LEU   B 1 260  ? 24.67600   108.38100 -33.39200 1.000 52.37423  ?  260  LEU   B N   1 
ATOM   16045 C  CA  . LEU   B 1 260  ? 23.24900   108.17500 -33.21100 1.000 38.74071  ?  260  LEU   B CA  1 
ATOM   16046 C  C   . LEU   B 1 260  ? 22.96600   107.66800 -31.80400 1.000 53.60654  ?  260  LEU   B C   1 
ATOM   16047 O  O   . LEU   B 1 260  ? 23.77700   106.94900 -31.21000 1.000 52.50670  ?  260  LEU   B O   1 
ATOM   16048 C  CB  . LEU   B 1 260  ? 22.70100   107.16400 -34.22900 1.000 34.82891  ?  260  LEU   B CB  1 
ATOM   16049 C  CG  . LEU   B 1 260  ? 21.96500   107.67900 -35.46400 1.000 31.10339  ?  260  LEU   B CG  1 
ATOM   16050 C  CD1 . LEU   B 1 260  ? 22.70200   108.84000 -36.06500 1.000 30.59629  ?  260  LEU   B CD1 1 
ATOM   16051 C  CD2 . LEU   B 1 260  ? 21.81600   106.56300 -36.48600 1.000 35.91120  ?  260  LEU   B CD2 1 
ATOM   16052 N  N   . ASP   B 1 261  ? 21.81100   108.05400 -31.27300 1.000 57.66299  ?  261  ASP   B N   1 
ATOM   16053 C  CA  . ASP   B 1 261  ? 21.29500   107.38100 -30.09400 1.000 54.27650  ?  261  ASP   B CA  1 
ATOM   16054 C  C   . ASP   B 1 261  ? 20.82000   105.98300 -30.47900 1.000 47.08042  ?  261  ASP   B C   1 
ATOM   16055 O  O   . ASP   B 1 261  ? 20.52700   105.70100 -31.64400 1.000 34.46527  ?  261  ASP   B O   1 
ATOM   16056 C  CB  . ASP   B 1 261  ? 20.14600   108.17400 -29.47200 1.000 47.31668  ?  261  ASP   B CB  1 
ATOM   16057 C  CG  . ASP   B 1 261  ? 20.13600   109.62300 -29.91100 1.000 71.86729  ?  261  ASP   B CG  1 
ATOM   16058 O  OD1 . ASP   B 1 261  ? 19.99300   109.87300 -31.12700 1.000 66.43263  ?  261  ASP   B OD1 1 
ATOM   16059 O  OD2 . ASP   B 1 261  ? 20.26400   110.51200 -29.04200 1.000 79.02539  -1 261  ASP   B OD2 1 
ATOM   16060 N  N   . LYS   B 1 262  ? 20.75500   105.09900 -29.48700 1.000 41.27816  ?  262  LYS   B N   1 
ATOM   16061 C  CA  . LYS   B 1 262  ? 20.32800   103.73000 -29.74800 1.000 42.25758  ?  262  LYS   B CA  1 
ATOM   16062 C  C   . LYS   B 1 262  ? 18.92000   103.71700 -30.32900 1.000 42.33301  ?  262  LYS   B C   1 
ATOM   16063 O  O   . LYS   B 1 262  ? 17.97200   104.19600 -29.69800 1.000 37.93763  ?  262  LYS   B O   1 
ATOM   16064 C  CB  . LYS   B 1 262  ? 20.38500   102.90200 -28.46700 1.000 40.68900  ?  262  LYS   B CB  1 
ATOM   16065 C  CG  . LYS   B 1 262  ? 21.78500   102.65100 -27.94800 1.000 43.57522  ?  262  LYS   B CG  1 
ATOM   16066 C  CD  . LYS   B 1 262  ? 21.79800   101.40400 -27.08800 1.000 37.13685  ?  262  LYS   B CD  1 
ATOM   16067 C  CE  . LYS   B 1 262  ? 22.71800   101.55800 -25.89600 1.000 55.51933  ?  262  LYS   B CE  1 
ATOM   16068 N  NZ  . LYS   B 1 262  ? 22.24300   100.71300 -24.76900 1.000 64.59152  ?  262  LYS   B NZ  1 
ATOM   16069 N  N   . SER   B 1 263  ? 18.78900   103.17300 -31.53500 1.000 40.21371  ?  263  SER   B N   1 
ATOM   16070 C  CA  . SER   B 1 263  ? 17.52600   103.18500 -32.26300 1.000 42.34695  ?  263  SER   B CA  1 
ATOM   16071 C  C   . SER   B 1 263  ? 17.59200   102.13300 -33.36400 1.000 42.82012  ?  263  SER   B C   1 
ATOM   16072 O  O   . SER   B 1 263  ? 18.55100   101.35900 -33.45200 1.000 40.24350  ?  263  SER   B O   1 
ATOM   16073 C  CB  . SER   B 1 263  ? 17.24400   104.57800 -32.83500 1.000 49.02414  ?  263  SER   B CB  1 
ATOM   16074 O  OG  . SER   B 1 263  ? 18.25900   104.95600 -33.75000 1.000 43.44203  ?  263  SER   B OG  1 
ATOM   16075 N  N   . LEU   B 1 264  ? 16.56000   102.10600 -34.21200 1.000 53.85255  ?  264  LEU   B N   1 
ATOM   16076 C  CA  . LEU   B 1 264  ? 16.57800   101.22100 -35.37200 1.000 42.04021  ?  264  LEU   B CA  1 
ATOM   16077 C  C   . LEU   B 1 264  ? 17.57300   101.70900 -36.41600 1.000 44.22484  ?  264  LEU   B C   1 
ATOM   16078 O  O   . LEU   B 1 264  ? 18.23500   100.90200 -37.07800 1.000 54.60284  ?  264  LEU   B O   1 
ATOM   16079 C  CB  . LEU   B 1 264  ? 15.17800   101.11800 -35.97800 1.000 30.73344  ?  264  LEU   B CB  1 
ATOM   16080 C  CG  . LEU   B 1 264  ? 14.07400   100.47500 -35.13800 1.000 36.18815  ?  264  LEU   B CG  1 
ATOM   16081 C  CD1 . LEU   B 1 264  ? 12.71000   100.78800 -35.72300 1.000 44.14815  ?  264  LEU   B CD1 1 
ATOM   16082 C  CD2 . LEU   B 1 264  ? 14.27300   98.97600  -35.05200 1.000 40.48840  ?  264  LEU   B CD2 1 
ATOM   16083 N  N   . ASP   B 1 265  ? 17.69000   103.03000 -36.57700 1.000 44.70019  ?  265  ASP   B N   1 
ATOM   16084 C  CA  . ASP   B 1 265  ? 18.60400   103.59000 -37.56400 1.000 53.05774  ?  265  ASP   B CA  1 
ATOM   16085 C  C   . ASP   B 1 265  ? 20.06200   103.34500 -37.20600 1.000 48.40833  ?  265  ASP   B C   1 
ATOM   16086 O  O   . ASP   B 1 265  ? 20.92200   103.39400 -38.09200 1.000 43.41375  ?  265  ASP   B O   1 
ATOM   16087 C  CB  . ASP   B 1 265  ? 18.34900   105.08900 -37.71700 1.000 48.75274  ?  265  ASP   B CB  1 
ATOM   16088 C  CG  . ASP   B 1 265  ? 16.89500   105.40400 -37.99900 1.000 59.84160  ?  265  ASP   B CG  1 
ATOM   16089 O  OD1 . ASP   B 1 265  ? 16.30500   104.75000 -38.88500 1.000 64.50663  ?  265  ASP   B OD1 1 
ATOM   16090 O  OD2 . ASP   B 1 265  ? 16.33900   106.29800 -37.32700 1.000 64.76000  -1 265  ASP   B OD2 1 
ATOM   16091 N  N   . MET   B 1 266  ? 20.35900   103.08800 -35.93200 1.000 44.29158  ?  266  MET   B N   1 
ATOM   16092 C  CA  . MET   B 1 266  ? 21.72800   102.76300 -35.55300 1.000 39.41226  ?  266  MET   B CA  1 
ATOM   16093 C  C   . MET   B 1 266  ? 22.14300   101.41400 -36.12300 1.000 39.81334  ?  266  MET   B C   1 
ATOM   16094 O  O   . MET   B 1 266  ? 23.26200   101.26400 -36.62500 1.000 44.67124  ?  266  MET   B O   1 
ATOM   16095 C  CB  . MET   B 1 266  ? 21.86700   102.77600 -34.03300 1.000 45.11121  ?  266  MET   B CB  1 
ATOM   16096 C  CG  . MET   B 1 266  ? 23.23200   103.21400 -33.53800 1.000 45.97018  ?  266  MET   B CG  1 
ATOM   16097 S  SD  . MET   B 1 266  ? 23.40400   102.92200 -31.77100 1.000 48.08426  ?  266  MET   B SD  1 
ATOM   16098 C  CE  . MET   B 1 266  ? 22.88600   101.21000 -31.69600 1.000 35.30113  ?  266  MET   B CE  1 
ATOM   16099 N  N   . ILE   B 1 267  ? 21.25000   100.42300 -36.06300 1.000 34.06584  ?  267  ILE   B N   1 
ATOM   16100 C  CA  . ILE   B 1 267  ? 21.54400   99.12400  -36.66000 1.000 33.07188  ?  267  ILE   B CA  1 
ATOM   16101 C  C   . ILE   B 1 267  ? 21.65900   99.25200  -38.17200 1.000 38.97786  ?  267  ILE   B C   1 
ATOM   16102 O  O   . ILE   B 1 267  ? 22.48200   98.58200  -38.80600 1.000 44.77785  ?  267  ILE   B O   1 
ATOM   16103 C  CB  . ILE   B 1 267  ? 20.47000   98.09500  -36.26500 1.000 28.58614  ?  267  ILE   B CB  1 
ATOM   16104 C  CG1 . ILE   B 1 267  ? 20.12000   98.22300  -34.78000 1.000 29.52899  ?  267  ILE   B CG1 1 
ATOM   16105 C  CG2 . ILE   B 1 267  ? 20.94500   96.68500  -36.58700 1.000 29.17439  ?  267  ILE   B CG2 1 
ATOM   16106 C  CD1 . ILE   B 1 267  ? 21.25800   97.87900  -33.84700 1.000 23.08306  ?  267  ILE   B CD1 1 
ATOM   16107 N  N   . VAL   B 1 268  ? 20.83700   100.11500 -38.77100 1.000 38.73900  ?  268  VAL   B N   1 
ATOM   16108 C  CA  . VAL   B 1 268  ? 20.89000   100.32000 -40.21500 1.000 44.40652  ?  268  VAL   B CA  1 
ATOM   16109 C  C   . VAL   B 1 268  ? 22.20000   100.98900 -40.60800 1.000 41.85545  ?  268  VAL   B C   1 
ATOM   16110 O  O   . VAL   B 1 268  ? 22.86600   100.57400 -41.56400 1.000 44.43311  ?  268  VAL   B O   1 
ATOM   16111 C  CB  . VAL   B 1 268  ? 19.67500   101.14100 -40.68300 1.000 42.94754  ?  268  VAL   B CB  1 
ATOM   16112 C  CG1 . VAL   B 1 268  ? 19.75500   101.40000 -42.17800 1.000 45.90445  ?  268  VAL   B CG1 1 
ATOM   16113 C  CG2 . VAL   B 1 268  ? 18.38300   100.42500 -40.32600 1.000 37.13532  ?  268  VAL   B CG2 1 
ATOM   16114 N  N   . SER   B 1 269  ? 22.59300   102.03300 -39.87300 1.000 34.92827  ?  269  SER   B N   1 
ATOM   16115 C  CA  . SER   B 1 269  ? 23.81300   102.76100 -40.21000 1.000 44.94043  ?  269  SER   B CA  1 
ATOM   16116 C  C   . SER   B 1 269  ? 25.05200   101.89800 -40.00700 1.000 50.45817  ?  269  SER   B C   1 
ATOM   16117 O  O   . SER   B 1 269  ? 25.99900   101.96900 -40.79900 1.000 52.51144  ?  269  SER   B O   1 
ATOM   16118 C  CB  . SER   B 1 269  ? 23.90700   104.03700 -39.37600 1.000 36.94766  ?  269  SER   B CB  1 
ATOM   16119 O  OG  . SER   B 1 269  ? 22.79400   104.88000 -39.61100 1.000 49.26208  ?  269  SER   B OG  1 
ATOM   16120 N  N   . ILE   B 1 270  ? 25.06700   101.08100 -38.95200 1.000 46.87338  ?  270  ILE   B N   1 
ATOM   16121 C  CA  . ILE   B 1 270  ? 26.22000   100.22400 -38.69100 1.000 36.71711  ?  270  ILE   B CA  1 
ATOM   16122 C  C   . ILE   B 1 270  ? 26.40200   99.21900  -39.82200 1.000 39.55076  ?  270  ILE   B C   1 
ATOM   16123 O  O   . ILE   B 1 270  ? 27.51000   99.02600  -40.33600 1.000 58.13179  ?  270  ILE   B O   1 
ATOM   16124 C  CB  . ILE   B 1 270  ? 26.07000   99.52400  -37.32900 1.000 29.11580  ?  270  ILE   B CB  1 
ATOM   16125 C  CG1 . ILE   B 1 270  ? 26.29200   100.52100 -36.19000 1.000 33.90717  ?  270  ILE   B CG1 1 
ATOM   16126 C  CG2 . ILE   B 1 270  ? 27.03900   98.36300  -37.21700 1.000 25.05692  ?  270  ILE   B CG2 1 
ATOM   16127 C  CD1 . ILE   B 1 270  ? 26.06400   99.93400  -34.81600 1.000 24.60495  ?  270  ILE   B CD1 1 
ATOM   16128 N  N   . LEU   B 1 271  ? 25.31300   98.56900  -40.23300 1.000 35.94732  ?  271  LEU   B N   1 
ATOM   16129 C  CA  . LEU   B 1 271  ? 25.39200   97.58200  -41.30100 1.000 40.88964  ?  271  LEU   B CA  1 
ATOM   16130 C  C   . LEU   B 1 271  ? 25.53400   98.21300  -42.68000 1.000 38.93264  ?  271  LEU   B C   1 
ATOM   16131 O  O   . LEU   B 1 271  ? 26.02500   97.54800  -43.60000 1.000 32.90622  ?  271  LEU   B O   1 
ATOM   16132 C  CB  . LEU   B 1 271  ? 24.16100   96.67400  -41.27200 1.000 29.92017  ?  271  LEU   B CB  1 
ATOM   16133 C  CG  . LEU   B 1 271  ? 24.05200   95.76100  -40.05000 1.000 33.04048  ?  271  LEU   B CG  1 
ATOM   16134 C  CD1 . LEU   B 1 271  ? 22.77800   94.93400  -40.10500 1.000 35.82527  ?  271  LEU   B CD1 1 
ATOM   16135 C  CD2 . LEU   B 1 271  ? 25.27300   94.86100  -39.94200 1.000 25.75265  ?  271  LEU   B CD2 1 
ATOM   16136 N  N   . ALA   B 1 272  ? 25.12000   99.47100  -42.84800 1.000 38.99805  ?  272  ALA   B N   1 
ATOM   16137 C  CA  . ALA   B 1 272  ? 25.28000   100.12800 -44.14100 1.000 44.68538  ?  272  ALA   B CA  1 
ATOM   16138 C  C   . ALA   B 1 272  ? 26.74200   100.45500 -44.41300 1.000 48.23495  ?  272  ALA   B C   1 
ATOM   16139 O  O   . ALA   B 1 272  ? 27.19700   100.38600 -45.56100 1.000 45.87890  ?  272  ALA   B O   1 
ATOM   16140 C  CB  . ALA   B 1 272  ? 24.43000   101.39500 -44.20200 1.000 41.97999  ?  272  ALA   B CB  1 
ATOM   16141 N  N   . VAL   B 1 273  ? 27.48900   100.81800 -43.36800 1.000 39.79599  ?  273  VAL   B N   1 
ATOM   16142 C  CA  . VAL   B 1 273  ? 28.91800   101.06600 -43.52300 1.000 33.67061  ?  273  VAL   B CA  1 
ATOM   16143 C  C   . VAL   B 1 273  ? 29.63300   99.79400  -43.95700 1.000 37.72824  ?  273  VAL   B C   1 
ATOM   16144 O  O   . VAL   B 1 273  ? 30.49100   99.81700  -44.84900 1.000 38.27153  ?  273  VAL   B O   1 
ATOM   16145 C  CB  . VAL   B 1 273  ? 29.50400   101.62600 -42.21500 1.000 37.17573  ?  273  VAL   B CB  1 
ATOM   16146 C  CG1 . VAL   B 1 273  ? 31.00500   101.78200 -42.33500 1.000 32.27221  ?  273  VAL   B CG1 1 
ATOM   16147 C  CG2 . VAL   B 1 273  ? 28.85000   102.95000 -41.86600 1.000 35.19144  ?  273  VAL   B CG2 1 
ATOM   16148 N  N   . MET   B 1 274  ? 29.28900   98.66500  -43.33500 1.000 35.42021  ?  274  MET   B N   1 
ATOM   16149 C  CA  . MET   B 1 274  ? 29.90500   97.39400  -43.70100 1.000 40.42976  ?  274  MET   B CA  1 
ATOM   16150 C  C   . MET   B 1 274  ? 29.58600   97.02300  -45.14300 1.000 32.90681  ?  274  MET   B C   1 
ATOM   16151 O  O   . MET   B 1 274  ? 30.47600   96.64300  -45.91100 1.000 35.18042  ?  274  MET   B O   1 
ATOM   16152 C  CB  . MET   B 1 274  ? 29.43700   96.29400  -42.74900 1.000 29.12657  ?  274  MET   B CB  1 
ATOM   16153 C  CG  . MET   B 1 274  ? 30.19200   96.24700  -41.43800 1.000 37.68399  ?  274  MET   B CG  1 
ATOM   16154 S  SD  . MET   B 1 274  ? 29.63200   94.89200  -40.39400 1.000 49.14313  ?  274  MET   B SD  1 
ATOM   16155 C  CE  . MET   B 1 274  ? 28.73400   95.79800  -39.14500 1.000 41.05772  ?  274  MET   B CE  1 
ATOM   16156 N  N   . LYS   B 1 275  ? 28.31300   97.12900  -45.52700 1.000 39.43104  ?  275  LYS   B N   1 
ATOM   16157 C  CA  . LYS   B 1 275  ? 27.91700   96.76900  -46.88400 1.000 32.64039  ?  275  LYS   B CA  1 
ATOM   16158 C  C   . LYS   B 1 275  ? 28.55600   97.69400  -47.91100 1.000 37.69430  ?  275  LYS   B C   1 
ATOM   16159 O  O   . LYS   B 1 275  ? 28.90700   97.25600  -49.01300 1.000 34.62745  ?  275  LYS   B O   1 
ATOM   16160 C  CB  . LYS   B 1 275  ? 26.39600   96.79100  -47.00100 1.000 43.72064  ?  275  LYS   B CB  1 
ATOM   16161 C  CG  . LYS   B 1 275  ? 25.71300   95.67600  -46.23300 1.000 36.99954  ?  275  LYS   B CG  1 
ATOM   16162 C  CD  . LYS   B 1 275  ? 24.27400   96.03200  -45.92300 1.000 40.55558  ?  275  LYS   B CD  1 
ATOM   16163 C  CE  . LYS   B 1 275  ? 23.51300   94.83000  -45.40300 1.000 39.33659  ?  275  LYS   B CE  1 
ATOM   16164 N  NZ  . LYS   B 1 275  ? 23.42000   93.75800  -46.43100 1.000 32.17850  ?  275  LYS   B NZ  1 
ATOM   16165 N  N   . ALA   B 1 276  ? 28.71600   98.97600  -47.57300 1.000 35.69515  ?  276  ALA   B N   1 
ATOM   16166 C  CA  . ALA   B 1 276  ? 29.43500   99.88000  -48.46300 1.000 36.74486  ?  276  ALA   B CA  1 
ATOM   16167 C  C   . ALA   B 1 276  ? 30.89300   99.46100  -48.60200 1.000 41.53024  ?  276  ALA   B C   1 
ATOM   16168 O  O   . ALA   B 1 276  ? 31.46900   99.54300  -49.69300 1.000 46.23362  ?  276  ALA   B O   1 
ATOM   16169 C  CB  . ALA   B 1 276  ? 29.33300   101.31700 -47.95300 1.000 31.81609  ?  276  ALA   B CB  1 
ATOM   16170 N  N   . GLY   B 1 277  ? 31.50300   99.00700  -47.50800 1.000 44.44236  ?  277  GLY   B N   1 
ATOM   16171 C  CA  . GLY   B 1 277  ? 32.86300   98.50800  -47.55000 1.000 36.54486  ?  277  GLY   B CA  1 
ATOM   16172 C  C   . GLY   B 1 277  ? 33.78300   99.08300  -46.49100 1.000 41.26126  ?  277  GLY   B C   1 
ATOM   16173 O  O   . GLY   B 1 277  ? 34.93100   98.64700  -46.35900 1.000 40.53441  ?  277  GLY   B O   1 
ATOM   16174 N  N   . GLY   B 1 278  ? 33.29400   100.05600 -45.72200 1.000 30.20891  ?  278  GLY   B N   1 
ATOM   16175 C  CA  . GLY   B 1 278  ? 34.10900   100.75500 -44.75600 1.000 30.30425  ?  278  GLY   B CA  1 
ATOM   16176 C  C   . GLY   B 1 278  ? 33.94100   100.23300 -43.33500 1.000 33.24570  ?  278  GLY   B C   1 
ATOM   16177 O  O   . GLY   B 1 278  ? 33.21600   99.28000  -43.06000 1.000 30.24229  ?  278  GLY   B O   1 
ATOM   16178 N  N   . ALA   B 1 279  ? 34.65000   100.89100 -42.42200 1.000 26.89917  ?  279  ALA   B N   1 
ATOM   16179 C  CA  . ALA   B 1 279  ? 34.56900   100.62300 -40.99600 1.000 34.16204  ?  279  ALA   B CA  1 
ATOM   16180 C  C   . ALA   B 1 279  ? 33.77900   101.73300 -40.31700 1.000 46.84347  ?  279  ALA   B C   1 
ATOM   16181 O  O   . ALA   B 1 279  ? 33.79800   102.88600 -40.75800 1.000 52.70950  ?  279  ALA   B O   1 
ATOM   16182 C  CB  . ALA   B 1 279  ? 35.96300   100.51500 -40.37300 1.000 41.01431  ?  279  ALA   B CB  1 
ATOM   16183 N  N   . TYR   B 1 280  ? 33.07700   101.38300 -39.24300 1.000 36.41591  ?  280  TYR   B N   1 
ATOM   16184 C  CA  . TYR   B 1 280  ? 32.18300   102.31500 -38.57200 1.000 38.25350  ?  280  TYR   B CA  1 
ATOM   16185 C  C   . TYR   B 1 280  ? 32.81300   102.78400 -37.26700 1.000 39.50054  ?  280  TYR   B C   1 
ATOM   16186 O  O   . TYR   B 1 280  ? 33.23400   101.96500 -36.44300 1.000 43.38277  ?  280  TYR   B O   1 
ATOM   16187 C  CB  . TYR   B 1 280  ? 30.79800   101.68800 -38.35200 1.000 30.54260  ?  280  TYR   B CB  1 
ATOM   16188 C  CG  . TYR   B 1 280  ? 30.55300   100.91900 -37.06500 1.000 31.69920  ?  280  TYR   B CG  1 
ATOM   16189 C  CD1 . TYR   B 1 280  ? 30.12300   101.57300 -35.91400 1.000 29.52730  ?  280  TYR   B CD1 1 
ATOM   16190 C  CD2 . TYR   B 1 280  ? 30.68800   99.53500  -37.01700 1.000 30.91205  ?  280  TYR   B CD2 1 
ATOM   16191 C  CE1 . TYR   B 1 280  ? 29.87500   100.87800 -34.74300 1.000 32.14315  ?  280  TYR   B CE1 1 
ATOM   16192 C  CE2 . TYR   B 1 280  ? 30.43800   98.83000  -35.84700 1.000 28.01770  ?  280  TYR   B CE2 1 
ATOM   16193 C  CZ  . TYR   B 1 280  ? 30.03200   99.50700  -34.71600 1.000 36.11281  ?  280  TYR   B CZ  1 
ATOM   16194 O  OH  . TYR   B 1 280  ? 29.78300   98.81000  -33.55400 1.000 34.95796  ?  280  TYR   B OH  1 
ATOM   16195 N  N   . VAL   B 1 281  ? 32.90000   104.10100 -37.10200 1.000 38.03483  ?  281  VAL   B N   1 
ATOM   16196 C  CA  . VAL   B 1 281  ? 33.48900   104.71500 -35.91400 1.000 33.64092  ?  281  VAL   B CA  1 
ATOM   16197 C  C   . VAL   B 1 281  ? 32.36300   105.22800 -35.02600 1.000 46.47469  ?  281  VAL   B C   1 
ATOM   16198 O  O   . VAL   B 1 281  ? 31.82900   106.32100 -35.26700 1.000 48.49415  ?  281  VAL   B O   1 
ATOM   16199 C  CB  . VAL   B 1 281  ? 34.45800   105.84700 -36.28800 1.000 32.44561  ?  281  VAL   B CB  1 
ATOM   16200 C  CG1 . VAL   B 1 281  ? 35.13200   106.40200 -35.04100 1.000 28.54718  ?  281  VAL   B CG1 1 
ATOM   16201 C  CG2 . VAL   B 1 281  ? 35.49400   105.35300 -37.28300 1.000 43.89699  ?  281  VAL   B CG2 1 
ATOM   16202 N  N   . PRO   B 1 282  ? 31.97300   104.48500 -33.99400 1.000 46.71949  ?  282  PRO   B N   1 
ATOM   16203 C  CA  . PRO   B 1 282  ? 30.83300   104.90600 -33.17500 1.000 29.76373  ?  282  PRO   B CA  1 
ATOM   16204 C  C   . PRO   B 1 282  ? 31.18600   106.09000 -32.28900 1.000 46.65623  ?  282  PRO   B C   1 
ATOM   16205 O  O   . PRO   B 1 282  ? 32.28100   106.16700 -31.72600 1.000 62.73868  ?  282  PRO   B O   1 
ATOM   16206 C  CB  . PRO   B 1 282  ? 30.52100   103.66000 -32.34300 1.000 33.39927  ?  282  PRO   B CB  1 
ATOM   16207 C  CG  . PRO   B 1 282  ? 31.82900   102.95300 -32.24300 1.000 33.43632  ?  282  PRO   B CG  1 
ATOM   16208 C  CD  . PRO   B 1 282  ? 32.54700   103.20800 -33.53600 1.000 43.29311  ?  282  PRO   B CD  1 
ATOM   16209 N  N   . ILE   B 1 283  ? 30.24200   107.02100 -32.17700 1.000 43.74624  ?  283  ILE   B N   1 
ATOM   16210 C  CA  . ILE   B 1 283  ? 30.38600   108.20900 -31.34300 1.000 47.17410  ?  283  ILE   B CA  1 
ATOM   16211 C  C   . ILE   B 1 283  ? 29.11200   108.36200 -30.52800 1.000 50.93138  ?  283  ILE   B C   1 
ATOM   16212 O  O   . ILE   B 1 283  ? 28.01900   108.48300 -31.09700 1.000 50.63190  ?  283  ILE   B O   1 
ATOM   16213 C  CB  . ILE   B 1 283  ? 30.65000   109.47400 -32.17500 1.000 46.84225  ?  283  ILE   B CB  1 
ATOM   16214 C  CG1 . ILE   B 1 283  ? 31.92100   109.31200 -33.00900 1.000 41.62251  ?  283  ILE   B CG1 1 
ATOM   16215 C  CG2 . ILE   B 1 283  ? 30.76100   110.69300 -31.27100 1.000 44.57884  ?  283  ILE   B CG2 1 
ATOM   16216 C  CD1 . ILE   B 1 283  ? 32.12100   110.41200 -34.01200 1.000 44.89040  ?  283  ILE   B CD1 1 
ATOM   16217 N  N   . ASP   B 1 284  ? 29.24600   108.35700 -29.20800 1.000 48.92884  ?  284  ASP   B N   1 
ATOM   16218 C  CA  . ASP   B 1 284  ? 28.08200   108.46100 -28.33900 1.000 50.15835  ?  284  ASP   B CA  1 
ATOM   16219 C  C   . ASP   B 1 284  ? 27.61900   109.91100 -28.27100 1.000 56.28676  ?  284  ASP   B C   1 
ATOM   16220 O  O   . ASP   B 1 284  ? 28.41900   110.79200 -27.93700 1.000 60.80811  ?  284  ASP   B O   1 
ATOM   16221 C  CB  . ASP   B 1 284  ? 28.41000   107.93800 -26.94700 1.000 50.08802  ?  284  ASP   B CB  1 
ATOM   16222 C  CG  . ASP   B 1 284  ? 27.17200   107.56100 -26.16400 1.000 51.39190  ?  284  ASP   B CG  1 
ATOM   16223 O  OD1 . ASP   B 1 284  ? 26.44600   108.47400 -25.71500 1.000 58.67231  ?  284  ASP   B OD1 1 
ATOM   16224 O  OD2 . ASP   B 1 284  ? 26.91300   106.34800 -26.01600 1.000 60.01088  -1 284  ASP   B OD2 1 
ATOM   16225 N  N   . PRO   B 1 285  ? 26.35300   110.20400 -28.58200 1.000 56.61389  ?  285  PRO   B N   1 
ATOM   16226 C  CA  . PRO   B 1 285  ? 25.89900   111.60500 -28.59100 1.000 54.30196  ?  285  PRO   B CA  1 
ATOM   16227 C  C   . PRO   B 1 285  ? 25.86500   112.25300 -27.21800 1.000 55.43310  ?  285  PRO   B C   1 
ATOM   16228 O  O   . PRO   B 1 285  ? 25.67700   113.47400 -27.13800 1.000 65.20693  ?  285  PRO   B O   1 
ATOM   16229 C  CB  . PRO   B 1 285  ? 24.48800   111.51700 -29.19200 1.000 60.00995  ?  285  PRO   B CB  1 
ATOM   16230 C  CG  . PRO   B 1 285  ? 24.43200   110.17900 -29.87500 1.000 61.74783  ?  285  PRO   B CG  1 
ATOM   16231 C  CD  . PRO   B 1 285  ? 25.31000   109.28300 -29.06100 1.000 66.94756  ?  285  PRO   B CD  1 
ATOM   16232 N  N   . ASP   B 1 286  ? 26.03200   111.48800 -26.14200 1.000 54.88749  ?  286  ASP   B N   1 
ATOM   16233 C  CA  . ASP   B 1 286  ? 26.04300   112.03200 -24.79200 1.000 56.97382  ?  286  ASP   B CA  1 
ATOM   16234 C  C   . ASP   B 1 286  ? 27.45200   112.18500 -24.23400 1.000 62.33985  ?  286  ASP   B C   1 
ATOM   16235 O  O   . ASP   B 1 286  ? 27.60800   112.54000 -23.06100 1.000 73.60724  ?  286  ASP   B O   1 
ATOM   16236 C  CB  . ASP   B 1 286  ? 25.20000   111.15600 -23.86300 1.000 50.07216  ?  286  ASP   B CB  1 
ATOM   16237 C  CG  . ASP   B 1 286  ? 23.72800   111.17900 -24.22300 1.000 65.28841  ?  286  ASP   B CG  1 
ATOM   16238 O  OD1 . ASP   B 1 286  ? 23.28100   112.17700 -24.82800 1.000 63.81246  ?  286  ASP   B OD1 1 
ATOM   16239 O  OD2 . ASP   B 1 286  ? 23.01900   110.20300 -23.90000 1.000 71.04577  -1 286  ASP   B OD2 1 
ATOM   16240 N  N   . TYR   B 1 287  ? 28.47700   111.92100 -25.04200 1.000 69.40688  ?  287  TYR   B N   1 
ATOM   16241 C  CA  . TYR   B 1 287  ? 29.84600   112.15700 -24.62200 1.000 67.04277  ?  287  TYR   B CA  1 
ATOM   16242 C  C   . TYR   B 1 287  ? 30.10400   113.65300 -24.46900 1.000 60.21775  ?  287  TYR   B C   1 
ATOM   16243 O  O   . TYR   B 1 287  ? 29.41000   114.47800 -25.07000 1.000 68.87296  ?  287  TYR   B O   1 
ATOM   16244 C  CB  . TYR   B 1 287  ? 30.83000   111.57500 -25.63500 1.000 60.52312  ?  287  TYR   B CB  1 
ATOM   16245 C  CG  . TYR   B 1 287  ? 31.17800   110.12000 -25.42200 1.000 56.50099  ?  287  TYR   B CG  1 
ATOM   16246 C  CD1 . TYR   B 1 287  ? 30.71700   109.42600 -24.31200 1.000 76.99681  ?  287  TYR   B CD1 1 
ATOM   16247 C  CD2 . TYR   B 1 287  ? 31.98300   109.44500 -26.32800 1.000 54.17450  ?  287  TYR   B CD2 1 
ATOM   16248 C  CE1 . TYR   B 1 287  ? 31.04000   108.09500 -24.11700 1.000 82.48461  ?  287  TYR   B CE1 1 
ATOM   16249 C  CE2 . TYR   B 1 287  ? 32.31300   108.11700 -26.14300 1.000 57.35239  ?  287  TYR   B CE2 1 
ATOM   16250 C  CZ  . TYR   B 1 287  ? 31.84000   107.44700 -25.03700 1.000 69.88053  ?  287  TYR   B CZ  1 
ATOM   16251 O  OH  . TYR   B 1 287  ? 32.16900   106.12400 -24.85200 1.000 80.52847  ?  287  TYR   B OH  1 
ATOM   16252 N  N   . PRO   B 1 288  ? 31.09100   114.03000 -23.65800 1.000 55.24136  ?  288  PRO   B N   1 
ATOM   16253 C  CA  . PRO   B 1 288  ? 31.53800   115.42600 -23.65500 1.000 59.61269  ?  288  PRO   B CA  1 
ATOM   16254 C  C   . PRO   B 1 288  ? 31.98800   115.84500 -25.04600 1.000 78.87035  ?  288  PRO   B C   1 
ATOM   16255 O  O   . PRO   B 1 288  ? 32.60600   115.06900 -25.77800 1.000 89.52127  ?  288  PRO   B O   1 
ATOM   16256 C  CB  . PRO   B 1 288  ? 32.70100   115.42500 -22.65700 1.000 57.76787  ?  288  PRO   B CB  1 
ATOM   16257 C  CG  . PRO   B 1 288  ? 32.41500   114.27100 -21.75500 1.000 57.40089  ?  288  PRO   B CG  1 
ATOM   16258 C  CD  . PRO   B 1 288  ? 31.76900   113.22900 -22.62400 1.000 73.71533  ?  288  PRO   B CD  1 
ATOM   16259 N  N   . GLY   B 1 289  ? 31.65900   117.08700 -25.41200 1.000 78.38429  ?  289  GLY   B N   1 
ATOM   16260 C  CA  . GLY   B 1 289  ? 31.99500   117.57500 -26.74000 1.000 59.17834  ?  289  GLY   B CA  1 
ATOM   16261 C  C   . GLY   B 1 289  ? 33.48000   117.52800 -27.04000 1.000 62.83578  ?  289  GLY   B C   1 
ATOM   16262 O  O   . GLY   B 1 289  ? 33.87800   117.42800 -28.20400 1.000 68.58538  ?  289  GLY   B O   1 
ATOM   16263 N  N   . GLU   B 1 290  ? 34.31600   117.60100 -26.00100 1.000 71.98555  ?  290  GLU   B N   1 
ATOM   16264 C  CA  . GLU   B 1 290  ? 35.75700   117.48400 -26.19600 1.000 72.23760  ?  290  GLU   B CA  1 
ATOM   16265 C  C   . GLU   B 1 290  ? 36.12300   116.12800 -26.78600 1.000 71.51351  ?  290  GLU   B C   1 
ATOM   16266 O  O   . GLU   B 1 290  ? 36.95500   116.04200 -27.69600 1.000 75.23726  ?  290  GLU   B O   1 
ATOM   16267 C  CB  . GLU   B 1 290  ? 36.48100   117.70700 -24.86700 1.000 79.60394  ?  290  GLU   B CB  1 
ATOM   16268 C  CG  . GLU   B 1 290  ? 36.06600   116.73400 -23.76800 1.000 96.52749  ?  290  GLU   B CG  1 
ATOM   16269 C  CD  . GLU   B 1 290  ? 36.05600   117.36100 -22.39100 1.000 108.32334 ?  290  GLU   B CD  1 
ATOM   16270 O  OE1 . GLU   B 1 290  ? 37.12700   117.41700 -21.75100 1.000 100.39316 ?  290  GLU   B OE1 1 
ATOM   16271 O  OE2 . GLU   B 1 290  ? 34.97300   117.80100 -21.95100 1.000 88.91229  -1 290  GLU   B OE2 1 
ATOM   16272 N  N   . ARG   B 1 291  ? 35.50300   115.05700 -26.28500 1.000 59.08768  ?  291  ARG   B N   1 
ATOM   16273 C  CA  . ARG   B 1 291  ? 35.79200   113.72800 -26.80600 1.000 58.68689  ?  291  ARG   B CA  1 
ATOM   16274 C  C   . ARG   B 1 291  ? 35.27400   113.58500 -28.23000 1.000 54.78346  ?  291  ARG   B C   1 
ATOM   16275 O  O   . ARG   B 1 291  ? 36.02500   113.20800 -29.13600 1.000 60.09328  ?  291  ARG   B O   1 
ATOM   16276 C  CB  . ARG   B 1 291  ? 35.19100   112.66300 -25.88500 1.000 58.33566  ?  291  ARG   B CB  1 
ATOM   16277 C  CG  . ARG   B 1 291  ? 35.66800   111.24400 -26.17200 1.000 59.07978  ?  291  ARG   B CG  1 
ATOM   16278 C  CD  . ARG   B 1 291  ? 35.38300   110.30600 -25.00600 1.000 60.21184  ?  291  ARG   B CD  1 
ATOM   16279 N  NE  . ARG   B 1 291  ? 35.60500   108.90900 -25.36100 1.000 65.44637  ?  291  ARG   B NE  1 
ATOM   16280 C  CZ  . ARG   B 1 291  ? 36.76100   108.27100 -25.22800 1.000 63.70640  ?  291  ARG   B CZ  1 
ATOM   16281 N  NH1 . ARG   B 1 291  ? 37.83500   108.87600 -24.74800 1.000 64.36443  ?  291  ARG   B NH1 1 
ATOM   16282 N  NH2 . ARG   B 1 291  ? 36.84000   106.99200 -25.58600 1.000 68.92177  ?  291  ARG   B NH2 1 
ATOM   16283 N  N   . ILE   B 1 292  ? 33.99700   113.91900 -28.44900 1.000 46.58752  ?  292  ILE   B N   1 
ATOM   16284 C  CA  . ILE   B 1 292  ? 33.41800   113.88500 -29.79300 1.000 45.57009  ?  292  ILE   B CA  1 
ATOM   16285 C  C   . ILE   B 1 292  ? 34.30000   114.64300 -30.77600 1.000 50.72559  ?  292  ILE   B C   1 
ATOM   16286 O  O   . ILE   B 1 292  ? 34.44600   114.24700 -31.94000 1.000 47.17062  ?  292  ILE   B O   1 
ATOM   16287 C  CB  . ILE   B 1 292  ? 31.98500   114.45000 -29.76500 1.000 49.53000  ?  292  ILE   B CB  1 
ATOM   16288 C  CG1 . ILE   B 1 292  ? 31.13500   113.68800 -28.74600 1.000 56.99915  ?  292  ILE   B CG1 1 
ATOM   16289 C  CG2 . ILE   B 1 292  ? 31.35300   114.39000 -31.15100 1.000 31.33752  ?  292  ILE   B CG2 1 
ATOM   16290 C  CD1 . ILE   B 1 292  ? 29.76300   114.28100 -28.52900 1.000 55.86309  ?  292  ILE   B CD1 1 
ATOM   16291 N  N   . ALA   B 1 293  ? 34.91700   115.73500 -30.32000 1.000 57.71282  ?  293  ALA   B N   1 
ATOM   16292 C  CA  . ALA   B 1 293  ? 35.86400   116.45800 -31.16200 1.000 60.73251  ?  293  ALA   B CA  1 
ATOM   16293 C  C   . ALA   B 1 293  ? 37.14700   115.65900 -31.35600 1.000 65.26898  ?  293  ALA   B C   1 
ATOM   16294 O  O   . ALA   B 1 293  ? 37.66500   115.55900 -32.47500 1.000 59.17085  ?  293  ALA   B O   1 
ATOM   16295 C  CB  . ALA   B 1 293  ? 36.16500   117.82800 -30.55300 1.000 58.54470  ?  293  ALA   B CB  1 
ATOM   16296 N  N   . TYR   B 1 294  ? 37.67500   115.08100 -30.27400 1.000 58.71408  ?  294  TYR   B N   1 
ATOM   16297 C  CA  . TYR   B 1 294  ? 38.89000   114.27900 -30.37600 1.000 53.22787  ?  294  TYR   B CA  1 
ATOM   16298 C  C   . TYR   B 1 294  ? 38.66100   113.04400 -31.23900 1.000 49.60107  ?  294  TYR   B C   1 
ATOM   16299 O  O   . TYR   B 1 294  ? 39.47100   112.72800 -32.11800 1.000 62.92901  ?  294  TYR   B O   1 
ATOM   16300 C  CB  . TYR   B 1 294  ? 39.37800   113.88300 -28.97900 1.000 58.78714  ?  294  TYR   B CB  1 
ATOM   16301 C  CG  . TYR   B 1 294  ? 40.60300   112.99000 -28.97300 1.000 73.91589  ?  294  TYR   B CG  1 
ATOM   16302 C  CD1 . TYR   B 1 294  ? 40.48100   111.60700 -29.05300 1.000 76.02544  ?  294  TYR   B CD1 1 
ATOM   16303 C  CD2 . TYR   B 1 294  ? 41.88000   113.52700 -28.87700 1.000 65.11916  ?  294  TYR   B CD2 1 
ATOM   16304 C  CE1 . TYR   B 1 294  ? 41.59200   110.79000 -29.05000 1.000 63.85585  ?  294  TYR   B CE1 1 
ATOM   16305 C  CE2 . TYR   B 1 294  ? 42.99900   112.71400 -28.86900 1.000 75.57570  ?  294  TYR   B CE2 1 
ATOM   16306 C  CZ  . TYR   B 1 294  ? 42.84700   111.34600 -28.95500 1.000 73.45787  ?  294  TYR   B CZ  1 
ATOM   16307 O  OH  . TYR   B 1 294  ? 43.95300   110.52900 -28.95000 1.000 91.00744  ?  294  TYR   B OH  1 
ATOM   16308 N  N   . MET   B 1 295  ? 37.55900   112.32800 -30.99800 1.000 45.72934  ?  295  MET   B N   1 
ATOM   16309 C  CA  . MET   B 1 295  ? 37.30300   111.09700 -31.74000 1.000 42.34653  ?  295  MET   B CA  1 
ATOM   16310 C  C   . MET   B 1 295  ? 37.06000   111.38200 -33.21600 1.000 52.34945  ?  295  MET   B C   1 
ATOM   16311 O  O   . MET   B 1 295  ? 37.48400   110.60800 -34.08200 1.000 63.18797  ?  295  MET   B O   1 
ATOM   16312 C  CB  . MET   B 1 295  ? 36.11900   110.34900 -31.12600 1.000 52.35900  ?  295  MET   B CB  1 
ATOM   16313 C  CG  . MET   B 1 295  ? 36.20700   110.23300 -29.60900 1.000 50.73991  ?  295  MET   B CG  1 
ATOM   16314 S  SD  . MET   B 1 295  ? 35.36800   108.81500 -28.87700 1.000 52.10844  ?  295  MET   B SD  1 
ATOM   16315 C  CE  . MET   B 1 295  ? 33.68200   109.08200 -29.40700 1.000 37.74682  ?  295  MET   B CE  1 
ATOM   16316 N  N   . LEU   B 1 296  ? 36.38400   112.49100 -33.52500 1.000 48.72037  ?  296  LEU   B N   1 
ATOM   16317 C  CA  . LEU   B 1 296  ? 36.20200   112.87200 -34.92100 1.000 53.48087  ?  296  LEU   B CA  1 
ATOM   16318 C  C   . LEU   B 1 296  ? 37.51200   113.31300 -35.55900 1.000 45.81601  ?  296  LEU   B C   1 
ATOM   16319 O  O   . LEU   B 1 296  ? 37.72200   113.08800 -36.75600 1.000 52.45464  ?  296  LEU   B O   1 
ATOM   16320 C  CB  . LEU   B 1 296  ? 35.16200   113.98500 -35.03800 1.000 47.08954  ?  296  LEU   B CB  1 
ATOM   16321 C  CG  . LEU   B 1 296  ? 33.71300   113.53700 -35.21300 1.000 49.38982  ?  296  LEU   B CG  1 
ATOM   16322 C  CD1 . LEU   B 1 296  ? 32.80000   114.74100 -35.36500 1.000 41.66115  ?  296  LEU   B CD1 1 
ATOM   16323 C  CD2 . LEU   B 1 296  ? 33.59300   112.61200 -36.41400 1.000 52.97341  ?  296  LEU   B CD2 1 
ATOM   16324 N  N   . ALA   B 1 297  ? 38.39900   113.93800 -34.78300 1.000 49.82134  ?  297  ALA   B N   1 
ATOM   16325 C  CA  . ALA   B 1 297  ? 39.66300   114.41100 -35.33700 1.000 57.51838  ?  297  ALA   B CA  1 
ATOM   16326 C  C   . ALA   B 1 297  ? 40.62000   113.25400 -35.59300 1.000 47.23188  ?  297  ALA   B C   1 
ATOM   16327 O  O   . ALA   B 1 297  ? 41.24900   113.18000 -36.65500 1.000 55.68906  ?  297  ALA   B O   1 
ATOM   16328 C  CB  . ALA   B 1 297  ? 40.29600   115.43800 -34.39900 1.000 43.09055  ?  297  ALA   B CB  1 
ATOM   16329 N  N   . ASP   B 1 298  ? 40.74100   112.33700 -34.62900 1.000 39.57312  ?  298  ASP   B N   1 
ATOM   16330 C  CA  . ASP   B 1 298  ? 41.68700   111.23300 -34.77000 1.000 46.67786  ?  298  ASP   B CA  1 
ATOM   16331 C  C   . ASP   B 1 298  ? 41.30100   110.31900 -35.92400 1.000 45.49591  ?  298  ASP   B C   1 
ATOM   16332 O  O   . ASP   B 1 298  ? 42.16300   109.88000 -36.69400 1.000 62.80401  ?  298  ASP   B O   1 
ATOM   16333 C  CB  . ASP   B 1 298  ? 41.76900   110.44000 -33.46600 1.000 38.07802  ?  298  ASP   B CB  1 
ATOM   16334 C  CG  . ASP   B 1 298  ? 42.99100   109.54300 -33.40700 1.000 64.79065  ?  298  ASP   B CG  1 
ATOM   16335 O  OD1 . ASP   B 1 298  ? 43.97600   109.82800 -34.12300 1.000 59.00437  ?  298  ASP   B OD1 1 
ATOM   16336 O  OD2 . ASP   B 1 298  ? 42.96500   108.55000 -32.65100 1.000 71.74685  -1 298  ASP   B OD2 1 
ATOM   16337 N  N   . SER   B 1 299  ? 40.01500   110.01800 -36.05900 1.000 51.47720  ?  299  SER   B N   1 
ATOM   16338 C  CA  . SER   B 1 299  ? 39.56000   109.19300 -37.16400 1.000 50.59297  ?  299  SER   B CA  1 
ATOM   16339 C  C   . SER   B 1 299  ? 39.72600   109.93400 -38.48600 1.000 57.65847  ?  299  SER   B C   1 
ATOM   16340 O  O   . SER   B 1 299  ? 39.62300   111.16100 -38.55600 1.000 61.78635  ?  299  SER   B O   1 
ATOM   16341 C  CB  . SER   B 1 299  ? 38.09700   108.79600 -36.96400 1.000 36.40862  ?  299  SER   B CB  1 
ATOM   16342 O  OG  . SER   B 1 299  ? 37.61700   108.02900 -38.05600 1.000 45.93879  ?  299  SER   B OG  1 
ATOM   16343 N  N   . SER   B 1 300  ? 39.98900   109.17100 -39.54500 1.000 57.41161  ?  300  SER   B N   1 
ATOM   16344 C  CA  . SER   B 1 300  ? 39.97100   109.70900 -40.89900 1.000 55.56350  ?  300  SER   B CA  1 
ATOM   16345 C  C   . SER   B 1 300  ? 38.55700   109.99300 -41.39500 1.000 67.86469  ?  300  SER   B C   1 
ATOM   16346 O  O   . SER   B 1 300  ? 38.37600   110.25800 -42.58700 1.000 75.19492  ?  300  SER   B O   1 
ATOM   16347 C  CB  . SER   B 1 300  ? 40.67800   108.74700 -41.86200 1.000 61.90637  ?  300  SER   B CB  1 
ATOM   16348 O  OG  . SER   B 1 300  ? 39.84700   107.64500 -42.19500 1.000 63.97808  ?  300  SER   B OG  1 
ATOM   16349 N  N   . ALA   B 1 301  ? 37.57100   109.95400 -40.50200 1.000 65.74326  ?  301  ALA   B N   1 
ATOM   16350 C  CA  . ALA   B 1 301  ? 36.17000   110.06300 -40.88800 1.000 57.91907  ?  301  ALA   B CA  1 
ATOM   16351 C  C   . ALA   B 1 301  ? 35.89200   111.38400 -41.59100 1.000 69.36150  ?  301  ALA   B C   1 
ATOM   16352 O  O   . ALA   B 1 301  ? 36.06600   112.46100 -41.01000 1.000 69.38268  ?  301  ALA   B O   1 
ATOM   16353 C  CB  . ALA   B 1 301  ? 35.27200   109.91500 -39.65700 1.000 49.08889  ?  301  ALA   B CB  1 
ATOM   16354 N  N   . ALA   B 1 302  ? 35.46300   111.29300 -42.84900 1.000 49.17008  ?  302  ALA   B N   1 
ATOM   16355 C  CA  . ALA   B 1 302  ? 34.94100   112.43900 -43.58200 1.000 57.31857  ?  302  ALA   B CA  1 
ATOM   16356 C  C   . ALA   B 1 302  ? 33.42300   112.48600 -43.58400 1.000 71.19112  ?  302  ALA   B C   1 
ATOM   16357 O  O   . ALA   B 1 302  ? 32.84300   113.57400 -43.66500 1.000 71.43913  ?  302  ALA   B O   1 
ATOM   16358 C  CB  . ALA   B 1 302  ? 35.44500   112.41700 -45.02800 1.000 67.23416  ?  302  ALA   B CB  1 
ATOM   16359 N  N   . ILE   B 1 303  ? 32.77800   111.32800 -43.48000 1.000 69.57704  ?  303  ILE   B N   1 
ATOM   16360 C  CA  . ILE   B 1 303  ? 31.32700   111.20100 -43.51100 1.000 52.00971  ?  303  ILE   B CA  1 
ATOM   16361 C  C   . ILE   B 1 303  ? 30.84700   110.87800 -42.10400 1.000 57.68606  ?  303  ILE   B C   1 
ATOM   16362 O  O   . ILE   B 1 303  ? 31.41700   110.01000 -41.43000 1.000 59.56010  ?  303  ILE   B O   1 
ATOM   16363 C  CB  . ILE   B 1 303  ? 30.89000   110.11600 -44.51100 1.000 57.18734  ?  303  ILE   B CB  1 
ATOM   16364 C  CG1 . ILE   B 1 303  ? 31.01400   110.63400 -45.94500 1.000 52.51772  ?  303  ILE   B CG1 1 
ATOM   16365 C  CG2 . ILE   B 1 303  ? 29.48000   109.63100 -44.21200 1.000 47.51409  ?  303  ILE   B CG2 1 
ATOM   16366 C  CD1 . ILE   B 1 303  ? 30.85600   109.55900 -46.99500 1.000 50.78561  ?  303  ILE   B CD1 1 
ATOM   16367 N  N   . LEU   B 1 304  ? 29.80600   111.57800 -41.65800 1.000 60.62939  ?  304  LEU   B N   1 
ATOM   16368 C  CA  . LEU   B 1 304  ? 29.21700   111.36300 -40.34100 1.000 59.14287  ?  304  LEU   B CA  1 
ATOM   16369 C  C   . LEU   B 1 304  ? 27.72700   111.10300 -40.50800 1.000 51.72943  ?  304  LEU   B C   1 
ATOM   16370 O  O   . LEU   B 1 304  ? 26.96300   112.02600 -40.81300 1.000 66.51100  ?  304  LEU   B O   1 
ATOM   16371 C  CB  . LEU   B 1 304  ? 29.45500   112.56100 -39.42500 1.000 54.98616  ?  304  LEU   B CB  1 
ATOM   16372 C  CG  . LEU   B 1 304  ? 28.73200   112.51100 -38.08000 1.000 37.33483  ?  304  LEU   B CG  1 
ATOM   16373 C  CD1 . LEU   B 1 304  ? 29.43500   111.57100 -37.11500 1.000 48.13042  ?  304  LEU   B CD1 1 
ATOM   16374 C  CD2 . LEU   B 1 304  ? 28.62300   113.90400 -37.50000 1.000 40.34871  ?  304  LEU   B CD2 1 
ATOM   16375 N  N   . LEU   B 1 305  ? 27.31500   109.85500 -40.31000 1.000 47.38088  ?  305  LEU   B N   1 
ATOM   16376 C  CA  . LEU   B 1 305  ? 25.90000   109.49600 -40.31900 1.000 40.69793  ?  305  LEU   B CA  1 
ATOM   16377 C  C   . LEU   B 1 305  ? 25.30500   109.92300 -38.98400 1.000 43.43500  ?  305  LEU   B C   1 
ATOM   16378 O  O   . LEU   B 1 305  ? 25.49600   109.25600 -37.96500 1.000 52.99643  ?  305  LEU   B O   1 
ATOM   16379 C  CB  . LEU   B 1 305  ? 25.72400   108.00100 -40.55000 1.000 36.06565  ?  305  LEU   B CB  1 
ATOM   16380 C  CG  . LEU   B 1 305  ? 26.38600   107.40400 -41.79200 1.000 40.49985  ?  305  LEU   B CG  1 
ATOM   16381 C  CD1 . LEU   B 1 305  ? 26.72800   105.94400 -41.55400 1.000 45.21885  ?  305  LEU   B CD1 1 
ATOM   16382 C  CD2 . LEU   B 1 305  ? 25.48000   107.54500 -43.00200 1.000 45.39340  ?  305  LEU   B CD2 1 
ATOM   16383 N  N   . THR   B 1 306  ? 24.59000   111.04700 -38.97700 1.000 57.99132  ?  306  THR   B N   1 
ATOM   16384 C  CA  . THR   B 1 306  ? 23.98100   111.56300 -37.76000 1.000 57.08971  ?  306  THR   B CA  1 
ATOM   16385 C  C   . THR   B 1 306  ? 22.58900   112.09400 -38.08600 1.000 60.45635  ?  306  THR   B C   1 
ATOM   16386 O  O   . THR   B 1 306  ? 22.11200   111.99300 -39.22100 1.000 55.08654  ?  306  THR   B O   1 
ATOM   16387 C  CB  . THR   B 1 306  ? 24.85700   112.64100 -37.11100 1.000 49.54918  ?  306  THR   B CB  1 
ATOM   16388 O  OG1 . THR   B 1 306  ? 24.33700   112.96400 -35.81500 1.000 56.74998  ?  306  THR   B OG1 1 
ATOM   16389 C  CG2 . THR   B 1 306  ? 24.88700   113.89300 -37.96700 1.000 46.07764  ?  306  THR   B CG2 1 
ATOM   16390 N  N   . ASN   B 1 307  ? 21.93000   112.64900 -37.07500 1.000 54.87030  ?  307  ASN   B N   1 
ATOM   16391 C  CA  . ASN   B 1 307  ? 20.60800   113.24700 -37.21200 1.000 49.19636  ?  307  ASN   B CA  1 
ATOM   16392 C  C   . ASN   B 1 307  ? 20.69600   114.74600 -36.93700 1.000 53.46199  ?  307  ASN   B C   1 
ATOM   16393 O  O   . ASN   B 1 307  ? 21.75800   115.28100 -36.61100 1.000 52.51405  ?  307  ASN   B O   1 
ATOM   16394 C  CB  . ASN   B 1 307  ? 19.59800   112.56500 -36.28100 1.000 44.07737  ?  307  ASN   B CB  1 
ATOM   16395 C  CG  . ASN   B 1 307  ? 20.05500   112.53200 -34.83000 1.000 59.98487  ?  307  ASN   B CG  1 
ATOM   16396 O  OD1 . ASN   B 1 307  ? 20.71100   113.45500 -34.34500 1.000 67.88613  ?  307  ASN   B OD1 1 
ATOM   16397 N  ND2 . ASN   B 1 307  ? 19.70700   111.45900 -34.12900 1.000 56.24179  ?  307  ASN   B ND2 1 
ATOM   16398 N  N   . ALA   B 1 308  ? 19.55300   115.42500 -37.06500 1.000 53.92781  ?  308  ALA   B N   1 
ATOM   16399 C  CA  . ALA   B 1 308  ? 19.52300   116.86900 -36.85400 1.000 59.58195  ?  308  ALA   B CA  1 
ATOM   16400 C  C   . ALA   B 1 308  ? 19.80800   117.23700 -35.40400 1.000 61.19050  ?  308  ALA   B C   1 
ATOM   16401 O  O   . ALA   B 1 308  ? 20.37300   118.30400 -35.13700 1.000 70.08252  ?  308  ALA   B O   1 
ATOM   16402 C  CB  . ALA   B 1 308  ? 18.17100   117.43400 -37.28800 1.000 38.96966  ?  308  ALA   B CB  1 
ATOM   16403 N  N   . LEU   B 1 309  ? 19.43000   116.37400 -34.45800 1.000 55.34825  ?  309  LEU   B N   1 
ATOM   16404 C  CA  . LEU   B 1 309  ? 19.63900   116.67800 -33.04700 1.000 49.00508  ?  309  LEU   B CA  1 
ATOM   16405 C  C   . LEU   B 1 309  ? 21.12000   116.76600 -32.70400 1.000 56.57177  ?  309  LEU   B C   1 
ATOM   16406 O  O   . LEU   B 1 309  ? 21.51400   117.56500 -31.84700 1.000 70.84313  ?  309  LEU   B O   1 
ATOM   16407 C  CB  . LEU   B 1 309  ? 18.95200   115.61700 -32.18300 1.000 43.39498  ?  309  LEU   B CB  1 
ATOM   16408 C  CG  . LEU   B 1 309  ? 18.27600   116.02300 -30.87000 1.000 59.10771  ?  309  LEU   B CG  1 
ATOM   16409 C  CD1 . LEU   B 1 309  ? 17.51800   114.83700 -30.29100 1.000 47.43919  ?  309  LEU   B CD1 1 
ATOM   16410 C  CD2 . LEU   B 1 309  ? 19.27200   116.56500 -29.85200 1.000 52.40243  ?  309  LEU   B CD2 1 
ATOM   16411 N  N   . HIS   B 1 310  ? 21.95600   115.96800 -33.36700 1.000 59.91149  ?  310  HIS   B N   1 
ATOM   16412 C  CA  . HIS   B 1 310  ? 23.36400   115.85200 -33.01600 1.000 58.40246  ?  310  HIS   B CA  1 
ATOM   16413 C  C   . HIS   B 1 310  ? 24.30200   116.41400 -34.07500 1.000 59.40390  ?  310  HIS   B C   1 
ATOM   16414 O  O   . HIS   B 1 310  ? 25.52300   116.29100 -33.92300 1.000 68.98570  ?  310  HIS   B O   1 
ATOM   16415 C  CB  . HIS   B 1 310  ? 23.71200   114.38300 -32.75000 1.000 57.61363  ?  310  HIS   B CB  1 
ATOM   16416 C  CG  . HIS   B 1 310  ? 22.78300   113.70800 -31.78800 1.000 58.99372  ?  310  HIS   B CG  1 
ATOM   16417 N  ND1 . HIS   B 1 310  ? 22.30500   114.32800 -30.65400 1.000 54.60682  ?  310  HIS   B ND1 1 
ATOM   16418 C  CD2 . HIS   B 1 310  ? 22.23800   112.46800 -31.79600 1.000 58.62201  ?  310  HIS   B CD2 1 
ATOM   16419 C  CE1 . HIS   B 1 310  ? 21.51100   113.49800 -30.00200 1.000 53.10902  ?  310  HIS   B CE1 1 
ATOM   16420 N  NE2 . HIS   B 1 310  ? 21.45200   112.36400 -30.67500 1.000 49.81018  ?  310  HIS   B NE2 1 
ATOM   16421 N  N   . GLU   B 1 311  ? 23.77100   117.02700 -35.13800 1.000 54.14399  ?  311  GLU   B N   1 
ATOM   16422 C  CA  . GLU   B 1 311  ? 24.62400   117.54800 -36.20400 1.000 54.87332  ?  311  GLU   B CA  1 
ATOM   16423 C  C   . GLU   B 1 311  ? 25.62700   118.56500 -35.67600 1.000 69.43945  ?  311  GLU   B C   1 
ATOM   16424 O  O   . GLU   B 1 311  ? 26.80400   118.54300 -36.05500 1.000 52.29745  ?  311  GLU   B O   1 
ATOM   16425 C  CB  . GLU   B 1 311  ? 23.76900   118.18200 -37.30100 1.000 61.38687  ?  311  GLU   B CB  1 
ATOM   16426 C  CG  . GLU   B 1 311  ? 23.42200   117.25400 -38.44400 1.000 75.78535  ?  311  GLU   B CG  1 
ATOM   16427 C  CD  . GLU   B 1 311  ? 22.74200   117.97700 -39.59100 1.000 89.03612  ?  311  GLU   B CD  1 
ATOM   16428 O  OE1 . GLU   B 1 311  ? 22.85700   119.21800 -39.66400 1.000 80.94821  ?  311  GLU   B OE1 1 
ATOM   16429 O  OE2 . GLU   B 1 311  ? 22.09100   117.30400 -40.41800 1.000 104.46466 -1 311  GLU   B OE2 1 
ATOM   16430 N  N   . GLU   B 1 312  ? 25.17900   119.46300 -34.79800 1.000 77.25375  ?  312  GLU   B N   1 
ATOM   16431 C  CA  . GLU   B 1 312  ? 26.02400   120.56300 -34.34900 1.000 78.91567  ?  312  GLU   B CA  1 
ATOM   16432 C  C   . GLU   B 1 312  ? 27.14900   120.10300 -33.43200 1.000 76.79286  ?  312  GLU   B C   1 
ATOM   16433 O  O   . GLU   B 1 312  ? 28.11300   120.85200 -33.23500 1.000 84.75930  ?  312  GLU   B O   1 
ATOM   16434 C  CB  . GLU   B 1 312  ? 25.16900   121.61500 -33.64500 1.000 88.13113  ?  312  GLU   B CB  1 
ATOM   16435 C  CG  . GLU   B 1 312  ? 23.98200   122.07500 -34.47100 1.000 97.44831  ?  312  GLU   B CG  1 
ATOM   16436 C  CD  . GLU   B 1 312  ? 23.05800   122.99500 -33.70300 1.000 117.04783 ?  312  GLU   B CD  1 
ATOM   16437 O  OE1 . GLU   B 1 312  ? 23.53500   123.67600 -32.77100 1.000 118.72007 ?  312  GLU   B OE1 1 
ATOM   16438 O  OE2 . GLU   B 1 312  ? 21.85300   123.03200 -34.02900 1.000 133.72896 -1 312  GLU   B OE2 1 
ATOM   16439 N  N   . LYS   B 1 313  ? 27.05500   118.89700 -32.87000 1.000 62.00711  ?  313  LYS   B N   1 
ATOM   16440 C  CA  . LYS   B 1 313  ? 28.12200   118.39500 -32.01500 1.000 57.32684  ?  313  LYS   B CA  1 
ATOM   16441 C  C   . LYS   B 1 313  ? 29.38700   118.05900 -32.79500 1.000 73.30116  ?  313  LYS   B C   1 
ATOM   16442 O  O   . LYS   B 1 313  ? 30.43700   117.85400 -32.17700 1.000 78.10603  ?  313  LYS   B O   1 
ATOM   16443 C  CB  . LYS   B 1 313  ? 27.64300   117.16400 -31.24300 1.000 64.59338  ?  313  LYS   B CB  1 
ATOM   16444 C  CG  . LYS   B 1 313  ? 26.24300   117.29900 -30.65800 1.000 78.00993  ?  313  LYS   B CG  1 
ATOM   16445 C  CD  . LYS   B 1 313  ? 26.03700   116.34400 -29.49000 1.000 56.11198  ?  313  LYS   B CD  1 
ATOM   16446 C  CE  . LYS   B 1 313  ? 24.55800   116.10600 -29.20400 1.000 63.88296  ?  313  LYS   B CE  1 
ATOM   16447 N  NZ  . LYS   B 1 313  ? 23.82000   117.33300 -28.79000 1.000 55.57021  ?  313  LYS   B NZ  1 
ATOM   16448 N  N   . ALA   B 1 314  ? 29.31200   117.99800 -34.12400 1.000 64.13966  ?  314  ALA   B N   1 
ATOM   16449 C  CA  . ALA   B 1 314  ? 30.48100   117.77400 -34.96300 1.000 54.15660  ?  314  ALA   B CA  1 
ATOM   16450 C  C   . ALA   B 1 314  ? 31.21700   119.06000 -35.31000 1.000 82.75214  ?  314  ALA   B C   1 
ATOM   16451 O  O   . ALA   B 1 314  ? 32.36300   118.99200 -35.76800 1.000 95.28099  ?  314  ALA   B O   1 
ATOM   16452 C  CB  . ALA   B 1 314  ? 30.07600   117.05700 -36.25500 1.000 47.81631  ?  314  ALA   B CB  1 
ATOM   16453 N  N   . ASN   B 1 315  ? 30.58800   120.22000 -35.10200 1.000 80.55096  ?  315  ASN   B N   1 
ATOM   16454 C  CA  . ASN   B 1 315  ? 31.19200   121.52100 -35.39600 1.000 85.66455  ?  315  ASN   B CA  1 
ATOM   16455 C  C   . ASN   B 1 315  ? 31.63600   121.60700 -36.85500 1.000 82.51747  ?  315  ASN   B C   1 
ATOM   16456 O  O   . ASN   B 1 315  ? 32.70700   122.13200 -37.17000 1.000 85.40127  ?  315  ASN   B O   1 
ATOM   16457 C  CB  . ASN   B 1 315  ? 32.35900   121.81900 -34.44900 1.000 78.60737  ?  315  ASN   B CB  1 
ATOM   16458 C  CG  . ASN   B 1 315  ? 32.66800   123.30000 -34.35400 1.000 95.99761  ?  315  ASN   B CG  1 
ATOM   16459 O  OD1 . ASN   B 1 315  ? 32.41500   124.06200 -35.28700 1.000 114.06716 ?  315  ASN   B OD1 1 
ATOM   16460 N  ND2 . ASN   B 1 315  ? 33.21300   123.71800 -33.21800 1.000 104.62484 ?  315  ASN   B ND2 1 
ATOM   16461 N  N   . GLY   B 1 316  ? 30.80500   121.07900 -37.75000 1.000 85.18058  ?  316  GLY   B N   1 
ATOM   16462 C  CA  . GLY   B 1 316  ? 31.09100   121.12900 -39.17500 1.000 96.12202  ?  316  GLY   B CA  1 
ATOM   16463 C  C   . GLY   B 1 316  ? 32.42600   120.53200 -39.56300 1.000 83.72924  ?  316  GLY   B C   1 
ATOM   16464 O  O   . GLY   B 1 316  ? 33.10700   121.06400 -40.44900 1.000 94.56303  ?  316  GLY   B O   1 
ATOM   16465 N  N   . ALA   B 1 317  ? 32.82200   119.44000 -38.91400 1.000 83.00769  ?  317  ALA   B N   1 
ATOM   16466 C  CA  . ALA   B 1 317  ? 34.09400   118.78900 -39.19000 1.000 83.73242  ?  317  ALA   B CA  1 
ATOM   16467 C  C   . ALA   B 1 317  ? 33.95700   117.58100 -40.10600 1.000 81.37675  ?  317  ALA   B C   1 
ATOM   16468 O  O   . ALA   B 1 317  ? 34.97200   116.97400 -40.46100 1.000 87.08539  ?  317  ALA   B O   1 
ATOM   16469 C  CB  . ALA   B 1 317  ? 34.76900   118.37000 -37.88100 1.000 61.53595  ?  317  ALA   B CB  1 
ATOM   16470 N  N   . CYS   B 1 318  ? 32.73600   117.22200 -40.49900 1.000 74.61155  ?  318  CYS   B N   1 
ATOM   16471 C  CA  . CYS   B 1 318  ? 32.51600   116.05900 -41.34400 1.000 82.74067  ?  318  CYS   B CA  1 
ATOM   16472 C  C   . CYS   B 1 318  ? 31.33200   116.31500 -42.26400 1.000 64.31319  ?  318  CYS   B C   1 
ATOM   16473 O  O   . CYS   B 1 318  ? 30.43500   117.09900 -41.94400 1.000 76.64643  ?  318  CYS   B O   1 
ATOM   16474 C  CB  . CYS   B 1 318  ? 32.26000   114.79500 -40.51300 1.000 78.81522  ?  318  CYS   B CB  1 
ATOM   16475 S  SG  . CYS   B 1 318  ? 33.69000   114.18400 -39.59600 1.000 91.72067  ?  318  CYS   B SG  1 
ATOM   16476 N  N   . ASP   B 1 319  ? 31.34400   115.64200 -43.41300 1.000 55.22083  ?  319  ASP   B N   1 
ATOM   16477 C  CA  . ASP   B 1 319  ? 30.18900   115.65300 -44.30000 1.000 60.82626  ?  319  ASP   B CA  1 
ATOM   16478 C  C   . ASP   B 1 319  ? 29.04600   114.87900 -43.65400 1.000 63.24996  ?  319  ASP   B C   1 
ATOM   16479 O  O   . ASP   B 1 319  ? 29.22000   113.73300 -43.22700 1.000 73.01033  ?  319  ASP   B O   1 
ATOM   16480 C  CB  . ASP   B 1 319  ? 30.55600   115.04900 -45.65500 1.000 60.51794  ?  319  ASP   B CB  1 
ATOM   16481 C  CG  . ASP   B 1 319  ? 29.38000   114.99800 -46.60800 1.000 84.34800  ?  319  ASP   B CG  1 
ATOM   16482 O  OD1 . ASP   B 1 319  ? 28.63000   115.99400 -46.68100 1.000 95.82465  ?  319  ASP   B OD1 1 
ATOM   16483 O  OD2 . ASP   B 1 319  ? 29.21400   113.96900 -47.29600 1.000 86.43574  -1 319  ASP   B OD2 1 
ATOM   16484 N  N   . ILE   B 1 320  ? 27.87700   115.50700 -43.57800 1.000 56.67066  ?  320  ILE   B N   1 
ATOM   16485 C  CA  . ILE   B 1 320  ? 26.75400   114.99500 -42.80400 1.000 49.51403  ?  320  ILE   B CA  1 
ATOM   16486 C  C   . ILE   B 1 320  ? 25.79400   114.26600 -43.73300 1.000 50.39169  ?  320  ILE   B C   1 
ATOM   16487 O  O   . ILE   B 1 320  ? 25.42100   114.78800 -44.79200 1.000 54.96745  ?  320  ILE   B O   1 
ATOM   16488 C  CB  . ILE   B 1 320  ? 26.03900   116.13300 -42.05500 1.000 47.84714  ?  320  ILE   B CB  1 
ATOM   16489 C  CG1 . ILE   B 1 320  ? 27.04300   116.96400 -41.24800 1.000 46.18373  ?  320  ILE   B CG1 1 
ATOM   16490 C  CG2 . ILE   B 1 320  ? 24.95500   115.57200 -41.15400 1.000 49.74108  ?  320  ILE   B CG2 1 
ATOM   16491 C  CD1 . ILE   B 1 320  ? 27.67200   116.22200 -40.09600 1.000 51.45302  ?  320  ILE   B CD1 1 
ATOM   16492 N  N   . ILE   B 1 321  ? 25.38700   113.06300 -43.33700 1.000 46.59329  ?  321  ILE   B N   1 
ATOM   16493 C  CA  . ILE   B 1 321  ? 24.40200   112.27300 -44.06800 1.000 43.56423  ?  321  ILE   B CA  1 
ATOM   16494 C  C   . ILE   B 1 321  ? 23.25500   112.02100 -43.09800 1.000 51.24430  ?  321  ILE   B C   1 
ATOM   16495 O  O   . ILE   B 1 321  ? 23.36700   111.17800 -42.20200 1.000 56.42001  ?  321  ILE   B O   1 
ATOM   16496 C  CB  . ILE   B 1 321  ? 24.98200   110.95500 -44.59300 1.000 46.76273  ?  321  ILE   B CB  1 
ATOM   16497 C  CG1 . ILE   B 1 321  ? 26.41600   111.15500 -45.07500 1.000 56.62279  ?  321  ILE   B CG1 1 
ATOM   16498 C  CG2 . ILE   B 1 321  ? 24.11900   110.41400 -45.72800 1.000 39.45835  ?  321  ILE   B CG2 1 
ATOM   16499 C  CD1 . ILE   B 1 321  ? 26.50700   111.86800 -46.40000 1.000 64.70954  ?  321  ILE   B CD1 1 
ATOM   16500 N  N   . ASP   B 1 322  ? 22.15500   112.74800 -43.25900 1.000 62.27842  ?  322  ASP   B N   1 
ATOM   16501 C  CA  . ASP   B 1 322  ? 21.02800   112.59600 -42.34900 1.000 62.84006  ?  322  ASP   B CA  1 
ATOM   16502 C  C   . ASP   B 1 322  ? 20.35100   111.24800 -42.56500 1.000 57.66051  ?  322  ASP   B C   1 
ATOM   16503 O  O   . ASP   B 1 322  ? 19.89200   110.94200 -43.66900 1.000 54.50540  ?  322  ASP   B O   1 
ATOM   16504 C  CB  . ASP   B 1 322  ? 20.02600   113.72900 -42.56400 1.000 67.92426  ?  322  ASP   B CB  1 
ATOM   16505 C  CG  . ASP   B 1 322  ? 18.96100   113.79600 -41.47800 1.000 79.71142  ?  322  ASP   B CG  1 
ATOM   16506 O  OD1 . ASP   B 1 322  ? 19.31800   113.90100 -40.28700 1.000 86.47959  ?  322  ASP   B OD1 1 
ATOM   16507 O  OD2 . ASP   B 1 322  ? 17.75800   113.76100 -41.81800 1.000 77.73056  -1 322  ASP   B OD2 1 
ATOM   16508 N  N   . VAL   B 1 323  ? 20.27000   110.44300 -41.49900 1.000 57.56939  ?  323  VAL   B N   1 
ATOM   16509 C  CA  . VAL   B 1 323  ? 19.60900   109.14200 -41.58500 1.000 55.95461  ?  323  VAL   B CA  1 
ATOM   16510 C  C   . VAL   B 1 323  ? 18.09200   109.23500 -41.65600 1.000 56.97520  ?  323  VAL   B C   1 
ATOM   16511 O  O   . VAL   B 1 323  ? 17.42900   108.18900 -41.70200 1.000 58.07624  ?  323  VAL   B O   1 
ATOM   16512 C  CB  . VAL   B 1 323  ? 20.00600   108.26900 -40.38200 1.000 50.55568  ?  323  VAL   B CB  1 
ATOM   16513 C  CG1 . VAL   B 1 323  ? 21.41200   107.78100 -40.56700 1.000 42.86444  ?  323  VAL   B CG1 1 
ATOM   16514 C  CG2 . VAL   B 1 323  ? 19.88800   109.08000 -39.09600 1.000 64.54145  ?  323  VAL   B CG2 1 
ATOM   16515 N  N   . HIS   B 1 324  ? 17.50600   110.45000 -41.65700 1.000 59.04479  ?  324  HIS   B N   1 
ATOM   16516 C  CA  . HIS   B 1 324  ? 16.06400   110.64100 -41.80500 1.000 58.07654  ?  324  HIS   B CA  1 
ATOM   16517 C  C   . HIS   B 1 324  ? 15.65700   111.25200 -43.13900 1.000 66.67551  ?  324  HIS   B C   1 
ATOM   16518 O  O   . HIS   B 1 324  ? 14.51200   111.06500 -43.56300 1.000 76.18113  ?  324  HIS   B O   1 
ATOM   16519 C  CB  . HIS   B 1 324  ? 15.51200   111.52000 -40.66700 1.000 67.10636  ?  324  HIS   B CB  1 
ATOM   16520 C  CG  . HIS   B 1 324  ? 15.48900   110.83200 -39.33600 1.000 73.42816  ?  324  HIS   B CG  1 
ATOM   16521 N  ND1 . HIS   B 1 324  ? 15.46900   111.50900 -38.13400 1.000 83.65057  ?  324  HIS   B ND1 1 
ATOM   16522 C  CD2 . HIS   B 1 324  ? 15.49300   109.51500 -39.02300 1.000 79.26296  ?  324  HIS   B CD2 1 
ATOM   16523 C  CE1 . HIS   B 1 324  ? 15.46100   110.63800 -37.14000 1.000 91.67599  ?  324  HIS   B CE1 1 
ATOM   16524 N  NE2 . HIS   B 1 324  ? 15.47500   109.42100 -37.65300 1.000 100.72615 ?  324  HIS   B NE2 1 
ATOM   16525 N  N   . ASP   B 1 325  ? 16.55400   111.96900 -43.80000 1.000 61.76973  ?  325  ASP   B N   1 
ATOM   16526 C  CA  . ASP   B 1 325  ? 16.28000   112.50100 -45.12500 1.000 61.81516  ?  325  ASP   B CA  1 
ATOM   16527 C  C   . ASP   B 1 325  ? 16.18200   111.35400 -46.12100 1.000 61.80038  ?  325  ASP   B C   1 
ATOM   16528 O  O   . ASP   B 1 325  ? 17.13300   110.56900 -46.24500 1.000 66.05438  ?  325  ASP   B O   1 
ATOM   16529 C  CB  . ASP   B 1 325  ? 17.37300   113.47800 -45.54100 1.000 60.96049  ?  325  ASP   B CB  1 
ATOM   16530 C  CG  . ASP   B 1 325  ? 17.32900   113.80600 -47.02500 1.000 71.72733  ?  325  ASP   B CG  1 
ATOM   16531 O  OD1 . ASP   B 1 325  ? 16.23500   114.13000 -47.53500 1.000 81.67144  ?  325  ASP   B OD1 1 
ATOM   16532 O  OD2 . ASP   B 1 325  ? 18.38800   113.73800 -47.68300 1.000 82.87663  -1 325  ASP   B OD2 1 
ATOM   16533 N  N   . PRO   B 1 326  ? 15.06700   111.21400 -46.83900 1.000 70.59048  ?  326  PRO   B N   1 
ATOM   16534 C  CA  . PRO   B 1 326  ? 14.93100   110.08600 -47.77400 1.000 73.40008  ?  326  PRO   B CA  1 
ATOM   16535 C  C   . PRO   B 1 326  ? 15.92200   110.11900 -48.92100 1.000 62.71797  ?  326  PRO   B C   1 
ATOM   16536 O  O   . PRO   B 1 326  ? 16.16200   109.07500 -49.54000 1.000 55.82770  ?  326  PRO   B O   1 
ATOM   16537 C  CB  . PRO   B 1 326  ? 13.48800   110.22200 -48.28000 1.000 67.58168  ?  326  PRO   B CB  1 
ATOM   16538 C  CG  . PRO   B 1 326  ? 12.79100   111.05000 -47.24600 1.000 70.39675  ?  326  PRO   B CG  1 
ATOM   16539 C  CD  . PRO   B 1 326  ? 13.82800   112.00100 -46.73300 1.000 60.88402  ?  326  PRO   B CD  1 
ATOM   16540 N  N   . ASP   B 1 327  ? 16.50500   111.28000 -49.22900 1.000 58.99066  ?  327  ASP   B N   1 
ATOM   16541 C  CA  . ASP   B 1 327  ? 17.48700   111.35600 -50.30400 1.000 80.80315  ?  327  ASP   B CA  1 
ATOM   16542 C  C   . ASP   B 1 327  ? 18.80400   110.68900 -49.93200 1.000 71.98292  ?  327  ASP   B C   1 
ATOM   16543 O  O   . ASP   B 1 327  ? 19.60900   110.39600 -50.82300 1.000 59.04801  ?  327  ASP   B O   1 
ATOM   16544 C  CB  . ASP   B 1 327  ? 17.72500   112.81600 -50.69200 1.000 75.31577  ?  327  ASP   B CB  1 
ATOM   16545 C  CG  . ASP   B 1 327  ? 16.52800   113.43400 -51.39000 1.000 82.68306  ?  327  ASP   B CG  1 
ATOM   16546 O  OD1 . ASP   B 1 327  ? 15.99400   112.80300 -52.32700 1.000 84.28045  ?  327  ASP   B OD1 1 
ATOM   16547 O  OD2 . ASP   B 1 327  ? 16.11700   114.54600 -50.99600 1.000 89.89753  -1 327  ASP   B OD2 1 
ATOM   16548 N  N   . SER   B 1 328  ? 19.04300   110.44400 -48.64400 1.000 72.81448  ?  328  SER   B N   1 
ATOM   16549 C  CA  . SER   B 1 328  ? 20.21900   109.69900 -48.21800 1.000 60.76330  ?  328  SER   B CA  1 
ATOM   16550 C  C   . SER   B 1 328  ? 20.07400   108.19900 -48.43500 1.000 62.41163  ?  328  SER   B C   1 
ATOM   16551 O  O   . SER   B 1 328  ? 21.05000   107.46600 -48.24300 1.000 66.12509  ?  328  SER   B O   1 
ATOM   16552 C  CB  . SER   B 1 328  ? 20.51200   109.97200 -46.74000 1.000 42.86080  ?  328  SER   B CB  1 
ATOM   16553 O  OG  . SER   B 1 328  ? 20.76000   111.34900 -46.51600 1.000 64.53047  ?  328  SER   B OG  1 
ATOM   16554 N  N   . TYR   B 1 329  ? 18.89200   107.73100 -48.82700 1.000 42.31592  ?  329  TYR   B N   1 
ATOM   16555 C  CA  . TYR   B 1 329  ? 18.62700   106.31700 -49.04600 1.000 55.96572  ?  329  TYR   B CA  1 
ATOM   16556 C  C   . TYR   B 1 329  ? 18.34100   106.08000 -50.52100 1.000 59.12003  ?  329  TYR   B C   1 
ATOM   16557 O  O   . TYR   B 1 329  ? 17.45300   106.71800 -51.09700 1.000 64.62168  ?  329  TYR   B O   1 
ATOM   16558 C  CB  . TYR   B 1 329  ? 17.44800   105.83900 -48.19400 1.000 54.31427  ?  329  TYR   B CB  1 
ATOM   16559 C  CG  . TYR   B 1 329  ? 17.72100   105.85200 -46.70800 1.000 42.29403  ?  329  TYR   B CG  1 
ATOM   16560 C  CD1 . TYR   B 1 329  ? 17.63000   107.02800 -45.97600 1.000 41.67125  ?  329  TYR   B CD1 1 
ATOM   16561 C  CD2 . TYR   B 1 329  ? 18.06700   104.68700 -46.03600 1.000 41.15073  ?  329  TYR   B CD2 1 
ATOM   16562 C  CE1 . TYR   B 1 329  ? 17.88000   107.04600 -44.61800 1.000 45.36929  ?  329  TYR   B CE1 1 
ATOM   16563 C  CE2 . TYR   B 1 329  ? 18.31800   104.69400 -44.67700 1.000 45.74233  ?  329  TYR   B CE2 1 
ATOM   16564 C  CZ  . TYR   B 1 329  ? 18.22200   105.87700 -43.97300 1.000 46.98901  ?  329  TYR   B CZ  1 
ATOM   16565 O  OH  . TYR   B 1 329  ? 18.47000   105.89300 -42.62100 1.000 46.94108  ?  329  TYR   B OH  1 
ATOM   16566 N  N   . SER   B 1 330  ? 19.09200   105.16300 -51.12500 1.000 52.05552  ?  330  SER   B N   1 
ATOM   16567 C  CA  . SER   B 1 330  ? 18.89400   104.82100 -52.52300 1.000 48.70101  ?  330  SER   B CA  1 
ATOM   16568 C  C   . SER   B 1 330  ? 17.61200   104.00700 -52.69300 1.000 55.78857  ?  330  SER   B C   1 
ATOM   16569 O  O   . SER   B 1 330  ? 16.88200   103.72400 -51.73900 1.000 57.65943  ?  330  SER   B O   1 
ATOM   16570 C  CB  . SER   B 1 330  ? 20.10000   104.05100 -53.05600 1.000 53.19569  ?  330  SER   B CB  1 
ATOM   16571 O  OG  . SER   B 1 330  ? 19.78500   103.37600 -54.26100 1.000 61.50463  ?  330  SER   B OG  1 
ATOM   16572 N  N   . GLU   B 1 331  ? 17.34000   103.62800 -53.93900 1.000 60.37581  ?  331  GLU   B N   1 
ATOM   16573 C  CA  . GLU   B 1 331  ? 16.19200   102.80100 -54.27500 1.000 58.79403  ?  331  GLU   B CA  1 
ATOM   16574 C  C   . GLU   B 1 331  ? 16.56100   101.33500 -54.44900 1.000 68.14929  ?  331  GLU   B C   1 
ATOM   16575 O  O   . GLU   B 1 331  ? 15.66200   100.49400 -54.56200 1.000 68.02927  ?  331  GLU   B O   1 
ATOM   16576 C  CB  . GLU   B 1 331  ? 15.52500   103.31100 -55.56100 1.000 75.66832  ?  331  GLU   B CB  1 
ATOM   16577 C  CG  . GLU   B 1 331  ? 15.38900   104.82900 -55.65100 1.000 94.99013  ?  331  GLU   B CG  1 
ATOM   16578 C  CD  . GLU   B 1 331  ? 16.67000   105.51200 -56.10700 1.000 100.91887 ?  331  GLU   B CD  1 
ATOM   16579 O  OE1 . GLU   B 1 331  ? 17.54100   104.82400 -56.68100 1.000 103.41219 ?  331  GLU   B OE1 1 
ATOM   16580 O  OE2 . GLU   B 1 331  ? 16.80900   106.73300 -55.88200 1.000 96.42747  -1 331  GLU   B OE2 1 
ATOM   16581 N  N   . ASN   B 1 332  ? 17.85200   101.01500 -54.46700 1.000 60.89321  ?  332  ASN   B N   1 
ATOM   16582 C  CA  . ASN   B 1 332  ? 18.32700   99.65600  -54.71200 1.000 59.84901  ?  332  ASN   B CA  1 
ATOM   16583 C  C   . ASN   B 1 332  ? 18.34100   98.91000  -53.38300 1.000 59.15087  ?  332  ASN   B C   1 
ATOM   16584 O  O   . ASN   B 1 332  ? 19.22900   99.11300  -52.55200 1.000 70.59246  ?  332  ASN   B O   1 
ATOM   16585 C  CB  . ASN   B 1 332  ? 19.70800   99.68400  -55.35800 1.000 58.41605  ?  332  ASN   B CB  1 
ATOM   16586 C  CG  . ASN   B 1 332  ? 20.03700   98.40000  -56.09500 1.000 70.14795  ?  332  ASN   B CG  1 
ATOM   16587 O  OD1 . ASN   B 1 332  ? 19.67200   97.30800  -55.65900 1.000 71.61061  ?  332  ASN   B OD1 1 
ATOM   16588 N  ND2 . ASN   B 1 332  ? 20.72700   98.52700  -57.22300 1.000 64.12323  ?  332  ASN   B ND2 1 
ATOM   16589 N  N   . THR   B 1 333  ? 17.34700   98.04700  -53.17800 1.000 55.88530  ?  333  THR   B N   1 
ATOM   16590 C  CA  . THR   B 1 333  ? 17.28300   97.24300  -51.96500 1.000 54.73074  ?  333  THR   B CA  1 
ATOM   16591 C  C   . THR   B 1 333  ? 18.14700   95.99200  -52.03900 1.000 55.80254  ?  333  THR   B C   1 
ATOM   16592 O  O   . THR   B 1 333  ? 18.26500   95.28100  -51.03500 1.000 68.75346  ?  333  THR   B O   1 
ATOM   16593 C  CB  . THR   B 1 333  ? 15.83500   96.84100  -51.66900 1.000 40.32790  ?  333  THR   B CB  1 
ATOM   16594 O  OG1 . THR   B 1 333  ? 15.39400   95.88600  -52.64300 1.000 39.06195  ?  333  THR   B OG1 1 
ATOM   16595 C  CG2 . THR   B 1 333  ? 14.92600   98.05900  -51.71200 1.000 36.35398  ?  333  THR   B CG2 1 
ATOM   16596 N  N   . ASN   B 1 334  ? 18.75100   95.71000  -53.18900 1.000 52.18519  ?  334  ASN   B N   1 
ATOM   16597 C  CA  . ASN   B 1 334  ? 19.53800   94.50100  -53.35700 1.000 60.97488  ?  334  ASN   B CA  1 
ATOM   16598 C  C   . ASN   B 1 334  ? 20.89000   94.63000  -52.66200 1.000 61.69620  ?  334  ASN   B C   1 
ATOM   16599 O  O   . ASN   B 1 334  ? 21.38000   95.72900  -52.38800 1.000 54.88011  ?  334  ASN   B O   1 
ATOM   16600 C  CB  . ASN   B 1 334  ? 19.73400   94.19200  -54.84200 1.000 57.23390  ?  334  ASN   B CB  1 
ATOM   16601 C  CG  . ASN   B 1 334  ? 18.46500   93.69700  -55.50600 1.000 73.98921  ?  334  ASN   B CG  1 
ATOM   16602 O  OD1 . ASN   B 1 334  ? 18.35100   92.52000  -55.84900 1.000 90.96862  ?  334  ASN   B OD1 1 
ATOM   16603 N  ND2 . ASN   B 1 334  ? 17.49800   94.59100  -55.68100 1.000 71.33637  ?  334  ASN   B ND2 1 
ATOM   16604 N  N   . ASN   B 1 335  ? 21.49300   93.47700  -52.37900 1.000 55.01667  ?  335  ASN   B N   1 
ATOM   16605 C  CA  . ASN   B 1 335  ? 22.78300   93.44800  -51.70400 1.000 48.87136  ?  335  ASN   B CA  1 
ATOM   16606 C  C   . ASN   B 1 335  ? 23.86800   94.06900  -52.57500 1.000 55.99192  ?  335  ASN   B C   1 
ATOM   16607 O  O   . ASN   B 1 335  ? 23.87200   93.91400  -53.79900 1.000 66.48958  ?  335  ASN   B O   1 
ATOM   16608 C  CB  . ASN   B 1 335  ? 23.16300   92.01300  -51.34500 1.000 30.40898  ?  335  ASN   B CB  1 
ATOM   16609 C  CG  . ASN   B 1 335  ? 22.33700   91.46300  -50.20500 1.000 38.36049  ?  335  ASN   B CG  1 
ATOM   16610 O  OD1 . ASN   B 1 335  ? 21.78500   92.21800  -49.40500 1.000 49.49812  ?  335  ASN   B OD1 1 
ATOM   16611 N  ND2 . ASN   B 1 335  ? 22.25400   90.14100  -50.11900 1.000 28.46516  ?  335  ASN   B ND2 1 
ATOM   16612 N  N   . LEU   B 1 336  ? 24.79500   94.76900  -51.93000 1.000 52.53514  ?  336  LEU   B N   1 
ATOM   16613 C  CA  . LEU   B 1 336  ? 25.88300   95.41000  -52.64700 1.000 51.07202  ?  336  LEU   B CA  1 
ATOM   16614 C  C   . LEU   B 1 336  ? 26.85800   94.36200  -53.18300 1.000 51.37047  ?  336  LEU   B C   1 
ATOM   16615 O  O   . LEU   B 1 336  ? 26.96100   93.25900  -52.63900 1.000 44.60038  ?  336  LEU   B O   1 
ATOM   16616 C  CB  . LEU   B 1 336  ? 26.62700   96.38400  -51.73500 1.000 45.27976  ?  336  LEU   B CB  1 
ATOM   16617 C  CG  . LEU   B 1 336  ? 26.07100   97.79500  -51.52400 1.000 42.09049  ?  336  LEU   B CG  1 
ATOM   16618 C  CD1 . LEU   B 1 336  ? 26.06200   98.55900  -52.83500 1.000 45.32080  ?  336  LEU   B CD1 1 
ATOM   16619 C  CD2 . LEU   B 1 336  ? 24.68200   97.76800  -50.90300 1.000 49.42701  ?  336  LEU   B CD2 1 
ATOM   16620 N  N   . PRO   B 1 337  ? 27.57700   94.67700  -54.26000 1.000 52.83138  ?  337  PRO   B N   1 
ATOM   16621 C  CA  . PRO   B 1 337  ? 28.66700   93.79400  -54.69900 1.000 41.80751  ?  337  PRO   B CA  1 
ATOM   16622 C  C   . PRO   B 1 337  ? 29.80300   93.82100  -53.68700 1.000 53.20280  ?  337  PRO   B C   1 
ATOM   16623 O  O   . PRO   B 1 337  ? 30.22400   94.88900  -53.23700 1.000 47.54058  ?  337  PRO   B O   1 
ATOM   16624 C  CB  . PRO   B 1 337  ? 29.09300   94.39100  -56.04700 1.000 40.25692  ?  337  PRO   B CB  1 
ATOM   16625 C  CG  . PRO   B 1 337  ? 27.95000   95.27000  -56.46800 1.000 50.25743  ?  337  PRO   B CG  1 
ATOM   16626 C  CD  . PRO   B 1 337  ? 27.35800   95.79000  -55.19700 1.000 58.82852  ?  337  PRO   B CD  1 
ATOM   16627 N  N   . HIS   B 1 338  ? 30.29500   92.63700  -53.32900 1.000 45.81058  ?  338  HIS   B N   1 
ATOM   16628 C  CA  . HIS   B 1 338  ? 31.28900   92.53100  -52.26800 1.000 55.73543  ?  338  HIS   B CA  1 
ATOM   16629 C  C   . HIS   B 1 338  ? 32.63000   93.09300  -52.71800 1.000 49.38793  ?  338  HIS   B C   1 
ATOM   16630 O  O   . HIS   B 1 338  ? 33.12400   92.76900  -53.80300 1.000 43.46781  ?  338  HIS   B O   1 
ATOM   16631 C  CB  . HIS   B 1 338  ? 31.43900   91.07700  -51.82600 1.000 45.87243  ?  338  HIS   B CB  1 
ATOM   16632 C  CG  . HIS   B 1 338  ? 30.28700   90.58000  -51.01300 1.000 66.99242  ?  338  HIS   B CG  1 
ATOM   16633 N  ND1 . HIS   B 1 338  ? 30.00900   89.24000  -50.85100 1.000 63.15144  ?  338  HIS   B ND1 1 
ATOM   16634 C  CD2 . HIS   B 1 338  ? 29.33800   91.24900  -50.31800 1.000 67.84306  ?  338  HIS   B CD2 1 
ATOM   16635 C  CE1 . HIS   B 1 338  ? 28.93700   89.10500  -50.09000 1.000 70.23193  ?  338  HIS   B CE1 1 
ATOM   16636 N  NE2 . HIS   B 1 338  ? 28.51100   90.30900  -49.75300 1.000 60.98500  ?  338  HIS   B NE2 1 
ATOM   16637 N  N   . VAL   B 1 339  ? 33.21600   93.94700  -51.87600 1.000 37.41206  ?  339  VAL   B N   1 
ATOM   16638 C  CA  . VAL   B 1 339  ? 34.49800   94.57700  -52.16300 1.000 41.61126  ?  339  VAL   B CA  1 
ATOM   16639 C  C   . VAL   B 1 339  ? 35.49400   94.42300  -51.02600 1.000 55.33552  ?  339  VAL   B C   1 
ATOM   16640 O  O   . VAL   B 1 339  ? 36.59300   94.97600  -51.10300 1.000 48.07189  ?  339  VAL   B O   1 
ATOM   16641 C  CB  . VAL   B 1 339  ? 34.32100   96.07000  -52.50900 1.000 40.01810  ?  339  VAL   B CB  1 
ATOM   16642 C  CG1 . VAL   B 1 339  ? 33.31700   96.24800  -53.64000 1.000 36.58751  ?  339  VAL   B CG1 1 
ATOM   16643 C  CG2 . VAL   B 1 339  ? 33.89500   96.85600  -51.27600 1.000 39.60744  ?  339  VAL   B CG2 1 
ATOM   16644 N  N   . ASN   B 1 340  ? 35.15400   93.68800  -49.97200 1.000 52.14694  ?  340  ASN   B N   1 
ATOM   16645 C  CA  . ASN   B 1 340  ? 35.97800   93.61200  -48.77600 1.000 39.73091  ?  340  ASN   B CA  1 
ATOM   16646 C  C   . ASN   B 1 340  ? 36.65200   92.25300  -48.65500 1.000 50.13179  ?  340  ASN   B C   1 
ATOM   16647 O  O   . ASN   B 1 340  ? 36.19700   91.24800  -49.20900 1.000 45.57208  ?  340  ASN   B O   1 
ATOM   16648 C  CB  . ASN   B 1 340  ? 35.14800   93.87700  -47.51600 1.000 33.97238  ?  340  ASN   B CB  1 
ATOM   16649 C  CG  . ASN   B 1 340  ? 34.51500   95.24800  -47.51500 1.000 45.72219  ?  340  ASN   B CG  1 
ATOM   16650 O  OD1 . ASN   B 1 340  ? 33.34400   95.40300  -47.86200 1.000 43.83282  ?  340  ASN   B OD1 1 
ATOM   16651 N  ND2 . ASN   B 1 340  ? 35.28800   96.25600  -47.12400 1.000 41.15768  ?  340  ASN   B ND2 1 
ATOM   16652 N  N   . ARG   B 1 341  ? 37.75100   92.24600  -47.90800 1.000 54.27326  ?  341  ARG   B N   1 
ATOM   16653 C  CA  . ARG   B 1 341  ? 38.49000   91.07000  -47.49700 1.000 37.22494  ?  341  ARG   B CA  1 
ATOM   16654 C  C   . ARG   B 1 341  ? 38.42400   90.94300  -45.97900 1.000 38.01640  ?  341  ARG   B C   1 
ATOM   16655 O  O   . ARG   B 1 341  ? 38.29300   91.95300  -45.28000 1.000 38.23228  ?  341  ARG   B O   1 
ATOM   16656 C  CB  . ARG   B 1 341  ? 39.95400   91.15400  -47.95000 1.000 43.60940  ?  341  ARG   B CB  1 
ATOM   16657 C  CG  . ARG   B 1 341  ? 40.12400   91.25100  -49.46000 1.000 71.85415  ?  341  ARG   B CG  1 
ATOM   16658 C  CD  . ARG   B 1 341  ? 41.38200   92.02300  -49.83900 1.000 73.88152  ?  341  ARG   B CD  1 
ATOM   16659 N  NE  . ARG   B 1 341  ? 41.32200   93.41500  -49.40800 1.000 89.13161  ?  341  ARG   B NE  1 
ATOM   16660 C  CZ  . ARG   B 1 341  ? 40.75600   94.39300  -50.10200 1.000 82.57963  ?  341  ARG   B CZ  1 
ATOM   16661 N  NH1 . ARG   B 1 341  ? 40.18300   94.16800  -51.27400 1.000 83.19648  ?  341  ARG   B NH1 1 
ATOM   16662 N  NH2 . ARG   B 1 341  ? 40.76200   95.62800  -49.60800 1.000 57.01292  ?  341  ARG   B NH2 1 
ATOM   16663 N  N   . PRO   B 1 342  ? 38.49700   89.72300  -45.44000 1.000 27.99143  ?  342  PRO   B N   1 
ATOM   16664 C  CA  . PRO   B 1 342  ? 38.36200   89.55600  -43.98200 1.000 22.85016  ?  342  PRO   B CA  1 
ATOM   16665 C  C   . PRO   B 1 342  ? 39.37400   90.34600  -43.16800 1.000 36.21896  ?  342  PRO   B C   1 
ATOM   16666 O  O   . PRO   B 1 342  ? 39.11200   90.62500  -41.99200 1.000 37.94818  ?  342  PRO   B O   1 
ATOM   16667 C  CB  . PRO   B 1 342  ? 38.54600   88.04600  -43.78500 1.000 27.91413  ?  342  PRO   B CB  1 
ATOM   16668 C  CG  . PRO   B 1 342  ? 38.14400   87.44900  -45.09100 1.000 32.50484  ?  342  PRO   B CG  1 
ATOM   16669 C  CD  . PRO   B 1 342  ? 38.58700   88.42900  -46.13800 1.000 28.41963  ?  342  PRO   B CD  1 
ATOM   16670 N  N   . ASP   B 1 343  ? 40.51600   90.71700  -43.74700 1.000 40.21457  ?  343  ASP   B N   1 
ATOM   16671 C  CA  . ASP   B 1 343  ? 41.52400   91.50400  -43.05100 1.000 34.72147  ?  343  ASP   B CA  1 
ATOM   16672 C  C   . ASP   B 1 343  ? 41.28400   93.00700  -43.17100 1.000 38.52357  ?  343  ASP   B C   1 
ATOM   16673 O  O   . ASP   B 1 343  ? 42.19700   93.79500  -42.90000 1.000 38.66846  ?  343  ASP   B O   1 
ATOM   16674 C  CB  . ASP   B 1 343  ? 42.92400   91.14400  -43.56300 1.000 35.29054  ?  343  ASP   B CB  1 
ATOM   16675 C  CG  . ASP   B 1 343  ? 42.99700   91.07300  -45.07800 1.000 54.38991  ?  343  ASP   B CG  1 
ATOM   16676 O  OD1 . ASP   B 1 343  ? 43.04600   92.13800  -45.72700 1.000 65.46096  ?  343  ASP   B OD1 1 
ATOM   16677 O  OD2 . ASP   B 1 343  ? 43.00900   89.94700  -45.62100 1.000 80.34079  -1 343  ASP   B OD2 1 
ATOM   16678 N  N   . ASP   B 1 344  ? 40.08400   93.42000  -43.56500 1.000 40.59304  ?  344  ASP   B N   1 
ATOM   16679 C  CA  . ASP   B 1 344  ? 39.74700   94.83100  -43.64700 1.000 35.70912  ?  344  ASP   B CA  1 
ATOM   16680 C  C   . ASP   B 1 344  ? 39.08800   95.29000  -42.35600 1.000 36.62703  ?  344  ASP   B C   1 
ATOM   16681 O  O   . ASP   B 1 344  ? 38.45800   94.50400  -41.64100 1.000 45.05266  ?  344  ASP   B O   1 
ATOM   16682 C  CB  . ASP   B 1 344  ? 38.81700   95.10600  -44.83000 1.000 37.33152  ?  344  ASP   B CB  1 
ATOM   16683 C  CG  . ASP   B 1 344  ? 39.52700   95.01200  -46.16600 1.000 53.79204  ?  344  ASP   B CG  1 
ATOM   16684 O  OD1 . ASP   B 1 344  ? 40.75300   95.24700  -46.20800 1.000 61.09379  ?  344  ASP   B OD1 1 
ATOM   16685 O  OD2 . ASP   B 1 344  ? 38.85500   94.71000  -47.17500 1.000 43.43335  -1 344  ASP   B OD2 1 
ATOM   16686 N  N   . LEU   B 1 345  ? 39.23600   96.58000  -42.06200 1.000 30.59426  ?  345  LEU   B N   1 
ATOM   16687 C  CA  . LEU   B 1 345  ? 38.63900   97.13300  -40.85200 1.000 29.70339  ?  345  LEU   B CA  1 
ATOM   16688 C  C   . LEU   B 1 345  ? 37.12100   97.02200  -40.88700 1.000 37.52666  ?  345  LEU   B C   1 
ATOM   16689 O  O   . LEU   B 1 345  ? 36.48900   97.09600  -41.95000 1.000 42.22590  ?  345  LEU   B O   1 
ATOM   16690 C  CB  . LEU   B 1 345  ? 39.04600   98.59600  -40.67900 1.000 34.44987  ?  345  LEU   B CB  1 
ATOM   16691 C  CG  . LEU   B 1 345  ? 40.48400   98.86100  -40.24100 1.000 35.26843  ?  345  LEU   B CG  1 
ATOM   16692 C  CD1 . LEU   B 1 345  ? 40.69300   100.34200 -39.95800 1.000 31.13145  ?  345  LEU   B CD1 1 
ATOM   16693 C  CD2 . LEU   B 1 345  ? 40.82800   98.02300  -39.02300 1.000 36.91291  ?  345  LEU   B CD2 1 
ATOM   16694 N  N   . VAL   B 1 346  ? 36.53400   96.83900  -39.69600 1.000 44.76504  ?  346  VAL   B N   1 
ATOM   16695 C  CA  . VAL   B 1 346  ? 35.08900   96.80200  -39.52100 1.000 37.51541  ?  346  VAL   B CA  1 
ATOM   16696 C  C   . VAL   B 1 346  ? 34.60300   97.87300  -38.55100 1.000 37.66455  ?  346  VAL   B C   1 
ATOM   16697 O  O   . VAL   B 1 346  ? 33.52100   98.43000  -38.73800 1.000 45.16186  ?  346  VAL   B O   1 
ATOM   16698 C  CB  . VAL   B 1 346  ? 34.61100   95.39800  -39.08100 1.000 28.94673  ?  346  VAL   B CB  1 
ATOM   16699 C  CG1 . VAL   B 1 346  ? 35.24800   94.98600  -37.75300 1.000 31.33038  ?  346  VAL   B CG1 1 
ATOM   16700 C  CG2 . VAL   B 1 346  ? 33.08200   95.35000  -38.98700 1.000 31.96167  ?  346  VAL   B CG2 1 
ATOM   16701 N  N   . TYR   B 1 347  ? 35.38000   98.17200  -37.50700 1.000 33.55402  ?  347  TYR   B N   1 
ATOM   16702 C  CA  . TYR   B 1 347  ? 35.04100   99.28300  -36.62900 1.000 33.88925  ?  347  TYR   B CA  1 
ATOM   16703 C  C   . TYR   B 1 347  ? 36.29700   99.78000  -35.92800 1.000 43.40006  ?  347  TYR   B C   1 
ATOM   16704 O  O   . TYR   B 1 347  ? 37.32100   99.09300  -35.88800 1.000 34.21626  ?  347  TYR   B O   1 
ATOM   16705 C  CB  . TYR   B 1 347  ? 33.95400   98.91200  -35.59800 1.000 37.79189  ?  347  TYR   B CB  1 
ATOM   16706 C  CG  . TYR   B 1 347  ? 34.32400   97.85700  -34.56800 1.000 34.21063  ?  347  TYR   B CG  1 
ATOM   16707 C  CD1 . TYR   B 1 347  ? 35.16500   98.15200  -33.49900 1.000 32.10389  ?  347  TYR   B CD1 1 
ATOM   16708 C  CD2 . TYR   B 1 347  ? 33.79300   96.57600  -34.64400 1.000 33.73803  ?  347  TYR   B CD2 1 
ATOM   16709 C  CE1 . TYR   B 1 347  ? 35.49500   97.19400  -32.56200 1.000 33.57113  ?  347  TYR   B CE1 1 
ATOM   16710 C  CE2 . TYR   B 1 347  ? 34.11400   95.61100  -33.70500 1.000 33.11471  ?  347  TYR   B CE2 1 
ATOM   16711 C  CZ  . TYR   B 1 347  ? 34.96500   95.92700  -32.66700 1.000 35.20256  ?  347  TYR   B CZ  1 
ATOM   16712 O  OH  . TYR   B 1 347  ? 35.29300   94.97500  -31.72900 1.000 43.04379  ?  347  TYR   B OH  1 
ATOM   16713 N  N   . VAL   B 1 348  ? 36.20100   100.99000 -35.37600 1.000 46.18942  ?  348  VAL   B N   1 
ATOM   16714 C  CA  . VAL   B 1 348  ? 37.26500   101.60200 -34.58400 1.000 44.41183  ?  348  VAL   B CA  1 
ATOM   16715 C  C   . VAL   B 1 348  ? 36.61800   102.16700 -33.32700 1.000 42.49424  ?  348  VAL   B C   1 
ATOM   16716 O  O   . VAL   B 1 348  ? 35.91000   103.17900 -33.39100 1.000 48.71762  ?  348  VAL   B O   1 
ATOM   16717 C  CB  . VAL   B 1 348  ? 38.01800   102.70000 -35.35200 1.000 32.08656  ?  348  VAL   B CB  1 
ATOM   16718 C  CG1 . VAL   B 1 348  ? 39.01300   103.41000 -34.43700 1.000 25.45425  ?  348  VAL   B CG1 1 
ATOM   16719 C  CG2 . VAL   B 1 348  ? 38.73300   102.12100 -36.56300 1.000 38.82803  ?  348  VAL   B CG2 1 
ATOM   16720 N  N   . MET   B 1 349  ? 36.83900   101.50900 -32.19300 1.000 36.39810  ?  349  MET   B N   1 
ATOM   16721 C  CA  . MET   B 1 349  ? 36.36000   101.98500 -30.90400 1.000 38.88122  ?  349  MET   B CA  1 
ATOM   16722 C  C   . MET   B 1 349  ? 37.53900   102.43600 -30.05400 1.000 41.29001  ?  349  MET   B C   1 
ATOM   16723 O  O   . MET   B 1 349  ? 38.64900   101.90800 -30.17000 1.000 43.36331  ?  349  MET   B O   1 
ATOM   16724 C  CB  . MET   B 1 349  ? 35.56100   100.90500 -30.16900 1.000 23.02108  ?  349  MET   B CB  1 
ATOM   16725 C  CG  . MET   B 1 349  ? 34.22400   100.60200 -30.81900 1.000 37.21727  ?  349  MET   B CG  1 
ATOM   16726 S  SD  . MET   B 1 349  ? 33.33800   99.23800  -30.04600 1.000 35.73153  ?  349  MET   B SD  1 
ATOM   16727 C  CE  . MET   B 1 349  ? 32.37200   98.64800  -31.43500 1.000 38.59025  ?  349  MET   B CE  1 
ATOM   16728 N  N   . TYR   B 1 350  ? 37.28800   103.41800 -29.19900 1.000 35.04944  ?  350  TYR   B N   1 
ATOM   16729 C  CA  . TYR   B 1 350  ? 38.33900   104.07200 -28.43700 1.000 31.50344  ?  350  TYR   B CA  1 
ATOM   16730 C  C   . TYR   B 1 350  ? 38.38300   103.56100 -27.00200 1.000 50.19944  ?  350  TYR   B C   1 
ATOM   16731 O  O   . TYR   B 1 350  ? 37.43300   102.95800 -26.49700 1.000 49.84198  ?  350  TYR   B O   1 
ATOM   16732 C  CB  . TYR   B 1 350  ? 38.14700   105.59100 -28.45800 1.000 39.01312  ?  350  TYR   B CB  1 
ATOM   16733 C  CG  . TYR   B 1 350  ? 38.48300   106.21700 -29.79300 1.000 44.38670  ?  350  TYR   B CG  1 
ATOM   16734 C  CD1 . TYR   B 1 350  ? 37.61100   106.11600 -30.87100 1.000 48.20189  ?  350  TYR   B CD1 1 
ATOM   16735 C  CD2 . TYR   B 1 350  ? 39.67500   106.90400 -29.97800 1.000 46.24728  ?  350  TYR   B CD2 1 
ATOM   16736 C  CE1 . TYR   B 1 350  ? 37.91800   106.68400 -32.09500 1.000 39.01629  ?  350  TYR   B CE1 1 
ATOM   16737 C  CE2 . TYR   B 1 350  ? 39.99000   107.47600 -31.19700 1.000 49.12351  ?  350  TYR   B CE2 1 
ATOM   16738 C  CZ  . TYR   B 1 350  ? 39.10800   107.36300 -32.25200 1.000 39.75605  ?  350  TYR   B CZ  1 
ATOM   16739 O  OH  . TYR   B 1 350  ? 39.41800   107.93100 -33.46600 1.000 50.81201  ?  350  TYR   B OH  1 
ATOM   16740 N  N   . THR   B 1 351  ? 39.51500   103.81200 -26.34900 1.000 59.62288  ?  351  THR   B N   1 
ATOM   16741 C  CA  . THR   B 1 351  ? 39.75600   103.33200 -24.99500 1.000 54.07293  ?  351  THR   B CA  1 
ATOM   16742 C  C   . THR   B 1 351  ? 39.13100   104.29700 -23.98900 1.000 68.57341  ?  351  THR   B C   1 
ATOM   16743 O  O   . THR   B 1 351  ? 38.34500   105.18100 -24.34000 1.000 72.91332  ?  351  THR   B O   1 
ATOM   16744 C  CB  . THR   B 1 351  ? 41.25200   103.15400 -24.75600 1.000 55.57663  ?  351  THR   B CB  1 
ATOM   16745 O  OG1 . THR   B 1 351  ? 41.89600   104.43500 -24.77200 1.000 74.49781  ?  351  THR   B OG1 1 
ATOM   16746 C  CG2 . THR   B 1 351  ? 41.86100   102.27600 -25.83900 1.000 40.06609  ?  351  THR   B CG2 1 
ATOM   16747 N  N   . SER   B 1 352  ? 39.48500   104.13800 -22.71300 1.000 65.90845  ?  352  SER   B N   1 
ATOM   16748 C  CA  . SER   B 1 352  ? 38.88000   104.95900 -21.66800 1.000 79.84812  ?  352  SER   B CA  1 
ATOM   16749 C  C   . SER   B 1 352  ? 39.42700   106.38100 -21.70000 1.000 101.38615 ?  352  SER   B C   1 
ATOM   16750 O  O   . SER   B 1 352  ? 38.66700   107.35200 -21.78800 1.000 87.41104  ?  352  SER   B O   1 
ATOM   16751 C  CB  . SER   B 1 352  ? 39.11700   104.32200 -20.29600 1.000 68.54677  ?  352  SER   B CB  1 
ATOM   16752 O  OG  . SER   B 1 352  ? 40.37200   104.70800 -19.76300 1.000 69.96912  ?  352  SER   B OG  1 
ATOM   16753 N  N   . GLY   B 1 353  ? 40.74700   106.52200 -21.63200 1.000 102.61591 ?  353  GLY   B N   1 
ATOM   16754 C  CA  . GLY   B 1 353  ? 41.36400   107.82500 -21.51000 1.000 93.19220  ?  353  GLY   B CA  1 
ATOM   16755 C  C   . GLY   B 1 353  ? 41.63900   108.26500 -20.09100 1.000 109.76875 ?  353  GLY   B C   1 
ATOM   16756 O  O   . GLY   B 1 353  ? 42.04400   109.41600 -19.88500 1.000 119.89047 ?  353  GLY   B O   1 
ATOM   16757 N  N   . SER   B 1 354  ? 41.42700   107.39100 -19.10500 1.000 103.55504 ?  354  SER   B N   1 
ATOM   16758 C  CA  . SER   B 1 354  ? 41.71800   107.75100 -17.72100 1.000 107.86815 ?  354  SER   B CA  1 
ATOM   16759 C  C   . SER   B 1 354  ? 43.21900   107.86300 -17.48300 1.000 107.91571 ?  354  SER   B C   1 
ATOM   16760 O  O   . SER   B 1 354  ? 43.67300   108.75900 -16.76200 1.000 108.52842 ?  354  SER   B O   1 
ATOM   16761 C  CB  . SER   B 1 354  ? 41.09500   106.72700 -16.77400 1.000 100.38535 ?  354  SER   B CB  1 
ATOM   16762 O  OG  . SER   B 1 354  ? 41.37200   105.40400 -17.20100 1.000 98.92200  ?  354  SER   B OG  1 
ATOM   16763 N  N   . THR   B 1 355  ? 44.00700   106.96600 -18.08200 1.000 108.78211 ?  355  THR   B N   1 
ATOM   16764 C  CA  . THR   B 1 355  ? 45.45500   107.02700 -17.93100 1.000 107.91814 ?  355  THR   B CA  1 
ATOM   16765 C  C   . THR   B 1 355  ? 46.08300   108.12400 -18.78200 1.000 104.19981 ?  355  THR   B C   1 
ATOM   16766 O  O   . THR   B 1 355  ? 47.21700   108.53000 -18.50500 1.000 96.21273  ?  355  THR   B O   1 
ATOM   16767 C  CB  . THR   B 1 355  ? 46.08500   105.67300 -18.28000 1.000 102.17153 ?  355  THR   B CB  1 
ATOM   16768 O  OG1 . THR   B 1 355  ? 47.39800   105.59200 -17.71200 1.000 88.67041  ?  355  THR   B OG1 1 
ATOM   16769 C  CG2 . THR   B 1 355  ? 46.18300   105.49200 -19.79100 1.000 77.67586  ?  355  THR   B CG2 1 
ATOM   16770 N  N   . GLY   B 1 356  ? 45.37500   108.61700 -19.79800 1.000 99.13692  ?  356  GLY   B N   1 
ATOM   16771 C  CA  . GLY   B 1 356  ? 45.90700   109.66500 -20.64600 1.000 90.38989  ?  356  GLY   B CA  1 
ATOM   16772 C  C   . GLY   B 1 356  ? 45.08900   109.92500 -21.89500 1.000 83.40543  ?  356  GLY   B C   1 
ATOM   16773 O  O   . GLY   B 1 356  ? 43.89400   110.22400 -21.81600 1.000 71.18340  ?  356  GLY   B O   1 
ATOM   16774 N  N   . LEU   B 1 357  ? 45.72700   109.81700 -23.05600 1.000 91.90324  ?  357  LEU   B N   1 
ATOM   16775 C  CA  . LEU   B 1 357  ? 45.06500   110.09600 -24.32000 1.000 84.15151  ?  357  LEU   B CA  1 
ATOM   16776 C  C   . LEU   B 1 357  ? 44.26100   108.88700 -24.78400 1.000 81.90505  ?  357  LEU   B C   1 
ATOM   16777 O  O   . LEU   B 1 357  ? 44.61300   107.73500 -24.51000 1.000 66.18793  ?  357  LEU   B O   1 
ATOM   16778 C  CB  . LEU   B 1 357  ? 46.09400   110.48300 -25.38300 1.000 81.32635  ?  357  LEU   B CB  1 
ATOM   16779 C  CG  . LEU   B 1 357  ? 45.69200   111.53200 -26.42200 1.000 65.92352  ?  357  LEU   B CG  1 
ATOM   16780 C  CD1 . LEU   B 1 357  ? 45.49400   112.89100 -25.77100 1.000 70.73950  ?  357  LEU   B CD1 1 
ATOM   16781 C  CD2 . LEU   B 1 357  ? 46.73400   111.61300 -27.52700 1.000 60.88024  ?  357  LEU   B CD2 1 
ATOM   16782 N  N   . ALA   B 1 358  ? 43.16800   109.15900 -25.49300 1.000 77.09784  ?  358  ALA   B N   1 
ATOM   16783 C  CA  . ALA   B 1 358  ? 42.31700   108.09800 -26.01100 1.000 55.90390  ?  358  ALA   B CA  1 
ATOM   16784 C  C   . ALA   B 1 358  ? 42.95400   107.46000 -27.23900 1.000 53.05524  ?  358  ALA   B C   1 
ATOM   16785 O  O   . ALA   B 1 358  ? 43.60500   108.13400 -28.04200 1.000 66.93485  ?  358  ALA   B O   1 
ATOM   16786 C  CB  . ALA   B 1 358  ? 40.93100   108.64100 -26.35800 1.000 68.77920  ?  358  ALA   B CB  1 
ATOM   16787 N  N   . LYS   B 1 359  ? 42.75800   106.15200 -27.38300 1.000 43.44452  ?  359  LYS   B N   1 
ATOM   16788 C  CA  . LYS   B 1 359  ? 43.39000   105.36600 -28.43400 1.000 40.81045  ?  359  LYS   B CA  1 
ATOM   16789 C  C   . LYS   B 1 359  ? 42.32600   104.72900 -29.31400 1.000 45.59029  ?  359  LYS   B C   1 
ATOM   16790 O  O   . LYS   B 1 359  ? 41.42800   104.04700 -28.81200 1.000 52.37634  ?  359  LYS   B O   1 
ATOM   16791 C  CB  . LYS   B 1 359  ? 44.29400   104.28600 -27.83600 1.000 39.46055  ?  359  LYS   B CB  1 
ATOM   16792 C  CG  . LYS   B 1 359  ? 45.56600   104.82600 -27.21400 1.000 54.47478  ?  359  LYS   B CG  1 
ATOM   16793 C  CD  . LYS   B 1 359  ? 46.25400   103.78100 -26.35400 1.000 66.16967  ?  359  LYS   B CD  1 
ATOM   16794 C  CE  . LYS   B 1 359  ? 45.69600   103.76200 -24.94200 1.000 77.24851  ?  359  LYS   B CE  1 
ATOM   16795 N  NZ  . LYS   B 1 359  ? 46.53200   102.92500 -24.03500 1.000 89.53269  ?  359  LYS   B NZ  1 
ATOM   16796 N  N   . GLY   B 1 360  ? 42.43600   104.94400 -30.62300 1.000 39.76743  ?  360  GLY   B N   1 
ATOM   16797 C  CA  . GLY   B 1 360  ? 41.52800   104.32400 -31.56900 1.000 37.24709  ?  360  GLY   B CA  1 
ATOM   16798 C  C   . GLY   B 1 360  ? 41.91400   102.89600 -31.89200 1.000 39.68757  ?  360  GLY   B C   1 
ATOM   16799 O  O   . GLY   B 1 360  ? 42.86600   102.65900 -32.64100 1.000 36.42637  ?  360  GLY   B O   1 
ATOM   16800 N  N   . VAL   B 1 361  ? 41.18200   101.93700 -31.33200 1.000 36.71130  ?  361  VAL   B N   1 
ATOM   16801 C  CA  . VAL   B 1 361  ? 41.49500   100.52300 -31.51600 1.000 25.41898  ?  361  VAL   B CA  1 
ATOM   16802 C  C   . VAL   B 1 361  ? 40.86500   100.04700 -32.81900 1.000 39.92272  ?  361  VAL   B C   1 
ATOM   16803 O  O   . VAL   B 1 361  ? 39.65200   100.16800 -33.01400 1.000 50.81068  ?  361  VAL   B O   1 
ATOM   16804 C  CB  . VAL   B 1 361  ? 41.00100   99.68900  -30.32600 1.000 26.18351  ?  361  VAL   B CB  1 
ATOM   16805 C  CG1 . VAL   B 1 361  ? 41.58800   98.29900  -30.38600 1.000 24.35275  ?  361  VAL   B CG1 1 
ATOM   16806 C  CG2 . VAL   B 1 361  ? 41.35900   100.37000 -29.01300 1.000 35.56387  ?  361  VAL   B CG2 1 
ATOM   16807 N  N   . MET   B 1 362  ? 41.68800   99.49800  -33.70900 1.000 30.00107  ?  362  MET   B N   1 
ATOM   16808 C  CA  . MET   B 1 362  ? 41.24700   99.07600  -35.03400 1.000 34.78388  ?  362  MET   B CA  1 
ATOM   16809 C  C   . MET   B 1 362  ? 41.02300   97.56700  -35.02500 1.000 36.83950  ?  362  MET   B C   1 
ATOM   16810 O  O   . MET   B 1 362  ? 41.97300   96.79200  -34.87000 1.000 46.15319  ?  362  MET   B O   1 
ATOM   16811 C  CB  . MET   B 1 362  ? 42.26800   99.47900  -36.09500 1.000 31.00177  ?  362  MET   B CB  1 
ATOM   16812 C  CG  . MET   B 1 362  ? 42.49800   100.98000 -36.18500 1.000 40.73366  ?  362  MET   B CG  1 
ATOM   16813 S  SD  . MET   B 1 362  ? 43.83500   101.42400 -37.31100 1.000 28.06288  ?  362  MET   B SD  1 
ATOM   16814 C  CE  . MET   B 1 362  ? 44.87300   99.97000  -37.18200 1.000 31.14633  ?  362  MET   B CE  1 
ATOM   16815 N  N   . ILE   B 1 363  ? 39.76800   97.15600  -35.18900 1.000 33.82393  ?  363  ILE   B N   1 
ATOM   16816 C  CA  . ILE   B 1 363  ? 39.38600   95.75000  -35.23100 1.000 33.63228  ?  363  ILE   B CA  1 
ATOM   16817 C  C   . ILE   B 1 363  ? 38.96700   95.41000  -36.65500 1.000 28.69003  ?  363  ILE   B C   1 
ATOM   16818 O  O   . ILE   B 1 363  ? 38.27200   96.19500  -37.31200 1.000 24.27426  ?  363  ILE   B O   1 
ATOM   16819 C  CB  . ILE   B 1 363  ? 38.25900   95.43800  -34.22200 1.000 29.62758  ?  363  ILE   B CB  1 
ATOM   16820 C  CG1 . ILE   B 1 363  ? 38.84000   94.89200  -32.91700 1.000 35.25833  ?  363  ILE   B CG1 1 
ATOM   16821 C  CG2 . ILE   B 1 363  ? 37.26900   94.43600  -34.79000 1.000 31.81123  ?  363  ILE   B CG2 1 
ATOM   16822 C  CD1 . ILE   B 1 363  ? 39.80800   95.81700  -32.23800 1.000 32.57074  ?  363  ILE   B CD1 1 
ATOM   16823 N  N   . GLU   B 1 364  ? 39.40300   94.24900  -37.13300 1.000 29.26430  ?  364  GLU   B N   1 
ATOM   16824 C  CA  . GLU   B 1 364  ? 39.14500   93.81300  -38.49700 1.000 33.56923  ?  364  GLU   B CA  1 
ATOM   16825 C  C   . GLU   B 1 364  ? 37.98200   92.82400  -38.54100 1.000 32.61192  ?  364  GLU   B C   1 
ATOM   16826 O  O   . GLU   B 1 364  ? 37.49000   92.35300  -37.51300 1.000 35.85856  ?  364  GLU   B O   1 
ATOM   16827 C  CB  . GLU   B 1 364  ? 40.41100   93.19700  -39.10200 1.000 39.19265  ?  364  GLU   B CB  1 
ATOM   16828 C  CG  . GLU   B 1 364  ? 41.55400   94.19200  -39.25400 1.000 38.98925  ?  364  GLU   B CG  1 
ATOM   16829 C  CD  . GLU   B 1 364  ? 42.86100   93.54200  -39.67100 1.000 53.12115  ?  364  GLU   B CD  1 
ATOM   16830 O  OE1 . GLU   B 1 364  ? 43.06200   92.34700  -39.36500 1.000 47.64642  ?  364  GLU   B OE1 1 
ATOM   16831 O  OE2 . GLU   B 1 364  ? 43.69000   94.22900  -40.30600 1.000 51.23676  -1 364  GLU   B OE2 1 
ATOM   16832 N  N   . HIS   B 1 365  ? 37.54700   92.51200  -39.76600 1.000 33.28838  ?  365  HIS   B N   1 
ATOM   16833 C  CA  . HIS   B 1 365  ? 36.36000   91.68100  -39.95700 1.000 31.00860  ?  365  HIS   B CA  1 
ATOM   16834 C  C   . HIS   B 1 365  ? 36.53700   90.29900  -39.33900 1.000 33.23418  ?  365  HIS   B C   1 
ATOM   16835 O  O   . HIS   B 1 365  ? 35.67000   89.82400  -38.59600 1.000 29.72773  ?  365  HIS   B O   1 
ATOM   16836 C  CB  . HIS   B 1 365  ? 36.03700   91.56000  -41.44700 1.000 25.63373  ?  365  HIS   B CB  1 
ATOM   16837 C  CG  . HIS   B 1 365  ? 35.10500   92.61700  -41.95300 1.000 43.42388  ?  365  HIS   B CG  1 
ATOM   16838 N  ND1 . HIS   B 1 365  ? 33.73900   92.54500  -41.78700 1.000 41.95475  ?  365  HIS   B ND1 1 
ATOM   16839 C  CD2 . HIS   B 1 365  ? 35.34200   93.76900  -42.62400 1.000 38.66406  ?  365  HIS   B CD2 1 
ATOM   16840 C  CE1 . HIS   B 1 365  ? 33.17400   93.60800  -42.33200 1.000 36.64456  ?  365  HIS   B CE1 1 
ATOM   16841 N  NE2 . HIS   B 1 365  ? 34.12500   94.36600  -42.84700 1.000 39.40760  ?  365  HIS   B NE2 1 
ATOM   16842 N  N   . HIS   B 1 366  ? 37.65600   89.63500  -39.63900 1.000 38.84415  ?  366  HIS   B N   1 
ATOM   16843 C  CA  . HIS   B 1 366  ? 37.86700   88.27200  -39.16200 1.000 37.52835  ?  366  HIS   B CA  1 
ATOM   16844 C  C   . HIS   B 1 366  ? 37.90800   88.18600  -37.64100 1.000 35.95971  ?  366  HIS   B C   1 
ATOM   16845 O  O   . HIS   B 1 366  ? 37.62000   87.12000  -37.08600 1.000 35.97935  ?  366  HIS   B O   1 
ATOM   16846 C  CB  . HIS   B 1 366  ? 39.15400   87.69800  -39.76100 1.000 29.96301  ?  366  HIS   B CB  1 
ATOM   16847 C  CG  . HIS   B 1 366  ? 40.39200   88.44000  -39.36400 1.000 40.13676  ?  366  HIS   B CG  1 
ATOM   16848 N  ND1 . HIS   B 1 366  ? 41.39700   87.86500  -38.61600 1.000 38.70713  ?  366  HIS   B ND1 1 
ATOM   16849 C  CD2 . HIS   B 1 366  ? 40.79000   89.71100  -39.61300 1.000 50.32719  ?  366  HIS   B CD2 1 
ATOM   16850 C  CE1 . HIS   B 1 366  ? 42.36000   88.74900  -38.42100 1.000 54.91169  ?  366  HIS   B CE1 1 
ATOM   16851 N  NE2 . HIS   B 1 366  ? 42.01600   89.87700  -39.01500 1.000 60.00402  ?  366  HIS   B NE2 1 
ATOM   16852 N  N   . ASN   B 1 367  ? 38.24900   89.27900  -36.95300 1.000 27.23229  ?  367  ASN   B N   1 
ATOM   16853 C  CA  . ASN   B 1 367  ? 38.23200   89.25900  -35.49400 1.000 29.64824  ?  367  ASN   B CA  1 
ATOM   16854 C  C   . ASN   B 1 367  ? 36.80900   89.14700  -34.96400 1.000 34.15380  ?  367  ASN   B C   1 
ATOM   16855 O  O   . ASN   B 1 367  ? 36.55600   88.42300  -33.99400 1.000 35.76598  ?  367  ASN   B O   1 
ATOM   16856 C  CB  . ASN   B 1 367  ? 38.90500   90.51300  -34.93900 1.000 33.87190  ?  367  ASN   B CB  1 
ATOM   16857 C  CG  . ASN   B 1 367  ? 40.26500   90.75400  -35.54300 1.000 26.24702  ?  367  ASN   B CG  1 
ATOM   16858 O  OD1 . ASN   B 1 367  ? 40.61500   91.88600  -35.87400 1.000 34.04830  ?  367  ASN   B OD1 1 
ATOM   16859 N  ND2 . ASN   B 1 367  ? 41.04000   89.68800  -35.70100 1.000 39.32740  ?  367  ASN   B ND2 1 
ATOM   16860 N  N   . LEU   B 1 368  ? 35.87000   89.86200  -35.58600 1.000 37.11818  ?  368  LEU   B N   1 
ATOM   16861 C  CA  . LEU   B 1 368  ? 34.47700   89.79500  -35.15800 1.000 25.81028  ?  368  LEU   B CA  1 
ATOM   16862 C  C   . LEU   B 1 368  ? 33.83200   88.48500  -35.59100 1.000 28.50621  ?  368  LEU   B C   1 
ATOM   16863 O  O   . LEU   B 1 368  ? 33.00000   87.92700  -34.86700 1.000 36.19388  ?  368  LEU   B O   1 
ATOM   16864 C  CB  . LEU   B 1 368  ? 33.70500   90.98500  -35.72100 1.000 21.21761  ?  368  LEU   B CB  1 
ATOM   16865 C  CG  . LEU   B 1 368  ? 32.32700   91.26900  -35.12900 1.000 28.17081  ?  368  LEU   B CG  1 
ATOM   16866 C  CD1 . LEU   B 1 368  ? 32.45400   91.82700  -33.71800 1.000 53.63762  ?  368  LEU   B CD1 1 
ATOM   16867 C  CD2 . LEU   B 1 368  ? 31.57000   92.22800  -36.02800 1.000 20.08205  ?  368  LEU   B CD2 1 
ATOM   16868 N  N   . VAL   B 1 369  ? 34.20000   87.98300  -36.77200 1.000 20.57731  ?  369  VAL   B N   1 
ATOM   16869 C  CA  . VAL   B 1 369  ? 33.66400   86.70900  -37.24300 1.000 28.07699  ?  369  VAL   B CA  1 
ATOM   16870 C  C   . VAL   B 1 369  ? 34.09300   85.57800  -36.31800 1.000 34.31724  ?  369  VAL   B C   1 
ATOM   16871 O  O   . VAL   B 1 369  ? 33.31500   84.65900  -36.03300 1.000 40.76834  ?  369  VAL   B O   1 
ATOM   16872 C  CB  . VAL   B 1 369  ? 34.10000   86.45500  -38.69900 1.000 36.51479  ?  369  VAL   B CB  1 
ATOM   16873 C  CG1 . VAL   B 1 369  ? 33.68100   85.06400  -39.15000 1.000 38.25994  ?  369  VAL   B CG1 1 
ATOM   16874 C  CG2 . VAL   B 1 369  ? 33.51500   87.51700  -39.61900 1.000 23.50047  ?  369  VAL   B CG2 1 
ATOM   16875 N  N   . ASN   B 1 370  ? 35.33500   85.63100  -35.82700 1.000 38.10574  ?  370  ASN   B N   1 
ATOM   16876 C  CA  . ASN   B 1 370  ? 35.82000   84.60400  -34.91000 1.000 38.85383  ?  370  ASN   B CA  1 
ATOM   16877 C  C   . ASN   B 1 370  ? 34.99000   84.56800  -33.63300 1.000 38.70994  ?  370  ASN   B C   1 
ATOM   16878 O  O   . ASN   B 1 370  ? 34.64900   83.49000  -33.13200 1.000 37.36814  ?  370  ASN   B O   1 
ATOM   16879 C  CB  . ASN   B 1 370  ? 37.29500   84.84900  -34.58800 1.000 29.20982  ?  370  ASN   B CB  1 
ATOM   16880 C  CG  . ASN   B 1 370  ? 37.91100   83.73000  -33.77200 1.000 34.33177  ?  370  ASN   B CG  1 
ATOM   16881 O  OD1 . ASN   B 1 370  ? 38.13700   82.62900  -34.27600 1.000 47.89480  ?  370  ASN   B OD1 1 
ATOM   16882 N  ND2 . ASN   B 1 370  ? 38.20000   84.01100  -32.50600 1.000 24.70786  ?  370  ASN   B ND2 1 
ATOM   16883 N  N   . PHE   B 1 371  ? 34.64500   85.74100  -33.09900 1.000 35.03187  ?  371  PHE   B N   1 
ATOM   16884 C  CA  . PHE   B 1 371  ? 33.85900   85.79700  -31.87200 1.000 35.36891  ?  371  PHE   B CA  1 
ATOM   16885 C  C   . PHE   B 1 371  ? 32.41400   85.38000  -32.12300 1.000 39.29969  ?  371  PHE   B C   1 
ATOM   16886 O  O   . PHE   B 1 371  ? 31.86200   84.54900  -31.39300 1.000 45.02324  ?  371  PHE   B O   1 
ATOM   16887 C  CB  . PHE   B 1 371  ? 33.92500   87.20500  -31.28100 1.000 27.54518  ?  371  PHE   B CB  1 
ATOM   16888 C  CG  . PHE   B 1 371  ? 33.34900   87.31200  -29.90100 1.000 32.14383  ?  371  PHE   B CG  1 
ATOM   16889 C  CD1 . PHE   B 1 371  ? 34.13300   87.05600  -28.78900 1.000 40.57469  ?  371  PHE   B CD1 1 
ATOM   16890 C  CD2 . PHE   B 1 371  ? 32.02600   87.67400  -29.71400 1.000 32.19293  ?  371  PHE   B CD2 1 
ATOM   16891 C  CE1 . PHE   B 1 371  ? 33.60800   87.15600  -27.51600 1.000 40.66508  ?  371  PHE   B CE1 1 
ATOM   16892 C  CE2 . PHE   B 1 371  ? 31.49400   87.77500  -28.44500 1.000 43.70457  ?  371  PHE   B CE2 1 
ATOM   16893 C  CZ  . PHE   B 1 371  ? 32.28600   87.51600  -27.34400 1.000 41.30950  ?  371  PHE   B CZ  1 
ATOM   16894 N  N   . CYS   B 1 372  ? 31.78700   85.94500  -33.15900 1.000 33.02345  ?  372  CYS   B N   1 
ATOM   16895 C  CA  . CYS   B 1 372  ? 30.37800   85.66300  -33.42000 1.000 30.36032  ?  372  CYS   B CA  1 
ATOM   16896 C  C   . CYS   B 1 372  ? 30.14500   84.20400  -33.79000 1.000 37.78243  ?  372  CYS   B C   1 
ATOM   16897 O  O   . CYS   B 1 372  ? 29.10400   83.63800  -33.44000 1.000 47.39981  ?  372  CYS   B O   1 
ATOM   16898 C  CB  . CYS   B 1 372  ? 29.85500   86.58000  -34.52500 1.000 27.60638  ?  372  CYS   B CB  1 
ATOM   16899 S  SG  . CYS   B 1 372  ? 29.88600   88.34000  -34.11200 1.000 33.88967  ?  372  CYS   B SG  1 
ATOM   16900 N  N   . GLU   B 1 373  ? 31.08900   83.58300  -34.49900 1.000 32.81199  ?  373  GLU   B N   1 
ATOM   16901 C  CA  . GLU   B 1 373  ? 30.96400   82.17300  -34.84600 1.000 32.15288  ?  373  GLU   B CA  1 
ATOM   16902 C  C   . GLU   B 1 373  ? 31.40600   81.25100  -33.71800 1.000 34.09651  ?  373  GLU   B C   1 
ATOM   16903 O  O   . GLU   B 1 373  ? 31.25800   80.03000  -33.84100 1.000 35.40797  ?  373  GLU   B O   1 
ATOM   16904 C  CB  . GLU   B 1 373  ? 31.76200   81.87300  -36.11800 1.000 40.96664  ?  373  GLU   B CB  1 
ATOM   16905 C  CG  . GLU   B 1 373  ? 31.22500   82.57800  -37.35800 1.000 36.64728  ?  373  GLU   B CG  1 
ATOM   16906 C  CD  . GLU   B 1 373  ? 30.14700   81.78200  -38.06900 1.000 49.42129  ?  373  GLU   B CD  1 
ATOM   16907 O  OE1 . GLU   B 1 373  ? 30.48400   80.75600  -38.69600 1.000 65.66664  ?  373  GLU   B OE1 1 
ATOM   16908 O  OE2 . GLU   B 1 373  ? 28.96300   82.17800  -38.00100 1.000 70.72525  -1 373  GLU   B OE2 1 
ATOM   16909 N  N   . TRP   B 1 374  ? 31.95200   81.80200  -32.63600 1.000 30.71416  ?  374  TRP   B N   1 
ATOM   16910 C  CA  . TRP   B 1 374  ? 32.13700   81.06800  -31.39100 1.000 30.00177  ?  374  TRP   B CA  1 
ATOM   16911 C  C   . TRP   B 1 374  ? 30.99900   81.29100  -30.40900 1.000 33.85743  ?  374  TRP   B C   1 
ATOM   16912 O  O   . TRP   B 1 374  ? 30.63400   80.36600  -29.67800 1.000 32.30121  ?  374  TRP   B O   1 
ATOM   16913 C  CB  . TRP   B 1 374  ? 33.45800   81.47400  -30.72600 1.000 27.41484  ?  374  TRP   B CB  1 
ATOM   16914 C  CG  . TRP   B 1 374  ? 33.52100   81.16900  -29.25400 1.000 28.50460  ?  374  TRP   B CG  1 
ATOM   16915 C  CD1 . TRP   B 1 374  ? 33.94800   80.01000  -28.67300 1.000 29.49201  ?  374  TRP   B CD1 1 
ATOM   16916 C  CD2 . TRP   B 1 374  ? 33.14400   82.04100  -28.17800 1.000 29.72190  ?  374  TRP   B CD2 1 
ATOM   16917 N  NE1 . TRP   B 1 374  ? 33.86000   80.10500  -27.30300 1.000 32.26270  ?  374  TRP   B NE1 1 
ATOM   16918 C  CE2 . TRP   B 1 374  ? 33.36900   81.34100  -26.97400 1.000 27.86405  ?  374  TRP   B CE2 1 
ATOM   16919 C  CE3 . TRP   B 1 374  ? 32.63700   83.34300  -28.11600 1.000 28.03609  ?  374  TRP   B CE3 1 
ATOM   16920 C  CZ2 . TRP   B 1 374  ? 33.10500   81.90100  -25.72500 1.000 26.73356  ?  374  TRP   B CZ2 1 
ATOM   16921 C  CZ3 . TRP   B 1 374  ? 32.37600   83.89600  -26.87400 1.000 28.05532  ?  374  TRP   B CZ3 1 
ATOM   16922 C  CH2 . TRP   B 1 374  ? 32.61100   83.17600  -25.69600 1.000 23.46900  ?  374  TRP   B CH2 1 
ATOM   16923 N  N   . TYR   B 1 375  ? 30.43000   82.49700  -30.39700 1.000 39.66807  ?  375  TYR   B N   1 
ATOM   16924 C  CA  . TYR   B 1 375  ? 29.37000   82.83500  -29.45400 1.000 28.22610  ?  375  TYR   B CA  1 
ATOM   16925 C  C   . TYR   B 1 375  ? 28.13200   81.97700  -29.68300 1.000 31.23205  ?  375  TYR   B C   1 
ATOM   16926 O  O   . TYR   B 1 375  ? 27.53400   81.46100  -28.73200 1.000 33.24555  ?  375  TYR   B O   1 
ATOM   16927 C  CB  . TYR   B 1 375  ? 29.03900   84.32200  -29.59000 1.000 33.73293  ?  375  TYR   B CB  1 
ATOM   16928 C  CG  . TYR   B 1 375  ? 28.03600   84.86900  -28.60100 1.000 43.78734  ?  375  TYR   B CG  1 
ATOM   16929 C  CD1 . TYR   B 1 375  ? 26.67100   84.80000  -28.85400 1.000 37.94891  ?  375  TYR   B CD1 1 
ATOM   16930 C  CD2 . TYR   B 1 375  ? 28.45500   85.49100  -27.43300 1.000 36.67110  ?  375  TYR   B CD2 1 
ATOM   16931 C  CE1 . TYR   B 1 375  ? 25.75400   85.31400  -27.96100 1.000 42.86866  ?  375  TYR   B CE1 1 
ATOM   16932 C  CE2 . TYR   B 1 375  ? 27.54400   86.00800  -26.53400 1.000 35.36066  ?  375  TYR   B CE2 1 
ATOM   16933 C  CZ  . TYR   B 1 375  ? 26.19600   85.91700  -26.80400 1.000 40.51496  ?  375  TYR   B CZ  1 
ATOM   16934 O  OH  . TYR   B 1 375  ? 25.28300   86.43200  -25.91500 1.000 48.96031  ?  375  TYR   B OH  1 
ATOM   16935 N  N   . ARG   B 1 376  ? 27.73200   81.81600  -30.94400 1.000 30.49637  ?  376  ARG   B N   1 
ATOM   16936 C  CA  . ARG   B 1 376  ? 26.49400   81.10000  -31.24500 1.000 42.15974  ?  376  ARG   B CA  1 
ATOM   16937 C  C   . ARG   B 1 376  ? 26.53800   79.63200  -30.83600 1.000 37.59966  ?  376  ARG   B C   1 
ATOM   16938 O  O   . ARG   B 1 376  ? 25.56800   79.16300  -30.21400 1.000 51.62416  ?  376  ARG   B O   1 
ATOM   16939 C  CB  . ARG   B 1 376  ? 26.15800   81.26300  -32.73200 1.000 41.52762  ?  376  ARG   B CB  1 
ATOM   16940 C  CG  . ARG   B 1 376  ? 24.81200   80.68000  -33.12600 1.000 40.13676  ?  376  ARG   B CG  1 
ATOM   16941 C  CD  . ARG   B 1 376  ? 24.59000   80.74600  -34.62900 1.000 34.89512  ?  376  ARG   B CD  1 
ATOM   16942 N  NE  . ARG   B 1 376  ? 25.63800   80.05300  -35.37000 1.000 37.61910  ?  376  ARG   B NE  1 
ATOM   16943 C  CZ  . ARG   B 1 376  ? 26.59000   80.65900  -36.06500 1.000 49.30565  ?  376  ARG   B CZ  1 
ATOM   16944 N  NH1 . ARG   B 1 376  ? 26.64400   81.97800  -36.16000 1.000 43.04528  ?  376  ARG   B NH1 1 
ATOM   16945 N  NH2 . ARG   B 1 376  ? 27.50900   79.92400  -36.68500 1.000 71.87952  ?  376  ARG   B NH2 1 
ATOM   16946 N  N   . PRO   B 1 377  ? 27.58500   78.85400  -31.13800 1.000 32.20565  ?  377  PRO   B N   1 
ATOM   16947 C  CA  . PRO   B 1 377  ? 27.59500   77.46200  -30.66000 1.000 28.00792  ?  377  PRO   B CA  1 
ATOM   16948 C  C   . PRO   B 1 377  ? 27.86200   77.33100  -29.17000 1.000 35.78613  ?  377  PRO   B C   1 
ATOM   16949 O  O   . PRO   B 1 377  ? 27.30800   76.42700  -28.53300 1.000 44.28039  ?  377  PRO   B O   1 
ATOM   16950 C  CB  . PRO   B 1 377  ? 28.70900   76.81600  -31.49400 1.000 20.42314  ?  377  PRO   B CB  1 
ATOM   16951 C  CG  . PRO   B 1 377  ? 29.62400   77.93700  -31.80800 1.000 43.99676  ?  377  PRO   B CG  1 
ATOM   16952 C  CD  . PRO   B 1 377  ? 28.73800   79.13000  -32.01700 1.000 35.36104  ?  377  PRO   B CD  1 
ATOM   16953 N  N   . TYR   B 1 378  ? 28.69700   78.20100  -28.59500 1.000 40.10449  ?  378  TYR   B N   1 
ATOM   16954 C  CA  . TYR   B 1 378  ? 29.03200   78.08900  -27.17700 1.000 29.86588  ?  378  TYR   B CA  1 
ATOM   16955 C  C   . TYR   B 1 378  ? 27.80300   78.30300  -26.30300 1.000 38.73725  ?  378  TYR   B C   1 
ATOM   16956 O  O   . TYR   B 1 378  ? 27.54400   77.52900  -25.37500 1.000 59.19250  ?  378  TYR   B O   1 
ATOM   16957 C  CB  . TYR   B 1 378  ? 30.13100   79.09300  -26.82100 1.000 30.36375  ?  378  TYR   B CB  1 
ATOM   16958 C  CG  . TYR   B 1 378  ? 30.62600   79.02200  -25.39200 1.000 28.08530  ?  378  TYR   B CG  1 
ATOM   16959 C  CD1 . TYR   B 1 378  ? 30.03000   79.77700  -24.38900 1.000 40.65099  ?  378  TYR   B CD1 1 
ATOM   16960 C  CD2 . TYR   B 1 378  ? 31.70300   78.21600  -25.05000 1.000 32.16833  ?  378  TYR   B CD2 1 
ATOM   16961 C  CE1 . TYR   B 1 378  ? 30.48400   79.72100  -23.08500 1.000 30.06211  ?  378  TYR   B CE1 1 
ATOM   16962 C  CE2 . TYR   B 1 378  ? 32.16600   78.15500  -23.74800 1.000 37.27307  ?  378  TYR   B CE2 1 
ATOM   16963 C  CZ  . TYR   B 1 378  ? 31.55300   78.91000  -22.77000 1.000 32.18994  ?  378  TYR   B CZ  1 
ATOM   16964 O  OH  . TYR   B 1 378  ? 32.00900   78.85200  -21.47400 1.000 37.93251  ?  378  TYR   B OH  1 
ATOM   16965 N  N   . PHE   B 1 379  ? 27.03600   79.35200  -26.58400 1.000 35.13144  ?  379  PHE   B N   1 
ATOM   16966 C  CA  . PHE   B 1 379  ? 25.83900   79.66300  -25.81700 1.000 37.53862  ?  379  PHE   B CA  1 
ATOM   16967 C  C   . PHE   B 1 379  ? 24.57100   79.08800  -26.43400 1.000 43.75046  ?  379  PHE   B C   1 
ATOM   16968 O  O   . PHE   B 1 379  ? 23.48400   79.30100  -25.88600 1.000 49.56303  ?  379  PHE   B O   1 
ATOM   16969 C  CB  . PHE   B 1 379  ? 25.69400   81.17900  -25.65700 1.000 34.01655  ?  379  PHE   B CB  1 
ATOM   16970 C  CG  . PHE   B 1 379  ? 26.84400   81.82300  -24.93900 1.000 39.28621  ?  379  PHE   B CG  1 
ATOM   16971 C  CD1 . PHE   B 1 379  ? 26.90500   81.81600  -23.55600 1.000 39.36892  ?  379  PHE   B CD1 1 
ATOM   16972 C  CD2 . PHE   B 1 379  ? 27.86300   82.44000  -25.64600 1.000 38.65093  ?  379  PHE   B CD2 1 
ATOM   16973 C  CE1 . PHE   B 1 379  ? 27.96000   82.40900  -22.89000 1.000 38.38433  ?  379  PHE   B CE1 1 
ATOM   16974 C  CE2 . PHE   B 1 379  ? 28.92100   83.03500  -24.98700 1.000 39.98262  ?  379  PHE   B CE2 1 
ATOM   16975 C  CZ  . PHE   B 1 379  ? 28.96900   83.02000  -23.60700 1.000 39.10895  ?  379  PHE   B CZ  1 
ATOM   16976 N  N   . GLY   B 1 380  ? 24.68100   78.37100  -27.55100 1.000 37.86146  ?  380  GLY   B N   1 
ATOM   16977 C  CA  . GLY   B 1 380  ? 23.53200   77.75300  -28.18400 1.000 42.51154  ?  380  GLY   B CA  1 
ATOM   16978 C  C   . GLY   B 1 380  ? 22.43500   78.73300  -28.54100 1.000 48.20650  ?  380  GLY   B C   1 
ATOM   16979 O  O   . GLY   B 1 380  ? 21.30600   78.61500  -28.05600 1.000 59.53013  ?  380  GLY   B O   1 
ATOM   16980 N  N   . VAL   B 1 381  ? 22.75200   79.70700  -29.38600 1.000 50.43773  ?  381  VAL   B N   1 
ATOM   16981 C  CA  . VAL   B 1 381  ? 21.80600   80.75600  -29.74600 1.000 51.00120  ?  381  VAL   B CA  1 
ATOM   16982 C  C   . VAL   B 1 381  ? 20.95600   80.26700  -30.91100 1.000 40.16057  ?  381  VAL   B C   1 
ATOM   16983 O  O   . VAL   B 1 381  ? 21.48200   79.88200  -31.96000 1.000 27.41379  ?  381  VAL   B O   1 
ATOM   16984 C  CB  . VAL   B 1 381  ? 22.53100   82.06300  -30.09800 1.000 41.05599  ?  381  VAL   B CB  1 
ATOM   16985 C  CG1 . VAL   B 1 381  ? 21.55100   83.22700  -30.09600 1.000 38.33581  ?  381  VAL   B CG1 1 
ATOM   16986 C  CG2 . VAL   B 1 381  ? 23.66500   82.31500  -29.12000 1.000 43.68914  ?  381  VAL   B CG2 1 
ATOM   16987 N  N   . THR   B 1 382  ? 19.64400   80.27700  -30.72200 1.000 48.47414  ?  382  THR   B N   1 
ATOM   16988 C  CA  . THR   B 1 382  ? 18.67400   79.90700  -31.73500 1.000 34.23837  ?  382  THR   B CA  1 
ATOM   16989 C  C   . THR   B 1 382  ? 17.93700   81.14200  -32.23500 1.000 40.23964  ?  382  THR   B C   1 
ATOM   16990 O  O   . THR   B 1 382  ? 17.97500   82.19900  -31.59700 1.000 33.35820  ?  382  THR   B O   1 
ATOM   16991 C  CB  . THR   B 1 382  ? 17.66500   78.89700  -31.17100 1.000 25.99049  ?  382  THR   B CB  1 
ATOM   16992 O  OG1 . THR   B 1 382  ? 17.08900   79.41700  -29.96700 1.000 41.74266  ?  382  THR   B OG1 1 
ATOM   16993 C  CG2 . THR   B 1 382  ? 18.35000   77.57400  -30.87200 1.000 38.68055  ?  382  THR   B CG2 1 
ATOM   16994 N  N   . PRO   B 1 383  ? 17.26700   81.05400  -33.38900 1.000 38.94014  ?  383  PRO   B N   1 
ATOM   16995 C  CA  . PRO   B 1 383  ? 16.44700   82.18800  -33.84500 1.000 29.96798  ?  383  PRO   B CA  1 
ATOM   16996 C  C   . PRO   B 1 383  ? 15.31300   82.54100  -32.89800 1.000 35.19091  ?  383  PRO   B C   1 
ATOM   16997 O  O   . PRO   B 1 383  ? 14.67300   83.58300  -33.09300 1.000 52.23160  ?  383  PRO   B O   1 
ATOM   16998 C  CB  . PRO   B 1 383  ? 15.91000   81.71300  -35.20200 1.000 35.95295  ?  383  PRO   B CB  1 
ATOM   16999 C  CG  . PRO   B 1 383  ? 16.91100   80.71700  -35.66700 1.000 36.74491  ?  383  PRO   B CG  1 
ATOM   17000 C  CD  . PRO   B 1 383  ? 17.38700   80.01500  -34.42800 1.000 38.86062  ?  383  PRO   B CD  1 
ATOM   17001 N  N   . ALA   B 1 384  ? 15.04300   81.71600  -31.88600 1.000 38.43828  ?  384  ALA   B N   1 
ATOM   17002 C  CA  . ALA   B 1 384  ? 14.01000   82.00000  -30.90100 1.000 39.24499  ?  384  ALA   B CA  1 
ATOM   17003 C  C   . ALA   B 1 384  ? 14.51300   82.82900  -29.72700 1.000 27.11442  ?  384  ALA   B C   1 
ATOM   17004 O  O   . ALA   B 1 384  ? 13.70800   83.21600  -28.87400 1.000 51.63678  ?  384  ALA   B O   1 
ATOM   17005 C  CB  . ALA   B 1 384  ? 13.40800   80.69300  -30.37700 1.000 38.73086  ?  384  ALA   B CB  1 
ATOM   17006 N  N   . ASP   B 1 385  ? 15.81300   83.10000  -29.65600 1.000 34.42161  ?  385  ASP   B N   1 
ATOM   17007 C  CA  . ASP   B 1 385  ? 16.36100   83.90300  -28.57600 1.000 29.54697  ?  385  ASP   B CA  1 
ATOM   17008 C  C   . ASP   B 1 385  ? 16.07200   85.38300  -28.80700 1.000 33.26945  ?  385  ASP   B C   1 
ATOM   17009 O  O   . ASP   B 1 385  ? 15.80800   85.82700  -29.92800 1.000 38.50023  ?  385  ASP   B O   1 
ATOM   17010 C  CB  . ASP   B 1 385  ? 17.86900   83.67900  -28.44600 1.000 31.63708  ?  385  ASP   B CB  1 
ATOM   17011 C  CG  . ASP   B 1 385  ? 18.21100   82.43100  -27.65300 1.000 34.80844  ?  385  ASP   B CG  1 
ATOM   17012 O  OD1 . ASP   B 1 385  ? 17.73100   82.30000  -26.50700 1.000 20.50026  ?  385  ASP   B OD1 1 
ATOM   17013 O  OD2 . ASP   B 1 385  ? 18.96000   81.57800  -28.17800 1.000 42.81848  -1 385  ASP   B OD2 1 
ATOM   17014 N  N   . LYS   B 1 386  ? 16.11500   86.14700  -27.71800 1.000 24.19036  ?  386  LYS   B N   1 
ATOM   17015 C  CA  . LYS   B 1 386  ? 15.95300   87.59400  -27.76100 1.000 29.83213  ?  386  LYS   B CA  1 
ATOM   17016 C  C   . LYS   B 1 386  ? 17.04000   88.22100  -26.90300 1.000 32.36233  ?  386  LYS   B C   1 
ATOM   17017 O  O   . LYS   B 1 386  ? 17.26400   87.78800  -25.76800 1.000 38.13529  ?  386  LYS   B O   1 
ATOM   17018 C  CB  . LYS   B 1 386  ? 14.56300   88.02100  -27.27300 1.000 30.48753  ?  386  LYS   B CB  1 
ATOM   17019 C  CG  . LYS   B 1 386  ? 13.41300   87.34600  -28.01100 1.000 35.26797  ?  386  LYS   B CG  1 
ATOM   17020 C  CD  . LYS   B 1 386  ? 12.28800   88.32300  -28.30900 1.000 62.12383  ?  386  LYS   B CD  1 
ATOM   17021 C  CE  . LYS   B 1 386  ? 10.96300   87.83700  -27.74800 1.000 43.28168  ?  386  LYS   B CE  1 
ATOM   17022 N  NZ  . LYS   B 1 386  ? 10.57200   86.50800  -28.29100 1.000 62.96016  ?  386  LYS   B NZ  1 
ATOM   17023 N  N   . ALA   B 1 387  ? 17.71600   89.23000  -27.44600 1.000 35.88226  ?  387  ALA   B N   1 
ATOM   17024 C  CA  . ALA   B 1 387  ? 18.87800   89.82300  -26.80500 1.000 35.60042  ?  387  ALA   B CA  1 
ATOM   17025 C  C   . ALA   B 1 387  ? 18.64000   91.29600  -26.50200 1.000 43.08111  ?  387  ALA   B C   1 
ATOM   17026 O  O   . ALA   B 1 387  ? 17.75300   91.94000  -27.07000 1.000 51.87025  ?  387  ALA   B O   1 
ATOM   17027 C  CB  . ALA   B 1 387  ? 20.13100   89.66800  -27.67600 1.000 33.18382  ?  387  ALA   B CB  1 
ATOM   17028 N  N   . LEU   B 1 388  ? 19.46500   91.82300  -25.60300 1.000 29.68052  ?  388  LEU   B N   1 
ATOM   17029 C  CA  . LEU   B 1 388  ? 19.36300   93.19500  -25.12600 1.000 29.89415  ?  388  LEU   B CA  1 
ATOM   17030 C  C   . LEU   B 1 388  ? 20.52600   94.01300  -25.67100 1.000 36.92337  ?  388  LEU   B C   1 
ATOM   17031 O  O   . LEU   B 1 388  ? 21.68700   93.61100  -25.54100 1.000 36.23426  ?  388  LEU   B O   1 
ATOM   17032 C  CB  . LEU   B 1 388  ? 19.36700   93.22600  -23.59600 1.000 26.73222  ?  388  LEU   B CB  1 
ATOM   17033 C  CG  . LEU   B 1 388  ? 18.27000   94.01800  -22.88800 1.000 45.04269  ?  388  LEU   B CG  1 
ATOM   17034 C  CD1 . LEU   B 1 388  ? 16.88000   93.53800  -23.28300 1.000 50.55991  ?  388  LEU   B CD1 1 
ATOM   17035 C  CD2 . LEU   B 1 388  ? 18.45800   93.96200  -21.37900 1.000 39.38820  ?  388  LEU   B CD2 1 
ATOM   17036 N  N   . VAL   B 1 389  ? 20.21700   95.15400  -26.28100 1.000 36.77935  ?  389  VAL   B N   1 
ATOM   17037 C  CA  . VAL   B 1 389  ? 21.26100   96.08600  -26.75000 1.000 35.16299  ?  389  VAL   B CA  1 
ATOM   17038 C  C   . VAL   B 1 389  ? 21.45600   97.09600  -25.62500 1.000 40.36115  ?  389  VAL   B C   1 
ATOM   17039 O  O   . VAL   B 1 389  ? 20.91800   98.20700  -25.62400 1.000 40.49820  ?  389  VAL   B O   1 
ATOM   17040 C  CB  . VAL   B 1 389  ? 20.90300   96.73700  -28.09100 1.000 24.48193  ?  389  VAL   B CB  1 
ATOM   17041 C  CG1 . VAL   B 1 389  ? 22.02600   97.65200  -28.55800 1.000 38.00604  ?  389  VAL   B CG1 1 
ATOM   17042 C  CG2 . VAL   B 1 389  ? 20.62600   95.67100  -29.14000 1.000 21.80493  ?  389  VAL   B CG2 1 
ATOM   17043 N  N   . TYR   B 1 390  ? 22.25200   96.69400  -24.63300 1.000 38.82249  ?  390  TYR   B N   1 
ATOM   17044 C  CA  . TYR   B 1 390  ? 22.46200   97.45600  -23.40700 1.000 42.88404  ?  390  TYR   B CA  1 
ATOM   17045 C  C   . TYR   B 1 390  ? 23.69700   98.34800  -23.48900 1.000 45.23885  ?  390  TYR   B C   1 
ATOM   17046 O  O   . TYR   B 1 390  ? 23.64500   99.52400  -23.11400 1.000 49.20997  ?  390  TYR   B O   1 
ATOM   17047 C  CB  . TYR   B 1 390  ? 22.57500   96.49100  -22.22000 1.000 30.91282  ?  390  TYR   B CB  1 
ATOM   17048 C  CG  . TYR   B 1 390  ? 22.74300   97.14100  -20.86000 1.000 37.80455  ?  390  TYR   B CG  1 
ATOM   17049 C  CD1 . TYR   B 1 390  ? 23.99700   97.53100  -20.40200 1.000 49.51478  ?  390  TYR   B CD1 1 
ATOM   17050 C  CD2 . TYR   B 1 390  ? 21.65300   97.33200  -20.02000 1.000 44.37012  ?  390  TYR   B CD2 1 
ATOM   17051 C  CE1 . TYR   B 1 390  ? 24.15600   98.11400  -19.16100 1.000 47.93723  ?  390  TYR   B CE1 1 
ATOM   17052 C  CE2 . TYR   B 1 390  ? 21.80600   97.91000  -18.77100 1.000 41.61353  ?  390  TYR   B CE2 1 
ATOM   17053 C  CZ  . TYR   B 1 390  ? 23.06000   98.30100  -18.35000 1.000 47.56317  ?  390  TYR   B CZ  1 
ATOM   17054 O  OH  . TYR   B 1 390  ? 23.22500   98.88000  -17.11400 1.000 61.78557  ?  390  TYR   B OH  1 
ATOM   17055 N  N   . SER   B 1 391  ? 24.81500   97.80200  -23.96200 1.000 41.63309  ?  391  SER   B N   1 
ATOM   17056 C  CA  . SER   B 1 391  ? 26.04800   98.57100  -24.04000 1.000 44.84470  ?  391  SER   B CA  1 
ATOM   17057 C  C   . SER   B 1 391  ? 25.96400   99.60800  -25.15100 1.000 50.25134  ?  391  SER   B C   1 
ATOM   17058 O  O   . SER   B 1 391  ? 25.36600   99.36900  -26.20400 1.000 50.53958  ?  391  SER   B O   1 
ATOM   17059 C  CB  . SER   B 1 391  ? 27.24000   97.64500  -24.27800 1.000 30.36986  ?  391  SER   B CB  1 
ATOM   17060 O  OG  . SER   B 1 391  ? 27.36700   96.70000  -23.23100 1.000 39.17365  ?  391  SER   B OG  1 
ATOM   17061 N  N   . SER   B 1 392  ? 26.57000   100.77000 -24.90700 1.000 33.34305  ?  392  SER   B N   1 
ATOM   17062 C  CA  . SER   B 1 392  ? 26.60500   101.81900 -25.91700 1.000 40.65691  ?  392  SER   B CA  1 
ATOM   17063 C  C   . SER   B 1 392  ? 27.37400   101.33700 -27.13900 1.000 53.16976  ?  392  SER   B C   1 
ATOM   17064 O  O   . SER   B 1 392  ? 28.35500   100.59800 -27.02000 1.000 50.53542  ?  392  SER   B O   1 
ATOM   17065 C  CB  . SER   B 1 392  ? 27.26000   103.07900 -25.35300 1.000 29.07219  ?  392  SER   B CB  1 
ATOM   17066 O  OG  . SER   B 1 392  ? 28.65800   103.05800 -25.57500 1.000 41.77483  ?  392  SER   B OG  1 
ATOM   17067 N  N   . PHE   B 1 393  ? 26.93300   101.76600 -28.32400 1.000 48.99180  ?  393  PHE   B N   1 
ATOM   17068 C  CA  . PHE   B 1 393  ? 27.56700   101.25500 -29.53200 1.000 55.24013  ?  393  PHE   B CA  1 
ATOM   17069 C  C   . PHE   B 1 393  ? 29.01200   101.71700 -29.67600 1.000 47.26982  ?  393  PHE   B C   1 
ATOM   17070 O  O   . PHE   B 1 393  ? 29.70900   101.23200 -30.57400 1.000 50.94085  ?  393  PHE   B O   1 
ATOM   17071 C  CB  . PHE   B 1 393  ? 26.73900   101.61300 -30.77500 1.000 49.21366  ?  393  PHE   B CB  1 
ATOM   17072 C  CG  . PHE   B 1 393  ? 26.94700   103.00900 -31.29300 1.000 46.30664  ?  393  PHE   B CG  1 
ATOM   17073 C  CD1 . PHE   B 1 393  ? 27.00300   104.10100 -30.44100 1.000 50.03845  ?  393  PHE   B CD1 1 
ATOM   17074 C  CD2 . PHE   B 1 393  ? 27.06100   103.22400 -32.65800 1.000 28.49675  ?  393  PHE   B CD2 1 
ATOM   17075 C  CE1 . PHE   B 1 393  ? 27.18500   105.38000 -30.94500 1.000 46.93661  ?  393  PHE   B CE1 1 
ATOM   17076 C  CE2 . PHE   B 1 393  ? 27.23900   104.49400 -33.16400 1.000 44.72644  ?  393  PHE   B CE2 1 
ATOM   17077 C  CZ  . PHE   B 1 393  ? 27.30100   105.57300 -32.30800 1.000 47.66479  ?  393  PHE   B CZ  1 
ATOM   17078 N  N   . SER   B 1 394  ? 29.47900   102.60500 -28.79900 1.000 33.76229  ?  394  SER   B N   1 
ATOM   17079 C  CA  . SER   B 1 394  ? 30.87700   103.00200 -28.72500 1.000 32.18473  ?  394  SER   B CA  1 
ATOM   17080 C  C   . SER   B 1 394  ? 31.69600   102.10100 -27.80500 1.000 39.18426  ?  394  SER   B C   1 
ATOM   17081 O  O   . SER   B 1 394  ? 32.84900   102.42800 -27.51000 1.000 36.06412  ?  394  SER   B O   1 
ATOM   17082 C  CB  . SER   B 1 394  ? 30.98800   104.45700 -28.25800 1.000 38.19111  ?  394  SER   B CB  1 
ATOM   17083 O  OG  . SER   B 1 394  ? 30.31500   105.33200 -29.14700 1.000 49.67717  ?  394  SER   B OG  1 
ATOM   17084 N  N   . PHE   B 1 395  ? 31.12900   100.98900 -27.33900 1.000 42.26416  ?  395  PHE   B N   1 
ATOM   17085 C  CA  . PHE   B 1 395  ? 31.84100   100.02800 -26.50500 1.000 47.04099  ?  395  PHE   B CA  1 
ATOM   17086 C  C   . PHE   B 1 395  ? 31.68500   98.62900  -27.07600 1.000 45.97765  ?  395  PHE   B C   1 
ATOM   17087 O  O   . PHE   B 1 395  ? 30.63000   98.28500  -27.61400 1.000 56.95656  ?  395  PHE   B O   1 
ATOM   17088 C  CB  . PHE   B 1 395  ? 31.34600   100.06100 -25.05400 1.000 38.33825  ?  395  PHE   B CB  1 
ATOM   17089 C  CG  . PHE   B 1 395  ? 32.18100   100.91900 -24.16100 1.000 51.29516  ?  395  PHE   B CG  1 
ATOM   17090 C  CD1 . PHE   B 1 395  ? 33.38700   100.44500 -23.66800 1.000 77.34194  ?  395  PHE   B CD1 1 
ATOM   17091 C  CD2 . PHE   B 1 395  ? 31.78000   102.20500 -23.83500 1.000 57.83141  ?  395  PHE   B CD2 1 
ATOM   17092 C  CE1 . PHE   B 1 395  ? 34.17700   101.22900 -22.85500 1.000 90.44660  ?  395  PHE   B CE1 1 
ATOM   17093 C  CE2 . PHE   B 1 395  ? 32.55500   102.99800 -23.01200 1.000 69.00141  ?  395  PHE   B CE2 1 
ATOM   17094 C  CZ  . PHE   B 1 395  ? 33.75800   102.51500 -22.52700 1.000 93.61681  ?  395  PHE   B CZ  1 
ATOM   17095 N  N   . ASP   B 1 396  ? 32.74800   97.82700  -26.95700 1.000 59.86772  ?  396  ASP   B N   1 
ATOM   17096 C  CA  . ASP   B 1 396  ? 32.77100   96.50600  -27.57900 1.000 41.42053  ?  396  ASP   B CA  1 
ATOM   17097 C  C   . ASP   B 1 396  ? 31.64900   95.60300  -27.08300 1.000 38.12175  ?  396  ASP   B C   1 
ATOM   17098 O  O   . ASP   B 1 396  ? 31.29100   94.64500  -27.77700 1.000 43.13143  ?  396  ASP   B O   1 
ATOM   17099 C  CB  . ASP   B 1 396  ? 34.12600   95.83000  -27.34600 1.000 39.95656  ?  396  ASP   B CB  1 
ATOM   17100 C  CG  . ASP   B 1 396  ? 34.80300   96.29900  -26.07600 1.000 68.11466  ?  396  ASP   B CG  1 
ATOM   17101 O  OD1 . ASP   B 1 396  ? 34.82700   97.52600  -25.83500 1.000 64.06074  ?  396  ASP   B OD1 1 
ATOM   17102 O  OD2 . ASP   B 1 396  ? 35.31300   95.44200  -25.32200 1.000 72.70864  -1 396  ASP   B OD2 1 
ATOM   17103 N  N   . GLY   B 1 397  ? 31.08800   95.88200  -25.90500 1.000 33.30010  ?  397  GLY   B N   1 
ATOM   17104 C  CA  . GLY   B 1 397  ? 29.92300   95.13900  -25.45500 1.000 37.24385  ?  397  GLY   B CA  1 
ATOM   17105 C  C   . GLY   B 1 397  ? 28.76100   95.21600  -26.42400 1.000 38.02113  ?  397  GLY   B C   1 
ATOM   17106 O  O   . GLY   B 1 397  ? 28.00900   94.24900  -26.57500 1.000 37.96311  ?  397  GLY   B O   1 
ATOM   17107 N  N   . SER   B 1 398  ? 28.59800   96.35900  -27.09900 1.000 33.01760  ?  398  SER   B N   1 
ATOM   17108 C  CA  . SER   B 1 398  ? 27.54400   96.48400  -28.10000 1.000 39.82602  ?  398  SER   B CA  1 
ATOM   17109 C  C   . SER   B 1 398  ? 27.79200   95.57700  -29.29600 1.000 36.51989  ?  398  SER   B C   1 
ATOM   17110 O  O   . SER   B 1 398  ? 26.83600   95.09000  -29.90900 1.000 51.05924  ?  398  SER   B O   1 
ATOM   17111 C  CB  . SER   B 1 398  ? 27.42600   97.92800  -28.56900 1.000 27.26787  ?  398  SER   B CB  1 
ATOM   17112 O  OG  . SER   B 1 398  ? 28.52100   98.27000  -29.40000 1.000 45.82028  ?  398  SER   B OG  1 
ATOM   17113 N  N   . ALA   B 1 399  ? 29.05900   95.36000  -29.66000 1.000 23.94025  ?  399  ALA   B N   1 
ATOM   17114 C  CA  . ALA   B 1 399  ? 29.35500   94.41600  -30.73000 1.000 27.60613  ?  399  ALA   B CA  1 
ATOM   17115 C  C   . ALA   B 1 399  ? 28.90300   93.01300  -30.35200 1.000 33.51862  ?  399  ALA   B C   1 
ATOM   17116 O  O   . ALA   B 1 399  ? 28.39700   92.26500  -31.19700 1.000 34.68702  ?  399  ALA   B O   1 
ATOM   17117 C  CB  . ALA   B 1 399  ? 30.84800   94.44000  -31.05700 1.000 30.12708  ?  399  ALA   B CB  1 
ATOM   17118 N  N   . LEU   B 1 400  ? 29.07200   92.64200  -29.08100 1.000 33.89822  ?  400  LEU   B N   1 
ATOM   17119 C  CA  . LEU   B 1 400  ? 28.51200   91.38600  -28.59300 1.000 33.03826  ?  400  LEU   B CA  1 
ATOM   17120 C  C   . LEU   B 1 400  ? 26.98900   91.42800  -28.60900 1.000 39.33702  ?  400  LEU   B C   1 
ATOM   17121 O  O   . LEU   B 1 400  ? 26.33700   90.42000  -28.90700 1.000 37.28713  ?  400  LEU   B O   1 
ATOM   17122 C  CB  . LEU   B 1 400  ? 29.03500   91.10000  -27.18300 1.000 31.93383  ?  400  LEU   B CB  1 
ATOM   17123 C  CG  . LEU   B 1 400  ? 28.84500   89.71900  -26.54400 1.000 33.10902  ?  400  LEU   B CG  1 
ATOM   17124 C  CD1 . LEU   B 1 400  ? 29.88300   89.51900  -25.45400 1.000 34.76282  ?  400  LEU   B CD1 1 
ATOM   17125 C  CD2 . LEU   B 1 400  ? 27.44800   89.53100  -25.96800 1.000 31.11479  ?  400  LEU   B CD2 1 
ATOM   17126 N  N   . ASP   B 1 401  ? 26.40700   92.58600  -28.29100 1.000 33.94091  ?  401  ASP   B N   1 
ATOM   17127 C  CA  . ASP   B 1 401  ? 24.95300   92.71400  -28.27000 1.000 24.21144  ?  401  ASP   B CA  1 
ATOM   17128 C  C   . ASP   B 1 401  ? 24.36000   92.49600  -29.65600 1.000 29.23448  ?  401  ASP   B C   1 
ATOM   17129 O  O   . ASP   B 1 401  ? 23.41000   91.72400  -29.82600 1.000 34.76998  ?  401  ASP   B O   1 
ATOM   17130 C  CB  . ASP   B 1 401  ? 24.55600   94.09200  -27.73800 1.000 23.57309  ?  401  ASP   B CB  1 
ATOM   17131 C  CG  . ASP   B 1 401  ? 24.92200   94.28600  -26.28300 1.000 34.83339  ?  401  ASP   B CG  1 
ATOM   17132 O  OD1 . ASP   B 1 401  ? 25.36000   93.30800  -25.64200 1.000 49.23512  ?  401  ASP   B OD1 1 
ATOM   17133 O  OD2 . ASP   B 1 401  ? 24.76800   95.42000  -25.78000 1.000 35.25826  -1 401  ASP   B OD2 1 
ATOM   17134 N  N   . ILE   B 1 402  ? 24.91800   93.16400  -30.66200 1.000 30.33240  ?  402  ILE   B N   1 
ATOM   17135 C  CA  . ILE   B 1 402  ? 24.30100   93.25800  -31.98000 1.000 30.41338  ?  402  ILE   B CA  1 
ATOM   17136 C  C   . ILE   B 1 402  ? 24.75500   92.12400  -32.88800 1.000 31.49606  ?  402  ILE   B C   1 
ATOM   17137 O  O   . ILE   B 1 402  ? 23.93600   91.35200  -33.39800 1.000 37.87258  ?  402  ILE   B O   1 
ATOM   17138 C  CB  . ILE   B 1 402  ? 24.62100   94.61800  -32.62400 1.000 27.57529  ?  402  ILE   B CB  1 
ATOM   17139 C  CG1 . ILE   B 1 402  ? 24.19400   95.75900  -31.69900 1.000 29.31273  ?  402  ILE   B CG1 1 
ATOM   17140 C  CG2 . ILE   B 1 402  ? 23.96300   94.73100  -33.99200 1.000 20.50825  ?  402  ILE   B CG2 1 
ATOM   17141 C  CD1 . ILE   B 1 402  ? 24.83700   97.08100  -32.03800 1.000 21.54123  ?  402  ILE   B CD1 1 
ATOM   17142 N  N   . PHE   B 1 403  ? 26.06900   92.01900  -33.09200 1.000 36.73190  ?  403  PHE   B N   1 
ATOM   17143 C  CA  . PHE   B 1 403  ? 26.59100   91.20000  -34.18200 1.000 29.82138  ?  403  PHE   B CA  1 
ATOM   17144 C  C   . PHE   B 1 403  ? 26.48300   89.71000  -33.88400 1.000 29.08146  ?  403  PHE   B C   1 
ATOM   17145 O  O   . PHE   B 1 403  ? 26.24800   88.90900  -34.79600 1.000 27.58668  ?  403  PHE   B O   1 
ATOM   17146 C  CB  . PHE   B 1 403  ? 28.03800   91.59500  -34.46200 1.000 28.60888  ?  403  PHE   B CB  1 
ATOM   17147 C  CG  . PHE   B 1 403  ? 28.20900   93.05000  -34.77600 1.000 27.80746  ?  403  PHE   B CG  1 
ATOM   17148 C  CD1 . PHE   B 1 403  ? 27.37200   93.67800  -35.68000 1.000 30.76675  ?  403  PHE   B CD1 1 
ATOM   17149 C  CD2 . PHE   B 1 403  ? 29.18900   93.79700  -34.14900 1.000 29.26320  ?  403  PHE   B CD2 1 
ATOM   17150 C  CE1 . PHE   B 1 403  ? 27.52000   95.01900  -35.96500 1.000 32.77820  ?  403  PHE   B CE1 1 
ATOM   17151 C  CE2 . PHE   B 1 403  ? 29.34400   95.13900  -34.42900 1.000 28.69101  ?  403  PHE   B CE2 1 
ATOM   17152 C  CZ  . PHE   B 1 403  ? 28.50900   95.75100  -35.33900 1.000 24.42817  ?  403  PHE   B CZ  1 
ATOM   17153 N  N   . THR   B 1 404  ? 26.65200   89.31800  -32.62000 1.000 30.49902  ?  404  THR   B N   1 
ATOM   17154 C  CA  . THR   B 1 404  ? 26.64600   87.89600  -32.29000 1.000 35.73618  ?  404  THR   B CA  1 
ATOM   17155 C  C   . THR   B 1 404  ? 25.26700   87.28200  -32.49800 1.000 36.51522  ?  404  THR   B C   1 
ATOM   17156 O  O   . THR   B 1 404  ? 25.15100   86.17200  -33.03200 1.000 39.57749  ?  404  THR   B O   1 
ATOM   17157 C  CB  . THR   B 1 404  ? 27.10400   87.68800  -30.84900 1.000 33.87654  ?  404  THR   B CB  1 
ATOM   17158 O  OG1 . THR   B 1 404  ? 26.15900   88.29100  -29.95800 1.000 37.33143  ?  404  THR   B OG1 1 
ATOM   17159 C  CG2 . THR   B 1 404  ? 28.47200   88.31500  -30.63300 1.000 38.99699  ?  404  THR   B CG2 1 
ATOM   17160 N  N   . HIS   B 1 405  ? 24.21200   87.98800  -32.08900 1.000 37.84971  ?  405  HIS   B N   1 
ATOM   17161 C  CA  . HIS   B 1 405  ? 22.86500   87.43700  -32.18300 1.000 34.41686  ?  405  HIS   B CA  1 
ATOM   17162 C  C   . HIS   B 1 405  ? 22.27500   87.58600  -33.57900 1.000 32.81393  ?  405  HIS   B C   1 
ATOM   17163 O  O   . HIS   B 1 405  ? 21.43800   86.76900  -33.98000 1.000 41.93438  ?  405  HIS   B O   1 
ATOM   17164 C  CB  . HIS   B 1 405  ? 21.95800   88.10100  -31.14800 1.000 30.58826  ?  405  HIS   B CB  1 
ATOM   17165 C  CG  . HIS   B 1 405  ? 22.48100   88.01000  -29.74800 1.000 38.00463  ?  405  HIS   B CG  1 
ATOM   17166 N  ND1 . HIS   B 1 405  ? 23.08000   89.07200  -29.10700 1.000 31.86680  ?  405  HIS   B ND1 1 
ATOM   17167 C  CD2 . HIS   B 1 405  ? 22.51000   86.97600  -28.87400 1.000 37.83190  ?  405  HIS   B CD2 1 
ATOM   17168 C  CE1 . HIS   B 1 405  ? 23.44800   88.69900  -27.89400 1.000 38.67373  ?  405  HIS   B CE1 1 
ATOM   17169 N  NE2 . HIS   B 1 405  ? 23.11400   87.43200  -27.72700 1.000 40.38171  ?  405  HIS   B NE2 1 
ATOM   17170 N  N   . LEU   B 1 406  ? 22.69200   88.60900  -34.33000 1.000 26.88280  ?  406  LEU   B N   1 
ATOM   17171 C  CA  . LEU   B 1 406  ? 22.18700   88.77200  -35.69000 1.000 29.58237  ?  406  LEU   B CA  1 
ATOM   17172 C  C   . LEU   B 1 406  ? 22.61200   87.62000  -36.59000 1.000 34.79076  ?  406  LEU   B C   1 
ATOM   17173 O  O   . LEU   B 1 406  ? 21.87900   87.25500  -37.51600 1.000 49.11079  ?  406  LEU   B O   1 
ATOM   17174 C  CB  . LEU   B 1 406  ? 22.65300   90.10500  -36.27600 1.000 21.78833  ?  406  LEU   B CB  1 
ATOM   17175 C  CG  . LEU   B 1 406  ? 21.80600   91.32700  -35.91700 1.000 27.76125  ?  406  LEU   B CG  1 
ATOM   17176 C  CD1 . LEU   B 1 406  ? 22.29600   92.55900  -36.66600 1.000 23.82252  ?  406  LEU   B CD1 1 
ATOM   17177 C  CD2 . LEU   B 1 406  ? 20.33100   91.06900  -36.20300 1.000 25.55223  ?  406  LEU   B CD2 1 
ATOM   17178 N  N   . LEU   B 1 407  ? 23.78200   87.03300  -36.33900 1.000 31.38732  ?  407  LEU   B N   1 
ATOM   17179 C  CA  . LEU   B 1 407  ? 24.22500   85.87800  -37.11000 1.000 36.03278  ?  407  LEU   B CA  1 
ATOM   17180 C  C   . LEU   B 1 407  ? 23.54500   84.58500  -36.68200 1.000 35.45095  ?  407  LEU   B C   1 
ATOM   17181 O  O   . LEU   B 1 407  ? 23.79400   83.54200  -37.29600 1.000 36.90247  ?  407  LEU   B O   1 
ATOM   17182 C  CB  . LEU   B 1 407  ? 25.74300   85.71700  -37.00600 1.000 28.63317  ?  407  LEU   B CB  1 
ATOM   17183 C  CG  . LEU   B 1 407  ? 26.58900   86.81500  -37.65200 1.000 38.24702  ?  407  LEU   B CG  1 
ATOM   17184 C  CD1 . LEU   B 1 407  ? 28.02100   86.33700  -37.84200 1.000 27.02538  ?  407  LEU   B CD1 1 
ATOM   17185 C  CD2 . LEU   B 1 407  ? 25.98400   87.26600  -38.97500 1.000 45.27947  ?  407  LEU   B CD2 1 
ATOM   17186 N  N   . ALA   B 1 408  ? 22.69600   84.62700  -35.65400 1.000 26.65499  ?  408  ALA   B N   1 
ATOM   17187 C  CA  . ALA   B 1 408  ? 21.98900   83.44700  -35.18000 1.000 35.47376  ?  408  ALA   B CA  1 
ATOM   17188 C  C   . ALA   B 1 408  ? 20.50900   83.44100  -35.53000 1.000 38.23710  ?  408  ALA   B C   1 
ATOM   17189 O  O   . ALA   B 1 408  ? 19.87200   82.38700  -35.42800 1.000 28.63755  ?  408  ALA   B O   1 
ATOM   17190 C  CB  . ALA   B 1 408  ? 22.14500   83.31300  -33.65900 1.000 26.42907  ?  408  ALA   B CB  1 
ATOM   17191 N  N   . GLY   B 1 409  ? 19.94900   84.57400  -35.94200 1.000 28.57968  ?  409  GLY   B N   1 
ATOM   17192 C  CA  . GLY   B 1 409  ? 18.52900   84.68100  -36.19300 1.000 41.05321  ?  409  GLY   B CA  1 
ATOM   17193 C  C   . GLY   B 1 409  ? 17.71600   85.23200  -35.04500 1.000 51.37734  ?  409  GLY   B C   1 
ATOM   17194 O  O   . GLY   B 1 409  ? 16.48200   85.23600  -35.12900 1.000 54.38787  ?  409  GLY   B O   1 
ATOM   17195 N  N   . ALA   B 1 410  ? 18.36300   85.70100  -33.98000 1.000 43.96493  ?  410  ALA   B N   1 
ATOM   17196 C  CA  . ALA   B 1 410  ? 17.67100   86.20000  -32.80400 1.000 36.68842  ?  410  ALA   B CA  1 
ATOM   17197 C  C   . ALA   B 1 410  ? 17.19500   87.63300  -33.03100 1.000 36.55562  ?  410  ALA   B C   1 
ATOM   17198 O  O   . ALA   B 1 410  ? 17.42700   88.23900  -34.08100 1.000 36.84195  ?  410  ALA   B O   1 
ATOM   17199 C  CB  . ALA   B 1 410  ? 18.57900   86.10800  -31.58000 1.000 37.25256  ?  410  ALA   B CB  1 
ATOM   17200 N  N   . ALA   B 1 411  ? 16.52100   88.18500  -32.02600 1.000 25.29190  ?  411  ALA   B N   1 
ATOM   17201 C  CA  . ALA   B 1 411  ? 15.94900   89.52200  -32.09400 1.000 31.56068  ?  411  ALA   B CA  1 
ATOM   17202 C  C   . ALA   B 1 411  ? 16.64800   90.42700  -31.09100 1.000 38.78130  ?  411  ALA   B C   1 
ATOM   17203 O  O   . ALA   B 1 411  ? 16.82600   90.05100  -29.92800 1.000 54.45859  ?  411  ALA   B O   1 
ATOM   17204 C  CB  . ALA   B 1 411  ? 14.44500   89.48900  -31.81800 1.000 45.35432  ?  411  ALA   B CB  1 
ATOM   17205 N  N   . LEU   B 1 412  ? 17.03900   91.61600  -31.54200 1.000 35.54470  ?  412  LEU   B N   1 
ATOM   17206 C  CA  . LEU   B 1 412  ? 17.70900   92.59600  -30.69800 1.000 35.71347  ?  412  LEU   B CA  1 
ATOM   17207 C  C   . LEU   B 1 412  ? 16.68500   93.58900  -30.16500 1.000 47.01776  ?  412  LEU   B C   1 
ATOM   17208 O  O   . LEU   B 1 412  ? 15.90800   94.16000  -30.93700 1.000 58.11509  ?  412  LEU   B O   1 
ATOM   17209 C  CB  . LEU   B 1 412  ? 18.79700   93.33900  -31.47500 1.000 27.10487  ?  412  LEU   B CB  1 
ATOM   17210 C  CG  . LEU   B 1 412  ? 19.76500   92.51300  -32.32100 1.000 34.17248  ?  412  LEU   B CG  1 
ATOM   17211 C  CD1 . LEU   B 1 412  ? 20.68700   93.43600  -33.09900 1.000 31.01545  ?  412  LEU   B CD1 1 
ATOM   17212 C  CD2 . LEU   B 1 412  ? 20.56700   91.55000  -31.46100 1.000 25.46511  ?  412  LEU   B CD2 1 
ATOM   17213 N  N   . HIS   B 1 413  ? 16.68900   93.79300  -28.85200 1.000 40.46072  ?  413  HIS   B N   1 
ATOM   17214 C  CA  . HIS   B 1 413  ? 15.81800   94.76100  -28.19800 1.000 29.28170  ?  413  HIS   B CA  1 
ATOM   17215 C  C   . HIS   B 1 413  ? 16.66600   95.92300  -27.70200 1.000 35.19336  ?  413  HIS   B C   1 
ATOM   17216 O  O   . HIS   B 1 413  ? 17.57400   95.72900  -26.88700 1.000 37.00698  ?  413  HIS   B O   1 
ATOM   17217 C  CB  . HIS   B 1 413  ? 15.05200   94.12000  -27.04200 1.000 31.76961  ?  413  HIS   B CB  1 
ATOM   17218 C  CG  . HIS   B 1 413  ? 13.95900   93.19800  -27.48000 1.000 40.97719  ?  413  HIS   B CG  1 
ATOM   17219 N  ND1 . HIS   B 1 413  ? 12.62600   93.46200  -27.24600 1.000 45.02903  ?  413  HIS   B ND1 1 
ATOM   17220 C  CD2 . HIS   B 1 413  ? 13.99800   92.01600  -28.13900 1.000 44.34218  ?  413  HIS   B CD2 1 
ATOM   17221 C  CE1 . HIS   B 1 413  ? 11.89200   92.48100  -27.73900 1.000 42.53903  ?  413  HIS   B CE1 1 
ATOM   17222 N  NE2 . HIS   B 1 413  ? 12.70000   91.59100  -28.28800 1.000 42.65734  ?  413  HIS   B NE2 1 
ATOM   17223 N  N   . ILE   B 1 414  ? 16.36700   97.12300  -28.18800 1.000 34.53023  ?  414  ILE   B N   1 
ATOM   17224 C  CA  . ILE   B 1 414  ? 17.13000   98.30900  -27.81500 1.000 38.46011  ?  414  ILE   B CA  1 
ATOM   17225 C  C   . ILE   B 1 414  ? 16.68900   98.77800  -26.43800 1.000 39.73218  ?  414  ILE   B C   1 
ATOM   17226 O  O   . ILE   B 1 414  ? 15.49500   98.98600  -26.19000 1.000 46.82687  ?  414  ILE   B O   1 
ATOM   17227 C  CB  . ILE   B 1 414  ? 16.95800   99.42700  -28.85500 1.000 35.29353  ?  414  ILE   B CB  1 
ATOM   17228 C  CG1 . ILE   B 1 414  ? 17.76100   99.12200  -30.11700 1.000 46.16348  ?  414  ILE   B CG1 1 
ATOM   17229 C  CG2 . ILE   B 1 414  ? 17.38900   100.76500 -28.27900 1.000 42.01658  ?  414  ILE   B CG2 1 
ATOM   17230 C  CD1 . ILE   B 1 414  ? 17.05500   98.21600  -31.05900 1.000 46.88962  ?  414  ILE   B CD1 1 
ATOM   17231 N  N   . VAL   B 1 415  ? 17.65200   98.94800  -25.53800 1.000 46.26536  ?  415  VAL   B N   1 
ATOM   17232 C  CA  . VAL   B 1 415  ? 17.41600   99.56000  -24.23400 1.000 54.16953  ?  415  VAL   B CA  1 
ATOM   17233 C  C   . VAL   B 1 415  ? 17.79400   101.03400 -24.34600 1.000 59.74110  ?  415  VAL   B C   1 
ATOM   17234 O  O   . VAL   B 1 415  ? 18.98000   101.34300 -24.55600 1.000 53.86161  ?  415  VAL   B O   1 
ATOM   17235 C  CB  . VAL   B 1 415  ? 18.22000   98.86800  -23.12900 1.000 48.17568  ?  415  VAL   B CB  1 
ATOM   17236 C  CG1 . VAL   B 1 415  ? 17.70700   99.28400  -21.76000 1.000 62.90337  ?  415  VAL   B CG1 1 
ATOM   17237 C  CG2 . VAL   B 1 415  ? 18.13600   97.38300  -23.29600 1.000 57.05469  ?  415  VAL   B CG2 1 
ATOM   17238 N  N   . PRO   B 1 416  ? 16.84800   101.96200 -24.22700 1.000 67.01706  ?  416  PRO   B N   1 
ATOM   17239 C  CA  . PRO   B 1 416  ? 17.20500   103.38200 -24.26200 1.000 70.87915  ?  416  PRO   B CA  1 
ATOM   17240 C  C   . PRO   B 1 416  ? 18.11900   103.73600 -23.09900 1.000 83.00413  ?  416  PRO   B C   1 
ATOM   17241 O  O   . PRO   B 1 416  ? 18.16200   103.05000 -22.07600 1.000 102.59029 ?  416  PRO   B O   1 
ATOM   17242 C  CB  . PRO   B 1 416  ? 15.85200   104.09600 -24.14700 1.000 73.88491  ?  416  PRO   B CB  1 
ATOM   17243 C  CG  . PRO   B 1 416  ? 14.82900   103.05900 -24.51500 1.000 77.43055  ?  416  PRO   B CG  1 
ATOM   17244 C  CD  . PRO   B 1 416  ? 15.40000   101.75500 -24.05900 1.000 58.42500  ?  416  PRO   B CD  1 
ATOM   17245 N  N   . SER   B 1 417  ? 18.86200   104.83400 -23.26700 1.000 82.26844  ?  417  SER   B N   1 
ATOM   17246 C  CA  . SER   B 1 417  ? 19.75800   105.28800 -22.21000 1.000 90.05741  ?  417  SER   B CA  1 
ATOM   17247 C  C   . SER   B 1 417  ? 19.01500   105.64900 -20.93000 1.000 111.47322 ?  417  SER   B C   1 
ATOM   17248 O  O   . SER   B 1 417  ? 19.66000   105.85300 -19.89600 1.000 110.90197 ?  417  SER   B O   1 
ATOM   17249 C  CB  . SER   B 1 417  ? 20.57700   106.49100 -22.68700 1.000 81.39099  ?  417  SER   B CB  1 
ATOM   17250 O  OG  . SER   B 1 417  ? 19.81100   107.68200 -22.64800 1.000 98.31587  ?  417  SER   B OG  1 
ATOM   17251 N  N   . GLU   B 1 418  ? 17.68500   105.73100 -20.97400 1.000 103.96971 ?  418  GLU   B N   1 
ATOM   17252 C  CA  . GLU   B 1 418  ? 16.87900   105.98800 -19.79100 1.000 96.26547  ?  418  GLU   B CA  1 
ATOM   17253 C  C   . GLU   B 1 418  ? 16.47300   104.71600 -19.06000 1.000 103.19639 ?  418  GLU   B C   1 
ATOM   17254 O  O   . GLU   B 1 418  ? 16.13200   104.78200 -17.87300 1.000 107.62202 ?  418  GLU   B O   1 
ATOM   17255 C  CB  . GLU   B 1 418  ? 15.62300   106.77900 -20.17600 1.000 107.05446 ?  418  GLU   B CB  1 
ATOM   17256 C  CG  . GLU   B 1 418  ? 14.79900   106.14900 -21.29700 1.000 113.25005 ?  418  GLU   B CG  1 
ATOM   17257 C  CD  . GLU   B 1 418  ? 13.76100   105.16300 -20.78900 1.000 115.43397 ?  418  GLU   B CD  1 
ATOM   17258 O  OE1 . GLU   B 1 418  ? 13.26400   105.35000 -19.65900 1.000 106.18049 ?  418  GLU   B OE1 1 
ATOM   17259 O  OE2 . GLU   B 1 418  ? 13.44400   104.20000 -21.52000 1.000 102.13787 -1 418  GLU   B OE2 1 
ATOM   17260 N  N   . ARG   B 1 419  ? 16.50500   103.56700 -19.73400 1.000 84.23199  ?  419  ARG   B N   1 
ATOM   17261 C  CA  . ARG   B 1 419  ? 16.07800   102.31100 -19.13300 1.000 80.95144  ?  419  ARG   B CA  1 
ATOM   17262 C  C   . ARG   B 1 419  ? 17.23300   101.47200 -18.60400 1.000 79.95375  ?  419  ARG   B C   1 
ATOM   17263 O  O   . ARG   B 1 419  ? 17.02100   100.65600 -17.70000 1.000 85.15718  ?  419  ARG   B O   1 
ATOM   17264 C  CB  . ARG   B 1 419  ? 15.27800   101.48900 -20.15200 1.000 81.16083  ?  419  ARG   B CB  1 
ATOM   17265 C  CG  . ARG   B 1 419  ? 14.50100   100.33100 -19.55000 1.000 87.62074  ?  419  ARG   B CG  1 
ATOM   17266 C  CD  . ARG   B 1 419  ? 13.44900   99.81000  -20.51200 1.000 86.07344  ?  419  ARG   B CD  1 
ATOM   17267 N  NE  . ARG   B 1 419  ? 12.33000   99.20400  -19.80100 1.000 88.26239  ?  419  ARG   B NE  1 
ATOM   17268 C  CZ  . ARG   B 1 419  ? 11.27500   99.87500  -19.35900 1.000 89.11935  ?  419  ARG   B CZ  1 
ATOM   17269 N  NH1 . ARG   B 1 419  ? 11.16200   101.18200 -19.53700 1.000 96.80918  ?  419  ARG   B NH1 1 
ATOM   17270 N  NH2 . ARG   B 1 419  ? 10.30900   99.22000  -18.72000 1.000 68.34836  ?  419  ARG   B NH2 1 
ATOM   17271 N  N   . LYS   B 1 420  ? 18.44500   101.66200 -19.12800 1.000 79.35476  ?  420  LYS   B N   1 
ATOM   17272 C  CA  . LYS   B 1 420  ? 19.57900   100.84000 -18.72400 1.000 75.49045  ?  420  LYS   B CA  1 
ATOM   17273 C  C   . LYS   B 1 420  ? 20.07100   101.14900 -17.31600 1.000 74.42866  ?  420  LYS   B C   1 
ATOM   17274 O  O   . LYS   B 1 420  ? 20.87000   100.37500 -16.77700 1.000 86.26409  ?  420  LYS   B O   1 
ATOM   17275 C  CB  . LYS   B 1 420  ? 20.72500   101.00700 -19.72400 1.000 68.56142  ?  420  LYS   B CB  1 
ATOM   17276 C  CG  . LYS   B 1 420  ? 21.11800   102.44700 -19.99300 1.000 72.86240  ?  420  LYS   B CG  1 
ATOM   17277 C  CD  . LYS   B 1 420  ? 22.34100   102.52500 -20.89300 1.000 77.40183  ?  420  LYS   B CD  1 
ATOM   17278 C  CE  . LYS   B 1 420  ? 23.49500   101.71600 -20.32200 1.000 62.11005  ?  420  LYS   B CE  1 
ATOM   17279 N  NZ  . LYS   B 1 420  ? 24.79700   102.09500 -20.93800 1.000 62.12790  ?  420  LYS   B NZ  1 
ATOM   17280 N  N   . TYR   B 1 421  ? 19.61900   102.24400 -16.70500 1.000 62.07634  ?  421  TYR   B N   1 
ATOM   17281 C  CA  . TYR   B 1 421  ? 20.06700   102.60000 -15.36500 1.000 71.08650  ?  421  TYR   B CA  1 
ATOM   17282 C  C   . TYR   B 1 421  ? 19.10900   102.14400 -14.27300 1.000 66.11599  ?  421  TYR   B C   1 
ATOM   17283 O  O   . TYR   B 1 421  ? 19.52100   102.04800 -13.11200 1.000 68.20649  ?  421  TYR   B O   1 
ATOM   17284 C  CB  . TYR   B 1 421  ? 20.27500   104.11600 -15.25300 1.000 84.98350  ?  421  TYR   B CB  1 
ATOM   17285 C  CG  . TYR   B 1 421  ? 21.27700   104.68600 -16.23800 1.000 102.95589 ?  421  TYR   B CG  1 
ATOM   17286 C  CD1 . TYR   B 1 421  ? 22.17600   103.86300 -16.90900 1.000 102.24191 ?  421  TYR   B CD1 1 
ATOM   17287 C  CD2 . TYR   B 1 421  ? 21.32300   106.05000 -16.49400 1.000 113.89727 ?  421  TYR   B CD2 1 
ATOM   17288 C  CE1 . TYR   B 1 421  ? 23.08700   104.38200 -17.80900 1.000 90.08591  ?  421  TYR   B CE1 1 
ATOM   17289 C  CE2 . TYR   B 1 421  ? 22.23200   106.57900 -17.39100 1.000 117.06233 ?  421  TYR   B CE2 1 
ATOM   17290 C  CZ  . TYR   B 1 421  ? 23.11100   105.74000 -18.04600 1.000 106.89848 ?  421  TYR   B CZ  1 
ATOM   17291 O  OH  . TYR   B 1 421  ? 24.01900   106.25900 -18.94000 1.000 101.64819 ?  421  TYR   B OH  1 
ATOM   17292 N  N   . ASP   B 1 422  ? 17.85400   101.86400 -14.61200 1.000 53.66080  ?  422  ASP   B N   1 
ATOM   17293 C  CA  . ASP   B 1 422  ? 16.87800   101.33600 -13.66200 1.000 62.28115  ?  422  ASP   B CA  1 
ATOM   17294 C  C   . ASP   B 1 422  ? 16.73700   99.84400  -13.93900 1.000 64.25652  ?  422  ASP   B C   1 
ATOM   17295 O  O   . ASP   B 1 422  ? 16.05700   99.43700  -14.88500 1.000 57.24450  ?  422  ASP   B O   1 
ATOM   17296 C  CB  . ASP   B 1 422  ? 15.54500   102.06700 -13.78200 1.000 60.90939  ?  422  ASP   B CB  1 
ATOM   17297 C  CG  . ASP   B 1 422  ? 14.55100   101.65400 -12.71100 1.000 62.30141  ?  422  ASP   B CG  1 
ATOM   17298 O  OD1 . ASP   B 1 422  ? 14.04600   100.51300 -12.76500 1.000 50.14852  ?  422  ASP   B OD1 1 
ATOM   17299 O  OD2 . ASP   B 1 422  ? 14.28700   102.47000 -11.80200 1.000 76.35040  -1 422  ASP   B OD2 1 
ATOM   17300 N  N   . LEU   B 1 423  ? 17.38900   99.02500  -13.11000 1.000 46.30473  ?  423  LEU   B N   1 
ATOM   17301 C  CA  . LEU   B 1 423  ? 17.38100   97.58600  -13.34300 1.000 59.99205  ?  423  LEU   B CA  1 
ATOM   17302 C  C   . LEU   B 1 423  ? 16.04300   96.94900  -12.99900 1.000 60.79015  ?  423  LEU   B C   1 
ATOM   17303 O  O   . LEU   B 1 423  ? 15.73500   95.87200  -13.52200 1.000 61.67751  ?  423  LEU   B O   1 
ATOM   17304 C  CB  . LEU   B 1 423  ? 18.50000   96.90800  -12.54800 1.000 60.93868  ?  423  LEU   B CB  1 
ATOM   17305 C  CG  . LEU   B 1 423  ? 19.94900   97.12200  -13.00400 1.000 63.70273  ?  423  LEU   B CG  1 
ATOM   17306 C  CD1 . LEU   B 1 423  ? 20.02800   97.55000  -14.46900 1.000 52.15515  ?  423  LEU   B CD1 1 
ATOM   17307 C  CD2 . LEU   B 1 423  ? 20.67300   98.11400  -12.10500 1.000 58.91077  ?  423  LEU   B CD2 1 
ATOM   17308 N  N   . ASP   B 1 424  ? 15.24400   97.58000  -12.13600 1.000 62.19382  ?  424  ASP   B N   1 
ATOM   17309 C  CA  . ASP   B 1 424  ? 13.91600   97.04400  -11.85500 1.000 70.24554  ?  424  ASP   B CA  1 
ATOM   17310 C  C   . ASP   B 1 424  ? 13.02500   97.13400  -13.08700 1.000 61.09557  ?  424  ASP   B C   1 
ATOM   17311 O  O   . ASP   B 1 424  ? 12.31200   96.17900  -13.41800 1.000 58.77297  ?  424  ASP   B O   1 
ATOM   17312 C  CB  . ASP   B 1 424  ? 13.28500   97.78100  -10.67500 1.000 68.92193  ?  424  ASP   B CB  1 
ATOM   17313 C  CG  . ASP   B 1 424  ? 12.24100   96.94400  -9.95600  1.000 76.98316  ?  424  ASP   B CG  1 
ATOM   17314 O  OD1 . ASP   B 1 424  ? 12.33100   95.69900  -10.01800 1.000 71.93721  ?  424  ASP   B OD1 1 
ATOM   17315 O  OD2 . ASP   B 1 424  ? 11.32800   97.53000  -9.33700  1.000 86.84710  -1 424  ASP   B OD2 1 
ATOM   17316 N  N   . ALA   B 1 425  ? 13.05800   98.27400  -13.78300 1.000 52.21992  ?  425  ALA   B N   1 
ATOM   17317 C  CA  . ALA   B 1 425  ? 12.32700   98.39300  -15.03900 1.000 51.60188  ?  425  ALA   B CA  1 
ATOM   17318 C  C   . ALA   B 1 425  ? 12.95400   97.53700  -16.13000 1.000 63.24464  ?  425  ALA   B C   1 
ATOM   17319 O  O   . ALA   B 1 425  ? 12.24600   97.05900  -17.02500 1.000 66.81420  ?  425  ALA   B O   1 
ATOM   17320 C  CB  . ALA   B 1 425  ? 12.26800   99.85600  -15.47800 1.000 48.98589  ?  425  ALA   B CB  1 
ATOM   17321 N  N   . LEU   B 1 426  ? 14.27100   97.33200  -16.07300 1.000 57.25858  ?  426  LEU   B N   1 
ATOM   17322 C  CA  . LEU   B 1 426  ? 14.92800   96.47900  -17.05600 1.000 51.69976  ?  426  LEU   B CA  1 
ATOM   17323 C  C   . LEU   B 1 426  ? 14.48700   95.02900  -16.90700 1.000 45.90669  ?  426  LEU   B C   1 
ATOM   17324 O  O   . LEU   B 1 426  ? 14.28000   94.33100  -17.90600 1.000 47.84371  ?  426  LEU   B O   1 
ATOM   17325 C  CB  . LEU   B 1 426  ? 16.44500   96.59800  -16.92300 1.000 57.11709  ?  426  LEU   B CB  1 
ATOM   17326 C  CG  . LEU   B 1 426  ? 17.25400   95.98300  -18.06400 1.000 50.38081  ?  426  LEU   B CG  1 
ATOM   17327 C  CD1 . LEU   B 1 426  ? 16.81500   96.58000  -19.39100 1.000 47.61602  ?  426  LEU   B CD1 1 
ATOM   17328 C  CD2 . LEU   B 1 426  ? 18.74100   96.20000  -17.83700 1.000 35.79729  ?  426  LEU   B CD2 1 
ATOM   17329 N  N   . ASN   B 1 427  ? 14.33500   94.55900  -15.66600 1.000 50.08771  ?  427  ASN   B N   1 
ATOM   17330 C  CA  . ASN   B 1 427  ? 13.85200   93.20000  -15.44900 1.000 50.53290  ?  427  ASN   B CA  1 
ATOM   17331 C  C   . ASN   B 1 427  ? 12.38000   93.06700  -15.81100 1.000 49.64513  ?  427  ASN   B C   1 
ATOM   17332 O  O   . ASN   B 1 427  ? 11.94500   91.99600  -16.25100 1.000 44.89628  ?  427  ASN   B O   1 
ATOM   17333 C  CB  . ASN   B 1 427  ? 14.08100   92.78600  -13.99700 1.000 39.34364  ?  427  ASN   B CB  1 
ATOM   17334 C  CG  . ASN   B 1 427  ? 13.97300   91.29000  -13.79800 1.000 49.51586  ?  427  ASN   B CG  1 
ATOM   17335 O  OD1 . ASN   B 1 427  ? 13.97600   90.52000  -14.75800 1.000 48.94780  ?  427  ASN   B OD1 1 
ATOM   17336 N  ND2 . ASN   B 1 427  ? 13.88700   90.86900  -12.54500 1.000 59.54460  ?  427  ASN   B ND2 1 
ATOM   17337 N  N   . ASP   B 1 428  ? 11.59900   94.13300  -15.62300 1.000 66.17456  ?  428  ASP   B N   1 
ATOM   17338 C  CA  . ASP   B 1 428  ? 10.22100   94.13200  -16.10200 1.000 54.41688  ?  428  ASP   B CA  1 
ATOM   17339 C  C   . ASP   B 1 428  ? 10.17900   93.97000  -17.61600 1.000 57.29853  ?  428  ASP   B C   1 
ATOM   17340 O  O   . ASP   B 1 428  ? 9.41300    93.15800  -18.14400 1.000 60.31784  ?  428  ASP   B O   1 
ATOM   17341 C  CB  . ASP   B 1 428  ? 9.51100    95.41900  -15.67600 1.000 53.16886  ?  428  ASP   B CB  1 
ATOM   17342 C  CG  . ASP   B 1 428  ? 9.27400    95.48700  -14.17900 1.000 56.99194  ?  428  ASP   B CG  1 
ATOM   17343 O  OD1 . ASP   B 1 428  ? 9.24200    94.42000  -13.53000 1.000 55.19722  ?  428  ASP   B OD1 1 
ATOM   17344 O  OD2 . ASP   B 1 428  ? 9.11100    96.60900  -13.65300 1.000 47.73747  -1 428  ASP   B OD2 1 
ATOM   17345 N  N   . TYR   B 1 429  ? 11.01300   94.73100  -18.33100 1.000 50.32414  ?  429  TYR   B N   1 
ATOM   17346 C  CA  . TYR   B 1 429  ? 11.07500   94.60300  -19.78300 1.000 42.85609  ?  429  TYR   B CA  1 
ATOM   17347 C  C   . TYR   B 1 429  ? 11.50500   93.19900  -20.19000 1.000 43.92315  ?  429  TYR   B C   1 
ATOM   17348 O  O   . TYR   B 1 429  ? 10.90500   92.58700  -21.08000 1.000 57.84224  ?  429  TYR   B O   1 
ATOM   17349 C  CB  . TYR   B 1 429  ? 12.03000   95.64800  -20.36400 1.000 31.08590  ?  429  TYR   B CB  1 
ATOM   17350 C  CG  . TYR   B 1 429  ? 12.00100   95.73400  -21.87500 1.000 35.36503  ?  429  TYR   B CG  1 
ATOM   17351 C  CD1 . TYR   B 1 429  ? 12.72900   94.84600  -22.65800 1.000 34.21944  ?  429  TYR   B CD1 1 
ATOM   17352 C  CD2 . TYR   B 1 429  ? 11.24700   96.70600  -22.52000 1.000 54.18887  ?  429  TYR   B CD2 1 
ATOM   17353 C  CE1 . TYR   B 1 429  ? 12.70300   94.92000  -24.03800 1.000 47.72460  ?  429  TYR   B CE1 1 
ATOM   17354 C  CE2 . TYR   B 1 429  ? 11.21600   96.78900  -23.90000 1.000 38.88377  ?  429  TYR   B CE2 1 
ATOM   17355 C  CZ  . TYR   B 1 429  ? 11.94500   95.89400  -24.65400 1.000 44.59325  ?  429  TYR   B CZ  1 
ATOM   17356 O  OH  . TYR   B 1 429  ? 11.91800   95.97000  -26.02800 1.000 36.90898  ?  429  TYR   B OH  1 
ATOM   17357 N  N   . CYS   B 1 430  ? 12.54900   92.67200  -19.54500 1.000 42.40953  ?  430  CYS   B N   1 
ATOM   17358 C  CA  . CYS   B 1 430  ? 13.04100   91.34500  -19.89900 1.000 38.48782  ?  430  CYS   B CA  1 
ATOM   17359 C  C   . CYS   B 1 430  ? 11.98300   90.27900  -19.64400 1.000 36.13774  ?  430  CYS   B C   1 
ATOM   17360 O  O   . CYS   B 1 430  ? 11.81800   89.35400  -20.44700 1.000 43.17372  ?  430  CYS   B O   1 
ATOM   17361 C  CB  . CYS   B 1 430  ? 14.32200   91.03400  -19.12500 1.000 40.52124  ?  430  CYS   B CB  1 
ATOM   17362 S  SG  . CYS   B 1 430  ? 15.73200   92.08600  -19.55900 1.000 43.38509  ?  430  CYS   B SG  1 
ATOM   17363 N  N   . ASN   B 1 431  ? 11.24500   90.39800  -18.53900 1.000 48.91187  ?  431  ASN   B N   1 
ATOM   17364 C  CA  . ASN   B 1 431  ? 10.19600   89.42500  -18.25000 1.000 52.12669  ?  431  ASN   B CA  1 
ATOM   17365 C  C   . ASN   B 1 431  ? 8.99400    89.61500  -19.16800 1.000 45.00476  ?  431  ASN   B C   1 
ATOM   17366 O  O   . ASN   B 1 431  ? 8.41600    88.63500  -19.65200 1.000 33.14214  ?  431  ASN   B O   1 
ATOM   17367 C  CB  . ASN   B 1 431  ? 9.77700    89.52500  -16.78400 1.000 35.12358  ?  431  ASN   B CB  1 
ATOM   17368 C  CG  . ASN   B 1 431  ? 10.84000   89.00000  -15.83800 1.000 44.90864  ?  431  ASN   B CG  1 
ATOM   17369 O  OD1 . ASN   B 1 431  ? 11.55900   88.05300  -16.15800 1.000 43.28827  ?  431  ASN   B OD1 1 
ATOM   17370 N  ND2 . ASN   B 1 431  ? 10.94300   89.61400  -14.66500 1.000 36.03818  ?  431  ASN   B ND2 1 
ATOM   17371 N  N   . GLN   B 1 432  ? 8.60500    90.86700  -19.42200 1.000 42.09782  ?  432  GLN   B N   1 
ATOM   17372 C  CA  . GLN   B 1 432  ? 7.45200    91.12500  -20.27800 1.000 36.52090  ?  432  GLN   B CA  1 
ATOM   17373 C  C   . GLN   B 1 432  ? 7.71500    90.72100  -21.72300 1.000 46.30114  ?  432  GLN   B C   1 
ATOM   17374 O  O   . GLN   B 1 432  ? 6.78500    90.31600  -22.42800 1.000 68.88360  ?  432  GLN   B O   1 
ATOM   17375 C  CB  . GLN   B 1 432  ? 7.06100    92.60200  -20.20800 1.000 50.47291  ?  432  GLN   B CB  1 
ATOM   17376 C  CG  . GLN   B 1 432  ? 6.41100    93.02100  -18.89700 1.000 56.30682  ?  432  GLN   B CG  1 
ATOM   17377 C  CD  . GLN   B 1 432  ? 6.41300    94.52700  -18.70400 1.000 65.35676  ?  432  GLN   B CD  1 
ATOM   17378 O  OE1 . GLN   B 1 432  ? 6.88000    95.27500  -19.56400 1.000 61.08593  ?  432  GLN   B OE1 1 
ATOM   17379 N  NE2 . GLN   B 1 432  ? 5.89300    94.97900  -17.56900 1.000 69.51430  ?  432  GLN   B NE2 1 
ATOM   17380 N  N   . GLU   B 1 433  ? 8.96400    90.81900  -22.18000 1.000 44.33389  ?  433  GLU   B N   1 
ATOM   17381 C  CA  . GLU   B 1 433  ? 9.30400    90.53100  -23.56700 1.000 44.44298  ?  433  GLU   B CA  1 
ATOM   17382 C  C   . GLU   B 1 433  ? 9.97900    89.17800  -23.75700 1.000 39.68769  ?  433  GLU   B C   1 
ATOM   17383 O  O   . GLU   B 1 433  ? 10.07400   88.71000  -24.89600 1.000 42.14600  ?  433  GLU   B O   1 
ATOM   17384 C  CB  . GLU   B 1 433  ? 10.20900   91.63300  -24.13100 1.000 37.08265  ?  433  GLU   B CB  1 
ATOM   17385 C  CG  . GLU   B 1 433  ? 9.62300    93.03400  -24.02900 1.000 56.74460  ?  433  GLU   B CG  1 
ATOM   17386 C  CD  . GLU   B 1 433  ? 8.40600    93.22700  -24.91300 1.000 69.06224  ?  433  GLU   B CD  1 
ATOM   17387 O  OE1 . GLU   B 1 433  ? 8.29400    92.51700  -25.93400 1.000 68.97193  ?  433  GLU   B OE1 1 
ATOM   17388 O  OE2 . GLU   B 1 433  ? 7.56300    94.08900  -24.58500 1.000 66.21769  -1 433  GLU   B OE2 1 
ATOM   17389 N  N   . GLY   B 1 434  ? 10.45000   88.54600  -22.68600 1.000 35.18028  ?  434  GLY   B N   1 
ATOM   17390 C  CA  . GLY   B 1 434  ? 11.05900   87.23400  -22.79400 1.000 41.25855  ?  434  GLY   B CA  1 
ATOM   17391 C  C   . GLY   B 1 434  ? 12.48200   87.26700  -23.31000 1.000 41.22014  ?  434  GLY   B C   1 
ATOM   17392 O  O   . GLY   B 1 434  ? 12.84300   86.49400  -24.20500 1.000 44.17482  ?  434  GLY   B O   1 
ATOM   17393 N  N   . ILE   B 1 435  ? 13.30100   88.16200  -22.75800 1.000 38.57389  ?  435  ILE   B N   1 
ATOM   17394 C  CA  . ILE   B 1 435  ? 14.70300   88.24000  -23.14300 1.000 28.25651  ?  435  ILE   B CA  1 
ATOM   17395 C  C   . ILE   B 1 435  ? 15.45400   87.06600  -22.53400 1.000 33.48882  ?  435  ILE   B C   1 
ATOM   17396 O  O   . ILE   B 1 435  ? 15.38700   86.82500  -21.32200 1.000 33.88280  ?  435  ILE   B O   1 
ATOM   17397 C  CB  . ILE   B 1 435  ? 15.30500   89.58200  -22.70000 1.000 37.14020  ?  435  ILE   B CB  1 
ATOM   17398 C  CG1 . ILE   B 1 435  ? 14.47600   90.74500  -23.25700 1.000 32.35957  ?  435  ILE   B CG1 1 
ATOM   17399 C  CG2 . ILE   B 1 435  ? 16.75900   89.68000  -23.12900 1.000 38.97706  ?  435  ILE   B CG2 1 
ATOM   17400 C  CD1 . ILE   B 1 435  ? 14.22700   90.66700  -24.75000 1.000 29.69199  ?  435  ILE   B CD1 1 
ATOM   17401 N  N   . THR   B 1 436  ? 16.18200   86.32900  -23.37200 1.000 24.39053  ?  436  THR   B N   1 
ATOM   17402 C  CA  . THR   B 1 436  ? 16.81300   85.08200  -22.95400 1.000 34.85301  ?  436  THR   B CA  1 
ATOM   17403 C  C   . THR   B 1 436  ? 18.31500   85.19700  -22.72600 1.000 36.52995  ?  436  THR   B C   1 
ATOM   17404 O  O   . THR   B 1 436  ? 18.84000   84.56700  -21.80400 1.000 34.22825  ?  436  THR   B O   1 
ATOM   17405 C  CB  . THR   B 1 436  ? 16.54600   83.98500  -23.98800 1.000 30.25269  ?  436  THR   B CB  1 
ATOM   17406 O  OG1 . THR   B 1 436  ? 16.89100   84.46100  -25.29500 1.000 32.20024  ?  436  THR   B OG1 1 
ATOM   17407 C  CG2 . THR   B 1 436  ? 15.08000   83.58100  -23.96600 1.000 35.53034  ?  436  THR   B CG2 1 
ATOM   17408 N  N   . ILE   B 1 437  ? 19.02500   85.97500  -23.54000 1.000 43.98298  ?  437  ILE   B N   1 
ATOM   17409 C  CA  . ILE   B 1 437  ? 20.48100   86.04300  -23.47500 1.000 35.06448  ?  437  ILE   B CA  1 
ATOM   17410 C  C   . ILE   B 1 437  ? 20.91800   87.48700  -23.67800 1.000 35.28496  ?  437  ILE   B C   1 
ATOM   17411 O  O   . ILE   B 1 437  ? 20.34100   88.21100  -24.49600 1.000 40.42659  ?  437  ILE   B O   1 
ATOM   17412 C  CB  . ILE   B 1 437  ? 21.13100   85.10500  -24.51700 1.000 31.93555  ?  437  ILE   B CB  1 
ATOM   17413 C  CG1 . ILE   B 1 437  ? 22.65500   85.11200  -24.38500 1.000 30.47935  ?  437  ILE   B CG1 1 
ATOM   17414 C  CG2 . ILE   B 1 437  ? 20.69500   85.47800  -25.93100 1.000 29.38848  ?  437  ILE   B CG2 1 
ATOM   17415 C  CD1 . ILE   B 1 437  ? 23.33000   83.97600  -25.12500 1.000 32.06080  ?  437  ILE   B CD1 1 
ATOM   17416 N  N   . SER   B 1 438  ? 21.92800   87.91000  -22.92100 1.000 33.71894  ?  438  SER   B N   1 
ATOM   17417 C  CA  . SER   B 1 438  ? 22.45100   89.26900  -23.01700 1.000 47.45442  ?  438  SER   B CA  1 
ATOM   17418 C  C   . SER   B 1 438  ? 23.78600   89.33500  -22.28800 1.000 47.11110  ?  438  SER   B C   1 
ATOM   17419 O  O   . SER   B 1 438  ? 24.15700   88.42400  -21.54200 1.000 39.37844  ?  438  SER   B O   1 
ATOM   17420 C  CB  . SER   B 1 438  ? 21.47300   90.29500  -22.43800 1.000 26.35819  ?  438  SER   B CB  1 
ATOM   17421 O  OG  . SER   B 1 438  ? 20.25700   90.30100  -23.16200 1.000 49.52497  ?  438  SER   B OG  1 
ATOM   17422 N  N   . TYR   B 1 439  ? 24.50500   90.42900  -22.51800 1.000 35.88041  ?  439  TYR   B N   1 
ATOM   17423 C  CA  . TYR   B 1 439  ? 25.71200   90.75400  -21.77300 1.000 32.82858  ?  439  TYR   B CA  1 
ATOM   17424 C  C   . TYR   B 1 439  ? 25.46300   92.00100  -20.93800 1.000 37.47096  ?  439  TYR   B C   1 
ATOM   17425 O  O   . TYR   B 1 439  ? 25.05300   93.03900  -21.47000 1.000 40.25528  ?  439  TYR   B O   1 
ATOM   17426 C  CB  . TYR   B 1 439  ? 26.91000   90.97900  -22.69900 1.000 42.35838  ?  439  TYR   B CB  1 
ATOM   17427 C  CG  . TYR   B 1 439  ? 28.00800   91.80000  -22.05500 1.000 39.87610  ?  439  TYR   B CG  1 
ATOM   17428 C  CD1 . TYR   B 1 439  ? 28.77500   91.27900  -21.02000 1.000 38.48891  ?  439  TYR   B CD1 1 
ATOM   17429 C  CD2 . TYR   B 1 439  ? 28.27000   93.09900  -22.47200 1.000 34.36995  ?  439  TYR   B CD2 1 
ATOM   17430 C  CE1 . TYR   B 1 439  ? 29.77300   92.02600  -20.42100 1.000 33.85073  ?  439  TYR   B CE1 1 
ATOM   17431 C  CE2 . TYR   B 1 439  ? 29.26600   93.85400  -21.88000 1.000 35.46426  ?  439  TYR   B CE2 1 
ATOM   17432 C  CZ  . TYR   B 1 439  ? 30.01400   93.31200  -20.85400 1.000 34.27327  ?  439  TYR   B CZ  1 
ATOM   17433 O  OH  . TYR   B 1 439  ? 31.00700   94.05700  -20.26000 1.000 31.59061  ?  439  TYR   B OH  1 
ATOM   17434 N  N   . LEU   B 1 440  ? 25.70600   91.89400  -19.63700 1.000 44.95554  ?  440  LEU   B N   1 
ATOM   17435 C  CA  . LEU   B 1 440  ? 25.61100   93.01600  -18.72700 1.000 46.24636  ?  440  LEU   B CA  1 
ATOM   17436 C  C   . LEU   B 1 440  ? 26.98000   93.28700  -18.11900 1.000 46.12683  ?  440  LEU   B C   1 
ATOM   17437 O  O   . LEU   B 1 440  ? 27.66400   92.33900  -17.70800 1.000 46.45188  ?  440  LEU   B O   1 
ATOM   17438 C  CB  . LEU   B 1 440  ? 24.59100   92.73700  -17.61100 1.000 38.74102  ?  440  LEU   B CB  1 
ATOM   17439 C  CG  . LEU   B 1 440  ? 23.11600   92.71400  -18.01300 1.000 31.07245  ?  440  LEU   B CG  1 
ATOM   17440 C  CD1 . LEU   B 1 440  ? 22.28200   92.04000  -16.93900 1.000 22.38946  ?  440  LEU   B CD1 1 
ATOM   17441 C  CD2 . LEU   B 1 440  ? 22.62000   94.12700  -18.26500 1.000 45.75888  ?  440  LEU   B CD2 1 
ATOM   17442 N  N   . PRO   B 1 441  ? 27.42400   94.54200  -18.06200 1.000 49.40227  ?  441  PRO   B N   1 
ATOM   17443 C  CA  . PRO   B 1 441  ? 28.66900   94.84900  -17.35200 1.000 35.88976  ?  441  PRO   B CA  1 
ATOM   17444 C  C   . PRO   B 1 441  ? 28.60800   94.38200  -15.90400 1.000 36.55115  ?  441  PRO   B C   1 
ATOM   17445 O  O   . PRO   B 1 441  ? 27.53400   94.19000  -15.32800 1.000 61.54117  ?  441  PRO   B O   1 
ATOM   17446 C  CB  . PRO   B 1 441  ? 28.76500   96.37600  -17.44700 1.000 49.86467  ?  441  PRO   B CB  1 
ATOM   17447 C  CG  . PRO   B 1 441  ? 28.00600   96.71200  -18.69100 1.000 54.27230  ?  441  PRO   B CG  1 
ATOM   17448 C  CD  . PRO   B 1 441  ? 26.87400   95.72100  -18.75200 1.000 54.92917  ?  441  PRO   B CD  1 
ATOM   17449 N  N   . THR   B 1 442  ? 29.79300   94.20200  -15.31600 1.000 38.84232  ?  442  THR   B N   1 
ATOM   17450 C  CA  . THR   B 1 442  ? 29.89000   93.55000  -14.01200 1.000 44.93979  ?  442  THR   B CA  1 
ATOM   17451 C  C   . THR   B 1 442  ? 29.10000   94.29800  -12.94300 1.000 40.56369  ?  442  THR   B C   1 
ATOM   17452 O  O   . THR   B 1 442  ? 28.49200   93.67600  -12.06400 1.000 50.85315  ?  442  THR   B O   1 
ATOM   17453 C  CB  . THR   B 1 442  ? 31.35600   93.41800  -13.60300 1.000 38.89035  ?  442  THR   B CB  1 
ATOM   17454 O  OG1 . THR   B 1 442  ? 32.10500   92.86300  -14.69200 1.000 42.11047  ?  442  THR   B OG1 1 
ATOM   17455 C  CG2 . THR   B 1 442  ? 31.48800   92.50600  -12.39300 1.000 42.02226  ?  442  THR   B CG2 1 
ATOM   17456 N  N   . GLY   B 1 443  ? 29.09100   95.62900  -13.00400 1.000 32.52548  ?  443  GLY   B N   1 
ATOM   17457 C  CA  . GLY   B 1 443  ? 28.35200   96.39300  -12.01100 1.000 40.78701  ?  443  GLY   B CA  1 
ATOM   17458 C  C   . GLY   B 1 443  ? 26.85200   96.20400  -12.13400 1.000 59.42281  ?  443  GLY   B C   1 
ATOM   17459 O  O   . GLY   B 1 443  ? 26.16600   95.91700  -11.14800 1.000 60.63531  ?  443  GLY   B O   1 
ATOM   17460 N  N   . ALA   B 1 444  ? 26.32200   96.36200  -13.34900 1.000 54.39197  ?  444  ALA   B N   1 
ATOM   17461 C  CA  . ALA   B 1 444  ? 24.88800   96.19600  -13.55700 1.000 36.51085  ?  444  ALA   B CA  1 
ATOM   17462 C  C   . ALA   B 1 444  ? 24.45300   94.75100  -13.35700 1.000 47.61807  ?  444  ALA   B C   1 
ATOM   17463 O  O   . ALA   B 1 444  ? 23.32600   94.50200  -12.91200 1.000 43.97554  ?  444  ALA   B O   1 
ATOM   17464 C  CB  . ALA   B 1 444  ? 24.50200   96.67800  -14.95400 1.000 38.11711  ?  444  ALA   B CB  1 
ATOM   17465 N  N   . ALA   B 1 445  ? 25.32400   93.79100  -13.67600 1.000 40.48978  ?  445  ALA   B N   1 
ATOM   17466 C  CA  . ALA   B 1 445  ? 24.98100   92.38500  -13.48700 1.000 40.26478  ?  445  ALA   B CA  1 
ATOM   17467 C  C   . ALA   B 1 445  ? 24.77500   92.06500  -12.01200 1.000 51.25506  ?  445  ALA   B C   1 
ATOM   17468 O  O   . ALA   B 1 445  ? 23.73200   91.52800  -11.62200 1.000 53.56664  ?  445  ALA   B O   1 
ATOM   17469 C  CB  . ALA   B 1 445  ? 26.06700   91.49400  -14.08900 1.000 34.17530  ?  445  ALA   B CB  1 
ATOM   17470 N  N   . GLU   B 1 446  ? 25.76100   92.40300  -11.17300 1.000 53.99336  ?  446  GLU   B N   1 
ATOM   17471 C  CA  . GLU   B 1 446  ? 25.65200   92.12400  -9.74400  1.000 47.37467  ?  446  GLU   B CA  1 
ATOM   17472 C  C   . GLU   B 1 446  ? 24.42200   92.78000  -9.12900  1.000 44.70588  ?  446  GLU   B C   1 
ATOM   17473 O  O   . GLU   B 1 446  ? 23.83600   92.23500  -8.18700  1.000 55.00693  ?  446  GLU   B O   1 
ATOM   17474 C  CB  . GLU   B 1 446  ? 26.91800   92.58400  -9.01800  1.000 61.48501  ?  446  GLU   B CB  1 
ATOM   17475 C  CG  . GLU   B 1 446  ? 28.15900   91.75800  -9.33000  1.000 58.78832  ?  446  GLU   B CG  1 
ATOM   17476 C  CD  . GLU   B 1 446  ? 29.32900   92.09300  -8.41900  1.000 60.48348  ?  446  GLU   B CD  1 
ATOM   17477 O  OE1 . GLU   B 1 446  ? 29.36000   93.21600  -7.87500  1.000 63.40636  ?  446  GLU   B OE1 1 
ATOM   17478 O  OE2 . GLU   B 1 446  ? 30.21400   91.22900  -8.24100  1.000 48.68786  -1 446  GLU   B OE2 1 
ATOM   17479 N  N   . GLN   B 1 447  ? 24.01500   93.94000  -9.64200  1.000 36.70508  ?  447  GLN   B N   1 
ATOM   17480 C  CA  . GLN   B 1 447  ? 22.79400   94.59000  -9.18300  1.000 45.23808  ?  447  GLN   B CA  1 
ATOM   17481 C  C   . GLN   B 1 447  ? 21.54700   94.07400  -9.88700  1.000 50.90179  ?  447  GLN   B C   1 
ATOM   17482 O  O   . GLN   B 1 447  ? 20.43600   94.43800  -9.48900  1.000 62.38751  ?  447  GLN   B O   1 
ATOM   17483 C  CB  . GLN   B 1 447  ? 22.89400   96.10700  -9.36800  1.000 50.71319  ?  447  GLN   B CB  1 
ATOM   17484 C  CG  . GLN   B 1 447  ? 23.92400   96.77100  -8.47100  1.000 58.32555  ?  447  GLN   B CG  1 
ATOM   17485 C  CD  . GLN   B 1 447  ? 23.78400   98.28000  -8.44300  1.000 71.69325  ?  447  GLN   B CD  1 
ATOM   17486 O  OE1 . GLN   B 1 447  ? 22.89400   98.84500  -9.07900  1.000 66.46683  ?  447  GLN   B OE1 1 
ATOM   17487 N  NE2 . GLN   B 1 447  ? 24.66400   98.94200  -7.70000  1.000 78.55137  ?  447  GLN   B NE2 1 
ATOM   17488 N  N   . PHE   B 1 448  ? 21.70100   93.25100  -10.92200 1.000 49.40641  ?  448  PHE   B N   1 
ATOM   17489 C  CA  . PHE   B 1 448  ? 20.56800   92.59800  -11.56200 1.000 37.10860  ?  448  PHE   B CA  1 
ATOM   17490 C  C   . PHE   B 1 448  ? 20.27700   91.22900  -10.96600 1.000 34.88851  ?  448  PHE   B C   1 
ATOM   17491 O  O   . PHE   B 1 448  ? 19.15600   90.72700  -11.11300 1.000 39.23260  ?  448  PHE   B O   1 
ATOM   17492 C  CB  . PHE   B 1 448  ? 20.82100   92.46600  -13.06900 1.000 41.83259  ?  448  PHE   B CB  1 
ATOM   17493 C  CG  . PHE   B 1 448  ? 19.64800   91.93400  -13.84400 1.000 47.02884  ?  448  PHE   B CG  1 
ATOM   17494 C  CD1 . PHE   B 1 448  ? 18.60100   92.76900  -14.20500 1.000 44.38667  ?  448  PHE   B CD1 1 
ATOM   17495 C  CD2 . PHE   B 1 448  ? 19.59700   90.60200  -14.22500 1.000 40.76739  ?  448  PHE   B CD2 1 
ATOM   17496 C  CE1 . PHE   B 1 448  ? 17.52300   92.28400  -14.92100 1.000 32.69306  ?  448  PHE   B CE1 1 
ATOM   17497 C  CE2 . PHE   B 1 448  ? 18.52100   90.11000  -14.94200 1.000 47.67281  ?  448  PHE   B CE2 1 
ATOM   17498 C  CZ  . PHE   B 1 448  ? 17.48300   90.95300  -15.29000 1.000 47.89272  ?  448  PHE   B CZ  1 
ATOM   17499 N  N   . MET   B 1 449  ? 21.25600   90.62200  -10.29200 1.000 43.63231  ?  449  MET   B N   1 
ATOM   17500 C  CA  . MET   B 1 449  ? 21.05500   89.32000  -9.66800  1.000 51.77199  ?  449  MET   B CA  1 
ATOM   17501 C  C   . MET   B 1 449  ? 20.07300   89.38000  -8.50900  1.000 55.51032  ?  449  MET   B C   1 
ATOM   17502 O  O   . MET   B 1 449  ? 19.46400   88.35800  -8.17500  1.000 60.04764  ?  449  MET   B O   1 
ATOM   17503 C  CB  . MET   B 1 449  ? 22.39300   88.76300  -9.18200  1.000 50.95507  ?  449  MET   B CB  1 
ATOM   17504 C  CG  . MET   B 1 449  ? 23.47400   88.77500  -10.24100 1.000 50.45609  ?  449  MET   B CG  1 
ATOM   17505 S  SD  . MET   B 1 449  ? 25.05200   88.11200  -9.68600  1.000 49.05562  ?  449  MET   B SD  1 
ATOM   17506 C  CE  . MET   B 1 449  ? 25.97200   88.18400  -11.21800 1.000 33.41955  ?  449  MET   B CE  1 
ATOM   17507 N  N   . GLN   B 1 450  ? 19.91200   90.54600  -7.88900  1.000 50.18493  ?  450  GLN   B N   1 
ATOM   17508 C  CA  . GLN   B 1 450  ? 18.99300   90.71600  -6.77300  1.000 51.30803  ?  450  GLN   B CA  1 
ATOM   17509 C  C   . GLN   B 1 450  ? 17.55400   90.94200  -7.21800  1.000 52.55124  ?  450  GLN   B C   1 
ATOM   17510 O  O   . GLN   B 1 450  ? 16.67300   91.07200  -6.36200  1.000 70.16803  ?  450  GLN   B O   1 
ATOM   17511 C  CB  . GLN   B 1 450  ? 19.46100   91.88000  -5.89500  1.000 63.57061  ?  450  GLN   B CB  1 
ATOM   17512 C  CG  . GLN   B 1 450  ? 19.77500   93.14500  -6.67400  1.000 68.39610  ?  450  GLN   B CG  1 
ATOM   17513 C  CD  . GLN   B 1 450  ? 20.52500   94.17300  -5.85100  1.000 86.09280  ?  450  GLN   B CD  1 
ATOM   17514 O  OE1 . GLN   B 1 450  ? 21.12700   93.84800  -4.82700  1.000 75.66328  ?  450  GLN   B OE1 1 
ATOM   17515 N  NE2 . GLN   B 1 450  ? 20.49200   95.42500  -6.29500  1.000 71.14542  ?  450  GLN   B NE2 1 
ATOM   17516 N  N   . MET   B 1 451  ? 17.29700   90.98900  -8.52100  1.000 45.13713  ?  451  MET   B N   1 
ATOM   17517 C  CA  . MET   B 1 451  ? 15.95700   91.14500  -9.06300  1.000 36.62799  ?  451  MET   B CA  1 
ATOM   17518 C  C   . MET   B 1 451  ? 15.38500   89.78200  -9.44000  1.000 50.81259  ?  451  MET   B C   1 
ATOM   17519 O  O   . MET   B 1 451  ? 16.12400   88.84700  -9.75700  1.000 39.46675  ?  451  MET   B O   1 
ATOM   17520 C  CB  . MET   B 1 451  ? 15.97100   92.06100  -10.28800 1.000 29.93910  ?  451  MET   B CB  1 
ATOM   17521 C  CG  . MET   B 1 451  ? 16.86500   93.28300  -10.14900 1.000 39.95473  ?  451  MET   B CG  1 
ATOM   17522 S  SD  . MET   B 1 451  ? 16.08300   94.66000  -9.29000  1.000 51.12685  ?  451  MET   B SD  1 
ATOM   17523 C  CE  . MET   B 1 451  ? 17.42500   95.84800  -9.26400  1.000 53.30451  ?  451  MET   B CE  1 
ATOM   17524 N  N   . ASP   B 1 452  ? 14.05700   89.67900  -9.40900  1.000 57.49115  ?  452  ASP   B N   1 
ATOM   17525 C  CA  . ASP   B 1 452  ? 13.36600   88.42200  -9.69600  1.000 60.34633  ?  452  ASP   B CA  1 
ATOM   17526 C  C   . ASP   B 1 452  ? 13.17200   88.31000  -11.20400 1.000 52.32116  ?  452  ASP   B C   1 
ATOM   17527 O  O   . ASP   B 1 452  ? 12.30900   88.97400  -11.78400 1.000 51.56835  ?  452  ASP   B O   1 
ATOM   17528 C  CB  . ASP   B 1 452  ? 12.03600   88.35500  -8.95400  1.000 46.82528  ?  452  ASP   B CB  1 
ATOM   17529 C  CG  . ASP   B 1 452  ? 11.43800   86.96300  -8.95800  1.000 79.02125  ?  452  ASP   B CG  1 
ATOM   17530 O  OD1 . ASP   B 1 452  ? 12.13100   86.02000  -8.51900  1.000 82.88063  ?  452  ASP   B OD1 1 
ATOM   17531 O  OD2 . ASP   B 1 452  ? 10.27700   86.81100  -9.39300  1.000 77.15104  -1 452  ASP   B OD2 1 
ATOM   17532 N  N   . ASN   B 1 453  ? 13.97900   87.46800  -11.84300 1.000 40.53844  ?  453  ASN   B N   1 
ATOM   17533 C  CA  . ASN   B 1 453  ? 13.97900   87.31200  -13.29100 1.000 31.45826  ?  453  ASN   B CA  1 
ATOM   17534 C  C   . ASN   B 1 453  ? 13.63700   85.87400  -13.64900 1.000 35.07083  ?  453  ASN   B C   1 
ATOM   17535 O  O   . ASN   B 1 453  ? 14.20900   84.93700  -13.08300 1.000 44.70042  ?  453  ASN   B O   1 
ATOM   17536 C  CB  . ASN   B 1 453  ? 15.34000   87.69600  -13.88400 1.000 36.53914  ?  453  ASN   B CB  1 
ATOM   17537 C  CG  . ASN   B 1 453  ? 15.47500   87.30000  -15.34300 1.000 35.38591  ?  453  ASN   B CG  1 
ATOM   17538 O  OD1 . ASN   B 1 453  ? 15.95500   86.21100  -15.66100 1.000 33.75202  ?  453  ASN   B OD1 1 
ATOM   17539 N  ND2 . ASN   B 1 453  ? 15.05300   88.18500  -16.23800 1.000 35.88519  ?  453  ASN   B ND2 1 
ATOM   17540 N  N   . GLN   B 1 454  ? 12.70600   85.70500  -14.58700 1.000 37.23590  ?  454  GLN   B N   1 
ATOM   17541 C  CA  . GLN   B 1 454  ? 12.34600   84.39000  -15.09500 1.000 37.12907  ?  454  GLN   B CA  1 
ATOM   17542 C  C   . GLN   B 1 454  ? 12.60400   84.24300  -16.58800 1.000 39.79613  ?  454  GLN   B C   1 
ATOM   17543 O  O   . GLN   B 1 454  ? 12.36700   83.16200  -17.14000 1.000 42.21155  ?  454  GLN   B O   1 
ATOM   17544 C  CB  . GLN   B 1 454  ? 10.86900   84.08500  -14.80300 1.000 40.40288  ?  454  GLN   B CB  1 
ATOM   17545 C  CG  . GLN   B 1 454  ? 10.42800   84.40600  -13.38400 1.000 42.49626  ?  454  GLN   B CG  1 
ATOM   17546 C  CD  . GLN   B 1 454  ? 9.72300    85.74500  -13.28400 1.000 62.36696  ?  454  GLN   B CD  1 
ATOM   17547 O  OE1 . GLN   B 1 454  ? 9.08300    86.19500  -14.23500 1.000 71.74373  ?  454  GLN   B OE1 1 
ATOM   17548 N  NE2 . GLN   B 1 454  ? 9.83600    86.38900  -12.12800 1.000 69.85619  ?  454  GLN   B NE2 1 
ATOM   17549 N  N   . SER   B 1 455  ? 13.09100   85.28900  -17.25400 1.000 30.48231  ?  455  SER   B N   1 
ATOM   17550 C  CA  . SER   B 1 455  ? 13.23700   85.27500  -18.70300 1.000 31.95157  ?  455  SER   B CA  1 
ATOM   17551 C  C   . SER   B 1 455  ? 14.60600   84.78500  -19.15600 1.000 39.15072  ?  455  SER   B C   1 
ATOM   17552 O  O   . SER   B 1 455  ? 14.70000   84.02600  -20.12700 1.000 39.66585  ?  455  SER   B O   1 
ATOM   17553 C  CB  . SER   B 1 455  ? 12.98800   86.67500  -19.26500 1.000 40.37488  ?  455  SER   B CB  1 
ATOM   17554 O  OG  . SER   B 1 455  ? 14.03800   87.55600  -18.90400 1.000 34.36890  ?  455  SER   B OG  1 
ATOM   17555 N  N   . PHE   B 1 456  ? 15.67000   85.20800  -18.48000 1.000 44.57267  ?  456  PHE   B N   1 
ATOM   17556 C  CA  . PHE   B 1 456  ? 17.01600   84.90300  -18.94400 1.000 30.69525  ?  456  PHE   B CA  1 
ATOM   17557 C  C   . PHE   B 1 456  ? 17.35100   83.43000  -18.75800 1.000 30.80961  ?  456  PHE   B C   1 
ATOM   17558 O  O   . PHE   B 1 456  ? 16.96900   82.80500  -17.76400 1.000 39.03765  ?  456  PHE   B O   1 
ATOM   17559 C  CB  . PHE   B 1 456  ? 18.04200   85.76000  -18.20500 1.000 27.60701  ?  456  PHE   B CB  1 
ATOM   17560 C  CG  . PHE   B 1 456  ? 18.22600   87.12500  -18.79400 1.000 29.78620  ?  456  PHE   B CG  1 
ATOM   17561 C  CD1 . PHE   B 1 456  ? 18.84700   87.28200  -20.02200 1.000 32.85405  ?  456  PHE   B CD1 1 
ATOM   17562 C  CD2 . PHE   B 1 456  ? 17.78800   88.25300  -18.11900 1.000 27.34130  ?  456  PHE   B CD2 1 
ATOM   17563 C  CE1 . PHE   B 1 456  ? 19.02100   88.53700  -20.57000 1.000 37.99596  ?  456  PHE   B CE1 1 
ATOM   17564 C  CE2 . PHE   B 1 456  ? 17.96000   89.51100  -18.66100 1.000 21.82956  ?  456  PHE   B CE2 1 
ATOM   17565 C  CZ  . PHE   B 1 456  ? 18.57700   89.65400  -19.88800 1.000 29.23410  ?  456  PHE   B CZ  1 
ATOM   17566 N  N   . ARG   B 1 457  ? 18.06600   82.87500  -19.73900 1.000 28.91507  ?  457  ARG   B N   1 
ATOM   17567 C  CA  . ARG   B 1 457  ? 18.70100   81.57200  -19.61200 1.000 37.24298  ?  457  ARG   B CA  1 
ATOM   17568 C  C   . ARG   B 1 457  ? 20.21900   81.65700  -19.55800 1.000 44.57389  ?  457  ARG   B C   1 
ATOM   17569 O  O   . ARG   B 1 457  ? 20.85500   80.73600  -19.03500 1.000 39.22380  ?  457  ARG   B O   1 
ATOM   17570 C  CB  . ARG   B 1 457  ? 18.29800   80.65900  -20.77900 1.000 29.76142  ?  457  ARG   B CB  1 
ATOM   17571 C  CG  . ARG   B 1 457  ? 18.80300   81.12500  -22.13500 1.000 29.99320  ?  457  ARG   B CG  1 
ATOM   17572 C  CD  . ARG   B 1 457  ? 18.48900   80.10900  -23.21900 1.000 30.45678  ?  457  ARG   B CD  1 
ATOM   17573 N  NE  . ARG   B 1 457  ? 19.12200   80.45300  -24.48600 1.000 29.60555  ?  457  ARG   B NE  1 
ATOM   17574 C  CZ  . ARG   B 1 457  ? 20.30000   79.99200  -24.88100 1.000 34.78125  ?  457  ARG   B CZ  1 
ATOM   17575 N  NH1 . ARG   B 1 457  ? 20.99600   79.14800  -24.13700 1.000 41.19083  ?  457  ARG   B NH1 1 
ATOM   17576 N  NH2 . ARG   B 1 457  ? 20.79200   80.38500  -26.05300 1.000 40.36092  ?  457  ARG   B NH2 1 
ATOM   17577 N  N   . VAL   B 1 458  ? 20.80500   82.73200  -20.08100 1.000 37.05432  ?  458  VAL   B N   1 
ATOM   17578 C  CA  . VAL   B 1 458  ? 22.24500   82.96200  -20.05700 1.000 35.46276  ?  458  VAL   B CA  1 
ATOM   17579 C  C   . VAL   B 1 458  ? 22.48300   84.44700  -19.83000 1.000 32.78120  ?  458  VAL   B C   1 
ATOM   17580 O  O   . VAL   B 1 458  ? 21.94700   85.28500  -20.56200 1.000 32.64164  ?  458  VAL   B O   1 
ATOM   17581 C  CB  . VAL   B 1 458  ? 22.92800   82.50500  -21.36300 1.000 31.87852  ?  458  VAL   B CB  1 
ATOM   17582 C  CG1 . VAL   B 1 458  ? 24.31200   83.12300  -21.48200 1.000 31.35649  ?  458  VAL   B CG1 1 
ATOM   17583 C  CG2 . VAL   B 1 458  ? 23.01800   80.98900  -21.41900 1.000 35.45309  ?  458  VAL   B CG2 1 
ATOM   17584 N  N   . VAL   B 1 459  ? 23.27900   84.77500  -18.81500 1.000 38.68952  ?  459  VAL   B N   1 
ATOM   17585 C  CA  . VAL   B 1 459  ? 23.66700   86.15100  -18.52600 1.000 37.35152  ?  459  VAL   B CA  1 
ATOM   17586 C  C   . VAL   B 1 459  ? 25.18700   86.19500  -18.47900 1.000 38.26739  ?  459  VAL   B C   1 
ATOM   17587 O  O   . VAL   B 1 459  ? 25.80400   85.58300  -17.59900 1.000 52.30912  ?  459  VAL   B O   1 
ATOM   17588 C  CB  . VAL   B 1 459  ? 23.06200   86.67000  -17.21600 1.000 33.20653  ?  459  VAL   B CB  1 
ATOM   17589 C  CG1 . VAL   B 1 459  ? 23.73100   87.97200  -16.80800 1.000 24.81255  ?  459  VAL   B CG1 1 
ATOM   17590 C  CG2 . VAL   B 1 459  ? 21.56500   86.87200  -17.37500 1.000 36.57701  ?  459  VAL   B CG2 1 
ATOM   17591 N  N   . ILE   B 1 460  ? 25.78900   86.91100  -19.42200 1.000 39.65235  ?  460  ILE   B N   1 
ATOM   17592 C  CA  . ILE   B 1 460  ? 27.23800   87.02600  -19.53200 1.000 38.18806  ?  460  ILE   B CA  1 
ATOM   17593 C  C   . ILE   B 1 460  ? 27.66700   88.35400  -18.92900 1.000 36.90070  ?  460  ILE   B C   1 
ATOM   17594 O  O   . ILE   B 1 460  ? 27.01500   89.38500  -19.14100 1.000 36.92239  ?  460  ILE   B O   1 
ATOM   17595 C  CB  . ILE   B 1 460  ? 27.68900   86.91000  -21.00000 1.000 37.85497  ?  460  ILE   B CB  1 
ATOM   17596 C  CG1 . ILE   B 1 460  ? 27.10700   85.64300  -21.62500 1.000 44.89715  ?  460  ILE   B CG1 1 
ATOM   17597 C  CG2 . ILE   B 1 460  ? 29.20700   86.90100  -21.09900 1.000 35.22326  ?  460  ILE   B CG2 1 
ATOM   17598 C  CD1 . ILE   B 1 460  ? 26.64400   85.83200  -23.04400 1.000 47.49957  ?  460  ILE   B CD1 1 
ATOM   17599 N  N   . THR   B 1 461  ? 28.76100   88.33300  -18.17200 1.000 39.93147  ?  461  THR   B N   1 
ATOM   17600 C  CA  . THR   B 1 461  ? 29.27100   89.53200  -17.52900 1.000 37.61889  ?  461  THR   B CA  1 
ATOM   17601 C  C   . THR   B 1 461  ? 30.78700   89.56200  -17.65600 1.000 36.42072  ?  461  THR   B C   1 
ATOM   17602 O  O   . THR   B 1 461  ? 31.42500   88.57200  -18.02500 1.000 39.05474  ?  461  THR   B O   1 
ATOM   17603 C  CB  . THR   B 1 461  ? 28.84400   89.60700  -16.05600 1.000 32.21446  ?  461  THR   B CB  1 
ATOM   17604 O  OG1 . THR   B 1 461  ? 29.08000   90.92800  -15.55600 1.000 27.01274  ?  461  THR   B OG1 1 
ATOM   17605 C  CG2 . THR   B 1 461  ? 29.62700   88.60900  -15.21800 1.000 37.19736  ?  461  THR   B CG2 1 
ATOM   17606 N  N   . GLY   B 1 462  ? 31.36000   90.71500  -17.35000 1.000 39.73849  ?  462  GLY   B N   1 
ATOM   17607 C  CA  . GLY   B 1 462  ? 32.78900   90.91200  -17.46300 1.000 38.80250  ?  462  GLY   B CA  1 
ATOM   17608 C  C   . GLY   B 1 462  ? 33.12800   92.37400  -17.61200 1.000 42.54095  ?  462  GLY   B C   1 
ATOM   17609 O  O   . GLY   B 1 462  ? 32.29100   93.20900  -17.95900 1.000 46.06980  ?  462  GLY   B O   1 
ATOM   17610 N  N   . GLY   B 1 463  ? 34.39400   92.68500  -17.34700 1.000 40.85219  ?  463  GLY   B N   1 
ATOM   17611 C  CA  . GLY   B 1 463  ? 34.85900   94.05800  -17.37200 1.000 41.91791  ?  463  GLY   B CA  1 
ATOM   17612 C  C   . GLY   B 1 463  ? 35.51000   94.44400  -16.06300 1.000 35.89715  ?  463  GLY   B C   1 
ATOM   17613 O  O   . GLY   B 1 463  ? 36.63900   94.94300  -16.04100 1.000 69.52401  ?  463  GLY   B O   1 
ATOM   17614 N  N   . ASP   B 1 464  ? 34.79800   94.22400  -14.96400 1.000 27.86285  ?  464  ASP   B N   1 
ATOM   17615 C  CA  . ASP   B 1 464  ? 35.35200   94.32600  -13.62300 1.000 34.94711  ?  464  ASP   B CA  1 
ATOM   17616 C  C   . ASP   B 1 464  ? 35.37900   92.94900  -12.97500 1.000 41.64395  ?  464  ASP   B C   1 
ATOM   17617 O  O   . ASP   B 1 464  ? 34.85500   91.96800  -13.51100 1.000 48.07405  ?  464  ASP   B O   1 
ATOM   17618 C  CB  . ASP   B 1 464  ? 34.55000   95.30400  -12.75700 1.000 40.72530  ?  464  ASP   B CB  1 
ATOM   17619 C  CG  . ASP   B 1 464  ? 35.02600   96.73500  -12.90000 1.000 69.27410  ?  464  ASP   B CG  1 
ATOM   17620 O  OD1 . ASP   B 1 464  ? 35.93700   96.98100  -13.71900 1.000 85.62829  ?  464  ASP   B OD1 1 
ATOM   17621 O  OD2 . ASP   B 1 464  ? 34.48100   97.61600  -12.20100 1.000 76.80819  -1 464  ASP   B OD2 1 
ATOM   17622 N  N   . VAL   B 1 465  ? 35.99900   92.88700  -11.79900 1.000 50.23104  ?  465  VAL   B N   1 
ATOM   17623 C  CA  . VAL   B 1 465  ? 36.13600   91.62200  -11.08800 1.000 58.25031  ?  465  VAL   B CA  1 
ATOM   17624 C  C   . VAL   B 1 465  ? 34.77400   91.20600  -10.54700 1.000 55.29901  ?  465  VAL   B C   1 
ATOM   17625 O  O   . VAL   B 1 465  ? 34.17000   91.91100  -9.73000  1.000 44.71112  ?  465  VAL   B O   1 
ATOM   17626 C  CB  . VAL   B 1 465  ? 37.17200   91.73400  -9.96300  1.000 38.48368  ?  465  VAL   B CB  1 
ATOM   17627 C  CG1 . VAL   B 1 465  ? 38.08500   90.51700  -9.96600  1.000 45.09136  ?  465  VAL   B CG1 1 
ATOM   17628 C  CG2 . VAL   B 1 465  ? 37.97500   93.01800  -10.10900 1.000 50.11465  ?  465  VAL   B CG2 1 
ATOM   17629 N  N   . LEU   B 1 466  ? 34.28300   90.05800  -11.00600 1.000 40.31940  ?  466  LEU   B N   1 
ATOM   17630 C  CA  . LEU   B 1 466  ? 33.00800   89.53600  -10.54000 1.000 35.02705  ?  466  LEU   B CA  1 
ATOM   17631 C  C   . LEU   B 1 466  ? 33.18400   88.87000  -9.18200  1.000 45.15612  ?  466  LEU   B C   1 
ATOM   17632 O  O   . LEU   B 1 466  ? 34.10200   88.06600  -8.98700  1.000 58.98880  ?  466  LEU   B O   1 
ATOM   17633 C  CB  . LEU   B 1 466  ? 32.43900   88.53900  -11.54800 1.000 44.08521  ?  466  LEU   B CB  1 
ATOM   17634 C  CG  . LEU   B 1 466  ? 31.09000   87.90900  -11.19200 1.000 32.93424  ?  466  LEU   B CG  1 
ATOM   17635 C  CD1 . LEU   B 1 466  ? 29.97000   88.93100  -11.31400 1.000 39.01382  ?  466  LEU   B CD1 1 
ATOM   17636 C  CD2 . LEU   B 1 466  ? 30.81300   86.69000  -12.06000 1.000 30.97182  ?  466  LEU   B CD2 1 
ATOM   17637 N  N   . LYS   B 1 467  ? 32.30300   89.21000  -8.24000  1.000 56.34597  ?  467  LYS   B N   1 
ATOM   17638 C  CA  . LYS   B 1 467  ? 32.31100   88.61500  -6.91300  1.000 49.93455  ?  467  LYS   B CA  1 
ATOM   17639 C  C   . LYS   B 1 467  ? 30.99200   87.96900  -6.52600  1.000 47.56374  ?  467  LYS   B C   1 
ATOM   17640 O  O   . LYS   B 1 467  ? 30.99500   87.06600  -5.68100  1.000 51.55499  ?  467  LYS   B O   1 
ATOM   17641 C  CB  . LYS   B 1 467  ? 32.66200   89.67000  -5.85200  1.000 47.02104  ?  467  LYS   B CB  1 
ATOM   17642 C  CG  . LYS   B 1 467  ? 34.01900   90.30800  -6.04300  1.000 41.88350  ?  467  LYS   B CG  1 
ATOM   17643 C  CD  . LYS   B 1 467  ? 34.04800   91.70100  -5.44800  1.000 42.95990  ?  467  LYS   B CD  1 
ATOM   17644 C  CE  . LYS   B 1 467  ? 32.97700   92.58200  -6.06700  1.000 55.36133  ?  467  LYS   B CE  1 
ATOM   17645 N  NZ  . LYS   B 1 467  ? 33.41000   94.00400  -6.13400  1.000 64.74071  ?  467  LYS   B NZ  1 
ATOM   17646 N  N   . LYS   B 1 468  ? 29.87800   88.39600  -7.11000  1.000 45.52324  ?  468  LYS   B N   1 
ATOM   17647 C  CA  . LYS   B 1 468  ? 28.56000   87.90100  -6.74500  1.000 40.52429  ?  468  LYS   B CA  1 
ATOM   17648 C  C   . LYS   B 1 468  ? 28.15100   86.77700  -7.68700  1.000 37.75165  ?  468  LYS   B C   1 
ATOM   17649 O  O   . LYS   B 1 468  ? 28.16000   86.95000  -8.91000  1.000 54.20460  ?  468  LYS   B O   1 
ATOM   17650 C  CB  . LYS   B 1 468  ? 27.53000   89.03000  -6.79100  1.000 29.40820  ?  468  LYS   B CB  1 
ATOM   17651 C  CG  . LYS   B 1 468  ? 26.22800   88.71400  -6.08000  1.000 46.19157  ?  468  LYS   B CG  1 
ATOM   17652 C  CD  . LYS   B 1 468  ? 25.22400   89.84100  -6.24900  1.000 61.13425  ?  468  LYS   B CD  1 
ATOM   17653 C  CE  . LYS   B 1 468  ? 24.15500   89.79200  -5.16900  1.000 74.67139  ?  468  LYS   B CE  1 
ATOM   17654 N  NZ  . LYS   B 1 468  ? 23.53400   88.44400  -5.05300  1.000 68.98059  ?  468  LYS   B NZ  1 
ATOM   17655 N  N   . ILE   B 1 469  ? 27.80500   85.62800  -7.11500  1.000 37.20120  ?  469  ILE   B N   1 
ATOM   17656 C  CA  . ILE   B 1 469  ? 27.24600   84.52800  -7.88700  1.000 38.43808  ?  469  ILE   B CA  1 
ATOM   17657 C  C   . ILE   B 1 469  ? 25.80000   84.22700  -7.51900  1.000 43.30367  ?  469  ILE   B C   1 
ATOM   17658 O  O   . ILE   B 1 469  ? 25.10200   83.56600  -8.30500  1.000 48.05927  ?  469  ILE   B O   1 
ATOM   17659 C  CB  . ILE   B 1 469  ? 28.10100   83.25200  -7.74700  1.000 35.49950  ?  469  ILE   B CB  1 
ATOM   17660 C  CG1 . ILE   B 1 469  ? 27.71000   82.48400  -6.48600  1.000 45.65877  ?  469  ILE   B CG1 1 
ATOM   17661 C  CG2 . ILE   B 1 469  ? 29.57600   83.60600  -7.70100  1.000 44.91453  ?  469  ILE   B CG2 1 
ATOM   17662 C  CD1 . ILE   B 1 469  ? 28.06300   81.02400  -6.53800  1.000 56.15976  ?  469  ILE   B CD1 1 
ATOM   17663 N  N   . GLU   B 1 470  ? 25.31900   84.68600  -6.36500  1.000 51.88423  ?  470  GLU   B N   1 
ATOM   17664 C  CA  . GLU   B 1 470  ? 23.94400   84.43100  -5.96500  1.000 54.30310  ?  470  GLU   B CA  1 
ATOM   17665 C  C   . GLU   B 1 470  ? 22.99500   85.30500  -6.77500  1.000 53.70253  ?  470  GLU   B C   1 
ATOM   17666 O  O   . GLU   B 1 470  ? 23.15300   86.52900  -6.82500  1.000 67.05738  ?  470  GLU   B O   1 
ATOM   17667 C  CB  . GLU   B 1 470  ? 23.77000   84.70700  -4.47300  1.000 63.90146  ?  470  GLU   B CB  1 
ATOM   17668 C  CG  . GLU   B 1 470  ? 23.02000   83.62800  -3.71800  1.000 74.32880  ?  470  GLU   B CG  1 
ATOM   17669 C  CD  . GLU   B 1 470  ? 22.68400   84.04900  -2.30200  1.000 101.74604 ?  470  GLU   B CD  1 
ATOM   17670 O  OE1 . GLU   B 1 470  ? 22.16100   85.16900  -2.12300  1.000 97.07759  ?  470  GLU   B OE1 1 
ATOM   17671 O  OE2 . GLU   B 1 470  ? 22.95300   83.26600  -1.36700  1.000 117.41372 -1 470  GLU   B OE2 1 
ATOM   17672 N  N   . ARG   B 1 471  ? 22.00600   84.67700  -7.40600  1.000 53.83354  ?  471  ARG   B N   1 
ATOM   17673 C  CA  . ARG   B 1 471  ? 21.08800   85.38500  -8.28500  1.000 47.77921  ?  471  ARG   B CA  1 
ATOM   17674 C  C   . ARG   B 1 471  ? 19.67300   84.86100  -8.08700  1.000 61.58028  ?  471  ARG   B C   1 
ATOM   17675 O  O   . ARG   B 1 471  ? 19.46500   83.68300  -7.78600  1.000 59.43714  ?  471  ARG   B O   1 
ATOM   17676 C  CB  . ARG   B 1 471  ? 21.51400   85.24700  -9.75400  1.000 48.43136  ?  471  ARG   B CB  1 
ATOM   17677 C  CG  . ARG   B 1 471  ? 21.87200   83.82800  -10.17500 1.000 49.47450  ?  471  ARG   B CG  1 
ATOM   17678 C  CD  . ARG   B 1 471  ? 23.01600   83.83500  -11.17900 1.000 38.19706  ?  471  ARG   B CD  1 
ATOM   17679 N  NE  . ARG   B 1 471  ? 23.14500   82.56600  -11.88600 1.000 45.58849  ?  471  ARG   B NE  1 
ATOM   17680 C  CZ  . ARG   B 1 471  ? 23.92500   81.56600  -11.49800 1.000 40.66311  ?  471  ARG   B CZ  1 
ATOM   17681 N  NH1 . ARG   B 1 471  ? 24.66100   81.64800  -10.40200 1.000 41.56526  ?  471  ARG   B NH1 1 
ATOM   17682 N  NH2 . ARG   B 1 471  ? 23.96800   80.45600  -12.23000 1.000 52.05960  ?  471  ARG   B NH2 1 
ATOM   17683 N  N   . ASN   B 1 472  ? 18.70200   85.76000  -8.24900  1.000 62.47106  ?  472  ASN   B N   1 
ATOM   17684 C  CA  . ASN   B 1 472  ? 17.28400   85.41200  -8.15200  1.000 49.39287  ?  472  ASN   B CA  1 
ATOM   17685 C  C   . ASN   B 1 472  ? 16.74100   85.10200  -9.54700  1.000 46.92260  ?  472  ASN   B C   1 
ATOM   17686 O  O   . ASN   B 1 472  ? 15.89900   85.80800  -10.10500 1.000 49.81456  ?  472  ASN   B O   1 
ATOM   17687 C  CB  . ASN   B 1 472  ? 16.50300   86.53600  -7.48400  1.000 50.24978  ?  472  ASN   B CB  1 
ATOM   17688 C  CG  . ASN   B 1 472  ? 16.51800   86.43800  -5.97300  1.000 67.82434  ?  472  ASN   B CG  1 
ATOM   17689 O  OD1 . ASN   B 1 472  ? 16.27200   85.37300  -5.40700  1.000 70.48016  ?  472  ASN   B OD1 1 
ATOM   17690 N  ND2 . ASN   B 1 472  ? 16.81000   87.55200  -5.31000  1.000 65.09718  ?  472  ASN   B ND2 1 
ATOM   17691 N  N   . GLY   B 1 473  ? 17.24900   84.01200  -10.10900 1.000 34.99111  ?  473  GLY   B N   1 
ATOM   17692 C  CA  . GLY   B 1 473  ? 16.82900   83.58900  -11.42900 1.000 36.46808  ?  473  GLY   B CA  1 
ATOM   17693 C  C   . GLY   B 1 473  ? 17.42400   82.24500  -11.77900 1.000 46.00955  ?  473  GLY   B C   1 
ATOM   17694 O  O   . GLY   B 1 473  ? 18.42700   81.81500  -11.20000 1.000 57.12314  ?  473  GLY   B O   1 
ATOM   17695 N  N   . THR   B 1 474  ? 16.78500   81.58500  -12.74300 1.000 54.24251  ?  474  THR   B N   1 
ATOM   17696 C  CA  . THR   B 1 474  ? 17.22400   80.27900  -13.23300 1.000 62.40378  ?  474  THR   B CA  1 
ATOM   17697 C  C   . THR   B 1 474  ? 18.11300   80.39100  -14.46100 1.000 66.59206  ?  474  THR   B C   1 
ATOM   17698 O  O   . THR   B 1 474  ? 18.04800   79.54400  -15.35800 1.000 69.56473  ?  474  THR   B O   1 
ATOM   17699 C  CB  . THR   B 1 474  ? 16.01000   79.40500  -13.52800 1.000 58.27276  ?  474  THR   B CB  1 
ATOM   17700 O  OG1 . THR   B 1 474  ? 15.00500   80.18900  -14.18500 1.000 58.70160  ?  474  THR   B OG1 1 
ATOM   17701 C  CG2 . THR   B 1 474  ? 15.44300   78.82500  -12.24100 1.000 55.25910  ?  474  THR   B CG2 1 
ATOM   17702 N  N   . TYR   B 1 475  ? 18.95200   81.42000  -14.53400 1.000 56.42420  ?  475  TYR   B N   1 
ATOM   17703 C  CA  . TYR   B 1 475  ? 19.84300   81.62000  -15.66600 1.000 42.99859  ?  475  TYR   B CA  1 
ATOM   17704 C  C   . TYR   B 1 475  ? 21.27600   81.27700  -15.28400 1.000 47.75703  ?  475  TYR   B C   1 
ATOM   17705 O  O   . TYR   B 1 475  ? 21.67300   81.38100  -14.12000 1.000 51.58735  ?  475  TYR   B O   1 
ATOM   17706 C  CB  . TYR   B 1 475  ? 19.77400   83.06200  -16.18400 1.000 32.87985  ?  475  TYR   B CB  1 
ATOM   17707 C  CG  . TYR   B 1 475  ? 20.00900   84.13300  -15.13900 1.000 35.79037  ?  475  TYR   B CG  1 
ATOM   17708 C  CD1 . TYR   B 1 475  ? 21.29500   84.53500  -14.80100 1.000 44.87589  ?  475  TYR   B CD1 1 
ATOM   17709 C  CD2 . TYR   B 1 475  ? 18.94200   84.75900  -14.50800 1.000 41.26497  ?  475  TYR   B CD2 1 
ATOM   17710 C  CE1 . TYR   B 1 475  ? 21.51200   85.52000  -13.85500 1.000 36.80633  ?  475  TYR   B CE1 1 
ATOM   17711 C  CE2 . TYR   B 1 475  ? 19.15000   85.74500  -13.56000 1.000 50.82315  ?  475  TYR   B CE2 1 
ATOM   17712 C  CZ  . TYR   B 1 475  ? 20.43700   86.12100  -13.23800 1.000 44.00834  ?  475  TYR   B CZ  1 
ATOM   17713 O  OH  . TYR   B 1 475  ? 20.64800   87.10100  -12.29600 1.000 57.98936  ?  475  TYR   B OH  1 
ATOM   17714 N  N   . LYS   B 1 476  ? 22.04700   80.86200  -16.28500 1.000 36.34229  ?  476  LYS   B N   1 
ATOM   17715 C  CA  . LYS   B 1 476  ? 23.46100   80.58400  -16.09400 1.000 32.60102  ?  476  LYS   B CA  1 
ATOM   17716 C  C   . LYS   B 1 476  ? 24.25200   81.88300  -16.05800 1.000 39.05176  ?  476  LYS   B C   1 
ATOM   17717 O  O   . LYS   B 1 476  ? 23.94000   82.83900  -16.77400 1.000 40.05100  ?  476  LYS   B O   1 
ATOM   17718 C  CB  . LYS   B 1 476  ? 23.98200   79.68800  -17.21500 1.000 27.67151  ?  476  LYS   B CB  1 
ATOM   17719 C  CG  . LYS   B 1 476  ? 23.35800   78.30600  -17.24900 1.000 32.92294  ?  476  LYS   B CG  1 
ATOM   17720 C  CD  . LYS   B 1 476  ? 23.67200   77.60400  -18.55800 1.000 33.59947  ?  476  LYS   B CD  1 
ATOM   17721 C  CE  . LYS   B 1 476  ? 23.74200   76.10000  -18.37400 1.000 36.15922  ?  476  LYS   B CE  1 
ATOM   17722 N  NZ  . LYS   B 1 476  ? 23.96200   75.40100  -19.66900 1.000 57.38413  ?  476  LYS   B NZ  1 
ATOM   17723 N  N   . LEU   B 1 477  ? 25.28000   81.91500  -15.21800 1.000 47.35254  ?  477  LEU   B N   1 
ATOM   17724 C  CA  . LEU   B 1 477  ? 26.14800   83.07500  -15.08800 1.000 38.40799  ?  477  LEU   B CA  1 
ATOM   17725 C  C   . LEU   B 1 477  ? 27.48700   82.79100  -15.75600 1.000 41.37488  ?  477  LEU   B C   1 
ATOM   17726 O  O   . LEU   B 1 477  ? 28.06300   81.71200  -15.58200 1.000 42.01130  ?  477  LEU   B O   1 
ATOM   17727 C  CB  . LEU   B 1 477  ? 26.36200   83.44200  -13.61900 1.000 26.58545  ?  477  LEU   B CB  1 
ATOM   17728 C  CG  . LEU   B 1 477  ? 27.15600   84.72700  -13.39800 1.000 38.48247  ?  477  LEU   B CG  1 
ATOM   17729 C  CD1 . LEU   B 1 477  ? 26.41500   85.90600  -14.00700 1.000 29.48355  ?  477  LEU   B CD1 1 
ATOM   17730 C  CD2 . LEU   B 1 477  ? 27.42200   84.94700  -11.91800 1.000 41.49769  ?  477  LEU   B CD2 1 
ATOM   17731 N  N   . TYR   B 1 478  ? 27.97600   83.76100  -16.52200 1.000 29.24754  ?  478  TYR   B N   1 
ATOM   17732 C  CA  . TYR   B 1 478  ? 29.22800   83.62500  -17.24800 1.000 34.52026  ?  478  TYR   B CA  1 
ATOM   17733 C  C   . TYR   B 1 478  ? 30.11800   84.82600  -16.97600 1.000 36.62114  ?  478  TYR   B C   1 
ATOM   17734 O  O   . TYR   B 1 478  ? 29.64600   85.96600  -16.95000 1.000 31.31904  ?  478  TYR   B O   1 
ATOM   17735 C  CB  . TYR   B 1 478  ? 28.98700   83.48900  -18.75400 1.000 37.87769  ?  478  TYR   B CB  1 
ATOM   17736 C  CG  . TYR   B 1 478  ? 28.46800   82.13400  -19.17600 1.000 39.85282  ?  478  TYR   B CG  1 
ATOM   17737 C  CD1 . TYR   B 1 478  ? 27.10600   81.86600  -19.19800 1.000 39.93436  ?  478  TYR   B CD1 1 
ATOM   17738 C  CD2 . TYR   B 1 478  ? 29.34100   81.12500  -19.55900 1.000 39.73521  ?  478  TYR   B CD2 1 
ATOM   17739 C  CE1 . TYR   B 1 478  ? 26.62900   80.62900  -19.58800 1.000 39.28424  ?  478  TYR   B CE1 1 
ATOM   17740 C  CE2 . TYR   B 1 478  ? 28.87400   79.88700  -19.95100 1.000 37.56518  ?  478  TYR   B CE2 1 
ATOM   17741 C  CZ  . TYR   B 1 478  ? 27.51800   79.64300  -19.96300 1.000 36.06597  ?  478  TYR   B CZ  1 
ATOM   17742 O  OH  . TYR   B 1 478  ? 27.05100   78.40900  -20.35200 1.000 41.87129  ?  478  TYR   B OH  1 
ATOM   17743 N  N   . ASN   B 1 479  ? 31.40600   84.56300  -16.77400 1.000 35.40029  ?  479  ASN   B N   1 
ATOM   17744 C  CA  . ASN   B 1 479  ? 32.41100   85.59800  -16.57700 1.000 26.52059  ?  479  ASN   B CA  1 
ATOM   17745 C  C   . ASN   B 1 479  ? 33.34500   85.60700  -17.77900 1.000 37.76827  ?  479  ASN   B C   1 
ATOM   17746 O  O   . ASN   B 1 479  ? 33.84200   84.55300  -18.19000 1.000 38.29237  ?  479  ASN   B O   1 
ATOM   17747 C  CB  . ASN   B 1 479  ? 33.19800   85.35700  -15.28700 1.000 28.15537  ?  479  ASN   B CB  1 
ATOM   17748 C  CG  . ASN   B 1 479  ? 33.81800   86.62700  -14.73600 1.000 41.55122  ?  479  ASN   B CG  1 
ATOM   17749 O  OD1 . ASN   B 1 479  ? 33.26200   87.71500  -14.87900 1.000 42.47093  ?  479  ASN   B OD1 1 
ATOM   17750 N  ND2 . ASN   B 1 479  ? 34.97900   86.49300  -14.10300 1.000 41.16275  ?  479  ASN   B ND2 1 
ATOM   17751 N  N   . GLY   B 1 480  ? 33.57500   86.78300  -18.33900 1.000 35.93852  ?  480  GLY   B N   1 
ATOM   17752 C  CA  . GLY   B 1 480  ? 34.39600   86.91200  -19.53300 1.000 34.49253  ?  480  GLY   B CA  1 
ATOM   17753 C  C   . GLY   B 1 480  ? 35.45800   87.97700  -19.37800 1.000 32.60695  ?  480  GLY   B C   1 
ATOM   17754 O  O   . GLY   B 1 480  ? 35.24000   88.99900  -18.72900 1.000 35.41208  ?  480  GLY   B O   1 
ATOM   17755 N  N   . TYR   B 1 481  ? 36.61600   87.72500  -19.98700 1.000 34.10579  ?  481  TYR   B N   1 
ATOM   17756 C  CA  . TYR   B 1 481  ? 37.74500   88.64300  -19.95400 1.000 39.43182  ?  481  TYR   B CA  1 
ATOM   17757 C  C   . TYR   B 1 481  ? 38.20500   88.93900  -21.37300 1.000 37.68287  ?  481  TYR   B C   1 
ATOM   17758 O  O   . TYR   B 1 481  ? 38.19200   88.05500  -22.23500 1.000 31.27135  ?  481  TYR   B O   1 
ATOM   17759 C  CB  . TYR   B 1 481  ? 38.91300   88.06800  -19.13800 1.000 35.68107  ?  481  TYR   B CB  1 
ATOM   17760 C  CG  . TYR   B 1 481  ? 40.22900   88.77600  -19.37500 1.000 36.75217  ?  481  TYR   B CG  1 
ATOM   17761 C  CD1 . TYR   B 1 481  ? 40.50300   89.99400  -18.76800 1.000 24.32265  ?  481  TYR   B CD1 1 
ATOM   17762 C  CD2 . TYR   B 1 481  ? 41.19600   88.22800  -20.21000 1.000 40.28057  ?  481  TYR   B CD2 1 
ATOM   17763 C  CE1 . TYR   B 1 481  ? 41.70200   90.64700  -18.98500 1.000 39.95963  ?  481  TYR   B CE1 1 
ATOM   17764 C  CE2 . TYR   B 1 481  ? 42.39800   88.87400  -20.43300 1.000 31.09151  ?  481  TYR   B CE2 1 
ATOM   17765 C  CZ  . TYR   B 1 481  ? 42.64500   90.08300  -19.81800 1.000 34.94765  ?  481  TYR   B CZ  1 
ATOM   17766 O  OH  . TYR   B 1 481  ? 43.83900   90.73200  -20.03300 1.000 47.10125  ?  481  TYR   B OH  1 
ATOM   17767 N  N   . GLY   B 1 482  ? 38.61900   90.18200  -21.60800 1.000 31.82642  ?  482  GLY   B N   1 
ATOM   17768 C  CA  . GLY   B 1 482  ? 39.13100   90.57400  -22.89900 1.000 34.62468  ?  482  GLY   B CA  1 
ATOM   17769 C  C   . GLY   B 1 482  ? 39.32000   92.07000  -23.03600 1.000 34.10033  ?  482  GLY   B C   1 
ATOM   17770 O  O   . GLY   B 1 482  ? 38.47800   92.87000  -22.61600 1.000 51.41205  ?  482  GLY   B O   1 
ATOM   17771 N  N   . PRO   B 1 483  ? 40.44200   92.47800  -23.61900 1.000 40.44520  ?  483  PRO   B N   1 
ATOM   17772 C  CA  . PRO   B 1 483  ? 40.64300   93.89200  -23.93300 1.000 33.34812  ?  483  PRO   B CA  1 
ATOM   17773 C  C   . PRO   B 1 483  ? 39.99700   94.25400  -25.26100 1.000 35.15344  ?  483  PRO   B C   1 
ATOM   17774 O  O   . PRO   B 1 483  ? 39.68700   93.39700  -26.09100 1.000 39.73588  ?  483  PRO   B O   1 
ATOM   17775 C  CB  . PRO   B 1 483  ? 42.16600   94.01900  -24.01100 1.000 23.01454  ?  483  PRO   B CB  1 
ATOM   17776 C  CG  . PRO   B 1 483  ? 42.60100   92.68500  -24.51700 1.000 23.24134  ?  483  PRO   B CG  1 
ATOM   17777 C  CD  . PRO   B 1 483  ? 41.63100   91.66900  -23.94600 1.000 39.61904  ?  483  PRO   B CD  1 
ATOM   17778 N  N   . THR   B 1 484  ? 39.79600   95.56000  -25.45000 1.000 28.18210  ?  484  THR   B N   1 
ATOM   17779 C  CA  . THR   B 1 484  ? 39.25900   96.03600  -26.71900 1.000 27.39098  ?  484  THR   B CA  1 
ATOM   17780 C  C   . THR   B 1 484  ? 40.21600   95.74000  -27.86700 1.000 32.34046  ?  484  THR   B C   1 
ATOM   17781 O  O   . THR   B 1 484  ? 39.78200   95.56800  -29.01100 1.000 39.91650  ?  484  THR   B O   1 
ATOM   17782 C  CB  . THR   B 1 484  ? 38.96500   97.53700  -26.64000 1.000 30.96634  ?  484  THR   B CB  1 
ATOM   17783 O  OG1 . THR   B 1 484  ? 38.31400   97.83400  -25.39900 1.000 35.08217  ?  484  THR   B OG1 1 
ATOM   17784 C  CG2 . THR   B 1 484  ? 38.05800   97.96400  -27.78100 1.000 33.73021  ?  484  THR   B CG2 1 
ATOM   17785 N  N   . GLU   B 1 485  ? 41.51800   95.65800  -27.57700 1.000 47.24815  ?  485  GLU   B N   1 
ATOM   17786 C  CA  . GLU   B 1 485  ? 42.50800   95.37400  -28.60800 1.000 33.35102  ?  485  GLU   B CA  1 
ATOM   17787 C  C   . GLU   B 1 485  ? 42.39600   93.95500  -29.14600 1.000 30.56846  ?  485  GLU   B C   1 
ATOM   17788 O  O   . GLU   B 1 485  ? 42.91200   93.67700  -30.23400 1.000 32.83678  ?  485  GLU   B O   1 
ATOM   17789 C  CB  . GLU   B 1 485  ? 43.91700   95.61500  -28.06300 1.000 35.41687  ?  485  GLU   B CB  1 
ATOM   17790 C  CG  . GLU   B 1 485  ? 44.24200   97.07600  -27.76800 1.000 34.67978  ?  485  GLU   B CG  1 
ATOM   17791 C  CD  . GLU   B 1 485  ? 43.73200   97.54300  -26.41500 1.000 38.65571  ?  485  GLU   B CD  1 
ATOM   17792 O  OE1 . GLU   B 1 485  ? 42.84900   96.87600  -25.83500 1.000 38.62271  ?  485  GLU   B OE1 1 
ATOM   17793 O  OE2 . GLU   B 1 485  ? 44.22600   98.58100  -25.92600 1.000 43.21790  -1 485  GLU   B OE2 1 
ATOM   17794 N  N   . CYS   B 1 486  ? 41.73600   93.05800  -28.41400 1.000 35.41412  ?  486  CYS   B N   1 
ATOM   17795 C  CA  . CYS   B 1 486  ? 41.51500   91.69600  -28.88300 1.000 40.89655  ?  486  CYS   B CA  1 
ATOM   17796 C  C   . CYS   B 1 486  ? 40.02300   91.39800  -28.99200 1.000 41.11539  ?  486  CYS   B C   1 
ATOM   17797 O  O   . CYS   B 1 486  ? 39.50800   90.47400  -28.35400 1.000 52.10469  ?  486  CYS   B O   1 
ATOM   17798 C  CB  . CYS   B 1 486  ? 42.20400   90.68800  -27.95900 1.000 44.32714  ?  486  CYS   B CB  1 
ATOM   17799 S  SG  . CYS   B 1 486  ? 44.00000   90.90300  -27.81400 1.000 66.94141  ?  486  CYS   B SG  1 
ATOM   17800 N  N   . THR   B 1 487  ? 39.33500   92.18900  -29.82200 1.000 41.93539  ?  487  THR   B N   1 
ATOM   17801 C  CA  . THR   B 1 487  ? 37.90700   92.05200  -30.13800 1.000 45.87758  ?  487  THR   B CA  1 
ATOM   17802 C  C   . THR   B 1 487  ? 37.12500   92.37400  -28.87200 1.000 52.56590  ?  487  THR   B C   1 
ATOM   17803 O  O   . THR   B 1 487  ? 37.28900   93.48400  -28.33700 1.000 74.52201  ?  487  THR   B O   1 
ATOM   17804 C  CB  . THR   B 1 487  ? 37.62200   90.68000  -30.77900 1.000 33.17685  ?  487  THR   B CB  1 
ATOM   17805 O  OG1 . THR   B 1 487  ? 38.70200   90.32900  -31.65500 1.000 65.37695  ?  487  THR   B OG1 1 
ATOM   17806 C  CG2 . THR   B 1 487  ? 36.33500   90.71700  -31.61100 1.000 43.00635  ?  487  THR   B CG2 1 
ATOM   17807 N  N   . ILE   B 1 488  ? 36.30300   91.46600  -28.35500 1.000 28.41000  ?  488  ILE   B N   1 
ATOM   17808 C  CA  . ILE   B 1 488  ? 35.42500   91.73700  -27.21800 1.000 37.86069  ?  488  ILE   B CA  1 
ATOM   17809 C  C   . ILE   B 1 488  ? 35.90800   90.99600  -25.97700 1.000 32.29718  ?  488  ILE   B C   1 
ATOM   17810 O  O   . ILE   B 1 488  ? 36.26300   91.61300  -24.96700 1.000 31.36135  ?  488  ILE   B O   1 
ATOM   17811 C  CB  . ILE   B 1 488  ? 33.96500   91.36600  -27.56900 1.000 30.47558  ?  488  ILE   B CB  1 
ATOM   17812 C  CG1 . ILE   B 1 488  ? 33.46300   92.18100  -28.76700 1.000 26.06571  ?  488  ILE   B CG1 1 
ATOM   17813 C  CG2 . ILE   B 1 488  ? 33.03200   91.47600  -26.35400 1.000 40.49464  ?  488  ILE   B CG2 1 
ATOM   17814 C  CD1 . ILE   B 1 488  ? 32.30700   91.51200  -29.50000 1.000 34.30827  ?  488  ILE   B CD1 1 
ATOM   17815 N  N   . MET   B 1 489  ? 35.94600   89.67000  -26.04300 1.000 30.35885  ?  489  MET   B N   1 
ATOM   17816 C  CA  . MET   B 1 489  ? 36.46200   88.82700  -24.98200 1.000 36.93404  ?  489  MET   B CA  1 
ATOM   17817 C  C   . MET   B 1 489  ? 37.34100   87.74300  -25.59300 1.000 41.47376  ?  489  MET   B C   1 
ATOM   17818 O  O   . MET   B 1 489  ? 37.18300   87.37000  -26.75900 1.000 35.20268  ?  489  MET   B O   1 
ATOM   17819 C  CB  . MET   B 1 489  ? 35.32500   88.19500  -24.17000 1.000 32.46690  ?  489  MET   B CB  1 
ATOM   17820 C  CG  . MET   B 1 489  ? 34.34300   89.20300  -23.59000 1.000 28.26914  ?  489  MET   B CG  1 
ATOM   17821 S  SD  . MET   B 1 489  ? 32.91400   88.38400  -22.86000 1.000 44.04301  ?  489  MET   B SD  1 
ATOM   17822 C  CE  . MET   B 1 489  ? 32.01900   89.77300  -22.17200 1.000 40.31411  ?  489  MET   B CE  1 
ATOM   17823 N  N   . VAL   B 1 490  ? 38.27400   87.24300  -24.78600 1.000 30.41640  ?  490  VAL   B N   1 
ATOM   17824 C  CA  . VAL   B 1 490  ? 39.15100   86.15800  -25.20400 1.000 26.24792  ?  490  VAL   B CA  1 
ATOM   17825 C  C   . VAL   B 1 490  ? 39.00700   84.91100  -24.34300 1.000 30.41577  ?  490  VAL   B C   1 
ATOM   17826 O  O   . VAL   B 1 490  ? 39.45500   83.83300  -24.76600 1.000 33.30102  ?  490  VAL   B O   1 
ATOM   17827 C  CB  . VAL   B 1 490  ? 40.62500   86.61400  -25.23600 1.000 29.07739  ?  490  VAL   B CB  1 
ATOM   17828 C  CG1 . VAL   B 1 490  ? 40.86600   87.53900  -26.41900 1.000 32.11704  ?  490  VAL   B CG1 1 
ATOM   17829 C  CG2 . VAL   B 1 490  ? 41.00600   87.29800  -23.92800 1.000 29.85741  ?  490  VAL   B CG2 1 
ATOM   17830 N  N   . THR   B 1 491  ? 38.40800   85.00100  -23.15800 1.000 39.39636  ?  491  THR   B N   1 
ATOM   17831 C  CA  . THR   B 1 491  ? 38.17000   83.84600  -22.30600 1.000 36.54920  ?  491  THR   B CA  1 
ATOM   17832 C  C   . THR   B 1 491  ? 36.71700   83.84800  -21.85200 1.000 32.89183  ?  491  THR   B C   1 
ATOM   17833 O  O   . THR   B 1 491  ? 36.00100   84.84400  -21.98500 1.000 38.02817  ?  491  THR   B O   1 
ATOM   17834 C  CB  . THR   B 1 491  ? 39.11000   83.83300  -21.09100 1.000 42.31635  ?  491  THR   B CB  1 
ATOM   17835 O  OG1 . THR   B 1 491  ? 38.93200   85.03400  -20.32900 1.000 41.24020  ?  491  THR   B OG1 1 
ATOM   17836 C  CG2 . THR   B 1 491  ? 40.56000   83.73100  -21.54000 1.000 46.37561  ?  491  THR   B CG2 1 
ATOM   17837 N  N   . MET   B 1 492  ? 36.28000   82.71200  -21.31100 1.000 30.90799  ?  492  MET   B N   1 
ATOM   17838 C  CA  . MET   B 1 492  ? 34.90800   82.57000  -20.84700 1.000 40.52353  ?  492  MET   B CA  1 
ATOM   17839 C  C   . MET   B 1 492  ? 34.85000   81.50300  -19.76400 1.000 44.56172  ?  492  MET   B C   1 
ATOM   17840 O  O   . MET   B 1 492  ? 35.49400   80.45700  -19.88100 1.000 48.16949  ?  492  MET   B O   1 
ATOM   17841 C  CB  . MET   B 1 492  ? 33.96500   82.21000  -22.00200 1.000 28.01788  ?  492  MET   B CB  1 
ATOM   17842 C  CG  . MET   B 1 492  ? 32.49700   82.19400  -21.61900 1.000 25.85482  ?  492  MET   B CG  1 
ATOM   17843 S  SD  . MET   B 1 492  ? 31.96000   83.76500  -20.91500 1.000 42.04081  ?  492  MET   B SD  1 
ATOM   17844 C  CE  . MET   B 1 492  ? 32.37100   84.89200  -22.24100 1.000 24.37775  ?  492  MET   B CE  1 
ATOM   17845 N  N   . PHE   B 1 493  ? 34.07300   81.77500  -18.71600 1.000 35.50617  ?  493  PHE   B N   1 
ATOM   17846 C  CA  . PHE   B 1 493  ? 33.93100   80.86100  -17.59100 1.000 35.36554  ?  493  PHE   B CA  1 
ATOM   17847 C  C   . PHE   B 1 493  ? 32.48000   80.83700  -17.13900 1.000 41.71083  ?  493  PHE   B C   1 
ATOM   17848 O  O   . PHE   B 1 493  ? 31.87500   81.89300  -16.94000 1.000 40.82538  ?  493  PHE   B O   1 
ATOM   17849 C  CB  . PHE   B 1 493  ? 34.83300   81.27500  -16.42200 1.000 28.61239  ?  493  PHE   B CB  1 
ATOM   17850 C  CG  . PHE   B 1 493  ? 34.77500   80.34000  -15.24700 1.000 40.20605  ?  493  PHE   B CG  1 
ATOM   17851 C  CD1 . PHE   B 1 493  ? 35.41800   79.11300  -15.28800 1.000 37.37450  ?  493  PHE   B CD1 1 
ATOM   17852 C  CD2 . PHE   B 1 493  ? 34.08400   80.69000  -14.09800 1.000 43.11138  ?  493  PHE   B CD2 1 
ATOM   17853 C  CE1 . PHE   B 1 493  ? 35.36800   78.25000  -14.20900 1.000 37.53935  ?  493  PHE   B CE1 1 
ATOM   17854 C  CE2 . PHE   B 1 493  ? 34.03000   79.83100  -13.01500 1.000 37.82663  ?  493  PHE   B CE2 1 
ATOM   17855 C  CZ  . PHE   B 1 493  ? 34.67300   78.61000  -13.07000 1.000 37.68354  ?  493  PHE   B CZ  1 
ATOM   17856 N  N   . GLU   B 1 494  ? 31.92900   79.63700  -16.97600 1.000 37.11772  ?  494  GLU   B N   1 
ATOM   17857 C  CA  . GLU   B 1 494  ? 30.59600   79.47300  -16.40900 1.000 38.28565  ?  494  GLU   B CA  1 
ATOM   17858 C  C   . GLU   B 1 494  ? 30.72100   79.31900  -14.89800 1.000 35.82361  ?  494  GLU   B C   1 
ATOM   17859 O  O   . GLU   B 1 494  ? 31.33700   78.36200  -14.41600 1.000 38.70273  ?  494  GLU   B O   1 
ATOM   17860 C  CB  . GLU   B 1 494  ? 29.88400   78.26400  -17.01400 1.000 41.20633  ?  494  GLU   B CB  1 
ATOM   17861 C  CG  . GLU   B 1 494  ? 28.48500   78.04300  -16.45700 1.000 47.69067  ?  494  GLU   B CG  1 
ATOM   17862 C  CD  . GLU   B 1 494  ? 27.80100   76.82300  -17.04300 1.000 44.43020  ?  494  GLU   B CD  1 
ATOM   17863 O  OE1 . GLU   B 1 494  ? 28.29500   76.29300  -18.06000 1.000 44.18687  ?  494  GLU   B OE1 1 
ATOM   17864 O  OE2 . GLU   B 1 494  ? 26.76900   76.39500  -16.48400 1.000 50.30628  -1 494  GLU   B OE2 1 
ATOM   17865 N  N   . VAL   B 1 495  ? 30.14100   80.26000  -14.15600 1.000 33.20614  ?  495  VAL   B N   1 
ATOM   17866 C  CA  . VAL   B 1 495  ? 30.20400   80.23000  -12.69800 1.000 26.16592  ?  495  VAL   B CA  1 
ATOM   17867 C  C   . VAL   B 1 495  ? 29.36400   79.05300  -12.20800 1.000 24.78566  ?  495  VAL   B C   1 
ATOM   17868 O  O   . VAL   B 1 495  ? 28.13200   79.09600  -12.25000 1.000 47.67064  ?  495  VAL   B O   1 
ATOM   17869 C  CB  . VAL   B 1 495  ? 29.72200   81.54900  -12.08600 1.000 26.61713  ?  495  VAL   B CB  1 
ATOM   17870 C  CG1 . VAL   B 1 495  ? 30.04600   81.58800  -10.60200 1.000 31.15337  ?  495  VAL   B CG1 1 
ATOM   17871 C  CG2 . VAL   B 1 495  ? 30.34800   82.73100  -12.81100 1.000 26.95156  ?  495  VAL   B CG2 1 
ATOM   17872 N  N   . ASP   B 1 496  ? 30.03200   77.99700  -11.74300 1.000 30.79460  ?  496  ASP   B N   1 
ATOM   17873 C  CA  . ASP   B 1 496  ? 29.35500   76.79500  -11.27500 1.000 44.54213  ?  496  ASP   B CA  1 
ATOM   17874 C  C   . ASP   B 1 496  ? 29.23200   76.72100  -9.76000  1.000 52.13478  ?  496  ASP   B C   1 
ATOM   17875 O  O   . ASP   B 1 496  ? 28.34200   76.02500  -9.26000  1.000 61.68933  ?  496  ASP   B O   1 
ATOM   17876 C  CB  . ASP   B 1 496  ? 30.08900   75.54500  -11.77800 1.000 49.09181  ?  496  ASP   B CB  1 
ATOM   17877 C  CG  . ASP   B 1 496  ? 31.57200   75.56400  -11.44400 1.000 55.62804  ?  496  ASP   B CG  1 
ATOM   17878 O  OD1 . ASP   B 1 496  ? 32.19500   76.64200  -11.54400 1.000 48.15146  ?  496  ASP   B OD1 1 
ATOM   17879 O  OD2 . ASP   B 1 496  ? 32.11500   74.50000  -11.07900 1.000 59.33339  -1 496  ASP   B OD2 1 
ATOM   17880 N  N   . LYS   B 1 497  ? 30.09200   77.41900  -9.02800  1.000 46.17012  ?  497  LYS   B N   1 
ATOM   17881 C  CA  . LYS   B 1 497  ? 30.11100   77.35800  -7.57300  1.000 46.42340  ?  497  LYS   B CA  1 
ATOM   17882 C  C   . LYS   B 1 497  ? 30.76700   78.63300  -7.06300  1.000 52.55352  ?  497  LYS   B C   1 
ATOM   17883 O  O   . LYS   B 1 497  ? 31.32200   79.41000  -7.85100  1.000 59.48799  ?  497  LYS   B O   1 
ATOM   17884 C  CB  . LYS   B 1 497  ? 30.86200   76.10600  -7.07900  1.000 57.68221  ?  497  LYS   B CB  1 
ATOM   17885 C  CG  . LYS   B 1 497  ? 32.34400   76.08600  -7.41600  1.000 45.24880  ?  497  LYS   B CG  1 
ATOM   17886 C  CD  . LYS   B 1 497  ? 32.85300   74.66100  -7.57200  1.000 46.11163  ?  497  LYS   B CD  1 
ATOM   17887 C  CE  . LYS   B 1 497  ? 34.34200   74.63600  -7.87000  1.000 65.19069  ?  497  LYS   B CE  1 
ATOM   17888 N  NZ  . LYS   B 1 497  ? 34.74400   73.39400  -8.58800  1.000 67.98151  ?  497  LYS   B NZ  1 
ATOM   17889 N  N   . PRO   B 1 498  ? 30.69500   78.89900  -5.75800  1.000 47.49133  ?  498  PRO   B N   1 
ATOM   17890 C  CA  . PRO   B 1 498  ? 31.41800   80.05600  -5.21600  1.000 56.86622  ?  498  PRO   B CA  1 
ATOM   17891 C  C   . PRO   B 1 498  ? 32.92500   79.88700  -5.35600  1.000 62.23998  ?  498  PRO   B C   1 
ATOM   17892 O  O   . PRO   B 1 498  ? 33.46200   78.78400  -5.23800  1.000 70.39683  ?  498  PRO   B O   1 
ATOM   17893 C  CB  . PRO   B 1 498  ? 30.98900   80.08600  -3.74500  1.000 50.27756  ?  498  PRO   B CB  1 
ATOM   17894 C  CG  . PRO   B 1 498  ? 29.67600   79.39200  -3.72200  1.000 54.08629  ?  498  PRO   B CG  1 
ATOM   17895 C  CD  . PRO   B 1 498  ? 29.76800   78.32200  -4.76800  1.000 40.86243  ?  498  PRO   B CD  1 
ATOM   17896 N  N   . TYR   B 1 499  ? 33.60500   81.00100  -5.61800  1.000 52.83682  ?  499  TYR   B N   1 
ATOM   17897 C  CA  . TYR   B 1 499  ? 35.05800   81.04700  -5.67100  1.000 43.60905  ?  499  TYR   B CA  1 
ATOM   17898 C  C   . TYR   B 1 499  ? 35.55300   82.25600  -4.89300  1.000 38.96054  ?  499  TYR   B C   1 
ATOM   17899 O  O   . TYR   B 1 499  ? 34.86900   83.28000  -4.80700  1.000 45.94696  ?  499  TYR   B O   1 
ATOM   17900 C  CB  . TYR   B 1 499  ? 35.58500   81.13600  -7.11200  1.000 42.25034  ?  499  TYR   B CB  1 
ATOM   17901 C  CG  . TYR   B 1 499  ? 35.31800   79.92300  -7.97000  1.000 46.30940  ?  499  TYR   B CG  1 
ATOM   17902 C  CD1 . TYR   B 1 499  ? 36.20800   78.85700  -7.99600  1.000 47.98025  ?  499  TYR   B CD1 1 
ATOM   17903 C  CD2 . TYR   B 1 499  ? 34.18900   79.85300  -8.77200  1.000 43.64953  ?  499  TYR   B CD2 1 
ATOM   17904 C  CE1 . TYR   B 1 499  ? 35.97100   77.74900  -8.78800  1.000 49.26459  ?  499  TYR   B CE1 1 
ATOM   17905 C  CE2 . TYR   B 1 499  ? 33.94300   78.75000  -9.56500  1.000 48.17159  ?  499  TYR   B CE2 1 
ATOM   17906 C  CZ  . TYR   B 1 499  ? 34.83600   77.70100  -9.57100  1.000 45.30037  ?  499  TYR   B CZ  1 
ATOM   17907 O  OH  . TYR   B 1 499  ? 34.59000   76.60300  -10.36400 1.000 56.16730  ?  499  TYR   B OH  1 
ATOM   17908 N  N   . ALA   B 1 500  ? 36.75200   82.13000  -4.32200  1.000 34.90887  ?  500  ALA   B N   1 
ATOM   17909 C  CA  . ALA   B 1 500  ? 37.41300   83.30300  -3.76200  1.000 37.85928  ?  500  ALA   B CA  1 
ATOM   17910 C  C   . ALA   B 1 500  ? 37.79200   84.28100  -4.86500  1.000 47.31622  ?  500  ALA   B C   1 
ATOM   17911 O  O   . ALA   B 1 500  ? 37.58500   85.49300  -4.73100  1.000 48.31631  ?  500  ALA   B O   1 
ATOM   17912 C  CB  . ALA   B 1 500  ? 38.64400   82.88600  -2.95900  1.000 50.91079  ?  500  ALA   B CB  1 
ATOM   17913 N  N   . ASN   B 1 501  ? 38.34700   83.76900  -5.96200  1.000 45.29690  ?  501  ASN   B N   1 
ATOM   17914 C  CA  . ASN   B 1 501  ? 38.57700   84.53700  -7.18100  1.000 41.92916  ?  501  ASN   B CA  1 
ATOM   17915 C  C   . ASN   B 1 501  ? 37.92700   83.77000  -8.32500  1.000 51.37389  ?  501  ASN   B C   1 
ATOM   17916 O  O   . ASN   B 1 501  ? 38.44900   82.73600  -8.75600  1.000 42.04567  ?  501  ASN   B O   1 
ATOM   17917 C  CB  . ASN   B 1 501  ? 40.07000   84.74800  -7.43900  1.000 40.86927  ?  501  ASN   B CB  1 
ATOM   17918 C  CG  . ASN   B 1 501  ? 40.33500   85.68200  -8.60700  1.000 49.48487  ?  501  ASN   B CG  1 
ATOM   17919 O  OD1 . ASN   B 1 501  ? 40.19300   85.30000  -9.77000  1.000 42.85715  ?  501  ASN   B OD1 1 
ATOM   17920 N  ND2 . ASN   B 1 501  ? 40.72900   86.91300  -8.30200  1.000 48.95997  ?  501  ASN   B ND2 1 
ATOM   17921 N  N   . ILE   B 1 502  ? 36.78700   84.26300  -8.80000  1.000 39.77864  ?  502  ILE   B N   1 
ATOM   17922 C  CA  . ILE   B 1 502  ? 36.05500   83.61000  -9.88200  1.000 37.43927  ?  502  ILE   B CA  1 
ATOM   17923 C  C   . ILE   B 1 502  ? 36.92400   83.62600  -11.13400 1.000 40.33773  ?  502  ILE   B C   1 
ATOM   17924 O  O   . ILE   B 1 502  ? 37.32500   84.70500  -11.59700 1.000 39.20369  ?  502  ILE   B O   1 
ATOM   17925 C  CB  . ILE   B 1 502  ? 34.70100   84.28700  -10.13800 1.000 37.97842  ?  502  ILE   B CB  1 
ATOM   17926 C  CG1 . ILE   B 1 502  ? 33.95800   84.50700  -8.82100  1.000 39.02388  ?  502  ILE   B CG1 1 
ATOM   17927 C  CG2 . ILE   B 1 502  ? 33.85800   83.44100  -11.08100 1.000 35.21627  ?  502  ILE   B CG2 1 
ATOM   17928 C  CD1 . ILE   B 1 502  ? 32.61100   85.17300  -8.98900  1.000 39.39035  ?  502  ILE   B CD1 1 
ATOM   17929 N  N   . PRO   B 1 503  ? 37.24200   82.46600  -11.70500 1.000 35.22764  ?  503  PRO   B N   1 
ATOM   17930 C  CA  . PRO   B 1 503  ? 38.14900   82.43600  -12.85700 1.000 45.08945  ?  503  PRO   B CA  1 
ATOM   17931 C  C   . PRO   B 1 503  ? 37.55100   83.13900  -14.06600 1.000 46.61677  ?  503  PRO   B C   1 
ATOM   17932 O  O   . PRO   B 1 503  ? 36.33400   83.16300  -14.26400 1.000 35.37555  ?  503  PRO   B O   1 
ATOM   17933 C  CB  . PRO   B 1 503  ? 38.33500   80.93600  -13.12400 1.000 33.73148  ?  503  PRO   B CB  1 
ATOM   17934 C  CG  . PRO   B 1 503  ? 37.94600   80.26300  -11.84500 1.000 38.58507  ?  503  PRO   B CG  1 
ATOM   17935 C  CD  . PRO   B 1 503  ? 36.86800   81.11600  -11.25600 1.000 34.32477  ?  503  PRO   B CD  1 
ATOM   17936 N  N   . ILE   B 1 504  ? 38.43500   83.72700  -14.87900 1.000 45.51611  ?  504  ILE   B N   1 
ATOM   17937 C  CA  . ILE   B 1 504  ? 38.00900   84.30700  -16.15100 1.000 27.84343  ?  504  ILE   B CA  1 
ATOM   17938 C  C   . ILE   B 1 504  ? 37.85800   83.25900  -17.23800 1.000 34.05883  ?  504  ILE   B C   1 
ATOM   17939 O  O   . ILE   B 1 504  ? 37.34900   83.57400  -18.32100 1.000 47.75854  ?  504  ILE   B O   1 
ATOM   17940 C  CB  . ILE   B 1 504  ? 38.98000   85.40500  -16.62300 1.000 34.07243  ?  504  ILE   B CB  1 
ATOM   17941 C  CG1 . ILE   B 1 504  ? 40.41500   84.87700  -16.66300 1.000 47.72432  ?  504  ILE   B CG1 1 
ATOM   17942 C  CG2 . ILE   B 1 504  ? 38.87900   86.62700  -15.72300 1.000 33.24448  ?  504  ILE   B CG2 1 
ATOM   17943 C  CD1 . ILE   B 1 504  ? 41.43700   85.92500  -17.05100 1.000 39.09383  ?  504  ILE   B CD1 1 
ATOM   17944 N  N   . GLY   B 1 505  ? 38.29000   82.03000  -16.98800 1.000 30.75641  ?  505  GLY   B N   1 
ATOM   17945 C  CA  . GLY   B 1 505  ? 37.95600   80.90800  -17.84000 1.000 30.91714  ?  505  GLY   B CA  1 
ATOM   17946 C  C   . GLY   B 1 505  ? 39.06400   80.47900  -18.77900 1.000 43.07180  ?  505  GLY   B C   1 
ATOM   17947 O  O   . GLY   B 1 505  ? 40.25100   80.75400  -18.58400 1.000 40.83702  ?  505  GLY   B O   1 
ATOM   17948 N  N   . LYS   B 1 506  ? 38.64700   79.77700  -19.82400 1.000 37.22418  ?  506  LYS   B N   1 
ATOM   17949 C  CA  . LYS   B 1 506  ? 39.51100   79.20700  -20.84100 1.000 37.74729  ?  506  LYS   B CA  1 
ATOM   17950 C  C   . LYS   B 1 506  ? 39.40800   79.99300  -22.14400 1.000 48.27584  ?  506  LYS   B C   1 
ATOM   17951 O  O   . LYS   B 1 506  ? 38.40300   80.66400  -22.40000 1.000 35.78625  ?  506  LYS   B O   1 
ATOM   17952 C  CB  . LYS   B 1 506  ? 39.13900   77.73600  -21.08200 1.000 27.58936  ?  506  LYS   B CB  1 
ATOM   17953 C  CG  . LYS   B 1 506  ? 39.60000   76.80700  -19.97100 1.000 34.37475  ?  506  LYS   B CG  1 
ATOM   17954 C  CD  . LYS   B 1 506  ? 38.86200   75.48000  -19.99900 1.000 49.53445  ?  506  LYS   B CD  1 
ATOM   17955 C  CE  . LYS   B 1 506  ? 39.30000   74.58900  -18.84600 1.000 50.86168  ?  506  LYS   B CE  1 
ATOM   17956 N  NZ  . LYS   B 1 506  ? 38.40600   73.40900  -18.67800 1.000 46.97003  ?  506  LYS   B NZ  1 
ATOM   17957 N  N   . PRO   B 1 507  ? 40.44000   79.93800  -22.99100 1.000 48.00340  ?  507  PRO   B N   1 
ATOM   17958 C  CA  . PRO   B 1 507  ? 40.42400   80.72900  -24.22700 1.000 32.43346  ?  507  PRO   B CA  1 
ATOM   17959 C  C   . PRO   B 1 507  ? 39.28900   80.32100  -25.15400 1.000 32.32005  ?  507  PRO   B C   1 
ATOM   17960 O  O   . PRO   B 1 507  ? 38.80500   79.18700  -25.12300 1.000 35.96620  ?  507  PRO   B O   1 
ATOM   17961 C  CB  . PRO   B 1 507  ? 41.78800   80.42600  -24.85900 1.000 32.25648  ?  507  PRO   B CB  1 
ATOM   17962 C  CG  . PRO   B 1 507  ? 42.63700   79.95000  -23.73500 1.000 32.74524  ?  507  PRO   B CG  1 
ATOM   17963 C  CD  . PRO   B 1 507  ? 41.71700   79.22500  -22.81000 1.000 49.51875  ?  507  PRO   B CD  1 
ATOM   17964 N  N   . ILE   B 1 508  ? 38.87000   81.26600  -25.99600 1.000 27.68834  ?  508  ILE   B N   1 
ATOM   17965 C  CA  . ILE   B 1 508  ? 37.80100   81.02000  -26.95800 1.000 39.37654  ?  508  ILE   B CA  1 
ATOM   17966 C  C   . ILE   B 1 508  ? 38.39900   80.42200  -28.22500 1.000 40.73155  ?  508  ILE   B C   1 
ATOM   17967 O  O   . ILE   B 1 508  ? 39.54500   79.96000  -28.22500 1.000 46.69475  ?  508  ILE   B O   1 
ATOM   17968 C  CB  . ILE   B 1 508  ? 37.00900   82.30400  -27.27000 1.000 31.18916  ?  508  ILE   B CB  1 
ATOM   17969 C  CG1 . ILE   B 1 508  ? 37.88600   83.31900  -28.00700 1.000 40.34995  ?  508  ILE   B CG1 1 
ATOM   17970 C  CG2 . ILE   B 1 508  ? 36.45800   82.91200  -25.99100 1.000 25.28875  ?  508  ILE   B CG2 1 
ATOM   17971 C  CD1 . ILE   B 1 508  ? 37.09600   84.39300  -28.72200 1.000 19.89662  ?  508  ILE   B CD1 1 
ATOM   17972 N  N   . ASP   B 1 509  ? 37.62700   80.42900  -29.31100 1.000 34.19400  ?  509  ASP   B N   1 
ATOM   17973 C  CA  . ASP   B 1 509  ? 38.06600   79.81100  -30.55500 1.000 31.71363  ?  509  ASP   B CA  1 
ATOM   17974 C  C   . ASP   B 1 509  ? 39.25700   80.55100  -31.15200 1.000 32.01398  ?  509  ASP   B C   1 
ATOM   17975 O  O   . ASP   B 1 509  ? 39.31100   81.78500  -31.14300 1.000 29.25663  ?  509  ASP   B O   1 
ATOM   17976 C  CB  . ASP   B 1 509  ? 36.92000   79.77700  -31.56400 1.000 37.71799  ?  509  ASP   B CB  1 
ATOM   17977 C  CG  . ASP   B 1 509  ? 36.01500   78.58000  -31.37400 1.000 49.45365  ?  509  ASP   B CG  1 
ATOM   17978 O  OD1 . ASP   B 1 509  ? 36.33900   77.71900  -30.52900 1.000 55.03125  ?  509  ASP   B OD1 1 
ATOM   17979 O  OD2 . ASP   B 1 509  ? 34.98300   78.50000  -32.07200 1.000 52.52944  -1 509  ASP   B OD2 1 
ATOM   17980 N  N   . ARG   B 1 510  ? 40.21000   79.77600  -31.67800 1.000 29.77077  ?  510  ARG   B N   1 
ATOM   17981 C  CA  . ARG   B 1 510  ? 41.40300   80.30400  -32.34500 1.000 31.20983  ?  510  ARG   B CA  1 
ATOM   17982 C  C   . ARG   B 1 510  ? 42.11000   81.34100  -31.47800 1.000 32.62725  ?  510  ARG   B C   1 
ATOM   17983 O  O   . ARG   B 1 510  ? 42.63500   82.34400  -31.96800 1.000 33.03814  ?  510  ARG   B O   1 
ATOM   17984 C  CB  . ARG   B 1 510  ? 41.05200   80.87900  -33.71800 1.000 27.35157  ?  510  ARG   B CB  1 
ATOM   17985 C  CG  . ARG   B 1 510  ? 40.39800   79.87100  -34.64700 1.000 34.03884  ?  510  ARG   B CG  1 
ATOM   17986 C  CD  . ARG   B 1 510  ? 40.03500   80.48900  -35.98700 1.000 52.24537  ?  510  ARG   B CD  1 
ATOM   17987 N  NE  . ARG   B 1 510  ? 39.19000   79.59800  -36.77400 1.000 66.95148  ?  510  ARG   B NE  1 
ATOM   17988 C  CZ  . ARG   B 1 510  ? 37.86500   79.64300  -36.78700 1.000 63.00536  ?  510  ARG   B CZ  1 
ATOM   17989 N  NH1 . ARG   B 1 510  ? 37.19700   80.54700  -36.08800 1.000 51.68656  ?  510  ARG   B NH1 1 
ATOM   17990 N  NH2 . ARG   B 1 510  ? 37.19300   78.76000  -37.52000 1.000 68.92717  ?  510  ARG   B NH2 1 
ATOM   17991 N  N   . THR   B 1 511  ? 42.12200   81.09200  -30.17100 1.000 34.67618  ?  511  THR   B N   1 
ATOM   17992 C  CA  . THR   B 1 511  ? 42.69800   82.00200  -29.19200 1.000 34.68752  ?  511  THR   B CA  1 
ATOM   17993 C  C   . THR   B 1 511  ? 43.55300   81.20100  -28.22400 1.000 36.11436  ?  511  THR   B C   1 
ATOM   17994 O  O   . THR   B 1 511  ? 43.13400   80.13800  -27.75300 1.000 29.96826  ?  511  THR   B O   1 
ATOM   17995 C  CB  . THR   B 1 511  ? 41.60100   82.76400  -28.43700 1.000 37.74334  ?  511  THR   B CB  1 
ATOM   17996 O  OG1 . THR   B 1 511  ? 40.86800   83.58600  -29.35500 1.000 38.50357  ?  511  THR   B OG1 1 
ATOM   17997 C  CG2 . THR   B 1 511  ? 42.20300   83.63900  -27.34800 1.000 39.51208  ?  511  THR   B CG2 1 
ATOM   17998 N  N   . ARG   B 1 512  ? 44.75200   81.70300  -27.93700 1.000 38.33788  ?  512  ARG   B N   1 
ATOM   17999 C  CA  . ARG   B 1 512  ? 45.67100   81.05600  -27.01300 1.000 23.11279  ?  512  ARG   B CA  1 
ATOM   18000 C  C   . ARG   B 1 512  ? 46.16700   82.08400  -26.00900 1.000 34.38325  ?  512  ARG   B C   1 
ATOM   18001 O  O   . ARG   B 1 512  ? 46.54500   83.19600  -26.38900 1.000 44.91704  ?  512  ARG   B O   1 
ATOM   18002 C  CB  . ARG   B 1 512  ? 46.84600   80.41600  -27.76100 1.000 22.80646  ?  512  ARG   B CB  1 
ATOM   18003 C  CG  . ARG   B 1 512  ? 46.95300   78.91600  -27.54500 1.000 37.91897  ?  512  ARG   B CG  1 
ATOM   18004 C  CD  . ARG   B 1 512  ? 47.81200   78.23500  -28.60400 1.000 58.89385  ?  512  ARG   B CD  1 
ATOM   18005 N  NE  . ARG   B 1 512  ? 49.12100   78.85900  -28.75500 1.000 70.43786  ?  512  ARG   B NE  1 
ATOM   18006 C  CZ  . ARG   B 1 512  ? 49.59900   79.32900  -29.89900 1.000 74.72276  ?  512  ARG   B CZ  1 
ATOM   18007 N  NH1 . ARG   B 1 512  ? 48.90900   79.24000  -31.02500 1.000 66.72591  ?  512  ARG   B NH1 1 
ATOM   18008 N  NH2 . ARG   B 1 512  ? 50.80300   79.89300  -29.91600 1.000 53.84021  ?  512  ARG   B NH2 1 
ATOM   18009 N  N   . ILE   B 1 513  ? 46.15300   81.71300  -24.73100 1.000 39.86462  ?  513  ILE   B N   1 
ATOM   18010 C  CA  . ILE   B 1 513  ? 46.58400   82.58200  -23.64200 1.000 39.96548  ?  513  ILE   B CA  1 
ATOM   18011 C  C   . ILE   B 1 513  ? 47.91400   82.06900  -23.11000 1.000 42.88612  ?  513  ILE   B C   1 
ATOM   18012 O  O   . ILE   B 1 513  ? 48.10000   80.85800  -22.93700 1.000 51.56604  ?  513  ILE   B O   1 
ATOM   18013 C  CB  . ILE   B 1 513  ? 45.52800   82.64600  -22.52200 1.000 40.69017  ?  513  ILE   B CB  1 
ATOM   18014 C  CG1 . ILE   B 1 513  ? 44.18400   83.12300  -23.07900 1.000 31.95057  ?  513  ILE   B CG1 1 
ATOM   18015 C  CG2 . ILE   B 1 513  ? 45.99400   83.55800  -21.39600 1.000 43.50589  ?  513  ILE   B CG2 1 
ATOM   18016 C  CD1 . ILE   B 1 513  ? 44.17600   84.57300  -23.50500 1.000 41.43345  ?  513  ILE   B CD1 1 
ATOM   18017 N  N   . LEU   B 1 514  ? 48.84100   82.99000  -22.85500 1.000 34.76763  ?  514  LEU   B N   1 
ATOM   18018 C  CA  . LEU   B 1 514  ? 50.17600   82.65200  -22.38200 1.000 39.50018  ?  514  LEU   B CA  1 
ATOM   18019 C  C   . LEU   B 1 514  ? 50.53000   83.52600  -21.18900 1.000 42.06663  ?  514  LEU   B C   1 
ATOM   18020 O  O   . LEU   B 1 514  ? 50.37000   84.75000  -21.24300 1.000 37.32705  ?  514  LEU   B O   1 
ATOM   18021 C  CB  . LEU   B 1 514  ? 51.21600   82.83100  -23.49200 1.000 38.60261  ?  514  LEU   B CB  1 
ATOM   18022 C  CG  . LEU   B 1 514  ? 51.06500   81.89600  -24.69000 1.000 38.59474  ?  514  LEU   B CG  1 
ATOM   18023 C  CD1 . LEU   B 1 514  ? 52.00500   82.30300  -25.80200 1.000 26.41707  ?  514  LEU   B CD1 1 
ATOM   18024 C  CD2 . LEU   B 1 514  ? 51.33100   80.46700  -24.27100 1.000 51.99899  ?  514  LEU   B CD2 1 
ATOM   18025 N  N   . ILE   B 1 515  ? 51.01200   82.89700  -20.12300 1.000 42.48421  ?  515  ILE   B N   1 
ATOM   18026 C  CA  . ILE   B 1 515  ? 51.46100   83.59600  -18.92500 1.000 45.90004  ?  515  ILE   B CA  1 
ATOM   18027 C  C   . ILE   B 1 515  ? 52.97800   83.71100  -19.00600 1.000 41.79758  ?  515  ILE   B C   1 
ATOM   18028 O  O   . ILE   B 1 515  ? 53.69500   82.71900  -18.84000 1.000 39.13607  ?  515  ILE   B O   1 
ATOM   18029 C  CB  . ILE   B 1 515  ? 51.02100   82.87100  -17.64600 1.000 38.46032  ?  515  ILE   B CB  1 
ATOM   18030 C  CG1 . ILE   B 1 515  ? 49.50000   82.71600  -17.61700 1.000 47.01564  ?  515  ILE   B CG1 1 
ATOM   18031 C  CG2 . ILE   B 1 515  ? 51.50000   83.62200  -16.41600 1.000 37.22744  ?  515  ILE   B CG2 1 
ATOM   18032 C  CD1 . ILE   B 1 515  ? 48.74900   84.02700  -17.68000 1.000 39.08490  ?  515  ILE   B CD1 1 
ATOM   18033 N  N   . LEU   B 1 516  ? 53.47000   84.91900  -19.26200 1.000 40.38921  ?  516  LEU   B N   1 
ATOM   18034 C  CA  . LEU   B 1 516  ? 54.89400   85.16700  -19.42400 1.000 48.77762  ?  516  LEU   B CA  1 
ATOM   18035 C  C   . LEU   B 1 516  ? 55.42800   85.99700  -18.26300 1.000 52.40630  ?  516  LEU   B C   1 
ATOM   18036 O  O   . LEU   B 1 516  ? 54.68300   86.69600  -17.57000 1.000 56.64252  ?  516  LEU   B O   1 
ATOM   18037 C  CB  . LEU   B 1 516  ? 55.17800   85.88100  -20.75000 1.000 45.10166  ?  516  LEU   B CB  1 
ATOM   18038 C  CG  . LEU   B 1 516  ? 54.68100   85.18500  -22.01800 1.000 34.09180  ?  516  LEU   B CG  1 
ATOM   18039 C  CD1 . LEU   B 1 516  ? 55.17300   85.92200  -23.25200 1.000 25.42153  ?  516  LEU   B CD1 1 
ATOM   18040 C  CD2 . LEU   B 1 516  ? 55.11500   83.72600  -22.04100 1.000 31.96193  ?  516  LEU   B CD2 1 
ATOM   18041 N  N   . ASP   B 1 517  ? 56.74100   85.91200  -18.06100 1.000 39.07819  ?  517  ASP   B N   1 
ATOM   18042 C  CA  . ASP   B 1 517  ? 57.41200   86.66700  -17.01300 1.000 52.70672  ?  517  ASP   B CA  1 
ATOM   18043 C  C   . ASP   B 1 517  ? 57.77400   88.05400  -17.54900 1.000 61.44932  ?  517  ASP   B C   1 
ATOM   18044 O  O   . ASP   B 1 517  ? 57.13600   88.56200  -18.47500 1.000 60.54030  ?  517  ASP   B O   1 
ATOM   18045 C  CB  . ASP   B 1 517  ? 58.63000   85.88600  -16.50500 1.000 44.42231  ?  517  ASP   B CB  1 
ATOM   18046 C  CG  . ASP   B 1 517  ? 59.63000   85.57100  -17.60500 1.000 60.54154  ?  517  ASP   B CG  1 
ATOM   18047 O  OD1 . ASP   B 1 517  ? 59.36700   85.90900  -18.77900 1.000 59.63808  ?  517  ASP   B OD1 1 
ATOM   18048 O  OD2 . ASP   B 1 517  ? 60.68600   84.98100  -17.29200 1.000 62.57550  -1 517  ASP   B OD2 1 
ATOM   18049 N  N   . GLU   B 1 518  ? 58.80000   88.68300  -16.97400 1.000 51.22293  ?  518  GLU   B N   1 
ATOM   18050 C  CA  . GLU   B 1 518  ? 59.24300   89.98800  -17.44800 1.000 54.19619  ?  518  GLU   B CA  1 
ATOM   18051 C  C   . GLU   B 1 518  ? 60.09400   89.89600  -18.70800 1.000 51.59464  ?  518  GLU   B C   1 
ATOM   18052 O  O   . GLU   B 1 518  ? 60.23400   90.89800  -19.41800 1.000 41.11407  ?  518  GLU   B O   1 
ATOM   18053 C  CB  . GLU   B 1 518  ? 60.02700   90.70900  -16.35000 1.000 45.66930  ?  518  GLU   B CB  1 
ATOM   18054 C  CG  . GLU   B 1 518  ? 59.16400   91.29500  -15.24500 1.000 52.64670  ?  518  GLU   B CG  1 
ATOM   18055 C  CD  . GLU   B 1 518  ? 59.00900   92.80000  -15.36300 1.000 90.49109  ?  518  GLU   B CD  1 
ATOM   18056 O  OE1 . GLU   B 1 518  ? 59.99300   93.47200  -15.73700 1.000 97.25052  ?  518  GLU   B OE1 1 
ATOM   18057 O  OE2 . GLU   B 1 518  ? 57.90300   93.31100  -15.08200 1.000 118.19003 -1 518  GLU   B OE2 1 
ATOM   18058 N  N   . ALA   B 1 519  ? 60.65900   88.72500  -19.00000 1.000 51.44111  ?  519  ALA   B N   1 
ATOM   18059 C  CA  . ALA   B 1 519  ? 61.48900   88.52000  -20.18000 1.000 35.75164  ?  519  ALA   B CA  1 
ATOM   18060 C  C   . ALA   B 1 519  ? 60.79300   87.64900  -21.22000 1.000 47.98698  ?  519  ALA   B C   1 
ATOM   18061 O  O   . ALA   B 1 519  ? 61.45300   86.97300  -22.01400 1.000 52.77590  ?  519  ALA   B O   1 
ATOM   18062 C  CB  . ALA   B 1 519  ? 62.83500   87.91200  -19.78900 1.000 44.41556  ?  519  ALA   B CB  1 
ATOM   18063 N  N   . LEU   B 1 520  ? 59.45800   87.65100  -21.21400 1.000 49.41432  ?  520  LEU   B N   1 
ATOM   18064 C  CA  . LEU   B 1 520  ? 58.65000   86.96100  -22.22300 1.000 40.93825  ?  520  LEU   B CA  1 
ATOM   18065 C  C   . LEU   B 1 520  ? 58.95700   85.46500  -22.26700 1.000 43.56567  ?  520  LEU   B C   1 
ATOM   18066 O  O   . LEU   B 1 520  ? 59.00900   84.85500  -23.33600 1.000 58.97606  ?  520  LEU   B O   1 
ATOM   18067 C  CB  . LEU   B 1 520  ? 58.83800   87.59300  -23.60500 1.000 35.59668  ?  520  LEU   B CB  1 
ATOM   18068 C  CG  . LEU   B 1 520  ? 58.80400   89.12200  -23.66400 1.000 40.24263  ?  520  LEU   B CG  1 
ATOM   18069 C  CD1 . LEU   B 1 520  ? 59.01100   89.61300  -25.08800 1.000 43.82788  ?  520  LEU   B CD1 1 
ATOM   18070 C  CD2 . LEU   B 1 520  ? 57.50600   89.66300  -23.08900 1.000 26.21178  ?  520  LEU   B CD2 1 
ATOM   18071 N  N   . ALA   B 1 521  ? 59.16300   84.86900  -21.09600 1.000 49.07678  ?  521  ALA   B N   1 
ATOM   18072 C  CA  . ALA   B 1 521  ? 59.43700   83.44600  -20.97700 1.000 53.24913  ?  521  ALA   B CA  1 
ATOM   18073 C  C   . ALA   B 1 521  ? 58.23900   82.73300  -20.36400 1.000 51.04859  ?  521  ALA   B C   1 
ATOM   18074 O  O   . ALA   B 1 521  ? 57.51900   83.29200  -19.53200 1.000 39.81134  ?  521  ALA   B O   1 
ATOM   18075 C  CB  . ALA   B 1 521  ? 60.68700   83.19200  -20.12900 1.000 38.40461  ?  521  ALA   B CB  1 
ATOM   18076 N  N   . LEU   B 1 522  ? 58.03400   81.48800  -20.78400 1.000 42.66626  ?  522  LEU   B N   1 
ATOM   18077 C  CA  . LEU   B 1 522  ? 56.87600   80.72600  -20.33700 1.000 44.86467  ?  522  LEU   B CA  1 
ATOM   18078 C  C   . LEU   B 1 522  ? 56.98500   80.41700  -18.84700 1.000 54.28545  ?  522  LEU   B C   1 
ATOM   18079 O  O   . LEU   B 1 522  ? 57.98700   79.86200  -18.38600 1.000 56.53090  ?  522  LEU   B O   1 
ATOM   18080 C  CB  . LEU   B 1 522  ? 56.75300   79.43500  -21.14400 1.000 39.38153  ?  522  LEU   B CB  1 
ATOM   18081 C  CG  . LEU   B 1 522  ? 55.37400   78.77800  -21.17500 1.000 42.81786  ?  522  LEU   B CG  1 
ATOM   18082 C  CD1 . LEU   B 1 522  ? 54.32800   79.78100  -21.63400 1.000 46.95031  ?  522  LEU   B CD1 1 
ATOM   18083 C  CD2 . LEU   B 1 522  ? 55.38700   77.56000  -22.08500 1.000 48.67806  ?  522  LEU   B CD2 1 
ATOM   18084 N  N   . GLN   B 1 523  ? 55.95000   80.78900  -18.09400 1.000 45.41953  ?  523  GLN   B N   1 
ATOM   18085 C  CA  . GLN   B 1 523  ? 55.82400   80.54400  -16.66200 1.000 36.45789  ?  523  GLN   B CA  1 
ATOM   18086 C  C   . GLN   B 1 523  ? 55.14100   79.20100  -16.41500 1.000 35.82232  ?  523  GLN   B C   1 
ATOM   18087 O  O   . GLN   B 1 523  ? 54.23100   78.82300  -17.15800 1.000 38.00885  ?  523  GLN   B O   1 
ATOM   18088 C  CB  . GLN   B 1 523  ? 55.01500   81.65300  -15.99200 1.000 29.17533  ?  523  GLN   B CB  1 
ATOM   18089 C  CG  . GLN   B 1 523  ? 55.64800   83.03500  -16.05900 1.000 37.88828  ?  523  GLN   B CG  1 
ATOM   18090 C  CD  . GLN   B 1 523  ? 56.63100   83.28500  -14.93200 1.000 46.17462  ?  523  GLN   B CD  1 
ATOM   18091 O  OE1 . GLN   B 1 523  ? 57.67800   82.64100  -14.84700 1.000 46.20897  ?  523  GLN   B OE1 1 
ATOM   18092 N  NE2 . GLN   B 1 523  ? 56.29500   84.22400  -14.05400 1.000 46.90524  ?  523  GLN   B NE2 1 
ATOM   18093 N  N   . PRO   B 1 524  ? 55.56300   78.46200  -15.39000 1.000 52.53233  ?  524  PRO   B N   1 
ATOM   18094 C  CA  . PRO   B 1 524  ? 54.89700   77.19300  -15.07500 1.000 44.23887  ?  524  PRO   B CA  1 
ATOM   18095 C  C   . PRO   B 1 524  ? 53.45200   77.41600  -14.65700 1.000 46.57649  ?  524  PRO   B C   1 
ATOM   18096 O  O   . PRO   B 1 524  ? 53.05500   78.50800  -14.24300 1.000 47.18842  ?  524  PRO   B O   1 
ATOM   18097 C  CB  . PRO   B 1 524  ? 55.72800   76.62900  -13.91400 1.000 35.49006  ?  524  PRO   B CB  1 
ATOM   18098 C  CG  . PRO   B 1 524  ? 57.03000   77.35400  -13.97500 1.000 28.96495  ?  524  PRO   B CG  1 
ATOM   18099 C  CD  . PRO   B 1 524  ? 56.71800   78.71500  -14.51300 1.000 46.09599  ?  524  PRO   B CD  1 
ATOM   18100 N  N   . ILE   B 1 525  ? 52.65600   76.35000  -14.77600 1.000 31.68531  ?  525  ILE   B N   1 
ATOM   18101 C  CA  . ILE   B 1 525  ? 51.26500   76.41200  -14.34200 1.000 30.72208  ?  525  ILE   B CA  1 
ATOM   18102 C  C   . ILE   B 1 525  ? 51.21800   76.71400  -12.85300 1.000 41.33699  ?  525  ILE   B C   1 
ATOM   18103 O  O   . ILE   B 1 525  ? 51.88800   76.05800  -12.04500 1.000 54.36208  ?  525  ILE   B O   1 
ATOM   18104 C  CB  . ILE   B 1 525  ? 50.53800   75.10100  -14.67600 1.000 34.23748  ?  525  ILE   B CB  1 
ATOM   18105 C  CG1 . ILE   B 1 525  ? 50.34300   74.97200  -16.18800 1.000 40.15723  ?  525  ILE   B CG1 1 
ATOM   18106 C  CG2 . ILE   B 1 525  ? 49.20200   75.02800  -13.95200 1.000 24.13703  ?  525  ILE   B CG2 1 
ATOM   18107 C  CD1 . ILE   B 1 525  ? 49.67200   73.68400  -16.61000 1.000 37.55770  ?  525  ILE   B CD1 1 
ATOM   18108 N  N   . GLY   B 1 526  ? 50.42900   77.72300  -12.48300 1.000 32.14098  ?  526  GLY   B N   1 
ATOM   18109 C  CA  . GLY   B 1 526  ? 50.33500   78.19100  -11.12600 1.000 35.37851  ?  526  GLY   B CA  1 
ATOM   18110 C  C   . GLY   B 1 526  ? 51.15200   79.43700  -10.85100 1.000 36.42413  ?  526  GLY   B C   1 
ATOM   18111 O  O   . GLY   B 1 526  ? 50.77400   80.23900  -9.99000  1.000 51.77895  ?  526  GLY   B O   1 
ATOM   18112 N  N   . VAL   B 1 527  ? 52.25900   79.61700  -11.56400 1.000 32.03408  ?  527  VAL   B N   1 
ATOM   18113 C  CA  . VAL   B 1 527  ? 53.07800   80.81400  -11.41600 1.000 44.36654  ?  527  VAL   B CA  1 
ATOM   18114 C  C   . VAL   B 1 527  ? 52.40000   81.96600  -12.14400 1.000 29.17416  ?  527  VAL   B C   1 
ATOM   18115 O  O   . VAL   B 1 527  ? 51.96300   81.82100  -13.29200 1.000 35.82544  ?  527  VAL   B O   1 
ATOM   18116 C  CB  . VAL   B 1 527  ? 54.49900   80.57200  -11.95100 1.000 42.63834  ?  527  VAL   B CB  1 
ATOM   18117 C  CG1 . VAL   B 1 527  ? 55.35700   81.81700  -11.76900 1.000 20.12645  ?  527  VAL   B CG1 1 
ATOM   18118 C  CG2 . VAL   B 1 527  ? 55.13000   79.37600  -11.25300 1.000 35.70861  ?  527  VAL   B CG2 1 
ATOM   18119 N  N   . ALA   B 1 528  ? 52.30500   83.11100  -11.47600 1.000 27.17414  ?  528  ALA   B N   1 
ATOM   18120 C  CA  . ALA   B 1 528  ? 51.65900   84.27000  -12.06400 1.000 26.57639  ?  528  ALA   B CA  1 
ATOM   18121 C  C   . ALA   B 1 528  ? 52.59000   84.96100  -13.05700 1.000 38.53354  ?  528  ALA   B C   1 
ATOM   18122 O  O   . ALA   B 1 528  ? 53.78700   84.67200  -13.14300 1.000 51.51876  ?  528  ALA   B O   1 
ATOM   18123 C  CB  . ALA   B 1 528  ? 51.22000   85.24900  -10.97700 1.000 32.82121  ?  528  ALA   B CB  1 
ATOM   18124 N  N   . GLY   B 1 529  ? 52.01900   85.89200  -13.81000 1.000 38.56806  ?  529  GLY   B N   1 
ATOM   18125 C  CA  . GLY   B 1 529  ? 52.77500   86.63100  -14.79900 1.000 45.20801  ?  529  GLY   B CA  1 
ATOM   18126 C  C   . GLY   B 1 529  ? 51.84100   87.47600  -15.64100 1.000 48.03408  ?  529  GLY   B C   1 
ATOM   18127 O  O   . GLY   B 1 529  ? 50.64800   87.58700  -15.35200 1.000 60.28506  ?  529  GLY   B O   1 
ATOM   18128 N  N   . GLU   B 1 530  ? 52.40400   88.06500  -16.69200 1.000 54.80034  ?  530  GLU   B N   1 
ATOM   18129 C  CA  . GLU   B 1 530  ? 51.61600   88.89500  -17.59000 1.000 45.14469  ?  530  GLU   B CA  1 
ATOM   18130 C  C   . GLU   B 1 530  ? 50.82900   88.02900  -18.56500 1.000 41.56800  ?  530  GLU   B C   1 
ATOM   18131 O  O   . GLU   B 1 530  ? 51.35800   87.07200  -19.13800 1.000 30.05762  ?  530  GLU   B O   1 
ATOM   18132 C  CB  . GLU   B 1 530  ? 52.51100   89.86600  -18.36100 1.000 44.34627  ?  530  GLU   B CB  1 
ATOM   18133 C  CG  . GLU   B 1 530  ? 51.73700   90.88000  -19.19500 1.000 40.73807  ?  530  GLU   B CG  1 
ATOM   18134 C  CD  . GLU   B 1 530  ? 52.63100   91.92400  -19.83200 1.000 43.08987  ?  530  GLU   B CD  1 
ATOM   18135 O  OE1 . GLU   B 1 530  ? 53.84900   91.67600  -19.94600 1.000 65.57552  ?  530  GLU   B OE1 1 
ATOM   18136 O  OE2 . GLU   B 1 530  ? 52.11600   92.99700  -20.21400 1.000 38.84989  -1 530  GLU   B OE2 1 
ATOM   18137 N  N   . LEU   B 1 531  ? 49.55600   88.37200  -18.74500 1.000 43.21483  ?  531  LEU   B N   1 
ATOM   18138 C  CA  . LEU   B 1 531  ? 48.69300   87.65500  -19.67400 1.000 41.66362  ?  531  LEU   B CA  1 
ATOM   18139 C  C   . LEU   B 1 531  ? 48.94900   88.16000  -21.09000 1.000 36.18127  ?  531  LEU   B C   1 
ATOM   18140 O  O   . LEU   B 1 531  ? 48.83700   89.36100  -21.35900 1.000 36.76019  ?  531  LEU   B O   1 
ATOM   18141 C  CB  . LEU   B 1 531  ? 47.22700   87.83200  -19.28300 1.000 35.39539  ?  531  LEU   B CB  1 
ATOM   18142 C  CG  . LEU   B 1 531  ? 46.20600   86.89800  -19.93900 1.000 32.58702  ?  531  LEU   B CG  1 
ATOM   18143 C  CD1 . LEU   B 1 531  ? 45.07800   86.58000  -18.97200 1.000 39.84521  ?  531  LEU   B CD1 1 
ATOM   18144 C  CD2 . LEU   B 1 531  ? 45.64800   87.50300  -21.21600 1.000 38.24120  ?  531  LEU   B CD2 1 
ATOM   18145 N  N   . PHE   B 1 532  ? 49.30800   87.24300  -21.98500 1.000 36.14430  ?  532  PHE   B N   1 
ATOM   18146 C  CA  . PHE   B 1 532  ? 49.54800   87.53800  -23.38900 1.000 32.60275  ?  532  PHE   B CA  1 
ATOM   18147 C  C   . PHE   B 1 532  ? 48.50600   86.82500  -24.24000 1.000 40.28881  ?  532  PHE   B C   1 
ATOM   18148 O  O   . PHE   B 1 532  ? 48.20600   85.64900  -24.01200 1.000 37.69867  ?  532  PHE   B O   1 
ATOM   18149 C  CB  . PHE   B 1 532  ? 50.95800   87.10300  -23.81600 1.000 36.28517  ?  532  PHE   B CB  1 
ATOM   18150 C  CG  . PHE   B 1 532  ? 52.03400   88.09400  -23.46800 1.000 37.87824  ?  532  PHE   B CG  1 
ATOM   18151 C  CD1 . PHE   B 1 532  ? 52.52200   88.18600  -22.17500 1.000 43.63912  ?  532  PHE   B CD1 1 
ATOM   18152 C  CD2 . PHE   B 1 532  ? 52.56400   88.92800  -24.44000 1.000 41.65104  ?  532  PHE   B CD2 1 
ATOM   18153 C  CE1 . PHE   B 1 532  ? 53.51400   89.09500  -21.85600 1.000 33.66642  ?  532  PHE   B CE1 1 
ATOM   18154 C  CE2 . PHE   B 1 532  ? 53.55600   89.83500  -24.12600 1.000 33.64026  ?  532  PHE   B CE2 1 
ATOM   18155 C  CZ  . PHE   B 1 532  ? 54.02900   89.92200  -22.83200 1.000 33.72573  ?  532  PHE   B CZ  1 
ATOM   18156 N  N   . ILE   B 1 533  ? 47.96400   87.54000  -25.22300 1.000 33.03264  ?  533  ILE   B N   1 
ATOM   18157 C  CA  . ILE   B 1 533  ? 46.91700   87.02400  -26.09700 1.000 42.68817  ?  533  ILE   B CA  1 
ATOM   18158 C  C   . ILE   B 1 533  ? 47.50400   86.81100  -27.48200 1.000 37.78809  ?  533  ILE   B C   1 
ATOM   18159 O  O   . ILE   B 1 533  ? 48.05400   87.74200  -28.08500 1.000 34.10519  ?  533  ILE   B O   1 
ATOM   18160 C  CB  . ILE   B 1 533  ? 45.71000   87.96700  -26.15400 1.000 38.38036  ?  533  ILE   B CB  1 
ATOM   18161 C  CG1 . ILE   B 1 533  ? 45.13100   88.13800  -24.75900 1.000 29.01414  ?  533  ILE   B CG1 1 
ATOM   18162 C  CG2 . ILE   B 1 533  ? 44.64400   87.41200  -27.07900 1.000 35.49223  ?  533  ILE   B CG2 1 
ATOM   18163 C  CD1 . ILE   B 1 533  ? 44.40000   89.43500  -24.58100 1.000 34.87071  ?  533  ILE   B CD1 1 
ATOM   18164 N  N   . VAL   B 1 534  ? 47.38600   85.58400  -27.98200 1.000 36.55483  ?  534  VAL   B N   1 
ATOM   18165 C  CA  . VAL   B 1 534  ? 47.78500   85.22900  -29.33600 1.000 42.26215  ?  534  VAL   B CA  1 
ATOM   18166 C  C   . VAL   B 1 534  ? 46.62000   84.49800  -29.98400 1.000 37.81917  ?  534  VAL   B C   1 
ATOM   18167 O  O   . VAL   B 1 534  ? 46.06100   83.56500  -29.39300 1.000 50.13489  ?  534  VAL   B O   1 
ATOM   18168 C  CB  . VAL   B 1 534  ? 49.06400   84.36200  -29.34800 1.000 36.85273  ?  534  VAL   B CB  1 
ATOM   18169 C  CG1 . VAL   B 1 534  ? 49.24900   83.66400  -28.01700 1.000 34.42070  ?  534  VAL   B CG1 1 
ATOM   18170 C  CG2 . VAL   B 1 534  ? 49.01900   83.34400  -30.48100 1.000 37.09080  ?  534  VAL   B CG2 1 
ATOM   18171 N  N   . GLY   B 1 535  ? 46.23500   84.93500  -31.17400 1.000 30.02751  ?  535  GLY   B N   1 
ATOM   18172 C  CA  . GLY   B 1 535  ? 45.16000   84.28200  -31.88900 1.000 33.78313  ?  535  GLY   B CA  1 
ATOM   18173 C  C   . GLY   B 1 535  ? 44.47500   85.22600  -32.85500 1.000 39.41926  ?  535  GLY   B C   1 
ATOM   18174 O  O   . GLY   B 1 535  ? 44.97300   86.31100  -33.16300 1.000 28.70003  ?  535  GLY   B O   1 
ATOM   18175 N  N   . GLU   B 1 536  ? 43.30900   84.77800  -33.32100 1.000 37.79312  ?  536  GLU   B N   1 
ATOM   18176 C  CA  . GLU   B 1 536  ? 42.52300   85.48100  -34.33100 1.000 37.96380  ?  536  GLU   B CA  1 
ATOM   18177 C  C   . GLU   B 1 536  ? 41.75100   86.67000  -33.77800 1.000 31.99164  ?  536  GLU   B C   1 
ATOM   18178 O  O   . GLU   B 1 536  ? 41.07300   87.35900  -34.54900 1.000 37.96550  ?  536  GLU   B O   1 
ATOM   18179 C  CB  . GLU   B 1 536  ? 41.55100   84.50500  -35.00100 1.000 27.58087  ?  536  GLU   B CB  1 
ATOM   18180 C  CG  . GLU   B 1 536  ? 42.14100   83.73500  -36.17500 1.000 29.37014  ?  536  GLU   B CG  1 
ATOM   18181 C  CD  . GLU   B 1 536  ? 41.75700   84.33200  -37.51900 1.000 30.53888  ?  536  GLU   B CD  1 
ATOM   18182 O  OE1 . GLU   B 1 536  ? 41.27900   85.48500  -37.54700 1.000 34.16424  ?  536  GLU   B OE1 1 
ATOM   18183 O  OE2 . GLU   B 1 536  ? 41.92600   83.64300  -38.54700 1.000 56.21803  -1 536  GLU   B OE2 1 
ATOM   18184 N  N   . GLY   B 1 537  ? 41.82800   86.93100  -32.47200 1.000 20.81245  ?  537  GLY   B N   1 
ATOM   18185 C  CA  . GLY   B 1 537  ? 41.11500   88.06900  -31.92200 1.000 23.98508  ?  537  GLY   B CA  1 
ATOM   18186 C  C   . GLY   B 1 537  ? 41.87800   89.37200  -31.97100 1.000 28.51081  ?  537  GLY   B C   1 
ATOM   18187 O  O   . GLY   B 1 537  ? 41.27700   90.43500  -31.79600 1.000 36.19047  ?  537  GLY   B O   1 
ATOM   18188 N  N   . LEU   B 1 538  ? 43.18600   89.31600  -32.21400 1.000 29.38792  ?  538  LEU   B N   1 
ATOM   18189 C  CA  . LEU   B 1 538  ? 44.01500   90.51300  -32.16900 1.000 30.19498  ?  538  LEU   B CA  1 
ATOM   18190 C  C   . LEU   B 1 538  ? 43.69000   91.43700  -33.33400 1.000 31.62015  ?  538  LEU   B C   1 
ATOM   18191 O  O   . LEU   B 1 538  ? 43.68700   91.01700  -34.49600 1.000 32.53811  ?  538  LEU   B O   1 
ATOM   18192 C  CB  . LEU   B 1 538  ? 45.49700   90.13800  -32.19500 1.000 42.08566  ?  538  LEU   B CB  1 
ATOM   18193 C  CG  . LEU   B 1 538  ? 46.14600   89.68200  -30.88400 1.000 44.40455  ?  538  LEU   B CG  1 
ATOM   18194 C  CD1 . LEU   B 1 538  ? 45.71400   88.27300  -30.51000 1.000 45.13543  ?  538  LEU   B CD1 1 
ATOM   18195 C  CD2 . LEU   B 1 538  ? 47.66200   89.77300  -30.97700 1.000 42.38829  ?  538  LEU   B CD2 1 
ATOM   18196 N  N   . GLY   B 1 539  ? 43.42000   92.70300  -33.01900 1.000 28.64689  ?  539  GLY   B N   1 
ATOM   18197 C  CA  . GLY   B 1 539  ? 43.14200   93.69700  -34.03100 1.000 33.00454  ?  539  GLY   B CA  1 
ATOM   18198 C  C   . GLY   B 1 539  ? 44.39600   94.16000  -34.74900 1.000 37.56870  ?  539  GLY   B C   1 
ATOM   18199 O  O   . GLY   B 1 539  ? 45.50900   93.69900  -34.49800 1.000 45.30904  ?  539  GLY   B O   1 
ATOM   18200 N  N   . ARG   B 1 540  ? 44.19800   95.10900  -35.66600 1.000 36.82017  ?  540  ARG   B N   1 
ATOM   18201 C  CA  . ARG   B 1 540  ? 45.31500   95.59300  -36.47100 1.000 35.83665  ?  540  ARG   B CA  1 
ATOM   18202 C  C   . ARG   B 1 540  ? 46.25400   96.48100  -35.66200 1.000 35.85619  ?  540  ARG   B C   1 
ATOM   18203 O  O   . ARG   B 1 540  ? 47.46600   96.48100  -35.90600 1.000 45.36658  ?  540  ARG   B O   1 
ATOM   18204 C  CB  . ARG   B 1 540  ? 44.79300   96.34400  -37.69600 1.000 27.41606  ?  540  ARG   B CB  1 
ATOM   18205 C  CG  . ARG   B 1 540  ? 45.84100   96.58600  -38.76800 1.000 39.40281  ?  540  ARG   B CG  1 
ATOM   18206 C  CD  . ARG   B 1 540  ? 45.29900   97.46200  -39.88300 1.000 33.78615  ?  540  ARG   B CD  1 
ATOM   18207 N  NE  . ARG   B 1 540  ? 44.22800   96.81300  -40.62800 1.000 22.90004  ?  540  ARG   B NE  1 
ATOM   18208 C  CZ  . ARG   B 1 540  ? 43.52900   97.40000  -41.58900 1.000 42.58967  ?  540  ARG   B CZ  1 
ATOM   18209 N  NH1 . ARG   B 1 540  ? 43.75800   98.65400  -41.94100 1.000 39.11480  ?  540  ARG   B NH1 1 
ATOM   18210 N  NH2 . ARG   B 1 540  ? 42.57400   96.71200  -42.21000 1.000 47.56140  ?  540  ARG   B NH2 1 
ATOM   18211 N  N   . GLY   B 1 541  ? 45.72700   97.23400  -34.70500 1.000 36.51835  ?  541  GLY   B N   1 
ATOM   18212 C  CA  . GLY   B 1 541  ? 46.52900   98.09000  -33.86200 1.000 25.93667  ?  541  GLY   B CA  1 
ATOM   18213 C  C   . GLY   B 1 541  ? 45.81800   99.39800  -33.59400 1.000 30.00226  ?  541  GLY   B C   1 
ATOM   18214 O  O   . GLY   B 1 541  ? 44.63400   99.55900  -33.88300 1.000 40.16692  ?  541  GLY   B O   1 
ATOM   18215 N  N   . TYR   B 1 542  ? 46.56100   100.34700 -33.03000 1.000 36.98234  ?  542  TYR   B N   1 
ATOM   18216 C  CA  . TYR   B 1 542  ? 46.01600   101.65100 -32.68500 1.000 37.53883  ?  542  TYR   B CA  1 
ATOM   18217 C  C   . TYR   B 1 542  ? 46.08100   102.59300 -33.88000 1.000 38.30359  ?  542  TYR   B C   1 
ATOM   18218 O  O   . TYR   B 1 542  ? 47.06300   102.60300 -34.62900 1.000 43.78858  ?  542  TYR   B O   1 
ATOM   18219 C  CB  . TYR   B 1 542  ? 46.77100   102.25600 -31.50100 1.000 34.90885  ?  542  TYR   B CB  1 
ATOM   18220 C  CG  . TYR   B 1 542  ? 46.71200   101.41700 -30.24400 1.000 49.28452  ?  542  TYR   B CG  1 
ATOM   18221 C  CD1 . TYR   B 1 542  ? 45.53600   101.30700 -29.51200 1.000 43.25644  ?  542  TYR   B CD1 1 
ATOM   18222 C  CD2 . TYR   B 1 542  ? 47.83500   100.74000 -29.78400 1.000 33.34036  ?  542  TYR   B CD2 1 
ATOM   18223 C  CE1 . TYR   B 1 542  ? 45.47700   100.54200 -28.36100 1.000 42.44779  ?  542  TYR   B CE1 1 
ATOM   18224 C  CE2 . TYR   B 1 542  ? 47.78700   99.97400  -28.63300 1.000 28.30843  ?  542  TYR   B CE2 1 
ATOM   18225 C  CZ  . TYR   B 1 542  ? 46.60600   99.87900  -27.92600 1.000 45.48062  ?  542  TYR   B CZ  1 
ATOM   18226 O  OH  . TYR   B 1 542  ? 46.55400   99.11700  -26.78000 1.000 45.63642  ?  542  TYR   B OH  1 
ATOM   18227 N  N   . LEU   B 1 543  ? 45.02700   103.38600 -34.05000 1.000 41.63776  ?  543  LEU   B N   1 
ATOM   18228 C  CA  . LEU   B 1 543  ? 44.96500   104.32800 -35.15800 1.000 32.40075  ?  543  LEU   B CA  1 
ATOM   18229 C  C   . LEU   B 1 543  ? 45.93900   105.47700 -34.92600 1.000 29.18502  ?  543  LEU   B C   1 
ATOM   18230 O  O   . LEU   B 1 543  ? 45.90800   106.12800 -33.87700 1.000 43.08086  ?  543  LEU   B O   1 
ATOM   18231 C  CB  . LEU   B 1 543  ? 43.54100   104.85600 -35.31600 1.000 34.38145  ?  543  LEU   B CB  1 
ATOM   18232 C  CG  . LEU   B 1 543  ? 43.28100   105.79900 -36.49100 1.000 40.56612  ?  543  LEU   B CG  1 
ATOM   18233 C  CD1 . LEU   B 1 543  ? 43.52400   105.08800 -37.81300 1.000 32.96455  ?  543  LEU   B CD1 1 
ATOM   18234 C  CD2 . LEU   B 1 543  ? 41.86700   106.35500 -36.42700 1.000 40.66452  ?  543  LEU   B CD2 1 
ATOM   18235 N  N   . ASN   B 1 544  ? 46.81300   105.71200 -35.90700 1.000 42.73083  ?  544  ASN   B N   1 
ATOM   18236 C  CA  . ASN   B 1 544  ? 47.78900   106.80200 -35.89300 1.000 44.80785  ?  544  ASN   B CA  1 
ATOM   18237 C  C   . ASN   B 1 544  ? 48.79400   106.68300 -34.75000 1.000 31.19598  ?  544  ASN   B C   1 
ATOM   18238 O  O   . ASN   B 1 544  ? 49.36600   107.68800 -34.31800 1.000 43.56875  ?  544  ASN   B O   1 
ATOM   18239 C  CB  . ASN   B 1 544  ? 47.09300   108.16800 -35.84000 1.000 49.96620  ?  544  ASN   B CB  1 
ATOM   18240 C  CG  . ASN   B 1 544  ? 46.07700   108.34800 -36.95000 1.000 52.29700  ?  544  ASN   B CG  1 
ATOM   18241 O  OD1 . ASN   B 1 544  ? 46.28500   107.89800 -38.07700 1.000 46.94537  ?  544  ASN   B OD1 1 
ATOM   18242 N  ND2 . ASN   B 1 544  ? 44.96700   109.00500 -36.63500 1.000 41.14387  ?  544  ASN   B ND2 1 
ATOM   18243 N  N   . ARG   B 1 545  ? 49.02100   105.47300 -34.23900 1.000 26.07210  ?  545  ARG   B N   1 
ATOM   18244 C  CA  . ARG   B 1 545  ? 50.01200   105.22900 -33.18700 1.000 40.48224  ?  545  ARG   B CA  1 
ATOM   18245 C  C   . ARG   B 1 545  ? 50.79700   103.97300 -33.53800 1.000 50.02409  ?  545  ARG   B C   1 
ATOM   18246 O  O   . ARG   B 1 545  ? 50.65100   102.92600 -32.89500 1.000 39.57930  ?  545  ARG   B O   1 
ATOM   18247 C  CB  . ARG   B 1 545  ? 49.34300   105.08900 -31.81700 1.000 38.68081  ?  545  ARG   B CB  1 
ATOM   18248 C  CG  . ARG   B 1 545  ? 48.23100   106.08600 -31.53600 1.000 42.77369  ?  545  ARG   B CG  1 
ATOM   18249 C  CD  . ARG   B 1 545  ? 48.59300   107.05800 -30.42500 1.000 38.79359  ?  545  ARG   B CD  1 
ATOM   18250 N  NE  . ARG   B 1 545  ? 47.43600   107.85100 -30.02400 1.000 67.59496  ?  545  ARG   B NE  1 
ATOM   18251 C  CZ  . ARG   B 1 545  ? 47.13800   109.04800 -30.51200 1.000 77.44720  ?  545  ARG   B CZ  1 
ATOM   18252 N  NH1 . ARG   B 1 545  ? 47.91800   109.64900 -31.39600 1.000 70.20154  ?  545  ARG   B NH1 1 
ATOM   18253 N  NH2 . ARG   B 1 545  ? 46.02800   109.65600 -30.10400 1.000 81.40235  ?  545  ARG   B NH2 1 
ATOM   18254 N  N   . PRO   B 1 546  ? 51.64900   104.04100 -34.56600 1.000 47.34198  ?  546  PRO   B N   1 
ATOM   18255 C  CA  . PRO   B 1 546  ? 52.41000   102.84300 -34.94900 1.000 31.61423  ?  546  PRO   B CA  1 
ATOM   18256 C  C   . PRO   B 1 546  ? 53.45100   102.43800 -33.92100 1.000 36.51646  ?  546  PRO   B C   1 
ATOM   18257 O  O   . PRO   B 1 546  ? 53.75100   101.24300 -33.80400 1.000 40.15727  ?  546  PRO   B O   1 
ATOM   18258 C  CB  . PRO   B 1 546  ? 53.05300   103.24900 -36.28100 1.000 17.89888  ?  546  PRO   B CB  1 
ATOM   18259 C  CG  . PRO   B 1 546  ? 53.16900   104.72900 -36.19600 1.000 34.67835  ?  546  PRO   B CG  1 
ATOM   18260 C  CD  . PRO   B 1 546  ? 51.96200   105.19300 -35.42900 1.000 40.57553  ?  546  PRO   B CD  1 
ATOM   18261 N  N   . GLU   B 1 547  ? 54.01000   103.39000 -33.17000 1.000 34.29595  ?  547  GLU   B N   1 
ATOM   18262 C  CA  . GLU   B 1 547  ? 54.99700   103.03600 -32.15500 1.000 43.11789  ?  547  GLU   B CA  1 
ATOM   18263 C  C   . GLU   B 1 547  ? 54.34400   102.36200 -30.95500 1.000 43.81634  ?  547  GLU   B C   1 
ATOM   18264 O  O   . GLU   B 1 547  ? 54.86200   101.36400 -30.44000 1.000 48.01460  ?  547  GLU   B O   1 
ATOM   18265 C  CB  . GLU   B 1 547  ? 55.78100   104.27300 -31.71600 1.000 48.23229  ?  547  GLU   B CB  1 
ATOM   18266 C  CG  . GLU   B 1 547  ? 57.01900   104.55100 -32.55500 1.000 52.89104  ?  547  GLU   B CG  1 
ATOM   18267 C  CD  . GLU   B 1 547  ? 56.70700   105.29000 -33.84000 1.000 58.84863  ?  547  GLU   B CD  1 
ATOM   18268 O  OE1 . GLU   B 1 547  ? 56.31400   106.47300 -33.76600 1.000 67.66099  ?  547  GLU   B OE1 1 
ATOM   18269 O  OE2 . GLU   B 1 547  ? 56.85200   104.68800 -34.92500 1.000 59.35334  -1 547  GLU   B OE2 1 
ATOM   18270 N  N   . LEU   B 1 548  ? 53.21000   102.89100 -30.49200 1.000 45.79914  ?  548  LEU   B N   1 
ATOM   18271 C  CA  . LEU   B 1 548  ? 52.49300   102.23700 -29.40300 1.000 42.77897  ?  548  LEU   B CA  1 
ATOM   18272 C  C   . LEU   B 1 548  ? 51.92900   100.89100 -29.83900 1.000 38.86880  ?  548  LEU   B C   1 
ATOM   18273 O  O   . LEU   B 1 548  ? 51.82500   99.96900  -29.02200 1.000 33.26367  ?  548  LEU   B O   1 
ATOM   18274 C  CB  . LEU   B 1 548  ? 51.37800   103.14300 -28.88600 1.000 37.27992  ?  548  LEU   B CB  1 
ATOM   18275 C  CG  . LEU   B 1 548  ? 50.58500   102.63100 -27.68500 1.000 36.07705  ?  548  LEU   B CG  1 
ATOM   18276 C  CD1 . LEU   B 1 548  ? 51.52100   102.16600 -26.57800 1.000 46.99146  ?  548  LEU   B CD1 1 
ATOM   18277 C  CD2 . LEU   B 1 548  ? 49.66400   103.72200 -27.18400 1.000 43.58802  ?  548  LEU   B CD2 1 
ATOM   18278 N  N   . THR   B 1 549  ? 51.56300   100.76000 -31.11700 1.000 36.35990  ?  549  THR   B N   1 
ATOM   18279 C  CA  . THR   B 1 549  ? 51.13000   99.46700  -31.63300 1.000 31.69478  ?  549  THR   B CA  1 
ATOM   18280 C  C   . THR   B 1 549  ? 52.23300   98.42800  -31.49000 1.000 39.68644  ?  549  THR   B C   1 
ATOM   18281 O  O   . THR   B 1 549  ? 51.98000   97.29200  -31.07300 1.000 34.76613  ?  549  THR   B O   1 
ATOM   18282 C  CB  . THR   B 1 549  ? 50.71100   99.59800  -33.09700 1.000 30.01337  ?  549  THR   B CB  1 
ATOM   18283 O  OG1 . THR   B 1 549  ? 49.71100   100.61700 -33.22000 1.000 47.42410  ?  549  THR   B OG1 1 
ATOM   18284 C  CG2 . THR   B 1 549  ? 50.15200   98.27800  -33.61100 1.000 32.24902  ?  549  THR   B CG2 1 
ATOM   18285 N  N   . ALA   B 1 550  ? 53.47100   98.80500  -31.82000 1.000 41.22207  ?  550  ALA   B N   1 
ATOM   18286 C  CA  . ALA   B 1 550  ? 54.58500   97.87300  -31.69900 1.000 31.37003  ?  550  ALA   B CA  1 
ATOM   18287 C  C   . ALA   B 1 550  ? 54.87500   97.52600  -30.24500 1.000 38.17828  ?  550  ALA   B C   1 
ATOM   18288 O  O   . ALA   B 1 550  ? 55.31000   96.40600  -29.95500 1.000 44.41003  ?  550  ALA   B O   1 
ATOM   18289 C  CB  . ALA   B 1 550  ? 55.82800   98.45700  -32.36900 1.000 27.24694  ?  550  ALA   B CB  1 
ATOM   18290 N  N   . GLU   B 1 551  ? 54.63600   98.46100  -29.32100 1.000 38.75445  ?  551  GLU   B N   1 
ATOM   18291 C  CA  . GLU   B 1 551  ? 54.89500   98.19000  -27.91000 1.000 25.22487  ?  551  GLU   B CA  1 
ATOM   18292 C  C   . GLU   B 1 551  ? 53.90600   97.17800  -27.34700 1.000 32.97834  ?  551  GLU   B C   1 
ATOM   18293 O  O   . GLU   B 1 551  ? 54.29500   96.27200  -26.60000 1.000 40.15338  ?  551  GLU   B O   1 
ATOM   18294 C  CB  . GLU   B 1 551  ? 54.84200   99.48600  -27.10300 1.000 27.14132  ?  551  GLU   B CB  1 
ATOM   18295 C  CG  . GLU   B 1 551  ? 55.87900   100.52200 -27.49700 1.000 50.22155  ?  551  GLU   B CG  1 
ATOM   18296 C  CD  . GLU   B 1 551  ? 55.78600   101.78000 -26.65400 1.000 77.72941  ?  551  GLU   B CD  1 
ATOM   18297 O  OE1 . GLU   B 1 551  ? 55.26900   101.69700 -25.52000 1.000 90.14291  ?  551  GLU   B OE1 1 
ATOM   18298 O  OE2 . GLU   B 1 551  ? 56.22300   102.85000 -27.12700 1.000 84.36256  -1 551  GLU   B OE2 1 
ATOM   18299 N  N   . LYS   B 1 552  ? 52.62200   97.31800  -27.68500 1.000 46.96100  ?  552  LYS   B N   1 
ATOM   18300 C  CA  . LYS   B 1 552  ? 51.59200   96.43100  -27.15700 1.000 37.40582  ?  552  LYS   B CA  1 
ATOM   18301 C  C   . LYS   B 1 552  ? 51.42000   95.17300  -28.00200 1.000 38.57542  ?  552  LYS   B C   1 
ATOM   18302 O  O   . LYS   B 1 552  ? 51.22600   94.08300  -27.45300 1.000 36.12002  ?  552  LYS   B O   1 
ATOM   18303 C  CB  . LYS   B 1 552  ? 50.25500   97.17200  -27.05400 1.000 42.14070  ?  552  LYS   B CB  1 
ATOM   18304 C  CG  . LYS   B 1 552  ? 50.32100   98.51300  -26.32700 1.000 41.29803  ?  552  LYS   B CG  1 
ATOM   18305 C  CD  . LYS   B 1 552  ? 50.91700   98.38000  -24.93100 1.000 43.67523  ?  552  LYS   B CD  1 
ATOM   18306 C  CE  . LYS   B 1 552  ? 50.13900   97.39000  -24.06900 1.000 59.29634  ?  552  LYS   B CE  1 
ATOM   18307 N  NZ  . LYS   B 1 552  ? 48.78900   97.88600  -23.66200 1.000 64.29215  ?  552  LYS   B NZ  1 
ATOM   18308 N  N   . PHE   B 1 553  ? 51.48000   95.30000  -29.32700 1.000 32.80473  ?  553  PHE   B N   1 
ATOM   18309 C  CA  . PHE   B 1 553  ? 51.41400   94.15800  -30.23600 1.000 30.82694  ?  553  PHE   B CA  1 
ATOM   18310 C  C   . PHE   B 1 553  ? 52.84700   93.80700  -30.62500 1.000 30.72910  ?  553  PHE   B C   1 
ATOM   18311 O  O   . PHE   B 1 553  ? 53.41200   94.39300  -31.55200 1.000 48.82581  ?  553  PHE   B O   1 
ATOM   18312 C  CB  . PHE   B 1 553  ? 50.56200   94.47300  -31.46100 1.000 39.45325  ?  553  PHE   B CB  1 
ATOM   18313 C  CG  . PHE   B 1 553  ? 49.15500   94.88700  -31.13500 1.000 34.54054  ?  553  PHE   B CG  1 
ATOM   18314 C  CD1 . PHE   B 1 553  ? 48.84900   96.21500  -30.88700 1.000 27.84327  ?  553  PHE   B CD1 1 
ATOM   18315 C  CD2 . PHE   B 1 553  ? 48.13800   93.94900  -31.08200 1.000 40.38906  ?  553  PHE   B CD2 1 
ATOM   18316 C  CE1 . PHE   B 1 553  ? 47.55600   96.59900  -30.58600 1.000 33.83921  ?  553  PHE   B CE1 1 
ATOM   18317 C  CE2 . PHE   B 1 553  ? 46.84100   94.32600  -30.78100 1.000 40.51756  ?  553  PHE   B CE2 1 
ATOM   18318 C  CZ  . PHE   B 1 553  ? 46.55100   95.65300  -30.53300 1.000 33.59922  ?  553  PHE   B CZ  1 
ATOM   18319 N  N   . ILE   B 1 554  ? 53.43400   92.85400  -29.91200 1.000 30.60222  ?  554  ILE   B N   1 
ATOM   18320 C  CA  . ILE   B 1 554  ? 54.82400   92.48400  -30.11600 1.000 38.38297  ?  554  ILE   B CA  1 
ATOM   18321 C  C   . ILE   B 1 554  ? 54.89400   91.19700  -30.92400 1.000 44.21159  ?  554  ILE   B C   1 
ATOM   18322 O  O   . ILE   B 1 554  ? 53.92300   90.44600  -31.04400 1.000 43.67525  ?  554  ILE   B O   1 
ATOM   18323 C  CB  . ILE   B 1 554  ? 55.58000   92.31600  -28.78100 1.000 24.18933  ?  554  ILE   B CB  1 
ATOM   18324 C  CG1 . ILE   B 1 554  ? 55.13400   91.02700  -28.08900 1.000 28.81491  ?  554  ILE   B CG1 1 
ATOM   18325 C  CG2 . ILE   B 1 554  ? 55.35300   93.51900  -27.88300 1.000 33.35434  ?  554  ILE   B CG2 1 
ATOM   18326 C  CD1 . ILE   B 1 554  ? 56.10600   90.51800  -27.05800 1.000 41.79539  ?  554  ILE   B CD1 1 
ATOM   18327 N  N   . VAL   B 1 555  ? 56.07200   90.94000  -31.48500 1.000 39.33851  ?  555  VAL   B N   1 
ATOM   18328 C  CA  . VAL   B 1 555  ? 56.41500   89.64900  -32.06700 1.000 44.90465  ?  555  VAL   B CA  1 
ATOM   18329 C  C   . VAL   B 1 555  ? 57.39200   88.98000  -31.11200 1.000 37.42282  ?  555  VAL   B C   1 
ATOM   18330 O  O   . VAL   B 1 555  ? 58.44800   89.54600  -30.80000 1.000 43.72731  ?  555  VAL   B O   1 
ATOM   18331 C  CB  . VAL   B 1 555  ? 57.01900   89.79200  -33.47200 1.000 24.00633  ?  555  VAL   B CB  1 
ATOM   18332 C  CG1 . VAL   B 1 555  ? 57.35900   88.42300  -34.03800 1.000 26.32847  ?  555  VAL   B CG1 1 
ATOM   18333 C  CG2 . VAL   B 1 555  ? 56.05900   90.53100  -34.38800 1.000 22.53365  ?  555  VAL   B CG2 1 
ATOM   18334 N  N   . HIS   B 1 556  ? 57.04000   87.78900  -30.64200 1.000 38.08110  ?  556  HIS   B N   1 
ATOM   18335 C  CA  . HIS   B 1 556  ? 57.82200   87.15700  -29.59100 1.000 47.29289  ?  556  HIS   B CA  1 
ATOM   18336 C  C   . HIS   B 1 556  ? 59.22300   86.82500  -30.10200 1.000 49.12844  ?  556  HIS   B C   1 
ATOM   18337 O  O   . HIS   B 1 556  ? 59.37600   86.32800  -31.22400 1.000 41.60229  ?  556  HIS   B O   1 
ATOM   18338 C  CB  . HIS   B 1 556  ? 57.12800   85.89200  -29.08900 1.000 47.89670  ?  556  HIS   B CB  1 
ATOM   18339 C  CG  . HIS   B 1 556  ? 57.68700   85.37500  -27.80200 1.000 45.80712  ?  556  HIS   B CG  1 
ATOM   18340 N  ND1 . HIS   B 1 556  ? 58.75100   84.50100  -27.75100 1.000 48.77752  ?  556  HIS   B ND1 1 
ATOM   18341 C  CD2 . HIS   B 1 556  ? 57.33900   85.62100  -26.51700 1.000 44.85614  ?  556  HIS   B CD2 1 
ATOM   18342 C  CE1 . HIS   B 1 556  ? 59.03000   84.22500  -26.48900 1.000 53.65661  ?  556  HIS   B CE1 1 
ATOM   18343 N  NE2 . HIS   B 1 556  ? 58.18800   84.89100  -25.72100 1.000 54.67111  ?  556  HIS   B NE2 1 
ATOM   18344 N  N   . PRO   B 1 557  ? 60.26600   87.08900  -29.30900 1.000 44.53292  ?  557  PRO   B N   1 
ATOM   18345 C  CA  . PRO   B 1 557  ? 61.63800   86.88700  -29.80000 1.000 44.99258  ?  557  PRO   B CA  1 
ATOM   18346 C  C   . PRO   B 1 557  ? 62.02500   85.42900  -29.99600 1.000 51.41432  ?  557  PRO   B C   1 
ATOM   18347 O  O   . PRO   B 1 557  ? 63.04100   85.16800  -30.65400 1.000 52.54949  ?  557  PRO   B O   1 
ATOM   18348 C  CB  . PRO   B 1 557  ? 62.49800   87.54300  -28.71100 1.000 44.13896  ?  557  PRO   B CB  1 
ATOM   18349 C  CG  . PRO   B 1 557  ? 61.65700   87.47000  -27.48000 1.000 60.67251  ?  557  PRO   B CG  1 
ATOM   18350 C  CD  . PRO   B 1 557  ? 60.24000   87.64300  -27.94500 1.000 49.18734  ?  557  PRO   B CD  1 
ATOM   18351 N  N   . GLN   B 1 558  ? 61.26700   84.47600  -29.45600 1.000 45.75430  ?  558  GLN   B N   1 
ATOM   18352 C  CA  . GLN   B 1 558  ? 61.56600   83.06000  -29.62600 1.000 43.55499  ?  558  GLN   B CA  1 
ATOM   18353 C  C   . GLN   B 1 558  ? 60.52700   82.32900  -30.46200 1.000 49.52868  ?  558  GLN   B C   1 
ATOM   18354 O  O   . GLN   B 1 558  ? 60.88600   81.60900  -31.40000 1.000 50.86011  ?  558  GLN   B O   1 
ATOM   18355 C  CB  . GLN   B 1 558  ? 61.70600   82.37600  -28.25700 1.000 45.97355  ?  558  GLN   B CB  1 
ATOM   18356 C  CG  . GLN   B 1 558  ? 63.00700   82.69200  -27.53600 1.000 50.06749  ?  558  GLN   B CG  1 
ATOM   18357 C  CD  . GLN   B 1 558  ? 62.84800   83.76700  -26.47900 1.000 66.03277  ?  558  GLN   B CD  1 
ATOM   18358 O  OE1 . GLN   B 1 558  ? 61.94000   83.70800  -25.64900 1.000 58.10993  ?  558  GLN   B OE1 1 
ATOM   18359 N  NE2 . GLN   B 1 558  ? 63.73600   84.75500  -26.50200 1.000 49.43493  ?  558  GLN   B NE2 1 
ATOM   18360 N  N   . THR   B 1 559  ? 59.24100   82.49100  -30.14700 1.000 56.70856  ?  559  THR   B N   1 
ATOM   18361 C  CA  . THR   B 1 559  ? 58.19500   81.83100  -30.91800 1.000 45.05767  ?  559  THR   B CA  1 
ATOM   18362 C  C   . THR   B 1 559  ? 57.89600   82.54400  -32.23000 1.000 47.56405  ?  559  THR   B C   1 
ATOM   18363 O  O   . THR   B 1 559  ? 57.36300   81.91900  -33.15300 1.000 49.73817  ?  559  THR   B O   1 
ATOM   18364 C  CB  . THR   B 1 559  ? 56.90900   81.72300  -30.09300 1.000 43.71439  ?  559  THR   B CB  1 
ATOM   18365 O  OG1 . THR   B 1 559  ? 56.22000   82.98000  -30.10700 1.000 52.01432  ?  559  THR   B OG1 1 
ATOM   18366 C  CG2 . THR   B 1 559  ? 57.22800   81.34900  -28.65500 1.000 41.97464  ?  559  THR   B CG2 1 
ATOM   18367 N  N   . GLY   B 1 560  ? 58.22800   83.83000  -32.33500 1.000 39.53287  ?  560  GLY   B N   1 
ATOM   18368 C  CA  . GLY   B 1 560  ? 57.95100   84.58200  -33.54200 1.000 47.45823  ?  560  GLY   B CA  1 
ATOM   18369 C  C   . GLY   B 1 560  ? 56.49800   84.92200  -33.76900 1.000 53.46511  ?  560  GLY   B C   1 
ATOM   18370 O  O   . GLY   B 1 560  ? 56.14500   85.36600  -34.86600 1.000 61.10939  ?  560  GLY   B O   1 
ATOM   18371 N  N   . GLU   B 1 561  ? 55.64400   84.73400  -32.76800 1.000 52.08271  ?  561  GLU   B N   1 
ATOM   18372 C  CA  . GLU   B 1 561  ? 54.21600   84.96800  -32.90900 1.000 37.99966  ?  561  GLU   B CA  1 
ATOM   18373 C  C   . GLU   B 1 561  ? 53.84900   86.37700  -32.46400 1.000 41.23647  ?  561  GLU   B C   1 
ATOM   18374 O  O   . GLU   B 1 561  ? 54.52900   86.98600  -31.63300 1.000 43.23914  ?  561  GLU   B O   1 
ATOM   18375 C  CB  . GLU   B 1 561  ? 53.42400   83.94400  -32.09500 1.000 38.65126  ?  561  GLU   B CB  1 
ATOM   18376 C  CG  . GLU   B 1 561  ? 53.66500   82.50600  -32.51300 1.000 47.10236  ?  561  GLU   B CG  1 
ATOM   18377 C  CD  . GLU   B 1 561  ? 52.87800   81.51800  -31.67600 1.000 65.56978  ?  561  GLU   B CD  1 
ATOM   18378 O  OE1 . GLU   B 1 561  ? 53.04000   81.52500  -30.43700 1.000 61.61267  ?  561  GLU   B OE1 1 
ATOM   18379 O  OE2 . GLU   B 1 561  ? 52.09000   80.74200  -32.25600 1.000 71.47018  -1 561  GLU   B OE2 1 
ATOM   18380 N  N   . ARG   B 1 562  ? 52.75900   86.89000  -33.02900 1.000 47.62582  ?  562  ARG   B N   1 
ATOM   18381 C  CA  . ARG   B 1 562  ? 52.24800   88.20400  -32.65900 1.000 36.93663  ?  562  ARG   B CA  1 
ATOM   18382 C  C   . ARG   B 1 562  ? 51.39200   88.06900  -31.40500 1.000 32.78765  ?  562  ARG   B C   1 
ATOM   18383 O  O   . ARG   B 1 562  ? 50.43600   87.28600  -31.38100 1.000 33.50348  ?  562  ARG   B O   1 
ATOM   18384 C  CB  . ARG   B 1 562  ? 51.44400   88.80600  -33.80900 1.000 24.73428  ?  562  ARG   B CB  1 
ATOM   18385 C  CG  . ARG   B 1 562  ? 51.11200   90.28300  -33.65100 1.000 24.22267  ?  562  ARG   B CG  1 
ATOM   18386 C  CD  . ARG   B 1 562  ? 50.64100   90.87300  -34.97400 1.000 32.76216  ?  562  ARG   B CD  1 
ATOM   18387 N  NE  . ARG   B 1 562  ? 50.42000   92.31300  -34.90400 1.000 44.03922  ?  562  ARG   B NE  1 
ATOM   18388 C  CZ  . ARG   B 1 562  ? 49.22600   92.89000  -34.89500 1.000 44.46389  ?  562  ARG   B CZ  1 
ATOM   18389 N  NH1 . ARG   B 1 562  ? 48.11200   92.17700  -34.95300 1.000 41.95992  ?  562  ARG   B NH1 1 
ATOM   18390 N  NH2 . ARG   B 1 562  ? 49.14700   94.21600  -34.83300 1.000 48.98265  ?  562  ARG   B NH2 1 
ATOM   18391 N  N   . MET   B 1 563  ? 51.74100   88.82100  -30.36400 1.000 30.71178  ?  563  MET   B N   1 
ATOM   18392 C  CA  . MET   B 1 563  ? 51.07000   88.74100  -29.07600 1.000 31.91876  ?  563  MET   B CA  1 
ATOM   18393 C  C   . MET   B 1 563  ? 50.72100   90.13800  -28.58900 1.000 36.40773  ?  563  MET   B C   1 
ATOM   18394 O  O   . MET   B 1 563  ? 51.40900   91.11300  -28.90400 1.000 39.76604  ?  563  MET   B O   1 
ATOM   18395 C  CB  . MET   B 1 563  ? 51.94400   88.03700  -28.02800 1.000 35.74897  ?  563  MET   B CB  1 
ATOM   18396 C  CG  . MET   B 1 563  ? 52.42000   86.65700  -28.43600 1.000 40.27600  ?  563  MET   B CG  1 
ATOM   18397 S  SD  . MET   B 1 563  ? 53.54400   85.93100  -27.23000 1.000 31.91412  ?  563  MET   B SD  1 
ATOM   18398 C  CE  . MET   B 1 563  ? 53.90100   84.36400  -28.01800 1.000 39.72329  ?  563  MET   B CE  1 
ATOM   18399 N  N   . TYR   B 1 564  ? 49.64800   90.22600  -27.81000 1.000 31.65735  ?  564  TYR   B N   1 
ATOM   18400 C  CA  . TYR   B 1 564  ? 49.23500   91.48000  -27.19700 1.000 30.32170  ?  564  TYR   B CA  1 
ATOM   18401 C  C   . TYR   B 1 564  ? 49.61300   91.48100  -25.72200 1.000 37.19844  ?  564  TYR   B C   1 
ATOM   18402 O  O   . TYR   B 1 564  ? 49.28400   90.54100  -24.99000 1.000 35.75869  ?  564  TYR   B O   1 
ATOM   18403 C  CB  . TYR   B 1 564  ? 47.73100   91.70900  -27.35500 1.000 31.50332  ?  564  TYR   B CB  1 
ATOM   18404 C  CG  . TYR   B 1 564  ? 47.25200   92.95600  -26.64900 1.000 35.09750  ?  564  TYR   B CG  1 
ATOM   18405 C  CD1 . TYR   B 1 564  ? 47.52100   94.21600  -27.16800 1.000 30.83031  ?  564  TYR   B CD1 1 
ATOM   18406 C  CD2 . TYR   B 1 564  ? 46.54100   92.87600  -25.45900 1.000 27.83220  ?  564  TYR   B CD2 1 
ATOM   18407 C  CE1 . TYR   B 1 564  ? 47.09400   95.36000  -26.52400 1.000 24.65623  ?  564  TYR   B CE1 1 
ATOM   18408 C  CE2 . TYR   B 1 564  ? 46.10700   94.01600  -24.80800 1.000 32.50516  ?  564  TYR   B CE2 1 
ATOM   18409 C  CZ  . TYR   B 1 564  ? 46.38600   95.25500  -25.34600 1.000 25.13705  ?  564  TYR   B CZ  1 
ATOM   18410 O  OH  . TYR   B 1 564  ? 45.95800   96.39200  -24.70200 1.000 48.12310  ?  564  TYR   B OH  1 
ATOM   18411 N  N   . ARG   B 1 565  ? 50.30600   92.53400  -25.29300 1.000 37.68917  ?  565  ARG   B N   1 
ATOM   18412 C  CA  . ARG   B 1 565  ? 50.63200   92.72700  -23.88400 1.000 36.27794  ?  565  ARG   B CA  1 
ATOM   18413 C  C   . ARG   B 1 565  ? 49.43100   93.35700  -23.19000 1.000 40.52004  ?  565  ARG   B C   1 
ATOM   18414 O  O   . ARG   B 1 565  ? 49.08000   94.50800  -23.46600 1.000 39.74695  ?  565  ARG   B O   1 
ATOM   18415 C  CB  . ARG   B 1 565  ? 51.86400   93.61400  -23.73300 1.000 43.51629  ?  565  ARG   B CB  1 
ATOM   18416 C  CG  . ARG   B 1 565  ? 53.08000   93.15300  -24.50800 1.000 44.01478  ?  565  ARG   B CG  1 
ATOM   18417 C  CD  . ARG   B 1 565  ? 54.26600   94.03900  -24.18800 1.000 54.29080  ?  565  ARG   B CD  1 
ATOM   18418 N  NE  . ARG   B 1 565  ? 54.43900   94.19100  -22.74800 1.000 62.07849  ?  565  ARG   B NE  1 
ATOM   18419 C  CZ  . ARG   B 1 565  ? 55.44200   93.67500  -22.05200 1.000 54.80139  ?  565  ARG   B CZ  1 
ATOM   18420 N  NH1 . ARG   B 1 565  ? 56.41700   93.00000  -22.64000 1.000 48.62123  ?  565  ARG   B NH1 1 
ATOM   18421 N  NH2 . ARG   B 1 565  ? 55.47200   93.84600  -20.73400 1.000 51.77869  ?  565  ARG   B NH2 1 
ATOM   18422 N  N   . THR   B 1 566  ? 48.79900   92.61400  -22.28300 1.000 34.03287  ?  566  THR   B N   1 
ATOM   18423 C  CA  . THR   B 1 566  ? 47.63100   93.15600  -21.59800 1.000 24.48690  ?  566  THR   B CA  1 
ATOM   18424 C  C   . THR   B 1 566  ? 48.01800   94.15300  -20.51800 1.000 32.50720  ?  566  THR   B C   1 
ATOM   18425 O  O   . THR   B 1 566  ? 47.30300   95.13400  -20.29200 1.000 44.26272  ?  566  THR   B O   1 
ATOM   18426 C  CB  . THR   B 1 566  ? 46.81000   92.02700  -20.98100 1.000 28.74293  ?  566  THR   B CB  1 
ATOM   18427 O  OG1 . THR   B 1 566  ? 47.62800   91.28400  -20.06700 1.000 31.53139  ?  566  THR   B OG1 1 
ATOM   18428 C  CG2 . THR   B 1 566  ? 46.29900   91.10700  -22.06100 1.000 29.70773  ?  566  THR   B CG2 1 
ATOM   18429 N  N   . GLY   B 1 567  ? 49.14400   93.92500  -19.84900 1.000 37.74379  ?  567  GLY   B N   1 
ATOM   18430 C  CA  . GLY   B 1 567  ? 49.42800   94.63800  -18.62500 1.000 33.80318  ?  567  GLY   B CA  1 
ATOM   18431 C  C   . GLY   B 1 567  ? 48.70200   94.09500  -17.41800 1.000 40.87564  ?  567  GLY   B C   1 
ATOM   18432 O  O   . GLY   B 1 567  ? 48.67900   94.75600  -16.37400 1.000 38.47063  ?  567  GLY   B O   1 
ATOM   18433 N  N   . ASP   B 1 568  ? 48.10300   92.91300  -17.53500 1.000 43.93228  ?  568  ASP   B N   1 
ATOM   18434 C  CA  . ASP   B 1 568  ? 47.35900   92.27400  -16.46200 1.000 41.00328  ?  568  ASP   B CA  1 
ATOM   18435 C  C   . ASP   B 1 568  ? 48.10800   91.04400  -15.96800 1.000 39.09145  ?  568  ASP   B C   1 
ATOM   18436 O  O   . ASP   B 1 568  ? 48.76000   90.33900  -16.74300 1.000 31.52102  ?  568  ASP   B O   1 
ATOM   18437 C  CB  . ASP   B 1 568  ? 45.95900   91.86600  -16.92900 1.000 32.54929  ?  568  ASP   B CB  1 
ATOM   18438 C  CG  . ASP   B 1 568  ? 45.16100   93.03200  -17.46600 1.000 45.50610  ?  568  ASP   B CG  1 
ATOM   18439 O  OD1 . ASP   B 1 568  ? 45.51400   94.19000  -17.15300 1.000 54.85895  ?  568  ASP   B OD1 1 
ATOM   18440 O  OD2 . ASP   B 1 568  ? 44.17800   92.79100  -18.19700 1.000 51.05208  -1 568  ASP   B OD2 1 
ATOM   18441 N  N   . ARG   B 1 569  ? 48.00400   90.79300  -14.66800 1.000 46.47341  ?  569  ARG   B N   1 
ATOM   18442 C  CA  . ARG   B 1 569  ? 48.62800   89.63800  -14.04000 1.000 35.18621  ?  569  ARG   B CA  1 
ATOM   18443 C  C   . ARG   B 1 569  ? 47.60500   88.51900  -13.90100 1.000 35.40313  ?  569  ARG   B C   1 
ATOM   18444 O  O   . ARG   B 1 569  ? 46.44800   88.76200  -13.54600 1.000 43.71531  ?  569  ARG   B O   1 
ATOM   18445 C  CB  . ARG   B 1 569  ? 49.20600   90.01000  -12.67300 1.000 37.86286  ?  569  ARG   B CB  1 
ATOM   18446 C  CG  . ARG   B 1 569  ? 49.97900   88.89300  -11.99200 1.000 60.68527  ?  569  ARG   B CG  1 
ATOM   18447 C  CD  . ARG   B 1 569  ? 50.65200   89.37500  -10.71200 1.000 50.73242  ?  569  ARG   B CD  1 
ATOM   18448 N  NE  . ARG   B 1 569  ? 49.83000   90.33700  -9.98700  1.000 76.39941  ?  569  ARG   B NE  1 
ATOM   18449 C  CZ  . ARG   B 1 569  ? 50.16300   91.60400  -9.78400  1.000 85.39570  ?  569  ARG   B CZ  1 
ATOM   18450 N  NH1 . ARG   B 1 569  ? 51.32100   92.08900  -10.20200 1.000 67.00033  ?  569  ARG   B NH1 1 
ATOM   18451 N  NH2 . ARG   B 1 569  ? 49.31600   92.40400  -9.14200  1.000 79.80575  ?  569  ARG   B NH2 1 
ATOM   18452 N  N   . ALA   B 1 570  ? 48.03400   87.29300  -14.19200 1.000 20.40860  ?  570  ALA   B N   1 
ATOM   18453 C  CA  . ALA   B 1 570  ? 47.13000   86.15200  -14.17700 1.000 31.01848  ?  570  ALA   B CA  1 
ATOM   18454 C  C   . ALA   B 1 570  ? 47.94000   84.88100  -13.97000 1.000 38.65939  ?  570  ALA   B C   1 
ATOM   18455 O  O   . ALA   B 1 570  ? 49.16800   84.87700  -14.08200 1.000 46.69136  ?  570  ALA   B O   1 
ATOM   18456 C  CB  . ALA   B 1 570  ? 46.31000   86.07200  -15.46800 1.000 41.12775  ?  570  ALA   B CB  1 
ATOM   18457 N  N   . ARG   B 1 571  ? 47.23000   83.79500  -13.66900 1.000 39.21709  ?  571  ARG   B N   1 
ATOM   18458 C  CA  . ARG   B 1 571  ? 47.85000   82.49100  -13.49200 1.000 35.46496  ?  571  ARG   B CA  1 
ATOM   18459 C  C   . ARG   B 1 571  ? 46.92300   81.41400  -14.03600 1.000 32.93499  ?  571  ARG   B C   1 
ATOM   18460 O  O   . ARG   B 1 571  ? 45.70500   81.59700  -14.10700 1.000 45.45050  ?  571  ARG   B O   1 
ATOM   18461 C  CB  . ARG   B 1 571  ? 48.17700   82.20700  -12.01800 1.000 51.28479  ?  571  ARG   B CB  1 
ATOM   18462 C  CG  . ARG   B 1 571  ? 47.06700   81.50400  -11.24500 1.000 62.68061  ?  571  ARG   B CG  1 
ATOM   18463 C  CD  . ARG   B 1 571  ? 47.53900   81.12000  -9.85400  1.000 58.04144  ?  571  ARG   B CD  1 
ATOM   18464 N  NE  . ARG   B 1 571  ? 47.77700   82.29200  -9.02000  1.000 67.63274  ?  571  ARG   B NE  1 
ATOM   18465 C  CZ  . ARG   B 1 571  ? 48.68500   82.35300  -8.05600  1.000 68.77348  ?  571  ARG   B CZ  1 
ATOM   18466 N  NH1 . ARG   B 1 571  ? 49.48800   81.33300  -7.79700  1.000 72.75271  ?  571  ARG   B NH1 1 
ATOM   18467 N  NH2 . ARG   B 1 571  ? 48.79600   83.46700  -7.33800  1.000 48.14410  ?  571  ARG   B NH2 1 
ATOM   18468 N  N   . PHE   B 1 572  ? 47.51600   80.28900  -14.42500 1.000 35.32449  ?  572  PHE   B N   1 
ATOM   18469 C  CA  . PHE   B 1 572  ? 46.76600   79.14600  -14.92900 1.000 31.35287  ?  572  PHE   B CA  1 
ATOM   18470 C  C   . PHE   B 1 572  ? 46.46400   78.19300  -13.77900 1.000 37.80572  ?  572  PHE   B C   1 
ATOM   18471 O  O   . PHE   B 1 572  ? 47.38100   77.72900  -13.09200 1.000 54.36562  ?  572  PHE   B O   1 
ATOM   18472 C  CB  . PHE   B 1 572  ? 47.54500   78.42300  -16.02700 1.000 43.87831  ?  572  PHE   B CB  1 
ATOM   18473 C  CG  . PHE   B 1 572  ? 47.10300   78.77200  -17.41800 1.000 51.42679  ?  572  PHE   B CG  1 
ATOM   18474 C  CD1 . PHE   B 1 572  ? 46.01400   78.13600  -17.99100 1.000 57.37455  ?  572  PHE   B CD1 1 
ATOM   18475 C  CD2 . PHE   B 1 572  ? 47.78000   79.72700  -18.15600 1.000 42.86170  ?  572  PHE   B CD2 1 
ATOM   18476 C  CE1 . PHE   B 1 572  ? 45.60400   78.45200  -19.27300 1.000 52.74080  ?  572  PHE   B CE1 1 
ATOM   18477 C  CE2 . PHE   B 1 572  ? 47.37500   80.04700  -19.43900 1.000 55.81851  ?  572  PHE   B CE2 1 
ATOM   18478 C  CZ  . PHE   B 1 572  ? 46.28500   79.40900  -19.99800 1.000 55.19241  ?  572  PHE   B CZ  1 
ATOM   18479 N  N   . LEU   B 1 573  ? 45.18600   77.90600  -13.57000 1.000 44.77488  ?  573  LEU   B N   1 
ATOM   18480 C  CA  . LEU   B 1 573  ? 44.77900   76.91600  -12.59000 1.000 33.50532  ?  573  LEU   B CA  1 
ATOM   18481 C  C   . LEU   B 1 573  ? 44.96300   75.51400  -13.16200 1.000 40.27835  ?  573  LEU   B C   1 
ATOM   18482 O  O   . LEU   B 1 573  ? 44.98400   75.33100  -14.38200 1.000 48.00528  ?  573  LEU   B O   1 
ATOM   18483 C  CB  . LEU   B 1 573  ? 43.32500   77.14800  -12.18800 1.000 27.22049  ?  573  LEU   B CB  1 
ATOM   18484 C  CG  . LEU   B 1 573  ? 43.00500   78.54900  -11.66100 1.000 37.72222  ?  573  LEU   B CG  1 
ATOM   18485 C  CD1 . LEU   B 1 573  ? 41.51900   78.68900  -11.36600 1.000 46.38238  ?  573  LEU   B CD1 1 
ATOM   18486 C  CD2 . LEU   B 1 573  ? 43.83100   78.86700  -10.42400 1.000 40.42212  ?  573  LEU   B CD2 1 
ATOM   18487 N  N   . PRO   B 1 574  ? 45.11700   74.50400  -12.30100 1.000 47.51631  ?  574  PRO   B N   1 
ATOM   18488 C  CA  . PRO   B 1 574  ? 45.35100   73.14200  -12.81500 1.000 43.16079  ?  574  PRO   B CA  1 
ATOM   18489 C  C   . PRO   B 1 574  ? 44.22700   72.61600  -13.69100 1.000 53.44516  ?  574  PRO   B C   1 
ATOM   18490 O  O   . PRO   B 1 574  ? 44.46900   71.73800  -14.53000 1.000 46.90450  ?  574  PRO   B O   1 
ATOM   18491 C  CB  . PRO   B 1 574  ? 45.51300   72.30700  -11.53600 1.000 47.61369  ?  574  PRO   B CB  1 
ATOM   18492 C  CG  . PRO   B 1 574  ? 44.89700   73.13800  -10.44500 1.000 57.27417  ?  574  PRO   B CG  1 
ATOM   18493 C  CD  . PRO   B 1 574  ? 45.17800   74.55300  -10.83000 1.000 42.36528  ?  574  PRO   B CD  1 
ATOM   18494 N  N   . ASP   B 1 575  ? 43.00600   73.12900  -13.53300 1.000 54.11454  ?  575  ASP   B N   1 
ATOM   18495 C  CA  . ASP   B 1 575  ? 41.90000   72.70900  -14.38400 1.000 51.43018  ?  575  ASP   B CA  1 
ATOM   18496 C  C   . ASP   B 1 575  ? 41.97300   73.30400  -15.78500 1.000 51.67560  ?  575  ASP   B C   1 
ATOM   18497 O  O   . ASP   B 1 575  ? 41.25200   72.84100  -16.67400 1.000 60.94137  ?  575  ASP   B O   1 
ATOM   18498 C  CB  . ASP   B 1 575  ? 40.56700   73.07900  -13.72800 1.000 40.69441  ?  575  ASP   B CB  1 
ATOM   18499 C  CG  . ASP   B 1 575  ? 40.47200   74.55400  -13.39300 1.000 59.51563  ?  575  ASP   B CG  1 
ATOM   18500 O  OD1 . ASP   B 1 575  ? 40.33400   75.36400  -14.33100 1.000 68.17989  ?  575  ASP   B OD1 1 
ATOM   18501 O  OD2 . ASP   B 1 575  ? 40.53900   74.90600  -12.19600 1.000 78.75616  -1 575  ASP   B OD2 1 
ATOM   18502 N  N   . GLY   B 1 576  ? 42.82100   74.30900  -16.00300 1.000 43.00105  ?  576  GLY   B N   1 
ATOM   18503 C  CA  . GLY   B 1 576  ? 42.96400   74.95900  -17.28800 1.000 46.30904  ?  576  GLY   B CA  1 
ATOM   18504 C  C   . GLY   B 1 576  ? 42.44200   76.37900  -17.33100 1.000 44.45731  ?  576  GLY   B C   1 
ATOM   18505 O  O   . GLY   B 1 576  ? 42.90100   77.16700  -18.16900 1.000 58.38923  ?  576  GLY   B O   1 
ATOM   18506 N  N   . ASN   B 1 577  ? 41.50000   76.72900  -16.46000 1.000 42.17973  ?  577  ASN   B N   1 
ATOM   18507 C  CA  . ASN   B 1 577  ? 40.96200   78.08100  -16.45100 1.000 49.03650  ?  577  ASN   B CA  1 
ATOM   18508 C  C   . ASN   B 1 577  ? 42.00900   79.06900  -15.95100 1.000 39.66909  ?  577  ASN   B C   1 
ATOM   18509 O  O   . ASN   B 1 577  ? 42.90900   78.72300  -15.18100 1.000 46.07436  ?  577  ASN   B O   1 
ATOM   18510 C  CB  . ASN   B 1 577  ? 39.71200   78.15700  -15.57400 1.000 49.49838  ?  577  ASN   B CB  1 
ATOM   18511 C  CG  . ASN   B 1 577  ? 38.63200   77.18500  -16.00900 1.000 44.32810  ?  577  ASN   B CG  1 
ATOM   18512 O  OD1 . ASN   B 1 577  ? 38.22400   77.16700  -17.16900 1.000 54.13158  ?  577  ASN   B OD1 1 
ATOM   18513 N  ND2 . ASN   B 1 577  ? 38.16800   76.36300  -15.07600 1.000 59.71618  ?  577  ASN   B ND2 1 
ATOM   18514 N  N   . ILE   B 1 578  ? 41.88100   80.30700  -16.39900 1.000 37.94961  ?  578  ILE   B N   1 
ATOM   18515 C  CA  . ILE   B 1 578  ? 42.81400   81.37100  -16.05800 1.000 34.37179  ?  578  ILE   B CA  1 
ATOM   18516 C  C   . ILE   B 1 578  ? 42.21900   82.19500  -14.92700 1.000 36.24685  ?  578  ILE   B C   1 
ATOM   18517 O  O   . ILE   B 1 578  ? 40.99600   82.33600  -14.80700 1.000 52.26964  ?  578  ILE   B O   1 
ATOM   18518 C  CB  . ILE   B 1 578  ? 43.12600   82.23200  -17.29900 1.000 41.78741  ?  578  ILE   B CB  1 
ATOM   18519 C  CG1 . ILE   B 1 578  ? 43.58400   81.32800  -18.44400 1.000 34.04947  ?  578  ILE   B CG1 1 
ATOM   18520 C  CG2 . ILE   B 1 578  ? 44.19100   83.27400  -16.99400 1.000 43.23552  ?  578  ILE   B CG2 1 
ATOM   18521 C  CD1 . ILE   B 1 578  ? 43.21600   81.84400  -19.80500 1.000 42.31856  ?  578  ILE   B CD1 1 
ATOM   18522 N  N   . GLU   B 1 579  ? 43.09000   82.73600  -14.07900 1.000 40.28009  ?  579  GLU   B N   1 
ATOM   18523 C  CA  . GLU   B 1 579  ? 42.68600   83.46100  -12.87900 1.000 38.96577  ?  579  GLU   B CA  1 
ATOM   18524 C  C   . GLU   B 1 579  ? 43.26200   84.86900  -12.94700 1.000 45.49523  ?  579  GLU   B C   1 
ATOM   18525 O  O   . GLU   B 1 579  ? 44.48300   85.04600  -12.88400 1.000 54.31618  ?  579  GLU   B O   1 
ATOM   18526 C  CB  . GLU   B 1 579  ? 43.16600   82.73100  -11.62500 1.000 40.52273  ?  579  GLU   B CB  1 
ATOM   18527 C  CG  . GLU   B 1 579  ? 42.32900   82.98400  -10.38700 1.000 61.69710  ?  579  GLU   B CG  1 
ATOM   18528 C  CD  . GLU   B 1 579  ? 42.84300   82.22800  -9.17700  1.000 66.36777  ?  579  GLU   B CD  1 
ATOM   18529 O  OE1 . GLU   B 1 579  ? 44.05700   82.31200  -8.89300  1.000 58.45051  ?  579  GLU   B OE1 1 
ATOM   18530 O  OE2 . GLU   B 1 579  ? 42.03400   81.54300  -8.51600  1.000 79.55468  -1 579  GLU   B OE2 1 
ATOM   18531 N  N   . PHE   B 1 580  ? 42.38900   85.86400  -13.07500 1.000 44.50867  ?  580  PHE   B N   1 
ATOM   18532 C  CA  . PHE   B 1 580  ? 42.82800   87.25400  -13.07700 1.000 36.30579  ?  580  PHE   B CA  1 
ATOM   18533 C  C   . PHE   B 1 580  ? 43.30100   87.65400  -11.68500 1.000 35.08971  ?  580  PHE   B C   1 
ATOM   18534 O  O   . PHE   B 1 580  ? 42.59200   87.44900  -10.69500 1.000 45.55897  ?  580  PHE   B O   1 
ATOM   18535 C  CB  . PHE   B 1 580  ? 41.69300   88.16600  -13.54000 1.000 27.50372  ?  580  PHE   B CB  1 
ATOM   18536 C  CG  . PHE   B 1 580  ? 42.07800   89.61300  -13.63800 1.000 20.11926  ?  580  PHE   B CG  1 
ATOM   18537 C  CD1 . PHE   B 1 580  ? 42.83000   90.07100  -14.70500 1.000 23.98148  ?  580  PHE   B CD1 1 
ATOM   18538 C  CD2 . PHE   B 1 580  ? 41.67800   90.51900  -12.66800 1.000 25.41307  ?  580  PHE   B CD2 1 
ATOM   18539 C  CE1 . PHE   B 1 580  ? 43.18400   91.40200  -14.80200 1.000 38.09077  ?  580  PHE   B CE1 1 
ATOM   18540 C  CE2 . PHE   B 1 580  ? 42.02800   91.85400  -12.76000 1.000 24.44424  ?  580  PHE   B CE2 1 
ATOM   18541 C  CZ  . PHE   B 1 580  ? 42.78300   92.29500  -13.82800 1.000 30.14719  ?  580  PHE   B CZ  1 
ATOM   18542 N  N   . LEU   B 1 581  ? 44.50300   88.22600  -11.60700 1.000 37.05332  ?  581  LEU   B N   1 
ATOM   18543 C  CA  . LEU   B 1 581  ? 45.11300   88.58700  -10.33400 1.000 35.31457  ?  581  LEU   B CA  1 
ATOM   18544 C  C   . LEU   B 1 581  ? 45.30500   90.08700  -10.15800 1.000 41.42619  ?  581  LEU   B C   1 
ATOM   18545 O  O   . LEU   B 1 581  ? 45.78800   90.51600  -9.10500  1.000 56.32153  ?  581  LEU   B O   1 
ATOM   18546 C  CB  . LEU   B 1 581  ? 46.46000   87.87400  -10.17100 1.000 33.05970  ?  581  LEU   B CB  1 
ATOM   18547 C  CG  . LEU   B 1 581  ? 46.43100   86.35100  -10.02200 1.000 35.74552  ?  581  LEU   B CG  1 
ATOM   18548 C  CD1 . LEU   B 1 581  ? 47.70100   85.87100  -9.33800  1.000 53.69505  ?  581  LEU   B CD1 1 
ATOM   18549 C  CD2 . LEU   B 1 581  ? 45.19800   85.88900  -9.25600  1.000 57.66203  ?  581  LEU   B CD2 1 
ATOM   18550 N  N   . GLY   B 1 582  ? 44.94100   90.89200  -11.14600 1.000 39.66500  ?  582  GLY   B N   1 
ATOM   18551 C  CA  . GLY   B 1 582  ? 45.06000   92.33200  -11.06700 1.000 41.99044  ?  582  GLY   B CA  1 
ATOM   18552 C  C   . GLY   B 1 582  ? 45.96100   92.88200  -12.15500 1.000 43.28322  ?  582  GLY   B C   1 
ATOM   18553 O  O   . GLY   B 1 582  ? 46.50600   92.15400  -12.98300 1.000 41.28415  ?  582  GLY   B O   1 
ATOM   18554 N  N   . ARG   B 1 583  ? 46.10400   94.20400  -12.13800 1.000 44.47188  ?  583  ARG   B N   1 
ATOM   18555 C  CA  . ARG   B 1 583  ? 46.96400   94.89300  -13.08800 1.000 45.90074  ?  583  ARG   B CA  1 
ATOM   18556 C  C   . ARG   B 1 583  ? 48.36400   95.05300  -12.51300 1.000 52.13400  ?  583  ARG   B C   1 
ATOM   18557 O  O   . ARG   B 1 583  ? 48.53300   95.34400  -11.32500 1.000 62.09501  ?  583  ARG   B O   1 
ATOM   18558 C  CB  . ARG   B 1 583  ? 46.38600   96.26000  -13.45400 1.000 46.19998  ?  583  ARG   B CB  1 
ATOM   18559 C  CG  . ARG   B 1 583  ? 45.20900   96.19400  -14.41100 1.000 40.30201  ?  583  ARG   B CG  1 
ATOM   18560 C  CD  . ARG   B 1 583  ? 45.06200   97.49400  -15.18100 1.000 48.26588  ?  583  ARG   B CD  1 
ATOM   18561 N  NE  . ARG   B 1 583  ? 46.30400   97.86200  -15.85000 1.000 63.60062  ?  583  ARG   B NE  1 
ATOM   18562 C  CZ  . ARG   B 1 583  ? 46.63700   97.48700  -17.07800 1.000 69.42059  ?  583  ARG   B CZ  1 
ATOM   18563 N  NH1 . ARG   B 1 583  ? 45.83300   96.73700  -17.81400 1.000 37.29105  ?  583  ARG   B NH1 1 
ATOM   18564 N  NH2 . ARG   B 1 583  ? 47.80700   97.87400  -17.57900 1.000 71.51200  ?  583  ARG   B NH2 1 
ATOM   18565 N  N   . LEU   B 1 584  ? 49.37000   94.86400  -13.37200 1.000 53.39596  ?  584  LEU   B N   1 
ATOM   18566 C  CA  . LEU   B 1 584  ? 50.75500   94.89900  -12.91400 1.000 53.04389  ?  584  LEU   B CA  1 
ATOM   18567 C  C   . LEU   B 1 584  ? 51.14400   96.27200  -12.37800 1.000 54.06574  ?  584  LEU   B C   1 
ATOM   18568 O  O   . LEU   B 1 584  ? 52.00400   96.36900  -11.49600 1.000 63.06290  ?  584  LEU   B O   1 
ATOM   18569 C  CB  . LEU   B 1 584  ? 51.69300   94.48200  -14.04800 1.000 31.43111  ?  584  LEU   B CB  1 
ATOM   18570 C  CG  . LEU   B 1 584  ? 51.66100   93.00200  -14.43800 1.000 34.46332  ?  584  LEU   B CG  1 
ATOM   18571 C  CD1 . LEU   B 1 584  ? 52.38400   92.77100  -15.75400 1.000 41.28493  ?  584  LEU   B CD1 1 
ATOM   18572 C  CD2 . LEU   B 1 584  ? 52.27600   92.14800  -13.34300 1.000 64.87883  ?  584  LEU   B CD2 1 
ATOM   18573 N  N   . ASP   B 1 585  ? 50.52600   97.33900  -12.88600 1.000 60.02203  ?  585  ASP   B N   1 
ATOM   18574 C  CA  . ASP   B 1 585  ? 50.83200   98.67800  -12.40000 1.000 65.24869  ?  585  ASP   B CA  1 
ATOM   18575 C  C   . ASP   B 1 585  ? 50.00100   99.07800  -11.18600 1.000 69.75018  ?  585  ASP   B C   1 
ATOM   18576 O  O   . ASP   B 1 585  ? 50.38400   100.01100 -10.47200 1.000 68.47424  ?  585  ASP   B O   1 
ATOM   18577 C  CB  . ASP   B 1 585  ? 50.64400   99.71100  -13.52200 1.000 76.33359  ?  585  ASP   B CB  1 
ATOM   18578 C  CG  . ASP   B 1 585  ? 49.19300   99.85500  -13.96400 1.000 89.48435  ?  585  ASP   B CG  1 
ATOM   18579 O  OD1 . ASP   B 1 585  ? 48.32400   99.11500  -13.45800 1.000 89.78946  ?  585  ASP   B OD1 1 
ATOM   18580 O  OD2 . ASP   B 1 585  ? 48.92000   100.71800 -14.82600 1.000 90.11635  -1 585  ASP   B OD2 1 
ATOM   18581 N  N   . ASN   B 1 586  ? 48.88100   98.39800  -10.93700 1.000 71.32272  ?  586  ASN   B N   1 
ATOM   18582 C  CA  . ASN   B 1 586  ? 48.00900   98.69100  -9.79800  1.000 82.36681  ?  586  ASN   B CA  1 
ATOM   18583 C  C   . ASN   B 1 586  ? 48.40200   97.91600  -8.54800  1.000 80.58078  ?  586  ASN   B C   1 
ATOM   18584 O  O   . ASN   B 1 586  ? 47.53700   97.43500  -7.80900  1.000 65.08582  ?  586  ASN   B O   1 
ATOM   18585 C  CB  . ASN   B 1 586  ? 46.55700   98.40900  -10.17200 1.000 85.49530  ?  586  ASN   B CB  1 
ATOM   18586 C  CG  . ASN   B 1 586  ? 45.93600   99.53000  -10.98100 1.000 94.39918  ?  586  ASN   B CG  1 
ATOM   18587 O  OD1 . ASN   B 1 586  ? 46.63300   100.42500 -11.45900 1.000 99.86381  ?  586  ASN   B OD1 1 
ATOM   18588 N  ND2 . ASN   B 1 586  ? 44.61700   99.48800  -11.13800 1.000 87.15047  ?  586  ASN   B ND2 1 
ATOM   18589 N  N   . LEU   B 1 587  ? 49.69800   97.78000  -8.28500  1.000 89.92281  ?  587  LEU   B N   1 
ATOM   18590 C  CA  . LEU   B 1 587  ? 50.19500   97.10300  -7.09300  1.000 88.09023  ?  587  LEU   B CA  1 
ATOM   18591 C  C   . LEU   B 1 587  ? 50.60000   98.16100  -6.07300  1.000 81.25663  ?  587  LEU   B C   1 
ATOM   18592 O  O   . LEU   B 1 587  ? 51.63400   98.81900  -6.22800  1.000 75.92905  ?  587  LEU   B O   1 
ATOM   18593 C  CB  . LEU   B 1 587  ? 51.37100   96.19000  -7.43400  1.000 81.92788  ?  587  LEU   B CB  1 
ATOM   18594 C  CG  . LEU   B 1 587  ? 51.15700   94.68200  -7.27700  1.000 74.60970  ?  587  LEU   B CG  1 
ATOM   18595 C  CD1 . LEU   B 1 587  ? 52.42200   93.92600  -7.65100  1.000 67.06613  ?  587  LEU   B CD1 1 
ATOM   18596 C  CD2 . LEU   B 1 587  ? 50.72900   94.34300  -5.86000  1.000 61.96286  ?  587  LEU   B CD2 1 
ATOM   18597 N  N   . VAL   B 1 588  ? 49.77900   98.33100  -5.03700  1.000 86.63374  ?  588  VAL   B N   1 
ATOM   18598 C  CA  . VAL   B 1 588  ? 50.10300   99.24100  -3.94400  1.000 80.83416  ?  588  VAL   B CA  1 
ATOM   18599 C  C   . VAL   B 1 588  ? 50.85600   98.45600  -2.87900  1.000 72.84686  ?  588  VAL   B C   1 
ATOM   18600 O  O   . VAL   B 1 588  ? 50.87800   97.22000  -2.90300  1.000 71.31617  ?  588  VAL   B O   1 
ATOM   18601 C  CB  . VAL   B 1 588  ? 48.83900   99.90300  -3.36300  1.000 67.78807  ?  588  VAL   B CB  1 
ATOM   18602 C  CG1 . VAL   B 1 588  ? 47.98300   100.48800 -4.47800  1.000 58.98133  ?  588  VAL   B CG1 1 
ATOM   18603 C  CG2 . VAL   B 1 588  ? 48.04500   98.90500  -2.53600  1.000 65.74659  ?  588  VAL   B CG2 1 
ATOM   18604 N  N   . LYS   B 1 589  ? 51.48300   99.16200  -1.94200  1.000 64.19169  ?  589  LYS   B N   1 
ATOM   18605 C  CA  . LYS   B 1 589  ? 52.26400   98.53300  -0.88800  1.000 77.50291  ?  589  LYS   B CA  1 
ATOM   18606 C  C   . LYS   B 1 589  ? 51.84400   99.08200  0.46700   1.000 78.13959  ?  589  LYS   B C   1 
ATOM   18607 O  O   . LYS   B 1 589  ? 51.64400   100.29100 0.62300   1.000 58.88564  ?  589  LYS   B O   1 
ATOM   18608 C  CB  . LYS   B 1 589  ? 53.76800   98.75600  -1.09200  1.000 77.13298  ?  589  LYS   B CB  1 
ATOM   18609 C  CG  . LYS   B 1 589  ? 54.32700   98.15700  -2.37100  1.000 71.33987  ?  589  LYS   B CG  1 
ATOM   18610 C  CD  . LYS   B 1 589  ? 55.37000   97.09000  -2.07700  1.000 84.48109  ?  589  LYS   B CD  1 
ATOM   18611 C  CE  . LYS   B 1 589  ? 56.27100   96.87000  -3.28100  1.000 97.66278  ?  589  LYS   B CE  1 
ATOM   18612 N  NZ  . LYS   B 1 589  ? 55.50400   96.89100  -4.55800  1.000 95.38729  ?  589  LYS   B NZ  1 
ATOM   18613 N  N   . ILE   B 1 590  ? 51.70900   98.18600  1.44100   1.000 62.92570  ?  590  ILE   B N   1 
ATOM   18614 C  CA  . ILE   B 1 590  ? 51.39000   98.54100  2.82000   1.000 51.51229  ?  590  ILE   B CA  1 
ATOM   18615 C  C   . ILE   B 1 590  ? 52.41100   97.84600  3.71000   1.000 58.15029  ?  590  ILE   B C   1 
ATOM   18616 O  O   . ILE   B 1 590  ? 52.42000   96.61200  3.80000   1.000 59.04234  ?  590  ILE   B O   1 
ATOM   18617 C  CB  . ILE   B 1 590  ? 49.96300   98.13600  3.21700   1.000 56.60268  ?  590  ILE   B CB  1 
ATOM   18618 C  CG1 . ILE   B 1 590  ? 48.95500   98.52400  2.13100   1.000 55.72110  ?  590  ILE   B CG1 1 
ATOM   18619 C  CG2 . ILE   B 1 590  ? 49.58700   98.77900  4.54500   1.000 60.78554  ?  590  ILE   B CG2 1 
ATOM   18620 C  CD1 . ILE   B 1 590  ? 48.57000   99.98400  2.13700   1.000 39.21467  ?  590  ILE   B CD1 1 
ATOM   18621 N  N   . ARG   B 1 591  ? 53.26600   98.63300  4.36700   1.000 62.56565  ?  591  ARG   B N   1 
ATOM   18622 C  CA  . ARG   B 1 591  ? 54.28500   98.11500  5.28500   1.000 67.15133  ?  591  ARG   B CA  1 
ATOM   18623 C  C   . ARG   B 1 591  ? 55.18200   97.08300  4.60000   1.000 65.78342  ?  591  ARG   B C   1 
ATOM   18624 O  O   . ARG   B 1 591  ? 55.41000   95.98500  5.11300   1.000 74.12426  ?  591  ARG   B O   1 
ATOM   18625 C  CB  . ARG   B 1 591  ? 53.64800   97.52900  6.54900   1.000 73.54953  ?  591  ARG   B CB  1 
ATOM   18626 C  CG  . ARG   B 1 591  ? 53.03300   98.56000  7.48100   1.000 69.82979  ?  591  ARG   B CG  1 
ATOM   18627 C  CD  . ARG   B 1 591  ? 52.74100   97.97800  8.86000   1.000 62.04256  ?  591  ARG   B CD  1 
ATOM   18628 N  NE  . ARG   B 1 591  ? 51.77800   96.88300  8.82100   1.000 60.31803  ?  591  ARG   B NE  1 
ATOM   18629 C  CZ  . ARG   B 1 591  ? 52.08900   95.60100  8.96300   1.000 60.82897  ?  591  ARG   B CZ  1 
ATOM   18630 N  NH1 . ARG   B 1 591  ? 53.33800   95.21000  9.15700   1.000 58.95175  ?  591  ARG   B NH1 1 
ATOM   18631 N  NH2 . ARG   B 1 591  ? 51.12200   94.68900  8.91300   1.000 51.22736  ?  591  ARG   B NH2 1 
ATOM   18632 N  N   . GLY   B 1 592  ? 55.69700   97.44800  3.42900   1.000 66.63386  ?  592  GLY   B N   1 
ATOM   18633 C  CA  . GLY   B 1 592  ? 56.58200   96.55400  2.70100   1.000 78.99659  ?  592  GLY   B CA  1 
ATOM   18634 C  C   . GLY   B 1 592  ? 55.92100   95.28300  2.22100   1.000 74.57533  ?  592  GLY   B C   1 
ATOM   18635 O  O   . GLY   B 1 592  ? 56.60100   94.26800  2.03400   1.000 71.85520  ?  592  GLY   B O   1 
ATOM   18636 N  N   . TYR   B 1 593  ? 54.60500   95.30600  2.02300   1.000 78.18320  ?  593  TYR   B N   1 
ATOM   18637 C  CA  . TYR   B 1 593  ? 53.85100   94.16100  1.52900   1.000 71.22841  ?  593  TYR   B CA  1 
ATOM   18638 C  C   . TYR   B 1 593  ? 53.11400   94.57100  0.26400   1.000 76.49155  ?  593  TYR   B C   1 
ATOM   18639 O  O   . TYR   B 1 593  ? 52.28800   95.48900  0.29400   1.000 81.46130  ?  593  TYR   B O   1 
ATOM   18640 C  CB  . TYR   B 1 593  ? 52.86000   93.65100  2.58000   1.000 61.71835  ?  593  TYR   B CB  1 
ATOM   18641 C  CG  . TYR   B 1 593  ? 53.46500   92.76300  3.64500   1.000 48.13989  ?  593  TYR   B CG  1 
ATOM   18642 C  CD1 . TYR   B 1 593  ? 53.67000   91.40900  3.41100   1.000 52.01058  ?  593  TYR   B CD1 1 
ATOM   18643 C  CD2 . TYR   B 1 593  ? 53.81200   93.27300  4.88900   1.000 45.19628  ?  593  TYR   B CD2 1 
ATOM   18644 C  CE1 . TYR   B 1 593  ? 54.21400   90.59000  4.38200   1.000 53.20498  ?  593  TYR   B CE1 1 
ATOM   18645 C  CE2 . TYR   B 1 593  ? 54.35900   92.46000  5.86800   1.000 49.94350  ?  593  TYR   B CE2 1 
ATOM   18646 C  CZ  . TYR   B 1 593  ? 54.55700   91.12000  5.60800   1.000 59.51595  ?  593  TYR   B CZ  1 
ATOM   18647 O  OH  . TYR   B 1 593  ? 55.09900   90.30500  6.57600   1.000 64.99064  ?  593  TYR   B OH  1 
ATOM   18648 N  N   . ARG   B 1 594  ? 53.41300   93.89500  -0.84300  1.000 69.70858  ?  594  ARG   B N   1 
ATOM   18649 C  CA  . ARG   B 1 594  ? 52.72100   94.14000  -2.10400  1.000 74.95178  ?  594  ARG   B CA  1 
ATOM   18650 C  C   . ARG   B 1 594  ? 51.35200   93.47300  -2.04200  1.000 82.41961  ?  594  ARG   B C   1 
ATOM   18651 O  O   . ARG   B 1 594  ? 51.25600   92.24300  -1.98700  1.000 88.78997  ?  594  ARG   B O   1 
ATOM   18652 C  CB  . ARG   B 1 594  ? 53.54100   93.61100  -3.27600  1.000 72.99148  ?  594  ARG   B CB  1 
ATOM   18653 N  N   . ILE   B 1 595  ? 50.29300   94.27900  -2.04400  1.000 73.33112  ?  595  ILE   B N   1 
ATOM   18654 C  CA  . ILE   B 1 595  ? 48.93500   93.76700  -1.92800  1.000 75.91999  ?  595  ILE   B CA  1 
ATOM   18655 C  C   . ILE   B 1 595  ? 48.13400   94.18000  -3.15400  1.000 91.38084  ?  595  ILE   B C   1 
ATOM   18656 O  O   . ILE   B 1 595  ? 48.41100   95.20200  -3.79300  1.000 83.39332  ?  595  ILE   B O   1 
ATOM   18657 C  CB  . ILE   B 1 595  ? 48.23500   94.25600  -0.64100  1.000 81.02108  ?  595  ILE   B CB  1 
ATOM   18658 C  CG1 . ILE   B 1 595  ? 47.69000   95.67100  -0.83500  1.000 73.68727  ?  595  ILE   B CG1 1 
ATOM   18659 C  CG2 . ILE   B 1 595  ? 49.19400   94.21900  0.53900   1.000 82.52258  ?  595  ILE   B CG2 1 
ATOM   18660 C  CD1 . ILE   B 1 595  ? 46.49300   95.97600  0.01500   1.000 58.96950  ?  595  ILE   B CD1 1 
ATOM   18661 N  N   . GLU   B 1 596  ? 47.13500   93.36700  -3.48200  1.000 83.85605  ?  596  GLU   B N   1 
ATOM   18662 C  CA  . GLU   B 1 596  ? 46.17900   93.69400  -4.53300  1.000 69.53698  ?  596  GLU   B CA  1 
ATOM   18663 C  C   . GLU   B 1 596  ? 44.84200   94.01300  -3.88100  1.000 68.70024  ?  596  GLU   B C   1 
ATOM   18664 O  O   . GLU   B 1 596  ? 44.22300   93.11700  -3.28500  1.000 71.05935  ?  596  GLU   B O   1 
ATOM   18665 C  CB  . GLU   B 1 596  ? 46.03300   92.53600  -5.52200  1.000 58.72148  ?  596  GLU   B CB  1 
ATOM   18666 C  CG  . GLU   B 1 596  ? 45.23100   92.88300  -6.76600  1.000 64.03283  ?  596  GLU   B CG  1 
ATOM   18667 C  CD  . GLU   B 1 596  ? 45.93600   93.89600  -7.65000  1.000 79.58816  ?  596  GLU   B CD  1 
ATOM   18668 O  OE1 . GLU   B 1 596  ? 47.17300   93.80200  -7.79700  1.000 84.32733  ?  596  GLU   B OE1 1 
ATOM   18669 O  OE2 . GLU   B 1 596  ? 45.25300   94.78900  -8.19400  1.000 77.27946  -1 596  GLU   B OE2 1 
ATOM   18670 N  N   . PRO   B 1 597  ? 44.36300   95.25700  -3.95400  1.000 65.49195  ?  597  PRO   B N   1 
ATOM   18671 C  CA  . PRO   B 1 597  ? 43.12200   95.61300  -3.24300  1.000 64.45985  ?  597  PRO   B CA  1 
ATOM   18672 C  C   . PRO   B 1 597  ? 41.90800   94.80400  -3.66700  1.000 59.72080  ?  597  PRO   B C   1 
ATOM   18673 O  O   . PRO   B 1 597  ? 40.92100   94.76600  -2.92200  1.000 75.51769  ?  597  PRO   B O   1 
ATOM   18674 C  CB  . PRO   B 1 597  ? 42.94300   97.10100  -3.57500  1.000 64.45165  ?  597  PRO   B CB  1 
ATOM   18675 C  CG  . PRO   B 1 597  ? 44.32100   97.58100  -3.91000  1.000 68.98381  ?  597  PRO   B CG  1 
ATOM   18676 C  CD  . PRO   B 1 597  ? 44.99400   96.42600  -4.59000  1.000 70.76783  ?  597  PRO   B CD  1 
ATOM   18677 N  N   . GLY   B 1 598  ? 41.94400   94.15600  -4.83400  1.000 62.24201  ?  598  GLY   B N   1 
ATOM   18678 C  CA  . GLY   B 1 598  ? 40.81000   93.36200  -5.27400  1.000 77.19792  ?  598  GLY   B CA  1 
ATOM   18679 C  C   . GLY   B 1 598  ? 40.66200   92.03000  -4.57300  1.000 66.76797  ?  598  GLY   B C   1 
ATOM   18680 O  O   . GLY   B 1 598  ? 39.58700   91.42500  -4.64100  1.000 65.73651  ?  598  GLY   B O   1 
ATOM   18681 N  N   . GLU   B 1 599  ? 41.71300   91.55900  -3.90200  1.000 63.13704  ?  599  GLU   B N   1 
ATOM   18682 C  CA  . GLU   B 1 599  ? 41.66200   90.28100  -3.20400  1.000 61.04889  ?  599  GLU   B CA  1 
ATOM   18683 C  C   . GLU   B 1 599  ? 40.92400   90.35800  -1.87400  1.000 56.76335  ?  599  GLU   B C   1 
ATOM   18684 O  O   . GLU   B 1 599  ? 40.72100   89.32000  -1.23600  1.000 53.84688  ?  599  GLU   B O   1 
ATOM   18685 C  CB  . GLU   B 1 599  ? 43.08100   89.75200  -2.97200  1.000 64.68213  ?  599  GLU   B CB  1 
ATOM   18686 C  CG  . GLU   B 1 599  ? 43.88700   89.55100  -4.24600  1.000 59.17765  ?  599  GLU   B CG  1 
ATOM   18687 C  CD  . GLU   B 1 599  ? 45.25400   88.94500  -3.98500  1.000 82.37576  ?  599  GLU   B CD  1 
ATOM   18688 O  OE1 . GLU   B 1 599  ? 45.73300   89.02100  -2.83300  1.000 82.63491  ?  599  GLU   B OE1 1 
ATOM   18689 O  OE2 . GLU   B 1 599  ? 45.84900   88.38800  -4.93100  1.000 86.08519  -1 599  GLU   B OE2 1 
ATOM   18690 N  N   . ILE   B 1 600  ? 40.51700   91.54800  -1.44600  1.000 64.97865  ?  600  ILE   B N   1 
ATOM   18691 C  CA  . ILE   B 1 600  ? 39.83500   91.72600  -0.17300  1.000 60.07033  ?  600  ILE   B CA  1 
ATOM   18692 C  C   . ILE   B 1 600  ? 38.32500   91.77500  -0.34500  1.000 65.67870  ?  600  ILE   B C   1 
ATOM   18693 O  O   . ILE   B 1 600  ? 37.58500   91.30000  0.51600   1.000 67.51096  ?  600  ILE   B O   1 
ATOM   18694 C  CB  . ILE   B 1 600  ? 40.35300   93.00100  0.52000   1.000 52.46420  ?  600  ILE   B CB  1 
ATOM   18695 C  CG1 . ILE   B 1 600  ? 41.85700   92.88800  0.72100   1.000 58.28618  ?  600  ILE   B CG1 1 
ATOM   18696 C  CG2 . ILE   B 1 600  ? 39.63100   93.23300  1.84300   1.000 61.94501  ?  600  ILE   B CG2 1 
ATOM   18697 C  CD1 . ILE   B 1 600  ? 42.40000   93.92200  1.67500   1.000 67.55201  ?  600  ILE   B CD1 1 
ATOM   18698 N  N   . GLU   B 1 601  ? 37.86800   92.35600  -1.45000  1.000 67.48268  ?  601  GLU   B N   1 
ATOM   18699 C  CA  . GLU   B 1 601  ? 36.43700   92.47100  -1.71300  1.000 57.36468  ?  601  GLU   B CA  1 
ATOM   18700 C  C   . GLU   B 1 601  ? 35.67300   91.15300  -1.62200  1.000 59.80794  ?  601  GLU   B C   1 
ATOM   18701 O  O   . GLU   B 1 601  ? 34.54700   91.16800  -1.09500  1.000 60.37340  ?  601  GLU   B O   1 
ATOM   18702 C  CB  . GLU   B 1 601  ? 36.23500   93.11400  -3.09100  1.000 58.13739  ?  601  GLU   B CB  1 
ATOM   18703 C  CG  . GLU   B 1 601  ? 37.00100   94.40700  -3.29000  1.000 68.41191  ?  601  GLU   B CG  1 
ATOM   18704 C  CD  . GLU   B 1 601  ? 36.89000   94.93400  -4.70500  1.000 79.23534  ?  601  GLU   B CD  1 
ATOM   18705 O  OE1 . GLU   B 1 601  ? 36.90000   94.11500  -5.64700  1.000 91.95548  ?  601  GLU   B OE1 1 
ATOM   18706 O  OE2 . GLU   B 1 601  ? 36.78600   96.16700  -4.87400  1.000 82.45914  -1 601  GLU   B OE2 1 
ATOM   18707 N  N   . PRO   B 1 602  ? 36.18100   90.01100  -2.10700  1.000 59.04641  ?  602  PRO   B N   1 
ATOM   18708 C  CA  . PRO   B 1 602  ? 35.39900   88.76600  -1.96800  1.000 57.61649  ?  602  PRO   B CA  1 
ATOM   18709 C  C   . PRO   B 1 602  ? 35.08400   88.39300  -0.52800  1.000 63.77806  ?  602  PRO   B C   1 
ATOM   18710 O  O   . PRO   B 1 602  ? 33.94300   88.01700  -0.22900  1.000 71.96677  ?  602  PRO   B O   1 
ATOM   18711 C  CB  . PRO   B 1 602  ? 36.29000   87.71700  -2.65600  1.000 49.73631  ?  602  PRO   B CB  1 
ATOM   18712 C  CG  . PRO   B 1 602  ? 37.64300   88.34400  -2.75300  1.000 60.30204  ?  602  PRO   B CG  1 
ATOM   18713 C  CD  . PRO   B 1 602  ? 37.37600   89.79400  -2.94100  1.000 58.74867  ?  602  PRO   B CD  1 
ATOM   18714 N  N   . PHE   B 1 603  ? 36.06200   88.48300  0.37800   1.000 66.41514  ?  603  PHE   B N   1 
ATOM   18715 C  CA  . PHE   B 1 603  ? 35.81600   88.09000  1.76300   1.000 63.93265  ?  603  PHE   B CA  1 
ATOM   18716 C  C   . PHE   B 1 603  ? 34.79900   89.00700  2.42900   1.000 59.77256  ?  603  PHE   B C   1 
ATOM   18717 O  O   . PHE   B 1 603  ? 33.97200   88.55100  3.22700   1.000 78.99339  ?  603  PHE   B O   1 
ATOM   18718 C  CB  . PHE   B 1 603  ? 37.12300   88.08600  2.55300   1.000 55.12502  ?  603  PHE   B CB  1 
ATOM   18719 C  CG  . PHE   B 1 603  ? 38.16600   87.17000  1.99000   1.000 64.72800  ?  603  PHE   B CG  1 
ATOM   18720 C  CD1 . PHE   B 1 603  ? 38.14500   85.81400  2.27400   1.000 67.35385  ?  603  PHE   B CD1 1 
ATOM   18721 C  CD2 . PHE   B 1 603  ? 39.17100   87.66400  1.17600   1.000 65.51013  ?  603  PHE   B CD2 1 
ATOM   18722 C  CE1 . PHE   B 1 603  ? 39.10600   84.96900  1.75600   1.000 70.78865  ?  603  PHE   B CE1 1 
ATOM   18723 C  CE2 . PHE   B 1 603  ? 40.13500   86.82400  0.65500   1.000 55.95134  ?  603  PHE   B CE2 1 
ATOM   18724 C  CZ  . PHE   B 1 603  ? 40.10200   85.47500  0.94500   1.000 57.71822  ?  603  PHE   B CZ  1 
ATOM   18725 N  N   . LEU   B 1 604  ? 34.84400   90.30300  2.11400   1.000 53.07746  ?  604  LEU   B N   1 
ATOM   18726 C  CA  . LEU   B 1 604  ? 33.89400   91.23600  2.70700   1.000 65.41380  ?  604  LEU   B CA  1 
ATOM   18727 C  C   . LEU   B 1 604  ? 32.47400   90.97100  2.22300   1.000 68.67640  ?  604  LEU   B C   1 
ATOM   18728 O  O   . LEU   B 1 604  ? 31.51000   91.28900  2.93000   1.000 75.10779  ?  604  LEU   B O   1 
ATOM   18729 C  CB  . LEU   B 1 604  ? 34.30900   92.67400  2.39500   1.000 65.21442  ?  604  LEU   B CB  1 
ATOM   18730 C  CG  . LEU   B 1 604  ? 33.91900   93.74000  3.42100   1.000 69.31391  ?  604  LEU   B CG  1 
ATOM   18731 C  CD1 . LEU   B 1 604  ? 34.63700   93.50000  4.74000   1.000 66.13535  ?  604  LEU   B CD1 1 
ATOM   18732 C  CD2 . LEU   B 1 604  ? 34.22000   95.13200  2.89300   1.000 60.25999  ?  604  LEU   B CD2 1 
ATOM   18733 N  N   . MET   B 1 605  ? 32.32200   90.38800  1.03100   1.000 75.65898  ?  605  MET   B N   1 
ATOM   18734 C  CA  . MET   B 1 605  ? 30.99400   90.06200  0.52500   1.000 69.50918  ?  605  MET   B CA  1 
ATOM   18735 C  C   . MET   B 1 605  ? 30.49200   88.73000  1.06700   1.000 65.64103  ?  605  MET   B C   1 
ATOM   18736 O  O   . MET   B 1 605  ? 29.27700   88.51400  1.14000   1.000 77.11666  ?  605  MET   B O   1 
ATOM   18737 C  CB  . MET   B 1 605  ? 31.00300   90.04400  -1.00500  1.000 53.18374  ?  605  MET   B CB  1 
ATOM   18738 C  CG  . MET   B 1 605  ? 29.65800   90.34900  -1.64500  1.000 59.75011  ?  605  MET   B CG  1 
ATOM   18739 S  SD  . MET   B 1 605  ? 29.71200   90.22000  -3.44600  1.000 99.55568  ?  605  MET   B SD  1 
ATOM   18740 C  CE  . MET   B 1 605  ? 29.79900   91.94400  -3.93900  1.000 66.86158  ?  605  MET   B CE  1 
ATOM   18741 N  N   . ASN   B 1 606  ? 31.40400   87.83400  1.45600   1.000 59.56536  ?  606  ASN   B N   1 
ATOM   18742 C  CA  . ASN   B 1 606  ? 31.00700   86.59800  2.11900   1.000 80.82469  ?  606  ASN   B CA  1 
ATOM   18743 C  C   . ASN   B 1 606  ? 30.37400   86.84900  3.48000   1.000 85.47564  ?  606  ASN   B C   1 
ATOM   18744 O  O   . ASN   B 1 606  ? 29.84500   85.90800  4.08200   1.000 87.25396  ?  606  ASN   B O   1 
ATOM   18745 C  CB  . ASN   B 1 606  ? 32.21400   85.67000  2.27600   1.000 65.86618  ?  606  ASN   B CB  1 
ATOM   18746 C  CG  . ASN   B 1 606  ? 32.86400   85.32900  0.95000   1.000 84.16595  ?  606  ASN   B CG  1 
ATOM   18747 O  OD1 . ASN   B 1 606  ? 32.23100   85.40600  -0.10300  1.000 85.47161  ?  606  ASN   B OD1 1 
ATOM   18748 N  ND2 . ASN   B 1 606  ? 34.13600   84.94800  0.99500   1.000 76.28612  ?  606  ASN   B ND2 1 
ATOM   18749 N  N   . HIS   B 1 607  ? 30.42700   88.08100  3.97500   1.000 79.64870  ?  607  HIS   B N   1 
ATOM   18750 C  CA  . HIS   B 1 607  ? 29.76100   88.42400  5.22000   1.000 85.10370  ?  607  HIS   B CA  1 
ATOM   18751 C  C   . HIS   B 1 607  ? 28.25400   88.22400  5.07200   1.000 91.76007  ?  607  HIS   B C   1 
ATOM   18752 O  O   . HIS   B 1 607  ? 27.69500   88.48900  4.00000   1.000 81.71920  ?  607  HIS   B O   1 
ATOM   18753 C  CB  . HIS   B 1 607  ? 30.07600   89.87300  5.59700   1.000 83.99587  ?  607  HIS   B CB  1 
ATOM   18754 C  CG  . HIS   B 1 607  ? 29.57600   90.27700  6.94900   1.000 94.05426  ?  607  HIS   B CG  1 
ATOM   18755 N  ND1 . HIS   B 1 607  ? 28.29100   90.72600  7.16500   1.000 83.71242  ?  607  HIS   B ND1 1 
ATOM   18756 C  CD2 . HIS   B 1 607  ? 30.19300   90.31100  8.15400   1.000 84.91551  ?  607  HIS   B CD2 1 
ATOM   18757 C  CE1 . HIS   B 1 607  ? 28.13600   91.01400  8.44500   1.000 78.99895  ?  607  HIS   B CE1 1 
ATOM   18758 N  NE2 . HIS   B 1 607  ? 29.27500   90.77100  9.06700   1.000 83.15693  ?  607  HIS   B NE2 1 
ATOM   18759 N  N   . PRO   B 1 608  ? 27.56900   87.74900  6.11700   1.000 84.15674  ?  608  PRO   B N   1 
ATOM   18760 C  CA  . PRO   B 1 608  ? 26.13400   87.44700  5.97000   1.000 76.49696  ?  608  PRO   B CA  1 
ATOM   18761 C  C   . PRO   B 1 608  ? 25.28400   88.65100  5.60100   1.000 67.14908  ?  608  PRO   B C   1 
ATOM   18762 O  O   . PRO   B 1 608  ? 24.33700   88.51400  4.81700   1.000 74.17961  ?  608  PRO   B O   1 
ATOM   18763 C  CB  . PRO   B 1 608  ? 25.75800   86.89000  7.35000   1.000 66.93907  ?  608  PRO   B CB  1 
ATOM   18764 C  CG  . PRO   B 1 608  ? 27.03700   86.37200  7.91100   1.000 62.09931  ?  608  PRO   B CG  1 
ATOM   18765 C  CD  . PRO   B 1 608  ? 28.09700   87.30900  7.41900   1.000 79.20575  ?  608  PRO   B CD  1 
ATOM   18766 N  N   . LEU   B 1 609  ? 25.59400   89.82800  6.13800   1.000 64.27076  ?  609  LEU   B N   1 
ATOM   18767 C  CA  . LEU   B 1 609  ? 24.76000   91.00600  5.94300   1.000 79.73796  ?  609  LEU   B CA  1 
ATOM   18768 C  C   . LEU   B 1 609  ? 25.19200   91.86800  4.76600   1.000 72.55871  ?  609  LEU   B C   1 
ATOM   18769 O  O   . LEU   B 1 609  ? 24.42300   92.73800  4.34100   1.000 58.89297  ?  609  LEU   B O   1 
ATOM   18770 C  CB  . LEU   B 1 609  ? 24.75600   91.85900  7.21700   1.000 78.71289  ?  609  LEU   B CB  1 
ATOM   18771 C  CG  . LEU   B 1 609  ? 24.29200   91.16500  8.49800   1.000 63.97630  ?  609  LEU   B CG  1 
ATOM   18772 C  CD1 . LEU   B 1 609  ? 24.82400   91.89100  9.72200   1.000 56.93110  ?  609  LEU   B CD1 1 
ATOM   18773 C  CD2 . LEU   B 1 609  ? 22.77500   91.08500  8.54200   1.000 65.99279  ?  609  LEU   B CD2 1 
ATOM   18774 N  N   . ILE   B 1 610  ? 26.38900   91.65500  4.23100   1.000 70.13404  ?  610  ILE   B N   1 
ATOM   18775 C  CA  . ILE   B 1 610  ? 26.93400   92.50700  3.18300   1.000 72.61893  ?  610  ILE   B CA  1 
ATOM   18776 C  C   . ILE   B 1 610  ? 26.62300   91.89100  1.82600   1.000 81.66665  ?  610  ILE   B C   1 
ATOM   18777 O  O   . ILE   B 1 610  ? 26.91100   90.71200  1.58600   1.000 66.75560  ?  610  ILE   B O   1 
ATOM   18778 C  CB  . ILE   B 1 610  ? 28.44600   92.70700  3.37100   1.000 80.21618  ?  610  ILE   B CB  1 
ATOM   18779 C  CG1 . ILE   B 1 610  ? 28.72600   93.29700  4.75400   1.000 78.03416  ?  610  ILE   B CG1 1 
ATOM   18780 C  CG2 . ILE   B 1 610  ? 28.99400   93.61500  2.28900   1.000 83.82932  ?  610  ILE   B CG2 1 
ATOM   18781 C  CD1 . ILE   B 1 610  ? 30.19500   93.40000  5.09400   1.000 73.61539  ?  610  ILE   B CD1 1 
ATOM   18782 N  N   . GLU   B 1 611  ? 26.03300   92.69100  0.93800   1.000 89.99069  ?  611  GLU   B N   1 
ATOM   18783 C  CA  . GLU   B 1 611  ? 25.65800   92.24600  -0.39900  1.000 89.46448  ?  611  GLU   B CA  1 
ATOM   18784 C  C   . GLU   B 1 611  ? 26.58900   92.75700  -1.49000  1.000 92.29059  ?  611  GLU   B C   1 
ATOM   18785 O  O   . GLU   B 1 611  ? 26.83100   92.03800  -2.46700  1.000 83.57064  ?  611  GLU   B O   1 
ATOM   18786 C  CB  . GLU   B 1 611  ? 24.22500   92.68600  -0.71900  1.000 85.23966  ?  611  GLU   B CB  1 
ATOM   18787 C  CG  . GLU   B 1 611  ? 23.14600   91.93400  0.04300   1.000 81.50431  ?  611  GLU   B CG  1 
ATOM   18788 C  CD  . GLU   B 1 611  ? 22.72200   90.65600  -0.65400  1.000 102.00415 ?  611  GLU   B CD  1 
ATOM   18789 O  OE1 . GLU   B 1 611  ? 22.97800   90.52600  -1.87100  1.000 103.43993 ?  611  GLU   B OE1 1 
ATOM   18790 O  OE2 . GLU   B 1 611  ? 22.13000   89.78300  0.01400   1.000 111.35505 -1 611  GLU   B OE2 1 
ATOM   18791 N  N   . LEU   B 1 612  ? 27.11000   93.97700  -1.35700  1.000 95.64771  ?  612  LEU   B N   1 
ATOM   18792 C  CA  . LEU   B 1 612  ? 28.03100   94.54600  -2.33000  1.000 87.43272  ?  612  LEU   B CA  1 
ATOM   18793 C  C   . LEU   B 1 612  ? 29.21800   95.16800  -1.60900  1.000 87.59769  ?  612  LEU   B C   1 
ATOM   18794 O  O   . LEU   B 1 612  ? 29.05100   95.83100  -0.58200  1.000 89.87317  ?  612  LEU   B O   1 
ATOM   18795 C  CB  . LEU   B 1 612  ? 27.33600   95.60500  -3.20200  1.000 70.77100  ?  612  LEU   B CB  1 
ATOM   18796 C  CG  . LEU   B 1 612  ? 26.27400   95.10500  -4.18500  1.000 56.82933  ?  612  LEU   B CG  1 
ATOM   18797 C  CD1 . LEU   B 1 612  ? 25.76200   96.24900  -5.04200  1.000 62.64414  ?  612  LEU   B CD1 1 
ATOM   18798 C  CD2 . LEU   B 1 612  ? 26.81700   93.98200  -5.06300  1.000 63.68725  ?  612  LEU   B CD2 1 
ATOM   18799 N  N   . THR   B 1 613  ? 30.42000   94.93900  -2.14300  1.000 89.65323  ?  613  THR   B N   1 
ATOM   18800 C  CA  . THR   B 1 613  ? 31.63800   95.52000  -1.59000  1.000 78.53118  ?  613  THR   B CA  1 
ATOM   18801 C  C   . THR   B 1 613  ? 32.50800   96.06900  -2.71000  1.000 75.20774  ?  613  THR   B C   1 
ATOM   18802 O  O   . THR   B 1 613  ? 32.40600   95.65700  -3.86900  1.000 81.26201  ?  613  THR   B O   1 
ATOM   18803 C  CB  . THR   B 1 613  ? 32.48000   94.51300  -0.78500  1.000 71.10997  ?  613  THR   B CB  1 
ATOM   18804 O  OG1 . THR   B 1 613  ? 33.38700   93.83500  -1.66400  1.000 76.57396  ?  613  THR   B OG1 1 
ATOM   18805 C  CG2 . THR   B 1 613  ? 31.60500   93.49300  -0.10100  1.000 85.58021  ?  613  THR   B CG2 1 
ATOM   18806 N  N   . THR   B 1 614  ? 33.38000   97.00500  -2.33800  1.000 77.31760  ?  614  THR   B N   1 
ATOM   18807 C  CA  . THR   B 1 614  ? 34.45700   97.45600  -3.21000  1.000 81.04203  ?  614  THR   B CA  1 
ATOM   18808 C  C   . THR   B 1 614  ? 35.53700   98.09100  -2.34300  1.000 69.08639  ?  614  THR   B C   1 
ATOM   18809 O  O   . THR   B 1 614  ? 35.23600   98.90800  -1.46700  1.000 61.86431  ?  614  THR   B O   1 
ATOM   18810 C  CB  . THR   B 1 614  ? 33.94800   98.43500  -4.28600  1.000 72.17425  ?  614  THR   B CB  1 
ATOM   18811 O  OG1 . THR   B 1 614  ? 35.02800   98.80100  -5.15400  1.000 74.52474  ?  614  THR   B OG1 1 
ATOM   18812 C  CG2 . THR   B 1 614  ? 33.33700   99.69200  -3.67000  1.000 61.96717  ?  614  THR   B CG2 1 
ATOM   18813 N  N   . VAL   B 1 615  ? 36.78400   97.68600  -2.56300  1.000 59.43712  ?  615  VAL   B N   1 
ATOM   18814 C  CA  . VAL   B 1 615  ? 37.92500   98.18200  -1.80200  1.000 68.76198  ?  615  VAL   B CA  1 
ATOM   18815 C  C   . VAL   B 1 615  ? 38.66400   99.20500  -2.65100  1.000 65.96201  ?  615  VAL   B C   1 
ATOM   18816 O  O   . VAL   B 1 615  ? 38.96200   98.95100  -3.82500  1.000 73.84376  ?  615  VAL   B O   1 
ATOM   18817 C  CB  . VAL   B 1 615  ? 38.85900   97.03400  -1.38000  1.000 68.78593  ?  615  VAL   B CB  1 
ATOM   18818 C  CG1 . VAL   B 1 615  ? 40.16300   97.58300  -0.81800  1.000 53.74029  ?  615  VAL   B CG1 1 
ATOM   18819 C  CG2 . VAL   B 1 615  ? 38.17400   96.14500  -0.35400  1.000 61.99472  ?  615  VAL   B CG2 1 
ATOM   18820 N  N   . LEU   B 1 616  ? 38.95600   100.36200 -2.06300  1.000 63.01644  ?  616  LEU   B N   1 
ATOM   18821 C  CA  . LEU   B 1 616  ? 39.65400   101.43900 -2.74800  1.000 69.66955  ?  616  LEU   B CA  1 
ATOM   18822 C  C   . LEU   B 1 616  ? 40.97500   101.73200 -2.05100  1.000 77.82992  ?  616  LEU   B C   1 
ATOM   18823 O  O   . LEU   B 1 616  ? 41.04200   101.78200 -0.81800  1.000 73.09443  ?  616  LEU   B O   1 
ATOM   18824 C  CB  . LEU   B 1 616  ? 38.79900   102.70800 -2.80300  1.000 66.86025  ?  616  LEU   B CB  1 
ATOM   18825 C  CG  . LEU   B 1 616  ? 38.19300   103.02900 -4.17000  1.000 87.38240  ?  616  LEU   B CG  1 
ATOM   18826 C  CD1 . LEU   B 1 616  ? 37.52300   104.39300 -4.15300  1.000 83.18613  ?  616  LEU   B CD1 1 
ATOM   18827 C  CD2 . LEU   B 1 616  ? 39.25800   102.95800 -5.25800  1.000 83.54343  ?  616  LEU   B CD2 1 
ATOM   18828 N  N   . ALA   B 1 617  ? 42.02200   101.92700 -2.84900  1.000 74.79021  ?  617  ALA   B N   1 
ATOM   18829 C  CA  . ALA   B 1 617  ? 43.36200   102.21400 -2.34300  1.000 56.99122  ?  617  ALA   B CA  1 
ATOM   18830 C  C   . ALA   B 1 617  ? 43.60100   103.71600 -2.46300  1.000 72.06260  ?  617  ALA   B C   1 
ATOM   18831 O  O   . ALA   B 1 617  ? 44.06200   104.21200 -3.49100  1.000 83.50164  ?  617  ALA   B O   1 
ATOM   18832 C  CB  . ALA   B 1 617  ? 44.41400   101.41300 -3.10100  1.000 49.62157  ?  617  ALA   B CB  1 
ATOM   18833 N  N   . LYS   B 1 618  ? 43.27400   104.44200 -1.39800  1.000 74.07797  ?  618  LYS   B N   1 
ATOM   18834 C  CA  . LYS   B 1 618  ? 43.55100   105.86700 -1.33400  1.000 69.34040  ?  618  LYS   B CA  1 
ATOM   18835 C  C   . LYS   B 1 618  ? 45.00900   106.10700 -0.95100  1.000 73.48462  ?  618  LYS   B C   1 
ATOM   18836 O  O   . LYS   B 1 618  ? 45.70700   105.21600 -0.45700  1.000 69.17774  ?  618  LYS   B O   1 
ATOM   18837 C  CB  . LYS   B 1 618  ? 42.61600   106.55000 -0.33500  1.000 65.31146  ?  618  LYS   B CB  1 
ATOM   18838 C  CG  . LYS   B 1 618  ? 41.37400   107.16100 -0.96300  1.000 75.09357  ?  618  LYS   B CG  1 
ATOM   18839 C  CD  . LYS   B 1 618  ? 41.73300   108.42500 -1.72800  1.000 93.34084  ?  618  LYS   B CD  1 
ATOM   18840 C  CE  . LYS   B 1 618  ? 40.68800   108.76700 -2.77500  1.000 86.00098  ?  618  LYS   B CE  1 
ATOM   18841 N  NZ  . LYS   B 1 618  ? 41.25900   109.65900 -3.82400  1.000 77.23456  ?  618  LYS   B NZ  1 
ATOM   18842 N  N   . GLU   B 1 619  ? 45.47000   107.33200 -1.19000  1.000 81.91658  ?  619  GLU   B N   1 
ATOM   18843 C  CA  . GLU   B 1 619  ? 46.86000   107.69400 -0.95900  1.000 83.03468  ?  619  GLU   B CA  1 
ATOM   18844 C  C   . GLU   B 1 619  ? 46.93900   108.90900 -0.04500  1.000 83.98300  ?  619  GLU   B C   1 
ATOM   18845 O  O   . GLU   B 1 619  ? 46.03300   109.74700 -0.01600  1.000 74.23158  ?  619  GLU   B O   1 
ATOM   18846 C  CB  . GLU   B 1 619  ? 47.59300   107.99200 -2.28100  1.000 68.56225  ?  619  GLU   B CB  1 
ATOM   18847 C  CG  . GLU   B 1 619  ? 49.11300   108.00000 -2.17200  1.000 82.76547  ?  619  GLU   B CG  1 
ATOM   18848 C  CD  . GLU   B 1 619  ? 49.78100   108.70700 -3.33800  1.000 97.94344  ?  619  GLU   B CD  1 
ATOM   18849 O  OE1 . GLU   B 1 619  ? 49.23200   109.72300 -3.81200  1.000 99.83694  ?  619  GLU   B OE1 1 
ATOM   18850 O  OE2 . GLU   B 1 619  ? 50.85500   108.24600 -3.78000  1.000 89.15334  -1 619  GLU   B OE2 1 
ATOM   18851 N  N   . GLN   B 1 620  ? 48.03400   108.98800 0.70500   1.000 90.49409  ?  620  GLN   B N   1 
ATOM   18852 C  CA  . GLN   B 1 620  ? 48.35800   110.14400 1.52500   1.000 91.48403  ?  620  GLN   B CA  1 
ATOM   18853 C  C   . GLN   B 1 620  ? 49.46000   110.96000 0.86000   1.000 85.66950  ?  620  GLN   B C   1 
ATOM   18854 O  O   . GLN   B 1 620  ? 50.25600   110.43800 0.07200   1.000 66.67854  ?  620  GLN   B O   1 
ATOM   18855 C  CB  . GLN   B 1 620  ? 48.79300   109.72200 2.93400   1.000 91.13498  ?  620  GLN   B CB  1 
ATOM   18856 C  CG  . GLN   B 1 620  ? 47.64200   109.47000 3.90200   1.000 84.97061  ?  620  GLN   B CG  1 
ATOM   18857 C  CD  . GLN   B 1 620  ? 47.13200   110.74400 4.55200   1.000 82.18064  ?  620  GLN   B CD  1 
ATOM   18858 O  OE1 . GLN   B 1 620  ? 47.69800   111.82000 4.36200   1.000 90.95088  ?  620  GLN   B OE1 1 
ATOM   18859 N  NE2 . GLN   B 1 620  ? 46.06100   110.62600 5.32900   1.000 70.12186  ?  620  GLN   B NE2 1 
ATOM   18860 N  N   . ALA   B 1 621  ? 49.49900   112.25400 1.19900   1.000 82.10647  ?  621  ALA   B N   1 
ATOM   18861 C  CA  . ALA   B 1 621  ? 50.43600   113.18100 0.57000   1.000 60.87606  ?  621  ALA   B CA  1 
ATOM   18862 C  C   . ALA   B 1 621  ? 51.88500   112.75500 0.77600   1.000 72.49799  ?  621  ALA   B C   1 
ATOM   18863 O  O   . ALA   B 1 621  ? 52.72800   112.97000 -0.10200  1.000 82.44144  ?  621  ALA   B O   1 
ATOM   18864 C  CB  . ALA   B 1 621  ? 50.20000   114.59100 1.11300   1.000 63.32144  ?  621  ALA   B CB  1 
ATOM   18865 N  N   . ASP   B 1 622  ? 52.19500   112.13700 1.91300   1.000 78.20016  ?  622  ASP   B N   1 
ATOM   18866 C  CA  . ASP   B 1 622  ? 53.52100   111.57200 2.12400   1.000 64.04148  ?  622  ASP   B CA  1 
ATOM   18867 C  C   . ASP   B 1 622  ? 53.82300   110.38400 1.20500   1.000 78.89646  ?  622  ASP   B C   1 
ATOM   18868 O  O   . ASP   B 1 622  ? 54.90000   109.79400 1.35500   1.000 88.02880  ?  622  ASP   B O   1 
ATOM   18869 C  CB  . ASP   B 1 622  ? 53.66400   111.14300 3.58600   1.000 53.19547  ?  622  ASP   B CB  1 
ATOM   18870 C  CG  . ASP   B 1 622  ? 52.32700   111.02800 4.28700   1.000 95.62304  ?  622  ASP   B CG  1 
ATOM   18871 O  OD1 . ASP   B 1 622  ? 51.56800   112.01600 4.28800   1.000 92.23692  ?  622  ASP   B OD1 1 
ATOM   18872 O  OD2 . ASP   B 1 622  ? 52.02800   109.93300 4.81200   1.000 99.20164  -1 622  ASP   B OD2 1 
ATOM   18873 N  N   . GLY   B 1 623  ? 52.93200   109.99400 0.28800   1.000 87.20019  ?  623  GLY   B N   1 
ATOM   18874 C  CA  . GLY   B 1 623  ? 53.12700   108.78600 -0.50300  1.000 93.69724  ?  623  GLY   B CA  1 
ATOM   18875 C  C   . GLY   B 1 623  ? 52.61200   107.50800 0.12700   1.000 88.99006  ?  623  GLY   B C   1 
ATOM   18876 O  O   . GLY   B 1 623  ? 52.76700   106.43100 -0.46800  1.000 80.42701  ?  623  GLY   B O   1 
ATOM   18877 N  N   . ARG   B 1 624  ? 52.01000   107.59000 1.30800   1.000 85.81879  ?  624  ARG   B N   1 
ATOM   18878 C  CA  . ARG   B 1 624  ? 51.50600   106.41300 1.99100   1.000 84.79251  ?  624  ARG   B CA  1 
ATOM   18879 C  C   . ARG   B 1 624  ? 50.16300   105.98600 1.41600   1.000 78.36246  ?  624  ARG   B C   1 
ATOM   18880 O  O   . ARG   B 1 624  ? 49.38000   106.80200 0.92100   1.000 75.50235  ?  624  ARG   B O   1 
ATOM   18881 C  CB  . ARG   B 1 624  ? 51.36600   106.67300 3.49200   1.000 90.38552  ?  624  ARG   B CB  1 
ATOM   18882 C  CG  . ARG   B 1 624  ? 52.59800   106.33100 4.32900   1.000 86.78194  ?  624  ARG   B CG  1 
ATOM   18883 C  CD  . ARG   B 1 624  ? 52.32800   106.70500 5.77000   1.000 79.81471  ?  624  ARG   B CD  1 
ATOM   18884 N  NE  . ARG   B 1 624  ? 51.61300   107.97300 5.79800   1.000 96.52907  ?  624  ARG   B NE  1 
ATOM   18885 C  CZ  . ARG   B 1 624  ? 50.95700   108.45600 6.84500   1.000 96.61554  ?  624  ARG   B CZ  1 
ATOM   18886 N  NH1 . ARG   B 1 624  ? 50.88200   107.78900 7.98600   1.000 83.06339  ?  624  ARG   B NH1 1 
ATOM   18887 N  NH2 . ARG   B 1 624  ? 50.36300   109.64200 6.74700   1.000 88.58695  ?  624  ARG   B NH2 1 
ATOM   18888 N  N   . LYS   B 1 625  ? 49.90900   104.68600 1.49100   1.000 80.33633  ?  625  LYS   B N   1 
ATOM   18889 C  CA  . LYS   B 1 625  ? 48.69600   104.07700 0.97200   1.000 75.00014  ?  625  LYS   B CA  1 
ATOM   18890 C  C   . LYS   B 1 625  ? 47.84100   103.58100 2.12900   1.000 74.34271  ?  625  LYS   B C   1 
ATOM   18891 O  O   . LYS   B 1 625  ? 48.36300   103.04400 3.11200   1.000 80.76950  ?  625  LYS   B O   1 
ATOM   18892 C  CB  . LYS   B 1 625  ? 49.03400   102.91400 0.03500   1.000 73.06110  ?  625  LYS   B CB  1 
ATOM   18893 C  CG  . LYS   B 1 625  ? 50.16700   103.21200 -0.93300  1.000 81.23817  ?  625  LYS   B CG  1 
ATOM   18894 C  CD  . LYS   B 1 625  ? 49.79800   104.34800 -1.87100  1.000 91.02721  ?  625  LYS   B CD  1 
ATOM   18895 C  CE  . LYS   B 1 625  ? 50.75000   104.41800 -3.05100  1.000 77.41991  ?  625  LYS   B CE  1 
ATOM   18896 N  NZ  . LYS   B 1 625  ? 50.17300   105.21600 -4.16800  1.000 68.05212  ?  625  LYS   B NZ  1 
ATOM   18897 N  N   . TYR   B 1 626  ? 46.52700   103.77700 2.02000   1.000 67.16737  ?  626  TYR   B N   1 
ATOM   18898 C  CA  . TYR   B 1 626  ? 45.58800   103.21000 2.97600   1.000 60.31473  ?  626  TYR   B CA  1 
ATOM   18899 C  C   . TYR   B 1 626  ? 44.35100   102.72300 2.24000   1.000 71.65880  ?  626  TYR   B C   1 
ATOM   18900 O  O   . TYR   B 1 626  ? 43.97400   103.26300 1.19600   1.000 82.41676  ?  626  TYR   B O   1 
ATOM   18901 C  CB  . TYR   B 1 626  ? 45.19700   104.20900 4.07800   1.000 59.03782  ?  626  TYR   B CB  1 
ATOM   18902 C  CG  . TYR   B 1 626  ? 44.35700   105.39100 3.64200   1.000 58.28570  ?  626  TYR   B CG  1 
ATOM   18903 C  CD1 . TYR   B 1 626  ? 44.93600   106.49600 3.03000   1.000 60.44949  ?  626  TYR   B CD1 1 
ATOM   18904 C  CD2 . TYR   B 1 626  ? 42.98900   105.41800 3.88300   1.000 55.00179  ?  626  TYR   B CD2 1 
ATOM   18905 C  CE1 . TYR   B 1 626  ? 44.17100   107.58500 2.64900   1.000 58.07706  ?  626  TYR   B CE1 1 
ATOM   18906 C  CE2 . TYR   B 1 626  ? 42.21700   106.50100 3.50600   1.000 69.15337  ?  626  TYR   B CE2 1 
ATOM   18907 C  CZ  . TYR   B 1 626  ? 42.81200   107.58100 2.89100   1.000 70.38702  ?  626  TYR   B CZ  1 
ATOM   18908 O  OH  . TYR   B 1 626  ? 42.04000   108.65600 2.51500   1.000 76.91078  ?  626  TYR   B OH  1 
ATOM   18909 N  N   . LEU   B 1 627  ? 43.73100   101.69000 2.79900   1.000 71.04853  ?  627  LEU   B N   1 
ATOM   18910 C  CA  . LEU   B 1 627  ? 42.56800   101.04700 2.20800   1.000 59.92998  ?  627  LEU   B CA  1 
ATOM   18911 C  C   . LEU   B 1 627  ? 41.30200   101.46900 2.93700   1.000 53.66734  ?  627  LEU   B C   1 
ATOM   18912 O  O   . LEU   B 1 627  ? 41.27200   101.53400 4.17100   1.000 75.52000  ?  627  LEU   B O   1 
ATOM   18913 C  CB  . LEU   B 1 627  ? 42.70200   99.52500  2.25800   1.000 58.25552  ?  627  LEU   B CB  1 
ATOM   18914 C  CG  . LEU   B 1 627  ? 43.88900   98.89000  1.53800   1.000 54.03942  ?  627  LEU   B CG  1 
ATOM   18915 C  CD1 . LEU   B 1 627  ? 44.15400   97.51400  2.11600   1.000 47.83615  ?  627  LEU   B CD1 1 
ATOM   18916 C  CD2 . LEU   B 1 627  ? 43.62400   98.80100  0.04400   1.000 63.36734  ?  627  LEU   B CD2 1 
ATOM   18917 N  N   . VAL   B 1 628  ? 40.25700   101.75100 2.16500   1.000 52.98167  ?  628  VAL   B N   1 
ATOM   18918 C  CA  . VAL   B 1 628  ? 38.93400   102.05200 2.69300   1.000 59.27512  ?  628  VAL   B CA  1 
ATOM   18919 C  C   . VAL   B 1 628  ? 37.93900   101.11300 2.02300   1.000 74.80351  ?  628  VAL   B C   1 
ATOM   18920 O  O   . VAL   B 1 628  ? 37.96400   100.94000 0.79900   1.000 73.47655  ?  628  VAL   B O   1 
ATOM   18921 C  CB  . VAL   B 1 628  ? 38.55600   103.53000 2.47500   1.000 55.71377  ?  628  VAL   B CB  1 
ATOM   18922 C  CG1 . VAL   B 1 628  ? 38.84600   103.95500 1.04900   1.000 78.90095  ?  628  VAL   B CG1 1 
ATOM   18923 C  CG2 . VAL   B 1 628  ? 37.09000   103.76800 2.83500   1.000 64.49238  ?  628  VAL   B CG2 1 
ATOM   18924 N  N   . GLY   B 1 629  ? 37.08200   100.48900 2.82800   1.000 70.77059  ?  629  GLY   B N   1 
ATOM   18925 C  CA  . GLY   B 1 629  ? 36.16400   99.48300  2.35000   1.000 63.48389  ?  629  GLY   B CA  1 
ATOM   18926 C  C   . GLY   B 1 629  ? 34.74200   100.00200 2.30100   1.000 74.06391  ?  629  GLY   B C   1 
ATOM   18927 O  O   . GLY   B 1 629  ? 34.18300   100.41400 3.32100   1.000 75.75019  ?  629  GLY   B O   1 
ATOM   18928 N  N   . TYR   B 1 630  ? 34.15800   99.97300  1.10600   1.000 61.76862  ?  630  TYR   B N   1 
ATOM   18929 C  CA  . TYR   B 1 630  ? 32.78700   100.40000 0.87700   1.000 65.36013  ?  630  TYR   B CA  1 
ATOM   18930 C  C   . TYR   B 1 630  ? 31.90500   99.16900  0.72000   1.000 74.25406  ?  630  TYR   B C   1 
ATOM   18931 O  O   . TYR   B 1 630  ? 32.22900   98.26600  -0.05800  1.000 71.58027  ?  630  TYR   B O   1 
ATOM   18932 C  CB  . TYR   B 1 630  ? 32.69200   101.27700 -0.37100  1.000 69.51375  ?  630  TYR   B CB  1 
ATOM   18933 C  CG  . TYR   B 1 630  ? 33.58900   102.49400 -0.33500  1.000 68.86894  ?  630  TYR   B CG  1 
ATOM   18934 C  CD1 . TYR   B 1 630  ? 34.89700   102.43400 -0.80100  1.000 59.90950  ?  630  TYR   B CD1 1 
ATOM   18935 C  CD2 . TYR   B 1 630  ? 33.12600   103.70300 0.16300   1.000 81.95052  ?  630  TYR   B CD2 1 
ATOM   18936 C  CE1 . TYR   B 1 630  ? 35.71800   103.54600 -0.76900  1.000 58.75764  ?  630  TYR   B CE1 1 
ATOM   18937 C  CE2 . TYR   B 1 630  ? 33.93900   104.81900 0.20100   1.000 78.76210  ?  630  TYR   B CE2 1 
ATOM   18938 C  CZ  . TYR   B 1 630  ? 35.23300   104.73600 -0.26700  1.000 69.96197  ?  630  TYR   B CZ  1 
ATOM   18939 O  OH  . TYR   B 1 630  ? 36.04500   105.84500 -0.23300  1.000 75.92688  ?  630  TYR   B OH  1 
ATOM   18940 N  N   . TYR   B 1 631  ? 30.79300   99.13500  1.45300   1.000 73.39279  ?  631  TYR   B N   1 
ATOM   18941 C  CA  . TYR   B 1 631  ? 29.91800   97.97300  1.45600   1.000 73.99031  ?  631  TYR   B CA  1 
ATOM   18942 C  C   . TYR   B 1 631  ? 28.46200   98.41500  1.47600   1.000 89.13236  ?  631  TYR   B C   1 
ATOM   18943 O  O   . TYR   B 1 631  ? 28.12700   99.51700  1.92000   1.000 86.15480  ?  631  TYR   B O   1 
ATOM   18944 C  CB  . TYR   B 1 631  ? 30.20700   97.05000  2.65000   1.000 76.14330  ?  631  TYR   B CB  1 
ATOM   18945 C  CG  . TYR   B 1 631  ? 29.82800   97.62800  3.99800   1.000 92.64046  ?  631  TYR   B CG  1 
ATOM   18946 C  CD1 . TYR   B 1 631  ? 30.63900   98.56200  4.62900   1.000 86.15345  ?  631  TYR   B CD1 1 
ATOM   18947 C  CD2 . TYR   B 1 631  ? 28.66000   97.23600  4.64100   1.000 89.37132  ?  631  TYR   B CD2 1 
ATOM   18948 C  CE1 . TYR   B 1 631  ? 30.29800   99.09300  5.85900   1.000 79.25187  ?  631  TYR   B CE1 1 
ATOM   18949 C  CE2 . TYR   B 1 631  ? 28.31100   97.75900  5.87300   1.000 78.48566  ?  631  TYR   B CE2 1 
ATOM   18950 C  CZ  . TYR   B 1 631  ? 29.13500   98.68700  6.47700   1.000 76.50862  ?  631  TYR   B CZ  1 
ATOM   18951 O  OH  . TYR   B 1 631  ? 28.79700   99.21500  7.70200   1.000 75.44263  ?  631  TYR   B OH  1 
ATOM   18952 N  N   . VAL   B 1 632  ? 27.59600   97.53000  0.98500   1.000 90.38020  ?  632  VAL   B N   1 
ATOM   18953 C  CA  . VAL   B 1 632  ? 26.15000   97.72300  1.00100   1.000 75.10386  ?  632  VAL   B CA  1 
ATOM   18954 C  C   . VAL   B 1 632  ? 25.55200   96.74100  1.99700   1.000 79.46536  ?  632  VAL   B C   1 
ATOM   18955 O  O   . VAL   B 1 632  ? 25.84900   95.54000  1.95100   1.000 72.14120  ?  632  VAL   B O   1 
ATOM   18956 C  CB  . VAL   B 1 632  ? 25.53500   97.53300  -0.39600  1.000 71.77814  ?  632  VAL   B CB  1 
ATOM   18957 C  CG1 . VAL   B 1 632  ? 24.02200   97.69700  -0.33600  1.000 81.85940  ?  632  VAL   B CG1 1 
ATOM   18958 C  CG2 . VAL   B 1 632  ? 26.13500   98.52000  -1.37500  1.000 69.72538  ?  632  VAL   B CG2 1 
ATOM   18959 N  N   . ALA   B 1 633  ? 24.71000   97.24800  2.88900   1.000 89.52759  ?  633  ALA   B N   1 
ATOM   18960 C  CA  . ALA   B 1 633  ? 24.11300   96.44600  3.94500   1.000 82.57698  ?  633  ALA   B CA  1 
ATOM   18961 C  C   . ALA   B 1 633  ? 22.80500   97.09700  4.35900   1.000 84.03596  ?  633  ALA   B C   1 
ATOM   18962 O  O   . ALA   B 1 633  ? 22.58300   98.28200  4.08000   1.000 79.19851  ?  633  ALA   B O   1 
ATOM   18963 C  CB  . ALA   B 1 633  ? 25.05800   96.31600  5.14800   1.000 93.34667  ?  633  ALA   B CB  1 
ATOM   18964 N  N   . PRO   B 1 634  ? 21.90800   96.34800  5.00900   1.000 86.57854  ?  634  PRO   B N   1 
ATOM   18965 C  CA  . PRO   B 1 634  ? 20.67600   96.98300  5.51500   1.000 77.61831  ?  634  PRO   B CA  1 
ATOM   18966 C  C   . PRO   B 1 634  ? 20.95100   98.09400  6.51400   1.000 84.46548  ?  634  PRO   B C   1 
ATOM   18967 O  O   . PRO   B 1 634  ? 20.34600   99.17200  6.42700   1.000 84.97854  ?  634  PRO   B O   1 
ATOM   18968 C  CB  . PRO   B 1 634  ? 19.91800   95.80700  6.14800   1.000 81.71674  ?  634  PRO   B CB  1 
ATOM   18969 C  CG  . PRO   B 1 634  ? 20.43900   94.59800  5.44500   1.000 87.28987  ?  634  PRO   B CG  1 
ATOM   18970 C  CD  . PRO   B 1 634  ? 21.88500   94.88400  5.17600   1.000 81.42409  ?  634  PRO   B CD  1 
ATOM   18971 N  N   . GLU   B 1 635  ? 21.85300   97.86200  7.46400   1.000 85.77193  ?  635  GLU   B N   1 
ATOM   18972 C  CA  . GLU   B 1 635  ? 22.23300   98.86500  8.44600   1.000 98.27347  ?  635  GLU   B CA  1 
ATOM   18973 C  C   . GLU   B 1 635  ? 23.74800   98.86500  8.58800   1.000 91.72311  ?  635  GLU   B C   1 
ATOM   18974 O  O   . GLU   B 1 635  ? 24.43600   97.94700  8.13200   1.000 79.65574  ?  635  GLU   B O   1 
ATOM   18975 C  CB  . GLU   B 1 635  ? 21.56300   98.61100  9.80300   1.000 82.41024  ?  635  GLU   B CB  1 
ATOM   18976 N  N   . GLU   B 1 636  ? 24.26500   99.91300  9.22500   1.000 90.81490  ?  636  GLU   B N   1 
ATOM   18977 C  CA  . GLU   B 1 636  ? 25.69900   100.00800 9.45600   1.000 77.89277  ?  636  GLU   B CA  1 
ATOM   18978 C  C   . GLU   B 1 636  ? 26.16800   98.87200  10.35800  1.000 81.00527  ?  636  GLU   B C   1 
ATOM   18979 O  O   . GLU   B 1 636  ? 25.45300   98.42700  11.25900  1.000 94.26328  ?  636  GLU   B O   1 
ATOM   18980 C  CB  . GLU   B 1 636  ? 26.05200   101.35800 10.08100  1.000 71.63181  ?  636  GLU   B CB  1 
ATOM   18981 N  N   . ILE   B 1 637  ? 27.38000   98.39500  10.09900  1.000 67.86848  ?  637  ILE   B N   1 
ATOM   18982 C  CA  . ILE   B 1 637  ? 27.95400   97.29500  10.86900  1.000 75.30226  ?  637  ILE   B CA  1 
ATOM   18983 C  C   . ILE   B 1 637  ? 29.13500   97.83900  11.66500  1.000 77.71648  ?  637  ILE   B C   1 
ATOM   18984 O  O   . ILE   B 1 637  ? 29.85900   98.71500  11.16900  1.000 78.21410  ?  637  ILE   B O   1 
ATOM   18985 C  CB  . ILE   B 1 637  ? 28.36700   96.13100  9.95300   1.000 73.82615  ?  637  ILE   B CB  1 
ATOM   18986 C  CG1 . ILE   B 1 637  ? 27.30100   95.89200  8.88300   1.000 84.89463  ?  637  ILE   B CG1 1 
ATOM   18987 C  CG2 . ILE   B 1 637  ? 28.54100   94.85200  10.74900  1.000 81.01262  ?  637  ILE   B CG2 1 
ATOM   18988 C  CD1 . ILE   B 1 637  ? 27.65100   94.78200  7.91300   1.000 73.26086  ?  637  ILE   B CD1 1 
ATOM   18989 N  N   . PRO   B 1 638  ? 29.34500   97.38300  12.90200  1.000 70.54464  ?  638  PRO   B N   1 
ATOM   18990 C  CA  . PRO   B 1 638  ? 30.48300   97.87000  13.69200  1.000 69.47877  ?  638  PRO   B CA  1 
ATOM   18991 C  C   . PRO   B 1 638  ? 31.81100   97.71200  12.96400  1.000 64.75327  ?  638  PRO   B C   1 
ATOM   18992 O  O   . PRO   B 1 638  ? 32.03200   96.74900  12.22700  1.000 67.75439  ?  638  PRO   B O   1 
ATOM   18993 C  CB  . PRO   B 1 638  ? 30.42700   97.00100  14.95100  1.000 85.69930  ?  638  PRO   B CB  1 
ATOM   18994 C  CG  . PRO   B 1 638  ? 28.98100   96.69400  15.11100  1.000 81.19686  ?  638  PRO   B CG  1 
ATOM   18995 C  CD  . PRO   B 1 638  ? 28.41400   96.58200  13.71800  1.000 63.43720  ?  638  PRO   B CD  1 
ATOM   18996 N  N   . HIS   B 1 639  ? 32.70000   98.68400  13.18500  1.000 65.99303  ?  639  HIS   B N   1 
ATOM   18997 C  CA  . HIS   B 1 639  ? 34.01600   98.66400  12.55500  1.000 54.54772  ?  639  HIS   B CA  1 
ATOM   18998 C  C   . HIS   B 1 639  ? 34.82400   97.45300  13.00400  1.000 59.80664  ?  639  HIS   B C   1 
ATOM   18999 O  O   . HIS   B 1 639  ? 35.44500   96.76500  12.18500  1.000 64.50758  ?  639  HIS   B O   1 
ATOM   19000 C  CB  . HIS   B 1 639  ? 34.75700   99.96500  12.87500  1.000 56.98993  ?  639  HIS   B CB  1 
ATOM   19001 C  CG  . HIS   B 1 639  ? 36.22500   99.91900  12.58600  1.000 81.99385  ?  639  HIS   B CG  1 
ATOM   19002 N  ND1 . HIS   B 1 639  ? 37.15800   99.55000  13.53100  1.000 74.40907  ?  639  HIS   B ND1 1 
ATOM   19003 C  CD2 . HIS   B 1 639  ? 36.92300   100.20900 11.46200  1.000 71.40276  ?  639  HIS   B CD2 1 
ATOM   19004 C  CE1 . HIS   B 1 639  ? 38.36700   99.60800  13.00000  1.000 60.20560  ?  639  HIS   B CE1 1 
ATOM   19005 N  NE2 . HIS   B 1 639  ? 38.25200   100.00500 11.74500  1.000 57.30546  ?  639  HIS   B NE2 1 
ATOM   19006 N  N   . GLY   B 1 640  ? 34.82600   97.17500  14.31000  1.000 62.26625  ?  640  GLY   B N   1 
ATOM   19007 C  CA  . GLY   B 1 640  ? 35.57100   96.03600  14.81600  1.000 63.86559  ?  640  GLY   B CA  1 
ATOM   19008 C  C   . GLY   B 1 640  ? 34.99100   94.70400  14.39000  1.000 70.42601  ?  640  GLY   B C   1 
ATOM   19009 O  O   . GLY   B 1 640  ? 35.72600   93.72300  14.24500  1.000 63.26544  ?  640  GLY   B O   1 
ATOM   19010 N  N   . GLU   B 1 641  ? 33.67100   94.64400  14.19000  1.000 57.81397  ?  641  GLU   B N   1 
ATOM   19011 C  CA  . GLU   B 1 641  ? 33.06200   93.41200  13.70400  1.000 62.39868  ?  641  GLU   B CA  1 
ATOM   19012 C  C   . GLU   B 1 641  ? 33.56000   93.06700  12.30800  1.000 72.36715  ?  641  GLU   B C   1 
ATOM   19013 O  O   . GLU   B 1 641  ? 33.62200   91.88700  11.94400  1.000 77.32014  ?  641  GLU   B O   1 
ATOM   19014 C  CB  . GLU   B 1 641  ? 31.53700   93.53900  13.71100  1.000 72.00420  ?  641  GLU   B CB  1 
ATOM   19015 C  CG  . GLU   B 1 641  ? 30.80500   92.20500  13.65000  1.000 78.80859  ?  641  GLU   B CG  1 
ATOM   19016 C  CD  . GLU   B 1 641  ? 29.31700   92.35800  13.39400  1.000 77.57411  ?  641  GLU   B CD  1 
ATOM   19017 O  OE1 . GLU   B 1 641  ? 28.67100   93.18400  14.07300  1.000 70.74695  ?  641  GLU   B OE1 1 
ATOM   19018 O  OE2 . GLU   B 1 641  ? 28.79600   91.65400  12.50400  1.000 91.49905  -1 641  GLU   B OE2 1 
ATOM   19019 N  N   . LEU   B 1 642  ? 33.92700   94.07800  11.51600  1.000 70.06747  ?  642  LEU   B N   1 
ATOM   19020 C  CA  . LEU   B 1 642  ? 34.45000   93.82100  10.18000  1.000 61.52256  ?  642  LEU   B CA  1 
ATOM   19021 C  C   . LEU   B 1 642  ? 35.91600   93.41400  10.23800  1.000 55.22136  ?  642  LEU   B C   1 
ATOM   19022 O  O   . LEU   B 1 642  ? 36.36200   92.56800  9.45500   1.000 66.23280  ?  642  LEU   B O   1 
ATOM   19023 C  CB  . LEU   B 1 642  ? 34.27300   95.05400  9.28900   1.000 44.86733  ?  642  LEU   B CB  1 
ATOM   19024 C  CG  . LEU   B 1 642  ? 32.89000   95.71100  9.18700   1.000 58.42760  ?  642  LEU   B CG  1 
ATOM   19025 C  CD1 . LEU   B 1 642  ? 32.72100   96.42300  7.85300   1.000 52.95008  ?  642  LEU   B CD1 1 
ATOM   19026 C  CD2 . LEU   B 1 642  ? 31.77800   94.70100  9.37500   1.000 76.26107  ?  642  LEU   B CD2 1 
ATOM   19027 N  N   . ARG   B 1 643  ? 36.67700   94.01400  11.15600  1.000 53.38486  ?  643  ARG   B N   1 
ATOM   19028 C  CA  . ARG   B 1 643  ? 38.05000   93.58000  11.37900  1.000 54.75221  ?  643  ARG   B CA  1 
ATOM   19029 C  C   . ARG   B 1 643  ? 38.10600   92.13800  11.85800  1.000 63.75040  ?  643  ARG   B C   1 
ATOM   19030 O  O   . ARG   B 1 643  ? 39.06600   91.42000  11.55700  1.000 66.50569  ?  643  ARG   B O   1 
ATOM   19031 C  CB  . ARG   B 1 643  ? 38.73600   94.49700  12.39000  1.000 49.18955  ?  643  ARG   B CB  1 
ATOM   19032 C  CG  . ARG   B 1 643  ? 39.01900   95.89800  11.88500  1.000 62.75233  ?  643  ARG   B CG  1 
ATOM   19033 C  CD  . ARG   B 1 643  ? 40.00200   96.59200  12.80800  1.000 68.74496  ?  643  ARG   B CD  1 
ATOM   19034 N  NE  . ARG   B 1 643  ? 41.10400   95.70500  13.16200  1.000 69.65786  ?  643  ARG   B NE  1 
ATOM   19035 C  CZ  . ARG   B 1 643  ? 42.24200   95.61600  12.48700  1.000 71.73911  ?  643  ARG   B CZ  1 
ATOM   19036 N  NH1 . ARG   B 1 643  ? 42.47900   96.37400  11.42900  1.000 57.75808  ?  643  ARG   B NH1 1 
ATOM   19037 N  NH2 . ARG   B 1 643  ? 43.16500   94.74400  12.88400  1.000 78.61371  ?  643  ARG   B NH2 1 
ATOM   19038 N  N   . GLU   B 1 644  ? 37.09400   91.69800  12.61000  1.000 63.97548  ?  644  GLU   B N   1 
ATOM   19039 C  CA  . GLU   B 1 644  ? 37.04800   90.30100  13.02700  1.000 71.77041  ?  644  GLU   B CA  1 
ATOM   19040 C  C   . GLU   B 1 644  ? 36.66800   89.39300  11.86600  1.000 71.42125  ?  644  GLU   B C   1 
ATOM   19041 O  O   . GLU   B 1 644  ? 37.20100   88.28500  11.73800  1.000 67.64355  ?  644  GLU   B O   1 
ATOM   19042 C  CB  . GLU   B 1 644  ? 36.06800   90.12400  14.18600  1.000 76.44777  ?  644  GLU   B CB  1 
ATOM   19043 C  CG  . GLU   B 1 644  ? 36.70900   90.20200  15.55900  1.000 82.15965  ?  644  GLU   B CG  1 
ATOM   19044 C  CD  . GLU   B 1 644  ? 35.80800   89.65200  16.64700  1.000 102.05721 ?  644  GLU   B CD  1 
ATOM   19045 O  OE1 . GLU   B 1 644  ? 34.57500   89.63900  16.44900  1.000 87.02909  ?  644  GLU   B OE1 1 
ATOM   19046 O  OE2 . GLU   B 1 644  ? 36.33400   89.22400  17.69600  1.000 114.14531 -1 644  GLU   B OE2 1 
ATOM   19047 N  N   . TRP   B 1 645  ? 35.74800   89.84300  11.01100  1.000 65.11575  ?  645  TRP   B N   1 
ATOM   19048 C  CA  . TRP   B 1 645  ? 35.34000   89.02900  9.87200   1.000 63.59944  ?  645  TRP   B CA  1 
ATOM   19049 C  C   . TRP   B 1 645  ? 36.48800   88.85800  8.88500   1.000 65.34977  ?  645  TRP   B C   1 
ATOM   19050 O  O   . TRP   B 1 645  ? 36.76500   87.74500  8.42500   1.000 66.00143  ?  645  TRP   B O   1 
ATOM   19051 C  CB  . TRP   B 1 645  ? 34.12500   89.65300  9.18600   1.000 72.27707  ?  645  TRP   B CB  1 
ATOM   19052 C  CG  . TRP   B 1 645  ? 33.53200   88.77600  8.12900   1.000 81.02218  ?  645  TRP   B CG  1 
ATOM   19053 C  CD1 . TRP   B 1 645  ? 33.57600   88.97100  6.77900   1.000 73.41284  ?  645  TRP   B CD1 1 
ATOM   19054 C  CD2 . TRP   B 1 645  ? 32.81400   87.55400  8.33500   1.000 78.04753  ?  645  TRP   B CD2 1 
ATOM   19055 N  NE1 . TRP   B 1 645  ? 32.92400   87.94900  6.13300   1.000 88.42140  ?  645  TRP   B NE1 1 
ATOM   19056 C  CE2 . TRP   B 1 645  ? 32.44700   87.06600  7.06600   1.000 86.36823  ?  645  TRP   B CE2 1 
ATOM   19057 C  CE3 . TRP   B 1 645  ? 32.44400   86.82600  9.47100   1.000 71.46705  ?  645  TRP   B CE3 1 
ATOM   19058 C  CZ2 . TRP   B 1 645  ? 31.72800   85.88300  6.90000   1.000 89.22934  ?  645  TRP   B CZ2 1 
ATOM   19059 C  CZ3 . TRP   B 1 645  ? 31.73100   85.65400  9.30400   1.000 66.47405  ?  645  TRP   B CZ3 1 
ATOM   19060 C  CH2 . TRP   B 1 645  ? 31.38000   85.19400  8.03000   1.000 81.18231  ?  645  TRP   B CH2 1 
ATOM   19061 N  N   . LEU   B 1 646  ? 37.17000   89.95600  8.55200   1.000 61.47362  ?  646  LEU   B N   1 
ATOM   19062 C  CA  . LEU   B 1 646  ? 38.32400   89.86300  7.66600   1.000 49.97010  ?  646  LEU   B CA  1 
ATOM   19063 C  C   . LEU   B 1 646  ? 39.49200   89.15800  8.34100   1.000 51.05550  ?  646  LEU   B C   1 
ATOM   19064 O  O   . LEU   B 1 646  ? 40.33900   88.57100  7.65900   1.000 49.95299  ?  646  LEU   B O   1 
ATOM   19065 C  CB  . LEU   B 1 646  ? 38.73500   91.25700  7.19900   1.000 41.43022  ?  646  LEU   B CB  1 
ATOM   19066 C  CG  . LEU   B 1 646  ? 37.68000   91.95900  6.34300   1.000 40.75467  ?  646  LEU   B CG  1 
ATOM   19067 C  CD1 . LEU   B 1 646  ? 38.09400   93.38400  6.03500   1.000 58.08198  ?  646  LEU   B CD1 1 
ATOM   19068 C  CD2 . LEU   B 1 646  ? 37.44300   91.17700  5.06200   1.000 49.64634  ?  646  LEU   B CD2 1 
ATOM   19069 N  N   . GLY   B 1 647  ? 39.55300   89.19400  9.67200   1.000 55.58340  ?  647  GLY   B N   1 
ATOM   19070 C  CA  . GLY   B 1 647  ? 40.58900   88.47500  10.38900  1.000 50.55999  ?  647  GLY   B CA  1 
ATOM   19071 C  C   . GLY   B 1 647  ? 40.47100   86.96800  10.31300  1.000 54.53906  ?  647  GLY   B C   1 
ATOM   19072 O  O   . GLY   B 1 647  ? 41.36500   86.27000  10.80400  1.000 52.27086  ?  647  GLY   B O   1 
ATOM   19073 N  N   . ASN   B 1 648  ? 39.39300   86.45400  9.71700   1.000 60.97031  ?  648  ASN   B N   1 
ATOM   19074 C  CA  . ASN   B 1 648  ? 39.22900   85.01500  9.56000   1.000 77.60245  ?  648  ASN   B CA  1 
ATOM   19075 C  C   . ASN   B 1 648  ? 39.99800   84.46100  8.36900   1.000 69.09195  ?  648  ASN   B C   1 
ATOM   19076 O  O   . ASN   B 1 648  ? 40.27100   83.25600  8.33500   1.000 68.11406  ?  648  ASN   B O   1 
ATOM   19077 C  CB  . ASN   B 1 648  ? 37.74600   84.66100  9.41700   1.000 84.16610  ?  648  ASN   B CB  1 
ATOM   19078 C  CG  . ASN   B 1 648  ? 37.02200   84.63100  10.74900  1.000 70.18624  ?  648  ASN   B CG  1 
ATOM   19079 O  OD1 . ASN   B 1 648  ? 36.35700   85.59300  11.13000  1.000 72.44084  ?  648  ASN   B OD1 1 
ATOM   19080 N  ND2 . ASN   B 1 648  ? 37.14900   83.51900  11.46400  1.000 69.03668  ?  648  ASN   B ND2 1 
ATOM   19081 N  N   . ASP   B 1 649  ? 40.34500   85.30600  7.38500   1.000 75.72170  ?  649  ASP   B N   1 
ATOM   19082 C  CA  . ASP   B 1 649  ? 41.09700   84.81600  6.23400   1.000 80.28802  ?  649  ASP   B CA  1 
ATOM   19083 C  C   . ASP   B 1 649  ? 42.01400   85.87300  5.62000   1.000 68.61019  ?  649  ASP   B C   1 
ATOM   19084 O  O   . ASP   B 1 649  ? 42.36500   85.74800  4.44000   1.000 82.00319  ?  649  ASP   B O   1 
ATOM   19085 C  CB  . ASP   B 1 649  ? 40.14700   84.28100  5.14200   1.000 78.23107  ?  649  ASP   B CB  1 
ATOM   19086 C  CG  . ASP   B 1 649  ? 38.68300   84.48800  5.48200   1.000 89.26768  ?  649  ASP   B CG  1 
ATOM   19087 O  OD1 . ASP   B 1 649  ? 38.21900   85.64700  5.45200   1.000 79.96086  ?  649  ASP   B OD1 1 
ATOM   19088 O  OD2 . ASP   B 1 649  ? 37.99500   83.48800  5.78100   1.000 99.96115  -1 649  ASP   B OD2 1 
ATOM   19089 N  N   . LEU   B 1 650  ? 42.41900   86.89600  6.36800   1.000 55.57304  ?  650  LEU   B N   1 
ATOM   19090 C  CA  . LEU   B 1 650  ? 43.28700   87.94000  5.84700   1.000 60.36018  ?  650  LEU   B CA  1 
ATOM   19091 C  C   . LEU   B 1 650  ? 44.24400   88.41700  6.92900   1.000 60.09513  ?  650  LEU   B C   1 
ATOM   19092 O  O   . LEU   B 1 650  ? 43.89900   88.41500  8.11600   1.000 61.78620  ?  650  LEU   B O   1 
ATOM   19093 C  CB  . LEU   B 1 650  ? 42.48500   89.13800  5.31000   1.000 48.85897  ?  650  LEU   B CB  1 
ATOM   19094 C  CG  . LEU   B 1 650  ? 42.00300   89.02800  3.86100   1.000 45.01553  ?  650  LEU   B CG  1 
ATOM   19095 C  CD1 . LEU   B 1 650  ? 41.26500   90.28400  3.43100   1.000 44.73800  ?  650  LEU   B CD1 1 
ATOM   19096 C  CD2 . LEU   B 1 650  ? 43.17900   88.76400  2.93800   1.000 69.27144  ?  650  LEU   B CD2 1 
ATOM   19097 N  N   . PRO   B 1 651  ? 45.45200   88.81200  6.54900   1.000 59.15721  ?  651  PRO   B N   1 
ATOM   19098 C  CA  . PRO   B 1 651  ? 46.41200   89.37000  7.50700   1.000 57.59714  ?  651  PRO   B CA  1 
ATOM   19099 C  C   . PRO   B 1 651  ? 46.03400   90.79600  7.89600   1.000 52.50642  ?  651  PRO   B C   1 
ATOM   19100 O  O   . PRO   B 1 651  ? 45.01600   91.33900  7.47500   1.000 50.71183  ?  651  PRO   B O   1 
ATOM   19101 C  CB  . PRO   B 1 651  ? 47.73900   89.33700  6.74100   1.000 45.48021  ?  651  PRO   B CB  1 
ATOM   19102 C  CG  . PRO   B 1 651  ? 47.52100   88.38500  5.61000   1.000 72.39289  ?  651  PRO   B CG  1 
ATOM   19103 C  CD  . PRO   B 1 651  ? 46.07800   88.51000  5.25400   1.000 62.67048  ?  651  PRO   B CD  1 
ATOM   19104 N  N   . ASP   B 1 652  ? 46.90100   91.40700  8.70500   1.000 49.02475  ?  652  ASP   B N   1 
ATOM   19105 C  CA  . ASP   B 1 652  ? 46.61600   92.73700  9.23400   1.000 43.71451  ?  652  ASP   B CA  1 
ATOM   19106 C  C   . ASP   B 1 652  ? 46.70200   93.80100  8.14600   1.000 48.69351  ?  652  ASP   B C   1 
ATOM   19107 O  O   . ASP   B 1 652  ? 45.79600   94.63200  8.00600   1.000 46.64190  ?  652  ASP   B O   1 
ATOM   19108 C  CB  . ASP   B 1 652  ? 47.57700   93.05600  10.37900  1.000 50.89534  ?  652  ASP   B CB  1 
ATOM   19109 C  CG  . ASP   B 1 652  ? 47.57900   94.52500  10.74600  1.000 80.30346  ?  652  ASP   B CG  1 
ATOM   19110 O  OD1 . ASP   B 1 652  ? 46.49500   95.07000  11.04600  1.000 88.08422  ?  652  ASP   B OD1 1 
ATOM   19111 O  OD2 . ASP   B 1 652  ? 48.67100   95.13100  10.74700  1.000 69.83405  -1 652  ASP   B OD2 1 
ATOM   19112 N  N   . TYR   B 1 653  ? 47.78800   93.79500  7.36700   1.000 58.24477  ?  653  TYR   B N   1 
ATOM   19113 C  CA  . TYR   B 1 653  ? 47.98500   94.82700  6.35400   1.000 47.06885  ?  653  TYR   B CA  1 
ATOM   19114 C  C   . TYR   B 1 653  ? 46.91200   94.78100  5.27800   1.000 48.31962  ?  653  TYR   B C   1 
ATOM   19115 O  O   . TYR   B 1 653  ? 46.65700   95.79800  4.62300   1.000 56.13107  ?  653  TYR   B O   1 
ATOM   19116 C  CB  . TYR   B 1 653  ? 49.37300   94.69300  5.72300   1.000 37.22866  ?  653  TYR   B CB  1 
ATOM   19117 C  CG  . TYR   B 1 653  ? 49.75000   93.27900  5.33600   1.000 42.33525  ?  653  TYR   B CG  1 
ATOM   19118 C  CD1 . TYR   B 1 653  ? 50.39200   92.44000  6.23700   1.000 40.86097  ?  653  TYR   B CD1 1 
ATOM   19119 C  CD2 . TYR   B 1 653  ? 49.47000   92.78600  4.06700   1.000 46.83406  ?  653  TYR   B CD2 1 
ATOM   19120 C  CE1 . TYR   B 1 653  ? 50.74000   91.14800  5.89000   1.000 53.40631  ?  653  TYR   B CE1 1 
ATOM   19121 C  CE2 . TYR   B 1 653  ? 49.81500   91.49300  3.71100   1.000 39.86740  ?  653  TYR   B CE2 1 
ATOM   19122 C  CZ  . TYR   B 1 653  ? 50.45000   90.67900  4.62700   1.000 47.58693  ?  653  TYR   B CZ  1 
ATOM   19123 O  OH  . TYR   B 1 653  ? 50.79700   89.39200  4.28200   1.000 58.41067  ?  653  TYR   B OH  1 
ATOM   19124 N  N   . MET   B 1 654  ? 46.27700   93.62800  5.08400   1.000 52.99359  ?  654  MET   B N   1 
ATOM   19125 C  CA  . MET   B 1 654  ? 45.14700   93.49800  4.17000   1.000 53.07403  ?  654  MET   B CA  1 
ATOM   19126 C  C   . MET   B 1 654  ? 43.82200   93.53700  4.91200   1.000 54.92500  ?  654  MET   B C   1 
ATOM   19127 O  O   . MET   B 1 654  ? 42.91700   92.74800  4.64200   1.000 83.12495  ?  654  MET   B O   1 
ATOM   19128 C  CB  . MET   B 1 654  ? 45.26800   92.22000  3.34500   1.000 55.59797  ?  654  MET   B CB  1 
ATOM   19129 C  CG  . MET   B 1 654  ? 45.76500   92.43900  1.91900   1.000 63.74736  ?  654  MET   B CG  1 
ATOM   19130 S  SD  . MET   B 1 654  ? 45.70000   90.92500  0.94200   1.000 68.12794  ?  654  MET   B SD  1 
ATOM   19131 C  CE  . MET   B 1 654  ? 46.59300   89.81000  2.02000   1.000 45.02881  ?  654  MET   B CE  1 
ATOM   19132 N  N   . ILE   B 1 655  ? 43.69200   94.44800  5.86700   1.000 40.97665  ?  655  ILE   B N   1 
ATOM   19133 C  CA  . ILE   B 1 655  ? 42.39700   94.73200  6.47100   1.000 47.79329  ?  655  ILE   B CA  1 
ATOM   19134 C  C   . ILE   B 1 655  ? 42.16600   96.23200  6.34300   1.000 56.56981  ?  655  ILE   B C   1 
ATOM   19135 O  O   . ILE   B 1 655  ? 42.93600   97.02200  6.90900   1.000 58.24342  ?  655  ILE   B O   1 
ATOM   19136 C  CB  . ILE   B 1 655  ? 42.32600   94.25900  7.93100   1.000 47.83902  ?  655  ILE   B CB  1 
ATOM   19137 C  CG1 . ILE   B 1 655  ? 42.21800   92.73500  7.99100   1.000 52.01297  ?  655  ILE   B CG1 1 
ATOM   19138 C  CG2 . ILE   B 1 655  ? 41.12500   94.87900  8.61900   1.000 59.48841  ?  655  ILE   B CG2 1 
ATOM   19139 C  CD1 . ILE   B 1 655  ? 42.05600   92.18800  9.39100   1.000 43.79196  ?  655  ILE   B CD1 1 
ATOM   19140 N  N   . PRO   B 1 656  ? 41.15700   96.66300  5.58400   1.000 61.69891  ?  656  PRO   B N   1 
ATOM   19141 C  CA  . PRO   B 1 656  ? 40.93100   98.10000  5.38900   1.000 54.33679  ?  656  PRO   B CA  1 
ATOM   19142 C  C   . PRO   B 1 656  ? 40.91200   98.87000  6.70100   1.000 57.36658  ?  656  PRO   B C   1 
ATOM   19143 O  O   . PRO   B 1 656  ? 40.34700   98.42400  7.70000   1.000 68.99648  ?  656  PRO   B O   1 
ATOM   19144 C  CB  . PRO   B 1 656  ? 39.57100   98.14600  4.68800   1.000 54.77015  ?  656  PRO   B CB  1 
ATOM   19145 C  CG  . PRO   B 1 656  ? 39.52900   96.88200  3.91100   1.000 67.92572  ?  656  PRO   B CG  1 
ATOM   19146 C  CD  . PRO   B 1 656  ? 40.27000   95.85000  4.73100   1.000 57.96980  ?  656  PRO   B CD  1 
ATOM   19147 N  N   . THR   B 1 657  ? 41.55800   100.03700 6.68600   1.000 59.24721  ?  657  THR   B N   1 
ATOM   19148 C  CA  . THR   B 1 657  ? 41.64500   100.86600 7.87900   1.000 59.73400  ?  657  THR   B CA  1 
ATOM   19149 C  C   . THR   B 1 657  ? 40.35900   101.64100 8.13300   1.000 61.47923  ?  657  THR   B C   1 
ATOM   19150 O  O   . THR   B 1 657  ? 40.07100   101.99600 9.28100   1.000 70.31082  ?  657  THR   B O   1 
ATOM   19151 C  CB  . THR   B 1 657  ? 42.82100   101.83600 7.75900   1.000 57.72119  ?  657  THR   B CB  1 
ATOM   19152 O  OG1 . THR   B 1 657  ? 43.63300   101.47000 6.63700   1.000 58.55784  ?  657  THR   B OG1 1 
ATOM   19153 C  CG2 . THR   B 1 657  ? 43.66700   101.79100 9.01500   1.000 51.77812  ?  657  THR   B CG2 1 
ATOM   19154 N  N   . TYR   B 1 658  ? 39.58100   101.90600 7.08500   1.000 55.42190  ?  658  TYR   B N   1 
ATOM   19155 C  CA  . TYR   B 1 658  ? 38.32900   102.64000 7.18800   1.000 64.53391  ?  658  TYR   B CA  1 
ATOM   19156 C  C   . TYR   B 1 658  ? 37.24000   101.88100 6.44200   1.000 62.90138  ?  658  TYR   B C   1 
ATOM   19157 O  O   . TYR   B 1 658  ? 37.49800   101.28300 5.39400   1.000 78.81387  ?  658  TYR   B O   1 
ATOM   19158 C  CB  . TYR   B 1 658  ? 38.46800   104.06200 6.62000   1.000 54.86102  ?  658  TYR   B CB  1 
ATOM   19159 C  CG  . TYR   B 1 658  ? 39.57000   104.87900 7.26300   1.000 61.24465  ?  658  TYR   B CG  1 
ATOM   19160 C  CD1 . TYR   B 1 658  ? 39.31900   105.65600 8.38600   1.000 68.04958  ?  658  TYR   B CD1 1 
ATOM   19161 C  CD2 . TYR   B 1 658  ? 40.86000   104.87400 6.74600   1.000 62.75186  ?  658  TYR   B CD2 1 
ATOM   19162 C  CE1 . TYR   B 1 658  ? 40.32100   106.40400 8.97700   1.000 71.08098  ?  658  TYR   B CE1 1 
ATOM   19163 C  CE2 . TYR   B 1 658  ? 41.86900   105.62000 7.33200   1.000 70.72198  ?  658  TYR   B CE2 1 
ATOM   19164 C  CZ  . TYR   B 1 658  ? 41.59300   106.38400 8.44700   1.000 69.72985  ?  658  TYR   B CZ  1 
ATOM   19165 O  OH  . TYR   B 1 658  ? 42.59000   107.12800 9.03500   1.000 79.39873  ?  658  TYR   B OH  1 
ATOM   19166 N  N   . PHE   B 1 659  ? 36.02700   101.89600 6.99100   1.000 57.18034  ?  659  PHE   B N   1 
ATOM   19167 C  CA  . PHE   B 1 659  ? 34.88000   101.23900 6.37900   1.000 63.50793  ?  659  PHE   B CA  1 
ATOM   19168 C  C   . PHE   B 1 659  ? 33.74700   102.24400 6.22700   1.000 74.26857  ?  659  PHE   B C   1 
ATOM   19169 O  O   . PHE   B 1 659  ? 33.55700   103.11200 7.08600   1.000 82.90492  ?  659  PHE   B O   1 
ATOM   19170 C  CB  . PHE   B 1 659  ? 34.40800   100.03500 7.20700   1.000 59.26549  ?  659  PHE   B CB  1 
ATOM   19171 C  CG  . PHE   B 1 659  ? 35.43800   98.94400  7.34100   1.000 63.11728  ?  659  PHE   B CG  1 
ATOM   19172 C  CD1 . PHE   B 1 659  ? 35.60700   98.00200  6.33900   1.000 69.24366  ?  659  PHE   B CD1 1 
ATOM   19173 C  CD2 . PHE   B 1 659  ? 36.22900   98.85500  8.47500   1.000 67.00289  ?  659  PHE   B CD2 1 
ATOM   19174 C  CE1 . PHE   B 1 659  ? 36.55000   96.99500  6.46300   1.000 59.38628  ?  659  PHE   B CE1 1 
ATOM   19175 C  CE2 . PHE   B 1 659  ? 37.17300   97.85100  8.60500   1.000 65.54740  ?  659  PHE   B CE2 1 
ATOM   19176 C  CZ  . PHE   B 1 659  ? 37.33300   96.92100  7.59700   1.000 67.25355  ?  659  PHE   B CZ  1 
ATOM   19177 N  N   . VAL   B 1 660  ? 32.99500   102.12300 5.13300   1.000 74.72713  ?  660  VAL   B N   1 
ATOM   19178 C  CA  . VAL   B 1 660  ? 31.92300   103.05500 4.79800   1.000 85.89999  ?  660  VAL   B CA  1 
ATOM   19179 C  C   . VAL   B 1 660  ? 30.67500   102.26300 4.43400   1.000 86.22288  ?  660  VAL   B C   1 
ATOM   19180 O  O   . VAL   B 1 660  ? 30.72400   101.38100 3.57000   1.000 87.62179  ?  660  VAL   B O   1 
ATOM   19181 C  CB  . VAL   B 1 660  ? 32.32400   103.99200 3.64200   1.000 77.41698  ?  660  VAL   B CB  1 
ATOM   19182 C  CG1 . VAL   B 1 660  ? 31.08900   104.48300 2.89700   1.000 68.63140  ?  660  VAL   B CG1 1 
ATOM   19183 C  CG2 . VAL   B 1 660  ? 33.12400   105.16800 4.17300   1.000 79.87057  ?  660  VAL   B CG2 1 
ATOM   19184 N  N   . HIS   B 1 661  ? 29.56000   102.58800 5.08300   1.000 87.13537  ?  661  HIS   B N   1 
ATOM   19185 C  CA  . HIS   B 1 661  ? 28.27800   101.94700 4.82300   1.000 81.09185  ?  661  HIS   B CA  1 
ATOM   19186 C  C   . HIS   B 1 661  ? 27.43900   102.81300 3.89400   1.000 78.01002  ?  661  HIS   B C   1 
ATOM   19187 O  O   . HIS   B 1 661  ? 27.21800   103.99700 4.16900   1.000 73.51499  ?  661  HIS   B O   1 
ATOM   19188 C  CB  . HIS   B 1 661  ? 27.51300   101.69500 6.12300   1.000 75.97812  ?  661  HIS   B CB  1 
ATOM   19189 C  CG  . HIS   B 1 661  ? 26.13300   101.15600 5.91300   1.000 72.87167  ?  661  HIS   B CG  1 
ATOM   19190 N  ND1 . HIS   B 1 661  ? 24.99900   101.91100 6.12000   1.000 82.96099  ?  661  HIS   B ND1 1 
ATOM   19191 C  CD2 . HIS   B 1 661  ? 25.70400   99.93800  5.50500   1.000 77.01086  ?  661  HIS   B CD2 1 
ATOM   19192 C  CE1 . HIS   B 1 661  ? 23.93100   101.18000 5.85400   1.000 73.48486  ?  661  HIS   B CE1 1 
ATOM   19193 N  NE2 . HIS   B 1 661  ? 24.33100   99.97900  5.47800   1.000 76.10178  ?  661  HIS   B NE2 1 
ATOM   19194 N  N   . MET   B 1 662  ? 26.96900   102.21500 2.80200   1.000 85.09827  ?  662  MET   B N   1 
ATOM   19195 C  CA  . MET   B 1 662  ? 26.07200   102.87400 1.86600   1.000 97.22457  ?  662  MET   B CA  1 
ATOM   19196 C  C   . MET   B 1 662  ? 24.95600   101.91200 1.49000   1.000 95.80211  ?  662  MET   B C   1 
ATOM   19197 O  O   . MET   B 1 662  ? 25.16600   100.70100 1.40000   1.000 100.55071 ?  662  MET   B O   1 
ATOM   19198 C  CB  . MET   B 1 662  ? 26.80400   103.33600 0.60300   1.000 81.15646  ?  662  MET   B CB  1 
ATOM   19199 C  CG  . MET   B 1 662  ? 27.81400   104.44000 0.83400   1.000 75.94864  ?  662  MET   B CG  1 
ATOM   19200 S  SD  . MET   B 1 662  ? 28.77300   104.75000 -0.65500  1.000 93.55026  ?  662  MET   B SD  1 
ATOM   19201 C  CE  . MET   B 1 662  ? 29.54600   103.15400 -0.87500  1.000 73.48616  ?  662  MET   B CE  1 
ATOM   19202 N  N   . LYS   B 1 663  ? 23.76600   102.46400 1.27000   1.000 85.74430  ?  663  LYS   B N   1 
ATOM   19203 C  CA  . LYS   B 1 663  ? 22.61600   101.66600 0.87000   1.000 71.97126  ?  663  LYS   B CA  1 
ATOM   19204 C  C   . LYS   B 1 663  ? 22.54600   101.43300 -0.63300  1.000 78.01722  ?  663  LYS   B C   1 
ATOM   19205 O  O   . LYS   B 1 663  ? 21.72300   100.62400 -1.07800  1.000 80.70761  ?  663  LYS   B O   1 
ATOM   19206 C  CB  . LYS   B 1 663  ? 21.31900   102.33200 1.34300   1.000 93.60079  ?  663  LYS   B CB  1 
ATOM   19207 N  N   . ALA   B 1 664  ? 23.38100   102.10800 -1.42100  1.000 98.56791  ?  664  ALA   B N   1 
ATOM   19208 C  CA  . ALA   B 1 664  ? 23.34100   101.97400 -2.87100  1.000 79.99925  ?  664  ALA   B CA  1 
ATOM   19209 C  C   . ALA   B 1 664  ? 24.69900   102.32200 -3.46100  1.000 86.01141  ?  664  ALA   B C   1 
ATOM   19210 O  O   . ALA   B 1 664  ? 25.23800   103.39900 -3.19000  1.000 87.65715  ?  664  ALA   B O   1 
ATOM   19211 C  CB  . ALA   B 1 664  ? 22.25800   102.87400 -3.47700  1.000 81.77761  ?  664  ALA   B CB  1 
ATOM   19212 N  N   . PHE   B 1 665  ? 25.24100   101.41100 -4.26400  1.000 87.72735  ?  665  PHE   B N   1 
ATOM   19213 C  CA  . PHE   B 1 665  ? 26.46700   101.68700 -5.00400  1.000 78.73024  ?  665  PHE   B CA  1 
ATOM   19214 C  C   . PHE   B 1 665  ? 26.13900   102.50300 -6.24800  1.000 79.97706  ?  665  PHE   B C   1 
ATOM   19215 O  O   . PHE   B 1 665  ? 25.32100   102.06400 -7.06500  1.000 71.78722  ?  665  PHE   B O   1 
ATOM   19216 C  CB  . PHE   B 1 665  ? 27.16300   100.39300 -5.41000  1.000 65.10881  ?  665  PHE   B CB  1 
ATOM   19217 C  CG  . PHE   B 1 665  ? 28.17600   99.90000  -4.41500  1.000 68.63411  ?  665  PHE   B CG  1 
ATOM   19218 C  CD1 . PHE   B 1 665  ? 28.31800   100.50900 -3.18000  1.000 68.47616  ?  665  PHE   B CD1 1 
ATOM   19219 C  CD2 . PHE   B 1 665  ? 29.00100   98.83000  -4.72700  1.000 73.85563  ?  665  PHE   B CD2 1 
ATOM   19220 C  CE1 . PHE   B 1 665  ? 29.25300   100.04800 -2.26900  1.000 71.74037  ?  665  PHE   B CE1 1 
ATOM   19221 C  CE2 . PHE   B 1 665  ? 29.93900   98.36900  -3.82400  1.000 61.53773  ?  665  PHE   B CE2 1 
ATOM   19222 C  CZ  . PHE   B 1 665  ? 30.06500   98.97900  -2.59300  1.000 74.62228  ?  665  PHE   B CZ  1 
ATOM   19223 N  N   . PRO   B 1 666  ? 26.73500   103.67900 -6.43100  1.000 89.80992  ?  666  PRO   B N   1 
ATOM   19224 C  CA  . PRO   B 1 666  ? 26.52100   104.42000 -7.67800  1.000 88.33623  ?  666  PRO   B CA  1 
ATOM   19225 C  C   . PRO   B 1 666  ? 27.19000   103.72100 -8.85100  1.000 83.27608  ?  666  PRO   B C   1 
ATOM   19226 O  O   . PRO   B 1 666  ? 28.31500   103.22700 -8.74600  1.000 73.57045  ?  666  PRO   B O   1 
ATOM   19227 C  CB  . PRO   B 1 666  ? 27.16100   105.78400 -7.39700  1.000 107.42297 ?  666  PRO   B CB  1 
ATOM   19228 C  CG  . PRO   B 1 666  ? 28.17600   105.50700 -6.33800  1.000 103.88374 ?  666  PRO   B CG  1 
ATOM   19229 C  CD  . PRO   B 1 666  ? 27.58700   104.41900 -5.48500  1.000 96.42354  ?  666  PRO   B CD  1 
ATOM   19230 N  N   . LEU   B 1 667  ? 26.48000   103.68200 -9.97400  1.000 76.38328  ?  667  LEU   B N   1 
ATOM   19231 C  CA  . LEU   B 1 667  ? 26.94500   103.01500 -11.18100 1.000 82.94418  ?  667  LEU   B CA  1 
ATOM   19232 C  C   . LEU   B 1 667  ? 27.19200   104.04400 -12.27600 1.000 83.13578  ?  667  LEU   B C   1 
ATOM   19233 O  O   . LEU   B 1 667  ? 26.40700   104.98200 -12.44700 1.000 82.72628  ?  667  LEU   B O   1 
ATOM   19234 C  CB  . LEU   B 1 667  ? 25.92600   101.97400 -11.65300 1.000 63.68893  ?  667  LEU   B CB  1 
ATOM   19235 C  CG  . LEU   B 1 667  ? 26.44900   100.56300 -11.92900 1.000 61.84698  ?  667  LEU   B CG  1 
ATOM   19236 C  CD1 . LEU   B 1 667  ? 27.22600   100.03300 -10.73600 1.000 73.48027  ?  667  LEU   B CD1 1 
ATOM   19237 C  CD2 . LEU   B 1 667  ? 25.30000   99.62900  -12.27200 1.000 48.59714  ?  667  LEU   B CD2 1 
ATOM   19238 N  N   . THR   B 1 668  ? 28.28800   103.86700 -13.01300 1.000 86.53819  ?  668  THR   B N   1 
ATOM   19239 C  CA  . THR   B 1 668  ? 28.62900   104.78100 -14.09200 1.000 101.29868 ?  668  THR   B CA  1 
ATOM   19240 C  C   . THR   B 1 668  ? 27.75200   104.50900 -15.31300 1.000 104.69807 ?  668  THR   B C   1 
ATOM   19241 O  O   . THR   B 1 668  ? 26.86000   103.65600 -15.30000 1.000 102.72130 ?  668  THR   B O   1 
ATOM   19242 C  CB  . THR   B 1 668  ? 30.11000   104.66700 -14.45200 1.000 91.37247  ?  668  THR   B CB  1 
ATOM   19243 O  OG1 . THR   B 1 668  ? 30.38100   103.36200 -14.97700 1.000 92.65107  ?  668  THR   B OG1 1 
ATOM   19244 C  CG2 . THR   B 1 668  ? 30.97700   104.90600 -13.22800 1.000 87.42846  ?  668  THR   B CG2 1 
ATOM   19245 N  N   . ALA   B 1 669  ? 28.01700   105.24700 -16.39200 1.000 102.38510 ?  669  ALA   B N   1 
ATOM   19246 C  CA  . ALA   B 1 669  ? 27.22100   105.12000 -17.60500 1.000 100.59504 ?  669  ALA   B CA  1 
ATOM   19247 C  C   . ALA   B 1 669  ? 27.49400   103.83000 -18.36600 1.000 97.38386  ?  669  ALA   B C   1 
ATOM   19248 O  O   . ALA   B 1 669  ? 26.72400   103.49500 -19.27200 1.000 103.26822 ?  669  ALA   B O   1 
ATOM   19249 C  CB  . ALA   B 1 669  ? 27.46600   106.32000 -18.52100 1.000 108.82446 ?  669  ALA   B CB  1 
ATOM   19250 N  N   . ASN   B 1 670  ? 28.55500   103.09800 -18.02600 1.000 82.96972  ?  670  ASN   B N   1 
ATOM   19251 C  CA  . ASN   B 1 670  ? 28.90300   101.86800 -18.72800 1.000 90.86327  ?  670  ASN   B CA  1 
ATOM   19252 C  C   . ASN   B 1 670  ? 28.92900   100.66200 -17.79800 1.000 91.01628  ?  670  ASN   B C   1 
ATOM   19253 O  O   . ASN   B 1 670  ? 29.72500   99.74000  -17.99000 1.000 77.71245  ?  670  ASN   B O   1 
ATOM   19254 C  CB  . ASN   B 1 670  ? 30.24100   102.02000 -19.44300 1.000 83.42455  ?  670  ASN   B CB  1 
ATOM   19255 C  CG  . ASN   B 1 670  ? 30.11100   102.79700 -20.72100 1.000 92.52483  ?  670  ASN   B CG  1 
ATOM   19256 O  OD1 . ASN   B 1 670  ? 30.66800   103.88600 -20.86500 1.000 90.60227  ?  670  ASN   B OD1 1 
ATOM   19257 N  ND2 . ASN   B 1 670  ? 29.35100   102.24900 -21.66000 1.000 92.11158  ?  670  ASN   B ND2 1 
ATOM   19258 N  N   . GLY   B 1 671  ? 28.05700   100.65200 -16.79600 1.000 82.49093  ?  671  GLY   B N   1 
ATOM   19259 C  CA  . GLY   B 1 671  ? 27.95300   99.50600  -15.91700 1.000 73.40320  ?  671  GLY   B CA  1 
ATOM   19260 C  C   . GLY   B 1 671  ? 29.15600   99.27900  -15.03000 1.000 85.23183  ?  671  GLY   B C   1 
ATOM   19261 O  O   . GLY   B 1 671  ? 29.39500   98.14600  -14.60300 1.000 83.80294  ?  671  GLY   B O   1 
ATOM   19262 N  N   . LYS   B 1 672  ? 29.92800   100.32300 -14.75200 1.000 93.11075  ?  672  LYS   B N   1 
ATOM   19263 C  CA  . LYS   B 1 672  ? 31.02800   100.26100 -13.80300 1.000 84.13463  ?  672  LYS   B CA  1 
ATOM   19264 C  C   . LYS   B 1 672  ? 30.65600   101.03500 -12.54500 1.000 79.12289  ?  672  LYS   B C   1 
ATOM   19265 O  O   . LYS   B 1 672  ? 29.77800   101.90200 -12.55900 1.000 78.76281  ?  672  LYS   B O   1 
ATOM   19266 C  CB  . LYS   B 1 672  ? 32.31800   100.83100 -14.40700 1.000 85.22190  ?  672  LYS   B CB  1 
ATOM   19267 C  CG  . LYS   B 1 672  ? 32.71600   100.23800 -15.75200 1.000 55.58495  ?  672  LYS   B CG  1 
ATOM   19268 C  CD  . LYS   B 1 672  ? 32.99100   98.74600  -15.65400 1.000 61.69857  ?  672  LYS   B CD  1 
ATOM   19269 C  CE  . LYS   B 1 672  ? 33.86400   98.26800  -16.80500 1.000 80.86776  ?  672  LYS   B CE  1 
ATOM   19270 N  NZ  . LYS   B 1 672  ? 35.25500   98.79600  -16.70400 1.000 64.77607  ?  672  LYS   B NZ  1 
ATOM   19271 N  N   . VAL   B 1 673  ? 31.33200   100.71000 -11.44900 1.000 83.72084  ?  673  VAL   B N   1 
ATOM   19272 C  CA  . VAL   B 1 673  ? 31.08100   101.38200 -10.18000 1.000 92.13954  ?  673  VAL   B CA  1 
ATOM   19273 C  C   . VAL   B 1 673  ? 31.72200   102.76200 -10.21000 1.000 100.34714 ?  673  VAL   B C   1 
ATOM   19274 O  O   . VAL   B 1 673  ? 32.84500   102.93400 -10.70100 1.000 91.79891  ?  673  VAL   B O   1 
ATOM   19275 C  CB  . VAL   B 1 673  ? 31.61200   100.54300 -9.00400  1.000 80.43886  ?  673  VAL   B CB  1 
ATOM   19276 C  CG1 . VAL   B 1 673  ? 31.04000   101.05100 -7.68800  1.000 70.92661  ?  673  VAL   B CG1 1 
ATOM   19277 C  CG2 . VAL   B 1 673  ? 31.28200   99.07400  -9.20700  1.000 69.27893  ?  673  VAL   B CG2 1 
ATOM   19278 N  N   . ASP   B 1 674  ? 31.00400   103.75800 -9.68800  1.000 95.99233  ?  674  ASP   B N   1 
ATOM   19279 C  CA  . ASP   B 1 674  ? 31.50100   105.13200 -9.64000  1.000 95.32489  ?  674  ASP   B CA  1 
ATOM   19280 C  C   . ASP   B 1 674  ? 32.43900   105.27600 -8.43900  1.000 106.35834 ?  674  ASP   B C   1 
ATOM   19281 O  O   . ASP   B 1 674  ? 32.11100   105.86100 -7.40400  1.000 103.46897 ?  674  ASP   B O   1 
ATOM   19282 C  CB  . ASP   B 1 674  ? 30.34200   106.11800 -9.58300  1.000 93.24984  ?  674  ASP   B CB  1 
ATOM   19283 C  CG  . ASP   B 1 674  ? 30.57200   107.33800 -10.45500 1.000 108.42064 ?  674  ASP   B CG  1 
ATOM   19284 O  OD1 . ASP   B 1 674  ? 31.71800   107.54300 -10.90600 1.000 101.90075 ?  674  ASP   B OD1 1 
ATOM   19285 O  OD2 . ASP   B 1 674  ? 29.60100   108.08500 -10.69900 1.000 120.61158 -1 674  ASP   B OD2 1 
ATOM   19286 N  N   . ARG   B 1 675  ? 33.64000   104.71300 -8.60300  1.000 106.79359 ?  675  ARG   B N   1 
ATOM   19287 C  CA  . ARG   B 1 675  ? 34.61800   104.70300 -7.52100  1.000 90.68301  ?  675  ARG   B CA  1 
ATOM   19288 C  C   . ARG   B 1 675  ? 35.08000   106.10900 -7.16200  1.000 83.41246  ?  675  ARG   B C   1 
ATOM   19289 O  O   . ARG   B 1 675  ? 35.43900   106.36800 -6.00800  1.000 80.35005  ?  675  ARG   B O   1 
ATOM   19290 C  CB  . ARG   B 1 675  ? 35.80800   103.82500 -7.91000  1.000 75.52207  ?  675  ARG   B CB  1 
ATOM   19291 C  CG  . ARG   B 1 675  ? 35.47000   102.34300 -7.98100  1.000 75.01234  ?  675  ARG   B CG  1 
ATOM   19292 C  CD  . ARG   B 1 675  ? 36.09800   101.67100 -9.19200  1.000 95.61968  ?  675  ARG   B CD  1 
ATOM   19293 N  NE  . ARG   B 1 675  ? 37.54300   101.85600 -9.24500  1.000 113.62044 ?  675  ARG   B NE  1 
ATOM   19294 C  CZ  . ARG   B 1 675  ? 38.36200   101.13200 -9.99600  1.000 107.38640 ?  675  ARG   B CZ  1 
ATOM   19295 N  NH1 . ARG   B 1 675  ? 37.91300   100.14200 -10.75100 1.000 99.21545  ?  675  ARG   B NH1 1 
ATOM   19296 N  NH2 . ARG   B 1 675  ? 39.66300   101.40600 -9.98600  1.000 94.23146  ?  675  ARG   B NH2 1 
ATOM   19297 N  N   . ARG   B 1 676  ? 35.07500   107.02600 -8.12700  1.000 94.26441  ?  676  ARG   B N   1 
ATOM   19298 C  CA  . ARG   B 1 676  ? 35.40200   108.42000 -7.85900  1.000 98.29844  ?  676  ARG   B CA  1 
ATOM   19299 C  C   . ARG   B 1 676  ? 34.24500   109.18700 -7.23100  1.000 104.03043 ?  676  ARG   B C   1 
ATOM   19300 O  O   . ARG   B 1 676  ? 34.38500   110.38900 -6.98100  1.000 101.30190 ?  676  ARG   B O   1 
ATOM   19301 C  CB  . ARG   B 1 676  ? 35.84100   109.11500 -9.15100  1.000 73.78642  ?  676  ARG   B CB  1 
ATOM   19302 N  N   . ALA   B 1 677  ? 33.11300   108.52800 -6.97200  1.000 101.28700 ?  677  ALA   B N   1 
ATOM   19303 C  CA  . ALA   B 1 677  ? 31.95600   109.16600 -6.36400  1.000 106.38805 ?  677  ALA   B CA  1 
ATOM   19304 C  C   . ALA   B 1 677  ? 31.63500   108.64100 -4.97300  1.000 106.39674 ?  677  ALA   B C   1 
ATOM   19305 O  O   . ALA   B 1 677  ? 30.74500   109.19100 -4.31400  1.000 102.47094 ?  677  ALA   B O   1 
ATOM   19306 C  CB  . ALA   B 1 677  ? 30.72100   108.99800 -7.26200  1.000 88.97669  ?  677  ALA   B CB  1 
ATOM   19307 N  N   . LEU   B 1 678  ? 32.32100   107.60000 -4.51400  1.000 102.48257 ?  678  LEU   B N   1 
ATOM   19308 C  CA  . LEU   B 1 678  ? 32.08700   107.09200 -3.17200  1.000 92.43470  ?  678  LEU   B CA  1 
ATOM   19309 C  C   . LEU   B 1 678  ? 32.61600   108.08900 -2.14300  1.000 91.06394  ?  678  LEU   B C   1 
ATOM   19310 O  O   . LEU   B 1 678  ? 33.69800   108.65600 -2.32700  1.000 87.42892  ?  678  LEU   B O   1 
ATOM   19311 C  CB  . LEU   B 1 678  ? 32.76200   105.73400 -2.99000  1.000 84.32366  ?  678  LEU   B CB  1 
ATOM   19312 C  CG  . LEU   B 1 678  ? 32.45000   104.69800 -4.07300  1.000 81.04421  ?  678  LEU   B CG  1 
ATOM   19313 C  CD1 . LEU   B 1 678  ? 33.22300   103.40800 -3.84200  1.000 70.81176  ?  678  LEU   B CD1 1 
ATOM   19314 C  CD2 . LEU   B 1 678  ? 30.95800   104.42500 -4.13600  1.000 73.01760  ?  678  LEU   B CD2 1 
ATOM   19315 N  N   . PRO   B 1 679  ? 31.87900   108.32800 -1.05800  1.000 91.59435  ?  679  PRO   B N   1 
ATOM   19316 C  CA  . PRO   B 1 679  ? 32.29000   109.36100 -0.10000  1.000 90.14762  ?  679  PRO   B CA  1 
ATOM   19317 C  C   . PRO   B 1 679  ? 33.63300   109.04300 0.54000   1.000 99.85691  ?  679  PRO   B C   1 
ATOM   19318 O  O   . PRO   B 1 679  ? 33.97500   107.88400 0.78600   1.000 100.16632 ?  679  PRO   B O   1 
ATOM   19319 C  CB  . PRO   B 1 679  ? 31.16000   109.35500 0.93700   1.000 78.13056  ?  679  PRO   B CB  1 
ATOM   19320 C  CG  . PRO   B 1 679  ? 30.51500   108.01300 0.79500   1.000 80.96858  ?  679  PRO   B CG  1 
ATOM   19321 C  CD  . PRO   B 1 679  ? 30.62300   107.67400 -0.66000  1.000 93.52065  ?  679  PRO   B CD  1 
ATOM   19322 N  N   . ASP   B 1 680  ? 34.39800   110.09800 0.80200   1.000 95.48509  ?  680  ASP   B N   1 
ATOM   19323 C  CA  . ASP   B 1 680  ? 35.71300   109.97800 1.40600   1.000 85.50411  ?  680  ASP   B CA  1 
ATOM   19324 C  C   . ASP   B 1 680  ? 35.59600   109.97500 2.93000   1.000 99.09260  ?  680  ASP   B C   1 
ATOM   19325 O  O   . ASP   B 1 680  ? 34.52500   110.19200 3.49900   1.000 94.27407  ?  680  ASP   B O   1 
ATOM   19326 C  CB  . ASP   B 1 680  ? 36.61900   111.11200 0.92600   1.000 67.63324  ?  680  ASP   B CB  1 
ATOM   19327 C  CG  . ASP   B 1 680  ? 38.04900   110.66300 0.70100   1.000 86.78091  ?  680  ASP   B CG  1 
ATOM   19328 O  OD1 . ASP   B 1 680  ? 38.64400   110.07500 1.62900   1.000 82.15504  ?  680  ASP   B OD1 1 
ATOM   19329 O  OD2 . ASP   B 1 680  ? 38.57500   110.88800 -0.41000  1.000 93.73731  -1 680  ASP   B OD2 1 
ATOM   19330 N  N   . VAL   B 1 681  ? 36.72300   109.72100 3.59300   1.000 100.95590 ?  681  VAL   B N   1 
ATOM   19331 C  CA  . VAL   B 1 681  ? 36.77100   109.60700 5.04300   1.000 88.27312  ?  681  VAL   B CA  1 
ATOM   19332 C  C   . VAL   B 1 681  ? 37.77800   110.61400 5.59200   1.000 93.31599  ?  681  VAL   B C   1 
ATOM   19333 O  O   . VAL   B 1 681  ? 38.60500   111.16600 4.86500   1.000 88.63133  ?  681  VAL   B O   1 
ATOM   19334 C  CB  . VAL   B 1 681  ? 37.11600   108.18000 5.50800   1.000 81.27718  ?  681  VAL   B CB  1 
ATOM   19335 C  CG1 . VAL   B 1 681  ? 35.87500   107.30100 5.49400   1.000 85.65453  ?  681  VAL   B CG1 1 
ATOM   19336 C  CG2 . VAL   B 1 681  ? 38.20600   107.58400 4.62500   1.000 81.44474  ?  681  VAL   B CG2 1 
ATOM   19337 N  N   . GLN   B 1 682  ? 37.69100   110.84800 6.90000   1.000 100.92082 ?  682  GLN   B N   1 
ATOM   19338 C  CA  . GLN   B 1 682  ? 38.62600   111.72300 7.60400   1.000 107.08211 ?  682  GLN   B CA  1 
ATOM   19339 C  C   . GLN   B 1 682  ? 39.89600   110.92800 7.87100   1.000 106.10604 ?  682  GLN   B C   1 
ATOM   19340 O  O   . GLN   B 1 682  ? 39.95800   110.11900 8.79900   1.000 100.88668 ?  682  GLN   B O   1 
ATOM   19341 C  CB  . GLN   B 1 682  ? 38.00600   112.24700 8.89600   1.000 108.88967 ?  682  GLN   B CB  1 
ATOM   19342 C  CG  . GLN   B 1 682  ? 38.71200   113.46000 9.49600   1.000 119.41778 ?  682  GLN   B CG  1 
ATOM   19343 C  CD  . GLN   B 1 682  ? 39.95500   113.09400 10.28700  1.000 111.03219 ?  682  GLN   B CD  1 
ATOM   19344 O  OE1 . GLN   B 1 682  ? 39.88100   112.39100 11.29400  1.000 108.14033 ?  682  GLN   B OE1 1 
ATOM   19345 N  NE2 . GLN   B 1 682  ? 41.10800   113.57300 9.83200   1.000 98.34364  ?  682  GLN   B NE2 1 
ATOM   19346 N  N   . ALA   B 1 683  ? 40.91600   111.15200 7.04700   1.000 102.17658 ?  683  ALA   B N   1 
ATOM   19347 C  CA  . ALA   B 1 683  ? 42.17300   110.41400 7.12700   1.000 79.04581  ?  683  ALA   B CA  1 
ATOM   19348 C  C   . ALA   B 1 683  ? 43.15100   111.21600 7.97700   1.000 69.00150  ?  683  ALA   B C   1 
ATOM   19349 O  O   . ALA   B 1 683  ? 43.71400   112.21400 7.51800   1.000 73.76224  ?  683  ALA   B O   1 
ATOM   19350 C  CB  . ALA   B 1 683  ? 42.73100   110.14800 5.73300   1.000 89.92630  ?  683  ALA   B CB  1 
ATOM   19351 N  N   . ASP   B 1 684  ? 43.34800   110.78300 9.22100   1.000 74.65003  ?  684  ASP   B N   1 
ATOM   19352 C  CA  . ASP   B 1 684  ? 44.38800   111.37600 10.04700  1.000 82.30892  ?  684  ASP   B CA  1 
ATOM   19353 C  C   . ASP   B 1 684  ? 45.75700   111.11900 9.42400   1.000 75.19528  ?  684  ASP   B C   1 
ATOM   19354 O  O   . ASP   B 1 684  ? 45.93500   110.22400 8.59400   1.000 72.28354  ?  684  ASP   B O   1 
ATOM   19355 C  CB  . ASP   B 1 684  ? 44.33400   110.82400 11.47600  1.000 76.95442  ?  684  ASP   B CB  1 
ATOM   19356 C  CG  . ASP   B 1 684  ? 44.26600   109.30500 11.52100  1.000 92.20204  ?  684  ASP   B CG  1 
ATOM   19357 O  OD1 . ASP   B 1 684  ? 45.02200   108.64900 10.78000  1.000 93.24786  ?  684  ASP   B OD1 1 
ATOM   19358 O  OD2 . ASP   B 1 684  ? 43.46700   108.76400 12.31500  1.000 88.92992  -1 684  ASP   B OD2 1 
ATOM   19359 N  N   . ALA   B 1 685  ? 46.73800   111.92100 9.83600   1.000 71.76952  ?  685  ALA   B N   1 
ATOM   19360 C  CA  . ALA   B 1 685  ? 48.06300   111.81400 9.24000   1.000 58.77520  ?  685  ALA   B CA  1 
ATOM   19361 C  C   . ALA   B 1 685  ? 48.77300   110.51700 9.60600   1.000 67.01238  ?  685  ALA   B C   1 
ATOM   19362 O  O   . ALA   B 1 685  ? 49.74200   110.15100 8.93500   1.000 74.39476  ?  685  ALA   B O   1 
ATOM   19363 C  CB  . ALA   B 1 685  ? 48.92500   113.00800 9.65100   1.000 63.19378  ?  685  ALA   B CB  1 
ATOM   19364 N  N   . GLU   B 1 686  ? 48.31800   109.80900 10.64100  1.000 65.29768  ?  686  GLU   B N   1 
ATOM   19365 C  CA  . GLU   B 1 686  ? 49.00700   108.61100 11.10300  1.000 65.81840  ?  686  GLU   B CA  1 
ATOM   19366 C  C   . GLU   B 1 686  ? 48.29900   107.31300 10.73200  1.000 68.01491  ?  686  GLU   B C   1 
ATOM   19367 O  O   . GLU   B 1 686  ? 48.86900   106.23900 10.95400  1.000 83.30948  ?  686  GLU   B O   1 
ATOM   19368 C  CB  . GLU   B 1 686  ? 49.21200   108.67100 12.62300  1.000 76.35015  ?  686  GLU   B CB  1 
ATOM   19369 C  CG  . GLU   B 1 686  ? 50.65000   108.97400 13.02300  1.000 81.89542  ?  686  GLU   B CG  1 
ATOM   19370 C  CD  . GLU   B 1 686  ? 50.75500   109.76000 14.31500  1.000 81.32236  ?  686  GLU   B CD  1 
ATOM   19371 O  OE1 . GLU   B 1 686  ? 49.87700   109.60400 15.18900  1.000 81.31835  ?  686  GLU   B OE1 1 
ATOM   19372 O  OE2 . GLU   B 1 686  ? 51.71900   110.54300 14.45100  1.000 72.50401  -1 686  GLU   B OE2 1 
ATOM   19373 N  N   . LEU   B 1 687  ? 47.08900   107.38200 10.17000  1.000 64.51617  ?  687  LEU   B N   1 
ATOM   19374 C  CA  . LEU   B 1 687  ? 46.36300   106.19600 9.69900   1.000 59.74793  ?  687  LEU   B CA  1 
ATOM   19375 C  C   . LEU   B 1 687  ? 46.18900   105.17000 10.81600  1.000 60.42631  ?  687  LEU   B C   1 
ATOM   19376 O  O   . LEU   B 1 687  ? 46.30900   103.96200 10.60000  1.000 56.21912  ?  687  LEU   B O   1 
ATOM   19377 C  CB  . LEU   B 1 687  ? 47.05400   105.57100 8.48600   1.000 68.92724  ?  687  LEU   B CB  1 
ATOM   19378 C  CG  . LEU   B 1 687  ? 46.57400   105.96800 7.08900   1.000 70.16452  ?  687  LEU   B CG  1 
ATOM   19379 C  CD1 . LEU   B 1 687  ? 46.23600   107.44600 7.00900   1.000 73.92820  ?  687  LEU   B CD1 1 
ATOM   19380 C  CD2 . LEU   B 1 687  ? 47.65100   105.61800 6.07600   1.000 69.94048  ?  687  LEU   B CD2 1 
ATOM   19381 N  N   . LEU   B 1 688  ? 45.90200   105.65700 12.02300  1.000 59.24972  ?  688  LEU   B N   1 
ATOM   19382 C  CA  . LEU   B 1 688  ? 45.78000   104.76900 13.17400  1.000 71.27688  ?  688  LEU   B CA  1 
ATOM   19383 C  C   . LEU   B 1 688  ? 44.42800   104.06800 13.20600  1.000 68.71803  ?  688  LEU   B C   1 
ATOM   19384 O  O   . LEU   B 1 688  ? 44.35900   102.86300 13.47600  1.000 60.80406  ?  688  LEU   B O   1 
ATOM   19385 C  CB  . LEU   B 1 688  ? 46.00800   105.55500 14.46500  1.000 56.92633  ?  688  LEU   B CB  1 
ATOM   19386 C  CG  . LEU   B 1 688  ? 47.43000   106.08400 14.65300  1.000 55.78167  ?  688  LEU   B CG  1 
ATOM   19387 C  CD1 . LEU   B 1 688  ? 47.51100   106.95500 15.89000  1.000 51.50080  ?  688  LEU   B CD1 1 
ATOM   19388 C  CD2 . LEU   B 1 688  ? 48.41700   104.93100 14.74100  1.000 55.16774  ?  688  LEU   B CD2 1 
ATOM   19389 N  N   . GLY   B 1 689  ? 43.35100   104.79700 12.93800  1.000 66.65686  ?  689  GLY   B N   1 
ATOM   19390 C  CA  . GLY   B 1 689  ? 42.02600   104.20600 12.91300  1.000 68.82727  ?  689  GLY   B CA  1 
ATOM   19391 C  C   . GLY   B 1 689  ? 41.54900   103.78700 14.29300  1.000 51.66746  ?  689  GLY   B C   1 
ATOM   19392 O  O   . GLY   B 1 689  ? 42.22600   103.94600 15.30800  1.000 59.51815  ?  689  GLY   B O   1 
ATOM   19393 N  N   . GLU   B 1 690  ? 40.34100   103.22900 14.31300  1.000 51.71089  ?  690  GLU   B N   1 
ATOM   19394 C  CA  . GLU   B 1 690  ? 39.73400   102.78900 15.55800  1.000 41.48257  ?  690  GLU   B CA  1 
ATOM   19395 C  C   . GLU   B 1 690  ? 40.50500   101.60200 16.13500  1.000 53.24835  ?  690  GLU   B C   1 
ATOM   19396 O  O   . GLU   B 1 690  ? 41.42400   101.05800 15.51600  1.000 76.48660  ?  690  GLU   B O   1 
ATOM   19397 C  CB  . GLU   B 1 690  ? 38.26700   102.42800 15.33500  1.000 64.07082  ?  690  GLU   B CB  1 
ATOM   19398 C  CG  . GLU   B 1 690  ? 37.51300   103.44900 14.49600  1.000 74.22731  ?  690  GLU   B CG  1 
ATOM   19399 C  CD  . GLU   B 1 690  ? 36.00900   103.26100 14.54700  1.000 82.26353  ?  690  GLU   B CD  1 
ATOM   19400 O  OE1 . GLU   B 1 690  ? 35.52100   102.60700 15.49200  1.000 80.59962  ?  690  GLU   B OE1 1 
ATOM   19401 O  OE2 . GLU   B 1 690  ? 35.31500   103.77100 13.64200  1.000 86.39270  -1 690  GLU   B OE2 1 
ATOM   19402 N  N   . ASP   B 1 691  ? 40.11800   101.20900 17.34700  1.000 55.46855  ?  691  ASP   B N   1 
ATOM   19403 C  CA  . ASP   B 1 691  ? 40.78500   100.18300 18.14400  1.000 66.67946  ?  691  ASP   B CA  1 
ATOM   19404 C  C   . ASP   B 1 691  ? 42.21600   100.55700 18.51000  1.000 52.69855  ?  691  ASP   B C   1 
ATOM   19405 O  O   . ASP   B 1 691  ? 42.98100   99.69400  18.95800  1.000 77.10401  ?  691  ASP   B O   1 
ATOM   19406 C  CB  . ASP   B 1 691  ? 40.76800   98.81500  17.44600  1.000 40.93549  ?  691  ASP   B CB  1 
ATOM   19407 N  N   . TYR   B 1 692  ? 42.60300   101.81900 18.33300  1.000 37.79954  ?  692  TYR   B N   1 
ATOM   19408 C  CA  . TYR   B 1 692  ? 43.91300   102.30400 18.74900  1.000 52.82157  ?  692  TYR   B CA  1 
ATOM   19409 C  C   . TYR   B 1 692  ? 43.77000   103.02400 20.08300  1.000 48.56999  ?  692  TYR   B C   1 
ATOM   19410 O  O   . TYR   B 1 692  ? 43.07200   104.04000 20.17300  1.000 42.13435  ?  692  TYR   B O   1 
ATOM   19411 C  CB  . TYR   B 1 692  ? 44.52700   103.23700 17.70400  1.000 41.92680  ?  692  TYR   B CB  1 
ATOM   19412 C  CG  . TYR   B 1 692  ? 45.87000   103.81100 18.12000  1.000 35.74557  ?  692  TYR   B CG  1 
ATOM   19413 C  CD1 . TYR   B 1 692  ? 47.05000   103.12300 17.86800  1.000 41.45858  ?  692  TYR   B CD1 1 
ATOM   19414 C  CD2 . TYR   B 1 692  ? 45.95700   105.03900 18.77000  1.000 30.10094  ?  692  TYR   B CD2 1 
ATOM   19415 C  CE1 . TYR   B 1 692  ? 48.27900   103.64000 18.25000  1.000 44.75131  ?  692  TYR   B CE1 1 
ATOM   19416 C  CE2 . TYR   B 1 692  ? 47.18000   105.56200 19.15700  1.000 31.94438  ?  692  TYR   B CE2 1 
ATOM   19417 C  CZ  . TYR   B 1 692  ? 48.33800   104.85900 18.89300  1.000 46.40987  ?  692  TYR   B CZ  1 
ATOM   19418 O  OH  . TYR   B 1 692  ? 49.55600   105.37600 19.27500  1.000 44.09356  ?  692  TYR   B OH  1 
ATOM   19419 N  N   . VAL   B 1 693  ? 44.42600   102.49800 21.11100  1.000 42.33190  ?  693  VAL   B N   1 
ATOM   19420 C  CA  . VAL   B 1 693  ? 44.49600   103.13900 22.41700  1.000 36.02984  ?  693  VAL   B CA  1 
ATOM   19421 C  C   . VAL   B 1 693  ? 45.94700   103.53900 22.64800  1.000 43.65706  ?  693  VAL   B C   1 
ATOM   19422 O  O   . VAL   B 1 693  ? 46.84900   102.69300 22.58900  1.000 35.45161  ?  693  VAL   B O   1 
ATOM   19423 C  CB  . VAL   B 1 693  ? 43.98300   102.21800 23.53400  1.000 25.54934  ?  693  VAL   B CB  1 
ATOM   19424 C  CG1 . VAL   B 1 693  ? 43.57100   103.03800 24.74600  1.000 47.01819  ?  693  VAL   B CG1 1 
ATOM   19425 C  CG2 . VAL   B 1 693  ? 42.82700   101.36600 23.03300  1.000 28.43081  ?  693  VAL   B CG2 1 
ATOM   19426 N  N   . ALA   B 1 694  ? 46.17300   104.82500 22.89600  1.000 33.66657  ?  694  ALA   B N   1 
ATOM   19427 C  CA  . ALA   B 1 694  ? 47.52300   105.33700 23.02500  1.000 24.89882  ?  694  ALA   B CA  1 
ATOM   19428 C  C   . ALA   B 1 694  ? 48.13400   104.92600 24.36400  1.000 33.72206  ?  694  ALA   B C   1 
ATOM   19429 O  O   . ALA   B 1 694  ? 47.41500   104.64300 25.32500  1.000 42.03921  ?  694  ALA   B O   1 
ATOM   19430 C  CB  . ALA   B 1 694  ? 47.52300   106.85800 22.88600  1.000 27.72888  ?  694  ALA   B CB  1 
ATOM   19431 N  N   . PRO   B 1 695  ? 49.46400   104.86600 24.44100  1.000 27.53515  ?  695  PRO   B N   1 
ATOM   19432 C  CA  . PRO   B 1 695  ? 50.11600   104.58400 25.72800  1.000 39.44266  ?  695  PRO   B CA  1 
ATOM   19433 C  C   . PRO   B 1 695  ? 49.72300   105.60800 26.78400  1.000 45.53378  ?  695  PRO   B C   1 
ATOM   19434 O  O   . PRO   B 1 695  ? 49.84400   106.81700 26.57800  1.000 48.88121  ?  695  PRO   B O   1 
ATOM   19435 C  CB  . PRO   B 1 695  ? 51.60800   104.66400 25.38900  1.000 39.50717  ?  695  PRO   B CB  1 
ATOM   19436 C  CG  . PRO   B 1 695  ? 51.67700   104.32300 23.94100  1.000 31.44701  ?  695  PRO   B CG  1 
ATOM   19437 C  CD  . PRO   B 1 695  ? 50.43000   104.89500 23.32900  1.000 36.19846  ?  695  PRO   B CD  1 
ATOM   19438 N  N   . THR   B 1 696  ? 49.25100   105.10900 27.92600  1.000 41.64568  ?  696  THR   B N   1 
ATOM   19439 C  CA  . THR   B 1 696  ? 48.73900   105.95000 29.00000  1.000 43.38581  ?  696  THR   B CA  1 
ATOM   19440 C  C   . THR   B 1 696  ? 49.75800   106.20100 30.10400  1.000 47.88837  ?  696  THR   B C   1 
ATOM   19441 O  O   . THR   B 1 696  ? 49.46300   106.95000 31.04000  1.000 52.03014  ?  696  THR   B O   1 
ATOM   19442 C  CB  . THR   B 1 696  ? 47.47400   105.32600 29.60200  1.000 35.22456  ?  696  THR   B CB  1 
ATOM   19443 O  OG1 . THR   B 1 696  ? 47.81900   104.13100 30.31300  1.000 36.50462  ?  696  THR   B OG1 1 
ATOM   19444 C  CG2 . THR   B 1 696  ? 46.48000   104.98100 28.50400  1.000 40.86084  ?  696  THR   B CG2 1 
ATOM   19445 N  N   . ASP   B 1 697  ? 50.93700   105.59400 30.02400  1.000 36.34997  ?  697  ASP   B N   1 
ATOM   19446 C  CA  . ASP   B 1 697  ? 52.00100   105.83500 30.99000  1.000 29.39959  ?  697  ASP   B CA  1 
ATOM   19447 C  C   . ASP   B 1 697  ? 53.33700   105.60200 30.29200  1.000 44.31907  ?  697  ASP   B C   1 
ATOM   19448 O  O   . ASP   B 1 697  ? 53.39600   105.43900 29.07000  1.000 50.04069  ?  697  ASP   B O   1 
ATOM   19449 C  CB  . ASP   B 1 697  ? 51.82500   104.95100 32.23100  1.000 35.50041  ?  697  ASP   B CB  1 
ATOM   19450 C  CG  . ASP   B 1 697  ? 51.65000   103.48900 31.88500  1.000 51.71264  ?  697  ASP   B CG  1 
ATOM   19451 O  OD1 . ASP   B 1 697  ? 51.57200   103.17100 30.68200  1.000 56.68997  ?  697  ASP   B OD1 1 
ATOM   19452 O  OD2 . ASP   B 1 697  ? 51.58800   102.65800 32.81600  1.000 64.53360  -1 697  ASP   B OD2 1 
ATOM   19453 N  N   . GLU   B 1 698  ? 54.41700   105.57700 31.07500  1.000 43.87944  ?  698  GLU   B N   1 
ATOM   19454 C  CA  . GLU   B 1 698  ? 55.74600   105.47800 30.48400  1.000 44.80066  ?  698  GLU   B CA  1 
ATOM   19455 C  C   . GLU   B 1 698  ? 56.10700   104.05200 30.09200  1.000 46.61608  ?  698  GLU   B C   1 
ATOM   19456 O  O   . GLU   B 1 698  ? 56.80000   103.85100 29.08900  1.000 51.56834  ?  698  GLU   B O   1 
ATOM   19457 C  CB  . GLU   B 1 698  ? 56.79400   106.04100 31.44500  1.000 57.28450  ?  698  GLU   B CB  1 
ATOM   19458 C  CG  . GLU   B 1 698  ? 58.11600   106.36800 30.77200  1.000 68.86831  ?  698  GLU   B CG  1 
ATOM   19459 C  CD  . GLU   B 1 698  ? 58.95600   107.33500 31.57800  1.000 86.69482  ?  698  GLU   B CD  1 
ATOM   19460 O  OE1 . GLU   B 1 698  ? 58.37400   108.15600 32.31700  1.000 83.99328  ?  698  GLU   B OE1 1 
ATOM   19461 O  OE2 . GLU   B 1 698  ? 60.20000   107.27300 31.47300  1.000 98.01041  -1 698  GLU   B OE2 1 
ATOM   19462 N  N   . LEU   B 1 699  ? 55.65400   103.05500 30.85600  1.000 49.15076  ?  699  LEU   B N   1 
ATOM   19463 C  CA  . LEU   B 1 699  ? 55.95800   101.67200 30.50200  1.000 45.07418  ?  699  LEU   B CA  1 
ATOM   19464 C  C   . LEU   B 1 699  ? 55.26800   101.27700 29.20200  1.000 49.30839  ?  699  LEU   B C   1 
ATOM   19465 O  O   . LEU   B 1 699  ? 55.90000   100.70900 28.30400  1.000 54.15233  ?  699  LEU   B O   1 
ATOM   19466 C  CB  . LEU   B 1 699  ? 55.55400   100.73100 31.63800  1.000 40.78282  ?  699  LEU   B CB  1 
ATOM   19467 C  CG  . LEU   B 1 699  ? 56.04800   99.29300  31.47000  1.000 33.59595  ?  699  LEU   B CG  1 
ATOM   19468 C  CD1 . LEU   B 1 699  ? 57.56700   99.26600  31.37800  1.000 40.72771  ?  699  LEU   B CD1 1 
ATOM   19469 C  CD2 . LEU   B 1 699  ? 55.55900   98.41400  32.60800  1.000 41.61680  ?  699  LEU   B CD2 1 
ATOM   19470 N  N   . GLU   B 1 700  ? 53.96900   101.57300 29.08000  1.000 38.29946  ?  700  GLU   B N   1 
ATOM   19471 C  CA  . GLU   B 1 700  ? 53.26400   101.28700 27.83400  1.000 40.24551  ?  700  GLU   B CA  1 
ATOM   19472 C  C   . GLU   B 1 700  ? 53.88500   102.02700 26.65700  1.000 37.70634  ?  700  GLU   B C   1 
ATOM   19473 O  O   . GLU   B 1 700  ? 53.86000   101.52600 25.52800  1.000 48.21187  ?  700  GLU   B O   1 
ATOM   19474 C  CB  . GLU   B 1 700  ? 51.78400   101.64700 27.96500  1.000 35.74357  ?  700  GLU   B CB  1 
ATOM   19475 C  CG  . GLU   B 1 700  ? 50.97500   100.66600 28.80100  1.000 36.87409  ?  700  GLU   B CG  1 
ATOM   19476 C  CD  . GLU   B 1 700  ? 49.56100   101.14900 29.06000  1.000 35.59635  ?  700  GLU   B CD  1 
ATOM   19477 O  OE1 . GLU   B 1 700  ? 49.27100   102.32900 28.77100  1.000 36.70437  ?  700  GLU   B OE1 1 
ATOM   19478 O  OE2 . GLU   B 1 700  ? 48.73700   100.34900 29.55300  1.000 45.86704  -1 700  GLU   B OE2 1 
ATOM   19479 N  N   . GLN   B 1 701  ? 54.44900   103.21300 26.89600  1.000 34.34264  ?  701  GLN   B N   1 
ATOM   19480 C  CA  . GLN   B 1 701  ? 55.14300   103.92400 25.82800  1.000 37.57432  ?  701  GLN   B CA  1 
ATOM   19481 C  C   . GLN   B 1 701  ? 56.45300   103.22900 25.47700  1.000 39.98586  ?  701  GLN   B C   1 
ATOM   19482 O  O   . GLN   B 1 701  ? 56.76500   103.03300 24.29600  1.000 45.35068  ?  701  GLN   B O   1 
ATOM   19483 C  CB  . GLN   B 1 701  ? 55.38600   105.37800 26.23600  1.000 39.55443  ?  701  GLN   B CB  1 
ATOM   19484 C  CG  . GLN   B 1 701  ? 55.11600   106.39000 25.13400  1.000 47.66804  ?  701  GLN   B CG  1 
ATOM   19485 C  CD  . GLN   B 1 701  ? 56.08800   106.26800 23.98000  1.000 63.35679  ?  701  GLN   B CD  1 
ATOM   19486 O  OE1 . GLN   B 1 701  ? 57.29400   106.44400 24.15100  1.000 62.89093  ?  701  GLN   B OE1 1 
ATOM   19487 N  NE2 . GLN   B 1 701  ? 55.56900   105.95900 22.79700  1.000 61.48534  ?  701  GLN   B NE2 1 
ATOM   19488 N  N   . GLN   B 1 702  ? 57.23100   102.84400 26.49400  1.000 41.22352  ?  702  GLN   B N   1 
ATOM   19489 C  CA  . GLN   B 1 702  ? 58.46400   102.10000 26.24700  1.000 42.95208  ?  702  GLN   B CA  1 
ATOM   19490 C  C   . GLN   B 1 702  ? 58.17800   100.80200 25.50400  1.000 40.30940  ?  702  GLN   B C   1 
ATOM   19491 O  O   . GLN   B 1 702  ? 58.85400   100.47100 24.52300  1.000 28.20702  ?  702  GLN   B O   1 
ATOM   19492 C  CB  . GLN   B 1 702  ? 59.18200   101.80900 27.56600  1.000 51.47296  ?  702  GLN   B CB  1 
ATOM   19493 C  CG  . GLN   B 1 702  ? 59.75300   103.02900 28.27000  1.000 84.70688  ?  702  GLN   B CG  1 
ATOM   19494 C  CD  . GLN   B 1 702  ? 60.54600   102.66400 29.51100  1.000 92.83654  ?  702  GLN   B CD  1 
ATOM   19495 O  OE1 . GLN   B 1 702  ? 60.52900   103.38600 30.50800  1.000 89.44769  ?  702  GLN   B OE1 1 
ATOM   19496 N  NE2 . GLN   B 1 702  ? 61.25000   101.53900 29.45300  1.000 72.91027  ?  702  GLN   B NE2 1 
ATOM   19497 N  N   . LEU   B 1 703  ? 57.17200   100.05200 25.96100  1.000 45.51691  ?  703  LEU   B N   1 
ATOM   19498 C  CA  . LEU   B 1 703  ? 56.81600   98.80100  25.30100  1.000 31.05126  ?  703  LEU   B CA  1 
ATOM   19499 C  C   . LEU   B 1 703  ? 56.32600   99.04500  23.88000  1.000 34.50434  ?  703  LEU   B C   1 
ATOM   19500 O  O   . LEU   B 1 703  ? 56.65300   98.28100  22.96500  1.000 37.29552  ?  703  LEU   B O   1 
ATOM   19501 C  CB  . LEU   B 1 703  ? 55.75200   98.06500  26.11700  1.000 37.91179  ?  703  LEU   B CB  1 
ATOM   19502 C  CG  . LEU   B 1 703  ? 56.19600   97.47800  27.45900  1.000 34.13014  ?  703  LEU   B CG  1 
ATOM   19503 C  CD1 . LEU   B 1 703  ? 54.98900   97.09700  28.29600  1.000 37.42580  ?  703  LEU   B CD1 1 
ATOM   19504 C  CD2 . LEU   B 1 703  ? 57.09900   96.27300  27.24600  1.000 35.55615  ?  703  LEU   B CD2 1 
ATOM   19505 N  N   . ALA   B 1 704  ? 55.54300   100.10800 23.67400  1.000 35.88414  ?  704  ALA   B N   1 
ATOM   19506 C  CA  . ALA   B 1 704  ? 55.04300   100.40800 22.33600  1.000 37.63320  ?  704  ALA   B CA  1 
ATOM   19507 C  C   . ALA   B 1 704  ? 56.18200   100.74000 21.38100  1.000 43.43137  ?  704  ALA   B C   1 
ATOM   19508 O  O   . ALA   B 1 704  ? 56.14700   100.35600 20.20600  1.000 46.41019  ?  704  ALA   B O   1 
ATOM   19509 C  CB  . ALA   B 1 704  ? 54.03900   101.55900 22.39200  1.000 28.41949  ?  704  ALA   B CB  1 
ATOM   19510 N  N   . GLN   B 1 705  ? 57.19900   101.45600 21.86600  1.000 36.62809  ?  705  GLN   B N   1 
ATOM   19511 C  CA  . GLN   B 1 705  ? 58.35800   101.74900 21.03000  1.000 30.69392  ?  705  GLN   B CA  1 
ATOM   19512 C  C   . GLN   B 1 705  ? 59.10700   100.47400 20.66400  1.000 34.90793  ?  705  GLN   B C   1 
ATOM   19513 O  O   . GLN   B 1 705  ? 59.50500   100.28900 19.50800  1.000 41.20926  ?  705  GLN   B O   1 
ATOM   19514 C  CB  . GLN   B 1 705  ? 59.28500   102.73500 21.74200  1.000 40.42199  ?  705  GLN   B CB  1 
ATOM   19515 C  CG  . GLN   B 1 705  ? 58.80700   104.18100 21.70400  1.000 54.39360  ?  705  GLN   B CG  1 
ATOM   19516 C  CD  . GLN   B 1 705  ? 59.09800   104.85800 20.37700  1.000 80.58213  ?  705  GLN   B CD  1 
ATOM   19517 O  OE1 . GLN   B 1 705  ? 58.18500   105.18200 19.61700  1.000 72.21910  ?  705  GLN   B OE1 1 
ATOM   19518 N  NE2 . GLN   B 1 705  ? 60.37800   105.08000 20.09600  1.000 75.34534  ?  705  GLN   B NE2 1 
ATOM   19519 N  N   . VAL   B 1 706  ? 59.30100   99.57800  21.63400  1.000 33.68530  ?  706  VAL   B N   1 
ATOM   19520 C  CA  . VAL   B 1 706  ? 59.97500   98.31500  21.34700  1.000 29.47625  ?  706  VAL   B CA  1 
ATOM   19521 C  C   . VAL   B 1 706  ? 59.11400   97.44700  20.44000  1.000 32.84197  ?  706  VAL   B C   1 
ATOM   19522 O  O   . VAL   B 1 706  ? 59.61600   96.82600  19.49500  1.000 39.61407  ?  706  VAL   B O   1 
ATOM   19523 C  CB  . VAL   B 1 706  ? 60.33200   97.58400  22.65400  1.000 27.12723  ?  706  VAL   B CB  1 
ATOM   19524 C  CG1 . VAL   B 1 706  ? 61.09600   96.30700  22.34500  1.000 28.98352  ?  706  VAL   B CG1 1 
ATOM   19525 C  CG2 . VAL   B 1 706  ? 61.14500   98.48800  23.56400  1.000 27.70832  ?  706  VAL   B CG2 1 
ATOM   19526 N  N   . TRP   B 1 707  ? 57.80700   97.38500  20.71300  1.000 38.00382  ?  707  TRP   B N   1 
ATOM   19527 C  CA  . TRP   B 1 707  ? 56.90100   96.64000  19.84600  1.000 39.24242  ?  707  TRP   B CA  1 
ATOM   19528 C  C   . TRP   B 1 707  ? 56.91700   97.17700  18.42100  1.000 43.28179  ?  707  TRP   B C   1 
ATOM   19529 O  O   . TRP   B 1 707  ? 56.71900   96.41500  17.46800  1.000 48.87520  ?  707  TRP   B O   1 
ATOM   19530 C  CB  . TRP   B 1 707  ? 55.48100   96.68400  20.41000  1.000 37.87966  ?  707  TRP   B CB  1 
ATOM   19531 C  CG  . TRP   B 1 707  ? 55.21100   95.65000  21.45900  1.000 45.29184  ?  707  TRP   B CG  1 
ATOM   19532 C  CD1 . TRP   B 1 707  ? 55.98600   95.35500  22.54100  1.000 40.39542  ?  707  TRP   B CD1 1 
ATOM   19533 C  CD2 . TRP   B 1 707  ? 54.07300   94.78300  21.53200  1.000 38.46960  ?  707  TRP   B CD2 1 
ATOM   19534 N  NE1 . TRP   B 1 707  ? 55.40700   94.35100  23.28000  1.000 39.26029  ?  707  TRP   B NE1 1 
ATOM   19535 C  CE2 . TRP   B 1 707  ? 54.23000   93.98400  22.68200  1.000 34.03749  ?  707  TRP   B CE2 1 
ATOM   19536 C  CE3 . TRP   B 1 707  ? 52.93900   94.60300  20.73500  1.000 36.95745  ?  707  TRP   B CE3 1 
ATOM   19537 C  CZ2 . TRP   B 1 707  ? 53.29700   93.02000  23.05300  1.000 38.57393  ?  707  TRP   B CZ2 1 
ATOM   19538 C  CZ3 . TRP   B 1 707  ? 52.01300   93.64600  21.10600  1.000 42.19897  ?  707  TRP   B CZ3 1 
ATOM   19539 C  CH2 . TRP   B 1 707  ? 52.19700   92.86700  22.25500  1.000 37.83733  ?  707  TRP   B CH2 1 
ATOM   19540 N  N   . SER   B 1 708  ? 57.15300   98.48000  18.25500  1.000 44.01705  ?  708  SER   B N   1 
ATOM   19541 C  CA  . SER   B 1 708  ? 57.18600   99.06300  16.91800  1.000 43.27963  ?  708  SER   B CA  1 
ATOM   19542 C  C   . SER   B 1 708  ? 58.41600   98.61000  16.14300  1.000 46.81750  ?  708  SER   B C   1 
ATOM   19543 O  O   . SER   B 1 708  ? 58.32300   98.28200  14.95400  1.000 44.46450  ?  708  SER   B O   1 
ATOM   19544 C  CB  . SER   B 1 708  ? 57.14300   100.58800 17.01300  1.000 42.85335  ?  708  SER   B CB  1 
ATOM   19545 O  OG  . SER   B 1 708  ? 55.89400   101.02900 17.51600  1.000 49.95033  ?  708  SER   B OG  1 
ATOM   19546 N  N   . HIS   B 1 709  ? 59.57800   98.58400  16.79900  1.000 47.07010  ?  709  HIS   B N   1 
ATOM   19547 C  CA  . HIS   B 1 709  ? 60.80600   98.20100  16.11000  1.000 52.10677  ?  709  HIS   B CA  1 
ATOM   19548 C  C   . HIS   B 1 709  ? 60.78700   96.72800  15.72100  1.000 50.13294  ?  709  HIS   B C   1 
ATOM   19549 O  O   . HIS   B 1 709  ? 61.18400   96.36900  14.60600  1.000 53.61353  ?  709  HIS   B O   1 
ATOM   19550 C  CB  . HIS   B 1 709  ? 62.01700   98.50700  16.99200  1.000 56.08971  ?  709  HIS   B CB  1 
ATOM   19551 C  CG  . HIS   B 1 709  ? 63.33000   98.21600  16.33600  1.000 56.63835  ?  709  HIS   B CG  1 
ATOM   19552 N  ND1 . HIS   B 1 709  ? 64.40500   97.69300  17.02200  1.000 61.72940  ?  709  HIS   B ND1 1 
ATOM   19553 C  CD2 . HIS   B 1 709  ? 63.74400   98.38000  15.05700  1.000 54.74447  ?  709  HIS   B CD2 1 
ATOM   19554 C  CE1 . HIS   B 1 709  ? 65.42300   97.54400  16.19400  1.000 77.84252  ?  709  HIS   B CE1 1 
ATOM   19555 N  NE2 . HIS   B 1 709  ? 65.04900   97.95400  14.99600  1.000 76.27898  ?  709  HIS   B NE2 1 
ATOM   19556 N  N   . VAL   B 1 710  ? 60.32600   95.86200  16.62400  1.000 43.70843  ?  710  VAL   B N   1 
ATOM   19557 C  CA  . VAL   B 1 710  ? 60.32700   94.42900  16.35000  1.000 36.70918  ?  710  VAL   B CA  1 
ATOM   19558 C  C   . VAL   B 1 710  ? 59.31500   94.09100  15.26300  1.000 50.58851  ?  710  VAL   B C   1 
ATOM   19559 O  O   . VAL   B 1 710  ? 59.63700   93.40700  14.28400  1.000 66.97025  ?  710  VAL   B O   1 
ATOM   19560 C  CB  . VAL   B 1 710  ? 60.05200   93.63700  17.64100  1.000 33.43032  ?  710  VAL   B CB  1 
ATOM   19561 C  CG1 . VAL   B 1 710  ? 59.86700   92.16900  17.32400  1.000 42.15827  ?  710  VAL   B CG1 1 
ATOM   19562 C  CG2 . VAL   B 1 710  ? 61.18700   93.83100  18.63400  1.000 44.96863  ?  710  VAL   B CG2 1 
ATOM   19563 N  N   . LEU   B 1 711  ? 58.07900   94.56600  15.41500  1.000 41.00131  ?  711  LEU   B N   1 
ATOM   19564 C  CA  . LEU   B 1 711  ? 57.01600   94.22000  14.47900  1.000 49.88780  ?  711  LEU   B CA  1 
ATOM   19565 C  C   . LEU   B 1 711  ? 57.03200   95.06000  13.21000  1.000 58.76786  ?  711  LEU   B C   1 
ATOM   19566 O  O   . LEU   B 1 711  ? 56.30200   94.73500  12.26700  1.000 71.25979  ?  711  LEU   B O   1 
ATOM   19567 C  CB  . LEU   B 1 711  ? 55.65300   94.35000  15.16200  1.000 41.66625  ?  711  LEU   B CB  1 
ATOM   19568 C  CG  . LEU   B 1 711  ? 55.36400   93.29900  16.23200  1.000 33.11334  ?  711  LEU   B CG  1 
ATOM   19569 C  CD1 . LEU   B 1 711  ? 53.97100   93.48400  16.80600  1.000 38.35490  ?  711  LEU   B CD1 1 
ATOM   19570 C  CD2 . LEU   B 1 711  ? 55.52900   91.90500  15.65100  1.000 49.16191  ?  711  LEU   B CD2 1 
ATOM   19571 N  N   . GLY   B 1 712  ? 57.83400   96.12000  13.15700  1.000 40.37906  ?  712  GLY   B N   1 
ATOM   19572 C  CA  . GLY   B 1 712  ? 57.90500   96.93400  11.95800  1.000 49.43014  ?  712  GLY   B CA  1 
ATOM   19573 C  C   . GLY   B 1 712  ? 56.67000   97.76100  11.68000  1.000 57.34499  ?  712  GLY   B C   1 
ATOM   19574 O  O   . GLY   B 1 712  ? 56.40100   98.09100  10.52100  1.000 64.04248  ?  712  GLY   B O   1 
ATOM   19575 N  N   . ILE   B 1 713  ? 55.90900   98.10200  12.70900  1.000 58.76386  ?  713  ILE   B N   1 
ATOM   19576 C  CA  . ILE   B 1 713  ? 54.72300   98.94700  12.59300  1.000 56.02074  ?  713  ILE   B CA  1 
ATOM   19577 C  C   . ILE   B 1 713  ? 55.03600   100.28200 13.25500  1.000 57.99994  ?  713  ILE   B C   1 
ATOM   19578 O  O   . ILE   B 1 713  ? 55.48300   100.29500 14.40700  1.000 56.06093  ?  713  ILE   B O   1 
ATOM   19579 C  CB  . ILE   B 1 713  ? 53.48900   98.29300  13.24200  1.000 61.30359  ?  713  ILE   B CB  1 
ATOM   19580 C  CG1 . ILE   B 1 713  ? 53.13000   97.00000  12.50700  1.000 48.48795  ?  713  ILE   B CG1 1 
ATOM   19581 C  CG2 . ILE   B 1 713  ? 52.31300   99.25800  13.25900  1.000 55.57383  ?  713  ILE   B CG2 1 
ATOM   19582 C  CD1 . ILE   B 1 713  ? 52.03300   96.20500  13.17200  1.000 49.38345  ?  713  ILE   B CD1 1 
ATOM   19583 N  N   . PRO   B 1 714  ? 54.82400   101.41600 12.57400  1.000 59.13632  ?  714  PRO   B N   1 
ATOM   19584 C  CA  . PRO   B 1 714  ? 55.24900   102.71200 13.12900  1.000 53.63392  ?  714  PRO   B CA  1 
ATOM   19585 C  C   . PRO   B 1 714  ? 54.66400   103.02900 14.49900  1.000 52.34140  ?  714  PRO   B C   1 
ATOM   19586 O  O   . PRO   B 1 714  ? 55.41200   103.18500 15.47000  1.000 64.74173  ?  714  PRO   B O   1 
ATOM   19587 C  CB  . PRO   B 1 714  ? 54.77300   103.71900 12.07000  1.000 26.34188  ?  714  PRO   B CB  1 
ATOM   19588 C  CG  . PRO   B 1 714  ? 53.77000   102.97600 11.23300  1.000 59.12032  ?  714  PRO   B CG  1 
ATOM   19589 C  CD  . PRO   B 1 714  ? 54.22100   101.55500 11.24000  1.000 59.48625  ?  714  PRO   B CD  1 
ATOM   19590 N  N   . GLN   B 1 715  ? 53.34100   103.13000 14.59900  1.000 43.24072  ?  715  GLN   B N   1 
ATOM   19591 C  CA  . GLN   B 1 715  ? 52.67300   103.48800 15.84500  1.000 47.51830  ?  715  GLN   B CA  1 
ATOM   19592 C  C   . GLN   B 1 715  ? 51.74700   102.35200 16.25300  1.000 58.28809  ?  715  GLN   B C   1 
ATOM   19593 O  O   . GLN   B 1 715  ? 50.82500   102.00100 15.50900  1.000 56.44514  ?  715  GLN   B O   1 
ATOM   19594 C  CB  . GLN   B 1 715  ? 51.89200   104.79500 15.69200  1.000 43.11427  ?  715  GLN   B CB  1 
ATOM   19595 C  CG  . GLN   B 1 715  ? 52.70900   105.93900 15.11500  1.000 64.91050  ?  715  GLN   B CG  1 
ATOM   19596 C  CD  . GLN   B 1 715  ? 52.89300   107.07900 16.09400  1.000 76.28065  ?  715  GLN   B CD  1 
ATOM   19597 O  OE1 . GLN   B 1 715  ? 51.92300   107.62600 16.61900  1.000 78.29594  ?  715  GLN   B OE1 1 
ATOM   19598 N  NE2 . GLN   B 1 715  ? 54.14500   107.44300 16.34900  1.000 77.81689  ?  715  GLN   B NE2 1 
ATOM   19599 N  N   . MET   B 1 716  ? 51.98900   101.78700 17.43200  1.000 42.26849  ?  716  MET   B N   1 
ATOM   19600 C  CA  . MET   B 1 716  ? 51.24400   100.63900 17.92200  1.000 44.08795  ?  716  MET   B CA  1 
ATOM   19601 C  C   . MET   B 1 716  ? 50.42900   101.01100 19.15500  1.000 53.78207  ?  716  MET   B C   1 
ATOM   19602 O  O   . MET   B 1 716  ? 50.85200   101.82600 19.98000  1.000 46.45053  ?  716  MET   B O   1 
ATOM   19603 C  CB  . MET   B 1 716  ? 52.18400   99.47800  18.25100  1.000 39.75740  ?  716  MET   B CB  1 
ATOM   19604 C  CG  . MET   B 1 716  ? 52.88900   98.90900  17.03500  1.000 54.09099  ?  716  MET   B CG  1 
ATOM   19605 S  SD  . MET   B 1 716  ? 53.15300   97.13700  17.19200  1.000 68.63631  ?  716  MET   B SD  1 
ATOM   19606 C  CE  . MET   B 1 716  ? 51.58500   96.64700  17.90100  1.000 52.88309  ?  716  MET   B CE  1 
ATOM   19607 N  N   . GLY   B 1 717  ? 49.25000   100.39600 19.27000  1.000 40.67020  ?  717  GLY   B N   1 
ATOM   19608 C  CA  . GLY   B 1 717  ? 48.35600   100.64300 20.37600  1.000 42.33659  ?  717  GLY   B CA  1 
ATOM   19609 C  C   . GLY   B 1 717  ? 48.47800   99.59300  21.46500  1.000 49.49115  ?  717  GLY   B C   1 
ATOM   19610 O  O   . GLY   B 1 717  ? 48.97300   98.49100  21.24300  1.000 56.40608  ?  717  GLY   B O   1 
ATOM   19611 N  N   . ILE   B 1 718  ? 48.00700   99.95400  22.66200  1.000 38.87742  ?  718  ILE   B N   1 
ATOM   19612 C  CA  . ILE   B 1 718  ? 48.13500   99.07100  23.81600  1.000 46.66945  ?  718  ILE   B CA  1 
ATOM   19613 C  C   . ILE   B 1 718  ? 47.21900   97.86000  23.74100  1.000 48.07828  ?  718  ILE   B C   1 
ATOM   19614 O  O   . ILE   B 1 718  ? 47.40500   96.90700  24.50500  1.000 50.62782  ?  718  ILE   B O   1 
ATOM   19615 C  CB  . ILE   B 1 718  ? 47.87200   99.84700  25.12200  1.000 36.73615  ?  718  ILE   B CB  1 
ATOM   19616 C  CG1 . ILE   B 1 718  ? 46.38800   100.18600 25.25400  1.000 39.86120  ?  718  ILE   B CG1 1 
ATOM   19617 C  CG2 . ILE   B 1 718  ? 48.70600   101.11600 25.15900  1.000 36.51806  ?  718  ILE   B CG2 1 
ATOM   19618 C  CD1 . ILE   B 1 718  ? 46.05200   100.95000 26.51200  1.000 45.25390  ?  718  ILE   B CD1 1 
ATOM   19619 N  N   . ASP   B 1 719  ? 46.23600   97.86900  22.84100  1.000 53.94419  ?  719  ASP   B N   1 
ATOM   19620 C  CA  . ASP   B 1 719  ? 45.34700   96.73200  22.64000  1.000 52.04374  ?  719  ASP   B CA  1 
ATOM   19621 C  C   . ASP   B 1 719  ? 45.62700   95.99500  21.33700  1.000 44.27200  ?  719  ASP   B C   1 
ATOM   19622 O  O   . ASP   B 1 719  ? 44.81800   95.15800  20.92300  1.000 44.82898  ?  719  ASP   B O   1 
ATOM   19623 C  CB  . ASP   B 1 719  ? 43.88600   97.18600  22.68800  1.000 35.57983  ?  719  ASP   B CB  1 
ATOM   19624 C  CG  . ASP   B 1 719  ? 43.35800   97.30000  24.10400  1.000 48.47386  ?  719  ASP   B CG  1 
ATOM   19625 O  OD1 . ASP   B 1 719  ? 44.03900   96.81600  25.03300  1.000 58.28441  ?  719  ASP   B OD1 1 
ATOM   19626 O  OD2 . ASP   B 1 719  ? 42.26400   97.87400  24.28800  1.000 60.28518  -1 719  ASP   B OD2 1 
ATOM   19627 N  N   . ASP   B 1 720  ? 46.74900   96.28300  20.68200  1.000 54.34419  ?  720  ASP   B N   1 
ATOM   19628 C  CA  . ASP   B 1 720  ? 47.11800   95.57700  19.46400  1.000 50.58147  ?  720  ASP   B CA  1 
ATOM   19629 C  C   . ASP   B 1 720  ? 47.76700   94.24100  19.80100  1.000 38.71332  ?  720  ASP   B C   1 
ATOM   19630 O  O   . ASP   B 1 720  ? 48.51400   94.12400  20.77600  1.000 58.61941  ?  720  ASP   B O   1 
ATOM   19631 C  CB  . ASP   B 1 720  ? 48.06800   96.42500  18.61900  1.000 47.30841  ?  720  ASP   B CB  1 
ATOM   19632 C  CG  . ASP   B 1 720  ? 47.39700   97.65400  18.04300  1.000 54.95063  ?  720  ASP   B CG  1 
ATOM   19633 O  OD1 . ASP   B 1 720  ? 46.17500   97.81800  18.24900  1.000 61.80816  ?  720  ASP   B OD1 1 
ATOM   19634 O  OD2 . ASP   B 1 720  ? 48.09300   98.45500  17.38500  1.000 46.60202  -1 720  ASP   B OD2 1 
ATOM   19635 N  N   . HIS   B 1 721  ? 47.48300   93.23500  18.97800  1.000 29.93030  ?  721  HIS   B N   1 
ATOM   19636 C  CA  . HIS   B 1 721  ? 47.89800   91.86500  19.24600  1.000 30.72637  ?  721  HIS   B CA  1 
ATOM   19637 C  C   . HIS   B 1 721  ? 49.23200   91.57500  18.56800  1.000 33.60352  ?  721  HIS   B C   1 
ATOM   19638 O  O   . HIS   B 1 721  ? 49.42100   91.90100  17.39300  1.000 49.74714  ?  721  HIS   B O   1 
ATOM   19639 C  CB  . HIS   B 1 721  ? 46.83000   90.88900  18.75500  1.000 26.01155  ?  721  HIS   B CB  1 
ATOM   19640 C  CG  . HIS   B 1 721  ? 46.93900   89.52100  19.35100  1.000 38.62971  ?  721  HIS   B CG  1 
ATOM   19641 N  ND1 . HIS   B 1 721  ? 47.97200   88.65900  19.05500  1.000 46.59359  ?  721  HIS   B ND1 1 
ATOM   19642 C  CD2 . HIS   B 1 721  ? 46.13900   88.86300  20.22300  1.000 37.64196  ?  721  HIS   B CD2 1 
ATOM   19643 C  CE1 . HIS   B 1 721  ? 47.80600   87.53100  19.72100  1.000 39.43796  ?  721  HIS   B CE1 1 
ATOM   19644 N  NE2 . HIS   B 1 721  ? 46.70100   87.62900  20.43800  1.000 35.82356  ?  721  HIS   B NE2 1 
ATOM   19645 N  N   . PHE   B 1 722  ? 50.15100   90.95100  19.30800  1.000 24.92361  ?  722  PHE   B N   1 
ATOM   19646 C  CA  . PHE   B 1 722  ? 51.47000   90.65700  18.75300  1.000 42.19303  ?  722  PHE   B CA  1 
ATOM   19647 C  C   . PHE   B 1 722  ? 51.37400   89.66200  17.60100  1.000 47.68297  ?  722  PHE   B C   1 
ATOM   19648 O  O   . PHE   B 1 722  ? 51.99200   89.85400  16.54800  1.000 51.82808  ?  722  PHE   B O   1 
ATOM   19649 C  CB  . PHE   B 1 722  ? 52.39400   90.12800  19.85100  1.000 44.46229  ?  722  PHE   B CB  1 
ATOM   19650 C  CG  . PHE   B 1 722  ? 53.84500   90.07600  19.45700  1.000 36.16018  ?  722  PHE   B CG  1 
ATOM   19651 C  CD1 . PHE   B 1 722  ? 54.67200   91.16900  19.66400  1.000 44.45780  ?  722  PHE   B CD1 1 
ATOM   19652 C  CD2 . PHE   B 1 722  ? 54.38500   88.93300  18.89000  1.000 44.52970  ?  722  PHE   B CD2 1 
ATOM   19653 C  CE1 . PHE   B 1 722  ? 56.00800   91.12500  19.30800  1.000 47.80804  ?  722  PHE   B CE1 1 
ATOM   19654 C  CE2 . PHE   B 1 722  ? 55.72000   88.88200  18.53100  1.000 53.38284  ?  722  PHE   B CE2 1 
ATOM   19655 C  CZ  . PHE   B 1 722  ? 56.53200   89.98000  18.74000  1.000 57.87972  ?  722  PHE   B CZ  1 
ATOM   19656 N  N   . LEU   B 1 723  ? 50.59000   88.59700  17.77900  1.000 44.12950  ?  723  LEU   B N   1 
ATOM   19657 C  CA  . LEU   B 1 723  ? 50.49200   87.55700  16.76100  1.000 45.48733  ?  723  LEU   B CA  1 
ATOM   19658 C  C   . LEU   B 1 723  ? 49.62200   87.97200  15.58100  1.000 49.27705  ?  723  LEU   B C   1 
ATOM   19659 O  O   . LEU   B 1 723  ? 49.81000   87.46100  14.47200  1.000 61.80753  ?  723  LEU   B O   1 
ATOM   19660 C  CB  . LEU   B 1 723  ? 49.95200   86.26600  17.38200  1.000 46.33187  ?  723  LEU   B CB  1 
ATOM   19661 C  CG  . LEU   B 1 723  ? 50.97300   85.22400  17.84700  1.000 42.51166  ?  723  LEU   B CG  1 
ATOM   19662 C  CD1 . LEU   B 1 723  ? 52.09100   85.85700  18.66200  1.000 42.78963  ?  723  LEU   B CD1 1 
ATOM   19663 C  CD2 . LEU   B 1 723  ? 50.27900   84.13300  18.64900  1.000 58.34812  ?  723  LEU   B CD2 1 
ATOM   19664 N  N   . GLU   B 1 724  ? 48.67300   88.88300  15.79000  1.000 47.71344  ?  724  GLU   B N   1 
ATOM   19665 C  CA  . GLU   B 1 724  ? 47.81100   89.34500  14.70900  1.000 50.77776  ?  724  GLU   B CA  1 
ATOM   19666 C  C   . GLU   B 1 724  ? 48.43600   90.46000  13.88200  1.000 50.74472  ?  724  GLU   B C   1 
ATOM   19667 O  O   . GLU   B 1 724  ? 47.84100   90.87200  12.88000  1.000 56.27982  ?  724  GLU   B O   1 
ATOM   19668 C  CB  . GLU   B 1 724  ? 46.46800   89.82300  15.26700  1.000 31.11209  ?  724  GLU   B CB  1 
ATOM   19669 C  CG  . GLU   B 1 724  ? 45.65000   88.74200  15.94700  1.000 50.69639  ?  724  GLU   B CG  1 
ATOM   19670 C  CD  . GLU   B 1 724  ? 44.32600   89.26400  16.46500  1.000 56.61166  ?  724  GLU   B CD  1 
ATOM   19671 O  OE1 . GLU   B 1 724  ? 44.00800   90.44100  16.19300  1.000 39.58249  ?  724  GLU   B OE1 1 
ATOM   19672 O  OE2 . GLU   B 1 724  ? 43.60500   88.50000  17.14200  1.000 72.51665  -1 724  GLU   B OE2 1 
ATOM   19673 N  N   . ARG   B 1 725  ? 49.60700   90.95500  14.26800  1.000 45.04901  ?  725  ARG   B N   1 
ATOM   19674 C  CA  . ARG   B 1 725  ? 50.24800   92.08000  13.60200  1.000 49.42786  ?  725  ARG   B CA  1 
ATOM   19675 C  C   . ARG   B 1 725  ? 51.64700   91.70900  13.12400  1.000 50.52449  ?  725  ARG   B C   1 
ATOM   19676 O  O   . ARG   B 1 725  ? 52.57900   92.51400  13.18000  1.000 60.33313  ?  725  ARG   B O   1 
ATOM   19677 C  CB  . ARG   B 1 725  ? 50.28900   93.29600  14.52500  1.000 35.98080  ?  725  ARG   B CB  1 
ATOM   19678 C  CG  . ARG   B 1 725  ? 48.91700   93.72900  15.02300  1.000 43.54526  ?  725  ARG   B CG  1 
ATOM   19679 C  CD  . ARG   B 1 725  ? 48.29700   94.78100  14.13300  1.000 51.98287  ?  725  ARG   B CD  1 
ATOM   19680 N  NE  . ARG   B 1 725  ? 48.92500   96.08100  14.33100  1.000 72.42865  ?  725  ARG   B NE  1 
ATOM   19681 C  CZ  . ARG   B 1 725  ? 48.66000   97.15800  13.60500  1.000 69.82681  ?  725  ARG   B CZ  1 
ATOM   19682 N  NH1 . ARG   B 1 725  ? 47.78900   97.12300  12.61000  1.000 72.09014  ?  725  ARG   B NH1 1 
ATOM   19683 N  NH2 . ARG   B 1 725  ? 49.28700   98.29700  13.88400  1.000 55.02277  ?  725  ARG   B NH2 1 
ATOM   19684 N  N   . GLY   B 1 726  ? 51.80600   90.47600  12.64800  1.000 45.56056  ?  726  GLY   B N   1 
ATOM   19685 C  CA  . GLY   B 1 726  ? 53.04900   90.03200  12.05500  1.000 62.71908  ?  726  GLY   B CA  1 
ATOM   19686 C  C   . GLY   B 1 726  ? 54.00000   89.31600  12.98800  1.000 50.74929  ?  726  GLY   B C   1 
ATOM   19687 O  O   . GLY   B 1 726  ? 55.09400   88.93600  12.55300  1.000 47.55811  ?  726  GLY   B O   1 
ATOM   19688 N  N   . GLY   B 1 727  ? 53.62300   89.11400  14.24700  1.000 52.59194  ?  727  GLY   B N   1 
ATOM   19689 C  CA  . GLY   B 1 727  ? 54.52100   88.46300  15.18700  1.000 52.83297  ?  727  GLY   B CA  1 
ATOM   19690 C  C   . GLY   B 1 727  ? 54.61200   86.97200  14.91900  1.000 56.49492  ?  727  GLY   B C   1 
ATOM   19691 O  O   . GLY   B 1 727  ? 53.59300   86.28400  14.78400  1.000 58.49467  ?  727  GLY   B O   1 
ATOM   19692 N  N   . ASP   B 1 728  ? 55.83400   86.46800  14.83400  1.000 60.74777  ?  728  ASP   B N   1 
ATOM   19693 C  CA  . ASP   B 1 728  ? 56.10400   85.04200  14.67500  1.000 57.13312  ?  728  ASP   B CA  1 
ATOM   19694 C  C   . ASP   B 1 728  ? 56.70900   84.52300  15.98000  1.000 62.53835  ?  728  ASP   B C   1 
ATOM   19695 O  O   . ASP   B 1 728  ? 56.13500   84.79200  17.03900  1.000 73.84810  ?  728  ASP   B O   1 
ATOM   19696 C  CB  . ASP   B 1 728  ? 56.95500   84.82700  13.42800  1.000 65.44471  ?  728  ASP   B CB  1 
ATOM   19697 C  CG  . ASP   B 1 728  ? 58.15200   85.76000  13.36900  1.000 79.89869  ?  728  ASP   B CG  1 
ATOM   19698 O  OD1 . ASP   B 1 728  ? 58.51800   86.33200  14.41600  1.000 74.03411  ?  728  ASP   B OD1 1 
ATOM   19699 O  OD2 . ASP   B 1 728  ? 58.72300   85.92500  12.27000  1.000 75.27874  -1 728  ASP   B OD2 1 
HETATM 19700 O  O   . 4HH   B 1 729  ? 60.29300   84.26700  18.48900  1.000 65.20352  ?  729  4HH   B O   1 
HETATM 19701 C  C   . 4HH   B 1 729  ? 59.88600   84.01700  17.35200  1.000 62.52991  ?  729  4HH   B C   1 
HETATM 19702 C  CA  . 4HH   B 1 729  ? 58.51100   83.39600  17.17900  1.000 58.76096  ?  729  4HH   B CA  1 
HETATM 19703 N  N   . 4HH   B 1 729  ? 57.82800   83.80000  15.95800  1.000 69.89069  ?  729  4HH   B N   1 
HETATM 19704 C  CB  . 4HH   B 1 729  ? 58.66200   81.87400  17.24200  1.000 59.14153  ?  729  4HH   B CB  1 
HETATM 19705 O  OG  . 4HH   B 1 729  ? 57.44200   81.23900  17.56000  1.000 66.76853  ?  729  4HH   B OG  1 
HETATM 19706 C  CJ  . 4HH   B 1 729  ? 59.24000   78.41500  16.97300  1.000 44.52153  ?  729  4HH   B CJ  1 
HETATM 19707 C  CK  . 4HH   B 1 729  ? 60.69100   78.83500  16.77400  1.000 65.41645  ?  729  4HH   B CK  1 
HETATM 19708 C  CL1 . 4HH   B 1 729  ? 61.20000   79.49600  18.05400  1.000 59.56762  ?  729  4HH   B CL1 1 
HETATM 19709 C  CL2 . 4HH   B 1 729  ? 60.80400   79.80600  15.59900  1.000 77.12920  ?  729  4HH   B CL2 1 
HETATM 19710 C  CL3 . 4HH   B 1 729  ? 62.86500   78.04000  15.80000  1.000 68.84298  ?  729  4HH   B CL3 1 
HETATM 19711 C  CM  . 4HH   B 1 729  ? 61.54700   77.60700  16.46200  1.000 73.83061  ?  729  4HH   B CM  1 
HETATM 19712 O  OM  . 4HH   B 1 729  ? 60.83500   76.77300  15.59300  1.000 86.37344  ?  729  4HH   B OM  1 
HETATM 19713 N  NN  . 4HH   B 1 729  ? 63.03700   77.91700  14.35200  1.000 79.41602  ?  729  4HH   B NN  1 
HETATM 19714 O  ON  . 4HH   B 1 729  ? 63.74300   78.47500  16.46400  1.000 54.44209  ?  729  4HH   B ON  1 
HETATM 19715 P  P   . 4HH   B 1 729  ? 57.05800   79.89600  16.68900  1.000 58.87624  ?  729  4HH   B P   1 
HETATM 19716 O  O1P . 4HH   B 1 729  ? 56.13400   80.35700  15.41600  1.000 50.91354  ?  729  4HH   B O1P 1 
HETATM 19717 O  O2P . 4HH   B 1 729  ? 56.29800   78.95400  17.53900  1.000 75.11505  ?  729  4HH   B O2P 1 
HETATM 19718 O  O3P . 4HH   B 1 729  ? 58.43100   79.19100  16.12400  1.000 65.70642  ?  729  4HH   B O3P 1 
HETATM 19719 C  CO  . 4HH   B 1 729  ? 64.28800   78.32500  13.70500  1.000 49.00705  ?  729  4HH   B CO  1 
HETATM 19720 C  CP  . 4HH   B 1 729  ? 65.39900   77.30600  14.03500  1.000 43.59077  ?  729  4HH   B CP  1 
HETATM 19721 C  CQ  . 4HH   B 1 729  ? 66.37300   77.07600  12.86000  1.000 56.75621  ?  729  4HH   B CQ  1 
HETATM 19722 C  CS  . 4HH   B 1 729  ? 67.13800   75.66400  10.89400  1.000 69.04227  ?  729  4HH   B CS  1 
HETATM 19723 C  CT  . 4HH   B 1 729  ? 68.05700   74.48200  11.22200  1.000 54.27947  ?  729  4HH   B CT  1 
HETATM 19724 N  NR  . 4HH   B 1 729  ? 66.21200   75.89200  12.01000  1.000 47.79038  ?  729  4HH   B NR  1 
HETATM 19725 O  OR  . 4HH   B 1 729  ? 67.24800   77.85000  12.64900  1.000 73.98448  ?  729  4HH   B OR  1 
HETATM 19726 S  SU  . 4HH   B 1 729  ? 69.64700   74.63700  10.37400  1.000 60.88043  ?  729  4HH   B SU  1 
ATOM   19727 N  N   . ILE   B 1 730  ? 60.62000   84.24900  16.26300  1.000 66.00182  ?  730  ILE   B N   1 
ATOM   19728 C  CA  . ILE   B 1 730  ? 61.86600   84.99900  16.35800  1.000 61.95228  ?  730  ILE   B CA  1 
ATOM   19729 C  C   . ILE   B 1 730  ? 61.60400   86.40400  16.88100  1.000 54.59836  ?  730  ILE   B C   1 
ATOM   19730 O  O   . ILE   B 1 730  ? 62.43500   86.97200  17.59900  1.000 57.16114  ?  730  ILE   B O   1 
ATOM   19731 C  CB  . ILE   B 1 730  ? 62.57300   85.02200  14.98800  1.000 64.31848  ?  730  ILE   B CB  1 
ATOM   19732 C  CG1 . ILE   B 1 730  ? 61.54200   85.18000  13.86900  1.000 71.57914  ?  730  ILE   B CG1 1 
ATOM   19733 C  CG2 . ILE   B 1 730  ? 63.39600   83.75800  14.78800  1.000 66.14972  ?  730  ILE   B CG2 1 
ATOM   19734 C  CD1 . ILE   B 1 730  ? 62.12700   85.14900  12.47400  1.000 58.37797  ?  730  ILE   B CD1 1 
ATOM   19735 N  N   . LYS   B 1 731  ? 60.43900   86.97600  16.56300  1.000 61.67689  ?  731  LYS   B N   1 
ATOM   19736 C  CA  . LYS   B 1 731  ? 60.14700   88.34600  16.97400  1.000 53.13492  ?  731  LYS   B CA  1 
ATOM   19737 C  C   . LYS   B 1 731  ? 59.84000   88.45300  18.46400  1.000 54.84112  ?  731  LYS   B C   1 
ATOM   19738 O  O   . LYS   B 1 731  ? 60.20300   89.45000  19.09500  1.000 59.33924  ?  731  LYS   B O   1 
ATOM   19739 C  CB  . LYS   B 1 731  ? 58.99400   88.90900  16.14600  1.000 42.35789  ?  731  LYS   B CB  1 
ATOM   19740 C  CG  . LYS   B 1 731  ? 59.42900   89.38500  14.76900  1.000 49.19159  ?  731  LYS   B CG  1 
ATOM   19741 C  CD  . LYS   B 1 731  ? 58.24300   89.78000  13.91000  1.000 62.04582  ?  731  LYS   B CD  1 
ATOM   19742 C  CE  . LYS   B 1 731  ? 58.67000   90.07700  12.48000  1.000 49.76794  ?  731  LYS   B CE  1 
ATOM   19743 N  NZ  . LYS   B 1 731  ? 57.50500   90.17200  11.55600  1.000 58.95959  ?  731  LYS   B NZ  1 
ATOM   19744 N  N   . VAL   B 1 732  ? 59.17500   87.45600  19.05200  1.000 49.03146  ?  732  VAL   B N   1 
ATOM   19745 C  CA  . VAL   B 1 732  ? 59.01100   87.48500  20.50300  1.000 57.44261  ?  732  VAL   B CA  1 
ATOM   19746 C  C   . VAL   B 1 732  ? 60.36300   87.31000  21.18200  1.000 51.09686  ?  732  VAL   B C   1 
ATOM   19747 O  O   . VAL   B 1 732  ? 60.62900   87.90900  22.23100  1.000 50.75057  ?  732  VAL   B O   1 
ATOM   19748 C  CB  . VAL   B 1 732  ? 57.98500   86.43000  20.96400  1.000 45.14941  ?  732  VAL   B CB  1 
ATOM   19749 C  CG1 . VAL   B 1 732  ? 57.65700   85.48500  19.84200  1.000 60.39050  ?  732  VAL   B CG1 1 
ATOM   19750 C  CG2 . VAL   B 1 732  ? 58.49000   85.66400  22.18000  1.000 45.45865  ?  732  VAL   B CG2 1 
ATOM   19751 N  N   . MET   B 1 733  ? 61.25200   86.51700  20.57700  1.000 45.06593  ?  733  MET   B N   1 
ATOM   19752 C  CA  . MET   B 1 733  ? 62.61500   86.40600  21.08700  1.000 63.04159  ?  733  MET   B CA  1 
ATOM   19753 C  C   . MET   B 1 733  ? 63.34000   87.74200  20.98200  1.000 57.94779  ?  733  MET   B C   1 
ATOM   19754 O  O   . MET   B 1 733  ? 63.97900   88.19300  21.94100  1.000 65.70942  ?  733  MET   B O   1 
ATOM   19755 C  CB  . MET   B 1 733  ? 63.37600   85.32200  20.32300  1.000 55.32495  ?  733  MET   B CB  1 
ATOM   19756 C  CG  . MET   B 1 733  ? 64.60400   84.78200  21.04500  1.000 68.46015  ?  733  MET   B CG  1 
ATOM   19757 S  SD  . MET   B 1 733  ? 64.16600   83.73100  22.44200  1.000 95.04140  ?  733  MET   B SD  1 
ATOM   19758 C  CE  . MET   B 1 733  ? 62.78500   82.83200  21.74100  1.000 68.49934  ?  733  MET   B CE  1 
ATOM   19759 N  N   . GLN   B 1 734  ? 63.24800   88.39200  19.81700  1.000 47.90627  ?  734  GLN   B N   1 
ATOM   19760 C  CA  . GLN   B 1 734  ? 63.82900   89.72200  19.66800  1.000 50.39992  ?  734  GLN   B CA  1 
ATOM   19761 C  C   . GLN   B 1 734  ? 63.19900   90.70300  20.64400  1.000 49.18961  ?  734  GLN   B C   1 
ATOM   19762 O  O   . GLN   B 1 734  ? 63.88300   91.58000  21.18300  1.000 53.21025  ?  734  GLN   B O   1 
ATOM   19763 C  CB  . GLN   B 1 734  ? 63.66500   90.21500  18.23100  1.000 53.44429  ?  734  GLN   B CB  1 
ATOM   19764 C  CG  . GLN   B 1 734  ? 64.35200   89.33900  17.20000  1.000 61.39100  ?  734  GLN   B CG  1 
ATOM   19765 C  CD  . GLN   B 1 734  ? 65.12100   90.13800  16.17300  1.000 78.45376  ?  734  GLN   B CD  1 
ATOM   19766 O  OE1 . GLN   B 1 734  ? 66.05700   90.86500  16.50900  1.000 70.51219  ?  734  GLN   B OE1 1 
ATOM   19767 N  NE2 . GLN   B 1 734  ? 64.73100   90.00900  14.91000  1.000 77.90919  ?  734  GLN   B NE2 1 
ATOM   19768 N  N   . LEU   B 1 735  ? 61.89300   90.56900  20.88800  1.000 50.64728  ?  735  LEU   B N   1 
ATOM   19769 C  CA  . LEU   B 1 735  ? 61.24400   91.39300  21.90200  1.000 51.49085  ?  735  LEU   B CA  1 
ATOM   19770 C  C   . LEU   B 1 735  ? 61.85600   91.14100  23.27400  1.000 49.84168  ?  735  LEU   B C   1 
ATOM   19771 O  O   . LEU   B 1 735  ? 62.29400   92.07700  23.95100  1.000 49.56997  ?  735  LEU   B O   1 
ATOM   19772 C  CB  . LEU   B 1 735  ? 59.74100   91.11700  21.92400  1.000 48.77658  ?  735  LEU   B CB  1 
ATOM   19773 C  CG  . LEU   B 1 735  ? 58.92800   91.97200  22.89900  1.000 45.34401  ?  735  LEU   B CG  1 
ATOM   19774 C  CD1 . LEU   B 1 735  ? 58.85900   93.41100  22.41600  1.000 49.83607  ?  735  LEU   B CD1 1 
ATOM   19775 C  CD2 . LEU   B 1 735  ? 57.53300   91.40100  23.10400  1.000 42.06510  ?  735  LEU   B CD2 1 
ATOM   19776 N  N   . ILE   B 1 736  ? 61.90800   89.87300  23.69100  1.000 56.81145  ?  736  ILE   B N   1 
ATOM   19777 C  CA  . ILE   B 1 736  ? 62.48500   89.53400  24.98900  1.000 52.65954  ?  736  ILE   B CA  1 
ATOM   19778 C  C   . ILE   B 1 736  ? 63.93300   90.00100  25.07000  1.000 50.52604  ?  736  ILE   B C   1 
ATOM   19779 O  O   . ILE   B 1 736  ? 64.39700   90.45300  26.12400  1.000 47.30203  ?  736  ILE   B O   1 
ATOM   19780 C  CB  . ILE   B 1 736  ? 62.35600   88.02200  25.24800  1.000 39.72966  ?  736  ILE   B CB  1 
ATOM   19781 C  CG1 . ILE   B 1 736  ? 60.88100   87.62800  25.34400  1.000 44.84740  ?  736  ILE   B CG1 1 
ATOM   19782 C  CG2 . ILE   B 1 736  ? 63.09900   87.62800  26.51300  1.000 53.64682  ?  736  ILE   B CG2 1 
ATOM   19783 C  CD1 . ILE   B 1 736  ? 60.65400   86.17000  25.66600  1.000 45.57663  ?  736  ILE   B CD1 1 
ATOM   19784 N  N   . HIS   B 1 737  ? 64.66400   89.91700  23.95600  1.000 45.77272  ?  737  HIS   B N   1 
ATOM   19785 C  CA  . HIS   B 1 737  ? 66.04200   90.39900  23.93700  1.000 53.14473  ?  737  HIS   B CA  1 
ATOM   19786 C  C   . HIS   B 1 737  ? 66.09400   91.92200  24.00500  1.000 52.07233  ?  737  HIS   B C   1 
ATOM   19787 O  O   . HIS   B 1 737  ? 66.84900   92.49100  24.80200  1.000 47.18123  ?  737  HIS   B O   1 
ATOM   19788 C  CB  . HIS   B 1 737  ? 66.76100   89.88900  22.68600  1.000 50.56861  ?  737  HIS   B CB  1 
ATOM   19789 C  CG  . HIS   B 1 737  ? 67.09400   88.43000  22.73200  1.000 58.77968  ?  737  HIS   B CG  1 
ATOM   19790 N  ND1 . HIS   B 1 737  ? 67.59700   87.74700  21.64500  1.000 51.00085  ?  737  HIS   B ND1 1 
ATOM   19791 C  CD2 . HIS   B 1 737  ? 67.00300   87.52500  23.73500  1.000 66.45977  ?  737  HIS   B CD2 1 
ATOM   19792 C  CE1 . HIS   B 1 737  ? 67.79700   86.48400  21.97500  1.000 59.17655  ?  737  HIS   B CE1 1 
ATOM   19793 N  NE2 . HIS   B 1 737  ? 67.44500   86.32200  23.23800  1.000 56.36881  ?  737  HIS   B NE2 1 
ATOM   19794 N  N   . GLN   B 1 738  ? 65.29300   92.60000  23.17800  1.000 51.48420  ?  738  GLN   B N   1 
ATOM   19795 C  CA  . GLN   B 1 738  ? 65.30200   94.05900  23.18200  1.000 42.31640  ?  738  GLN   B CA  1 
ATOM   19796 C  C   . GLN   B 1 738  ? 64.68800   94.62500  24.45700  1.000 42.95971  ?  738  GLN   B C   1 
ATOM   19797 O  O   . GLN   B 1 738  ? 65.09000   95.70400  24.90400  1.000 55.40279  ?  738  GLN   B O   1 
ATOM   19798 C  CB  . GLN   B 1 738  ? 64.57300   94.60000  21.95200  1.000 39.97797  ?  738  GLN   B CB  1 
ATOM   19799 C  CG  . GLN   B 1 738  ? 65.30500   94.34200  20.64000  1.000 52.62528  ?  738  GLN   B CG  1 
ATOM   19800 C  CD  . GLN   B 1 738  ? 64.54500   94.85600  19.43300  1.000 55.44522  ?  738  GLN   B CD  1 
ATOM   19801 O  OE1 . GLN   B 1 738  ? 63.87500   95.88600  19.49900  1.000 51.89419  ?  738  GLN   B OE1 1 
ATOM   19802 N  NE2 . GLN   B 1 738  ? 64.64200   94.13400  18.32200  1.000 57.26357  ?  738  GLN   B NE2 1 
ATOM   19803 N  N   . LEU   B 1 739  ? 63.71900   93.92500  25.05200  1.000 50.52764  ?  739  LEU   B N   1 
ATOM   19804 C  CA  . LEU   B 1 739  ? 63.19300   94.36000  26.34300  1.000 51.95052  ?  739  LEU   B CA  1 
ATOM   19805 C  C   . LEU   B 1 739  ? 64.19200   94.11400  27.46100  1.000 46.36145  ?  739  LEU   B C   1 
ATOM   19806 O  O   . LEU   B 1 739  ? 64.22700   94.87200  28.43700  1.000 45.06084  ?  739  LEU   B O   1 
ATOM   19807 C  CB  . LEU   B 1 739  ? 61.87600   93.65100  26.65800  1.000 52.74001  ?  739  LEU   B CB  1 
ATOM   19808 C  CG  . LEU   B 1 739  ? 60.66500   94.02700  25.80700  1.000 49.47166  ?  739  LEU   B CG  1 
ATOM   19809 C  CD1 . LEU   B 1 739  ? 59.42500   93.30700  26.30700  1.000 39.58436  ?  739  LEU   B CD1 1 
ATOM   19810 C  CD2 . LEU   B 1 739  ? 60.46000   95.53100  25.81400  1.000 52.68508  ?  739  LEU   B CD2 1 
ATOM   19811 N  N   . LYS   B 1 740  ? 65.00000   93.05800  27.34300  1.000 47.25587  ?  740  LYS   B N   1 
ATOM   19812 C  CA  . LYS   B 1 740  ? 66.03900   92.81200  28.33400  1.000 50.26099  ?  740  LYS   B CA  1 
ATOM   19813 C  C   . LYS   B 1 740  ? 67.08500   93.91800  28.31200  1.000 47.15051  ?  740  LYS   B C   1 
ATOM   19814 O  O   . LYS   B 1 740  ? 67.60800   94.30300  29.36200  1.000 44.22206  ?  740  LYS   B O   1 
ATOM   19815 C  CB  . LYS   B 1 740  ? 66.68700   91.45100  28.08600  1.000 51.98548  ?  740  LYS   B CB  1 
ATOM   19816 C  CG  . LYS   B 1 740  ? 67.33600   90.82300  29.30900  1.000 34.27244  ?  740  LYS   B CG  1 
ATOM   19817 C  CD  . LYS   B 1 740  ? 67.12700   89.31300  29.31300  1.000 80.96639  ?  740  LYS   B CD  1 
ATOM   19818 C  CE  . LYS   B 1 740  ? 67.20400   88.74000  27.90200  1.000 74.39224  ?  740  LYS   B CE  1 
ATOM   19819 N  NZ  . LYS   B 1 740  ? 67.09500   87.25500  27.87800  1.000 60.43052  ?  740  LYS   B NZ  1 
ATOM   19820 N  N   . ASN   B 1 741  ? 67.39400   94.44700  27.12300  1.000 51.10606  ?  741  ASN   B N   1 
ATOM   19821 C  CA  . ASN   B 1 741  ? 68.32900   95.55800  26.97300  1.000 42.96915  ?  741  ASN   B CA  1 
ATOM   19822 C  C   . ASN   B 1 741  ? 67.75400   96.88500  27.45000  1.000 52.02453  ?  741  ASN   B C   1 
ATOM   19823 O  O   . ASN   B 1 741  ? 68.45500   97.90100  27.38800  1.000 61.71332  ?  741  ASN   B O   1 
ATOM   19824 C  CB  . ASN   B 1 741  ? 68.77000   95.67700  25.51000  1.000 51.69062  ?  741  ASN   B CB  1 
ATOM   19825 C  CG  . ASN   B 1 741  ? 69.48500   94.43200  25.00900  1.000 57.49261  ?  741  ASN   B CG  1 
ATOM   19826 O  OD1 . ASN   B 1 741  ? 70.05100   93.67000  25.79100  1.000 62.99707  ?  741  ASN   B OD1 1 
ATOM   19827 N  ND2 . ASN   B 1 741  ? 69.46200   94.22400  23.69600  1.000 53.95533  ?  741  ASN   B ND2 1 
ATOM   19828 N  N   . ILE   B 1 742  ? 66.50200   96.90400  27.90800  1.000 59.84549  ?  742  ILE   B N   1 
ATOM   19829 C  CA  . ILE   B 1 742  ? 65.91100   98.05500  28.58200  1.000 60.12408  ?  742  ILE   B CA  1 
ATOM   19830 C  C   . ILE   B 1 742  ? 65.70500   97.79700  30.06700  1.000 57.28154  ?  742  ILE   B C   1 
ATOM   19831 O  O   . ILE   B 1 742  ? 65.32800   98.72000  30.80500  1.000 52.68866  ?  742  ILE   B O   1 
ATOM   19832 C  CB  . ILE   B 1 742  ? 64.58400   98.47200  27.91400  1.000 59.33201  ?  742  ILE   B CB  1 
ATOM   19833 C  CG1 . ILE   B 1 742  ? 64.71800   98.43900  26.39100  1.000 50.38857  ?  742  ILE   B CG1 1 
ATOM   19834 C  CG2 . ILE   B 1 742  ? 64.17000   99.88100  28.32600  1.000 65.91327  ?  742  ILE   B CG2 1 
ATOM   19835 C  CD1 . ILE   B 1 742  ? 65.64400   99.50000  25.83200  1.000 47.50984  ?  742  ILE   B CD1 1 
ATOM   19836 N  N   . GLY   B 1 743  ? 65.96400   96.58100  30.53600  1.000 45.52839  ?  743  GLY   B N   1 
ATOM   19837 C  CA  . GLY   B 1 743  ? 65.74100   96.24600  31.92800  1.000 57.78587  ?  743  GLY   B CA  1 
ATOM   19838 C  C   . GLY   B 1 743  ? 64.42500   95.56100  32.20400  1.000 55.05775  ?  743  GLY   B C   1 
ATOM   19839 O  O   . GLY   B 1 743  ? 63.97700   95.55000  33.35700  1.000 57.29855  ?  743  GLY   B O   1 
ATOM   19840 N  N   . LEU   B 1 744  ? 63.79100   94.99200  31.18400  1.000 52.41603  ?  744  LEU   B N   1 
ATOM   19841 C  CA  . LEU   B 1 744  ? 62.49300   94.34600  31.30800  1.000 47.98263  ?  744  LEU   B CA  1 
ATOM   19842 C  C   . LEU   B 1 744  ? 62.64900   92.85000  31.07600  1.000 52.21008  ?  744  LEU   B C   1 
ATOM   19843 O  O   . LEU   B 1 744  ? 63.21500   92.43100  30.05800  1.000 44.69635  ?  744  LEU   B O   1 
ATOM   19844 C  CB  . LEU   B 1 744  ? 61.49600   94.94000  30.31000  1.000 50.41709  ?  744  LEU   B CB  1 
ATOM   19845 C  CG  . LEU   B 1 744  ? 61.26400   96.45000  30.40500  1.000 50.59556  ?  744  LEU   B CG  1 
ATOM   19846 C  CD1 . LEU   B 1 744  ? 60.51100   96.97000  29.19400  1.000 53.73001  ?  744  LEU   B CD1 1 
ATOM   19847 C  CD2 . LEU   B 1 744  ? 60.51100   96.78300  31.68100  1.000 46.54171  ?  744  LEU   B CD2 1 
ATOM   19848 N  N   . SER   B 1 745  ? 62.13800   92.05300  32.01000  1.000 45.94287  ?  745  SER   B N   1 
ATOM   19849 C  CA  . SER   B 1 745  ? 62.27900   90.60100  31.97800  1.000 48.92852  ?  745  SER   B CA  1 
ATOM   19850 C  C   . SER   B 1 745  ? 60.95600   89.98300  31.53900  1.000 49.40822  ?  745  SER   B C   1 
ATOM   19851 O  O   . SER   B 1 745  ? 59.95600   90.06300  32.26000  1.000 44.37146  ?  745  SER   B O   1 
ATOM   19852 C  CB  . SER   B 1 745  ? 62.69800   90.07400  33.34800  1.000 33.11793  ?  745  SER   B CB  1 
ATOM   19853 O  OG  . SER   B 1 745  ? 63.70100   90.89300  33.92400  1.000 71.94988  ?  745  SER   B OG  1 
ATOM   19854 N  N   . LEU   B 1 746  ? 60.95600   89.36500  30.36200  1.000 34.98535  ?  746  LEU   B N   1 
ATOM   19855 C  CA  . LEU   B 1 746  ? 59.79700   88.66500  29.83200  1.000 40.30250  ?  746  LEU   B CA  1 
ATOM   19856 C  C   . LEU   B 1 746  ? 60.16800   87.22000  29.53200  1.000 57.35920  ?  746  LEU   B C   1 
ATOM   19857 O  O   . LEU   B 1 746  ? 61.26900   86.94000  29.04900  1.000 48.15589  ?  746  LEU   B O   1 
ATOM   19858 C  CB  . LEU   B 1 746  ? 59.27100   89.33700  28.55900  1.000 41.11258  ?  746  LEU   B CB  1 
ATOM   19859 C  CG  . LEU   B 1 746  ? 57.97100   88.76300  27.98900  1.000 36.92273  ?  746  LEU   B CG  1 
ATOM   19860 C  CD1 . LEU   B 1 746  ? 56.81500   88.96400  28.96100  1.000 30.73504  ?  746  LEU   B CD1 1 
ATOM   19861 C  CD2 . LEU   B 1 746  ? 57.65600   89.37400  26.63200  1.000 41.48605  ?  746  LEU   B CD2 1 
ATOM   19862 N  N   . ARG   B 1 747  ? 59.24900   86.30800  29.82600  1.000 50.37505  ?  747  ARG   B N   1 
ATOM   19863 C  CA  . ARG   B 1 747  ? 59.41200   84.90400  29.48400  1.000 45.98483  ?  747  ARG   B CA  1 
ATOM   19864 C  C   . ARG   B 1 747  ? 58.62800   84.57200  28.22000  1.000 48.37225  ?  747  ARG   B C   1 
ATOM   19865 O  O   . ARG   B 1 747  ? 57.66800   85.25600  27.85400  1.000 50.58146  ?  747  ARG   B O   1 
ATOM   19866 C  CB  . ARG   B 1 747  ? 58.95700   84.00100  30.63200  1.000 45.70143  ?  747  ARG   B CB  1 
ATOM   19867 C  CG  . ARG   B 1 747  ? 59.86600   84.02100  31.84700  1.000 51.44170  ?  747  ARG   B CG  1 
ATOM   19868 C  CD  . ARG   B 1 747  ? 59.66800   82.76000  32.67000  1.000 55.47649  ?  747  ARG   B CD  1 
ATOM   19869 N  NE  . ARG   B 1 747  ? 58.25400   82.45100  32.84200  1.000 52.38060  ?  747  ARG   B NE  1 
ATOM   19870 C  CZ  . ARG   B 1 747  ? 57.54300   82.76300  33.91700  1.000 71.84227  ?  747  ARG   B CZ  1 
ATOM   19871 N  NH1 . ARG   B 1 747  ? 58.09200   83.36900  34.95700  1.000 73.15087  ?  747  ARG   B NH1 1 
ATOM   19872 N  NH2 . ARG   B 1 747  ? 56.24900   82.45700  33.95000  1.000 66.60231  ?  747  ARG   B NH2 1 
ATOM   19873 N  N   . TYR   B 1 748  ? 59.05600   83.49600  27.55600  1.000 47.21248  ?  748  TYR   B N   1 
ATOM   19874 C  CA  . TYR   B 1 748  ? 58.42700   83.09500  26.30100  1.000 49.76260  ?  748  TYR   B CA  1 
ATOM   19875 C  C   . TYR   B 1 748  ? 56.94900   82.77900  26.49700  1.000 51.52900  ?  748  TYR   B C   1 
ATOM   19876 O  O   . TYR   B 1 748  ? 56.10700   83.17900  25.68500  1.000 39.13092  ?  748  TYR   B O   1 
ATOM   19877 C  CB  . TYR   B 1 748  ? 59.16500   81.89100  25.71600  1.000 47.88989  ?  748  TYR   B CB  1 
ATOM   19878 C  CG  . TYR   B 1 748  ? 58.92100   81.67800  24.24100  1.000 49.41534  ?  748  TYR   B CG  1 
ATOM   19879 C  CD1 . TYR   B 1 748  ? 59.63100   82.40100  23.29100  1.000 50.12908  ?  748  TYR   B CD1 1 
ATOM   19880 C  CD2 . TYR   B 1 748  ? 57.98600   80.75000  23.79800  1.000 66.36170  ?  748  TYR   B CD2 1 
ATOM   19881 C  CE1 . TYR   B 1 748  ? 59.41400   82.21100  21.94300  1.000 54.95920  ?  748  TYR   B CE1 1 
ATOM   19882 C  CE2 . TYR   B 1 748  ? 57.76400   80.55200  22.45200  1.000 69.83351  ?  748  TYR   B CE2 1 
ATOM   19883 C  CZ  . TYR   B 1 748  ? 58.47900   81.28600  21.52900  1.000 68.49136  ?  748  TYR   B CZ  1 
ATOM   19884 O  OH  . TYR   B 1 748  ? 58.26000   81.09100  20.18800  1.000 84.20723  ?  748  TYR   B OH  1 
ATOM   19885 N  N   . ASP   B 1 749  ? 56.61400   82.06700  27.57600  1.000 48.04517  ?  749  ASP   B N   1 
ATOM   19886 C  CA  . ASP   B 1 749  ? 55.22200   81.72800  27.84600  1.000 44.56269  ?  749  ASP   B CA  1 
ATOM   19887 C  C   . ASP   B 1 749  ? 54.38500   82.94600  28.20800  1.000 45.86481  ?  749  ASP   B C   1 
ATOM   19888 O  O   . ASP   B 1 749  ? 53.16400   82.92200  28.02200  1.000 40.70307  ?  749  ASP   B O   1 
ATOM   19889 C  CB  . ASP   B 1 749  ? 55.14300   80.69900  28.97300  1.000 53.40109  ?  749  ASP   B CB  1 
ATOM   19890 C  CG  . ASP   B 1 749  ? 55.89900   81.13600  30.21200  1.000 49.34960  ?  749  ASP   B CG  1 
ATOM   19891 O  OD1 . ASP   B 1 749  ? 57.12900   81.33400  30.12100  1.000 61.35302  ?  749  ASP   B OD1 1 
ATOM   19892 O  OD2 . ASP   B 1 749  ? 55.26100   81.29500  31.27400  1.000 57.01648  -1 749  ASP   B OD2 1 
ATOM   19893 N  N   . GLN   B 1 750  ? 55.00900   84.00800  28.71700  1.000 45.65606  ?  750  GLN   B N   1 
ATOM   19894 C  CA  . GLN   B 1 750  ? 54.25900   85.16500  29.18600  1.000 47.69774  ?  750  GLN   B CA  1 
ATOM   19895 C  C   . GLN   B 1 750  ? 53.78500   86.06600  28.05200  1.000 39.40569  ?  750  GLN   B C   1 
ATOM   19896 O  O   . GLN   B 1 750  ? 52.80300   86.79500  28.22900  1.000 47.62735  ?  750  GLN   B O   1 
ATOM   19897 C  CB  . GLN   B 1 750  ? 55.10700   85.96100  30.17900  1.000 44.02625  ?  750  GLN   B CB  1 
ATOM   19898 C  CG  . GLN   B 1 750  ? 55.52100   85.14900  31.39900  1.000 41.47470  ?  750  GLN   B CG  1 
ATOM   19899 C  CD  . GLN   B 1 750  ? 56.14200   85.99600  32.49000  1.000 36.94703  ?  750  GLN   B CD  1 
ATOM   19900 O  OE1 . GLN   B 1 750  ? 56.81600   86.98800  32.21500  1.000 40.57851  ?  750  GLN   B OE1 1 
ATOM   19901 N  NE2 . GLN   B 1 750  ? 55.91100   85.61200  33.74000  1.000 50.35279  ?  750  GLN   B NE2 1 
ATOM   19902 N  N   . LEU   B 1 751  ? 54.45100   86.03300  26.89600  1.000 37.73745  ?  751  LEU   B N   1 
ATOM   19903 C  CA  . LEU   B 1 751  ? 53.97500   86.80800  25.75500  1.000 31.17678  ?  751  LEU   B CA  1 
ATOM   19904 C  C   . LEU   B 1 751  ? 52.68400   86.22200  25.20100  1.000 37.24723  ?  751  LEU   B C   1 
ATOM   19905 O  O   . LEU   B 1 751  ? 51.75400   86.96300  24.85900  1.000 42.16727  ?  751  LEU   B O   1 
ATOM   19906 C  CB  . LEU   B 1 751  ? 55.05700   86.86500  24.67400  1.000 31.35379  ?  751  LEU   B CB  1 
ATOM   19907 C  CG  . LEU   B 1 751  ? 54.95300   87.89900  23.54400  1.000 32.43120  ?  751  LEU   B CG  1 
ATOM   19908 C  CD1 . LEU   B 1 751  ? 53.99300   87.46300  22.43900  1.000 30.25927  ?  751  LEU   B CD1 1 
ATOM   19909 C  CD2 . LEU   B 1 751  ? 54.55900   89.26200  24.09500  1.000 28.30260  ?  751  LEU   B CD2 1 
ATOM   19910 N  N   . PHE   B 1 752  ? 52.60400   84.89400  25.10800  1.000 34.76002  ?  752  PHE   B N   1 
ATOM   19911 C  CA  . PHE   B 1 752  ? 51.41200   84.25800  24.56300  1.000 27.02238  ?  752  PHE   B CA  1 
ATOM   19912 C  C   . PHE   B 1 752  ? 50.24100   84.29200  25.53500  1.000 35.68916  ?  752  PHE   B C   1 
ATOM   19913 O  O   . PHE   B 1 752  ? 49.09900   84.07100  25.11700  1.000 46.52259  ?  752  PHE   B O   1 
ATOM   19914 C  CB  . PHE   B 1 752  ? 51.73000   82.82100  24.15700  1.000 22.64567  ?  752  PHE   B CB  1 
ATOM   19915 C  CG  . PHE   B 1 752  ? 52.74900   82.72000  23.05900  1.000 27.55789  ?  752  PHE   B CG  1 
ATOM   19916 C  CD1 . PHE   B 1 752  ? 52.36300   82.77400  21.73000  1.000 36.88972  ?  752  PHE   B CD1 1 
ATOM   19917 C  CD2 . PHE   B 1 752  ? 54.09500   82.58400  23.35500  1.000 35.66258  ?  752  PHE   B CD2 1 
ATOM   19918 C  CE1 . PHE   B 1 752  ? 53.29900   82.68800  20.71600  1.000 25.37991  ?  752  PHE   B CE1 1 
ATOM   19919 C  CE2 . PHE   B 1 752  ? 55.03600   82.49600  22.34500  1.000 37.06818  ?  752  PHE   B CE2 1 
ATOM   19920 C  CZ  . PHE   B 1 752  ? 54.63700   82.54700  21.02400  1.000 49.73117  ?  752  PHE   B CZ  1 
ATOM   19921 N  N   . THR   B 1 753  ? 50.49100   84.56300  26.81500  1.000 35.87214  ?  753  THR   B N   1 
ATOM   19922 C  CA  . THR   B 1 753  ? 49.40900   84.76200  27.76800  1.000 32.70117  ?  753  THR   B CA  1 
ATOM   19923 C  C   . THR   B 1 753  ? 49.05600   86.23000  27.95200  1.000 46.45959  ?  753  THR   B C   1 
ATOM   19924 O  O   . THR   B 1 753  ? 47.99700   86.53400  28.51400  1.000 56.66561  ?  753  THR   B O   1 
ATOM   19925 C  CB  . THR   B 1 753  ? 49.76900   84.15600  29.12700  1.000 26.42055  ?  753  THR   B CB  1 
ATOM   19926 O  OG1 . THR   B 1 753  ? 50.99100   84.73600  29.60000  1.000 38.16781  ?  753  THR   B OG1 1 
ATOM   19927 C  CG2 . THR   B 1 753  ? 49.93600   82.65000  29.00800  1.000 29.58407  ?  753  THR   B CG2 1 
ATOM   19928 N  N   . HIS   B 1 754  ? 49.91700   87.13900  27.49900  1.000 44.60243  ?  754  HIS   B N   1 
ATOM   19929 C  CA  . HIS   B 1 754  ? 49.65500   88.57900  27.53400  1.000 43.49639  ?  754  HIS   B CA  1 
ATOM   19930 C  C   . HIS   B 1 754  ? 50.05500   89.17000  26.19000  1.000 35.25143  ?  754  HIS   B C   1 
ATOM   19931 O  O   . HIS   B 1 754  ? 51.06300   89.87600  26.07400  1.000 37.10289  ?  754  HIS   B O   1 
ATOM   19932 C  CB  . HIS   B 1 754  ? 50.41200   89.24600  28.68500  1.000 47.59068  ?  754  HIS   B CB  1 
ATOM   19933 C  CG  . HIS   B 1 754  ? 50.07500   88.69000  30.03300  1.000 46.23933  ?  754  HIS   B CG  1 
ATOM   19934 N  ND1 . HIS   B 1 754  ? 50.61100   87.51300  30.51000  1.000 29.65291  ?  754  HIS   B ND1 1 
ATOM   19935 C  CD2 . HIS   B 1 754  ? 49.25400   89.15100  31.00700  1.000 50.05509  ?  754  HIS   B CD2 1 
ATOM   19936 C  CE1 . HIS   B 1 754  ? 50.13600   87.27300  31.71900  1.000 39.77662  ?  754  HIS   B CE1 1 
ATOM   19937 N  NE2 . HIS   B 1 754  ? 49.31100   88.25200  32.04400  1.000 48.21724  ?  754  HIS   B NE2 1 
ATOM   19938 N  N   . PRO   B 1 755  ? 49.27300   88.90200  25.14300  1.000 31.76742  ?  755  PRO   B N   1 
ATOM   19939 C  CA  . PRO   B 1 755  ? 49.70100   89.27400  23.78800  1.000 34.02583  ?  755  PRO   B CA  1 
ATOM   19940 C  C   . PRO   B 1 755  ? 49.41400   90.72300  23.42000  1.000 37.60546  ?  755  PRO   B C   1 
ATOM   19941 O  O   . PRO   B 1 755  ? 49.37000   91.06200  22.23400  1.000 36.41117  ?  755  PRO   B O   1 
ATOM   19942 C  CB  . PRO   B 1 755  ? 48.90000   88.31100  22.90700  1.000 32.25097  ?  755  PRO   B CB  1 
ATOM   19943 C  CG  . PRO   B 1 755  ? 47.63200   88.10900  23.67000  1.000 40.73544  ?  755  PRO   B CG  1 
ATOM   19944 C  CD  . PRO   B 1 755  ? 47.99600   88.16700  25.13600  1.000 41.00691  ?  755  PRO   B CD  1 
ATOM   19945 N  N   . THR   B 1 756  ? 49.21200   91.58400  24.41500  1.000 33.84510  ?  756  THR   B N   1 
ATOM   19946 C  CA  . THR   B 1 756  ? 49.01700   93.00800  24.18100  1.000 35.50778  ?  756  THR   B CA  1 
ATOM   19947 C  C   . THR   B 1 756  ? 49.86600   93.80200  25.16200  1.000 36.01511  ?  756  THR   B C   1 
ATOM   19948 O  O   . THR   B 1 756  ? 50.30200   93.29000  26.19500  1.000 40.19525  ?  756  THR   B O   1 
ATOM   19949 C  CB  . THR   B 1 756  ? 47.54300   93.42500  24.31700  1.000 40.45648  ?  756  THR   B CB  1 
ATOM   19950 O  OG1 . THR   B 1 756  ? 47.05400   93.06300  25.61500  1.000 40.37859  ?  756  THR   B OG1 1 
ATOM   19951 C  CG2 . THR   B 1 756  ? 46.69200   92.75600  23.24900  1.000 38.18632  ?  756  THR   B CG2 1 
ATOM   19952 N  N   . ILE   B 1 757  ? 50.09500   95.07200  24.82100  1.000 34.36623  ?  757  ILE   B N   1 
ATOM   19953 C  CA  . ILE   B 1 757  ? 50.88900   95.94100  25.68300  1.000 33.49850  ?  757  ILE   B CA  1 
ATOM   19954 C  C   . ILE   B 1 757  ? 50.14900   96.22300  26.98400  1.000 36.98866  ?  757  ILE   B C   1 
ATOM   19955 O  O   . ILE   B 1 757  ? 50.75500   96.26000  28.06300  1.000 39.00656  ?  757  ILE   B O   1 
ATOM   19956 C  CB  . ILE   B 1 757  ? 51.25000   97.23700  24.93500  1.000 39.02092  ?  757  ILE   B CB  1 
ATOM   19957 C  CG1 . ILE   B 1 757  ? 52.24000   96.93400  23.81000  1.000 35.69143  ?  757  ILE   B CG1 1 
ATOM   19958 C  CG2 . ILE   B 1 757  ? 51.82100   98.27800  25.88800  1.000 34.75597  ?  757  ILE   B CG2 1 
ATOM   19959 C  CD1 . ILE   B 1 757  ? 52.36800   98.04300  22.79900  1.000 34.94454  ?  757  ILE   B CD1 1 
ATOM   19960 N  N   . ARG   B 1 758  ? 48.83000   96.41500  26.90600  1.000 40.79204  ?  758  ARG   B N   1 
ATOM   19961 C  CA  . ARG   B 1 758  ? 48.03600   96.65400  28.10800  1.000 39.42390  ?  758  ARG   B CA  1 
ATOM   19962 C  C   . ARG   B 1 758  ? 48.17800   95.50100  29.09400  1.000 35.23033  ?  758  ARG   B C   1 
ATOM   19963 O  O   . ARG   B 1 758  ? 48.41300   95.71400  30.28900  1.000 43.93174  ?  758  ARG   B O   1 
ATOM   19964 C  CB  . ARG   B 1 758  ? 46.56900   96.86600  27.73200  1.000 36.15153  ?  758  ARG   B CB  1 
ATOM   19965 C  CG  . ARG   B 1 758  ? 45.70300   97.36800  28.87500  1.000 43.08617  ?  758  ARG   B CG  1 
ATOM   19966 C  CD  . ARG   B 1 758  ? 44.22500   97.13100  28.60500  1.000 52.69139  ?  758  ARG   B CD  1 
ATOM   19967 N  NE  . ARG   B 1 758  ? 43.71700   97.92300  27.49100  1.000 58.43351  ?  758  ARG   B NE  1 
ATOM   19968 C  CZ  . ARG   B 1 758  ? 43.14400   99.11200  27.61800  1.000 65.86503  ?  758  ARG   B CZ  1 
ATOM   19969 N  NH1 . ARG   B 1 758  ? 43.00900   99.69200  28.79900  1.000 72.21122  ?  758  ARG   B NH1 1 
ATOM   19970 N  NH2 . ARG   B 1 758  ? 42.69100   99.73300  26.53200  1.000 71.67772  ?  758  ARG   B NH2 1 
ATOM   19971 N  N   . GLN   B 1 759  ? 48.04400   94.26600  28.60600  1.000 30.81798  ?  759  GLN   B N   1 
ATOM   19972 C  CA  . GLN   B 1 759  ? 48.24200   93.10700  29.47000  1.000 35.70965  ?  759  GLN   B CA  1 
ATOM   19973 C  C   . GLN   B 1 759  ? 49.70100   92.94900  29.87200  1.000 39.70573  ?  759  GLN   B C   1 
ATOM   19974 O  O   . GLN   B 1 759  ? 49.98900   92.47300  30.97500  1.000 56.07536  ?  759  GLN   B O   1 
ATOM   19975 C  CB  . GLN   B 1 759  ? 47.75100   91.84100  28.77200  1.000 39.13672  ?  759  GLN   B CB  1 
ATOM   19976 C  CG  . GLN   B 1 759  ? 46.26900   91.84100  28.45300  1.000 47.38871  ?  759  GLN   B CG  1 
ATOM   19977 C  CD  . GLN   B 1 759  ? 45.84400   90.60100  27.69600  1.000 54.14688  ?  759  GLN   B CD  1 
ATOM   19978 O  OE1 . GLN   B 1 759  ? 45.89600   90.56200  26.46600  1.000 32.67645  ?  759  GLN   B OE1 1 
ATOM   19979 N  NE2 . GLN   B 1 759  ? 45.42400   89.57600  28.42900  1.000 65.93655  ?  759  GLN   B NE2 1 
ATOM   19980 N  N   . LEU   B 1 760  ? 50.63000   93.33700  28.99500  1.000 40.91964  ?  760  LEU   B N   1 
ATOM   19981 C  CA  . LEU   B 1 760  ? 52.04600   93.18400  29.30800  1.000 34.09559  ?  760  LEU   B CA  1 
ATOM   19982 C  C   . LEU   B 1 760  ? 52.48200   94.17300  30.37900  1.000 40.39809  ?  760  LEU   B C   1 
ATOM   19983 O  O   . LEU   B 1 760  ? 53.33400   93.85400  31.21600  1.000 48.39103  ?  760  LEU   B O   1 
ATOM   19984 C  CB  . LEU   B 1 760  ? 52.88200   93.35500  28.04000  1.000 45.22387  ?  760  LEU   B CB  1 
ATOM   19985 C  CG  . LEU   B 1 760  ? 54.17500   92.54500  27.96900  1.000 41.77095  ?  760  LEU   B CG  1 
ATOM   19986 C  CD1 . LEU   B 1 760  ? 53.89800   91.09600  28.32900  1.000 40.23197  ?  760  LEU   B CD1 1 
ATOM   19987 C  CD2 . LEU   B 1 760  ? 54.78100   92.64500  26.57900  1.000 32.19370  ?  760  LEU   B CD2 1 
ATOM   19988 N  N   . LYS   B 1 761  ? 51.90800   95.37900  30.36900  1.000 39.81599  ?  761  LYS   B N   1 
ATOM   19989 C  CA  . LYS   B 1 761  ? 52.21100   96.35800  31.40800  1.000 37.16089  ?  761  LYS   B CA  1 
ATOM   19990 C  C   . LYS   B 1 761  ? 51.81900   95.83100  32.78200  1.000 41.08920  ?  761  LYS   B C   1 
ATOM   19991 O  O   . LYS   B 1 761  ? 52.59700   95.92200  33.73800  1.000 46.93522  ?  761  LYS   B O   1 
ATOM   19992 C  CB  . LYS   B 1 761  ? 51.49900   97.68000  31.10300  1.000 42.97316  ?  761  LYS   B CB  1 
ATOM   19993 C  CG  . LYS   B 1 761  ? 51.67500   98.77600  32.15500  1.000 34.68565  ?  761  LYS   B CG  1 
ATOM   19994 C  CD  . LYS   B 1 761  ? 50.51200   98.79800  33.14400  1.000 52.15371  ?  761  LYS   B CD  1 
ATOM   19995 C  CE  . LYS   B 1 761  ? 50.58400   99.99100  34.08300  1.000 62.74779  ?  761  LYS   B CE  1 
ATOM   19996 N  NZ  . LYS   B 1 761  ? 50.11000   101.24200 33.42900  1.000 62.42962  ?  761  LYS   B NZ  1 
ATOM   19997 N  N   . ARG   B 1 762  ? 50.61100   95.27200  32.89800  1.000 36.85695  ?  762  ARG   B N   1 
ATOM   19998 C  CA  . ARG   B 1 762  ? 50.14900   94.74900  34.18100  1.000 35.44873  ?  762  ARG   B CA  1 
ATOM   19999 C  C   . ARG   B 1 762  ? 51.06300   93.64100  34.68700  1.000 45.85402  ?  762  ARG   B C   1 
ATOM   20000 O  O   . ARG   B 1 762  ? 51.45700   93.63400  35.85800  1.000 60.85618  ?  762  ARG   B O   1 
ATOM   20001 C  CB  . ARG   B 1 762  ? 48.71600   94.23700  34.05600  1.000 56.86662  ?  762  ARG   B CB  1 
ATOM   20002 C  CG  . ARG   B 1 762  ? 47.68300   95.30100  33.75000  1.000 55.17730  ?  762  ARG   B CG  1 
ATOM   20003 C  CD  . ARG   B 1 762  ? 46.36000   94.64900  33.39900  1.000 47.59923  ?  762  ARG   B CD  1 
ATOM   20004 N  NE  . ARG   B 1 762  ? 45.38300   95.60600  32.89800  1.000 43.01874  ?  762  ARG   B NE  1 
ATOM   20005 C  CZ  . ARG   B 1 762  ? 44.40600   95.29700  32.05800  1.000 51.77163  ?  762  ARG   B CZ  1 
ATOM   20006 N  NH1 . ARG   B 1 762  ? 44.27300   94.07200  31.57500  1.000 56.75300  ?  762  ARG   B NH1 1 
ATOM   20007 N  NH2 . ARG   B 1 762  ? 43.54500   96.24000  31.68700  1.000 53.33594  ?  762  ARG   B NH2 1 
ATOM   20008 N  N   . LEU   B 1 763  ? 51.40800   92.69100  33.81500  1.000 39.13573  ?  763  LEU   B N   1 
ATOM   20009 C  CA  . LEU   B 1 763  ? 52.24800   91.56900  34.22700  1.000 40.84814  ?  763  LEU   B CA  1 
ATOM   20010 C  C   . LEU   B 1 763  ? 53.60200   92.04900  34.73200  1.000 50.60324  ?  763  LEU   B C   1 
ATOM   20011 O  O   . LEU   B 1 763  ? 54.03200   91.68800  35.83300  1.000 60.37003  ?  763  LEU   B O   1 
ATOM   20012 C  CB  . LEU   B 1 763  ? 52.42800   90.59300  33.06500  1.000 49.20700  ?  763  LEU   B CB  1 
ATOM   20013 C  CG  . LEU   B 1 763  ? 53.38500   89.42700  33.32300  1.000 34.30340  ?  763  LEU   B CG  1 
ATOM   20014 C  CD1 . LEU   B 1 763  ? 52.71200   88.34400  34.15100  1.000 37.51873  ?  763  LEU   B CD1 1 
ATOM   20015 C  CD2 . LEU   B 1 763  ? 53.91400   88.86200  32.01600  1.000 39.05546  ?  763  LEU   B CD2 1 
ATOM   20016 N  N   . LEU   B 1 764  ? 54.29100   92.87100  33.93700  1.000 52.05620  ?  764  LEU   B N   1 
ATOM   20017 C  CA  . LEU   B 1 764  ? 55.61700   93.33500  34.33000  1.000 46.08255  ?  764  LEU   B CA  1 
ATOM   20018 C  C   . LEU   B 1 764  ? 55.55600   94.26600  35.53500  1.000 45.30328  ?  764  LEU   B C   1 
ATOM   20019 O  O   . LEU   B 1 764  ? 56.52200   94.34400  36.30300  1.000 49.30074  ?  764  LEU   B O   1 
ATOM   20020 C  CB  . LEU   B 1 764  ? 56.29700   94.02500  33.14900  1.000 49.12330  ?  764  LEU   B CB  1 
ATOM   20021 C  CG  . LEU   B 1 764  ? 56.40900   93.18000  31.87800  1.000 40.77731  ?  764  LEU   B CG  1 
ATOM   20022 C  CD1 . LEU   B 1 764  ? 57.03600   93.98300  30.75200  1.000 31.73940  ?  764  LEU   B CD1 1 
ATOM   20023 C  CD2 . LEU   B 1 764  ? 57.20100   91.90800  32.13900  1.000 51.58916  ?  764  LEU   B CD2 1 
ATOM   20024 N  N   . THR   B 1 765  ? 54.43900   94.97300  35.72200  1.000 38.15990  ?  765  THR   B N   1 
ATOM   20025 C  CA  . THR   B 1 765  ? 54.30100   95.83800  36.89000  1.000 49.29739  ?  765  THR   B CA  1 
ATOM   20026 C  C   . THR   B 1 765  ? 53.95200   95.03800  38.14000  1.000 49.33399  ?  765  THR   B C   1 
ATOM   20027 O  O   . THR   B 1 765  ? 54.52700   95.27300  39.20900  1.000 56.08445  ?  765  THR   B O   1 
ATOM   20028 C  CB  . THR   B 1 765  ? 53.24000   96.91100  36.63600  1.000 43.32889  ?  765  THR   B CB  1 
ATOM   20029 O  OG1 . THR   B 1 765  ? 53.62200   97.70900  35.50800  1.000 54.77133  ?  765  THR   B OG1 1 
ATOM   20030 C  CG2 . THR   B 1 765  ? 53.08400   97.80900  37.85400  1.000 38.24342  ?  765  THR   B CG2 1 
ATOM   20031 N  N   . GLU   B 1 766  ? 53.01900   94.08900  38.02500  1.000 48.58811  ?  766  GLU   B N   1 
ATOM   20032 C  CA  . GLU   B 1 766  ? 52.59900   93.30700  39.18400  1.000 52.07902  ?  766  GLU   B CA  1 
ATOM   20033 C  C   . GLU   B 1 766  ? 53.65200   92.28500  39.59900  1.000 54.34274  ?  766  GLU   B C   1 
ATOM   20034 O  O   . GLU   B 1 766  ? 53.87700   92.07900  40.79700  1.000 56.92536  ?  766  GLU   B O   1 
ATOM   20035 C  CB  . GLU   B 1 766  ? 51.26800   92.61100  38.89300  1.000 43.58429  ?  766  GLU   B CB  1 
ATOM   20036 C  CG  . GLU   B 1 766  ? 50.09600   93.56600  38.73700  1.000 55.37835  ?  766  GLU   B CG  1 
ATOM   20037 C  CD  . GLU   B 1 766  ? 48.82800   92.86300  38.29900  1.000 66.46800  ?  766  GLU   B CD  1 
ATOM   20038 O  OE1 . GLU   B 1 766  ? 48.81300   91.61400  38.28900  1.000 57.47963  ?  766  GLU   B OE1 1 
ATOM   20039 O  OE2 . GLU   B 1 766  ? 47.85000   93.56300  37.95900  1.000 60.87540  -1 766  GLU   B OE2 1 
ATOM   20040 N  N   . GLN   B 1 767  ? 54.30200   91.63300  38.63600  1.000 55.79612  ?  767  GLN   B N   1 
ATOM   20041 C  CA  . GLN   B 1 767  ? 55.35100   90.66800  38.94500  1.000 53.30485  ?  767  GLN   B CA  1 
ATOM   20042 C  C   . GLN   B 1 767  ? 56.70700   91.32100  39.18400  1.000 53.31525  ?  767  GLN   B C   1 
ATOM   20043 O  O   . GLN   B 1 767  ? 57.67400   90.60700  39.47100  1.000 51.71666  ?  767  GLN   B O   1 
ATOM   20044 C  CB  . GLN   B 1 767  ? 55.46800   89.63600  37.81900  1.000 55.18309  ?  767  GLN   B CB  1 
ATOM   20045 C  CG  . GLN   B 1 767  ? 54.16500   88.92100  37.49800  1.000 58.60884  ?  767  GLN   B CG  1 
ATOM   20046 C  CD  . GLN   B 1 767  ? 53.64800   88.09900  38.66100  1.000 64.19807  ?  767  GLN   B CD  1 
ATOM   20047 O  OE1 . GLN   B 1 767  ? 54.42400   87.49900  39.40400  1.000 69.55786  ?  767  GLN   B OE1 1 
ATOM   20048 N  NE2 . GLN   B 1 767  ? 52.33100   88.07000  38.82600  1.000 69.48377  ?  767  GLN   B NE2 1 
ATOM   20049 N  N   . LYS   B 1 768  ? 56.79400   92.65000  39.06700  1.000 52.79828  ?  768  LYS   B N   1 
ATOM   20050 C  CA  . LYS   B 1 768  ? 58.02400   93.40800  39.31400  1.000 53.57879  ?  768  LYS   B CA  1 
ATOM   20051 C  C   . LYS   B 1 768  ? 59.17700   92.93000  38.43700  1.000 60.15606  ?  768  LYS   B C   1 
ATOM   20052 O  O   . LYS   B 1 768  ? 60.32800   92.87300  38.87800  1.000 69.40526  ?  768  LYS   B O   1 
ATOM   20053 C  CB  . LYS   B 1 768  ? 58.41400   93.36300  40.79500  1.000 57.79626  ?  768  LYS   B CB  1 
ATOM   20054 C  CG  . LYS   B 1 768  ? 57.41000   94.05400  41.70700  1.000 49.33443  ?  768  LYS   B CG  1 
ATOM   20055 C  CD  . LYS   B 1 768  ? 57.79900   93.94100  43.17400  1.000 68.54855  ?  768  LYS   B CD  1 
ATOM   20056 C  CE  . LYS   B 1 768  ? 56.85800   94.75000  44.06100  1.000 45.00854  ?  768  LYS   B CE  1 
ATOM   20057 N  NZ  . LYS   B 1 768  ? 57.24700   94.66500  45.49700  1.000 52.78241  ?  768  LYS   B NZ  1 
ATOM   20058 N  N   . GLN   B 1 769  ? 58.87600   92.58200  37.18400  1.000 69.70271  ?  769  GLN   B N   1 
ATOM   20059 C  CA  . GLN   B 1 769  ? 59.89000   92.15200  36.22800  1.000 50.63583  ?  769  GLN   B CA  1 
ATOM   20060 C  C   . GLN   B 1 769  ? 60.40200   93.36400  35.46800  1.000 60.25894  ?  769  GLN   B C   1 
ATOM   20061 O  O   . GLN   B 1 769  ? 60.72200   93.28200  34.27600  1.000 64.39606  ?  769  GLN   B O   1 
ATOM   20062 C  CB  . GLN   B 1 769  ? 59.32400   91.09800  35.27200  1.000 53.91489  ?  769  GLN   B CB  1 
ATOM   20063 C  CG  . GLN   B 1 769  ? 58.74600   89.86500  35.96100  1.000 65.71350  ?  769  GLN   B CG  1 
ATOM   20064 C  CD  . GLN   B 1 769  ? 58.04800   88.91700  34.99800  1.000 70.37002  ?  769  GLN   B CD  1 
ATOM   20065 O  OE1 . GLN   B 1 769  ? 57.29400   88.03500  35.41600  1.000 72.60535  ?  769  GLN   B OE1 1 
ATOM   20066 N  NE2 . GLN   B 1 769  ? 58.29500   89.09400  33.70600  1.000 51.89798  ?  769  GLN   B NE2 1 
ATOM   20067 N  N   . VAL   B 1 770  ? 60.46600   94.49900  36.15900  1.000 75.64935  ?  770  VAL   B N   1 
ATOM   20068 C  CA  . VAL   B 1 770  ? 60.89000   95.77100  35.59700  1.000 77.20873  ?  770  VAL   B CA  1 
ATOM   20069 C  C   . VAL   B 1 770  ? 62.04400   96.29000  36.44600  1.000 80.69862  ?  770  VAL   B C   1 
ATOM   20070 O  O   . VAL   B 1 770  ? 62.21200   95.90800  37.60700  1.000 90.25468  ?  770  VAL   B O   1 
ATOM   20071 C  CB  . VAL   B 1 770  ? 59.72300   96.79000  35.54000  1.000 72.95160  ?  770  VAL   B CB  1 
ATOM   20072 C  CG1 . VAL   B 1 770  ? 59.15500   97.03400  36.93000  1.000 75.07630  ?  770  VAL   B CG1 1 
ATOM   20073 C  CG2 . VAL   B 1 770  ? 60.14100   98.10000  34.88100  1.000 82.87478  ?  770  VAL   B CG2 1 
ATOM   20074 N  N   . ASN   B 1 771  A 62.86300   97.14900  35.83500  1.000 84.44938  ?  770  ASN   B N   1 
ATOM   20075 C  CA  . ASN   B 1 771  A 64.03300   97.74700  36.47600  1.000 94.92674  ?  770  ASN   B CA  1 
ATOM   20076 C  C   . ASN   B 1 771  A 65.05100   96.66700  36.84600  1.000 84.21129  ?  770  ASN   B C   1 
ATOM   20077 O  O   . ASN   B 1 771  A 65.37600   96.44700  38.01500  1.000 85.49855  ?  770  ASN   B O   1 
ATOM   20078 C  CB  . ASN   B 1 771  A 63.63400   98.58100  37.70000  1.000 89.84966  ?  770  ASN   B CB  1 
ATOM   20079 C  CG  . ASN   B 1 771  A 62.69900   99.72400  37.35300  1.000 91.07692  ?  770  ASN   B CG  1 
ATOM   20080 O  OD1 . ASN   B 1 771  A 62.82800   100.35500 36.30400  1.000 92.62725  ?  770  ASN   B OD1 1 
ATOM   20081 N  ND2 . ASN   B 1 771  A 61.74800   99.99600  38.23900  1.000 102.52011 ?  770  ASN   B ND2 1 
ATOM   20082 N  N   . GLY   B 1 772  B 65.54900   95.98900  35.81200  1.000 89.58051  ?  770  GLY   B N   1 
ATOM   20083 C  CA  . GLY   B 1 772  B 66.53200   94.94400  35.96200  1.000 86.75280  ?  770  GLY   B CA  1 
ATOM   20084 C  C   . GLY   B 1 772  B 67.90300   95.34600  35.43800  1.000 84.99759  ?  770  GLY   B C   1 
ATOM   20085 O  O   . GLY   B 1 772  B 68.12600   96.44700  34.93700  1.000 77.78876  ?  770  GLY   B O   1 
ATOM   20086 N  N   . LEU   B 1 773  ? 68.83100   94.40000  35.55800  1.000 100.45989 ?  771  LEU   B N   1 
ATOM   20087 C  CA  . LEU   B 1 773  ? 70.22800   94.63200  35.22000  1.000 99.64057  ?  771  LEU   B CA  1 
ATOM   20088 C  C   . LEU   B 1 773  ? 70.50300   94.20300  33.78500  1.000 77.43498  ?  771  LEU   B C   1 
ATOM   20089 O  O   . LEU   B 1 773  ? 70.14300   93.09300  33.37800  1.000 70.46963  ?  771  LEU   B O   1 
ATOM   20090 C  CB  . LEU   B 1 773  ? 71.14600   93.88200  36.18500  1.000 98.30236  ?  771  LEU   B CB  1 
ATOM   20091 C  CG  . LEU   B 1 773  ? 70.46500   93.16600  37.35300  1.000 94.45183  ?  771  LEU   B CG  1 
ATOM   20092 C  CD1 . LEU   B 1 773  ? 70.15300   91.71900  36.98800  1.000 96.44602  ?  771  LEU   B CD1 1 
ATOM   20093 C  CD2 . LEU   B 1 773  ? 71.32100   93.24500  38.61100  1.000 68.84008  ?  771  LEU   B CD2 1 
ATOM   20094 N  N   . LEU   B 1 774  ? 71.14100   95.09300  33.02600  1.000 77.14272  ?  772  LEU   B N   1 
ATOM   20095 C  CA  . LEU   B 1 774  ? 71.53700   94.83100  31.64600  1.000 75.48897  ?  772  LEU   B CA  1 
ATOM   20096 C  C   . LEU   B 1 774  ? 72.83300   94.03500  31.67600  1.000 78.51347  ?  772  LEU   B C   1 
ATOM   20097 O  O   . LEU   B 1 774  ? 73.90400   94.59100  31.92000  1.000 80.51770  ?  772  LEU   B O   1 
ATOM   20098 C  CB  . LEU   B 1 774  ? 71.72500   96.13500  30.88000  1.000 70.37532  ?  772  LEU   B CB  1 
ATOM   20099 C  CG  . LEU   B 1 774  ? 70.62100   97.19700  30.77500  1.000 71.81360  ?  772  LEU   B CG  1 
ATOM   20100 C  CD1 . LEU   B 1 774  ? 69.30800   96.56200  30.41100  1.000 84.42293  ?  772  LEU   B CD1 1 
ATOM   20101 C  CD2 . LEU   B 1 774  ? 70.47400   98.02400  32.04300  1.000 83.86571  ?  772  LEU   B CD2 1 
ATOM   20102 N  N   . GLU   B 1 775  ? 72.75400   92.72900  31.42100  1.000 73.62705  ?  773  GLU   B N   1 
ATOM   20103 C  CA  . GLU   B 1 775  ? 73.93400   91.88200  31.52800  1.000 73.67743  ?  773  GLU   B CA  1 
ATOM   20104 C  C   . GLU   B 1 775  ? 74.51500   91.60800  30.14600  1.000 64.30908  ?  773  GLU   B C   1 
ATOM   20105 O  O   . GLU   B 1 775  ? 73.97800   90.76700  29.40900  1.000 72.13237  ?  773  GLU   B O   1 
ATOM   20106 C  CB  . GLU   B 1 775  ? 73.58600   90.57000  32.23600  1.000 69.18003  ?  773  GLU   B CB  1 
ATOM   20107 C  CG  . GLU   B 1 775  ? 73.00200   90.76100  33.62500  1.000 71.94281  ?  773  GLU   B CG  1 
ATOM   20108 C  CD  . GLU   B 1 775  ? 72.96800   89.47400  34.42300  1.000 94.42794  ?  773  GLU   B CD  1 
ATOM   20109 O  OE1 . GLU   B 1 775  ? 73.67200   88.51600  34.03800  1.000 105.24533 ?  773  GLU   B OE1 1 
ATOM   20110 O  OE2 . GLU   B 1 775  ? 72.23800   89.41900  35.43400  1.000 101.89982 -1 773  GLU   B OE2 1 
ATOM   20111 N  N   . PRO   B 1 776  ? 75.59800   92.26700  29.75000  1.000 58.18392  ?  774  PRO   B N   1 
ATOM   20112 C  CA  . PRO   B 1 776  ? 76.18900   92.02600  28.43100  1.000 67.45804  ?  774  PRO   B CA  1 
ATOM   20113 C  C   . PRO   B 1 776  ? 77.00700   90.73700  28.43100  1.000 75.91550  ?  774  PRO   B C   1 
ATOM   20114 O  O   . PRO   B 1 776  ? 77.15800   90.06000  29.44700  1.000 72.34346  ?  774  PRO   B O   1 
ATOM   20115 C  CB  . PRO   B 1 776  ? 77.08200   93.25500  28.20800  1.000 58.33084  ?  774  PRO   B CB  1 
ATOM   20116 C  CG  . PRO   B 1 776  ? 76.75100   94.21500  29.32900  1.000 78.07120  ?  774  PRO   B CG  1 
ATOM   20117 C  CD  . PRO   B 1 776  ? 76.29000   93.35500  30.45500  1.000 66.17675  ?  774  PRO   B CD  1 
ATOM   20118 N  N   . LEU   B 1 777  ? 77.54400   90.41100  27.25700  1.000 63.37056  ?  775  LEU   B N   1 
ATOM   20119 C  CA  . LEU   B 1 777  ? 78.35900   89.21700  27.06200  1.000 66.46361  ?  775  LEU   B CA  1 
ATOM   20120 C  C   . LEU   B 1 777  ? 79.82600   89.63500  27.06200  1.000 66.14024  ?  775  LEU   B C   1 
ATOM   20121 O  O   . LEU   B 1 777  ? 80.27300   90.35000  26.16000  1.000 67.61337  ?  775  LEU   B O   1 
ATOM   20122 C  CB  . LEU   B 1 777  ? 77.98500   88.51600  25.75800  1.000 69.13959  ?  775  LEU   B CB  1 
ATOM   20123 C  CG  . LEU   B 1 777  ? 78.30000   87.02400  25.64700  1.000 75.49592  ?  775  LEU   B CG  1 
ATOM   20124 C  CD1 . LEU   B 1 777  ? 77.33400   86.21700  26.49800  1.000 65.02568  ?  775  LEU   B CD1 1 
ATOM   20125 C  CD2 . LEU   B 1 777  ? 78.25200   86.57300  24.19600  1.000 70.02327  ?  775  LEU   B CD2 1 
ATOM   20126 N  N   . ARG   B 1 778  ? 80.56900   89.19100  28.07200  1.000 57.19729  ?  776  ARG   B N   1 
ATOM   20127 C  CA  . ARG   B 1 778  ? 81.97800   89.54800  28.17500  1.000 60.44269  ?  776  ARG   B CA  1 
ATOM   20128 C  C   . ARG   B 1 778  ? 82.80000   88.79700  27.13400  1.000 62.78676  ?  776  ARG   B C   1 
ATOM   20129 O  O   . ARG   B 1 778  ? 82.61500   87.59700  26.91700  1.000 68.65870  ?  776  ARG   B O   1 
ATOM   20130 C  CB  . ARG   B 1 778  ? 82.50200   89.24400  29.57800  1.000 53.03975  ?  776  ARG   B CB  1 
ATOM   20131 N  N   . GLU   B 1 779  ? 83.71700   89.51500  26.48900  1.000 66.28313  ?  777  GLU   B N   1 
ATOM   20132 C  CA  . GLU   B 1 779  ? 84.57200   88.91600  25.47500  1.000 66.34971  ?  777  GLU   B CA  1 
ATOM   20133 C  C   . GLU   B 1 779  ? 85.71500   88.14600  26.12000  1.000 61.49124  ?  777  GLU   B C   1 
ATOM   20134 O  O   . GLU   B 1 779  ? 86.29300   88.58000  27.12100  1.000 74.00769  ?  777  GLU   B O   1 
ATOM   20135 C  CB  . GLU   B 1 779  ? 85.12600   89.98800  24.53700  1.000 74.52676  ?  777  GLU   B CB  1 
ATOM   20136 C  CG  . GLU   B 1 779  ? 84.34800   90.12400  23.24000  1.000 74.52714  ?  777  GLU   B CG  1 
ATOM   20137 C  CD  . GLU   B 1 779  ? 84.38900   88.85800  22.40600  1.000 84.89454  ?  777  GLU   B CD  1 
ATOM   20138 O  OE1 . GLU   B 1 779  ? 85.49500   88.31300  22.19900  1.000 80.84244  ?  777  GLU   B OE1 1 
ATOM   20139 O  OE2 . GLU   B 1 779  ? 83.31300   88.39900  21.96700  1.000 79.39247  -1 777  GLU   B OE2 1 
ATOM   20140 N  N   . LEU   B 1 780  ? 86.03800   86.99500  25.53800  1.000 76.54152  ?  778  LEU   B N   1 
ATOM   20141 C  CA  . LEU   B 1 780  ? 87.09600   86.14300  26.06100  1.000 82.07082  ?  778  LEU   B CA  1 
ATOM   20142 C  C   . LEU   B 1 780  ? 88.45900   86.70300  25.67700  1.000 88.51162  ?  778  LEU   B C   1 
ATOM   20143 O  O   . LEU   B 1 780  ? 88.67800   87.09600  24.52600  1.000 79.68651  ?  778  LEU   B O   1 
ATOM   20144 C  CB  . LEU   B 1 780  ? 86.94000   84.71700  25.53300  1.000 69.34452  ?  778  LEU   B CB  1 
ATOM   20145 C  CG  . LEU   B 1 780  ? 86.27000   83.68900  26.45000  1.000 76.52255  ?  778  LEU   B CG  1 
ATOM   20146 C  CD1 . LEU   B 1 780  ? 87.26600   83.14900  27.46500  1.000 85.93734  ?  778  LEU   B CD1 1 
ATOM   20147 C  CD2 . LEU   B 1 780  ? 85.05900   84.28400  27.15400  1.000 55.18314  ?  778  LEU   B CD2 1 
ATOM   20148 N  N   . ASP   B 1 781  ? 89.37300   86.74200  26.64400  1.000 97.78380  ?  779  ASP   B N   1 
ATOM   20149 C  CA  . ASP   B 1 781  ? 90.73200   87.18100  26.37100  1.000 103.77575 ?  779  ASP   B CA  1 
ATOM   20150 C  C   . ASP   B 1 781  ? 91.43700   86.18300  25.45300  1.000 89.25582  ?  779  ASP   B C   1 
ATOM   20151 O  O   . ASP   B 1 781  ? 90.94300   85.08500  25.17900  1.000 95.93483  ?  779  ASP   B O   1 
ATOM   20152 C  CB  . ASP   B 1 781  ? 91.51200   87.35900  27.67400  1.000 106.17305 ?  779  ASP   B CB  1 
ATOM   20153 C  CG  . ASP   B 1 781  ? 91.24100   88.69500  28.33900  1.000 107.77283 ?  779  ASP   B CG  1 
ATOM   20154 O  OD1 . ASP   B 1 781  ? 90.39600   89.45800  27.82600  1.000 110.68765 ?  779  ASP   B OD1 1 
ATOM   20155 O  OD2 . ASP   B 1 781  ? 91.88000   88.98600  29.37200  1.000 98.16149  -1 779  ASP   B OD2 1 
ATOM   20156 N  N   . GLU   B 1 782  ? 92.61600   86.58000  24.97900  1.000 68.41785  ?  780  GLU   B N   1 
ATOM   20157 C  CA  . GLU   B 1 782  ? 93.33800   85.77800  24.00100  1.000 76.76871  ?  780  GLU   B CA  1 
ATOM   20158 C  C   . GLU   B 1 782  ? 93.76100   84.44100  24.59800  1.000 74.70075  ?  780  GLU   B C   1 
ATOM   20159 O  O   . GLU   B 1 782  ? 94.12800   84.35200  25.77200  1.000 83.96282  ?  780  GLU   B O   1 
ATOM   20160 C  CB  . GLU   B 1 782  ? 94.56500   86.53900  23.49300  1.000 76.33626  ?  780  GLU   B CB  1 
ATOM   20161 C  CG  . GLU   B 1 782  ? 95.16400   85.99300  22.19900  1.000 77.00860  ?  780  GLU   B CG  1 
ATOM   20162 C  CD  . GLU   B 1 782  ? 96.28500   84.98900  22.42500  1.000 94.50131  ?  780  GLU   B CD  1 
ATOM   20163 O  OE1 . GLU   B 1 782  ? 96.47200   84.53300  23.57300  1.000 101.24628 ?  780  GLU   B OE1 1 
ATOM   20164 O  OE2 . GLU   B 1 782  ? 96.98900   84.66000  21.44700  1.000 95.88291  -1 780  GLU   B OE2 1 
ATOM   20165 N  N   . GLN   B 1 783  ? 93.70900   83.40000  23.77000  1.000 80.46200  ?  781  GLN   B N   1 
ATOM   20166 C  CA  . GLN   B 1 783  ? 94.16700   82.06900  24.14000  1.000 73.83998  ?  781  GLN   B CA  1 
ATOM   20167 C  C   . GLN   B 1 783  ? 94.64700   81.36000  22.88200  1.000 91.44837  ?  781  GLN   B C   1 
ATOM   20168 O  O   . GLN   B 1 783  ? 94.39200   81.80000  21.75900  1.000 105.38524 ?  781  GLN   B O   1 
ATOM   20169 C  CB  . GLN   B 1 783  ? 93.06300   81.25800  24.83200  1.000 67.29380  ?  781  GLN   B CB  1 
ATOM   20170 C  CG  . GLN   B 1 783  ? 92.92100   81.53000  26.32100  1.000 79.29340  ?  781  GLN   B CG  1 
ATOM   20171 C  CD  . GLN   B 1 783  ? 91.49000   81.40300  26.80500  1.000 88.07516  ?  781  GLN   B CD  1 
ATOM   20172 O  OE1 . GLN   B 1 783  ? 90.90700   80.31900  26.78300  1.000 80.70970  ?  781  GLN   B OE1 1 
ATOM   20173 N  NE2 . GLN   B 1 783  ? 90.91500   82.51700  27.24300  1.000 91.88104  ?  781  GLN   B NE2 1 
ATOM   20174 N  N   . ALA   B 1 784  ? 95.36000   80.25300  23.08200  1.000 93.81027  ?  782  ALA   B N   1 
ATOM   20175 C  CA  . ALA   B 1 784  ? 95.74600   79.42300  21.95000  1.000 88.41927  ?  782  ALA   B CA  1 
ATOM   20176 C  C   . ALA   B 1 784  ? 94.64400   78.44400  21.57700  1.000 80.66623  ?  782  ALA   B C   1 
ATOM   20177 O  O   . ALA   B 1 784  ? 94.53000   78.05800  20.40900  1.000 78.98214  ?  782  ALA   B O   1 
ATOM   20178 C  CB  . ALA   B 1 784  ? 97.04400   78.67500  22.25800  1.000 82.45135  ?  782  ALA   B CB  1 
ATOM   20179 N  N   . GLU   B 1 785  ? 93.82600   78.04700  22.54800  1.000 71.96631  ?  783  GLU   B N   1 
ATOM   20180 C  CA  . GLU   B 1 785  ? 92.69700   77.15700  22.32600  1.000 76.02341  ?  783  GLU   B CA  1 
ATOM   20181 C  C   . GLU   B 1 785  ? 91.54300   77.60100  23.21200  1.000 78.92874  ?  783  GLU   B C   1 
ATOM   20182 O  O   . GLU   B 1 785  ? 91.75000   77.98300  24.36800  1.000 93.66998  ?  783  GLU   B O   1 
ATOM   20183 C  CB  . GLU   B 1 785  ? 93.06500   75.69800  22.62000  1.000 65.41892  ?  783  GLU   B CB  1 
ATOM   20184 C  CG  . GLU   B 1 785  ? 94.06500   75.10100  21.64000  1.000 81.08953  ?  783  GLU   B CG  1 
ATOM   20185 C  CD  . GLU   B 1 785  ? 94.73200   73.84700  22.16900  1.000 102.03443 ?  783  GLU   B CD  1 
ATOM   20186 O  OE1 . GLU   B 1 785  ? 94.36500   73.39400  23.27400  1.000 102.23238 ?  783  GLU   B OE1 1 
ATOM   20187 O  OE2 . GLU   B 1 785  ? 95.62900   73.31800  21.48000  1.000 91.07209  -1 783  GLU   B OE2 1 
ATOM   20188 N  N   . TYR   B 1 786  ? 90.33300   77.55100  22.66600  1.000 71.36544  ?  784  TYR   B N   1 
ATOM   20189 C  CA  . TYR   B 1 786  ? 89.13300   77.98200  23.36300  1.000 75.38572  ?  784  TYR   B CA  1 
ATOM   20190 C  C   . TYR   B 1 786  ? 88.19000   76.80100  23.54200  1.000 65.02184  ?  784  TYR   B C   1 
ATOM   20191 O  O   . TYR   B 1 786  ? 88.33200   75.75400  22.90500  1.000 70.77476  ?  784  TYR   B O   1 
ATOM   20192 C  CB  . TYR   B 1 786  ? 88.43100   79.11900  22.60700  1.000 74.77397  ?  784  TYR   B CB  1 
ATOM   20193 C  CG  . TYR   B 1 786  ? 89.31000   80.32400  22.34300  1.000 70.75628  ?  784  TYR   B CG  1 
ATOM   20194 C  CD1 . TYR   B 1 786  ? 90.21700   80.32800  21.29000  1.000 74.05493  ?  784  TYR   B CD1 1 
ATOM   20195 C  CD2 . TYR   B 1 786  ? 89.23000   81.46000  23.14000  1.000 74.52616  ?  784  TYR   B CD2 1 
ATOM   20196 C  CE1 . TYR   B 1 786  ? 91.02400   81.42400  21.04200  1.000 84.20209  ?  784  TYR   B CE1 1 
ATOM   20197 C  CE2 . TYR   B 1 786  ? 90.03300   82.56400  22.89700  1.000 69.63858  ?  784  TYR   B CE2 1 
ATOM   20198 C  CZ  . TYR   B 1 786  ? 90.92800   82.53900  21.84600  1.000 83.91625  ?  784  TYR   B CZ  1 
ATOM   20199 O  OH  . TYR   B 1 786  ? 91.73000   83.62900  21.59500  1.000 76.44555  ?  784  TYR   B OH  1 
ATOM   20200 N  N   . GLU   B 1 787  ? 87.21300   76.98600  24.42200  1.000 59.41825  ?  785  GLU   B N   1 
ATOM   20201 C  CA  . GLU   B 1 787  ? 86.26000   75.93700  24.75100  1.000 81.49658  ?  785  GLU   B CA  1 
ATOM   20202 C  C   . GLU   B 1 787  ? 85.09100   75.95900  23.77400  1.000 86.70597  ?  785  GLU   B C   1 
ATOM   20203 O  O   . GLU   B 1 787  ? 84.54300   77.02400  23.46900  1.000 86.30260  ?  785  GLU   B O   1 
ATOM   20204 C  CB  . GLU   B 1 787  ? 85.76600   76.09900  26.18900  1.000 81.97734  ?  785  GLU   B CB  1 
ATOM   20205 C  CG  . GLU   B 1 787  ? 85.54600   77.54100  26.61700  1.000 98.39281  ?  785  GLU   B CG  1 
ATOM   20206 C  CD  . GLU   B 1 787  ? 85.51800   77.70200  28.12400  1.000 102.79284 ?  785  GLU   B CD  1 
ATOM   20207 O  OE1 . GLU   B 1 787  ? 84.78200   76.94300  28.79100  1.000 92.65346  ?  785  GLU   B OE1 1 
ATOM   20208 O  OE2 . GLU   B 1 787  ? 86.23700   78.58300  28.64200  1.000 101.45663 -1 785  GLU   B OE2 1 
ATOM   20209 N  N   . THR   B 1 788  ? 84.72300   74.77800  23.27900  1.000 83.97948  ?  786  THR   B N   1 
ATOM   20210 C  CA  . THR   B 1 788  ? 83.59600   74.62500  22.37300  1.000 58.19373  ?  786  THR   B CA  1 
ATOM   20211 C  C   . THR   B 1 788  ? 82.28100   74.66500  23.14600  1.000 69.40510  ?  786  THR   B C   1 
ATOM   20212 O  O   . THR   B 1 788  ? 82.24800   74.67700  24.38000  1.000 87.61391  ?  786  THR   B O   1 
ATOM   20213 C  CB  . THR   B 1 788  ? 83.70800   73.32000  21.58100  1.000 60.23236  ?  786  THR   B CB  1 
ATOM   20214 O  OG1 . THR   B 1 788  ? 83.99300   72.22900  22.46700  1.000 69.41744  ?  786  THR   B OG1 1 
ATOM   20215 C  CG2 . THR   B 1 788  ? 84.80900   73.42100  20.53900  1.000 64.86289  ?  786  THR   B CG2 1 
ATOM   20216 N  N   . SER   B 1 789  ? 81.18400   74.70000  22.40000  1.000 70.23119  ?  787  SER   B N   1 
ATOM   20217 C  CA  . SER   B 1 789  ? 79.85100   74.65200  22.97500  1.000 66.56689  ?  787  SER   B CA  1 
ATOM   20218 C  C   . SER   B 1 789  ? 79.31600   73.22600  22.92300  1.000 65.11532  ?  787  SER   B C   1 
ATOM   20219 O  O   . SER   B 1 789  ? 79.89400   72.33600  22.29400  1.000 66.86195  ?  787  SER   B O   1 
ATOM   20220 C  CB  . SER   B 1 789  ? 78.90200   75.60700  22.24200  1.000 58.73958  ?  787  SER   B CB  1 
ATOM   20221 O  OG  . SER   B 1 789  ? 78.21900   74.94700  21.19000  1.000 65.33423  ?  787  SER   B OG  1 
ATOM   20222 N  N   . ALA   B 1 790  ? 78.18800   73.02000  23.60600  1.000 66.30978  ?  788  ALA   B N   1 
ATOM   20223 C  CA  . ALA   B 1 790  ? 77.57400   71.69800  23.65400  1.000 64.12709  ?  788  ALA   B CA  1 
ATOM   20224 C  C   . ALA   B 1 790  ? 77.19700   71.21500  22.25900  1.000 83.73676  ?  788  ALA   B C   1 
ATOM   20225 O  O   . ALA   B 1 790  ? 77.48900   70.07400  21.88300  1.000 83.41790  ?  788  ALA   B O   1 
ATOM   20226 C  CB  . ALA   B 1 790  ? 76.35200   71.72800  24.56900  1.000 52.40889  ?  788  ALA   B CB  1 
ATOM   20227 N  N   . VAL   B 1 791  ? 76.55100   72.07700  21.47000  1.000 81.34343  ?  789  VAL   B N   1 
ATOM   20228 C  CA  . VAL   B 1 791  ? 76.16800   71.68400  20.11800  1.000 53.31041  ?  789  VAL   B CA  1 
ATOM   20229 C  C   . VAL   B 1 791  ? 77.39200   71.59400  19.21400  1.000 56.63386  ?  789  VAL   B C   1 
ATOM   20230 O  O   . VAL   B 1 791  ? 77.40300   70.82000  18.25000  1.000 69.77870  ?  789  VAL   B O   1 
ATOM   20231 C  CB  . VAL   B 1 791  ? 75.11000   72.65400  19.56100  1.000 62.06867  ?  789  VAL   B CB  1 
ATOM   20232 C  CG1 . VAL   B 1 791  ? 73.91100   72.72000  20.49800  1.000 67.94067  ?  789  VAL   B CG1 1 
ATOM   20233 C  CG2 . VAL   B 1 791  ? 75.69900   74.03900  19.35800  1.000 65.73731  ?  789  VAL   B CG2 1 
ATOM   20234 N  N   . GLU   B 1 792  ? 78.44000   72.37000  19.50500  1.000 65.23922  ?  790  GLU   B N   1 
ATOM   20235 C  CA  . GLU   B 1 792  ? 79.67900   72.24500  18.74500  1.000 64.76579  ?  790  GLU   B CA  1 
ATOM   20236 C  C   . GLU   B 1 792  ? 80.37900   70.93200  19.05800  1.000 71.16793  ?  790  GLU   B C   1 
ATOM   20237 O  O   . GLU   B 1 792  ? 81.00400   70.32600  18.17800  1.000 73.92282  ?  790  GLU   B O   1 
ATOM   20238 C  CB  . GLU   B 1 792  ? 80.60600   73.42300  19.03800  1.000 55.96337  ?  790  GLU   B CB  1 
ATOM   20239 C  CG  . GLU   B 1 792  ? 80.19700   74.71700  18.37500  1.000 67.86439  ?  790  GLU   B CG  1 
ATOM   20240 C  CD  . GLU   B 1 792  ? 81.24800   75.79100  18.53900  1.000 69.69862  ?  790  GLU   B CD  1 
ATOM   20241 O  OE1 . GLU   B 1 792  ? 82.06100   75.67700  19.48100  1.000 74.06731  ?  790  GLU   B OE1 1 
ATOM   20242 O  OE2 . GLU   B 1 792  ? 81.26000   76.74700  17.73800  1.000 70.04213  -1 790  GLU   B OE2 1 
ATOM   20243 N  N   . LYS   B 1 793  ? 80.29500   70.48500  20.31200  1.000 68.19021  ?  791  LYS   B N   1 
ATOM   20244 C  CA  . LYS   B 1 793  ? 80.84700   69.18600  20.67300  1.000 75.47110  ?  791  LYS   B CA  1 
ATOM   20245 C  C   . LYS   B 1 793  ? 80.10400   68.05800  19.96800  1.000 75.57687  ?  791  LYS   B C   1 
ATOM   20246 O  O   . LYS   B 1 793  ? 80.72800   67.13800  19.42600  1.000 74.92846  ?  791  LYS   B O   1 
ATOM   20247 C  CB  . LYS   B 1 793  ? 80.79500   69.00000  22.19000  1.000 74.54320  ?  791  LYS   B CB  1 
ATOM   20248 C  CG  . LYS   B 1 793  ? 81.77500   69.86600  22.96900  1.000 76.01222  ?  791  LYS   B CG  1 
ATOM   20249 C  CD  . LYS   B 1 793  ? 81.56100   69.71000  24.46800  1.000 60.46449  ?  791  LYS   B CD  1 
ATOM   20250 C  CE  . LYS   B 1 793  ? 82.66700   70.38000  25.27000  1.000 76.06940  ?  791  LYS   B CE  1 
ATOM   20251 N  NZ  . LYS   B 1 793  ? 82.70300   71.85700  25.07600  1.000 71.05049  ?  791  LYS   B NZ  1 
ATOM   20252 N  N   . ARG   B 1 794  ? 78.76900   68.12200  19.95200  1.000 68.78581  ?  792  ARG   B N   1 
ATOM   20253 C  CA  . ARG   B 1 794  ? 77.97900   67.06100  19.33500  1.000 63.37640  ?  792  ARG   B CA  1 
ATOM   20254 C  C   . ARG   B 1 794  ? 78.23000   66.97700  17.83500  1.000 57.88391  ?  792  ARG   B C   1 
ATOM   20255 O  O   . ARG   B 1 794  ? 78.26900   65.87900  17.27000  1.000 52.89696  ?  792  ARG   B O   1 
ATOM   20256 C  CB  . ARG   B 1 794  ? 76.49200   67.28000  19.62200  1.000 44.04190  ?  792  ARG   B CB  1 
ATOM   20257 N  N   . MET   B 1 795  ? 78.40100   68.12100  17.16900  1.000 64.98537  ?  793  MET   B N   1 
ATOM   20258 C  CA  . MET   B 1 795  ? 78.70400   68.09200  15.74100  1.000 69.47094  ?  793  MET   B CA  1 
ATOM   20259 C  C   . MET   B 1 795  ? 80.08100   67.49600  15.48500  1.000 62.74300  ?  793  MET   B C   1 
ATOM   20260 O  O   . MET   B 1 795  ? 80.28600   66.79800  14.48500  1.000 56.92247  ?  793  MET   B O   1 
ATOM   20261 C  CB  . MET   B 1 795  ? 78.60500   69.49700  15.15000  1.000 59.28110  ?  793  MET   B CB  1 
ATOM   20262 C  CG  . MET   B 1 795  ? 77.17900   69.93500  14.88900  1.000 59.60311  ?  793  MET   B CG  1 
ATOM   20263 S  SD  . MET   B 1 795  ? 76.38300   68.83700  13.70300  1.000 67.78358  ?  793  MET   B SD  1 
ATOM   20264 C  CE  . MET   B 1 795  ? 74.69300   68.86800  14.29200  1.000 66.40890  ?  793  MET   B CE  1 
ATOM   20265 N  N   . TYR   B 1 796  ? 81.03500   67.75400  16.38200  1.000 66.30462  ?  794  TYR   B N   1 
ATOM   20266 C  CA  . TYR   B 1 796  ? 82.36900   67.18700  16.22300  1.000 62.54889  ?  794  TYR   B CA  1 
ATOM   20267 C  C   . TYR   B 1 796  ? 82.34000   65.66800  16.34000  1.000 66.94788  ?  794  TYR   B C   1 
ATOM   20268 O  O   . TYR   B 1 796  ? 83.00900   64.97200  15.56800  1.000 64.19872  ?  794  TYR   B O   1 
ATOM   20269 C  CB  . TYR   B 1 796  ? 83.32100   67.78900  17.25700  1.000 53.58841  ?  794  TYR   B CB  1 
ATOM   20270 C  CG  . TYR   B 1 796  ? 84.78800   67.52000  16.98500  1.000 56.56383  ?  794  TYR   B CG  1 
ATOM   20271 C  CD1 . TYR   B 1 796  ? 85.37900   66.31900  17.35800  1.000 60.87799  ?  794  TYR   B CD1 1 
ATOM   20272 C  CD2 . TYR   B 1 796  ? 85.58300   68.47400  16.36300  1.000 68.66023  ?  794  TYR   B CD2 1 
ATOM   20273 C  CE1 . TYR   B 1 796  ? 86.71900   66.07400  17.11300  1.000 54.02916  ?  794  TYR   B CE1 1 
ATOM   20274 C  CE2 . TYR   B 1 796  ? 86.92400   68.23700  16.11400  1.000 71.12865  ?  794  TYR   B CE2 1 
ATOM   20275 C  CZ  . TYR   B 1 796  ? 87.48500   67.03700  16.49000  1.000 56.07256  ?  794  TYR   B CZ  1 
ATOM   20276 O  OH  . TYR   B 1 796  ? 88.81900   66.80400  16.24100  1.000 51.27575  ?  794  TYR   B OH  1 
ATOM   20277 N  N   . ILE   B 1 797  ? 81.56700   65.13200  17.28900  1.000 65.89239  ?  795  ILE   B N   1 
ATOM   20278 C  CA  . ILE   B 1 797  ? 81.59700   63.68900  17.50700  1.000 72.62533  ?  795  ILE   B CA  1 
ATOM   20279 C  C   . ILE   B 1 797  ? 80.90200   62.94700  16.37100  1.000 71.24626  ?  795  ILE   B C   1 
ATOM   20280 O  O   . ILE   B 1 797  ? 81.33100   61.85200  15.99300  1.000 74.48813  ?  795  ILE   B O   1 
ATOM   20281 C  CB  . ILE   B 1 797  ? 80.99700   63.31900  18.88000  1.000 58.35266  ?  795  ILE   B CB  1 
ATOM   20282 C  CG1 . ILE   B 1 797  ? 79.47900   63.50400  18.89800  1.000 65.42253  ?  795  ILE   B CG1 1 
ATOM   20283 C  CG2 . ILE   B 1 797  ? 81.64100   64.14000  19.98300  1.000 45.74934  ?  795  ILE   B CG2 1 
ATOM   20284 C  CD1 . ILE   B 1 797  ? 78.80300   62.87100  20.09400  1.000 74.93312  ?  795  ILE   B CD1 1 
ATOM   20285 N  N   . ILE   B 1 798  ? 79.83800   63.51900  15.79700  1.000 56.12082  ?  796  ILE   B N   1 
ATOM   20286 C  CA  . ILE   B 1 798  ? 79.13600   62.84300  14.70900  1.000 52.48825  ?  796  ILE   B CA  1 
ATOM   20287 C  C   . ILE   B 1 798  ? 80.01900   62.76900  13.47100  1.000 50.99768  ?  796  ILE   B C   1 
ATOM   20288 O  O   . ILE   B 1 798  ? 80.06800   61.74100  12.78500  1.000 65.78843  ?  796  ILE   B O   1 
ATOM   20289 C  CB  . ILE   B 1 798  ? 77.80100   63.54500  14.40400  1.000 35.88109  ?  796  ILE   B CB  1 
ATOM   20290 C  CG1 . ILE   B 1 798  ? 76.91300   63.58300  15.64500  1.000 47.13300  ?  796  ILE   B CG1 1 
ATOM   20291 C  CG2 . ILE   B 1 798  ? 77.07400   62.83500  13.27500  1.000 40.41106  ?  796  ILE   B CG2 1 
ATOM   20292 C  CD1 . ILE   B 1 798  ? 75.66900   64.42800  15.47100  1.000 37.95646  ?  796  ILE   B CD1 1 
ATOM   20293 N  N   . GLN   B 1 799  ? 80.72800   63.85700  13.16400  1.000 55.01558  ?  797  GLN   B N   1 
ATOM   20294 C  CA  . GLN   B 1 799  ? 81.62100   63.85300  12.01200  1.000 59.66970  ?  797  GLN   B CA  1 
ATOM   20295 C  C   . GLN   B 1 799  ? 82.79400   62.90100  12.21600  1.000 65.50664  ?  797  GLN   B C   1 
ATOM   20296 O  O   . GLN   B 1 799  ? 83.32800   62.36400  11.23900  1.000 68.00299  ?  797  GLN   B O   1 
ATOM   20297 C  CB  . GLN   B 1 799  ? 82.12000   65.27300  11.73500  1.000 49.63689  ?  797  GLN   B CB  1 
ATOM   20298 C  CG  . GLN   B 1 799  ? 83.00500   65.40200  10.50400  1.000 60.28677  ?  797  GLN   B CG  1 
ATOM   20299 C  CD  . GLN   B 1 799  ? 82.27300   65.07100  9.21800   1.000 64.61265  ?  797  GLN   B CD  1 
ATOM   20300 O  OE1 . GLN   B 1 799  ? 81.11800   65.45400  9.03100   1.000 70.29628  ?  797  GLN   B OE1 1 
ATOM   20301 N  NE2 . GLN   B 1 799  ? 82.94300   64.35200  8.32400   1.000 72.40660  ?  797  GLN   B NE2 1 
ATOM   20302 N  N   . GLN   B 1 800  ? 83.19600   62.66300  13.46700  1.000 71.25019  ?  798  GLN   B N   1 
ATOM   20303 C  CA  . GLN   B 1 800  ? 84.33800   61.78800  13.70900  1.000 73.25837  ?  798  GLN   B CA  1 
ATOM   20304 C  C   . GLN   B 1 800  ? 84.01200   60.32600  13.42900  1.000 68.56542  ?  798  GLN   B C   1 
ATOM   20305 O  O   . GLN   B 1 800  ? 84.88500   59.58600  12.96300  1.000 72.40940  ?  798  GLN   B O   1 
ATOM   20306 C  CB  . GLN   B 1 800  ? 84.84200   61.94700  15.14300  1.000 63.72831  ?  798  GLN   B CB  1 
ATOM   20307 C  CG  . GLN   B 1 800  ? 85.57900   63.24900  15.38900  1.000 62.41706  ?  798  GLN   B CG  1 
ATOM   20308 C  CD  . GLN   B 1 800  ? 86.33600   63.72800  14.16400  1.000 66.73836  ?  798  GLN   B CD  1 
ATOM   20309 O  OE1 . GLN   B 1 800  ? 85.99600   64.75400  13.57500  1.000 68.68668  ?  798  GLN   B OE1 1 
ATOM   20310 N  NE2 . GLN   B 1 800  ? 87.37200   62.99000  13.77800  1.000 50.27746  ?  798  GLN   B NE2 1 
ATOM   20311 N  N   . GLN   B 1 801  ? 82.77800   59.89300  13.70600  1.000 69.68586  ?  799  GLN   B N   1 
ATOM   20312 C  CA  . GLN   B 1 801  ? 82.36700   58.51600  13.45300  1.000 70.75862  ?  799  GLN   B CA  1 
ATOM   20313 C  C   . GLN   B 1 801  ? 82.67600   58.13300  12.01300  1.000 74.71282  ?  799  GLN   B C   1 
ATOM   20314 O  O   . GLN   B 1 801  ? 83.54400   57.29100  11.76200  1.000 85.81111  ?  799  GLN   B O   1 
ATOM   20315 C  CB  . GLN   B 1 801  ? 80.87800   58.33200  13.75000  1.000 55.78183  ?  799  GLN   B CB  1 
ATOM   20316 C  CG  . GLN   B 1 801  ? 80.38000   59.24000  14.85300  1.000 66.54123  ?  799  GLN   B CG  1 
ATOM   20317 C  CD  . GLN   B 1 801  ? 79.16800   58.70600  15.58300  1.000 93.53816  ?  799  GLN   B CD  1 
ATOM   20318 O  OE1 . GLN   B 1 801  ? 79.20200   58.52000  16.79800  1.000 84.47548  ?  799  GLN   B OE1 1 
ATOM   20319 N  NE2 . GLN   B 1 801  ? 78.08600   58.46900  14.85200  1.000 98.04239  ?  799  GLN   B NE2 1 
ATOM   20320 N  N   . ASP   B 1 802  ? 81.99100   58.75700  11.06600  1.000 59.73661  ?  800  ASP   B N   1 
ATOM   20321 C  CA  . ASP   B 1 802  ? 82.29900   58.61600  9.64700   1.000 66.21074  ?  800  ASP   B CA  1 
ATOM   20322 C  C   . ASP   B 1 802  ? 82.94000   59.92500  9.19800   1.000 66.61550  ?  800  ASP   B C   1 
ATOM   20323 O  O   . ASP   B 1 802  ? 82.24400   60.91200  8.94200   1.000 78.48696  ?  800  ASP   B O   1 
ATOM   20324 C  CB  . ASP   B 1 802  ? 81.04800   58.29400  8.83800   1.000 67.02334  ?  800  ASP   B CB  1 
ATOM   20325 C  CG  . ASP   B 1 802  ? 81.36700   57.89100  7.41500   1.000 77.26515  ?  800  ASP   B CG  1 
ATOM   20326 O  OD1 . ASP   B 1 802  ? 82.54600   57.58300  7.13600   1.000 82.64473  ?  800  ASP   B OD1 1 
ATOM   20327 O  OD2 . ASP   B 1 802  ? 80.44400   57.88700  6.57400   1.000 79.23302  -1 800  ASP   B OD2 1 
ATOM   20328 N  N   . VAL   B 1 803  ? 84.27400   59.93300  9.11200   1.000 53.63307  ?  801  VAL   B N   1 
ATOM   20329 C  CA  . VAL   B 1 803  ? 84.98700   61.14300  8.72300   1.000 58.17381  ?  801  VAL   B CA  1 
ATOM   20330 C  C   . VAL   B 1 803  ? 84.72500   61.51600  7.27200   1.000 74.89959  ?  801  VAL   B C   1 
ATOM   20331 O  O   . VAL   B 1 803  ? 84.97000   62.66200  6.87700   1.000 70.49228  ?  801  VAL   B O   1 
ATOM   20332 C  CB  . VAL   B 1 803  ? 86.49800   60.98200  8.97300   1.000 40.42413  ?  801  VAL   B CB  1 
ATOM   20333 C  CG1 . VAL   B 1 803  ? 86.82200   61.24400  10.43600  1.000 50.82959  ?  801  VAL   B CG1 1 
ATOM   20334 C  CG2 . VAL   B 1 803  ? 86.95300   59.59000  8.56400   1.000 59.54960  ?  801  VAL   B CG2 1 
ATOM   20335 N  N   . GLU   B 1 804  ? 84.23100   60.57900  6.46500   1.000 70.13946  ?  802  GLU   B N   1 
ATOM   20336 C  CA  . GLU   B 1 804  ? 83.91800   60.82800  5.06600   1.000 62.50316  ?  802  GLU   B CA  1 
ATOM   20337 C  C   . GLU   B 1 804  ? 82.44200   61.13200  4.84300   1.000 61.12614  ?  802  GLU   B C   1 
ATOM   20338 O  O   . GLU   B 1 804  ? 81.98700   61.13600  3.69400   1.000 63.54120  ?  802  GLU   B O   1 
ATOM   20339 C  CB  . GLU   B 1 804  ? 84.34100   59.63000  4.21400   1.000 58.79637  ?  802  GLU   B CB  1 
ATOM   20340 C  CG  . GLU   B 1 804  ? 85.80900   59.24500  4.34900   1.000 60.74023  ?  802  GLU   B CG  1 
ATOM   20341 C  CD  . GLU   B 1 804  ? 86.71800   60.03100  3.42200   1.000 74.85171  ?  802  GLU   B CD  1 
ATOM   20342 O  OE1 . GLU   B 1 804  ? 86.85300   61.25900  3.60700   1.000 76.82428  ?  802  GLU   B OE1 1 
ATOM   20343 O  OE2 . GLU   B 1 804  ? 87.29500   59.41600  2.50000   1.000 77.55639  -1 802  GLU   B OE2 1 
ATOM   20344 N  N   . SER   B 1 805  ? 81.68700   61.38300  5.90900   1.000 57.02838  ?  803  SER   B N   1 
ATOM   20345 C  CA  . SER   B 1 805  ? 80.26500   61.67100  5.78600   1.000 46.68390  ?  803  SER   B CA  1 
ATOM   20346 C  C   . SER   B 1 805  ? 80.04300   63.10400  5.32400   1.000 51.68328  ?  803  SER   B C   1 
ATOM   20347 O  O   . SER   B 1 805  ? 80.78100   64.01800  5.70200   1.000 56.66601  ?  803  SER   B O   1 
ATOM   20348 C  CB  . SER   B 1 805  ? 79.55500   61.44200  7.12100   1.000 50.99128  ?  803  SER   B CB  1 
ATOM   20349 O  OG  . SER   B 1 805  ? 78.25800   62.01500  7.11600   1.000 37.91884  ?  803  SER   B OG  1 
ATOM   20350 N  N   . ILE   B 1 806  ? 79.01700   63.29400  4.49800   1.000 55.42991  ?  804  ILE   B N   1 
ATOM   20351 C  CA  . ILE   B 1 806  ? 78.59100   64.61300  4.05300   1.000 41.59379  ?  804  ILE   B CA  1 
ATOM   20352 C  C   . ILE   B 1 806  ? 77.17500   64.92300  4.53200   1.000 39.66209  ?  804  ILE   B C   1 
ATOM   20353 O  O   . ILE   B 1 806  ? 76.53400   65.83800  4.02700   1.000 56.46655  ?  804  ILE   B O   1 
ATOM   20354 C  CB  . ILE   B 1 806  ? 78.70100   64.74800  2.52200   1.000 31.87628  ?  804  ILE   B CB  1 
ATOM   20355 C  CG1 . ILE   B 1 806  ? 77.90900   63.63600  1.82900   1.000 47.84510  ?  804  ILE   B CG1 1 
ATOM   20356 C  CG2 . ILE   B 1 806  ? 80.15800   64.73000  2.08700   1.000 47.43733  ?  804  ILE   B CG2 1 
ATOM   20357 C  CD1 . ILE   B 1 806  ? 77.85900   63.76600  0.31900   1.000 46.32203  ?  804  ILE   B CD1 1 
ATOM   20358 N  N   . ALA   B 1 807  ? 76.68400   64.16200  5.51400   1.000 34.20580  ?  805  ALA   B N   1 
ATOM   20359 C  CA  . ALA   B 1 807  ? 75.30600   64.32400  5.96300   1.000 49.79516  ?  805  ALA   B CA  1 
ATOM   20360 C  C   . ALA   B 1 807  ? 75.07400   65.68200  6.60800   1.000 50.18692  ?  805  ALA   B C   1 
ATOM   20361 O  O   . ALA   B 1 807  ? 73.95900   66.21200  6.55500   1.000 45.96798  ?  805  ALA   B O   1 
ATOM   20362 C  CB  . ALA   B 1 807  ? 74.93400   63.20600  6.93700   1.000 42.15992  ?  805  ALA   B CB  1 
ATOM   20363 N  N   . TYR   B 1 808  ? 76.10500   66.26300  7.21900   1.000 50.01686  ?  806  TYR   B N   1 
ATOM   20364 C  CA  . TYR   B 1 808  ? 75.98200   67.56900  7.85100   1.000 46.50888  ?  806  TYR   B CA  1 
ATOM   20365 C  C   . TYR   B 1 808  ? 76.72500   68.65500  7.08300   1.000 61.34965  ?  806  TYR   B C   1 
ATOM   20366 O  O   . TYR   B 1 808  ? 77.04100   69.70800  7.64700   1.000 60.87426  ?  806  TYR   B O   1 
ATOM   20367 C  CB  . TYR   B 1 808  ? 76.45100   67.49700  9.30400   1.000 56.44359  ?  806  TYR   B CB  1 
ATOM   20368 C  CG  . TYR   B 1 808  ? 75.48100   66.73600  10.17900  1.000 54.78945  ?  806  TYR   B CG  1 
ATOM   20369 C  CD1 . TYR   B 1 808  ? 75.58500   65.36000  10.33300  1.000 55.17031  ?  806  TYR   B CD1 1 
ATOM   20370 C  CD2 . TYR   B 1 808  ? 74.44500   67.39200  10.83000  1.000 53.95844  ?  806  TYR   B CD2 1 
ATOM   20371 C  CE1 . TYR   B 1 808  ? 74.69300   64.66100  11.12300  1.000 48.07500  ?  806  TYR   B CE1 1 
ATOM   20372 C  CE2 . TYR   B 1 808  ? 73.54800   66.70200  11.62300  1.000 52.05176  ?  806  TYR   B CE2 1 
ATOM   20373 C  CZ  . TYR   B 1 808  ? 73.67600   65.33700  11.76500  1.000 59.14961  ?  806  TYR   B CZ  1 
ATOM   20374 O  OH  . TYR   B 1 808  ? 72.78500   64.64700  12.55400  1.000 73.62042  ?  806  TYR   B OH  1 
ATOM   20375 N  N   . ASN   B 1 809  ? 77.01000   68.41700  5.80400   1.000 51.81817  ?  807  ASN   B N   1 
ATOM   20376 C  CA  . ASN   B 1 809  ? 77.45700   69.47800  4.91500   1.000 51.54241  ?  807  ASN   B CA  1 
ATOM   20377 C  C   . ASN   B 1 809  ? 76.25400   70.28400  4.44400   1.000 56.54269  ?  807  ASN   B C   1 
ATOM   20378 O  O   . ASN   B 1 809  ? 75.19500   69.72600  4.14300   1.000 62.67707  ?  807  ASN   B O   1 
ATOM   20379 C  CB  . ASN   B 1 809  ? 78.20800   68.90000  3.71600   1.000 37.37034  ?  807  ASN   B CB  1 
ATOM   20380 C  CG  . ASN   B 1 809  ? 79.48100   68.18600  4.11500   1.000 48.71629  ?  807  ASN   B CG  1 
ATOM   20381 O  OD1 . ASN   B 1 809  ? 79.60400   67.69200  5.23600   1.000 73.62491  ?  807  ASN   B OD1 1 
ATOM   20382 N  ND2 . ASN   B 1 809  ? 80.44100   68.13200  3.20000   1.000 58.45319  ?  807  ASN   B ND2 1 
ATOM   20383 N  N   . VAL   B 1 810  ? 76.41900   71.60100  4.38700   1.000 51.41483  ?  808  VAL   B N   1 
ATOM   20384 C  CA  . VAL   B 1 810  ? 75.33500   72.52000  4.05800   1.000 52.86086  ?  808  VAL   B CA  1 
ATOM   20385 C  C   . VAL   B 1 810  ? 75.66200   73.16000  2.71600   1.000 56.46830  ?  808  VAL   B C   1 
ATOM   20386 O  O   . VAL   B 1 810  ? 76.59600   73.96500  2.61300   1.000 59.46104  ?  808  VAL   B O   1 
ATOM   20387 C  CB  . VAL   B 1 810  ? 75.13900   73.58100  5.14900   1.000 56.08629  ?  808  VAL   B CB  1 
ATOM   20388 C  CG1 . VAL   B 1 810  ? 73.77700   74.23700  5.01200   1.000 48.15289  ?  808  VAL   B CG1 1 
ATOM   20389 C  CG2 . VAL   B 1 810  ? 75.30300   72.96000  6.53000   1.000 54.56353  ?  808  VAL   B CG2 1 
ATOM   20390 N  N   . VAL   B 1 811  ? 74.89200   72.81100  1.68600   1.000 55.17636  ?  809  VAL   B N   1 
ATOM   20391 C  CA  . VAL   B 1 811  ? 75.13100   73.26500  0.32100   1.000 34.02842  ?  809  VAL   B CA  1 
ATOM   20392 C  C   . VAL   B 1 811  ? 73.96700   74.14400  -0.11400  1.000 43.04717  ?  809  VAL   B C   1 
ATOM   20393 O  O   . VAL   B 1 811  ? 72.80000   73.77200  0.06200   1.000 45.60700  ?  809  VAL   B O   1 
ATOM   20394 C  CB  . VAL   B 1 811  ? 75.30700   72.07900  -0.64300  1.000 37.17424  ?  809  VAL   B CB  1 
ATOM   20395 C  CG1 . VAL   B 1 811  ? 75.89800   72.54900  -1.96200  1.000 40.84698  ?  809  VAL   B CG1 1 
ATOM   20396 C  CG2 . VAL   B 1 811  ? 76.17300   71.00000  -0.01000  1.000 39.25584  ?  809  VAL   B CG2 1 
ATOM   20397 N  N   . TYR   B 1 812  ? 74.28400   75.30500  -0.68600  1.000 42.11883  ?  810  TYR   B N   1 
ATOM   20398 C  CA  . TYR   B 1 812  ? 73.29200   76.22000  -1.23100  1.000 38.64486  ?  810  TYR   B CA  1 
ATOM   20399 C  C   . TYR   B 1 812  ? 73.74000   76.69500  -2.60600  1.000 34.53722  ?  810  TYR   B C   1 
ATOM   20400 O  O   . TYR   B 1 812  ? 74.93000   76.68200  -2.93100  1.000 39.09270  ?  810  TYR   B O   1 
ATOM   20401 C  CB  . TYR   B 1 812  ? 73.06700   77.43400  -0.31700  1.000 34.00104  ?  810  TYR   B CB  1 
ATOM   20402 C  CG  . TYR   B 1 812  ? 72.14500   77.18400  0.85600   1.000 44.82013  ?  810  TYR   B CG  1 
ATOM   20403 C  CD1 . TYR   B 1 812  ? 72.62300   76.63700  2.04000   1.000 43.19484  ?  810  TYR   B CD1 1 
ATOM   20404 C  CD2 . TYR   B 1 812  ? 70.79700   77.51300  0.78400   1.000 39.38545  ?  810  TYR   B CD2 1 
ATOM   20405 C  CE1 . TYR   B 1 812  ? 71.78200   76.41400  3.11500   1.000 33.42498  ?  810  TYR   B CE1 1 
ATOM   20406 C  CE2 . TYR   B 1 812  ? 69.95000   77.29400  1.85400   1.000 42.06561  ?  810  TYR   B CE2 1 
ATOM   20407 C  CZ  . TYR   B 1 812  ? 70.44700   76.74400  3.01600   1.000 36.45611  ?  810  TYR   B CZ  1 
ATOM   20408 O  OH  . TYR   B 1 812  ? 69.60700   76.52500  4.08400   1.000 48.71536  ?  810  TYR   B OH  1 
ATOM   20409 N  N   . THR   B 1 813  ? 72.76900   77.11800  -3.41700  1.000 38.90896  ?  811  THR   B N   1 
ATOM   20410 C  CA  . THR   B 1 813  ? 73.03300   77.64700  -4.74900  1.000 31.66129  ?  811  THR   B CA  1 
ATOM   20411 C  C   . THR   B 1 813  ? 72.23800   78.92500  -4.96300  1.000 30.44815  ?  811  THR   B C   1 
ATOM   20412 O  O   . THR   B 1 813  ? 71.11300   79.05700  -4.47400  1.000 39.85885  ?  811  THR   B O   1 
ATOM   20413 C  CB  . THR   B 1 813  ? 72.67400   76.64500  -5.85100  1.000 36.73647  ?  811  THR   B CB  1 
ATOM   20414 O  OG1 . THR   B 1 813  ? 71.29500   76.27000  -5.73000  1.000 49.60648  ?  811  THR   B OG1 1 
ATOM   20415 C  CG2 . THR   B 1 813  ? 73.54300   75.41100  -5.75400  1.000 38.14470  ?  811  THR   B CG2 1 
ATOM   20416 N  N   . ILE   B 1 814  ? 72.83700   79.86600  -5.69100  1.000 36.99191  ?  812  ILE   B N   1 
ATOM   20417 C  CA  . ILE   B 1 814  ? 72.19000   81.12100  -6.06300  1.000 37.77721  ?  812  ILE   B CA  1 
ATOM   20418 C  C   . ILE   B 1 814  ? 72.49600   81.37700  -7.53100  1.000 37.70712  ?  812  ILE   B C   1 
ATOM   20419 O  O   . ILE   B 1 814  ? 73.66800   81.43600  -7.91900  1.000 61.51759  ?  812  ILE   B O   1 
ATOM   20420 C  CB  . ILE   B 1 814  ? 72.66500   82.31100  -5.21000  1.000 39.75502  ?  812  ILE   B CB  1 
ATOM   20421 C  CG1 . ILE   B 1 814  ? 73.02200   81.86200  -3.79200  1.000 51.47386  ?  812  ILE   B CG1 1 
ATOM   20422 C  CG2 . ILE   B 1 814  ? 71.59300   83.38800  -5.15900  1.000 39.36785  ?  812  ILE   B CG2 1 
ATOM   20423 C  CD1 . ILE   B 1 814  ? 73.50300   82.98200  -2.90700  1.000 59.28894  ?  812  ILE   B CD1 1 
ATOM   20424 N  N   . ASN   B 1 815  ? 71.45500   81.53500  -8.34600  1.000 37.57501  ?  813  ASN   B N   1 
ATOM   20425 C  CA  . ASN   B 1 815  ? 71.62100   81.77000  -9.78000  1.000 39.10228  ?  813  ASN   B CA  1 
ATOM   20426 C  C   . ASN   B 1 815  ? 71.67200   83.27500  -10.01700 1.000 37.67179  ?  813  ASN   B C   1 
ATOM   20427 O  O   . ASN   B 1 815  ? 70.63700   83.94100  -10.08700 1.000 50.65739  ?  813  ASN   B O   1 
ATOM   20428 C  CB  . ASN   B 1 815  ? 70.49200   81.12300  -10.57500 1.000 31.71636  ?  813  ASN   B CB  1 
ATOM   20429 C  CG  . ASN   B 1 815  ? 70.19800   79.70400  -10.12900 1.000 41.03712  ?  813  ASN   B CG  1 
ATOM   20430 O  OD1 . ASN   B 1 815  ? 71.02300   78.80400  -10.29000 1.000 45.97339  ?  813  ASN   B OD1 1 
ATOM   20431 N  ND2 . ASN   B 1 815  ? 69.01000   79.49600  -9.57500  1.000 60.74307  ?  813  ASN   B ND2 1 
ATOM   20432 N  N   . PHE   B 1 816  ? 72.88100   83.81300  -10.13700 1.000 40.47077  ?  814  PHE   B N   1 
ATOM   20433 C  CA  . PHE   B 1 816  ? 73.06100   85.21800  -10.45700 1.000 47.96864  ?  814  PHE   B CA  1 
ATOM   20434 C  C   . PHE   B 1 816  ? 72.91500   85.44800  -11.95600 1.000 55.59119  ?  814  PHE   B C   1 
ATOM   20435 O  O   . PHE   B 1 816  ? 73.11100   84.53100  -12.75800 1.000 65.45402  ?  814  PHE   B O   1 
ATOM   20436 C  CB  . PHE   B 1 816  ? 74.43800   85.69400  -10.00000 1.000 52.60131  ?  814  PHE   B CB  1 
ATOM   20437 C  CG  . PHE   B 1 816  ? 74.54500   85.93300  -8.52200  1.000 58.09301  ?  814  PHE   B CG  1 
ATOM   20438 C  CD1 . PHE   B 1 816  ? 74.03500   87.09000  -7.95500  1.000 44.69241  ?  814  PHE   B CD1 1 
ATOM   20439 C  CD2 . PHE   B 1 816  ? 75.17300   85.01100  -7.70100  1.000 46.33605  ?  814  PHE   B CD2 1 
ATOM   20440 C  CE1 . PHE   B 1 816  ? 74.13700   87.31600  -6.59700  1.000 36.24732  ?  814  PHE   B CE1 1 
ATOM   20441 C  CE2 . PHE   B 1 816  ? 75.27900   85.23200  -6.34100  1.000 53.31688  ?  814  PHE   B CE2 1 
ATOM   20442 C  CZ  . PHE   B 1 816  ? 74.76000   86.38600  -5.78800  1.000 56.97960  ?  814  PHE   B CZ  1 
ATOM   20443 N  N   . PRO   B 1 817  ? 72.56600   86.66400  -12.36500 1.000 53.85330  ?  815  PRO   B N   1 
ATOM   20444 C  CA  . PRO   B 1 817  ? 72.63900   87.00400  -13.78800 1.000 43.12542  ?  815  PRO   B CA  1 
ATOM   20445 C  C   . PRO   B 1 817  ? 74.08600   87.04200  -14.25000 1.000 58.33519  ?  815  PRO   B C   1 
ATOM   20446 O  O   . PRO   B 1 817  ? 75.01900   87.16800  -13.45500 1.000 73.30987  ?  815  PRO   B O   1 
ATOM   20447 C  CB  . PRO   B 1 817  ? 71.99300   88.39200  -13.85800 1.000 40.99087  ?  815  PRO   B CB  1 
ATOM   20448 C  CG  . PRO   B 1 817  ? 72.19400   88.96100  -12.48900 1.000 39.43064  ?  815  PRO   B CG  1 
ATOM   20449 C  CD  . PRO   B 1 817  ? 72.07500   87.79200  -11.55300 1.000 58.98593  ?  815  PRO   B CD  1 
ATOM   20450 N  N   . LEU   B 1 818  ? 74.26800   86.92800  -15.56600 1.000 58.07522  ?  816  LEU   B N   1 
ATOM   20451 C  CA  . LEU   B 1 818  ? 75.61500   86.98800  -16.12600 1.000 50.34808  ?  816  LEU   B CA  1 
ATOM   20452 C  C   . LEU   B 1 818  ? 76.24900   88.36700  -15.99400 1.000 54.83102  ?  816  LEU   B C   1 
ATOM   20453 O  O   . LEU   B 1 818  ? 77.42500   88.52200  -16.34300 1.000 58.88383  ?  816  LEU   B O   1 
ATOM   20454 C  CB  . LEU   B 1 818  ? 75.59400   86.57100  -17.59800 1.000 36.35137  ?  816  LEU   B CB  1 
ATOM   20455 C  CG  . LEU   B 1 818  ? 75.21400   85.12100  -17.90600 1.000 46.14060  ?  816  LEU   B CG  1 
ATOM   20456 C  CD1 . LEU   B 1 818  ? 75.22700   84.87300  -19.40400 1.000 42.25407  ?  816  LEU   B CD1 1 
ATOM   20457 C  CD2 . LEU   B 1 818  ? 76.14900   84.15600  -17.19900 1.000 57.71596  ?  816  LEU   B CD2 1 
ATOM   20458 N  N   . THR   B 1 819  ? 75.51200   89.35800  -15.49600 1.000 60.79089  ?  817  THR   B N   1 
ATOM   20459 C  CA  . THR   B 1 819  ? 75.98800   90.73100  -15.40600 1.000 47.90400  ?  817  THR   B CA  1 
ATOM   20460 C  C   . THR   B 1 819  ? 76.75500   91.01800  -14.12200 1.000 55.23363  ?  817  THR   B C   1 
ATOM   20461 O  O   . THR   B 1 819  ? 77.12900   92.17200  -13.88900 1.000 60.21688  ?  817  THR   B O   1 
ATOM   20462 C  CB  . THR   B 1 819  ? 74.81000   91.70600  -15.51700 1.000 56.41461  ?  817  THR   B CB  1 
ATOM   20463 O  OG1 . THR   B 1 819  ? 74.16000   91.82100  -14.24600 1.000 61.79302  ?  817  THR   B OG1 1 
ATOM   20464 C  CG2 . THR   B 1 819  ? 73.80300   91.20800  -16.54400 1.000 47.57908  ?  817  THR   B CG2 1 
ATOM   20465 N  N   . VAL   B 1 820  ? 76.99200   90.01200  -13.28200 1.000 57.07555  ?  818  VAL   B N   1 
ATOM   20466 C  CA  . VAL   B 1 820  ? 77.75900   90.19200  -12.05500 1.000 55.40521  ?  818  VAL   B CA  1 
ATOM   20467 C  C   . VAL   B 1 820  ? 79.16500   89.65900  -12.27600 1.000 56.97854  ?  818  VAL   B C   1 
ATOM   20468 O  O   . VAL   B 1 820  ? 79.38200   88.68300  -13.00400 1.000 58.01551  ?  818  VAL   B O   1 
ATOM   20469 C  CB  . VAL   B 1 820  ? 77.09000   89.50400  -10.84400 1.000 42.47889  ?  818  VAL   B CB  1 
ATOM   20470 C  CG1 . VAL   B 1 820  ? 75.72600   90.11700  -10.56800 1.000 37.10266  ?  818  VAL   B CG1 1 
ATOM   20471 C  CG2 . VAL   B 1 820  ? 76.97900   88.00700  -11.07300 1.000 65.69042  ?  818  VAL   B CG2 1 
ATOM   20472 N  N   . ASP   B 1 821  ? 80.13400   90.31600  -11.64500 1.000 55.57428  ?  819  ASP   B N   1 
ATOM   20473 C  CA  . ASP   B 1 821  ? 81.53000   89.91900  -11.76700 1.000 63.33657  ?  819  ASP   B CA  1 
ATOM   20474 C  C   . ASP   B 1 821  ? 81.79900   88.74000  -10.84000 1.000 65.50627  ?  819  ASP   B C   1 
ATOM   20475 O  O   . ASP   B 1 821  ? 81.57000   88.83200  -9.62900  1.000 66.74472  ?  819  ASP   B O   1 
ATOM   20476 C  CB  . ASP   B 1 821  ? 82.44600   91.09400  -11.43400 1.000 60.68057  ?  819  ASP   B CB  1 
ATOM   20477 C  CG  . ASP   B 1 821  ? 83.88600   90.83900  -11.82700 1.000 73.70794  ?  819  ASP   B CG  1 
ATOM   20478 O  OD1 . ASP   B 1 821  ? 84.16000   89.79000  -12.44700 1.000 90.35813  ?  819  ASP   B OD1 1 
ATOM   20479 O  OD2 . ASP   B 1 821  ? 84.74400   91.69100  -11.51600 1.000 96.01852  -1 819  ASP   B OD2 1 
ATOM   20480 N  N   . THR   B 1 822  ? 82.27600   87.63200  -11.41200 1.000 49.24456  ?  820  THR   B N   1 
ATOM   20481 C  CA  . THR   B 1 822  ? 82.56400   86.44900  -10.60800 1.000 56.77329  ?  820  THR   B CA  1 
ATOM   20482 C  C   . THR   B 1 822  ? 83.60200   86.74300  -9.53300  1.000 61.17220  ?  820  THR   B C   1 
ATOM   20483 O  O   . THR   B 1 822  ? 83.52500   86.19600  -8.42600  1.000 58.57440  ?  820  THR   B O   1 
ATOM   20484 C  CB  . THR   B 1 822  ? 83.03500   85.30800  -11.51000 1.000 55.61921  ?  820  THR   B CB  1 
ATOM   20485 O  OG1 . THR   B 1 822  ? 82.05500   85.06800  -12.52800 1.000 51.55498  ?  820  THR   B OG1 1 
ATOM   20486 C  CG2 . THR   B 1 822  ? 83.24000   84.03400  -10.70400 1.000 58.29629  ?  820  THR   B CG2 1 
ATOM   20487 N  N   . GLU   B 1 823  ? 84.56900   87.61400  -9.83000  1.000 62.20021  ?  821  GLU   B N   1 
ATOM   20488 C  CA  . GLU   B 1 823  ? 85.57900   87.96000  -8.83700  1.000 66.76043  ?  821  GLU   B CA  1 
ATOM   20489 C  C   . GLU   B 1 823  ? 85.00000   88.82000  -7.72200  1.000 62.70924  ?  821  GLU   B C   1 
ATOM   20490 O  O   . GLU   B 1 823  ? 85.44000   88.71600  -6.57200  1.000 53.99264  ?  821  GLU   B O   1 
ATOM   20491 C  CB  . GLU   B 1 823  ? 86.75000   88.67100  -9.51100  1.000 59.59187  ?  821  GLU   B CB  1 
ATOM   20492 C  CG  . GLU   B 1 823  ? 87.31100   87.90600  -10.69400 1.000 72.29271  ?  821  GLU   B CG  1 
ATOM   20493 C  CD  . GLU   B 1 823  ? 87.61000   86.45800  -10.35500 1.000 84.39048  ?  821  GLU   B CD  1 
ATOM   20494 O  OE1 . GLU   B 1 823  ? 88.44900   86.21600  -9.46100  1.000 90.85844  ?  821  GLU   B OE1 1 
ATOM   20495 O  OE2 . GLU   B 1 823  ? 86.99600   85.56100  -10.97200 1.000 63.55435  -1 821  GLU   B OE2 1 
ATOM   20496 N  N   . GLN   B 1 824  ? 84.01500   89.66700  -8.03800  1.000 58.71676  ?  822  GLN   B N   1 
ATOM   20497 C  CA  . GLN   B 1 824  ? 83.37800   90.47000  -7.00000  1.000 51.69542  ?  822  GLN   B CA  1 
ATOM   20498 C  C   . GLN   B 1 824  ? 82.63300   89.59400  -6.00300  1.000 63.62242  ?  822  GLN   B C   1 
ATOM   20499 O  O   . GLN   B 1 824  ? 82.46300   89.97900  -4.84000  1.000 64.17790  ?  822  GLN   B O   1 
ATOM   20500 C  CB  . GLN   B 1 824  ? 82.43300   91.49300  -7.63000  1.000 42.47901  ?  822  GLN   B CB  1 
ATOM   20501 C  CG  . GLN   B 1 824  ? 81.93200   92.54700  -6.65700  1.000 61.24454  ?  822  GLN   B CG  1 
ATOM   20502 C  CD  . GLN   B 1 824  ? 80.98600   93.53900  -7.30300  1.000 73.45048  ?  822  GLN   B CD  1 
ATOM   20503 O  OE1 . GLN   B 1 824  ? 79.76800   93.43800  -7.15500  1.000 66.35629  ?  822  GLN   B OE1 1 
ATOM   20504 N  NE2 . GLN   B 1 824  ? 81.54300   94.50800  -8.02100  1.000 53.79346  ?  822  GLN   B NE2 1 
ATOM   20505 N  N   . ILE   B 1 825  ? 82.18500   88.41300  -6.43600  1.000 57.80853  ?  823  ILE   B N   1 
ATOM   20506 C  CA  . ILE   B 1 825  ? 81.61300   87.45300  -5.49900  1.000 51.85570  ?  823  ILE   B CA  1 
ATOM   20507 C  C   . ILE   B 1 825  ? 82.71100   86.82800  -4.64900  1.000 53.84678  ?  823  ILE   B C   1 
ATOM   20508 O  O   . ILE   B 1 825  ? 82.52100   86.57200  -3.45400  1.000 63.12550  ?  823  ILE   B O   1 
ATOM   20509 C  CB  . ILE   B 1 825  ? 80.80500   86.38400  -6.25600  1.000 48.44859  ?  823  ILE   B CB  1 
ATOM   20510 C  CG1 . ILE   B 1 825  ? 79.91000   87.03900  -7.30900  1.000 60.15900  ?  823  ILE   B CG1 1 
ATOM   20511 C  CG2 . ILE   B 1 825  ? 79.96800   85.56500  -5.28600  1.000 46.00216  ?  823  ILE   B CG2 1 
ATOM   20512 C  CD1 . ILE   B 1 825  ? 79.13400   86.05000  -8.15000  1.000 48.77679  ?  823  ILE   B CD1 1 
ATOM   20513 N  N   . ARG   B 1 826  ? 83.87700   86.57700  -5.24800  1.000 50.00863  ?  824  ARG   B N   1 
ATOM   20514 C  CA  . ARG   B 1 826  ? 84.98600   85.98800  -4.50300  1.000 54.84390  ?  824  ARG   B CA  1 
ATOM   20515 C  C   . ARG   B 1 826  ? 85.50100   86.94300  -3.43400  1.000 59.97159  ?  824  ARG   B C   1 
ATOM   20516 O  O   . ARG   B 1 826  ? 85.73200   86.54100  -2.28800  1.000 63.11325  ?  824  ARG   B O   1 
ATOM   20517 C  CB  . ARG   B 1 826  ? 86.11200   85.59700  -5.46000  1.000 49.60015  ?  824  ARG   B CB  1 
ATOM   20518 C  CG  . ARG   B 1 826  ? 87.41100   85.19200  -4.77100  1.000 53.50313  ?  824  ARG   B CG  1 
ATOM   20519 C  CD  . ARG   B 1 826  ? 88.54200   85.07200  -5.78200  1.000 64.33278  ?  824  ARG   B CD  1 
ATOM   20520 N  NE  . ARG   B 1 826  ? 88.76600   86.32600  -6.49200  1.000 87.22470  ?  824  ARG   B NE  1 
ATOM   20521 C  CZ  . ARG   B 1 826  ? 89.92400   86.97300  -6.53300  1.000 91.59596  ?  824  ARG   B CZ  1 
ATOM   20522 N  NH1 . ARG   B 1 826  ? 91.00800   86.49100  -5.94700  1.000 102.70634 ?  824  ARG   B NH1 1 
ATOM   20523 N  NH2 . ARG   B 1 826  ? 89.99500   88.13400  -7.18000  1.000 63.58248  ?  824  ARG   B NH2 1 
ATOM   20524 N  N   . VAL   B 1 827  ? 85.69000   88.21500  -3.79100  1.000 51.84626  ?  825  VAL   B N   1 
ATOM   20525 C  CA  . VAL   B 1 827  ? 86.24100   89.16600  -2.83100  1.000 56.03980  ?  825  VAL   B CA  1 
ATOM   20526 C  C   . VAL   B 1 827  ? 85.25400   89.43300  -1.70100  1.000 57.57100  ?  825  VAL   B C   1 
ATOM   20527 O  O   . VAL   B 1 827  ? 85.66000   89.62700  -0.54900  1.000 61.74979  ?  825  VAL   B O   1 
ATOM   20528 C  CB  . VAL   B 1 827  ? 86.66500   90.46800  -3.54000  1.000 44.69643  ?  825  VAL   B CB  1 
ATOM   20529 C  CG1 . VAL   B 1 827  ? 87.66100   90.16600  -4.64800  1.000 57.30622  ?  825  VAL   B CG1 1 
ATOM   20530 C  CG2 . VAL   B 1 827  ? 85.45900   91.21400  -4.09400  1.000 59.25581  ?  825  VAL   B CG2 1 
ATOM   20531 N  N   . ALA   B 1 828  ? 83.95000   89.43200  -1.99600  1.000 57.06457  ?  826  ALA   B N   1 
ATOM   20532 C  CA  . ALA   B 1 828  ? 82.96300   89.65200  -0.94600  1.000 55.10739  ?  826  ALA   B CA  1 
ATOM   20533 C  C   . ALA   B 1 828  ? 82.86000   88.45000  -0.01900  1.000 53.86982  ?  826  ALA   B C   1 
ATOM   20534 O  O   . ALA   B 1 828  ? 82.58600   88.61300  1.17500   1.000 51.27674  ?  826  ALA   B O   1 
ATOM   20535 C  CB  . ALA   B 1 828  ? 81.60100   89.97300  -1.56100  1.000 52.82369  ?  826  ALA   B CB  1 
ATOM   20536 N  N   . LEU   B 1 829  ? 83.07500   87.24200  -0.54500  1.000 55.66164  ?  827  LEU   B N   1 
ATOM   20537 C  CA  . LEU   B 1 829  ? 83.11200   86.06100  0.31000   1.000 54.96328  ?  827  LEU   B CA  1 
ATOM   20538 C  C   . LEU   B 1 829  ? 84.38600   86.02600  1.14400   1.000 61.06351  ?  827  LEU   B C   1 
ATOM   20539 O  O   . LEU   B 1 829  ? 84.35400   85.64600  2.32000   1.000 58.28137  ?  827  LEU   B O   1 
ATOM   20540 C  CB  . LEU   B 1 829  ? 82.98700   84.79400  -0.53500  1.000 47.01118  ?  827  LEU   B CB  1 
ATOM   20541 C  CG  . LEU   B 1 829  ? 81.61100   84.50500  -1.13300  1.000 45.31560  ?  827  LEU   B CG  1 
ATOM   20542 C  CD1 . LEU   B 1 829  ? 81.66100   83.25600  -1.99900  1.000 29.76600  ?  827  LEU   B CD1 1 
ATOM   20543 C  CD2 . LEU   B 1 829  ? 80.56900   84.36100  -0.03300  1.000 14.80188  ?  827  LEU   B CD2 1 
ATOM   20544 N  N   . GLU   B 1 830  ? 85.51700   86.41900  0.55300   1.000 56.96931  ?  828  GLU   B N   1 
ATOM   20545 C  CA  . GLU   B 1 830  ? 86.76700   86.45900  1.30600   1.000 56.57079  ?  828  GLU   B CA  1 
ATOM   20546 C  C   . GLU   B 1 830  ? 86.70400   87.49100  2.42500   1.000 58.93975  ?  828  GLU   B C   1 
ATOM   20547 O  O   . GLU   B 1 830  ? 87.27800   87.28300  3.50100   1.000 55.03887  ?  828  GLU   B O   1 
ATOM   20548 C  CB  . GLU   B 1 830  ? 87.93800   86.74300  0.36500   1.000 33.77947  ?  828  GLU   B CB  1 
ATOM   20549 C  CG  . GLU   B 1 830  ? 88.34100   85.54500  -0.48100  1.000 51.65839  ?  828  GLU   B CG  1 
ATOM   20550 C  CD  . GLU   B 1 830  ? 89.31700   85.90300  -1.58300  1.000 56.23285  ?  828  GLU   B CD  1 
ATOM   20551 O  OE1 . GLU   B 1 830  ? 89.45100   87.10600  -1.89400  1.000 54.67544  ?  828  GLU   B OE1 1 
ATOM   20552 O  OE2 . GLU   B 1 830  ? 89.95000   84.98100  -2.14100  1.000 54.25816  -1 828  GLU   B OE2 1 
ATOM   20553 N  N   . GLN   B 1 831  ? 86.01000   88.60900  2.19300   1.000 56.03275  ?  829  GLN   B N   1 
ATOM   20554 C  CA  . GLN   B 1 831  ? 85.76400   89.56100  3.27200   1.000 54.81669  ?  829  GLN   B CA  1 
ATOM   20555 C  C   . GLN   B 1 831  ? 84.96800   88.91600  4.39800   1.000 52.38749  ?  829  GLN   B C   1 
ATOM   20556 O  O   . GLN   B 1 831  ? 85.22400   89.17800  5.57900   1.000 69.04105  ?  829  GLN   B O   1 
ATOM   20557 C  CB  . GLN   B 1 831  ? 85.02200   90.78800  2.73900   1.000 62.58441  ?  829  GLN   B CB  1 
ATOM   20558 C  CG  . GLN   B 1 831  ? 85.90700   91.98300  2.42800   1.000 86.31299  ?  829  GLN   B CG  1 
ATOM   20559 C  CD  . GLN   B 1 831  ? 85.10600   93.19500  1.98800   1.000 87.40339  ?  829  GLN   B CD  1 
ATOM   20560 O  OE1 . GLN   B 1 831  ? 84.72600   93.31200  0.82300   1.000 67.02929  ?  829  GLN   B OE1 1 
ATOM   20561 N  NE2 . GLN   B 1 831  ? 84.84200   94.10300  2.92200   1.000 79.51916  ?  829  GLN   B NE2 1 
ATOM   20562 N  N   . LEU   B 1 832  ? 83.99400   88.07100  4.05100   1.000 56.61438  ?  830  LEU   B N   1 
ATOM   20563 C  CA  . LEU   B 1 832  ? 83.16800   87.43800  5.07200   1.000 48.26750  ?  830  LEU   B CA  1 
ATOM   20564 C  C   . LEU   B 1 832  ? 83.95400   86.41900  5.88500   1.000 60.54764  ?  830  LEU   B C   1 
ATOM   20565 O  O   . LEU   B 1 832  ? 83.64100   86.19600  7.06000   1.000 59.90798  ?  830  LEU   B O   1 
ATOM   20566 C  CB  . LEU   B 1 832  ? 81.94300   86.79000  4.42800   1.000 45.45630  ?  830  LEU   B CB  1 
ATOM   20567 C  CG  . LEU   B 1 832  ? 80.86600   87.78900  4.00500   1.000 54.99580  ?  830  LEU   B CG  1 
ATOM   20568 C  CD1 . LEU   B 1 832  ? 79.66100   87.09000  3.39900   1.000 54.17529  ?  830  LEU   B CD1 1 
ATOM   20569 C  CD2 . LEU   B 1 832  ? 80.45300   88.62700  5.19700   1.000 56.88449  ?  830  LEU   B CD2 1 
ATOM   20570 N  N   . VAL   B 1 833  ? 84.97000   85.79300  5.28600   1.000 51.53127  ?  831  VAL   B N   1 
ATOM   20571 C  CA  . VAL   B 1 833  ? 85.84900   84.91400  6.05400   1.000 58.22689  ?  831  VAL   B CA  1 
ATOM   20572 C  C   . VAL   B 1 833  ? 86.55500   85.70600  7.14600   1.000 64.59044  ?  831  VAL   B C   1 
ATOM   20573 O  O   . VAL   B 1 833  ? 86.64400   85.26400  8.29800   1.000 65.67550  ?  831  VAL   B O   1 
ATOM   20574 C  CB  . VAL   B 1 833  ? 86.85600   84.21100  5.12400   1.000 56.40309  ?  831  VAL   B CB  1 
ATOM   20575 C  CG1 . VAL   B 1 833  ? 87.71800   83.23900  5.91500   1.000 45.11421  ?  831  VAL   B CG1 1 
ATOM   20576 C  CG2 . VAL   B 1 833  ? 86.13200   83.49400  3.99600   1.000 51.67463  ?  831  VAL   B CG2 1 
ATOM   20577 N  N   . LEU   B 1 834  ? 87.05400   86.89600  6.80400   1.000 63.28938  ?  832  LEU   B N   1 
ATOM   20578 C  CA  . LEU   B 1 834  ? 87.72200   87.73700  7.79000   1.000 56.17691  ?  832  LEU   B CA  1 
ATOM   20579 C  C   . LEU   B 1 834  ? 86.73800   88.27400  8.82000   1.000 48.75524  ?  832  LEU   B C   1 
ATOM   20580 O  O   . LEU   B 1 834  ? 87.06100   88.36300  10.01000  1.000 71.00345  ?  832  LEU   B O   1 
ATOM   20581 C  CB  . LEU   B 1 834  ? 88.43600   88.89100  7.08800   1.000 55.33138  ?  832  LEU   B CB  1 
ATOM   20582 C  CG  . LEU   B 1 834  ? 89.25800   88.51700  5.85300   1.000 78.50082  ?  832  LEU   B CG  1 
ATOM   20583 C  CD1 . LEU   B 1 834  ? 89.59400   89.75600  5.03500   1.000 50.90007  ?  832  LEU   B CD1 1 
ATOM   20584 C  CD2 . LEU   B 1 834  ? 90.52300   87.77400  6.25600   1.000 85.36957  ?  832  LEU   B CD2 1 
ATOM   20585 N  N   . ARG   B 1 835  ? 85.53000   88.63300  8.38200   1.000 37.88222  ?  833  ARG   B N   1 
ATOM   20586 C  CA  . ARG   B 1 835  ? 84.58600   89.28700  9.28100   1.000 45.47537  ?  833  ARG   B CA  1 
ATOM   20587 C  C   . ARG   B 1 835  ? 84.09700   88.33600  10.37000  1.000 58.46664  ?  833  ARG   B C   1 
ATOM   20588 O  O   . ARG   B 1 835  ? 83.96500   88.73400  11.53300  1.000 44.65336  ?  833  ARG   B O   1 
ATOM   20589 C  CB  . ARG   B 1 835  ? 83.41100   89.85100  8.48200   1.000 43.19564  ?  833  ARG   B CB  1 
ATOM   20590 C  CG  . ARG   B 1 835  ? 82.45500   90.66900  9.32200   1.000 52.26972  ?  833  ARG   B CG  1 
ATOM   20591 C  CD  . ARG   B 1 835  ? 81.60200   91.59800  8.48400   1.000 39.77953  ?  833  ARG   B CD  1 
ATOM   20592 N  NE  . ARG   B 1 835  ? 80.96200   92.60900  9.31600   1.000 62.14977  ?  833  ARG   B NE  1 
ATOM   20593 C  CZ  . ARG   B 1 835  ? 79.86800   92.40200  10.03500  1.000 55.74254  ?  833  ARG   B CZ  1 
ATOM   20594 N  NH1 . ARG   B 1 835  ? 79.26600   91.22500  10.05500  1.000 74.93925  ?  833  ARG   B NH1 1 
ATOM   20595 N  NH2 . ARG   B 1 835  ? 79.36500   93.40200  10.75300  1.000 51.18131  ?  833  ARG   B NH2 1 
ATOM   20596 N  N   . HIS   B 1 836  ? 83.84200   87.07800  10.02200  1.000 56.45004  ?  834  HIS   B N   1 
ATOM   20597 C  CA  . HIS   B 1 836  ? 83.26800   86.10600  10.94500  1.000 58.22293  ?  834  HIS   B CA  1 
ATOM   20598 C  C   . HIS   B 1 836  ? 84.34400   85.12300  11.39100  1.000 67.10140  ?  834  HIS   B C   1 
ATOM   20599 O  O   . HIS   B 1 836  ? 84.96100   84.45000  10.55700  1.000 59.68378  ?  834  HIS   B O   1 
ATOM   20600 C  CB  . HIS   B 1 836  ? 82.09200   85.38000  10.29200  1.000 57.22504  ?  834  HIS   B CB  1 
ATOM   20601 C  CG  . HIS   B 1 836  ? 81.00700   86.30100  9.82600   1.000 54.65284  ?  834  HIS   B CG  1 
ATOM   20602 N  ND1 . HIS   B 1 836  ? 80.18400   86.98000  10.69800  1.000 46.46853  ?  834  HIS   B ND1 1 
ATOM   20603 C  CD2 . HIS   B 1 836  ? 80.61800   86.66500  8.58100   1.000 62.41513  ?  834  HIS   B CD2 1 
ATOM   20604 C  CE1 . HIS   B 1 836  ? 79.33000   87.71800  10.01100  1.000 62.50298  ?  834  HIS   B CE1 1 
ATOM   20605 N  NE2 . HIS   B 1 836  ? 79.57300   87.54500  8.72400   1.000 60.92532  ?  834  HIS   B NE2 1 
ATOM   20606 N  N   . GLU   B 1 837  ? 84.56300   85.04400  12.70900  1.000 62.24757  ?  835  GLU   B N   1 
ATOM   20607 C  CA  . GLU   B 1 837  ? 85.57600   84.14100  13.25100  1.000 59.22006  ?  835  GLU   B CA  1 
ATOM   20608 C  C   . GLU   B 1 837  ? 85.27300   82.68300  12.93200  1.000 65.09308  ?  835  GLU   B C   1 
ATOM   20609 O  O   . GLU   B 1 837  ? 86.19900   81.89100  12.72300  1.000 54.62157  ?  835  GLU   B O   1 
ATOM   20610 C  CB  . GLU   B 1 837  ? 85.68900   84.32100  14.76500  1.000 61.31057  ?  835  GLU   B CB  1 
ATOM   20611 C  CG  . GLU   B 1 837  ? 86.68300   85.37500  15.20300  1.000 80.59773  ?  835  GLU   B CG  1 
ATOM   20612 C  CD  . GLU   B 1 837  ? 87.02200   85.26500  16.67400  1.000 69.48916  ?  835  GLU   B CD  1 
ATOM   20613 O  OE1 . GLU   B 1 837  ? 86.38300   84.45000  17.37400  1.000 62.82210  ?  835  GLU   B OE1 1 
ATOM   20614 O  OE2 . GLU   B 1 837  ? 87.93000   85.99000  17.12900  1.000 75.70161  -1 835  GLU   B OE2 1 
ATOM   20615 N  N   . GLY   B 1 838  ? 83.99000   82.31000  12.90100  1.000 60.79569  ?  836  GLY   B N   1 
ATOM   20616 C  CA  . GLY   B 1 838  ? 83.62700   80.93500  12.60200  1.000 39.30013  ?  836  GLY   B CA  1 
ATOM   20617 C  C   . GLY   B 1 838  ? 84.17700   80.43500  11.28100  1.000 56.57369  ?  836  GLY   B C   1 
ATOM   20618 O  O   . GLY   B 1 838  ? 84.54800   79.26600  11.16500  1.000 60.16905  ?  836  GLY   B O   1 
ATOM   20619 N  N   . LEU   B 1 839  ? 84.24000   81.30700  10.27100  1.000 55.48309  ?  837  LEU   B N   1 
ATOM   20620 C  CA  . LEU   B 1 839  ? 84.83000   80.94300  8.98800   1.000 56.88524  ?  837  LEU   B CA  1 
ATOM   20621 C  C   . LEU   B 1 839  ? 86.34400   80.78800  9.05800   1.000 58.28207  ?  837  LEU   B C   1 
ATOM   20622 O  O   . LEU   B 1 839  ? 86.94000   80.27600  8.10600   1.000 59.27678  ?  837  LEU   B O   1 
ATOM   20623 C  CB  . LEU   B 1 839  ? 84.45100   81.98300  7.93300   1.000 55.10670  ?  837  LEU   B CB  1 
ATOM   20624 C  CG  . LEU   B 1 839  ? 83.00300   81.87500  7.44900   1.000 39.83969  ?  837  LEU   B CG  1 
ATOM   20625 C  CD1 . LEU   B 1 839  ? 82.48800   83.20700  6.93200   1.000 36.75313  ?  837  LEU   B CD1 1 
ATOM   20626 C  CD2 . LEU   B 1 839  ? 82.89500   80.80900  6.37200   1.000 28.77041  ?  837  LEU   B CD2 1 
ATOM   20627 N  N   . ARG   B 1 840  ? 86.97500   81.21900  10.15000  1.000 68.26913  ?  838  ARG   B N   1 
ATOM   20628 C  CA  . ARG   B 1 840  ? 88.39200   80.97100  10.38400  1.000 68.43762  ?  838  ARG   B CA  1 
ATOM   20629 C  C   . ARG   B 1 840  ? 88.62100   80.08500  11.60000  1.000 70.49248  ?  838  ARG   B C   1 
ATOM   20630 O  O   . ARG   B 1 840  ? 89.76600   79.93500  12.04100  1.000 72.44102  ?  838  ARG   B O   1 
ATOM   20631 C  CB  . ARG   B 1 840  ? 89.14900   82.29200  10.55200  1.000 65.58537  ?  838  ARG   B CB  1 
ATOM   20632 C  CG  . ARG   B 1 840  ? 89.08900   83.20300  9.34100   1.000 70.92057  ?  838  ARG   B CG  1 
ATOM   20633 C  CD  . ARG   B 1 840  ? 89.54500   84.60400  9.70200   1.000 70.28258  ?  838  ARG   B CD  1 
ATOM   20634 N  NE  . ARG   B 1 840  ? 88.99500   85.02300  10.98600  1.000 76.36558  ?  838  ARG   B NE  1 
ATOM   20635 C  CZ  . ARG   B 1 840  ? 88.96100   86.27700  11.41400  1.000 74.66279  ?  838  ARG   B CZ  1 
ATOM   20636 N  NH1 . ARG   B 1 840  ? 89.41700   87.27300  10.67200  1.000 79.88865  ?  838  ARG   B NH1 1 
ATOM   20637 N  NH2 . ARG   B 1 840  ? 88.45000   86.53900  12.61400  1.000 65.71766  ?  838  ARG   B NH2 1 
ATOM   20638 N  N   . SER   B 1 841  ? 87.56400   79.49600  12.15300  1.000 59.97964  ?  839  SER   B N   1 
ATOM   20639 C  CA  . SER   B 1 841  ? 87.67300   78.65300  13.33300  1.000 47.43841  ?  839  SER   B CA  1 
ATOM   20640 C  C   . SER   B 1 841  ? 88.00400   77.21900  12.94100  1.000 60.18103  ?  839  SER   B C   1 
ATOM   20641 O  O   . SER   B 1 841  ? 87.48700   76.69700  11.94900  1.000 66.57870  ?  839  SER   B O   1 
ATOM   20642 C  CB  . SER   B 1 841  ? 86.37200   78.68200  14.13700  1.000 55.44560  ?  839  SER   B CB  1 
ATOM   20643 O  OG  . SER   B 1 841  ? 86.05000   80.00100  14.54400  1.000 72.76650  ?  839  SER   B OG  1 
ATOM   20644 N  N   . THR   B 1 842  ? 88.87700   76.59100  13.72700  1.000 74.24076  ?  840  THR   B N   1 
ATOM   20645 C  CA  . THR   B 1 842  ? 89.21300   75.18300  13.58300  1.000 71.02456  ?  840  THR   B CA  1 
ATOM   20646 C  C   . THR   B 1 842  ? 88.91900   74.46000  14.89000  1.000 62.66689  ?  840  THR   B C   1 
ATOM   20647 O  O   . THR   B 1 842  ? 89.06800   75.02500  15.97800  1.000 71.62465  ?  840  THR   B O   1 
ATOM   20648 C  CB  . THR   B 1 842  ? 90.68900   74.98400  13.19800  1.000 69.23525  ?  840  THR   B CB  1 
ATOM   20649 O  OG1 . THR   B 1 842  ? 91.52800   75.31300  14.31200  1.000 88.46649  ?  840  THR   B OG1 1 
ATOM   20650 C  CG2 . THR   B 1 842  ? 91.05700   75.87000  12.01900  1.000 63.47971  ?  840  THR   B CG2 1 
ATOM   20651 N  N   . TYR   B 1 843  ? 88.50000   73.20300  14.77600  1.000 61.72713  ?  841  TYR   B N   1 
ATOM   20652 C  CA  . TYR   B 1 843  ? 88.07500   72.40600  15.92000  1.000 62.23168  ?  841  TYR   B CA  1 
ATOM   20653 C  C   . TYR   B 1 843  ? 89.02500   71.22900  16.08300  1.000 75.55606  ?  841  TYR   B C   1 
ATOM   20654 O  O   . TYR   B 1 843  ? 89.18700   70.42400  15.16100  1.000 78.05030  ?  841  TYR   B O   1 
ATOM   20655 C  CB  . TYR   B 1 843  ? 86.63200   71.92400  15.74600  1.000 52.65237  ?  841  TYR   B CB  1 
ATOM   20656 C  CG  . TYR   B 1 843  ? 85.61300   73.04500  15.73900  1.000 55.89186  ?  841  TYR   B CG  1 
ATOM   20657 C  CD1 . TYR   B 1 843  ? 85.44700   73.85300  14.62100  1.000 48.90981  ?  841  TYR   B CD1 1 
ATOM   20658 C  CD2 . TYR   B 1 843  ? 84.82300   73.30000  16.85300  1.000 58.51805  ?  841  TYR   B CD2 1 
ATOM   20659 C  CE1 . TYR   B 1 843  ? 84.52300   74.88100  14.61200  1.000 60.47379  ?  841  TYR   B CE1 1 
ATOM   20660 C  CE2 . TYR   B 1 843  ? 83.89400   74.32500  16.85300  1.000 51.16489  ?  841  TYR   B CE2 1 
ATOM   20661 C  CZ  . TYR   B 1 843  ? 83.75000   75.11200  15.73000  1.000 64.00934  ?  841  TYR   B CZ  1 
ATOM   20662 O  OH  . TYR   B 1 843  ? 82.82800   76.13300  15.72500  1.000 73.64621  ?  841  TYR   B OH  1 
ATOM   20663 N  N   . HIS   B 1 844  ? 89.65200   71.13600  17.25400  1.000 81.55718  ?  842  HIS   B N   1 
ATOM   20664 C  CA  . HIS   B 1 844  ? 90.56200   70.04100  17.56000  1.000 65.55494  ?  842  HIS   B CA  1 
ATOM   20665 C  C   . HIS   B 1 844  ? 90.13700   69.35000  18.84700  1.000 71.41726  ?  842  HIS   B C   1 
ATOM   20666 O  O   . HIS   B 1 844  ? 89.08100   69.65900  19.41100  1.000 64.04051  ?  842  HIS   B O   1 
ATOM   20667 C  CB  . HIS   B 1 844  ? 91.99900   70.54700  17.68600  1.000 60.43792  ?  842  HIS   B CB  1 
ATOM   20668 C  CG  . HIS   B 1 844  ? 92.45800   71.35500  16.51400  1.000 70.24480  ?  842  HIS   B CG  1 
ATOM   20669 N  ND1 . HIS   B 1 844  ? 93.18100   70.81300  15.47400  1.000 78.16603  ?  842  HIS   B ND1 1 
ATOM   20670 C  CD2 . HIS   B 1 844  ? 92.30300   72.66800  16.22100  1.000 74.63394  ?  842  HIS   B CD2 1 
ATOM   20671 C  CE1 . HIS   B 1 844  ? 93.45200   71.75700  14.59000  1.000 87.20296  ?  842  HIS   B CE1 1 
ATOM   20672 N  NE2 . HIS   B 1 844  ? 92.93000   72.89100  15.01800  1.000 91.04852  ?  842  HIS   B NE2 1 
ATOM   20673 N  N   . MET   B 1 845  ? 90.95700   68.41800  19.32300  1.000 77.12920  ?  843  MET   B N   1 
ATOM   20674 C  CA  . MET   B 1 845  ? 90.69900   67.72000  20.57300  1.000 79.38544  ?  843  MET   B CA  1 
ATOM   20675 C  C   . MET   B 1 845  ? 91.98200   67.66700  21.38500  1.000 84.25793  ?  843  MET   B C   1 
ATOM   20676 O  O   . MET   B 1 845  ? 93.03700   67.29300  20.86300  1.000 92.04325  ?  843  MET   B O   1 
ATOM   20677 C  CB  . MET   B 1 845  ? 90.16600   66.30700  20.32600  1.000 58.67302  ?  843  MET   B CB  1 
ATOM   20678 C  CG  . MET   B 1 845  ? 89.31500   65.78600  21.46700  1.000 78.99926  ?  843  MET   B CG  1 
ATOM   20679 S  SD  . MET   B 1 845  ? 88.37600   64.32200  21.01500  1.000 91.66332  ?  843  MET   B SD  1 
ATOM   20680 C  CE  . MET   B 1 845  ? 87.05900   64.37200  22.22900  1.000 67.13782  ?  843  MET   B CE  1 
ATOM   20681 N  N   . ARG   B 1 846  ? 91.88700   68.04600  22.65500  1.000 79.32085  ?  844  ARG   B N   1 
ATOM   20682 C  CA  . ARG   B 1 846  ? 93.01800   68.05200  23.57800  1.000 81.19200  ?  844  ARG   B CA  1 
ATOM   20683 C  C   . ARG   B 1 846  ? 92.75300   66.98300  24.63300  1.000 87.04078  ?  844  ARG   B C   1 
ATOM   20684 O  O   . ARG   B 1 846  ? 92.04800   67.22800  25.61600  1.000 80.44021  ?  844  ARG   B O   1 
ATOM   20685 C  CB  . ARG   B 1 846  ? 93.20400   69.43300  24.20000  1.000 71.08511  ?  844  ARG   B CB  1 
ATOM   20686 C  CG  . ARG   B 1 846  ? 94.36700   69.53700  25.17300  1.000 73.81492  ?  844  ARG   B CG  1 
ATOM   20687 C  CD  . ARG   B 1 846  ? 95.36300   70.60400  24.73500  1.000 80.83338  ?  844  ARG   B CD  1 
ATOM   20688 N  NE  . ARG   B 1 846  ? 96.21800   70.14800  23.64500  1.000 91.47160  ?  844  ARG   B NE  1 
ATOM   20689 C  CZ  . ARG   B 1 846  ? 97.12800   70.90000  23.04000  1.000 90.37469  ?  844  ARG   B CZ  1 
ATOM   20690 N  NH1 . ARG   B 1 846  ? 97.31400   72.16600  23.37600  1.000 95.44866  ?  844  ARG   B NH1 1 
ATOM   20691 N  NH2 . ARG   B 1 846  ? 97.87000   70.36800  22.07300  1.000 75.70246  ?  844  ARG   B NH2 1 
ATOM   20692 N  N   . GLY   B 1 847  ? 93.31600   65.79600  24.42000  1.000 78.38712  ?  845  GLY   B N   1 
ATOM   20693 C  CA  . GLY   B 1 847  ? 93.10100   64.68600  25.32500  1.000 78.92622  ?  845  GLY   B CA  1 
ATOM   20694 C  C   . GLY   B 1 847  ? 91.69100   64.13900  25.25200  1.000 75.37694  ?  845  GLY   B C   1 
ATOM   20695 O  O   . GLY   B 1 847  ? 91.37100   63.34200  24.36600  1.000 77.46551  ?  845  GLY   B O   1 
ATOM   20696 N  N   . ASP   B 1 848  ? 90.83500   64.56800  26.18100  1.000 74.57633  ?  846  ASP   B N   1 
ATOM   20697 C  CA  . ASP   B 1 848  ? 89.45000   64.11500  26.24100  1.000 80.35399  ?  846  ASP   B CA  1 
ATOM   20698 C  C   . ASP   B 1 848  ? 88.46300   65.27000  26.13400  1.000 75.29330  ?  846  ASP   B C   1 
ATOM   20699 O  O   . ASP   B 1 848  ? 87.31400   65.14000  26.56900  1.000 74.55249  ?  846  ASP   B O   1 
ATOM   20700 C  CB  . ASP   B 1 848  ? 89.20000   63.33000  27.53100  1.000 83.04591  ?  846  ASP   B CB  1 
ATOM   20701 C  CG  . ASP   B 1 848  ? 89.96400   62.02200  27.57800  1.000 89.50919  ?  846  ASP   B CG  1 
ATOM   20702 O  OD1 . ASP   B 1 848  ? 91.21000   62.05200  27.48400  1.000 92.01810  ?  846  ASP   B OD1 1 
ATOM   20703 O  OD2 . ASP   B 1 848  ? 89.31900   60.96200  27.71700  1.000 92.08275  -1 846  ASP   B OD2 1 
ATOM   20704 N  N   . GLU   B 1 849  ? 88.88000   66.39900  25.56500  1.000 75.54378  ?  847  GLU   B N   1 
ATOM   20705 C  CA  . GLU   B 1 849  ? 88.03600   67.58300  25.49000  1.000 74.46196  ?  847  GLU   B CA  1 
ATOM   20706 C  C   . GLU   B 1 849  ? 88.05500   68.14000  24.07600  1.000 88.18455  ?  847  GLU   B C   1 
ATOM   20707 O  O   . GLU   B 1 849  ? 89.12400   68.31000  23.48300  1.000 78.22412  ?  847  GLU   B O   1 
ATOM   20708 C  CB  . GLU   B 1 849  ? 88.49400   68.65200  26.48700  1.000 60.46071  ?  847  GLU   B CB  1 
ATOM   20709 C  CG  . GLU   B 1 849  ? 87.34500   69.39200  27.14500  1.000 71.25511  ?  847  GLU   B CG  1 
ATOM   20710 C  CD  . GLU   B 1 849  ? 86.35400   68.44500  27.79400  1.000 87.77648  ?  847  GLU   B CD  1 
ATOM   20711 O  OE1 . GLU   B 1 849  ? 86.78500   67.58600  28.59100  1.000 87.27875  ?  847  GLU   B OE1 1 
ATOM   20712 O  OE2 . GLU   B 1 849  ? 85.14500   68.55000  27.49500  1.000 89.88017  -1 847  GLU   B OE2 1 
ATOM   20713 N  N   . ILE   B 1 850  ? 86.86900   68.42700  23.54600  1.000 84.80800  ?  848  ILE   B N   1 
ATOM   20714 C  CA  . ILE   B 1 850  ? 86.73100   69.03700  22.22700  1.000 73.35853  ?  848  ILE   B CA  1 
ATOM   20715 C  C   . ILE   B 1 850  ? 87.03200   70.52600  22.34400  1.000 72.60661  ?  848  ILE   B C   1 
ATOM   20716 O  O   . ILE   B 1 850  ? 86.30300   71.26800  23.00900  1.000 73.07848  ?  848  ILE   B O   1 
ATOM   20717 C  CB  . ILE   B 1 850  ? 85.32900   68.79800  21.65700  1.000 59.58775  ?  848  ILE   B CB  1 
ATOM   20718 C  CG1 . ILE   B 1 850  ? 85.10900   67.30400  21.42300  1.000 61.79070  ?  848  ILE   B CG1 1 
ATOM   20719 C  CG2 . ILE   B 1 850  ? 85.13400   69.58500  20.37300  1.000 64.51328  ?  848  ILE   B CG2 1 
ATOM   20720 C  CD1 . ILE   B 1 850  ? 83.66100   66.90600  21.33500  1.000 57.59458  ?  848  ILE   B CD1 1 
ATOM   20721 N  N   . VAL   B 1 851  ? 88.10800   70.96800  21.69300  1.000 70.12932  ?  849  VAL   B N   1 
ATOM   20722 C  CA  . VAL   B 1 851  ? 88.56300   72.34800  21.81200  1.000 78.64192  ?  849  VAL   B CA  1 
ATOM   20723 C  C   . VAL   B 1 851  ? 88.32300   73.09700  20.50700  1.000 76.58448  ?  849  VAL   B C   1 
ATOM   20724 O  O   . VAL   B 1 851  ? 87.80600   72.53100  19.53800  1.000 89.88131  ?  849  VAL   B O   1 
ATOM   20725 C  CB  . VAL   B 1 851  ? 90.04900   72.40600  22.21500  1.000 76.35132  ?  849  VAL   B CB  1 
ATOM   20726 C  CG1 . VAL   B 1 851  ? 90.28000   71.61300  23.49000  1.000 70.21597  ?  849  VAL   B CG1 1 
ATOM   20727 C  CG2 . VAL   B 1 851  ? 90.92900   71.88600  21.08800  1.000 70.21989  ?  849  VAL   B CG2 1 
ATOM   20728 N  N   . LYS   B 1 852  ? 88.69700   74.37500  20.47700  1.000 77.56736  ?  850  LYS   B N   1 
ATOM   20729 C  CA  . LYS   B 1 852  ? 88.52200   75.21700  19.30400  1.000 73.14285  ?  850  LYS   B CA  1 
ATOM   20730 C  C   . LYS   B 1 852  ? 89.72000   76.14600  19.16700  1.000 72.31172  ?  850  LYS   B C   1 
ATOM   20731 O  O   . LYS   B 1 852  ? 90.28800   76.60100  20.16300  1.000 75.87701  ?  850  LYS   B O   1 
ATOM   20732 C  CB  . LYS   B 1 852  ? 87.22700   76.04400  19.38600  1.000 73.11323  ?  850  LYS   B CB  1 
ATOM   20733 C  CG  . LYS   B 1 852  ? 87.01100   76.98100  18.20500  1.000 68.65555  ?  850  LYS   B CG  1 
ATOM   20734 C  CD  . LYS   B 1 852  ? 85.95600   78.03600  18.49300  1.000 60.73795  ?  850  LYS   B CD  1 
ATOM   20735 C  CE  . LYS   B 1 852  ? 84.56900   77.43000  18.58300  1.000 65.95474  ?  850  LYS   B CE  1 
ATOM   20736 N  NZ  . LYS   B 1 852  ? 83.51700   78.47500  18.72400  1.000 56.65275  ?  850  LYS   B NZ  1 
ATOM   20737 N  N   . ARG   B 1 853  ? 90.10100   76.42000  17.92100  1.000 80.68836  ?  851  ARG   B N   1 
ATOM   20738 C  CA  . ARG   B 1 853  ? 91.14800   77.38200  17.61200  1.000 75.58148  ?  851  ARG   B CA  1 
ATOM   20739 C  C   . ARG   B 1 853  ? 90.64700   78.35600  16.55400  1.000 71.67351  ?  851  ARG   B C   1 
ATOM   20740 O  O   . ARG   B 1 853  ? 89.64200   78.11300  15.88200  1.000 74.88181  ?  851  ARG   B O   1 
ATOM   20741 C  CB  . ARG   B 1 853  ? 92.43200   76.69200  17.13000  1.000 71.00015  ?  851  ARG   B CB  1 
ATOM   20742 C  CG  . ARG   B 1 853  ? 93.13100   75.88200  18.20600  1.000 88.05458  ?  851  ARG   B CG  1 
ATOM   20743 C  CD  . ARG   B 1 853  ? 94.64200   75.89700  18.02600  1.000 99.88753  ?  851  ARG   B CD  1 
ATOM   20744 N  NE  . ARG   B 1 853  ? 95.12600   74.77500  17.23200  1.000 90.04116  ?  851  ARG   B NE  1 
ATOM   20745 C  CZ  . ARG   B 1 853  ? 95.41100   73.57900  17.72900  1.000 86.33814  ?  851  ARG   B CZ  1 
ATOM   20746 N  NH1 . ARG   B 1 853  ? 95.24100   73.30600  19.01200  1.000 66.65846  ?  851  ARG   B NH1 1 
ATOM   20747 N  NH2 . ARG   B 1 853  ? 95.87700   72.63400  16.91800  1.000 97.98037  ?  851  ARG   B NH2 1 
ATOM   20748 N  N   . ILE   B 1 854  ? 91.35700   79.47500  16.42400  1.000 61.45701  ?  852  ILE   B N   1 
ATOM   20749 C  CA  . ILE   B 1 854  ? 91.04400   80.50300  15.43500  1.000 61.36808  ?  852  ILE   B CA  1 
ATOM   20750 C  C   . ILE   B 1 854  ? 92.34500   80.95400  14.78800  1.000 47.67584  ?  852  ILE   B C   1 
ATOM   20751 O  O   . ILE   B 1 854  ? 93.33200   81.21500  15.48400  1.000 51.80254  ?  852  ILE   B O   1 
ATOM   20752 C  CB  . ILE   B 1 854  ? 90.30600   81.70700  16.05700  1.000 54.87224  ?  852  ILE   B CB  1 
ATOM   20753 C  CG1 . ILE   B 1 854  ? 88.96400   81.27600  16.65400  1.000 58.33741  ?  852  ILE   B CG1 1 
ATOM   20754 C  CG2 . ILE   B 1 854  ? 90.08900   82.80000  15.01800  1.000 63.60124  ?  852  ILE   B CG2 1 
ATOM   20755 C  CD1 . ILE   B 1 854  ? 88.90600   81.37400  18.16200  1.000 72.53369  ?  852  ILE   B CD1 1 
ATOM   20756 N  N   . VAL   B 1 855  ? 92.35100   81.04200  13.46100  1.000 47.55952  ?  853  VAL   B N   1 
ATOM   20757 C  CA  . VAL   B 1 855  ? 93.51800   81.50000  12.71200  1.000 56.31219  ?  853  VAL   B CA  1 
ATOM   20758 C  C   . VAL   B 1 855  ? 93.20000   82.87000  12.11800  1.000 74.96815  ?  853  VAL   B C   1 
ATOM   20759 O  O   . VAL   B 1 855  ? 92.09600   83.07600  11.59400  1.000 77.10251  ?  853  VAL   B O   1 
ATOM   20760 C  CB  . VAL   B 1 855  ? 93.92100   80.47700  11.63400  1.000 56.88857  ?  853  VAL   B CB  1 
ATOM   20761 C  CG1 . VAL   B 1 855  ? 92.73800   80.13900  10.73500  1.000 49.36134  ?  853  VAL   B CG1 1 
ATOM   20762 C  CG2 . VAL   B 1 855  ? 95.10300   80.98200  10.81600  1.000 64.27422  ?  853  VAL   B CG2 1 
ATOM   20763 N  N   . PRO   B 1 856  ? 94.11800   83.84100  12.19500  1.000 75.66494  ?  854  PRO   B N   1 
ATOM   20764 C  CA  . PRO   B 1 856  ? 93.80800   85.19200  11.69700  1.000 73.89317  ?  854  PRO   B CA  1 
ATOM   20765 C  C   . PRO   B 1 856  ? 93.63900   85.28500  10.18600  1.000 72.52168  ?  854  PRO   B C   1 
ATOM   20766 O  O   . PRO   B 1 856  ? 93.26000   86.35700  9.69700   1.000 63.04279  ?  854  PRO   B O   1 
ATOM   20767 C  CB  . PRO   B 1 856  ? 95.01100   86.02300  12.16500  1.000 80.20210  ?  854  PRO   B CB  1 
ATOM   20768 C  CG  . PRO   B 1 856  ? 95.60400   85.24100  13.29200  1.000 78.12228  ?  854  PRO   B CG  1 
ATOM   20769 C  CD  . PRO   B 1 856  ? 95.39300   83.80600  12.92800  1.000 59.68256  ?  854  PRO   B CD  1 
ATOM   20770 N  N   . ARG   B 1 857  ? 93.90600   84.22000  9.43400   1.000 72.53420  ?  855  ARG   B N   1 
ATOM   20771 C  CA  . ARG   B 1 857  ? 93.77500   84.27100  7.98500   1.000 78.31057  ?  855  ARG   B CA  1 
ATOM   20772 C  C   . ARG   B 1 857  ? 93.42800   82.88700  7.45800   1.000 86.40491  ?  855  ARG   B C   1 
ATOM   20773 O  O   . ARG   B 1 857  ? 93.87600   81.87100  7.99600   1.000 88.79460  ?  855  ARG   B O   1 
ATOM   20774 C  CB  . ARG   B 1 857  ? 95.05800   84.78700  7.32300   1.000 56.79207  ?  855  ARG   B CB  1 
ATOM   20775 N  N   . ALA   B 1 858  ? 92.62500   82.86000  6.39600   1.000 70.42730  ?  856  ALA   B N   1 
ATOM   20776 C  CA  . ALA   B 1 858  ? 92.22000   81.61900  5.75300   1.000 53.12226  ?  856  ALA   B CA  1 
ATOM   20777 C  C   . ALA   B 1 858  ? 92.14100   81.83800  4.25000   1.000 59.42332  ?  856  ALA   B C   1 
ATOM   20778 O  O   . ALA   B 1 858  ? 91.86400   82.94700  3.78400   1.000 83.64431  ?  856  ALA   B O   1 
ATOM   20779 C  CB  . ALA   B 1 858  ? 90.87200   81.12000  6.28900   1.000 56.60031  ?  856  ALA   B CB  1 
ATOM   20780 N  N   . GLU   B 1 859  ? 92.38800   80.77100  3.49100   1.000 42.22754  ?  857  GLU   B N   1 
ATOM   20781 C  CA  . GLU   B 1 859  ? 92.38300   80.82500  2.03200   1.000 66.55093  ?  857  GLU   B CA  1 
ATOM   20782 C  C   . GLU   B 1 859  ? 91.14600   80.09600  1.52200   1.000 78.19698  ?  857  GLU   B C   1 
ATOM   20783 O  O   . GLU   B 1 859  ? 91.04100   78.87100  1.65000   1.000 77.45463  ?  857  GLU   B O   1 
ATOM   20784 C  CB  . GLU   B 1 859  ? 93.65900   80.21600  1.45300   1.000 75.04119  ?  857  GLU   B CB  1 
ATOM   20785 C  CG  . GLU   B 1 859  ? 93.97600   80.69800  0.04600   1.000 66.86807  ?  857  GLU   B CG  1 
ATOM   20786 C  CD  . GLU   B 1 859  ? 95.08900   79.90600  -0.61000  1.000 97.99322  ?  857  GLU   B CD  1 
ATOM   20787 O  OE1 . GLU   B 1 859  ? 95.85800   79.24100  0.11500   1.000 105.05416 ?  857  GLU   B OE1 1 
ATOM   20788 O  OE2 . GLU   B 1 859  ? 95.19100   79.94700  -1.85500  1.000 125.30872 -1 857  GLU   B OE2 1 
ATOM   20789 N  N   . LEU   B 1 860  ? 90.21900   80.84900  0.93600   1.000 78.38187  ?  858  LEU   B N   1 
ATOM   20790 C  CA  . LEU   B 1 860  ? 88.97200   80.28600  0.44100   1.000 59.87268  ?  858  LEU   B CA  1 
ATOM   20791 C  C   . LEU   B 1 860  ? 89.19700   79.54300  -0.87000  1.000 46.39738  ?  858  LEU   B C   1 
ATOM   20792 O  O   . LEU   B 1 860  ? 90.00600   79.95600  -1.70500  1.000 53.17421  ?  858  LEU   B O   1 
ATOM   20793 C  CB  . LEU   B 1 860  ? 87.93800   81.39600  0.24100   1.000 64.81183  ?  858  LEU   B CB  1 
ATOM   20794 C  CG  . LEU   B 1 860  ? 86.56500   81.01700  -0.31900  1.000 61.43811  ?  858  LEU   B CG  1 
ATOM   20795 C  CD1 . LEU   B 1 860  ? 85.77300   80.19600  0.68600   1.000 44.63518  ?  858  LEU   B CD1 1 
ATOM   20796 C  CD2 . LEU   B 1 860  ? 85.79700   82.26500  -0.72900  1.000 61.00510  ?  858  LEU   B CD2 1 
ATOM   20797 N  N   . SER   B 1 861  ? 88.47600   78.43900  -1.04400  1.000 38.51158  ?  859  SER   B N   1 
ATOM   20798 C  CA  . SER   B 1 861  ? 88.48600   77.69900  -2.29700  1.000 53.13339  ?  859  SER   B CA  1 
ATOM   20799 C  C   . SER   B 1 861  ? 87.37400   78.22500  -3.19500  1.000 63.04382  ?  859  SER   B C   1 
ATOM   20800 O  O   . SER   B 1 861  ? 86.21200   78.29000  -2.78000  1.000 58.87516  ?  859  SER   B O   1 
ATOM   20801 C  CB  . SER   B 1 861  ? 88.31100   76.20100  -2.04600  1.000 37.91136  ?  859  SER   B CB  1 
ATOM   20802 O  OG  . SER   B 1 861  ? 88.48300   75.46200  -3.24200  1.000 72.15419  ?  859  SER   B OG  1 
ATOM   20803 N  N   . PHE   B 1 862  ? 87.73300   78.60600  -4.42300  1.000 46.49216  ?  860  PHE   B N   1 
ATOM   20804 C  CA  . PHE   B 1 862  ? 86.79200   79.22100  -5.36400  1.000 34.22750  ?  860  PHE   B CA  1 
ATOM   20805 C  C   . PHE   B 1 862  ? 87.05200   78.61200  -6.74100  1.000 44.59008  ?  860  PHE   B C   1 
ATOM   20806 O  O   . PHE   B 1 862  ? 87.89000   79.10200  -7.50100  1.000 68.19489  ?  860  PHE   B O   1 
ATOM   20807 C  CB  . PHE   B 1 862  ? 86.94200   80.73700  -5.37600  1.000 37.11737  ?  860  PHE   B CB  1 
ATOM   20808 C  CG  . PHE   B 1 862  ? 85.70800   81.46700  -5.82600  1.000 52.30693  ?  860  PHE   B CG  1 
ATOM   20809 C  CD1 . PHE   B 1 862  ? 84.70500   81.77600  -4.92200  1.000 55.36548  ?  860  PHE   B CD1 1 
ATOM   20810 C  CD2 . PHE   B 1 862  ? 85.55400   81.85100  -7.14700  1.000 48.08521  ?  860  PHE   B CD2 1 
ATOM   20811 C  CE1 . PHE   B 1 862  ? 83.56900   82.45000  -5.32800  1.000 52.94913  ?  860  PHE   B CE1 1 
ATOM   20812 C  CE2 . PHE   B 1 862  ? 84.42000   82.52500  -7.56100  1.000 44.18466  ?  860  PHE   B CE2 1 
ATOM   20813 C  CZ  . PHE   B 1 862  ? 83.42700   82.82500  -6.64900  1.000 66.17983  ?  860  PHE   B CZ  1 
ATOM   20814 N  N   . VAL   B 1 863  ? 86.32300   77.54600  -7.05400  1.000 50.87840  ?  861  VAL   B N   1 
ATOM   20815 C  CA  . VAL   B 1 863  ? 86.48400   76.83400  -8.31700  1.000 42.24987  ?  861  VAL   B CA  1 
ATOM   20816 C  C   . VAL   B 1 863  ? 85.58400   77.47800  -9.36400  1.000 47.01681  ?  861  VAL   B C   1 
ATOM   20817 O  O   . VAL   B 1 863  ? 84.35600   77.46700  -9.23100  1.000 60.71460  ?  861  VAL   B O   1 
ATOM   20818 C  CB  . VAL   B 1 863  ? 86.15800   75.34200  -8.15700  1.000 40.08245  ?  861  VAL   B CB  1 
ATOM   20819 C  CG1 . VAL   B 1 863  ? 86.31400   74.62000  -9.48500  1.000 48.55315  ?  861  VAL   B CG1 1 
ATOM   20820 C  CG2 . VAL   B 1 863  ? 87.04800   74.71600  -7.09400  1.000 72.88162  ?  861  VAL   B CG2 1 
ATOM   20821 N  N   . ARG   B 1 864  ? 86.19400   78.03700  -10.40600 1.000 49.66997  ?  862  ARG   B N   1 
ATOM   20822 C  CA  . ARG   B 1 864  ? 85.45700   78.60300  -11.52800 1.000 52.72885  ?  862  ARG   B CA  1 
ATOM   20823 C  C   . ARG   B 1 864  ? 85.25600   77.52400  -12.58600 1.000 50.27815  ?  862  ARG   B C   1 
ATOM   20824 O  O   . ARG   B 1 864  ? 86.22900   76.95600  -13.09300 1.000 52.97270  ?  862  ARG   B O   1 
ATOM   20825 C  CB  . ARG   B 1 864  ? 86.19700   79.80600  -12.11300 1.000 49.24128  ?  862  ARG   B CB  1 
ATOM   20826 C  CG  . ARG   B 1 864  ? 85.89200   81.12400  -11.41700 1.000 56.19056  ?  862  ARG   B CG  1 
ATOM   20827 C  CD  . ARG   B 1 864  ? 86.96800   82.16200  -11.69400 1.000 60.90524  ?  862  ARG   B CD  1 
ATOM   20828 N  NE  . ARG   B 1 864  ? 88.19200   81.87500  -10.95700 1.000 75.75034  ?  862  ARG   B NE  1 
ATOM   20829 C  CZ  . ARG   B 1 864  ? 88.48400   82.37900  -9.76500  1.000 77.40351  ?  862  ARG   B CZ  1 
ATOM   20830 N  NH1 . ARG   B 1 864  ? 87.67100   83.22800  -9.15700  1.000 81.95462  ?  862  ARG   B NH1 1 
ATOM   20831 N  NH2 . ARG   B 1 864  ? 89.61900   82.02400  -9.17000  1.000 86.88499  ?  862  ARG   B NH2 1 
ATOM   20832 N  N   . GLN   B 1 865  ? 83.99700   77.24200  -12.91400 1.000 46.09626  ?  863  GLN   B N   1 
ATOM   20833 C  CA  . GLN   B 1 865  ? 83.65600   76.20400  -13.87300 1.000 47.37317  ?  863  GLN   B CA  1 
ATOM   20834 C  C   . GLN   B 1 865  ? 82.69300   76.75200  -14.91700 1.000 52.33044  ?  863  GLN   B C   1 
ATOM   20835 O  O   . GLN   B 1 865  ? 82.05500   77.79100  -14.72800 1.000 53.18222  ?  863  GLN   B O   1 
ATOM   20836 C  CB  . GLN   B 1 865  ? 83.03500   74.98300  -13.18400 1.000 39.17609  ?  863  GLN   B CB  1 
ATOM   20837 C  CG  . GLN   B 1 865  ? 84.00900   74.17900  -12.34600 1.000 32.05503  ?  863  GLN   B CG  1 
ATOM   20838 C  CD  . GLN   B 1 865  ? 83.33300   73.04400  -11.60600 1.000 38.60123  ?  863  GLN   B CD  1 
ATOM   20839 O  OE1 . GLN   B 1 865  ? 83.50400   71.87400  -11.94900 1.000 43.45077  ?  863  GLN   B OE1 1 
ATOM   20840 N  NE2 . GLN   B 1 865  ? 82.55800   73.38500  -10.58200 1.000 36.61291  ?  863  GLN   B NE2 1 
ATOM   20841 N  N   . THR   B 1 866  ? 82.60100   76.02800  -16.03000 1.000 46.34069  ?  864  THR   B N   1 
ATOM   20842 C  CA  . THR   B 1 866  ? 81.69400   76.34200  -17.12500 1.000 48.54601  ?  864  THR   B CA  1 
ATOM   20843 C  C   . THR   B 1 866  ? 80.81900   75.12600  -17.39300 1.000 54.02630  ?  864  THR   B C   1 
ATOM   20844 O  O   . THR   B 1 866  ? 81.32500   74.00200  -17.47100 1.000 56.51449  ?  864  THR   B O   1 
ATOM   20845 C  CB  . THR   B 1 866  ? 82.47100   76.74000  -18.38800 1.000 46.86986  ?  864  THR   B CB  1 
ATOM   20846 O  OG1 . THR   B 1 866  ? 82.75200   78.14600  -18.36000 1.000 58.16001  ?  864  THR   B OG1 1 
ATOM   20847 C  CG2 . THR   B 1 866  ? 81.68500   76.40200  -19.64900 1.000 45.22460  ?  864  THR   B CG2 1 
ATOM   20848 N  N   . GLY   B 1 867  ? 79.51300   75.34700  -17.52000 1.000 46.72562  ?  865  GLY   B N   1 
ATOM   20849 C  CA  . GLY   B 1 867  ? 78.60700   74.24100  -17.75500 1.000 46.62800  ?  865  GLY   B CA  1 
ATOM   20850 C  C   . GLY   B 1 867  ? 77.37900   74.58900  -18.57000 1.000 47.32378  ?  865  GLY   B C   1 
ATOM   20851 O  O   . GLY   B 1 867  ? 77.25200   75.70300  -19.08500 1.000 52.66412  ?  865  GLY   B O   1 
ATOM   20852 N  N   . GLU   B 1 868  ? 76.47500   73.62500  -18.70200 1.000 54.08707  ?  866  GLU   B N   1 
ATOM   20853 C  CA  . GLU   B 1 868  ? 75.18400   73.79900  -19.35000 1.000 40.85566  ?  866  GLU   B CA  1 
ATOM   20854 C  C   . GLU   B 1 868  ? 74.08300   73.44200  -18.35800 1.000 46.87663  ?  866  GLU   B C   1 
ATOM   20855 O  O   . GLU   B 1 868  ? 74.34800   73.01300  -17.23300 1.000 48.55764  ?  866  GLU   B O   1 
ATOM   20856 C  CB  . GLU   B 1 868  ? 75.08500   72.94400  -20.61600 1.000 38.55544  ?  866  GLU   B CB  1 
ATOM   20857 C  CG  . GLU   B 1 868  ? 75.11900   71.45000  -20.35700 1.000 42.73713  ?  866  GLU   B CG  1 
ATOM   20858 C  CD  . GLU   B 1 868  ? 75.11000   70.63800  -21.63500 1.000 55.02415  ?  866  GLU   B CD  1 
ATOM   20859 O  OE1 . GLU   B 1 868  ? 74.93900   71.23700  -22.71800 1.000 40.44369  ?  866  GLU   B OE1 1 
ATOM   20860 O  OE2 . GLU   B 1 868  ? 75.27600   69.40300  -21.55700 1.000 65.49030  -1 866  GLU   B OE2 1 
ATOM   20861 N  N   . GLU   B 1 869  ? 72.83200   73.61600  -18.79000 1.000 50.63515  ?  867  GLU   B N   1 
ATOM   20862 C  CA  . GLU   B 1 869  ? 71.70700   73.40800  -17.88400 1.000 38.27300  ?  867  GLU   B CA  1 
ATOM   20863 C  C   . GLU   B 1 869  ? 71.65200   71.97000  -17.38600 1.000 43.42053  ?  867  GLU   B C   1 
ATOM   20864 O  O   . GLU   B 1 869  ? 71.40100   71.72500  -16.20000 1.000 59.88169  ?  867  GLU   B O   1 
ATOM   20865 C  CB  . GLU   B 1 869  ? 70.40100   73.79000  -18.57500 1.000 43.70783  ?  867  GLU   B CB  1 
ATOM   20866 C  CG  . GLU   B 1 869  ? 69.37200   74.36500  -17.62700 1.000 52.62071  ?  867  GLU   B CG  1 
ATOM   20867 C  CD  . GLU   B 1 869  ? 69.91700   75.54100  -16.84000 1.000 72.75397  ?  867  GLU   B CD  1 
ATOM   20868 O  OE1 . GLU   B 1 869  ? 70.50100   76.45500  -17.46300 1.000 60.72673  ?  867  GLU   B OE1 1 
ATOM   20869 O  OE2 . GLU   B 1 869  ? 69.77700   75.54400  -15.59900 1.000 78.67548  -1 867  GLU   B OE2 1 
ATOM   20870 N  N   . GLU   B 1 870  ? 71.89600   71.00800  -18.27100 1.000 35.66015  ?  868  GLU   B N   1 
ATOM   20871 C  CA  . GLU   B 1 870  ? 71.86500   69.59200  -17.91400 1.000 39.43521  ?  868  GLU   B CA  1 
ATOM   20872 C  C   . GLU   B 1 870  ? 73.21900   69.08500  -17.44100 1.000 51.29867  ?  868  GLU   B C   1 
ATOM   20873 O  O   . GLU   B 1 870  ? 73.58900   67.93800  -17.69900 1.000 59.26405  ?  868  GLU   B O   1 
ATOM   20874 C  CB  . GLU   B 1 870  ? 71.36400   68.78200  -19.10500 1.000 43.82157  ?  868  GLU   B CB  1 
ATOM   20875 C  CG  . GLU   B 1 870  ? 70.21200   69.45300  -19.84400 1.000 56.06594  ?  868  GLU   B CG  1 
ATOM   20876 C  CD  . GLU   B 1 870  ? 69.55600   68.54400  -20.86000 1.000 58.49095  ?  868  GLU   B CD  1 
ATOM   20877 O  OE1 . GLU   B 1 870  ? 70.10300   67.45300  -21.12000 1.000 57.78417  ?  868  GLU   B OE1 1 
ATOM   20878 O  OE2 . GLU   B 1 870  ? 68.48900   68.91800  -21.39400 1.000 55.97894  -1 868  GLU   B OE2 1 
ATOM   20879 N  N   . SER   B 1 871  ? 73.97700   69.92500  -16.73600 1.000 52.90887  ?  869  SER   B N   1 
ATOM   20880 C  CA  . SER   B 1 871  ? 75.31600   69.55300  -16.29300 1.000 40.38032  ?  869  SER   B CA  1 
ATOM   20881 C  C   . SER   B 1 871  ? 75.65900   70.20300  -14.95900 1.000 45.65898  ?  869  SER   B C   1 
ATOM   20882 O  O   . SER   B 1 871  ? 76.60900   69.78500  -14.29100 1.000 48.82693  ?  869  SER   B O   1 
ATOM   20883 C  CB  . SER   B 1 871  ? 76.35500   69.95200  -17.33900 1.000 32.73594  ?  869  SER   B CB  1 
ATOM   20884 O  OG  . SER   B 1 871  ? 76.64300   71.33600  -17.26400 1.000 43.60987  ?  869  SER   B OG  1 
ATOM   20885 N  N   . VAL   B 1 872  ? 74.89300   71.22600  -14.56800 1.000 42.62619  ?  870  VAL   B N   1 
ATOM   20886 C  CA  . VAL   B 1 872  ? 75.20300   71.97400  -13.35100 1.000 37.87318  ?  870  VAL   B CA  1 
ATOM   20887 C  C   . VAL   B 1 872  ? 75.18200   71.05800  -12.13300 1.000 38.21935  ?  870  VAL   B C   1 
ATOM   20888 O  O   . VAL   B 1 872  ? 76.01900   71.18200  -11.23000 1.000 41.31035  ?  870  VAL   B O   1 
ATOM   20889 C  CB  . VAL   B 1 872  ? 74.22600   73.15500  -13.19000 1.000 29.82834  ?  870  VAL   B CB  1 
ATOM   20890 C  CG1 . VAL   B 1 872  ? 74.38900   73.80500  -11.82400 1.000 32.82824  ?  870  VAL   B CG1 1 
ATOM   20891 C  CG2 . VAL   B 1 872  ? 74.44900   74.17900  -14.29000 1.000 35.01092  ?  870  VAL   B CG2 1 
ATOM   20892 N  N   . GLN   B 1 873  ? 74.23900   70.11600  -12.09500 1.000 41.45299  ?  871  GLN   B N   1 
ATOM   20893 C  CA  . GLN   B 1 873  ? 74.13500   69.22700  -10.94200 1.000 50.03988  ?  871  GLN   B CA  1 
ATOM   20894 C  C   . GLN   B 1 873  ? 75.31300   68.26300  -10.87200 1.000 44.96557  ?  871  GLN   B C   1 
ATOM   20895 O  O   . GLN   B 1 873  ? 75.85800   68.02000  -9.78900  1.000 46.84348  ?  871  GLN   B O   1 
ATOM   20896 C  CB  . GLN   B 1 873  ? 72.81300   68.46400  -10.99200 1.000 63.54724  ?  871  GLN   B CB  1 
ATOM   20897 C  CG  . GLN   B 1 873  ? 71.59400   69.36600  -11.07000 1.000 46.68489  ?  871  GLN   B CG  1 
ATOM   20898 C  CD  . GLN   B 1 873  ? 70.29400   68.59000  -11.07200 1.000 59.78125  ?  871  GLN   B CD  1 
ATOM   20899 O  OE1 . GLN   B 1 873  ? 69.81000   68.17500  -12.12400 1.000 74.43146  ?  871  GLN   B OE1 1 
ATOM   20900 N  NE2 . GLN   B 1 873  ? 69.72300   68.38600  -9.89100  1.000 46.32584  ?  871  GLN   B NE2 1 
ATOM   20901 N  N   . SER   B 1 874  ? 75.72300   67.70500  -12.01500 1.000 48.19551  ?  872  SER   B N   1 
ATOM   20902 C  CA  . SER   B 1 874  ? 76.84900   66.77700  -12.02200 1.000 43.16106  ?  872  SER   B CA  1 
ATOM   20903 C  C   . SER   B 1 874  ? 78.16300   67.47900  -11.71200 1.000 47.17459  ?  872  SER   B C   1 
ATOM   20904 O  O   . SER   B 1 874  ? 79.09500   66.84600  -11.20500 1.000 63.10428  ?  872  SER   B O   1 
ATOM   20905 C  CB  . SER   B 1 874  ? 76.93400   66.06200  -13.37000 1.000 42.60933  ?  872  SER   B CB  1 
ATOM   20906 O  OG  . SER   B 1 874  ? 77.09500   66.99400  -14.42500 1.000 61.08083  ?  872  SER   B OG  1 
ATOM   20907 N  N   . LEU   B 1 875  ? 78.26300   68.77300  -12.01900 1.000 40.17044  ?  873  LEU   B N   1 
ATOM   20908 C  CA  . LEU   B 1 875  ? 79.44500   69.54400  -11.66100 1.000 38.14637  ?  873  LEU   B CA  1 
ATOM   20909 C  C   . LEU   B 1 875  ? 79.44700   69.95500  -10.19700 1.000 44.59159  ?  873  LEU   B C   1 
ATOM   20910 O  O   . LEU   B 1 875  ? 80.51600   70.24000  -9.64500  1.000 59.05532  ?  873  LEU   B O   1 
ATOM   20911 C  CB  . LEU   B 1 875  ? 79.55000   70.79400  -12.53700 1.000 31.89300  ?  873  LEU   B CB  1 
ATOM   20912 C  CG  . LEU   B 1 875  ? 79.76400   70.55300  -14.03000 1.000 42.24803  ?  873  LEU   B CG  1 
ATOM   20913 C  CD1 . LEU   B 1 875  ? 79.84000   71.87400  -14.77700 1.000 40.33869  ?  873  LEU   B CD1 1 
ATOM   20914 C  CD2 . LEU   B 1 875  ? 81.01900   69.73000  -14.25600 1.000 56.11169  ?  873  LEU   B CD2 1 
ATOM   20915 N  N   . LEU   B 1 876  ? 78.27800   69.99300  -9.56400  1.000 47.43627  ?  874  LEU   B N   1 
ATOM   20916 C  CA  . LEU   B 1 876  ? 78.16900   70.38300  -8.16600  1.000 46.34321  ?  874  LEU   B CA  1 
ATOM   20917 C  C   . LEU   B 1 876  ? 78.26600   69.19800  -7.21800  1.000 44.29762  ?  874  LEU   B C   1 
ATOM   20918 O  O   . LEU   B 1 876  ? 78.76400   69.34900  -6.09600  1.000 50.56881  ?  874  LEU   B O   1 
ATOM   20919 C  CB  . LEU   B 1 876  ? 76.84600   71.11500  -7.93400  1.000 32.45070  ?  874  LEU   B CB  1 
ATOM   20920 C  CG  . LEU   B 1 876  ? 76.74500   71.79000  -6.57300  1.000 34.86692  ?  874  LEU   B CG  1 
ATOM   20921 C  CD1 . LEU   B 1 876  ? 77.93300   72.70600  -6.40600  1.000 45.40798  ?  874  LEU   B CD1 1 
ATOM   20922 C  CD2 . LEU   B 1 876  ? 75.45100   72.55700  -6.46100  1.000 36.64927  ?  874  LEU   B CD2 1 
ATOM   20923 N  N   . ALA   B 1 877  ? 77.79700   68.02500  -7.64800  1.000 42.85515  ?  875  ALA   B N   1 
ATOM   20924 C  CA  . ALA   B 1 877  ? 77.85000   66.83800  -6.80100  1.000 34.77578  ?  875  ALA   B CA  1 
ATOM   20925 C  C   . ALA   B 1 877  ? 79.28600   66.46400  -6.46100  1.000 45.87486  ?  875  ALA   B C   1 
ATOM   20926 O  O   . ALA   B 1 877  ? 79.58600   66.07400  -5.32700  1.000 59.79640  ?  875  ALA   B O   1 
ATOM   20927 C  CB  . ALA   B 1 877  ? 77.14600   65.67700  -7.50000  1.000 45.77090  ?  875  ALA   B CB  1 
ATOM   20928 N  N   . GLU   B 1 878  ? 80.18700   66.57700  -7.43800  1.000 48.42865  ?  876  GLU   B N   1 
ATOM   20929 C  CA  . GLU   B 1 878  ? 81.59100   66.24900  -7.21800  1.000 47.34995  ?  876  GLU   B CA  1 
ATOM   20930 C  C   . GLU   B 1 878  ? 82.26000   67.21500  -6.25100  1.000 48.24998  ?  876  GLU   B C   1 
ATOM   20931 O  O   . GLU   B 1 878  ? 83.23200   66.84600  -5.58400  1.000 72.88651  ?  876  GLU   B O   1 
ATOM   20932 C  CB  . GLU   B 1 878  ? 82.32800   66.24900  -8.55500  1.000 51.08734  ?  876  GLU   B CB  1 
ATOM   20933 C  CG  . GLU   B 1 878  ? 81.77300   67.27500  -9.52700  1.000 73.83728  ?  876  GLU   B CG  1 
ATOM   20934 C  CD  . GLU   B 1 878  ? 82.66500   67.50000  -10.72900 1.000 85.50814  ?  876  GLU   B CD  1 
ATOM   20935 O  OE1 . GLU   B 1 878  ? 82.63800   66.66200  -11.65400 1.000 84.59993  ?  876  GLU   B OE1 1 
ATOM   20936 O  OE2 . GLU   B 1 878  ? 83.39100   68.51700  -10.74700 1.000 66.61165  -1 876  GLU   B OE2 1 
ATOM   20937 N  N   . GLN   B 1 879  ? 81.76900   68.45000  -6.16900  1.000 42.66057  ?  877  GLN   B N   1 
ATOM   20938 C  CA  . GLN   B 1 879  ? 82.38300   69.44300  -5.29800  1.000 50.95191  ?  877  GLN   B CA  1 
ATOM   20939 C  C   . GLN   B 1 879  ? 81.95700   69.29100  -3.84400  1.000 53.34145  ?  877  GLN   B C   1 
ATOM   20940 O  O   . GLN   B 1 879  ? 82.60200   69.86500  -2.95900  1.000 50.72640  ?  877  GLN   B O   1 
ATOM   20941 C  CB  . GLN   B 1 879  ? 82.04600   70.85300  -5.78700  1.000 44.04582  ?  877  GLN   B CB  1 
ATOM   20942 C  CG  . GLN   B 1 879  ? 82.47300   71.14100  -7.21800  1.000 44.24735  ?  877  GLN   B CG  1 
ATOM   20943 C  CD  . GLN   B 1 879  ? 83.84700   71.77600  -7.30500  1.000 58.81908  ?  877  GLN   B CD  1 
ATOM   20944 O  OE1 . GLN   B 1 879  ? 83.97600   72.95300  -7.63800  1.000 70.51632  ?  877  GLN   B OE1 1 
ATOM   20945 N  NE2 . GLN   B 1 879  ? 84.88100   70.99700  -7.01000  1.000 55.61715  ?  877  GLN   B NE2 1 
ATOM   20946 N  N   . ILE   B 1 880  ? 80.88900   68.54000  -3.58100  1.000 46.55274  ?  878  ILE   B N   1 
ATOM   20947 C  CA  . ILE   B 1 880  ? 80.41500   68.29800  -2.22000  1.000 52.27438  ?  878  ILE   B CA  1 
ATOM   20948 C  C   . ILE   B 1 880  ? 81.28400   67.18800  -1.63500  1.000 54.09455  ?  878  ILE   B C   1 
ATOM   20949 O  O   . ILE   B 1 880  ? 81.08600   66.00800  -1.92700  1.000 60.25614  ?  878  ILE   B O   1 
ATOM   20950 C  CB  . ILE   B 1 880  ? 78.93000   67.93400  -2.19000  1.000 46.85683  ?  878  ILE   B CB  1 
ATOM   20951 C  CG1 . ILE   B 1 880  ? 78.10000   69.06200  -2.80700  1.000 45.87504  ?  878  ILE   B CG1 1 
ATOM   20952 C  CG2 . ILE   B 1 880  ? 78.48200   67.65200  -0.76800  1.000 37.18513  ?  878  ILE   B CG2 1 
ATOM   20953 C  CD1 . ILE   B 1 880  ? 76.67900   68.66700  -3.13100  1.000 40.94852  ?  878  ILE   B CD1 1 
ATOM   20954 N  N   . LYS   B 1 881  ? 82.25200   67.56400  -0.81300  1.000 62.10845  ?  879  LYS   B N   1 
ATOM   20955 C  CA  . LYS   B 1 881  ? 83.24100   66.64900  -0.26700  1.000 57.47321  ?  879  LYS   B CA  1 
ATOM   20956 C  C   . LYS   B 1 881  ? 83.26500   66.75800  1.24800   1.000 55.54001  ?  879  LYS   B C   1 
ATOM   20957 O  O   . LYS   B 1 881  ? 82.83800   67.77100  1.81300   1.000 51.60541  ?  879  LYS   B O   1 
ATOM   20958 C  CB  . LYS   B 1 881  ? 84.63500   66.95000  -0.83900  1.000 45.09512  ?  879  LYS   B CB  1 
ATOM   20959 C  CG  . LYS   B 1 881  ? 84.71300   66.85500  -2.35400  1.000 43.12203  ?  879  LYS   B CG  1 
ATOM   20960 C  CD  . LYS   B 1 881  ? 85.86900   65.97300  -2.79300  1.000 51.92654  ?  879  LYS   B CD  1 
ATOM   20961 C  CE  . LYS   B 1 881  ? 86.02500   65.98300  -4.30200  1.000 50.30639  ?  879  LYS   B CE  1 
ATOM   20962 N  NZ  . LYS   B 1 881  ? 86.23300   67.36400  -4.81900  1.000 55.78196  ?  879  LYS   B NZ  1 
ATOM   20963 N  N   . PRO   B 1 882  ? 83.74900   65.72200  1.93800   1.000 64.78087  ?  880  PRO   B N   1 
ATOM   20964 C  CA  . PRO   B 1 882  ? 83.82100   65.78500  3.40200   1.000 52.26644  ?  880  PRO   B CA  1 
ATOM   20965 C  C   . PRO   B 1 882  ? 84.76900   66.87800  3.87200   1.000 55.63140  ?  880  PRO   B C   1 
ATOM   20966 O  O   . PRO   B 1 882  ? 85.76800   67.19200  3.22100   1.000 61.24953  ?  880  PRO   B O   1 
ATOM   20967 C  CB  . PRO   B 1 882  ? 84.33900   64.39600  3.79400   1.000 51.05264  ?  880  PRO   B CB  1 
ATOM   20968 C  CG  . PRO   B 1 882  ? 84.00100   63.52200  2.63600   1.000 62.52920  ?  880  PRO   B CG  1 
ATOM   20969 C  CD  . PRO   B 1 882  ? 84.12200   64.39300  1.42600   1.000 66.37995  ?  880  PRO   B CD  1 
ATOM   20970 N  N   . PHE   B 1 883  ? 84.44000   67.45900  5.02000   1.000 55.66844  ?  881  PHE   B N   1 
ATOM   20971 C  CA  . PHE   B 1 883  ? 85.25400   68.49000  5.64100   1.000 45.63916  ?  881  PHE   B CA  1 
ATOM   20972 C  C   . PHE   B 1 883  ? 86.12800   67.89400  6.73800   1.000 59.10406  ?  881  PHE   B C   1 
ATOM   20973 O  O   . PHE   B 1 883  ? 85.73500   66.95200  7.43000   1.000 67.21411  ?  881  PHE   B O   1 
ATOM   20974 C  CB  . PHE   B 1 883  ? 84.38100   69.59600  6.23900   1.000 54.36128  ?  881  PHE   B CB  1 
ATOM   20975 C  CG  . PHE   B 1 883  ? 83.99800   70.66800  5.26200   1.000 56.07008  ?  881  PHE   B CG  1 
ATOM   20976 C  CD1 . PHE   B 1 883  ? 84.93900   71.57900  4.81100   1.000 63.94903  ?  881  PHE   B CD1 1 
ATOM   20977 C  CD2 . PHE   B 1 883  ? 82.69400   70.78000  4.81200   1.000 54.26602  ?  881  PHE   B CD2 1 
ATOM   20978 C  CE1 . PHE   B 1 883  ? 84.59000   72.57400  3.91800   1.000 52.95079  ?  881  PHE   B CE1 1 
ATOM   20979 C  CE2 . PHE   B 1 883  ? 82.33800   71.77300  3.92000   1.000 62.33850  ?  881  PHE   B CE2 1 
ATOM   20980 C  CZ  . PHE   B 1 883  ? 83.28800   72.67100  3.47200   1.000 61.68012  ?  881  PHE   B CZ  1 
ATOM   20981 N  N   . ASP   B 1 884  ? 87.32200   68.45600  6.88700   1.000 63.48888  ?  882  ASP   B N   1 
ATOM   20982 C  CA  . ASP   B 1 884  ? 88.17100   68.19700  8.04200   1.000 64.90739  ?  882  ASP   B CA  1 
ATOM   20983 C  C   . ASP   B 1 884  ? 87.95500   69.35100  9.01300   1.000 67.85294  ?  882  ASP   B C   1 
ATOM   20984 O  O   . ASP   B 1 884  ? 88.28900   70.49900  8.70400   1.000 74.67422  ?  882  ASP   B O   1 
ATOM   20985 C  CB  . ASP   B 1 884  ? 89.63900   68.06900  7.63600   1.000 73.43443  ?  882  ASP   B CB  1 
ATOM   20986 C  CG  . ASP   B 1 884  ? 90.53000   67.63200  8.78800   1.000 71.91172  ?  882  ASP   B CG  1 
ATOM   20987 O  OD1 . ASP   B 1 884  ? 90.00800   67.40300  9.90100   1.000 59.43995  ?  882  ASP   B OD1 1 
ATOM   20988 O  OD2 . ASP   B 1 884  ? 91.75600   67.51400  8.58100   1.000 68.45013  -1 882  ASP   B OD2 1 
ATOM   20989 N  N   . LEU   B 1 885  ? 87.38800   69.04800  10.18200  1.000 51.13356  ?  883  LEU   B N   1 
ATOM   20990 C  CA  . LEU   B 1 885  ? 87.04200   70.09200  11.14100  1.000 48.19478  ?  883  LEU   B CA  1 
ATOM   20991 C  C   . LEU   B 1 885  ? 88.26100   70.78800  11.73100  1.000 60.39516  ?  883  LEU   B C   1 
ATOM   20992 O  O   . LEU   B 1 885  ? 88.09300   71.68700  12.56300  1.000 59.84834  ?  883  LEU   B O   1 
ATOM   20993 C  CB  . LEU   B 1 885  ? 86.17700   69.50900  12.26300  1.000 45.88976  ?  883  LEU   B CB  1 
ATOM   20994 C  CG  . LEU   B 1 885  ? 84.84800   68.86600  11.85100  1.000 57.07821  ?  883  LEU   B CG  1 
ATOM   20995 C  CD1 . LEU   B 1 885  ? 83.87500   68.84400  13.02200  1.000 57.95829  ?  883  LEU   B CD1 1 
ATOM   20996 C  CD2 . LEU   B 1 885  ? 84.22700   69.56800  10.64800  1.000 70.36911  ?  883  LEU   B CD2 1 
ATOM   20997 N  N   . ALA   B 1 886  ? 89.47200   70.40400  11.32500  1.000 68.40073  ?  884  ALA   B N   1 
ATOM   20998 C  CA  . ALA   B 1 886  ? 90.69300   71.05700  11.76700  1.000 60.41905  ?  884  ALA   B CA  1 
ATOM   20999 C  C   . ALA   B 1 886  ? 91.32900   71.93300  10.69800  1.000 63.41079  ?  884  ALA   B C   1 
ATOM   21000 O  O   . ALA   B 1 886  ? 92.28500   72.65400  11.00400  1.000 82.38800  ?  884  ALA   B O   1 
ATOM   21001 C  CB  . ALA   B 1 886  ? 91.71500   70.01100  12.23700  1.000 63.23387  ?  884  ALA   B CB  1 
ATOM   21002 N  N   . LYS   B 1 887  ? 90.83800   71.88800  9.46200   1.000 65.43634  ?  885  LYS   B N   1 
ATOM   21003 C  CA  . LYS   B 1 887  ? 91.33600   72.72900  8.38100   1.000 76.81120  ?  885  LYS   B CA  1 
ATOM   21004 C  C   . LYS   B 1 887  ? 90.30700   73.80200  8.05400   1.000 69.93742  ?  885  LYS   B C   1 
ATOM   21005 O  O   . LYS   B 1 887  ? 89.13100   73.49400  7.83400   1.000 58.40429  ?  885  LYS   B O   1 
ATOM   21006 C  CB  . LYS   B 1 887  ? 91.64600   71.90400  7.13000   1.000 66.02316  ?  885  LYS   B CB  1 
ATOM   21007 C  CG  . LYS   B 1 887  ? 92.81100   70.94000  7.27600   1.000 67.11458  ?  885  LYS   B CG  1 
ATOM   21008 C  CD  . LYS   B 1 887  ? 93.39700   70.59400  5.91500   1.000 68.40505  ?  885  LYS   B CD  1 
ATOM   21009 C  CE  . LYS   B 1 887  ? 94.03700   69.21600  5.91500   1.000 69.47868  ?  885  LYS   B CE  1 
ATOM   21010 N  NZ  . LYS   B 1 887  ? 93.01700   68.14000  6.07400   1.000 57.36960  ?  885  LYS   B NZ  1 
ATOM   21011 N  N   . ALA   B 1 888  ? 90.75500   75.05200  8.01000   1.000 62.80277  ?  886  ALA   B N   1 
ATOM   21012 C  CA  . ALA   B 1 888  ? 89.91800   76.20800  7.73800   1.000 46.83827  ?  886  ALA   B CA  1 
ATOM   21013 C  C   . ALA   B 1 888  ? 90.27700   76.83500  6.39500   1.000 56.91186  ?  886  ALA   B C   1 
ATOM   21014 O  O   . ALA   B 1 888  ? 91.39600   76.66500  5.89900   1.000 63.75655  ?  886  ALA   B O   1 
ATOM   21015 C  CB  . ALA   B 1 888  ? 90.06700   77.25300  8.85300   1.000 56.05385  ?  886  ALA   B CB  1 
ATOM   21016 N  N   . PRO   B 1 889  ? 89.34400   77.57100  5.76600   1.000 51.33275  ?  887  PRO   B N   1 
ATOM   21017 C  CA  . PRO   B 1 889  ? 87.97000   77.87300  6.19900   1.000 49.70949  ?  887  PRO   B CA  1 
ATOM   21018 C  C   . PRO   B 1 889  ? 87.03600   76.68000  6.03800   1.000 49.89505  ?  887  PRO   B C   1 
ATOM   21019 O  O   . PRO   B 1 889  ? 87.16900   75.91200  5.08800   1.000 49.09012  ?  887  PRO   B O   1 
ATOM   21020 C  CB  . PRO   B 1 889  ? 87.57700   79.03900  5.28300   1.000 36.51471  ?  887  PRO   B CB  1 
ATOM   21021 C  CG  . PRO   B 1 889  ? 88.33300   78.77300  4.01900   1.000 54.70379  ?  887  PRO   B CG  1 
ATOM   21022 C  CD  . PRO   B 1 889  ? 89.65500   78.20100  4.47000   1.000 55.06181  ?  887  PRO   B CD  1 
ATOM   21023 N  N   . LEU   B 1 890  ? 86.08400   76.48800  6.95400   1.000 37.29047  ?  888  LEU   B N   1 
ATOM   21024 C  CA  . LEU   B 1 890  ? 85.08600   75.42900  6.81200   1.000 52.10394  ?  888  LEU   B CA  1 
ATOM   21025 C  C   . LEU   B 1 890  ? 83.98400   75.79400  5.82600   1.000 59.19336  ?  888  LEU   B C   1 
ATOM   21026 O  O   . LEU   B 1 890  ? 82.79800   75.57800  6.09300   1.000 45.35310  ?  888  LEU   B O   1 
ATOM   21027 C  CB  . LEU   B 1 890  ? 84.50000   75.08000  8.17800   1.000 41.23389  ?  888  LEU   B CB  1 
ATOM   21028 C  CG  . LEU   B 1 890  ? 85.33600   74.09300  8.99500   1.000 51.25744  ?  888  LEU   B CG  1 
ATOM   21029 C  CD1 . LEU   B 1 890  ? 84.49000   73.44200  10.07600  1.000 47.04819  ?  888  LEU   B CD1 1 
ATOM   21030 C  CD2 . LEU   B 1 890  ? 85.96800   73.03900  8.09400   1.000 47.54075  ?  888  LEU   B CD2 1 
ATOM   21031 N  N   . LEU   B 1 891  ? 84.36100   76.35200  4.67700   1.000 50.41482  ?  889  LEU   B N   1 
ATOM   21032 C  CA  . LEU   B 1 891  ? 83.42200   76.71800  3.62700   1.000 37.42686  ?  889  LEU   B CA  1 
ATOM   21033 C  C   . LEU   B 1 891  ? 84.16300   76.73400  2.30000   1.000 46.09833  ?  889  LEU   B C   1 
ATOM   21034 O  O   . LEU   B 1 891  ? 85.22900   77.34800  2.18900   1.000 63.40065  ?  889  LEU   B O   1 
ATOM   21035 C  CB  . LEU   B 1 891  ? 82.78600   78.08600  3.89500   1.000 40.99567  ?  889  LEU   B CB  1 
ATOM   21036 C  CG  . LEU   B 1 891  ? 81.75900   78.57300  2.86800   1.000 49.77027  ?  889  LEU   B CG  1 
ATOM   21037 C  CD1 . LEU   B 1 891  ? 80.42600   78.86000  3.54300   1.000 52.66402  ?  889  LEU   B CD1 1 
ATOM   21038 C  CD2 . LEU   B 1 891  ? 82.26900   79.80300  2.13000   1.000 36.41977  ?  889  LEU   B CD2 1 
ATOM   21039 N  N   . ARG   B 1 892  ? 83.60500   76.05100  1.30700   1.000 57.01639  ?  890  ARG   B N   1 
ATOM   21040 C  CA  . ARG   B 1 892  ? 84.12400   76.05800  -0.05000  1.000 54.27544  ?  890  ARG   B CA  1 
ATOM   21041 C  C   . ARG   B 1 892  ? 83.07400   76.67000  -0.96800  1.000 57.99877  ?  890  ARG   B C   1 
ATOM   21042 O  O   . ARG   B 1 892  ? 81.88300   76.69100  -0.64800  1.000 56.72361  ?  890  ARG   B O   1 
ATOM   21043 C  CB  . ARG   B 1 892  ? 84.49100   74.64300  -0.51500  1.000 47.79796  ?  890  ARG   B CB  1 
ATOM   21044 C  CG  . ARG   B 1 892  ? 85.23800   73.81700  0.52800   1.000 46.38047  ?  890  ARG   B CG  1 
ATOM   21045 C  CD  . ARG   B 1 892  ? 85.68500   72.48200  -0.05100  1.000 50.15280  ?  890  ARG   B CD  1 
ATOM   21046 N  NE  . ARG   B 1 892  ? 86.17400   71.55800  0.96500   1.000 32.09301  ?  890  ARG   B NE  1 
ATOM   21047 C  CZ  . ARG   B 1 892  ? 85.49700   70.50900  1.41300   1.000 51.05765  ?  890  ARG   B CZ  1 
ATOM   21048 N  NH1 . ARG   B 1 892  ? 84.29000   70.21800  0.95400   1.000 61.01483  ?  890  ARG   B NH1 1 
ATOM   21049 N  NH2 . ARG   B 1 892  ? 86.04600   69.72900  2.34000   1.000 47.70079  ?  890  ARG   B NH2 1 
ATOM   21050 N  N   . ALA   B 1 893  ? 83.51600   77.17500  -2.11600  1.000 50.75971  ?  891  ALA   B N   1 
ATOM   21051 C  CA  . ALA   B 1 893  ? 82.61600   77.91000  -2.99100  1.000 34.91091  ?  891  ALA   B CA  1 
ATOM   21052 C  C   . ALA   B 1 893  ? 83.08600   77.78800  -4.43600  1.000 44.75919  ?  891  ALA   B C   1 
ATOM   21053 O  O   . ALA   B 1 893  ? 84.07100   77.10900  -4.74000  1.000 54.26155  ?  891  ALA   B O   1 
ATOM   21054 C  CB  . ALA   B 1 893  ? 82.51400   79.37500  -2.55100  1.000 30.90319  ?  891  ALA   B CB  1 
ATOM   21055 N  N   . GLY   B 1 894  ? 82.36500   78.45600  -5.32400  1.000 47.86426  ?  892  GLY   B N   1 
ATOM   21056 C  CA  . GLY   B 1 894  ? 82.65400   78.43200  -6.74400  1.000 50.27263  ?  892  GLY   B CA  1 
ATOM   21057 C  C   . GLY   B 1 894  ? 81.46100   78.91100  -7.53700  1.000 54.10240  ?  892  GLY   B C   1 
ATOM   21058 O  O   . GLY   B 1 894  ? 80.34100   79.00600  -7.03400  1.000 45.28921  ?  892  GLY   B O   1 
ATOM   21059 N  N   . VAL   B 1 895  ? 81.71800   79.21900  -8.80700  1.000 47.31969  ?  893  VAL   B N   1 
ATOM   21060 C  CA  . VAL   B 1 895  ? 80.69800   79.74300  -9.71100  1.000 42.05960  ?  893  VAL   B CA  1 
ATOM   21061 C  C   . VAL   B 1 895  ? 80.69800   78.90900  -10.98400 1.000 45.98500  ?  893  VAL   B C   1 
ATOM   21062 O  O   . VAL   B 1 895  ? 81.70300   78.86800  -11.70600 1.000 47.37963  ?  893  VAL   B O   1 
ATOM   21063 C  CB  . VAL   B 1 895  ? 80.92300   81.22800  -10.04400 1.000 40.47766  ?  893  VAL   B CB  1 
ATOM   21064 C  CG1 . VAL   B 1 895  ? 80.01600   81.66300  -11.19100 1.000 34.05994  ?  893  VAL   B CG1 1 
ATOM   21065 C  CG2 . VAL   B 1 895  ? 80.67200   82.09000  -8.81800  1.000 47.73634  ?  893  VAL   B CG2 1 
ATOM   21066 N  N   . ILE   B 1 896  ? 79.57800   78.24800  -11.25600 1.000 45.07815  ?  894  ILE   B N   1 
ATOM   21067 C  CA  . ILE   B 1 896  ? 79.35400   77.58000  -12.53200 1.000 45.16521  ?  894  ILE   B CA  1 
ATOM   21068 C  C   . ILE   B 1 896  ? 78.70800   78.58100  -13.47800 1.000 47.47950  ?  894  ILE   B C   1 
ATOM   21069 O  O   . ILE   B 1 896  ? 77.70100   79.21100  -13.13500 1.000 49.25381  ?  894  ILE   B O   1 
ATOM   21070 C  CB  . ILE   B 1 896  ? 78.47300   76.33200  -12.35500 1.000 30.77136  ?  894  ILE   B CB  1 
ATOM   21071 C  CG1 . ILE   B 1 896  ? 79.19700   75.27900  -11.51500 1.000 37.35609  ?  894  ILE   B CG1 1 
ATOM   21072 C  CG2 . ILE   B 1 896  ? 78.07200   75.75900  -13.70600 1.000 42.16565  ?  894  ILE   B CG2 1 
ATOM   21073 C  CD1 . ILE   B 1 896  ? 78.33400   74.09100  -11.15800 1.000 36.41109  ?  894  ILE   B CD1 1 
ATOM   21074 N  N   . GLU   B 1 897  ? 79.29200   78.74700  -14.66000 1.000 44.55530  ?  895  GLU   B N   1 
ATOM   21075 C  CA  . GLU   B 1 897  ? 78.80700   79.71100  -15.63900 1.000 44.08356  ?  895  GLU   B CA  1 
ATOM   21076 C  C   . GLU   B 1 897  ? 78.21400   78.96600  -16.82600 1.000 47.62436  ?  895  GLU   B C   1 
ATOM   21077 O  O   . GLU   B 1 897  ? 78.91600   78.20600  -17.50200 1.000 46.44996  ?  895  GLU   B O   1 
ATOM   21078 C  CB  . GLU   B 1 897  ? 79.92700   80.64700  -16.09300 1.000 36.42879  ?  895  GLU   B CB  1 
ATOM   21079 C  CG  . GLU   B 1 897  ? 79.46300   81.74600  -17.03700 1.000 38.20792  ?  895  GLU   B CG  1 
ATOM   21080 C  CD  . GLU   B 1 897  ? 80.48000   82.86100  -17.18600 1.000 61.81768  ?  895  GLU   B CD  1 
ATOM   21081 O  OE1 . GLU   B 1 897  ? 81.38000   82.96900  -16.32600 1.000 70.74548  ?  895  GLU   B OE1 1 
ATOM   21082 O  OE2 . GLU   B 1 897  ? 80.37900   83.63100  -18.16400 1.000 69.41999  -1 895  GLU   B OE2 1 
ATOM   21083 N  N   . THR   B 1 898  ? 76.92700   79.18000  -17.06800 1.000 53.14423  ?  896  THR   B N   1 
ATOM   21084 C  CA  . THR   B 1 898  ? 76.24600   78.65400  -18.23600 1.000 47.77427  ?  896  THR   B CA  1 
ATOM   21085 C  C   . THR   B 1 898  ? 76.20000   79.74200  -19.31100 1.000 53.59945  ?  896  THR   B C   1 
ATOM   21086 O  O   . THR   B 1 898  ? 77.01700   80.67000  -19.31100 1.000 64.67498  ?  896  THR   B O   1 
ATOM   21087 C  CB  . THR   B 1 898  ? 74.84900   78.15900  -17.84000 1.000 53.69221  ?  896  THR   B CB  1 
ATOM   21088 O  OG1 . THR   B 1 898  ? 74.07700   79.25500  -17.33400 1.000 63.85166  ?  896  THR   B OG1 1 
ATOM   21089 C  CG2 . THR   B 1 898  ? 74.94800   77.08000  -16.77200 1.000 47.22931  ?  896  THR   B CG2 1 
ATOM   21090 N  N   . ALA   B 1 899  ? 75.25000   79.63600  -20.23500 1.000 47.94791  ?  897  ALA   B N   1 
ATOM   21091 C  CA  . ALA   B 1 899  ? 75.02200   80.67400  -21.22800 1.000 44.42483  ?  897  ALA   B CA  1 
ATOM   21092 C  C   . ALA   B 1 899  ? 73.91600   81.63600  -20.81900 1.000 57.94763  ?  897  ALA   B C   1 
ATOM   21093 O  O   . ALA   B 1 899  ? 73.65400   82.60300  -21.54100 1.000 58.70625  ?  897  ALA   B O   1 
ATOM   21094 C  CB  . ALA   B 1 899  ? 74.69100   80.04500  -22.58500 1.000 58.02440  ?  897  ALA   B CB  1 
ATOM   21095 N  N   . ASP   B 1 900  ? 73.27100   81.40000  -19.67700 1.000 58.25086  ?  898  ASP   B N   1 
ATOM   21096 C  CA  . ASP   B 1 900  ? 72.15600   82.22100  -19.22600 1.000 51.33305  ?  898  ASP   B CA  1 
ATOM   21097 C  C   . ASP   B 1 900  ? 72.22800   82.63000  -17.76400 1.000 55.38737  ?  898  ASP   B C   1 
ATOM   21098 O  O   . ASP   B 1 900  ? 71.53200   83.57800  -17.38000 1.000 65.26115  ?  898  ASP   B O   1 
ATOM   21099 C  CB  . ASP   B 1 900  ? 70.82400   81.49300  -19.46800 1.000 57.12774  ?  898  ASP   B CB  1 
ATOM   21100 C  CG  . ASP   B 1 900  ? 70.89000   80.01800  -19.10900 1.000 77.84989  ?  898  ASP   B CG  1 
ATOM   21101 O  OD1 . ASP   B 1 900  ? 71.94000   79.38700  -19.36000 1.000 71.77338  ?  898  ASP   B OD1 1 
ATOM   21102 O  OD2 . ASP   B 1 900  ? 69.89100   79.48700  -18.57900 1.000 92.16395  -1 898  ASP   B OD2 1 
ATOM   21103 N  N   . LYS   B 1 901  ? 73.03300   81.96300  -16.93800 1.000 56.94903  ?  899  LYS   B N   1 
ATOM   21104 C  CA  . LYS   B 1 901  ? 73.10600   82.29700  -15.52300 1.000 50.26037  ?  899  LYS   B CA  1 
ATOM   21105 C  C   . LYS   B 1 901  ? 74.48200   81.94200  -14.97900 1.000 59.89253  ?  899  LYS   B C   1 
ATOM   21106 O  O   . LYS   B 1 901  ? 75.23200   81.16200  -15.57400 1.000 50.74000  ?  899  LYS   B O   1 
ATOM   21107 C  CB  . LYS   B 1 901  ? 72.01500   81.57900  -14.71600 1.000 37.99503  ?  899  LYS   B CB  1 
ATOM   21108 C  CG  . LYS   B 1 901  ? 71.91500   80.08000  -14.97200 1.000 43.36524  ?  899  LYS   B CG  1 
ATOM   21109 C  CD  . LYS   B 1 901  ? 71.50200   79.33300  -13.71000 1.000 53.90857  ?  899  LYS   B CD  1 
ATOM   21110 C  CE  . LYS   B 1 901  ? 70.87200   77.98600  -14.03000 1.000 48.21514  ?  899  LYS   B CE  1 
ATOM   21111 N  NZ  . LYS   B 1 901  ? 69.47100   78.13400  -14.51300 1.000 58.73816  ?  899  LYS   B NZ  1 
ATOM   21112 N  N   . LYS   B 1 902  ? 74.80500   82.54500  -13.83600 1.000 55.28596  ?  900  LYS   B N   1 
ATOM   21113 C  CA  . LYS   B 1 902  ? 76.00200   82.24000  -13.05200 1.000 50.74136  ?  900  LYS   B CA  1 
ATOM   21114 C  C   . LYS   B 1 902  ? 75.53300   81.68600  -11.71400 1.000 49.76298  ?  900  LYS   B C   1 
ATOM   21115 O  O   . LYS   B 1 902  ? 75.10700   82.44700  -10.83800 1.000 49.52348  ?  900  LYS   B O   1 
ATOM   21116 C  CB  . LYS   B 1 902  ? 76.87200   83.47700  -12.84200 1.000 52.36250  ?  900  LYS   B CB  1 
ATOM   21117 C  CG  . LYS   B 1 902  ? 77.71700   83.89600  -14.02900 1.000 47.27339  ?  900  LYS   B CG  1 
ATOM   21118 C  CD  . LYS   B 1 902  ? 78.53900   85.13100  -13.67500 1.000 53.08650  ?  900  LYS   B CD  1 
ATOM   21119 C  CE  . LYS   B 1 902  ? 79.42300   85.59200  -14.82200 1.000 61.81756  ?  900  LYS   B CE  1 
ATOM   21120 N  NZ  . LYS   B 1 902  ? 80.36000   86.66400  -14.38200 1.000 43.61667  ?  900  LYS   B NZ  1 
ATOM   21121 N  N   . VAL   B 1 903  ? 75.61200   80.37300  -11.54500 1.000 44.90308  ?  901  VAL   B N   1 
ATOM   21122 C  CA  . VAL   B 1 903  ? 75.19000   79.74100  -10.30200 1.000 46.25015  ?  901  VAL   B CA  1 
ATOM   21123 C  C   . VAL   B 1 903  ? 76.35200   79.78800  -9.31600  1.000 45.40148  ?  901  VAL   B C   1 
ATOM   21124 O  O   . VAL   B 1 903  ? 77.43500   79.25200  -9.58100  1.000 38.63258  ?  901  VAL   B O   1 
ATOM   21125 C  CB  . VAL   B 1 903  ? 74.69400   78.30500  -10.54400 1.000 31.40990  ?  901  VAL   B CB  1 
ATOM   21126 C  CG1 . VAL   B 1 903  ? 75.23600   77.75900  -11.85100 1.000 39.52439  ?  901  VAL   B CG1 1 
ATOM   21127 C  CG2 . VAL   B 1 903  ? 75.04300   77.39400  -9.37300  1.000 36.51657  ?  901  VAL   B CG2 1 
ATOM   21128 N  N   . LEU   B 1 904  ? 76.13600   80.47900  -8.19800  1.000 40.14411  ?  902  LEU   B N   1 
ATOM   21129 C  CA  . LEU   B 1 904  ? 77.09600   80.54500  -7.10600  1.000 38.72425  ?  902  LEU   B CA  1 
ATOM   21130 C  C   . LEU   B 1 904  ? 76.75700   79.45300  -6.10200  1.000 41.97196  ?  902  LEU   B C   1 
ATOM   21131 O  O   . LEU   B 1 904  ? 75.64600   79.42500  -5.56100  1.000 52.48769  ?  902  LEU   B O   1 
ATOM   21132 C  CB  . LEU   B 1 904  ? 77.06800   81.92400  -6.44500  1.000 41.88492  ?  902  LEU   B CB  1 
ATOM   21133 C  CG  . LEU   B 1 904  ? 77.99400   82.25600  -5.26500  1.000 34.46839  ?  902  LEU   B CG  1 
ATOM   21134 C  CD1 . LEU   B 1 904  ? 77.36600   81.90300  -3.91900  1.000 39.45079  ?  902  LEU   B CD1 1 
ATOM   21135 C  CD2 . LEU   B 1 904  ? 79.34300   81.57700  -5.41900  1.000 43.11030  ?  902  LEU   B CD2 1 
ATOM   21136 N  N   . TRP   B 1 905  ? 77.70600   78.55500  -5.86100  1.000 41.23989  ?  903  TRP   B N   1 
ATOM   21137 C  CA  . TRP   B 1 905  ? 77.52400   77.45500  -4.92900  1.000 35.94537  ?  903  TRP   B CA  1 
ATOM   21138 C  C   . TRP   B 1 905  ? 78.48700   77.60200  -3.76500  1.000 49.50816  ?  903  TRP   B C   1 
ATOM   21139 O  O   . TRP   B 1 905  ? 79.63400   78.02000  -3.94800  1.000 64.74611  ?  903  TRP   B O   1 
ATOM   21140 C  CB  . TRP   B 1 905  ? 77.74100   76.10300  -5.62100  1.000 31.68074  ?  903  TRP   B CB  1 
ATOM   21141 C  CG  . TRP   B 1 905  ? 79.17800   75.77300  -5.95000  1.000 42.68027  ?  903  TRP   B CG  1 
ATOM   21142 C  CD1 . TRP   B 1 905  ? 79.81900   75.98100  -7.13900  1.000 49.08321  ?  903  TRP   B CD1 1 
ATOM   21143 C  CD2 . TRP   B 1 905  ? 80.13500   75.14400  -5.08600  1.000 45.73461  ?  903  TRP   B CD2 1 
ATOM   21144 N  NE1 . TRP   B 1 905  ? 81.11600   75.53100  -7.06400  1.000 43.99155  ?  903  TRP   B NE1 1 
ATOM   21145 C  CE2 . TRP   B 1 905  ? 81.33500   75.01400  -5.81400  1.000 49.45901  ?  903  TRP   B CE2 1 
ATOM   21146 C  CE3 . TRP   B 1 905  ? 80.09500   74.68500  -3.76600  1.000 56.63027  ?  903  TRP   B CE3 1 
ATOM   21147 C  CZ2 . TRP   B 1 905  ? 82.48200   74.44400  -5.26500  1.000 52.24621  ?  903  TRP   B CZ2 1 
ATOM   21148 C  CZ3 . TRP   B 1 905  ? 81.23400   74.12100  -3.22400  1.000 49.97686  ?  903  TRP   B CZ3 1 
ATOM   21149 C  CH2 . TRP   B 1 905  ? 82.41100   74.00500  -3.97100  1.000 45.70856  ?  903  TRP   B CH2 1 
ATOM   21150 N  N   . PHE   B 1 906  ? 78.01500   77.26900  -2.56600  1.000 46.20747  ?  904  PHE   B N   1 
ATOM   21151 C  CA  . PHE   B 1 906  ? 78.89400   77.17100  -1.41200  1.000 51.18890  ?  904  PHE   B CA  1 
ATOM   21152 C  C   . PHE   B 1 906  ? 78.50700   75.95400  -0.58600  1.000 49.04792  ?  904  PHE   B C   1 
ATOM   21153 O  O   . PHE   B 1 906  ? 77.34200   75.54800  -0.55000  1.000 47.74974  ?  904  PHE   B O   1 
ATOM   21154 C  CB  . PHE   B 1 906  ? 78.88800   78.45600  -0.55100  1.000 43.62904  ?  904  PHE   B CB  1 
ATOM   21155 C  CG  . PHE   B 1 906  ? 77.59800   78.72000  0.18700   1.000 37.27398  ?  904  PHE   B CG  1 
ATOM   21156 C  CD1 . PHE   B 1 906  ? 77.30200   78.05200  1.36800   1.000 46.62425  ?  904  PHE   B CD1 1 
ATOM   21157 C  CD2 . PHE   B 1 906  ? 76.71200   79.68500  -0.26600  1.000 40.92135  ?  904  PHE   B CD2 1 
ATOM   21158 C  CE1 . PHE   B 1 906  ? 76.13000   78.30700  2.05200   1.000 60.73006  ?  904  PHE   B CE1 1 
ATOM   21159 C  CE2 . PHE   B 1 906  ? 75.53900   79.94800  0.42100   1.000 56.03372  ?  904  PHE   B CE2 1 
ATOM   21160 C  CZ  . PHE   B 1 906  ? 75.25000   79.26000  1.58200   1.000 61.50693  ?  904  PHE   B CZ  1 
ATOM   21161 N  N   . ASP   B 1 907  ? 79.50900   75.37100  0.06900   1.000 48.94786  ?  905  ASP   B N   1 
ATOM   21162 C  CA  . ASP   B 1 907  ? 79.33400   74.19900  0.91700   1.000 52.13628  ?  905  ASP   B CA  1 
ATOM   21163 C  C   . ASP   B 1 907  ? 79.99100   74.48400  2.25800   1.000 54.65666  ?  905  ASP   B C   1 
ATOM   21164 O  O   . ASP   B 1 907  ? 81.18500   74.79400  2.31100   1.000 57.09269  ?  905  ASP   B O   1 
ATOM   21165 C  CB  . ASP   B 1 907  ? 79.94300   72.95200  0.27000   1.000 55.47826  ?  905  ASP   B CB  1 
ATOM   21166 C  CG  . ASP   B 1 907  ? 79.66600   71.68600  1.06200   1.000 71.31119  ?  905  ASP   B CG  1 
ATOM   21167 O  OD1 . ASP   B 1 907  ? 78.78300   71.70900  1.94800   1.000 68.02095  ?  905  ASP   B OD1 1 
ATOM   21168 O  OD2 . ASP   B 1 907  ? 80.33600   70.66400  0.79900   1.000 66.81154  -1 905  ASP   B OD2 1 
ATOM   21169 N  N   . SER   B 1 908  ? 79.21700   74.38000  3.33100   1.000 54.02842  ?  906  SER   B N   1 
ATOM   21170 C  CA  . SER   B 1 908  ? 79.69700   74.63100  4.68100   1.000 48.76602  ?  906  SER   B CA  1 
ATOM   21171 C  C   . SER   B 1 908  ? 79.45100   73.39500  5.54500   1.000 63.77104  ?  906  SER   B C   1 
ATOM   21172 O  O   . SER   B 1 908  ? 79.04900   72.33600  5.05600   1.000 69.42955  ?  906  SER   B O   1 
ATOM   21173 C  CB  . SER   B 1 908  ? 79.02200   75.87500  5.26400   1.000 51.81104  ?  906  SER   B CB  1 
ATOM   21174 O  OG  . SER   B 1 908  ? 79.56200   76.20200  6.53200   1.000 59.20747  ?  906  SER   B OG  1 
ATOM   21175 N  N   . HIS   B 1 909  ? 79.70400   73.53800  6.84300   1.000 68.75336  ?  907  HIS   B N   1 
ATOM   21176 C  CA  . HIS   B 1 909  ? 79.47200   72.48500  7.82000   1.000 57.16469  ?  907  HIS   B CA  1 
ATOM   21177 C  C   . HIS   B 1 909  ? 78.48400   72.99200  8.85900   1.000 57.51651  ?  907  HIS   B C   1 
ATOM   21178 O  O   . HIS   B 1 909  ? 78.52000   74.16800  9.23800   1.000 64.41977  ?  907  HIS   B O   1 
ATOM   21179 C  CB  . HIS   B 1 909  ? 80.78100   72.05500  8.49500   1.000 60.97878  ?  907  HIS   B CB  1 
ATOM   21180 C  CG  . HIS   B 1 909  ? 80.77500   70.64100  8.98700   1.000 65.36690  ?  907  HIS   B CG  1 
ATOM   21181 N  ND1 . HIS   B 1 909  ? 80.07700   70.24200  10.10700  1.000 56.99828  ?  907  HIS   B ND1 1 
ATOM   21182 C  CD2 . HIS   B 1 909  ? 81.38900   69.53000  8.51200   1.000 57.68253  ?  907  HIS   B CD2 1 
ATOM   21183 C  CE1 . HIS   B 1 909  ? 80.25700   68.94800  10.29800  1.000 53.79014  ?  907  HIS   B CE1 1 
ATOM   21184 N  NE2 . HIS   B 1 909  ? 81.04900   68.49200  9.34400   1.000 55.42695  ?  907  HIS   B NE2 1 
ATOM   21185 N  N   . HIS   B 1 910  ? 77.60000   72.10500  9.32100   1.000 56.16962  ?  908  HIS   B N   1 
ATOM   21186 C  CA  . HIS   B 1 910  ? 76.59300   72.50900  10.29400  1.000 57.01317  ?  908  HIS   B CA  1 
ATOM   21187 C  C   . HIS   B 1 910  ? 77.20000   72.91900  11.63000  1.000 65.83082  ?  908  HIS   B C   1 
ATOM   21188 O  O   . HIS   B 1 910  ? 76.48100   73.45600  12.47900  1.000 72.59959  ?  908  HIS   B O   1 
ATOM   21189 C  CB  . HIS   B 1 910  ? 75.57700   71.38500  10.50200  1.000 51.96700  ?  908  HIS   B CB  1 
ATOM   21190 C  CG  . HIS   B 1 910  ? 74.17700   71.87100  10.71200  1.000 50.12921  ?  908  HIS   B CG  1 
ATOM   21191 N  ND1 . HIS   B 1 910  ? 73.10200   71.36700  10.01200  1.000 67.30224  ?  908  HIS   B ND1 1 
ATOM   21192 C  CD2 . HIS   B 1 910  ? 73.67600   72.81700  11.54100  1.000 53.81333  ?  908  HIS   B CD2 1 
ATOM   21193 C  CE1 . HIS   B 1 910  ? 71.99900   71.98200  10.40100  1.000 75.04723  ?  908  HIS   B CE1 1 
ATOM   21194 N  NE2 . HIS   B 1 910  ? 72.31900   72.86600  11.32800  1.000 75.00565  ?  908  HIS   B NE2 1 
ATOM   21195 N  N   . ILE   B 1 911  ? 78.49800   72.68200  11.83500  1.000 62.82995  ?  909  ILE   B N   1 
ATOM   21196 C  CA  . ILE   B 1 911  ? 79.17500   73.21400  13.00800  1.000 59.27830  ?  909  ILE   B CA  1 
ATOM   21197 C  C   . ILE   B 1 911  ? 79.35400   74.72200  12.89700  1.000 62.97162  ?  909  ILE   B C   1 
ATOM   21198 O  O   . ILE   B 1 911  ? 79.63800   75.38800  13.90000  1.000 69.30859  ?  909  ILE   B O   1 
ATOM   21199 C  CB  . ILE   B 1 911  ? 80.52800   72.50400  13.20600  1.000 56.58566  ?  909  ILE   B CB  1 
ATOM   21200 C  CG1 . ILE   B 1 911  ? 80.95900   72.56600  14.67200  1.000 63.40017  ?  909  ILE   B CG1 1 
ATOM   21201 C  CG2 . ILE   B 1 911  ? 81.59200   73.12100  12.30900  1.000 42.32463  ?  909  ILE   B CG2 1 
ATOM   21202 C  CD1 . ILE   B 1 911  ? 81.90000   71.45100  15.07700  1.000 63.24148  ?  909  ILE   B CD1 1 
ATOM   21203 N  N   . LEU   B 1 912  ? 79.18200   75.28000  11.70100  1.000 64.56664  ?  910  LEU   B N   1 
ATOM   21204 C  CA  . LEU   B 1 912  ? 79.32000   76.71100  11.46500  1.000 58.55145  ?  910  LEU   B CA  1 
ATOM   21205 C  C   . LEU   B 1 912  ? 78.03300   77.34800  10.96800  1.000 53.83039  ?  910  LEU   B C   1 
ATOM   21206 O  O   . LEU   B 1 912  ? 77.60400   78.37200  11.51100  1.000 63.23919  ?  910  LEU   B O   1 
ATOM   21207 C  CB  . LEU   B 1 912  ? 80.45400   76.97000  10.45900  1.000 37.77202  ?  910  LEU   B CB  1 
ATOM   21208 C  CG  . LEU   B 1 912  ? 80.57800   78.39200  9.90800   1.000 40.60698  ?  910  LEU   B CG  1 
ATOM   21209 C  CD1 . LEU   B 1 912  ? 80.76600   79.40300  11.02900  1.000 39.05061  ?  910  LEU   B CD1 1 
ATOM   21210 C  CD2 . LEU   B 1 912  ? 81.72200   78.47600  8.91100   1.000 30.00303  ?  910  LEU   B CD2 1 
ATOM   21211 N  N   . LEU   B 1 913  ? 77.40200   76.77300  9.95100   1.000 51.28513  ?  911  LEU   B N   1 
ATOM   21212 C  CA  . LEU   B 1 913  ? 76.24500   77.37900  9.30800   1.000 59.84498  ?  911  LEU   B CA  1 
ATOM   21213 C  C   . LEU   B 1 913  ? 74.97100   76.71600  9.81800   1.000 51.21572  ?  911  LEU   B C   1 
ATOM   21214 O  O   . LEU   B 1 913  ? 74.75700   75.52000  9.59400   1.000 71.25792  ?  911  LEU   B O   1 
ATOM   21215 C  CB  . LEU   B 1 913  ? 76.34700   77.25100  7.78900   1.000 50.78848  ?  911  LEU   B CB  1 
ATOM   21216 C  CG  . LEU   B 1 913  ? 75.79600   78.42600  6.98500   1.000 54.43749  ?  911  LEU   B CG  1 
ATOM   21217 C  CD1 . LEU   B 1 913  ? 76.52300   79.70800  7.35600   1.000 48.80131  ?  911  LEU   B CD1 1 
ATOM   21218 C  CD2 . LEU   B 1 913  ? 75.92400   78.14600  5.50200   1.000 63.48065  ?  911  LEU   B CD2 1 
ATOM   21219 N  N   . ASP   B 1 914  ? 74.13600   77.48800  10.50500  1.000 39.35845  ?  912  ASP   B N   1 
ATOM   21220 C  CA  . ASP   B 1 914  ? 72.82100   77.03100  10.92900  1.000 46.60055  ?  912  ASP   B CA  1 
ATOM   21221 C  C   . ASP   B 1 914  ? 71.75700   77.86700  10.21400  1.000 53.03839  ?  912  ASP   B C   1 
ATOM   21222 O  O   . ASP   B 1 914  ? 72.04100   78.56700  9.23800   1.000 40.28653  ?  912  ASP   B O   1 
ATOM   21223 C  CB  . ASP   B 1 914  ? 72.69000   77.08200  12.45800  1.000 62.93635  ?  912  ASP   B CB  1 
ATOM   21224 C  CG  . ASP   B 1 914  ? 72.48400   78.49100  12.99700  1.000 60.88082  ?  912  ASP   B CG  1 
ATOM   21225 O  OD1 . ASP   B 1 914  ? 72.92200   79.46000  12.34900  1.000 67.08812  ?  912  ASP   B OD1 1 
ATOM   21226 O  OD2 . ASP   B 1 914  ? 71.88200   78.62700  14.08500  1.000 52.96618  -1 912  ASP   B OD2 1 
ATOM   21227 N  N   . GLY   B 1 915  ? 70.52100   77.78600  10.71000  1.000 51.91764  ?  913  GLY   B N   1 
ATOM   21228 C  CA  . GLY   B 1 915  ? 69.42800   78.49200  10.05800  1.000 46.80688  ?  913  GLY   B CA  1 
ATOM   21229 C  C   . GLY   B 1 915  ? 69.61900   79.99600  10.05300  1.000 50.09941  ?  913  GLY   B C   1 
ATOM   21230 O  O   . GLY   B 1 915  ? 69.49900   80.64700  9.01200   1.000 43.96928  ?  913  GLY   B O   1 
ATOM   21231 N  N   . LEU   B 1 916  ? 69.92600   80.57100  11.21800  1.000 49.74163  ?  914  LEU   B N   1 
ATOM   21232 C  CA  . LEU   B 1 916  ? 70.03200   82.02200  11.31600  1.000 45.78896  ?  914  LEU   B CA  1 
ATOM   21233 C  C   . LEU   B 1 916  ? 71.37300   82.54300  10.81500  1.000 43.90292  ?  914  LEU   B C   1 
ATOM   21234 O  O   . LEU   B 1 916  ? 71.44300   83.67600  10.32700  1.000 61.89151  ?  914  LEU   B O   1 
ATOM   21235 C  CB  . LEU   B 1 916  ? 69.79300   82.47800  12.75600  1.000 52.04019  ?  914  LEU   B CB  1 
ATOM   21236 C  CG  . LEU   B 1 916  ? 68.33700   82.73400  13.16200  1.000 71.41672  ?  914  LEU   B CG  1 
ATOM   21237 C  CD1 . LEU   B 1 916  ? 67.68200   83.72200  12.20600  1.000 59.21228  ?  914  LEU   B CD1 1 
ATOM   21238 C  CD2 . LEU   B 1 916  ? 67.53000   81.44200  13.24300  1.000 44.19344  ?  914  LEU   B CD2 1 
ATOM   21239 N  N   . SER   B 1 917  ? 72.44300   81.75000  10.92700  1.000 45.82836  ?  915  SER   B N   1 
ATOM   21240 C  CA  . SER   B 1 917  ? 73.71200   82.16100  10.33200  1.000 53.29650  ?  915  SER   B CA  1 
ATOM   21241 C  C   . SER   B 1 917  ? 73.60600   82.23600  8.81700   1.000 54.74830  ?  915  SER   B C   1 
ATOM   21242 O  O   . SER   B 1 917  ? 74.32600   83.01200  8.17900   1.000 48.30959  ?  915  SER   B O   1 
ATOM   21243 C  CB  . SER   B 1 917  ? 74.83200   81.20100  10.73300  1.000 50.03748  ?  915  SER   B CB  1 
ATOM   21244 O  OG  . SER   B 1 917  ? 74.93700   81.09800  12.14100  1.000 56.07450  ?  915  SER   B OG  1 
ATOM   21245 N  N   . LYS   B 1 918  ? 72.71600   81.43600  8.22700   1.000 50.64911  ?  916  LYS   B N   1 
ATOM   21246 C  CA  . LYS   B 1 918  ? 72.47900   81.51300  6.79200   1.000 48.06310  ?  916  LYS   B CA  1 
ATOM   21247 C  C   . LYS   B 1 918  ? 71.86300   82.85500  6.41800   1.000 42.42299  ?  916  LYS   B C   1 
ATOM   21248 O  O   . LYS   B 1 918  ? 72.28000   83.49800  5.44700   1.000 44.60580  ?  916  LYS   B O   1 
ATOM   21249 C  CB  . LYS   B 1 918  ? 71.57400   80.36000  6.35600   1.000 40.70717  ?  916  LYS   B CB  1 
ATOM   21250 C  CG  . LYS   B 1 918  ? 71.20200   80.37900  4.88900   1.000 34.37331  ?  916  LYS   B CG  1 
ATOM   21251 C  CD  . LYS   B 1 918  ? 69.80400   79.81700  4.67600   1.000 39.07913  ?  916  LYS   B CD  1 
ATOM   21252 C  CE  . LYS   B 1 918  ? 68.75700   80.66800  5.38000   1.000 47.00886  ?  916  LYS   B CE  1 
ATOM   21253 N  NZ  . LYS   B 1 918  ? 67.36900   80.26800  5.01600   1.000 62.96779  ?  916  LYS   B NZ  1 
ATOM   21254 N  N   . SER   B 1 919  ? 70.86200   83.29400  7.18500   1.000 38.90610  ?  917  SER   B N   1 
ATOM   21255 C  CA  . SER   B 1 919  ? 70.22000   84.57400  6.90600   1.000 52.86807  ?  917  SER   B CA  1 
ATOM   21256 C  C   . SER   B 1 919  ? 71.18400   85.73800  7.09600   1.000 59.39902  ?  917  SER   B C   1 
ATOM   21257 O  O   . SER   B 1 919  ? 71.10700   86.73200  6.36500   1.000 71.17515  ?  917  SER   B O   1 
ATOM   21258 C  CB  . SER   B 1 919  ? 68.99200   84.75200  7.80000   1.000 53.40317  ?  917  SER   B CB  1 
ATOM   21259 O  OG  . SER   B 1 919  ? 68.10300   83.65700  7.66700   1.000 55.17523  ?  917  SER   B OG  1 
ATOM   21260 N  N   . ILE   B 1 920  ? 72.09300   85.63200  8.06700   1.000 52.58493  ?  918  ILE   B N   1 
ATOM   21261 C  CA  . ILE   B 1 920  ? 73.08700   86.68000  8.27300   1.000 56.90412  ?  918  ILE   B CA  1 
ATOM   21262 C  C   . ILE   B 1 920  ? 74.08000   86.70400  7.11900   1.000 39.37875  ?  918  ILE   B C   1 
ATOM   21263 O  O   . ILE   B 1 920  ? 74.44200   87.77400  6.61600   1.000 53.79949  ?  918  ILE   B O   1 
ATOM   21264 C  CB  . ILE   B 1 920  ? 73.79000   86.48000  9.62800   1.000 59.56057  ?  918  ILE   B CB  1 
ATOM   21265 C  CG1 . ILE   B 1 920  ? 72.78300   86.62300  10.77100  1.000 54.89799  ?  918  ILE   B CG1 1 
ATOM   21266 C  CG2 . ILE   B 1 920  ? 74.93800   87.46700  9.79100   1.000 57.02123  ?  918  ILE   B CG2 1 
ATOM   21267 C  CD1 . ILE   B 1 920  ? 73.21000   85.93700  12.04800  1.000 55.33139  ?  918  ILE   B CD1 1 
ATOM   21268 N  N   . LEU   B 1 921  ? 74.52900   85.52800  6.67600   1.000 38.81371  ?  919  LEU   B N   1 
ATOM   21269 C  CA  . LEU   B 1 921  ? 75.44400   85.46500  5.54200   1.000 48.43002  ?  919  LEU   B CA  1 
ATOM   21270 C  C   . LEU   B 1 921  ? 74.79600   86.00100  4.27200   1.000 51.92305  ?  919  LEU   B C   1 
ATOM   21271 O  O   . LEU   B 1 921  ? 75.48400   86.56800  3.41500   1.000 48.42192  ?  919  LEU   B O   1 
ATOM   21272 C  CB  . LEU   B 1 921  ? 75.91500   84.02600  5.33000   1.000 36.41216  ?  919  LEU   B CB  1 
ATOM   21273 C  CG  . LEU   B 1 921  ? 77.12400   83.82000  4.41800   1.000 29.02499  ?  919  LEU   B CG  1 
ATOM   21274 C  CD1 . LEU   B 1 921  ? 78.40700   84.19300  5.14500   1.000 56.87641  ?  919  LEU   B CD1 1 
ATOM   21275 C  CD2 . LEU   B 1 921  ? 77.18200   82.38600  3.91700   1.000 31.13108  ?  919  LEU   B CD2 1 
ATOM   21276 N  N   . ALA   B 1 922  ? 73.47800   85.83700  4.13400   1.000 45.49044  ?  920  ALA   B N   1 
ATOM   21277 C  CA  . ALA   B 1 922  ? 72.79400   86.32800  2.94300   1.000 51.12633  ?  920  ALA   B CA  1 
ATOM   21278 C  C   . ALA   B 1 922  ? 72.66500   87.84500  2.96200   1.000 51.76859  ?  920  ALA   B C   1 
ATOM   21279 O  O   . ALA   B 1 922  ? 72.86900   88.50300  1.93500   1.000 50.47508  ?  920  ALA   B O   1 
ATOM   21280 C  CB  . ALA   B 1 922  ? 71.41800   85.67400  2.82100   1.000 46.27884  ?  920  ALA   B CB  1 
ATOM   21281 N  N   . ARG   B 1 923  ? 72.32600   88.42000  4.11900   1.000 55.33074  ?  921  ARG   B N   1 
ATOM   21282 C  CA  . ARG   B 1 923  ? 72.16200   89.86600  4.19700   1.000 50.70834  ?  921  ARG   B CA  1 
ATOM   21283 C  C   . ARG   B 1 923  ? 73.48600   90.60500  4.06500   1.000 48.38358  ?  921  ARG   B C   1 
ATOM   21284 O  O   . ARG   B 1 923  ? 73.49000   91.77400  3.66800   1.000 60.19696  ?  921  ARG   B O   1 
ATOM   21285 C  CB  . ARG   B 1 923  ? 71.47400   90.26000  5.50700   1.000 52.45692  ?  921  ARG   B CB  1 
ATOM   21286 C  CG  . ARG   B 1 923  ? 72.38000   90.33100  6.72600   1.000 58.26335  ?  921  ARG   B CG  1 
ATOM   21287 C  CD  . ARG   B 1 923  ? 71.69000   91.08700  7.85200   1.000 54.90693  ?  921  ARG   B CD  1 
ATOM   21288 N  NE  . ARG   B 1 923  ? 70.41200   90.48100  8.20500   1.000 73.16394  ?  921  ARG   B NE  1 
ATOM   21289 C  CZ  . ARG   B 1 923  ? 70.12800   89.96300  9.39300   1.000 84.95659  ?  921  ARG   B CZ  1 
ATOM   21290 N  NH1 . ARG   B 1 923  ? 70.99600   90.00500  10.39100  1.000 79.63851  ?  921  ARG   B NH1 1 
ATOM   21291 N  NH2 . ARG   B 1 923  ? 68.94100   89.39500  9.58600   1.000 81.52323  ?  921  ARG   B NH2 1 
ATOM   21292 N  N   . GLU   B 1 924  ? 74.60500   89.95300  4.37600   1.000 41.65814  ?  922  GLU   B N   1 
ATOM   21293 C  CA  . GLU   B 1 924  ? 75.89900   90.61400  4.29000   1.000 50.87564  ?  922  GLU   B CA  1 
ATOM   21294 C  C   . GLU   B 1 924  ? 76.52000   90.49100  2.90500   1.000 56.12368  ?  922  GLU   B C   1 
ATOM   21295 O  O   . GLU   B 1 924  ? 77.17900   91.42700  2.44000   1.000 66.37871  ?  922  GLU   B O   1 
ATOM   21296 C  CB  . GLU   B 1 924  ? 76.84800   90.05300  5.35200   1.000 47.99111  ?  922  GLU   B CB  1 
ATOM   21297 C  CG  . GLU   B 1 924  ? 76.37300   90.31600  6.77200   1.000 47.49067  ?  922  GLU   B CG  1 
ATOM   21298 C  CD  . GLU   B 1 924  ? 77.48900   90.23700  7.79000   1.000 49.15396  ?  922  GLU   B CD  1 
ATOM   21299 O  OE1 . GLU   B 1 924  ? 78.65400   90.05000  7.38500   1.000 47.68533  ?  922  GLU   B OE1 1 
ATOM   21300 O  OE2 . GLU   B 1 924  ? 77.20200   90.36800  8.99900   1.000 47.42000  -1 922  GLU   B OE2 1 
ATOM   21301 N  N   . LEU   B 1 925  ? 76.32100   89.35700  2.23000   1.000 48.85907  ?  923  LEU   B N   1 
ATOM   21302 C  CA  . LEU   B 1 925  ? 76.79800   89.23700  0.85700   1.000 45.07257  ?  923  LEU   B CA  1 
ATOM   21303 C  C   . LEU   B 1 925  ? 76.04900   90.19000  -0.06500  1.000 43.52816  ?  923  LEU   B C   1 
ATOM   21304 O  O   . LEU   B 1 925  ? 76.63700   90.75800  -0.99200  1.000 52.04259  ?  923  LEU   B O   1 
ATOM   21305 C  CB  . LEU   B 1 925  ? 76.65700   87.79500  0.37000   1.000 46.50985  ?  923  LEU   B CB  1 
ATOM   21306 C  CG  . LEU   B 1 925  ? 77.35700   87.49400  -0.95600  1.000 45.77135  ?  923  LEU   B CG  1 
ATOM   21307 C  CD1 . LEU   B 1 925  ? 78.85800   87.69800  -0.82100  1.000 41.51278  ?  923  LEU   B CD1 1 
ATOM   21308 C  CD2 . LEU   B 1 925  ? 77.04200   86.08400  -1.42900  1.000 47.24717  ?  923  LEU   B CD2 1 
ATOM   21309 N  N   . GLN   B 1 926  ? 74.75100   90.38200  0.18200   1.000 49.87406  ?  924  GLN   B N   1 
ATOM   21310 C  CA  . GLN   B 1 926  ? 73.97400   91.32700  -0.61300  1.000 61.62527  ?  924  GLN   B CA  1 
ATOM   21311 C  C   . GLN   B 1 926  ? 74.49100   92.74900  -0.43200  1.000 66.10271  ?  924  GLN   B C   1 
ATOM   21312 O  O   . GLN   B 1 926  ? 74.54400   93.52700  -1.39300  1.000 85.04964  ?  924  GLN   B O   1 
ATOM   21313 C  CB  . GLN   B 1 926  ? 72.49800   91.24000  -0.22800  1.000 49.89738  ?  924  GLN   B CB  1 
ATOM   21314 C  CG  . GLN   B 1 926  ? 71.54100   91.26900  -1.40700  1.000 51.60770  ?  924  GLN   B CG  1 
ATOM   21315 C  CD  . GLN   B 1 926  ? 70.09200   91.36500  -0.97500  1.000 59.01043  ?  924  GLN   B CD  1 
ATOM   21316 O  OE1 . GLN   B 1 926  ? 69.79200   91.78800  0.14200   1.000 62.45374  ?  924  GLN   B OE1 1 
ATOM   21317 N  NE2 . GLN   B 1 926  ? 69.18300   90.97200  -1.86000  1.000 59.42762  ?  924  GLN   B NE2 1 
ATOM   21318 N  N   . ALA   B 1 927  ? 74.88200   93.10400  0.79300   1.000 55.73511  ?  925  ALA   B N   1 
ATOM   21319 C  CA  . ALA   B 1 927  ? 75.41500   94.43800  1.04800   1.000 52.51332  ?  925  ALA   B CA  1 
ATOM   21320 C  C   . ALA   B 1 927  ? 76.80600   94.60200  0.44300   1.000 61.79887  ?  925  ALA   B C   1 
ATOM   21321 O  O   . ALA   B 1 927  ? 77.08500   95.60600  -0.22400  1.000 79.79443  ?  925  ALA   B O   1 
ATOM   21322 C  CB  . ALA   B 1 927  ? 75.43700   94.71400  2.55300   1.000 48.91904  ?  925  ALA   B CB  1 
ATOM   21323 N  N   . LEU   B 1 928  ? 77.69200   93.62200  0.66000   1.000 43.57034  ?  926  LEU   B N   1 
ATOM   21324 C  CA  . LEU   B 1 928  ? 79.03700   93.69300  0.09100   1.000 43.54318  ?  926  LEU   B CA  1 
ATOM   21325 C  C   . LEU   B 1 928  ? 79.00800   93.72000  -1.43100  1.000 55.59975  ?  926  LEU   B C   1 
ATOM   21326 O  O   . LEU   B 1 928  ? 79.83400   94.39400  -2.05600  1.000 68.21535  ?  926  LEU   B O   1 
ATOM   21327 C  CB  . LEU   B 1 928  ? 79.87800   92.51200  0.56600   1.000 52.35748  ?  926  LEU   B CB  1 
ATOM   21328 C  CG  . LEU   B 1 928  ? 80.20300   92.49000  2.05900   1.000 44.31265  ?  926  LEU   B CG  1 
ATOM   21329 C  CD1 . LEU   B 1 928  ? 80.56900   91.08300  2.50000   1.000 48.99054  ?  926  LEU   B CD1 1 
ATOM   21330 C  CD2 . LEU   B 1 928  ? 81.31600   93.47800  2.39800   1.000 66.24060  ?  926  LEU   B CD2 1 
ATOM   21331 N  N   . LEU   B 1 929  ? 78.08200   92.97900  -2.04700  1.000 56.50225  ?  927  LEU   B N   1 
ATOM   21332 C  CA  . LEU   B 1 929  ? 77.92600   93.04300  -3.49500  1.000 60.55050  ?  927  LEU   B CA  1 
ATOM   21333 C  C   . LEU   B 1 929  ? 77.28100   94.34600  -3.94300  1.000 63.72205  ?  927  LEU   B C   1 
ATOM   21334 O  O   . LEU   B 1 929  ? 77.51100   94.78500  -5.07500  1.000 60.25297  ?  927  LEU   B O   1 
ATOM   21335 C  CB  . LEU   B 1 929  ? 77.10600   91.85100  -3.99500  1.000 44.63205  ?  927  LEU   B CB  1 
ATOM   21336 C  CG  . LEU   B 1 929  ? 77.84600   90.51500  -4.02300  1.000 40.36734  ?  927  LEU   B CG  1 
ATOM   21337 C  CD1 . LEU   B 1 929  ? 76.88800   89.37100  -4.31100  1.000 34.94602  ?  927  LEU   B CD1 1 
ATOM   21338 C  CD2 . LEU   B 1 929  ? 78.97000   90.55000  -5.04900  1.000 64.78329  ?  927  LEU   B CD2 1 
ATOM   21339 N  N   . GLY   B 1 930  ? 76.47500   94.97400  -3.08800  1.000 58.43762  ?  928  GLY   B N   1 
ATOM   21340 C  CA  . GLY   B 1 930  ? 75.90600   96.26900  -3.40200  1.000 67.81979  ?  928  GLY   B CA  1 
ATOM   21341 C  C   . GLY   B 1 930  ? 76.78700   97.41700  -2.95000  1.000 71.87677  ?  928  GLY   B C   1 
ATOM   21342 O  O   . GLY   B 1 930  ? 76.32500   98.55700  -2.83900  1.000 56.30742  ?  928  GLY   B O   1 
ATOM   21343 N  N   . GLN   B 1 931  ? 78.05800   97.11300  -2.68400  1.000 70.28288  ?  929  GLN   B N   1 
ATOM   21344 C  CA  . GLN   B 1 931  ? 79.06300   98.08800  -2.26000  1.000 58.05568  ?  929  GLN   B CA  1 
ATOM   21345 C  C   . GLN   B 1 931  ? 78.56600   98.91500  -1.07400  1.000 61.36404  ?  929  GLN   B C   1 
ATOM   21346 O  O   . GLN   B 1 931  ? 78.43400   100.13900 -1.13300  1.000 69.60673  ?  929  GLN   B O   1 
ATOM   21347 C  CB  . GLN   B 1 931  ? 79.48600   98.98900  -3.42700  1.000 54.80402  ?  929  GLN   B CB  1 
ATOM   21348 C  CG  . GLN   B 1 931  ? 80.40100   98.31500  -4.44800  1.000 70.89676  ?  929  GLN   B CG  1 
ATOM   21349 C  CD  . GLN   B 1 931  ? 79.66100   97.84100  -5.68700  1.000 93.54211  ?  929  GLN   B CD  1 
ATOM   21350 O  OE1 . GLN   B 1 931  ? 78.69100   98.46300  -6.12100  1.000 104.07839 ?  929  GLN   B OE1 1 
ATOM   21351 N  NE2 . GLN   B 1 931  ? 80.11600   96.73300  -6.26000  1.000 98.32839  ?  929  GLN   B NE2 1 
ATOM   21352 N  N   . GLN   B 1 932  ? 78.28100   98.20900  0.01700   1.000 62.55463  ?  930  GLN   B N   1 
ATOM   21353 C  CA  . GLN   B 1 932  ? 77.83000   98.81700  1.25900   1.000 64.49217  ?  930  GLN   B CA  1 
ATOM   21354 C  C   . GLN   B 1 932  ? 78.82700   98.51000  2.36400   1.000 73.00372  ?  930  GLN   B C   1 
ATOM   21355 O  O   . GLN   B 1 932  ? 79.29600   97.37400  2.49700   1.000 73.88906  ?  930  GLN   B O   1 
ATOM   21356 C  CB  . GLN   B 1 932  ? 76.43400   98.32200  1.65400   1.000 51.02932  ?  930  GLN   B CB  1 
ATOM   21357 C  CG  . GLN   B 1 932  ? 75.33100   99.34100  1.40200   1.000 66.30954  ?  930  GLN   B CG  1 
ATOM   21358 C  CD  . GLN   B 1 932  ? 73.99100   98.70000  1.08300   1.000 91.39332  ?  930  GLN   B CD  1 
ATOM   21359 O  OE1 . GLN   B 1 932  ? 73.73100   97.55500  1.45100   1.000 89.11053  ?  930  GLN   B OE1 1 
ATOM   21360 N  NE2 . GLN   B 1 932  ? 73.13600   99.43900  0.38300   1.000 94.47935  ?  930  GLN   B NE2 1 
ATOM   21361 N  N   . VAL   B 1 933  ? 79.15000   99.53300  3.14900   1.000 84.20000  ?  931  VAL   B N   1 
ATOM   21362 C  CA  . VAL   B 1 933  ? 80.09500   99.39300  4.24900   1.000 91.03905  ?  931  VAL   B CA  1 
ATOM   21363 C  C   . VAL   B 1 933  ? 79.40400   98.63900  5.37900   1.000 87.04779  ?  931  VAL   B C   1 
ATOM   21364 O  O   . VAL   B 1 933  ? 78.48000   99.15700  6.01300   1.000 84.87273  ?  931  VAL   B O   1 
ATOM   21365 C  CB  . VAL   B 1 933  ? 80.60500   100.75500 4.72600   1.000 93.61785  ?  931  VAL   B CB  1 
ATOM   21366 C  CG1 . VAL   B 1 933  ? 81.63500   100.56300 5.82100   1.000 76.68020  ?  931  VAL   B CG1 1 
ATOM   21367 C  CG2 . VAL   B 1 933  ? 81.19000   101.53400 3.55800   1.000 83.83223  ?  931  VAL   B CG2 1 
ATOM   21368 N  N   . LEU   B 1 934  ? 79.84900   97.41100  5.62600   1.000 79.47837  ?  932  LEU   B N   1 
ATOM   21369 C  CA  . LEU   B 1 934  ? 79.34600   96.61200  6.73000   1.000 73.25292  ?  932  LEU   B CA  1 
ATOM   21370 C  C   . LEU   B 1 934  ? 80.05000   96.99500  8.02200   1.000 79.50953  ?  932  LEU   B C   1 
ATOM   21371 O  O   . LEU   B 1 934  ? 81.27700   97.13500  8.06300   1.000 76.84447  ?  932  LEU   B O   1 
ATOM   21372 C  CB  . LEU   B 1 934  ? 79.53700   95.12100  6.46000   1.000 50.24624  ?  932  LEU   B CB  1 
ATOM   21373 C  CG  . LEU   B 1 934  ? 78.38200   94.39800  5.76700   1.000 49.10520  ?  932  LEU   B CG  1 
ATOM   21374 C  CD1 . LEU   B 1 934  ? 78.86900   93.08900  5.21100   1.000 52.47336  ?  932  LEU   B CD1 1 
ATOM   21375 C  CD2 . LEU   B 1 934  ? 77.24500   94.13600  6.72200   1.000 66.87009  ?  932  LEU   B CD2 1 
ATOM   21376 N  N   . SER   B 1 935  ? 79.25600   97.16400  9.07700   1.000 76.37557  ?  933  SER   B N   1 
ATOM   21377 C  CA  . SER   B 1 935  ? 79.79100   97.43200  10.39400  1.000 74.16371  ?  933  SER   B CA  1 
ATOM   21378 C  C   . SER   B 1 935  ? 80.72600   96.30500  10.82900  1.000 77.19988  ?  933  SER   B C   1 
ATOM   21379 O  O   . SER   B 1 935  ? 80.63500   95.17600  10.33900  1.000 90.23119  ?  933  SER   B O   1 
ATOM   21380 C  CB  . SER   B 1 935  ? 78.65000   97.58800  11.40100  1.000 77.95971  ?  933  SER   B CB  1 
ATOM   21381 O  OG  . SER   B 1 935  ? 77.52100   96.81000  11.03500  1.000 71.55205  ?  933  SER   B OG  1 
ATOM   21382 N  N   . PRO   B 1 936  ? 81.66100   96.60400  11.72500  1.000 80.45772  ?  934  PRO   B N   1 
ATOM   21383 C  CA  . PRO   B 1 936  ? 82.48500   95.54900  12.32300  1.000 80.05234  ?  934  PRO   B CA  1 
ATOM   21384 C  C   . PRO   B 1 936  ? 81.70900   94.75400  13.35800  1.000 76.71206  ?  934  PRO   B C   1 
ATOM   21385 O  O   . PRO   B 1 936  ? 80.82800   95.27300  14.04800  1.000 58.11909  ?  934  PRO   B O   1 
ATOM   21386 C  CB  . PRO   B 1 936  ? 83.63100   96.32900  12.98300  1.000 76.83076  ?  934  PRO   B CB  1 
ATOM   21387 C  CG  . PRO   B 1 936  ? 83.63800   97.66000  12.28900  1.000 77.64351  ?  934  PRO   B CG  1 
ATOM   21388 C  CD  . PRO   B 1 936  ? 82.19400   97.94300  12.02300  1.000 79.20634  ?  934  PRO   B CD  1 
ATOM   21389 N  N   . VAL   B 1 937  ? 82.06300   93.47400  13.46700  1.000 65.19578  ?  935  VAL   B N   1 
ATOM   21390 C  CA  . VAL   B 1 937  ? 81.36700   92.60300  14.40300  1.000 57.70487  ?  935  VAL   B CA  1 
ATOM   21391 C  C   . VAL   B 1 937  ? 81.81900   92.90300  15.82900  1.000 78.30580  ?  935  VAL   B C   1 
ATOM   21392 O  O   . VAL   B 1 937  ? 82.90700   93.43600  16.07600  1.000 94.28157  ?  935  VAL   B O   1 
ATOM   21393 C  CB  . VAL   B 1 937  ? 81.58900   91.12500  14.04600  1.000 58.16162  ?  935  VAL   B CB  1 
ATOM   21394 C  CG1 . VAL   B 1 937  ? 82.78700   90.56200  14.79900  1.000 82.97044  ?  935  VAL   B CG1 1 
ATOM   21395 C  CG2 . VAL   B 1 937  ? 80.33700   90.32900  14.33300  1.000 57.34814  ?  935  VAL   B CG2 1 
ATOM   21396 N  N   . GLU   B 1 938  ? 80.95800   92.55600  16.78500  1.000 73.40959  ?  936  GLU   B N   1 
ATOM   21397 C  CA  . GLU   B 1 938  ? 81.17700   92.89800  18.18600  1.000 63.26205  ?  936  GLU   B CA  1 
ATOM   21398 C  C   . GLU   B 1 938  ? 81.61600   91.69400  19.01300  1.000 64.67677  ?  936  GLU   B C   1 
ATOM   21399 O  O   . GLU   B 1 938  ? 82.71500   91.69000  19.57600  1.000 84.89847  ?  936  GLU   B O   1 
ATOM   21400 C  CB  . GLU   B 1 938  ? 79.90600   93.51900  18.77800  1.000 70.80750  ?  936  GLU   B CB  1 
ATOM   21401 C  CG  . GLU   B 1 938  ? 79.96200   95.03300  18.90000  1.000 97.21305  ?  936  GLU   B CG  1 
ATOM   21402 C  CD  . GLU   B 1 938  ? 80.83300   95.49900  20.05600  1.000 116.73615 ?  936  GLU   B CD  1 
ATOM   21403 O  OE1 . GLU   B 1 938  ? 80.34000   95.52400  21.20400  1.000 113.47830 ?  936  GLU   B OE1 1 
ATOM   21404 O  OE2 . GLU   B 1 938  ? 82.01400   95.83700  19.81700  1.000 118.27077 -1 936  GLU   B OE2 1 
ATOM   21405 N  N   . LYS   B 1 939  ? 80.77500   90.67000  19.09600  1.000 63.34902  ?  937  LYS   B N   1 
ATOM   21406 C  CA  . LYS   B 1 939  ? 81.04900   89.51500  19.93400  1.000 61.08525  ?  937  LYS   B CA  1 
ATOM   21407 C  C   . LYS   B 1 939  ? 81.49900   88.32900  19.08700  1.000 60.30984  ?  937  LYS   B C   1 
ATOM   21408 O  O   . LYS   B 1 939  ? 81.53900   88.38200  17.85500  1.000 63.69502  ?  937  LYS   B O   1 
ATOM   21409 C  CB  . LYS   B 1 939  ? 79.81900   89.16200  20.77400  1.000 57.43396  ?  937  LYS   B CB  1 
ATOM   21410 C  CG  . LYS   B 1 939  ? 79.23100   90.33800  21.54200  1.000 60.34603  ?  937  LYS   B CG  1 
ATOM   21411 C  CD  . LYS   B 1 939  ? 80.26600   90.99500  22.44600  1.000 67.43915  ?  937  LYS   B CD  1 
ATOM   21412 C  CE  . LYS   B 1 939  ? 79.68800   92.18500  23.20500  1.000 67.75854  ?  937  LYS   B CE  1 
ATOM   21413 N  NZ  . LYS   B 1 939  ? 78.65800   91.80000  24.21000  1.000 72.47331  ?  937  LYS   B NZ  1 
ATOM   21414 N  N   . THR   B 1 940  ? 81.84600   87.24200  19.77500  1.000 63.46834  ?  938  THR   B N   1 
ATOM   21415 C  CA  . THR   B 1 940  ? 82.35700   86.03000  19.15700  1.000 60.86706  ?  938  THR   B CA  1 
ATOM   21416 C  C   . THR   B 1 940  ? 81.67100   84.81700  19.76900  1.000 61.27477  ?  938  THR   B C   1 
ATOM   21417 O  O   . THR   B 1 940  ? 81.07900   84.89000  20.84900  1.000 68.25645  ?  938  THR   B O   1 
ATOM   21418 C  CB  . THR   B 1 940  ? 83.88600   85.89900  19.32300  1.000 58.68792  ?  938  THR   B CB  1 
ATOM   21419 O  OG1 . THR   B 1 940  ? 84.23200   85.95500  20.71400  1.000 72.18082  ?  938  THR   B OG1 1 
ATOM   21420 C  CG2 . THR   B 1 940  ? 84.60400   87.01400  18.58300  1.000 55.77671  ?  938  THR   B CG2 1 
ATOM   21421 N  N   . TYR   B 1 941  ? 81.75000   83.69100  19.05300  1.000 58.66204  ?  939  TYR   B N   1 
ATOM   21422 C  CA  . TYR   B 1 941  ? 81.15300   82.46200  19.56500  1.000 62.24771  ?  939  TYR   B CA  1 
ATOM   21423 C  C   . TYR   B 1 941  ? 81.91100   81.95200  20.78100  1.000 71.24844  ?  939  TYR   B C   1 
ATOM   21424 O  O   . TYR   B 1 941  ? 81.29900   81.45000  21.72900  1.000 65.96339  ?  939  TYR   B O   1 
ATOM   21425 C  CB  . TYR   B 1 941  ? 81.11200   81.38600  18.47900  1.000 71.68028  ?  939  TYR   B CB  1 
ATOM   21426 C  CG  . TYR   B 1 941  ? 80.11200   80.28300  18.77000  1.000 67.76529  ?  939  TYR   B CG  1 
ATOM   21427 C  CD1 . TYR   B 1 941  ? 78.77700   80.42900  18.40200  1.000 65.00141  ?  939  TYR   B CD1 1 
ATOM   21428 C  CD2 . TYR   B 1 941  ? 80.49700   79.10300  19.42100  1.000 80.50283  ?  939  TYR   B CD2 1 
ATOM   21429 C  CE1 . TYR   B 1 941  ? 77.85100   79.43900  18.66100  1.000 69.99501  ?  939  TYR   B CE1 1 
ATOM   21430 C  CE2 . TYR   B 1 941  ? 79.57000   78.10300  19.69000  1.000 76.66295  ?  939  TYR   B CE2 1 
ATOM   21431 C  CZ  . TYR   B 1 941  ? 78.24500   78.28300  19.29900  1.000 74.24727  ?  939  TYR   B CZ  1 
ATOM   21432 O  OH  . TYR   B 1 941  ? 77.27800   77.32700  19.53700  1.000 84.05400  ?  939  TYR   B OH  1 
ATOM   21433 N  N   . LYS   B 1 942  ? 83.24300   82.07500  20.77300  1.000 70.72181  ?  940  LYS   B N   1 
ATOM   21434 C  CA  . LYS   B 1 942  ? 84.05300   81.63500  21.90500  1.000 66.03215  ?  940  LYS   B CA  1 
ATOM   21435 C  C   . LYS   B 1 942  ? 83.58700   82.27100  23.20700  1.000 66.76852  ?  940  LYS   B C   1 
ATOM   21436 O  O   . LYS   B 1 942  ? 83.70300   81.65900  24.27500  1.000 78.50650  ?  940  LYS   B O   1 
ATOM   21437 C  CB  . LYS   B 1 942  ? 85.53100   81.95800  21.65100  1.000 51.44736  ?  940  LYS   B CB  1 
ATOM   21438 C  CG  . LYS   B 1 942  ? 85.84600   83.44500  21.60400  1.000 67.57336  ?  940  LYS   B CG  1 
ATOM   21439 C  CD  . LYS   B 1 942  ? 87.10100   83.74500  20.79500  1.000 52.60392  ?  940  LYS   B CD  1 
ATOM   21440 C  CE  . LYS   B 1 942  ? 87.47700   85.21900  20.90100  1.000 63.52770  ?  940  LYS   B CE  1 
ATOM   21441 N  NZ  . LYS   B 1 942  ? 88.57500   85.60800  19.97200  1.000 47.19232  ?  940  LYS   B NZ  1 
ATOM   21442 N  N   . SER   B 1 943  ? 83.04900   83.49400  23.13700  1.000 62.10955  ?  941  SER   B N   1 
ATOM   21443 C  CA  . SER   B 1 943  ? 82.49100   84.13000  24.32400  1.000 64.82883  ?  941  SER   B CA  1 
ATOM   21444 C  C   . SER   B 1 943  ? 81.17200   83.48400  24.72500  1.000 71.58389  ?  941  SER   B C   1 
ATOM   21445 O  O   . SER   B 1 943  ? 80.93800   83.22800  25.91200  1.000 86.07741  ?  941  SER   B O   1 
ATOM   21446 C  CB  . SER   B 1 943  ? 82.29800   85.62600  24.07100  1.000 57.98839  ?  941  SER   B CB  1 
ATOM   21447 O  OG  . SER   B 1 943  ? 83.42700   86.18200  23.42100  1.000 62.10830  ?  941  SER   B OG  1 
ATOM   21448 N  N   . PHE   B 1 944  ? 80.29800   83.21200  23.75200  1.000 67.38472  ?  942  PHE   B N   1 
ATOM   21449 C  CA  . PHE   B 1 944  ? 79.03000   82.56100  24.06600  1.000 66.56428  ?  942  PHE   B CA  1 
ATOM   21450 C  C   . PHE   B 1 944  ? 79.25500   81.15400  24.59800  1.000 67.61883  ?  942  PHE   B C   1 
ATOM   21451 O  O   . PHE   B 1 944  ? 78.50500   80.68000  25.45900  1.000 67.62827  ?  942  PHE   B O   1 
ATOM   21452 C  CB  . PHE   B 1 944  ? 78.12800   82.52200  22.83300  1.000 60.29145  ?  942  PHE   B CB  1 
ATOM   21453 C  CG  . PHE   B 1 944  ? 76.83000   81.79600  23.05700  1.000 62.17604  ?  942  PHE   B CG  1 
ATOM   21454 C  CD1 . PHE   B 1 944  ? 75.76300   82.43200  23.67000  1.000 71.27562  ?  942  PHE   B CD1 1 
ATOM   21455 C  CD2 . PHE   B 1 944  ? 76.67800   80.47700  22.65800  1.000 45.89784  ?  942  PHE   B CD2 1 
ATOM   21456 C  CE1 . PHE   B 1 944  ? 74.56800   81.76900  23.88000  1.000 66.89651  ?  942  PHE   B CE1 1 
ATOM   21457 C  CE2 . PHE   B 1 944  ? 75.48600   79.80900  22.86600  1.000 46.21201  ?  942  PHE   B CE2 1 
ATOM   21458 C  CZ  . PHE   B 1 944  ? 74.43000   80.45600  23.47700  1.000 63.14422  ?  942  PHE   B CZ  1 
ATOM   21459 N  N   . ALA   B 1 945  ? 80.28100   80.47000  24.08800  1.000 64.34579  ?  943  ALA   B N   1 
ATOM   21460 C  CA  . ALA   B 1 945  ? 80.59500   79.13000  24.56800  1.000 73.74785  ?  943  ALA   B CA  1 
ATOM   21461 C  C   . ALA   B 1 945  ? 80.85400   79.13900  26.06700  1.000 72.52235  ?  943  ALA   B C   1 
ATOM   21462 O  O   . ALA   B 1 945  ? 80.29900   78.32300  26.81100  1.000 64.25497  ?  943  ALA   B O   1 
ATOM   21463 C  CB  . ALA   B 1 945  ? 81.80100   78.57400  23.81200  1.000 78.97219  ?  943  ALA   B CB  1 
ATOM   21464 N  N   . ARG   B 1 946  ? 81.68800   80.07200  26.53100  1.000 79.83349  ?  944  ARG   B N   1 
ATOM   21465 C  CA  . ARG   B 1 946  ? 81.92900   80.20000  27.96300  1.000 69.49619  ?  944  ARG   B CA  1 
ATOM   21466 C  C   . ARG   B 1 946  ? 80.63700   80.51700  28.70600  1.000 70.01706  ?  944  ARG   B C   1 
ATOM   21467 O  O   . ARG   B 1 946  ? 80.27000   79.81600  29.65400  1.000 81.29610  ?  944  ARG   B O   1 
ATOM   21468 C  CB  . ARG   B 1 946  ? 82.98500   81.27400  28.22400  1.000 51.71440  ?  944  ARG   B CB  1 
ATOM   21469 N  N   . TRP   B 1 947  ? 79.92100   81.56000  28.26900  1.000 56.06728  ?  945  TRP   B N   1 
ATOM   21470 C  CA  . TRP   B 1 947  ? 78.70700   81.98500  28.96400  1.000 65.94424  ?  945  TRP   B CA  1 
ATOM   21471 C  C   . TRP   B 1 947  ? 77.73800   80.82800  29.17000  1.000 76.12650  ?  945  TRP   B C   1 
ATOM   21472 O  O   . TRP   B 1 947  ? 77.16400   80.67400  30.25500  1.000 75.98177  ?  945  TRP   B O   1 
ATOM   21473 C  CB  . TRP   B 1 947  ? 78.02000   83.11100  28.18700  1.000 57.56307  ?  945  TRP   B CB  1 
ATOM   21474 C  CG  . TRP   B 1 947  ? 76.71200   83.55100  28.79300  1.000 64.15613  ?  945  TRP   B CG  1 
ATOM   21475 C  CD1 . TRP   B 1 947  ? 76.51600   84.60000  29.64400  1.000 72.82997  ?  945  TRP   B CD1 1 
ATOM   21476 C  CD2 . TRP   B 1 947  ? 75.42300   82.95200  28.59200  1.000 68.16782  ?  945  TRP   B CD2 1 
ATOM   21477 N  NE1 . TRP   B 1 947  ? 75.18800   84.69100  29.98500  1.000 74.69384  ?  945  TRP   B NE1 1 
ATOM   21478 C  CE2 . TRP   B 1 947  ? 74.49600   83.69100  29.35400  1.000 73.91562  ?  945  TRP   B CE2 1 
ATOM   21479 C  CE3 . TRP   B 1 947  ? 74.96400   81.86400  27.84300  1.000 73.10649  ?  945  TRP   B CE3 1 
ATOM   21480 C  CZ2 . TRP   B 1 947  ? 73.14000   83.37600  29.38800  1.000 82.66748  ?  945  TRP   B CZ2 1 
ATOM   21481 C  CZ3 . TRP   B 1 947  ? 73.61800   81.55200  27.88100  1.000 76.33202  ?  945  TRP   B CZ3 1 
ATOM   21482 C  CH2 . TRP   B 1 947  ? 72.72200   82.30600  28.64700  1.000 82.91398  ?  945  TRP   B CH2 1 
ATOM   21483 N  N   . GLN   B 1 948  ? 77.54700   80.00000  28.14300  1.000 70.66874  ?  946  GLN   B N   1 
ATOM   21484 C  CA  . GLN   B 1 948  ? 76.59100   78.90600  28.25800  1.000 77.40550  ?  946  GLN   B CA  1 
ATOM   21485 C  C   . GLN   B 1 948  ? 77.16900   77.72000  29.01900  1.000 91.73994  ?  946  GLN   B C   1 
ATOM   21486 O  O   . GLN   B 1 948  ? 76.42800   77.02200  29.72200  1.000 99.47292  ?  946  GLN   B O   1 
ATOM   21487 C  CB  . GLN   B 1 948  ? 76.12200   78.46500  26.87200  1.000 74.92918  ?  946  GLN   B CB  1 
ATOM   21488 C  CG  . GLN   B 1 948  ? 74.67100   78.00800  26.84400  1.000 57.87745  ?  946  GLN   B CG  1 
ATOM   21489 C  CD  . GLN   B 1 948  ? 74.35500   77.13700  25.64800  1.000 41.56727  ?  946  GLN   B CD  1 
ATOM   21490 O  OE1 . GLN   B 1 948  ? 75.24200   76.50600  25.07400  1.000 51.88123  ?  946  GLN   B OE1 1 
ATOM   21491 N  NE2 . GLN   B 1 948  ? 73.08400   77.09400  25.26600  1.000 54.00226  ?  946  GLN   B NE2 1 
ATOM   21492 N  N   . ASN   B 1 949  ? 78.47800   77.47500  28.89700  1.000 77.32151  ?  947  ASN   B N   1 
ATOM   21493 C  CA  . ASN   B 1 949  ? 79.08600   76.36200  29.61900  1.000 80.73623  ?  947  ASN   B CA  1 
ATOM   21494 C  C   . ASN   B 1 949  ? 78.95900   76.54900  31.12500  1.000 82.68327  ?  947  ASN   B C   1 
ATOM   21495 O  O   . ASN   B 1 949  ? 78.78200   75.57400  31.86500  1.000 91.09156  ?  947  ASN   B O   1 
ATOM   21496 C  CB  . ASN   B 1 949  ? 80.55200   76.20700  29.21300  1.000 90.73504  ?  947  ASN   B CB  1 
ATOM   21497 C  CG  . ASN   B 1 949  ? 80.71500   75.55000  27.85200  1.000 80.88439  ?  947  ASN   B CG  1 
ATOM   21498 O  OD1 . ASN   B 1 949  ? 79.73400   75.27800  27.16000  1.000 78.32914  ?  947  ASN   B OD1 1 
ATOM   21499 N  ND2 . ASN   B 1 949  ? 81.96000   75.30100  27.46000  1.000 63.87957  ?  947  ASN   B ND2 1 
ATOM   21500 N  N   . GLU   B 1 950  ? 79.03600   77.79400  31.60100  1.000 76.78347  ?  948  GLU   B N   1 
ATOM   21501 C  CA  . GLU   B 1 950  ? 78.86100   78.03500  33.02800  1.000 87.23350  ?  948  GLU   B CA  1 
ATOM   21502 C  C   . GLU   B 1 950  ? 77.39100   78.14300  33.41000  1.000 80.95914  ?  948  GLU   B C   1 
ATOM   21503 O  O   . GLU   B 1 950  ? 77.03700   77.87900  34.56500  1.000 81.26549  ?  948  GLU   B O   1 
ATOM   21504 C  CB  . GLU   B 1 950  ? 79.60200   79.30500  33.45900  1.000 74.73059  ?  948  GLU   B CB  1 
ATOM   21505 C  CG  . GLU   B 1 950  ? 80.80700   79.70500  32.60300  1.000 78.89609  ?  948  GLU   B CG  1 
ATOM   21506 C  CD  . GLU   B 1 950  ? 82.01400   78.78200  32.73400  1.000 98.69324  ?  948  GLU   B CD  1 
ATOM   21507 O  OE1 . GLU   B 1 950  ? 81.88800   77.67400  33.29500  1.000 99.42563  ?  948  GLU   B OE1 1 
ATOM   21508 O  OE2 . GLU   B 1 950  ? 83.10500   79.17600  32.26600  1.000 91.53100  -1 948  GLU   B OE2 1 
ATOM   21509 N  N   . TRP   B 1 951  ? 76.52500   78.52500  32.46500  1.000 69.09968  ?  949  TRP   B N   1 
ATOM   21510 C  CA  . TRP   B 1 951  ? 75.10400   78.64200  32.77700  1.000 71.15276  ?  949  TRP   B CA  1 
ATOM   21511 C  C   . TRP   B 1 951  ? 74.50400   77.29200  33.14100  1.000 89.72069  ?  949  TRP   B C   1 
ATOM   21512 O  O   . TRP   B 1 951  ? 73.50100   77.23000  33.86200  1.000 95.52838  ?  949  TRP   B O   1 
ATOM   21513 C  CB  . TRP   B 1 951  ? 74.34900   79.26200  31.60100  1.000 69.23093  ?  949  TRP   B CB  1 
ATOM   21514 C  CG  . TRP   B 1 951  ? 72.85800   79.20300  31.75700  1.000 66.85976  ?  949  TRP   B CG  1 
ATOM   21515 C  CD1 . TRP   B 1 951  ? 72.07400   80.05800  32.47600  1.000 65.52961  ?  949  TRP   B CD1 1 
ATOM   21516 C  CD2 . TRP   B 1 951  ? 71.97100   78.23300  31.18300  1.000 74.81732  ?  949  TRP   B CD2 1 
ATOM   21517 N  NE1 . TRP   B 1 951  ? 70.75500   79.68200  32.38400  1.000 72.52770  ?  949  TRP   B NE1 1 
ATOM   21518 C  CE2 . TRP   B 1 951  ? 70.66500   78.56500  31.59600  1.000 76.74659  ?  949  TRP   B CE2 1 
ATOM   21519 C  CE3 . TRP   B 1 951  ? 72.15500   77.11800  30.36000  1.000 70.61911  ?  949  TRP   B CE3 1 
ATOM   21520 C  CZ2 . TRP   B 1 951  ? 69.54900   77.82200  31.21400  1.000 65.39427  ?  949  TRP   B CZ2 1 
ATOM   21521 C  CZ3 . TRP   B 1 951  ? 71.04600   76.38300  29.98100  1.000 78.24316  ?  949  TRP   B CZ3 1 
ATOM   21522 C  CH2 . TRP   B 1 951  ? 69.76000   76.73700  30.40900  1.000 60.02671  ?  949  TRP   B CH2 1 
ATOM   21523 N  N   . PHE   B 1 952  ? 75.10900   76.20100  32.66400  1.000 97.29146  ?  950  PHE   B N   1 
ATOM   21524 C  CA  . PHE   B 1 952  ? 74.60800   74.86900  32.97900  1.000 93.63488  ?  950  PHE   B CA  1 
ATOM   21525 C  C   . PHE   B 1 952  ? 74.60300   74.59500  34.47900  1.000 98.67875  ?  950  PHE   B C   1 
ATOM   21526 O  O   . PHE   B 1 952  ? 73.83500   73.74300  34.94000  1.000 90.55432  ?  950  PHE   B O   1 
ATOM   21527 C  CB  . PHE   B 1 952  ? 75.44100   73.81600  32.24800  1.000 109.02076 ?  950  PHE   B CB  1 
ATOM   21528 C  CG  . PHE   B 1 952  ? 75.39900   73.94500  30.75100  1.000 107.06847 ?  950  PHE   B CG  1 
ATOM   21529 C  CD1 . PHE   B 1 952  ? 74.21800   74.26400  30.09700  1.000 90.08415  ?  950  PHE   B CD1 1 
ATOM   21530 C  CD2 . PHE   B 1 952  ? 76.54400   73.75100  29.99700  1.000 98.94631  ?  950  PHE   B CD2 1 
ATOM   21531 C  CE1 . PHE   B 1 952  ? 74.18200   74.38100  28.72000  1.000 87.84238  ?  950  PHE   B CE1 1 
ATOM   21532 C  CE2 . PHE   B 1 952  ? 76.51400   73.86700  28.62100  1.000 86.64419  ?  950  PHE   B CE2 1 
ATOM   21533 C  CZ  . PHE   B 1 952  ? 75.33300   74.18300  27.98200  1.000 86.30315  ?  950  PHE   B CZ  1 
ATOM   21534 N  N   . ALA   B 1 953  ? 75.42200   75.31300  35.25000  1.000 102.46881 ?  951  ALA   B N   1 
ATOM   21535 C  CA  . ALA   B 1 953  ? 75.43000   75.19400  36.70700  1.000 85.02799  ?  951  ALA   B CA  1 
ATOM   21536 C  C   . ALA   B 1 953  ? 74.61900   76.34500  37.30400  1.000 77.99037  ?  951  ALA   B C   1 
ATOM   21537 O  O   . ALA   B 1 953  ? 75.14800   77.40000  37.66200  1.000 86.70174  ?  951  ALA   B O   1 
ATOM   21538 C  CB  . ALA   B 1 953  ? 76.86300   75.19800  37.22000  1.000 61.99354  ?  951  ALA   B CB  1 
ATOM   21539 N  N   . SER   B 1 954  ? 73.31400   76.12700  37.43300  1.000 85.91358  ?  952  SER   B N   1 
ATOM   21540 C  CA  . SER   B 1 954  ? 72.40100   77.15900  37.92200  1.000 90.75569  ?  952  SER   B CA  1 
ATOM   21541 C  C   . SER   B 1 954  ? 71.14400   76.46600  38.43100  1.000 91.28454  ?  952  SER   B C   1 
ATOM   21542 O  O   . SER   B 1 954  ? 71.07100   75.22600  38.46300  1.000 82.61997  ?  952  SER   B O   1 
ATOM   21543 C  CB  . SER   B 1 954  ? 72.07200   78.17200  36.82300  1.000 87.32327  ?  952  SER   B CB  1 
ATOM   21544 O  OG  . SER   B 1 954  ? 71.41300   77.55500  35.73400  1.000 81.32598  ?  952  SER   B OG  1 
ATOM   21545 N  N   . ASP   B 1 955  ? 70.17100   77.26500  38.89100  1.000 114.44171 ?  953  ASP   B N   1 
ATOM   21546 C  CA  . ASP   B 1 955  ? 68.92500   76.58000  39.20100  1.000 113.71199 ?  953  ASP   B CA  1 
ATOM   21547 C  C   . ASP   B 1 955  ? 68.05700   76.49900  37.96900  1.000 117.71627 ?  953  ASP   B C   1 
ATOM   21548 O  O   . ASP   B 1 955  ? 67.18300   75.63400  37.89000  1.000 112.73168 ?  953  ASP   B O   1 
ATOM   21549 C  CB  . ASP   B 1 955  ? 68.17400   77.25500  40.32000  1.000 112.10216 ?  953  ASP   B CB  1 
ATOM   21550 C  CG  . ASP   B 1 955  ? 68.17600   78.72300  40.17100  1.000 125.61006 ?  953  ASP   B CG  1 
ATOM   21551 O  OD1 . ASP   B 1 955  ? 68.74500   79.15500  39.16700  1.000 115.99474 ?  953  ASP   B OD1 1 
ATOM   21552 O  OD2 . ASP   B 1 955  ? 67.64100   79.41100  41.06100  1.000 144.81082 -1 953  ASP   B OD2 1 
ATOM   21553 N  N   . GLU   B 1 956  ? 68.32000   77.37200  36.99200  1.000 116.75993 ?  954  GLU   B N   1 
ATOM   21554 C  CA  . GLU   B 1 956  ? 67.47500   77.48600  35.81000  1.000 100.11598 ?  954  GLU   B CA  1 
ATOM   21555 C  C   . GLU   B 1 956  ? 67.66400   76.29400  34.87900  1.000 97.71289  ?  954  GLU   B C   1 
ATOM   21556 O  O   . GLU   B 1 956  ? 66.68900   75.66500  34.45100  1.000 109.99146 ?  954  GLU   B O   1 
ATOM   21557 C  CB  . GLU   B 1 956  ? 67.79200   78.79900  35.09400  1.000 86.48665  ?  954  GLU   B CB  1 
ATOM   21558 C  CG  . GLU   B 1 956  ? 66.79300   79.21900  34.05200  1.000 87.71954  ?  954  GLU   B CG  1 
ATOM   21559 C  CD  . GLU   B 1 956  ? 67.07100   80.61300  33.52900  1.000 97.75101  ?  954  GLU   B CD  1 
ATOM   21560 O  OE1 . GLU   B 1 956  ? 68.21300   81.09400  33.68800  1.000 96.13780  ?  954  GLU   B OE1 1 
ATOM   21561 O  OE2 . GLU   B 1 956  ? 66.14500   81.23100  32.96400  1.000 103.17858 -1 954  GLU   B OE2 1 
ATOM   21562 N  N   . TYR   B 1 957  ? 68.92000   75.97300  34.55000  1.000 85.76985  ?  955  TYR   B N   1 
ATOM   21563 C  CA  . TYR   B 1 957  ? 69.20500   74.79000  33.74400  1.000 98.05906  ?  955  TYR   B CA  1 
ATOM   21564 C  C   . TYR   B 1 957  ? 68.63000   73.53600  34.38600  1.000 95.12380  ?  955  TYR   B C   1 
ATOM   21565 O  O   . TYR   B 1 957  ? 68.22900   72.60400  33.67800  1.000 92.39948  ?  955  TYR   B O   1 
ATOM   21566 C  CB  . TYR   B 1 957  ? 70.71400   74.64000  33.55000  1.000 93.89378  ?  955  TYR   B CB  1 
ATOM   21567 C  CG  . TYR   B 1 957  ? 71.13200   73.39000  32.80400  1.000 107.40676 ?  955  TYR   B CG  1 
ATOM   21568 C  CD1 . TYR   B 1 957  ? 71.08400   73.34000  31.41800  1.000 109.32574 ?  955  TYR   B CD1 1 
ATOM   21569 C  CD2 . TYR   B 1 957  ? 71.58800   72.26700  33.48400  1.000 111.12137 ?  955  TYR   B CD2 1 
ATOM   21570 C  CE1 . TYR   B 1 957  ? 71.47100   72.20700  30.72900  1.000 118.09381 ?  955  TYR   B CE1 1 
ATOM   21571 C  CE2 . TYR   B 1 957  ? 71.97900   71.12700  32.80100  1.000 123.40499 ?  955  TYR   B CE2 1 
ATOM   21572 C  CZ  . TYR   B 1 957  ? 71.91800   71.10400  31.42400  1.000 125.32831 ?  955  TYR   B CZ  1 
ATOM   21573 O  OH  . TYR   B 1 957  ? 72.30400   69.97500  30.73700  1.000 131.43634 ?  955  TYR   B OH  1 
ATOM   21574 N  N   . GLU   B 1 958  ? 68.58400   73.50100  35.72600  1.000 97.14414  ?  956  GLU   B N   1 
ATOM   21575 C  CA  . GLU   B 1 958  ? 67.96200   72.39200  36.43900  1.000 86.60093  ?  956  GLU   B CA  1 
ATOM   21576 C  C   . GLU   B 1 958  ? 66.44000   72.50100  36.44000  1.000 80.45420  ?  956  GLU   B C   1 
ATOM   21577 O  O   . GLU   B 1 958  ? 65.75800   71.47300  36.38200  1.000 86.43603  ?  956  GLU   B O   1 
ATOM   21578 C  CB  . GLU   B 1 958  ? 68.53300   72.30300  37.85900  1.000 103.09624 ?  956  GLU   B CB  1 
ATOM   21579 C  CG  . GLU   B 1 958  ? 69.87200   71.49600  37.92700  1.000 112.90835 ?  956  GLU   B CG  1 
ATOM   21580 C  CD  . GLU   B 1 958  ? 70.99400   71.96300  36.99600  1.000 111.21487 ?  956  GLU   B CD  1 
ATOM   21581 O  OE1 . GLU   B 1 958  ? 71.08800   73.24800  36.79300  1.000 110.71857 ?  956  GLU   B OE1 1 
ATOM   21582 O  OE2 . GLU   B 1 958  ? 71.71000   71.05200  36.46900  1.000 106.03679 -1 956  GLU   B OE2 1 
ATOM   21583 N  N   . GLN   B 1 959  ? 65.89500   73.72600  36.47600  1.000 91.14629  ?  957  GLN   B N   1 
ATOM   21584 C  CA  . GLN   B 1 959  ? 64.45800   73.91300  36.27400  1.000 91.32216  ?  957  GLN   B CA  1 
ATOM   21585 C  C   . GLN   B 1 959  ? 64.02800   73.47700  34.88000  1.000 86.84987  ?  957  GLN   B C   1 
ATOM   21586 O  O   . GLN   B 1 959  ? 62.86800   73.09900  34.67700  1.000 99.22715  ?  957  GLN   B O   1 
ATOM   21587 C  CB  . GLN   B 1 959  ? 64.07500   75.37800  36.50400  1.000 96.59408  ?  957  GLN   B CB  1 
ATOM   21588 C  CG  . GLN   B 1 959  ? 63.40400   75.64500  37.84000  1.000 105.69218 ?  957  GLN   B CG  1 
ATOM   21589 C  CD  . GLN   B 1 959  ? 64.14700   75.00800  38.99300  1.000 112.59089 ?  957  GLN   B CD  1 
ATOM   21590 O  OE1 . GLN   B 1 959  ? 63.68300   74.03200  39.58000  1.000 112.28979 ?  957  GLN   B OE1 1 
ATOM   21591 N  NE2 . GLN   B 1 959  ? 65.30700   75.56000  39.32500  1.000 111.29645 ?  957  GLN   B NE2 1 
ATOM   21592 N  N   . GLN   B 1 960  ? 64.93800   73.52900  33.90700  1.000 87.03409  ?  958  GLN   B N   1 
ATOM   21593 C  CA  . GLN   B 1 960  ? 64.67600   72.99000  32.58000  1.000 77.22076  ?  958  GLN   B CA  1 
ATOM   21594 C  C   . GLN   B 1 960  ? 64.94300   71.48800  32.50800  1.000 92.89665  ?  958  GLN   B C   1 
ATOM   21595 O  O   . GLN   B 1 960  ? 64.13600   70.74800  31.93700  1.000 89.48188  ?  958  GLN   B O   1 
ATOM   21596 C  CB  . GLN   B 1 960  ? 65.52100   73.73300  31.54600  1.000 79.24567  ?  958  GLN   B CB  1 
ATOM   21597 C  CG  . GLN   B 1 960  ? 65.32200   75.23000  31.56800  1.000 79.35453  ?  958  GLN   B CG  1 
ATOM   21598 C  CD  . GLN   B 1 960  ? 65.78700   75.90200  30.29400  1.000 75.09586  ?  958  GLN   B CD  1 
ATOM   21599 O  OE1 . GLN   B 1 960  ? 65.61700   77.11200  30.13400  1.000 53.90833  ?  958  GLN   B OE1 1 
ATOM   21600 N  NE2 . GLN   B 1 960  ? 66.35600   75.12100  29.36700  1.000 89.57293  ?  958  GLN   B NE2 1 
ATOM   21601 N  N   . ILE   B 1 961  ? 66.04800   71.01800  33.09900  1.000 88.35617  ?  959  ILE   B N   1 
ATOM   21602 C  CA  . ILE   B 1 961  ? 66.33700   69.58400  33.13000  1.000 82.29350  ?  959  ILE   B CA  1 
ATOM   21603 C  C   . ILE   B 1 961  ? 65.22900   68.82000  33.84600  1.000 81.29331  ?  959  ILE   B C   1 
ATOM   21604 O  O   . ILE   B 1 961  ? 64.98000   67.64500  33.54500  1.000 77.43319  ?  959  ILE   B O   1 
ATOM   21605 C  CB  . ILE   B 1 961  ? 67.71400   69.33500  33.78300  1.000 73.52752  ?  959  ILE   B CB  1 
ATOM   21606 C  CG1 . ILE   B 1 961  ? 68.47400   68.22700  33.05000  1.000 70.17524  ?  959  ILE   B CG1 1 
ATOM   21607 C  CG2 . ILE   B 1 961  ? 67.56600   68.98000  35.26200  1.000 80.12323  ?  959  ILE   B CG2 1 
ATOM   21608 C  CD1 . ILE   B 1 961  ? 69.87000   67.98900  33.59000  1.000 78.95050  ?  959  ILE   B CD1 1 
ATOM   21609 N  N   . ALA   B 1 962  ? 64.54700   69.46700  34.79600  1.000 83.09670  ?  960  ALA   B N   1 
ATOM   21610 C  CA  . ALA   B 1 962  ? 63.46900   68.80100  35.51800  1.000 96.45382  ?  960  ALA   B CA  1 
ATOM   21611 C  C   . ALA   B 1 962  ? 62.26400   68.57200  34.61800  1.000 99.13574  ?  960  ALA   B C   1 
ATOM   21612 O  O   . ALA   B 1 962  ? 61.56700   67.56000  34.75400  1.000 102.15456 ?  960  ALA   B O   1 
ATOM   21613 C  CB  . ALA   B 1 962  ? 63.07100   69.61900  36.74600  1.000 74.81428  ?  960  ALA   B CB  1 
ATOM   21614 N  N   . TYR   B 1 963  ? 62.00200   69.50300  33.69700  1.000 87.67009  ?  961  TYR   B N   1 
ATOM   21615 C  CA  . TYR   B 1 963  ? 60.86300   69.36500  32.79600  1.000 88.94319  ?  961  TYR   B CA  1 
ATOM   21616 C  C   . TYR   B 1 963  ? 60.89400   68.03600  32.05900  1.000 101.03905 ?  961  TYR   B C   1 
ATOM   21617 O  O   . TYR   B 1 963  ? 59.87100   67.35400  31.95100  1.000 109.39764 ?  961  TYR   B O   1 
ATOM   21618 C  CB  . TYR   B 1 963  ? 60.84200   70.52200  31.79800  1.000 72.68520  ?  961  TYR   B CB  1 
ATOM   21619 C  CG  . TYR   B 1 963  ? 59.82100   70.37500  30.69000  1.000 77.40846  ?  961  TYR   B CG  1 
ATOM   21620 C  CD1 . TYR   B 1 963  ? 58.45900   70.38200  30.96500  1.000 77.83662  ?  961  TYR   B CD1 1 
ATOM   21621 C  CD2 . TYR   B 1 963  ? 60.22000   70.24600  29.36500  1.000 79.52760  ?  961  TYR   B CD2 1 
ATOM   21622 C  CE1 . TYR   B 1 963  ? 57.52300   70.25300  29.95200  1.000 85.80415  ?  961  TYR   B CE1 1 
ATOM   21623 C  CE2 . TYR   B 1 963  ? 59.29200   70.11800  28.34600  1.000 86.75671  ?  961  TYR   B CE2 1 
ATOM   21624 C  CZ  . TYR   B 1 963  ? 57.94500   70.12300  28.64500  1.000 92.72456  ?  961  TYR   B CZ  1 
ATOM   21625 O  OH  . TYR   B 1 963  ? 57.02000   69.99700  27.63200  1.000 77.73537  ?  961  TYR   B OH  1 
ATOM   21626 N  N   . TRP   B 1 964  ? 62.06700   67.64200  31.56200  1.000 88.35438  ?  962  TRP   B N   1 
ATOM   21627 C  CA  . TRP   B 1 964  ? 62.17300   66.41000  30.79000  1.000 89.54098  ?  962  TRP   B CA  1 
ATOM   21628 C  C   . TRP   B 1 964  ? 62.33700   65.19600  31.69400  1.000 91.34334  ?  962  TRP   B C   1 
ATOM   21629 O  O   . TRP   B 1 964  ? 61.76400   64.13500  31.42000  1.000 88.90240  ?  962  TRP   B O   1 
ATOM   21630 C  CB  . TRP   B 1 964  ? 63.34000   66.51600  29.81100  1.000 100.42818 ?  962  TRP   B CB  1 
ATOM   21631 C  CG  . TRP   B 1 964  ? 63.44600   67.87100  29.18600  1.000 99.51301  ?  962  TRP   B CG  1 
ATOM   21632 C  CD1 . TRP   B 1 964  ? 64.13900   68.94000  29.66900  1.000 97.24859  ?  962  TRP   B CD1 1 
ATOM   21633 C  CD2 . TRP   B 1 964  ? 62.83800   68.30700  27.96300  1.000 91.73372  ?  962  TRP   B CD2 1 
ATOM   21634 N  NE1 . TRP   B 1 964  ? 64.00200   70.01600  28.82600  1.000 77.25043  ?  962  TRP   B NE1 1 
ATOM   21635 C  CE2 . TRP   B 1 964  ? 63.20800   69.65300  27.77000  1.000 75.21902  ?  962  TRP   B CE2 1 
ATOM   21636 C  CE3 . TRP   B 1 964  ? 62.01800   67.69000  27.01300  1.000 87.96750  ?  962  TRP   B CE3 1 
ATOM   21637 C  CZ2 . TRP   B 1 964  ? 62.78600   70.39200  26.66700  1.000 68.85076  ?  962  TRP   B CZ2 1 
ATOM   21638 C  CZ3 . TRP   B 1 964  ? 61.60100   68.42600  25.91800  1.000 70.42521  ?  962  TRP   B CZ3 1 
ATOM   21639 C  CH2 . TRP   B 1 964  ? 61.98600   69.76300  25.75400  1.000 66.33378  ?  962  TRP   B CH2 1 
ATOM   21640 N  N   . LYS   B 1 965  ? 63.11200   65.33100  32.77400  1.000 95.15734  ?  963  LYS   B N   1 
ATOM   21641 C  CA  . LYS   B 1 965  ? 63.25300   64.24000  33.73200  1.000 93.20382  ?  963  LYS   B CA  1 
ATOM   21642 C  C   . LYS   B 1 965  ? 61.92400   63.87300  34.37800  1.000 81.06248  ?  963  LYS   B C   1 
ATOM   21643 O  O   . LYS   B 1 965  ? 61.79500   62.77400  34.92900  1.000 77.85870  ?  963  LYS   B O   1 
ATOM   21644 C  CB  . LYS   B 1 965  ? 64.27900   64.61400  34.80300  1.000 68.55005  ?  963  LYS   B CB  1 
ATOM   21645 C  CG  . LYS   B 1 965  ? 65.45500   63.65600  34.89900  1.000 72.09977  ?  963  LYS   B CG  1 
ATOM   21646 C  CD  . LYS   B 1 965  ? 66.58200   64.24500  35.73200  1.000 82.57860  ?  963  LYS   B CD  1 
ATOM   21647 C  CE  . LYS   B 1 965  ? 67.80100   63.33600  35.73200  1.000 75.40412  ?  963  LYS   B CE  1 
ATOM   21648 N  NZ  . LYS   B 1 965  ? 68.98300   63.99000  36.36000  1.000 66.79968  ?  963  LYS   B NZ  1 
ATOM   21649 N  N   . THR   B 1 966  ? 60.93600   64.76600  34.31900  1.000 75.83505  ?  964  THR   B N   1 
ATOM   21650 C  CA  . THR   B 1 966  ? 59.58600   64.49400  34.79400  1.000 88.34522  ?  964  THR   B CA  1 
ATOM   21651 C  C   . THR   B 1 966  ? 58.59200   64.32700  33.65100  1.000 86.14771  ?  964  THR   B C   1 
ATOM   21652 O  O   . THR   B 1 966  ? 57.38000   64.35300  33.88800  1.000 80.17956  ?  964  THR   B O   1 
ATOM   21653 C  CB  . THR   B 1 966  ? 59.11800   65.61100  35.73100  1.000 104.19782 ?  964  THR   B CB  1 
ATOM   21654 O  OG1 . THR   B 1 966  ? 59.07500   66.85300  35.01500  1.000 102.60579 ?  964  THR   B OG1 1 
ATOM   21655 C  CG2 . THR   B 1 966  ? 60.06200   65.74700  36.91900  1.000 102.90515 ?  964  THR   B CG2 1 
ATOM   21656 N  N   . LEU   B 1 967  ? 59.07300   64.15500  32.41900  1.000 87.83420  ?  965  LEU   B N   1 
ATOM   21657 C  CA  . LEU   B 1 967  ? 58.19700   64.02700  31.26000  1.000 80.81346  ?  965  LEU   B CA  1 
ATOM   21658 C  C   . LEU   B 1 967  ? 58.63700   62.87600  30.36300  1.000 85.87204  ?  965  LEU   B C   1 
ATOM   21659 O  O   . LEU   B 1 967  ? 57.80000   62.20000  29.75700  1.000 88.52523  ?  965  LEU   B O   1 
ATOM   21660 C  CB  . LEU   B 1 967  ? 58.17500   65.33500  30.46500  1.000 68.81318  ?  965  LEU   B CB  1 
ATOM   21661 C  CG  . LEU   B 1 967  ? 57.48100   65.37800  29.10100  1.000 76.65102  ?  965  LEU   B CG  1 
ATOM   21662 C  CD1 . LEU   B 1 967  ? 55.98100   65.57500  29.25400  1.000 63.11160  ?  965  LEU   B CD1 1 
ATOM   21663 C  CD2 . LEU   B 1 967  ? 58.08600   66.46900  28.22800  1.000 66.48682  ?  965  LEU   B CD2 1 
ATOM   21664 N  N   . LEU   B 1 968  ? 59.94700   62.64500  30.27500  1.000 81.83894  ?  966  LEU   B N   1 
ATOM   21665 C  CA  . LEU   B 1 968  ? 60.51000   61.66300  29.35700  1.000 97.42473  ?  966  LEU   B CA  1 
ATOM   21666 C  C   . LEU   B 1 968  ? 61.08000   60.43900  30.05600  1.000 105.77906 ?  966  LEU   B C   1 
ATOM   21667 O  O   . LEU   B 1 968  ? 61.63500   59.56300  29.38300  1.000 107.19507 ?  966  LEU   B O   1 
ATOM   21668 C  CB  . LEU   B 1 968  ? 61.60400   62.31200  28.49800  1.000 78.21480  ?  966  LEU   B CB  1 
ATOM   21669 C  CG  . LEU   B 1 968  ? 61.22600   63.56800  27.71400  1.000 78.90358  ?  966  LEU   B CG  1 
ATOM   21670 C  CD1 . LEU   B 1 968  ? 62.41700   64.07900  26.92000  1.000 71.86213  ?  966  LEU   B CD1 1 
ATOM   21671 C  CD2 . LEU   B 1 968  ? 60.05000   63.29300  26.79600  1.000 95.25889  ?  966  LEU   B CD2 1 
ATOM   21672 N  N   . GLN   B 1 969  ? 60.96700   60.35000  31.37800  1.000 105.59431 ?  967  GLN   B N   1 
ATOM   21673 C  CA  . GLN   B 1 969  ? 61.52000   59.22100  32.11600  1.000 98.69039  ?  967  GLN   B CA  1 
ATOM   21674 C  C   . GLN   B 1 969  ? 60.58200   58.02000  32.17500  1.000 101.82592 ?  967  GLN   B C   1 
ATOM   21675 O  O   . GLN   B 1 969  ? 61.03800   56.92300  32.51800  1.000 95.98524  ?  967  GLN   B O   1 
ATOM   21676 C  CB  . GLN   B 1 969  ? 61.88900   59.65300  33.54000  1.000 74.36106  ?  967  GLN   B CB  1 
ATOM   21677 N  N   . GLY   B 1 970  ? 59.30300   58.18700  31.85000  1.000 87.42132  ?  968  GLY   B N   1 
ATOM   21678 C  CA  . GLY   B 1 970  ? 58.37200   57.07700  31.92400  1.000 85.94677  ?  968  GLY   B CA  1 
ATOM   21679 C  C   . GLY   B 1 970  ? 58.16600   56.35900  30.60400  1.000 91.45603  ?  968  GLY   B C   1 
ATOM   21680 O  O   . GLY   B 1 970  ? 59.11500   56.15500  29.84100  1.000 88.30039  ?  968  GLY   B O   1 
ATOM   21681 N  N   . GLU   B 1 971  ? 56.92300   55.97000  30.32300  1.000 87.41290  ?  969  GLU   B N   1 
ATOM   21682 C  CA  . GLU   B 1 971  ? 56.60400   55.27000  29.08500  1.000 82.31816  ?  969  GLU   B CA  1 
ATOM   21683 C  C   . GLU   B 1 971  ? 56.65100   56.25100  27.92000  1.000 89.82382  ?  969  GLU   B C   1 
ATOM   21684 O  O   . GLU   B 1 971  ? 55.78800   57.12600  27.79600  1.000 89.25177  ?  969  GLU   B O   1 
ATOM   21685 C  CB  . GLU   B 1 971  ? 55.23000   54.60900  29.18600  1.000 96.36544  ?  969  GLU   B CB  1 
ATOM   21686 N  N   . LEU   B 1 972  ? 57.65100   56.10200  27.06300  1.000 92.27146  ?  970  LEU   B N   1 
ATOM   21687 C  CA  . LEU   B 1 972  ? 57.80400   56.99100  25.91900  1.000 82.01779  ?  970  LEU   B CA  1 
ATOM   21688 C  C   . LEU   B 1 972  ? 56.94000   56.50200  24.76300  1.000 71.24012  ?  970  LEU   B C   1 
ATOM   21689 O  O   . LEU   B 1 972  ? 56.96300   55.30800  24.44400  1.000 63.60525  ?  970  LEU   B O   1 
ATOM   21690 C  CB  . LEU   B 1 972  ? 59.26500   57.06000  25.49000  1.000 80.45163  ?  970  LEU   B CB  1 
ATOM   21691 C  CG  . LEU   B 1 972  ? 60.22100   57.63000  26.53900  1.000 82.49216  ?  970  LEU   B CG  1 
ATOM   21692 C  CD1 . LEU   B 1 972  ? 61.63100   57.09500  26.33600  1.000 66.16620  ?  970  LEU   B CD1 1 
ATOM   21693 C  CD2 . LEU   B 1 972  ? 60.20700   59.15100  26.49200  1.000 69.92083  ?  970  LEU   B CD2 1 
ATOM   21694 N  N   . PRO   B 1 973  ? 56.16500   57.38000  24.12500  1.000 74.38355  ?  971  PRO   B N   1 
ATOM   21695 C  CA  . PRO   B 1 973  ? 55.32900   56.94300  23.00200  1.000 74.14059  ?  971  PRO   B CA  1 
ATOM   21696 C  C   . PRO   B 1 973  ? 56.17400   56.41400  21.85500  1.000 84.10219  ?  971  PRO   B C   1 
ATOM   21697 O  O   . PRO   B 1 973  ? 57.32400   56.81400  21.65900  1.000 99.33872  ?  971  PRO   B O   1 
ATOM   21698 C  CB  . PRO   B 1 973  ? 54.57500   58.21700  22.60000  1.000 68.77991  ?  971  PRO   B CB  1 
ATOM   21699 C  CG  . PRO   B 1 973  ? 54.63100   59.09300  23.81000  1.000 75.49806  ?  971  PRO   B CG  1 
ATOM   21700 C  CD  . PRO   B 1 973  ? 55.94900   58.79700  24.45800  1.000 70.82565  ?  971  PRO   B CD  1 
ATOM   21701 N  N   . ALA   B 1 974  ? 55.58800   55.49400  21.09700  1.000 77.94115  ?  972  ALA   B N   1 
ATOM   21702 C  CA  . ALA   B 1 974  ? 56.24100   54.87900  19.94800  1.000 80.05683  ?  972  ALA   B CA  1 
ATOM   21703 C  C   . ALA   B 1 974  ? 55.42000   55.19500  18.70900  1.000 79.12958  ?  972  ALA   B C   1 
ATOM   21704 O  O   . ALA   B 1 974  ? 54.27600   54.74400  18.58600  1.000 72.76134  ?  972  ALA   B O   1 
ATOM   21705 C  CB  . ALA   B 1 974  ? 56.38600   53.37000  20.14200  1.000 73.22210  ?  972  ALA   B CB  1 
ATOM   21706 N  N   . VAL   B 1 975  ? 55.99400   55.97400  17.80000  1.000 82.55837  ?  973  VAL   B N   1 
ATOM   21707 C  CA  . VAL   B 1 975  ? 55.35200   56.25800  16.52300  1.000 69.20335  ?  973  VAL   B CA  1 
ATOM   21708 C  C   . VAL   B 1 975  ? 55.84600   55.22700  15.51200  1.000 77.07012  ?  973  VAL   B C   1 
ATOM   21709 O  O   . VAL   B 1 975  ? 57.04700   55.11900  15.24000  1.000 83.18341  ?  973  VAL   B O   1 
ATOM   21710 C  CB  . VAL   B 1 975  ? 55.60700   57.70600  16.07000  1.000 67.85012  ?  973  VAL   B CB  1 
ATOM   21711 C  CG1 . VAL   B 1 975  ? 57.05900   57.96000  15.64800  1.000 68.05112  ?  973  VAL   B CG1 1 
ATOM   21712 C  CG2 . VAL   B 1 975  ? 54.62700   58.10600  14.97100  1.000 71.03040  ?  973  VAL   B CG2 1 
ATOM   21713 N  N   . GLN   B 1 976  ? 54.92400   54.41200  15.01300  1.000 74.65047  ?  974  GLN   B N   1 
ATOM   21714 C  CA  . GLN   B 1 976  ? 55.23700   53.32100  14.09600  1.000 74.35387  ?  974  GLN   B CA  1 
ATOM   21715 C  C   . GLN   B 1 976  ? 54.72900   53.72400  12.71900  1.000 73.76209  ?  974  GLN   B C   1 
ATOM   21716 O  O   . GLN   B 1 976  ? 53.59100   53.43700  12.34500  1.000 73.83269  ?  974  GLN   B O   1 
ATOM   21717 C  CB  . GLN   B 1 976  ? 54.62400   52.00800  14.57100  1.000 67.73006  ?  974  GLN   B CB  1 
ATOM   21718 C  CG  . GLN   B 1 976  ? 55.53500   51.20100  15.48000  1.000 81.29876  ?  974  GLN   B CG  1 
ATOM   21719 C  CD  . GLN   B 1 976  ? 54.78300   50.51500  16.60300  1.000 107.43670 ?  974  GLN   B CD  1 
ATOM   21720 O  OE1 . GLN   B 1 976  ? 53.82000   51.06000  17.14500  1.000 96.13139  ?  974  GLN   B OE1 1 
ATOM   21721 N  NE2 . GLN   B 1 976  ? 55.21900   49.31400  16.95900  1.000 102.07484 ?  974  GLN   B NE2 1 
ATOM   21722 N  N   . LEU   B 1 977  ? 55.58300   54.41200  11.97200  1.000 72.16142  ?  975  LEU   B N   1 
ATOM   21723 C  CA  . LEU   B 1 977  ? 55.23300   54.81600  10.62700  1.000 70.97857  ?  975  LEU   B CA  1 
ATOM   21724 C  C   . LEU   B 1 977  ? 55.24300   53.61100  9.69200   1.000 70.87902  ?  975  LEU   B C   1 
ATOM   21725 O  O   . LEU   B 1 977  ? 56.03500   52.68100  9.87000   1.000 55.89509  ?  975  LEU   B O   1 
ATOM   21726 C  CB  . LEU   B 1 977  ? 56.20700   55.86900  10.12000  1.000 60.26668  ?  975  LEU   B CB  1 
ATOM   21727 C  CG  . LEU   B 1 977  ? 56.07100   57.24200  10.75900  1.000 62.45421  ?  975  LEU   B CG  1 
ATOM   21728 C  CD1 . LEU   B 1 977  ? 57.40200   57.92100  10.65300  1.000 48.25053  ?  975  LEU   B CD1 1 
ATOM   21729 C  CD2 . LEU   B 1 977  ? 55.01600   58.05200  10.04200  1.000 59.27397  ?  975  LEU   B CD2 1 
ATOM   21730 N  N   . PRO   B 1 978  ? 54.36600   53.60100  8.68900   1.000 61.90703  ?  976  PRO   B N   1 
ATOM   21731 C  CA  . PRO   B 1 978  ? 54.39700   52.51800  7.69900   1.000 50.47271  ?  976  PRO   B CA  1 
ATOM   21732 C  C   . PRO   B 1 978  ? 55.68200   52.54400  6.88900   1.000 58.91440  ?  976  PRO   B C   1 
ATOM   21733 O  O   . PRO   B 1 978  ? 55.74800   53.19300  5.84300   1.000 71.24167  ?  976  PRO   B O   1 
ATOM   21734 C  CB  . PRO   B 1 978  ? 53.16800   52.80300  6.82700   1.000 47.93773  ?  976  PRO   B CB  1 
ATOM   21735 C  CG  . PRO   B 1 978  ? 52.92100   54.26800  6.99200   1.000 61.89401  ?  976  PRO   B CG  1 
ATOM   21736 C  CD  . PRO   B 1 978  ? 53.30600   54.58300  8.40700   1.000 66.63599  ?  976  PRO   B CD  1 
ATOM   21737 N  N   . THR   B 1 979  ? 56.71200   51.85900  7.37200   1.000 51.32782  ?  977  THR   B N   1 
ATOM   21738 C  CA  . THR   B 1 979  ? 58.00100   51.80500  6.70300   1.000 43.42879  ?  977  THR   B CA  1 
ATOM   21739 C  C   . THR   B 1 979  ? 58.25300   50.40500  6.16100   1.000 45.99401  ?  977  THR   B C   1 
ATOM   21740 O  O   . THR   B 1 979  ? 57.62900   49.42700  6.58000   1.000 58.05795  ?  977  THR   B O   1 
ATOM   21741 C  CB  . THR   B 1 979  ? 59.13900   52.19900  7.65300   1.000 52.46768  ?  977  THR   B CB  1 
ATOM   21742 O  OG1 . THR   B 1 979  ? 59.33200   51.16600  8.62700   1.000 63.92869  ?  977  THR   B OG1 1 
ATOM   21743 C  CG2 . THR   B 1 979  ? 58.81200   53.50200  8.36300   1.000 63.70281  ?  977  THR   B CG2 1 
ATOM   21744 N  N   . LYS   B 1 980  ? 59.18300   50.32300  5.21400   1.000 57.58454  ?  978  LYS   B N   1 
ATOM   21745 C  CA  . LYS   B 1 980  ? 59.64100   49.03500  4.72100   1.000 55.90925  ?  978  LYS   B CA  1 
ATOM   21746 C  C   . LYS   B 1 980  ? 60.48200   48.34900  5.79700   1.000 61.14099  ?  978  LYS   B C   1 
ATOM   21747 O  O   . LYS   B 1 980  ? 60.73400   48.89900  6.87300   1.000 66.14207  ?  978  LYS   B O   1 
ATOM   21748 C  CB  . LYS   B 1 980  ? 60.41900   49.22000  3.41900   1.000 50.99043  ?  978  LYS   B CB  1 
ATOM   21749 C  CG  . LYS   B 1 980  ? 59.56200   49.76700  2.28400   1.000 54.97186  ?  978  LYS   B CG  1 
ATOM   21750 C  CD  . LYS   B 1 980  ? 60.38700   50.45700  1.20600   1.000 68.10564  ?  978  LYS   B CD  1 
ATOM   21751 C  CE  . LYS   B 1 980  ? 61.24500   49.47600  0.42600   1.000 73.12982  ?  978  LYS   B CE  1 
ATOM   21752 N  NZ  . LYS   B 1 980  ? 61.87300   50.12600  -0.76000  1.000 69.72533  ?  978  LYS   B NZ  1 
ATOM   21753 N  N   . LYS   B 1 981  ? 60.90600   47.11900  5.50700   1.000 63.02530  ?  979  LYS   B N   1 
ATOM   21754 C  CA  . LYS   B 1 981  ? 61.71000   46.35400  6.45300   1.000 70.55907  ?  979  LYS   B CA  1 
ATOM   21755 C  C   . LYS   B 1 981  ? 62.94000   47.14800  6.86900   1.000 77.12295  ?  979  LYS   B C   1 
ATOM   21756 O  O   . LYS   B 1 981  ? 63.80500   47.45100  6.04100   1.000 67.37916  ?  979  LYS   B O   1 
ATOM   21757 C  CB  . LYS   B 1 981  ? 62.11900   45.01600  5.83300   1.000 69.53186  ?  979  LYS   B CB  1 
ATOM   21758 N  N   . ARG   B 1 982  ? 63.00300   47.49500  8.15200   1.000 81.14989  ?  980  ARG   B N   1 
ATOM   21759 C  CA  . ARG   B 1 982  ? 64.02900   48.41300  8.62500   1.000 65.67422  ?  980  ARG   B CA  1 
ATOM   21760 C  C   . ARG   B 1 982  ? 65.41800   47.80800  8.43700   1.000 52.58588  ?  980  ARG   B C   1 
ATOM   21761 O  O   . ARG   B 1 982  ? 65.60800   46.60400  8.64400   1.000 57.67111  ?  980  ARG   B O   1 
ATOM   21762 C  CB  . ARG   B 1 982  ? 63.81000   48.76200  10.09900  1.000 72.96115  ?  980  ARG   B CB  1 
ATOM   21763 C  CG  . ARG   B 1 982  ? 62.63300   49.69100  10.36200  1.000 75.19267  ?  980  ARG   B CG  1 
ATOM   21764 C  CD  . ARG   B 1 982  ? 62.73700   50.31400  11.74700  1.000 73.60924  ?  980  ARG   B CD  1 
ATOM   21765 N  NE  . ARG   B 1 982  ? 63.87000   51.22600  11.85000  1.000 74.24184  ?  980  ARG   B NE  1 
ATOM   21766 C  CZ  . ARG   B 1 982  ? 63.76700   52.54700  11.91200  1.000 68.26273  ?  980  ARG   B CZ  1 
ATOM   21767 N  NH1 . ARG   B 1 982  ? 62.58900   53.14800  11.91500  1.000 62.74217  ?  980  ARG   B NH1 1 
ATOM   21768 N  NH2 . ARG   B 1 982  ? 64.87400   53.28200  11.97800  1.000 63.61883  ?  980  ARG   B NH2 1 
ATOM   21769 N  N   . PRO   B 1 983  ? 66.40400   48.60800  8.04100   1.000 45.88819  ?  981  PRO   B N   1 
ATOM   21770 C  CA  . PRO   B 1 983  ? 67.77200   48.10300  7.88600   1.000 68.78532  ?  981  PRO   B CA  1 
ATOM   21771 C  C   . PRO   B 1 983  ? 68.32500   47.61600  9.21200   1.000 76.15835  ?  981  PRO   B C   1 
ATOM   21772 O  O   . PRO   B 1 983  ? 67.79500   47.96200  10.28000  1.000 79.99351  ?  981  PRO   B O   1 
ATOM   21773 C  CB  . PRO   B 1 983  ? 68.54400   49.33100  7.37800   1.000 69.44408  ?  981  PRO   B CB  1 
ATOM   21774 C  CG  . PRO   B 1 983  ? 67.50200   50.20600  6.76400   1.000 59.02259  ?  981  PRO   B CG  1 
ATOM   21775 C  CD  . PRO   B 1 983  ? 66.27600   50.00700  7.60000   1.000 75.15073  ?  981  PRO   B CD  1 
ATOM   21776 N  N   . PRO   B 1 984  ? 69.38800   46.80600  9.18900   1.000 78.77287  ?  982  PRO   B N   1 
ATOM   21777 C  CA  . PRO   B 1 984  ? 69.94700   46.33000  10.46600  1.000 88.20366  ?  982  PRO   B CA  1 
ATOM   21778 C  C   . PRO   B 1 984  ? 70.56000   47.44200  11.29800  1.000 102.11958 ?  982  PRO   B C   1 
ATOM   21779 O  O   . PRO   B 1 984  ? 70.39700   47.45500  12.52400  1.000 100.53427 ?  982  PRO   B O   1 
ATOM   21780 C  CB  . PRO   B 1 984  ? 70.99500   45.29600  10.02600  1.000 96.59181  ?  982  PRO   B CB  1 
ATOM   21781 C  CG  . PRO   B 1 984  ? 71.39800   45.74700  8.65900   1.000 96.03274  ?  982  PRO   B CG  1 
ATOM   21782 C  CD  . PRO   B 1 984  ? 70.14800   46.29900  8.03600   1.000 99.21775  ?  982  PRO   B CD  1 
ATOM   21783 N  N   . GLN   B 1 985  ? 71.25700   48.38000  10.66100  1.000 96.74560  ?  983  GLN   B N   1 
ATOM   21784 C  CA  . GLN   B 1 985  ? 71.84000   49.53000  11.32500  1.000 95.77196  ?  983  GLN   B CA  1 
ATOM   21785 C  C   . GLN   B 1 985  ? 71.07800   50.79100  10.90900  1.000 93.27044  ?  983  GLN   B C   1 
ATOM   21786 O  O   . GLN   B 1 985  ? 69.95000   50.71000  10.40200  1.000 87.68634  ?  983  GLN   B O   1 
ATOM   21787 C  CB  . GLN   B 1 985  ? 73.33500   49.59800  10.99600  1.000 75.71975  ?  983  GLN   B CB  1 
ATOM   21788 N  N   . LEU   B 1 986  ? 71.69200   51.95200  11.12000  1.000 89.22509  ?  984  LEU   B N   1 
ATOM   21789 C  CA  . LEU   B 1 986  ? 71.09900   53.23100  10.75000  1.000 83.20648  ?  984  LEU   B CA  1 
ATOM   21790 C  C   . LEU   B 1 986  ? 71.61800   53.65000  9.38000   1.000 81.75322  ?  984  LEU   B C   1 
ATOM   21791 O  O   . LEU   B 1 986  ? 72.81700   53.89500  9.21500   1.000 78.03186  ?  984  LEU   B O   1 
ATOM   21792 C  CB  . LEU   B 1 986  ? 71.40900   54.30500  11.79200  1.000 71.80084  ?  984  LEU   B CB  1 
ATOM   21793 C  CG  . LEU   B 1 986  ? 70.32300   54.56300  12.83700  1.000 78.91115  ?  984  LEU   B CG  1 
ATOM   21794 C  CD1 . LEU   B 1 986  ? 70.69700   55.74000  13.72400  1.000 78.60387  ?  984  LEU   B CD1 1 
ATOM   21795 C  CD2 . LEU   B 1 986  ? 68.97900   54.80100  12.16400  1.000 78.85796  ?  984  LEU   B CD2 1 
ATOM   21796 N  N   . THR   B 1 987  ? 70.71500   53.73000  8.40700   1.000 74.71784  ?  985  THR   B N   1 
ATOM   21797 C  CA  . THR   B 1 987  ? 71.03600   54.20900  7.07100   1.000 70.12807  ?  985  THR   B CA  1 
ATOM   21798 C  C   . THR   B 1 987  ? 70.68800   55.68800  6.96100   1.000 64.67813  ?  985  THR   B C   1 
ATOM   21799 O  O   . THR   B 1 987  ? 69.70200   56.14900  7.54400   1.000 63.34047  ?  985  THR   B O   1 
ATOM   21800 C  CB  . THR   B 1 987  ? 70.28300   53.41200  6.00500   1.000 64.61746  ?  985  THR   B CB  1 
ATOM   21801 O  OG1 . THR   B 1 987  ? 68.88900   53.36800  6.33500   1.000 69.18905  ?  985  THR   B OG1 1 
ATOM   21802 C  CG2 . THR   B 1 987  ? 70.82500   51.99500  5.92000   1.000 68.06834  ?  985  THR   B CG2 1 
ATOM   21803 N  N   . PHE   B 1 988  ? 71.50400   56.43100  6.21000   1.000 50.56269  ?  986  PHE   B N   1 
ATOM   21804 C  CA  . PHE   B 1 988  ? 71.33100   57.87500  6.09400   1.000 48.75370  ?  986  PHE   B CA  1 
ATOM   21805 C  C   . PHE   B 1 988  ? 71.21500   58.32800  4.64200   1.000 54.80780  ?  986  PHE   B C   1 
ATOM   21806 O  O   . PHE   B 1 988  ? 71.42700   59.50900  4.34900   1.000 57.17668  ?  986  PHE   B O   1 
ATOM   21807 C  CB  . PHE   B 1 988  ? 72.47800   58.61200  6.79100   1.000 58.65815  ?  986  PHE   B CB  1 
ATOM   21808 C  CG  . PHE   B 1 988  ? 72.72800   58.14500  8.19800   1.000 72.92844  ?  986  PHE   B CG  1 
ATOM   21809 C  CD1 . PHE   B 1 988  ? 71.88000   58.51800  9.22900   1.000 78.59347  ?  986  PHE   B CD1 1 
ATOM   21810 C  CD2 . PHE   B 1 988  ? 73.81400   57.33500  8.49000   1.000 78.35821  ?  986  PHE   B CD2 1 
ATOM   21811 C  CE1 . PHE   B 1 988  ? 72.10900   58.08900  10.52500  1.000 90.41470  ?  986  PHE   B CE1 1 
ATOM   21812 C  CE2 . PHE   B 1 988  ? 74.04900   56.90400  9.78400   1.000 87.48585  ?  986  PHE   B CE2 1 
ATOM   21813 C  CZ  . PHE   B 1 988  ? 73.19500   57.28100  10.80200  1.000 96.56047  ?  986  PHE   B CZ  1 
ATOM   21814 N  N   . ASP   B 1 989  ? 70.88500   57.41800  3.72800   1.000 48.80015  ?  987  ASP   B N   1 
ATOM   21815 C  CA  . ASP   B 1 989  ? 70.65600   57.76600  2.33200   1.000 40.54109  ?  987  ASP   B CA  1 
ATOM   21816 C  C   . ASP   B 1 989  ? 69.19000   58.13400  2.14600   1.000 40.55451  ?  987  ASP   B C   1 
ATOM   21817 O  O   . ASP   B 1 989  ? 68.30100   57.40600  2.59900   1.000 52.53367  ?  987  ASP   B O   1 
ATOM   21818 C  CB  . ASP   B 1 989  ? 71.03200   56.60300  1.41300   1.000 53.55424  ?  987  ASP   B CB  1 
ATOM   21819 C  CG  . ASP   B 1 989  ? 72.29100   55.88400  1.86300   1.000 78.07036  ?  987  ASP   B CG  1 
ATOM   21820 O  OD1 . ASP   B 1 989  ? 72.20300   55.05900  2.79700   1.000 79.53987  ?  987  ASP   B OD1 1 
ATOM   21821 O  OD2 . ASP   B 1 989  ? 73.36700   56.14300  1.28300   1.000 91.42462  -1 987  ASP   B OD2 1 
ATOM   21822 N  N   . GLY   B 1 990  ? 68.93500   59.25900  1.48000   1.000 43.80802  ?  988  GLY   B N   1 
ATOM   21823 C  CA  . GLY   B 1 990  ? 67.57700   59.74700  1.38300   1.000 47.20039  ?  988  GLY   B CA  1 
ATOM   21824 C  C   . GLY   B 1 990  ? 67.29100   60.47800  0.08900   1.000 39.38966  ?  988  GLY   B C   1 
ATOM   21825 O  O   . GLY   B 1 990  ? 68.14400   60.59800  -0.79200  1.000 32.28745  ?  988  GLY   B O   1 
ATOM   21826 N  N   . ALA   B 1 991  ? 66.05300   60.96000  -0.01200  1.000 35.13612  ?  989  ALA   B N   1 
ATOM   21827 C  CA  . ALA   B 1 991  ? 65.58000   61.73700  -1.14900  1.000 39.72236  ?  989  ALA   B CA  1 
ATOM   21828 C  C   . ALA   B 1 991  ? 64.60700   62.78700  -0.62900  1.000 39.00461  ?  989  ALA   B C   1 
ATOM   21829 O  O   . ALA   B 1 991  ? 64.39300   62.91400  0.58100   1.000 39.18010  ?  989  ALA   B O   1 
ATOM   21830 C  CB  . ALA   B 1 991  ? 64.93400   60.83800  -2.20600  1.000 46.03476  ?  989  ALA   B CB  1 
ATOM   21831 N  N   . ILE   B 1 992  ? 63.99900   63.53600  -1.55000  1.000 40.79085  ?  990  ILE   B N   1 
ATOM   21832 C  CA  . ILE   B 1 992  ? 63.19900   64.70100  -1.18600  1.000 46.01549  ?  990  ILE   B CA  1 
ATOM   21833 C  C   . ILE   B 1 992  ? 61.99300   64.83700  -2.10400  1.000 39.19586  ?  990  ILE   B C   1 
ATOM   21834 O  O   . ILE   B 1 992  ? 62.12000   64.76000  -3.33100  1.000 41.17805  ?  990  ILE   B O   1 
ATOM   21835 C  CB  . ILE   B 1 992  ? 64.04800   65.98400  -1.21500  1.000 46.84729  ?  990  ILE   B CB  1 
ATOM   21836 C  CG1 . ILE   B 1 992  ? 64.90900   66.02100  0.04200   1.000 55.74113  ?  990  ILE   B CG1 1 
ATOM   21837 C  CG2 . ILE   B 1 992  ? 63.17300   67.23100  -1.34800  1.000 51.98046  ?  990  ILE   B CG2 1 
ATOM   21838 C  CD1 . ILE   B 1 992  ? 65.44800   67.35600  0.35600   1.000 67.35254  ?  990  ILE   B CD1 1 
ATOM   21839 N  N   . GLN   B 1 993  ? 60.82200   65.04000  -1.50000  1.000 36.89627  ?  991  GLN   B N   1 
ATOM   21840 C  CA  . GLN   B 1 993  ? 59.60000   65.42800  -2.18900  1.000 40.62353  ?  991  GLN   B CA  1 
ATOM   21841 C  C   . GLN   B 1 993  ? 59.03700   66.66800  -1.50800  1.000 40.25149  ?  991  GLN   B C   1 
ATOM   21842 O  O   . GLN   B 1 993  ? 59.34600   66.95300  -0.34700  1.000 52.30799  ?  991  GLN   B O   1 
ATOM   21843 C  CB  . GLN   B 1 993  ? 58.55600   64.30000  -2.18000  1.000 36.10217  ?  991  GLN   B CB  1 
ATOM   21844 C  CG  . GLN   B 1 993  ? 58.81100   63.18600  -3.18300  1.000 42.54676  ?  991  GLN   B CG  1 
ATOM   21845 C  CD  . GLN   B 1 993  ? 58.22400   63.48800  -4.54800  1.000 60.91593  ?  991  GLN   B CD  1 
ATOM   21846 O  OE1 . GLN   B 1 993  ? 57.50700   64.47300  -4.72300  1.000 63.10637  ?  991  GLN   B OE1 1 
ATOM   21847 N  NE2 . GLN   B 1 993  ? 58.52300   62.63800  -5.52400  1.000 87.02383  ?  991  GLN   B NE2 1 
ATOM   21848 N  N   . MET   B 1 994  ? 58.19700   67.40800  -2.23200  1.000 33.76594  ?  992  MET   B N   1 
ATOM   21849 C  CA  . MET   B 1 994  ? 57.71800   68.68900  -1.73300  1.000 41.78133  ?  992  MET   B CA  1 
ATOM   21850 C  C   . MET   B 1 994  ? 56.22400   68.84900  -1.98200  1.000 45.35875  ?  992  MET   B C   1 
ATOM   21851 O  O   . MET   B 1 994  ? 55.69500   68.37700  -2.99400  1.000 55.50253  ?  992  MET   B O   1 
ATOM   21852 C  CB  . MET   B 1 994  ? 58.48300   69.85300  -2.38100  1.000 32.80213  ?  992  MET   B CB  1 
ATOM   21853 C  CG  . MET   B 1 994  ? 58.29800   71.19700  -1.68600  1.000 45.96747  ?  992  MET   B CG  1 
ATOM   21854 S  SD  . MET   B 1 994  ? 57.38300   72.38800  -2.68600  1.000 75.06043  ?  992  MET   B SD  1 
ATOM   21855 C  CE  . MET   B 1 994  ? 58.41200   72.45900  -4.15100  1.000 65.36641  ?  992  MET   B CE  1 
ATOM   21856 N  N   . TYR   B 1 995  ? 55.55400   69.51700  -1.04200  1.000 45.26457  ?  993  TYR   B N   1 
ATOM   21857 C  CA  . TYR   B 1 995  ? 54.15000   69.89200  -1.15600  1.000 44.89321  ?  993  TYR   B CA  1 
ATOM   21858 C  C   . TYR   B 1 995  ? 54.03400   71.40200  -1.01200  1.000 41.05840  ?  993  TYR   B C   1 
ATOM   21859 O  O   . TYR   B 1 995  ? 54.50000   71.97500  -0.02000  1.000 36.33565  ?  993  TYR   B O   1 
ATOM   21860 C  CB  . TYR   B 1 995  ? 53.29200   69.18600  -0.10000  1.000 34.68721  ?  993  TYR   B CB  1 
ATOM   21861 C  CG  . TYR   B 1 995  ? 51.92500   69.80800  0.12800   1.000 41.83636  ?  993  TYR   B CG  1 
ATOM   21862 C  CD1 . TYR   B 1 995  ? 51.05800   70.05100  -0.93200  1.000 38.69597  ?  993  TYR   B CD1 1 
ATOM   21863 C  CD2 . TYR   B 1 995  ? 51.49300   70.12900  1.41000   1.000 40.97966  ?  993  TYR   B CD2 1 
ATOM   21864 C  CE1 . TYR   B 1 995  ? 49.80900   70.61400  -0.72200  1.000 47.62826  ?  993  TYR   B CE1 1 
ATOM   21865 C  CE2 . TYR   B 1 995  ? 50.24300   70.68800  1.63000   1.000 42.67578  ?  993  TYR   B CE2 1 
ATOM   21866 C  CZ  . TYR   B 1 995  ? 49.40600   70.93000  0.56000   1.000 50.62462  ?  993  TYR   B CZ  1 
ATOM   21867 O  OH  . TYR   B 1 995  ? 48.16400   71.48600  0.77100   1.000 47.30171  ?  993  TYR   B OH  1 
ATOM   21868 N  N   . ARG   B 1 996  ? 53.41300   72.03500  -2.00300  1.000 44.47013  ?  994  ARG   B N   1 
ATOM   21869 C  CA  . ARG   B 1 996  ? 53.23400   73.48000  -2.04000  1.000 48.47395  ?  994  ARG   B CA  1 
ATOM   21870 C  C   . ARG   B 1 996  ? 51.81400   73.82300  -1.60700  1.000 56.46955  ?  994  ARG   B C   1 
ATOM   21871 O  O   . ARG   B 1 996  ? 50.84500   73.40200  -2.25000  1.000 52.43779  ?  994  ARG   B O   1 
ATOM   21872 C  CB  . ARG   B 1 996  ? 53.50900   74.02500  -3.44100  1.000 30.39604  ?  994  ARG   B CB  1 
ATOM   21873 C  CG  . ARG   B 1 996  ? 53.01100   75.44800  -3.68000  1.000 37.24466  ?  994  ARG   B CG  1 
ATOM   21874 C  CD  . ARG   B 1 996  ? 54.14500   76.45700  -3.61000  1.000 36.37929  ?  994  ARG   B CD  1 
ATOM   21875 N  NE  . ARG   B 1 996  ? 53.67200   77.83200  -3.71000  1.000 45.23254  ?  994  ARG   B NE  1 
ATOM   21876 C  CZ  . ARG   B 1 996  ? 54.29200   78.87400  -3.17200  1.000 47.05134  ?  994  ARG   B CZ  1 
ATOM   21877 N  NH1 . ARG   B 1 996  ? 55.41100   78.73000  -2.48300  1.000 50.33155  ?  994  ARG   B NH1 1 
ATOM   21878 N  NH2 . ARG   B 1 996  ? 53.76800   80.08800  -3.31900  1.000 64.82065  ?  994  ARG   B NH2 1 
ATOM   21879 N  N   . VAL   B 1 997  ? 51.70000   74.57900  -0.52100  1.000 46.15724  ?  995  VAL   B N   1 
ATOM   21880 C  CA  . VAL   B 1 997  ? 50.42600   75.13500  -0.08600  1.000 51.82030  ?  995  VAL   B CA  1 
ATOM   21881 C  C   . VAL   B 1 997  ? 50.23200   76.46300  -0.80300  1.000 48.91940  ?  995  VAL   B C   1 
ATOM   21882 O  O   . VAL   B 1 997  ? 51.03500   77.38700  -0.63100  1.000 50.31807  ?  995  VAL   B O   1 
ATOM   21883 C  CB  . VAL   B 1 997  ? 50.39500   75.32100  1.43500   1.000 46.72561  ?  995  VAL   B CB  1 
ATOM   21884 C  CG1 . VAL   B 1 997  ? 48.97300   75.53800  1.90100   1.000 47.62882  ?  995  VAL   B CG1 1 
ATOM   21885 C  CG2 . VAL   B 1 997  ? 51.01800   74.12400  2.12300   1.000 47.41111  ?  995  VAL   B CG2 1 
ATOM   21886 N  N   . ASN   B 1 998  ? 49.16300   76.56300  -1.59900  1.000 52.84388  ?  996  ASN   B N   1 
ATOM   21887 C  CA  . ASN   B 1 998  ? 48.97200   77.72900  -2.45000  1.000 54.77881  ?  996  ASN   B CA  1 
ATOM   21888 C  C   . ASN   B 1 998  ? 48.87400   78.99900  -1.60000  1.000 63.94010  ?  996  ASN   B C   1 
ATOM   21889 O  O   . ASN   B 1 998  ? 48.61300   78.92900  -0.39600  1.000 58.97675  ?  996  ASN   B O   1 
ATOM   21890 C  CB  . ASN   B 1 998  ? 47.73300   77.54300  -3.34800  1.000 42.93006  ?  996  ASN   B CB  1 
ATOM   21891 C  CG  . ASN   B 1 998  ? 46.40400   77.58600  -2.58800  1.000 56.15189  ?  996  ASN   B CG  1 
ATOM   21892 O  OD1 . ASN   B 1 998  ? 46.19700   78.40000  -1.69300  1.000 74.53754  ?  996  ASN   B OD1 1 
ATOM   21893 N  ND2 . ASN   B 1 998  ? 45.48100   76.71200  -2.98100  1.000 65.02753  ?  996  ASN   B ND2 1 
ATOM   21894 N  N   . PRO   B 1 999  ? 49.11400   80.17000  -2.20000  1.000 64.36036  ?  997  PRO   B N   1 
ATOM   21895 C  CA  . PRO   B 1 999  ? 49.02800   81.42200  -1.42600  1.000 62.12579  ?  997  PRO   B CA  1 
ATOM   21896 C  C   . PRO   B 1 999  ? 47.69300   81.62200  -0.73300  1.000 70.04340  ?  997  PRO   B C   1 
ATOM   21897 O  O   . PRO   B 1 999  ? 47.65200   82.21000  0.35700   1.000 67.37882  ?  997  PRO   B O   1 
ATOM   21898 C  CB  . PRO   B 1 999  ? 49.27400   82.50000  -2.48900  1.000 47.72453  ?  997  PRO   B CB  1 
ATOM   21899 C  CG  . PRO   B 1 999  ? 50.10100   81.82100  -3.51900  1.000 49.98986  ?  997  PRO   B CG  1 
ATOM   21900 C  CD  . PRO   B 1 999  ? 49.61700   80.40100  -3.56800  1.000 50.19091  ?  997  PRO   B CD  1 
ATOM   21901 N  N   . GLU   B 1 1000 ? 46.59800   81.14000  -1.32700  1.000 65.55711  ?  998  GLU   B N   1 
ATOM   21902 C  CA  . GLU   B 1 1000 ? 45.28000   81.30800  -0.72300  1.000 59.19652  ?  998  GLU   B CA  1 
ATOM   21903 C  C   . GLU   B 1 1000 ? 45.18700   80.57300  0.60900   1.000 57.51935  ?  998  GLU   B C   1 
ATOM   21904 O  O   . GLU   B 1 1000 ? 44.79700   81.15500  1.62800   1.000 73.07953  ?  998  GLU   B O   1 
ATOM   21905 C  CB  . GLU   B 1 1000 ? 44.20900   80.81100  -1.69300  1.000 61.54654  ?  998  GLU   B CB  1 
ATOM   21906 C  CG  . GLU   B 1 1000 ? 42.89400   81.56100  -1.64900  1.000 81.69707  ?  998  GLU   B CG  1 
ATOM   21907 C  CD  . GLU   B 1 1000 ? 41.91100   81.03800  -2.67700  1.000 83.72765  ?  998  GLU   B CD  1 
ATOM   21908 O  OE1 . GLU   B 1 1000 ? 41.40100   79.91200  -2.49500  1.000 62.67824  ?  998  GLU   B OE1 1 
ATOM   21909 O  OE2 . GLU   B 1 1000 ? 41.66200   81.74600  -3.67600  1.000 76.74254  -1 998  GLU   B OE2 1 
ATOM   21910 N  N   . ILE   B 1 1001 ? 45.54600   79.28700  0.62000   1.000 54.89208  ?  999  ILE   B N   1 
ATOM   21911 C  CA  . ILE   B 1 1001 ? 45.45600   78.49900  1.84600   1.000 53.86503  ?  999  ILE   B CA  1 
ATOM   21912 C  C   . ILE   B 1 1001 ? 46.46400   78.99300  2.87500   1.000 47.26822  ?  999  ILE   B C   1 
ATOM   21913 O  O   . ILE   B 1 1001 ? 46.16800   79.05100  4.07400   1.000 54.97493  ?  999  ILE   B O   1 
ATOM   21914 C  CB  . ILE   B 1 1001 ? 45.64200   77.00200  1.53700   1.000 51.80075  ?  999  ILE   B CB  1 
ATOM   21915 C  CG1 . ILE   B 1 1001 ? 44.62300   76.54100  0.49200   1.000 52.23852  ?  999  ILE   B CG1 1 
ATOM   21916 C  CG2 . ILE   B 1 1001 ? 45.50900   76.17100  2.80500   1.000 64.93581  ?  999  ILE   B CG2 1 
ATOM   21917 C  CD1 . ILE   B 1 1001 ? 43.18300   76.80300  0.88400   1.000 58.16039  ?  999  ILE   B CD1 1 
ATOM   21918 N  N   . THR   B 1 1002 ? 47.66900   79.35700  2.42500   1.000 62.95570  ?  1000 THR   B N   1 
ATOM   21919 C  CA  . THR   B 1 1002 ? 48.66800   79.91500  3.33300   1.000 68.09959  ?  1000 THR   B CA  1 
ATOM   21920 C  C   . THR   B 1 1002 ? 48.12700   81.14300  4.05300   1.000 72.77190  ?  1000 THR   B C   1 
ATOM   21921 O  O   . THR   B 1 1002 ? 48.34300   81.31800  5.25800   1.000 54.73529  ?  1000 THR   B O   1 
ATOM   21922 C  CB  . THR   B 1 1002 ? 49.93700   80.27300  2.56100   1.000 54.31978  ?  1000 THR   B CB  1 
ATOM   21923 O  OG1 . THR   B 1 1002 ? 50.31900   79.17500  1.72300   1.000 48.96997  ?  1000 THR   B OG1 1 
ATOM   21924 C  CG2 . THR   B 1 1002 ? 51.07100   80.59000  3.52200   1.000 56.02306  ?  1000 THR   B CG2 1 
ATOM   21925 N  N   . ARG   B 1 1003 ? 47.41300   82.00200  3.32400   1.000 63.57948  ?  1001 ARG   B N   1 
ATOM   21926 C  CA  . ARG   B 1 1003 ? 46.81400   83.18500  3.92800   1.000 59.61039  ?  1001 ARG   B CA  1 
ATOM   21927 C  C   . ARG   B 1 1003 ? 45.76100   82.80300  4.96100   1.000 73.47216  ?  1001 ARG   B C   1 
ATOM   21928 O  O   . ARG   B 1 1003 ? 45.62800   83.46500  5.99800   1.000 73.05901  ?  1001 ARG   B O   1 
ATOM   21929 C  CB  . ARG   B 1 1003 ? 46.20900   84.05500  2.82900   1.000 58.22559  ?  1001 ARG   B CB  1 
ATOM   21930 C  CG  . ARG   B 1 1003 ? 46.15700   85.54000  3.11500   1.000 80.66057  ?  1001 ARG   B CG  1 
ATOM   21931 C  CD  . ARG   B 1 1003 ? 45.59400   86.23600  1.89400   1.000 74.29626  ?  1001 ARG   B CD  1 
ATOM   21932 N  NE  . ARG   B 1 1003 ? 44.43600   85.50600  1.39200   1.000 79.88851  ?  1001 ARG   B NE  1 
ATOM   21933 C  CZ  . ARG   B 1 1003 ? 44.07700   85.44500  0.11700   1.000 83.12041  ?  1001 ARG   B CZ  1 
ATOM   21934 N  NH1 . ARG   B 1 1003 ? 44.76400   86.06900  -0.82600  1.000 87.71942  ?  1001 ARG   B NH1 1 
ATOM   21935 N  NH2 . ARG   B 1 1003 ? 43.00800   84.72900  -0.22200  1.000 61.79731  ?  1001 ARG   B NH2 1 
ATOM   21936 N  N   . LYS   B 1 1004 ? 45.00400   81.73300  4.69800   1.000 67.57219  ?  1002 LYS   B N   1 
ATOM   21937 C  CA  . LYS   B 1 1004 ? 43.99400   81.28800  5.65500   1.000 67.71787  ?  1002 LYS   B CA  1 
ATOM   21938 C  C   . LYS   B 1 1004 ? 44.63200   80.61200  6.86300   1.000 63.11059  ?  1002 LYS   B C   1 
ATOM   21939 O  O   . LYS   B 1 1004 ? 44.13400   80.74200  7.98700   1.000 60.42846  ?  1002 LYS   B O   1 
ATOM   21940 C  CB  . LYS   B 1 1004 ? 42.99500   80.34700  4.97600   1.000 48.60483  ?  1002 LYS   B CB  1 
ATOM   21941 C  CG  . LYS   B 1 1004 ? 41.87800   81.06700  4.23100   1.000 77.24099  ?  1002 LYS   B CG  1 
ATOM   21942 C  CD  . LYS   B 1 1004 ? 40.96100   80.10800  3.47700   1.000 88.77856  ?  1002 LYS   B CD  1 
ATOM   21943 C  CE  . LYS   B 1 1004 ? 39.94000   79.44800  4.39200   1.000 87.69544  ?  1002 LYS   B CE  1 
ATOM   21944 N  NZ  . LYS   B 1 1004 ? 38.74200   78.98900  3.62800   1.000 73.71555  ?  1002 LYS   B NZ  1 
ATOM   21945 N  N   . LEU   B 1 1005 ? 45.73400   79.88800  6.65300   1.000 49.21540  ?  1003 LEU   B N   1 
ATOM   21946 C  CA  . LEU   B 1 1005 ? 46.39100   79.20000  7.76000   1.000 49.43443  ?  1003 LEU   B CA  1 
ATOM   21947 C  C   . LEU   B 1 1005 ? 46.91100   80.19400  8.79200   1.000 66.46286  ?  1003 LEU   B C   1 
ATOM   21948 O  O   . LEU   B 1 1005 ? 46.71800   80.01200  10.00000  1.000 61.04283  ?  1003 LEU   B O   1 
ATOM   21949 C  CB  . LEU   B 1 1005 ? 47.53000   78.32600  7.23400   1.000 55.02711  ?  1003 LEU   B CB  1 
ATOM   21950 C  CG  . LEU   B 1 1005 ? 47.14200   77.10900  6.39400   1.000 43.56346  ?  1003 LEU   B CG  1 
ATOM   21951 C  CD1 . LEU   B 1 1005 ? 48.37800   76.40800  5.86200   1.000 48.44437  ?  1003 LEU   B CD1 1 
ATOM   21952 C  CD2 . LEU   B 1 1005 ? 46.29800   76.15500  7.21200   1.000 49.50488  ?  1003 LEU   B CD2 1 
ATOM   21953 N  N   . LYS   B 1 1006 ? 47.57400   81.25700  8.33000   1.000 74.17993  ?  1004 LYS   B N   1 
ATOM   21954 C  CA  . LYS   B 1 1006 ? 48.10900   82.24700  9.25800   1.000 71.59411  ?  1004 LYS   B CA  1 
ATOM   21955 C  C   . LYS   B 1 1006 ? 46.99400   83.06600  9.89400   1.000 58.85432  ?  1004 LYS   B C   1 
ATOM   21956 O  O   . LYS   B 1 1006 ? 47.05700   83.38800  11.08700  1.000 52.74349  ?  1004 LYS   B O   1 
ATOM   21957 C  CB  . LYS   B 1 1006 ? 49.10300   83.15900  8.53900   1.000 74.65327  ?  1004 LYS   B CB  1 
ATOM   21958 C  CG  . LYS   B 1 1006 ? 50.19000   82.40900  7.79400   1.000 67.46647  ?  1004 LYS   B CG  1 
ATOM   21959 C  CD  . LYS   B 1 1006 ? 51.51200   83.15800  7.82500   1.000 66.60305  ?  1004 LYS   B CD  1 
ATOM   21960 C  CE  . LYS   B 1 1006 ? 51.93200   83.59300  6.43300   1.000 68.29469  ?  1004 LYS   B CE  1 
ATOM   21961 N  NZ  . LYS   B 1 1006 ? 53.41200   83.71300  6.32200   1.000 51.37331  ?  1004 LYS   B NZ  1 
ATOM   21962 N  N   . ALA   B 1 1007 ? 45.96800   83.41200  9.11300   1.000 50.51509  ?  1005 ALA   B N   1 
ATOM   21963 C  CA  . ALA   B 1 1007 ? 44.83800   84.15100  9.66300   1.000 69.51576  ?  1005 ALA   B CA  1 
ATOM   21964 C  C   . ALA   B 1 1007 ? 44.11500   83.33700  10.72700  1.000 68.46605  ?  1005 ALA   B C   1 
ATOM   21965 O  O   . ALA   B 1 1007 ? 43.69700   83.87800  11.75800  1.000 76.52185  ?  1005 ALA   B O   1 
ATOM   21966 C  CB  . ALA   B 1 1007 ? 43.87500   84.54900  8.54500   1.000 52.16829  ?  1005 ALA   B CB  1 
ATOM   21967 N  N   . THR   B 1 1008 ? 43.96200   82.03200  10.49700  1.000 65.62973  ?  1006 THR   B N   1 
ATOM   21968 C  CA  . THR   B 1 1008 ? 43.30000   81.18800  11.48500  1.000 51.85235  ?  1006 THR   B CA  1 
ATOM   21969 C  C   . THR   B 1 1008 ? 44.14900   81.04200  12.74000  1.000 50.19500  ?  1006 THR   B C   1 
ATOM   21970 O  O   . THR   B 1 1008 ? 43.62400   81.06900  13.85800  1.000 70.44291  ?  1006 THR   B O   1 
ATOM   21971 C  CB  . THR   B 1 1008 ? 42.99100   79.81700  10.88900  1.000 52.14374  ?  1006 THR   B CB  1 
ATOM   21972 O  OG1 . THR   B 1 1008 ? 42.65700   79.96200  9.50300   1.000 64.05160  ?  1006 THR   B OG1 1 
ATOM   21973 C  CG2 . THR   B 1 1008 ? 41.81800   79.19800  11.61300  1.000 60.45923  ?  1006 THR   B CG2 1 
ATOM   21974 N  N   . ALA   B 1 1009 ? 45.46500   80.88800  12.57700  1.000 49.85203  ?  1007 ALA   B N   1 
ATOM   21975 C  CA  . ALA   B 1 1009 ? 46.33900   80.80200  13.74100  1.000 62.04276  ?  1007 ALA   B CA  1 
ATOM   21976 C  C   . ALA   B 1 1009 ? 46.33000   82.10500  14.53100  1.000 76.43763  ?  1007 ALA   B C   1 
ATOM   21977 O  O   . ALA   B 1 1009 ? 46.33900   82.09000  15.76800  1.000 71.28719  ?  1007 ALA   B O   1 
ATOM   21978 C  CB  . ALA   B 1 1009 ? 47.75900   80.44300  13.30400  1.000 66.04456  ?  1007 ALA   B CB  1 
ATOM   21979 N  N   . ALA   B 1 1010 ? 46.29400   83.24300  13.83500  1.000 73.96370  ?  1008 ALA   B N   1 
ATOM   21980 C  CA  . ALA   B 1 1010 ? 46.32500   84.53300  14.51600  1.000 77.85813  ?  1008 ALA   B CA  1 
ATOM   21981 C  C   . ALA   B 1 1010 ? 45.05000   84.76900  15.31600  1.000 70.21852  ?  1008 ALA   B C   1 
ATOM   21982 O  O   . ALA   B 1 1010 ? 45.10100   85.21600  16.46800  1.000 69.29788  ?  1008 ALA   B O   1 
ATOM   21983 C  CB  . ALA   B 1 1010 ? 46.54000   85.65600  13.50100  1.000 64.58173  ?  1008 ALA   B CB  1 
ATOM   21984 N  N   . LYS   B 1 1011 ? 43.89200   84.47000  14.72100  1.000 58.89300  ?  1009 LYS   B N   1 
ATOM   21985 C  CA  . LYS   B 1 1011 ? 42.62600   84.73000  15.39900  1.000 66.66745  ?  1009 LYS   B CA  1 
ATOM   21986 C  C   . LYS   B 1 1011 ? 42.48200   83.90500  16.67000  1.000 69.45395  ?  1009 LYS   B C   1 
ATOM   21987 O  O   . LYS   B 1 1011 ? 41.74800   84.29800  17.58400  1.000 69.07781  ?  1009 LYS   B O   1 
ATOM   21988 C  CB  . LYS   B 1 1011 ? 41.45700   84.45200  14.45500  1.000 51.72145  ?  1009 LYS   B CB  1 
ATOM   21989 C  CG  . LYS   B 1 1011 ? 40.15800   85.10600  14.88500  1.000 66.71155  ?  1009 LYS   B CG  1 
ATOM   21990 C  CD  . LYS   B 1 1011 ? 38.96100   84.48200  14.19300  1.000 74.72001  ?  1009 LYS   B CD  1 
ATOM   21991 C  CE  . LYS   B 1 1011 ? 37.74400   85.37100  14.35800  1.000 75.19316  ?  1009 LYS   B CE  1 
ATOM   21992 N  NZ  . LYS   B 1 1011 ? 38.11600   86.79600  14.12300  1.000 78.49589  ?  1009 LYS   B NZ  1 
ATOM   21993 N  N   . HIS   B 1 1012 ? 43.17400   82.77000  16.75300  1.000 66.86307  ?  1010 HIS   B N   1 
ATOM   21994 C  CA  . HIS   B 1 1012 ? 43.04700   81.85200  17.87700  1.000 69.92825  ?  1010 HIS   B CA  1 
ATOM   21995 C  C   . HIS   B 1 1012 ? 44.33200   81.76800  18.70100  1.000 68.04181  ?  1010 HIS   B C   1 
ATOM   21996 O  O   . HIS   B 1 1012 ? 44.64900   80.71600  19.26200  1.000 68.28059  ?  1010 HIS   B O   1 
ATOM   21997 C  CB  . HIS   B 1 1012 ? 42.62800   80.46800  17.38500  1.000 41.71188  ?  1010 HIS   B CB  1 
ATOM   21998 C  CG  . HIS   B 1 1012 ? 41.37400   80.47800  16.56500  1.000 41.17770  ?  1010 HIS   B CG  1 
ATOM   21999 N  ND1 . HIS   B 1 1012 ? 40.12900   80.71800  17.10800  1.000 54.66258  ?  1010 HIS   B ND1 1 
ATOM   22000 C  CD2 . HIS   B 1 1012 ? 41.17200   80.27700  15.24200  1.000 65.71432  ?  1010 HIS   B CD2 1 
ATOM   22001 C  CE1 . HIS   B 1 1012 ? 39.21500   80.66700  16.15500  1.000 68.04109  ?  1010 HIS   B CE1 1 
ATOM   22002 N  NE2 . HIS   B 1 1012 ? 39.82200   80.40100  15.01200  1.000 74.13683  ?  1010 HIS   B NE2 1 
ATOM   22003 N  N   . ASP   B 1 1013 ? 45.07100   82.87700  18.78500  1.000 50.66620  ?  1011 ASP   B N   1 
ATOM   22004 C  CA  . ASP   B 1 1013 ? 46.27500   82.98500  19.61300  1.000 52.03562  ?  1011 ASP   B CA  1 
ATOM   22005 C  C   . ASP   B 1 1013 ? 47.26200   81.85600  19.32300  1.000 60.28563  ?  1011 ASP   B C   1 
ATOM   22006 O  O   . ASP   B 1 1013 ? 47.71300   81.14400  20.22200  1.000 72.15251  ?  1011 ASP   B O   1 
ATOM   22007 C  CB  . ASP   B 1 1013 ? 45.92000   83.01800  21.10200  1.000 58.16431  ?  1011 ASP   B CB  1 
ATOM   22008 C  CG  . ASP   B 1 1013 ? 46.14500   84.38000  21.72600  1.000 55.48238  ?  1011 ASP   B CG  1 
ATOM   22009 O  OD1 . ASP   B 1 1013 ? 46.82700   85.21500  21.09400  1.000 59.01808  ?  1011 ASP   B OD1 1 
ATOM   22010 O  OD2 . ASP   B 1 1013 ? 45.63100   84.62100  22.84000  1.000 44.35135  -1 1011 ASP   B OD2 1 
ATOM   22011 N  N   . LEU   B 1 1014 ? 47.60700   81.70200  18.04900  1.000 69.65461  ?  1012 LEU   B N   1 
ATOM   22012 C  CA  . LEU   B 1 1014 ? 48.49600   80.63200  17.62800  1.000 78.44798  ?  1012 LEU   B CA  1 
ATOM   22013 C  C   . LEU   B 1 1014 ? 49.46100   81.14600  16.57300  1.000 65.43102  ?  1012 LEU   B C   1 
ATOM   22014 O  O   . LEU   B 1 1014 ? 49.12100   82.01300  15.76400  1.000 53.33907  ?  1012 LEU   B O   1 
ATOM   22015 C  CB  . LEU   B 1 1014 ? 47.71100   79.43700  17.06900  1.000 76.18936  ?  1012 LEU   B CB  1 
ATOM   22016 C  CG  . LEU   B 1 1014 ? 46.94200   78.57600  18.07100  1.000 60.21322  ?  1012 LEU   B CG  1 
ATOM   22017 C  CD1 . LEU   B 1 1014 ? 45.78800   77.86900  17.37900  1.000 51.98993  ?  1012 LEU   B CD1 1 
ATOM   22018 C  CD2 . LEU   B 1 1014 ? 47.87400   77.56700  18.73000  1.000 56.15263  ?  1012 LEU   B CD2 1 
ATOM   22019 N  N   . THR   B 1 1015 ? 50.67200   80.60700  16.59600  1.000 58.87391  ?  1013 THR   B N   1 
ATOM   22020 C  CA  . THR   B 1 1015 ? 51.62300   80.83200  15.52200  1.000 50.19772  ?  1013 THR   B CA  1 
ATOM   22021 C  C   . THR   B 1 1015 ? 51.44100   79.76500  14.45000  1.000 57.80621  ?  1013 THR   B C   1 
ATOM   22022 O  O   . THR   B 1 1015 ? 50.90100   78.68500  14.70100  1.000 65.90925  ?  1013 THR   B O   1 
ATOM   22023 C  CB  . THR   B 1 1015 ? 53.05800   80.81000  16.04800  1.000 45.56186  ?  1013 THR   B CB  1 
ATOM   22024 O  OG1 . THR   B 1 1015 ? 53.43200   79.46500  16.37100  1.000 50.17130  ?  1013 THR   B OG1 1 
ATOM   22025 C  CG2 . THR   B 1 1015 ? 53.18100   81.67300  17.29100  1.000 60.37314  ?  1013 THR   B CG2 1 
ATOM   22026 N  N   . LEU   B 1 1016 ? 51.89400   80.08400  13.23500  1.000 52.57933  ?  1014 LEU   B N   1 
ATOM   22027 C  CA  . LEU   B 1 1016 ? 51.75600   79.13100  12.13800  1.000 55.42167  ?  1014 LEU   B CA  1 
ATOM   22028 C  C   . LEU   B 1 1016 ? 52.52000   77.84500  12.41900  1.000 59.91879  ?  1014 LEU   B C   1 
ATOM   22029 O  O   . LEU   B 1 1016 ? 52.11400   76.77000  11.96300  1.000 61.31185  ?  1014 LEU   B O   1 
ATOM   22030 C  CB  . LEU   B 1 1016 ? 52.22500   79.75700  10.82600  1.000 43.15645  ?  1014 LEU   B CB  1 
ATOM   22031 C  CG  . LEU   B 1 1016 ? 51.93500   78.92200  9.57700   1.000 51.33584  ?  1014 LEU   B CG  1 
ATOM   22032 C  CD1 . LEU   B 1 1016 ? 50.45300   78.58900  9.48600   1.000 67.50719  ?  1014 LEU   B CD1 1 
ATOM   22033 C  CD2 . LEU   B 1 1016 ? 52.40500   79.64200  8.32500   1.000 51.47123  ?  1014 LEU   B CD2 1 
ATOM   22034 N  N   . TYR   B 1 1017 ? 53.62000   77.93300  13.16900  1.000 45.08486  ?  1015 TYR   B N   1 
ATOM   22035 C  CA  . TYR   B 1 1017 ? 54.31800   76.72800  13.60300  1.000 43.20916  ?  1015 TYR   B CA  1 
ATOM   22036 C  C   . TYR   B 1 1017 ? 53.41500   75.85400  14.46300  1.000 50.32703  ?  1015 TYR   B C   1 
ATOM   22037 O  O   . TYR   B 1 1017 ? 53.35900   74.63300  14.27600  1.000 54.60096  ?  1015 TYR   B O   1 
ATOM   22038 C  CB  . TYR   B 1 1017 ? 55.58800   77.10900  14.36400  1.000 44.64406  ?  1015 TYR   B CB  1 
ATOM   22039 C  CG  . TYR   B 1 1017 ? 56.29700   75.95200  15.03000  1.000 48.26815  ?  1015 TYR   B CG  1 
ATOM   22040 C  CD1 . TYR   B 1 1017 ? 57.19500   75.16300  14.32500  1.000 57.79676  ?  1015 TYR   B CD1 1 
ATOM   22041 C  CD2 . TYR   B 1 1017 ? 56.08000   75.65900  16.37000  1.000 53.89460  ?  1015 TYR   B CD2 1 
ATOM   22042 C  CE1 . TYR   B 1 1017 ? 57.85000   74.10900  14.93400  1.000 54.62638  ?  1015 TYR   B CE1 1 
ATOM   22043 C  CE2 . TYR   B 1 1017 ? 56.72800   74.60700  16.98500  1.000 56.68913  ?  1015 TYR   B CE2 1 
ATOM   22044 C  CZ  . TYR   B 1 1017 ? 57.61200   73.83600  16.26300  1.000 52.85737  ?  1015 TYR   B CZ  1 
ATOM   22045 O  OH  . TYR   B 1 1017 ? 58.26000   72.78900  16.87400  1.000 56.39249  ?  1015 TYR   B OH  1 
ATOM   22046 N  N   . MET   B 1 1018 ? 52.69300   76.46300  15.40700  1.000 53.45541  ?  1016 MET   B N   1 
ATOM   22047 C  CA  . MET   B 1 1018 ? 51.78700   75.69700  16.25800  1.000 56.71330  ?  1016 MET   B CA  1 
ATOM   22048 C  C   . MET   B 1 1018 ? 50.66600   75.06700  15.44200  1.000 50.36928  ?  1016 MET   B C   1 
ATOM   22049 O  O   . MET   B 1 1018 ? 50.27100   73.92400  15.69500  1.000 67.62365  ?  1016 MET   B O   1 
ATOM   22050 C  CB  . MET   B 1 1018 ? 51.21400   76.59500  17.35400  1.000 61.22289  ?  1016 MET   B CB  1 
ATOM   22051 C  CG  . MET   B 1 1018 ? 52.25800   77.15900  18.30100  1.000 66.72878  ?  1016 MET   B CG  1 
ATOM   22052 S  SD  . MET   B 1 1018 ? 51.62500   78.50400  19.32300  1.000 69.49955  ?  1016 MET   B SD  1 
ATOM   22053 C  CE  . MET   B 1 1018 ? 53.07900   78.87300  20.30500  1.000 53.81119  ?  1016 MET   B CE  1 
ATOM   22054 N  N   . LEU   B 1 1019 ? 50.14000   75.79900  14.45800  1.000 44.80655  ?  1017 LEU   B N   1 
ATOM   22055 C  CA  . LEU   B 1 1019 ? 49.10700   75.23700  13.59400  1.000 42.99774  ?  1017 LEU   B CA  1 
ATOM   22056 C  C   . LEU   B 1 1019 ? 49.66000   74.09900  12.74600  1.000 53.46795  ?  1017 LEU   B C   1 
ATOM   22057 O  O   . LEU   B 1 1019 ? 48.97900   73.09000  12.53100  1.000 55.32665  ?  1017 LEU   B O   1 
ATOM   22058 C  CB  . LEU   B 1 1019 ? 48.51700   76.33000  12.70400  1.000 37.83199  ?  1017 LEU   B CB  1 
ATOM   22059 C  CG  . LEU   B 1 1019 ? 47.30100   75.95800  11.85300  1.000 32.46778  ?  1017 LEU   B CG  1 
ATOM   22060 C  CD1 . LEU   B 1 1019 ? 46.00800   76.20300  12.61200  1.000 31.07874  ?  1017 LEU   B CD1 1 
ATOM   22061 C  CD2 . LEU   B 1 1019 ? 47.31400   76.73900  10.55800  1.000 44.21238  ?  1017 LEU   B CD2 1 
ATOM   22062 N  N   . MET   B 1 1020 ? 50.89500   74.24100  12.25800  1.000 57.84982  ?  1018 MET   B N   1 
ATOM   22063 C  CA  . MET   B 1 1020 ? 51.50300   73.18400  11.45700  1.000 57.06288  ?  1018 MET   B CA  1 
ATOM   22064 C  C   . MET   B 1 1020 ? 51.96700   72.02200  12.32900  1.000 64.59361  ?  1018 MET   B C   1 
ATOM   22065 O  O   . MET   B 1 1020 ? 51.73500   70.85600  11.99000  1.000 66.13102  ?  1018 MET   B O   1 
ATOM   22066 C  CB  . MET   B 1 1020 ? 52.67000   73.74300  10.64100  1.000 41.81078  ?  1018 MET   B CB  1 
ATOM   22067 C  CG  . MET   B 1 1020 ? 52.25400   74.71000  9.54400   1.000 39.38295  ?  1018 MET   B CG  1 
ATOM   22068 S  SD  . MET   B 1 1020 ? 50.86000   74.10100  8.57700   1.000 50.67358  ?  1018 MET   B SD  1 
ATOM   22069 C  CE  . MET   B 1 1020 ? 51.59100   73.97900  6.94700   1.000 61.74310  ?  1018 MET   B CE  1 
ATOM   22070 N  N   . LEU   B 1 1021 ? 52.62800   72.32100  13.45400  1.000 53.94572  ?  1019 LEU   B N   1 
ATOM   22071 C  CA  . LEU   B 1 1021 ? 53.04900   71.26000  14.36600  1.000 60.94834  ?  1019 LEU   B CA  1 
ATOM   22072 C  C   . LEU   B 1 1021 ? 51.85900   70.43500  14.82900  1.000 67.09745  ?  1019 LEU   B C   1 
ATOM   22073 O  O   . LEU   B 1 1021 ? 51.97900   69.22500  15.05200  1.000 70.42254  ?  1019 LEU   B O   1 
ATOM   22074 C  CB  . LEU   B 1 1021 ? 53.78100   71.85100  15.57000  1.000 45.94085  ?  1019 LEU   B CB  1 
ATOM   22075 C  CG  . LEU   B 1 1021 ? 54.18300   70.84100  16.64500  1.000 54.37152  ?  1019 LEU   B CG  1 
ATOM   22076 C  CD1 . LEU   B 1 1021 ? 55.37700   70.01000  16.18700  1.000 50.38258  ?  1019 LEU   B CD1 1 
ATOM   22077 C  CD2 . LEU   B 1 1021 ? 54.46500   71.54100  17.96400  1.000 55.20893  ?  1019 LEU   B CD2 1 
ATOM   22078 N  N   . THR   B 1 1022 ? 50.70400   71.07800  14.98700  1.000 54.50413  ?  1020 THR   B N   1 
ATOM   22079 C  CA  . THR   B 1 1022 ? 49.46000   70.36600  15.23300  1.000 53.85591  ?  1020 THR   B CA  1 
ATOM   22080 C  C   . THR   B 1 1022 ? 49.22000   69.38600  14.08900  1.000 66.23393  ?  1020 THR   B C   1 
ATOM   22081 O  O   . THR   B 1 1022 ? 49.48200   68.18700  14.23800  1.000 80.05573  ?  1020 THR   B O   1 
ATOM   22082 C  CB  . THR   B 1 1022 ? 48.30100   71.35500  15.38000  1.000 66.45590  ?  1020 THR   B CB  1 
ATOM   22083 O  OG1 . THR   B 1 1022 ? 48.67500   72.38300  16.30300  1.000 72.23807  ?  1020 THR   B OG1 1 
ATOM   22084 C  CG2 . THR   B 1 1022 ? 47.05900   70.66400  15.90800  1.000 47.82088  ?  1020 THR   B CG2 1 
ATOM   22085 N  N   . ILE   B 1 1023 ? 48.78300   69.89900  12.93200  1.000 57.22314  ?  1021 ILE   B N   1 
ATOM   22086 C  CA  . ILE   B 1 1023 ? 48.41500   69.09800  11.76400  1.000 43.43207  ?  1021 ILE   B CA  1 
ATOM   22087 C  C   . ILE   B 1 1023 ? 49.40000   67.95800  11.51900  1.000 56.30944  ?  1021 ILE   B C   1 
ATOM   22088 O  O   . ILE   B 1 1023 ? 49.00300   66.85600  11.12400  1.000 56.05996  ?  1021 ILE   B O   1 
ATOM   22089 C  CB  . ILE   B 1 1023 ? 48.29800   69.99400  10.51700  1.000 45.39614  ?  1021 ILE   B CB  1 
ATOM   22090 C  CG1 . ILE   B 1 1023 ? 47.25300   71.08800  10.74100  1.000 47.34433  ?  1021 ILE   B CG1 1 
ATOM   22091 C  CG2 . ILE   B 1 1023 ? 47.93200   69.17300  9.29000   1.000 55.19269  ?  1021 ILE   B CG2 1 
ATOM   22092 C  CD1 . ILE   B 1 1023 ? 47.05800   71.99000  9.54600   1.000 55.43424  ?  1021 ILE   B CD1 1 
ATOM   22093 N  N   . VAL   B 1 1024 ? 50.68900   68.20400  11.76500  1.000 50.60631  ?  1022 VAL   B N   1 
ATOM   22094 C  CA  . VAL   B 1 1024 ? 51.68400   67.14200  11.63400  1.000 56.22922  ?  1022 VAL   B CA  1 
ATOM   22095 C  C   . VAL   B 1 1024 ? 51.43000   66.03900  12.65500  1.000 56.88309  ?  1022 VAL   B C   1 
ATOM   22096 O  O   . VAL   B 1 1024 ? 51.48100   64.84600  12.33000  1.000 61.60592  ?  1022 VAL   B O   1 
ATOM   22097 C  CB  . VAL   B 1 1024 ? 53.10600   67.72200  11.76500  1.000 53.64017  ?  1022 VAL   B CB  1 
ATOM   22098 C  CG1 . VAL   B 1 1024 ? 54.09700   66.63400  12.14100  1.000 42.36580  ?  1022 VAL   B CG1 1 
ATOM   22099 C  CG2 . VAL   B 1 1024 ? 53.52900   68.38200  10.46500  1.000 60.76158  ?  1022 VAL   B CG2 1 
ATOM   22100 N  N   . SER   B 1 1025 ? 51.14900   66.41900  13.90400  1.000 64.32091  ?  1023 SER   B N   1 
ATOM   22101 C  CA  . SER   B 1 1025 ? 50.98000   65.42800  14.96400  1.000 75.83405  ?  1023 SER   B CA  1 
ATOM   22102 C  C   . SER   B 1 1025 ? 49.76400   64.54600  14.71400  1.000 67.96421  ?  1023 SER   B C   1 
ATOM   22103 O  O   . SER   B 1 1025 ? 49.82700   63.32500  14.91900  1.000 69.68250  ?  1023 SER   B O   1 
ATOM   22104 C  CB  . SER   B 1 1025 ? 50.86700   66.12700  16.31900  1.000 74.49182  ?  1023 SER   B CB  1 
ATOM   22105 O  OG  . SER   B 1 1025 ? 52.00900   66.92300  16.57800  1.000 72.49059  ?  1023 SER   B OG  1 
ATOM   22106 N  N   . ILE   B 1 1026 ? 48.64800   65.14500  14.28100  1.000 60.32513  ?  1024 ILE   B N   1 
ATOM   22107 C  CA  . ILE   B 1 1026 ? 47.46400   64.35300  13.95500  1.000 62.24076  ?  1024 ILE   B CA  1 
ATOM   22108 C  C   . ILE   B 1 1026 ? 47.75000   63.44900  12.76600  1.000 68.75222  ?  1024 ILE   B C   1 
ATOM   22109 O  O   . ILE   B 1 1026 ? 47.27800   62.30600  12.70300  1.000 71.53237  ?  1024 ILE   B O   1 
ATOM   22110 C  CB  . ILE   B 1 1026 ? 46.25200   65.26500  13.68900  1.000 54.92297  ?  1024 ILE   B CB  1 
ATOM   22111 C  CG1 . ILE   B 1 1026 ? 45.86800   66.04500  14.94600  1.000 73.83888  ?  1024 ILE   B CG1 1 
ATOM   22112 C  CG2 . ILE   B 1 1026 ? 45.04900   64.45800  13.26400  1.000 67.42519  ?  1024 ILE   B CG2 1 
ATOM   22113 C  CD1 . ILE   B 1 1026 ? 46.60600   67.36700  15.08400  1.000 63.72216  ?  1024 ILE   B CD1 1 
ATOM   22114 N  N   . TRP   B 1 1027 ? 48.53800   63.94600  11.81200  1.000 78.18851  ?  1025 TRP   B N   1 
ATOM   22115 C  CA  . TRP   B 1 1027 ? 48.95600   63.13100  10.67900  1.000 68.56070  ?  1025 TRP   B CA  1 
ATOM   22116 C  C   . TRP   B 1 1027 ? 49.76500   61.92600  11.14200  1.000 69.57857  ?  1025 TRP   B C   1 
ATOM   22117 O  O   . TRP   B 1 1027 ? 49.49800   60.79000  10.73300  1.000 79.57803  ?  1025 TRP   B O   1 
ATOM   22118 C  CB  . TRP   B 1 1027 ? 49.75300   63.99400  9.69800   1.000 56.80314  ?  1025 TRP   B CB  1 
ATOM   22119 C  CG  . TRP   B 1 1027 ? 50.25800   63.27500  8.48500   1.000 60.75003  ?  1025 TRP   B CG  1 
ATOM   22120 C  CD1 . TRP   B 1 1027 ? 49.51500   62.62300  7.54300   1.000 68.41058  ?  1025 TRP   B CD1 1 
ATOM   22121 C  CD2 . TRP   B 1 1027 ? 51.62300   63.16100  8.06800   1.000 56.12439  ?  1025 TRP   B CD2 1 
ATOM   22122 N  NE1 . TRP   B 1 1027 ? 50.33600   62.09900  6.57200   1.000 52.93455  ?  1025 TRP   B NE1 1 
ATOM   22123 C  CE2 . TRP   B 1 1027 ? 51.63500   62.41600  6.87100   1.000 60.34793  ?  1025 TRP   B CE2 1 
ATOM   22124 C  CE3 . TRP   B 1 1027 ? 52.83800   63.61200  8.59400   1.000 51.02554  ?  1025 TRP   B CE3 1 
ATOM   22125 C  CZ2 . TRP   B 1 1027 ? 52.81400   62.11200  6.19300   1.000 60.01554  ?  1025 TRP   B CZ2 1 
ATOM   22126 C  CZ3 . TRP   B 1 1027 ? 54.00700   63.30900  7.91900   1.000 57.82182  ?  1025 TRP   B CZ3 1 
ATOM   22127 C  CH2 . TRP   B 1 1027 ? 53.98700   62.56700  6.73200   1.000 41.46288  ?  1025 TRP   B CH2 1 
ATOM   22128 N  N   . LEU   B 1 1028 ? 50.74700   62.15100  12.02000  1.000 52.70416  ?  1026 LEU   B N   1 
ATOM   22129 C  CA  . LEU   B 1 1028 ? 51.54300   61.03700  12.52800  1.000 65.35818  ?  1026 LEU   B CA  1 
ATOM   22130 C  C   . LEU   B 1 1028 ? 50.70900   60.11300  13.40600  1.000 67.32281  ?  1026 LEU   B C   1 
ATOM   22131 O  O   . LEU   B 1 1028 ? 50.90500   58.89300  13.39300  1.000 70.21070  ?  1026 LEU   B O   1 
ATOM   22132 C  CB  . LEU   B 1 1028 ? 52.75300   61.55500  13.30600  1.000 54.22343  ?  1026 LEU   B CB  1 
ATOM   22133 C  CG  . LEU   B 1 1028 ? 53.87100   62.21200  12.49600  1.000 64.98644  ?  1026 LEU   B CG  1 
ATOM   22134 C  CD1 . LEU   B 1 1028 ? 55.15900   62.24400  13.30300  1.000 58.81004  ?  1026 LEU   B CD1 1 
ATOM   22135 C  CD2 . LEU   B 1 1028 ? 54.07800   61.49200  11.17300  1.000 74.85664  ?  1026 LEU   B CD2 1 
ATOM   22136 N  N   . SER   B 1 1029 ? 49.77400   60.67500  14.17400  1.000 67.23415  ?  1027 SER   B N   1 
ATOM   22137 C  CA  . SER   B 1 1029 ? 48.96700   59.85600  15.07100  1.000 75.47946  ?  1027 SER   B CA  1 
ATOM   22138 C  C   . SER   B 1 1029 ? 48.04500   58.93000  14.28800  1.000 70.99275  ?  1027 SER   B C   1 
ATOM   22139 O  O   . SER   B 1 1029 ? 47.95500   57.73300  14.58300  1.000 76.81836  ?  1027 SER   B O   1 
ATOM   22140 C  CB  . SER   B 1 1029 ? 48.16300   60.75000  16.01400  1.000 80.59866  ?  1027 SER   B CB  1 
ATOM   22141 O  OG  . SER   B 1 1029 ? 47.49100   59.97800  16.99000  1.000 84.80225  ?  1027 SER   B OG  1 
ATOM   22142 N  N   . LYS   B 1 1030 ? 47.35500   59.46700  13.27900  1.000 54.42559  ?  1028 LYS   B N   1 
ATOM   22143 C  CA  . LYS   B 1 1030 ? 46.44500   58.64900  12.48600  1.000 62.64914  ?  1028 LYS   B CA  1 
ATOM   22144 C  C   . LYS   B 1 1030 ? 47.17400   57.56200  11.70700  1.000 72.23884  ?  1028 LYS   B C   1 
ATOM   22145 O  O   . LYS   B 1 1030 ? 46.55500   56.55600  11.34300  1.000 73.13293  ?  1028 LYS   B O   1 
ATOM   22146 C  CB  . LYS   B 1 1030 ? 45.63000   59.53800  11.54700  1.000 55.01866  ?  1028 LYS   B CB  1 
ATOM   22147 C  CG  . LYS   B 1 1030 ? 44.68300   60.46000  12.29400  1.000 56.67989  ?  1028 LYS   B CG  1 
ATOM   22148 C  CD  . LYS   B 1 1030 ? 43.52600   60.92100  11.43200  1.000 67.15540  ?  1028 LYS   B CD  1 
ATOM   22149 C  CE  . LYS   B 1 1030 ? 42.30800   61.21700  12.29400  1.000 59.79254  ?  1028 LYS   B CE  1 
ATOM   22150 N  NZ  . LYS   B 1 1030 ? 41.45700   60.00800  12.49300  1.000 66.28117  ?  1028 LYS   B NZ  1 
ATOM   22151 N  N   . MET   B 1 1031 ? 48.47100   57.73700  11.44500  1.000 66.69205  ?  1029 MET   B N   1 
ATOM   22152 C  CA  . MET   B 1 1031 ? 49.26400   56.64000  10.90200  1.000 65.02305  ?  1029 MET   B CA  1 
ATOM   22153 C  C   . MET   B 1 1031 ? 49.56500   55.59800  11.96800  1.000 65.08482  ?  1029 MET   B C   1 
ATOM   22154 O  O   . MET   B 1 1031 ? 49.70000   54.41000  11.65300  1.000 70.72713  ?  1029 MET   B O   1 
ATOM   22155 C  CB  . MET   B 1 1031 ? 50.56400   57.17300  10.30100  1.000 58.39699  ?  1029 MET   B CB  1 
ATOM   22156 C  CG  . MET   B 1 1031 ? 50.35500   58.19900  9.20400   1.000 65.86797  ?  1029 MET   B CG  1 
ATOM   22157 S  SD  . MET   B 1 1031 ? 51.89700   58.84500  8.53300   1.000 71.69428  ?  1029 MET   B SD  1 
ATOM   22158 C  CE  . MET   B 1 1031 ? 51.63800   58.54300  6.78800   1.000 55.48882  ?  1029 MET   B CE  1 
ATOM   22159 N  N   . ASN   B 1 1032 ? 49.67300   56.01900  13.22500  1.000 57.66923  ?  1030 ASN   B N   1 
ATOM   22160 C  CA  . ASN   B 1 1032 ? 49.89000   55.11200  14.34900  1.000 69.65005  ?  1030 ASN   B CA  1 
ATOM   22161 C  C   . ASN   B 1 1032 ? 48.58100   54.55800  14.89300  1.000 71.95538  ?  1030 ASN   B C   1 
ATOM   22162 O  O   . ASN   B 1 1032 ? 48.40600   54.44400  16.11100  1.000 68.56264  ?  1030 ASN   B O   1 
ATOM   22163 C  CB  . ASN   B 1 1032 ? 50.67200   55.83000  15.44400  1.000 66.67600  ?  1030 ASN   B CB  1 
ATOM   22164 C  CG  . ASN   B 1 1032 ? 51.62200   54.90800  16.18100  1.000 75.42195  ?  1030 ASN   B CG  1 
ATOM   22165 O  OD1 . ASN   B 1 1032 ? 52.19400   53.99100  15.59200  1.000 75.09005  ?  1030 ASN   B OD1 1 
ATOM   22166 N  ND2 . ASN   B 1 1032 ? 51.79200   55.14400  17.47700  1.000 87.89675  ?  1030 ASN   B ND2 1 
ATOM   22167 N  N   . SER   B 1 1033 ? 47.64500   54.21500  14.00100  1.000 83.99653  ?  1031 SER   B N   1 
ATOM   22168 C  CA  . SER   B 1 1033 ? 46.33200   53.68300  14.37500  1.000 80.08030  ?  1031 SER   B CA  1 
ATOM   22169 C  C   . SER   B 1 1033 ? 45.58300   54.63900  15.30100  1.000 77.67978  ?  1031 SER   B C   1 
ATOM   22170 O  O   . SER   B 1 1033 ? 44.95000   54.22200  16.27300  1.000 85.20205  ?  1031 SER   B O   1 
ATOM   22171 C  CB  . SER   B 1 1033 ? 46.45200   52.29300  15.00500  1.000 92.92282  ?  1031 SER   B CB  1 
ATOM   22172 O  OG  . SER   B 1 1033 ? 46.94000   51.35000  14.06700  1.000 78.03004  ?  1031 SER   B OG  1 
ATOM   22173 N  N   . ASP   B 1 1034 ? 45.66000   55.93500  14.99000  1.000 76.90798  ?  1032 ASP   B N   1 
ATOM   22174 C  CA  . ASP   B 1 1034 ? 44.96700   56.98200  15.74400  1.000 62.04516  ?  1032 ASP   B CA  1 
ATOM   22175 C  C   . ASP   B 1 1034 ? 45.36400   56.96000  17.22000  1.000 65.41051  ?  1032 ASP   B C   1 
ATOM   22176 O  O   . ASP   B 1 1034 ? 44.52000   56.89500  18.11700  1.000 63.02550  ?  1032 ASP   B O   1 
ATOM   22177 C  CB  . ASP   B 1 1034 ? 43.45100   56.86500  15.57500  1.000 53.09275  ?  1032 ASP   B CB  1 
ATOM   22178 C  CG  . ASP   B 1 1034 ? 43.02400   56.93200  14.12300  1.000 64.50305  ?  1032 ASP   B CG  1 
ATOM   22179 O  OD1 . ASP   B 1 1034 ? 43.35300   55.99700  13.36400  1.000 73.61776  ?  1032 ASP   B OD1 1 
ATOM   22180 O  OD2 . ASP   B 1 1034 ? 42.36300   57.92100  13.74000  1.000 68.23057  -1 1032 ASP   B OD2 1 
ATOM   22181 N  N   . SER   B 1 1035 ? 46.67000   57.01500  17.46500  1.000 64.37251  ?  1033 SER   B N   1 
ATOM   22182 C  CA  . SER   B 1 1035 ? 47.18800   57.09200  18.82100  1.000 68.80074  ?  1033 SER   B CA  1 
ATOM   22183 C  C   . SER   B 1 1035 ? 46.78100   58.40900  19.47900  1.000 86.96304  ?  1033 SER   B C   1 
ATOM   22184 O  O   . SER   B 1 1035 ? 46.38900   59.37400  18.81700  1.000 84.36159  ?  1033 SER   B O   1 
ATOM   22185 C  CB  . SER   B 1 1035 ? 48.71100   56.95700  18.81800  1.000 63.14740  ?  1033 SER   B CB  1 
ATOM   22186 O  OG  . SER   B 1 1035 ? 49.27100   57.45300  20.02100  1.000 70.23584  ?  1033 SER   B OG  1 
ATOM   22187 N  N   . ASN   B 1 1036 ? 46.88000   58.44100  20.80900  1.000 87.48895  ?  1034 ASN   B N   1 
ATOM   22188 C  CA  . ASN   B 1 1036 ? 46.56100   59.63700  21.57500  1.000 83.53669  ?  1034 ASN   B CA  1 
ATOM   22189 C  C   . ASN   B 1 1036 ? 47.78800   60.36400  22.10700  1.000 77.59636  ?  1034 ASN   B C   1 
ATOM   22190 O  O   . ASN   B 1 1036 ? 47.65300   61.49500  22.58800  1.000 78.67026  ?  1034 ASN   B O   1 
ATOM   22191 C  CB  . ASN   B 1 1036 ? 45.63200   59.29100  22.74800  1.000 84.92635  ?  1034 ASN   B CB  1 
ATOM   22192 C  CG  . ASN   B 1 1036 ? 44.19700   59.07600  22.30900  1.000 100.48444 ?  1034 ASN   B CG  1 
ATOM   22193 O  OD1 . ASN   B 1 1036 ? 43.45500   60.03300  22.08700  1.000 102.27744 ?  1034 ASN   B OD1 1 
ATOM   22194 N  ND2 . ASN   B 1 1036 ? 43.79800   57.81600  22.18200  1.000 108.26836 ?  1034 ASN   B ND2 1 
ATOM   22195 N  N   . GLN   B 1 1037 ? 48.96900   59.75600  22.03400  1.000 58.20725  ?  1035 GLN   B N   1 
ATOM   22196 C  CA  . GLN   B 1 1037 ? 50.20300   60.38200  22.49800  1.000 72.35537  ?  1035 GLN   B CA  1 
ATOM   22197 C  C   . GLN   B 1 1037 ? 51.30100   60.09700  21.48700  1.000 81.37232  ?  1035 GLN   B C   1 
ATOM   22198 O  O   . GLN   B 1 1037 ? 51.63400   58.93300  21.24400  1.000 90.56340  ?  1035 GLN   B O   1 
ATOM   22199 C  CB  . GLN   B 1 1037 ? 50.59800   59.86700  23.88500  1.000 67.29241  ?  1035 GLN   B CB  1 
ATOM   22200 C  CG  . GLN   B 1 1037 ? 50.01200   60.67000  25.03200  1.000 73.77950  ?  1035 GLN   B CG  1 
ATOM   22201 C  CD  . GLN   B 1 1037 ? 51.02600   61.60700  25.65700  1.000 88.51269  ?  1035 GLN   B CD  1 
ATOM   22202 O  OE1 . GLN   B 1 1037 ? 50.95300   62.82400  25.48900  1.000 95.05615  ?  1035 GLN   B OE1 1 
ATOM   22203 N  NE2 . GLN   B 1 1037 ? 51.97900   61.04100  26.38800  1.000 84.69146  ?  1035 GLN   B NE2 1 
ATOM   22204 N  N   . VAL   B 1 1038 ? 51.86200   61.15400  20.90300  1.000 84.48128  ?  1036 VAL   B N   1 
ATOM   22205 C  CA  . VAL   B 1 1038 ? 52.88600   61.03400  19.87600  1.000 69.81646  ?  1036 VAL   B CA  1 
ATOM   22206 C  C   . VAL   B 1 1038 ? 54.15500   61.73400  20.35400  1.000 63.78419  ?  1036 VAL   B C   1 
ATOM   22207 O  O   . VAL   B 1 1038 ? 54.15100   62.49000  21.32600  1.000 69.79366  ?  1036 VAL   B O   1 
ATOM   22208 C  CB  . VAL   B 1 1038 ? 52.42500   61.60800  18.52200  1.000 72.03395  ?  1036 VAL   B CB  1 
ATOM   22209 C  CG1 . VAL   B 1 1038 ? 51.00300   61.16700  18.21500  1.000 70.00675  ?  1036 VAL   B CG1 1 
ATOM   22210 C  CG2 . VAL   B 1 1038 ? 52.54000   63.12600  18.51700  1.000 68.48042  ?  1036 VAL   B CG2 1 
ATOM   22211 N  N   . ILE   B 1 1039 ? 55.25000   61.46800  19.64600  1.000 55.65714  ?  1037 ILE   B N   1 
ATOM   22212 C  CA  . ILE   B 1 1039 ? 56.54700   62.07000  19.92700  1.000 58.32503  ?  1037 ILE   B CA  1 
ATOM   22213 C  C   . ILE   B 1 1039 ? 57.15500   62.53400  18.61100  1.000 69.15562  ?  1037 ILE   B C   1 
ATOM   22214 O  O   . ILE   B 1 1039 ? 57.09500   61.82300  17.60200  1.000 63.91804  ?  1037 ILE   B O   1 
ATOM   22215 C  CB  . ILE   B 1 1039 ? 57.48500   61.08600  20.66100  1.000 48.24645  ?  1037 ILE   B CB  1 
ATOM   22216 C  CG1 . ILE   B 1 1039 ? 58.90300   61.65300  20.75700  1.000 58.31040  ?  1037 ILE   B CG1 1 
ATOM   22217 C  CG2 . ILE   B 1 1039 ? 57.48100   59.72300  19.98000  1.000 74.85497  ?  1037 ILE   B CG2 1 
ATOM   22218 C  CD1 . ILE   B 1 1039 ? 59.87200   60.74800  21.48000  1.000 56.22451  ?  1037 ILE   B CD1 1 
ATOM   22219 N  N   . LEU   B 1 1040 ? 57.72800   63.73500  18.61800  1.000 68.24314  ?  1038 LEU   B N   1 
ATOM   22220 C  CA  . LEU   B 1 1040 ? 58.26100   64.35300  17.41200  1.000 47.52166  ?  1038 LEU   B CA  1 
ATOM   22221 C  C   . LEU   B 1 1040 ? 59.61600   64.96800  17.73700  1.000 54.98244  ?  1038 LEU   B C   1 
ATOM   22222 O  O   . LEU   B 1 1040 ? 60.15900   64.79100  18.83200  1.000 68.39749  ?  1038 LEU   B O   1 
ATOM   22223 C  CB  . LEU   B 1 1040 ? 57.28100   65.39900  16.86500  1.000 61.48176  ?  1038 LEU   B CB  1 
ATOM   22224 C  CG  . LEU   B 1 1040 ? 56.46000   65.02200  15.63600  1.000 77.18961  ?  1038 LEU   B CG  1 
ATOM   22225 C  CD1 . LEU   B 1 1040 ? 55.30200   65.99000  15.47800  1.000 71.42658  ?  1038 LEU   B CD1 1 
ATOM   22226 C  CD2 . LEU   B 1 1040 ? 57.33900   65.02700  14.39500  1.000 82.90093  ?  1038 LEU   B CD2 1 
ATOM   22227 N  N   . GLY   B 1 1041 ? 60.16500   65.69500  16.76700  1.000 60.36888  ?  1039 GLY   B N   1 
ATOM   22228 C  CA  . GLY   B 1 1041 ? 61.38200   66.44700  16.98000  1.000 57.54899  ?  1039 GLY   B CA  1 
ATOM   22229 C  C   . GLY   B 1 1041 ? 61.25000   67.82300  16.36100  1.000 59.84789  ?  1039 GLY   B C   1 
ATOM   22230 O  O   . GLY   B 1 1041 ? 60.46300   68.04100  15.43700  1.000 57.69472  ?  1039 GLY   B O   1 
ATOM   22231 N  N   . THR   B 1 1042 ? 62.03300   68.75900  16.89300  1.000 61.93143  ?  1040 THR   B N   1 
ATOM   22232 C  CA  . THR   B 1 1042 ? 61.97300   70.13200  16.41900  1.000 50.49645  ?  1040 THR   B CA  1 
ATOM   22233 C  C   . THR   B 1 1042 ? 63.31400   70.80700  16.66500  1.000 45.77353  ?  1040 THR   B C   1 
ATOM   22234 O  O   . THR   B 1 1042 ? 64.11700   70.36000  17.48800  1.000 52.51573  ?  1040 THR   B O   1 
ATOM   22235 C  CB  . THR   B 1 1042 ? 60.83900   70.91300  17.09800  1.000 43.58738  ?  1040 THR   B CB  1 
ATOM   22236 O  OG1 . THR   B 1 1042 ? 60.50700   72.06300  16.31100  1.000 44.85738  ?  1040 THR   B OG1 1 
ATOM   22237 C  CG2 . THR   B 1 1042 ? 61.25400   71.36400  18.49100  1.000 49.02128  ?  1040 THR   B CG2 1 
ATOM   22238 N  N   . VAL   B 1 1043 ? 63.54600   71.88900  15.92800  1.000 53.59942  ?  1041 VAL   B N   1 
ATOM   22239 C  CA  . VAL   B 1 1043 ? 64.77200   72.67400  16.02000  1.000 54.25741  ?  1041 VAL   B CA  1 
ATOM   22240 C  C   . VAL   B 1 1043 ? 64.42200   74.03400  16.60400  1.000 60.28130  ?  1041 VAL   B C   1 
ATOM   22241 O  O   . VAL   B 1 1043 ? 63.44300   74.66300  16.18400  1.000 52.32961  ?  1041 VAL   B O   1 
ATOM   22242 C  CB  . VAL   B 1 1043 ? 65.44700   72.82900  14.64600  1.000 50.95449  ?  1041 VAL   B CB  1 
ATOM   22243 C  CG1 . VAL   B 1 1043 ? 66.84500   73.35800  14.80900  1.000 63.63050  ?  1041 VAL   B CG1 1 
ATOM   22244 C  CG2 . VAL   B 1 1043 ? 65.47200   71.51000  13.91800  1.000 57.11081  ?  1041 VAL   B CG2 1 
ATOM   22245 N  N   . THR   B 1 1044 ? 65.22000   74.48900  17.56300  1.000 61.35646  ?  1042 THR   B N   1 
ATOM   22246 C  CA  . THR   B 1 1044 ? 65.04400   75.79500  18.17700  1.000 62.54066  ?  1042 THR   B CA  1 
ATOM   22247 C  C   . THR   B 1 1044 ? 66.18300   76.72100  17.77000  1.000 58.45400  ?  1042 THR   B C   1 
ATOM   22248 O  O   . THR   B 1 1044 ? 67.24800   76.27600  17.33800  1.000 56.71434  ?  1042 THR   B O   1 
ATOM   22249 C  CB  . THR   B 1 1044 ? 64.97300   75.68100  19.70300  1.000 59.06772  ?  1042 THR   B CB  1 
ATOM   22250 O  OG1 . THR   B 1 1044 ? 66.15800   75.04000  20.19300  1.000 74.83970  ?  1042 THR   B OG1 1 
ATOM   22251 C  CG2 . THR   B 1 1044 ? 63.75300   74.87200  20.11700  1.000 37.81491  ?  1042 THR   B CG2 1 
ATOM   22252 N  N   . ASP   B 1 1045 ? 65.93900   78.02600  17.91400  1.000 57.89316  ?  1043 ASP   B N   1 
ATOM   22253 C  CA  . ASP   B 1 1045 ? 66.91400   79.02400  17.48000  1.000 56.73420  ?  1043 ASP   B CA  1 
ATOM   22254 C  C   . ASP   B 1 1045 ? 68.24300   78.85900  18.20600  1.000 63.41896  ?  1043 ASP   B C   1 
ATOM   22255 O  O   . ASP   B 1 1045 ? 69.31300   78.91100  17.58800  1.000 62.29596  ?  1043 ASP   B O   1 
ATOM   22256 C  CB  . ASP   B 1 1045 ? 66.35300   80.43000  17.70000  1.000 59.52624  ?  1043 ASP   B CB  1 
ATOM   22257 C  CG  . ASP   B 1 1045 ? 65.69600   80.58900  19.06000  1.000 83.85884  ?  1043 ASP   B CG  1 
ATOM   22258 O  OD1 . ASP   B 1 1045 ? 64.60800   80.00900  19.26800  1.000 82.51832  ?  1043 ASP   B OD1 1 
ATOM   22259 O  OD2 . ASP   B 1 1045 ? 66.27400   81.27900  19.92600  1.000 79.04860  -1 1043 ASP   B OD2 1 
ATOM   22260 N  N   . GLY   B 1 1046 ? 68.19600   78.66000  19.52100  1.000 65.30840  ?  1044 GLY   B N   1 
ATOM   22261 C  CA  . GLY   B 1 1046 ? 69.40500   78.54500  20.31000  1.000 69.02661  ?  1044 GLY   B CA  1 
ATOM   22262 C  C   . GLY   B 1 1046 ? 70.11100   79.85000  20.58800  1.000 75.68476  ?  1044 GLY   B C   1 
ATOM   22263 O  O   . GLY   B 1 1046 ? 71.27300   79.83000  21.01200  1.000 77.70029  ?  1044 GLY   B O   1 
ATOM   22264 N  N   . ARG   B 1 1047 ? 69.45100   80.98600  20.35800  1.000 74.08809  ?  1045 ARG   B N   1 
ATOM   22265 C  CA  . ARG   B 1 1047 ? 70.03400   82.30100  20.62100  1.000 77.80898  ?  1045 ARG   B CA  1 
ATOM   22266 C  C   . ARG   B 1 1047 ? 69.63600   82.71500  22.03600  1.000 81.31465  ?  1045 ARG   B C   1 
ATOM   22267 O  O   . ARG   B 1 1047 ? 68.71500   83.50300  22.25800  1.000 76.49606  ?  1045 ARG   B O   1 
ATOM   22268 C  CB  . ARG   B 1 1047 ? 69.56700   83.30900  19.57800  1.000 72.84189  ?  1045 ARG   B CB  1 
ATOM   22269 C  CG  . ARG   B 1 1047 ? 69.70800   82.81900  18.14400  1.000 65.65919  ?  1045 ARG   B CG  1 
ATOM   22270 C  CD  . ARG   B 1 1047 ? 71.11400   83.03900  17.61400  1.000 61.29045  ?  1045 ARG   B CD  1 
ATOM   22271 N  NE  . ARG   B 1 1047 ? 71.37300   82.28000  16.39700  1.000 55.01923  ?  1045 ARG   B NE  1 
ATOM   22272 C  CZ  . ARG   B 1 1047 ? 72.32800   82.56700  15.52200  1.000 59.44287  ?  1045 ARG   B CZ  1 
ATOM   22273 N  NH1 . ARG   B 1 1047 ? 73.11000   83.62400  15.67300  1.000 59.82598  ?  1045 ARG   B NH1 1 
ATOM   22274 N  NH2 . ARG   B 1 1047 ? 72.50600   81.77200  14.47100  1.000 66.91238  ?  1045 ARG   B NH2 1 
ATOM   22275 N  N   . GLN   B 1 1048 ? 70.35600   82.15700  23.01300  1.000 71.16318  ?  1046 GLN   B N   1 
ATOM   22276 C  CA  . GLN   B 1 1048 ? 69.99100   82.37200  24.41000  1.000 74.52955  ?  1046 GLN   B CA  1 
ATOM   22277 C  C   . GLN   B 1 1048 ? 70.34300   83.78100  24.86800  1.000 75.45427  ?  1046 GLN   B C   1 
ATOM   22278 O  O   . GLN   B 1 1048 ? 69.55200   84.42900  25.56300  1.000 76.88212  ?  1046 GLN   B O   1 
ATOM   22279 C  CB  . GLN   B 1 1048 ? 70.67600   81.33200  25.29600  1.000 78.22573  ?  1046 GLN   B CB  1 
ATOM   22280 C  CG  . GLN   B 1 1048 ? 70.04500   81.18400  26.66900  1.000 71.93005  ?  1046 GLN   B CG  1 
ATOM   22281 C  CD  . GLN   B 1 1048 ? 70.62500   80.02400  27.45400  1.000 71.44562  ?  1046 GLN   B CD  1 
ATOM   22282 O  OE1 . GLN   B 1 1048 ? 71.42800   79.24800  26.93600  1.000 66.30675  ?  1046 GLN   B OE1 1 
ATOM   22283 N  NE2 . GLN   B 1 1048 ? 70.22300   79.90400  28.71400  1.000 74.77771  ?  1046 GLN   B NE2 1 
ATOM   22284 N  N   . HIS   B 1 1049 ? 71.52000   84.27100  24.49300  1.000 70.92435  ?  1047 HIS   B N   1 
ATOM   22285 C  CA  . HIS   B 1 1049 ? 71.90500   85.60300  24.93300  1.000 81.00598  ?  1047 HIS   B CA  1 
ATOM   22286 C  C   . HIS   B 1 1049 ? 71.39500   86.66000  23.95600  1.000 72.10604  ?  1047 HIS   B C   1 
ATOM   22287 O  O   . HIS   B 1 1049 ? 71.21300   86.38300  22.77000  1.000 72.58341  ?  1047 HIS   B O   1 
ATOM   22288 C  CB  . HIS   B 1 1049 ? 73.42400   85.70000  25.05500  1.000 78.23297  ?  1047 HIS   B CB  1 
ATOM   22289 C  CG  . HIS   B 1 1049 ? 73.89200   86.88300  25.84300  1.000 80.90843  ?  1047 HIS   B CG  1 
ATOM   22290 N  ND1 . HIS   B 1 1049 ? 73.73700   86.97700  27.20900  1.000 83.35581  ?  1047 HIS   B ND1 1 
ATOM   22291 C  CD2 . HIS   B 1 1049 ? 74.50400   88.02600  25.45400  1.000 83.12160  ?  1047 HIS   B CD2 1 
ATOM   22292 C  CE1 . HIS   B 1 1049 ? 74.23700   88.12600  27.62900  1.000 86.07698  ?  1047 HIS   B CE1 1 
ATOM   22293 N  NE2 . HIS   B 1 1049 ? 74.70900   88.78100  26.58300  1.000 93.90079  ?  1047 HIS   B NE2 1 
ATOM   22294 N  N   . PRO   B 1 1050 ? 71.10600   87.88000  24.41200  1.000 67.23012  ?  1048 PRO   B N   1 
ATOM   22295 C  CA  . PRO   B 1 1050 ? 70.71100   88.93100  23.46000  1.000 59.50429  ?  1048 PRO   B CA  1 
ATOM   22296 C  C   . PRO   B 1 1050 ? 71.82300   89.34600  22.51400  1.000 68.81529  ?  1048 PRO   B C   1 
ATOM   22297 O  O   . PRO   B 1 1050 ? 71.53100   89.91600  21.45500  1.000 68.09048  ?  1048 PRO   B O   1 
ATOM   22298 C  CB  . PRO   B 1 1050 ? 70.29600   90.09100  24.37100  1.000 57.98437  ?  1048 PRO   B CB  1 
ATOM   22299 C  CG  . PRO   B 1 1050 ? 69.87800   89.43100  25.63800  1.000 60.70047  ?  1048 PRO   B CG  1 
ATOM   22300 C  CD  . PRO   B 1 1050 ? 70.80300   88.25700  25.80200  1.000 83.62839  ?  1048 PRO   B CD  1 
ATOM   22301 N  N   . ASP   B 1 1051 ? 73.08100   89.08800  22.85400  1.000 73.94705  ?  1049 ASP   B N   1 
ATOM   22302 C  CA  . ASP   B 1 1051 ? 74.19700   89.47800  22.00600  1.000 70.69083  ?  1049 ASP   B CA  1 
ATOM   22303 C  C   . ASP   B 1 1051 ? 74.60900   88.39700  21.01600  1.000 58.19642  ?  1049 ASP   B C   1 
ATOM   22304 O  O   . ASP   B 1 1051 ? 75.62400   88.55800  20.33200  1.000 52.29242  ?  1049 ASP   B O   1 
ATOM   22305 C  CB  . ASP   B 1 1051 ? 75.40600   89.86900  22.86000  1.000 55.69513  ?  1049 ASP   B CB  1 
ATOM   22306 C  CG  . ASP   B 1 1051 ? 75.15700   91.11700  23.68200  1.000 65.52202  ?  1049 ASP   B CG  1 
ATOM   22307 O  OD1 . ASP   B 1 1051 ? 74.31300   91.93800  23.26200  1.000 66.71635  ?  1049 ASP   B OD1 1 
ATOM   22308 O  OD2 . ASP   B 1 1051 ? 75.80100   91.28100  24.74100  1.000 72.46871  -1 1049 ASP   B OD2 1 
ATOM   22309 N  N   . THR   B 1 1052 ? 73.86400   87.29900  20.91300  1.000 65.37716  ?  1050 THR   B N   1 
ATOM   22310 C  CA  . THR   B 1 1052 ? 74.22200   86.27200  19.94800  1.000 64.12454  ?  1050 THR   B CA  1 
ATOM   22311 C  C   . THR   B 1 1052 ? 73.31500   86.28700  18.71900  1.000 61.28291  ?  1050 THR   B C   1 
ATOM   22312 O  O   . THR   B 1 1052 ? 73.24900   85.29500  17.98700  1.000 69.09274  ?  1050 THR   B O   1 
ATOM   22313 C  CB  . THR   B 1 1052 ? 74.22200   84.88500  20.58900  1.000 65.20234  ?  1050 THR   B CB  1 
ATOM   22314 O  OG1 . THR   B 1 1052 ? 74.33300   83.92400  19.55300  1.000 89.33445  ?  1050 THR   B OG1 1 
ATOM   22315 C  CG2 . THR   B 1 1052 ? 72.92900   84.57400  21.33300  1.000 66.98840  ?  1050 THR   B CG2 1 
ATOM   22316 N  N   . ARG   B 1 1053 ? 72.62100   87.39900  18.46700  1.000 59.77857  ?  1051 ARG   B N   1 
ATOM   22317 C  CA  . ARG   B 1 1053 ? 71.67100   87.43600  17.35900  1.000 59.41409  ?  1051 ARG   B CA  1 
ATOM   22318 C  C   . ARG   B 1 1053 ? 72.35200   87.60800  16.00400  1.000 56.31034  ?  1051 ARG   B C   1 
ATOM   22319 O  O   . ARG   B 1 1053 ? 71.78400   87.21500  14.98000  1.000 73.25036  ?  1051 ARG   B O   1 
ATOM   22320 C  CB  . ARG   B 1 1053 ? 70.65200   88.54900  17.59700  1.000 66.43469  ?  1051 ARG   B CB  1 
ATOM   22321 C  CG  . ARG   B 1 1053 ? 69.88500   88.39700  18.90500  1.000 61.59541  ?  1051 ARG   B CG  1 
ATOM   22322 C  CD  . ARG   B 1 1053 ? 69.00100   89.60400  19.16900  1.000 69.08332  ?  1051 ARG   B CD  1 
ATOM   22323 N  NE  . ARG   B 1 1053 ? 69.69500   90.64600  19.91800  1.000 58.01286  ?  1051 ARG   B NE  1 
ATOM   22324 C  CZ  . ARG   B 1 1053 ? 69.26100   91.89200  20.04800  1.000 62.64551  ?  1051 ARG   B CZ  1 
ATOM   22325 N  NH1 . ARG   B 1 1053 ? 68.15100   92.30300  19.45500  1.000 60.17400  ?  1051 ARG   B NH1 1 
ATOM   22326 N  NH2 . ARG   B 1 1053 ? 69.96000   92.74900  20.78700  1.000 61.98128  ?  1051 ARG   B NH2 1 
ATOM   22327 N  N   . GLU   B 1 1054 ? 73.56200   88.16700  15.97100  1.000 59.65952  ?  1052 GLU   B N   1 
ATOM   22328 C  CA  . GLU   B 1 1054 ? 74.24000   88.48800  14.71900  1.000 64.41501  ?  1052 GLU   B CA  1 
ATOM   22329 C  C   . GLU   B 1 1054 ? 75.55500   87.73100  14.57600  1.000 47.75569  ?  1052 GLU   B C   1 
ATOM   22330 O  O   . GLU   B 1 1054 ? 76.46600   88.17900  13.87500  1.000 53.03118  ?  1052 GLU   B O   1 
ATOM   22331 C  CB  . GLU   B 1 1054 ? 74.47700   89.99100  14.60400  1.000 69.11544  ?  1052 GLU   B CB  1 
ATOM   22332 C  CG  . GLU   B 1 1054 ? 73.20400   90.79600  14.38700  1.000 82.34826  ?  1052 GLU   B CG  1 
ATOM   22333 C  CD  . GLU   B 1 1054 ? 72.45100   90.36300  13.14200  1.000 103.22495 ?  1052 GLU   B CD  1 
ATOM   22334 O  OE1 . GLU   B 1 1054 ? 73.05100   90.37800  12.04600  1.000 107.73101 ?  1052 GLU   B OE1 1 
ATOM   22335 O  OE2 . GLU   B 1 1054 ? 71.26300   89.99600  13.26200  1.000 92.80767  -1 1052 GLU   B OE2 1 
ATOM   22336 N  N   . LEU   B 1 1055 ? 75.67300   86.57900  15.22800  1.000 54.97330  ?  1053 LEU   B N   1 
ATOM   22337 C  CA  . LEU   B 1 1055 ? 76.90600   85.80600  15.20100  1.000 63.88689  ?  1053 LEU   B CA  1 
ATOM   22338 C  C   . LEU   B 1 1055 ? 76.77100   84.61500  14.26400  1.000 59.71409  ?  1053 LEU   B C   1 
ATOM   22339 O  O   . LEU   B 1 1055 ? 75.72600   83.96000  14.21500  1.000 62.91265  ?  1053 LEU   B O   1 
ATOM   22340 C  CB  . LEU   B 1 1055 ? 77.28400   85.30600  16.59100  1.000 62.16012  ?  1053 LEU   B CB  1 
ATOM   22341 C  CG  . LEU   B 1 1055 ? 77.00300   86.14700  17.83000  1.000 58.61354  ?  1053 LEU   B CG  1 
ATOM   22342 C  CD1 . LEU   B 1 1055 ? 77.64800   85.43300  18.99300  1.000 65.40787  ?  1053 LEU   B CD1 1 
ATOM   22343 C  CD2 . LEU   B 1 1055 ? 77.50600   87.58900  17.70600  1.000 62.69206  ?  1053 LEU   B CD2 1 
ATOM   22344 N  N   . LEU   B 1 1056 ? 77.85200   84.32400  13.54700  1.000 37.69527  ?  1054 LEU   B N   1 
ATOM   22345 C  CA  . LEU   B 1 1056 ? 77.88300   83.23100  12.58100  1.000 46.18757  ?  1054 LEU   B CA  1 
ATOM   22346 C  C   . LEU   B 1 1056 ? 78.41100   81.98600  13.28500  1.000 47.69382  ?  1054 LEU   B C   1 
ATOM   22347 O  O   . LEU   B 1 1056 ? 79.61800   81.84200  13.49600  1.000 55.75777  ?  1054 LEU   B O   1 
ATOM   22348 C  CB  . LEU   B 1 1056 ? 78.74500   83.60400  11.38000  1.000 45.37905  ?  1054 LEU   B CB  1 
ATOM   22349 C  CG  . LEU   B 1 1056 ? 78.12700   83.35400  10.00300  1.000 48.05305  ?  1054 LEU   B CG  1 
ATOM   22350 C  CD1 . LEU   B 1 1056 ? 77.19500   84.49300  9.60300   1.000 46.87864  ?  1054 LEU   B CD1 1 
ATOM   22351 C  CD2 . LEU   B 1 1056 ? 79.20600   83.13700  8.95100   1.000 35.52896  ?  1054 LEU   B CD2 1 
ATOM   22352 N  N   . GLY   B 1 1057 ? 77.50800   81.08400  13.64900  1.000 54.09956  ?  1055 GLY   B N   1 
ATOM   22353 C  CA  . GLY   B 1 1057 ? 77.91300   79.86300  14.31700  1.000 59.23987  ?  1055 GLY   B CA  1 
ATOM   22354 C  C   . GLY   B 1 1057 ? 76.75700   78.89300  14.41200  1.000 67.26847  ?  1055 GLY   B C   1 
ATOM   22355 O  O   . GLY   B 1 1057 ? 75.65900   79.14500  13.91100  1.000 60.55032  ?  1055 GLY   B O   1 
ATOM   22356 N  N   . MET   B 1 1058 ? 77.02600   77.76900  15.06900  1.000 70.54544  ?  1056 MET   B N   1 
ATOM   22357 C  CA  . MET   B 1 1058 ? 76.03200   76.72100  15.26500  1.000 61.61863  ?  1056 MET   B CA  1 
ATOM   22358 C  C   . MET   B 1 1058 ? 75.36500   76.93000  16.62000  1.000 59.94560  ?  1056 MET   B C   1 
ATOM   22359 O  O   . MET   B 1 1058 ? 76.01800   76.81900  17.66400  1.000 71.53250  ?  1056 MET   B O   1 
ATOM   22360 C  CB  . MET   B 1 1058 ? 76.68500   75.34300  15.16900  1.000 59.39982  ?  1056 MET   B CB  1 
ATOM   22361 C  CG  . MET   B 1 1058 ? 75.86000   74.20300  15.74000  1.000 77.49197  ?  1056 MET   B CG  1 
ATOM   22362 S  SD  . MET   B 1 1058 ? 74.25400   73.99300  14.95100  1.000 74.85614  ?  1056 MET   B SD  1 
ATOM   22363 C  CE  . MET   B 1 1058 ? 73.67600   72.49000  15.74200  1.000 66.44841  ?  1056 MET   B CE  1 
ATOM   22364 N  N   . PHE   B 1 1059 ? 74.06800   77.23900  16.60300  1.000 55.79756  ?  1057 PHE   B N   1 
ATOM   22365 C  CA  . PHE   B 1 1059 ? 73.32000   77.51500  17.81900  1.000 59.84613  ?  1057 PHE   B CA  1 
ATOM   22366 C  C   . PHE   B 1 1059 ? 72.10100   76.63400  18.01700  1.000 69.25681  ?  1057 PHE   B C   1 
ATOM   22367 O  O   . PHE   B 1 1059 ? 71.62900   76.52300  19.15300  1.000 80.83775  ?  1057 PHE   B O   1 
ATOM   22368 C  CB  . PHE   B 1 1059 ? 72.83100   78.97200  17.84500  1.000 63.20610  ?  1057 PHE   B CB  1 
ATOM   22369 C  CG  . PHE   B 1 1059 ? 73.92400   79.99200  17.90300  1.000 67.33258  ?  1057 PHE   B CG  1 
ATOM   22370 C  CD1 . PHE   B 1 1059 ? 74.47700   80.50000  16.74200  1.000 75.72912  ?  1057 PHE   B CD1 1 
ATOM   22371 C  CD2 . PHE   B 1 1059 ? 74.37600   80.46600  19.11900  1.000 60.31807  ?  1057 PHE   B CD2 1 
ATOM   22372 C  CE1 . PHE   B 1 1059 ? 75.47100   81.45300  16.79300  1.000 69.75698  ?  1057 PHE   B CE1 1 
ATOM   22373 C  CE2 . PHE   B 1 1059 ? 75.37900   81.39800  19.17600  1.000 68.97071  ?  1057 PHE   B CE2 1 
ATOM   22374 C  CZ  . PHE   B 1 1059 ? 75.91900   81.90700  18.01100  1.000 64.72641  ?  1057 PHE   B CZ  1 
ATOM   22375 N  N   . VAL   B 1 1060 ? 71.56500   76.02600  16.95700  1.000 78.12165  ?  1058 VAL   B N   1 
ATOM   22376 C  CA  . VAL   B 1 1060 ? 70.25600   75.39400  17.04900  1.000 64.47568  ?  1058 VAL   B CA  1 
ATOM   22377 C  C   . VAL   B 1 1060 ? 70.32100   74.14400  17.92000  1.000 72.46203  ?  1058 VAL   B C   1 
ATOM   22378 O  O   . VAL   B 1 1060 ? 71.35200   73.46200  18.00700  1.000 76.32890  ?  1058 VAL   B O   1 
ATOM   22379 C  CB  . VAL   B 1 1060 ? 69.71500   75.07100  15.64500  1.000 51.98622  ?  1058 VAL   B CB  1 
ATOM   22380 C  CG1 . VAL   B 1 1060 ? 69.37400   76.35300  14.90200  1.000 79.50289  ?  1058 VAL   B CG1 1 
ATOM   22381 C  CG2 . VAL   B 1 1060 ? 70.71800   74.25600  14.85900  1.000 61.07880  ?  1058 VAL   B CG2 1 
ATOM   22382 N  N   . ASN   B 1 1061 ? 69.20100   73.84200  18.57600  1.000 60.71180  ?  1059 ASN   B N   1 
ATOM   22383 C  CA  . ASN   B 1 1061 ? 69.08800   72.72700  19.50300  1.000 64.36677  ?  1059 ASN   B CA  1 
ATOM   22384 C  C   . ASN   B 1 1061 ? 67.91200   71.85600  19.09000  1.000 68.77600  ?  1059 ASN   B C   1 
ATOM   22385 O  O   . ASN   B 1 1061 ? 66.85000   72.36600  18.72000  1.000 68.61712  ?  1059 ASN   B O   1 
ATOM   22386 C  CB  . ASN   B 1 1061 ? 68.90900   73.23800  20.94500  1.000 75.73490  ?  1059 ASN   B CB  1 
ATOM   22387 C  CG  . ASN   B 1 1061 ? 68.75700   72.11800  21.96400  1.000 87.51053  ?  1059 ASN   B CG  1 
ATOM   22388 O  OD1 . ASN   B 1 1061 ? 68.82800   70.93400  21.63200  1.000 85.13941  ?  1059 ASN   B OD1 1 
ATOM   22389 N  ND2 . ASN   B 1 1061 ? 68.55700   72.49700  23.22200  1.000 72.95124  ?  1059 ASN   B ND2 1 
ATOM   22390 N  N   . THR   B 1 1062 ? 68.10900   70.54000  19.14300  1.000 66.41291  ?  1060 THR   B N   1 
ATOM   22391 C  CA  . THR   B 1 1062 ? 67.05400   69.58800  18.82300  1.000 60.58948  ?  1060 THR   B CA  1 
ATOM   22392 C  C   . THR   B 1 1062 ? 66.30500   69.21400  20.09600  1.000 52.89225  ?  1060 THR   B C   1 
ATOM   22393 O  O   . THR   B 1 1062 ? 66.92000   68.92300  21.12600  1.000 60.39942  ?  1060 THR   B O   1 
ATOM   22394 C  CB  . THR   B 1 1062 ? 67.63100   68.34300  18.14800  1.000 59.41290  ?  1060 THR   B CB  1 
ATOM   22395 O  OG1 . THR   B 1 1062 ? 66.65200   67.29700  18.15300  1.000 81.07436  ?  1060 THR   B OG1 1 
ATOM   22396 C  CG2 . THR   B 1 1062 ? 68.88600   67.87300  18.86500  1.000 55.83348  ?  1060 THR   B CG2 1 
ATOM   22397 N  N   . LEU   B 1 1063 ? 64.97300   69.22600  20.02100  1.000 49.27110  ?  1061 LEU   B N   1 
ATOM   22398 C  CA  . LEU   B 1 1063 ? 64.13000   69.05900  21.19600  1.000 64.90233  ?  1061 LEU   B CA  1 
ATOM   22399 C  C   . LEU   B 1 1063 ? 63.09100   67.97200  20.95500  1.000 66.74233  ?  1061 LEU   B C   1 
ATOM   22400 O  O   . LEU   B 1 1063 ? 62.37100   68.01500  19.94200  1.000 70.10953  ?  1061 LEU   B O   1 
ATOM   22401 C  CB  . LEU   B 1 1063 ? 63.43500   70.38000  21.55000  1.000 57.85351  ?  1061 LEU   B CB  1 
ATOM   22402 C  CG  . LEU   B 1 1063 ? 63.89300   71.09700  22.81800  1.000 53.22531  ?  1061 LEU   B CG  1 
ATOM   22403 C  CD1 . LEU   B 1 1063 ? 65.39900   71.29800  22.81300  1.000 55.19121  ?  1061 LEU   B CD1 1 
ATOM   22404 C  CD2 . LEU   B 1 1063 ? 63.17300   72.42500  22.93200  1.000 62.78279  ?  1061 LEU   B CD2 1 
ATOM   22405 N  N   . PRO   B 1 1064 ? 62.97400   66.99100  21.85000  1.000 69.21732  ?  1062 PRO   B N   1 
ATOM   22406 C  CA  . PRO   B 1 1064 ? 61.88100   66.01100  21.74500  1.000 61.80706  ?  1062 PRO   B CA  1 
ATOM   22407 C  C   . PRO   B 1 1064 ? 60.55500   66.66100  22.11300  1.000 53.23406  ?  1062 PRO   B C   1 
ATOM   22408 O  O   . PRO   B 1 1064 ? 60.40400   67.21000  23.20600  1.000 68.49991  ?  1062 PRO   B O   1 
ATOM   22409 C  CB  . PRO   B 1 1064 ? 62.27700   64.92200  22.75200  1.000 65.47374  ?  1062 PRO   B CB  1 
ATOM   22410 C  CG  . PRO   B 1 1064 ? 63.71900   65.18800  23.08500  1.000 86.94097  ?  1062 PRO   B CG  1 
ATOM   22411 C  CD  . PRO   B 1 1064 ? 63.91800   66.65600  22.92800  1.000 76.51789  ?  1062 PRO   B CD  1 
ATOM   22412 N  N   . LEU   B 1 1065 ? 59.59500   66.60100  21.19500  1.000 53.02053  ?  1063 LEU   B N   1 
ATOM   22413 C  CA  . LEU   B 1 1065 ? 58.28000   67.21100  21.38700  1.000 68.76875  ?  1063 LEU   B CA  1 
ATOM   22414 C  C   . LEU   B 1 1065 ? 57.25600   66.10600  21.63000  1.000 80.49647  ?  1063 LEU   B C   1 
ATOM   22415 O  O   . LEU   B 1 1065 ? 56.68500   65.54700  20.69300  1.000 77.40132  ?  1063 LEU   B O   1 
ATOM   22416 C  CB  . LEU   B 1 1065 ? 57.89000   68.07500  20.19500  1.000 60.06537  ?  1063 LEU   B CB  1 
ATOM   22417 C  CG  . LEU   B 1 1065 ? 58.38900   69.51700  20.24500  1.000 66.07310  ?  1063 LEU   B CG  1 
ATOM   22418 C  CD1 . LEU   B 1 1065 ? 57.61400   70.36700  19.25800  1.000 60.29922  ?  1063 LEU   B CD1 1 
ATOM   22419 C  CD2 . LEU   B 1 1065 ? 58.27000   70.08000  21.65400  1.000 63.16355  ?  1063 LEU   B CD2 1 
ATOM   22420 N  N   . LEU   B 1 1066 ? 57.02200   65.80500  22.90400  1.000 81.19726  ?  1064 LEU   B N   1 
ATOM   22421 C  CA  . LEU   B 1 1066 ? 56.01400   64.82900  23.29600  1.000 62.63827  ?  1064 LEU   B CA  1 
ATOM   22422 C  C   . LEU   B 1 1066 ? 54.66000   65.52900  23.33000  1.000 47.79943  ?  1064 LEU   B C   1 
ATOM   22423 O  O   . LEU   B 1 1066 ? 54.43600   66.42000  24.15400  1.000 63.29818  ?  1064 LEU   B O   1 
ATOM   22424 C  CB  . LEU   B 1 1066 ? 56.37400   64.22200  24.64900  1.000 46.76626  ?  1064 LEU   B CB  1 
ATOM   22425 C  CG  . LEU   B 1 1066 ? 55.81200   62.83800  24.96800  1.000 47.26979  ?  1064 LEU   B CG  1 
ATOM   22426 C  CD1 . LEU   B 1 1066 ? 56.82300   62.04100  25.77000  1.000 69.92990  ?  1064 LEU   B CD1 1 
ATOM   22427 C  CD2 . LEU   B 1 1066 ? 54.50900   62.95800  25.73100  1.000 58.14315  ?  1064 LEU   B CD2 1 
ATOM   22428 N  N   . LEU   B 1 1067 ? 53.76200   65.13900  22.43100  1.000 53.39445  ?  1065 LEU   B N   1 
ATOM   22429 C  CA  . LEU   B 1 1067 ? 52.47800   65.80300  22.26200  1.000 64.46736  ?  1065 LEU   B CA  1 
ATOM   22430 C  C   . LEU   B 1 1067 ? 51.33600   64.82300  22.50100  1.000 65.52675  ?  1065 LEU   B C   1 
ATOM   22431 O  O   . LEU   B 1 1067 ? 51.54100   63.62000  22.68800  1.000 72.63543  ?  1065 LEU   B O   1 
ATOM   22432 C  CB  . LEU   B 1 1067 ? 52.36300   66.42700  20.86500  1.000 67.57764  ?  1065 LEU   B CB  1 
ATOM   22433 C  CG  . LEU   B 1 1067 ? 53.29300   67.61000  20.58300  1.000 71.19076  ?  1065 LEU   B CG  1 
ATOM   22434 C  CD1 . LEU   B 1 1067 ? 54.13800   67.35900  19.34200  1.000 71.08483  ?  1065 LEU   B CD1 1 
ATOM   22435 C  CD2 . LEU   B 1 1067 ? 52.49100   68.89400  20.43800  1.000 59.54521  ?  1065 LEU   B CD2 1 
ATOM   22436 N  N   . SER   B 1 1068 ? 50.11600   65.35900  22.49100  1.000 57.82739  ?  1066 SER   B N   1 
ATOM   22437 C  CA  . SER   B 1 1068 ? 48.91300   64.58100  22.75500  1.000 54.08437  ?  1066 SER   B CA  1 
ATOM   22438 C  C   . SER   B 1 1068 ? 47.78100   65.07800  21.86900  1.000 66.95019  ?  1066 SER   B C   1 
ATOM   22439 O  O   . SER   B 1 1068 ? 47.63000   66.28600  21.66400  1.000 66.86474  ?  1066 SER   B O   1 
ATOM   22440 C  CB  . SER   B 1 1068 ? 48.49800   64.68000  24.22700  1.000 51.84462  ?  1066 SER   B CB  1 
ATOM   22441 O  OG  . SER   B 1 1068 ? 49.61000   64.49500  25.08400  1.000 72.01093  ?  1066 SER   B OG  1 
ATOM   22442 N  N   . ILE   B 1 1069 ? 46.98500   64.14400  21.35200  1.000 69.59900  ?  1067 ILE   B N   1 
ATOM   22443 C  CA  . ILE   B 1 1069 ? 45.84600   64.45900  20.49700  1.000 59.14643  ?  1067 ILE   B CA  1 
ATOM   22444 C  C   . ILE   B 1 1069 ? 44.62600   63.71800  21.02500  1.000 83.24416  ?  1067 ILE   B C   1 
ATOM   22445 O  O   . ILE   B 1 1069 ? 44.69100   62.51000  21.28000  1.000 87.97458  ?  1067 ILE   B O   1 
ATOM   22446 C  CB  . ILE   B 1 1069 ? 46.10200   64.08700  19.02300  1.000 63.46759  ?  1067 ILE   B CB  1 
ATOM   22447 C  CG1 . ILE   B 1 1069 ? 47.34300   64.80300  18.48500  1.000 68.40082  ?  1067 ILE   B CG1 1 
ATOM   22448 C  CG2 . ILE   B 1 1069 ? 44.88800   64.42300  18.16500  1.000 64.23078  ?  1067 ILE   B CG2 1 
ATOM   22449 C  CD1 . ILE   B 1 1069 ? 48.60700   63.96900  18.54100  1.000 83.82296  ?  1067 ILE   B CD1 1 
ATOM   22450 N  N   . ASP   B 1 1070 ? 43.52100   64.44100  21.19200  1.000 79.78014  ?  1068 ASP   B N   1 
ATOM   22451 C  CA  . ASP   B 1 1070 ? 42.23500   63.86500  21.56900  1.000 65.38706  ?  1068 ASP   B CA  1 
ATOM   22452 C  C   . ASP   B 1 1070 ? 41.33500   63.91200  20.34100  1.000 78.84639  ?  1068 ASP   B C   1 
ATOM   22453 O  O   . ASP   B 1 1070 ? 40.84200   64.98200  19.96700  1.000 84.14139  ?  1068 ASP   B O   1 
ATOM   22454 C  CB  . ASP   B 1 1070 ? 41.61700   64.61800  22.74800  1.000 81.09810  ?  1068 ASP   B CB  1 
ATOM   22455 C  CG  . ASP   B 1 1070 ? 40.29200   64.02200  23.19800  1.000 92.12063  ?  1068 ASP   B CG  1 
ATOM   22456 O  OD1 . ASP   B 1 1070 ? 39.29800   64.11700  22.44700  1.000 74.50609  ?  1068 ASP   B OD1 1 
ATOM   22457 O  OD2 . ASP   B 1 1070 ? 40.24700   63.45000  24.30700  1.000 108.72465 -1 1068 ASP   B OD2 1 
ATOM   22458 N  N   . HIS   B 1 1071 ? 41.12500   62.75200  19.71600  1.000 69.07998  ?  1069 HIS   B N   1 
ATOM   22459 C  CA  . HIS   B 1 1071 ? 40.34800   62.70400  18.48300  1.000 61.46649  ?  1069 HIS   B CA  1 
ATOM   22460 C  C   . HIS   B 1 1071 ? 38.87900   63.02300  18.72600  1.000 69.10563  ?  1069 HIS   B C   1 
ATOM   22461 O  O   . HIS   B 1 1071 ? 38.20000   63.52800  17.82500  1.000 76.01206  ?  1069 HIS   B O   1 
ATOM   22462 C  CB  . HIS   B 1 1071 ? 40.49600   61.33200  17.82700  1.000 57.54431  ?  1069 HIS   B CB  1 
ATOM   22463 C  CG  . HIS   B 1 1071 ? 41.91800   60.93600  17.57600  1.000 75.17173  ?  1069 HIS   B CG  1 
ATOM   22464 N  ND1 . HIS   B 1 1071 ? 42.46900   60.90000  16.31300  1.000 73.73354  ?  1069 HIS   B ND1 1 
ATOM   22465 C  CD2 . HIS   B 1 1071 ? 42.90400   60.56600  18.42700  1.000 65.90311  ?  1069 HIS   B CD2 1 
ATOM   22466 C  CE1 . HIS   B 1 1071 ? 43.73200   60.52100  16.39700  1.000 61.80118  ?  1069 HIS   B CE1 1 
ATOM   22467 N  NE2 . HIS   B 1 1071 ? 44.02100   60.31200  17.66900  1.000 59.43631  ?  1069 HIS   B NE2 1 
ATOM   22468 N  N   . GLU   B 1 1072 ? 38.37100   62.74100  19.92800  1.000 77.12019  ?  1070 GLU   B N   1 
ATOM   22469 C  CA  . GLU   B 1 1072 ? 36.97200   63.02500  20.22500  1.000 74.59905  ?  1070 GLU   B CA  1 
ATOM   22470 C  C   . GLU   B 1 1072 ? 36.69900   64.51700  20.35900  1.000 83.94477  ?  1070 GLU   B C   1 
ATOM   22471 O  O   . GLU   B 1 1072 ? 35.54600   64.93800  20.21800  1.000 69.99778  ?  1070 GLU   B O   1 
ATOM   22472 C  CB  . GLU   B 1 1072 ? 36.54300   62.30300  21.50300  1.000 65.71658  ?  1070 GLU   B CB  1 
ATOM   22473 C  CG  . GLU   B 1 1072 ? 35.27800   61.47700  21.34100  1.000 72.81434  ?  1070 GLU   B CG  1 
ATOM   22474 C  CD  . GLU   B 1 1072 ? 35.47100   60.30200  20.40200  1.000 75.95956  ?  1070 GLU   B CD  1 
ATOM   22475 O  OE1 . GLU   B 1 1072 ? 36.47100   59.57000  20.56200  1.000 71.04524  ?  1070 GLU   B OE1 1 
ATOM   22476 O  OE2 . GLU   B 1 1072 ? 34.62900   60.11500  19.49800  1.000 66.60542  -1 1070 GLU   B OE2 1 
ATOM   22477 N  N   . GLU   B 1 1073 ? 37.72500   65.32100  20.62600  1.000 91.69138  ?  1071 GLU   B N   1 
ATOM   22478 C  CA  . GLU   B 1 1073 ? 37.56000   66.76200  20.73100  1.000 86.71536  ?  1071 GLU   B CA  1 
ATOM   22479 C  C   . GLU   B 1 1073 ? 37.79200   67.39700  19.35900  1.000 86.34558  ?  1071 GLU   B C   1 
ATOM   22480 O  O   . GLU   B 1 1073 ? 37.90500   66.70700  18.34200  1.000 80.82516  ?  1071 GLU   B O   1 
ATOM   22481 C  CB  . GLU   B 1 1073 ? 38.49300   67.32600  21.80000  1.000 79.04060  ?  1071 GLU   B CB  1 
ATOM   22482 C  CG  . GLU   B 1 1073 ? 37.81200   68.31200  22.73500  1.000 80.12949  ?  1071 GLU   B CG  1 
ATOM   22483 C  CD  . GLU   B 1 1073 ? 36.64400   67.69700  23.48300  1.000 86.50991  ?  1071 GLU   B CD  1 
ATOM   22484 O  OE1 . GLU   B 1 1073 ? 36.85700   66.70600  24.21400  1.000 89.65866  ?  1071 GLU   B OE1 1 
ATOM   22485 O  OE2 . GLU   B 1 1073 ? 35.50900   68.19800  23.33200  1.000 77.87491  -1 1071 GLU   B OE2 1 
ATOM   22486 N  N   . SER   B 1 1074 ? 37.87300   68.72100  19.31800  1.000 82.38214  ?  1072 SER   B N   1 
ATOM   22487 C  CA  . SER   B 1 1074 ? 37.92800   69.45800  18.06400  1.000 80.44019  ?  1072 SER   B CA  1 
ATOM   22488 C  C   . SER   B 1 1074 ? 39.36800   69.78700  17.68000  1.000 84.31796  ?  1072 SER   B C   1 
ATOM   22489 O  O   . SER   B 1 1074 ? 40.31100   69.60200  18.45300  1.000 70.76519  ?  1072 SER   B O   1 
ATOM   22490 C  CB  . SER   B 1 1074 ? 37.09600   70.74000  18.16300  1.000 72.28492  ?  1072 SER   B CB  1 
ATOM   22491 O  OG  . SER   B 1 1074 ? 37.08400   71.43600  16.92900  1.000 85.22476  ?  1072 SER   B OG  1 
ATOM   22492 N  N   . PHE   B 1 1075 ? 39.52200   70.28100  16.44800  1.000 84.04271  ?  1073 PHE   B N   1 
ATOM   22493 C  CA  . PHE   B 1 1075 ? 40.83400   70.71600  15.98000  1.000 79.69510  ?  1073 PHE   B CA  1 
ATOM   22494 C  C   . PHE   B 1 1075 ? 41.29700   71.95800  16.73000  1.000 77.62517  ?  1073 PHE   B C   1 
ATOM   22495 O  O   . PHE   B 1 1075 ? 42.45700   72.04100  17.14900  1.000 56.36480  ?  1073 PHE   B O   1 
ATOM   22496 C  CB  . PHE   B 1 1075 ? 40.79000   70.97800  14.47300  1.000 76.42217  ?  1073 PHE   B CB  1 
ATOM   22497 C  CG  . PHE   B 1 1075 ? 42.08900   71.47600  13.90000  1.000 77.28683  ?  1073 PHE   B CG  1 
ATOM   22498 C  CD1 . PHE   B 1 1075 ? 43.26800   70.77600  14.10500  1.000 61.81945  ?  1073 PHE   B CD1 1 
ATOM   22499 C  CD2 . PHE   B 1 1075 ? 42.12900   72.63500  13.14000  1.000 70.43714  ?  1073 PHE   B CD2 1 
ATOM   22500 C  CE1 . PHE   B 1 1075 ? 44.46300   71.23000  13.57500  1.000 57.26743  ?  1073 PHE   B CE1 1 
ATOM   22501 C  CE2 . PHE   B 1 1075 ? 43.32100   73.09200  12.60600  1.000 68.20018  ?  1073 PHE   B CE2 1 
ATOM   22502 C  CZ  . PHE   B 1 1075 ? 44.48900   72.38800  12.82500  1.000 60.72195  ?  1073 PHE   B CZ  1 
ATOM   22503 N  N   . LEU   B 1 1076 ? 40.39800   72.92900  16.91500  1.000 65.62096  ?  1074 LEU   B N   1 
ATOM   22504 C  CA  . LEU   B 1 1076 ? 40.75400   74.14300  17.64100  1.000 57.24682  ?  1074 LEU   B CA  1 
ATOM   22505 C  C   . LEU   B 1 1076 ? 41.09000   73.83500  19.09500  1.000 64.84049  ?  1074 LEU   B C   1 
ATOM   22506 O  O   . LEU   B 1 1076 ? 41.97900   74.46500  19.67900  1.000 73.35819  ?  1074 LEU   B O   1 
ATOM   22507 C  CB  . LEU   B 1 1076 ? 39.61700   75.16100  17.55000  1.000 54.05511  ?  1074 LEU   B CB  1 
ATOM   22508 C  CG  . LEU   B 1 1076 ? 39.85800   76.52100  18.20700  1.000 60.95331  ?  1074 LEU   B CG  1 
ATOM   22509 C  CD1 . LEU   B 1 1076 ? 41.21000   77.09100  17.79900  1.000 56.63221  ?  1074 LEU   B CD1 1 
ATOM   22510 C  CD2 . LEU   B 1 1076 ? 38.74000   77.48800  17.85000  1.000 55.19852  ?  1074 LEU   B CD2 1 
ATOM   22511 N  N   . HIS   B 1 1077 ? 40.39100   72.87000  19.69500  1.000 61.09859  ?  1075 HIS   B N   1 
ATOM   22512 C  CA  . HIS   B 1 1077 ? 40.73900   72.43900  21.04400  1.000 73.11726  ?  1075 HIS   B CA  1 
ATOM   22513 C  C   . HIS   B 1 1077 ? 42.14500   71.85400  21.07500  1.000 65.68486  ?  1075 HIS   B C   1 
ATOM   22514 O  O   . HIS   B 1 1077 ? 43.00500   72.30700  21.83900  1.000 66.23070  ?  1075 HIS   B O   1 
ATOM   22515 C  CB  . HIS   B 1 1077 ? 39.71600   71.42300  21.55600  1.000 72.02357  ?  1075 HIS   B CB  1 
ATOM   22516 C  CG  . HIS   B 1 1077 ? 40.06100   70.84300  22.89300  1.000 70.01094  ?  1075 HIS   B CG  1 
ATOM   22517 N  ND1 . HIS   B 1 1077 ? 40.79800   69.68700  23.03500  1.000 85.62578  ?  1075 HIS   B ND1 1 
ATOM   22518 C  CD2 . HIS   B 1 1077 ? 39.77000   71.25900  24.14800  1.000 65.99736  ?  1075 HIS   B CD2 1 
ATOM   22519 C  CE1 . HIS   B 1 1077 ? 40.94500   69.41500  24.31900  1.000 82.48965  ?  1075 HIS   B CE1 1 
ATOM   22520 N  NE2 . HIS   B 1 1077 ? 40.33100   70.35400  25.01600  1.000 91.07711  ?  1075 HIS   B NE2 1 
ATOM   22521 N  N   . ASN   B 1 1078 ? 42.40200   70.85100  20.22900  1.000 64.65779  ?  1076 ASN   B N   1 
ATOM   22522 C  CA  . ASN   B 1 1078 ? 43.72900   70.24600  20.17300  1.000 77.89711  ?  1076 ASN   B CA  1 
ATOM   22523 C  C   . ASN   B 1 1078 ? 44.79500   71.25500  19.76800  1.000 71.46790  ?  1076 ASN   B C   1 
ATOM   22524 O  O   . ASN   B 1 1078 ? 45.96500   71.10200  20.13800  1.000 58.72984  ?  1076 ASN   B O   1 
ATOM   22525 C  CB  . ASN   B 1 1078 ? 43.72800   69.05800  19.21000  1.000 74.95425  ?  1076 ASN   B CB  1 
ATOM   22526 C  CG  . ASN   B 1 1078 ? 43.33100   67.76200  19.88600  1.000 68.84131  ?  1076 ASN   B CG  1 
ATOM   22527 O  OD1 . ASN   B 1 1078 ? 44.10800   67.18500  20.64700  1.000 65.39946  ?  1076 ASN   B OD1 1 
ATOM   22528 N  ND2 . ASN   B 1 1078 ? 42.12000   67.29300  19.60800  1.000 67.60175  ?  1076 ASN   B ND2 1 
ATOM   22529 N  N   . LEU   B 1 1079 ? 44.41500   72.28600  19.00900  1.000 60.56062  ?  1077 LEU   B N   1 
ATOM   22530 C  CA  . LEU   B 1 1079 ? 45.35500   73.35600  18.68700  1.000 54.13081  ?  1077 LEU   B CA  1 
ATOM   22531 C  C   . LEU   B 1 1079 ? 45.85500   74.04300  19.95100  1.000 60.12228  ?  1077 LEU   B C   1 
ATOM   22532 O  O   . LEU   B 1 1079 ? 47.05700   74.28900  20.10600  1.000 67.64871  ?  1077 LEU   B O   1 
ATOM   22533 C  CB  . LEU   B 1 1079 ? 44.69500   74.36800  17.75100  1.000 58.72452  ?  1077 LEU   B CB  1 
ATOM   22534 C  CG  . LEU   B 1 1079 ? 44.80600   74.12400  16.24600  1.000 54.38879  ?  1077 LEU   B CG  1 
ATOM   22535 C  CD1 . LEU   B 1 1079 ? 43.84800   75.03300  15.49700  1.000 41.69921  ?  1077 LEU   B CD1 1 
ATOM   22536 C  CD2 . LEU   B 1 1079 ? 46.23000   74.35800  15.78100  1.000 44.90463  ?  1077 LEU   B CD2 1 
ATOM   22537 N  N   . GLN   B 1 1080 ? 44.94000   74.35500  20.87300  1.000 58.30652  ?  1078 GLN   B N   1 
ATOM   22538 C  CA  . GLN   B 1 1080 ? 45.33300   75.01500  22.11400  1.000 64.12102  ?  1078 GLN   B CA  1 
ATOM   22539 C  C   . GLN   B 1 1080 ? 46.16600   74.09100  22.99500  1.000 73.63248  ?  1078 GLN   B C   1 
ATOM   22540 O  O   . GLN   B 1 1080 ? 47.10300   74.54300  23.66500  1.000 68.96774  ?  1078 GLN   B O   1 
ATOM   22541 C  CB  . GLN   B 1 1080 ? 44.09200   75.50000  22.86400  1.000 45.17234  ?  1078 GLN   B CB  1 
ATOM   22542 N  N   . GLN   B 1 1081 ? 45.84000   72.79500  23.01100  1.000 81.69009  ?  1079 GLN   B N   1 
ATOM   22543 C  CA  . GLN   B 1 1081 ? 46.62800   71.84400  23.78900  1.000 68.97835  ?  1079 GLN   B CA  1 
ATOM   22544 C  C   . GLN   B 1 1081 ? 48.06000   71.77100  23.27400  1.000 66.67900  ?  1079 GLN   B C   1 
ATOM   22545 O  O   . GLN   B 1 1081 ? 49.00400   71.62100  24.06000  1.000 74.65378  ?  1079 GLN   B O   1 
ATOM   22546 C  CB  . GLN   B 1 1081 ? 45.98300   70.45700  23.74900  1.000 66.71811  ?  1079 GLN   B CB  1 
ATOM   22547 C  CG  . GLN   B 1 1081 ? 44.46100   70.44500  23.79000  1.000 51.48164  ?  1079 GLN   B CG  1 
ATOM   22548 C  CD  . GLN   B 1 1081 ? 43.89400   70.76300  25.16000  1.000 84.17750  ?  1079 GLN   B CD  1 
ATOM   22549 O  OE1 . GLN   B 1 1081 ? 43.64900   69.86400  25.96500  1.000 93.31141  ?  1079 GLN   B OE1 1 
ATOM   22550 N  NE2 . GLN   B 1 1081 ? 43.66800   72.04400  25.42600  1.000 83.63757  ?  1079 GLN   B NE2 1 
ATOM   22551 N  N   . VAL   B 1 1082 ? 48.23900   71.87300  21.95400  1.000 63.82016  ?  1080 VAL   B N   1 
ATOM   22552 C  CA  . VAL   B 1 1082 ? 49.57800   71.81000  21.37200  1.000 78.83554  ?  1080 VAL   B CA  1 
ATOM   22553 C  C   . VAL   B 1 1082 ? 50.42800   72.97600  21.86000  1.000 80.52174  ?  1080 VAL   B C   1 
ATOM   22554 O  O   . VAL   B 1 1082 ? 51.61100   72.80900  22.18400  1.000 63.60969  ?  1080 VAL   B O   1 
ATOM   22555 C  CB  . VAL   B 1 1082 ? 49.49000   71.76700  19.83500  1.000 56.30274  ?  1080 VAL   B CB  1 
ATOM   22556 C  CG1 . VAL   B 1 1082 ? 50.84000   72.07600  19.21100  1.000 62.59769  ?  1080 VAL   B CG1 1 
ATOM   22557 C  CG2 . VAL   B 1 1082 ? 49.00200   70.40500  19.37400  1.000 43.06057  ?  1080 VAL   B CG2 1 
ATOM   22558 N  N   . LYS   B 1 1083 ? 49.84000   74.17400  21.93000  1.000 63.80358  ?  1081 LYS   B N   1 
ATOM   22559 C  CA  . LYS   B 1 1083 ? 50.56700   75.31800  22.47300  1.000 62.65877  ?  1081 LYS   B CA  1 
ATOM   22560 C  C   . LYS   B 1 1083 ? 50.93700   75.08500  23.93100  1.000 66.91175  ?  1081 LYS   B C   1 
ATOM   22561 O  O   . LYS   B 1 1083 ? 52.08200   75.31300  24.33900  1.000 64.41551  ?  1081 LYS   B O   1 
ATOM   22562 C  CB  . LYS   B 1 1083 ? 49.73800   76.59500  22.32900  1.000 60.77867  ?  1081 LYS   B CB  1 
ATOM   22563 C  CG  . LYS   B 1 1083 ? 50.11600   77.66400  23.34600  1.000 71.12629  ?  1081 LYS   B CG  1 
ATOM   22564 C  CD  . LYS   B 1 1083 ? 49.80100   79.06900  22.86700  1.000 65.71942  ?  1081 LYS   B CD  1 
ATOM   22565 C  CE  . LYS   B 1 1083 ? 48.30900   79.32100  22.80300  1.000 55.59003  ?  1081 LYS   B CE  1 
ATOM   22566 N  NZ  . LYS   B 1 1083 ? 48.02800   80.75900  22.54100  1.000 56.84217  ?  1081 LYS   B NZ  1 
ATOM   22567 N  N   . ALA   B 1 1084 ? 49.97500   74.61800  24.73300  1.000 72.04768  ?  1082 ALA   B N   1 
ATOM   22568 C  CA  . ALA   B 1 1084 ? 50.22700   74.37600  26.14800  1.000 67.22607  ?  1082 ALA   B CA  1 
ATOM   22569 C  C   . ALA   B 1 1084 ? 51.26900   73.28900  26.37300  1.000 60.41935  ?  1082 ALA   B C   1 
ATOM   22570 O  O   . ALA   B 1 1084 ? 51.82900   73.20100  27.47000  1.000 55.26041  ?  1082 ALA   B O   1 
ATOM   22571 C  CB  . ALA   B 1 1084 ? 48.92300   74.00900  26.85700  1.000 50.73247  ?  1082 ALA   B CB  1 
ATOM   22572 N  N   . LYS   B 1 1085 ? 51.53700   72.45900  25.36600  1.000 59.64425  ?  1083 LYS   B N   1 
ATOM   22573 C  CA  . LYS   B 1 1085 ? 52.60500   71.47400  25.45500  1.000 71.15595  ?  1083 LYS   B CA  1 
ATOM   22574 C  C   . LYS   B 1 1085 ? 53.91000   71.97000  24.85200  1.000 72.84511  ?  1083 LYS   B C   1 
ATOM   22575 O  O   . LYS   B 1 1085 ? 54.97200   71.41500  25.16100  1.000 75.38307  ?  1083 LYS   B O   1 
ATOM   22576 C  CB  . LYS   B 1 1085 ? 52.18400   70.17400  24.76200  1.000 52.26577  ?  1083 LYS   B CB  1 
ATOM   22577 N  N   . LEU   B 1 1086 ? 53.85700   73.00500  24.01300  1.000 58.64827  ?  1084 LEU   B N   1 
ATOM   22578 C  CA  . LEU   B 1 1086 ? 55.03300   73.52900  23.33000  1.000 78.92197  ?  1084 LEU   B CA  1 
ATOM   22579 C  C   . LEU   B 1 1086 ? 55.77300   74.56600  24.16800  1.000 79.28329  ?  1084 LEU   B C   1 
ATOM   22580 O  O   . LEU   B 1 1086 ? 56.99600   74.48300  24.32200  1.000 67.10580  ?  1084 LEU   B O   1 
ATOM   22581 C  CB  . LEU   B 1 1086 ? 54.62300   74.13400  21.98500  1.000 69.90239  ?  1084 LEU   B CB  1 
ATOM   22582 C  CG  . LEU   B 1 1086 ? 55.74400   74.79500  21.18400  1.000 58.84968  ?  1084 LEU   B CG  1 
ATOM   22583 C  CD1 . LEU   B 1 1086 ? 56.77700   73.76600  20.74500  1.000 38.34837  ?  1084 LEU   B CD1 1 
ATOM   22584 C  CD2 . LEU   B 1 1086 ? 55.17600   75.54900  19.99300  1.000 74.82948  ?  1084 LEU   B CD2 1 
ATOM   22585 N  N   . LEU   B 1 1087 ? 55.04600   75.54600  24.70400  1.000 65.52837  ?  1085 LEU   B N   1 
ATOM   22586 C  CA  . LEU   B 1 1087 ? 55.66200   76.58700  25.52300  1.000 54.26683  ?  1085 LEU   B CA  1 
ATOM   22587 C  C   . LEU   B 1 1087 ? 56.49000   76.05200  26.68800  1.000 62.59215  ?  1085 LEU   B C   1 
ATOM   22588 O  O   . LEU   B 1 1087 ? 57.56100   76.62200  26.95400  1.000 74.47735  ?  1085 LEU   B O   1 
ATOM   22589 C  CB  . LEU   B 1 1087 ? 54.57400   77.54500  26.03000  1.000 47.45300  ?  1085 LEU   B CB  1 
ATOM   22590 C  CG  . LEU   B 1 1087 ? 53.75900   78.26800  24.95600  1.000 69.22615  ?  1085 LEU   B CG  1 
ATOM   22591 C  CD1 . LEU   B 1 1087 ? 52.59700   79.02300  25.58200  1.000 54.62026  ?  1085 LEU   B CD1 1 
ATOM   22592 C  CD2 . LEU   B 1 1087 ? 54.64800   79.21100  24.16200  1.000 70.14549  ?  1085 LEU   B CD2 1 
ATOM   22593 N  N   . PRO   B 1 1088 ? 56.07700   75.00800  27.41900  1.000 61.71401  ?  1086 PRO   B N   1 
ATOM   22594 C  CA  . PRO   B 1 1088 ? 56.98100   74.44500  28.43500  1.000 58.80733  ?  1086 PRO   B CA  1 
ATOM   22595 C  C   . PRO   B 1 1088 ? 58.29000   73.93900  27.85900  1.000 62.59098  ?  1086 PRO   B C   1 
ATOM   22596 O  O   . PRO   B 1 1088 ? 59.32100   74.00300  28.54000  1.000 64.02749  ?  1086 PRO   B O   1 
ATOM   22597 C  CB  . PRO   B 1 1088 ? 56.15300   73.30500  29.04500  1.000 73.44553  ?  1086 PRO   B CB  1 
ATOM   22598 C  CG  . PRO   B 1 1088 ? 54.74600   73.71200  28.82700  1.000 69.36405  ?  1086 PRO   B CG  1 
ATOM   22599 C  CD  . PRO   B 1 1088 ? 54.73400   74.40300  27.49900  1.000 63.10270  ?  1086 PRO   B CD  1 
ATOM   22600 N  N   . ALA   B 1 1089 ? 58.28000   73.43800  26.62100  1.000 75.47760  ?  1087 ALA   B N   1 
ATOM   22601 C  CA  . ALA   B 1 1089 ? 59.51600   72.99600  25.98500  1.000 83.75390  ?  1087 ALA   B CA  1 
ATOM   22602 C  C   . ALA   B 1 1089 ? 60.31700   74.17200  25.43500  1.000 76.48196  ?  1087 ALA   B C   1 
ATOM   22603 O  O   . ALA   B 1 1089 ? 61.53600   74.23100  25.61800  1.000 65.10857  ?  1087 ALA   B O   1 
ATOM   22604 C  CB  . ALA   B 1 1089 ? 59.20500   71.98300  24.88100  1.000 69.55551  ?  1087 ALA   B CB  1 
ATOM   22605 N  N   . LEU   B 1 1090 ? 59.65200   75.12300  24.77300  1.000 81.76575  ?  1088 LEU   B N   1 
ATOM   22606 C  CA  . LEU   B 1 1090 ? 60.35100   76.28900  24.24600  1.000 68.60578  ?  1088 LEU   B CA  1 
ATOM   22607 C  C   . LEU   B 1 1090 ? 60.90100   77.19600  25.34200  1.000 77.56869  ?  1088 LEU   B C   1 
ATOM   22608 O  O   . LEU   B 1 1090 ? 61.85300   77.93900  25.09100  1.000 88.78235  ?  1088 LEU   B O   1 
ATOM   22609 C  CB  . LEU   B 1 1090 ? 59.42500   77.07400  23.32000  1.000 54.81773  ?  1088 LEU   B CB  1 
ATOM   22610 C  CG  . LEU   B 1 1090 ? 59.00400   76.35000  22.03900  1.000 59.53022  ?  1088 LEU   B CG  1 
ATOM   22611 C  CD1 . LEU   B 1 1090 ? 58.30900   77.31200  21.09100  1.000 59.95415  ?  1088 LEU   B CD1 1 
ATOM   22612 C  CD2 . LEU   B 1 1090 ? 60.19000   75.67400  21.35100  1.000 66.37726  ?  1088 LEU   B CD2 1 
ATOM   22613 N  N   . GLN   B 1 1091 ? 60.31700   77.17300  26.54000  1.000 73.49302  ?  1089 GLN   B N   1 
ATOM   22614 C  CA  . GLN   B 1 1091 ? 60.99300   77.78100  27.67700  1.000 91.99876  ?  1089 GLN   B CA  1 
ATOM   22615 C  C   . GLN   B 1 1091 ? 62.25500   76.99900  28.01200  1.000 77.25030  ?  1089 GLN   B C   1 
ATOM   22616 O  O   . GLN   B 1 1091 ? 63.31100   77.58700  28.28400  1.000 84.89172  ?  1089 GLN   B O   1 
ATOM   22617 C  CB  . GLN   B 1 1091 ? 60.06200   77.84300  28.89100  1.000 78.13988  ?  1089 GLN   B CB  1 
ATOM   22618 C  CG  . GLN   B 1 1091 ? 60.02300   79.19500  29.60400  1.000 75.33155  ?  1089 GLN   B CG  1 
ATOM   22619 C  CD  . GLN   B 1 1091 ? 61.30600   79.51800  30.33400  1.000 94.77936  ?  1089 GLN   B CD  1 
ATOM   22620 O  OE1 . GLN   B 1 1091 ? 61.82500   78.70300  31.09400  1.000 98.67541  ?  1089 GLN   B OE1 1 
ATOM   22621 N  NE2 . GLN   B 1 1091 ? 61.83300   80.70100  30.09700  1.000 88.32598  ?  1089 GLN   B NE2 1 
ATOM   22622 N  N   . ASN   B 1 1092 ? 62.17000   75.67100  27.96500  1.000 69.41124  ?  1090 ASN   B N   1 
ATOM   22623 C  CA  . ASN   B 1 1092 ? 63.23800   74.78400  28.41800  1.000 81.43358  ?  1090 ASN   B CA  1 
ATOM   22624 C  C   . ASN   B 1 1092 ? 64.06000   74.24400  27.25300  1.000 87.73251  ?  1090 ASN   B C   1 
ATOM   22625 O  O   . ASN   B 1 1092 ? 64.38900   73.05200  27.20600  1.000 91.82778  ?  1090 ASN   B O   1 
ATOM   22626 C  CB  . ASN   B 1 1092 ? 62.63600   73.65200  29.23600  1.000 86.99919  ?  1090 ASN   B CB  1 
ATOM   22627 C  CG  . ASN   B 1 1092 ? 61.81300   74.17100  30.39500  1.000 79.52716  ?  1090 ASN   B CG  1 
ATOM   22628 O  OD1 . ASN   B 1 1092 ? 62.16700   75.17800  31.01800  1.000 78.18333  ?  1090 ASN   B OD1 1 
ATOM   22629 N  ND2 . ASN   B 1 1092 ? 60.72600   73.49100  30.70100  1.000 76.56396  ?  1090 ASN   B ND2 1 
ATOM   22630 N  N   . GLN   B 1 1093 ? 64.36600   75.11000  26.28400  1.000 79.24644  ?  1091 GLN   B N   1 
ATOM   22631 C  CA  . GLN   B 1 1093 ? 64.99800   74.74800  25.02100  1.000 60.14196  ?  1091 GLN   B CA  1 
ATOM   22632 C  C   . GLN   B 1 1093 ? 66.52000   74.87400  25.03900  1.000 64.72318  ?  1091 GLN   B C   1 
ATOM   22633 O  O   . GLN   B 1 1093 ? 67.14700   74.74600  23.98200  1.000 73.08533  ?  1091 GLN   B O   1 
ATOM   22634 C  CB  . GLN   B 1 1093 ? 64.44300   75.62700  23.89600  1.000 67.12453  ?  1091 GLN   B CB  1 
ATOM   22635 C  CG  . GLN   B 1 1093 ? 64.72600   77.11400  24.09100  1.000 70.13965  ?  1091 GLN   B CG  1 
ATOM   22636 C  CD  . GLN   B 1 1093 ? 64.98200   77.84700  22.78500  1.000 74.87914  ?  1091 GLN   B CD  1 
ATOM   22637 O  OE1 . GLN   B 1 1093 ? 64.16300   78.65000  22.33400  1.000 68.96860  ?  1091 GLN   B OE1 1 
ATOM   22638 N  NE2 . GLN   B 1 1093 ? 66.13200   77.57900  22.17500  1.000 61.04195  ?  1091 GLN   B NE2 1 
ATOM   22639 N  N   . TYR   B 1 1094 ? 67.13300   75.13300  26.19500  1.000 72.29366  ?  1092 TYR   B N   1 
ATOM   22640 C  CA  . TYR   B 1 1094 ? 68.57400   75.35900  26.25500  1.000 77.09549  ?  1092 TYR   B CA  1 
ATOM   22641 C  C   . TYR   B 1 1094 ? 69.31500   74.23100  26.96200  1.000 68.01813  ?  1092 TYR   B C   1 
ATOM   22642 O  O   . TYR   B 1 1094 ? 70.44400   74.42700  27.42300  1.000 60.48412  ?  1092 TYR   B O   1 
ATOM   22643 C  CB  . TYR   B 1 1094 ? 68.87200   76.70500  26.91600  1.000 69.59157  ?  1092 TYR   B CB  1 
ATOM   22644 C  CG  . TYR   B 1 1094 ? 68.22600   77.85800  26.18500  1.000 78.76858  ?  1092 TYR   B CG  1 
ATOM   22645 C  CD1 . TYR   B 1 1094 ? 68.70000   78.27200  24.94600  1.000 62.81552  ?  1092 TYR   B CD1 1 
ATOM   22646 C  CD2 . TYR   B 1 1094 ? 67.12900   78.51700  26.72100  1.000 82.47444  ?  1092 TYR   B CD2 1 
ATOM   22647 C  CE1 . TYR   B 1 1094 ? 68.10200   79.31600  24.26500  1.000 60.11044  ?  1092 TYR   B CE1 1 
ATOM   22648 C  CE2 . TYR   B 1 1094 ? 66.52700   79.56400  26.05000  1.000 81.92170  ?  1092 TYR   B CE2 1 
ATOM   22649 C  CZ  . TYR   B 1 1094 ? 67.01800   79.96000  24.82400  1.000 76.38748  ?  1092 TYR   B CZ  1 
ATOM   22650 O  OH  . TYR   B 1 1094 ? 66.42000   81.00300  24.15300  1.000 81.10578  ?  1092 TYR   B OH  1 
ATOM   22651 N  N   . VAL   B 1 1095 ? 68.71000   73.05200  27.04300  1.000 79.64284  ?  1093 VAL   B N   1 
ATOM   22652 C  CA  . VAL   B 1 1095 ? 69.37400   71.86100  27.56100  1.000 86.69760  ?  1093 VAL   B CA  1 
ATOM   22653 C  C   . VAL   B 1 1095 ? 70.00400   71.13200  26.37700  1.000 77.66328  ?  1093 VAL   B C   1 
ATOM   22654 O  O   . VAL   B 1 1095 ? 69.29200   70.83400  25.40500  1.000 81.60597  ?  1093 VAL   B O   1 
ATOM   22655 C  CB  . VAL   B 1 1095 ? 68.39000   70.94800  28.30200  1.000 89.02558  ?  1093 VAL   B CB  1 
ATOM   22656 C  CG1 . VAL   B 1 1095 ? 69.13300   70.01700  29.25200  1.000 91.30522  ?  1093 VAL   B CG1 1 
ATOM   22657 C  CG2 . VAL   B 1 1095 ? 67.35300   71.77700  29.04400  1.000 76.31738  ?  1093 VAL   B CG2 1 
ATOM   22658 N  N   . PRO   B 1 1096 ? 71.30600   70.85100  26.40100  1.000 69.52145  ?  1094 PRO   B N   1 
ATOM   22659 C  CA  . PRO   B 1 1096 ? 71.91100   70.09500  25.29700  1.000 76.51296  ?  1094 PRO   B CA  1 
ATOM   22660 C  C   . PRO   B 1 1096 ? 71.24400   68.73700  25.13400  1.000 84.99507  ?  1094 PRO   B C   1 
ATOM   22661 O  O   . PRO   B 1 1096 ? 70.89900   68.07300  26.11300  1.000 105.44521 ?  1094 PRO   B O   1 
ATOM   22662 C  CB  . PRO   B 1 1096 ? 73.38000   69.96100  25.71500  1.000 71.61079  ?  1094 PRO   B CB  1 
ATOM   22663 C  CG  . PRO   B 1 1096 ? 73.40400   70.25400  27.18200  1.000 98.91269  ?  1094 PRO   B CG  1 
ATOM   22664 C  CD  . PRO   B 1 1096 ? 72.29800   71.23400  27.41700  1.000 65.40269  ?  1094 PRO   B CD  1 
ATOM   22665 N  N   . PHE   B 1 1097 ? 71.05600   68.33400  23.87600  1.000 86.80950  ?  1095 PHE   B N   1 
ATOM   22666 C  CA  . PHE   B 1 1097 ? 70.32800   67.10100  23.59100  1.000 82.07870  ?  1095 PHE   B CA  1 
ATOM   22667 C  C   . PHE   B 1 1097 ? 71.05100   65.87700  24.13600  1.000 86.26914  ?  1095 PHE   B C   1 
ATOM   22668 O  O   . PHE   B 1 1097 ? 70.40300   64.90700  24.54300  1.000 93.47039  ?  1095 PHE   B O   1 
ATOM   22669 C  CB  . PHE   B 1 1097 ? 70.10800   66.96400  22.08500  1.000 76.88856  ?  1095 PHE   B CB  1 
ATOM   22670 C  CG  . PHE   B 1 1097 ? 69.13000   65.88700  21.70900  1.000 67.53781  ?  1095 PHE   B CG  1 
ATOM   22671 C  CD1 . PHE   B 1 1097 ? 67.78400   66.02700  21.99700  1.000 69.10059  ?  1095 PHE   B CD1 1 
ATOM   22672 C  CD2 . PHE   B 1 1097 ? 69.55500   64.74000  21.05800  1.000 67.46245  ?  1095 PHE   B CD2 1 
ATOM   22673 C  CE1 . PHE   B 1 1097 ? 66.88000   65.04100  21.65000  1.000 64.31496  ?  1095 PHE   B CE1 1 
ATOM   22674 C  CE2 . PHE   B 1 1097 ? 68.65600   63.75100  20.70800  1.000 55.98702  ?  1095 PHE   B CE2 1 
ATOM   22675 C  CZ  . PHE   B 1 1097 ? 67.31600   63.90200  21.00500  1.000 61.66458  ?  1095 PHE   B CZ  1 
ATOM   22676 N  N   . ASP   B 1 1098 ? 72.38700   65.89900  24.14900  1.000 68.45672  ?  1096 ASP   B N   1 
ATOM   22677 C  CA  . ASP   B 1 1098 ? 73.13400   64.77600  24.70400  1.000 88.64782  ?  1096 ASP   B CA  1 
ATOM   22678 C  C   . ASP   B 1 1098 ? 72.84400   64.61000  26.19100  1.000 99.06503  ?  1096 ASP   B C   1 
ATOM   22679 O  O   . ASP   B 1 1098 ? 72.73900   63.48400  26.69100  1.000 95.96439  ?  1096 ASP   B O   1 
ATOM   22680 C  CB  . ASP   B 1 1098 ? 74.62900   64.97200  24.45900  1.000 80.42291  ?  1096 ASP   B CB  1 
ATOM   22681 C  CG  . ASP   B 1 1098 ? 75.38100   63.66000  24.36700  1.000 102.68344 ?  1096 ASP   B CG  1 
ATOM   22682 O  OD1 . ASP   B 1 1098 ? 74.72200   62.59800  24.32800  1.000 103.37843 ?  1096 ASP   B OD1 1 
ATOM   22683 O  OD2 . ASP   B 1 1098 ? 76.63000   63.69000  24.34000  1.000 104.82461 -1 1096 ASP   B OD2 1 
ATOM   22684 N  N   . LYS   B 1 1099 ? 72.70900   65.72400  26.91600  1.000 93.54831  ?  1097 LYS   B N   1 
ATOM   22685 C  CA  . LYS   B 1 1099 ? 72.30900   65.65100  28.31600  1.000 86.51597  ?  1097 LYS   B CA  1 
ATOM   22686 C  C   . LYS   B 1 1099 ? 70.82900   65.31900  28.45700  1.000 84.22431  ?  1097 LYS   B C   1 
ATOM   22687 O  O   . LYS   B 1 1099 ? 70.41900   64.73800  29.46800  1.000 104.24827 ?  1097 LYS   B O   1 
ATOM   22688 C  CB  . LYS   B 1 1099 ? 72.63100   66.96700  29.02400  1.000 70.93282  ?  1097 LYS   B CB  1 
ATOM   22689 N  N   . ILE   B 1 1100 ? 70.01700   65.68000  27.45900  1.000 78.22796  ?  1098 ILE   B N   1 
ATOM   22690 C  CA  . ILE   B 1 1100 ? 68.59900   65.32700  27.47300  1.000 68.61971  ?  1098 ILE   B CA  1 
ATOM   22691 C  C   . ILE   B 1 1100 ? 68.42500   63.81400  27.46300  1.000 83.67543  ?  1098 ILE   B C   1 
ATOM   22692 O  O   . ILE   B 1 1100 ? 67.56500   63.26700  28.16600  1.000 83.54493  ?  1098 ILE   B O   1 
ATOM   22693 C  CB  . ILE   B 1 1100 ? 67.87900   65.98700  26.28100  1.000 82.42278  ?  1098 ILE   B CB  1 
ATOM   22694 C  CG1 . ILE   B 1 1100 ? 67.49500   67.42800  26.61500  1.000 85.60797  ?  1098 ILE   B CG1 1 
ATOM   22695 C  CG2 . ILE   B 1 1100 ? 66.65200   65.18000  25.86700  1.000 90.36381  ?  1098 ILE   B CG2 1 
ATOM   22696 C  CD1 . ILE   B 1 1100 ? 66.27000   67.53100  27.47300  1.000 67.72770  ?  1098 ILE   B CD1 1 
ATOM   22697 N  N   . LEU   B 1 1101 ? 69.24400   63.11500  26.67300  1.000 86.19968  ?  1099 LEU   B N   1 
ATOM   22698 C  CA  . LEU   B 1 1101 ? 69.11100   61.66600  26.55900  1.000 93.21661  ?  1099 LEU   B CA  1 
ATOM   22699 C  C   . LEU   B 1 1101 ? 69.36500   60.97500  27.89300  1.000 98.90142  ?  1099 LEU   B C   1 
ATOM   22700 O  O   . LEU   B 1 1101 ? 68.69100   59.99400  28.22800  1.000 107.66811 ?  1099 LEU   B O   1 
ATOM   22701 C  CB  . LEU   B 1 1101 ? 70.06500   61.13200  25.49100  1.000 90.96048  ?  1099 LEU   B CB  1 
ATOM   22702 C  CG  . LEU   B 1 1101 ? 69.66200   61.38300  24.03700  1.000 80.62919  ?  1099 LEU   B CG  1 
ATOM   22703 C  CD1 . LEU   B 1 1101 ? 70.60600   60.65700  23.08900  1.000 53.25437  ?  1099 LEU   B CD1 1 
ATOM   22704 C  CD2 . LEU   B 1 1101 ? 68.22100   60.95500  23.80700  1.000 76.26477  ?  1099 LEU   B CD2 1 
ATOM   22705 N  N   . GLU   B 1 1102 ? 70.33400   61.47000  28.66700  1.000 81.06933  ?  1100 GLU   B N   1 
ATOM   22706 C  CA  . GLU   B 1 1102 ? 70.62000   60.86000  29.96200  1.000 87.33934  ?  1100 GLU   B CA  1 
ATOM   22707 C  C   . GLU   B 1 1102 ? 69.45100   61.02300  30.92600  1.000 85.71890  ?  1100 GLU   B C   1 
ATOM   22708 O  O   . GLU   B 1 1102 ? 69.17400   60.12500  31.72900  1.000 97.56021  ?  1100 GLU   B O   1 
ATOM   22709 C  CB  . GLU   B 1 1102 ? 71.89100   61.46000  30.56200  1.000 83.77600  ?  1100 GLU   B CB  1 
ATOM   22710 C  CG  . GLU   B 1 1102 ? 73.16400   60.72200  30.18800  1.000 104.28104 ?  1100 GLU   B CG  1 
ATOM   22711 C  CD  . GLU   B 1 1102 ? 74.20500   60.77800  31.28900  1.000 123.08107 ?  1100 GLU   B CD  1 
ATOM   22712 O  OE1 . GLU   B 1 1102 ? 73.97200   61.48700  32.29000  1.000 126.11037 ?  1100 GLU   B OE1 1 
ATOM   22713 O  OE2 . GLU   B 1 1102 ? 75.25100   60.10900  31.15700  1.000 117.32753 -1 1100 GLU   B OE2 1 
ATOM   22714 N  N   . ALA   B 1 1103 ? 68.75400   62.16100  30.86300  1.000 84.07809  ?  1101 ALA   B N   1 
ATOM   22715 C  CA  . ALA   B 1 1103 ? 67.64100   62.40000  31.77700  1.000 102.36525 ?  1101 ALA   B CA  1 
ATOM   22716 C  C   . ALA   B 1 1103 ? 66.51100   61.40400  31.54700  1.000 104.20227 ?  1101 ALA   B C   1 
ATOM   22717 O  O   . ALA   B 1 1103 ? 65.90400   60.91000  32.50400  1.000 96.13168  ?  1101 ALA   B O   1 
ATOM   22718 C  CB  . ALA   B 1 1103 ? 67.13500   63.83400  31.62400  1.000 89.33492  ?  1101 ALA   B CB  1 
ATOM   22719 N  N   . ALA   B 1 1104 ? 66.21300   61.09800  30.28300  1.000 103.39193 ?  1102 ALA   B N   1 
ATOM   22720 C  CA  . ALA   B 1 1104 ? 65.18300   60.11600  29.96800  1.000 96.48078  ?  1102 ALA   B CA  1 
ATOM   22721 C  C   . ALA   B 1 1104 ? 65.67000   58.68300  30.13400  1.000 103.17395 ?  1102 ALA   B C   1 
ATOM   22722 O  O   . ALA   B 1 1104 ? 64.84500   57.78500  30.33800  1.000 93.63789  ?  1102 ALA   B O   1 
ATOM   22723 C  CB  . ALA   B 1 1104 ? 64.67700   60.32500  28.54000  1.000 79.46173  ?  1102 ALA   B CB  1 
ATOM   22724 N  N   . ARG   B 1 1105 ? 66.98100   58.45900  30.05900  1.000 100.02062 ?  1103 ARG   B N   1 
ATOM   22725 C  CA  . ARG   B 1 1105 ? 67.58800   57.13200  30.16200  1.000 106.02146 ?  1103 ARG   B CA  1 
ATOM   22726 C  C   . ARG   B 1 1105 ? 66.92800   56.15700  29.18700  1.000 112.01888 ?  1103 ARG   B C   1 
ATOM   22727 O  O   . ARG   B 1 1105 ? 66.36400   55.12800  29.56300  1.000 110.74074 ?  1103 ARG   B O   1 
ATOM   22728 C  CB  . ARG   B 1 1105 ? 67.52900   56.61200  31.60100  1.000 107.21172 ?  1103 ARG   B CB  1 
ATOM   22729 C  CG  . ARG   B 1 1105 ? 68.62300   55.60900  31.93700  1.000 96.45877  ?  1103 ARG   B CG  1 
ATOM   22730 C  CD  . ARG   B 1 1105 ? 68.70000   55.37300  33.43400  1.000 101.54519 ?  1103 ARG   B CD  1 
ATOM   22731 N  NE  . ARG   B 1 1105 ? 68.76700   56.63000  34.17000  1.000 95.60344  ?  1103 ARG   B NE  1 
ATOM   22732 C  CZ  . ARG   B 1 1105 ? 68.75900   56.72700  35.49200  1.000 92.25109  ?  1103 ARG   B CZ  1 
ATOM   22733 N  NH1 . ARG   B 1 1105 ? 68.69500   55.65400  36.26300  1.000 85.07628  ?  1103 ARG   B NH1 1 
ATOM   22734 N  NH2 . ARG   B 1 1105 ? 68.81400   57.93100  36.05500  1.000 93.75647  ?  1103 ARG   B NH2 1 
ATOM   22735 N  N   . VAL   B 1 1106 ? 67.00600   56.51400  27.91500  1.000 97.44760  ?  1104 VAL   B N   1 
ATOM   22736 C  CA  . VAL   B 1 1106 ? 66.44500   55.72300  26.82700  1.000 76.45784  ?  1104 VAL   B CA  1 
ATOM   22737 C  C   . VAL   B 1 1106 ? 67.49700   54.73200  26.34800  1.000 75.18232  ?  1104 VAL   B C   1 
ATOM   22738 O  O   . VAL   B 1 1106 ? 68.70000   55.01100  26.36800  1.000 84.73083  ?  1104 VAL   B O   1 
ATOM   22739 C  CB  . VAL   B 1 1106 ? 65.95500   56.64600  25.69000  1.000 93.83188  ?  1104 VAL   B CB  1 
ATOM   22740 C  CG1 . VAL   B 1 1106 ? 67.08200   57.55700  25.21900  1.000 98.27412  ?  1104 VAL   B CG1 1 
ATOM   22741 C  CG2 . VAL   B 1 1106 ? 65.38100   55.83900  24.53200  1.000 105.61108 ?  1104 VAL   B CG2 1 
ATOM   22742 N  N   . LYS   B 1 1107 ? 67.04400   53.55400  25.93100  1.000 70.99956  ?  1105 LYS   B N   1 
ATOM   22743 C  CA  . LYS   B 1 1107 ? 67.93500   52.50500  25.46200  1.000 78.87692  ?  1105 LYS   B CA  1 
ATOM   22744 C  C   . LYS   B 1 1107 ? 68.26200   52.69000  23.98400  1.000 69.79731  ?  1105 LYS   B C   1 
ATOM   22745 O  O   . LYS   B 1 1107 ? 67.53200   53.34200  23.23400  1.000 77.04104  ?  1105 LYS   B O   1 
ATOM   22746 C  CB  . LYS   B 1 1107 ? 67.31100   51.12700  25.69100  1.000 86.66560  ?  1105 LYS   B CB  1 
ATOM   22747 N  N   . ARG   B 1 1108 ? 69.38100   52.10000  23.57100  1.000 68.63323  ?  1106 ARG   B N   1 
ATOM   22748 C  CA  . ARG   B 1 1108 ? 69.82200   52.15500  22.18300  1.000 77.47359  ?  1106 ARG   B CA  1 
ATOM   22749 C  C   . ARG   B 1 1108 ? 69.23900   50.97400  21.41900  1.000 88.69551  ?  1106 ARG   B C   1 
ATOM   22750 O  O   . ARG   B 1 1108 ? 69.41800   49.81800  21.81900  1.000 103.28846 ?  1106 ARG   B O   1 
ATOM   22751 C  CB  . ARG   B 1 1108 ? 71.34800   52.14800  22.09100  1.000 71.25949  ?  1106 ARG   B CB  1 
ATOM   22752 C  CG  . ARG   B 1 1108 ? 71.98600   53.48900  22.38600  1.000 81.28580  ?  1106 ARG   B CG  1 
ATOM   22753 C  CD  . ARG   B 1 1108 ? 73.42800   53.53600  21.90800  1.000 78.29078  ?  1106 ARG   B CD  1 
ATOM   22754 N  NE  . ARG   B 1 1108 ? 74.36300   53.64800  23.02000  1.000 93.02530  ?  1106 ARG   B NE  1 
ATOM   22755 C  CZ  . ARG   B 1 1108 ? 74.59400   54.76700  23.69200  1.000 104.25578 ?  1106 ARG   B CZ  1 
ATOM   22756 N  NH1 . ARG   B 1 1108 ? 73.96700   55.89400  23.39400  1.000 107.33937 ?  1106 ARG   B NH1 1 
ATOM   22757 N  NH2 . ARG   B 1 1108 ? 75.46900   54.75400  24.69200  1.000 93.59341  ?  1106 ARG   B NH2 1 
ATOM   22758 N  N   . GLU   B 1 1109 ? 68.54400   51.26700  20.32200  1.000 86.00524  ?  1107 GLU   B N   1 
ATOM   22759 C  CA  . GLU   B 1 1109 ? 68.01600   50.23500  19.44300  1.000 92.30728  ?  1107 GLU   B CA  1 
ATOM   22760 C  C   . GLU   B 1 1109 ? 68.90700   49.97600  18.23600  1.000 96.35161  ?  1107 GLU   B C   1 
ATOM   22761 O  O   . GLU   B 1 1109 ? 68.70900   48.97100  17.54500  1.000 103.54534 ?  1107 GLU   B O   1 
ATOM   22762 C  CB  . GLU   B 1 1109 ? 66.60800   50.61200  18.96500  1.000 89.73607  ?  1107 GLU   B CB  1 
ATOM   22763 C  CG  . GLU   B 1 1109 ? 65.67900   51.08900  20.07400  1.000 97.09001  ?  1107 GLU   B CG  1 
ATOM   22764 C  CD  . GLU   B 1 1109 ? 65.34000   49.99900  21.07600  1.000 93.87842  ?  1107 GLU   B CD  1 
ATOM   22765 O  OE1 . GLU   B 1 1109 ? 65.49500   48.80500  20.74000  1.000 95.81081  ?  1107 GLU   B OE1 1 
ATOM   22766 O  OE2 . GLU   B 1 1109 ? 64.91900   50.33800  22.20200  1.000 85.13817  -1 1107 GLU   B OE2 1 
ATOM   22767 N  N   . GLY   B 1 1110 ? 69.87300   50.84500  17.97100  1.000 84.80864  ?  1108 GLY   B N   1 
ATOM   22768 C  CA  . GLY   B 1 1110 ? 70.76500   50.67900  16.82400  1.000 99.96417  ?  1108 GLY   B CA  1 
ATOM   22769 C  C   . GLY   B 1 1110 ? 70.16900   51.03700  15.48400  1.000 93.46569  ?  1108 GLY   B C   1 
ATOM   22770 O  O   . GLY   B 1 1110 ? 70.75900   51.81700  14.73000  1.000 86.02706  ?  1108 GLY   B O   1 
ATOM   22771 N  N   . ASN   B 1 1111 ? 69.00200   50.48400  15.16300  1.000 90.23018  ?  1109 ASN   B N   1 
ATOM   22772 C  CA  . ASN   B 1 1111 ? 68.31700   50.77300  13.91200  1.000 91.72354  ?  1109 ASN   B CA  1 
ATOM   22773 C  C   . ASN   B 1 1111 ? 67.40600   51.99000  14.00200  1.000 90.48548  ?  1109 ASN   B C   1 
ATOM   22774 O  O   . ASN   B 1 1111 ? 66.77100   52.34400  13.00400  1.000 91.30239  ?  1109 ASN   B O   1 
ATOM   22775 C  CB  . ASN   B 1 1111 ? 67.50100   49.55500  13.46200  1.000 88.37142  ?  1109 ASN   B CB  1 
ATOM   22776 C  CG  . ASN   B 1 1111 ? 66.25200   49.34100  14.30300  1.000 87.45199  ?  1109 ASN   B CG  1 
ATOM   22777 O  OD1 . ASN   B 1 1111 ? 66.24300   49.60400  15.50600  1.000 97.33435  ?  1109 ASN   B OD1 1 
ATOM   22778 N  ND2 . ASN   B 1 1111 ? 65.18900   48.86300  13.66700  1.000 76.90044  ?  1109 ASN   B ND2 1 
ATOM   22779 N  N   . ARG   B 1 1112 ? 67.32400   52.63500  15.16400  1.000 74.94739  ?  1110 ARG   B N   1 
ATOM   22780 C  CA  . ARG   B 1 1112 ? 66.43200   53.76700  15.36200  1.000 79.89597  ?  1110 ARG   B CA  1 
ATOM   22781 C  C   . ARG   B 1 1112 ? 67.18700   54.92100  16.00400  1.000 68.45374  ?  1110 ARG   B C   1 
ATOM   22782 O  O   . ARG   B 1 1112 ? 68.22400   54.73700  16.64700  1.000 73.36622  ?  1110 ARG   B O   1 
ATOM   22783 C  CB  . ARG   B 1 1112 ? 65.22100   53.38600  16.22900  1.000 69.78879  ?  1110 ARG   B CB  1 
ATOM   22784 C  CG  . ARG   B 1 1112 ? 64.34700   52.30500  15.61700  1.000 79.52617  ?  1110 ARG   B CG  1 
ATOM   22785 C  CD  . ARG   B 1 1112 ? 63.25200   51.85300  16.56800  1.000 84.42212  ?  1110 ARG   B CD  1 
ATOM   22786 N  NE  . ARG   B 1 1112 ? 62.09300   52.73800  16.54900  1.000 75.58128  ?  1110 ARG   B NE  1 
ATOM   22787 C  CZ  . ARG   B 1 1112 ? 61.11500   52.66600  15.65700  1.000 79.26553  ?  1110 ARG   B CZ  1 
ATOM   22788 N  NH1 . ARG   B 1 1112 ? 61.14100   51.78400  14.67100  1.000 77.26838  ?  1110 ARG   B NH1 1 
ATOM   22789 N  NH2 . ARG   B 1 1112 ? 60.08400   53.50200  15.75500  1.000 92.42462  ?  1110 ARG   B NH2 1 
ATOM   22790 N  N   . HIS   B 1 1113 ? 66.64900   56.12000  15.81300  1.000 79.70485  ?  1111 HIS   B N   1 
ATOM   22791 C  CA  . HIS   B 1 1113 ? 67.21200   57.32200  16.40000  1.000 77.74807  ?  1111 HIS   B CA  1 
ATOM   22792 C  C   . HIS   B 1 1113 ? 66.71200   57.49800  17.83200  1.000 79.24916  ?  1111 HIS   B C   1 
ATOM   22793 O  O   . HIS   B 1 1113 ? 65.62700   57.02400  18.18000  1.000 79.96234  ?  1111 HIS   B O   1 
ATOM   22794 C  CB  . HIS   B 1 1113 ? 66.84300   58.54400  15.56600  1.000 79.92945  ?  1111 HIS   B CB  1 
ATOM   22795 C  CG  . HIS   B 1 1113 ? 67.57300   58.62400  14.26200  1.000 92.89280  ?  1111 HIS   B CG  1 
ATOM   22796 N  ND1 . HIS   B 1 1113 ? 68.80300   59.23300  14.13500  1.000 92.92184  ?  1111 HIS   B ND1 1 
ATOM   22797 C  CD2 . HIS   B 1 1113 ? 67.25000   58.16900  13.02800  1.000 92.71585  ?  1111 HIS   B CD2 1 
ATOM   22798 C  CE1 . HIS   B 1 1113 ? 69.20500   59.15000  12.87900  1.000 78.70592  ?  1111 HIS   B CE1 1 
ATOM   22799 N  NE2 . HIS   B 1 1113 ? 68.28100   58.51000  12.18700  1.000 89.21206  ?  1111 HIS   B NE2 1 
ATOM   22800 N  N   . PRO   B 1 1114 ? 67.49200   58.16400  18.68200  1.000 79.92384  ?  1112 PRO   B N   1 
ATOM   22801 C  CA  . PRO   B 1 1114 ? 67.07300   58.34400  20.07800  1.000 65.23968  ?  1112 PRO   B CA  1 
ATOM   22802 C  C   . PRO   B 1 1114 ? 65.77500   59.13400  20.17700  1.000 72.22590  ?  1112 PRO   B C   1 
ATOM   22803 O  O   . PRO   B 1 1114 ? 65.60100   60.16300  19.51900  1.000 79.27337  ?  1112 PRO   B O   1 
ATOM   22804 C  CB  . PRO   B 1 1114 ? 68.24900   59.10300  20.70400  1.000 73.13252  ?  1112 PRO   B CB  1 
ATOM   22805 C  CG  . PRO   B 1 1114 ? 69.41700   58.78200  19.82800  1.000 82.37792  ?  1112 PRO   B CG  1 
ATOM   22806 C  CD  . PRO   B 1 1114 ? 68.85500   58.67100  18.44500  1.000 81.14889  ?  1112 PRO   B CD  1 
ATOM   22807 N  N   . LEU   B 1 1115 ? 64.85700   58.62500  21.00100  1.000 67.22480  ?  1113 LEU   B N   1 
ATOM   22808 C  CA  . LEU   B 1 1115 ? 63.56800   59.25500  21.27700  1.000 65.85057  ?  1113 LEU   B CA  1 
ATOM   22809 C  C   . LEU   B 1 1115 ? 62.69200   59.35900  20.03300  1.000 79.30737  ?  1113 LEU   B C   1 
ATOM   22810 O  O   . LEU   B 1 1115 ? 61.79500   58.53300  19.83700  1.000 88.17194  ?  1113 LEU   B O   1 
ATOM   22811 C  CB  . LEU   B 1 1115 ? 63.77400   60.63100  21.91500  1.000 67.94522  ?  1113 LEU   B CB  1 
ATOM   22812 C  CG  . LEU   B 1 1115 ? 64.13100   60.53700  23.39900  1.000 81.46076  ?  1113 LEU   B CG  1 
ATOM   22813 C  CD1 . LEU   B 1 1115 ? 64.53300   61.88300  23.96900  1.000 65.61225  ?  1113 LEU   B CD1 1 
ATOM   22814 C  CD2 . LEU   B 1 1115 ? 62.96100   59.95100  24.17700  1.000 78.85911  ?  1113 LEU   B CD2 1 
ATOM   22815 N  N   . PHE   B 1 1116 ? 62.92400   60.36100  19.19200  1.000 75.67544  ?  1114 PHE   B N   1 
ATOM   22816 C  CA  . PHE   B 1 1116 ? 62.07500   60.58000  18.03100  1.000 65.32265  ?  1114 PHE   B CA  1 
ATOM   22817 C  C   . PHE   B 1 1116 ? 62.75700   60.10800  16.75100  1.000 58.38228  ?  1114 PHE   B C   1 
ATOM   22818 O  O   . PHE   B 1 1116 ? 63.98600   60.10400  16.64000  1.000 65.32220  ?  1114 PHE   B O   1 
ATOM   22819 C  CB  . PHE   B 1 1116 ? 61.68100   62.05700  17.90100  1.000 56.27312  ?  1114 PHE   B CB  1 
ATOM   22820 C  CG  . PHE   B 1 1116 ? 62.84300   62.98800  17.68200  1.000 51.29783  ?  1114 PHE   B CG  1 
ATOM   22821 C  CD1 . PHE   B 1 1116 ? 63.28900   63.27400  16.40200  1.000 57.15961  ?  1114 PHE   B CD1 1 
ATOM   22822 C  CD2 . PHE   B 1 1116 ? 63.47600   63.59300  18.75600  1.000 72.56930  ?  1114 PHE   B CD2 1 
ATOM   22823 C  CE1 . PHE   B 1 1116 ? 64.35200   64.13000  16.19600  1.000 71.00627  ?  1114 PHE   B CE1 1 
ATOM   22824 C  CE2 . PHE   B 1 1116 ? 64.54000   64.45300  18.55700  1.000 78.73224  ?  1114 PHE   B CE2 1 
ATOM   22825 C  CZ  . PHE   B 1 1116 ? 64.97800   64.72100  17.27500  1.000 71.31175  ?  1114 PHE   B CZ  1 
ATOM   22826 N  N   . ASP   B 1 1117 ? 61.93200   59.70400  15.78200  1.000 60.40782  ?  1115 ASP   B N   1 
ATOM   22827 C  CA  . ASP   B 1 1117 ? 62.38800   59.34900  14.44700  1.000 57.70897  ?  1115 ASP   B CA  1 
ATOM   22828 C  C   . ASP   B 1 1117 ? 61.89300   60.29900  13.36500  1.000 47.61962  ?  1115 ASP   B C   1 
ATOM   22829 O  O   . ASP   B 1 1117 ? 62.33900   60.18400  12.21800  1.000 55.89135  ?  1115 ASP   B O   1 
ATOM   22830 C  CB  . ASP   B 1 1117 ? 61.95600   57.91500  14.09700  1.000 73.07381  ?  1115 ASP   B CB  1 
ATOM   22831 C  CG  . ASP   B 1 1117 ? 62.76600   56.87000  14.83400  1.000 78.09310  ?  1115 ASP   B CG  1 
ATOM   22832 O  OD1 . ASP   B 1 1117 ? 63.99500   56.81300  14.62000  1.000 73.22920  ?  1115 ASP   B OD1 1 
ATOM   22833 O  OD2 . ASP   B 1 1117 ? 62.17900   56.12100  15.64300  1.000 67.55085  -1 1115 ASP   B OD2 1 
ATOM   22834 N  N   . VAL   B 1 1118 ? 60.99600   61.22900  13.69300  1.000 49.10787  ?  1116 VAL   B N   1 
ATOM   22835 C  CA  . VAL   B 1 1118 ? 60.48700   62.22700  12.76100  1.000 46.35561  ?  1116 VAL   B CA  1 
ATOM   22836 C  C   . VAL   B 1 1118 ? 60.88000   63.60600  13.26800  1.000 54.60020  ?  1116 VAL   B C   1 
ATOM   22837 O  O   . VAL   B 1 1118 ? 60.83600   63.86800  14.47400  1.000 69.54932  ?  1116 VAL   B O   1 
ATOM   22838 C  CB  . VAL   B 1 1118 ? 58.95600   62.12800  12.60500  1.000 48.64037  ?  1116 VAL   B CB  1 
ATOM   22839 C  CG1 . VAL   B 1 1118 ? 58.47500   62.93900  11.40000  1.000 54.11734  ?  1116 VAL   B CG1 1 
ATOM   22840 C  CG2 . VAL   B 1 1118 ? 58.55000   60.68700  12.48500  1.000 56.29759  ?  1116 VAL   B CG2 1 
ATOM   22841 N  N   . MET   B 1 1119 ? 61.24000   64.49300  12.34400  1.000 55.52339  ?  1117 MET   B N   1 
ATOM   22842 C  CA  . MET   B 1 1119 ? 61.69200   65.83600  12.67300  1.000 47.01549  ?  1117 MET   B CA  1 
ATOM   22843 C  C   . MET   B 1 1119 ? 60.81600   66.86300  11.97200  1.000 47.00352  ?  1117 MET   B C   1 
ATOM   22844 O  O   . MET   B 1 1119 ? 60.46900   66.69900  10.79800  1.000 63.18215  ?  1117 MET   B O   1 
ATOM   22845 C  CB  . MET   B 1 1119 ? 63.15400   66.03000  12.26300  1.000 51.40963  ?  1117 MET   B CB  1 
ATOM   22846 C  CG  . MET   B 1 1119 ? 63.73300   67.38500  12.61700  1.000 52.60399  ?  1117 MET   B CG  1 
ATOM   22847 S  SD  . MET   B 1 1119 ? 64.14800   67.54000  14.36200  1.000 67.73129  ?  1117 MET   B SD  1 
ATOM   22848 C  CE  . MET   B 1 1119 ? 65.87000   68.01900  14.24500  1.000 53.84009  ?  1117 MET   B CE  1 
ATOM   22849 N  N   . PHE   B 1 1120 ? 60.45900   67.92300  12.69400  1.000 46.53234  ?  1118 PHE   B N   1 
ATOM   22850 C  CA  . PHE   B 1 1120 ? 59.67300   69.02000  12.14400  1.000 45.33689  ?  1118 PHE   B CA  1 
ATOM   22851 C  C   . PHE   B 1 1120 ? 60.46800   70.31200  12.27200  1.000 56.67292  ?  1118 PHE   B C   1 
ATOM   22852 O  O   . PHE   B 1 1120 ? 60.79800   70.73300  13.38600  1.000 68.40261  ?  1118 PHE   B O   1 
ATOM   22853 C  CB  . PHE   B 1 1120 ? 58.32200   69.14500  12.85200  1.000 49.70965  ?  1118 PHE   B CB  1 
ATOM   22854 C  CG  . PHE   B 1 1120 ? 57.42200   70.18400  12.25000  1.000 52.64761  ?  1118 PHE   B CG  1 
ATOM   22855 C  CD1 . PHE   B 1 1120 ? 56.98000   70.05900  10.94400  1.000 45.94530  ?  1118 PHE   B CD1 1 
ATOM   22856 C  CD2 . PHE   B 1 1120 ? 57.01700   71.28400  12.98700  1.000 54.32614  ?  1118 PHE   B CD2 1 
ATOM   22857 C  CE1 . PHE   B 1 1120 ? 56.15500   71.01200  10.38200  1.000 49.38706  ?  1118 PHE   B CE1 1 
ATOM   22858 C  CE2 . PHE   B 1 1120 ? 56.18900   72.24200  12.43000  1.000 49.48402  ?  1118 PHE   B CE2 1 
ATOM   22859 C  CZ  . PHE   B 1 1120 ? 55.75900   72.10500  11.12600  1.000 51.62063  ?  1118 PHE   B CZ  1 
ATOM   22860 N  N   . MET   B 1 1121 ? 60.77900   70.93000  11.13500  1.000 52.80403  ?  1119 MET   B N   1 
ATOM   22861 C  CA  . MET   B 1 1121 ? 61.45800   72.21600  11.09400  1.000 49.22717  ?  1119 MET   B CA  1 
ATOM   22862 C  C   . MET   B 1 1121 ? 60.56000   73.24500  10.42200  1.000 51.43394  ?  1119 MET   B C   1 
ATOM   22863 O  O   . MET   B 1 1121 ? 59.72400   72.90700  9.57800   1.000 52.87800  ?  1119 MET   B O   1 
ATOM   22864 C  CB  . MET   B 1 1121 ? 62.78900   72.12700  10.34000  1.000 48.07031  ?  1119 MET   B CB  1 
ATOM   22865 C  CG  . MET   B 1 1121 ? 63.72800   71.05500  10.85800  1.000 55.90905  ?  1119 MET   B CG  1 
ATOM   22866 S  SD  . MET   B 1 1121 ? 65.32000   71.07600  10.01100  1.000 74.45766  ?  1119 MET   B SD  1 
ATOM   22867 C  CE  . MET   B 1 1121 ? 66.11700   69.64600  10.73500  1.000 61.37269  ?  1119 MET   B CE  1 
ATOM   22868 N  N   . MET   B 1 1122 ? 60.74000   74.51000  10.80200  1.000 53.71700  ?  1120 MET   B N   1 
ATOM   22869 C  CA  . MET   B 1 1122 ? 59.95400   75.59200  10.20600  1.000 43.06838  ?  1120 MET   B CA  1 
ATOM   22870 C  C   . MET   B 1 1122 ? 60.78800   76.87300  10.27500  1.000 64.16204  ?  1120 MET   B C   1 
ATOM   22871 O  O   . MET   B 1 1122 ? 60.71800   77.62600  11.24900  1.000 79.99715  ?  1120 MET   B O   1 
ATOM   22872 C  CB  . MET   B 1 1122 ? 58.61000   75.75900  10.89700  1.000 33.85671  ?  1120 MET   B CB  1 
ATOM   22873 C  CG  . MET   B 1 1122 ? 57.75200   76.85200  10.29100  1.000 34.18602  ?  1120 MET   B CG  1 
ATOM   22874 S  SD  . MET   B 1 1122 ? 56.04000   76.34700  10.06500  1.000 59.95512  ?  1120 MET   B SD  1 
ATOM   22875 C  CE  . MET   B 1 1122 ? 55.37900   77.80600  9.27000   1.000 59.82324  ?  1120 MET   B CE  1 
ATOM   22876 N  N   . GLN   B 1 1123 ? 61.57500   77.10400  9.22900   1.000 60.69240  ?  1121 GLN   B N   1 
ATOM   22877 C  CA  . GLN   B 1 1123 ? 62.30100   78.35600  9.08700   1.000 63.87155  ?  1121 GLN   B CA  1 
ATOM   22878 C  C   . GLN   B 1 1123 ? 61.35200   79.44600  8.60700   1.000 75.78159  ?  1121 GLN   B C   1 
ATOM   22879 O  O   . GLN   B 1 1123 ? 60.45400   79.19100  7.79600   1.000 57.75146  ?  1121 GLN   B O   1 
ATOM   22880 C  CB  . GLN   B 1 1123 ? 63.46800   78.19200  8.11100   1.000 64.83452  ?  1121 GLN   B CB  1 
ATOM   22881 C  CG  . GLN   B 1 1123 ? 64.35600   79.42500  7.98000   1.000 83.64178  ?  1121 GLN   B CG  1 
ATOM   22882 C  CD  . GLN   B 1 1123 ? 65.74600   79.21400  8.55100   1.000 80.44958  ?  1121 GLN   B CD  1 
ATOM   22883 O  OE1 . GLN   B 1 1123 ? 66.41300   78.22400  8.24400   1.000 74.58535  ?  1121 GLN   B OE1 1 
ATOM   22884 N  NE2 . GLN   B 1 1123 ? 66.19000   80.14400  9.38700   1.000 56.28967  ?  1121 GLN   B NE2 1 
ATOM   22885 N  N   . GLY   B 1 1124 ? 61.55000   80.65800  9.11400   1.000 70.93223  ?  1122 GLY   B N   1 
ATOM   22886 C  CA  . GLY   B 1 1124 ? 60.66800   81.75400  8.78700   1.000 59.75293  ?  1122 GLY   B CA  1 
ATOM   22887 C  C   . GLY   B 1 1124 ? 60.83300   82.23800  7.36200   1.000 72.80699  ?  1122 GLY   B C   1 
ATOM   22888 O  O   . GLY   B 1 1124 ? 61.42800   81.58500  6.50300   1.000 79.55989  ?  1122 GLY   B O   1 
ATOM   22889 N  N   . ALA   B 1 1125 ? 60.28500   83.41400  7.12000   1.000 62.93384  ?  1123 ALA   B N   1 
ATOM   22890 C  CA  . ALA   B 1 1125 ? 60.36200   84.03400  5.80900   1.000 52.74706  ?  1123 ALA   B CA  1 
ATOM   22891 C  C   . ALA   B 1 1125 ? 61.74900   84.63300  5.58100   1.000 55.54461  ?  1123 ALA   B C   1 
ATOM   22892 O  O   . ALA   B 1 1125 ? 62.41500   85.05100  6.53100   1.000 53.66338  ?  1123 ALA   B O   1 
ATOM   22893 C  CB  . ALA   B 1 1125 ? 59.30200   85.11900  5.67400   1.000 52.47527  ?  1123 ALA   B CB  1 
ATOM   22894 N  N   . PRO   B 1 1126 ? 62.21000   84.67600  4.33200   1.000 64.37136  ?  1124 PRO   B N   1 
ATOM   22895 C  CA  . PRO   B 1 1126 ? 63.53200   85.25500  4.05300   1.000 49.38462  ?  1124 PRO   B CA  1 
ATOM   22896 C  C   . PRO   B 1 1126 ? 63.54900   86.75000  4.34000   1.000 62.90054  ?  1124 PRO   B C   1 
ATOM   22897 O  O   . PRO   B 1 1126 ? 62.66900   87.49300  3.89800   1.000 59.02645  ?  1124 PRO   B O   1 
ATOM   22898 C  CB  . PRO   B 1 1126 ? 63.74300   84.96500  2.55900   1.000 42.59637  ?  1124 PRO   B CB  1 
ATOM   22899 C  CG  . PRO   B 1 1126 ? 62.78900   83.85400  2.24300   1.000 49.81127  ?  1124 PRO   B CG  1 
ATOM   22900 C  CD  . PRO   B 1 1126 ? 61.60700   84.08200  3.12900   1.000 64.77912  ?  1124 PRO   B CD  1 
ATOM   22901 N  N   . GLU   B 1 1127 ? 64.56600   87.18700  5.08700   1.000 74.29946  ?  1125 GLU   B N   1 
ATOM   22902 C  CA  . GLU   B 1 1127 ? 64.69300   88.59900  5.42800   1.000 69.87730  ?  1125 GLU   B CA  1 
ATOM   22903 C  C   . GLU   B 1 1127 ? 65.24100   89.42200  4.26900   1.000 63.35531  ?  1125 GLU   B C   1 
ATOM   22904 O  O   . GLU   B 1 1127 ? 64.90700   90.60600  4.14400   1.000 74.20230  ?  1125 GLU   B O   1 
ATOM   22905 C  CB  . GLU   B 1 1127 ? 65.59400   88.76400  6.65400   1.000 66.92717  ?  1125 GLU   B CB  1 
ATOM   22906 C  CG  . GLU   B 1 1127 ? 65.25100   87.84400  7.81700   1.000 84.41368  ?  1125 GLU   B CG  1 
ATOM   22907 C  CD  . GLU   B 1 1127 ? 64.57700   88.56800  8.96900   1.000 101.20932 ?  1125 GLU   B CD  1 
ATOM   22908 O  OE1 . GLU   B 1 1127 ? 63.84800   89.55100  8.71800   1.000 103.04473 ?  1125 GLU   B OE1 1 
ATOM   22909 O  OE2 . GLU   B 1 1127 ? 64.78300   88.15300  10.12900  1.000 90.22261  -1 1125 GLU   B OE2 1 
ATOM   22910 N  N   . THR   B 1 1128 ? 66.07400   88.82600  3.42100   1.000 52.80797  ?  1126 THR   B N   1 
ATOM   22911 C  CA  . THR   B 1 1128 ? 66.66600   89.50900  2.28200   1.000 40.35400  ?  1126 THR   B CA  1 
ATOM   22912 C  C   . THR   B 1 1128 ? 66.28300   88.80200  0.99000   1.000 43.51573  ?  1126 THR   B C   1 
ATOM   22913 O  O   . THR   B 1 1128 ? 65.97000   87.60900  0.97800   1.000 50.92260  ?  1126 THR   B O   1 
ATOM   22914 C  CB  . THR   B 1 1128 ? 68.19100   89.57200  2.40200   1.000 43.83889  ?  1126 THR   B CB  1 
ATOM   22915 O  OG1 . THR   B 1 1128 ? 68.70100   88.26900  2.71600   1.000 61.09215  ?  1126 THR   B OG1 1 
ATOM   22916 C  CG2 . THR   B 1 1128 ? 68.58900   90.54500  3.49000   1.000 53.67761  ?  1126 THR   B CG2 1 
ATOM   22917 N  N   . GLU   B 1 1129 ? 66.31800   89.55900  -0.10900  1.000 47.49247  ?  1127 GLU   B N   1 
ATOM   22918 C  CA  . GLU   B 1 1129 ? 65.94600   88.99200  -1.40100  1.000 49.06238  ?  1127 GLU   B CA  1 
ATOM   22919 C  C   . GLU   B 1 1129 ? 66.94800   87.93500  -1.85100  1.000 51.39615  ?  1127 GLU   B C   1 
ATOM   22920 O  O   . GLU   B 1 1129 ? 66.56700   86.94300  -2.48300  1.000 59.64145  ?  1127 GLU   B O   1 
ATOM   22921 C  CB  . GLU   B 1 1129 ? 65.82700   90.09300  -2.45300  1.000 53.44277  ?  1127 GLU   B CB  1 
ATOM   22922 C  CG  . GLU   B 1 1129 ? 65.24300   89.60100  -3.76700  1.000 77.60923  ?  1127 GLU   B CG  1 
ATOM   22923 C  CD  . GLU   B 1 1129 ? 65.49000   90.55300  -4.91800  1.000 79.56845  ?  1127 GLU   B CD  1 
ATOM   22924 O  OE1 . GLU   B 1 1129 ? 65.67100   91.76200  -4.66700  1.000 79.63446  ?  1127 GLU   B OE1 1 
ATOM   22925 O  OE2 . GLU   B 1 1129 ? 65.51000   90.08600  -6.07700  1.000 89.30595  -1 1127 GLU   B OE2 1 
ATOM   22926 N  N   . LEU   B 1 1130 ? 68.23200   88.13500  -1.54300  1.000 42.96318  ?  1128 LEU   B N   1 
ATOM   22927 C  CA  . LEU   B 1 1130 ? 69.22600   87.11400  -1.85400  1.000 34.07650  ?  1128 LEU   B CA  1 
ATOM   22928 C  C   . LEU   B 1 1130 ? 68.89700   85.80700  -1.14400  1.000 45.26128  ?  1128 LEU   B C   1 
ATOM   22929 O  O   . LEU   B 1 1130 ? 68.99300   84.72800  -1.73800  1.000 50.49670  ?  1128 LEU   B O   1 
ATOM   22930 C  CB  . LEU   B 1 1130 ? 70.62300   87.61000  -1.47200  1.000 42.14596  ?  1128 LEU   B CB  1 
ATOM   22931 C  CG  . LEU   B 1 1130 ? 71.84500   86.82100  -1.95500  1.000 37.70343  ?  1128 LEU   B CG  1 
ATOM   22932 C  CD1 . LEU   B 1 1130 ? 73.01100   87.76400  -2.18900  1.000 36.11270  ?  1128 LEU   B CD1 1 
ATOM   22933 C  CD2 . LEU   B 1 1130 ? 72.24000   85.74600  -0.95600  1.000 49.41050  ?  1128 LEU   B CD2 1 
ATOM   22934 N  N   . GLU   B 1 1131 ? 68.48600   85.89000  0.12500   1.000 49.16332  ?  1129 GLU   B N   1 
ATOM   22935 C  CA  . GLU   B 1 1131 ? 68.09900   84.69400  0.86500   1.000 49.21202  ?  1129 GLU   B CA  1 
ATOM   22936 C  C   . GLU   B 1 1131 ? 66.90700   84.00500  0.21300   1.000 44.51511  ?  1129 GLU   B C   1 
ATOM   22937 O  O   . GLU   B 1 1131 ? 66.82200   82.77100  0.20300   1.000 46.20911  ?  1129 GLU   B O   1 
ATOM   22938 C  CB  . GLU   B 1 1131 ? 67.78500   85.06100  2.31600   1.000 50.16687  ?  1129 GLU   B CB  1 
ATOM   22939 C  CG  . GLU   B 1 1131 ? 67.58500   83.87600  3.24500   1.000 44.62706  ?  1129 GLU   B CG  1 
ATOM   22940 C  CD  . GLU   B 1 1131 ? 67.25500   84.30300  4.66200   1.000 63.39024  ?  1129 GLU   B CD  1 
ATOM   22941 O  OE1 . GLU   B 1 1131 ? 67.25300   85.52400  4.93000   1.000 63.81589  ?  1129 GLU   B OE1 1 
ATOM   22942 O  OE2 . GLU   B 1 1131 ? 66.99500   83.42100  5.50800   1.000 74.37267  -1 1129 GLU   B OE2 1 
ATOM   22943 N  N   . SER   B 1 1132 ? 65.97800   84.78600  -0.34400  1.000 48.09118  ?  1130 SER   B N   1 
ATOM   22944 C  CA  . SER   B 1 1132 ? 64.82000   84.19900  -1.01000  1.000 45.03694  ?  1130 SER   B CA  1 
ATOM   22945 C  C   . SER   B 1 1132 ? 65.21900   83.45200  -2.27500  1.000 50.34907  ?  1130 SER   B C   1 
ATOM   22946 O  O   . SER   B 1 1132 ? 64.56800   82.46700  -2.64300  1.000 55.50629  ?  1130 SER   B O   1 
ATOM   22947 C  CB  . SER   B 1 1132 ? 63.79600   85.28400  -1.34200  1.000 42.69655  ?  1130 SER   B CB  1 
ATOM   22948 O  OG  . SER   B 1 1132 ? 64.23400   86.08100  -2.42900  1.000 61.74680  ?  1130 SER   B OG  1 
ATOM   22949 N  N   . ASN   B 1 1133 ? 66.28200   83.89600  -2.94800  1.000 45.98350  ?  1131 ASN   B N   1 
ATOM   22950 C  CA  . ASN   B 1 1133 ? 66.74200   83.28600  -4.18700  1.000 51.06263  ?  1131 ASN   B CA  1 
ATOM   22951 C  C   . ASN   B 1 1133 ? 67.82700   82.23600  -3.96600  1.000 57.63611  ?  1131 ASN   B C   1 
ATOM   22952 O  O   . ASN   B 1 1133 ? 68.54000   81.88700  -4.91500  1.000 49.71101  ?  1131 ASN   B O   1 
ATOM   22953 C  CB  . ASN   B 1 1133 ? 67.24300   84.36700  -5.14800  1.000 49.01011  ?  1131 ASN   B CB  1 
ATOM   22954 C  CG  . ASN   B 1 1133 ? 66.13600   85.28800  -5.61600  1.000 46.25824  ?  1131 ASN   B CG  1 
ATOM   22955 O  OD1 . ASN   B 1 1133 ? 65.05500   84.83600  -5.99500  1.000 55.27429  ?  1131 ASN   B OD1 1 
ATOM   22956 N  ND2 . ASN   B 1 1133 ? 66.39700   86.58900  -5.58600  1.000 52.24175  ?  1131 ASN   B ND2 1 
ATOM   22957 N  N   . MET   B 1 1134 ? 67.97100   81.73000  -2.74500  1.000 50.55462  ?  1132 MET   B N   1 
ATOM   22958 C  CA  . MET   B 1 1134 ? 68.90100   80.65000  -2.45600  1.000 32.46349  ?  1132 MET   B CA  1 
ATOM   22959 C  C   . MET   B 1 1134 ? 68.16400   79.31800  -2.42300  1.000 38.04919  ?  1132 MET   B C   1 
ATOM   22960 O  O   . MET   B 1 1134 ? 66.99600   79.24200  -2.03300  1.000 69.67805  ?  1132 MET   B O   1 
ATOM   22961 C  CB  . MET   B 1 1134 ? 69.61700   80.87000  -1.12500  1.000 33.65613  ?  1132 MET   B CB  1 
ATOM   22962 C  CG  . MET   B 1 1134 ? 70.51000   82.08800  -1.09600  1.000 48.06297  ?  1132 MET   B CG  1 
ATOM   22963 S  SD  . MET   B 1 1134 ? 71.56200   82.09500  0.36100   1.000 43.93905  ?  1132 MET   B SD  1 
ATOM   22964 C  CE  . MET   B 1 1134 ? 70.40000   81.50600  1.58500   1.000 40.48394  ?  1132 MET   B CE  1 
ATOM   22965 N  N   . HIS   B 1 1135 ? 68.86700   78.26400  -2.82400  1.000 29.71469  ?  1133 HIS   B N   1 
ATOM   22966 C  CA  . HIS   B 1 1135 ? 68.29400   76.92900  -2.92700  1.000 41.24077  ?  1133 HIS   B CA  1 
ATOM   22967 C  C   . HIS   B 1 1135 ? 69.12400   75.96500  -2.09500  1.000 43.01759  ?  1133 HIS   B C   1 
ATOM   22968 O  O   . HIS   B 1 1135 ? 70.30500   75.75100  -2.38400  1.000 49.76477  ?  1133 HIS   B O   1 
ATOM   22969 C  CB  . HIS   B 1 1135 ? 68.23800   76.47600  -4.38700  1.000 41.92969  ?  1133 HIS   B CB  1 
ATOM   22970 C  CG  . HIS   B 1 1135 ? 67.37000   77.33700  -5.25000  1.000 51.92946  ?  1133 HIS   B CG  1 
ATOM   22971 N  ND1 . HIS   B 1 1135 ? 67.82000   77.91700  -6.41700  1.000 42.25982  ?  1133 HIS   B ND1 1 
ATOM   22972 C  CD2 . HIS   B 1 1135 ? 66.07700   77.71600  -5.11600  1.000 58.44024  ?  1133 HIS   B CD2 1 
ATOM   22973 C  CE1 . HIS   B 1 1135 ? 66.84200   78.61700  -6.96300  1.000 57.45062  ?  1133 HIS   B CE1 1 
ATOM   22974 N  NE2 . HIS   B 1 1135 ? 65.77300   78.51200  -6.19300  1.000 68.81753  ?  1133 HIS   B NE2 1 
ATOM   22975 N  N   . HIS   B 1 1136 ? 68.51100   75.39200  -1.06300  1.000 37.82704  ?  1134 HIS   B N   1 
ATOM   22976 C  CA  . HIS   B 1 1136 ? 69.18400   74.36700  -0.27900  1.000 42.81644  ?  1134 HIS   B CA  1 
ATOM   22977 C  C   . HIS   B 1 1136 ? 69.23800   73.07300  -1.08100  1.000 40.66287  ?  1134 HIS   B C   1 
ATOM   22978 O  O   . HIS   B 1 1136 ? 68.24200   72.66200  -1.68300  1.000 48.21427  ?  1134 HIS   B O   1 
ATOM   22979 C  CB  . HIS   B 1 1136 ? 68.46000   74.14600  1.04900   1.000 44.06743  ?  1134 HIS   B CB  1 
ATOM   22980 C  CG  . HIS   B 1 1136 ? 69.23900   73.32600  2.03100   1.000 43.09197  ?  1134 HIS   B CG  1 
ATOM   22981 N  ND1 . HIS   B 1 1136 ? 68.64700   72.39900  2.86000   1.000 57.38306  ?  1134 HIS   B ND1 1 
ATOM   22982 C  CD2 . HIS   B 1 1136 ? 70.56200   73.29600  2.31800   1.000 53.81049  ?  1134 HIS   B CD2 1 
ATOM   22983 C  CE1 . HIS   B 1 1136 ? 69.57200   71.83000  3.61300   1.000 66.23684  ?  1134 HIS   B CE1 1 
ATOM   22984 N  NE2 . HIS   B 1 1136 ? 70.74300   72.35700  3.30500   1.000 56.84203  ?  1134 HIS   B NE2 1 
ATOM   22985 N  N   . ILE   B 1 1137 ? 70.40600   72.43800  -1.10500  1.000 49.60580  ?  1135 ILE   B N   1 
ATOM   22986 C  CA  . ILE   B 1 1137 ? 70.62800   71.23600  -1.89700  1.000 48.30246  ?  1135 ILE   B CA  1 
ATOM   22987 C  C   . ILE   B 1 1137 ? 70.79900   70.05100  -0.96000  1.000 43.78213  ?  1135 ILE   B C   1 
ATOM   22988 O  O   . ILE   B 1 1137 ? 71.44600   70.16000  0.08800   1.000 42.46495  ?  1135 ILE   B O   1 
ATOM   22989 C  CB  . ILE   B 1 1137 ? 71.85300   71.37900  -2.82000  1.000 43.81174  ?  1135 ILE   B CB  1 
ATOM   22990 C  CG1 . ILE   B 1 1137 ? 71.96800   72.81100  -3.33900  1.000 47.21141  ?  1135 ILE   B CG1 1 
ATOM   22991 C  CG2 . ILE   B 1 1137 ? 71.73500   70.42000  -3.98800  1.000 49.29478  ?  1135 ILE   B CG2 1 
ATOM   22992 C  CD1 . ILE   B 1 1137 ? 70.85600   73.21000  -4.27800  1.000 41.63382  ?  1135 ILE   B CD1 1 
ATOM   22993 N  N   . ASN   B 1 1138 ? 70.22000   68.91800  -1.34500  1.000 41.60092  ?  1136 ASN   B N   1 
ATOM   22994 C  CA  . ASN   B 1 1138 ? 70.35300   67.66800  -0.61300  1.000 38.50611  ?  1136 ASN   B CA  1 
ATOM   22995 C  C   . ASN   B 1 1138 ? 71.22100   66.71800  -1.42500  1.000 36.18616  ?  1136 ASN   B C   1 
ATOM   22996 O  O   . ASN   B 1 1138 ? 70.98200   66.52100  -2.62100  1.000 37.40586  ?  1136 ASN   B O   1 
ATOM   22997 C  CB  . ASN   B 1 1138 ? 68.98300   67.04400  -0.34200  1.000 39.73794  ?  1136 ASN   B CB  1 
ATOM   22998 C  CG  . ASN   B 1 1138 ? 69.04100   65.93200  0.68300   1.000 41.66638  ?  1136 ASN   B CG  1 
ATOM   22999 O  OD1 . ASN   B 1 1138 ? 69.08600   64.75200  0.33600   1.000 48.84342  ?  1136 ASN   B OD1 1 
ATOM   23000 N  ND2 . ASN   B 1 1138 ? 69.04400   66.30400  1.95700   1.000 56.26564  ?  1136 ASN   B ND2 1 
ATOM   23001 N  N   . ALA   B 1 1139 ? 72.23500   66.14100  -0.77700  1.000 39.70258  ?  1137 ALA   B N   1 
ATOM   23002 C  CA  . ALA   B 1 1139 ? 73.16100   65.22300  -1.42800  1.000 38.96210  ?  1137 ALA   B CA  1 
ATOM   23003 C  C   . ALA   B 1 1139 ? 72.68000   63.77800  -1.39400  1.000 46.78248  ?  1137 ALA   B C   1 
ATOM   23004 O  O   . ALA   B 1 1139 ? 73.50500   62.85400  -1.39000  1.000 55.05953  ?  1137 ALA   B O   1 
ATOM   23005 C  CB  . ALA   B 1 1139 ? 74.54700   65.33800  -0.79000  1.000 37.49982  ?  1137 ALA   B CB  1 
ATOM   23006 N  N   . GLY   B 1 1140 ? 71.37100   63.55600  -1.37700  1.000 36.26051  ?  1138 GLY   B N   1 
ATOM   23007 C  CA  . GLY   B 1 1140 ? 70.85300   62.21000  -1.22000  1.000 41.14941  ?  1138 GLY   B CA  1 
ATOM   23008 C  C   . GLY   B 1 1140 ? 70.99400   61.68600  0.19200   1.000 38.67528  ?  1138 GLY   B C   1 
ATOM   23009 O  O   . GLY   B 1 1140 ? 71.28500   60.49800  0.38400   1.000 48.73852  ?  1138 GLY   B O   1 
ATOM   23010 N  N   . ILE   B 1 1141 ? 70.79600   62.54600  1.18600   1.000 41.04819  ?  1139 ILE   B N   1 
ATOM   23011 C  CA  . ILE   B 1 1141 ? 70.98600   62.20300  2.58800   1.000 43.94634  ?  1139 ILE   B CA  1 
ATOM   23012 C  C   . ILE   B 1 1141 ? 69.67500   62.40700  3.33400   1.000 45.21060  ?  1139 ILE   B C   1 
ATOM   23013 O  O   . ILE   B 1 1141 ? 68.87400   63.28400  2.99700   1.000 41.01796  ?  1139 ILE   B O   1 
ATOM   23014 C  CB  . ILE   B 1 1141 ? 72.10700   63.04700  3.23000   1.000 47.33867  ?  1139 ILE   B CB  1 
ATOM   23015 C  CG1 . ILE   B 1 1141 ? 71.93900   64.51700  2.83100   1.000 65.44692  ?  1139 ILE   B CG1 1 
ATOM   23016 C  CG2 . ILE   B 1 1141 ? 73.47300   62.51900  2.81700   1.000 25.89284  ?  1139 ILE   B CG2 1 
ATOM   23017 C  CD1 . ILE   B 1 1141 ? 72.33400   65.50600  3.90300   1.000 51.89971  ?  1139 ILE   B CD1 1 
ATOM   23018 N  N   . SER   B 1 1142 ? 69.46400   61.58500  4.36000   1.000 44.27482  ?  1140 SER   B N   1 
ATOM   23019 C  CA  . SER   B 1 1142 ? 68.29400   61.69400  5.23100   1.000 34.74545  ?  1140 SER   B CA  1 
ATOM   23020 C  C   . SER   B 1 1142 ? 68.78700   61.51700  6.66300   1.000 50.07577  ?  1140 SER   B C   1 
ATOM   23021 O  O   . SER   B 1 1142 ? 69.10600   60.40000  7.08000   1.000 60.55043  ?  1140 SER   B O   1 
ATOM   23022 C  CB  . SER   B 1 1142 ? 67.23200   60.66200  4.87200   1.000 35.72909  ?  1140 SER   B CB  1 
ATOM   23023 O  OG  . SER   B 1 1142 ? 66.02000   60.91200  5.56200   1.000 47.07695  ?  1140 SER   B OG  1 
ATOM   23024 N  N   . LYS   B 1 1143 ? 68.85700   62.62400  7.40800   1.000 48.97293  ?  1141 LYS   B N   1 
ATOM   23025 C  CA  . LYS   B 1 1143 ? 69.36500   62.56200  8.77500   1.000 60.50715  ?  1141 LYS   B CA  1 
ATOM   23026 C  C   . LYS   B 1 1143 ? 68.48600   61.69500  9.66400   1.000 55.02074  ?  1141 LYS   B C   1 
ATOM   23027 O  O   . LYS   B 1 1143 ? 68.99100   61.03100  10.57600  1.000 73.47289  ?  1141 LYS   B O   1 
ATOM   23028 C  CB  . LYS   B 1 1143 ? 69.48400   63.97000  9.36000   1.000 67.41403  ?  1141 LYS   B CB  1 
ATOM   23029 C  CG  . LYS   B 1 1143 ? 70.51400   64.84100  8.66500   1.000 67.08352  ?  1141 LYS   B CG  1 
ATOM   23030 C  CD  . LYS   B 1 1143 ? 70.61200   66.21100  9.31300   1.000 49.99310  ?  1141 LYS   B CD  1 
ATOM   23031 C  CE  . LYS   B 1 1143 ? 70.84100   67.28500  8.26400   1.000 54.92483  ?  1141 LYS   B CE  1 
ATOM   23032 N  NZ  . LYS   B 1 1143 ? 71.90600   66.89200  7.30300   1.000 58.41029  ?  1141 LYS   B NZ  1 
ATOM   23033 N  N   . PHE   B 1 1144 ? 67.18000   61.68100  9.41800   1.000 48.22420  ?  1142 PHE   B N   1 
ATOM   23034 C  CA  . PHE   B 1 1144 ? 66.24200   60.88600  10.19400  1.000 61.53356  ?  1142 PHE   B CA  1 
ATOM   23035 C  C   . PHE   B 1 1144 ? 65.43600   60.00800  9.24600   1.000 59.32209  ?  1142 PHE   B C   1 
ATOM   23036 O  O   . PHE   B 1 1144 ? 65.64700   60.01300  8.02900   1.000 71.03453  ?  1142 PHE   B O   1 
ATOM   23037 C  CB  . PHE   B 1 1144 ? 65.32000   61.78300  11.03100  1.000 66.83027  ?  1142 PHE   B CB  1 
ATOM   23038 C  CG  . PHE   B 1 1144 ? 66.05400   62.71400  11.95300  1.000 75.50484  ?  1142 PHE   B CG  1 
ATOM   23039 C  CD1 . PHE   B 1 1144 ? 66.41300   62.30800  13.22700  1.000 69.31517  ?  1142 PHE   B CD1 1 
ATOM   23040 C  CD2 . PHE   B 1 1144 ? 66.38500   63.99600  11.54600  1.000 81.46402  ?  1142 PHE   B CD2 1 
ATOM   23041 C  CE1 . PHE   B 1 1144 ? 67.08900   63.16100  14.07800  1.000 65.31866  ?  1142 PHE   B CE1 1 
ATOM   23042 C  CE2 . PHE   B 1 1144 ? 67.06100   64.85500  12.39300  1.000 68.90162  ?  1142 PHE   B CE2 1 
ATOM   23043 C  CZ  . PHE   B 1 1144 ? 67.41300   64.43600  13.66000  1.000 60.18923  ?  1142 PHE   B CZ  1 
ATOM   23044 N  N   . ASP   B 1 1145 ? 64.50400   59.23800  9.81300   1.000 47.22343  ?  1143 ASP   B N   1 
ATOM   23045 C  CA  . ASP   B 1 1145 ? 63.60300   58.44900  8.97900   1.000 47.28863  ?  1143 ASP   B CA  1 
ATOM   23046 C  C   . ASP   B 1 1145 ? 62.77400   59.34800  8.07300   1.000 41.17503  ?  1143 ASP   B C   1 
ATOM   23047 O  O   . ASP   B 1 1145 ? 62.61900   59.06900  6.87900   1.000 48.35318  ?  1143 ASP   B O   1 
ATOM   23048 C  CB  . ASP   B 1 1145 ? 62.69000   57.58900  9.85100   1.000 49.76432  ?  1143 ASP   B CB  1 
ATOM   23049 C  CG  . ASP   B 1 1145 ? 63.45400   56.58500  10.68600  1.000 62.27856  ?  1143 ASP   B CG  1 
ATOM   23050 O  OD1 . ASP   B 1 1145 ? 64.69200   56.71700  10.79600  1.000 64.87564  ?  1143 ASP   B OD1 1 
ATOM   23051 O  OD2 . ASP   B 1 1145 ? 62.81200   55.66000  11.22900  1.000 52.66928  -1 1143 ASP   B OD2 1 
ATOM   23052 N  N   . LEU   B 1 1146 ? 62.23900   60.43500  8.62300   1.000 40.50879  ?  1144 LEU   B N   1 
ATOM   23053 C  CA  . LEU   B 1 1146 ? 61.44600   61.38500  7.85700   1.000 41.26280  ?  1144 LEU   B CA  1 
ATOM   23054 C  C   . LEU   B 1 1146 ? 61.58900   62.75700  8.49400   1.000 39.05305  ?  1144 LEU   B C   1 
ATOM   23055 O  O   . LEU   B 1 1146 ? 61.44800   62.89100  9.71300   1.000 48.34319  ?  1144 LEU   B O   1 
ATOM   23056 C  CB  . LEU   B 1 1146 ? 59.97200   60.96800  7.81100   1.000 35.49415  ?  1144 LEU   B CB  1 
ATOM   23057 C  CG  . LEU   B 1 1146 ? 59.02300   61.94200  7.11400   1.000 43.95338  ?  1144 LEU   B CG  1 
ATOM   23058 C  CD1 . LEU   B 1 1146 ? 59.34600   62.03800  5.63000   1.000 55.08564  ?  1144 LEU   B CD1 1 
ATOM   23059 C  CD2 . LEU   B 1 1146 ? 57.57800   61.52800  7.33200   1.000 40.41643  ?  1144 LEU   B CD2 1 
ATOM   23060 N  N   . THR   B 1 1147 ? 61.87100   63.76700  7.67500   1.000 42.94571  ?  1145 THR   B N   1 
ATOM   23061 C  CA  . THR   B 1 1147 ? 62.03300   65.13600  8.15000   1.000 44.42526  ?  1145 THR   B CA  1 
ATOM   23062 C  C   . THR   B 1 1147 ? 61.13900   66.04800  7.32700   1.000 45.44647  ?  1145 THR   B C   1 
ATOM   23063 O  O   . THR   B 1 1147 ? 61.26000   66.09300  6.09800   1.000 58.99510  ?  1145 THR   B O   1 
ATOM   23064 C  CB  . THR   B 1 1147 ? 63.49100   65.59400  8.05600   1.000 49.07609  ?  1145 THR   B CB  1 
ATOM   23065 O  OG1 . THR   B 1 1147 ? 64.31900   64.73500  8.85100   1.000 64.49138  ?  1145 THR   B OG1 1 
ATOM   23066 C  CG2 . THR   B 1 1147 ? 63.63000   67.02400  8.55300   1.000 38.06525  ?  1145 THR   B CG2 1 
ATOM   23067 N  N   . LEU   B 1 1148 ? 60.24500   66.76600  7.99800   1.000 36.55611  ?  1146 LEU   B N   1 
ATOM   23068 C  CA  . LEU   B 1 1148 ? 59.37900   67.74400  7.35400   1.000 45.11493  ?  1146 LEU   B CA  1 
ATOM   23069 C  C   . LEU   B 1 1148 ? 59.87800   69.14700  7.66600   1.000 52.66534  ?  1146 LEU   B C   1 
ATOM   23070 O  O   . LEU   B 1 1148 ? 60.06200   69.49900  8.83600   1.000 61.17877  ?  1146 LEU   B O   1 
ATOM   23071 C  CB  . LEU   B 1 1148 ? 57.92800   67.59700  7.81600   1.000 42.20343  ?  1146 LEU   B CB  1 
ATOM   23072 C  CG  . LEU   B 1 1148 ? 57.06400   66.49300  7.20700   1.000 40.91701  ?  1146 LEU   B CG  1 
ATOM   23073 C  CD1 . LEU   B 1 1148 ? 57.33600   65.15300  7.86900   1.000 42.37719  ?  1146 LEU   B CD1 1 
ATOM   23074 C  CD2 . LEU   B 1 1148 ? 55.59600   66.86500  7.32000   1.000 28.99510  ?  1146 LEU   B CD2 1 
ATOM   23075 N  N   . GLU   B 1 1149 ? 60.09500   69.94400  6.62400   1.000 29.18808  ?  1147 GLU   B N   1 
ATOM   23076 C  CA  . GLU   B 1 1149 ? 60.47100   71.34200  6.77300   1.000 30.13403  ?  1147 GLU   B CA  1 
ATOM   23077 C  C   . GLU   B 1 1149 ? 59.48600   72.20800  6.00500   1.000 38.07010  ?  1147 GLU   B C   1 
ATOM   23078 O  O   . GLU   B 1 1149 ? 59.25600   71.98500  4.81200   1.000 55.74377  ?  1147 GLU   B O   1 
ATOM   23079 C  CB  . GLU   B 1 1149 ? 61.89600   71.60100  6.28100   1.000 49.11023  ?  1147 GLU   B CB  1 
ATOM   23080 C  CG  . GLU   B 1 1149 ? 62.33100   73.05100  6.44100   1.000 53.98105  ?  1147 GLU   B CG  1 
ATOM   23081 C  CD  . GLU   B 1 1149 ? 63.82100   73.24700  6.25300   1.000 59.91487  ?  1147 GLU   B CD  1 
ATOM   23082 O  OE1 . GLU   B 1 1149 ? 64.43700   72.46200  5.50200   1.000 50.88509  ?  1147 GLU   B OE1 1 
ATOM   23083 O  OE2 . GLU   B 1 1149 ? 64.37800   74.18300  6.86600   1.000 67.65299  -1 1147 GLU   B OE2 1 
ATOM   23084 N  N   . VAL   B 1 1150 ? 58.90700   73.18900  6.69000   1.000 37.53350  ?  1148 VAL   B N   1 
ATOM   23085 C  CA  . VAL   B 1 1150 ? 57.97200   74.13100  6.08700   1.000 38.89147  ?  1148 VAL   B CA  1 
ATOM   23086 C  C   . VAL   B 1 1150 ? 58.72300   75.42600  5.81500   1.000 46.68677  ?  1148 VAL   B C   1 
ATOM   23087 O  O   . VAL   B 1 1150 ? 59.27400   76.04000  6.73700   1.000 54.75735  ?  1148 VAL   B O   1 
ATOM   23088 C  CB  . VAL   B 1 1150 ? 56.75400   74.37100  6.99100   1.000 38.97484  ?  1148 VAL   B CB  1 
ATOM   23089 C  CG1 . VAL   B 1 1150 ? 55.74900   75.28000  6.29900   1.000 41.81420  ?  1148 VAL   B CG1 1 
ATOM   23090 C  CG2 . VAL   B 1 1150 ? 56.11100   73.04700  7.37200   1.000 46.12236  ?  1148 VAL   B CG2 1 
ATOM   23091 N  N   . LEU   B 1 1151 ? 58.75200   75.83900  4.55000   1.000 45.54126  ?  1149 LEU   B N   1 
ATOM   23092 C  CA  . LEU   B 1 1151 ? 59.48800   77.02100  4.11900   1.000 50.11201  ?  1149 LEU   B CA  1 
ATOM   23093 C  C   . LEU   B 1 1151 ? 58.50500   78.03800  3.55800   1.000 53.13102  ?  1149 LEU   B C   1 
ATOM   23094 O  O   . LEU   B 1 1151 ? 57.76900   77.73600  2.61200   1.000 51.61290  ?  1149 LEU   B O   1 
ATOM   23095 C  CB  . LEU   B 1 1151 ? 60.54100   76.65500  3.07200   1.000 37.68340  ?  1149 LEU   B CB  1 
ATOM   23096 C  CG  . LEU   B 1 1151 ? 61.59500   75.63200  3.49800   1.000 41.22579  ?  1149 LEU   B CG  1 
ATOM   23097 C  CD1 . LEU   B 1 1151 ? 62.03700   74.80200  2.30700   1.000 49.95755  ?  1149 LEU   B CD1 1 
ATOM   23098 C  CD2 . LEU   B 1 1151 ? 62.78900   76.32300  4.13600   1.000 56.72379  ?  1149 LEU   B CD2 1 
ATOM   23099 N  N   . GLU   B 1 1152 ? 58.49500   79.23500  4.13800   1.000 62.02194  ?  1150 GLU   B N   1 
ATOM   23100 C  CA  . GLU   B 1 1152 ? 57.64100   80.32100  3.66100   1.000 52.83641  ?  1150 GLU   B CA  1 
ATOM   23101 C  C   . GLU   B 1 1152 ? 58.36200   81.01200  2.51100   1.000 53.40887  ?  1150 GLU   B C   1 
ATOM   23102 O  O   . GLU   B 1 1152 ? 59.25900   81.82900  2.72400   1.000 69.32002  ?  1150 GLU   B O   1 
ATOM   23103 C  CB  . GLU   B 1 1152 ? 57.32200   81.29500  4.78900   1.000 46.63973  ?  1150 GLU   B CB  1 
ATOM   23104 C  CG  . GLU   B 1 1152 ? 56.90200   80.61800  6.08500   1.000 71.24143  ?  1150 GLU   B CG  1 
ATOM   23105 C  CD  . GLU   B 1 1152 ? 56.52300   81.60600  7.17100   1.000 86.11798  ?  1150 GLU   B CD  1 
ATOM   23106 O  OE1 . GLU   B 1 1152 ? 56.06300   82.71800  6.83400   1.000 81.02527  ?  1150 GLU   B OE1 1 
ATOM   23107 O  OE2 . GLU   B 1 1152 ? 56.68600   81.26900  8.36300   1.000 73.68165  -1 1150 GLU   B OE2 1 
ATOM   23108 N  N   . ARG   B 1 1153 ? 57.97300   80.67600  1.28400   1.000 49.94021  ?  1151 ARG   B N   1 
ATOM   23109 C  CA  . ARG   B 1 1153 ? 58.60100   81.21300  0.08700   1.000 54.19169  ?  1151 ARG   B CA  1 
ATOM   23110 C  C   . ARG   B 1 1153 ? 57.53400   81.51200  -0.95600  1.000 56.54611  ?  1151 ARG   B C   1 
ATOM   23111 O  O   . ARG   B 1 1153 ? 56.59400   80.73000  -1.13100  1.000 53.84468  ?  1151 ARG   B O   1 
ATOM   23112 C  CB  . ARG   B 1 1153 ? 59.63300   80.23300  -0.49000  1.000 46.23156  ?  1151 ARG   B CB  1 
ATOM   23113 C  CG  . ARG   B 1 1153 ? 61.09100   80.62700  -0.28100  1.000 45.61621  ?  1151 ARG   B CG  1 
ATOM   23114 C  CD  . ARG   B 1 1153 ? 61.59700   80.29900  1.11700   1.000 35.35045  ?  1151 ARG   B CD  1 
ATOM   23115 N  NE  . ARG   B 1 1153 ? 63.04500   80.12200  1.12400   1.000 45.72176  ?  1151 ARG   B NE  1 
ATOM   23116 C  CZ  . ARG   B 1 1153 ? 63.80100   80.12200  2.21400   1.000 62.60073  ?  1151 ARG   B CZ  1 
ATOM   23117 N  NH1 . ARG   B 1 1153 ? 63.28200   80.31400  3.41600   1.000 73.86249  ?  1151 ARG   B NH1 1 
ATOM   23118 N  NH2 . ARG   B 1 1153 ? 65.11200   79.93000  2.09400   1.000 62.30168  ?  1151 ARG   B NH2 1 
ATOM   23119 N  N   . GLU   B 1 1154 ? 57.68400   82.65000  -1.63800  1.000 57.56381  ?  1152 GLU   B N   1 
ATOM   23120 C  CA  . GLU   B 1 1154 ? 56.80500   83.03900  -2.74400  1.000 54.56684  ?  1152 GLU   B CA  1 
ATOM   23121 C  C   . GLU   B 1 1154 ? 55.35300   83.18500  -2.28800  1.000 63.74272  ?  1152 GLU   B C   1 
ATOM   23122 O  O   . GLU   B 1 1154 ? 54.42800   82.71300  -2.95200  1.000 55.28373  ?  1152 GLU   B O   1 
ATOM   23123 C  CB  . GLU   B 1 1154 ? 56.90700   82.04900  -3.90800  1.000 66.96316  ?  1152 GLU   B CB  1 
ATOM   23124 C  CG  . GLU   B 1 1154 ? 58.30500   81.87000  -4.47600  1.000 76.76804  ?  1152 GLU   B CG  1 
ATOM   23125 C  CD  . GLU   B 1 1154 ? 58.68800   82.96600  -5.45200  1.000 85.54905  ?  1152 GLU   B CD  1 
ATOM   23126 O  OE1 . GLU   B 1 1154 ? 57.84900   83.85400  -5.71600  1.000 80.60000  ?  1152 GLU   B OE1 1 
ATOM   23127 O  OE2 . GLU   B 1 1154 ? 59.82900   82.93600  -5.95800  1.000 98.98494  -1 1152 GLU   B OE2 1 
ATOM   23128 N  N   . ASN   B 1 1155 ? 55.15400   83.84700  -1.14500  1.000 69.17897  ?  1153 ASN   B N   1 
ATOM   23129 C  CA  . ASN   B 1 1155 ? 53.82400   84.07000  -0.57000  1.000 61.92113  ?  1153 ASN   B CA  1 
ATOM   23130 C  C   . ASN   B 1 1155 ? 53.06000   82.76500  -0.36500  1.000 54.92146  ?  1153 ASN   B C   1 
ATOM   23131 O  O   . ASN   B 1 1155 ? 51.82800   82.73900  -0.41800  1.000 56.45142  ?  1153 ASN   B O   1 
ATOM   23132 C  CB  . ASN   B 1 1155 ? 52.99900   85.04100  -1.42100  1.000 37.59850  ?  1153 ASN   B CB  1 
ATOM   23133 C  CG  . ASN   B 1 1155 ? 53.44400   86.47900  -1.25900  1.000 55.95673  ?  1153 ASN   B CG  1 
ATOM   23134 O  OD1 . ASN   B 1 1155 ? 53.80100   87.14300  -2.23100  1.000 70.97656  ?  1153 ASN   B OD1 1 
ATOM   23135 N  ND2 . ASN   B 1 1155 ? 53.42300   86.97100  -0.02400  1.000 65.11819  ?  1153 ASN   B ND2 1 
ATOM   23136 N  N   . GLY   B 1 1156 ? 53.78200   81.67400  -0.12700  1.000 59.62433  ?  1154 GLY   B N   1 
ATOM   23137 C  CA  . GLY   B 1 1156 ? 53.16700   80.38100  0.09100   1.000 52.21919  ?  1154 GLY   B CA  1 
ATOM   23138 C  C   . GLY   B 1 1156 ? 53.95800   79.53200  1.06300   1.000 52.83991  ?  1154 GLY   B C   1 
ATOM   23139 O  O   . GLY   B 1 1156 ? 54.76600   80.05700  1.83500   1.000 57.85318  ?  1154 GLY   B O   1 
ATOM   23140 N  N   . LEU   B 1 1157 ? 53.74100   78.21900  1.03700   1.000 41.30685  ?  1155 LEU   B N   1 
ATOM   23141 C  CA  . LEU   B 1 1157 ? 54.43800   77.29400  1.92300   1.000 47.79501  ?  1155 LEU   B CA  1 
ATOM   23142 C  C   . LEU   B 1 1157 ? 54.98100   76.13600  1.10300   1.000 43.15829  ?  1155 LEU   B C   1 
ATOM   23143 O  O   . LEU   B 1 1157 ? 54.21900   75.44600  0.41900   1.000 48.45465  ?  1155 LEU   B O   1 
ATOM   23144 C  CB  . LEU   B 1 1157 ? 53.51300   76.78100  3.03000   1.000 57.31005  ?  1155 LEU   B CB  1 
ATOM   23145 C  CG  . LEU   B 1 1157 ? 53.24400   77.76500  4.16800   1.000 49.73458  ?  1155 LEU   B CG  1 
ATOM   23146 C  CD1 . LEU   B 1 1157 ? 52.50100   77.08700  5.30300   1.000 46.73773  ?  1155 LEU   B CD1 1 
ATOM   23147 C  CD2 . LEU   B 1 1157 ? 54.54800   78.36100  4.66000   1.000 52.96945  ?  1155 LEU   B CD2 1 
ATOM   23148 N  N   . ASN   B 1 1158 ? 56.29400   75.92900  1.17200   1.000 39.01933  ?  1156 ASN   B N   1 
ATOM   23149 C  CA  . ASN   B 1 1158 ? 56.97000   74.81600  0.51000   1.000 42.88468  ?  1156 ASN   B CA  1 
ATOM   23150 C  C   . ASN   B 1 1158 ? 57.33200   73.79800  1.58500   1.000 40.07162  ?  1156 ASN   B C   1 
ATOM   23151 O  O   . ASN   B 1 1158 ? 58.31900   73.96800  2.30700   1.000 41.57695  ?  1156 ASN   B O   1 
ATOM   23152 C  CB  . ASN   B 1 1158 ? 58.20400   75.29400  -0.24900  1.000 38.26116  ?  1156 ASN   B CB  1 
ATOM   23153 C  CG  . ASN   B 1 1158 ? 57.85400   76.02600  -1.52800  1.000 44.57150  ?  1156 ASN   B CG  1 
ATOM   23154 O  OD1 . ASN   B 1 1158 ? 56.68700   76.31000  -1.79300  1.000 50.43772  ?  1156 ASN   B OD1 1 
ATOM   23155 N  ND2 . ASN   B 1 1158 ? 58.86600   76.33900  -2.32800  1.000 46.02836  ?  1156 ASN   B ND2 1 
ATOM   23156 N  N   . ILE   B 1 1159 ? 56.52900   72.74400  1.69100   1.000 35.48882  ?  1157 ILE   B N   1 
ATOM   23157 C  CA  . ILE   B 1 1159 ? 56.71800   71.71800  2.71000   1.000 36.12372  ?  1157 ILE   B CA  1 
ATOM   23158 C  C   . ILE   B 1 1159 ? 57.58200   70.61600  2.11000   1.000 41.84649  ?  1157 ILE   B C   1 
ATOM   23159 O  O   . ILE   B 1 1159 ? 57.14600   69.88900  1.21400   1.000 48.25777  ?  1157 ILE   B O   1 
ATOM   23160 C  CB  . ILE   B 1 1159 ? 55.37600   71.17100  3.21000   1.000 39.19576  ?  1157 ILE   B CB  1 
ATOM   23161 C  CG1 . ILE   B 1 1159 ? 54.45100   72.32400  3.60100   1.000 41.06856  ?  1157 ILE   B CG1 1 
ATOM   23162 C  CG2 . ILE   B 1 1159 ? 55.59000   70.23800  4.39000   1.000 32.92859  ?  1157 ILE   B CG2 1 
ATOM   23163 C  CD1 . ILE   B 1 1159 ? 53.12200   71.88000  4.16300   1.000 39.65958  ?  1157 ILE   B CD1 1 
ATOM   23164 N  N   . VAL   B 1 1160 ? 58.80900   70.48900  2.60900   1.000 47.27447  ?  1158 VAL   B N   1 
ATOM   23165 C  CA  . VAL   B 1 1160 ? 59.78900   69.54300  2.08600   1.000 49.45273  ?  1158 VAL   B CA  1 
ATOM   23166 C  C   . VAL   B 1 1160 ? 59.73700   68.26400  2.90800   1.000 52.01359  ?  1158 VAL   B C   1 
ATOM   23167 O  O   . VAL   B 1 1160 ? 59.65200   68.30500  4.14200   1.000 54.38403  ?  1158 VAL   B O   1 
ATOM   23168 C  CB  . VAL   B 1 1160 ? 61.20400   70.15500  2.10000   1.000 43.91739  ?  1158 VAL   B CB  1 
ATOM   23169 C  CG1 . VAL   B 1 1160 ? 62.22300   69.16500  1.56300   1.000 46.10103  ?  1158 VAL   B CG1 1 
ATOM   23170 C  CG2 . VAL   B 1 1160 ? 61.22900   71.44000  1.29000   1.000 42.35702  ?  1158 VAL   B CG2 1 
ATOM   23171 N  N   . PHE   B 1 1161 ? 59.78500   67.12400  2.22200   1.000 52.76939  ?  1159 PHE   B N   1 
ATOM   23172 C  CA  . PHE   B 1 1161 ? 59.77400   65.80500  2.85100   1.000 42.06727  ?  1159 PHE   B CA  1 
ATOM   23173 C  C   . PHE   B 1 1161 ? 61.11000   65.12900  2.55600   1.000 42.74584  ?  1159 PHE   B C   1 
ATOM   23174 O  O   . PHE   B 1 1161 ? 61.33000   64.63300  1.44700   1.000 48.34393  ?  1159 PHE   B O   1 
ATOM   23175 C  CB  . PHE   B 1 1161 ? 58.60700   64.96200  2.34200   1.000 35.61723  ?  1159 PHE   B CB  1 
ATOM   23176 C  CG  . PHE   B 1 1161 ? 57.26100   65.43000  2.81900   1.000 34.16408  ?  1159 PHE   B CG  1 
ATOM   23177 C  CD1 . PHE   B 1 1161 ? 56.66500   66.55200  2.26800   1.000 43.40723  ?  1159 PHE   B CD1 1 
ATOM   23178 C  CD2 . PHE   B 1 1161 ? 56.58400   64.73500  3.80700   1.000 36.13318  ?  1159 PHE   B CD2 1 
ATOM   23179 C  CE1 . PHE   B 1 1161 ? 55.42400   66.97900  2.70300   1.000 41.97840  ?  1159 PHE   B CE1 1 
ATOM   23180 C  CE2 . PHE   B 1 1161 ? 55.34200   65.15600  4.24500   1.000 36.92004  ?  1159 PHE   B CE2 1 
ATOM   23181 C  CZ  . PHE   B 1 1161 ? 54.76200   66.28000  3.69200   1.000 37.08239  ?  1159 PHE   B CZ  1 
ATOM   23182 N  N   . GLU   B 1 1162 ? 62.00000   65.11200  3.54600   1.000 42.30457  ?  1160 GLU   B N   1 
ATOM   23183 C  CA  . GLU   B 1 1162 ? 63.28700   64.43000  3.44300   1.000 46.43381  ?  1160 GLU   B CA  1 
ATOM   23184 C  C   . GLU   B 1 1162 ? 63.14200   63.05300  4.07900   1.000 51.62712  ?  1160 GLU   B C   1 
ATOM   23185 O  O   . GLU   B 1 1162 ? 63.00500   62.93800  5.30200   1.000 48.23227  ?  1160 GLU   B O   1 
ATOM   23186 C  CB  . GLU   B 1 1162 ? 64.39000   65.24200  4.11900   1.000 42.78388  ?  1160 GLU   B CB  1 
ATOM   23187 C  CG  . GLU   B 1 1162 ? 65.69700   64.49100  4.30300   1.000 48.70844  ?  1160 GLU   B CG  1 
ATOM   23188 C  CD  . GLU   B 1 1162 ? 66.73100   65.30100  5.06100   1.000 57.31852  ?  1160 GLU   B CD  1 
ATOM   23189 O  OE1 . GLU   B 1 1162 ? 67.26500   66.27300  4.48600   1.000 64.64211  ?  1160 GLU   B OE1 1 
ATOM   23190 O  OE2 . GLU   B 1 1162 ? 67.00000   64.97300  6.23600   1.000 50.00865  -1 1160 GLU   B OE2 1 
ATOM   23191 N  N   . TYR   B 1 1163 ? 63.17200   62.01000  3.25100   1.000 52.86646  ?  1161 TYR   B N   1 
ATOM   23192 C  CA  . TYR   B 1 1163 ? 62.85900   60.65900  3.69300   1.000 48.67145  ?  1161 TYR   B CA  1 
ATOM   23193 C  C   . TYR   B 1 1163 ? 63.99500   59.70700  3.35700   1.000 43.45161  ?  1161 TYR   B C   1 
ATOM   23194 O  O   . TYR   B 1 1163 ? 64.62600   59.82300  2.30400   1.000 49.16064  ?  1161 TYR   B O   1 
ATOM   23195 C  CB  . TYR   B 1 1163 ? 61.56500   60.15500  3.04900   1.000 38.00751  ?  1161 TYR   B CB  1 
ATOM   23196 C  CG  . TYR   B 1 1163 ? 61.60100   60.08900  1.53500   1.000 38.29784  ?  1161 TYR   B CG  1 
ATOM   23197 C  CD1 . TYR   B 1 1163 ? 61.29700   61.20500  0.76500   1.000 42.43854  ?  1161 TYR   B CD1 1 
ATOM   23198 C  CD2 . TYR   B 1 1163 ? 61.91900   58.90600  0.87600   1.000 41.75953  ?  1161 TYR   B CD2 1 
ATOM   23199 C  CE1 . TYR   B 1 1163 ? 61.31800   61.14800  -0.61800  1.000 43.57236  ?  1161 TYR   B CE1 1 
ATOM   23200 C  CE2 . TYR   B 1 1163 ? 61.94200   58.84100  -0.50600  1.000 36.50291  ?  1161 TYR   B CE2 1 
ATOM   23201 C  CZ  . TYR   B 1 1163 ? 61.64100   59.96500  -1.24800  1.000 40.36025  ?  1161 TYR   B CZ  1 
ATOM   23202 O  OH  . TYR   B 1 1163 ? 61.66300   59.90500  -2.62400  1.000 35.35406  ?  1161 TYR   B OH  1 
ATOM   23203 N  N   . ASN   B 1 1164 ? 64.23400   58.75400  4.25600   1.000 48.35245  ?  1162 ASN   B N   1 
ATOM   23204 C  CA  . ASN   B 1 1164 ? 65.22900   57.71800  4.02100   1.000 43.45333  ?  1162 ASN   B CA  1 
ATOM   23205 C  C   . ASN   B 1 1164 ? 64.72800   56.73800  2.96400   1.000 51.01466  ?  1162 ASN   B C   1 
ATOM   23206 O  O   . ASN   B 1 1164 ? 63.61900   56.20600  3.07000   1.000 50.52599  ?  1162 ASN   B O   1 
ATOM   23207 C  CB  . ASN   B 1 1164 ? 65.53800   56.98900  5.32700   1.000 37.53131  ?  1162 ASN   B CB  1 
ATOM   23208 C  CG  . ASN   B 1 1164 ? 66.52100   55.85800  5.14500   1.000 45.07719  ?  1162 ASN   B CG  1 
ATOM   23209 O  OD1 . ASN   B 1 1164 ? 66.13400   54.69400  5.06900   1.000 60.73303  ?  1162 ASN   B OD1 1 
ATOM   23210 N  ND2 . ASN   B 1 1164 ? 67.80300   56.19200  5.07500   1.000 60.94989  ?  1162 ASN   B ND2 1 
ATOM   23211 N  N   . THR   B 1 1165 ? 65.55400   56.49700  1.94200   1.000 52.73563  ?  1163 THR   B N   1 
ATOM   23212 C  CA  . THR   B 1 1165 ? 65.13000   55.67200  0.81500   1.000 42.70732  ?  1163 THR   B CA  1 
ATOM   23213 C  C   . THR   B 1 1165 ? 65.02500   54.19400  1.16800   1.000 41.79562  ?  1163 THR   B C   1 
ATOM   23214 O  O   . THR   B 1 1165 ? 64.37900   53.44200  0.42900   1.000 51.58188  ?  1163 THR   B O   1 
ATOM   23215 C  CB  . THR   B 1 1165 ? 66.09000   55.85100  -0.36200  1.000 44.34115  ?  1163 THR   B CB  1 
ATOM   23216 O  OG1 . THR   B 1 1165 ? 67.44100   55.86600  0.11600   1.000 57.33730  ?  1163 THR   B OG1 1 
ATOM   23217 C  CG2 . THR   B 1 1165 ? 65.79500   57.15100  -1.09800  1.000 39.05016  ?  1163 THR   B CG2 1 
ATOM   23218 N  N   . HIS   B 1 1166 ? 65.64300   53.75600  2.26600   1.000 45.14333  ?  1164 HIS   B N   1 
ATOM   23219 C  CA  . HIS   B 1 1166 ? 65.52800   52.36400  2.67900   1.000 41.80967  ?  1164 HIS   B CA  1 
ATOM   23220 C  C   . HIS   B 1 1166 ? 64.20500   52.07600  3.37600   1.000 53.94567  ?  1164 HIS   B C   1 
ATOM   23221 O  O   . HIS   B 1 1166 ? 63.76500   50.92100  3.39400   1.000 64.76367  ?  1164 HIS   B O   1 
ATOM   23222 C  CB  . HIS   B 1 1166 ? 66.68400   51.97900  3.60900   1.000 42.47178  ?  1164 HIS   B CB  1 
ATOM   23223 C  CG  . HIS   B 1 1166 ? 68.04500   52.17400  3.01100   1.000 54.70942  ?  1164 HIS   B CG  1 
ATOM   23224 N  ND1 . HIS   B 1 1166 ? 69.03400   51.21700  3.09000   1.000 44.82654  ?  1164 HIS   B ND1 1 
ATOM   23225 C  CD2 . HIS   B 1 1166 ? 68.58600   53.21600  2.33600   1.000 66.78612  ?  1164 HIS   B CD2 1 
ATOM   23226 C  CE1 . HIS   B 1 1166 ? 70.12300   51.66000  2.48700   1.000 53.04696  ?  1164 HIS   B CE1 1 
ATOM   23227 N  NE2 . HIS   B 1 1166 ? 69.87700   52.87000  2.02000   1.000 62.61630  ?  1164 HIS   B NE2 1 
ATOM   23228 N  N   . LEU   B 1 1167 ? 63.56300   53.09900  3.94300   1.000 48.31787  ?  1165 LEU   B N   1 
ATOM   23229 C  CA  . LEU   B 1 1167 ? 62.31700   52.93000  4.67800   1.000 53.30762  ?  1165 LEU   B CA  1 
ATOM   23230 C  C   . LEU   B 1 1167 ? 61.08500   53.32600  3.87800   1.000 41.33728  ?  1165 LEU   B C   1 
ATOM   23231 O  O   . LEU   B 1 1167 ? 59.99000   52.83600  4.17400   1.000 54.28592  ?  1165 LEU   B O   1 
ATOM   23232 C  CB  . LEU   B 1 1167 ? 62.35900   53.74900  5.97400   1.000 56.94301  ?  1165 LEU   B CB  1 
ATOM   23233 C  CG  . LEU   B 1 1167 ? 63.54400   53.47300  6.90200   1.000 44.13011  ?  1165 LEU   B CG  1 
ATOM   23234 C  CD1 . LEU   B 1 1167 ? 63.82800   54.67700  7.78500   1.000 48.03040  ?  1165 LEU   B CD1 1 
ATOM   23235 C  CD2 . LEU   B 1 1167 ? 63.28000   52.24100  7.75000   1.000 51.91642  ?  1165 LEU   B CD2 1 
ATOM   23236 N  N   . PHE   B 1 1168 ? 61.23200   54.19500  2.88200   1.000 50.34977  ?  1166 PHE   B N   1 
ATOM   23237 C  CA  . PHE   B 1 1168 ? 60.12800   54.63800  2.04400   1.000 50.69920  ?  1166 PHE   B CA  1 
ATOM   23238 C  C   . PHE   B 1 1168 ? 60.56400   54.60600  0.58700   1.000 46.41982  ?  1166 PHE   B C   1 
ATOM   23239 O  O   . PHE   B 1 1168 ? 61.68400   55.01200  0.26300   1.000 55.18797  ?  1166 PHE   B O   1 
ATOM   23240 C  CB  . PHE   B 1 1168 ? 59.67900   56.06500  2.40900   1.000 36.09734  ?  1166 PHE   B CB  1 
ATOM   23241 C  CG  . PHE   B 1 1168 ? 59.43800   56.27800  3.87800   1.000 46.45128  ?  1166 PHE   B CG  1 
ATOM   23242 C  CD1 . PHE   B 1 1168 ? 58.18200   56.06800  4.42500   1.000 44.03097  ?  1166 PHE   B CD1 1 
ATOM   23243 C  CD2 . PHE   B 1 1168 ? 60.46200   56.70600  4.71000   1.000 47.87170  ?  1166 PHE   B CD2 1 
ATOM   23244 C  CE1 . PHE   B 1 1168 ? 57.95400   56.26900  5.77400   1.000 42.95557  ?  1166 PHE   B CE1 1 
ATOM   23245 C  CE2 . PHE   B 1 1168 ? 60.24000   56.90800  6.06100   1.000 46.74037  ?  1166 PHE   B CE2 1 
ATOM   23246 C  CZ  . PHE   B 1 1168 ? 58.98400   56.69000  6.59300   1.000 48.28902  ?  1166 PHE   B CZ  1 
ATOM   23247 N  N   . ASP   B 1 1169 ? 59.68900   54.12600  -0.29400  1.000 45.80816  ?  1167 ASP   B N   1 
ATOM   23248 C  CA  . ASP   B 1 1169 ? 59.93800   54.25600  -1.72000  1.000 56.38236  ?  1167 ASP   B CA  1 
ATOM   23249 C  C   . ASP   B 1 1169 ? 59.21700   55.49400  -2.25100  1.000 48.59509  ?  1167 ASP   B C   1 
ATOM   23250 O  O   . ASP   B 1 1169 ? 58.59000   56.24900  -1.50400  1.000 57.05067  ?  1167 ASP   B O   1 
ATOM   23251 C  CB  . ASP   B 1 1169 ? 59.54600   52.98200  -2.48500  1.000 66.92934  ?  1167 ASP   B CB  1 
ATOM   23252 C  CG  . ASP   B 1 1169 ? 58.03800   52.73400  -2.54600  1.000 77.94529  ?  1167 ASP   B CG  1 
ATOM   23253 O  OD1 . ASP   B 1 1169 ? 57.25500   53.67200  -2.80200  1.000 78.96157  ?  1167 ASP   B OD1 1 
ATOM   23254 O  OD2 . ASP   B 1 1169 ? 57.63500   51.56200  -2.39100  1.000 82.03515  -1 1167 ASP   B OD2 1 
ATOM   23255 N  N   . GLU   B 1 1170 ? 59.30200   55.69300  -3.56800  1.000 52.98529  ?  1168 GLU   B N   1 
ATOM   23256 C  CA  . GLU   B 1 1170 ? 58.71600   56.88300  -4.17400  1.000 62.89122  ?  1168 GLU   B CA  1 
ATOM   23257 C  C   . GLU   B 1 1170 ? 57.19500   56.87600  -4.06900  1.000 60.32921  ?  1168 GLU   B C   1 
ATOM   23258 O  O   . GLU   B 1 1170 ? 56.57800   57.92300  -3.84300  1.000 51.65098  ?  1168 GLU   B O   1 
ATOM   23259 C  CB  . GLU   B 1 1170 ? 59.15600   56.99400  -5.63400  1.000 57.70807  ?  1168 GLU   B CB  1 
ATOM   23260 N  N   . GLY   B 1 1171 ? 56.57000   55.70800  -4.23000  1.000 54.61584  ?  1169 GLY   B N   1 
ATOM   23261 C  CA  . GLY   B 1 1171 ? 55.12000   55.64300  -4.16400  1.000 54.97723  ?  1169 GLY   B CA  1 
ATOM   23262 C  C   . GLY   B 1 1171 ? 54.57500   55.81100  -2.76100  1.000 48.86719  ?  1169 GLY   B C   1 
ATOM   23263 O  O   . GLY   B 1 1171 ? 53.48800   56.36700  -2.57700  1.000 53.04607  ?  1169 GLY   B O   1 
ATOM   23264 N  N   . MET   B 1 1172 ? 55.31300   55.33700  -1.75700  1.000 53.94238  ?  1170 MET   B N   1 
ATOM   23265 C  CA  . MET   B 1 1172 ? 54.86700   55.47500  -0.37500  1.000 46.78614  ?  1170 MET   B CA  1 
ATOM   23266 C  C   . MET   B 1 1172 ? 54.86200   56.93500  0.05600   1.000 52.20076  ?  1170 MET   B C   1 
ATOM   23267 O  O   . MET   B 1 1172 ? 53.87200   57.42900  0.60900   1.000 58.21175  ?  1170 MET   B O   1 
ATOM   23268 C  CB  . MET   B 1 1172 ? 55.76500   54.65200  0.54300   1.000 44.54474  ?  1170 MET   B CB  1 
ATOM   23269 C  CG  . MET   B 1 1172 ? 55.94800   53.21700  0.09100   1.000 46.37567  ?  1170 MET   B CG  1 
ATOM   23270 S  SD  . MET   B 1 1172 ? 56.84600   52.26900  1.32400   1.000 50.87046  ?  1170 MET   B SD  1 
ATOM   23271 C  CE  . MET   B 1 1172 ? 56.06300   52.89900  2.80100   1.000 50.35101  ?  1170 MET   B CE  1 
ATOM   23272 N  N   . ILE   B 1 1173 ? 55.97000   57.63800  -0.18700  1.000 53.17847  ?  1171 ILE   B N   1 
ATOM   23273 C  CA  . ILE   B 1 1173 ? 56.06900   59.04100  0.20100   1.000 43.34582  ?  1171 ILE   B CA  1 
ATOM   23274 C  C   . ILE   B 1 1173 ? 55.01400   59.86900  -0.51700  1.000 36.42176  ?  1171 ILE   B C   1 
ATOM   23275 O  O   . ILE   B 1 1173 ? 54.43000   60.79400  0.06200   1.000 45.76336  ?  1171 ILE   B O   1 
ATOM   23276 C  CB  . ILE   B 1 1173 ? 57.49300   59.56000  -0.07000  1.000 32.04202  ?  1171 ILE   B CB  1 
ATOM   23277 C  CG1 . ILE   B 1 1173 ? 58.41000   59.18600  1.09200   1.000 45.93103  ?  1171 ILE   B CG1 1 
ATOM   23278 C  CG2 . ILE   B 1 1173 ? 57.49600   61.06500  -0.29300  1.000 44.99704  ?  1171 ILE   B CG2 1 
ATOM   23279 C  CD1 . ILE   B 1 1173 ? 58.06600   59.89500  2.38500   1.000 41.85408  ?  1171 ILE   B CD1 1 
ATOM   23280 N  N   . LEU   B 1 1174 ? 54.73600   59.54100  -1.78000  1.000 37.34590  ?  1172 LEU   B N   1 
ATOM   23281 C  CA  . LEU   B 1 1174 ? 53.71800   60.27800  -2.52100  1.000 46.58539  ?  1172 LEU   B CA  1 
ATOM   23282 C  C   . LEU   B 1 1174 ? 52.33400   60.08200  -1.91800  1.000 55.16613  ?  1172 LEU   B C   1 
ATOM   23283 O  O   . LEU   B 1 1174 ? 51.51500   61.00900  -1.93400  1.000 43.73723  ?  1172 LEU   B O   1 
ATOM   23284 C  CB  . LEU   B 1 1174 ? 53.73500   59.86400  -3.99200  1.000 39.88487  ?  1172 LEU   B CB  1 
ATOM   23285 C  CG  . LEU   B 1 1174 ? 54.86800   60.48100  -4.81500  1.000 38.03620  ?  1172 LEU   B CG  1 
ATOM   23286 C  CD1 . LEU   B 1 1174 ? 54.87800   59.93200  -6.23300  1.000 54.36477  ?  1172 LEU   B CD1 1 
ATOM   23287 C  CD2 . LEU   B 1 1174 ? 54.74800   61.99800  -4.82500  1.000 48.97987  ?  1172 LEU   B CD2 1 
ATOM   23288 N  N   . ARG   B 1 1175 ? 52.05100   58.89300  -1.38100  1.000 50.16148  ?  1173 ARG   B N   1 
ATOM   23289 C  CA  . ARG   B 1 1175 ? 50.81700   58.70600  -0.62500  1.000 53.72062  ?  1173 ARG   B CA  1 
ATOM   23290 C  C   . ARG   B 1 1175 ? 50.82800   59.54700  0.64400   1.000 61.55855  ?  1173 ARG   B C   1 
ATOM   23291 O  O   . ARG   B 1 1175 ? 49.86700   60.27100  0.93200   1.000 67.84438  ?  1173 ARG   B O   1 
ATOM   23292 C  CB  . ARG   B 1 1175 ? 50.61900   57.23100  -0.27700  1.000 46.91306  ?  1173 ARG   B CB  1 
ATOM   23293 C  CG  . ARG   B 1 1175 ? 50.07500   56.37100  -1.39900  1.000 61.16818  ?  1173 ARG   B CG  1 
ATOM   23294 C  CD  . ARG   B 1 1175 ? 49.51900   55.07800  -0.83100  1.000 54.04255  ?  1173 ARG   B CD  1 
ATOM   23295 N  NE  . ARG   B 1 1175 ? 50.37300   54.55400  0.22700   1.000 46.94387  ?  1173 ARG   B NE  1 
ATOM   23296 C  CZ  . ARG   B 1 1175 ? 51.32800   53.65400  0.04100   1.000 55.98496  ?  1173 ARG   B CZ  1 
ATOM   23297 N  NH1 . ARG   B 1 1175 ? 51.56500   53.13500  -1.15300  1.000 55.07458  ?  1173 ARG   B NH1 1 
ATOM   23298 N  NH2 . ARG   B 1 1175 ? 52.06300   53.26300  1.07800   1.000 54.20605  ?  1173 ARG   B NH2 1 
ATOM   23299 N  N   . MET   B 1 1176 ? 51.91800   59.46600  1.41100   1.000 52.52554  ?  1174 MET   B N   1 
ATOM   23300 C  CA  . MET   B 1 1176 ? 52.01300   60.20900  2.66300   1.000 47.86785  ?  1174 MET   B CA  1 
ATOM   23301 C  C   . MET   B 1 1176 ? 51.90300   61.71000  2.42900   1.000 51.62133  ?  1174 MET   B C   1 
ATOM   23302 O  O   . MET   B 1 1176 ? 51.30600   62.43000  3.23800   1.000 58.21901  ?  1174 MET   B O   1 
ATOM   23303 C  CB  . MET   B 1 1176 ? 53.32600   59.87000  3.36300   1.000 42.19198  ?  1174 MET   B CB  1 
ATOM   23304 C  CG  . MET   B 1 1176 ? 53.51600   58.38900  3.63300   1.000 39.74744  ?  1174 MET   B CG  1 
ATOM   23305 S  SD  . MET   B 1 1176 ? 55.15400   58.04700  4.29400   1.000 42.35500  ?  1174 MET   B SD  1 
ATOM   23306 C  CE  . MET   B 1 1176 ? 55.34200   59.43300  5.41100   1.000 43.15871  ?  1174 MET   B CE  1 
ATOM   23307 N  N   . VAL   B 1 1177 ? 52.47600   62.20100  1.32900   1.000 54.46250  ?  1175 VAL   B N   1 
ATOM   23308 C  CA  . VAL   B 1 1177 ? 52.36600   63.61900  0.99900   1.000 51.46754  ?  1175 VAL   B CA  1 
ATOM   23309 C  C   . VAL   B 1 1177 ? 50.91900   63.98000  0.68200   1.000 51.74912  ?  1175 VAL   B C   1 
ATOM   23310 O  O   . VAL   B 1 1177 ? 50.39600   64.99400  1.15700   1.000 61.24696  ?  1175 VAL   B O   1 
ATOM   23311 C  CB  . VAL   B 1 1177 ? 53.30700   63.97300  -0.16600  1.000 49.85363  ?  1175 VAL   B CB  1 
ATOM   23312 C  CG1 . VAL   B 1 1177 ? 52.90500   65.29900  -0.79500  1.000 47.14553  ?  1175 VAL   B CG1 1 
ATOM   23313 C  CG2 . VAL   B 1 1177 ? 54.75000   64.02700  0.31700   1.000 39.23308  ?  1175 VAL   B CG2 1 
ATOM   23314 N  N   . ALA   B 1 1178 ? 50.24900   63.15000  -0.12200  1.000 56.09364  ?  1176 ALA   B N   1 
ATOM   23315 C  CA  . ALA   B 1 1178 ? 48.85500   63.41800  -0.46200  1.000 53.22305  ?  1176 ALA   B CA  1 
ATOM   23316 C  C   . ALA   B 1 1178 ? 47.94500   63.30100  0.75400   1.000 53.50551  ?  1176 ALA   B C   1 
ATOM   23317 O  O   . ALA   B 1 1178 ? 46.89100   63.94600  0.80100   1.000 58.92888  ?  1176 ALA   B O   1 
ATOM   23318 C  CB  . ALA   B 1 1178 ? 48.39000   62.47000  -1.56700  1.000 58.27236  ?  1176 ALA   B CB  1 
ATOM   23319 N  N   . GLN   B 1 1179 ? 48.32900   62.48700  1.74000   1.000 54.02054  ?  1177 GLN   B N   1 
ATOM   23320 C  CA  . GLN   B 1 1179 ? 47.54700   62.39400  2.96800   1.000 44.59672  ?  1177 GLN   B CA  1 
ATOM   23321 C  C   . GLN   B 1 1179 ? 47.70900   63.64700  3.81800   1.000 51.56580  ?  1177 GLN   B C   1 
ATOM   23322 O  O   . GLN   B 1 1179 ? 46.75300   64.09600  4.46000   1.000 61.29737  ?  1177 GLN   B O   1 
ATOM   23323 C  CB  . GLN   B 1 1179 ? 47.95800   61.15000  3.75800   1.000 53.14584  ?  1177 GLN   B CB  1 
ATOM   23324 C  CG  . GLN   B 1 1179 ? 47.63300   59.83600  3.06500   1.000 46.21518  ?  1177 GLN   B CG  1 
ATOM   23325 C  CD  . GLN   B 1 1179 ? 48.41000   58.66500  3.63700   1.000 53.24753  ?  1177 GLN   B CD  1 
ATOM   23326 O  OE1 . GLN   B 1 1179 ? 49.19600   58.82100  4.57100   1.000 61.84065  ?  1177 GLN   B OE1 1 
ATOM   23327 N  NE2 . GLN   B 1 1179 ? 48.19700   57.48200  3.07200   1.000 53.11219  ?  1177 GLN   B NE2 1 
ATOM   23328 N  N   . PHE   B 1 1180 ? 48.91200   64.22600  3.83200   1.000 56.09098  ?  1178 PHE   B N   1 
ATOM   23329 C  CA  . PHE   B 1 1180 ? 49.13800   65.44900  4.59400   1.000 47.16746  ?  1178 PHE   B CA  1 
ATOM   23330 C  C   . PHE   B 1 1180 ? 48.32400   66.60900  4.03400   1.000 49.40465  ?  1178 PHE   B C   1 
ATOM   23331 O  O   . PHE   B 1 1180 ? 47.72100   67.37400  4.79500   1.000 66.00553  ?  1178 PHE   B O   1 
ATOM   23332 C  CB  . PHE   B 1 1180 ? 50.62700   65.79200  4.60100   1.000 43.12177  ?  1178 PHE   B CB  1 
ATOM   23333 C  CG  . PHE   B 1 1180 ? 50.97600   66.94500  5.49500   1.000 49.51387  ?  1178 PHE   B CG  1 
ATOM   23334 C  CD1 . PHE   B 1 1180 ? 51.20600   66.74200  6.84500   1.000 60.95111  ?  1178 PHE   B CD1 1 
ATOM   23335 C  CD2 . PHE   B 1 1180 ? 51.07900   68.23000  4.98900   1.000 42.79535  ?  1178 PHE   B CD2 1 
ATOM   23336 C  CE1 . PHE   B 1 1180 ? 51.52900   67.79700  7.67400   1.000 51.13856  ?  1178 PHE   B CE1 1 
ATOM   23337 C  CE2 . PHE   B 1 1180 ? 51.40200   69.29000  5.81300   1.000 49.44609  ?  1178 PHE   B CE2 1 
ATOM   23338 C  CZ  . PHE   B 1 1180 ? 51.62800   69.07300  7.15800   1.000 58.06368  ?  1178 PHE   B CZ  1 
ATOM   23339 N  N   . GLU   B 1 1181 ? 48.30400   66.76100  2.70700   1.000 43.14422  ?  1179 GLU   B N   1 
ATOM   23340 C  CA  . GLU   B 1 1181 ? 47.48500   67.80200  2.09500   1.000 46.89865  ?  1179 GLU   B CA  1 
ATOM   23341 C  C   . GLU   B 1 1181 ? 46.01000   67.59300  2.41000   1.000 64.00391  ?  1179 GLU   B C   1 
ATOM   23342 O  O   . GLU   B 1 1181 ? 45.27300   68.55900  2.64000   1.000 70.55766  ?  1179 GLU   B O   1 
ATOM   23343 C  CB  . GLU   B 1 1181 ? 47.70900   67.83100  0.58300   1.000 39.30627  ?  1179 GLU   B CB  1 
ATOM   23344 C  CG  . GLU   B 1 1181 ? 46.72500   68.72000  -0.16600  1.000 55.43331  ?  1179 GLU   B CG  1 
ATOM   23345 C  CD  . GLU   B 1 1181 ? 47.00100   68.78900  -1.65400  1.000 58.56433  ?  1179 GLU   B CD  1 
ATOM   23346 O  OE1 . GLU   B 1 1181 ? 47.42700   67.76700  -2.23400  1.000 59.96544  ?  1179 GLU   B OE1 1 
ATOM   23347 O  OE2 . GLU   B 1 1181 ? 46.79400   69.87100  -2.24300  1.000 61.10915  -1 1179 GLU   B OE2 1 
ATOM   23348 N  N   . HIS   B 1 1182 ? 45.56500   66.33400  2.42900   1.000 55.20773  ?  1180 HIS   B N   1 
ATOM   23349 C  CA  . HIS   B 1 1182 ? 44.16100   66.04300  2.69900   1.000 52.26565  ?  1180 HIS   B CA  1 
ATOM   23350 C  C   . HIS   B 1 1182 ? 43.77300   66.48100  4.10600   1.000 56.72023  ?  1180 HIS   B C   1 
ATOM   23351 O  O   . HIS   B 1 1182 ? 42.72500   67.10500  4.30700   1.000 65.30683  ?  1180 HIS   B O   1 
ATOM   23352 C  CB  . HIS   B 1 1182 ? 43.89300   64.55100  2.49700   1.000 61.61937  ?  1180 HIS   B CB  1 
ATOM   23353 C  CG  . HIS   B 1 1182 ? 42.44700   64.21500  2.30300   1.000 64.74356  ?  1180 HIS   B CG  1 
ATOM   23354 N  ND1 . HIS   B 1 1182 ? 41.74800   63.40300  3.16900   1.000 65.87605  ?  1180 HIS   B ND1 1 
ATOM   23355 C  CD2 . HIS   B 1 1182 ? 41.56900   64.58100  1.33900   1.000 53.72512  ?  1180 HIS   B CD2 1 
ATOM   23356 C  CE1 . HIS   B 1 1182 ? 40.50200   63.28300  2.74800   1.000 77.52122  ?  1180 HIS   B CE1 1 
ATOM   23357 N  NE2 . HIS   B 1 1182 ? 40.36700   63.98800  1.63900   1.000 71.51810  ?  1180 HIS   B NE2 1 
ATOM   23358 N  N   . LEU   B 1 1183 ? 44.61400   66.16900  5.09500   1.000 40.27688  ?  1181 LEU   B N   1 
ATOM   23359 C  CA  . LEU   B 1 1183 ? 44.35400   66.62800  6.45600   1.000 52.85801  ?  1181 LEU   B CA  1 
ATOM   23360 C  C   . LEU   B 1 1183 ? 44.44700   68.14400  6.55600   1.000 68.96584  ?  1181 LEU   B C   1 
ATOM   23361 O  O   . LEU   B 1 1183 ? 43.62100   68.77900  7.22200   1.000 79.18824  ?  1181 LEU   B O   1 
ATOM   23362 C  CB  . LEU   B 1 1183 ? 45.33700   65.98100  7.42700   1.000 44.09557  ?  1181 LEU   B CB  1 
ATOM   23363 C  CG  . LEU   B 1 1183 ? 45.09800   64.52000  7.78800   1.000 62.36443  ?  1181 LEU   B CG  1 
ATOM   23364 C  CD1 . LEU   B 1 1183 ? 46.26000   64.03300  8.60700   1.000 54.16645  ?  1181 LEU   B CD1 1 
ATOM   23365 C  CD2 . LEU   B 1 1183 ? 43.80300   64.37100  8.56200   1.000 63.27193  ?  1181 LEU   B CD2 1 
ATOM   23366 N  N   . LEU   B 1 1184 ? 45.45200   68.73700  5.91000   1.000 56.22696  ?  1182 LEU   B N   1 
ATOM   23367 C  CA  . LEU   B 1 1184 ? 45.62900   70.18300  5.96700   1.000 59.43341  ?  1182 LEU   B CA  1 
ATOM   23368 C  C   . LEU   B 1 1184 ? 44.40800   70.90300  5.40600   1.000 52.74745  ?  1182 LEU   B C   1 
ATOM   23369 O  O   . LEU   B 1 1184 ? 43.84100   71.78900  6.05700   1.000 55.37469  ?  1182 LEU   B O   1 
ATOM   23370 C  CB  . LEU   B 1 1184 ? 46.89700   70.57700  5.20700   1.000 66.94492  ?  1182 LEU   B CB  1 
ATOM   23371 C  CG  . LEU   B 1 1184 ? 47.73600   71.73700  5.74800   1.000 56.20181  ?  1182 LEU   B CG  1 
ATOM   23372 C  CD1 . LEU   B 1 1184 ? 49.05300   71.83200  4.99500   1.000 51.89888  ?  1182 LEU   B CD1 1 
ATOM   23373 C  CD2 . LEU   B 1 1184 ? 46.97900   73.04200  5.64600   1.000 58.03431  ?  1182 LEU   B CD2 1 
ATOM   23374 N  N   . LEU   B 1 1185 ? 43.97900   70.52600  4.19900   1.000 48.95791  ?  1183 LEU   B N   1 
ATOM   23375 C  CA  . LEU   B 1 1185 ? 42.80400   71.14700  3.60000   1.000 66.53621  ?  1183 LEU   B CA  1 
ATOM   23376 C  C   . LEU   B 1 1185 ? 41.51600   70.78500  4.33000   1.000 69.52807  ?  1183 LEU   B C   1 
ATOM   23377 O  O   . LEU   B 1 1185 ? 40.50300   71.47000  4.14700   1.000 68.06563  ?  1183 LEU   B O   1 
ATOM   23378 C  CB  . LEU   B 1 1185 ? 42.69600   70.76000  2.12400   1.000 44.25353  ?  1183 LEU   B CB  1 
ATOM   23379 C  CG  . LEU   B 1 1185 ? 43.80600   71.29200  1.21600   1.000 43.55278  ?  1183 LEU   B CG  1 
ATOM   23380 C  CD1 . LEU   B 1 1185 ? 43.50500   70.97900  -0.24100  1.000 33.33857  ?  1183 LEU   B CD1 1 
ATOM   23381 C  CD2 . LEU   B 1 1185 ? 43.99600   72.78800  1.42100   1.000 70.35497  ?  1183 LEU   B CD2 1 
ATOM   23382 N  N   . GLN   B 1 1186 ? 41.52600   69.72800  5.14400   1.000 71.03648  ?  1184 GLN   B N   1 
ATOM   23383 C  CA  . GLN   B 1 1186 ? 40.36100   69.41200  5.96400   1.000 63.56876  ?  1184 GLN   B CA  1 
ATOM   23384 C  C   . GLN   B 1 1186 ? 40.31800   70.27800  7.21600   1.000 63.78204  ?  1184 GLN   B C   1 
ATOM   23385 O  O   . GLN   B 1 1186 ? 39.26700   70.82400  7.56700   1.000 82.10906  ?  1184 GLN   B O   1 
ATOM   23386 C  CB  . GLN   B 1 1186 ? 40.36700   67.93100  6.34900   1.000 61.99888  ?  1184 GLN   B CB  1 
ATOM   23387 C  CG  . GLN   B 1 1186 ? 39.72100   67.00500  5.33200   1.000 69.02277  ?  1184 GLN   B CG  1 
ATOM   23388 C  CD  . GLN   B 1 1186 ? 39.73000   65.55800  5.78600   1.000 74.51903  ?  1184 GLN   B CD  1 
ATOM   23389 O  OE1 . GLN   B 1 1186 ? 38.72000   65.03900  6.26200   1.000 70.43950  ?  1184 GLN   B OE1 1 
ATOM   23390 N  NE2 . GLN   B 1 1186 ? 40.87500   64.90000  5.64600   1.000 70.25647  ?  1184 GLN   B NE2 1 
ATOM   23391 N  N   . ALA   B 1 1187 ? 41.45600   70.41400  7.89900   1.000 60.22513  ?  1185 ALA   B N   1 
ATOM   23392 C  CA  . ALA   B 1 1187 ? 41.48000   71.14500  9.16000   1.000 68.76274  ?  1185 ALA   B CA  1 
ATOM   23393 C  C   . ALA   B 1 1187 ? 41.27200   72.64000  8.95700   1.000 68.94631  ?  1185 ALA   B C   1 
ATOM   23394 O  O   . ALA   B 1 1187 ? 40.71500   73.30700  9.83600   1.000 70.60919  ?  1185 ALA   B O   1 
ATOM   23395 C  CB  . ALA   B 1 1187 ? 42.79700   70.88800  9.89100   1.000 59.55769  ?  1185 ALA   B CB  1 
ATOM   23396 N  N   . VAL   B 1 1188 ? 41.70000   73.18500  7.81600   1.000 61.49397  ?  1186 VAL   B N   1 
ATOM   23397 C  CA  . VAL   B 1 1188 ? 41.58900   74.62700  7.62100   1.000 68.25975  ?  1186 VAL   B CA  1 
ATOM   23398 C  C   . VAL   B 1 1188 ? 40.14200   75.03300  7.36500   1.000 67.11825  ?  1186 VAL   B C   1 
ATOM   23399 O  O   . VAL   B 1 1188 ? 39.73000   76.14200  7.72600   1.000 73.39285  ?  1186 VAL   B O   1 
ATOM   23400 C  CB  . VAL   B 1 1188 ? 42.52300   75.10000  6.48900   1.000 74.93990  ?  1186 VAL   B CB  1 
ATOM   23401 C  CG1 . VAL   B 1 1188 ? 41.94300   74.77300  5.11800   1.000 68.79164  ?  1186 VAL   B CG1 1 
ATOM   23402 C  CG2 . VAL   B 1 1188 ? 42.79000   76.59000  6.61900   1.000 64.11963  ?  1186 VAL   B CG2 1 
ATOM   23403 N  N   . HIS   B 1 1189 ? 39.34400   74.15500  6.75700   1.000 63.96131  ?  1187 HIS   B N   1 
ATOM   23404 C  CA  . HIS   B 1 1189 ? 37.93100   74.41700  6.52200   1.000 64.32145  ?  1187 HIS   B CA  1 
ATOM   23405 C  C   . HIS   B 1 1189 ? 37.04200   73.80000  7.59000   1.000 65.66933  ?  1187 HIS   B C   1 
ATOM   23406 O  O   . HIS   B 1 1189 ? 35.82500   74.01200  7.56700   1.000 79.94023  ?  1187 HIS   B O   1 
ATOM   23407 C  CB  . HIS   B 1 1189 ? 37.51600   73.89800  5.14400   1.000 69.08386  ?  1187 HIS   B CB  1 
ATOM   23408 C  CG  . HIS   B 1 1189 ? 38.31100   74.48000  4.01800   1.000 82.06452  ?  1187 HIS   B CG  1 
ATOM   23409 N  ND1 . HIS   B 1 1189 ? 39.12000   73.71700  3.20400   1.000 81.36206  ?  1187 HIS   B ND1 1 
ATOM   23410 C  CD2 . HIS   B 1 1189 ? 38.42900   75.75500  3.57600   1.000 83.22244  ?  1187 HIS   B CD2 1 
ATOM   23411 C  CE1 . HIS   B 1 1189 ? 39.69800   74.49500  2.30500   1.000 73.18409  ?  1187 HIS   B CE1 1 
ATOM   23412 N  NE2 . HIS   B 1 1189 ? 39.29600   75.73600  2.51000   1.000 74.99456  ?  1187 HIS   B NE2 1 
ATOM   23413 N  N   . GLY   B 1 1190 ? 37.62100   73.04100  8.51600   1.000 65.68977  ?  1188 GLY   B N   1 
ATOM   23414 C  CA  . GLY   B 1 1190 ? 36.87500   72.42500  9.59200   1.000 67.44827  ?  1188 GLY   B CA  1 
ATOM   23415 C  C   . GLY   B 1 1190 ? 37.61800   72.48300  10.91200  1.000 67.72220  ?  1188 GLY   B C   1 
ATOM   23416 O  O   . GLY   B 1 1190 ? 38.24400   71.50200  11.32400  1.000 81.42141  ?  1188 GLY   B O   1 
ATOM   23417 N  N   . LEU   B 1 1191 ? 37.56500   73.63500  11.57900  1.000 63.09224  ?  1189 LEU   B N   1 
ATOM   23418 C  CA  . LEU   B 1 1191 ? 38.18900   73.80600  12.88300  1.000 80.74925  ?  1189 LEU   B CA  1 
ATOM   23419 C  C   . LEU   B 1 1191 ? 37.24200   73.50100  14.03500  1.000 78.11552  ?  1189 LEU   B C   1 
ATOM   23420 O  O   . LEU   B 1 1191 ? 37.70700   73.13600  15.12100  1.000 68.43111  ?  1189 LEU   B O   1 
ATOM   23421 C  CB  . LEU   B 1 1191 ? 38.72200   75.23200  13.02200  1.000 86.00083  ?  1189 LEU   B CB  1 
ATOM   23422 C  CG  . LEU   B 1 1191 ? 39.26200   75.75100  11.69000  1.000 82.24050  ?  1189 LEU   B CG  1 
ATOM   23423 C  CD1 . LEU   B 1 1191 ? 38.62500   77.08400  11.33300  1.000 71.91157  ?  1189 LEU   B CD1 1 
ATOM   23424 C  CD2 . LEU   B 1 1191 ? 40.77800   75.84300  11.72100  1.000 77.67962  ?  1189 LEU   B CD2 1 
ATOM   23425 N  N   . ASP   B 1 1192 ? 35.93200   73.66200  13.82400  1.000 77.60440  ?  1190 ASP   B N   1 
ATOM   23426 C  CA  . ASP   B 1 1192 ? 34.91100   73.21400  14.76100  1.000 76.55041  ?  1190 ASP   B CA  1 
ATOM   23427 C  C   . ASP   B 1 1192 ? 34.65100   71.71500  14.67100  1.000 81.56603  ?  1190 ASP   B C   1 
ATOM   23428 O  O   . ASP   B 1 1192 ? 34.00700   71.15900  15.56800  1.000 81.87076  ?  1190 ASP   B O   1 
ATOM   23429 C  CB  . ASP   B 1 1192 ? 33.60100   73.96400  14.50900  1.000 82.87075  ?  1190 ASP   B CB  1 
ATOM   23430 C  CG  . ASP   B 1 1192 ? 33.06800   73.74400  13.10500  1.000 97.04752  ?  1190 ASP   B CG  1 
ATOM   23431 O  OD1 . ASP   B 1 1192 ? 33.88800   73.62400  12.17100  1.000 77.72605  ?  1190 ASP   B OD1 1 
ATOM   23432 O  OD2 . ASP   B 1 1192 ? 31.83000   73.68100  12.93500  1.000 120.70381 -1 1190 ASP   B OD2 1 
ATOM   23433 N  N   . GLN   B 1 1193 ? 35.11900   71.05600  13.61300  1.000 75.24069  ?  1191 GLN   B N   1 
ATOM   23434 C  CA  . GLN   B 1 1193 ? 34.93000   69.62300  13.46600  1.000 68.54540  ?  1191 GLN   B CA  1 
ATOM   23435 C  C   . GLN   B 1 1193 ? 35.86800   68.85300  14.38300  1.000 67.68668  ?  1191 GLN   B C   1 
ATOM   23436 O  O   . GLN   B 1 1193 ? 36.93500   69.33700  14.77200  1.000 69.54379  ?  1191 GLN   B O   1 
ATOM   23437 C  CB  . GLN   B 1 1193 ? 35.16200   69.18700  12.02000  1.000 72.65693  ?  1191 GLN   B CB  1 
ATOM   23438 C  CG  . GLN   B 1 1193 ? 33.92900   69.26600  11.14500  1.000 74.20691  ?  1191 GLN   B CG  1 
ATOM   23439 C  CD  . GLN   B 1 1193 ? 33.90400   68.18500  10.08600  1.000 81.19008  ?  1191 GLN   B CD  1 
ATOM   23440 O  OE1 . GLN   B 1 1193 ? 32.92700   67.44600  9.96100   1.000 87.62513  ?  1191 GLN   B OE1 1 
ATOM   23441 N  NE2 . GLN   B 1 1193 ? 34.98100   68.08400  9.31600   1.000 80.82672  ?  1191 GLN   B NE2 1 
ATOM   23442 N  N   . GLN   B 1 1194 ? 35.46200   67.63200  14.71400  1.000 60.66860  ?  1192 GLN   B N   1 
ATOM   23443 C  CA  . GLN   B 1 1194 ? 36.26000   66.77900  15.57800  1.000 77.97934  ?  1192 GLN   B CA  1 
ATOM   23444 C  C   . GLN   B 1 1194 ? 37.39500   66.14700  14.78500  1.000 71.64977  ?  1192 GLN   B C   1 
ATOM   23445 O  O   . GLN   B 1 1194 ? 37.23900   65.81200  13.60700  1.000 80.64283  ?  1192 GLN   B O   1 
ATOM   23446 C  CB  . GLN   B 1 1194 ? 35.38400   65.69900  16.21000  1.000 87.43803  ?  1192 GLN   B CB  1 
ATOM   23447 C  CG  . GLN   B 1 1194 ? 33.99400   66.19700  16.58100  1.000 90.13443  ?  1192 GLN   B CG  1 
ATOM   23448 C  CD  . GLN   B 1 1194 ? 33.26300   65.26000  17.52000  1.000 97.80334  ?  1192 GLN   B CD  1 
ATOM   23449 O  OE1 . GLN   B 1 1194 ? 33.82700   64.27500  17.99400  1.000 91.31375  ?  1192 GLN   B OE1 1 
ATOM   23450 N  NE2 . GLN   B 1 1194 ? 32.00100   65.56700  17.79900  1.000 94.01404  ?  1192 GLN   B NE2 1 
ATOM   23451 N  N   . VAL   B 1 1195 ? 38.54900   65.99700  15.44000  1.000 54.19374  ?  1193 VAL   B N   1 
ATOM   23452 C  CA  . VAL   B 1 1195 ? 39.70900   65.39300  14.78900  1.000 61.42617  ?  1193 VAL   B CA  1 
ATOM   23453 C  C   . VAL   B 1 1195 ? 39.39600   63.97200  14.33400  1.000 68.94433  ?  1193 VAL   B C   1 
ATOM   23454 O  O   . VAL   B 1 1195 ? 39.93200   63.50300  13.32100  1.000 71.68399  ?  1193 VAL   B O   1 
ATOM   23455 C  CB  . VAL   B 1 1195 ? 40.92300   65.45000  15.74000  1.000 63.20526  ?  1193 VAL   B CB  1 
ATOM   23456 C  CG1 . VAL   B 1 1195 ? 42.00100   64.46800  15.31800  1.000 62.59273  ?  1193 VAL   B CG1 1 
ATOM   23457 C  CG2 . VAL   B 1 1195 ? 41.48700   66.86500  15.78200  1.000 79.86687  ?  1193 VAL   B CG2 1 
ATOM   23458 N  N   . LYS   B 1 1196 ? 38.50300   63.27700  15.04500  1.000 66.68552  ?  1194 LYS   B N   1 
ATOM   23459 C  CA  . LYS   B 1 1196 ? 38.13000   61.92400  14.64400  1.000 62.60131  ?  1194 LYS   B CA  1 
ATOM   23460 C  C   . LYS   B 1 1196 ? 37.48800   61.90100  13.26200  1.000 65.19328  ?  1194 LYS   B C   1 
ATOM   23461 O  O   . LYS   B 1 1196 ? 37.57800   60.89100  12.55600  1.000 75.40827  ?  1194 LYS   B O   1 
ATOM   23462 C  CB  . LYS   B 1 1196 ? 37.18500   61.30500  15.67800  1.000 72.36817  ?  1194 LYS   B CB  1 
ATOM   23463 C  CG  . LYS   B 1 1196 ? 35.69800   61.50200  15.38400  1.000 73.66270  ?  1194 LYS   B CG  1 
ATOM   23464 C  CD  . LYS   B 1 1196 ? 34.82800   60.80100  16.41900  1.000 68.08205  ?  1194 LYS   B CD  1 
ATOM   23465 C  CE  . LYS   B 1 1196 ? 33.36300   60.75400  15.99700  1.000 75.92017  ?  1194 LYS   B CE  1 
ATOM   23466 N  NZ  . LYS   B 1 1196 ? 33.08400   59.71100  14.96900  1.000 85.66883  ?  1194 LYS   B NZ  1 
ATOM   23467 N  N   . ARG   B 1 1197 ? 36.84500   62.99700  12.85600  1.000 54.43715  ?  1195 ARG   B N   1 
ATOM   23468 C  CA  . ARG   B 1 1197 ? 36.19000   63.06700  11.55600  1.000 63.01417  ?  1195 ARG   B CA  1 
ATOM   23469 C  C   . ARG   B 1 1197 ? 37.15300   63.41900  10.42900  1.000 68.80901  ?  1195 ARG   B C   1 
ATOM   23470 O  O   . ARG   B 1 1197 ? 36.71000   63.58600  9.28800   1.000 66.81511  ?  1195 ARG   B O   1 
ATOM   23471 C  CB  . ARG   B 1 1197 ? 35.04800   64.08600  11.59100  1.000 73.14357  ?  1195 ARG   B CB  1 
ATOM   23472 C  CG  . ARG   B 1 1197 ? 33.79000   63.64200  10.85600  1.000 80.49048  ?  1195 ARG   B CG  1 
ATOM   23473 C  CD  . ARG   B 1 1197 ? 32.86100   62.85700  11.77200  1.000 81.98053  ?  1195 ARG   B CD  1 
ATOM   23474 N  NE  . ARG   B 1 1197 ? 32.35300   63.68000  12.86300  1.000 106.10208 ?  1195 ARG   B NE  1 
ATOM   23475 C  CZ  . ARG   B 1 1197 ? 31.39100   63.30900  13.69800  1.000 109.11352 ?  1195 ARG   B CZ  1 
ATOM   23476 N  NH1 . ARG   B 1 1197 ? 30.80500   62.12700  13.59600  1.000 100.74969 ?  1195 ARG   B NH1 1 
ATOM   23477 N  NH2 . ARG   B 1 1197 ? 31.00400   64.14700  14.65600  1.000 106.30445 ?  1195 ARG   B NH2 1 
ATOM   23478 N  N   . PHE   B 1 1198 ? 38.44400   63.54600  10.72000  1.000 59.53531  ?  1196 PHE   B N   1 
ATOM   23479 C  CA  . PHE   B 1 1198 ? 39.45100   63.79500  9.69800   1.000 64.51654  ?  1196 PHE   B CA  1 
ATOM   23480 C  C   . PHE   B 1 1198 ? 39.96600   62.46600  9.16500   1.000 73.36484  ?  1196 PHE   B C   1 
ATOM   23481 O  O   . PHE   B 1 1198 ? 40.41300   61.61300  9.93700   1.000 67.00862  ?  1196 PHE   B O   1 
ATOM   23482 C  CB  . PHE   B 1 1198 ? 40.60000   64.62600  10.26600  1.000 71.93131  ?  1196 PHE   B CB  1 
ATOM   23483 C  CG  . PHE   B 1 1198 ? 40.22200   66.04300  10.59100  1.000 73.19328  ?  1196 PHE   B CG  1 
ATOM   23484 C  CD1 . PHE   B 1 1198 ? 39.13000   66.64000  9.98200   1.000 71.04202  ?  1196 PHE   B CD1 1 
ATOM   23485 C  CD2 . PHE   B 1 1198 ? 40.96000   66.78000  11.50300  1.000 62.80201  ?  1196 PHE   B CD2 1 
ATOM   23486 C  CE1 . PHE   B 1 1198 ? 38.78000   67.94300  10.27800  1.000 64.93621  ?  1196 PHE   B CE1 1 
ATOM   23487 C  CE2 . PHE   B 1 1198 ? 40.61500   68.08300  11.80300  1.000 54.65728  ?  1196 PHE   B CE2 1 
ATOM   23488 C  CZ  . PHE   B 1 1198 ? 39.52400   68.66600  11.19000  1.000 65.55001  ?  1196 PHE   B CZ  1 
ATOM   23489 N  N   . GLU   B 1 1199 ? 39.89900   62.28900  7.85100   1.000 70.16785  ?  1197 GLU   B N   1 
ATOM   23490 C  CA  . GLU   B 1 1199 ? 40.27500   61.03300  7.21700   1.000 71.95934  ?  1197 GLU   B CA  1 
ATOM   23491 C  C   . GLU   B 1 1199 ? 41.67200   61.13800  6.62100   1.000 74.77659  ?  1197 GLU   B C   1 
ATOM   23492 O  O   . GLU   B 1 1199 ? 41.97900   62.09500  5.90200   1.000 69.80984  ?  1197 GLU   B O   1 
ATOM   23493 C  CB  . GLU   B 1 1199 ? 39.26200   60.64300  6.14000   1.000 71.44659  ?  1197 GLU   B CB  1 
ATOM   23494 C  CG  . GLU   B 1 1199 ? 38.58400   61.81800  5.46200   1.000 81.75731  ?  1197 GLU   B CG  1 
ATOM   23495 C  CD  . GLU   B 1 1199 ? 37.54600   61.37900  4.44800   1.000 107.88581 ?  1197 GLU   B CD  1 
ATOM   23496 O  OE1 . GLU   B 1 1199 ? 37.36600   60.15400  4.27200   1.000 90.21366  ?  1197 GLU   B OE1 1 
ATOM   23497 O  OE2 . GLU   B 1 1199 ? 36.91000   62.25600  3.82700   1.000 120.54901 -1 1197 GLU   B OE2 1 
ATOM   23498 N  N   . LEU   B 1 1200 ? 42.51400   60.14900  6.92800   1.000 74.34424  ?  1198 LEU   B N   1 
ATOM   23499 C  CA  . LEU   B 1 1200 ? 43.86000   60.11200  6.36900   1.000 63.51226  ?  1198 LEU   B CA  1 
ATOM   23500 C  C   . LEU   B 1 1200 ? 43.83400   59.69200  4.90500   1.000 54.32432  ?  1198 LEU   B C   1 
ATOM   23501 O  O   . LEU   B 1 1200 ? 44.61900   60.19600  4.09300   1.000 60.10486  ?  1198 LEU   B O   1 
ATOM   23502 C  CB  . LEU   B 1 1200 ? 44.73200   59.15800  7.18600   1.000 45.34182  ?  1198 LEU   B CB  1 
ATOM   23503 C  CG  . LEU   B 1 1200 ? 46.24800   59.31700  7.09400   1.000 50.81656  ?  1198 LEU   B CG  1 
ATOM   23504 C  CD1 . LEU   B 1 1200 ? 46.67200   60.61600  7.74300   1.000 65.56857  ?  1198 LEU   B CD1 1 
ATOM   23505 C  CD2 . LEU   B 1 1200 ? 46.94900   58.14100  7.75000   1.000 62.10418  ?  1198 LEU   B CD2 1 
ATOM   23506 N  N   . VAL   B 1 1201 ? 42.93500   58.77800  4.55000   1.000 54.14926  ?  1199 VAL   B N   1 
ATOM   23507 C  CA  . VAL   B 1 1201 ? 42.85400   58.25900  3.19100   1.000 65.63681  ?  1199 VAL   B CA  1 
ATOM   23508 C  C   . VAL   B 1 1201 ? 42.20500   59.29900  2.28500   1.000 68.47834  ?  1199 VAL   B C   1 
ATOM   23509 O  O   . VAL   B 1 1201 ? 41.39100   60.12000  2.72300   1.000 74.29668  ?  1199 VAL   B O   1 
ATOM   23510 C  CB  . VAL   B 1 1201 ? 42.08100   56.92300  3.17500   1.000 67.20785  ?  1199 VAL   B CB  1 
ATOM   23511 C  CG1 . VAL   B 1 1201 ? 40.58400   57.15700  3.33700   1.000 67.68720  ?  1199 VAL   B CG1 1 
ATOM   23512 C  CG2 . VAL   B 1 1201 ? 42.37700   56.13600  1.90800   1.000 64.80775  ?  1199 VAL   B CG2 1 
ATOM   23513 N  N   . THR   B 1 1202 ? 42.58300   59.27700  1.01000   1.000 70.23099  ?  1200 THR   B N   1 
ATOM   23514 C  CA  . THR   B 1 1202 ? 42.02400   60.16800  0.00600   1.000 70.24854  ?  1200 THR   B CA  1 
ATOM   23515 C  C   . THR   B 1 1202 ? 41.19500   59.37300  -0.99500  1.000 69.03060  ?  1200 THR   B C   1 
ATOM   23516 O  O   . THR   B 1 1202 ? 41.26800   58.14300  -1.06600  1.000 75.85051  ?  1200 THR   B O   1 
ATOM   23517 C  CB  . THR   B 1 1202 ? 43.12900   60.95100  -0.71600  1.000 71.64256  ?  1200 THR   B CB  1 
ATOM   23518 O  OG1 . THR   B 1 1202 ? 42.58700   61.58100  -1.88500  1.000 77.05037  ?  1200 THR   B OG1 1 
ATOM   23519 C  CG2 . THR   B 1 1202 ? 44.26200   60.02900  -1.12000  1.000 48.42047  ?  1200 THR   B CG2 1 
ATOM   23520 N  N   . GLU   B 1 1203 ? 40.39700   60.10400  -1.77800  1.000 72.64505  ?  1201 GLU   B N   1 
ATOM   23521 C  CA  . GLU   B 1 1203 ? 39.49400   59.46000  -2.72800  1.000 74.92257  ?  1201 GLU   B CA  1 
ATOM   23522 C  C   . GLU   B 1 1203 ? 40.25500   58.67400  -3.78800  1.000 65.32231  ?  1201 GLU   B C   1 
ATOM   23523 O  O   . GLU   B 1 1203 ? 39.76900   57.63900  -4.25800  1.000 69.01776  ?  1201 GLU   B O   1 
ATOM   23524 C  CB  . GLU   B 1 1203 ? 38.59200   60.50300  -3.38600  1.000 78.56188  ?  1201 GLU   B CB  1 
ATOM   23525 C  CG  . GLU   B 1 1203 ? 37.87100   61.41700  -2.40400  1.000 96.42797  ?  1201 GLU   B CG  1 
ATOM   23526 C  CD  . GLU   B 1 1203 ? 37.16500   60.65400  -1.29900  1.000 95.98171  ?  1201 GLU   B CD  1 
ATOM   23527 O  OE1 . GLU   B 1 1203 ? 36.13600   60.00600  -1.58400  1.000 87.43820  ?  1201 GLU   B OE1 1 
ATOM   23528 O  OE2 . GLU   B 1 1203 ? 37.64100   60.70000  -0.14400  1.000 94.41111  -1 1201 GLU   B OE2 1 
ATOM   23529 N  N   . ASP   B 1 1204 ? 41.44200   59.14400  -4.17800  1.000 71.81108  ?  1202 ASP   B N   1 
ATOM   23530 C  CA  . ASP   B 1 1204 ? 42.24500   58.39300  -5.13800  1.000 74.17090  ?  1202 ASP   B CA  1 
ATOM   23531 C  C   . ASP   B 1 1204 ? 42.79600   57.11300  -4.52500  1.000 70.72315  ?  1202 ASP   B C   1 
ATOM   23532 O  O   . ASP   B 1 1204 ? 42.92500   56.10100  -5.22300  1.000 75.49374  ?  1202 ASP   B O   1 
ATOM   23533 C  CB  . ASP   B 1 1204 ? 43.38100   59.26300  -5.67500  1.000 72.67606  ?  1202 ASP   B CB  1 
ATOM   23534 C  CG  . ASP   B 1 1204 ? 42.92900   60.19300  -6.78400  1.000 84.46567  ?  1202 ASP   B CG  1 
ATOM   23535 O  OD1 . ASP   B 1 1204 ? 42.21300   61.17300  -6.48700  1.000 91.14101  ?  1202 ASP   B OD1 1 
ATOM   23536 O  OD2 . ASP   B 1 1204 ? 43.28700   59.94100  -7.95400  1.000 94.30491  -1 1202 ASP   B OD2 1 
ATOM   23537 N  N   . GLU   B 1 1205 ? 43.12700   57.13500  -3.23200  1.000 68.01236  ?  1203 GLU   B N   1 
ATOM   23538 C  CA  . GLU   B 1 1205 ? 43.54000   55.90800  -2.56200  1.000 72.14514  ?  1203 GLU   B CA  1 
ATOM   23539 C  C   . GLU   B 1 1205 ? 42.37100   54.94900  -2.38500  1.000 67.79691  ?  1203 GLU   B C   1 
ATOM   23540 O  O   . GLU   B 1 1205 ? 42.56300   53.72800  -2.40800  1.000 75.13396  ?  1203 GLU   B O   1 
ATOM   23541 C  CB  . GLU   B 1 1205 ? 44.16700   56.23000  -1.20500  1.000 70.85615  ?  1203 GLU   B CB  1 
ATOM   23542 C  CG  . GLU   B 1 1205 ? 45.59100   56.76100  -1.27000  1.000 75.01217  ?  1203 GLU   B CG  1 
ATOM   23543 C  CD  . GLU   B 1 1205 ? 46.08100   57.28000  0.07100   1.000 84.40145  ?  1203 GLU   B CD  1 
ATOM   23544 O  OE1 . GLU   B 1 1205 ? 45.48300   56.91600  1.10600   1.000 73.53887  ?  1203 GLU   B OE1 1 
ATOM   23545 O  OE2 . GLU   B 1 1205 ? 47.05800   58.05800  0.09100   1.000 85.80720  -1 1203 GLU   B OE2 1 
ATOM   23546 N  N   . LYS   B 1 1206 ? 41.15900   55.48100  -2.20900  1.000 65.20690  ?  1204 LYS   B N   1 
ATOM   23547 C  CA  . LYS   B 1 1206 ? 39.99400   54.62800  -2.00500  1.000 63.62076  ?  1204 LYS   B CA  1 
ATOM   23548 C  C   . LYS   B 1 1206 ? 39.69600   53.80500  -3.25000  1.000 66.29290  ?  1204 LYS   B C   1 
ATOM   23549 O  O   . LYS   B 1 1206 ? 39.47000   52.59200  -3.16900  1.000 76.97938  ?  1204 LYS   B O   1 
ATOM   23550 C  CB  . LYS   B 1 1206 ? 38.78300   55.47900  -1.62000  1.000 70.43864  ?  1204 LYS   B CB  1 
ATOM   23551 C  CG  . LYS   B 1 1206 ? 38.84600   56.08400  -0.22400  1.000 80.31801  ?  1204 LYS   B CG  1 
ATOM   23552 C  CD  . LYS   B 1 1206 ? 37.58600   56.88700  0.07100   1.000 71.80696  ?  1204 LYS   B CD  1 
ATOM   23553 C  CE  . LYS   B 1 1206 ? 37.34700   57.03900  1.56700   1.000 72.20050  ?  1204 LYS   B CE  1 
ATOM   23554 N  NZ  . LYS   B 1 1206 ? 37.72200   58.38600  2.08100   1.000 75.52192  ?  1204 LYS   B NZ  1 
ATOM   23555 N  N   . ARG   B 1 1207 ? 39.70200   54.45200  -4.41800  1.000 62.47568  ?  1205 ARG   B N   1 
ATOM   23556 C  CA  . ARG   B 1 1207 ? 39.35900   53.75400  -5.65100  1.000 69.91399  ?  1205 ARG   B CA  1 
ATOM   23557 C  C   . ARG   B 1 1207 ? 40.40400   52.70300  -6.00600  1.000 77.51189  ?  1205 ARG   B C   1 
ATOM   23558 O  O   . ARG   B 1 1207 ? 40.05300   51.59800  -6.43500  1.000 85.76176  ?  1205 ARG   B O   1 
ATOM   23559 C  CB  . ARG   B 1 1207 ? 39.19600   54.74600  -6.80100  1.000 62.42453  ?  1205 ARG   B CB  1 
ATOM   23560 C  CG  . ARG   B 1 1207 ? 38.02700   54.39100  -7.70400  1.000 66.70326  ?  1205 ARG   B CG  1 
ATOM   23561 C  CD  . ARG   B 1 1207 ? 36.70400   54.77800  -7.03000  1.000 91.96098  ?  1205 ARG   B CD  1 
ATOM   23562 N  NE  . ARG   B 1 1207 ? 35.55400   53.98900  -7.46200  1.000 108.28956 ?  1205 ARG   B NE  1 
ATOM   23563 C  CZ  . ARG   B 1 1207 ? 34.77900   53.28400  -6.64600  1.000 102.21678 ?  1205 ARG   B CZ  1 
ATOM   23564 N  NH1 . ARG   B 1 1207 ? 34.97900   53.27600  -5.33900  1.000 95.07823  ?  1205 ARG   B NH1 1 
ATOM   23565 N  NH2 . ARG   B 1 1207 ? 33.78000   52.56700  -7.15600  1.000 86.80980  ?  1205 ARG   B NH2 1 
ATOM   23566 N  N   . ASP   B 1 1208 ? 41.69000   53.02900  -5.84200  1.000 70.10735  ?  1206 ASP   B N   1 
ATOM   23567 C  CA  . ASP   B 1 1208 ? 42.74100   52.04800  -6.10600  1.000 74.22226  ?  1206 ASP   B CA  1 
ATOM   23568 C  C   . ASP   B 1 1208 ? 42.55300   50.79400  -5.26400  1.000 73.81769  ?  1206 ASP   B C   1 
ATOM   23569 O  O   . ASP   B 1 1208 ? 42.73000   49.67600  -5.75900  1.000 82.52023  ?  1206 ASP   B O   1 
ATOM   23570 C  CB  . ASP   B 1 1208 ? 44.11500   52.66100  -5.84600  1.000 78.26415  ?  1206 ASP   B CB  1 
ATOM   23571 C  CG  . ASP   B 1 1208 ? 44.68400   53.34900  -7.06400  1.000 90.02982  ?  1206 ASP   B CG  1 
ATOM   23572 O  OD1 . ASP   B 1 1208 ? 43.89100   53.81400  -7.91000  1.000 87.20069  ?  1206 ASP   B OD1 1 
ATOM   23573 O  OD2 . ASP   B 1 1208 ? 45.92700   53.40600  -7.18400  1.000 104.95776 -1 1206 ASP   B OD2 1 
ATOM   23574 N  N   . LEU   B 1 1209 ? 42.19500   50.96200  -3.99000  1.000 74.38799  ?  1207 LEU   B N   1 
ATOM   23575 C  CA  . LEU   B 1 1209 ? 41.90200   49.81400  -3.13800  1.000 77.42997  ?  1207 LEU   B CA  1 
ATOM   23576 C  C   . LEU   B 1 1209 ? 40.76800   48.97800  -3.72200  1.000 79.60951  ?  1207 LEU   B C   1 
ATOM   23577 O  O   . LEU   B 1 1209 ? 40.86400   47.74700  -3.80100  1.000 82.16976  ?  1207 LEU   B O   1 
ATOM   23578 C  CB  . LEU   B 1 1209 ? 41.55600   50.29300  -1.72900  1.000 54.26415  ?  1207 LEU   B CB  1 
ATOM   23579 C  CG  . LEU   B 1 1209 ? 42.22800   49.55100  -0.57500  1.000 72.77547  ?  1207 LEU   B CG  1 
ATOM   23580 C  CD1 . LEU   B 1 1209 ? 43.71200   49.36300  -0.85200  1.000 53.49396  ?  1207 LEU   B CD1 1 
ATOM   23581 C  CD2 . LEU   B 1 1209 ? 42.02000   50.31200  0.72200   1.000 88.12951  ?  1207 LEU   B CD2 1 
ATOM   23582 N  N   . PHE   B 1 1210 ? 39.68700   49.63700  -4.14900  1.000 62.98295  ?  1208 PHE   B N   1 
ATOM   23583 C  CA  . PHE   B 1 1210 ? 38.58000   48.93000  -4.78600  1.000 65.66076  ?  1208 PHE   B CA  1 
ATOM   23584 C  C   . PHE   B 1 1210 ? 39.04400   48.19100  -6.03700  1.000 69.52035  ?  1208 PHE   B C   1 
ATOM   23585 O  O   . PHE   B 1 1210 ? 38.74500   47.00600  -6.21800  1.000 86.92182  ?  1208 PHE   B O   1 
ATOM   23586 C  CB  . PHE   B 1 1210 ? 37.45900   49.91800  -5.12300  1.000 73.83190  ?  1208 PHE   B CB  1 
ATOM   23587 C  CG  . PHE   B 1 1210 ? 36.27400   49.28700  -5.80400  1.000 77.57231  ?  1208 PHE   B CG  1 
ATOM   23588 C  CD1 . PHE   B 1 1210 ? 35.24300   48.73600  -5.06000  1.000 80.76069  ?  1208 PHE   B CD1 1 
ATOM   23589 C  CD2 . PHE   B 1 1210 ? 36.18800   49.25000  -7.18700  1.000 75.41676  ?  1208 PHE   B CD2 1 
ATOM   23590 C  CE1 . PHE   B 1 1210 ? 34.15400   48.15500  -5.68200  1.000 91.02153  ?  1208 PHE   B CE1 1 
ATOM   23591 C  CE2 . PHE   B 1 1210 ? 35.10300   48.66900  -7.81500  1.000 75.25873  ?  1208 PHE   B CE2 1 
ATOM   23592 C  CZ  . PHE   B 1 1210 ? 34.08500   48.12200  -7.06100  1.000 71.64062  ?  1208 PHE   B CZ  1 
ATOM   23593 N  N   . LEU   B 1 1211 ? 39.77900   48.87900  -6.91500  1.000 70.96140  ?  1209 LEU   B N   1 
ATOM   23594 C  CA  . LEU   B 1 1211 ? 40.24500   48.27200  -8.15700  1.000 76.61251  ?  1209 LEU   B CA  1 
ATOM   23595 C  C   . LEU   B 1 1211 ? 41.33600   47.22800  -7.94500  1.000 81.59671  ?  1209 LEU   B C   1 
ATOM   23596 O  O   . LEU   B 1 1211 ? 41.61900   46.46400  -8.87500  1.000 89.33469  ?  1209 LEU   B O   1 
ATOM   23597 C  CB  . LEU   B 1 1211 ? 40.75500   49.35300  -9.11500  1.000 74.49883  ?  1209 LEU   B CB  1 
ATOM   23598 C  CG  . LEU   B 1 1211 ? 39.74700   49.97700  -10.08600 1.000 89.67768  ?  1209 LEU   B CG  1 
ATOM   23599 C  CD1 . LEU   B 1 1211 ? 38.66400   50.75800  -9.35000  1.000 92.60960  ?  1209 LEU   B CD1 1 
ATOM   23600 C  CD2 . LEU   B 1 1211 ? 40.46300   50.86300  -11.09600 1.000 71.30167  ?  1209 LEU   B CD2 1 
ATOM   23601 N  N   . ARG   B 1 1212 ? 41.95400   47.17200  -6.76300  1.000 68.20089  ?  1210 ARG   B N   1 
ATOM   23602 C  CA  . ARG   B 1 1212 ? 43.01500   46.21200  -6.49100  1.000 72.85164  ?  1210 ARG   B CA  1 
ATOM   23603 C  C   . ARG   B 1 1212 ? 42.63100   45.14200  -5.47900  1.000 84.80266  ?  1210 ARG   B C   1 
ATOM   23604 O  O   . ARG   B 1 1212 ? 43.35500   44.14700  -5.35800  1.000 86.71226  ?  1210 ARG   B O   1 
ATOM   23605 C  CB  . ARG   B 1 1212 ? 44.28000   46.93000  -5.99100  1.000 75.12093  ?  1210 ARG   B CB  1 
ATOM   23606 C  CG  . ARG   B 1 1212 ? 45.31800   47.20300  -7.07600  1.000 73.45738  ?  1210 ARG   B CG  1 
ATOM   23607 C  CD  . ARG   B 1 1212 ? 45.73300   48.67200  -7.11500  1.000 63.51542  ?  1210 ARG   B CD  1 
ATOM   23608 N  NE  . ARG   B 1 1212 ? 46.43100   49.09700  -5.90800  1.000 67.78243  ?  1210 ARG   B NE  1 
ATOM   23609 C  CZ  . ARG   B 1 1212 ? 47.74500   49.25200  -5.81200  1.000 81.74212  ?  1210 ARG   B CZ  1 
ATOM   23610 N  NH1 . ARG   B 1 1212 ? 48.54600   49.02300  -6.84000  1.000 86.54425  ?  1210 ARG   B NH1 1 
ATOM   23611 N  NH2 . ARG   B 1 1212 ? 48.26900   49.64400  -4.65400  1.000 83.50690  ?  1210 ARG   B NH2 1 
ATOM   23612 N  N   . VAL   B 1 1213 ? 41.53200   45.31600  -4.74300  1.000 87.84281  ?  1211 VAL   B N   1 
ATOM   23613 C  CA  . VAL   B 1 1213 ? 41.17600   44.38500  -3.67600  1.000 77.17254  ?  1211 VAL   B CA  1 
ATOM   23614 C  C   . VAL   B 1 1213 ? 39.70600   43.99500  -3.78200  1.000 68.11621  ?  1211 VAL   B C   1 
ATOM   23615 O  O   . VAL   B 1 1213 ? 39.37800   42.82000  -3.98400  1.000 78.57686  ?  1211 VAL   B O   1 
ATOM   23616 C  CB  . VAL   B 1 1213 ? 41.47400   44.98400  -2.28800  1.000 56.01661  ?  1211 VAL   B CB  1 
ATOM   23617 C  CG1 . VAL   B 1 1213 ? 41.27200   43.94200  -1.20500  1.000 61.48101  ?  1211 VAL   B CG1 1 
ATOM   23618 C  CG2 . VAL   B 1 1213 ? 42.88300   45.55100  -2.22200  1.000 61.11604  ?  1211 VAL   B CG2 1 
ATOM   23619 N  N   . ASN   B 1 1214 ? 38.81100   44.97600  -3.64800  1.000 66.31523  ?  1212 ASN   B N   1 
ATOM   23620 C  CA  . ASN   B 1 1214 ? 37.38200   44.72900  -3.48900  1.000 65.12470  ?  1212 ASN   B CA  1 
ATOM   23621 C  C   . ASN   B 1 1214 ? 36.60200   44.87400  -4.79400  1.000 68.48102  ?  1212 ASN   B C   1 
ATOM   23622 O  O   . ASN   B 1 1214 ? 35.45300   45.32700  -4.77900  1.000 70.57966  ?  1212 ASN   B O   1 
ATOM   23623 C  CB  . ASN   B 1 1214 ? 36.80500   45.66200  -2.42700  1.000 58.46776  ?  1212 ASN   B CB  1 
ATOM   23624 C  CG  . ASN   B 1 1214 ? 37.44300   45.46100  -1.06800  1.000 55.49791  ?  1212 ASN   B CG  1 
ATOM   23625 O  OD1 . ASN   B 1 1214 ? 37.72600   44.33500  -0.66300  1.000 72.68473  ?  1212 ASN   B OD1 1 
ATOM   23626 N  ND2 . ASN   B 1 1214 ? 37.67600   46.55800  -0.35700  1.000 58.06301  ?  1212 ASN   B ND2 1 
ATOM   23627 N  N   . ASP   B 1 1215 ? 37.19800   44.49900  -5.92500  1.000 64.94049  ?  1213 ASP   B N   1 
ATOM   23628 C  CA  . ASP   B 1 1215 ? 36.48900   44.46800  -7.19700  1.000 66.73464  ?  1213 ASP   B CA  1 
ATOM   23629 C  C   . ASP   B 1 1215 ? 36.00300   43.06700  -7.54900  1.000 77.90600  ?  1213 ASP   B C   1 
ATOM   23630 O  O   . ASP   B 1 1215 ? 35.76800   42.77100  -8.72500  1.000 79.52431  ?  1213 ASP   B O   1 
ATOM   23631 C  CB  . ASP   B 1 1215 ? 37.37600   45.02200  -8.31400  1.000 72.39554  ?  1213 ASP   B CB  1 
ATOM   23632 C  CG  . ASP   B 1 1215 ? 36.57700   45.48500  -9.51800  1.000 82.13523  ?  1213 ASP   B CG  1 
ATOM   23633 O  OD1 . ASP   B 1 1215 ? 35.32900   45.49600  -9.43800  1.000 89.59072  ?  1213 ASP   B OD1 1 
ATOM   23634 O  OD2 . ASP   B 1 1215 ? 37.19500   45.83300  -10.54600 1.000 77.87837  -1 1213 ASP   B OD2 1 
ATOM   23635 N  N   . THR   B 1 1216 ? 35.85100   42.20000  -6.55200  1.000 79.82532  ?  1214 THR   B N   1 
ATOM   23636 C  CA  . THR   B 1 1216 ? 35.41400   40.82800  -6.78000  1.000 75.85331  ?  1214 THR   B CA  1 
ATOM   23637 C  C   . THR   B 1 1216 ? 33.90100   40.80800  -6.95300  1.000 72.12628  ?  1214 THR   B C   1 
ATOM   23638 O  O   . THR   B 1 1216 ? 33.15500   41.08100  -6.00700  1.000 77.12994  ?  1214 THR   B O   1 
ATOM   23639 C  CB  . THR   B 1 1216 ? 35.84800   39.93300  -5.62400  1.000 85.23932  ?  1214 THR   B CB  1 
ATOM   23640 O  OG1 . THR   B 1 1216 ? 35.58600   40.59500  -4.38100  1.000 73.79369  ?  1214 THR   B OG1 1 
ATOM   23641 C  CG2 . THR   B 1 1216 ? 37.33500   39.61200  -5.72500  1.000 73.05458  ?  1214 THR   B CG2 1 
ATOM   23642 N  N   . ALA   B 1 1217 ? 33.44700   40.48900  -8.16400  1.000 76.24570  ?  1215 ALA   B N   1 
ATOM   23643 C  CA  . ALA   B 1 1217 ? 32.01600   40.42600  -8.45300  1.000 76.20002  ?  1215 ALA   B CA  1 
ATOM   23644 C  C   . ALA   B 1 1217 ? 31.82600   39.55000  -9.68400  1.000 77.54755  ?  1215 ALA   B C   1 
ATOM   23645 O  O   . ALA   B 1 1217 ? 32.25900   39.92200  -10.77900 1.000 58.38628  ?  1215 ALA   B O   1 
ATOM   23646 C  CB  . ALA   B 1 1217 ? 31.44000   41.82000  -8.67200  1.000 62.27692  ?  1215 ALA   B CB  1 
ATOM   23647 N  N   . LYS   B 1 1218 ? 31.18900   38.39600  -9.50100  1.000 83.39865  ?  1216 LYS   B N   1 
ATOM   23648 C  CA  . LYS   B 1 1218 ? 30.91400   37.47300  -10.59100 1.000 76.58573  ?  1216 LYS   B CA  1 
ATOM   23649 C  C   . LYS   B 1 1218 ? 29.51500   36.90400  -10.41000 1.000 83.31266  ?  1216 LYS   B C   1 
ATOM   23650 O  O   . LYS   B 1 1218 ? 29.03500   36.74200  -9.28500  1.000 78.61287  ?  1216 LYS   B O   1 
ATOM   23651 C  CB  . LYS   B 1 1218 ? 31.96100   36.34700  -10.65000 1.000 65.29980  ?  1216 LYS   B CB  1 
ATOM   23652 C  CG  . LYS   B 1 1218 ? 31.89800   35.48800  -11.90500 1.000 78.32914  ?  1216 LYS   B CG  1 
ATOM   23653 C  CD  . LYS   B 1 1218 ? 33.18400   34.69800  -12.10400 1.000 77.53446  ?  1216 LYS   B CD  1 
ATOM   23654 C  CE  . LYS   B 1 1218 ? 33.09300   33.79700  -13.32600 1.000 81.52647  ?  1216 LYS   B CE  1 
ATOM   23655 N  NZ  . LYS   B 1 1218 ? 34.41900   33.23700  -13.71300 1.000 81.08769  ?  1216 LYS   B NZ  1 
ATOM   23656 N  N   . ALA   B 1 1219 ? 28.85700   36.61700  -11.53100 1.000 94.20707  ?  1217 ALA   B N   1 
ATOM   23657 C  CA  . ALA   B 1 1219 ? 27.49800   36.08600  -11.51900 1.000 76.70482  ?  1217 ALA   B CA  1 
ATOM   23658 C  C   . ALA   B 1 1219 ? 27.55600   34.57900  -11.30400 1.000 82.81547  ?  1217 ALA   B C   1 
ATOM   23659 O  O   . ALA   B 1 1219 ? 28.05400   33.84000  -12.16100 1.000 89.60018  ?  1217 ALA   B O   1 
ATOM   23660 C  CB  . ALA   B 1 1219 ? 26.77500   36.42900  -12.81800 1.000 60.36065  ?  1217 ALA   B CB  1 
ATOM   23661 N  N   . TYR   B 1 1220 ? 27.04600   34.11900  -10.16200 1.000 81.81013  ?  1218 TYR   B N   1 
ATOM   23662 C  CA  . TYR   B 1 1220 ? 27.06800   32.70700  -9.83500  1.000 74.69884  ?  1218 TYR   B CA  1 
ATOM   23663 C  C   . TYR   B 1 1220 ? 25.65100   32.15400  -9.73600  1.000 84.21584  ?  1218 TYR   B C   1 
ATOM   23664 O  O   . TYR   B 1 1220 ? 24.75100   32.83800  -9.23500  1.000 79.93044  ?  1218 TYR   B O   1 
ATOM   23665 C  CB  . TYR   B 1 1220 ? 27.82300   32.46200  -8.52000  1.000 73.67417  ?  1218 TYR   B CB  1 
ATOM   23666 C  CG  . TYR   B 1 1220 ? 29.32700   32.51700  -8.68300  1.000 81.46091  ?  1218 TYR   B CG  1 
ATOM   23667 C  CD1 . TYR   B 1 1220 ? 29.92400   32.14200  -9.88000  1.000 76.85491  ?  1218 TYR   B CD1 1 
ATOM   23668 C  CD2 . TYR   B 1 1220 ? 30.14800   32.94700  -7.64800  1.000 75.57970  ?  1218 TYR   B CD2 1 
ATOM   23669 C  CE1 . TYR   B 1 1220 ? 31.29500   32.18800  -10.04300 1.000 78.98854  ?  1218 TYR   B CE1 1 
ATOM   23670 C  CE2 . TYR   B 1 1220 ? 31.52500   32.99600  -7.80200  1.000 72.48682  ?  1218 TYR   B CE2 1 
ATOM   23671 C  CZ  . TYR   B 1 1220 ? 32.09100   32.61600  -9.00200  1.000 72.09042  ?  1218 TYR   B CZ  1 
ATOM   23672 O  OH  . TYR   B 1 1220 ? 33.45600   32.66100  -9.16700  1.000 75.68453  ?  1218 TYR   B OH  1 
ATOM   23673 N  N   . PRO   B 1 1221 ? 25.42400   30.92700  -10.20800 1.000 89.55078  ?  1219 PRO   B N   1 
ATOM   23674 C  CA  . PRO   B 1 1221 ? 24.05400   30.40700  -10.29800 1.000 69.37165  ?  1219 PRO   B CA  1 
ATOM   23675 C  C   . PRO   B 1 1221 ? 23.40000   30.25200  -8.93300  1.000 71.70931  ?  1219 PRO   B C   1 
ATOM   23676 O  O   . PRO   B 1 1221 ? 24.06600   30.08100  -7.91000  1.000 73.88199  ?  1219 PRO   B O   1 
ATOM   23677 C  CB  . PRO   B 1 1221 ? 24.23500   29.04700  -10.98300 1.000 64.87610  ?  1219 PRO   B CB  1 
ATOM   23678 C  CG  . PRO   B 1 1221 ? 25.55800   29.14100  -11.68100 1.000 76.85204  ?  1219 PRO   B CG  1 
ATOM   23679 C  CD  . PRO   B 1 1221 ? 26.40600   30.00800  -10.80600 1.000 77.62982  ?  1219 PRO   B CD  1 
ATOM   23680 N  N   . ASN   B 1 1222 ? 22.06700   30.30700  -8.93600  1.000 65.01515  ?  1220 ASN   B N   1 
ATOM   23681 C  CA  . ASN   B 1 1222 ? 21.25900   30.20000  -7.73000  1.000 82.82190  ?  1220 ASN   B CA  1 
ATOM   23682 C  C   . ASN   B 1 1222 ? 20.75700   28.78100  -7.48300  1.000 76.75624  ?  1220 ASN   B C   1 
ATOM   23683 O  O   . ASN   B 1 1222 ? 19.77300   28.59500  -6.75900  1.000 69.95208  ?  1220 ASN   B O   1 
ATOM   23684 C  CB  . ASN   B 1 1222 ? 20.07800   31.17000  -7.80300  1.000 69.43392  ?  1220 ASN   B CB  1 
ATOM   23685 C  CG  . ASN   B 1 1222 ? 20.15700   32.26800  -6.76000  1.000 87.45303  ?  1220 ASN   B CG  1 
ATOM   23686 O  OD1 . ASN   B 1 1222 ? 21.23400   32.58800  -6.25700  1.000 108.16171 ?  1220 ASN   B OD1 1 
ATOM   23687 N  ND2 . ASN   B 1 1222 ? 19.01000   32.84800  -6.42500  1.000 87.23500  ?  1220 ASN   B ND2 1 
ATOM   23688 N  N   . LYS   B 1 1223 ? 21.40800   27.77900  -8.06900  1.000 70.89361  ?  1221 LYS   B N   1 
ATOM   23689 C  CA  . LYS   B 1 1223 ? 21.00100   26.39200  -7.88600  1.000 66.95414  ?  1221 LYS   B CA  1 
ATOM   23690 C  C   . LYS   B 1 1223 ? 21.49700   25.88900  -6.53700  1.000 74.83251  ?  1221 LYS   B C   1 
ATOM   23691 O  O   . LYS   B 1 1223 ? 22.70900   25.79400  -6.31200  1.000 91.30437  ?  1221 LYS   B O   1 
ATOM   23692 C  CB  . LYS   B 1 1223 ? 21.54400   25.52300  -9.01800  1.000 57.38065  ?  1221 LYS   B CB  1 
ATOM   23693 N  N   . LEU   B 1 1224 ? 20.56500   25.56400  -5.64300  1.000 62.35001  ?  1222 LEU   B N   1 
ATOM   23694 C  CA  . LEU   B 1 1224 ? 20.93700   25.10900  -4.31000  1.000 64.76538  ?  1222 LEU   B CA  1 
ATOM   23695 C  C   . LEU   B 1 1224 ? 21.72900   23.80800  -4.38700  1.000 75.27225  ?  1222 LEU   B C   1 
ATOM   23696 O  O   . LEU   B 1 1224 ? 21.57300   23.01200  -5.31700  1.000 80.55207  ?  1222 LEU   B O   1 
ATOM   23697 C  CB  . LEU   B 1 1224 ? 19.69000   24.91600  -3.44700  1.000 62.46917  ?  1222 LEU   B CB  1 
ATOM   23698 C  CG  . LEU   B 1 1224 ? 18.72100   26.09900  -3.41500  1.000 61.37154  ?  1222 LEU   B CG  1 
ATOM   23699 C  CD1 . LEU   B 1 1224 ? 17.44400   25.76400  -4.17200  1.000 69.51747  ?  1222 LEU   B CD1 1 
ATOM   23700 C  CD2 . LEU   B 1 1224 ? 18.41600   26.51800  -1.98300  1.000 64.00797  ?  1222 LEU   B CD2 1 
ATOM   23701 N  N   . ILE   B 1 1225 ? 22.59200   23.59900  -3.38800  1.000 78.25272  ?  1223 ILE   B N   1 
ATOM   23702 C  CA  . ILE   B 1 1225 ? 23.44400   22.41600  -3.37100  1.000 74.54039  ?  1223 ILE   B CA  1 
ATOM   23703 C  C   . ILE   B 1 1225 ? 22.63200   21.13500  -3.21700  1.000 63.90036  ?  1223 ILE   B C   1 
ATOM   23704 O  O   . ILE   B 1 1225 ? 23.08800   20.06100  -3.62700  1.000 68.00749  ?  1223 ILE   B O   1 
ATOM   23705 C  CB  . ILE   B 1 1225 ? 24.50100   22.53900  -2.25300  1.000 56.88258  ?  1223 ILE   B CB  1 
ATOM   23706 C  CG1 . ILE   B 1 1225 ? 25.72000   21.67600  -2.57600  1.000 56.74181  ?  1223 ILE   B CG1 1 
ATOM   23707 C  CG2 . ILE   B 1 1225 ? 23.91300   22.16400  -0.89700  1.000 52.77593  ?  1223 ILE   B CG2 1 
ATOM   23708 C  CD1 . ILE   B 1 1225 ? 26.50800   22.18200  -3.75900  1.000 66.06946  ?  1223 ILE   B CD1 1 
ATOM   23709 N  N   . MET   B 1 1226 ? 21.42900   21.22300  -2.64500  1.000 67.15232  ?  1224 MET   B N   1 
ATOM   23710 C  CA  . MET   B 1 1226 ? 20.57700   20.04800  -2.50800  1.000 52.85069  ?  1224 MET   B CA  1 
ATOM   23711 C  C   . MET   B 1 1226 ? 20.01900   19.61600  -3.85700  1.000 68.55092  ?  1224 MET   B C   1 
ATOM   23712 O  O   . MET   B 1 1226 ? 19.98400   18.41900  -4.16800  1.000 72.64628  ?  1224 MET   B O   1 
ATOM   23713 C  CB  . MET   B 1 1226 ? 19.44400   20.35100  -1.53100  1.000 40.46267  ?  1224 MET   B CB  1 
ATOM   23714 C  CG  . MET   B 1 1226 ? 19.76600   21.49800  -0.59200  1.000 62.45599  ?  1224 MET   B CG  1 
ATOM   23715 S  SD  . MET   B 1 1226 ? 18.33300   22.12800  0.29800   1.000 94.82519  ?  1224 MET   B SD  1 
ATOM   23716 C  CE  . MET   B 1 1226 ? 17.37200   22.82500  -1.04100  1.000 81.99141  ?  1224 MET   B CE  1 
ATOM   23717 N  N   . SER   B 1 1227 ? 19.57600   20.57700  -4.67100  1.000 76.38957  ?  1225 SER   B N   1 
ATOM   23718 C  CA  . SER   B 1 1227 ? 19.02900   20.25800  -5.98300  1.000 73.33480  ?  1225 SER   B CA  1 
ATOM   23719 C  C   . SER   B 1 1227 ? 20.10700   19.85800  -6.98000  1.000 80.56575  ?  1225 SER   B C   1 
ATOM   23720 O  O   . SER   B 1 1227 ? 19.80000   19.16600  -7.95700  1.000 86.91736  ?  1225 SER   B O   1 
ATOM   23721 C  CB  . SER   B 1 1227 ? 18.23700   21.44800  -6.52500  1.000 72.68096  ?  1225 SER   B CB  1 
ATOM   23722 O  OG  . SER   B 1 1227 ? 17.16300   21.77900  -5.66300  1.000 79.55569  ?  1225 SER   B OG  1 
ATOM   23723 N  N   . MET   B 1 1228 ? 21.35500   20.28000  -6.76400  1.000 76.72180  ?  1226 MET   B N   1 
ATOM   23724 C  CA  . MET   B 1 1228 ? 22.43200   19.89300  -7.67000  1.000 80.30034  ?  1226 MET   B CA  1 
ATOM   23725 C  C   . MET   B 1 1228 ? 22.65500   18.38700  -7.64000  1.000 90.16415  ?  1226 MET   B C   1 
ATOM   23726 O  O   . MET   B 1 1228 ? 22.80700   17.74900  -8.68800  1.000 87.10339  ?  1226 MET   B O   1 
ATOM   23727 C  CB  . MET   B 1 1228 ? 23.71800   20.63700  -7.31200  1.000 79.73876  ?  1226 MET   B CB  1 
ATOM   23728 C  CG  . MET   B 1 1228 ? 23.80300   22.03000  -7.90600  1.000 91.87834  ?  1226 MET   B CG  1 
ATOM   23729 S  SD  . MET   B 1 1228 ? 25.48000   22.69000  -7.88100  1.000 95.44218  ?  1226 MET   B SD  1 
ATOM   23730 C  CE  . MET   B 1 1228 ? 25.44500   23.73500  -9.33600  1.000 63.70809  ?  1226 MET   B CE  1 
ATOM   23731 N  N   . LEU   B 1 1229 ? 22.67500   17.79800  -6.44100  1.000 91.15721  ?  1227 LEU   B N   1 
ATOM   23732 C  CA  . LEU   B 1 1229 ? 22.79600   16.34900  -6.33500  1.000 82.59124  ?  1227 LEU   B CA  1 
ATOM   23733 C  C   . LEU   B 1 1229 ? 21.61900   15.65100  -7.00400  1.000 92.65758  ?  1227 LEU   B C   1 
ATOM   23734 O  O   . LEU   B 1 1229 ? 21.78900   14.60400  -7.63900  1.000 88.27934  ?  1227 LEU   B O   1 
ATOM   23735 C  CB  . LEU   B 1 1229 ? 22.90100   15.93400  -4.86700  1.000 70.35220  ?  1227 LEU   B CB  1 
ATOM   23736 C  CG  . LEU   B 1 1229 ? 23.13300   14.44400  -4.60600  1.000 66.02994  ?  1227 LEU   B CG  1 
ATOM   23737 C  CD1 . LEU   B 1 1229 ? 24.52300   14.02800  -5.06200  1.000 71.02436  ?  1227 LEU   B CD1 1 
ATOM   23738 C  CD2 . LEU   B 1 1229 ? 22.92100   14.11200  -3.13800  1.000 59.29790  ?  1227 LEU   B CD2 1 
ATOM   23739 N  N   . GLU   B 1 1230 ? 20.41700   16.22200  -6.88000  1.000 74.95414  ?  1228 GLU   B N   1 
ATOM   23740 C  CA  . GLU   B 1 1230 ? 19.24600   15.64000  -7.52900  1.000 77.62717  ?  1228 GLU   B CA  1 
ATOM   23741 C  C   . GLU   B 1 1230 ? 19.40600   15.62900  -9.04300  1.000 89.76213  ?  1228 GLU   B C   1 
ATOM   23742 O  O   . GLU   B 1 1230 ? 19.15800   14.61100  -9.70000  1.000 107.51379 ?  1228 GLU   B O   1 
ATOM   23743 C  CB  . GLU   B 1 1230 ? 17.98500   16.40800  -7.12900  1.000 65.20707  ?  1228 GLU   B CB  1 
ATOM   23744 C  CG  . GLU   B 1 1230 ? 17.66500   16.35700  -5.64400  1.000 75.20026  ?  1228 GLU   B CG  1 
ATOM   23745 C  CD  . GLU   B 1 1230 ? 16.30500   16.94600  -5.31500  1.000 74.72593  ?  1228 GLU   B CD  1 
ATOM   23746 O  OE1 . GLU   B 1 1230 ? 15.64300   17.47200  -6.23500  1.000 71.13309  ?  1228 GLU   B OE1 1 
ATOM   23747 O  OE2 . GLU   B 1 1230 ? 15.89500   16.87900  -4.13700  1.000 62.16883  -1 1228 GLU   B OE2 1 
ATOM   23748 N  N   . ASP   B 1 1231 ? 19.81600   16.76200  -9.61700  1.000 81.08171  ?  1229 ASP   B N   1 
ATOM   23749 C  CA  . ASP   B 1 1231 ? 20.03000   16.82900  -11.05900 1.000 92.83228  ?  1229 ASP   B CA  1 
ATOM   23750 C  C   . ASP   B 1 1231 ? 21.18000   15.92500  -11.48200 1.000 79.64106  ?  1229 ASP   B C   1 
ATOM   23751 O  O   . ASP   B 1 1231 ? 21.07000   15.18100  -12.46300 1.000 82.95970  ?  1229 ASP   B O   1 
ATOM   23752 C  CB  . ASP   B 1 1231 ? 20.29700   18.27300  -11.48500 1.000 99.61123  ?  1229 ASP   B CB  1 
ATOM   23753 C  CG  . ASP   B 1 1231 ? 19.18400   19.21700  -11.07900 1.000 95.08077  ?  1229 ASP   B CG  1 
ATOM   23754 O  OD1 . ASP   B 1 1231 ? 18.22200   18.75800  -10.42800 1.000 114.30558 ?  1229 ASP   B OD1 1 
ATOM   23755 O  OD2 . ASP   B 1 1231 ? 19.27200   20.41700  -11.41200 1.000 92.88460  -1 1229 ASP   B OD2 1 
ATOM   23756 N  N   . TRP   B 1 1232 ? 22.29400   15.97400  -10.74600 1.000 83.72089  ?  1230 TRP   B N   1 
ATOM   23757 C  CA  . TRP   B 1 1232 ? 23.44500   15.15000  -11.09700 1.000 99.74063  ?  1230 TRP   B CA  1 
ATOM   23758 C  C   . TRP   B 1 1232 ? 23.13800   13.66500  -10.95100 1.000 92.00809  ?  1230 TRP   B C   1 
ATOM   23759 O  O   . TRP   B 1 1232 ? 23.66600   12.84800  -11.71400 1.000 88.53173  ?  1230 TRP   B O   1 
ATOM   23760 C  CB  . TRP   B 1 1232 ? 24.65200   15.53200  -10.23700 1.000 94.77321  ?  1230 TRP   B CB  1 
ATOM   23761 C  CG  . TRP   B 1 1232 ? 25.36300   16.74300  -10.71200 1.000 101.95201 ?  1230 TRP   B CG  1 
ATOM   23762 C  CD1 . TRP   B 1 1232 ? 25.41000   17.98200  -10.10800 1.000 86.98745  ?  1230 TRP   B CD1 1 
ATOM   23763 C  CD2 . TRP   B 1 1232 ? 26.14200   16.85000  -11.90100 1.000 118.96297 ?  1230 TRP   B CD2 1 
ATOM   23764 N  NE1 . TRP   B 1 1232 ? 26.17000   18.84300  -10.86100 1.000 85.76408  ?  1230 TRP   B NE1 1 
ATOM   23765 C  CE2 . TRP   B 1 1232 ? 26.62900   18.17000  -11.96500 1.000 117.64014 ?  1230 TRP   B CE2 1 
ATOM   23766 C  CE3 . TRP   B 1 1232 ? 26.47400   15.95600  -12.92300 1.000 106.49823 ?  1230 TRP   B CE3 1 
ATOM   23767 C  CZ2 . TRP   B 1 1232 ? 27.43400   18.61600  -13.01000 1.000 120.01278 ?  1230 TRP   B CZ2 1 
ATOM   23768 C  CZ3 . TRP   B 1 1232 ? 27.28000   16.39800  -13.95900 1.000 102.22388 ?  1230 TRP   B CZ3 1 
ATOM   23769 C  CH2 . TRP   B 1 1232 ? 27.74300   17.72000  -14.00400 1.000 111.80642 ?  1230 TRP   B CH2 1 
ATOM   23770 N  N   . ALA   B 1 1233 ? 22.28700   13.29500  -9.98900  1.000 86.12540  ?  1231 ALA   B N   1 
ATOM   23771 C  CA  . ALA   B 1 1233 ? 21.95200   11.88500  -9.81200  1.000 91.54077  ?  1231 ALA   B CA  1 
ATOM   23772 C  C   . ALA   B 1 1233 ? 21.12900   11.35800  -10.98200 1.000 103.38266 ?  1231 ALA   B C   1 
ATOM   23773 O  O   . ALA   B 1 1233 ? 21.30900   10.21100  -11.40400 1.000 100.21849 ?  1231 ALA   B O   1 
ATOM   23774 C  CB  . ALA   B 1 1233 ? 21.20200   11.67400  -8.49700  1.000 74.48982  ?  1231 ALA   B CB  1 
ATOM   23775 N  N   . ALA   B 1 1234 ? 20.22400   12.17800  -11.51900 1.000 92.78352  ?  1232 ALA   B N   1 
ATOM   23776 C  CA  . ALA   B 1 1234 ? 19.38500   11.72400  -12.62300 1.000 84.77843  ?  1232 ALA   B CA  1 
ATOM   23777 C  C   . ALA   B 1 1234 ? 20.20800   11.47200  -13.88100 1.000 95.36055  ?  1232 ALA   B C   1 
ATOM   23778 O  O   . ALA   B 1 1234 ? 19.95600   10.50500  -14.60900 1.000 99.60108  ?  1232 ALA   B O   1 
ATOM   23779 C  CB  . ALA   B 1 1234 ? 18.28200   12.74600  -12.89800 1.000 84.78683  ?  1232 ALA   B CB  1 
ATOM   23780 N  N   . ALA   B 1 1235 ? 21.20100   12.32300  -14.14900 1.000 103.65376 ?  1233 ALA   B N   1 
ATOM   23781 C  CA  . ALA   B 1 1235 ? 22.00700   12.17400  -15.35600 1.000 96.36331  ?  1233 ALA   B CA  1 
ATOM   23782 C  C   . ALA   B 1 1235 ? 23.00900   11.03300  -15.22400 1.000 90.05686  ?  1233 ALA   B C   1 
ATOM   23783 O  O   . ALA   B 1 1235 ? 23.13600   10.20200  -16.13000 1.000 95.38491  ?  1233 ALA   B O   1 
ATOM   23784 C  CB  . ALA   B 1 1235 ? 22.72600   13.48700  -15.67200 1.000 87.61503  ?  1233 ALA   B CB  1 
ATOM   23785 N  N   . THR   B 1 1236 ? 23.73300   10.97700  -14.10400 1.000 88.19437  ?  1234 THR   B N   1 
ATOM   23786 C  CA  . THR   B 1 1236 ? 24.74900   9.95500   -13.85500 1.000 96.52303  ?  1234 THR   B CA  1 
ATOM   23787 C  C   . THR   B 1 1236 ? 24.40500   9.22500   -12.56200 1.000 100.94140 ?  1234 THR   B C   1 
ATOM   23788 O  O   . THR   B 1 1236 ? 25.02800   9.46400   -11.51600 1.000 99.68806  ?  1234 THR   B O   1 
ATOM   23789 C  CB  . THR   B 1 1236 ? 26.14700   10.56700  -13.78400 1.000 95.61232  ?  1234 THR   B CB  1 
ATOM   23790 O  OG1 . THR   B 1 1236 ? 26.13800   11.67900  -12.88000 1.000 106.83366 ?  1234 THR   B OG1 1 
ATOM   23791 C  CG2 . THR   B 1 1236 ? 26.59300   11.04000  -15.16000 1.000 96.04402  ?  1234 THR   B CG2 1 
ATOM   23792 N  N   . PRO   B 1 1237 ? 23.42100   8.32000   -12.59400 1.000 99.04893  ?  1235 PRO   B N   1 
ATOM   23793 C  CA  . PRO   B 1 1237 ? 23.05000   7.60200   -11.36400 1.000 88.61657  ?  1235 PRO   B CA  1 
ATOM   23794 C  C   . PRO   B 1 1237 ? 24.07300   6.56800   -10.93700 1.000 82.87466  ?  1235 PRO   B C   1 
ATOM   23795 O  O   . PRO   B 1 1237 ? 24.09100   6.19300   -9.75900  1.000 87.07239  ?  1235 PRO   B O   1 
ATOM   23796 C  CB  . PRO   B 1 1237 ? 21.71100   6.93700   -11.72700 1.000 89.18614  ?  1235 PRO   B CB  1 
ATOM   23797 C  CG  . PRO   B 1 1237 ? 21.30100   7.53100   -13.05500 1.000 92.53619  ?  1235 PRO   B CG  1 
ATOM   23798 C  CD  . PRO   B 1 1237 ? 22.56800   7.93800   -13.72900 1.000 97.81933  ?  1235 PRO   B CD  1 
ATOM   23799 N  N   . ASP   B 1 1238 ? 24.92000   6.09600   -11.84900 1.000 82.94168  ?  1236 ASP   B N   1 
ATOM   23800 C  CA  . ASP   B 1 1238 ? 25.87700   5.03900   -11.55900 1.000 92.33253  ?  1236 ASP   B CA  1 
ATOM   23801 C  C   . ASP   B 1 1238 ? 27.27100   5.56700   -11.24700 1.000 98.02498  ?  1236 ASP   B C   1 
ATOM   23802 O  O   . ASP   B 1 1238 ? 28.19800   4.76900   -11.07600 1.000 91.72440  ?  1236 ASP   B O   1 
ATOM   23803 C  CB  . ASP   B 1 1238 ? 25.94000   4.05300   -12.72700 1.000 95.29638  ?  1236 ASP   B CB  1 
ATOM   23804 C  CG  . ASP   B 1 1238 ? 24.94700   2.91700   -12.58400 1.000 107.69346 ?  1236 ASP   B CG  1 
ATOM   23805 O  OD1 . ASP   B 1 1238 ? 23.78700   3.18000   -12.20000 1.000 103.96199 ?  1236 ASP   B OD1 1 
ATOM   23806 O  OD2 . ASP   B 1 1238 ? 25.32500   1.75900   -12.86300 1.000 116.19721 -1 1236 ASP   B OD2 1 
ATOM   23807 N  N   . LYS   B 1 1239 ? 27.44200   6.88100   -11.15800 1.000 97.05044  ?  1237 LYS   B N   1 
ATOM   23808 C  CA  . LYS   B 1 1239 ? 28.75000   7.43400   -10.84500 1.000 92.37978  ?  1237 LYS   B CA  1 
ATOM   23809 C  C   . LYS   B 1 1239 ? 28.99900   7.40000   -9.34200  1.000 86.95128  ?  1237 LYS   B C   1 
ATOM   23810 O  O   . LYS   B 1 1239 ? 28.08000   7.55100   -8.53300  1.000 85.94777  ?  1237 LYS   B O   1 
ATOM   23811 C  CB  . LYS   B 1 1239 ? 28.87500   8.86700   -11.36100 1.000 85.44764  ?  1237 LYS   B CB  1 
ATOM   23812 C  CG  . LYS   B 1 1239 ? 30.31500   9.29500   -11.55100 1.000 82.18205  ?  1237 LYS   B CG  1 
ATOM   23813 C  CD  . LYS   B 1 1239 ? 30.48000   10.79300  -11.45900 1.000 74.52335  ?  1237 LYS   B CD  1 
ATOM   23814 C  CE  . LYS   B 1 1239 ? 31.95000   11.16000  -11.50200 1.000 73.57405  ?  1237 LYS   B CE  1 
ATOM   23815 N  NZ  . LYS   B 1 1239 ? 32.71900   10.41400  -10.46800 1.000 68.97645  ?  1237 LYS   B NZ  1 
ATOM   23816 N  N   . THR   B 1 1240 ? 30.26300   7.20000   -8.97400  1.000 73.58710  ?  1238 THR   B N   1 
ATOM   23817 C  CA  . THR   B 1 1240 ? 30.64300   7.08300   -7.57200  1.000 71.00764  ?  1238 THR   B CA  1 
ATOM   23818 C  C   . THR   B 1 1240 ? 30.68800   8.45800   -6.91700  1.000 79.11815  ?  1238 THR   B C   1 
ATOM   23819 O  O   . THR   B 1 1240 ? 31.38100   9.36300   -7.39500  1.000 77.98058  ?  1238 THR   B O   1 
ATOM   23820 C  CB  . THR   B 1 1240 ? 32.00100   6.39400   -7.44500  1.000 70.52530  ?  1238 THR   B CB  1 
ATOM   23821 O  OG1 . THR   B 1 1240 ? 31.91200   5.06000   -7.96100  1.000 80.71593  ?  1238 THR   B OG1 1 
ATOM   23822 C  CG2 . THR   B 1 1240 ? 32.43700   6.34200   -5.98900  1.000 60.28942  ?  1238 THR   B CG2 1 
ATOM   23823 N  N   . ALA   B 1 1241 ? 29.95100   8.61200   -5.81900  1.000 75.26973  ?  1239 ALA   B N   1 
ATOM   23824 C  CA  . ALA   B 1 1241 ? 29.90100   9.85800   -5.06300  1.000 63.04440  ?  1239 ALA   B CA  1 
ATOM   23825 C  C   . ALA   B 1 1241 ? 30.63200   9.78400   -3.73500  1.000 66.22564  ?  1239 ALA   B C   1 
ATOM   23826 O  O   . ALA   B 1 1241 ? 31.33300   10.72900  -3.36800  1.000 71.52851  ?  1239 ALA   B O   1 
ATOM   23827 C  CB  . ALA   B 1 1241 ? 28.44500   10.26500  -4.80800  1.000 59.07276  ?  1239 ALA   B CB  1 
ATOM   23828 N  N   . LEU   B 1 1242 ? 30.48600   8.68600   -3.00200  1.000 58.39770  ?  1240 LEU   B N   1 
ATOM   23829 C  CA  . LEU   B 1 1242 ? 31.13700   8.51400   -1.71400  1.000 62.12219  ?  1240 LEU   B CA  1 
ATOM   23830 C  C   . LEU   B 1 1242 ? 32.02600   7.28100   -1.74400  1.000 56.21025  ?  1240 LEU   B C   1 
ATOM   23831 O  O   . LEU   B 1 1242 ? 31.68000   6.26700   -2.36200  1.000 63.67362  ?  1240 LEU   B O   1 
ATOM   23832 C  CB  . LEU   B 1 1242 ? 30.10900   8.39000   -0.58400  1.000 53.03751  ?  1240 LEU   B CB  1 
ATOM   23833 C  CG  . LEU   B 1 1242 ? 29.07500   9.51500   -0.48600  1.000 54.49322  ?  1240 LEU   B CG  1 
ATOM   23834 C  CD1 . LEU   B 1 1242 ? 28.13500   9.29000   0.68800   1.000 53.36728  ?  1240 LEU   B CD1 1 
ATOM   23835 C  CD2 . LEU   B 1 1242 ? 29.74500   10.88000  -0.38700  1.000 67.22310  ?  1240 LEU   B CD2 1 
ATOM   23836 N  N   . VAL   B 1 1243 ? 33.17500   7.37800   -1.08100  1.000 54.83893  ?  1241 VAL   B N   1 
ATOM   23837 C  CA  . VAL   B 1 1243 ? 34.08200   6.24500   -0.92800  1.000 47.47855  ?  1241 VAL   B CA  1 
ATOM   23838 C  C   . VAL   B 1 1243 ? 34.50100   6.12600   0.53500   1.000 58.80874  ?  1241 VAL   B C   1 
ATOM   23839 O  O   . VAL   B 1 1243 ? 35.43700   6.80400   0.97700   1.000 62.68041  ?  1241 VAL   B O   1 
ATOM   23840 C  CB  . VAL   B 1 1243 ? 35.31200   6.38700   -1.84200  1.000 49.49768  ?  1241 VAL   B CB  1 
ATOM   23841 C  CG1 . VAL   B 1 1243 ? 36.26500   5.22000   -1.64200  1.000 55.34244  ?  1241 VAL   B CG1 1 
ATOM   23842 C  CG2 . VAL   B 1 1243 ? 34.88600   6.48800   -3.30300  1.000 55.25736  ?  1241 VAL   B CG2 1 
ATOM   23843 N  N   . PHE   B 1 1244 ? 33.82500   5.27000   1.29300   1.000 56.45220  ?  1242 PHE   B N   1 
ATOM   23844 C  CA  . PHE   B 1 1244 ? 34.16200   5.03200   2.69100   1.000 57.39563  ?  1242 PHE   B CA  1 
ATOM   23845 C  C   . PHE   B 1 1244 ? 34.67300   3.60500   2.83900   1.000 70.88832  ?  1242 PHE   B C   1 
ATOM   23846 O  O   . PHE   B 1 1244 ? 33.96100   2.65200   2.50100   1.000 78.46197  ?  1242 PHE   B O   1 
ATOM   23847 C  CB  . PHE   B 1 1244 ? 32.96000   5.27800   3.60600   1.000 48.74584  ?  1242 PHE   B CB  1 
ATOM   23848 C  CG  . PHE   B 1 1244 ? 33.28300   5.14600   5.06500   1.000 51.69940  ?  1242 PHE   B CG  1 
ATOM   23849 C  CD1 . PHE   B 1 1244 ? 34.19700   5.99800   5.66000   1.000 59.41040  ?  1242 PHE   B CD1 1 
ATOM   23850 C  CD2 . PHE   B 1 1244 ? 32.68100   4.17100   5.84100   1.000 56.10388  ?  1242 PHE   B CD2 1 
ATOM   23851 C  CE1 . PHE   B 1 1244 ? 34.50700   5.88300   7.00200   1.000 62.20832  ?  1242 PHE   B CE1 1 
ATOM   23852 C  CE2 . PHE   B 1 1244 ? 32.98500   4.05100   7.18600   1.000 72.58030  ?  1242 PHE   B CE2 1 
ATOM   23853 C  CZ  . PHE   B 1 1244 ? 33.90000   4.90800   7.76600   1.000 62.20879  ?  1242 PHE   B CZ  1 
ATOM   23854 N  N   . ARG   B 1 1245 ? 35.90500   3.46400   3.33700   1.000 72.72135  ?  1243 ARG   B N   1 
ATOM   23855 C  CA  . ARG   B 1 1245 ? 36.55000   2.16400   3.47500   1.000 65.17531  ?  1243 ARG   B CA  1 
ATOM   23856 C  C   . ARG   B 1 1245 ? 36.51100   1.40200   2.15500   1.000 69.57600  ?  1243 ARG   B C   1 
ATOM   23857 O  O   . ARG   B 1 1245 ? 37.06200   1.86900   1.15300   1.000 73.89667  ?  1243 ARG   B O   1 
ATOM   23858 C  CB  . ARG   B 1 1245 ? 35.90100   1.36300   4.61000   1.000 47.56638  ?  1243 ARG   B CB  1 
ATOM   23859 C  CG  . ARG   B 1 1245 ? 36.16700   1.98000   5.98100   1.000 59.25732  ?  1243 ARG   B CG  1 
ATOM   23860 C  CD  . ARG   B 1 1245 ? 35.34300   1.36700   7.10600   1.000 66.86174  ?  1243 ARG   B CD  1 
ATOM   23861 N  NE  . ARG   B 1 1245 ? 36.18400   0.72800   8.11200   1.000 83.89989  ?  1243 ARG   B NE  1 
ATOM   23862 C  CZ  . ARG   B 1 1245 ? 36.13100   -0.56100  8.41800   1.000 96.77355  ?  1243 ARG   B CZ  1 
ATOM   23863 N  NH1 . ARG   B 1 1245 ? 35.25700   -1.37200  7.84400   1.000 89.42413  ?  1243 ARG   B NH1 1 
ATOM   23864 N  NH2 . ARG   B 1 1245 ? 36.96900   -1.04700  9.33000   1.000 82.85881  ?  1243 ARG   B NH2 1 
ATOM   23865 N  N   . GLU   B 1 1246 ? 35.85900   0.24200   2.13200   1.000 70.48744  ?  1244 GLU   B N   1 
ATOM   23866 C  CA  . GLU   B 1 1246 ? 35.74400   -0.54700  0.91300   1.000 69.63039  ?  1244 GLU   B CA  1 
ATOM   23867 C  C   . GLU   B 1 1246 ? 34.39400   -0.37800  0.22700   1.000 56.57159  ?  1244 GLU   B C   1 
ATOM   23868 O  O   . GLU   B 1 1246 ? 34.08700   -1.12900  -0.70500  1.000 52.09064  ?  1244 GLU   B O   1 
ATOM   23869 C  CB  . GLU   B 1 1246 ? 36.00500   -2.02500  1.21200   1.000 62.75301  ?  1244 GLU   B CB  1 
ATOM   23870 C  CG  . GLU   B 1 1246 ? 37.44800   -2.32300  1.58800   1.000 68.56474  ?  1244 GLU   B CG  1 
ATOM   23871 C  CD  . GLU   B 1 1246 ? 38.43500   -1.89700  0.51500   1.000 81.64700  ?  1244 GLU   B CD  1 
ATOM   23872 O  OE1 . GLU   B 1 1246 ? 38.18700   -2.18600  -0.67500  1.000 71.12053  ?  1244 GLU   B OE1 1 
ATOM   23873 O  OE2 . GLU   B 1 1246 ? 39.45700   -1.26700  0.86100   1.000 84.02262  -1 1244 GLU   B OE2 1 
ATOM   23874 N  N   . GLN   B 1 1247 ? 33.59200   0.59400   0.65100   1.000 58.46546  ?  1245 GLN   B N   1 
ATOM   23875 C  CA  . GLN   B 1 1247 ? 32.28800   0.85100   0.06000   1.000 56.83214  ?  1245 GLN   B CA  1 
ATOM   23876 C  C   . GLN   B 1 1247 ? 32.38200   1.98000   -0.95900  1.000 48.24268  ?  1245 GLN   B C   1 
ATOM   23877 O  O   . GLN   B 1 1247 ? 33.23900   2.86200   -0.86000  1.000 58.54581  ?  1245 GLN   B O   1 
ATOM   23878 C  CB  . GLN   B 1 1247 ? 31.26300   1.21600   1.13600   1.000 62.92640  ?  1245 GLN   B CB  1 
ATOM   23879 C  CG  . GLN   B 1 1247 ? 31.45300   0.48200   2.45300   1.000 85.64879  ?  1245 GLN   B CG  1 
ATOM   23880 C  CD  . GLN   B 1 1247 ? 30.49500   0.96200   3.52600   1.000 86.55284  ?  1245 GLN   B CD  1 
ATOM   23881 O  OE1 . GLN   B 1 1247 ? 29.45100   1.54000   3.22600   1.000 64.10475  ?  1245 GLN   B OE1 1 
ATOM   23882 N  NE2 . GLN   B 1 1247 ? 30.85000   0.73100   4.78500   1.000 71.35029  ?  1245 GLN   B NE2 1 
ATOM   23883 N  N   . ARG   B 1 1248 ? 31.48500   1.94500   -1.94400  1.000 48.94934  ?  1246 ARG   B N   1 
ATOM   23884 C  CA  . ARG   B 1 1248 ? 31.41500   2.97800   -2.97900  1.000 50.00646  ?  1246 ARG   B CA  1 
ATOM   23885 C  C   . ARG   B 1 1248 ? 29.94400   3.30700   -3.21300  1.000 57.48706  ?  1246 ARG   B C   1 
ATOM   23886 O  O   . ARG   B 1 1248 ? 29.25300   2.60100   -3.95400  1.000 67.83939  ?  1246 ARG   B O   1 
ATOM   23887 C  CB  . ARG   B 1 1248 ? 32.10000   2.52600   -4.26300  1.000 46.51832  ?  1246 ARG   B CB  1 
ATOM   23888 C  CG  . ARG   B 1 1248 ? 33.61800   2.52500   -4.18000  1.000 58.38732  ?  1246 ARG   B CG  1 
ATOM   23889 C  CD  . ARG   B 1 1248 ? 34.25300   2.03700   -5.47200  1.000 72.41625  ?  1246 ARG   B CD  1 
ATOM   23890 N  NE  . ARG   B 1 1248 ? 35.39500   2.85800   -5.85700  1.000 86.27903  ?  1246 ARG   B NE  1 
ATOM   23891 C  CZ  . ARG   B 1 1248 ? 35.40000   3.70300   -6.87900  1.000 83.04714  ?  1246 ARG   B CZ  1 
ATOM   23892 N  NH1 . ARG   B 1 1248 ? 34.34700   3.83900   -7.67000  1.000 72.45890  ?  1246 ARG   B NH1 1 
ATOM   23893 N  NH2 . ARG   B 1 1248 ? 36.49100   4.42500   -7.11900  1.000 90.05614  ?  1246 ARG   B NH2 1 
ATOM   23894 N  N   . VAL   B 1 1249 ? 29.47200   4.37600   -2.57900  1.000 51.41594  ?  1247 VAL   B N   1 
ATOM   23895 C  CA  . VAL   B 1 1249 ? 28.08900   4.81500   -2.73100  1.000 56.31710  ?  1247 VAL   B CA  1 
ATOM   23896 C  C   . VAL   B 1 1249 ? 27.97200   5.64800   -4.00000  1.000 56.33934  ?  1247 VAL   B C   1 
ATOM   23897 O  O   . VAL   B 1 1249 ? 28.80000   6.52900   -4.25700  1.000 59.02380  ?  1247 VAL   B O   1 
ATOM   23898 C  CB  . VAL   B 1 1249 ? 27.63300   5.61300   -1.49900  1.000 47.36491  ?  1247 VAL   B CB  1 
ATOM   23899 C  CG1 . VAL   B 1 1249 ? 26.15500   5.96400   -1.61000  1.000 51.61856  ?  1247 VAL   B CG1 1 
ATOM   23900 C  CG2 . VAL   B 1 1249 ? 27.91100   4.83100   -0.22400  1.000 35.20245  ?  1247 VAL   B CG2 1 
ATOM   23901 N  N   . THR   B 1 1250 ? 26.94400   5.37500   -4.79400  1.000 54.87328  ?  1248 THR   B N   1 
ATOM   23902 C  CA  . THR   B 1 1250 ? 26.74200   6.07400   -6.05300  1.000 71.38441  ?  1248 THR   B CA  1 
ATOM   23903 C  C   . THR   B 1 1250 ? 25.77000   7.23800   -5.87000  1.000 71.85567  ?  1248 THR   B C   1 
ATOM   23904 O  O   . THR   B 1 1250 ? 25.07300   7.35000   -4.85800  1.000 68.07225  ?  1248 THR   B O   1 
ATOM   23905 C  CB  . THR   B 1 1250 ? 26.23900   5.11100   -7.13400  1.000 77.60280  ?  1248 THR   B CB  1 
ATOM   23906 O  OG1 . THR   B 1 1250 ? 26.41800   5.70900   -8.42200  1.000 92.97915  ?  1248 THR   B OG1 1 
ATOM   23907 C  CG2 . THR   B 1 1250 ? 24.76900   4.80500   -6.94300  1.000 68.91508  ?  1248 THR   B CG2 1 
ATOM   23908 N  N   . TYR   B 1 1251 ? 25.74400   8.12000   -6.87500  1.000 65.60361  ?  1249 TYR   B N   1 
ATOM   23909 C  CA  . TYR   B 1 1251 ? 24.87300   9.29200   -6.82600  1.000 64.38027  ?  1249 TYR   B CA  1 
ATOM   23910 C  C   . TYR   B 1 1251 ? 23.42200   8.89400   -6.60100  1.000 73.74410  ?  1249 TYR   B C   1 
ATOM   23911 O  O   . TYR   B 1 1251 ? 22.71700   9.51500   -5.79700  1.000 71.48939  ?  1249 TYR   B O   1 
ATOM   23912 C  CB  . TYR   B 1 1251 ? 25.00400   10.09700  -8.11700  1.000 78.87158  ?  1249 TYR   B CB  1 
ATOM   23913 C  CG  . TYR   B 1 1251 ? 26.17700   11.04900  -8.14400  1.000 85.83517  ?  1249 TYR   B CG  1 
ATOM   23914 C  CD1 . TYR   B 1 1251 ? 27.47800   10.57700  -8.24300  1.000 79.29583  ?  1249 TYR   B CD1 1 
ATOM   23915 C  CD2 . TYR   B 1 1251 ? 25.98100   12.42200  -8.08300  1.000 80.63538  ?  1249 TYR   B CD2 1 
ATOM   23916 C  CE1 . TYR   B 1 1251 ? 28.55300   11.44400  -8.27100  1.000 75.42269  ?  1249 TYR   B CE1 1 
ATOM   23917 C  CE2 . TYR   B 1 1251 ? 27.04800   13.29800  -8.11200  1.000 81.10785  ?  1249 TYR   B CE2 1 
ATOM   23918 C  CZ  . TYR   B 1 1251 ? 28.33200   12.80400  -8.20600  1.000 82.07362  ?  1249 TYR   B CZ  1 
ATOM   23919 O  OH  . TYR   B 1 1251 ? 29.40000   13.67200  -8.23400  1.000 78.90106  ?  1249 TYR   B OH  1 
ATOM   23920 N  N   . ARG   B 1 1252 ? 22.96000   7.86100   -7.30500  1.000 82.04428  ?  1250 ARG   B N   1 
ATOM   23921 C  CA  . ARG   B 1 1252 ? 21.59700   7.38500   -7.10900  1.000 77.52021  ?  1250 ARG   B CA  1 
ATOM   23922 C  C   . ARG   B 1 1252 ? 21.40000   6.87200   -5.68800  1.000 75.78098  ?  1250 ARG   B C   1 
ATOM   23923 O  O   . ARG   B 1 1252 ? 20.49400   7.32000   -4.97500  1.000 67.45461  ?  1250 ARG   B O   1 
ATOM   23924 C  CB  . ARG   B 1 1252 ? 21.27200   6.29500   -8.13100  1.000 82.04225  ?  1250 ARG   B CB  1 
ATOM   23925 C  CG  . ARG   B 1 1252 ? 19.82800   5.83200   -8.08400  1.000 94.56098  ?  1250 ARG   B CG  1 
ATOM   23926 C  CD  . ARG   B 1 1252 ? 19.53900   4.70500   -9.06800  1.000 87.67465  ?  1250 ARG   B CD  1 
ATOM   23927 N  NE  . ARG   B 1 1252 ? 20.33000   3.50600   -8.81000  1.000 91.02989  ?  1250 ARG   B NE  1 
ATOM   23928 C  CZ  . ARG   B 1 1252 ? 20.02300   2.57700   -7.91400  1.000 92.53717  ?  1250 ARG   B CZ  1 
ATOM   23929 N  NH1 . ARG   B 1 1252 ? 18.96000   2.69100   -7.13400  1.000 86.55235  ?  1250 ARG   B NH1 1 
ATOM   23930 N  NH2 . ARG   B 1 1252 ? 20.80400   1.50700   -7.79400  1.000 92.71344  ?  1250 ARG   B NH2 1 
ATOM   23931 N  N   . GLU   B 1 1253 ? 22.25300   5.93600   -5.25600  1.000 67.57297  ?  1251 GLU   B N   1 
ATOM   23932 C  CA  . GLU   B 1 1253 ? 22.14000   5.37600   -3.91100  1.000 61.67963  ?  1251 GLU   B CA  1 
ATOM   23933 C  C   . GLU   B 1 1253 ? 22.17100   6.46500   -2.84900  1.000 74.33848  ?  1251 GLU   B C   1 
ATOM   23934 O  O   . GLU   B 1 1253 ? 21.39100   6.42700   -1.89000  1.000 77.56040  ?  1251 GLU   B O   1 
ATOM   23935 C  CB  . GLU   B 1 1253 ? 23.26000   4.36700   -3.66400  1.000 66.63564  ?  1251 GLU   B CB  1 
ATOM   23936 C  CG  . GLU   B 1 1253 ? 23.09200   3.05400   -4.40100  1.000 77.20651  ?  1251 GLU   B CG  1 
ATOM   23937 C  CD  . GLU   B 1 1253 ? 24.39700   2.29400   -4.52300  1.000 92.07365  ?  1251 GLU   B CD  1 
ATOM   23938 O  OE1 . GLU   B 1 1253 ? 25.36700   2.65900   -3.82500  1.000 69.91399  ?  1251 GLU   B OE1 1 
ATOM   23939 O  OE2 . GLU   B 1 1253 ? 24.45500   1.33800   -5.32400  1.000 105.94743 -1 1251 GLU   B OE2 1 
ATOM   23940 N  N   . LEU   B 1 1254 ? 23.07000   7.44000   -2.99700  1.000 72.66591  ?  1252 LEU   B N   1 
ATOM   23941 C  CA  . LEU   B 1 1254 ? 23.09100   8.56400   -2.06800  1.000 70.05627  ?  1252 LEU   B CA  1 
ATOM   23942 C  C   . LEU   B 1 1254 ? 21.74600   9.27900   -2.06400  1.000 74.77090  ?  1252 LEU   B C   1 
ATOM   23943 O  O   . LEU   B 1 1254 ? 21.05300   9.31600   -1.04100  1.000 69.54189  ?  1252 LEU   B O   1 
ATOM   23944 C  CB  . LEU   B 1 1254 ? 24.22500   9.52500   -2.43100  1.000 68.10731  ?  1252 LEU   B CB  1 
ATOM   23945 C  CG  . LEU   B 1 1254 ? 24.43700   10.70200  -1.47500  1.000 63.74706  ?  1252 LEU   B CG  1 
ATOM   23946 C  CD1 . LEU   B 1 1254 ? 24.42400   10.22700  -0.03400  1.000 42.44978  ?  1252 LEU   B CD1 1 
ATOM   23947 C  CD2 . LEU   B 1 1254 ? 25.74400   11.40900  -1.78300  1.000 63.28825  ?  1252 LEU   B CD2 1 
ATOM   23948 N  N   . ASN   B 1 1255 ? 21.34700   9.81600   -3.22200  1.000 65.93733  ?  1253 ASN   B N   1 
ATOM   23949 C  CA  . ASN   B 1 1255 ? 20.08800   10.54900  -3.33700  1.000 66.81300  ?  1253 ASN   B CA  1 
ATOM   23950 C  C   . ASN   B 1 1255 ? 18.92700   9.77600   -2.72000  1.000 72.82920  ?  1253 ASN   B C   1 
ATOM   23951 O  O   . ASN   B 1 1255 ? 18.15100   10.32700  -1.93100  1.000 73.20812  ?  1253 ASN   B O   1 
ATOM   23952 C  CB  . ASN   B 1 1255 ? 19.81000   10.86000  -4.80800  1.000 55.21543  ?  1253 ASN   B CB  1 
ATOM   23953 C  CG  . ASN   B 1 1255 ? 18.69800   11.87400  -4.99500  1.000 77.03991  ?  1253 ASN   B CG  1 
ATOM   23954 O  OD1 . ASN   B 1 1255 ? 17.62700   11.76600  -4.39800  1.000 78.59023  ?  1253 ASN   B OD1 1 
ATOM   23955 N  ND2 . ASN   B 1 1255 ? 18.95200   12.87300  -5.82900  1.000 80.23291  ?  1253 ASN   B ND2 1 
ATOM   23956 N  N   . GLU   B 1 1256 ? 18.80300   8.49000   -3.05700  1.000 66.32125  ?  1254 GLU   B N   1 
ATOM   23957 C  CA  . GLU   B 1 1256 ? 17.71500   7.67900   -2.51500  1.000 76.60269  ?  1254 GLU   B CA  1 
ATOM   23958 C  C   . GLU   B 1 1256 ? 17.77400   7.61900   -0.99300  1.000 76.36550  ?  1254 GLU   B C   1 
ATOM   23959 O  O   . GLU   B 1 1256 ? 16.78300   7.90400   -0.31000  1.000 69.54327  ?  1254 GLU   B O   1 
ATOM   23960 C  CB  . GLU   B 1 1256 ? 17.76600   6.27100   -3.10800  1.000 83.81836  ?  1254 GLU   B CB  1 
ATOM   23961 C  CG  . GLU   B 1 1256 ? 17.61400   6.21600   -4.61800  1.000 95.33767  ?  1254 GLU   B CG  1 
ATOM   23962 C  CD  . GLU   B 1 1256 ? 17.63500   4.79500   -5.14300  1.000 106.32083 ?  1254 GLU   B CD  1 
ATOM   23963 O  OE1 . GLU   B 1 1256 ? 17.71000   3.85900   -4.31900  1.000 112.73741 ?  1254 GLU   B OE1 1 
ATOM   23964 O  OE2 . GLU   B 1 1256 ? 17.57800   4.61300   -6.37900  1.000 96.20549  -1 1254 GLU   B OE2 1 
ATOM   23965 N  N   . ARG   B 1 1257 ? 18.93300   7.24600   -0.44300  1.000 65.77470  ?  1255 ARG   B N   1 
ATOM   23966 C  CA  . ARG   B 1 1257 ? 19.07000   7.15800   1.00700   1.000 62.23573  ?  1255 ARG   B CA  1 
ATOM   23967 C  C   . ARG   B 1 1257 ? 18.87200   8.51300   1.67100   1.000 68.59077  ?  1255 ARG   B C   1 
ATOM   23968 O  O   . ARG   B 1 1257 ? 18.36900   8.58300   2.79800   1.000 71.68810  ?  1255 ARG   B O   1 
ATOM   23969 C  CB  . ARG   B 1 1257 ? 20.43700   6.57100   1.36700   1.000 51.02820  ?  1255 ARG   B CB  1 
ATOM   23970 C  CG  . ARG   B 1 1257 ? 20.58700   5.11400   0.95100   1.000 72.76241  ?  1255 ARG   B CG  1 
ATOM   23971 C  CD  . ARG   B 1 1257 ? 22.03900   4.70000   0.75700   1.000 65.01556  ?  1255 ARG   B CD  1 
ATOM   23972 N  NE  . ARG   B 1 1257 ? 22.69600   4.33200   2.00500   1.000 87.27340  ?  1255 ARG   B NE  1 
ATOM   23973 C  CZ  . ARG   B 1 1257 ? 23.82300   3.63700   2.07800   1.000 75.16921  ?  1255 ARG   B CZ  1 
ATOM   23974 N  NH1 . ARG   B 1 1257 ? 24.43700   3.20200   0.98900   1.000 64.13677  ?  1255 ARG   B NH1 1 
ATOM   23975 N  NH2 . ARG   B 1 1257 ? 24.34400   3.36700   3.27200   1.000 46.16504  ?  1255 ARG   B NH2 1 
ATOM   23976 N  N   . VAL   B 1 1258 ? 19.24800   9.59700   0.98900   1.000 65.08508  ?  1256 VAL   B N   1 
ATOM   23977 C  CA  . VAL   B 1 1258 ? 18.97600   10.92700  1.52300   1.000 64.56935  ?  1256 VAL   B CA  1 
ATOM   23978 C  C   . VAL   B 1 1258 ? 17.48300   11.22200  1.47800   1.000 60.74167  ?  1256 VAL   B C   1 
ATOM   23979 O  O   . VAL   B 1 1258 ? 16.92600   11.81900  2.40700   1.000 66.39794  ?  1256 VAL   B O   1 
ATOM   23980 C  CB  . VAL   B 1 1258 ? 19.78400   11.99300  0.76200   1.000 58.46721  ?  1256 VAL   B CB  1 
ATOM   23981 C  CG1 . VAL   B 1 1258 ? 19.50600   13.35100  1.34900   1.000 61.70352  ?  1256 VAL   B CG1 1 
ATOM   23982 C  CG2 . VAL   B 1 1258 ? 21.26600   11.69900  0.85400   1.000 47.07310  ?  1256 VAL   B CG2 1 
ATOM   23983 N  N   . ASN   B 1 1259 ? 16.81200   10.80900  0.39900   1.000 59.95952  ?  1257 ASN   B N   1 
ATOM   23984 C  CA  . ASN   B 1 1259 ? 15.37600   11.04600  0.28500   1.000 68.46391  ?  1257 ASN   B CA  1 
ATOM   23985 C  C   . ASN   B 1 1259 ? 14.61100   10.34100  1.39600   1.000 59.23674  ?  1257 ASN   B C   1 
ATOM   23986 O  O   . ASN   B 1 1259 ? 13.65600   10.89800  1.95000   1.000 61.45881  ?  1257 ASN   B O   1 
ATOM   23987 C  CB  . ASN   B 1 1259 ? 14.87100   10.58400  -1.08200  1.000 60.10256  ?  1257 ASN   B CB  1 
ATOM   23988 C  CG  . ASN   B 1 1259 ? 15.46800   11.37900  -2.22400  1.000 68.53864  ?  1257 ASN   B CG  1 
ATOM   23989 O  OD1 . ASN   B 1 1259 ? 15.94600   12.49700  -2.03600  1.000 77.05932  ?  1257 ASN   B OD1 1 
ATOM   23990 N  ND2 . ASN   B 1 1259 ? 15.45000   10.80100  -3.41900  1.000 74.25500  ?  1257 ASN   B ND2 1 
ATOM   23991 N  N   . GLN   B 1 1260 ? 15.01900   9.11700   1.73700   1.000 57.94778  ?  1258 GLN   B N   1 
ATOM   23992 C  CA  . GLN   B 1 1260 ? 14.31700   8.35800   2.76800   1.000 60.65378  ?  1258 GLN   B CA  1 
ATOM   23993 C  C   . GLN   B 1 1260 ? 14.39000   9.06400   4.11600   1.000 65.07194  ?  1258 GLN   B C   1 
ATOM   23994 O  O   . GLN   B 1 1260 ? 13.37300   9.23400   4.79800   1.000 67.12295  ?  1258 GLN   B O   1 
ATOM   23995 C  CB  . GLN   B 1 1260 ? 14.90000   6.94800   2.86600   1.000 62.20189  ?  1258 GLN   B CB  1 
ATOM   23996 C  CG  . GLN   B 1 1260 ? 14.89100   6.18200   1.55600   1.000 61.97831  ?  1258 GLN   B CG  1 
ATOM   23997 C  CD  . GLN   B 1 1260 ? 15.55500   4.82600   1.67400   1.000 65.56769  ?  1258 GLN   B CD  1 
ATOM   23998 O  OE1 . GLN   B 1 1260 ? 16.07500   4.28800   0.69700   1.000 62.34711  ?  1258 GLN   B OE1 1 
ATOM   23999 N  NE2 . GLN   B 1 1260 ? 15.54000   4.26500   2.87700   1.000 68.71348  ?  1258 GLN   B NE2 1 
ATOM   24000 N  N   . LEU   B 1 1261 ? 15.59100   9.48400   4.51800   1.000 62.09879  ?  1259 LEU   B N   1 
ATOM   24001 C  CA  . LEU   B 1 1261 ? 15.72900   10.21700  5.77100   1.000 63.89094  ?  1259 LEU   B CA  1 
ATOM   24002 C  C   . LEU   B 1 1261 ? 15.07100   11.58900  5.68700   1.000 62.67581  ?  1259 LEU   B C   1 
ATOM   24003 O  O   . LEU   B 1 1261 ? 14.63200   12.12800  6.71000   1.000 52.01822  ?  1259 LEU   B O   1 
ATOM   24004 C  CB  . LEU   B 1 1261 ? 17.20700   10.34900  6.13800   1.000 52.09071  ?  1259 LEU   B CB  1 
ATOM   24005 C  CG  . LEU   B 1 1261 ? 17.54300   10.89800  7.52500   1.000 51.95012  ?  1259 LEU   B CG  1 
ATOM   24006 C  CD1 . LEU   B 1 1261 ? 16.90000   10.05100  8.61100   1.000 55.01167  ?  1259 LEU   B CD1 1 
ATOM   24007 C  CD2 . LEU   B 1 1261 ? 19.04900   10.96200  7.71700   1.000 55.59627  ?  1259 LEU   B CD2 1 
ATOM   24008 N  N   . ALA   B 1 1262 ? 14.97800   12.15800  4.48300   1.000 57.23197  ?  1260 ALA   B N   1 
ATOM   24009 C  CA  . ALA   B 1 1262 ? 14.34800   13.46500  4.32500   1.000 59.72715  ?  1260 ALA   B CA  1 
ATOM   24010 C  C   . ALA   B 1 1262 ? 12.84200   13.38100  4.54500   1.000 65.56661  ?  1260 ALA   B C   1 
ATOM   24011 O  O   . ALA   B 1 1262 ? 12.26500   14.20700  5.26100   1.000 65.67409  ?  1260 ALA   B O   1 
ATOM   24012 C  CB  . ALA   B 1 1262 ? 14.65900   14.03400  2.94100   1.000 52.53148  ?  1260 ALA   B CB  1 
ATOM   24013 N  N   . HIS   B 1 1263 ? 12.18800   12.39000  3.92800   1.000 61.37387  ?  1261 HIS   B N   1 
ATOM   24014 C  CA  . HIS   B 1 1263 ? 10.75200   12.21400  4.12900   1.000 50.24000  ?  1261 HIS   B CA  1 
ATOM   24015 C  C   . HIS   B 1 1263 ? 10.42200   11.98000  5.59600   1.000 55.98755  ?  1261 HIS   B C   1 
ATOM   24016 O  O   . HIS   B 1 1263 ? 9.35600    12.39400  6.06700   1.000 69.36573  ?  1261 HIS   B O   1 
ATOM   24017 C  CB  . HIS   B 1 1263 ? 10.23100   11.04900  3.28500   1.000 51.70828  ?  1261 HIS   B CB  1 
ATOM   24018 C  CG  . HIS   B 1 1263 ? 10.37800   11.25300  1.80900   1.000 55.55179  ?  1261 HIS   B CG  1 
ATOM   24019 N  ND1 . HIS   B 1 1263 ? 9.93300    12.38800  1.16500   1.000 71.82316  ?  1261 HIS   B ND1 1 
ATOM   24020 C  CD2 . HIS   B 1 1263 ? 10.90600   10.45900  0.84800   1.000 61.91729  ?  1261 HIS   B CD2 1 
ATOM   24021 C  CE1 . HIS   B 1 1263 ? 10.19000   12.28800  -0.12700  1.000 64.37589  ?  1261 HIS   B CE1 1 
ATOM   24022 N  NE2 . HIS   B 1 1263 ? 10.78100   11.12700  -0.34600  1.000 53.54888  ?  1261 HIS   B NE2 1 
ATOM   24023 N  N   . THR   B 1 1264 ? 11.31900   11.32100  6.33200   1.000 53.29674  ?  1262 THR   B N   1 
ATOM   24024 C  CA  . THR   B 1 1264 ? 11.09600   11.12200  7.75800   1.000 59.43782  ?  1262 THR   B CA  1 
ATOM   24025 C  C   . THR   B 1 1264 ? 11.21600   12.43500  8.52000   1.000 63.84739  ?  1262 THR   B C   1 
ATOM   24026 O  O   . THR   B 1 1264 ? 10.43900   12.69400  9.44700   1.000 62.02959  ?  1262 THR   B O   1 
ATOM   24027 C  CB  . THR   B 1 1264 ? 12.08400   10.09300  8.30800   1.000 65.02122  ?  1262 THR   B CB  1 
ATOM   24028 O  OG1 . THR   B 1 1264 ? 12.19900   9.00000   7.38800   1.000 66.15484  ?  1262 THR   B OG1 1 
ATOM   24029 C  CG2 . THR   B 1 1264 ? 11.60500   9.56500   9.65300   1.000 43.15478  ?  1262 THR   B CG2 1 
ATOM   24030 N  N   . LEU   B 1 1265 ? 12.17800   13.28000  8.13900   1.000 75.07910  ?  1263 LEU   B N   1 
ATOM   24031 C  CA  . LEU   B 1 1265 ? 12.36200   14.55400  8.82900   1.000 70.43095  ?  1263 LEU   B CA  1 
ATOM   24032 C  C   . LEU   B 1 1265 ? 11.18700   15.49400  8.58300   1.000 63.07281  ?  1263 LEU   B C   1 
ATOM   24033 O  O   . LEU   B 1 1265 ? 10.74300   16.19200  9.50200   1.000 57.60443  ?  1263 LEU   B O   1 
ATOM   24034 C  CB  . LEU   B 1 1265 ? 13.67400   15.20700  8.39300   1.000 63.34512  ?  1263 LEU   B CB  1 
ATOM   24035 C  CG  . LEU   B 1 1265 ? 14.95700   14.50700  8.84500   1.000 65.47363  ?  1263 LEU   B CG  1 
ATOM   24036 C  CD1 . LEU   B 1 1265 ? 16.18200   15.34000  8.49800   1.000 48.73093  ?  1263 LEU   B CD1 1 
ATOM   24037 C  CD2 . LEU   B 1 1265 ? 14.90700   14.20700  10.33600  1.000 61.83977  ?  1263 LEU   B CD2 1 
ATOM   24038 N  N   . ARG   B 1 1266 ? 10.67600   15.53100  7.34900   1.000 50.44446  ?  1264 ARG   B N   1 
ATOM   24039 C  CA  . ARG   B 1 1266 ? 9.48400    16.32500  7.06900   1.000 62.06519  ?  1264 ARG   B CA  1 
ATOM   24040 C  C   . ARG   B 1 1266 ? 8.29000    15.81300  7.86600   1.000 65.56372  ?  1264 ARG   B C   1 
ATOM   24041 O  O   . ARG   B 1 1266 ? 7.49700    16.60500  8.39000   1.000 68.56396  ?  1264 ARG   B O   1 
ATOM   24042 C  CB  . ARG   B 1 1266 ? 9.18600    16.30900  5.56900   1.000 50.30669  ?  1264 ARG   B CB  1 
ATOM   24043 C  CG  . ARG   B 1 1266 ? 10.33500   16.82500  4.71900   1.000 56.62333  ?  1264 ARG   B CG  1 
ATOM   24044 C  CD  . ARG   B 1 1266 ? 10.24700   16.34100  3.27800   1.000 61.08751  ?  1264 ARG   B CD  1 
ATOM   24045 N  NE  . ARG   B 1 1266 ? 9.33600    17.14200  2.47000   1.000 73.17013  ?  1264 ARG   B NE  1 
ATOM   24046 C  CZ  . ARG   B 1 1266 ? 9.67900    18.25700  1.83900   1.000 76.44467  ?  1264 ARG   B CZ  1 
ATOM   24047 N  NH1 . ARG   B 1 1266 ? 10.90300   18.75400  1.92600   1.000 55.06480  ?  1264 ARG   B NH1 1 
ATOM   24048 N  NH2 . ARG   B 1 1266 ? 8.77100    18.89100  1.10400   1.000 75.73826  ?  1264 ARG   B NH2 1 
ATOM   24049 N  N   . GLU   B 1 1267 ? 8.15400    14.48800  7.97500   1.000 59.99520  ?  1265 GLU   B N   1 
ATOM   24050 C  CA  . GLU   B 1 1267 ? 7.12300    13.90800  8.83000   1.000 61.99787  ?  1265 GLU   B CA  1 
ATOM   24051 C  C   . GLU   B 1 1267 ? 7.33200    14.28700  10.29200  1.000 69.54159  ?  1265 GLU   B C   1 
ATOM   24052 O  O   . GLU   B 1 1267 ? 6.36200    14.37900  11.05400  1.000 71.50437  ?  1265 GLU   B O   1 
ATOM   24053 C  CB  . GLU   B 1 1267 ? 7.11000    12.38500  8.66500   1.000 62.45697  ?  1265 GLU   B CB  1 
ATOM   24054 C  CG  . GLU   B 1 1267 ? 6.10900    11.64700  9.54600   1.000 81.99340  ?  1265 GLU   B CG  1 
ATOM   24055 C  CD  . GLU   B 1 1267 ? 4.73400    11.53000  8.91500   1.000 90.45071  ?  1265 GLU   B CD  1 
ATOM   24056 O  OE1 . GLU   B 1 1267 ? 4.63400    11.62300  7.67300   1.000 80.48938  ?  1265 GLU   B OE1 1 
ATOM   24057 O  OE2 . GLU   B 1 1267 ? 3.75200    11.33900  9.66300   1.000 86.03784  -1 1265 GLU   B OE2 1 
ATOM   24058 N  N   . LYS   B 1 1268 ? 8.58100    14.51500  10.70200  1.000 64.51602  ?  1266 LYS   B N   1 
ATOM   24059 C  CA  . LYS   B 1 1268 ? 8.87700    14.95100  12.06100  1.000 70.36859  ?  1266 LYS   B CA  1 
ATOM   24060 C  C   . LYS   B 1 1268 ? 8.65500    16.44300  12.26800  1.000 71.56180  ?  1266 LYS   B C   1 
ATOM   24061 O  O   . LYS   B 1 1268 ? 8.79800    16.92300  13.39800  1.000 58.40774  ?  1266 LYS   B O   1 
ATOM   24062 C  CB  . LYS   B 1 1268 ? 10.31800   14.58700  12.43400  1.000 71.95027  ?  1266 LYS   B CB  1 
ATOM   24063 C  CG  . LYS   B 1 1268 ? 10.57200   13.09200  12.53200  1.000 68.81211  ?  1266 LYS   B CG  1 
ATOM   24064 C  CD  . LYS   B 1 1268 ? 9.49900    12.41100  13.36500  1.000 86.69124  ?  1266 LYS   B CD  1 
ATOM   24065 C  CE  . LYS   B 1 1268 ? 9.51200    10.90700  13.16100  1.000 80.97854  ?  1266 LYS   B CE  1 
ATOM   24066 N  NZ  . LYS   B 1 1268 ? 8.13800    10.37600  12.93800  1.000 78.65069  ?  1266 LYS   B NZ  1 
ATOM   24067 N  N   . GLY   B 1 1269 ? 8.31500    17.18200  11.21900  1.000 67.25732  ?  1267 GLY   B N   1 
ATOM   24068 C  CA  . GLY   B 1 1269 ? 8.02000    18.59000  11.33100  1.000 66.84323  ?  1267 GLY   B CA  1 
ATOM   24069 C  C   . GLY   B 1 1269 ? 9.13300    19.53100  10.93300  1.000 72.60806  ?  1267 GLY   B C   1 
ATOM   24070 O  O   . GLY   B 1 1269 ? 9.26200    20.59800  11.54400  1.000 78.53730  ?  1267 GLY   B O   1 
ATOM   24071 N  N   . VAL   B 1 1270 ? 9.93800    19.17800  9.93600   1.000 71.58589  ?  1268 VAL   B N   1 
ATOM   24072 C  CA  . VAL   B 1 1270 ? 11.02700   20.03300  9.47800   1.000 64.93242  ?  1268 VAL   B CA  1 
ATOM   24073 C  C   . VAL   B 1 1270 ? 10.50200   20.95100  8.38300   1.000 69.45295  ?  1268 VAL   B C   1 
ATOM   24074 O  O   . VAL   B 1 1270 ? 10.03800   20.48900  7.33500   1.000 49.63275  ?  1268 VAL   B O   1 
ATOM   24075 C  CB  . VAL   B 1 1270 ? 12.22100   19.20500  8.98000   1.000 59.40387  ?  1268 VAL   B CB  1 
ATOM   24076 C  CG1 . VAL   B 1 1270 ? 13.11000   20.04700  8.07900   1.000 44.68910  ?  1268 VAL   B CG1 1 
ATOM   24077 C  CG2 . VAL   B 1 1270 ? 13.02100   18.69300  10.15100  1.000 54.86036  ?  1268 VAL   B CG2 1 
ATOM   24078 N  N   . GLN   B 1 1271 ? 10.56900   22.25000  8.63400   1.000 74.53537  ?  1269 GLN   B N   1 
ATOM   24079 C  CA  . GLN   B 1 1271 ? 10.23300   23.29600  7.68100   1.000 72.82211  ?  1269 GLN   B CA  1 
ATOM   24080 C  C   . GLN   B 1 1271 ? 11.41400   24.24500  7.59500   1.000 69.86587  ?  1269 GLN   B C   1 
ATOM   24081 O  O   . GLN   B 1 1271 ? 12.34100   24.16800  8.40800   1.000 70.12267  ?  1269 GLN   B O   1 
ATOM   24082 C  CB  . GLN   B 1 1271 ? 8.95900    24.04200  8.11800   1.000 79.69167  ?  1269 GLN   B CB  1 
ATOM   24083 C  CG  . GLN   B 1 1271 ? 7.75800    23.13600  8.35100   1.000 70.65893  ?  1269 GLN   B CG  1 
ATOM   24084 C  CD  . GLN   B 1 1271 ? 7.34100    23.08700  9.80900   1.000 93.18993  ?  1269 GLN   B CD  1 
ATOM   24085 O  OE1 . GLN   B 1 1271 ? 7.71200    23.95300  10.60200  1.000 86.35136  ?  1269 GLN   B OE1 1 
ATOM   24086 N  NE2 . GLN   B 1 1271 ? 6.56600    22.07000  10.17000  1.000 85.79878  ?  1269 GLN   B NE2 1 
ATOM   24087 N  N   . PRO   B 1 1272 ? 11.43600   25.13800  6.58600   1.000 58.39382  ?  1270 PRO   B N   1 
ATOM   24088 C  CA  . PRO   B 1 1272 ? 12.53600   26.10900  6.47000   1.000 58.13400  ?  1270 PRO   B CA  1 
ATOM   24089 C  C   . PRO   B 1 1272 ? 12.94400   26.77400  7.77900   1.000 66.03647  ?  1270 PRO   B C   1 
ATOM   24090 O  O   . PRO   B 1 1272 ? 12.09500   27.13300  8.60200   1.000 62.45633  ?  1270 PRO   B O   1 
ATOM   24091 C  CB  . PRO   B 1 1272 ? 11.97800   27.13900  5.48100   1.000 54.78161  ?  1270 PRO   B CB  1 
ATOM   24092 C  CG  . PRO   B 1 1272 ? 10.93900   26.39000  4.67100   1.000 76.57079  ?  1270 PRO   B CG  1 
ATOM   24093 C  CD  . PRO   B 1 1272 ? 10.65900   25.06400  5.33700   1.000 72.49668  ?  1270 PRO   B CD  1 
ATOM   24094 N  N   . ASP   B 1 1273 ? 14.25800   26.91700  7.97300   1.000 65.61076  ?  1271 ASP   B N   1 
ATOM   24095 C  CA  . ASP   B 1 1273 ? 14.90000   27.56200  9.11800   1.000 69.77835  ?  1271 ASP   B CA  1 
ATOM   24096 C  C   . ASP   B 1 1273 ? 14.74100   26.79000  10.42200  1.000 61.96035  ?  1271 ASP   B C   1 
ATOM   24097 O  O   . ASP   B 1 1273 ? 15.03100   27.33900  11.49300  1.000 42.75371  ?  1271 ASP   B O   1 
ATOM   24098 C  CB  . ASP   B 1 1273 ? 14.40600   29.00100  9.32000   1.000 84.57284  ?  1271 ASP   B CB  1 
ATOM   24099 C  CG  . ASP   B 1 1273 ? 14.96200   29.96000  8.28400   1.000 74.85976  ?  1271 ASP   B CG  1 
ATOM   24100 O  OD1 . ASP   B 1 1273 ? 15.77800   29.52500  7.44400   1.000 77.26316  ?  1271 ASP   B OD1 1 
ATOM   24101 O  OD2 . ASP   B 1 1273 ? 14.58300   31.15000  8.31100   1.000 60.64877  -1 1271 ASP   B OD2 1 
ATOM   24102 N  N   . ASP   B 1 1274 ? 14.30000   25.53500  10.37000  1.000 70.42813  ?  1272 ASP   B N   1 
ATOM   24103 C  CA  . ASP   B 1 1274 ? 14.26000   24.68300  11.55100  1.000 59.57414  ?  1272 ASP   B CA  1 
ATOM   24104 C  C   . ASP   B 1 1274 ? 15.60700   23.99000  11.71600  1.000 49.58236  ?  1272 ASP   B C   1 
ATOM   24105 O  O   . ASP   B 1 1274 ? 16.16500   23.46500  10.74700  1.000 49.15849  ?  1272 ASP   B O   1 
ATOM   24106 C  CB  . ASP   B 1 1274 ? 13.13600   23.65200  11.44500  1.000 55.91749  ?  1272 ASP   B CB  1 
ATOM   24107 C  CG  . ASP   B 1 1274 ? 11.75800   24.27900  11.54500  1.000 66.86242  ?  1272 ASP   B CG  1 
ATOM   24108 O  OD1 . ASP   B 1 1274 ? 11.67500   25.48100  11.87500  1.000 76.62452  ?  1272 ASP   B OD1 1 
ATOM   24109 O  OD2 . ASP   B 1 1274 ? 10.75900   23.57200  11.29400  1.000 74.01153  -1 1272 ASP   B OD2 1 
ATOM   24110 N  N   . LEU   B 1 1275 ? 16.12500   23.99200  12.94100  1.000 50.99467  ?  1273 LEU   B N   1 
ATOM   24111 C  CA  . LEU   B 1 1275 ? 17.44800   23.45300  13.21700  1.000 54.27623  ?  1273 LEU   B CA  1 
ATOM   24112 C  C   . LEU   B 1 1275 ? 17.37000   21.98400  13.61000  1.000 62.27671  ?  1273 LEU   B C   1 
ATOM   24113 O  O   . LEU   B 1 1275 ? 16.47800   21.57100  14.35700  1.000 57.58291  ?  1273 LEU   B O   1 
ATOM   24114 C  CB  . LEU   B 1 1275 ? 18.13400   24.25000  14.32600  1.000 42.88857  ?  1273 LEU   B CB  1 
ATOM   24115 C  CG  . LEU   B 1 1275 ? 18.38200   25.72200  14.00100  1.000 46.85693  ?  1273 LEU   B CG  1 
ATOM   24116 C  CD1 . LEU   B 1 1275 ? 19.21500   26.37400  15.09300  1.000 57.77533  ?  1273 LEU   B CD1 1 
ATOM   24117 C  CD2 . LEU   B 1 1275 ? 19.05000   25.86500  12.64000  1.000 54.01985  ?  1273 LEU   B CD2 1 
ATOM   24118 N  N   . VAL   B 1 1276 ? 18.32100   21.20300  13.10500  1.000 70.75167  ?  1274 VAL   B N   1 
ATOM   24119 C  CA  . VAL   B 1 1276 ? 18.40100   19.77000  13.35900  1.000 64.80895  ?  1274 VAL   B CA  1 
ATOM   24120 C  C   . VAL   B 1 1276 ? 19.82600   19.44700  13.78400  1.000 61.69950  ?  1274 VAL   B C   1 
ATOM   24121 O  O   . VAL   B 1 1276 ? 20.76800   19.64000  13.00600  1.000 57.99302  ?  1274 VAL   B O   1 
ATOM   24122 C  CB  . VAL   B 1 1276 ? 18.00600   18.94300  12.12500  1.000 56.11963  ?  1274 VAL   B CB  1 
ATOM   24123 C  CG1 . VAL   B 1 1276 ? 18.31300   17.48000  12.35800  1.000 65.15177  ?  1274 VAL   B CG1 1 
ATOM   24124 C  CG2 . VAL   B 1 1276 ? 16.53400   19.14000  11.80400  1.000 49.36443  ?  1274 VAL   B CG2 1 
ATOM   24125 N  N   . MET   B 1 1277 ? 19.98300   18.94900  15.00700  1.000 62.83575  ?  1275 MET   B N   1 
ATOM   24126 C  CA  . MET   B 1 1277 ? 21.30100   18.66300  15.55100  1.000 51.16957  ?  1275 MET   B CA  1 
ATOM   24127 C  C   . MET   B 1 1277 ? 21.80400   17.30500  15.07900  1.000 65.15205  ?  1275 MET   B C   1 
ATOM   24128 O  O   . MET   B 1 1277 ? 21.03300   16.35100  14.94800  1.000 68.21056  ?  1275 MET   B O   1 
ATOM   24129 C  CB  . MET   B 1 1277 ? 21.25900   18.70300  17.07600  1.000 42.35660  ?  1275 MET   B CB  1 
ATOM   24130 C  CG  . MET   B 1 1277 ? 20.69500   19.99400  17.62100  1.000 38.67488  ?  1275 MET   B CG  1 
ATOM   24131 S  SD  . MET   B 1 1277 ? 20.62600   19.99000  19.41500  1.000 73.00789  ?  1275 MET   B SD  1 
ATOM   24132 C  CE  . MET   B 1 1277 ? 22.21600   19.26400  19.80800  1.000 68.31431  ?  1275 MET   B CE  1 
ATOM   24133 N  N   . LEU   B 1 1278 ? 23.11100   17.22200  14.83300  1.000 58.56423  ?  1276 LEU   B N   1 
ATOM   24134 C  CA  . LEU   B 1 1278 ? 23.75100   16.00900  14.33900  1.000 47.45055  ?  1276 LEU   B CA  1 
ATOM   24135 C  C   . LEU   B 1 1278 ? 24.87400   15.61300  15.28600  1.000 54.80662  ?  1276 LEU   B C   1 
ATOM   24136 O  O   . LEU   B 1 1278 ? 25.78300   16.41000  15.54100  1.000 59.33398  ?  1276 LEU   B O   1 
ATOM   24137 C  CB  . LEU   B 1 1278 ? 24.30600   16.21200  12.92800  1.000 26.27749  ?  1276 LEU   B CB  1 
ATOM   24138 C  CG  . LEU   B 1 1278 ? 23.35200   16.64800  11.81800  1.000 36.29743  ?  1276 LEU   B CG  1 
ATOM   24139 C  CD1 . LEU   B 1 1278 ? 24.12400   16.79200  10.52800  1.000 41.85935  ?  1276 LEU   B CD1 1 
ATOM   24140 C  CD2 . LEU   B 1 1278 ? 22.22600   15.65200  11.64900  1.000 50.57806  ?  1276 LEU   B CD2 1 
ATOM   24141 N  N   . MET   B 1 1279 ? 24.81900   14.38200  15.79400  1.000 59.00796  ?  1277 MET   B N   1 
ATOM   24142 C  CA  . MET   B 1 1279 ? 25.87900   13.81500  16.63000  1.000 54.88652  ?  1277 MET   B CA  1 
ATOM   24143 C  C   . MET   B 1 1279 ? 26.31600   12.50500  15.97900  1.000 56.58345  ?  1277 MET   B C   1 
ATOM   24144 O  O   . MET   B 1 1279 ? 25.71100   11.45500  16.21100  1.000 59.47717  ?  1277 MET   B O   1 
ATOM   24145 C  CB  . MET   B 1 1279 ? 25.40500   13.61000  18.06700  1.000 52.48452  ?  1277 MET   B CB  1 
ATOM   24146 C  CG  . MET   B 1 1279 ? 25.04300   14.90000  18.78200  1.000 58.35238  ?  1277 MET   B CG  1 
ATOM   24147 S  SD  . MET   B 1 1279 ? 24.32700   14.62900  20.41400  1.000 89.97710  ?  1277 MET   B SD  1 
ATOM   24148 C  CE  . MET   B 1 1279 ? 25.74500   14.01000  21.31500  1.000 69.35434  ?  1277 MET   B CE  1 
ATOM   24149 N  N   . ALA   B 1 1280 ? 27.36700   12.57000  15.16300  1.000 61.13401  ?  1278 ALA   B N   1 
ATOM   24150 C  CA  . ALA   B 1 1280 ? 27.84800   11.39900  14.44700  1.000 50.27353  ?  1278 ALA   B CA  1 
ATOM   24151 C  C   . ALA   B 1 1280 ? 29.33100   11.55600  14.14900  1.000 58.37772  ?  1278 ALA   B C   1 
ATOM   24152 O  O   . ALA   B 1 1280 ? 29.86300   12.66900  14.10400  1.000 61.35783  ?  1278 ALA   B O   1 
ATOM   24153 C  CB  . ALA   B 1 1280 ? 27.06600   11.17500  13.14700  1.000 36.90203  ?  1278 ALA   B CB  1 
ATOM   24154 N  N   . GLU   B 1 1281 ? 29.99300   10.42200  13.94700  1.000 56.10786  ?  1279 GLU   B N   1 
ATOM   24155 C  CA  . GLU   B 1 1281 ? 31.38600   10.40300  13.53300  1.000 45.47623  ?  1279 GLU   B CA  1 
ATOM   24156 C  C   . GLU   B 1 1281 ? 31.47300   10.30800  12.01100  1.000 52.86010  ?  1279 GLU   B C   1 
ATOM   24157 O  O   . GLU   B 1 1281 ? 30.46800   10.14100  11.31600  1.000 54.36937  ?  1279 GLU   B O   1 
ATOM   24158 C  CB  . GLU   B 1 1281 ? 32.12700   9.24100   14.19400  1.000 41.05992  ?  1279 GLU   B CB  1 
ATOM   24159 C  CG  . GLU   B 1 1281 ? 31.85200   9.10400   15.68500  1.000 60.90539  ?  1279 GLU   B CG  1 
ATOM   24160 C  CD  . GLU   B 1 1281 ? 32.76700   8.09800   16.35800  1.000 73.30057  ?  1279 GLU   B CD  1 
ATOM   24161 O  OE1 . GLU   B 1 1281 ? 33.99600   8.17800   16.14800  1.000 74.61289  ?  1279 GLU   B OE1 1 
ATOM   24162 O  OE2 . GLU   B 1 1281 ? 32.25800   7.22500   17.09200  1.000 78.45787  -1 1279 GLU   B OE2 1 
ATOM   24163 N  N   . ARG   B 1 1282 ? 32.69500   10.42600  11.49300  1.000 41.90108  ?  1280 ARG   B N   1 
ATOM   24164 C  CA  . ARG   B 1 1282 ? 32.89400   10.40100  10.04900  1.000 39.98806  ?  1280 ARG   B CA  1 
ATOM   24165 C  C   . ARG   B 1 1282 ? 32.43400   9.06300   9.48400   1.000 53.65910  ?  1280 ARG   B C   1 
ATOM   24166 O  O   . ARG   B 1 1282 ? 32.95600   8.00700   9.85500   1.000 58.62495  ?  1280 ARG   B O   1 
ATOM   24167 C  CB  . ARG   B 1 1282 ? 34.36200   10.66100  9.71100   1.000 47.09410  ?  1280 ARG   B CB  1 
ATOM   24168 C  CG  . ARG   B 1 1282 ? 34.54300   11.56200  8.49800   1.000 65.59722  ?  1280 ARG   B CG  1 
ATOM   24169 C  CD  . ARG   B 1 1282 ? 36.00500   11.81000  8.15400   1.000 61.56437  ?  1280 ARG   B CD  1 
ATOM   24170 N  NE  . ARG   B 1 1282 ? 36.66400   12.68900  9.11300   1.000 66.41353  ?  1280 ARG   B NE  1 
ATOM   24171 C  CZ  . ARG   B 1 1282 ? 37.57600   12.29200  9.99000   1.000 73.13444  ?  1280 ARG   B CZ  1 
ATOM   24172 N  NH1 . ARG   B 1 1282 ? 37.97500   11.03200  10.04900  1.000 68.73588  ?  1280 ARG   B NH1 1 
ATOM   24173 N  NH2 . ARG   B 1 1282 ? 38.10400   13.18200  10.82400  1.000 85.24568  ?  1280 ARG   B NH2 1 
ATOM   24174 N  N   . SER   B 1 1283 ? 31.44900   9.10800   8.59900   1.000 43.93475  ?  1281 SER   B N   1 
ATOM   24175 C  CA  . SER   B 1 1283 ? 30.78400   7.90400   8.11000   1.000 51.81615  ?  1281 SER   B CA  1 
ATOM   24176 C  C   . SER   B 1 1283 ? 29.96400   8.28300   6.88300   1.000 54.57197  ?  1281 SER   B C   1 
ATOM   24177 O  O   . SER   B 1 1283 ? 30.03700   9.41700   6.39200   1.000 66.23979  ?  1281 SER   B O   1 
ATOM   24178 C  CB  . SER   B 1 1283 ? 29.90900   7.28400   9.20100   1.000 62.82340  ?  1281 SER   B CB  1 
ATOM   24179 O  OG  . SER   B 1 1283 ? 28.98500   8.23500   9.70300   1.000 46.99528  ?  1281 SER   B OG  1 
ATOM   24180 N  N   . VAL   B 1 1284 ? 29.18100   7.32700   6.38300   1.000 52.83180  ?  1282 VAL   B N   1 
ATOM   24181 C  CA  . VAL   B 1 1284 ? 28.20900   7.64100   5.34400   1.000 50.67457  ?  1282 VAL   B CA  1 
ATOM   24182 C  C   . VAL   B 1 1284 ? 26.93700   8.20800   5.96300   1.000 49.95494  ?  1282 VAL   B C   1 
ATOM   24183 O  O   . VAL   B 1 1284 ? 26.23600   9.00700   5.33100   1.000 56.66496  ?  1282 VAL   B O   1 
ATOM   24184 C  CB  . VAL   B 1 1284 ? 27.91700   6.39400   4.49000   1.000 55.35280  ?  1282 VAL   B CB  1 
ATOM   24185 C  CG1 . VAL   B 1 1284 ? 27.05500   6.75300   3.28600   1.000 57.80431  ?  1282 VAL   B CG1 1 
ATOM   24186 C  CG2 . VAL   B 1 1284 ? 29.21800   5.74400   4.04400   1.000 64.62904  ?  1282 VAL   B CG2 1 
ATOM   24187 N  N   . GLU   B 1 1285 ? 26.62700   7.82100   7.20400   1.000 55.61886  ?  1283 GLU   B N   1 
ATOM   24188 C  CA  . GLU   B 1 1285 ? 25.44800   8.35600   7.87600   1.000 54.35584  ?  1283 GLU   B CA  1 
ATOM   24189 C  C   . GLU   B 1 1285 ? 25.57000   9.86000   8.08700   1.000 58.78929  ?  1283 GLU   B C   1 
ATOM   24190 O  O   . GLU   B 1 1285 ? 24.58200   10.59300  7.96100   1.000 66.28709  ?  1283 GLU   B O   1 
ATOM   24191 C  CB  . GLU   B 1 1285 ? 25.23200   7.64600   9.21400   1.000 46.85694  ?  1283 GLU   B CB  1 
ATOM   24192 C  CG  . GLU   B 1 1285 ? 25.22900   6.12700   9.12200   1.000 57.28606  ?  1283 GLU   B CG  1 
ATOM   24193 C  CD  . GLU   B 1 1285 ? 26.59900   5.52100   9.37000   1.000 55.94488  ?  1283 GLU   B CD  1 
ATOM   24194 O  OE1 . GLU   B 1 1285 ? 27.01400   5.44600   10.54600  1.000 47.82418  ?  1283 GLU   B OE1 1 
ATOM   24195 O  OE2 . GLU   B 1 1285 ? 27.26300   5.12600   8.38900   1.000 72.36086  -1 1283 GLU   B OE2 1 
ATOM   24196 N  N   . MET   B 1 1286 ? 26.77500   10.33800  8.40800   1.000 53.34579  ?  1284 MET   B N   1 
ATOM   24197 C  CA  . MET   B 1 1286 ? 26.97300   11.77300  8.58600   1.000 49.24391  ?  1284 MET   B CA  1 
ATOM   24198 C  C   . MET   B 1 1286 ? 26.70900   12.52700  7.28800   1.000 48.54125  ?  1284 MET   B C   1 
ATOM   24199 O  O   . MET   B 1 1286 ? 26.12000   13.61400  7.30100   1.000 58.23942  ?  1284 MET   B O   1 
ATOM   24200 C  CB  . MET   B 1 1286 ? 28.38800   12.05600  9.09100   1.000 40.57291  ?  1284 MET   B CB  1 
ATOM   24201 C  CG  . MET   B 1 1286 ? 28.62700   13.51800  9.44200   1.000 58.50467  ?  1284 MET   B CG  1 
ATOM   24202 S  SD  . MET   B 1 1286 ? 30.33800   14.04900  9.22300   1.000 43.41029  ?  1284 MET   B SD  1 
ATOM   24203 C  CE  . MET   B 1 1286 ? 31.09400   13.45000  10.72900  1.000 39.99027  ?  1284 MET   B CE  1 
ATOM   24204 N  N   . MET   B 1 1287 ? 27.13200   11.96200  6.15600   1.000 46.62946  ?  1285 MET   B N   1 
ATOM   24205 C  CA  . MET   B 1 1287 ? 26.89000   12.60900  4.87100   1.000 54.50747  ?  1285 MET   B CA  1 
ATOM   24206 C  C   . MET   B 1 1287 ? 25.41700   12.54100  4.48800   1.000 61.48126  ?  1285 MET   B C   1 
ATOM   24207 O  O   . MET   B 1 1287 ? 24.83700   13.53500  4.03400   1.000 66.63234  ?  1285 MET   B O   1 
ATOM   24208 C  CB  . MET   B 1 1287 ? 27.76000   11.96800  3.78900   1.000 44.45150  ?  1285 MET   B CB  1 
ATOM   24209 C  CG  . MET   B 1 1287 ? 29.23200   12.32200  3.89500   1.000 56.85182  ?  1285 MET   B CG  1 
ATOM   24210 S  SD  . MET   B 1 1287 ? 29.54300   14.07300  3.58600   1.000 50.99969  ?  1285 MET   B SD  1 
ATOM   24211 C  CE  . MET   B 1 1287 ? 29.17700   14.18900  1.83200   1.000 44.28898  ?  1285 MET   B CE  1 
ATOM   24212 N  N   . VAL   B 1 1288 ? 24.79400   11.37300  4.66200   1.000 60.64985  ?  1286 VAL   B N   1 
ATOM   24213 C  CA  . VAL   B 1 1288 ? 23.38400   11.22400  4.31400   1.000 61.86870  ?  1286 VAL   B CA  1 
ATOM   24214 C  C   . VAL   B 1 1288 ? 22.52300   12.13800  5.17600   1.000 59.22316  ?  1286 VAL   B C   1 
ATOM   24215 O  O   . VAL   B 1 1288 ? 21.57300   12.76300  4.68700   1.000 65.42917  ?  1286 VAL   B O   1 
ATOM   24216 C  CB  . VAL   B 1 1288 ? 22.95400   9.75000   4.43800   1.000 59.08184  ?  1286 VAL   B CB  1 
ATOM   24217 C  CG1 . VAL   B 1 1288 ? 21.44400   9.61700   4.29200   1.000 62.19909  ?  1286 VAL   B CG1 1 
ATOM   24218 C  CG2 . VAL   B 1 1288 ? 23.66200   8.90400   3.39300   1.000 47.18310  ?  1286 VAL   B CG2 1 
ATOM   24219 N  N   . ALA   B 1 1289 ? 22.84900   12.24400  6.46600   1.000 42.39668  ?  1287 ALA   B N   1 
ATOM   24220 C  CA  . ALA   B 1 1289 ? 22.07400   13.09900  7.36100   1.000 50.78812  ?  1287 ALA   B CA  1 
ATOM   24221 C  C   . ALA   B 1 1289 ? 22.12700   14.55500  6.91500   1.000 55.68816  ?  1287 ALA   B C   1 
ATOM   24222 O  O   . ALA   B 1 1289 ? 21.08900   15.21600  6.79300   1.000 50.88975  ?  1287 ALA   B O   1 
ATOM   24223 C  CB  . ALA   B 1 1289 ? 22.58300   12.95800  8.79500   1.000 47.48952  ?  1287 ALA   B CB  1 
ATOM   24224 N  N   . ILE   B 1 1290 ? 23.33400   15.06600  6.65600   1.000 47.72305  ?  1288 ILE   B N   1 
ATOM   24225 C  CA  . ILE   B 1 1290 ? 23.50400   16.47500  6.30300   1.000 42.62501  ?  1288 ILE   B CA  1 
ATOM   24226 C  C   . ILE   B 1 1290 ? 22.63500   16.83900  5.10500   1.000 45.48812  ?  1288 ILE   B C   1 
ATOM   24227 O  O   . ILE   B 1 1290 ? 21.87400   17.81300  5.14000   1.000 53.17017  ?  1288 ILE   B O   1 
ATOM   24228 C  CB  . ILE   B 1 1290 ? 24.98900   16.78200  6.04100   1.000 45.33674  ?  1288 ILE   B CB  1 
ATOM   24229 C  CG1 . ILE   B 1 1290 ? 25.71500   16.99900  7.36500   1.000 40.85520  ?  1288 ILE   B CG1 1 
ATOM   24230 C  CG2 . ILE   B 1 1290 ? 25.14400   17.99600  5.14200   1.000 53.63118  ?  1288 ILE   B CG2 1 
ATOM   24231 C  CD1 . ILE   B 1 1290 ? 27.20500   17.02200  7.23300   1.000 42.68476  ?  1288 ILE   B CD1 1 
ATOM   24232 N  N   . PHE   B 1 1291 ? 22.72800   16.05300  4.03000   1.000 42.93598  ?  1289 PHE   B N   1 
ATOM   24233 C  CA  . PHE   B 1 1291 ? 21.88900   16.31100  2.86400   1.000 42.33429  ?  1289 PHE   B CA  1 
ATOM   24234 C  C   . PHE   B 1 1291 ? 20.41400   16.07500  3.16800   1.000 57.52443  ?  1289 PHE   B C   1 
ATOM   24235 O  O   . PHE   B 1 1291 ? 19.54900   16.67200  2.51700   1.000 55.02865  ?  1289 PHE   B O   1 
ATOM   24236 C  CB  . PHE   B 1 1291 ? 22.32900   15.43700  1.68900   1.000 52.13653  ?  1289 PHE   B CB  1 
ATOM   24237 C  CG  . PHE   B 1 1291 ? 23.53800   15.95100  0.96300   1.000 56.10997  ?  1289 PHE   B CG  1 
ATOM   24238 C  CD1 . PHE   B 1 1291 ? 23.40400   16.85600  -0.07800  1.000 56.09684  ?  1289 PHE   B CD1 1 
ATOM   24239 C  CD2 . PHE   B 1 1291 ? 24.80700   15.51800  1.30800   1.000 52.57598  ?  1289 PHE   B CD2 1 
ATOM   24240 C  CE1 . PHE   B 1 1291 ? 24.51300   17.32500  -0.75500  1.000 62.99058  ?  1289 PHE   B CE1 1 
ATOM   24241 C  CE2 . PHE   B 1 1291 ? 25.92100   15.98300  0.63400   1.000 63.51696  ?  1289 PHE   B CE2 1 
ATOM   24242 C  CZ  . PHE   B 1 1291 ? 25.77300   16.88800  -0.39900  1.000 70.94299  ?  1289 PHE   B CZ  1 
ATOM   24243 N  N   . ALA   B 1 1292 ? 20.10800   15.21400  4.14200   1.000 64.31235  ?  1290 ALA   B N   1 
ATOM   24244 C  CA  . ALA   B 1 1292 ? 18.71200   14.93400  4.46800   1.000 55.74210  ?  1290 ALA   B CA  1 
ATOM   24245 C  C   . ALA   B 1 1292 ? 18.06200   16.10900  5.18600   1.000 62.16380  ?  1290 ALA   B C   1 
ATOM   24246 O  O   . ALA   B 1 1292 ? 16.88800   16.41400  4.94800   1.000 64.81864  ?  1290 ALA   B O   1 
ATOM   24247 C  CB  . ALA   B 1 1292 ? 18.61000   13.66700  5.31300   1.000 51.02705  ?  1290 ALA   B CB  1 
ATOM   24248 N  N   . VAL   B 1 1293 ? 18.80200   16.77400  6.07700   1.000 52.52728  ?  1291 VAL   B N   1 
ATOM   24249 C  CA  . VAL   B 1 1293 ? 18.28100   17.98300  6.71000   1.000 49.80105  ?  1291 VAL   B CA  1 
ATOM   24250 C  C   . VAL   B 1 1293 ? 18.02200   19.05400  5.66000   1.000 58.11693  ?  1291 VAL   B C   1 
ATOM   24251 O  O   . VAL   B 1 1293 ? 17.05800   19.82400  5.75800   1.000 62.34837  ?  1291 VAL   B O   1 
ATOM   24252 C  CB  . VAL   B 1 1293 ? 19.25000   18.48200  7.79800   1.000 49.12673  ?  1291 VAL   B CB  1 
ATOM   24253 C  CG1 . VAL   B 1 1293 ? 18.57300   19.53400  8.66500   1.000 58.02117  ?  1291 VAL   B CG1 1 
ATOM   24254 C  CG2 . VAL   B 1 1293 ? 19.74500   17.32300  8.64400   1.000 51.33862  ?  1291 VAL   B CG2 1 
ATOM   24255 N  N   . LEU   B 1 1294 ? 18.87100   19.11300  4.63300   1.000 48.15842  ?  1292 LEU   B N   1 
ATOM   24256 C  CA  . LEU   B 1 1294 ? 18.70600   20.11900  3.59200   1.000 56.91117  ?  1292 LEU   B CA  1 
ATOM   24257 C  C   . LEU   B 1 1294 ? 17.49400   19.81500  2.71900   1.000 53.16991  ?  1292 LEU   B C   1 
ATOM   24258 O  O   . LEU   B 1 1294 ? 16.64200   20.68400  2.50000   1.000 62.08954  ?  1292 LEU   B O   1 
ATOM   24259 C  CB  . LEU   B 1 1294 ? 19.97500   20.20900  2.74500   1.000 46.96643  ?  1292 LEU   B CB  1 
ATOM   24260 C  CG  . LEU   B 1 1294 ? 21.27000   20.57000  3.47500   1.000 44.90251  ?  1292 LEU   B CG  1 
ATOM   24261 C  CD1 . LEU   B 1 1294 ? 22.32300   21.03500  2.48100   1.000 45.54004  ?  1292 LEU   B CD1 1 
ATOM   24262 C  CD2 . LEU   B 1 1294 ? 21.02500   21.62400  4.54700   1.000 38.08628  ?  1292 LEU   B CD2 1 
ATOM   24263 N  N   . LYS   B 1 1295 ? 17.39800   18.58000  2.21400   1.000 55.76206  ?  1293 LYS   B N   1 
ATOM   24264 C  CA  . LYS   B 1 1295 ? 16.26900   18.21000  1.36500   1.000 61.44639  ?  1293 LYS   B CA  1 
ATOM   24265 C  C   . LYS   B 1 1295 ? 14.94600   18.35000  2.10600   1.000 59.05194  ?  1293 LYS   B C   1 
ATOM   24266 O  O   . LYS   B 1 1295 ? 13.93300   18.74300  1.51400   1.000 53.77990  ?  1293 LYS   B O   1 
ATOM   24267 C  CB  . LYS   B 1 1295 ? 16.43600   16.78100  0.85100   1.000 60.31573  ?  1293 LYS   B CB  1 
ATOM   24268 C  CG  . LYS   B 1 1295 ? 17.41700   16.63700  -0.29400  1.000 52.23698  ?  1293 LYS   B CG  1 
ATOM   24269 C  CD  . LYS   B 1 1295 ? 17.13300   15.37000  -1.07800  1.000 55.81775  ?  1293 LYS   B CD  1 
ATOM   24270 C  CE  . LYS   B 1 1295 ? 18.06000   15.23600  -2.26800  1.000 56.88022  ?  1293 LYS   B CE  1 
ATOM   24271 N  NZ  . LYS   B 1 1295 ? 17.63100   14.12600  -3.16000  1.000 70.29230  ?  1293 LYS   B NZ  1 
ATOM   24272 N  N   . ALA   B 1 1296 ? 14.93200   18.02500  3.39900   1.000 49.72689  ?  1294 ALA   B N   1 
ATOM   24273 C  CA  . ALA   B 1 1296 ? 13.72200   18.21400  4.19000   1.000 54.09604  ?  1294 ALA   B CA  1 
ATOM   24274 C  C   . ALA   B 1 1296 ? 13.36300   19.69100  4.29400   1.000 61.56169  ?  1294 ALA   B C   1 
ATOM   24275 O  O   . ALA   B 1 1296 ? 12.18200   20.05600  4.25100   1.000 61.36432  ?  1294 ALA   B O   1 
ATOM   24276 C  CB  . ALA   B 1 1296 ? 13.90000   17.60000  5.57800   1.000 54.14816  ?  1294 ALA   B CB  1 
ATOM   24277 N  N   . GLY   B 1 1297 ? 14.36800   20.55500  4.42500   1.000 63.07617  ?  1295 GLY   B N   1 
ATOM   24278 C  CA  . GLY   B 1 1297 ? 14.13600   21.98500  4.43400   1.000 56.72536  ?  1295 GLY   B CA  1 
ATOM   24279 C  C   . GLY   B 1 1297 ? 14.79700   22.72500  5.57800   1.000 61.49874  ?  1295 GLY   B C   1 
ATOM   24280 O  O   . GLY   B 1 1297 ? 14.70800   23.95300  5.65800   1.000 68.09304  ?  1295 GLY   B O   1 
ATOM   24281 N  N   . GLY   B 1 1298 ? 15.46900   21.99900  6.46500   1.000 55.58908  ?  1296 GLY   B N   1 
ATOM   24282 C  CA  . GLY   B 1 1298 ? 16.06300   22.57400  7.65000   1.000 51.62699  ?  1296 GLY   B CA  1 
ATOM   24283 C  C   . GLY   B 1 1298 ? 17.54100   22.87100  7.49100   1.000 57.62631  ?  1296 GLY   B C   1 
ATOM   24284 O  O   . GLY   B 1 1298 ? 18.08500   22.91400  6.38200   1.000 47.84782  ?  1296 GLY   B O   1 
ATOM   24285 N  N   . ALA   B 1 1299 ? 18.19700   23.09000  8.62800   1.000 46.42027  ?  1297 ALA   B N   1 
ATOM   24286 C  CA  . ALA   B 1 1299 ? 19.62700   23.34400  8.68600   1.000 49.50225  ?  1297 ALA   B CA  1 
ATOM   24287 C  C   . ALA   B 1 1299 ? 20.25600   22.39700  9.69500   1.000 58.81042  ?  1297 ALA   B C   1 
ATOM   24288 O  O   . ALA   B 1 1299 ? 19.64400   22.05500  10.71000  1.000 53.53561  ?  1297 ALA   B O   1 
ATOM   24289 C  CB  . ALA   B 1 1299 ? 19.92700   24.79900  9.07100   1.000 50.94221  ?  1297 ALA   B CB  1 
ATOM   24290 N  N   . TYR   B 1 1300 ? 21.48300   21.97000  9.41300   1.000 58.74029  ?  1298 TYR   B N   1 
ATOM   24291 C  CA  . TYR   B 1 1300 ? 22.16400   20.99700  10.25400  1.000 53.38268  ?  1298 TYR   B CA  1 
ATOM   24292 C  C   . TYR   B 1 1300 ? 23.10300   21.71300  11.21900  1.000 49.12644  ?  1298 TYR   B C   1 
ATOM   24293 O  O   . TYR   B 1 1300 ? 23.91500   22.54600  10.80700  1.000 62.91384  ?  1298 TYR   B O   1 
ATOM   24294 C  CB  . TYR   B 1 1300 ? 22.91100   19.95800  9.40700   1.000 49.90432  ?  1298 TYR   B CB  1 
ATOM   24295 C  CG  . TYR   B 1 1300 ? 24.32200   20.30000  8.95200   1.000 59.58974  ?  1298 TYR   B CG  1 
ATOM   24296 C  CD1 . TYR   B 1 1300 ? 25.42300   20.01800  9.75600   1.000 47.57756  ?  1298 TYR   B CD1 1 
ATOM   24297 C  CD2 . TYR   B 1 1300 ? 24.55600   20.85200  7.69800   1.000 48.86286  ?  1298 TYR   B CD2 1 
ATOM   24298 C  CE1 . TYR   B 1 1300 ? 26.71000   20.31000  9.34000   1.000 45.55104  ?  1298 TYR   B CE1 1 
ATOM   24299 C  CE2 . TYR   B 1 1300 ? 25.84200   21.14500  7.27200   1.000 42.95509  ?  1298 TYR   B CE2 1 
ATOM   24300 C  CZ  . TYR   B 1 1300 ? 26.91400   20.87200  8.09800   1.000 51.73490  ?  1298 TYR   B CZ  1 
ATOM   24301 O  OH  . TYR   B 1 1300 ? 28.19400   21.16100  7.68100   1.000 53.69923  ?  1298 TYR   B OH  1 
ATOM   24302 N  N   . LEU   B 1 1301 ? 22.96100   21.40100  12.50800  1.000 42.29865  ?  1299 LEU   B N   1 
ATOM   24303 C  CA  . LEU   B 1 1301 ? 23.81700   21.93700  13.56000  1.000 43.57587  ?  1299 LEU   B CA  1 
ATOM   24304 C  C   . LEU   B 1 1301 ? 24.79200   20.85700  14.00700  1.000 58.21888  ?  1299 LEU   B C   1 
ATOM   24305 O  O   . LEU   B 1 1301 ? 24.39900   19.92300  14.72400  1.000 68.50551  ?  1299 LEU   B O   1 
ATOM   24306 C  CB  . LEU   B 1 1301 ? 22.97500   22.43100  14.74200  1.000 48.38323  ?  1299 LEU   B CB  1 
ATOM   24307 C  CG  . LEU   B 1 1301 ? 23.65400   22.69600  16.08900  1.000 39.50024  ?  1299 LEU   B CG  1 
ATOM   24308 C  CD1 . LEU   B 1 1301 ? 24.82200   23.65300  15.95000  1.000 58.74303  ?  1299 LEU   B CD1 1 
ATOM   24309 C  CD2 . LEU   B 1 1301 ? 22.63700   23.23500  17.08000  1.000 52.58459  ?  1299 LEU   B CD2 1 
ATOM   24310 N  N   . PRO   B 1 1302 ? 26.06200   20.92800  13.60800  1.000 53.58861  ?  1300 PRO   B N   1 
ATOM   24311 C  CA  . PRO   B 1 1302 ? 27.02000   19.87400  13.97000  1.000 38.04559  ?  1300 PRO   B CA  1 
ATOM   24312 C  C   . PRO   B 1 1302 ? 27.49700   20.02300  15.40900  1.000 44.28902  ?  1300 PRO   B C   1 
ATOM   24313 O  O   . PRO   B 1 1302 ? 27.97400   21.08500  15.81700  1.000 58.16724  ?  1300 PRO   B O   1 
ATOM   24314 C  CB  . PRO   B 1 1302 ? 28.16600   20.08900  12.97600  1.000 39.79945  ?  1300 PRO   B CB  1 
ATOM   24315 C  CG  . PRO   B 1 1302 ? 28.09900   21.53600  12.65200  1.000 58.41238  ?  1300 PRO   B CG  1 
ATOM   24316 C  CD  . PRO   B 1 1302 ? 26.64900   21.92600  12.69700  1.000 58.07130  ?  1300 PRO   B CD  1 
ATOM   24317 N  N   . ILE   B 1 1303 ? 27.36700   18.94400  16.17500  1.000 48.12627  ?  1301 ILE   B N   1 
ATOM   24318 C  CA  . ILE   B 1 1303 ? 27.84700   18.87600  17.54800  1.000 58.48640  ?  1301 ILE   B CA  1 
ATOM   24319 C  C   . ILE   B 1 1303 ? 28.71500   17.63100  17.67600  1.000 55.79485  ?  1301 ILE   B C   1 
ATOM   24320 O  O   . ILE   B 1 1303 ? 28.32200   16.54800  17.22700  1.000 53.40624  ?  1301 ILE   B O   1 
ATOM   24321 C  CB  . ILE   B 1 1303 ? 26.68000   18.86000  18.55700  1.000 68.67142  ?  1301 ILE   B CB  1 
ATOM   24322 C  CG1 . ILE   B 1 1303 ? 26.99200   17.96100  19.75800  1.000 66.22318  ?  1301 ILE   B CG1 1 
ATOM   24323 C  CG2 . ILE   B 1 1303 ? 25.37100   18.46600  17.87700  1.000 56.25752  ?  1301 ILE   B CG2 1 
ATOM   24324 C  CD1 . ILE   B 1 1303 ? 27.67800   18.68600  20.89300  1.000 66.24539  ?  1301 ILE   B CD1 1 
ATOM   24325 N  N   . ASP   B 1 1304 ? 29.89900   17.79200  18.26300  1.000 62.04214  ?  1302 ASP   B N   1 
ATOM   24326 C  CA  . ASP   B 1 1304 ? 30.85100   16.69200  18.33400  1.000 59.14117  ?  1302 ASP   B CA  1 
ATOM   24327 C  C   . ASP   B 1 1304 ? 30.29000   15.56200  19.19100  1.000 67.31497  ?  1302 ASP   B C   1 
ATOM   24328 O  O   . ASP   B 1 1304 ? 29.80500   15.81600  20.30200  1.000 70.01394  ?  1302 ASP   B O   1 
ATOM   24329 C  CB  . ASP   B 1 1304 ? 32.18300   17.17200  18.90900  1.000 74.95488  ?  1302 ASP   B CB  1 
ATOM   24330 C  CG  . ASP   B 1 1304 ? 33.21600   16.06600  18.98700  1.000 77.61168  ?  1302 ASP   B CG  1 
ATOM   24331 O  OD1 . ASP   B 1 1304 ? 33.90700   15.81800  17.97700  1.000 86.16961  ?  1302 ASP   B OD1 1 
ATOM   24332 O  OD2 . ASP   B 1 1304 ? 33.33300   15.43600  20.05900  1.000 70.91339  -1 1302 ASP   B OD2 1 
ATOM   24333 N  N   . PRO   B 1 1305 ? 30.33800   14.31200  18.72200  1.000 75.58943  ?  1303 PRO   B N   1 
ATOM   24334 C  CA  . PRO   B 1 1305 ? 29.76400   13.21200  19.51400  1.000 67.45243  ?  1303 PRO   B CA  1 
ATOM   24335 C  C   . PRO   B 1 1305 ? 30.48200   12.96500  20.82900  1.000 68.62250  ?  1303 PRO   B C   1 
ATOM   24336 O  O   . PRO   B 1 1305 ? 29.83600   12.57400  21.80900  1.000 66.60392  ?  1303 PRO   B O   1 
ATOM   24337 C  CB  . PRO   B 1 1305 ? 29.88300   12.00800  18.56900  1.000 65.03423  ?  1303 PRO   B CB  1 
ATOM   24338 C  CG  . PRO   B 1 1305 ? 30.98100   12.36500  17.62600  1.000 69.62034  ?  1303 PRO   B CG  1 
ATOM   24339 C  CD  . PRO   B 1 1305 ? 30.88000   13.84900  17.43200  1.000 64.39579  ?  1303 PRO   B CD  1 
ATOM   24340 N  N   . HIS   B 1 1306 ? 31.79700   13.18100  20.88700  1.000 71.59744  ?  1304 HIS   B N   1 
ATOM   24341 C  CA  . HIS   B 1 1306 ? 32.58100   12.93100  22.09000  1.000 74.31606  ?  1304 HIS   B CA  1 
ATOM   24342 C  C   . HIS   B 1 1306 ? 32.88600   14.21000  22.86100  1.000 69.61960  ?  1304 HIS   B C   1 
ATOM   24343 O  O   . HIS   B 1 1306 ? 33.91600   14.29700  23.53900  1.000 64.18711  ?  1304 HIS   B O   1 
ATOM   24344 C  CB  . HIS   B 1 1306 ? 33.87800   12.20300  21.73500  1.000 70.18590  ?  1304 HIS   B CB  1 
ATOM   24345 C  CG  . HIS   B 1 1306 ? 33.72100   11.18400  20.65000  1.000 69.40984  ?  1304 HIS   B CG  1 
ATOM   24346 N  ND1 . HIS   B 1 1306 ? 33.07500   9.98200   20.84300  1.000 65.08276  ?  1304 HIS   B ND1 1 
ATOM   24347 C  CD2 . HIS   B 1 1306 ? 34.12900   11.18900  19.35900  1.000 68.53153  ?  1304 HIS   B CD2 1 
ATOM   24348 C  CE1 . HIS   B 1 1306 ? 33.09100   9.29100   19.71700  1.000 64.34338  ?  1304 HIS   B CE1 1 
ATOM   24349 N  NE2 . HIS   B 1 1306 ? 33.72500   10.00100  18.80200  1.000 59.28271  ?  1304 HIS   B NE2 1 
ATOM   24350 N  N   . SER   B 1 1307 ? 32.00200   15.22400  22.76300  1.000 68.18492  ?  1305 SER   B N   1 
ATOM   24351 C  CA  . SER   B 1 1307 ? 32.20000   16.43500  23.54200  1.000 69.64901  ?  1305 SER   B CA  1 
ATOM   24352 C  C   . SER   B 1 1307 ? 31.58200   16.27600  24.92700  1.000 81.65727  ?  1305 SER   B C   1 
ATOM   24353 O  O   . SER   B 1 1307 ? 30.63600   15.50100  25.10500  1.000 89.41017  ?  1305 SER   B O   1 
ATOM   24354 C  CB  . SER   B 1 1307 ? 31.57000   17.63400  22.83900  1.000 70.03700  ?  1305 SER   B CB  1 
ATOM   24355 O  OG  . SER   B 1 1307 ? 30.16100   17.62000  22.97900  1.000 77.20411  ?  1305 SER   B OG  1 
ATOM   24356 N  N   . PRO   B 1 1308 ? 32.10300   16.98700  25.92700  1.000 78.18111  ?  1306 PRO   B N   1 
ATOM   24357 C  CA  . PRO   B 1 1308 ? 31.51600   16.89900  27.26900  1.000 65.17661  ?  1306 PRO   B CA  1 
ATOM   24358 C  C   . PRO   B 1 1308 ? 30.05600   17.32400  27.26300  1.000 76.45304  ?  1306 PRO   B C   1 
ATOM   24359 O  O   . PRO   B 1 1308 ? 29.62800   18.15300  26.45500  1.000 77.37004  ?  1306 PRO   B O   1 
ATOM   24360 C  CB  . PRO   B 1 1308 ? 32.37800   17.85600  28.09900  1.000 69.68643  ?  1306 PRO   B CB  1 
ATOM   24361 C  CG  . PRO   B 1 1308 ? 33.67700   17.92200  27.36700  1.000 72.60442  ?  1306 PRO   B CG  1 
ATOM   24362 C  CD  . PRO   B 1 1308 ? 33.33700   17.79200  25.91200  1.000 79.97099  ?  1306 PRO   B CD  1 
ATOM   24363 N  N   . ALA   B 1 1309 ? 29.28900   16.73400  28.18400  1.000 82.46213  ?  1307 ALA   B N   1 
ATOM   24364 C  CA  . ALA   B 1 1309 ? 27.84700   16.95400  28.21200  1.000 77.50756  ?  1307 ALA   B CA  1 
ATOM   24365 C  C   . ALA   B 1 1309 ? 27.50000   18.42100  28.43500  1.000 88.14124  ?  1307 ALA   B C   1 
ATOM   24366 O  O   . ALA   B 1 1309 ? 26.45600   18.88800  27.96200  1.000 89.11546  ?  1307 ALA   B O   1 
ATOM   24367 C  CB  . ALA   B 1 1309 ? 27.20900   16.08400  29.29500  1.000 68.29270  ?  1307 ALA   B CB  1 
ATOM   24368 N  N   . GLU   B 1 1310 ? 28.36200   19.16000  29.14100  1.000 87.75158  ?  1308 GLU   B N   1 
ATOM   24369 C  CA  . GLU   B 1 1310 ? 28.13000   20.58500  29.36000  1.000 88.85868  ?  1308 GLU   B CA  1 
ATOM   24370 C  C   . GLU   B 1 1310 ? 27.90300   21.32400  28.04600  1.000 94.14007  ?  1308 GLU   B C   1 
ATOM   24371 O  O   . GLU   B 1 1310 ? 27.00200   22.16600  27.94400  1.000 85.52263  ?  1308 GLU   B O   1 
ATOM   24372 C  CB  . GLU   B 1 1310 ? 29.30900   21.19100  30.13000  1.000 95.10296  ?  1308 GLU   B CB  1 
ATOM   24373 C  CG  . GLU   B 1 1310 ? 30.68900   20.91000  29.53200  1.000 106.88347 ?  1308 GLU   B CG  1 
ATOM   24374 C  CD  . GLU   B 1 1310 ? 31.14900   21.99100  28.56800  1.000 111.91848 ?  1308 GLU   B CD  1 
ATOM   24375 O  OE1 . GLU   B 1 1310 ? 30.67600   23.14100  28.68800  1.000 93.49268  ?  1308 GLU   B OE1 1 
ATOM   24376 O  OE2 . GLU   B 1 1310 ? 31.98200   21.68900  27.68700  1.000 113.32524 -1 1308 GLU   B OE2 1 
ATOM   24377 N  N   . ARG   B 1 1311 ? 28.69400   21.00600  27.02000  1.000 80.84727  ?  1309 ARG   B N   1 
ATOM   24378 C  CA  . ARG   B 1 1311 ? 28.53000   21.66500  25.73100  1.000 86.17816  ?  1309 ARG   B CA  1 
ATOM   24379 C  C   . ARG   B 1 1311 ? 27.23900   21.22000  25.05200  1.000 87.24870  ?  1309 ARG   B C   1 
ATOM   24380 O  O   . ARG   B 1 1311 ? 26.45400   22.05400  24.58700  1.000 93.17238  ?  1309 ARG   B O   1 
ATOM   24381 C  CB  . ARG   B 1 1311 ? 29.74200   21.37600  24.84800  1.000 84.21172  ?  1309 ARG   B CB  1 
ATOM   24382 C  CG  . ARG   B 1 1311 ? 29.90100   22.30700  23.66800  1.000 87.11971  ?  1309 ARG   B CG  1 
ATOM   24383 C  CD  . ARG   B 1 1311 ? 31.02000   21.83000  22.77300  1.000 108.33179 ?  1309 ARG   B CD  1 
ATOM   24384 N  NE  . ARG   B 1 1311 ? 30.50800   21.33500  21.50300  1.000 110.38843 ?  1309 ARG   B NE  1 
ATOM   24385 C  CZ  . ARG   B 1 1311 ? 31.26800   20.81400  20.54900  1.000 105.37862 ?  1309 ARG   B CZ  1 
ATOM   24386 N  NH1 . ARG   B 1 1311 ? 32.58500   20.75600  20.67000  1.000 102.83622 ?  1309 ARG   B NH1 1 
ATOM   24387 N  NH2 . ARG   B 1 1311 ? 30.69300   20.33000  19.45100  1.000 75.44507  ?  1309 ARG   B NH2 1 
ATOM   24388 N  N   . ILE   B 1 1312 ? 27.00100   19.90500  24.99500  1.000 76.40035  ?  1310 ILE   B N   1 
ATOM   24389 C  CA  . ILE   B 1 1312 ? 25.77000   19.38800  24.39800  1.000 80.94861  ?  1310 ILE   B CA  1 
ATOM   24390 C  C   . ILE   B 1 1312 ? 24.55300   20.02800  25.05400  1.000 88.86882  ?  1310 ILE   B C   1 
ATOM   24391 O  O   . ILE   B 1 1312 ? 23.60700   20.44200  24.37200  1.000 86.04060  ?  1310 ILE   B O   1 
ATOM   24392 C  CB  . ILE   B 1 1312 ? 25.72800   17.85100  24.50200  1.000 81.08865  ?  1310 ILE   B CB  1 
ATOM   24393 C  CG1 . ILE   B 1 1312 ? 27.13000   17.27000  24.30200  1.000 87.87035  ?  1310 ILE   B CG1 1 
ATOM   24394 C  CG2 . ILE   B 1 1312 ? 24.75600   17.27000  23.48300  1.000 68.61483  ?  1310 ILE   B CG2 1 
ATOM   24395 C  CD1 . ILE   B 1 1312 ? 27.17600   15.75700  24.20500  1.000 85.13599  ?  1310 ILE   B CD1 1 
ATOM   24396 N  N   . ALA   B 1 1313 ? 24.57200   20.14300  26.38700  1.000 88.37713  ?  1311 ALA   B N   1 
ATOM   24397 C  CA  . ALA   B 1 1313 ? 23.46700   20.77900  27.09900  1.000 85.02052  ?  1311 ALA   B CA  1 
ATOM   24398 C  C   . ALA   B 1 1313 ? 23.34400   22.25500  26.73000  1.000 87.40010  ?  1311 ALA   B C   1 
ATOM   24399 O  O   . ALA   B 1 1313 ? 22.24000   22.74900  26.47100  1.000 75.63899  ?  1311 ALA   B O   1 
ATOM   24400 C  CB  . ALA   B 1 1313 ? 23.65100   20.60800  28.60700  1.000 78.27799  ?  1311 ALA   B CB  1 
ATOM   24401 N  N   . TYR   B 1 1314 ? 24.46700   22.97900  26.71500  1.000 84.17283  ?  1312 TYR   B N   1 
ATOM   24402 C  CA  . TYR   B 1 1314 ? 24.45900   24.36100  26.23800  1.000 80.84215  ?  1312 TYR   B CA  1 
ATOM   24403 C  C   . TYR   B 1 1314 ? 23.89300   24.43600  24.82500  1.000 79.77839  ?  1312 TYR   B C   1 
ATOM   24404 O  O   . TYR   B 1 1314 ? 22.88900   25.11500  24.58100  1.000 83.03375  ?  1312 TYR   B O   1 
ATOM   24405 C  CB  . TYR   B 1 1314 ? 25.87800   24.94700  26.30200  1.000 77.26138  ?  1312 TYR   B CB  1 
ATOM   24406 C  CG  . TYR   B 1 1314 ? 26.06300   26.37000  25.77300  1.000 90.13941  ?  1312 TYR   B CG  1 
ATOM   24407 C  CD1 . TYR   B 1 1314 ? 24.99100   27.13100  25.30700  1.000 97.66119  ?  1312 TYR   B CD1 1 
ATOM   24408 C  CD2 . TYR   B 1 1314 ? 27.32800   26.94600  25.74000  1.000 83.33166  ?  1312 TYR   B CD2 1 
ATOM   24409 C  CE1 . TYR   B 1 1314 ? 25.17600   28.40800  24.82300  1.000 97.68113  ?  1312 TYR   B CE1 1 
ATOM   24410 C  CE2 . TYR   B 1 1314 ? 27.51800   28.22800  25.26000  1.000 85.41211  ?  1312 TYR   B CE2 1 
ATOM   24411 C  CZ  . TYR   B 1 1314 ? 26.43900   28.95300  24.80100  1.000 93.89114  ?  1312 TYR   B CZ  1 
ATOM   24412 O  OH  . TYR   B 1 1314 ? 26.61700   30.23000  24.32000  1.000 102.32137 ?  1312 TYR   B OH  1 
ATOM   24413 N  N   . ILE   B 1 1315 ? 24.52400   23.73600  23.87700  1.000 73.56592  ?  1313 ILE   B N   1 
ATOM   24414 C  CA  . ILE   B 1 1315 ? 24.06700   23.78100  22.49000  1.000 72.57254  ?  1313 ILE   B CA  1 
ATOM   24415 C  C   . ILE   B 1 1315 ? 22.59500   23.39600  22.39800  1.000 76.99104  ?  1313 ILE   B C   1 
ATOM   24416 O  O   . ILE   B 1 1315 ? 21.83700   23.97300  21.60900  1.000 68.86423  ?  1313 ILE   B O   1 
ATOM   24417 C  CB  . ILE   B 1 1315 ? 24.95000   22.88200  21.60500  1.000 60.85972  ?  1313 ILE   B CB  1 
ATOM   24418 C  CG1 . ILE   B 1 1315 ? 26.41000   23.33100  21.68400  1.000 57.50691  ?  1313 ILE   B CG1 1 
ATOM   24419 C  CG2 . ILE   B 1 1315 ? 24.47300   22.92500  20.16900  1.000 58.02858  ?  1313 ILE   B CG2 1 
ATOM   24420 C  CD1 . ILE   B 1 1315 ? 27.29100   22.75200  20.60000  1.000 56.05863  ?  1313 ILE   B CD1 1 
ATOM   24421 N  N   . PHE   B 1 1316 ? 22.16300   22.42900  23.21500  1.000 83.50432  ?  1314 PHE   B N   1 
ATOM   24422 C  CA  . PHE   B 1 1316 ? 20.74400   22.09200  23.30100  1.000 84.56748  ?  1314 PHE   B CA  1 
ATOM   24423 C  C   . PHE   B 1 1316 ? 19.90400   23.31400  23.65500  1.000 80.90749  ?  1314 PHE   B C   1 
ATOM   24424 O  O   . PHE   B 1 1316 ? 18.93400   23.64200  22.96300  1.000 85.20538  ?  1314 PHE   B O   1 
ATOM   24425 C  CB  . PHE   B 1 1316 ? 20.53100   20.99000  24.34200  1.000 90.66383  ?  1314 PHE   B CB  1 
ATOM   24426 C  CG  . PHE   B 1 1316 ? 20.51600   19.60200  23.76900  1.000 88.86998  ?  1314 PHE   B CG  1 
ATOM   24427 C  CD1 . PHE   B 1 1316 ? 19.76800   19.31100  22.64500  1.000 89.19762  ?  1314 PHE   B CD1 1 
ATOM   24428 C  CD2 . PHE   B 1 1316 ? 21.24500   18.58300  24.36300  1.000 93.64763  ?  1314 PHE   B CD2 1 
ATOM   24429 C  CE1 . PHE   B 1 1316 ? 19.75000   18.03600  22.11900  1.000 88.09125  ?  1314 PHE   B CE1 1 
ATOM   24430 C  CE2 . PHE   B 1 1316 ? 21.23300   17.30600  23.83900  1.000 84.72709  ?  1314 PHE   B CE2 1 
ATOM   24431 C  CZ  . PHE   B 1 1316 ? 20.48400   17.03200  22.71600  1.000 78.78790  ?  1314 PHE   B CZ  1 
ATOM   24432 N  N   . ALA   B 1 1317 ? 20.26800   24.00400  24.74000  1.000 82.12547  ?  1315 ALA   B N   1 
ATOM   24433 C  CA  . ALA   B 1 1317 ? 19.45000   25.11000  25.22600  1.000 72.54421  ?  1315 ALA   B CA  1 
ATOM   24434 C  C   . ALA   B 1 1317 ? 19.54900   26.32700  24.31500  1.000 78.42697  ?  1315 ALA   B C   1 
ATOM   24435 O  O   . ALA   B 1 1317 ? 18.53200   26.95700  24.00200  1.000 95.89621  ?  1315 ALA   B O   1 
ATOM   24436 C  CB  . ALA   B 1 1317 ? 19.86000   25.47500  26.65300  1.000 58.78521  ?  1315 ALA   B CB  1 
ATOM   24437 N  N   . ASP   B 1 1318 ? 20.76100   26.67500  23.88000  1.000 76.42880  ?  1316 ASP   B N   1 
ATOM   24438 C  CA  . ASP   B 1 1318 ? 20.94800   27.89400  23.10200  1.000 73.93398  ?  1316 ASP   B CA  1 
ATOM   24439 C  C   . ASP   B 1 1318 ? 20.35900   27.79200  21.70300  1.000 71.52322  ?  1316 ASP   B C   1 
ATOM   24440 O  O   . ASP   B 1 1318 ? 20.11100   28.82500  21.07200  1.000 84.40261  ?  1316 ASP   B O   1 
ATOM   24441 C  CB  . ASP   B 1 1318 ? 22.43400   28.23400  23.01000  1.000 77.16425  ?  1316 ASP   B CB  1 
ATOM   24442 C  CG  . ASP   B 1 1318 ? 22.68600   29.72300  22.86900  1.000 90.33581  ?  1316 ASP   B CG  1 
ATOM   24443 O  OD1 . ASP   B 1 1318 ? 22.17600   30.49600  23.70900  1.000 100.58367 ?  1316 ASP   B OD1 1 
ATOM   24444 O  OD2 . ASP   B 1 1318 ? 23.40400   30.12000  21.92800  1.000 95.03330  -1 1316 ASP   B OD2 1 
ATOM   24445 N  N   . SER   B 1 1319 ? 20.13500   26.58000  21.20000  1.000 71.36130  ?  1317 SER   B N   1 
ATOM   24446 C  CA  . SER   B 1 1319 ? 19.57700   26.40300  19.86700  1.000 78.40215  ?  1317 SER   B CA  1 
ATOM   24447 C  C   . SER   B 1 1319 ? 18.07000   26.21700  19.86400  1.000 81.49637  ?  1317 SER   B C   1 
ATOM   24448 O  O   . SER   B 1 1319 ? 17.42100   26.55000  18.86600  1.000 72.09143  ?  1317 SER   B O   1 
ATOM   24449 C  CB  . SER   B 1 1319 ? 20.23400   25.20800  19.16600  1.000 78.26495  ?  1317 SER   B CB  1 
ATOM   24450 O  OG  . SER   B 1 1319 ? 20.33700   24.09600  20.03700  1.000 85.67148  ?  1317 SER   B OG  1 
ATOM   24451 N  N   . GLY   B 1 1320 ? 17.49500   25.71000  20.95200  1.000 83.68760  ?  1318 GLY   B N   1 
ATOM   24452 C  CA  . GLY   B 1 1320 ? 16.07900   25.39000  20.95100  1.000 93.41400  ?  1318 GLY   B CA  1 
ATOM   24453 C  C   . GLY   B 1 1320 ? 15.70900   24.36100  19.91000  1.000 104.55588 ?  1318 GLY   B C   1 
ATOM   24454 O  O   . GLY   B 1 1320 ? 14.55800   24.32000  19.46200  1.000 97.65113  ?  1318 GLY   B O   1 
ATOM   24455 N  N   . ALA   B 1 1321 ? 16.66800   23.53500  19.50000  1.000 92.61071  ?  1319 ALA   B N   1 
ATOM   24456 C  CA  . ALA   B 1 1321 ? 16.42300   22.53900  18.47300  1.000 86.35502  ?  1319 ALA   B CA  1 
ATOM   24457 C  C   . ALA   B 1 1321 ? 15.61900   21.38700  19.04900  1.000 84.47540  ?  1319 ALA   B C   1 
ATOM   24458 O  O   . ALA   B 1 1321 ? 15.83600   20.95800  20.18600  1.000 89.51574  ?  1319 ALA   B O   1 
ATOM   24459 C  CB  . ALA   B 1 1321 ? 17.73700   22.02400  17.89000  1.000 74.31656  ?  1319 ALA   B CB  1 
ATOM   24460 N  N   . LYS   B 1 1322 ? 14.68200   20.89000  18.25100  1.000 72.58522  ?  1320 LYS   B N   1 
ATOM   24461 C  CA  . LYS   B 1 1322 ? 13.76400   19.85900  18.69800  1.000 79.81128  ?  1320 LYS   B CA  1 
ATOM   24462 C  C   . LYS   B 1 1322 ? 14.01700   18.51600  18.02400  1.000 72.74950  ?  1320 LYS   B C   1 
ATOM   24463 O  O   . LYS   B 1 1322 ? 13.14400   17.65700  18.08200  1.000 83.55476  ?  1320 LYS   B O   1 
ATOM   24464 C  CB  . LYS   B 1 1322 ? 12.32000   20.29300  18.44100  1.000 74.98772  ?  1320 LYS   B CB  1 
ATOM   24465 C  CG  . LYS   B 1 1322 ? 12.03700   21.74200  18.75500  1.000 68.01182  ?  1320 LYS   B CG  1 
ATOM   24466 C  CD  . LYS   B 1 1322 ? 12.20800   22.01700  20.23200  1.000 82.91205  ?  1320 LYS   B CD  1 
ATOM   24467 C  CE  . LYS   B 1 1322 ? 11.17500   23.01600  20.71500  1.000 89.25137  ?  1320 LYS   B CE  1 
ATOM   24468 N  NZ  . LYS   B 1 1322 ? 11.14900   23.10400  22.19900  1.000 90.21883  ?  1320 LYS   B NZ  1 
ATOM   24469 N  N   . LEU   B 1 1323 ? 15.16300   18.32100  17.36100  1.000 68.41507  ?  1321 LEU   B N   1 
ATOM   24470 C  CA  . LEU   B 1 1323 ? 15.40900   17.11100  16.56200  1.000 62.59004  ?  1321 LEU   B CA  1 
ATOM   24471 C  C   . LEU   B 1 1323 ? 16.90900   16.86500  16.53000  1.000 71.80757  ?  1321 LEU   B C   1 
ATOM   24472 O  O   . LEU   B 1 1323 ? 17.67900   17.76200  16.17000  1.000 68.48926  ?  1321 LEU   B O   1 
ATOM   24473 C  CB  . LEU   B 1 1323 ? 14.82800   17.22500  15.12400  1.000 63.57513  ?  1321 LEU   B CB  1 
ATOM   24474 C  CG  . LEU   B 1 1323 ? 14.99800   16.32000  13.88000  1.000 77.28507  ?  1321 LEU   B CG  1 
ATOM   24475 C  CD1 . LEU   B 1 1323 ? 14.82100   14.76700  14.19600  1.000 74.46520  ?  1321 LEU   B CD1 1 
ATOM   24476 C  CD2 . LEU   B 1 1323 ? 14.03600   16.90400  12.80100  1.000 56.21772  ?  1321 LEU   B CD2 1 
ATOM   24477 N  N   . VAL   B 1 1324 ? 17.31800   15.65800  16.92100  1.000 74.12012  ?  1322 VAL   B N   1 
ATOM   24478 C  CA  . VAL   B 1 1324 ? 18.72000   15.25200  16.94400  1.000 63.98172  ?  1322 VAL   B CA  1 
ATOM   24479 C  C   . VAL   B 1 1324 ? 18.85500   13.96500  16.14800  1.000 59.16853  ?  1322 VAL   B C   1 
ATOM   24480 O  O   . VAL   B 1 1324 ? 18.20600   12.96100  16.46800  1.000 62.90682  ?  1322 VAL   B O   1 
ATOM   24481 C  CB  . VAL   B 1 1324 ? 19.25000   15.04700  18.37200  1.000 53.90447  ?  1322 VAL   B CB  1 
ATOM   24482 C  CG1 . VAL   B 1 1324 ? 20.65800   14.47400  18.32500  1.000 55.86418  ?  1322 VAL   B CG1 1 
ATOM   24483 C  CG2 . VAL   B 1 1324 ? 19.23200   16.35500  19.13100  1.000 63.01624  ?  1322 VAL   B CG2 1 
ATOM   24484 N  N   . LEU   B 1 1325 ? 19.69500   13.99100  15.12100  1.000 53.04453  ?  1323 LEU   B N   1 
ATOM   24485 C  CA  . LEU   B 1 1325 ? 19.99600   12.81600  14.31100  1.000 45.01225  ?  1323 LEU   B CA  1 
ATOM   24486 C  C   . LEU   B 1 1325 ? 21.33400   12.28000  14.80500  1.000 50.71999  ?  1323 LEU   B C   1 
ATOM   24487 O  O   . LEU   B 1 1325 ? 22.39300   12.80600  14.45500  1.000 59.78763  ?  1323 LEU   B O   1 
ATOM   24488 C  CB  . LEU   B 1 1325 ? 20.03500   13.16800  12.82700  1.000 42.71835  ?  1323 LEU   B CB  1 
ATOM   24489 C  CG  . LEU   B 1 1325 ? 18.74700   13.29400  12.00300  1.000 54.74022  ?  1323 LEU   B CG  1 
ATOM   24490 C  CD1 . LEU   B 1 1325 ? 17.64700   14.00400  12.75100  1.000 70.75973  ?  1323 LEU   B CD1 1 
ATOM   24491 C  CD2 . LEU   B 1 1325 ? 19.04200   14.02000  10.69800  1.000 46.66410  ?  1323 LEU   B CD2 1 
ATOM   24492 N  N   . ALA   B 1 1326 ? 21.28500   11.24400  15.63500  1.000 59.48154  ?  1324 ALA   B N   1 
ATOM   24493 C  CA  . ALA   B 1 1326 ? 22.46900   10.71200  16.28900  1.000 51.36060  ?  1324 ALA   B CA  1 
ATOM   24494 C  C   . ALA   B 1 1326 ? 22.71300   9.27400   15.85900  1.000 55.05852  ?  1324 ALA   B C   1 
ATOM   24495 O  O   . ALA   B 1 1326 ? 21.78900   8.55900   15.46100  1.000 55.34975  ?  1324 ALA   B O   1 
ATOM   24496 C  CB  . ALA   B 1 1326 ? 22.33500   10.77800  17.81600  1.000 41.93619  ?  1324 ALA   B CB  1 
ATOM   24497 N  N   . GLN   B 1 1327 ? 23.97400   8.86100   15.93600  1.000 57.06896  ?  1325 GLN   B N   1 
ATOM   24498 C  CA  . GLN   B 1 1327 ? 24.32000   7.46500   15.74100  1.000 53.18849  ?  1325 GLN   B CA  1 
ATOM   24499 C  C   . GLN   B 1 1327 ? 23.93100   6.65500   16.97500  1.000 62.49766  ?  1325 GLN   B C   1 
ATOM   24500 O  O   . GLN   B 1 1327 ? 23.55800   7.19900   18.01800  1.000 65.88164  ?  1325 GLN   B O   1 
ATOM   24501 C  CB  . GLN   B 1 1327 ? 25.81200   7.31200   15.44700  1.000 51.24079  ?  1325 GLN   B CB  1 
ATOM   24502 C  CG  . GLN   B 1 1327 ? 26.21800   7.71200   14.03600  1.000 51.84433  ?  1325 GLN   B CG  1 
ATOM   24503 C  CD  . GLN   B 1 1327 ? 27.71800   7.62800   13.81500  1.000 56.49414  ?  1325 GLN   B CD  1 
ATOM   24504 O  OE1 . GLN   B 1 1327 ? 28.50000   7.69400   14.76400  1.000 44.10190  ?  1325 GLN   B OE1 1 
ATOM   24505 N  NE2 . GLN   B 1 1327 ? 28.12600   7.47900   12.55900  1.000 43.87671  ?  1325 GLN   B NE2 1 
ATOM   24506 N  N   . SER   B 1 1328 ? 24.02200   5.33300   16.84200  1.000 67.62877  ?  1326 SER   B N   1 
ATOM   24507 C  CA  . SER   B 1 1328 ? 23.65900   4.43000   17.93400  1.000 53.11467  ?  1326 SER   B CA  1 
ATOM   24508 C  C   . SER   B 1 1328 ? 24.37600   4.73000   19.24700  1.000 57.95888  ?  1326 SER   B C   1 
ATOM   24509 O  O   . SER   B 1 1328 ? 23.69700   4.81000   20.28300  1.000 71.84901  ?  1326 SER   B O   1 
ATOM   24510 C  CB  . SER   B 1 1328 ? 23.90000   2.98100   17.48900  1.000 52.14332  ?  1326 SER   B CB  1 
ATOM   24511 O  OG  . SER   B 1 1328 ? 24.01800   2.11900   18.60700  1.000 85.83834  ?  1326 SER   B OG  1 
ATOM   24512 N  N   . PRO   B 1 1329 ? 25.70200   4.90900   19.29400  1.000 56.32240  ?  1327 PRO   B N   1 
ATOM   24513 C  CA  . PRO   B 1 1329 ? 26.35600   5.16000   20.58800  1.000 61.54443  ?  1327 PRO   B CA  1 
ATOM   24514 C  C   . PRO   B 1 1329 ? 26.11300   6.55000   21.15400  1.000 75.57412  ?  1327 PRO   B C   1 
ATOM   24515 O  O   . PRO   B 1 1329 ? 26.63500   6.85500   22.23300  1.000 80.33268  ?  1327 PRO   B O   1 
ATOM   24516 C  CB  . PRO   B 1 1329 ? 27.85000   4.95600   20.27400  1.000 55.36383  ?  1327 PRO   B CB  1 
ATOM   24517 C  CG  . PRO   B 1 1329 ? 27.89300   4.27800   18.94000  1.000 62.37618  ?  1327 PRO   B CG  1 
ATOM   24518 C  CD  . PRO   B 1 1329 ? 26.69800   4.78800   18.21500  1.000 58.15728  ?  1327 PRO   B CD  1 
ATOM   24519 N  N   . PHE   B 1 1330 ? 25.34400   7.40400   20.47600  1.000 71.36758  ?  1328 PHE   B N   1 
ATOM   24520 C  CA  . PHE   B 1 1330 ? 25.12200   8.76700   20.94200  1.000 64.09168  ?  1328 PHE   B CA  1 
ATOM   24521 C  C   . PHE   B 1 1330 ? 23.64300   9.10600   21.08100  1.000 73.80418  ?  1328 PHE   B C   1 
ATOM   24522 O  O   . PHE   B 1 1330 ? 23.30800   10.27300  21.32200  1.000 78.15763  ?  1328 PHE   B O   1 
ATOM   24523 C  CB  . PHE   B 1 1330 ? 25.80500   9.76800   20.00200  1.000 69.71300  ?  1328 PHE   B CB  1 
ATOM   24524 C  CG  . PHE   B 1 1330 ? 27.18400   9.34900   19.57800  1.000 62.82249  ?  1328 PHE   B CG  1 
ATOM   24525 C  CD1 . PHE   B 1 1330 ? 28.19900   9.21400   20.51100  1.000 48.37464  ?  1328 PHE   B CD1 1 
ATOM   24526 C  CD2 . PHE   B 1 1330 ? 27.46500   9.08600   18.24700  1.000 61.97305  ?  1328 PHE   B CD2 1 
ATOM   24527 C  CE1 . PHE   B 1 1330 ? 29.46700   8.82400   20.12600  1.000 48.24069  ?  1328 PHE   B CE1 1 
ATOM   24528 C  CE2 . PHE   B 1 1330 ? 28.73200   8.69800   17.85500  1.000 60.29830  ?  1328 PHE   B CE2 1 
ATOM   24529 C  CZ  . PHE   B 1 1330 ? 29.73400   8.56500   18.79500  1.000 62.28869  ?  1328 PHE   B CZ  1 
ATOM   24530 N  N   . VAL   B 1 1331 ? 22.75000   8.12500   20.93400  1.000 81.48233  ?  1329 VAL   B N   1 
ATOM   24531 C  CA  . VAL   B 1 1331 ? 21.32900   8.37500   21.14800  1.000 73.46269  ?  1329 VAL   B CA  1 
ATOM   24532 C  C   . VAL   B 1 1331 ? 21.05900   8.68800   22.61400  1.000 72.65431  ?  1329 VAL   B C   1 
ATOM   24533 O  O   . VAL   B 1 1331 ? 20.22300   9.53900   22.94000  1.000 79.08784  ?  1329 VAL   B O   1 
ATOM   24534 C  CB  . VAL   B 1 1331 ? 20.49900   7.17400   20.65600  1.000 60.78430  ?  1329 VAL   B CB  1 
ATOM   24535 C  CG1 . VAL   B 1 1331 ? 19.07000   7.25900   21.16700  1.000 53.42479  ?  1329 VAL   B CG1 1 
ATOM   24536 C  CG2 . VAL   B 1 1331 ? 20.51200   7.10900   19.13600  1.000 56.98534  ?  1329 VAL   B CG2 1 
ATOM   24537 N  N   . GLU   B 1 1332 ? 21.77500   8.01900   23.52200  1.000 86.96352  ?  1330 GLU   B N   1 
ATOM   24538 C  CA  . GLU   B 1 1332 ? 21.58000   8.26400   24.94700  1.000 84.02351  ?  1330 GLU   B CA  1 
ATOM   24539 C  C   . GLU   B 1 1332 ? 22.06200   9.65000   25.35500  1.000 87.20262  ?  1330 GLU   B C   1 
ATOM   24540 O  O   . GLU   B 1 1332 ? 21.49000   10.25900  26.26600  1.000 93.69051  ?  1330 GLU   B O   1 
ATOM   24541 C  CB  . GLU   B 1 1332 ? 22.29300   7.19200   25.77200  1.000 89.94551  ?  1330 GLU   B CB  1 
ATOM   24542 C  CG  . GLU   B 1 1332 ? 23.68000   6.81300   25.26700  1.000 96.74142  ?  1330 GLU   B CG  1 
ATOM   24543 C  CD  . GLU   B 1 1332 ? 23.65900   5.59000   24.36800  1.000 108.60091 ?  1330 GLU   B CD  1 
ATOM   24544 O  OE1 . GLU   B 1 1332 ? 22.92000   5.59700   23.36000  1.000 98.22311  ?  1330 GLU   B OE1 1 
ATOM   24545 O  OE2 . GLU   B 1 1332 ? 24.37400   4.61300   24.67700  1.000 105.82308 -1 1330 GLU   B OE2 1 
ATOM   24546 N  N   . LYS   B 1 1333 ? 23.10800   10.16300  24.70200  1.000 82.83668  ?  1331 LYS   B N   1 
ATOM   24547 C  CA  . LYS   B 1 1333 ? 23.58400   11.50500  25.01900  1.000 76.09079  ?  1331 LYS   B CA  1 
ATOM   24548 C  C   . LYS   B 1 1333 ? 22.52800   12.55400  24.69400  1.000 73.90937  ?  1331 LYS   B C   1 
ATOM   24549 O  O   . LYS   B 1 1333 ? 22.38800   13.55100  25.41200  1.000 80.20613  ?  1331 LYS   B O   1 
ATOM   24550 C  CB  . LYS   B 1 1333 ? 24.88100   11.79500  24.26100  1.000 72.38317  ?  1331 LYS   B CB  1 
ATOM   24551 C  CG  . LYS   B 1 1333 ? 26.04700   10.87900  24.62100  1.000 75.13148  ?  1331 LYS   B CG  1 
ATOM   24552 C  CD  . LYS   B 1 1333 ? 27.31800   11.31000  23.89500  1.000 67.94130  ?  1331 LYS   B CD  1 
ATOM   24553 C  CE  . LYS   B 1 1333 ? 28.56700   10.66800  24.48900  1.000 62.30050  ?  1331 LYS   B CE  1 
ATOM   24554 N  NZ  . LYS   B 1 1333 ? 28.68800   9.21900   24.16500  1.000 65.03240  ?  1331 LYS   B NZ  1 
ATOM   24555 N  N   . ALA   B 1 1334 ? 21.76600   12.34100  23.62300  1.000 67.25999  ?  1332 ALA   B N   1 
ATOM   24556 C  CA  . ALA   B 1 1334 ? 20.75700   13.30100  23.19000  1.000 71.88982  ?  1332 ALA   B CA  1 
ATOM   24557 C  C   . ALA   B 1 1334 ? 19.42100   13.02700  23.86300  1.000 89.45645  ?  1332 ALA   B C   1 
ATOM   24558 O  O   . ALA   B 1 1334 ? 18.36400   13.35600  23.31300  1.000 85.49699  ?  1332 ALA   B O   1 
ATOM   24559 C  CB  . ALA   B 1 1334 ? 20.60500   13.26300  21.67000  1.000 54.52572  ?  1332 ALA   B CB  1 
ATOM   24560 N  N   . SER   B 1 1335 ? 19.45800   12.43600  25.05600  1.000 85.59506  ?  1333 SER   B N   1 
ATOM   24561 C  CA  . SER   B 1 1335 ? 18.22400   12.04300  25.72900  1.000 89.86577  ?  1333 SER   B CA  1 
ATOM   24562 C  C   . SER   B 1 1335 ? 17.35300   13.24600  26.06800  1.000 95.53857  ?  1333 SER   B C   1 
ATOM   24563 O  O   . SER   B 1 1335 ? 16.12300   13.12500  26.12000  1.000 77.29772  ?  1333 SER   B O   1 
ATOM   24564 C  CB  . SER   B 1 1335 ? 18.54400   11.24500  26.99400  1.000 89.36979  ?  1333 SER   B CB  1 
ATOM   24565 O  OG  . SER   B 1 1335 ? 19.44000   11.95700  27.83100  1.000 87.31017  ?  1333 SER   B OG  1 
ATOM   24566 N  N   . MET   B 1 1336 ? 17.96400   14.40900  26.28900  1.000 92.89866  ?  1334 MET   B N   1 
ATOM   24567 C  CA  . MET   B 1 1336 ? 17.22600   15.59600  26.69800  1.000 95.52736  ?  1334 MET   B CA  1 
ATOM   24568 C  C   . MET   B 1 1336 ? 16.61700   16.35300  25.52300  1.000 75.79248  ?  1334 MET   B C   1 
ATOM   24569 O  O   . MET   B 1 1336 ? 15.95600   17.37500  25.74100  1.000 74.40143  ?  1334 MET   B O   1 
ATOM   24570 C  CB  . MET   B 1 1336 ? 18.13700   16.52200  27.51100  1.000 74.75819  ?  1334 MET   B CB  1 
ATOM   24571 C  CG  . MET   B 1 1336 ? 17.58400   16.90500  28.88200  1.000 78.30490  ?  1334 MET   B CG  1 
ATOM   24572 S  SD  . MET   B 1 1336 ? 16.97400   15.50200  29.84200  1.000 119.22524 ?  1334 MET   B SD  1 
ATOM   24573 C  CE  . MET   B 1 1336 ? 18.38500   14.39600  29.79000  1.000 86.27901  ?  1334 MET   B CE  1 
ATOM   24574 N  N   . ALA   B 1 1337 ? 16.81300   15.88200  24.29400  1.000 63.42682  ?  1335 ALA   B N   1 
ATOM   24575 C  CA  . ALA   B 1 1337 ? 16.12000   16.46200  23.15900  1.000 66.79924  ?  1335 ALA   B CA  1 
ATOM   24576 C  C   . ALA   B 1 1337 ? 14.68000   15.96700  23.11700  1.000 75.28051  ?  1335 ALA   B C   1 
ATOM   24577 O  O   . ALA   B 1 1337 ? 14.25700   15.11600  23.90700  1.000 77.74971  ?  1335 ALA   B O   1 
ATOM   24578 C  CB  . ALA   B 1 1337 ? 16.82900   16.11600  21.85100  1.000 65.46419  ?  1335 ALA   B CB  1 
ATOM   24579 N  N   . GLU   B 1 1338 ? 13.91700   16.50900  22.17300  1.000 68.14083  ?  1336 GLU   B N   1 
ATOM   24580 C  CA  . GLU   B 1 1338 ? 12.52600   16.09200  22.04900  1.000 76.33670  ?  1336 GLU   B CA  1 
ATOM   24581 C  C   . GLU   B 1 1338 ? 12.41100   14.82600  21.21300  1.000 70.30920  ?  1336 GLU   B C   1 
ATOM   24582 O  O   . GLU   B 1 1338 ? 11.90100   13.80100  21.67400  1.000 75.74162  ?  1336 GLU   B O   1 
ATOM   24583 C  CB  . GLU   B 1 1338 ? 11.68200   17.22500  21.46300  1.000 78.64120  ?  1336 GLU   B CB  1 
ATOM   24584 C  CG  . GLU   B 1 1338 ? 11.66700   18.45800  22.34000  1.000 89.01679  ?  1336 GLU   B CG  1 
ATOM   24585 C  CD  . GLU   B 1 1338 ? 10.39900   19.26900  22.18400  1.000 88.64760  ?  1336 GLU   B CD  1 
ATOM   24586 O  OE1 . GLU   B 1 1338 ? 9.67100    19.06100  21.19000  1.000 85.41183  ?  1336 GLU   B OE1 1 
ATOM   24587 O  OE2 . GLU   B 1 1338 ? 10.12600   20.11100  23.06400  1.000 80.40009  -1 1336 GLU   B OE2 1 
ATOM   24588 N  N   . VAL   B 1 1339 ? 12.90800   14.86000  19.99300  1.000 72.58424  ?  1337 VAL   B N   1 
ATOM   24589 C  CA  . VAL   B 1 1339 ? 12.82800   13.71700  19.10700  1.000 69.70652  ?  1337 VAL   B CA  1 
ATOM   24590 C  C   . VAL   B 1 1339 ? 14.25000   13.39900  18.69900  1.000 58.24780  ?  1337 VAL   B C   1 
ATOM   24591 O  O   . VAL   B 1 1339 ? 14.99100   14.31900  18.34900  1.000 64.70056  ?  1337 VAL   B O   1 
ATOM   24592 C  CB  . VAL   B 1 1339 ? 11.89700   14.03400  17.92200  1.000 47.60432  ?  1337 VAL   B CB  1 
ATOM   24593 C  CG1 . VAL   B 1 1339 ? 10.48000   14.39000  18.54400  1.000 63.55336  ?  1337 VAL   B CG1 1 
ATOM   24594 C  CG2 . VAL   B 1 1339 ? 12.47500   15.13800  16.91000  1.000 60.91082  ?  1337 VAL   B CG2 1 
ATOM   24595 N  N   . VAL   B 1 1340 ? 14.64900   12.12400  18.79800  1.000 49.02102  ?  1338 VAL   B N   1 
ATOM   24596 C  CA  . VAL   B 1 1340 ? 16.00200   11.66600  18.47100  1.000 55.26457  ?  1338 VAL   B CA  1 
ATOM   24597 C  C   . VAL   B 1 1340 ? 15.85700   10.50300  17.50500  1.000 55.93742  ?  1338 VAL   B C   1 
ATOM   24598 O  O   . VAL   B 1 1340 ? 15.15300   9.53100   17.80400  1.000 49.55625  ?  1338 VAL   B O   1 
ATOM   24599 C  CB  . VAL   B 1 1340 ? 16.79500   11.23900  19.72000  1.000 49.28089  ?  1338 VAL   B CB  1 
ATOM   24600 C  CG1 . VAL   B 1 1340 ? 18.20500   10.80600  19.34500  1.000 40.52864  ?  1338 VAL   B CG1 1 
ATOM   24601 C  CG2 . VAL   B 1 1340 ? 16.83400   12.36300  20.74000  1.000 51.47430  ?  1338 VAL   B CG2 1 
ATOM   24602 N  N   . LEU   B 1 1341 ? 16.48600   10.61500  16.34100  1.000 62.84471  ?  1339 LEU   B N   1 
ATOM   24603 C  CA  . LEU   B 1 1341 ? 16.40100   9.60000   15.30000  1.000 59.76260  ?  1339 LEU   B CA  1 
ATOM   24604 C  C   . LEU   B 1 1341 ? 17.75200   8.91400   15.16800  1.000 74.00879  ?  1339 LEU   B C   1 
ATOM   24605 O  O   . LEU   B 1 1341 ? 18.75400   9.56400   14.84900  1.000 76.86323  ?  1339 LEU   B O   1 
ATOM   24606 C  CB  . LEU   B 1 1341 ? 15.97400   10.21700  13.96900  1.000 49.18943  ?  1339 LEU   B CB  1 
ATOM   24607 C  CG  . LEU   B 1 1341 ? 14.53300   10.72500  13.90900  1.000 59.54824  ?  1339 LEU   B CG  1 
ATOM   24608 C  CD1 . LEU   B 1 1341 ? 14.14600   11.06000  12.47700  1.000 66.71075  ?  1339 LEU   B CD1 1 
ATOM   24609 C  CD2 . LEU   B 1 1341 ? 13.57900   9.70200   14.50500  1.000 59.68138  ?  1339 LEU   B CD2 1 
ATOM   24610 N  N   . ASP   B 1 1342 ? 17.77400   7.60700   15.41400  1.000 70.24536  ?  1340 ASP   B N   1 
ATOM   24611 C  CA  . ASP   B 1 1342 ? 18.99600   6.82600   15.27400  1.000 59.94085  ?  1340 ASP   B CA  1 
ATOM   24612 C  C   . ASP   B 1 1342 ? 19.31800   6.64500   13.79600  1.000 60.85755  ?  1340 ASP   B C   1 
ATOM   24613 O  O   . ASP   B 1 1342 ? 18.53400   6.04900   13.05100  1.000 54.18618  ?  1340 ASP   B O   1 
ATOM   24614 C  CB  . ASP   B 1 1342 ? 18.83500   5.47300   15.96400  1.000 54.81121  ?  1340 ASP   B CB  1 
ATOM   24615 C  CG  . ASP   B 1 1342 ? 20.16100   4.77200   16.20600  1.000 65.22320  ?  1340 ASP   B CG  1 
ATOM   24616 O  OD1 . ASP   B 1 1342 ? 21.07700   4.89200   15.36400  1.000 64.94467  ?  1340 ASP   B OD1 1 
ATOM   24617 O  OD2 . ASP   B 1 1342 ? 20.28800   4.09300   17.24700  1.000 69.84029  -1 1340 ASP   B OD2 1 
ATOM   24618 N  N   . LEU   B 1 1343 ? 20.47300   7.16100   13.36900  1.000 66.98509  ?  1341 LEU   B N   1 
ATOM   24619 C  CA  . LEU   B 1 1343 ? 20.88700   7.02100   11.97900  1.000 61.36173  ?  1341 LEU   B CA  1 
ATOM   24620 C  C   . LEU   B 1 1343 ? 21.28000   5.59400   11.62300  1.000 64.58169  ?  1341 LEU   B C   1 
ATOM   24621 O  O   . LEU   B 1 1343 ? 21.48300   5.30400   10.43900  1.000 54.71719  ?  1341 LEU   B O   1 
ATOM   24622 C  CB  . LEU   B 1 1343 ? 22.05000   7.96900   11.67900  1.000 51.22100  ?  1341 LEU   B CB  1 
ATOM   24623 C  CG  . LEU   B 1 1343 ? 21.74100   9.46400   11.78500  1.000 52.92908  ?  1341 LEU   B CG  1 
ATOM   24624 C  CD1 . LEU   B 1 1343 ? 22.97500   10.29500  11.47200  1.000 47.13493  ?  1341 LEU   B CD1 1 
ATOM   24625 C  CD2 . LEU   B 1 1343 ? 20.59100   9.83700   10.86300  1.000 54.48521  ?  1341 LEU   B CD2 1 
ATOM   24626 N  N   . ASN   B 1 1344 ? 21.39100   4.70400   12.61000  1.000 60.41642  ?  1342 ASN   B N   1 
ATOM   24627 C  CA  . ASN   B 1 1344 ? 21.72600   3.30400   12.38500  1.000 64.22182  ?  1342 ASN   B CA  1 
ATOM   24628 C  C   . ASN   B 1 1344 ? 20.51700   2.39500   12.58400  1.000 66.04297  ?  1342 ASN   B C   1 
ATOM   24629 O  O   . ASN   B 1 1344 ? 20.66700   1.21100   12.89600  1.000 70.23737  ?  1342 ASN   B O   1 
ATOM   24630 C  CB  . ASN   B 1 1344 ? 22.87100   2.87600   13.30000  1.000 60.65257  ?  1342 ASN   B CB  1 
ATOM   24631 C  CG  . ASN   B 1 1344 ? 24.09800   3.74800   13.14000  1.000 56.55308  ?  1342 ASN   B CG  1 
ATOM   24632 O  OD1 . ASN   B 1 1344 ? 24.55600   4.37400   14.09500  1.000 65.19517  ?  1342 ASN   B OD1 1 
ATOM   24633 N  ND2 . ASN   B 1 1344 ? 24.63600   3.79500   11.92600  1.000 41.11182  ?  1342 ASN   B ND2 1 
ATOM   24634 N  N   . SER   B 1 1345 ? 19.31500   2.93900   12.41200  1.000 61.49277  ?  1343 SER   B N   1 
ATOM   24635 C  CA  . SER   B 1 1345 ? 18.07700   2.18400   12.54600  1.000 56.54939  ?  1343 SER   B CA  1 
ATOM   24636 C  C   . SER   B 1 1345 ? 17.23600   2.39500   11.29800  1.000 68.60663  ?  1343 SER   B C   1 
ATOM   24637 O  O   . SER   B 1 1345 ? 17.01200   3.53700   10.88300  1.000 73.46751  ?  1343 SER   B O   1 
ATOM   24638 C  CB  . SER   B 1 1345 ? 17.29700   2.61200   13.79400  1.000 41.68893  ?  1343 SER   B CB  1 
ATOM   24639 O  OG  . SER   B 1 1345 ? 16.05100   1.94000   13.87400  1.000 52.02197  ?  1343 SER   B OG  1 
ATOM   24640 N  N   . ALA   B 1 1346 ? 16.77300   1.29400   10.70100  1.000 60.84242  ?  1344 ALA   B N   1 
ATOM   24641 C  CA  . ALA   B 1 1346 ? 15.95100   1.39200   9.50100   1.000 48.08985  ?  1344 ALA   B CA  1 
ATOM   24642 C  C   . ALA   B 1 1346 ? 14.61600   2.07200   9.77100   1.000 57.35970  ?  1344 ALA   B C   1 
ATOM   24643 O  O   . ALA   B 1 1346 ? 13.96500   2.53100   8.82600   1.000 62.04335  ?  1344 ALA   B O   1 
ATOM   24644 C  CB  . ALA   B 1 1346 ? 15.72200   0.00300   8.90500   1.000 53.16184  ?  1344 ALA   B CB  1 
ATOM   24645 N  N   . SER   B 1 1347 ? 14.19500   2.14600   11.03700  1.000 63.15549  ?  1345 SER   B N   1 
ATOM   24646 C  CA  . SER   B 1 1347 ? 12.95600   2.84200   11.36900  1.000 57.90648  ?  1345 SER   B CA  1 
ATOM   24647 C  C   . SER   B 1 1347 ? 13.04300   4.32600   11.04100  1.000 67.96645  ?  1345 SER   B C   1 
ATOM   24648 O  O   . SER   B 1 1347 ? 12.03800   4.93900   10.66300  1.000 71.91330  ?  1345 SER   B O   1 
ATOM   24649 C  CB  . SER   B 1 1347 ? 12.62500   2.64600   12.84900  1.000 55.44302  ?  1345 SER   B CB  1 
ATOM   24650 O  OG  . SER   B 1 1347 ? 13.62500   3.21600   13.67600  1.000 62.10027  ?  1345 SER   B OG  1 
ATOM   24651 N  N   . SER   B 1 1348 ? 14.23000   4.91700   11.17500  1.000 64.86310  ?  1346 SER   B N   1 
ATOM   24652 C  CA  . SER   B 1 1348 ? 14.42100   6.33100   10.88500  1.000 71.57229  ?  1346 SER   B CA  1 
ATOM   24653 C  C   . SER   B 1 1348 ? 14.46500   6.63200   9.39300   1.000 64.12614  ?  1346 SER   B C   1 
ATOM   24654 O  O   . SER   B 1 1348 ? 14.42500   7.80800   9.01300   1.000 72.16229  ?  1346 SER   B O   1 
ATOM   24655 C  CB  . SER   B 1 1348 ? 15.70500   6.82700   11.55200  1.000 62.35476  ?  1346 SER   B CB  1 
ATOM   24656 O  OG  . SER   B 1 1348 ? 15.67900   6.56600   12.94500  1.000 55.74335  ?  1346 SER   B OG  1 
ATOM   24657 N  N   . TYR   B 1 1349 ? 14.54900   5.61300   8.54500   1.000 66.22591  ?  1347 TYR   B N   1 
ATOM   24658 C  CA  . TYR   B 1 1349 ? 14.51900   5.77900   7.10100   1.000 65.50698  ?  1347 TYR   B CA  1 
ATOM   24659 C  C   . TYR   B 1 1349 ? 13.18000   5.28900   6.56600   1.000 66.27135  ?  1347 TYR   B C   1 
ATOM   24660 O  O   . TYR   B 1 1349 ? 12.52400   4.43800   7.17100   1.000 78.29013  ?  1347 TYR   B O   1 
ATOM   24661 C  CB  . TYR   B 1 1349 ? 15.66900   5.02100   6.43100   1.000 59.58056  ?  1347 TYR   B CB  1 
ATOM   24662 C  CG  . TYR   B 1 1349 ? 17.04500   5.51000   6.83300   1.000 59.84253  ?  1347 TYR   B CG  1 
ATOM   24663 C  CD1 . TYR   B 1 1349 ? 17.60900   5.13900   8.04700   1.000 58.18502  ?  1347 TYR   B CD1 1 
ATOM   24664 C  CD2 . TYR   B 1 1349 ? 17.78300   6.33600   5.99500   1.000 70.36209  ?  1347 TYR   B CD2 1 
ATOM   24665 C  CE1 . TYR   B 1 1349 ? 18.86400   5.58100   8.41900   1.000 63.87531  ?  1347 TYR   B CE1 1 
ATOM   24666 C  CE2 . TYR   B 1 1349 ? 19.04100   6.78300   6.35800   1.000 65.36258  ?  1347 TYR   B CE2 1 
ATOM   24667 C  CZ  . TYR   B 1 1349 ? 19.57600   6.40200   7.57100   1.000 55.17346  ?  1347 TYR   B CZ  1 
ATOM   24668 O  OH  . TYR   B 1 1349 ? 20.82700   6.84200   7.93900   1.000 56.40866  ?  1347 TYR   B OH  1 
ATOM   24669 N  N   . ALA   B 1 1350 ? 12.77500   5.83800   5.42800   1.000 65.10633  ?  1348 ALA   B N   1 
ATOM   24670 C  CA  . ALA   B 1 1350 ? 11.47000   5.56000   4.84700   1.000 63.91787  ?  1348 ALA   B CA  1 
ATOM   24671 C  C   . ALA   B 1 1350 ? 11.62500   4.70300   3.59200   1.000 80.98013  ?  1348 ALA   B C   1 
ATOM   24672 O  O   . ALA   B 1 1350 ? 12.73600   4.38900   3.15700   1.000 80.18295  ?  1348 ALA   B O   1 
ATOM   24673 C  CB  . ALA   B 1 1350 ? 10.73600   6.86700   4.54400   1.000 63.53180  ?  1348 ALA   B CB  1 
ATOM   24674 N  N   . ALA   B 1 1351 ? 10.48400   4.32000   3.01300   1.000 77.21288  ?  1349 ALA   B N   1 
ATOM   24675 C  CA  . ALA   B 1 1351 ? 10.46300   3.50900   1.79900   1.000 71.14907  ?  1349 ALA   B CA  1 
ATOM   24676 C  C   . ALA   B 1 1351 ? 10.55900   4.33400   0.52400   1.000 80.70429  ?  1349 ALA   B C   1 
ATOM   24677 O  O   . ALA   B 1 1351 ? 11.11200   3.85400   -0.47400  1.000 79.74720  ?  1349 ALA   B O   1 
ATOM   24678 C  CB  . ALA   B 1 1351 ? 9.18700    2.66200   1.74500   1.000 71.90037  ?  1349 ALA   B CB  1 
ATOM   24679 N  N   . ASP   B 1 1352 ? 10.02400   5.55200   0.52600   1.000 80.82464  ?  1350 ASP   B N   1 
ATOM   24680 C  CA  . ASP   B 1 1352 ? 10.02600   6.38600   -0.66900  1.000 77.00187  ?  1350 ASP   B CA  1 
ATOM   24681 C  C   . ASP   B 1 1352 ? 11.44400   6.84700   -0.98500  1.000 70.39126  ?  1350 ASP   B C   1 
ATOM   24682 O  O   . ASP   B 1 1352 ? 12.06700   7.55500   -0.18700  1.000 70.09858  ?  1350 ASP   B O   1 
ATOM   24683 C  CB  . ASP   B 1 1352 ? 9.10300    7.58700   -0.47100  1.000 69.70145  ?  1350 ASP   B CB  1 
ATOM   24684 C  CG  . ASP   B 1 1352 ? 8.79000    8.30100   -1.76900  1.000 87.20660  ?  1350 ASP   B CG  1 
ATOM   24685 O  OD1 . ASP   B 1 1352 ? 9.13500    7.76300   -2.84300  1.000 86.79279  ?  1350 ASP   B OD1 1 
ATOM   24686 O  OD2 . ASP   B 1 1352 ? 8.19700    9.40000   -1.71700  1.000 87.14601  -1 1350 ASP   B OD2 1 
ATOM   24687 N  N   . THR   B 1 1353 ? 11.95300   6.45100   -2.15300  1.000 74.83810  ?  1351 THR   B N   1 
ATOM   24688 C  CA  . THR   B 1 1353 ? 13.27000   6.86100   -2.62000  1.000 76.19423  ?  1351 THR   B CA  1 
ATOM   24689 C  C   . THR   B 1 1353 ? 13.19600   7.95900   -3.67600  1.000 81.64516  ?  1351 THR   B C   1 
ATOM   24690 O  O   . THR   B 1 1353 ? 14.17300   8.18300   -4.39900  1.000 86.85486  ?  1351 THR   B O   1 
ATOM   24691 C  CB  . THR   B 1 1353 ? 14.04000   5.65700   -3.16500  1.000 75.77967  ?  1351 THR   B CB  1 
ATOM   24692 O  OG1 . THR   B 1 1353 ? 13.27600   5.02700   -4.20100  1.000 84.85213  ?  1351 THR   B OG1 1 
ATOM   24693 C  CG2 . THR   B 1 1353 ? 14.30600   4.65100   -2.05700  1.000 70.71218  ?  1351 THR   B CG2 1 
ATOM   24694 N  N   . SER   B 1 1354 ? 12.06100   8.64300   -3.78200  1.000 84.90384  ?  1352 SER   B N   1 
ATOM   24695 C  CA  . SER   B 1 1354 ? 11.91000   9.75200   -4.71000  1.000 88.92633  ?  1352 SER   B CA  1 
ATOM   24696 C  C   . SER   B 1 1354 ? 12.27200   11.06500  -4.02600  1.000 92.53552  ?  1352 SER   B C   1 
ATOM   24697 O  O   . SER   B 1 1354 ? 12.14200   11.21100  -2.80700  1.000 83.42907  ?  1352 SER   B O   1 
ATOM   24698 C  CB  . SER   B 1 1354 ? 10.48100   9.81900   -5.25400  1.000 89.26871  ?  1352 SER   B CB  1 
ATOM   24699 O  OG  . SER   B 1 1354 ? 9.53900    9.97200   -4.20700  1.000 86.32574  ?  1352 SER   B OG  1 
ATOM   24700 N  N   . ASN   B 1 1355 ? 12.72600   12.02100  -4.82900  1.000 85.68609  ?  1353 ASN   B N   1 
ATOM   24701 C  CA  . ASN   B 1 1355 ? 13.21400   13.28400  -4.29400  1.000 72.91041  ?  1353 ASN   B CA  1 
ATOM   24702 C  C   . ASN   B 1 1355 ? 12.07800   14.04800  -3.61800  1.000 71.15864  ?  1353 ASN   B C   1 
ATOM   24703 O  O   . ASN   B 1 1355 ? 10.99200   14.18000  -4.20000  1.000 73.03198  ?  1353 ASN   B O   1 
ATOM   24704 C  CB  . ASN   B 1 1355 ? 13.82900   14.12700  -5.41000  1.000 61.71348  ?  1353 ASN   B CB  1 
ATOM   24705 C  CG  . ASN   B 1 1355 ? 14.92100   13.38900  -6.16100  1.000 70.88410  ?  1353 ASN   B CG  1 
ATOM   24706 O  OD1 . ASN   B 1 1355 ? 15.15900   12.20400  -5.92700  1.000 85.99229  ?  1353 ASN   B OD1 1 
ATOM   24707 N  ND2 . ASN   B 1 1355 ? 15.58400   14.08500  -7.07600  1.000 68.97573  ?  1353 ASN   B ND2 1 
ATOM   24708 N  N   . PRO   B 1 1356 ? 12.27800   14.55300  -2.40400  1.000 68.39244  ?  1354 PRO   B N   1 
ATOM   24709 C  CA  . PRO   B 1 1356 ? 11.21400   15.28800  -1.71300  1.000 61.28471  ?  1354 PRO   B CA  1 
ATOM   24710 C  C   . PRO   B 1 1356 ? 10.94700   16.62100  -2.38800  1.000 80.86264  ?  1354 PRO   B C   1 
ATOM   24711 O  O   . PRO   B 1 1356 ? 11.77100   17.10300  -3.18000  1.000 74.07298  ?  1354 PRO   B O   1 
ATOM   24712 C  CB  . PRO   B 1 1356 ? 11.78000   15.48400  -0.29600  1.000 50.80841  ?  1354 PRO   B CB  1 
ATOM   24713 C  CG  . PRO   B 1 1356 ? 12.89700   14.49400  -0.17800  1.000 69.90327  ?  1354 PRO   B CG  1 
ATOM   24714 C  CD  . PRO   B 1 1356 ? 13.46500   14.37600  -1.55300  1.000 69.46268  ?  1354 PRO   B CD  1 
ATOM   24715 N  N   . PRO   B 1 1357 ? 9.80200    17.24400  -2.10800  1.000 95.79761  ?  1355 PRO   B N   1 
ATOM   24716 C  CA  . PRO   B 1 1357 ? 9.51600    18.55700  -2.69900  1.000 81.77044  ?  1355 PRO   B CA  1 
ATOM   24717 C  C   . PRO   B 1 1357 ? 10.47200   19.62500  -2.18700  1.000 84.73555  ?  1355 PRO   B C   1 
ATOM   24718 O  O   . PRO   B 1 1357 ? 10.87200   19.62300  -1.02000  1.000 89.07061  ?  1355 PRO   B O   1 
ATOM   24719 C  CB  . PRO   B 1 1357 ? 8.07500    18.84100  -2.25700  1.000 79.08184  ?  1355 PRO   B CB  1 
ATOM   24720 C  CG  . PRO   B 1 1357 ? 7.50300    17.50000  -1.92000  1.000 88.92573  ?  1355 PRO   B CG  1 
ATOM   24721 C  CD  . PRO   B 1 1357 ? 8.64600    16.70500  -1.37200  1.000 82.49221  ?  1355 PRO   B CD  1 
ATOM   24722 N  N   . LEU   B 1 1358 ? 10.83200   20.54700  -3.07800  1.000 75.17596  ?  1356 LEU   B N   1 
ATOM   24723 C  CA  . LEU   B 1 1358 ? 11.73600   21.64000  -2.74000  1.000 75.44233  ?  1356 LEU   B CA  1 
ATOM   24724 C  C   . LEU   B 1 1358 ? 10.97700   22.69600  -1.94400  1.000 64.03636  ?  1356 LEU   B C   1 
ATOM   24725 O  O   . LEU   B 1 1358 ? 9.95300    23.21200  -2.40500  1.000 74.57752  ?  1356 LEU   B O   1 
ATOM   24726 C  CB  . LEU   B 1 1358 ? 12.33600   22.23700  -4.01300  1.000 56.07642  ?  1356 LEU   B CB  1 
ATOM   24727 C  CG  . LEU   B 1 1358 ? 13.61200   23.08100  -3.92300  1.000 71.10328  ?  1356 LEU   B CG  1 
ATOM   24728 C  CD1 . LEU   B 1 1358 ? 14.30300   23.11800  -5.27400  1.000 65.68281  ?  1356 LEU   B CD1 1 
ATOM   24729 C  CD2 . LEU   B 1 1358 ? 13.32000   24.49700  -3.45200  1.000 60.45968  ?  1356 LEU   B CD2 1 
ATOM   24730 N  N   . VAL   B 1 1359 ? 11.47600   23.01900  -0.74800  1.000 63.19901  ?  1357 VAL   B N   1 
ATOM   24731 C  CA  . VAL   B 1 1359 ? 10.83300   23.99200  0.12700   1.000 75.11058  ?  1357 VAL   B CA  1 
ATOM   24732 C  C   . VAL   B 1 1359 ? 11.77100   25.10800  0.55900   1.000 78.55957  ?  1357 VAL   B C   1 
ATOM   24733 O  O   . VAL   B 1 1359 ? 11.35000   26.00100  1.29700   1.000 63.54521  ?  1357 VAL   B O   1 
ATOM   24734 C  CB  . VAL   B 1 1359 ? 10.21700   23.31300  1.36900   1.000 68.48865  ?  1357 VAL   B CB  1 
ATOM   24735 C  CG1 . VAL   B 1 1359 ? 9.46300    22.05500  0.97900   1.000 73.44398  ?  1357 VAL   B CG1 1 
ATOM   24736 C  CG2 . VAL   B 1 1359 ? 11.29100   23.00000  2.39800   1.000 59.72614  ?  1357 VAL   B CG2 1 
ATOM   24737 N  N   . ASN   B 1 1360 ? 13.02800   25.09600  0.12600   1.000 86.19358  ?  1358 ASN   B N   1 
ATOM   24738 C  CA  . ASN   B 1 1360 ? 14.01600   26.05800  0.59000   1.000 73.95160  ?  1358 ASN   B CA  1 
ATOM   24739 C  C   . ASN   B 1 1360 ? 14.21100   27.18600  -0.41700  1.000 66.05724  ?  1358 ASN   B C   1 
ATOM   24740 O  O   . ASN   B 1 1360 ? 14.04500   27.00700  -1.62600  1.000 66.24719  ?  1358 ASN   B O   1 
ATOM   24741 C  CB  . ASN   B 1 1360 ? 15.35900   25.37700  0.86200   1.000 61.48899  ?  1358 ASN   B CB  1 
ATOM   24742 C  CG  . ASN   B 1 1360 ? 15.38300   24.65000  2.19100   1.000 65.86236  ?  1358 ASN   B CG  1 
ATOM   24743 O  OD1 . ASN   B 1 1360 ? 15.90600   23.54100  2.29500   1.000 69.78957  ?  1358 ASN   B OD1 1 
ATOM   24744 N  ND2 . ASN   B 1 1360 ? 14.81100   25.27300  3.21600   1.000 57.25410  ?  1358 ASN   B ND2 1 
ATOM   24745 N  N   . GLN   B 1 1361 ? 14.57000   28.35100  0.10500   1.000 69.23455  ?  1359 GLN   B N   1 
ATOM   24746 C  CA  . GLN   B 1 1361 ? 14.87600   29.54500  -0.66200  1.000 76.05945  ?  1359 GLN   B CA  1 
ATOM   24747 C  C   . GLN   B 1 1361 ? 16.34200   29.91300  -0.47200  1.000 77.95563  ?  1359 GLN   B C   1 
ATOM   24748 O  O   . GLN   B 1 1361 ? 16.97300   29.49000  0.50500   1.000 80.93138  ?  1359 GLN   B O   1 
ATOM   24749 C  CB  . GLN   B 1 1361 ? 13.97700   30.71400  -0.23100  1.000 77.61704  ?  1359 GLN   B CB  1 
ATOM   24750 C  CG  . GLN   B 1 1361 ? 12.64000   30.76600  -0.95400  1.000 86.84513  ?  1359 GLN   B CG  1 
ATOM   24751 C  CD  . GLN   B 1 1361 ? 12.53600   31.94700  -1.90100  1.000 110.36001 ?  1359 GLN   B CD  1 
ATOM   24752 O  OE1 . GLN   B 1 1361 ? 12.51000   33.10000  -1.47000  1.000 116.10129 ?  1359 GLN   B OE1 1 
ATOM   24753 N  NE2 . GLN   B 1 1361 ? 12.48000   31.66500  -3.19800  1.000 105.33343 ?  1359 GLN   B NE2 1 
ATOM   24754 N  N   . PRO   B 1 1362 ? 16.92400   30.68600  -1.39500  1.000 81.53404  ?  1360 PRO   B N   1 
ATOM   24755 C  CA  . PRO   B 1 1362 ? 18.34900   31.03600  -1.26400  1.000 67.60385  ?  1360 PRO   B CA  1 
ATOM   24756 C  C   . PRO   B 1 1362 ? 18.70000   31.73000  0.04100   1.000 61.24032  ?  1360 PRO   B C   1 
ATOM   24757 O  O   . PRO   B 1 1362 ? 19.86000   31.66300  0.46600   1.000 66.45713  ?  1360 PRO   B O   1 
ATOM   24758 C  CB  . PRO   B 1 1362 ? 18.59500   31.95400  -2.46900  1.000 58.27713  ?  1360 PRO   B CB  1 
ATOM   24759 C  CG  . PRO   B 1 1362 ? 17.57500   31.53500  -3.46800  1.000 68.84498  ?  1360 PRO   B CG  1 
ATOM   24760 C  CD  . PRO   B 1 1362 ? 16.35800   31.15200  -2.67500  1.000 89.15491  ?  1360 PRO   B CD  1 
ATOM   24761 N  N   . GLY   B 1 1363 ? 17.74500   32.38600  0.69100   1.000 53.28247  ?  1361 GLY   B N   1 
ATOM   24762 C  CA  . GLY   B 1 1363 ? 17.99000   33.07700  1.93700   1.000 63.81286  ?  1361 GLY   B CA  1 
ATOM   24763 C  C   . GLY   B 1 1363 ? 17.70300   32.28100  3.19100   1.000 54.60528  ?  1361 GLY   B C   1 
ATOM   24764 O  O   . GLY   B 1 1363 ? 17.76500   32.84000  4.29000   1.000 45.41951  ?  1361 GLY   B O   1 
ATOM   24765 N  N   . ASP   B 1 1364 ? 17.39000   30.99500  3.06500   1.000 62.68699  ?  1362 ASP   B N   1 
ATOM   24766 C  CA  . ASP   B 1 1364 ? 17.09200   30.15700  4.21500   1.000 61.29220  ?  1362 ASP   B CA  1 
ATOM   24767 C  C   . ASP   B 1 1364 ? 18.36900   29.55600  4.78900   1.000 60.65168  ?  1362 ASP   B C   1 
ATOM   24768 O  O   . ASP   B 1 1364 ? 19.37000   29.38300  4.08800   1.000 69.54875  ?  1362 ASP   B O   1 
ATOM   24769 C  CB  . ASP   B 1 1364 ? 16.11500   29.04300  3.83400   1.000 58.79574  ?  1362 ASP   B CB  1 
ATOM   24770 C  CG  . ASP   B 1 1364 ? 14.69100   29.54200  3.69300   1.000 60.98414  ?  1362 ASP   B CG  1 
ATOM   24771 O  OD1 . ASP   B 1 1364 ? 14.27000   30.38000  4.51900   1.000 66.41878  ?  1362 ASP   B OD1 1 
ATOM   24772 O  OD2 . ASP   B 1 1364 ? 13.99400   29.10000  2.75700   1.000 67.77938  -1 1362 ASP   B OD2 1 
ATOM   24773 N  N   . LEU   B 1 1365 ? 18.32100   29.23700  6.08000   1.000 53.74749  ?  1363 LEU   B N   1 
ATOM   24774 C  CA  . LEU   B 1 1365 ? 19.49000   28.70500  6.76500   1.000 52.97555  ?  1363 LEU   B CA  1 
ATOM   24775 C  C   . LEU   B 1 1365 ? 19.85000   27.32300  6.23600   1.000 63.00240  ?  1363 LEU   B C   1 
ATOM   24776 O  O   . LEU   B 1 1365 ? 18.98400   26.46700  6.03700   1.000 62.63080  ?  1363 LEU   B O   1 
ATOM   24777 C  CB  . LEU   B 1 1365 ? 19.24100   28.64000  8.27200   1.000 44.50209  ?  1363 LEU   B CB  1 
ATOM   24778 C  CG  . LEU   B 1 1365 ? 19.12500   29.98300  8.99700   1.000 52.07305  ?  1363 LEU   B CG  1 
ATOM   24779 C  CD1 . LEU   B 1 1365 ? 19.16200   29.78300  10.50400  1.000 49.41000  ?  1363 LEU   B CD1 1 
ATOM   24780 C  CD2 . LEU   B 1 1365 ? 20.22500   30.93500  8.54900   1.000 61.58250  ?  1363 LEU   B CD2 1 
ATOM   24781 N  N   . VAL   B 1 1366 ? 21.14500   27.11200  6.00400   1.000 61.98884  ?  1364 VAL   B N   1 
ATOM   24782 C  CA  . VAL   B 1 1366 ? 21.64700   25.82100  5.56900   1.000 47.93204  ?  1364 VAL   B CA  1 
ATOM   24783 C  C   . VAL   B 1 1366 ? 22.40300   25.08900  6.67600   1.000 46.93417  ?  1364 VAL   B C   1 
ATOM   24784 O  O   . VAL   B 1 1366 ? 22.32700   23.85700  6.74800   1.000 51.93903  ?  1364 VAL   B O   1 
ATOM   24785 C  CB  . VAL   B 1 1366 ? 22.52600   25.97400  4.30800   1.000 52.22036  ?  1364 VAL   B CB  1 
ATOM   24786 C  CG1 . VAL   B 1 1366 ? 23.75400   26.82600  4.59700   1.000 56.75115  ?  1364 VAL   B CG1 1 
ATOM   24787 C  CG2 . VAL   B 1 1366 ? 22.92300   24.61500  3.75200   1.000 52.54544  ?  1364 VAL   B CG2 1 
ATOM   24788 N  N   . TYR   B 1 1367 ? 23.10700   25.80500  7.55200   1.000 43.31336  ?  1365 TYR   B N   1 
ATOM   24789 C  CA  . TYR   B 1 1367 ? 23.77100   25.18600  8.69100   1.000 47.89253  ?  1365 TYR   B CA  1 
ATOM   24790 C  C   . TYR   B 1 1367 ? 24.04500   26.25300  9.74100   1.000 46.17163  ?  1365 TYR   B C   1 
ATOM   24791 O  O   . TYR   B 1 1367 ? 24.04300   27.45200  9.45100   1.000 48.84525  ?  1365 TYR   B O   1 
ATOM   24792 C  CB  . TYR   B 1 1367 ? 25.07300   24.47500  8.28200   1.000 54.32355  ?  1365 TYR   B CB  1 
ATOM   24793 C  CG  . TYR   B 1 1367 ? 26.21600   25.38600  7.87000   1.000 48.38516  ?  1365 TYR   B CG  1 
ATOM   24794 C  CD1 . TYR   B 1 1367 ? 27.04000   25.97900  8.82200   1.000 44.19853  ?  1365 TYR   B CD1 1 
ATOM   24795 C  CD2 . TYR   B 1 1367 ? 26.49000   25.62900  6.52800   1.000 53.93966  ?  1365 TYR   B CD2 1 
ATOM   24796 C  CE1 . TYR   B 1 1367 ? 28.08300   26.80600  8.45100   1.000 50.12727  ?  1365 TYR   B CE1 1 
ATOM   24797 C  CE2 . TYR   B 1 1367 ? 27.53900   26.45300  6.14900   1.000 65.18843  ?  1365 TYR   B CE2 1 
ATOM   24798 C  CZ  . TYR   B 1 1367 ? 28.33200   27.03700  7.11600   1.000 63.07497  ?  1365 TYR   B CZ  1 
ATOM   24799 O  OH  . TYR   B 1 1367 ? 29.37700   27.85600  6.74900   1.000 46.56283  ?  1365 TYR   B OH  1 
ATOM   24800 N  N   . VAL   B 1 1368 ? 24.28800   25.79400  10.96500  1.000 39.43089  ?  1366 VAL   B N   1 
ATOM   24801 C  CA  . VAL   B 1 1368 ? 24.64500   26.65700  12.08600  1.000 45.76288  ?  1366 VAL   B CA  1 
ATOM   24802 C  C   . VAL   B 1 1368 ? 25.90300   26.08000  12.71800  1.000 48.86560  ?  1366 VAL   B C   1 
ATOM   24803 O  O   . VAL   B 1 1368 ? 25.87000   24.97800  13.27800  1.000 56.37096  ?  1366 VAL   B O   1 
ATOM   24804 C  CB  . VAL   B 1 1368 ? 23.51700   26.76900  13.12100  1.000 38.50969  ?  1366 VAL   B CB  1 
ATOM   24805 C  CG1 . VAL   B 1 1368 ? 24.02300   27.44500  14.38900  1.000 44.74912  ?  1366 VAL   B CG1 1 
ATOM   24806 C  CG2 . VAL   B 1 1368 ? 22.34600   27.53900  12.54000  1.000 39.26401  ?  1366 VAL   B CG2 1 
ATOM   24807 N  N   . MET   B 1 1369 ? 27.00900   26.81200  12.62300  1.000 54.95589  ?  1367 MET   B N   1 
ATOM   24808 C  CA  . MET   B 1 1369 ? 28.27500   26.39700  13.21400  1.000 58.63785  ?  1367 MET   B CA  1 
ATOM   24809 C  C   . MET   B 1 1369 ? 28.51000   27.14200  14.51900  1.000 59.58619  ?  1367 MET   B C   1 
ATOM   24810 O  O   . MET   B 1 1369 ? 28.48500   28.37700  14.54700  1.000 63.77481  ?  1367 MET   B O   1 
ATOM   24811 C  CB  . MET   B 1 1369 ? 29.44800   26.65600  12.26700  1.000 51.21273  ?  1367 MET   B CB  1 
ATOM   24812 C  CG  . MET   B 1 1369 ? 29.59800   25.66100  11.12500  1.000 68.52672  ?  1367 MET   B CG  1 
ATOM   24813 S  SD  . MET   B 1 1369 ? 30.24600   24.03300  11.55400  1.000 44.05189  ?  1367 MET   B SD  1 
ATOM   24814 C  CE  . MET   B 1 1369 ? 31.05000   24.36700  13.11600  1.000 48.68737  ?  1367 MET   B CE  1 
ATOM   24815 N  N   . TYR   B 1 1370 ? 28.75100   26.39500  15.59100  1.000 53.38571  ?  1368 TYR   B N   1 
ATOM   24816 C  CA  . TYR   B 1 1370 ? 29.10900   27.00700  16.86200  1.000 55.45385  ?  1368 TYR   B CA  1 
ATOM   24817 C  C   . TYR   B 1 1370 ? 30.60100   27.31400  16.90300  1.000 55.79978  ?  1368 TYR   B C   1 
ATOM   24818 O  O   . TYR   B 1 1370 ? 31.41900   26.56300  16.36500  1.000 59.41381  ?  1368 TYR   B O   1 
ATOM   24819 C  CB  . TYR   B 1 1370 ? 28.71300   26.10000  18.02700  1.000 58.30593  ?  1368 TYR   B CB  1 
ATOM   24820 C  CG  . TYR   B 1 1370 ? 27.34300   26.42100  18.58500  1.000 58.36293  ?  1368 TYR   B CG  1 
ATOM   24821 C  CD1 . TYR   B 1 1370 ? 26.21000   26.31600  17.79200  1.000 61.20459  ?  1368 TYR   B CD1 1 
ATOM   24822 C  CD2 . TYR   B 1 1370 ? 27.18500   26.83800  19.90200  1.000 63.04631  ?  1368 TYR   B CD2 1 
ATOM   24823 C  CE1 . TYR   B 1 1370 ? 24.95600   26.61300  18.29200  1.000 73.74184  ?  1368 TYR   B CE1 1 
ATOM   24824 C  CE2 . TYR   B 1 1370 ? 25.93300   27.13600  20.41200  1.000 70.18774  ?  1368 TYR   B CE2 1 
ATOM   24825 C  CZ  . TYR   B 1 1370 ? 24.82200   27.02200  19.60200  1.000 72.28244  ?  1368 TYR   B CZ  1 
ATOM   24826 O  OH  . TYR   B 1 1370 ? 23.57600   27.31800  20.10500  1.000 62.20221  ?  1368 TYR   B OH  1 
ATOM   24827 N  N   . THR   B 1 1371 ? 30.94800   28.43300  17.53900  1.000 69.04375  ?  1369 THR   B N   1 
ATOM   24828 C  CA  . THR   B 1 1371 ? 32.32300   28.90800  17.55600  1.000 75.37268  ?  1369 THR   B CA  1 
ATOM   24829 C  C   . THR   B 1 1371 ? 33.16000   28.12000  18.55900  1.000 86.96910  ?  1369 THR   B C   1 
ATOM   24830 O  O   . THR   B 1 1371 ? 32.65600   27.32600  19.35700  1.000 95.72740  ?  1369 THR   B O   1 
ATOM   24831 C  CB  . THR   B 1 1371 ? 32.40200   30.40300  17.89000  1.000 71.29375  ?  1369 THR   B CB  1 
ATOM   24832 O  OG1 . THR   B 1 1371 ? 32.19000   30.60500  19.29400  1.000 79.91437  ?  1369 THR   B OG1 1 
ATOM   24833 C  CG2 . THR   B 1 1371 ? 31.37500   31.19400  17.09900  1.000 62.31387  ?  1369 THR   B CG2 1 
ATOM   24834 N  N   . SER   B 1 1372 ? 34.46500   28.36200  18.50900  1.000 91.92404  ?  1370 SER   B N   1 
ATOM   24835 C  CA  . SER   B 1 1372 ? 35.39900   27.72400  19.41800  1.000 86.48462  ?  1370 SER   B CA  1 
ATOM   24836 C  C   . SER   B 1 1372 ? 35.91100   28.72600  20.45300  1.000 93.77982  ?  1370 SER   B C   1 
ATOM   24837 O  O   . SER   B 1 1372 ? 35.65500   29.92700  20.35100  1.000 91.36319  ?  1370 SER   B O   1 
ATOM   24838 C  CB  . SER   B 1 1372 ? 36.56600   27.11500  18.64000  1.000 84.25004  ?  1370 SER   B CB  1 
ATOM   24839 O  OG  . SER   B 1 1372 ? 36.28600   27.06500  17.24800  1.000 81.25159  ?  1370 SER   B OG  1 
ATOM   24840 N  N   . THR   B 1 1375 ? 38.45300   31.79900  24.98800  1.000 109.00143 ?  1373 THR   B N   1 
ATOM   24841 C  CA  . THR   B 1 1375 ? 37.31000   32.69000  24.81000  1.000 113.02683 ?  1373 THR   B CA  1 
ATOM   24842 C  C   . THR   B 1 1375 ? 36.24700   32.45600  25.88300  1.000 114.88647 ?  1373 THR   B C   1 
ATOM   24843 O  O   . THR   B 1 1375 ? 36.53200   32.54300  27.07800  1.000 100.24920 ?  1373 THR   B O   1 
ATOM   24844 C  CB  . THR   B 1 1375 ? 36.67900   32.52700  23.40700  1.000 102.29417 ?  1373 THR   B CB  1 
ATOM   24845 O  OG1 . THR   B 1 1375 ? 36.35200   31.15000  23.16800  1.000 115.28595 ?  1373 THR   B OG1 1 
ATOM   24846 C  CG2 . THR   B 1 1375 ? 37.64300   33.00600  22.33600  1.000 87.43486  ?  1373 THR   B CG2 1 
ATOM   24847 N  N   . GLY   B 1 1376 ? 35.02600   32.17300  25.46000  1.000 106.79998 ?  1374 GLY   B N   1 
ATOM   24848 C  CA  . GLY   B 1 1376 ? 33.92300   31.96000  26.38000  1.000 91.76817  ?  1374 GLY   B CA  1 
ATOM   24849 C  C   . GLY   B 1 1376 ? 32.86500   31.06400  25.78400  1.000 92.95709  ?  1374 GLY   B C   1 
ATOM   24850 O  O   . GLY   B 1 1376 ? 33.15900   30.19800  24.95400  1.000 91.89601  ?  1374 GLY   B O   1 
ATOM   24851 N  N   . LYS   B 1 1377 ? 31.62600   31.27300  26.21800  1.000 102.36070 ?  1375 LYS   B N   1 
ATOM   24852 C  CA  . LYS   B 1 1377 ? 30.48700   30.48200  25.78300  1.000 92.89065  ?  1375 LYS   B CA  1 
ATOM   24853 C  C   . LYS   B 1 1377 ? 30.37500   30.50600  24.25900  1.000 91.23921  ?  1375 LYS   B C   1 
ATOM   24854 O  O   . LYS   B 1 1377 ? 30.30000   31.59500  23.66700  1.000 97.55540  ?  1375 LYS   B O   1 
ATOM   24855 C  CB  . LYS   B 1 1377 ? 29.21200   31.02700  26.42200  1.000 75.29078  ?  1375 LYS   B CB  1 
ATOM   24856 N  N   . PRO   B 1 1378 ? 30.39000   29.35000  23.59200  1.000 78.58380  ?  1376 PRO   B N   1 
ATOM   24857 C  CA  . PRO   B 1 1378 ? 30.31400   29.33800  22.12300  1.000 72.07667  ?  1376 PRO   B CA  1 
ATOM   24858 C  C   . PRO   B 1 1378 ? 29.04800   30.00300  21.60200  1.000 74.37595  ?  1376 PRO   B C   1 
ATOM   24859 O  O   . PRO   B 1 1378 ? 28.04800   30.13200  22.30600  1.000 87.28093  ?  1376 PRO   B O   1 
ATOM   24860 C  CB  . PRO   B 1 1378 ? 30.34800   27.84300  21.77900  1.000 75.37466  ?  1376 PRO   B CB  1 
ATOM   24861 C  CG  . PRO   B 1 1378 ? 31.06800   27.21200  22.93100  1.000 82.97423  ?  1376 PRO   B CG  1 
ATOM   24862 C  CD  . PRO   B 1 1378 ? 30.70500   28.02100  24.14600  1.000 68.06481  ?  1376 PRO   B CD  1 
ATOM   24863 N  N   . LYS   B 1 1379 ? 29.11000   30.43900  20.34200  1.000 62.56179  ?  1377 LYS   B N   1 
ATOM   24864 C  CA  . LYS   B 1 1379 ? 27.99800   31.11100  19.68800  1.000 66.54843  ?  1377 LYS   B CA  1 
ATOM   24865 C  C   . LYS   B 1 1379 ? 27.69500   30.42600  18.36500  1.000 52.79772  ?  1377 LYS   B C   1 
ATOM   24866 O  O   . LYS   B 1 1379 ? 28.59600   29.90800  17.70300  1.000 61.64308  ?  1377 LYS   B O   1 
ATOM   24867 C  CB  . LYS   B 1 1379 ? 28.31100   32.60300  19.45600  1.000 57.86923  ?  1377 LYS   B CB  1 
ATOM   24868 N  N   . GLY   B 1 1380 ? 26.42300   30.41100  17.98100  1.000 46.98209  ?  1378 GLY   B N   1 
ATOM   24869 C  CA  . GLY   B 1 1380 ? 26.00500   29.74800  16.76400  1.000 42.75235  ?  1378 GLY   B CA  1 
ATOM   24870 C  C   . GLY   B 1 1380 ? 25.93100   30.69100  15.57900  1.000 43.43830  ?  1378 GLY   B C   1 
ATOM   24871 O  O   . GLY   B 1 1380 ? 25.10900   31.61100  15.55900  1.000 55.87558  ?  1378 GLY   B O   1 
ATOM   24872 N  N   . VAL   B 1 1381 ? 26.77900   30.44700  14.57900  1.000 52.18334  ?  1379 VAL   B N   1 
ATOM   24873 C  CA  . VAL   B 1 1381 ? 26.81900   31.27600  13.37700  1.000 54.71161  ?  1379 VAL   B CA  1 
ATOM   24874 C  C   . VAL   B 1 1381 ? 25.79400   30.74400  12.38100  1.000 43.82413  ?  1379 VAL   B C   1 
ATOM   24875 O  O   . VAL   B 1 1381 ? 25.92700   29.62200  11.88100  1.000 49.89178  ?  1379 VAL   B O   1 
ATOM   24876 C  CB  . VAL   B 1 1381 ? 28.22600   31.29400  12.76600  1.000 49.56478  ?  1379 VAL   B CB  1 
ATOM   24877 C  CG1 . VAL   B 1 1381 ? 28.23900   32.13300  11.49200  1.000 48.91339  ?  1379 VAL   B CG1 1 
ATOM   24878 C  CG2 . VAL   B 1 1381 ? 29.24000   31.82500  13.76600  1.000 43.19216  ?  1379 VAL   B CG2 1 
ATOM   24879 N  N   . MET   B 1 1382 ? 24.77600   31.54700  12.08800  1.000 41.74556  ?  1380 MET   B N   1 
ATOM   24880 C  CA  . MET   B 1 1382 ? 23.70000   31.13700  11.19000  1.000 54.72685  ?  1380 MET   B CA  1 
ATOM   24881 C  C   . MET   B 1 1382 ? 24.08100   31.51300  9.76100   1.000 52.14213  ?  1380 MET   B C   1 
ATOM   24882 O  O   . MET   B 1 1382 ? 24.18700   32.69800  9.42900   1.000 61.71460  ?  1380 MET   B O   1 
ATOM   24883 C  CB  . MET   B 1 1382 ? 22.38000   31.78300  11.60000  1.000 57.95693  ?  1380 MET   B CB  1 
ATOM   24884 C  CG  . MET   B 1 1382 ? 22.15200   31.81200  13.10500  1.000 55.08645  ?  1380 MET   B CG  1 
ATOM   24885 S  SD  . MET   B 1 1382 ? 20.56900   32.54400  13.55800  1.000 69.28987  ?  1380 MET   B SD  1 
ATOM   24886 C  CE  . MET   B 1 1382 ? 20.28600   33.61800  12.15800  1.000 58.75298  ?  1380 MET   B CE  1 
ATOM   24887 N  N   . ILE   B 1 1383 ? 24.28200   30.50400  8.91800   1.000 51.00959  ?  1381 ILE   B N   1 
ATOM   24888 C  CA  . ILE   B 1 1383 ? 24.69200   30.68900  7.53200   1.000 53.65403  ?  1381 ILE   B CA  1 
ATOM   24889 C  C   . ILE   B 1 1383 ? 23.52700   30.32400  6.62300   1.000 62.01253  ?  1381 ILE   B C   1 
ATOM   24890 O  O   . ILE   B 1 1383 ? 22.85200   29.31000  6.83700   1.000 56.79216  ?  1381 ILE   B O   1 
ATOM   24891 C  CB  . ILE   B 1 1383 ? 25.93800   29.84200  7.20100   1.000 35.44208  ?  1381 ILE   B CB  1 
ATOM   24892 C  CG1 . ILE   B 1 1383 ? 27.12700   30.29200  8.05300   1.000 48.76620  ?  1381 ILE   B CG1 1 
ATOM   24893 C  CG2 . ILE   B 1 1383 ? 26.27700   29.93000  5.71700   1.000 51.53250  ?  1381 ILE   B CG2 1 
ATOM   24894 C  CD1 . ILE   B 1 1383 ? 27.62500   31.68100  7.72000   1.000 49.99356  ?  1381 ILE   B CD1 1 
ATOM   24895 N  N   . GLU   B 1 1384 ? 23.29000   31.15300  5.61200   1.000 58.57792  ?  1382 GLU   B N   1 
ATOM   24896 C  CA  . GLU   B 1 1384 ? 22.21400   30.92000  4.66300   1.000 57.57848  ?  1382 GLU   B CA  1 
ATOM   24897 C  C   . GLU   B 1 1384 ? 22.71100   30.09700  3.47600   1.000 55.69634  ?  1382 GLU   B C   1 
ATOM   24898 O  O   . GLU   B 1 1384 ? 23.90500   29.82300  3.32800   1.000 69.38456  ?  1382 GLU   B O   1 
ATOM   24899 C  CB  . GLU   B 1 1384 ? 21.62500   32.24900  4.18900   1.000 52.30903  ?  1382 GLU   B CB  1 
ATOM   24900 C  CG  . GLU   B 1 1384 ? 21.05000   33.09800  5.31000   1.000 50.33685  ?  1382 GLU   B CG  1 
ATOM   24901 C  CD  . GLU   B 1 1384 ? 20.45900   34.40000  4.81200   1.000 64.77693  ?  1382 GLU   B CD  1 
ATOM   24902 O  OE1 . GLU   B 1 1384 ? 20.73500   34.77700  3.65200   1.000 65.49224  ?  1382 GLU   B OE1 1 
ATOM   24903 O  OE2 . GLU   B 1 1384 ? 19.71500   35.04600  5.57900   1.000 62.95754  -1 1382 GLU   B OE2 1 
ATOM   24904 N  N   . HIS   B 1 1385 ? 21.76800   29.70100  2.61800   1.000 53.65076  ?  1383 HIS   B N   1 
ATOM   24905 C  CA  . HIS   B 1 1385 ? 22.10900   28.86800  1.46800   1.000 59.39296  ?  1383 HIS   B CA  1 
ATOM   24906 C  C   . HIS   B 1 1385 ? 22.94200   29.63800  0.45200   1.000 50.78715  ?  1383 HIS   B C   1 
ATOM   24907 O  O   . HIS   B 1 1385 ? 23.98800   29.15600  -0.00100  1.000 52.25801  ?  1383 HIS   B O   1 
ATOM   24908 C  CB  . HIS   B 1 1385 ? 20.83700   28.32300  0.81500   1.000 65.22883  ?  1383 HIS   B CB  1 
ATOM   24909 C  CG  . HIS   B 1 1385 ? 20.47800   26.93800  1.25400   1.000 64.67944  ?  1383 HIS   B CG  1 
ATOM   24910 N  ND1 . HIS   B 1 1385 ? 19.68100   26.68700  2.35100   1.000 63.91184  ?  1383 HIS   B ND1 1 
ATOM   24911 C  CD2 . HIS   B 1 1385 ? 20.81100   25.72800  0.74600   1.000 57.85836  ?  1383 HIS   B CD2 1 
ATOM   24912 C  CE1 . HIS   B 1 1385 ? 19.53600   25.38200  2.49700   1.000 66.00817  ?  1383 HIS   B CE1 1 
ATOM   24913 N  NE2 . HIS   B 1 1385 ? 20.21200   24.77700  1.53600   1.000 68.12513  ?  1383 HIS   B NE2 1 
ATOM   24914 N  N   . GLY   B 1 1386 ? 22.48900   30.83600  0.07300   1.000 45.85813  ?  1384 GLY   B N   1 
ATOM   24915 C  CA  . GLY   B 1 1386 ? 23.22200   31.62200  -0.90700  1.000 56.66172  ?  1384 GLY   B CA  1 
ATOM   24916 C  C   . GLY   B 1 1386 ? 24.62100   31.98400  -0.45400  1.000 66.81932  ?  1384 GLY   B C   1 
ATOM   24917 O  O   . GLY   B 1 1386 ? 25.52900   32.12100  -1.28000  1.000 65.69180  ?  1384 GLY   B O   1 
ATOM   24918 N  N   . ALA   B 1 1387 ? 24.81700   32.14500  0.85600   1.000 56.86752  ?  1385 ALA   B N   1 
ATOM   24919 C  CA  . ALA   B 1 1387 ? 26.15600   32.38500  1.38100   1.000 50.70420  ?  1385 ALA   B CA  1 
ATOM   24920 C  C   . ALA   B 1 1387 ? 27.07600   31.20500  1.09400   1.000 60.29572  ?  1385 ALA   B C   1 
ATOM   24921 O  O   . ALA   B 1 1387 ? 28.23300   31.39000  0.69900   1.000 69.19675  ?  1385 ALA   B O   1 
ATOM   24922 C  CB  . ALA   B 1 1387 ? 26.08700   32.65800  2.88400   1.000 64.81314  ?  1385 ALA   B CB  1 
ATOM   24923 N  N   . LEU   B 1 1388 ? 26.57400   29.98300  1.28500   1.000 57.86203  ?  1386 LEU   B N   1 
ATOM   24924 C  CA  . LEU   B 1 1388 ? 27.37200   28.79800  0.99200   1.000 51.87217  ?  1386 LEU   B CA  1 
ATOM   24925 C  C   . LEU   B 1 1388 ? 27.61200   28.64900  -0.50500  1.000 62.23984  ?  1386 LEU   B C   1 
ATOM   24926 O  O   . LEU   B 1 1388 ? 28.69000   28.21700  -0.92800  1.000 61.53582  ?  1386 LEU   B O   1 
ATOM   24927 C  CB  . LEU   B 1 1388 ? 26.68000   27.55500  1.55100   1.000 50.60863  ?  1386 LEU   B CB  1 
ATOM   24928 C  CG  . LEU   B 1 1388 ? 27.34000   26.20800  1.25700   1.000 53.48375  ?  1386 LEU   B CG  1 
ATOM   24929 C  CD1 . LEU   B 1 1388 ? 28.70900   26.13100  1.91100   1.000 51.08090  ?  1386 LEU   B CD1 1 
ATOM   24930 C  CD2 . LEU   B 1 1388 ? 26.45200   25.06100  1.71500   1.000 49.67545  ?  1386 LEU   B CD2 1 
ATOM   24931 N  N   . LEU   B 1 1389 ? 26.61800   29.00700  -1.32200  1.000 54.03773  ?  1387 LEU   B N   1 
ATOM   24932 C  CA  . LEU   B 1 1389 ? 26.75000   28.85300  -2.76700  1.000 50.34633  ?  1387 LEU   B CA  1 
ATOM   24933 C  C   . LEU   B 1 1389 ? 27.82200   29.76700  -3.34600  1.000 54.30407  ?  1387 LEU   B C   1 
ATOM   24934 O  O   . LEU   B 1 1389 ? 28.47200   29.40500  -4.33300  1.000 51.11010  ?  1387 LEU   B O   1 
ATOM   24935 C  CB  . LEU   B 1 1389 ? 25.40800   29.12500  -3.44600  1.000 52.06277  ?  1387 LEU   B CB  1 
ATOM   24936 C  CG  . LEU   B 1 1389 ? 24.56300   27.89900  -3.78300  1.000 52.43581  ?  1387 LEU   B CG  1 
ATOM   24937 C  CD1 . LEU   B 1 1389 ? 23.18200   28.31900  -4.25700  1.000 53.99558  ?  1387 LEU   B CD1 1 
ATOM   24938 C  CD2 . LEU   B 1 1389 ? 25.26500   27.06500  -4.84000  1.000 48.76679  ?  1387 LEU   B CD2 1 
ATOM   24939 N  N   . ASN   B 1 1390 ? 28.02400   30.94400  -2.75200  1.000 53.02514  ?  1388 ASN   B N   1 
ATOM   24940 C  CA  . ASN   B 1 1390 ? 28.97200   31.89700  -3.31800  1.000 54.26216  ?  1388 ASN   B CA  1 
ATOM   24941 C  C   . ASN   B 1 1390 ? 30.41300   31.45500  -3.08600  1.000 52.98276  ?  1388 ASN   B C   1 
ATOM   24942 O  O   . ASN   B 1 1390 ? 31.24200   31.52500  -4.00000  1.000 52.83443  ?  1388 ASN   B O   1 
ATOM   24943 C  CB  . ASN   B 1 1390 ? 28.72700   33.28700  -2.73400  1.000 52.79182  ?  1388 ASN   B CB  1 
ATOM   24944 C  CG  . ASN   B 1 1390 ? 29.51800   34.36500  -3.44800  1.000 62.40826  ?  1388 ASN   B CG  1 
ATOM   24945 O  OD1 . ASN   B 1 1390 ? 29.23100   34.70000  -4.59700  1.000 53.20341  ?  1388 ASN   B OD1 1 
ATOM   24946 N  ND2 . ASN   B 1 1390 ? 30.51500   34.91800  -2.76800  1.000 66.00867  ?  1388 ASN   B ND2 1 
ATOM   24947 N  N   . VAL   B 1 1391 ? 30.73100   30.99600  -1.87300  1.000 43.74567  ?  1389 VAL   B N   1 
ATOM   24948 C  CA  . VAL   B 1 1391 ? 32.08300   30.51200  -1.61000  1.000 52.80701  ?  1389 VAL   B CA  1 
ATOM   24949 C  C   . VAL   B 1 1391 ? 32.34200   29.21000  -2.35900  1.000 63.10156  ?  1389 VAL   B C   1 
ATOM   24950 O  O   . VAL   B 1 1391 ? 33.46200   28.96500  -2.82200  1.000 54.36798  ?  1389 VAL   B O   1 
ATOM   24951 C  CB  . VAL   B 1 1391 ? 32.31200   30.36200  -0.09200  1.000 45.95111  ?  1389 VAL   B CB  1 
ATOM   24952 C  CG1 . VAL   B 1 1391 ? 31.26500   29.45200  0.52500   1.000 50.65026  ?  1389 VAL   B CG1 1 
ATOM   24953 C  CG2 . VAL   B 1 1391 ? 33.71500   29.84100  0.19500   1.000 53.39479  ?  1389 VAL   B CG2 1 
ATOM   24954 N  N   . LEU   B 1 1392 ? 31.31900   28.36400  -2.51300  1.000 62.18833  ?  1390 LEU   B N   1 
ATOM   24955 C  CA  . LEU   B 1 1392 ? 31.50500   27.11400  -3.24300  1.000 60.65516  ?  1390 LEU   B CA  1 
ATOM   24956 C  C   . LEU   B 1 1392 ? 31.71400   27.36400  -4.73100  1.000 54.61902  ?  1390 LEU   B C   1 
ATOM   24957 O  O   . LEU   B 1 1392 ? 32.59800   26.75700  -5.34800  1.000 64.83522  ?  1390 LEU   B O   1 
ATOM   24958 C  CB  . LEU   B 1 1392 ? 30.30900   26.18900  -3.01800  1.000 56.05887  ?  1390 LEU   B CB  1 
ATOM   24959 C  CG  . LEU   B 1 1392 ? 30.20500   25.51300  -1.65100  1.000 56.99970  ?  1390 LEU   B CG  1 
ATOM   24960 C  CD1 . LEU   B 1 1392 ? 28.99600   24.59600  -1.61600  1.000 50.78539  ?  1390 LEU   B CD1 1 
ATOM   24961 C  CD2 . LEU   B 1 1392 ? 31.47900   24.74700  -1.32100  1.000 48.22957  ?  1390 LEU   B CD2 1 
ATOM   24962 N  N   . HIS   B 1 1393 ? 30.90900   28.24700  -5.32700  1.000 49.82741  ?  1391 HIS   B N   1 
ATOM   24963 C  CA  . HIS   B 1 1393 ? 31.08900   28.56800  -6.74000  1.000 73.68834  ?  1391 HIS   B CA  1 
ATOM   24964 C  C   . HIS   B 1 1393 ? 32.44000   29.22700  -6.98500  1.000 68.45423  ?  1391 HIS   B C   1 
ATOM   24965 O  O   . HIS   B 1 1393 ? 33.12100   28.91700  -7.97000  1.000 63.42590  ?  1391 HIS   B O   1 
ATOM   24966 C  CB  . HIS   B 1 1393 ? 29.95800   29.47600  -7.22300  1.000 56.79651  ?  1391 HIS   B CB  1 
ATOM   24967 C  CG  . HIS   B 1 1393 ? 28.72200   28.74100  -7.64000  1.000 67.38896  ?  1391 HIS   B CG  1 
ATOM   24968 N  ND1 . HIS   B 1 1393 ? 28.76000   27.58900  -8.39700  1.000 62.95567  ?  1391 HIS   B ND1 1 
ATOM   24969 C  CD2 . HIS   B 1 1393 ? 27.41200   28.99600  -7.41000  1.000 74.24643  ?  1391 HIS   B CD2 1 
ATOM   24970 C  CE1 . HIS   B 1 1393 ? 27.52700   27.16600  -8.61200  1.000 72.83240  ?  1391 HIS   B CE1 1 
ATOM   24971 N  NE2 . HIS   B 1 1393 ? 26.69000   28.00200  -8.02400  1.000 70.60306  ?  1391 HIS   B NE2 1 
ATOM   24972 N  N   . GLY   B 1 1394 ? 32.84500   30.13700  -6.09700  1.000 60.81055  ?  1392 GLY   B N   1 
ATOM   24973 C  CA  . GLY   B 1 1394 ? 34.11500   30.82100  -6.28000  1.000 63.72222  ?  1392 GLY   B CA  1 
ATOM   24974 C  C   . GLY   B 1 1394 ? 35.30900   29.90100  -6.11200  1.000 60.69741  ?  1392 GLY   B C   1 
ATOM   24975 O  O   . GLY   B 1 1394 ? 36.25700   29.95200  -6.90000  1.000 59.70635  ?  1392 GLY   B O   1 
ATOM   24976 N  N   . MET   B 1 1395 ? 35.28400   29.05100  -5.08000  1.000 52.13015  ?  1393 MET   B N   1 
ATOM   24977 C  CA  . MET   B 1 1395 ? 36.36400   28.08700  -4.89500  1.000 54.97576  ?  1393 MET   B CA  1 
ATOM   24978 C  C   . MET   B 1 1395 ? 36.41000   27.07500  -6.03400  1.000 63.51554  ?  1393 MET   B C   1 
ATOM   24979 O  O   . MET   B 1 1395 ? 37.48400   26.55000  -6.35000  1.000 59.79306  ?  1393 MET   B O   1 
ATOM   24980 C  CB  . MET   B 1 1395 ? 36.21400   27.37400  -3.55100  1.000 42.87791  ?  1393 MET   B CB  1 
ATOM   24981 C  CG  . MET   B 1 1395 ? 36.48900   28.25800  -2.34100  1.000 53.66252  ?  1393 MET   B CG  1 
ATOM   24982 S  SD  . MET   B 1 1395 ? 38.22300   28.72300  -2.16000  1.000 60.80003  ?  1393 MET   B SD  1 
ATOM   24983 C  CE  . MET   B 1 1395 ? 38.93100   27.19700  -1.54800  1.000 44.28961  ?  1393 MET   B CE  1 
ATOM   24984 N  N   . GLN   B 1 1396 ? 35.26300   26.78900  -6.65700  1.000 67.16903  ?  1394 GLN   B N   1 
ATOM   24985 C  CA  . GLN   B 1 1396 ? 35.26200   25.96200  -7.85800  1.000 69.75353  ?  1394 GLN   B CA  1 
ATOM   24986 C  C   . GLN   B 1 1396 ? 35.82800   26.71900  -9.05200  1.000 73.64646  ?  1394 GLN   B C   1 
ATOM   24987 O  O   . GLN   B 1 1396 ? 36.48700   26.12300  -9.91000  1.000 82.34475  ?  1394 GLN   B O   1 
ATOM   24988 C  CB  . GLN   B 1 1396 ? 33.84300   25.47500  -8.16000  1.000 74.47578  ?  1394 GLN   B CB  1 
ATOM   24989 C  CG  . GLN   B 1 1396 ? 33.74000   24.51700  -9.34100  1.000 69.59608  ?  1394 GLN   B CG  1 
ATOM   24990 C  CD  . GLN   B 1 1396 ? 34.21900   23.11700  -9.00500  1.000 74.40399  ?  1394 GLN   B CD  1 
ATOM   24991 O  OE1 . GLN   B 1 1396 ? 34.33700   22.75200  -7.83400  1.000 68.50742  ?  1394 GLN   B OE1 1 
ATOM   24992 N  NE2 . GLN   B 1 1396 ? 34.49200   22.32300  -10.03400 1.000 77.31381  ?  1394 GLN   B NE2 1 
ATOM   24993 N  N   . ASP   B 1 1397 ? 35.58700   28.03000  -9.12500  1.000 70.09992  ?  1395 ASP   B N   1 
ATOM   24994 C  CA  . ASP   B 1 1397 ? 36.12900   28.81700  -10.22500 1.000 69.82046  ?  1395 ASP   B CA  1 
ATOM   24995 C  C   . ASP   B 1 1397 ? 37.63800   28.98600  -10.09900 1.000 68.06012  ?  1395 ASP   B C   1 
ATOM   24996 O  O   . ASP   B 1 1397 ? 38.33500   29.09100  -11.11400 1.000 70.50651  ?  1395 ASP   B O   1 
ATOM   24997 C  CB  . ASP   B 1 1397 ? 35.42700   30.17500  -10.27800 1.000 66.93024  ?  1395 ASP   B CB  1 
ATOM   24998 C  CG  . ASP   B 1 1397 ? 35.16800   30.64400  -11.69700 1.000 94.24826  ?  1395 ASP   B CG  1 
ATOM   24999 O  OD1 . ASP   B 1 1397 ? 34.58100   29.86700  -12.48100 1.000 98.90778  ?  1395 ASP   B OD1 1 
ATOM   25000 O  OD2 . ASP   B 1 1397 ? 35.56100   31.78200  -12.03100 1.000 105.94593 -1 1395 ASP   B OD2 1 
ATOM   25001 N  N   . GLU   B 1 1398 ? 38.15900   28.99900  -8.87200  1.000 63.95690  ?  1396 GLU   B N   1 
ATOM   25002 C  CA  . GLU   B 1 1398 ? 39.59200   29.12500  -8.63200  1.000 68.82903  ?  1396 GLU   B CA  1 
ATOM   25003 C  C   . GLU   B 1 1398 ? 40.28600   27.76700  -8.58200  1.000 73.22807  ?  1396 GLU   B C   1 
ATOM   25004 O  O   . GLU   B 1 1398 ? 41.28700   27.55300  -9.27300  1.000 79.63772  ?  1396 GLU   B O   1 
ATOM   25005 C  CB  . GLU   B 1 1398 ? 39.84000   29.89000  -7.32800  1.000 76.33688  ?  1396 GLU   B CB  1 
ATOM   25006 C  CG  . GLU   B 1 1398 ? 39.47500   31.36200  -7.39400  1.000 84.87416  ?  1396 GLU   B CG  1 
ATOM   25007 C  CD  . GLU   B 1 1398 ? 40.39300   32.14700  -8.31000  1.000 99.56484  ?  1396 GLU   B CD  1 
ATOM   25008 O  OE1 . GLU   B 1 1398 ? 41.61800   31.90300  -8.27600  1.000 95.57980  ?  1396 GLU   B OE1 1 
ATOM   25009 O  OE2 . GLU   B 1 1398 ? 39.89000   33.00100  -9.07000  1.000 104.18871 -1 1396 GLU   B OE2 1 
ATOM   25010 N  N   . TYR   B 1 1399 ? 39.76800   26.84400  -7.76900  1.000 76.28395  ?  1397 TYR   B N   1 
ATOM   25011 C  CA  . TYR   B 1 1399 ? 40.33700   25.50900  -7.59500  1.000 74.00630  ?  1397 TYR   B CA  1 
ATOM   25012 C  C   . TYR   B 1 1399 ? 39.25500   24.49400  -7.94900  1.000 74.72579  ?  1397 TYR   B C   1 
ATOM   25013 O  O   . TYR   B 1 1399 ? 38.54800   23.98600  -7.06500  1.000 71.23754  ?  1397 TYR   B O   1 
ATOM   25014 C  CB  . TYR   B 1 1399 ? 40.85600   25.32000  -6.17100  1.000 65.35817  ?  1397 TYR   B CB  1 
ATOM   25015 C  CG  . TYR   B 1 1399 ? 41.55200   26.55000  -5.62800  1.000 74.44253  ?  1397 TYR   B CG  1 
ATOM   25016 C  CD1 . TYR   B 1 1399 ? 42.81200   26.91500  -6.08300  1.000 84.79517  ?  1397 TYR   B CD1 1 
ATOM   25017 C  CD2 . TYR   B 1 1399 ? 40.94500   27.35100  -4.66900  1.000 68.30660  ?  1397 TYR   B CD2 1 
ATOM   25018 C  CE1 . TYR   B 1 1399 ? 43.45000   28.04100  -5.59600  1.000 71.02305  ?  1397 TYR   B CE1 1 
ATOM   25019 C  CE2 . TYR   B 1 1399 ? 41.57600   28.47800  -4.17400  1.000 75.61899  ?  1397 TYR   B CE2 1 
ATOM   25020 C  CZ  . TYR   B 1 1399 ? 42.82900   28.81700  -4.64200  1.000 69.17288  ?  1397 TYR   B CZ  1 
ATOM   25021 O  OH  . TYR   B 1 1399 ? 43.46500   29.93700  -4.15700  1.000 73.81563  ?  1397 TYR   B OH  1 
ATOM   25022 N  N   . PRO   B 1 1400 ? 39.10100   24.17200  -9.23400  1.000 79.22810  ?  1398 PRO   B N   1 
ATOM   25023 C  CA  . PRO   B 1 1400 ? 37.94300   23.37800  -9.67600  1.000 83.54140  ?  1398 PRO   B CA  1 
ATOM   25024 C  C   . PRO   B 1 1400 ? 38.07600   21.90100  -9.32500  1.000 86.12545  ?  1398 PRO   B C   1 
ATOM   25025 O  O   . PRO   B 1 1400 ? 39.11100   21.27700  -9.57100  1.000 77.26129  ?  1398 PRO   B O   1 
ATOM   25026 C  CB  . PRO   B 1 1400 ? 37.93100   23.58700  -11.19500 1.000 64.45019  ?  1398 PRO   B CB  1 
ATOM   25027 C  CG  . PRO   B 1 1400 ? 39.35700   23.87500  -11.53700 1.000 79.31648  ?  1398 PRO   B CG  1 
ATOM   25028 C  CD  . PRO   B 1 1400 ? 39.92600   24.62900  -10.36600 1.000 63.28688  ?  1398 PRO   B CD  1 
ATOM   25029 N  N   . LEU   B 1 1401 ? 37.00600   21.34700  -8.75700  1.000 94.73426  ?  1399 LEU   B N   1 
ATOM   25030 C  CA  . LEU   B 1 1401 ? 36.85800   19.91700  -8.49200  1.000 91.96226  ?  1399 LEU   B CA  1 
ATOM   25031 C  C   . LEU   B 1 1401 ? 35.85100   19.39400  -9.51600  1.000 97.38711  ?  1399 LEU   B C   1 
ATOM   25032 O  O   . LEU   B 1 1401 ? 34.65000   19.32000  -9.24900  1.000 91.21044  ?  1399 LEU   B O   1 
ATOM   25033 C  CB  . LEU   B 1 1401 ? 36.39900   19.66400  -7.04900  1.000 75.75883  ?  1399 LEU   B CB  1 
ATOM   25034 C  CG  . LEU   B 1 1401 ? 36.55600   18.28700  -6.38500  1.000 55.74075  ?  1399 LEU   B CG  1 
ATOM   25035 C  CD1 . LEU   B 1 1401 ? 35.66700   17.21800  -7.01200  1.000 76.40416  ?  1399 LEU   B CD1 1 
ATOM   25036 C  CD2 . LEU   B 1 1401 ? 38.00600   17.84500  -6.39400  1.000 66.35247  ?  1399 LEU   B CD2 1 
ATOM   25037 N  N   . LEU   B 1 1402 ? 36.35000   19.04000  -10.69600 1.000 90.62445  ?  1400 LEU   B N   1 
ATOM   25038 C  CA  . LEU   B 1 1402 ? 35.51600   18.56200  -11.78600 1.000 93.08460  ?  1400 LEU   B CA  1 
ATOM   25039 C  C   . LEU   B 1 1402 ? 35.34900   17.04800  -11.67500 1.000 97.65952  ?  1400 LEU   B C   1 
ATOM   25040 O  O   . LEU   B 1 1402 ? 35.71400   16.42800  -10.67300 1.000 99.45948  ?  1400 LEU   B O   1 
ATOM   25041 C  CB  . LEU   B 1 1402 ? 36.12500   18.96900  -13.12500 1.000 86.15298  ?  1400 LEU   B CB  1 
ATOM   25042 C  CG  . LEU   B 1 1402 ? 36.34200   20.47000  -13.33100 1.000 85.77248  ?  1400 LEU   B CG  1 
ATOM   25043 C  CD1 . LEU   B 1 1402 ? 37.60500   20.72800  -14.13800 1.000 61.59141  ?  1400 LEU   B CD1 1 
ATOM   25044 C  CD2 . LEU   B 1 1402 ? 35.13600   21.10800  -14.00800 1.000 86.78916  ?  1400 LEU   B CD2 1 
ATOM   25045 N  N   . GLN   B 1 1403 ? 34.78700   16.43300  -12.71000 1.000 102.85911 ?  1401 GLN   B N   1 
ATOM   25046 C  CA  . GLN   B 1 1403 ? 34.75700   14.98300  -12.76700 1.000 96.53602  ?  1401 GLN   B CA  1 
ATOM   25047 C  C   . GLN   B 1 1403 ? 36.18000   14.45000  -12.88000 1.000 103.21741 ?  1401 GLN   B C   1 
ATOM   25048 O  O   . GLN   B 1 1403 ? 37.09100   15.15300  -13.32300 1.000 114.96013 ?  1401 GLN   B O   1 
ATOM   25049 C  CB  . GLN   B 1 1403 ? 33.90600   14.51300  -13.94300 1.000 85.68777  ?  1401 GLN   B CB  1 
ATOM   25050 C  CG  . GLN   B 1 1403 ? 34.70300   14.30600  -15.20400 1.000 104.44420 ?  1401 GLN   B CG  1 
ATOM   25051 C  CD  . GLN   B 1 1403 ? 33.84600   13.94800  -16.41200 1.000 117.02749 ?  1401 GLN   B CD  1 
ATOM   25052 O  OE1 . GLN   B 1 1403 ? 32.64000   14.20200  -16.45300 1.000 115.35574 ?  1401 GLN   B OE1 1 
ATOM   25053 N  NE2 . GLN   B 1 1403 ? 34.47900   13.33400  -17.40500 1.000 120.48893 ?  1401 GLN   B NE2 1 
ATOM   25054 N  N   . ASP   B 1 1404 ? 36.36800   13.19900  -12.45600 1.000 97.59565  ?  1402 ASP   B N   1 
ATOM   25055 C  CA  . ASP   B 1 1404 ? 37.66300   12.52800  -12.31100 1.000 110.18515 ?  1402 ASP   B CA  1 
ATOM   25056 C  C   . ASP   B 1 1404 ? 38.51600   13.13900  -11.20000 1.000 107.37093 ?  1402 ASP   B C   1 
ATOM   25057 O  O   . ASP   B 1 1404 ? 39.66800   12.71800  -11.01600 1.000 90.66328  ?  1402 ASP   B O   1 
ATOM   25058 C  CB  . ASP   B 1 1404 ? 38.48300   12.52100  -13.61600 1.000 110.34374 ?  1402 ASP   B CB  1 
ATOM   25059 C  CG  . ASP   B 1 1404 ? 37.79900   11.76400  -14.74000 1.000 117.26485 ?  1402 ASP   B CG  1 
ATOM   25060 O  OD1 . ASP   B 1 1404 ? 36.54900   11.87400  -14.84300 1.000 118.43301 ?  1402 ASP   B OD1 1 
ATOM   25061 O  OD2 . ASP   B 1 1404 ? 38.52100   11.08200  -15.51300 1.000 119.94233 -1 1402 ASP   B OD2 1 
ATOM   25062 N  N   . ASP   B 1 1405 ? 37.99900   14.11400  -10.45500 1.000 103.08152 ?  1403 ASP   B N   1 
ATOM   25063 C  CA  . ASP   B 1 1405 ? 38.69400   14.74300  -9.34200  1.000 92.91331  ?  1403 ASP   B CA  1 
ATOM   25064 C  C   . ASP   B 1 1405 ? 38.02600   14.33800  -8.03400  1.000 86.78694  ?  1403 ASP   B C   1 
ATOM   25065 O  O   . ASP   B 1 1405 ? 36.86300   13.92700  -8.00900  1.000 81.18208  ?  1403 ASP   B O   1 
ATOM   25066 C  CB  . ASP   B 1 1405 ? 38.69600   16.26900  -9.49700  1.000 81.99370  ?  1403 ASP   B CB  1 
ATOM   25067 C  CG  . ASP   B 1 1405 ? 39.12400   16.71300  -10.88300 1.000 99.20073  ?  1403 ASP   B CG  1 
ATOM   25068 O  OD1 . ASP   B 1 1405 ? 39.89300   15.97700  -11.53300 1.000 102.15376 ?  1403 ASP   B OD1 1 
ATOM   25069 O  OD2 . ASP   B 1 1405 ? 38.68800   17.80000  -11.32400 1.000 101.00896 -1 1403 ASP   B OD2 1 
ATOM   25070 N  N   . ALA   B 1 1406 ? 38.77600   14.45900  -6.93700  1.000 82.07293  ?  1404 ALA   B N   1 
ATOM   25071 C  CA  . ALA   B 1 1406 ? 38.33700   13.92400  -5.65600  1.000 70.96253  ?  1404 ALA   B CA  1 
ATOM   25072 C  C   . ALA   B 1 1406 ? 38.74000   14.84300  -4.51000  1.000 84.42502  ?  1404 ALA   B C   1 
ATOM   25073 O  O   . ALA   B 1 1406 ? 39.69300   15.62300  -4.60400  1.000 84.34923  ?  1404 ALA   B O   1 
ATOM   25074 C  CB  . ALA   B 1 1406 ? 38.90400   12.52000  -5.41400  1.000 72.93866  ?  1404 ALA   B CB  1 
ATOM   25075 N  N   . PHE   B 1 1407 ? 37.99900   14.71000  -3.40800  1.000 78.75927  ?  1405 PHE   B N   1 
ATOM   25076 C  CA  . PHE   B 1 1407 ? 38.18400   15.48300  -2.18900  1.000 60.61778  ?  1405 PHE   B CA  1 
ATOM   25077 C  C   . PHE   B 1 1407 ? 38.27600   14.52200  -1.01100  1.000 54.52070  ?  1405 PHE   B C   1 
ATOM   25078 O  O   . PHE   B 1 1407 ? 37.64300   13.46200  -1.00800  1.000 66.17031  ?  1405 PHE   B O   1 
ATOM   25079 C  CB  . PHE   B 1 1407 ? 37.01900   16.47100  -1.98000  1.000 47.61318  ?  1405 PHE   B CB  1 
ATOM   25080 C  CG  . PHE   B 1 1407 ? 37.44900   17.84800  -1.55700  1.000 64.02644  ?  1405 PHE   B CG  1 
ATOM   25081 C  CD1 . PHE   B 1 1407 ? 38.29300   18.02900  -0.47300  1.000 65.78237  ?  1405 PHE   B CD1 1 
ATOM   25082 C  CD2 . PHE   B 1 1407 ? 37.01000   18.96600  -2.25000  1.000 63.65196  ?  1405 PHE   B CD2 1 
ATOM   25083 C  CE1 . PHE   B 1 1407 ? 38.68900   19.29900  -0.08600  1.000 58.20411  ?  1405 PHE   B CE1 1 
ATOM   25084 C  CE2 . PHE   B 1 1407 ? 37.40100   20.23700  -1.86900  1.000 59.12415  ?  1405 PHE   B CE2 1 
ATOM   25085 C  CZ  . PHE   B 1 1407 ? 38.24200   20.40400  -0.78600  1.000 66.28875  ?  1405 PHE   B CZ  1 
ATOM   25086 N  N   . LEU   B 1 1408 ? 39.07400   14.89300  -0.01100  1.000 54.23199  ?  1406 LEU   B N   1 
ATOM   25087 C  CA  . LEU   B 1 1408 ? 39.31500   14.05600  1.16200   1.000 68.52703  ?  1406 LEU   B CA  1 
ATOM   25088 C  C   . LEU   B 1 1408 ? 38.68600   14.71900  2.38200   1.000 68.55901  ?  1406 LEU   B C   1 
ATOM   25089 O  O   . LEU   B 1 1408 ? 39.13300   15.78600  2.81700   1.000 81.62293  ?  1406 LEU   B O   1 
ATOM   25090 C  CB  . LEU   B 1 1408 ? 40.81000   13.82700  1.38000   1.000 56.96945  ?  1406 LEU   B CB  1 
ATOM   25091 C  CG  . LEU   B 1 1408 ? 41.18700   12.92700  2.56300   1.000 61.40212  ?  1406 LEU   B CG  1 
ATOM   25092 C  CD1 . LEU   B 1 1408 ? 40.76600   11.49000  2.32300   1.000 57.10800  ?  1406 LEU   B CD1 1 
ATOM   25093 C  CD2 . LEU   B 1 1408 ? 42.67300   12.98800  2.85100   1.000 69.90588  ?  1406 LEU   B CD2 1 
ATOM   25094 N  N   . LEU   B 1 1409 ? 37.65800   14.08000  2.93500   1.000 52.46544  ?  1407 LEU   B N   1 
ATOM   25095 C  CA  . LEU   B 1 1409 ? 37.01900   14.55800  4.15500   1.000 55.33494  ?  1407 LEU   B CA  1 
ATOM   25096 C  C   . LEU   B 1 1409 ? 37.88100   14.15800  5.34600   1.000 49.50440  ?  1407 LEU   B C   1 
ATOM   25097 O  O   . LEU   B 1 1409 ? 37.93400   12.98200  5.71700   1.000 63.74585  ?  1407 LEU   B O   1 
ATOM   25098 C  CB  . LEU   B 1 1409 ? 35.60900   13.98700  4.27600   1.000 47.64221  ?  1407 LEU   B CB  1 
ATOM   25099 C  CG  . LEU   B 1 1409 ? 34.77400   14.48800  5.46000   1.000 35.61797  ?  1407 LEU   B CG  1 
ATOM   25100 C  CD1 . LEU   B 1 1409 ? 34.48500   15.98200  5.34700   1.000 46.33370  ?  1407 LEU   B CD1 1 
ATOM   25101 C  CD2 . LEU   B 1 1409 ? 33.48300   13.69400  5.59600   1.000 41.92473  ?  1407 LEU   B CD2 1 
ATOM   25102 N  N   . LYS   B 1 1410 ? 38.56900   15.13500  5.93900   1.000 52.26312  ?  1408 LYS   B N   1 
ATOM   25103 C  CA  . LYS   B 1 1410 ? 39.37100   14.90300  7.13200   1.000 48.91818  ?  1408 LYS   B CA  1 
ATOM   25104 C  C   . LYS   B 1 1410 ? 39.07600   15.88600  8.25300   1.000 57.77629  ?  1408 LYS   B C   1 
ATOM   25105 O  O   . LYS   B 1 1410 ? 39.47400   15.62800  9.39400   1.000 67.17185  ?  1408 LYS   B O   1 
ATOM   25106 C  CB  . LYS   B 1 1410 ? 40.87200   14.97000  6.80300   1.000 52.00845  ?  1408 LYS   B CB  1 
ATOM   25107 C  CG  . LYS   B 1 1410 ? 41.47700   16.36700  6.92700   1.000 67.22618  ?  1408 LYS   B CG  1 
ATOM   25108 C  CD  . LYS   B 1 1410 ? 42.81500   16.47700  6.20000   1.000 64.02307  ?  1408 LYS   B CD  1 
ATOM   25109 C  CE  . LYS   B 1 1410 ? 43.99000   16.05300  7.07000   1.000 42.65474  ?  1408 LYS   B CE  1 
ATOM   25110 N  NZ  . LYS   B 1 1410 ? 44.35400   17.08100  8.08300   1.000 44.14275  ?  1408 LYS   B NZ  1 
ATOM   25111 N  N   . THR   B 1 1411 ? 38.39700   16.99400  7.97100   1.000 62.25126  ?  1409 THR   B N   1 
ATOM   25112 C  CA  . THR   B 1 1411 ? 38.15600   18.03900  8.95600   1.000 54.91753  ?  1409 THR   B CA  1 
ATOM   25113 C  C   . THR   B 1 1411 ? 36.87400   17.74200  9.72000   1.000 45.87039  ?  1409 THR   B C   1 
ATOM   25114 O  O   . THR   B 1 1411 ? 35.85500   17.39200  9.11700   1.000 53.79801  ?  1409 THR   B O   1 
ATOM   25115 C  CB  . THR   B 1 1411 ? 38.06400   19.40500  8.27300   1.000 50.61336  ?  1409 THR   B CB  1 
ATOM   25116 O  OG1 . THR   B 1 1411 ? 39.11900   19.52800  7.30700   1.000 46.13614  ?  1409 THR   B OG1 1 
ATOM   25117 C  CG2 . THR   B 1 1411 ? 38.20000   20.52000  9.29700   1.000 48.78913  ?  1409 THR   B CG2 1 
ATOM   25118 N  N   . THR   B 1 1412 ? 36.93500   17.87400  11.04400  1.000 46.63144  ?  1410 THR   B N   1 
ATOM   25119 C  CA  . THR   B 1 1412 ? 35.77700   17.59000  11.88400  1.000 51.88857  ?  1410 THR   B CA  1 
ATOM   25120 C  C   . THR   B 1 1412 ? 34.60700   18.47800  11.48800  1.000 56.86565  ?  1410 THR   B C   1 
ATOM   25121 O  O   . THR   B 1 1412 ? 34.77800   19.66900  11.21900  1.000 61.22127  ?  1410 THR   B O   1 
ATOM   25122 C  CB  . THR   B 1 1412 ? 36.12100   17.80800  13.35800  1.000 51.06968  ?  1410 THR   B CB  1 
ATOM   25123 O  OG1 . THR   B 1 1412 ? 37.47700   17.41200  13.59700  1.000 79.98083  ?  1410 THR   B OG1 1 
ATOM   25124 C  CG2 . THR   B 1 1412 ? 35.20300   16.97800  14.23700  1.000 61.36753  ?  1410 THR   B CG2 1 
ATOM   25125 N  N   . TYR   B 1 1413 ? 33.40600   17.89600  11.44700  1.000 61.77580  ?  1411 TYR   B N   1 
ATOM   25126 C  CA  . TYR   B 1 1413 ? 32.26700   18.67600  10.98000  1.000 55.39266  ?  1411 TYR   B CA  1 
ATOM   25127 C  C   . TYR   B 1 1413 ? 31.86900   19.78700  11.94900  1.000 53.14923  ?  1411 TYR   B C   1 
ATOM   25128 O  O   . TYR   B 1 1413 ? 30.93200   20.53400  11.64700  1.000 54.85095  ?  1411 TYR   B O   1 
ATOM   25129 C  CB  . TYR   B 1 1413 ? 31.07000   17.76300  10.66900  1.000 50.39598  ?  1411 TYR   B CB  1 
ATOM   25130 C  CG  . TYR   B 1 1413 ? 30.30600   17.17300  11.84300  1.000 51.09565  ?  1411 TYR   B CG  1 
ATOM   25131 C  CD1 . TYR   B 1 1413 ? 30.94500   16.78800  13.01500  1.000 51.44533  ?  1411 TYR   B CD1 1 
ATOM   25132 C  CD2 . TYR   B 1 1413 ? 28.93100   16.97700  11.75600  1.000 49.96138  ?  1411 TYR   B CD2 1 
ATOM   25133 C  CE1 . TYR   B 1 1413 ? 30.23000   16.24100  14.07400  1.000 58.82929  ?  1411 TYR   B CE1 1 
ATOM   25134 C  CE2 . TYR   B 1 1413 ? 28.21300   16.43500  12.80500  1.000 45.58312  ?  1411 TYR   B CE2 1 
ATOM   25135 C  CZ  . TYR   B 1 1413 ? 28.86300   16.06700  13.96100  1.000 46.65591  ?  1411 TYR   B CZ  1 
ATOM   25136 O  OH  . TYR   B 1 1413 ? 28.13800   15.52800  14.99800  1.000 54.06733  ?  1411 TYR   B OH  1 
ATOM   25137 N  N   . ILE   B 1 1414 ? 32.57100   19.93400  13.07500  1.000 47.41822  ?  1412 ILE   B N   1 
ATOM   25138 C  CA  . ILE   B 1 1414 ? 32.41400   21.08700  13.95500  1.000 54.96556  ?  1412 ILE   B CA  1 
ATOM   25139 C  C   . ILE   B 1 1414 ? 33.38800   22.18400  13.53700  1.000 50.88648  ?  1412 ILE   B C   1 
ATOM   25140 O  O   . ILE   B 1 1414 ? 33.72300   23.07000  14.33200  1.000 54.56695  ?  1412 ILE   B O   1 
ATOM   25141 C  CB  . ILE   B 1 1414 ? 32.62600   20.70800  15.43200  1.000 50.26618  ?  1412 ILE   B CB  1 
ATOM   25142 C  CG1 . ILE   B 1 1414 ? 34.03400   20.15400  15.64600  1.000 53.11416  ?  1412 ILE   B CG1 1 
ATOM   25143 C  CG2 . ILE   B 1 1414 ? 31.58500   19.70100  15.87500  1.000 50.52522  ?  1412 ILE   B CG2 1 
ATOM   25144 C  CD1 . ILE   B 1 1414 ? 34.41200   19.98700  17.10200  1.000 61.87231  ?  1412 ILE   B CD1 1 
ATOM   25145 N  N   . PHE   B 1 1415 ? 33.83700   22.14400  12.28400  1.000 59.09119  ?  1413 PHE   B N   1 
ATOM   25146 C  CA  . PHE   B 1 1415 ? 34.68200   23.18700  11.72100  1.000 47.26980  ?  1413 PHE   B CA  1 
ATOM   25147 C  C   . PHE   B 1 1415 ? 34.16300   23.54400  10.33700  1.000 52.22667  ?  1413 PHE   B C   1 
ATOM   25148 O  O   . PHE   B 1 1415 ? 33.81000   22.65800  9.55400   1.000 54.98661  ?  1413 PHE   B O   1 
ATOM   25149 C  CB  . PHE   B 1 1415 ? 36.15100   22.75000  11.64000  1.000 54.21923  ?  1413 PHE   B CB  1 
ATOM   25150 C  CG  . PHE   B 1 1415 ? 36.79100   22.52700  12.98000  1.000 68.01091  ?  1413 PHE   B CG  1 
ATOM   25151 C  CD1 . PHE   B 1 1415 ? 36.90500   23.56600  13.88800  1.000 69.65511  ?  1413 PHE   B CD1 1 
ATOM   25152 C  CD2 . PHE   B 1 1415 ? 37.28700   21.28000  13.33100  1.000 68.84955  ?  1413 PHE   B CD2 1 
ATOM   25153 C  CE1 . PHE   B 1 1415 ? 37.49400   23.36700  15.12200  1.000 70.35774  ?  1413 PHE   B CE1 1 
ATOM   25154 C  CE2 . PHE   B 1 1415 ? 37.87800   21.07600  14.56400  1.000 67.11899  ?  1413 PHE   B CE2 1 
ATOM   25155 C  CZ  . PHE   B 1 1415 ? 37.98200   22.12000  15.46000  1.000 66.82508  ?  1413 PHE   B CZ  1 
ATOM   25156 N  N   . ASP   B 1 1416 ? 34.12500   24.84700  10.03900  1.000 62.32652  ?  1414 ASP   B N   1 
ATOM   25157 C  CA  . ASP   B 1 1416 ? 33.52800   25.30300  8.78800   1.000 61.12995  ?  1414 ASP   B CA  1 
ATOM   25158 C  C   . ASP   B 1 1416 ? 34.27000   24.76900  7.56800   1.000 53.90093  ?  1414 ASP   B C   1 
ATOM   25159 O  O   . ASP   B 1 1416 ? 33.67300   24.64000  6.49300   1.000 54.61181  ?  1414 ASP   B O   1 
ATOM   25160 C  CB  . ASP   B 1 1416 ? 33.47600   26.83300  8.75100   1.000 65.42119  ?  1414 ASP   B CB  1 
ATOM   25161 C  CG  . ASP   B 1 1416 ? 34.79200   27.47500  9.14300   1.000 84.76430  ?  1414 ASP   B CG  1 
ATOM   25162 O  OD1 . ASP   B 1 1416 ? 35.33300   27.11800  10.21000  1.000 101.17243 ?  1414 ASP   B OD1 1 
ATOM   25163 O  OD2 . ASP   B 1 1416 ? 35.28700   28.33600  8.38300   1.000 80.69475  -1 1414 ASP   B OD2 1 
ATOM   25164 N  N   . ILE   B 1 1417 ? 35.55900   24.44500  7.71300   1.000 49.80457  ?  1415 ILE   B N   1 
ATOM   25165 C  CA  . ILE   B 1 1417 ? 36.32500   23.89700  6.59500   1.000 58.76429  ?  1415 ILE   B CA  1 
ATOM   25166 C  C   . ILE   B 1 1417 ? 35.67300   22.62600  6.06400   1.000 47.59988  ?  1415 ILE   B C   1 
ATOM   25167 O  O   . ILE   B 1 1417 ? 35.73300   22.34100  4.86100   1.000 53.51181  ?  1415 ILE   B O   1 
ATOM   25168 C  CB  . ILE   B 1 1417 ? 37.79000   23.65000  7.01800   1.000 61.28982  ?  1415 ILE   B CB  1 
ATOM   25169 C  CG1 . ILE   B 1 1417 ? 38.46800   24.96300  7.42100   1.000 50.10061  ?  1415 ILE   B CG1 1 
ATOM   25170 C  CG2 . ILE   B 1 1417 ? 38.58000   22.97700  5.90200   1.000 65.86255  ?  1415 ILE   B CG2 1 
ATOM   25171 C  CD1 . ILE   B 1 1417 ? 38.48600   25.21600  8.91500   1.000 63.15154  ?  1415 ILE   B CD1 1 
ATOM   25172 N  N   . SER   B 1 1418 ? 35.02300   21.85400  6.94200   1.000 60.30224  ?  1416 SER   B N   1 
ATOM   25173 C  CA  . SER   B 1 1418 ? 34.35400   20.63000  6.51100   1.000 47.30398  ?  1416 SER   B CA  1 
ATOM   25174 C  C   . SER   B 1 1418 ? 33.29000   20.91900  5.46200   1.000 46.15530  ?  1416 SER   B C   1 
ATOM   25175 O  O   . SER   B 1 1418 ? 33.09500   20.13000  4.53000   1.000 56.22715  ?  1416 SER   B O   1 
ATOM   25176 C  CB  . SER   B 1 1418 ? 33.73000   19.92400  7.71300   1.000 41.63640  ?  1416 SER   B CB  1 
ATOM   25177 O  OG  . SER   B 1 1418 ? 34.62800   19.89000  8.80600   1.000 63.11359  ?  1416 SER   B OG  1 
ATOM   25178 N  N   . VAL   B 1 1419 ? 32.59500   22.05200  5.59400   1.000 43.14104  ?  1417 VAL   B N   1 
ATOM   25179 C  CA  . VAL   B 1 1419 ? 31.52100   22.38400  4.66400   1.000 42.93052  ?  1417 VAL   B CA  1 
ATOM   25180 C  C   . VAL   B 1 1419 ? 32.06100   22.56000  3.25100   1.000 48.96144  ?  1417 VAL   B C   1 
ATOM   25181 O  O   . VAL   B 1 1419 ? 31.35100   22.30300  2.27000   1.000 58.62405  ?  1417 VAL   B O   1 
ATOM   25182 C  CB  . VAL   B 1 1419 ? 30.77300   23.64000  5.14900   1.000 45.30641  ?  1417 VAL   B CB  1 
ATOM   25183 C  CG1 . VAL   B 1 1419 ? 29.41500   23.73600  4.48200   1.000 46.16311  ?  1417 VAL   B CG1 1 
ATOM   25184 C  CG2 . VAL   B 1 1419 ? 30.62700   23.61500  6.66300   1.000 42.04452  ?  1417 VAL   B CG2 1 
ATOM   25185 N  N   . ALA   B 1 1420 ? 33.31600   22.99400  3.11800   1.000 52.12907  ?  1418 ALA   B N   1 
ATOM   25186 C  CA  . ALA   B 1 1420 ? 33.94300   23.06400  1.80400   1.000 46.43829  ?  1418 ALA   B CA  1 
ATOM   25187 C  C   . ALA   B 1 1420 ? 34.31500   21.68900  1.27100   1.000 50.19406  ?  1418 ALA   B C   1 
ATOM   25188 O  O   . ALA   B 1 1420 ? 34.44700   21.52400  0.05400   1.000 54.77493  ?  1418 ALA   B O   1 
ATOM   25189 C  CB  . ALA   B 1 1420 ? 35.18700   23.95200  1.85500   1.000 42.81148  ?  1418 ALA   B CB  1 
ATOM   25190 N  N   . GLU   B 1 1421 ? 34.49900   20.70700  2.15200   1.000 53.68552  ?  1419 GLU   B N   1 
ATOM   25191 C  CA  . GLU   B 1 1421 ? 34.76900   19.33400  1.74800   1.000 57.23052  ?  1419 GLU   B CA  1 
ATOM   25192 C  C   . GLU   B 1 1421 ? 33.48600   18.53200  1.58200   1.000 53.97021  ?  1419 GLU   B C   1 
ATOM   25193 O  O   . GLU   B 1 1421 ? 33.37900   17.71000  0.66500   1.000 61.79011  ?  1419 GLU   B O   1 
ATOM   25194 C  CB  . GLU   B 1 1421 ? 35.67400   18.64900  2.77700   1.000 46.36551  ?  1419 GLU   B CB  1 
ATOM   25195 C  CG  . GLU   B 1 1421 ? 36.89600   19.46000  3.17300   1.000 52.86001  ?  1419 GLU   B CG  1 
ATOM   25196 C  CD  . GLU   B 1 1421 ? 37.64700   18.85200  4.34300   1.000 50.99546  ?  1419 GLU   B CD  1 
ATOM   25197 O  OE1 . GLU   B 1 1421 ? 37.13000   17.89100  4.95100   1.000 42.52952  ?  1419 GLU   B OE1 1 
ATOM   25198 O  OE2 . GLU   B 1 1421 ? 38.75400   19.33600  4.65600   1.000 59.27800  -1 1419 GLU   B OE2 1 
ATOM   25199 N  N   . ILE   B 1 1422 ? 32.50800   18.76500  2.45800   1.000 44.73041  ?  1420 ILE   B N   1 
ATOM   25200 C  CA  . ILE   B 1 1422 ? 31.25300   18.02500  2.40100   1.000 33.98913  ?  1420 ILE   B CA  1 
ATOM   25201 C  C   . ILE   B 1 1422 ? 30.47100   18.39100  1.14500   1.000 46.29391  ?  1420 ILE   B C   1 
ATOM   25202 O  O   . ILE   B 1 1422 ? 29.80900   17.53800  0.54000   1.000 56.33950  ?  1420 ILE   B O   1 
ATOM   25203 C  CB  . ILE   B 1 1422 ? 30.44000   18.27900  3.68300   1.000 38.49155  ?  1420 ILE   B CB  1 
ATOM   25204 C  CG1 . ILE   B 1 1422 ? 31.15300   17.65100  4.88300   1.000 27.54101  ?  1420 ILE   B CG1 1 
ATOM   25205 C  CG2 . ILE   B 1 1422 ? 29.02400   17.73800  3.55300   1.000 52.30299  ?  1420 ILE   B CG2 1 
ATOM   25206 C  CD1 . ILE   B 1 1422 ? 30.49800   17.95000  6.20700   1.000 35.32925  ?  1420 ILE   B CD1 1 
ATOM   25207 N  N   . PHE   B 1 1423 ? 30.54800   19.65000  0.71900   1.000 53.08222  ?  1421 PHE   B N   1 
ATOM   25208 C  CA  . PHE   B 1 1423 ? 29.82200   20.11600  -0.45500  1.000 46.97652  ?  1421 PHE   B CA  1 
ATOM   25209 C  C   . PHE   B 1 1423 ? 30.73900   20.50000  -1.60800  1.000 56.01736  ?  1421 PHE   B C   1 
ATOM   25210 O  O   . PHE   B 1 1423 ? 30.26400   21.07600  -2.59100  1.000 55.14273  ?  1421 PHE   B O   1 
ATOM   25211 C  CB  . PHE   B 1 1423 ? 28.93400   21.30900  -0.09400  1.000 40.90987  ?  1421 PHE   B CB  1 
ATOM   25212 C  CG  . PHE   B 1 1423 ? 27.86600   20.99700  0.91200   1.000 49.94148  ?  1421 PHE   B CG  1 
ATOM   25213 C  CD1 . PHE   B 1 1423 ? 26.87800   20.06800  0.63100   1.000 51.08095  ?  1421 PHE   B CD1 1 
ATOM   25214 C  CD2 . PHE   B 1 1423 ? 27.83500   21.65200  2.13200   1.000 48.49113  ?  1421 PHE   B CD2 1 
ATOM   25215 C  CE1 . PHE   B 1 1423 ? 25.89000   19.78700  1.55400   1.000 51.95324  ?  1421 PHE   B CE1 1 
ATOM   25216 C  CE2 . PHE   B 1 1423 ? 26.84800   21.37600  3.05900   1.000 52.81140  ?  1421 PHE   B CE2 1 
ATOM   25217 C  CZ  . PHE   B 1 1423 ? 25.87500   20.44300  2.76900   1.000 58.19743  ?  1421 PHE   B CZ  1 
ATOM   25218 N  N   . GLY   B 1 1424 ? 32.03800   20.20000  -1.52000  1.000 59.34220  ?  1422 GLY   B N   1 
ATOM   25219 C  CA  . GLY   B 1 1424 ? 32.97200   20.67200  -2.52900  1.000 64.08843  ?  1422 GLY   B CA  1 
ATOM   25220 C  C   . GLY   B 1 1424 ? 32.99900   19.86500  -3.80700  1.000 76.75680  ?  1422 GLY   B C   1 
ATOM   25221 O  O   . GLY   B 1 1424 ? 33.52900   20.34000  -4.81700  1.000 71.56602  ?  1422 GLY   B O   1 
ATOM   25222 N  N   . TRP   B 1 1425 ? 32.44700   18.65400  -3.78700  1.000 83.87211  ?  1423 TRP   B N   1 
ATOM   25223 C  CA  . TRP   B 1 1425 ? 32.42600   17.79500  -4.96200  1.000 67.61780  ?  1423 TRP   B CA  1 
ATOM   25224 C  C   . TRP   B 1 1425 ? 31.12900   17.88900  -5.75300  1.000 65.42118  ?  1423 TRP   B C   1 
ATOM   25225 O  O   . TRP   B 1 1425 ? 31.09500   17.44900  -6.90700  1.000 71.56711  ?  1423 TRP   B O   1 
ATOM   25226 C  CB  . TRP   B 1 1425 ? 32.65500   16.33600  -4.54900  1.000 71.25331  ?  1423 TRP   B CB  1 
ATOM   25227 C  CG  . TRP   B 1 1425 ? 31.68100   15.86900  -3.51500  1.000 73.37576  ?  1423 TRP   B CG  1 
ATOM   25228 C  CD1 . TRP   B 1 1425 ? 31.77500   16.04200  -2.16500  1.000 56.23519  ?  1423 TRP   B CD1 1 
ATOM   25229 C  CD2 . TRP   B 1 1425 ? 30.45800   15.15600  -3.74400  1.000 78.49491  ?  1423 TRP   B CD2 1 
ATOM   25230 N  NE1 . TRP   B 1 1425 ? 30.69100   15.47800  -1.53900  1.000 62.45367  ?  1423 TRP   B NE1 1 
ATOM   25231 C  CE2 . TRP   B 1 1425 ? 29.86700   14.92800  -2.48500  1.000 68.35749  ?  1423 TRP   B CE2 1 
ATOM   25232 C  CE3 . TRP   B 1 1425 ? 29.80800   14.68700  -4.89000  1.000 67.01200  ?  1423 TRP   B CE3 1 
ATOM   25233 C  CZ2 . TRP   B 1 1425 ? 28.65700   14.25300  -2.34000  1.000 63.32194  ?  1423 TRP   B CZ2 1 
ATOM   25234 C  CZ3 . TRP   B 1 1425 ? 28.60600   14.01600  -4.74300  1.000 69.21319  ?  1423 TRP   B CZ3 1 
ATOM   25235 C  CH2 . TRP   B 1 1425 ? 28.04300   13.80600  -3.47800  1.000 71.58466  ?  1423 TRP   B CH2 1 
ATOM   25236 N  N   . VAL   B 1 1426 ? 30.07300   18.44900  -5.17000  1.000 64.89456  ?  1424 VAL   B N   1 
ATOM   25237 C  CA  . VAL   B 1 1426 ? 28.77200   18.52300  -5.83200  1.000 60.42145  ?  1424 VAL   B CA  1 
ATOM   25238 C  C   . VAL   B 1 1426 ? 28.81500   19.56300  -6.95100  1.000 82.61158  ?  1424 VAL   B C   1 
ATOM   25239 O  O   . VAL   B 1 1426 ? 28.22700   19.32400  -8.01600  1.000 91.64474  ?  1424 VAL   B O   1 
ATOM   25240 C  CB  . VAL   B 1 1426 ? 27.64700   18.80800  -4.82000  1.000 59.55765  ?  1424 VAL   B CB  1 
ATOM   25241 C  CG1 . VAL   B 1 1426 ? 26.28400   18.61800  -5.46500  1.000 65.35024  ?  1424 VAL   B CG1 1 
ATOM   25242 C  CG2 . VAL   B 1 1426 ? 27.79800   17.91500  -3.59700  1.000 53.09186  ?  1424 VAL   B CG2 1 
ATOM   25243 N  N   . PRO   B 1 1427 ? 29.45400   20.72400  -6.77400  1.000 83.71119  ?  1425 PRO   B N   1 
ATOM   25244 C  CA  . PRO   B 1 1427 ? 29.78000   21.55300  -7.94100  1.000 72.36285  ?  1425 PRO   B CA  1 
ATOM   25245 C  C   . PRO   B 1 1427 ? 30.58900   20.74600  -8.94400  1.000 81.07929  ?  1425 PRO   B C   1 
ATOM   25246 O  O   . PRO   B 1 1427 ? 31.62200   20.16000  -8.60900  1.000 67.55917  ?  1425 PRO   B O   1 
ATOM   25247 C  CB  . PRO   B 1 1427 ? 30.60200   22.70300  -7.35000  1.000 72.57634  ?  1425 PRO   B CB  1 
ATOM   25248 C  CG  . PRO   B 1 1427 ? 30.30700   22.72100  -5.89900  1.000 85.28848  ?  1425 PRO   B CG  1 
ATOM   25249 C  CD  . PRO   B 1 1427 ? 29.53000   21.50100  -5.52600  1.000 82.34434  ?  1425 PRO   B CD  1 
ATOM   25250 N  N   . GLY   B 1 1428 ? 30.11700   20.70900  -10.18200 1.000 83.07524  ?  1426 GLY   B N   1 
ATOM   25251 C  CA  . GLY   B 1 1428 ? 30.68800   19.75100  -11.10900 1.000 97.65920  ?  1426 GLY   B CA  1 
ATOM   25252 C  C   . GLY   B 1 1428 ? 30.18600   18.35500  -10.79700 1.000 109.94315 ?  1426 GLY   B C   1 
ATOM   25253 O  O   . GLY   B 1 1428 ? 29.03300   18.15900  -10.39800 1.000 115.23116 ?  1426 GLY   B O   1 
ATOM   25254 N  N   . ARG   B 1 1429 ? 31.06800   17.36700  -10.95100 1.000 100.73321 ?  1427 ARG   B N   1 
ATOM   25255 C  CA  . ARG   B 1 1429 ? 30.65200   15.96900  -10.89700 1.000 95.42883  ?  1427 ARG   B CA  1 
ATOM   25256 C  C   . ARG   B 1 1429 ? 31.79700   15.12900  -10.32300 1.000 90.44564  ?  1427 ARG   B C   1 
ATOM   25257 O  O   . ARG   B 1 1429 ? 32.36900   14.24600  -10.96200 1.000 87.14691  ?  1427 ARG   B O   1 
ATOM   25258 C  CB  . ARG   B 1 1429 ? 30.22200   15.48800  -12.28400 1.000 111.90293 ?  1427 ARG   B CB  1 
ATOM   25259 C  CG  . ARG   B 1 1429 ? 29.48600   14.16300  -12.30500 1.000 102.84762 ?  1427 ARG   B CG  1 
ATOM   25260 C  CD  . ARG   B 1 1429 ? 29.63200   13.43400  -13.64600 1.000 95.57889  ?  1427 ARG   B CD  1 
ATOM   25261 N  NE  . ARG   B 1 1429 ? 28.66500   13.86200  -14.65100 1.000 114.62482 ?  1427 ARG   B NE  1 
ATOM   25262 C  CZ  . ARG   B 1 1429 ? 28.97700   14.52600  -15.76000 1.000 124.36453 ?  1427 ARG   B CZ  1 
ATOM   25263 N  NH1 . ARG   B 1 1429 ? 30.22600   14.87900  -16.03300 1.000 119.79111 ?  1427 ARG   B NH1 1 
ATOM   25264 N  NH2 . ARG   B 1 1429 ? 28.01200   14.84600  -16.61700 1.000 122.83829 ?  1427 ARG   B NH2 1 
ATOM   25265 N  N   . GLY   B 1 1430 ? 32.14100   15.39000  -9.06100  1.000 92.46694  ?  1428 GLY   B N   1 
ATOM   25266 C  CA  . GLY   B 1 1430 ? 33.26800   14.72300  -8.44000  1.000 86.20075  ?  1428 GLY   B CA  1 
ATOM   25267 C  C   . GLY   B 1 1430 ? 32.91900   13.62100  -7.46000  1.000 74.59093  ?  1428 GLY   B C   1 
ATOM   25268 O  O   . GLY   B 1 1430 ? 31.82500   13.04800  -7.50800  1.000 77.84773  ?  1428 GLY   B O   1 
ATOM   25269 N  N   . LYS   B 1 1431 ? 33.85700   13.30700  -6.56700  1.000 65.08799  ?  1429 LYS   B N   1 
ATOM   25270 C  CA  . LYS   B 1 1431 ? 33.66100   12.27700  -5.55700  1.000 63.89332  ?  1429 LYS   B CA  1 
ATOM   25271 C  C   . LYS   B 1 1431 ? 34.32600   12.69400  -4.25500  1.000 74.00550  ?  1429 LYS   B C   1 
ATOM   25272 O  O   . LYS   B 1 1431 ? 35.42600   13.25500  -4.26000  1.000 84.51187  ?  1429 LYS   B O   1 
ATOM   25273 C  CB  . LYS   B 1 1431 ? 34.22600   10.92400  -6.01200  1.000 68.51250  ?  1429 LYS   B CB  1 
ATOM   25274 N  N   . LEU   B 1 1432 ? 33.65300   12.41800  -3.14200  1.000 64.05781  ?  1430 LEU   B N   1 
ATOM   25275 C  CA  . LEU   B 1 1432 ? 34.22300   12.59500  -1.81300  1.000 61.38199  ?  1430 LEU   B CA  1 
ATOM   25276 C  C   . LEU   B 1 1432 ? 34.57200   11.22900  -1.24700  1.000 65.61883  ?  1430 LEU   B C   1 
ATOM   25277 O  O   . LEU   B 1 1432 ? 33.70900   10.34900  -1.16900  1.000 72.04708  ?  1430 LEU   B O   1 
ATOM   25278 C  CB  . LEU   B 1 1432 ? 33.26100   13.30700  -0.86300  1.000 64.08265  ?  1430 LEU   B CB  1 
ATOM   25279 C  CG  . LEU   B 1 1432 ? 33.81600   13.31800  0.56600   1.000 67.06030  ?  1430 LEU   B CG  1 
ATOM   25280 C  CD1 . LEU   B 1 1432 ? 34.71100   14.52300  0.79700   1.000 62.15742  ?  1430 LEU   B CD1 1 
ATOM   25281 C  CD2 . LEU   B 1 1432 ? 32.69600   13.26800  1.60000   1.000 42.50740  ?  1430 LEU   B CD2 1 
ATOM   25282 N  N   . VAL   B 1 1433 ? 35.82500   11.05300  -0.85000  1.000 56.68330  ?  1431 VAL   B N   1 
ATOM   25283 C  CA  . VAL   B 1 1433 ? 36.23900   9.86600   -0.11700  1.000 65.51312  ?  1431 VAL   B CA  1 
ATOM   25284 C  C   . VAL   B 1 1433 ? 36.32500   10.23900  1.35700   1.000 63.36965  ?  1431 VAL   B C   1 
ATOM   25285 O  O   . VAL   B 1 1433 ? 36.85900   11.29700  1.71600   1.000 53.58859  ?  1431 VAL   B O   1 
ATOM   25286 C  CB  . VAL   B 1 1433 ? 37.56200   9.29400   -0.66300  1.000 58.45673  ?  1431 VAL   B CB  1 
ATOM   25287 C  CG1 . VAL   B 1 1433 ? 37.53300   9.29000   -2.18200  1.000 51.37887  ?  1431 VAL   B CG1 1 
ATOM   25288 C  CG2 . VAL   B 1 1433 ? 38.76800   10.05800  -0.16400  1.000 65.93146  ?  1431 VAL   B CG2 1 
ATOM   25289 N  N   . ILE   B 1 1434 ? 35.73700   9.40500   2.20500   1.000 64.20604  ?  1432 ILE   B N   1 
ATOM   25290 C  CA  . ILE   B 1 1434 ? 35.59800   9.69600   3.62500   1.000 55.70867  ?  1432 ILE   B CA  1 
ATOM   25291 C  C   . ILE   B 1 1434 ? 36.71300   8.96700   4.35800   1.000 60.60196  ?  1432 ILE   B C   1 
ATOM   25292 O  O   . ILE   B 1 1434 ? 36.73000   7.73200   4.41500   1.000 76.46657  ?  1432 ILE   B O   1 
ATOM   25293 C  CB  . ILE   B 1 1434 ? 34.21700   9.28700   4.15000   1.000 54.50421  ?  1432 ILE   B CB  1 
ATOM   25294 C  CG1 . ILE   B 1 1434 ? 33.12500   10.08600  3.43600   1.000 51.53894  ?  1432 ILE   B CG1 1 
ATOM   25295 C  CG2 . ILE   B 1 1434 ? 34.14000   9.49500   5.65200   1.000 50.24087  ?  1432 ILE   B CG2 1 
ATOM   25296 C  CD1 . ILE   B 1 1434 ? 31.73200   9.53600   3.63400   1.000 57.17958  ?  1432 ILE   B CD1 1 
ATOM   25297 N  N   . LEU   B 1 1435 ? 37.65300   9.73100   4.90600   1.000 55.79515  ?  1433 LEU   B N   1 
ATOM   25298 C  CA  . LEU   B 1 1435 ? 38.71300   9.14200   5.70700   1.000 49.87405  ?  1433 LEU   B CA  1 
ATOM   25299 C  C   . LEU   B 1 1435 ? 38.11600   8.45700   6.93000   1.000 51.93001  ?  1433 LEU   B C   1 
ATOM   25300 O  O   . LEU   B 1 1435 ? 37.06300   8.85300   7.43900   1.000 49.57008  ?  1433 LEU   B O   1 
ATOM   25301 C  CB  . LEU   B 1 1435 ? 39.71600   10.21600  6.13300   1.000 44.83166  ?  1433 LEU   B CB  1 
ATOM   25302 C  CG  . LEU   B 1 1435 ? 41.15000   9.77000   6.42100   1.000 61.83366  ?  1433 LEU   B CG  1 
ATOM   25303 C  CD1 . LEU   B 1 1435 ? 41.81200   9.26800   5.14900   1.000 66.19816  ?  1433 LEU   B CD1 1 
ATOM   25304 C  CD2 . LEU   B 1 1435 ? 41.95500   10.90400  7.03800   1.000 61.34704  ?  1433 LEU   B CD2 1 
ATOM   25305 N  N   . GLU   B 1 1436 ? 38.78700   7.40400   7.38700   1.000 52.16548  ?  1434 GLU   B N   1 
ATOM   25306 C  CA  . GLU   B 1 1436 ? 38.33400   6.70200   8.57600   1.000 46.71360  ?  1434 GLU   B CA  1 
ATOM   25307 C  C   . GLU   B 1 1436 ? 38.29100   7.66500   9.76100   1.000 47.26906  ?  1434 GLU   B C   1 
ATOM   25308 O  O   . GLU   B 1 1436 ? 39.08700   8.60600   9.83500   1.000 58.00102  ?  1434 GLU   B O   1 
ATOM   25309 C  CB  . GLU   B 1 1436 ? 39.25400   5.52400   8.89000   1.000 73.03783  ?  1434 GLU   B CB  1 
ATOM   25310 C  CG  . GLU   B 1 1436 ? 39.06500   4.31500   7.98700   1.000 83.59616  ?  1434 GLU   B CG  1 
ATOM   25311 C  CD  . GLU   B 1 1436 ? 38.42200   3.14400   8.70800   1.000 89.55316  ?  1434 GLU   B CD  1 
ATOM   25312 O  OE1 . GLU   B 1 1436 ? 37.42900   3.35900   9.43500   1.000 79.27201  ?  1434 GLU   B OE1 1 
ATOM   25313 O  OE2 . GLU   B 1 1436 ? 38.91900   2.00800   8.55400   1.000 102.43869 -1 1434 GLU   B OE2 1 
ATOM   25314 N  N   . PRO   B 1 1437 ? 37.35200   7.47300   10.68600  1.000 54.05771  ?  1435 PRO   B N   1 
ATOM   25315 C  CA  . PRO   B 1 1437 ? 37.32900   8.31300   11.88800  1.000 51.41748  ?  1435 PRO   B CA  1 
ATOM   25316 C  C   . PRO   B 1 1437 ? 38.63900   8.20400   12.65300  1.000 68.78230  ?  1435 PRO   B C   1 
ATOM   25317 O  O   . PRO   B 1 1437 ? 39.21400   7.12200   12.78600  1.000 69.14699  ?  1435 PRO   B O   1 
ATOM   25318 C  CB  . PRO   B 1 1437 ? 36.15600   7.74600   12.69600  1.000 49.53923  ?  1435 PRO   B CB  1 
ATOM   25319 C  CG  . PRO   B 1 1437 ? 35.29000   7.09000   11.69100  1.000 64.48561  ?  1435 PRO   B CG  1 
ATOM   25320 C  CD  . PRO   B 1 1437 ? 36.20900   6.54700   10.63600  1.000 64.14424  ?  1435 PRO   B CD  1 
ATOM   25321 N  N   . GLU   B 1 1438 ? 39.11300   9.35200   13.13800  1.000 69.01527  ?  1436 GLU   B N   1 
ATOM   25322 C  CA  . GLU   B 1 1438 ? 40.35300   9.50700   13.89600  1.000 69.35882  ?  1436 GLU   B CA  1 
ATOM   25323 C  C   . GLU   B 1 1438 ? 41.60000   9.20900   13.07600  1.000 77.25431  ?  1436 GLU   B C   1 
ATOM   25324 O  O   . GLU   B 1 1438 ? 42.70300   9.17700   13.63800  1.000 77.69280  ?  1436 GLU   B O   1 
ATOM   25325 C  CB  . GLU   B 1 1438 ? 40.36900   8.63900   15.16100  1.000 55.63957  ?  1436 GLU   B CB  1 
ATOM   25326 C  CG  . GLU   B 1 1438 ? 39.34400   9.03400   16.20500  1.000 74.49597  ?  1436 GLU   B CG  1 
ATOM   25327 C  CD  . GLU   B 1 1438 ? 39.68200   10.33200  16.91700  1.000 105.26785 ?  1436 GLU   B CD  1 
ATOM   25328 O  OE1 . GLU   B 1 1438 ? 40.71700   10.95500  16.59300  1.000 106.19155 ?  1436 GLU   B OE1 1 
ATOM   25329 O  OE2 . GLU   B 1 1438 ? 38.90800   10.72800  17.81100  1.000 122.06879 -1 1436 GLU   B OE2 1 
ATOM   25330 N  N   . ALA   B 1 1439 ? 41.46400   8.99400   11.76900  1.000 68.63192  ?  1437 ALA   B N   1 
ATOM   25331 C  CA  . ALA   B 1 1439 ? 42.59700   8.75000   10.88900  1.000 61.66965  ?  1437 ALA   B CA  1 
ATOM   25332 C  C   . ALA   B 1 1439 ? 43.21300   10.03900  10.34900  1.000 69.06935  ?  1437 ALA   B C   1 
ATOM   25333 O  O   . ALA   B 1 1439 ? 44.10500   9.97400   9.49700   1.000 71.72122  ?  1437 ALA   B O   1 
ATOM   25334 C  CB  . ALA   B 1 1439 ? 42.18200   7.84800   9.72400   1.000 57.44447  ?  1437 ALA   B CB  1 
ATOM   25335 N  N   . GLU   B 1 1440 ? 42.75900   11.20600  10.82100  1.000 78.38474  ?  1438 GLU   B N   1 
ATOM   25336 C  CA  . GLU   B 1 1440 ? 43.37000   12.46600  10.41700  1.000 79.64189  ?  1438 GLU   B CA  1 
ATOM   25337 C  C   . GLU   B 1 1440 ? 44.73600   12.68500  11.05700  1.000 67.65219  ?  1438 GLU   B C   1 
ATOM   25338 O  O   . GLU   B 1 1440 ? 45.53600   13.46000  10.52100  1.000 59.18435  ?  1438 GLU   B O   1 
ATOM   25339 C  CB  . GLU   B 1 1440 ? 42.45500   13.64500  10.76600  1.000 59.89444  ?  1438 GLU   B CB  1 
ATOM   25340 C  CG  . GLU   B 1 1440 ? 42.30500   13.90400  12.25900  1.000 68.94669  ?  1438 GLU   B CG  1 
ATOM   25341 C  CD  . GLU   B 1 1440 ? 40.92600   13.55500  12.78200  1.000 81.44082  ?  1438 GLU   B CD  1 
ATOM   25342 O  OE1 . GLU   B 1 1440 ? 39.93700   14.13500  12.28700  1.000 93.47505  ?  1438 GLU   B OE1 1 
ATOM   25343 O  OE2 . GLU   B 1 1440 ? 40.82900   12.69600  13.68300  1.000 86.37869  -1 1438 GLU   B OE2 1 
ATOM   25344 N  N   . LYS   B 1 1441 ? 45.02200   12.03000  12.18500  1.000 58.56761  ?  1439 LYS   B N   1 
ATOM   25345 C  CA  . LYS   B 1 1441 ? 46.30200   12.16600  12.86900  1.000 73.83619  ?  1439 LYS   B CA  1 
ATOM   25346 C  C   . LYS   B 1 1441 ? 47.33400   11.14700  12.40600  1.000 77.82895  ?  1439 LYS   B C   1 
ATOM   25347 O  O   . LYS   B 1 1441 ? 48.38500   11.01600  13.04300  1.000 78.34040  ?  1439 LYS   B O   1 
ATOM   25348 C  CB  . LYS   B 1 1441 ? 46.11600   12.04900  14.38200  1.000 70.88261  ?  1439 LYS   B CB  1 
ATOM   25349 C  CG  . LYS   B 1 1441 ? 45.56700   13.29700  15.04300  1.000 70.35756  ?  1439 LYS   B CG  1 
ATOM   25350 C  CD  . LYS   B 1 1441 ? 44.08100   13.17000  15.31200  1.000 80.74802  ?  1439 LYS   B CD  1 
ATOM   25351 C  CE  . LYS   B 1 1441 ? 43.79900   11.98900  16.22600  1.000 83.25138  ?  1439 LYS   B CE  1 
ATOM   25352 N  NZ  . LYS   B 1 1441 ? 42.49700   12.10300  16.93900  1.000 96.83380  ?  1439 LYS   B NZ  1 
ATOM   25353 N  N   . ASN   B 1 1442 ? 47.05600   10.41700  11.33200  1.000 77.27687  ?  1440 ASN   B N   1 
ATOM   25354 C  CA  . ASN   B 1 1442 ? 48.02100   9.49200   10.73900  1.000 64.65573  ?  1440 ASN   B CA  1 
ATOM   25355 C  C   . ASN   B 1 1442 ? 48.30900   9.93900   9.31500   1.000 75.17050  ?  1440 ASN   B C   1 
ATOM   25356 O  O   . ASN   B 1 1442 ? 47.49000   9.70100   8.40900   1.000 73.61742  ?  1440 ASN   B O   1 
ATOM   25357 C  CB  . ASN   B 1 1442 ? 47.49800   8.05800   10.75800  1.000 66.77247  ?  1440 ASN   B CB  1 
ATOM   25358 C  CG  . ASN   B 1 1442 ? 48.45700   7.08400   10.10600  1.000 82.42213  ?  1440 ASN   B CG  1 
ATOM   25359 O  OD1 . ASN   B 1 1442 ? 48.39400   6.84700   8.90100   1.000 90.63269  ?  1440 ASN   B OD1 1 
ATOM   25360 N  ND2 . ASN   B 1 1442 ? 49.35800   6.51800   10.90000  1.000 83.90091  ?  1440 ASN   B ND2 1 
ATOM   25361 N  N   . PRO   B 1 1443 ? 49.44700   10.59200  9.06400   1.000 73.83948  ?  1441 PRO   B N   1 
ATOM   25362 C  CA  . PRO   B 1 1443 ? 49.74200   11.04900  7.69600   1.000 73.53344  ?  1441 PRO   B CA  1 
ATOM   25363 C  C   . PRO   B 1 1443 ? 49.86900   9.91900   6.69200   1.000 70.88515  ?  1441 PRO   B C   1 
ATOM   25364 O  O   . PRO   B 1 1443 ? 49.66300   10.14900  5.49400   1.000 67.42467  ?  1441 PRO   B O   1 
ATOM   25365 C  CB  . PRO   B 1 1443 ? 51.06400   11.81300  7.85800   1.000 61.74130  ?  1441 PRO   B CB  1 
ATOM   25366 C  CG  . PRO   B 1 1443 ? 51.66900   11.27000  9.11400   1.000 59.59397  ?  1441 PRO   B CG  1 
ATOM   25367 C  CD  . PRO   B 1 1443 ? 50.51500   10.94700  10.01300  1.000 61.27184  ?  1441 PRO   B CD  1 
ATOM   25368 N  N   . LYS   B 1 1444 ? 50.20500   8.70700   7.13800   1.000 65.86294  ?  1442 LYS   B N   1 
ATOM   25369 C  CA  . LYS   B 1 1444 ? 50.24900   7.57500   6.22000   1.000 75.92432  ?  1442 LYS   B CA  1 
ATOM   25370 C  C   . LYS   B 1 1444 ? 48.85500   7.23100   5.71000   1.000 88.02964  ?  1442 LYS   B C   1 
ATOM   25371 O  O   . LYS   B 1 1444 ? 48.66800   7.00000   4.50900   1.000 77.04547  ?  1442 LYS   B O   1 
ATOM   25372 C  CB  . LYS   B 1 1444 ? 50.88800   6.36600   6.90500   1.000 60.64306  ?  1442 LYS   B CB  1 
ATOM   25373 N  N   . ALA   B 1 1445 ? 47.86300   7.20100   6.60600   1.000 73.06178  ?  1443 ALA   B N   1 
ATOM   25374 C  CA  . ALA   B 1 1445 ? 46.48800   6.95300   6.18400   1.000 71.29730  ?  1443 ALA   B CA  1 
ATOM   25375 C  C   . ALA   B 1 1445 ? 46.00300   8.03700   5.23300   1.000 78.37589  ?  1443 ALA   B C   1 
ATOM   25376 O  O   . ALA   B 1 1445 ? 45.31000   7.74900   4.24900   1.000 73.00128  ?  1443 ALA   B O   1 
ATOM   25377 C  CB  . ALA   B 1 1445 ? 45.57100   6.85900   7.40300   1.000 52.81710  ?  1443 ALA   B CB  1 
ATOM   25378 N  N   . ILE   B 1 1446 ? 46.35700   9.29400   5.51300   1.000 68.94946  ?  1444 ILE   B N   1 
ATOM   25379 C  CA  . ILE   B 1 1446 ? 46.03800   10.38000  4.59200   1.000 70.23946  ?  1444 ILE   B CA  1 
ATOM   25380 C  C   . ILE   B 1 1446 ? 46.68100   10.12600  3.23700   1.000 74.19430  ?  1444 ILE   B C   1 
ATOM   25381 O  O   . ILE   B 1 1446 ? 46.07400   10.37000  2.18700   1.000 64.93656  ?  1444 ILE   B O   1 
ATOM   25382 C  CB  . ILE   B 1 1446 ? 46.48700   11.72900  5.18400   1.000 63.51572  ?  1444 ILE   B CB  1 
ATOM   25383 C  CG1 . ILE   B 1 1446 ? 45.89800   11.92600  6.58100   1.000 69.33926  ?  1444 ILE   B CG1 1 
ATOM   25384 C  CG2 . ILE   B 1 1446 ? 46.08800   12.87500  4.26800   1.000 50.24167  ?  1444 ILE   B CG2 1 
ATOM   25385 C  CD1 . ILE   B 1 1446 ? 46.36300   13.19300  7.26200   1.000 53.66741  ?  1444 ILE   B CD1 1 
ATOM   25386 N  N   . TRP   B 1 1447 ? 47.91200   9.61000   3.23800   1.000 79.80992  ?  1445 TRP   B N   1 
ATOM   25387 C  CA  . TRP   B 1 1447 ? 48.63500   9.43500   1.98500   1.000 85.99436  ?  1445 TRP   B CA  1 
ATOM   25388 C  C   . TRP   B 1 1447 ? 48.10400   8.24500   1.19600   1.000 82.09494  ?  1445 TRP   B C   1 
ATOM   25389 O  O   . TRP   B 1 1447 ? 48.02100   8.30100   -0.03700  1.000 70.36822  ?  1445 TRP   B O   1 
ATOM   25390 C  CB  . TRP   B 1 1447 ? 50.13200   9.29000   2.26100   1.000 85.51210  ?  1445 TRP   B CB  1 
ATOM   25391 C  CG  . TRP   B 1 1447 ? 51.00300   9.43000   1.04100   1.000 85.37167  ?  1445 TRP   B CG  1 
ATOM   25392 C  CD1 . TRP   B 1 1447 ? 52.09700   8.67600   0.72500   1.000 79.78378  ?  1445 TRP   B CD1 1 
ATOM   25393 C  CD2 . TRP   B 1 1447 ? 50.85000   10.37900  -0.02600  1.000 78.91422  ?  1445 TRP   B CD2 1 
ATOM   25394 N  NE1 . TRP   B 1 1447 ? 52.63600   9.09700   -0.46600  1.000 81.46136  ?  1445 TRP   B NE1 1 
ATOM   25395 C  CE2 . TRP   B 1 1447 ? 51.88800   10.13900  -0.94800  1.000 85.74024  ?  1445 TRP   B CE2 1 
ATOM   25396 C  CE3 . TRP   B 1 1447 ? 49.94000   11.40900  -0.29000  1.000 89.70466  ?  1445 TRP   B CE3 1 
ATOM   25397 C  CZ2 . TRP   B 1 1447 ? 52.03800   10.88900  -2.11100  1.000 86.11010  ?  1445 TRP   B CZ2 1 
ATOM   25398 C  CZ3 . TRP   B 1 1447 ? 50.09000   12.14700  -1.44200  1.000 94.83833  ?  1445 TRP   B CZ3 1 
ATOM   25399 C  CH2 . TRP   B 1 1447 ? 51.13000   11.88600  -2.33800  1.000 81.25912  ?  1445 TRP   B CH2 1 
ATOM   25400 N  N   . GLN   B 1 1448 ? 47.73700   7.16200   1.88600   1.000 81.53943  ?  1446 GLN   B N   1 
ATOM   25401 C  CA  . GLN   B 1 1448 ? 47.12100   6.02800   1.20400   1.000 77.25881  ?  1446 GLN   B CA  1 
ATOM   25402 C  C   . GLN   B 1 1448 ? 45.84200   6.44700   0.49300   1.000 69.19417  ?  1446 GLN   B C   1 
ATOM   25403 O  O   . GLN   B 1 1448 ? 45.54200   5.95800   -0.60300  1.000 69.26799  ?  1446 GLN   B O   1 
ATOM   25404 C  CB  . GLN   B 1 1448 ? 46.83200   4.90700   2.20200   1.000 77.66651  ?  1446 GLN   B CB  1 
ATOM   25405 C  CG  . GLN   B 1 1448 ? 48.06300   4.33500   2.87600   1.000 79.09915  ?  1446 GLN   B CG  1 
ATOM   25406 C  CD  . GLN   B 1 1448 ? 47.71700   3.48000   4.07700   1.000 76.10113  ?  1446 GLN   B CD  1 
ATOM   25407 O  OE1 . GLN   B 1 1448 ? 46.55500   3.38900   4.47400   1.000 81.45000  ?  1446 GLN   B OE1 1 
ATOM   25408 N  NE2 . GLN   B 1 1448 ? 48.72700   2.85000   4.66500   1.000 71.99813  ?  1446 GLN   B NE2 1 
ATOM   25409 N  N   . ALA   B 1 1449 ? 45.07800   7.35700   1.10200   1.000 70.10741  ?  1447 ALA   B N   1 
ATOM   25410 C  CA  . ALA   B 1 1449 ? 43.85600   7.84000   0.47100   1.000 63.96599  ?  1447 ALA   B CA  1 
ATOM   25411 C  C   . ALA   B 1 1449 ? 44.14900   8.68500   -0.76100  1.000 73.96503  ?  1447 ALA   B C   1 
ATOM   25412 O  O   . ALA   B 1 1449 ? 43.38300   8.64800   -1.73000  1.000 73.38040  ?  1447 ALA   B O   1 
ATOM   25413 C  CB  . ALA   B 1 1449 ? 43.02900   8.64000   1.47700   1.000 63.79447  ?  1447 ALA   B CB  1 
ATOM   25414 N  N   . VAL   B 1 1450 ? 45.24500   9.44500   -0.75000  1.000 66.22057  ?  1448 VAL   B N   1 
ATOM   25415 C  CA  . VAL   B 1 1450 ? 45.54200   10.32200  -1.87900  1.000 77.02503  ?  1448 VAL   B CA  1 
ATOM   25416 C  C   . VAL   B 1 1450 ? 46.05700   9.51300   -3.06300  1.000 89.80384  ?  1448 VAL   B C   1 
ATOM   25417 O  O   . VAL   B 1 1450 ? 45.62500   9.71200   -4.20400  1.000 99.85194  ?  1448 VAL   B O   1 
ATOM   25418 C  CB  . VAL   B 1 1450 ? 46.54000   11.42000  -1.46900  1.000 70.82058  ?  1448 VAL   B CB  1 
ATOM   25419 C  CG1 . VAL   B 1 1450 ? 46.85500   12.31300  -2.66300  1.000 70.75465  ?  1448 VAL   B CG1 1 
ATOM   25420 C  CG2 . VAL   B 1 1450 ? 45.98100   12.24900  -0.32600  1.000 77.85923  ?  1448 VAL   B CG2 1 
ATOM   25421 N  N   . VAL   B 1 1451 ? 46.98900   8.59000   -2.81400  1.000 79.15230  ?  1449 VAL   B N   1 
ATOM   25422 C  CA  . VAL   B 1 1451 ? 47.55500   7.82400   -3.92000  1.000 79.24239  ?  1449 VAL   B CA  1 
ATOM   25423 C  C   . VAL   B 1 1451 ? 46.54200   6.82100   -4.46100  1.000 83.45928  ?  1449 VAL   B C   1 
ATOM   25424 O  O   . VAL   B 1 1451 ? 46.55700   6.49800   -5.65500  1.000 96.33415  ?  1449 VAL   B O   1 
ATOM   25425 C  CB  . VAL   B 1 1451 ? 48.86500   7.13200   -3.49200  1.000 76.27777  ?  1449 VAL   B CB  1 
ATOM   25426 C  CG1 . VAL   B 1 1451 ? 49.75800   8.10300   -2.73900  1.000 80.91604  ?  1449 VAL   B CG1 1 
ATOM   25427 C  CG2 . VAL   B 1 1451 ? 48.58900   5.88800   -2.65400  1.000 77.06633  ?  1449 VAL   B CG2 1 
ATOM   25428 N  N   . GLY   B 1 1452 ? 45.64100   6.32800   -3.61300  1.000 79.73611  ?  1450 GLY   B N   1 
ATOM   25429 C  CA  . GLY   B 1 1452 ? 44.69500   5.31300   -4.02800  1.000 79.98625  ?  1450 GLY   B CA  1 
ATOM   25430 C  C   . GLY   B 1 1452 ? 43.46600   5.87900   -4.70600  1.000 92.20042  ?  1450 GLY   B C   1 
ATOM   25431 O  O   . GLY   B 1 1452 ? 43.26600   5.68400   -5.90800  1.000 103.33928 ?  1450 GLY   B O   1 
ATOM   25432 N  N   . ALA   B 1 1453 ? 42.63400   6.58600   -3.93900  1.000 72.55161  ?  1451 ALA   B N   1 
ATOM   25433 C  CA  . ALA   B 1 1453 ? 41.42200   7.17300   -4.49700  1.000 64.84694  ?  1451 ALA   B CA  1 
ATOM   25434 C  C   . ALA   B 1 1453 ? 41.72000   8.27100   -5.51100  1.000 95.32350  ?  1451 ALA   B C   1 
ATOM   25435 O  O   . ALA   B 1 1453 ? 40.85000   8.59600   -6.32600  1.000 83.59172  ?  1451 ALA   B O   1 
ATOM   25436 C  CB  . ALA   B 1 1453 ? 40.54200   7.72300   -3.37500  1.000 67.60317  ?  1451 ALA   B CB  1 
ATOM   25437 N  N   . GLY   B 1 1454 ? 42.92100   8.84400   -5.48100  1.000 98.05765  ?  1452 GLY   B N   1 
ATOM   25438 C  CA  . GLY   B 1 1454 ? 43.29100   9.88400   -6.42000  1.000 88.23195  ?  1452 GLY   B CA  1 
ATOM   25439 C  C   . GLY   B 1 1454 ? 42.86900   11.26500  -5.96500  1.000 88.76613  ?  1452 GLY   B C   1 
ATOM   25440 O  O   . GLY   B 1 1454 ? 42.19600   11.99000  -6.70400  1.000 90.89150  ?  1452 GLY   B O   1 
ATOM   25441 N  N   . ILE   B 1 1455 ? 43.26500   11.64100  -4.74900  1.000 81.58957  ?  1453 ILE   B N   1 
ATOM   25442 C  CA  . ILE   B 1 1455 ? 42.84300   12.91600  -4.18300  1.000 83.56080  ?  1453 ILE   B CA  1 
ATOM   25443 C  C   . ILE   B 1 1455 ? 43.48300   14.05900  -4.95700  1.000 86.81769  ?  1453 ILE   B C   1 
ATOM   25444 O  O   . ILE   B 1 1455 ? 44.70800   14.10500  -5.13400  1.000 87.39902  ?  1453 ILE   B O   1 
ATOM   25445 C  CB  . ILE   B 1 1455 ? 43.19300   12.98800  -2.69000  1.000 80.09729  ?  1453 ILE   B CB  1 
ATOM   25446 C  CG1 . ILE   B 1 1455 ? 42.36600   11.96900  -1.89900  1.000 67.67757  ?  1453 ILE   B CG1 1 
ATOM   25447 C  CG2 . ILE   B 1 1455 ? 42.99500   14.40300  -2.15600  1.000 84.22867  ?  1453 ILE   B CG2 1 
ATOM   25448 C  CD1 . ILE   B 1 1455 ? 40.92700   11.86000  -2.35500  1.000 67.05174  ?  1453 ILE   B CD1 1 
ATOM   25449 N  N   . THR   B 1 1456 ? 42.65000   14.98300  -5.43100  1.000 85.59940  ?  1454 THR   B N   1 
ATOM   25450 C  CA  . THR   B 1 1456 ? 43.10500   16.19000  -6.10600  1.000 76.79631  ?  1454 THR   B CA  1 
ATOM   25451 C  C   . THR   B 1 1456 ? 42.98500   17.44000  -5.25000  1.000 70.94599  ?  1454 THR   B C   1 
ATOM   25452 O  O   . THR   B 1 1456 ? 43.79400   18.35700  -5.40300  1.000 78.83903  ?  1454 THR   B O   1 
ATOM   25453 C  CB  . THR   B 1 1456 ? 42.31800   16.40500  -7.40500  1.000 80.68229  ?  1454 THR   B CB  1 
ATOM   25454 O  OG1 . THR   B 1 1456 ? 40.94100   16.07000  -7.19000  1.000 81.16584  ?  1454 THR   B OG1 1 
ATOM   25455 C  CG2 . THR   B 1 1456 ? 42.87600   15.53900  -8.52200  1.000 85.05467  ?  1454 THR   B CG2 1 
ATOM   25456 N  N   . HIS   B 1 1457 ? 41.99600   17.49800  -4.36100  1.000 75.21796  ?  1455 HIS   B N   1 
ATOM   25457 C  CA  . HIS   B 1 1457 ? 41.79700   18.62300  -3.45600  1.000 72.44940  ?  1455 HIS   B CA  1 
ATOM   25458 C  C   . HIS   B 1 1457 ? 41.85200   18.10400  -2.02800  1.000 62.41747  ?  1455 HIS   B C   1 
ATOM   25459 O  O   . HIS   B 1 1457 ? 41.08200   17.21000  -1.66200  1.000 73.71962  ?  1455 HIS   B O   1 
ATOM   25460 C  CB  . HIS   B 1 1457 ? 40.45800   19.31900  -3.71400  1.000 64.92186  ?  1455 HIS   B CB  1 
ATOM   25461 C  CG  . HIS   B 1 1457 ? 40.35900   19.97800  -5.05500  1.000 75.50445  ?  1455 HIS   B CG  1 
ATOM   25462 N  ND1 . HIS   B 1 1457 ? 40.83500   19.39500  -6.21000  1.000 74.07691  ?  1455 HIS   B ND1 1 
ATOM   25463 C  CD2 . HIS   B 1 1457 ? 39.82400   21.16500  -5.42700  1.000 71.95870  ?  1455 HIS   B CD2 1 
ATOM   25464 C  CE1 . HIS   B 1 1457 ? 40.60200   20.19600  -7.23400  1.000 80.99691  ?  1455 HIS   B CE1 1 
ATOM   25465 N  NE2 . HIS   B 1 1457 ? 39.99100   21.27800  -6.78500  1.000 74.39529  ?  1455 HIS   B NE2 1 
ATOM   25466 N  N   . ILE   B 1 1458 ? 42.75600   18.65900  -1.22700  1.000 61.47854  ?  1456 ILE   B N   1 
ATOM   25467 C  CA  . ILE   B 1 1458 ? 42.86400   18.30500  0.18200   1.000 57.30315  ?  1456 ILE   B CA  1 
ATOM   25468 C  C   . ILE   B 1 1458 ? 43.05800   19.58400  0.98700   1.000 66.72056  ?  1456 ILE   B C   1 
ATOM   25469 O  O   . ILE   B 1 1458 ? 43.80100   20.48400  0.58000   1.000 60.97865  ?  1456 ILE   B O   1 
ATOM   25470 C  CB  . ILE   B 1 1458 ? 44.00300   17.29100  0.43400   1.000 54.57360  ?  1456 ILE   B CB  1 
ATOM   25471 C  CG1 . ILE   B 1 1458 ? 43.92700   16.73800  1.85600   1.000 57.65954  ?  1456 ILE   B CG1 1 
ATOM   25472 C  CG2 . ILE   B 1 1458 ? 45.37300   17.90700  0.17000   1.000 61.90186  ?  1456 ILE   B CG2 1 
ATOM   25473 C  CD1 . ILE   B 1 1458 ? 44.92700   15.64300  2.12100   1.000 55.43031  ?  1456 ILE   B CD1 1 
ATOM   25474 N  N   . ASN   B 1 1459 ? 42.36000   19.67600  2.11400   1.000 58.85169  ?  1457 ASN   B N   1 
ATOM   25475 C  CA  . ASN   B 1 1459 ? 42.43300   20.83700  2.98900   1.000 44.29727  ?  1457 ASN   B CA  1 
ATOM   25476 C  C   . ASN   B 1 1459 ? 43.26100   20.48800  4.21700   1.000 52.69991  ?  1457 ASN   B C   1 
ATOM   25477 O  O   . ASN   B 1 1459 ? 43.02600   19.45900  4.85900   1.000 63.11967  ?  1457 ASN   B O   1 
ATOM   25478 C  CB  . ASN   B 1 1459 ? 41.03500   21.30300  3.39800   1.000 55.01365  ?  1457 ASN   B CB  1 
ATOM   25479 C  CG  . ASN   B 1 1459 ? 40.24500   21.87300  2.23300   1.000 55.02750  ?  1457 ASN   B CG  1 
ATOM   25480 O  OD1 . ASN   B 1 1459 ? 40.65800   21.76700  1.07900   1.000 56.44971  ?  1457 ASN   B OD1 1 
ATOM   25481 N  ND2 . ASN   B 1 1459 ? 39.10200   22.47800  2.53300   1.000 59.43809  ?  1457 ASN   B ND2 1 
ATOM   25482 N  N   . PHE   B 1 1460 ? 44.22900   21.34200  4.53600   1.000 61.60434  ?  1458 PHE   B N   1 
ATOM   25483 C  CA  . PHE   B 1 1460 ? 45.14300   21.10700  5.64100   1.000 67.52747  ?  1458 PHE   B CA  1 
ATOM   25484 C  C   . PHE   B 1 1460 ? 45.19500   22.32300  6.55200   1.000 67.05545  ?  1458 PHE   B C   1 
ATOM   25485 O  O   . PHE   B 1 1460 ? 45.00300   23.46200  6.11500   1.000 58.05548  ?  1458 PHE   B O   1 
ATOM   25486 C  CB  . PHE   B 1 1460 ? 46.56400   20.79300  5.14500   1.000 74.99903  ?  1458 PHE   B CB  1 
ATOM   25487 C  CG  . PHE   B 1 1460 ? 46.89400   19.32900  5.12900   1.000 66.40964  ?  1458 PHE   B CG  1 
ATOM   25488 C  CD1 . PHE   B 1 1460 ? 47.11500   18.64300  6.31300   1.000 68.89931  ?  1458 PHE   B CD1 1 
ATOM   25489 C  CD2 . PHE   B 1 1460 ? 47.00300   18.64300  3.93200   1.000 51.29646  ?  1458 PHE   B CD2 1 
ATOM   25490 C  CE1 . PHE   B 1 1460 ? 47.42500   17.29500  6.30300   1.000 55.16761  ?  1458 PHE   B CE1 1 
ATOM   25491 C  CE2 . PHE   B 1 1460 ? 47.31600   17.29700  3.91600   1.000 56.83594  ?  1458 PHE   B CE2 1 
ATOM   25492 C  CZ  . PHE   B 1 1460 ? 47.52600   16.62200  5.10300   1.000 58.16394  ?  1458 PHE   B CZ  1 
ATOM   25493 N  N   . VAL   B 1 1461 ? 45.45400   22.06500  7.82800   1.000 73.05588  ?  1459 VAL   B N   1 
ATOM   25494 C  CA  . VAL   B 1 1461 ? 45.81800   23.11200  8.77500   1.000 67.83948  ?  1459 VAL   B CA  1 
ATOM   25495 C  C   . VAL   B 1 1461 ? 47.34100   23.17500  8.76100   1.000 80.88632  ?  1459 VAL   B C   1 
ATOM   25496 O  O   . VAL   B 1 1461 ? 47.99300   22.12100  8.71400   1.000 89.15737  ?  1459 VAL   B O   1 
ATOM   25497 C  CB  . VAL   B 1 1461 ? 45.26300   22.82300  10.17900  1.000 68.54821  ?  1459 VAL   B CB  1 
ATOM   25498 C  CG1 . VAL   B 1 1461 ? 45.17600   24.10100  10.99900  1.000 64.73825  ?  1459 VAL   B CG1 1 
ATOM   25499 C  CG2 . VAL   B 1 1461 ? 43.90100   22.15000  10.08200  1.000 100.68934 ?  1459 VAL   B CG2 1 
ATOM   25500 N  N   . PRO   B 1 1462 ? 47.94900   24.36600  8.76300   1.000 84.14013  ?  1460 PRO   B N   1 
ATOM   25501 C  CA  . PRO   B 1 1462 ? 49.42000   24.43800  8.68900   1.000 80.16054  ?  1460 PRO   B CA  1 
ATOM   25502 C  C   . PRO   B 1 1462 ? 50.14100   23.62100  9.75100   1.000 70.83998  ?  1460 PRO   B C   1 
ATOM   25503 O  O   . PRO   B 1 1462 ? 51.18000   23.01800  9.45500   1.000 64.22966  ?  1460 PRO   B O   1 
ATOM   25504 C  CB  . PRO   B 1 1462 ? 49.69300   25.94000  8.84200   1.000 77.33657  ?  1460 PRO   B CB  1 
ATOM   25505 C  CG  . PRO   B 1 1462 ? 48.47700   26.58700  8.27700   1.000 69.29649  ?  1460 PRO   B CG  1 
ATOM   25506 C  CD  . PRO   B 1 1462 ? 47.32600   25.69800  8.66400   1.000 69.14143  ?  1460 PRO   B CD  1 
ATOM   25507 N  N   . SER   B 1 1463 ? 49.61600   23.57600  10.97900  1.000 67.66596  ?  1461 SER   B N   1 
ATOM   25508 C  CA  . SER   B 1 1463 ? 50.24700   22.78300  12.02900  1.000 71.50899  ?  1461 SER   B CA  1 
ATOM   25509 C  C   . SER   B 1 1463 ? 50.17700   21.28700  11.75100  1.000 73.39813  ?  1461 SER   B C   1 
ATOM   25510 O  O   . SER   B 1 1463 ? 51.00600   20.53300  12.27100  1.000 59.86837  ?  1461 SER   B O   1 
ATOM   25511 C  CB  . SER   B 1 1463 ? 49.60300   23.08700  13.38400  1.000 54.15527  ?  1461 SER   B CB  1 
ATOM   25512 O  OG  . SER   B 1 1463 ? 48.22300   22.76700  13.38000  1.000 79.87700  ?  1461 SER   B OG  1 
ATOM   25513 N  N   . MET   B 1 1464 ? 49.21000   20.84200  10.94800  1.000 80.58509  ?  1462 MET   B N   1 
ATOM   25514 C  CA  . MET   B 1 1464 ? 49.07200   19.43600  10.59800  1.000 68.84807  ?  1462 MET   B CA  1 
ATOM   25515 C  C   . MET   B 1 1464 ? 49.65600   19.09800  9.23400   1.000 80.05537  ?  1462 MET   B C   1 
ATOM   25516 O  O   . MET   B 1 1464 ? 49.81300   17.91200  8.92300   1.000 89.11054  ?  1462 MET   B O   1 
ATOM   25517 C  CB  . MET   B 1 1464 ? 47.59500   19.02400  10.63700  1.000 54.04004  ?  1462 MET   B CB  1 
ATOM   25518 C  CG  . MET   B 1 1464 ? 47.06900   18.75900  12.03700  1.000 57.61635  ?  1462 MET   B CG  1 
ATOM   25519 S  SD  . MET   B 1 1464 ? 47.26900   17.03500  12.52900  1.000 99.93361  ?  1462 MET   B SD  1 
ATOM   25520 C  CE  . MET   B 1 1464 ? 47.13600   17.16000  14.31200  1.000 56.05837  ?  1462 MET   B CE  1 
ATOM   25521 N  N   . LEU   B 1 1465 ? 49.97900   20.10200  8.41400   1.000 69.73574  ?  1463 LEU   B N   1 
ATOM   25522 C  CA  . LEU   B 1 1465 ? 50.63000   19.83000  7.13900   1.000 65.50392  ?  1463 LEU   B CA  1 
ATOM   25523 C  C   . LEU   B 1 1465 ? 52.11200   19.52600  7.32300   1.000 82.17089  ?  1463 LEU   B C   1 
ATOM   25524 O  O   . LEU   B 1 1465 ? 52.71300   18.85200  6.48200   1.000 83.12770  ?  1463 LEU   B O   1 
ATOM   25525 C  CB  . LEU   B 1 1465 ? 50.43200   21.01600  6.19000   1.000 66.42669  ?  1463 LEU   B CB  1 
ATOM   25526 C  CG  . LEU   B 1 1465 ? 50.95400   20.92300  4.75100   1.000 61.96258  ?  1463 LEU   B CG  1 
ATOM   25527 C  CD1 . LEU   B 1 1465 ? 50.69200   19.55200  4.15500   1.000 61.34314  ?  1463 LEU   B CD1 1 
ATOM   25528 C  CD2 . LEU   B 1 1465 ? 50.31000   22.00100  3.89100   1.000 53.26057  ?  1463 LEU   B CD2 1 
ATOM   25529 N  N   . ILE   B 1 1466 ? 52.70700   20.00500  8.42200   1.000 80.59654  ?  1464 ILE   B N   1 
ATOM   25530 C  CA  . ILE   B 1 1466 ? 54.11100   19.70300  8.70100   1.000 80.50747  ?  1464 ILE   B CA  1 
ATOM   25531 C  C   . ILE   B 1 1466 ? 54.34400   18.20500  8.83700   1.000 73.69499  ?  1464 ILE   B C   1 
ATOM   25532 O  O   . ILE   B 1 1466 ? 55.21300   17.67300  8.12500   1.000 84.44493  ?  1464 ILE   B O   1 
ATOM   25533 C  CB  . ILE   B 1 1466 ? 54.58200   20.49100  9.94400   1.000 73.63268  ?  1464 ILE   B CB  1 
ATOM   25534 C  CG1 . ILE   B 1 1466 ? 54.50100   22.00100  9.69800   1.000 63.94586  ?  1464 ILE   B CG1 1 
ATOM   25535 C  CG2 . ILE   B 1 1466 ? 55.98800   20.07600  10.32700  1.000 79.64127  ?  1464 ILE   B CG2 1 
ATOM   25536 C  CD1 . ILE   B 1 1466 ? 54.67200   22.82900  10.95800  1.000 64.23619  ?  1464 ILE   B CD1 1 
ATOM   25537 N  N   . PRO   B 1 1467 ? 53.62200   17.46400  9.69000   1.000 72.00270  ?  1465 PRO   B N   1 
ATOM   25538 C  CA  . PRO   B 1 1467 ? 53.89800   16.02300  9.79900   1.000 69.68320  ?  1465 PRO   B CA  1 
ATOM   25539 C  C   . PRO   B 1 1467 ? 53.60900   15.26500  8.52400   1.000 70.40715  ?  1465 PRO   B C   1 
ATOM   25540 O  O   . PRO   B 1 1467 ? 54.26900   14.25100  8.26100   1.000 76.23706  ?  1465 PRO   B O   1 
ATOM   25541 C  CB  . PRO   B 1 1467 ? 52.97300   15.56400  10.93800  1.000 63.31774  ?  1465 PRO   B CB  1 
ATOM   25542 C  CG  . PRO   B 1 1467 ? 52.61900   16.80000  11.66900  1.000 70.70077  ?  1465 PRO   B CG  1 
ATOM   25543 C  CD  . PRO   B 1 1467 ? 52.55200   17.85700  10.61800  1.000 73.98679  ?  1465 PRO   B CD  1 
ATOM   25544 N  N   . PHE   B 1 1468 ? 52.61500   15.70500  7.74900   1.000 68.02808  ?  1466 PHE   B N   1 
ATOM   25545 C  CA  . PHE   B 1 1468 ? 52.42700   15.21800  6.39100   1.000 63.17726  ?  1466 PHE   B CA  1 
ATOM   25546 C  C   . PHE   B 1 1468 ? 53.77900   15.32700  5.69900   1.000 73.20933  ?  1466 PHE   B C   1 
ATOM   25547 O  O   . PHE   B 1 1468 ? 54.51500   14.33700  5.61800   1.000 86.69248  ?  1466 PHE   B O   1 
ATOM   25548 C  CB  . PHE   B 1 1468 ? 51.33800   16.02800  5.66900   1.000 55.79932  ?  1466 PHE   B CB  1 
ATOM   25549 C  CG  . PHE   B 1 1468 ? 50.84600   15.41000  4.37300   1.000 55.66602  ?  1466 PHE   B CG  1 
ATOM   25550 C  CD1 . PHE   B 1 1468 ? 50.32600   14.12300  4.34200   1.000 59.21568  ?  1466 PHE   B CD1 1 
ATOM   25551 C  CD2 . PHE   B 1 1468 ? 50.86700   16.14100  3.19300   1.000 62.39560  ?  1466 PHE   B CD2 1 
ATOM   25552 C  CE1 . PHE   B 1 1468 ? 49.86700   13.57100  3.15100   1.000 67.71295  ?  1466 PHE   B CE1 1 
ATOM   25553 C  CE2 . PHE   B 1 1468 ? 50.40900   15.59600  2.00600   1.000 48.03062  ?  1466 PHE   B CE2 1 
ATOM   25554 C  CZ  . PHE   B 1 1468 ? 49.91000   14.31100  1.98400   1.000 49.79901  ?  1466 PHE   B CZ  1 
ATOM   25555 N  N   . VAL   B 1 1469 ? 54.13700   16.54000  5.26700   1.000 86.04335  ?  1467 VAL   B N   1 
ATOM   25556 C  CA  . VAL   B 1 1469 ? 55.40300   16.82900  4.59500   1.000 92.13839  ?  1467 VAL   B CA  1 
ATOM   25557 C  C   . VAL   B 1 1469 ? 56.57300   16.07200  5.21600   1.000 86.98793  ?  1467 VAL   B C   1 
ATOM   25558 O  O   . VAL   B 1 1469 ? 57.41400   15.52000  4.49800   1.000 82.51986  ?  1467 VAL   B O   1 
ATOM   25559 C  CB  . VAL   B 1 1469 ? 55.67300   18.34400  4.60400   1.000 89.14488  ?  1467 VAL   B CB  1 
ATOM   25560 C  CG1 . VAL   B 1 1469 ? 57.12900   18.63800  4.25500   1.000 97.03319  ?  1467 VAL   B CG1 1 
ATOM   25561 C  CG2 . VAL   B 1 1469 ? 54.74800   19.04100  3.63200   1.000 73.22398  ?  1467 VAL   B CG2 1 
ATOM   25562 N  N   . GLU   B 1 1470 ? 56.62300   16.01700  6.54900   1.000 82.56987  ?  1468 GLU   B N   1 
ATOM   25563 C  CA  . GLU   B 1 1470 ? 57.69900   15.32700  7.25500   1.000 87.00008  ?  1468 GLU   B CA  1 
ATOM   25564 C  C   . GLU   B 1 1470 ? 57.59300   13.80900  7.15000   1.000 86.46260  ?  1468 GLU   B C   1 
ATOM   25565 O  O   . GLU   B 1 1470 ? 58.22100   13.08600  7.93000   1.000 81.84586  ?  1468 GLU   B O   1 
ATOM   25566 C  CB  . GLU   B 1 1470 ? 57.71500   15.73800  8.73100   1.000 73.78313  ?  1468 GLU   B CB  1 
ATOM   25567 C  CG  . GLU   B 1 1470 ? 58.33700   17.09800  9.00600   1.000 85.67568  ?  1468 GLU   B CG  1 
ATOM   25568 C  CD  . GLU   B 1 1470 ? 58.41100   17.41000  10.48800  1.000 99.48007  ?  1468 GLU   B CD  1 
ATOM   25569 O  OE1 . GLU   B 1 1470 ? 57.83200   16.64500  11.28700  1.000 99.83348  ?  1468 GLU   B OE1 1 
ATOM   25570 O  OE2 . GLU   B 1 1470 ? 59.05100   18.41600  10.85800  1.000 104.24991 -1 1468 GLU   B OE2 1 
ATOM   25571 N  N   . TYR   B 1 1471 ? 56.81400   13.31800  6.20900   1.000 78.05317  ?  1469 TYR   B N   1 
ATOM   25572 C  CA  . TYR   B 1 1471 ? 56.61800   11.88700  6.00800   1.000 82.15534  ?  1469 TYR   B CA  1 
ATOM   25573 C  C   . TYR   B 1 1471 ? 56.78400   11.49400  4.54800   1.000 94.81585  ?  1469 TYR   B C   1 
ATOM   25574 O  O   . TYR   B 1 1471 ? 57.28100   10.39900  4.25900   1.000 111.23216 ?  1469 TYR   B O   1 
ATOM   25575 C  CB  . TYR   B 1 1471 ? 55.23800   11.46500  6.53500   1.000 87.96791  ?  1469 TYR   B CB  1 
ATOM   25576 C  CG  . TYR   B 1 1471 ? 54.57400   10.31700  5.80300   1.000 92.55908  ?  1469 TYR   B CG  1 
ATOM   25577 C  CD1 . TYR   B 1 1471 ? 54.80000   9.00200   6.18400   1.000 84.78164  ?  1469 TYR   B CD1 1 
ATOM   25578 C  CD2 . TYR   B 1 1471 ? 53.70000   10.55200  4.74600   1.000 86.01446  ?  1469 TYR   B CD2 1 
ATOM   25579 C  CE1 . TYR   B 1 1471 ? 54.19100   7.95000   5.52500   1.000 68.45157  ?  1469 TYR   B CE1 1 
ATOM   25580 C  CE2 . TYR   B 1 1471 ? 53.09000   9.50700   4.08000   1.000 87.57527  ?  1469 TYR   B CE2 1 
ATOM   25581 C  CZ  . TYR   B 1 1471 ? 53.33600   8.20800   4.47300   1.000 83.53089  ?  1469 TYR   B CZ  1 
ATOM   25582 O  OH  . TYR   B 1 1471 ? 52.72500   7.16800   3.81100   1.000 89.64088  ?  1469 TYR   B OH  1 
ATOM   25583 N  N   . LEU   B 1 1472 ? 56.37800   12.35900  3.61300   1.000 92.57269  ?  1470 LEU   B N   1 
ATOM   25584 C  CA  . LEU   B 1 1472 ? 56.52600   12.07300  2.19500   1.000 93.27981  ?  1470 LEU   B CA  1 
ATOM   25585 C  C   . LEU   B 1 1472 ? 57.90100   12.47700  1.66800   1.000 103.69752 ?  1470 LEU   B C   1 
ATOM   25586 O  O   . LEU   B 1 1472 ? 58.05200   12.65700  0.45400   1.000 105.68855 ?  1470 LEU   B O   1 
ATOM   25587 C  CB  . LEU   B 1 1472 ? 55.42800   12.76800  1.37500   1.000 88.47901  ?  1470 LEU   B CB  1 
ATOM   25588 C  CG  . LEU   B 1 1472 ? 53.93700   12.74400  1.73700   1.000 84.92549  ?  1470 LEU   B CG  1 
ATOM   25589 C  CD1 . LEU   B 1 1472 ? 53.68400   13.83100  2.75000   1.000 71.89360  ?  1470 LEU   B CD1 1 
ATOM   25590 C  CD2 . LEU   B 1 1472 ? 53.06500   12.99600  0.53100   1.000 73.13141  ?  1470 LEU   B CD2 1 
ATOM   25591 N  N   . GLU   B 1 1473 ? 58.89600   12.61100  2.55600   1.000 115.90994 ?  1471 GLU   B N   1 
ATOM   25592 C  CA  . GLU   B 1 1473 ? 60.23200   13.03300  2.14100   1.000 114.85491 ?  1471 GLU   B CA  1 
ATOM   25593 C  C   . GLU   B 1 1473 ? 60.86200   12.03700  1.17500   1.000 123.05231 ?  1471 GLU   B C   1 
ATOM   25594 O  O   . GLU   B 1 1473 ? 61.49700   12.43200  0.19000   1.000 106.33972 ?  1471 GLU   B O   1 
ATOM   25595 C  CB  . GLU   B 1 1473 ? 61.12000   13.23000  3.37300   1.000 91.05010  ?  1471 GLU   B CB  1 
ATOM   25596 C  CG  . GLU   B 1 1473 ? 60.96700   12.15500  4.45500   1.000 108.90573 ?  1471 GLU   B CG  1 
ATOM   25597 C  CD  . GLU   B 1 1473 ? 61.78400   10.90500  4.17400   1.000 125.16074 ?  1471 GLU   B CD  1 
ATOM   25598 O  OE1 . GLU   B 1 1473 ? 62.92200   11.03800  3.68000   1.000 129.27345 ?  1471 GLU   B OE1 1 
ATOM   25599 O  OE2 . GLU   B 1 1473 ? 61.28100   9.79000   4.43400   1.000 117.67075 -1 1471 GLU   B OE2 1 
ATOM   25600 N  N   . GLY   B 1 1474 ? 60.69200   10.74300  1.43300   1.000 122.36137 ?  1472 GLY   B N   1 
ATOM   25601 C  CA  . GLY   B 1 1474 ? 61.34100   9.72600   0.63200   1.000 114.53493 ?  1472 GLY   B CA  1 
ATOM   25602 C  C   . GLY   B 1 1474 ? 60.38800   8.96800   -0.26600  1.000 114.25190 ?  1472 GLY   B C   1 
ATOM   25603 O  O   . GLY   B 1 1474 ? 60.79400   8.43600   -1.30300  1.000 117.98380 ?  1472 GLY   B O   1 
ATOM   25604 N  N   . ARG   B 1 1475 ? 59.11600   8.91600   0.12400   1.000 103.15106 ?  1473 ARG   B N   1 
ATOM   25605 C  CA  . ARG   B 1 1475 ? 58.12300   8.18600   -0.65200  1.000 100.32849 ?  1473 ARG   B CA  1 
ATOM   25606 C  C   . ARG   B 1 1475 ? 58.00400   8.77100   -2.05400  1.000 100.86234 ?  1473 ARG   B C   1 
ATOM   25607 O  O   . ARG   B 1 1475 ? 57.92200   9.99000   -2.22800  1.000 102.51386 ?  1473 ARG   B O   1 
ATOM   25608 C  CB  . ARG   B 1 1475 ? 56.77000   8.22300   0.05800   1.000 91.91149  ?  1473 ARG   B CB  1 
ATOM   25609 N  N   . THR   B 1 1476 ? 58.00600   7.89200   -3.05600  1.000 105.66727 ?  1474 THR   B N   1 
ATOM   25610 C  CA  . THR   B 1 1476 ? 57.90100   8.28700   -4.45500  1.000 109.64185 ?  1474 THR   B CA  1 
ATOM   25611 C  C   . THR   B 1 1476 ? 56.64300   7.72000   -5.10500  1.000 107.89329 ?  1474 THR   B C   1 
ATOM   25612 O  O   . THR   B 1 1476 ? 56.62600   7.44300   -6.30600  1.000 96.52386  ?  1474 THR   B O   1 
ATOM   25613 C  CB  . THR   B 1 1476 ? 59.14500   7.86300   -5.23700  1.000 115.02885 ?  1474 THR   B CB  1 
ATOM   25614 O  OG1 . THR   B 1 1476 ? 59.36400   6.45700   -5.06800  1.000 121.51650 ?  1474 THR   B OG1 1 
ATOM   25615 C  CG2 . THR   B 1 1476 ? 60.36700   8.62800   -4.74900  1.000 113.26402 ?  1474 THR   B CG2 1 
ATOM   25616 N  N   . GLU   B 1 1477 ? 55.58500   7.53800   -4.31800  1.000 103.95929 ?  1475 GLU   B N   1 
ATOM   25617 C  CA  . GLU   B 1 1477 ? 54.31000   7.10600   -4.87000  1.000 81.16638  ?  1475 GLU   B CA  1 
ATOM   25618 C  C   . GLU   B 1 1477 ? 53.71500   8.20100   -5.75100  1.000 87.84958  ?  1475 GLU   B C   1 
ATOM   25619 O  O   . GLU   B 1 1477 ? 53.94700   9.39500   -5.53900  1.000 94.72707  ?  1475 GLU   B O   1 
ATOM   25620 C  CB  . GLU   B 1 1477 ? 53.33000   6.74400   -3.75200  1.000 60.89243  ?  1475 GLU   B CB  1 
ATOM   25621 C  CG  . GLU   B 1 1477 ? 53.71900   5.52500   -2.91700  1.000 78.38861  ?  1475 GLU   B CG  1 
ATOM   25622 C  CD  . GLU   B 1 1477 ? 54.78600   5.82700   -1.87500  1.000 85.52885  ?  1475 GLU   B CD  1 
ATOM   25623 O  OE1 . GLU   B 1 1477 ? 55.95400   6.04400   -2.26000  1.000 104.23803 ?  1475 GLU   B OE1 1 
ATOM   25624 O  OE2 . GLU   B 1 1477 ? 54.45400   5.84900   -0.67000  1.000 50.00950  ?  1475 GLU   B OE2 1 
ATOM   25625 N  N   . ALA   B 1 1478 ? 52.94100   7.78000   -6.74900  1.000 82.43254  ?  1476 ALA   B N   1 
ATOM   25626 C  CA  . ALA   B 1 1478 ? 52.35300   8.69700   -7.71400  1.000 88.63855  ?  1476 ALA   B CA  1 
ATOM   25627 C  C   . ALA   B 1 1478 ? 50.99500   9.18100   -7.22500  1.000 95.48515  ?  1476 ALA   B C   1 
ATOM   25628 O  O   . ALA   B 1 1478 ? 50.16600   8.38500   -6.77000  1.000 85.13134  ?  1476 ALA   B O   1 
ATOM   25629 C  CB  . ALA   B 1 1478 ? 52.21000   8.03100   -9.08300  1.000 85.10240  ?  1476 ALA   B CB  1 
ATOM   25630 N  N   . ASN   B 1 1479 ? 50.77400   10.48800  -7.33400  1.000 106.85105 ?  1477 ASN   B N   1 
ATOM   25631 C  CA  . ASN   B 1 1479 ? 49.55000   11.13000  -6.88600  1.000 98.03043  ?  1477 ASN   B CA  1 
ATOM   25632 C  C   . ASN   B 1 1479 ? 49.03200   12.05400  -7.97700  1.000 89.02523  ?  1477 ASN   B C   1 
ATOM   25633 O  O   . ASN   B 1 1479 ? 49.78500   12.52000  -8.83800  1.000 86.18017  ?  1477 ASN   B O   1 
ATOM   25634 C  CB  . ASN   B 1 1479 ? 49.77800   11.92700  -5.59200  1.000 83.39382  ?  1477 ASN   B CB  1 
ATOM   25635 C  CG  . ASN   B 1 1479 ? 50.98300   12.85400  -5.67800  1.000 99.26600  ?  1477 ASN   B CG  1 
ATOM   25636 O  OD1 . ASN   B 1 1479 ? 52.03500   12.57900  -5.09900  1.000 104.71340 ?  1477 ASN   B OD1 1 
ATOM   25637 N  ND2 . ASN   B 1 1479 ? 50.83400   13.95900  -6.40300  1.000 94.77417  ?  1477 ASN   B ND2 1 
ATOM   25638 N  N   . ARG   B 1 1480 ? 47.72500   12.31200  -7.93300  1.000 76.75255  ?  1478 ARG   B N   1 
ATOM   25639 C  CA  . ARG   B 1 1480 ? 47.09600   13.31700  -8.77500  1.000 88.34420  ?  1478 ARG   B CA  1 
ATOM   25640 C  C   . ARG   B 1 1480 ? 46.80300   14.60600  -8.01200  1.000 94.38437  ?  1478 ARG   B C   1 
ATOM   25641 O  O   . ARG   B 1 1480 ? 46.02700   15.43900  -8.49200  1.000 83.49997  ?  1478 ARG   B O   1 
ATOM   25642 C  CB  . ARG   B 1 1480 ? 45.81400   12.76600  -9.40100  1.000 76.75325  ?  1478 ARG   B CB  1 
ATOM   25643 C  CG  . ARG   B 1 1480 ? 45.96700   12.40600  -10.87100 1.000 92.27805  ?  1478 ARG   B CG  1 
ATOM   25644 C  CD  . ARG   B 1 1480 ? 44.70800   11.77800  -11.44900 1.000 86.42210  ?  1478 ARG   B CD  1 
ATOM   25645 N  NE  . ARG   B 1 1480 ? 43.93700   12.71300  -12.26000 1.000 90.56778  ?  1478 ARG   B NE  1 
ATOM   25646 C  CZ  . ARG   B 1 1480 ? 42.77200   13.23600  -11.90300 1.000 103.33150 ?  1478 ARG   B CZ  1 
ATOM   25647 N  NH1 . ARG   B 1 1480 ? 42.20700   12.93800  -10.74400 1.000 88.41485  ?  1478 ARG   B NH1 1 
ATOM   25648 N  NH2 . ARG   B 1 1480 ? 42.15500   14.07400  -12.73200 1.000 86.02881  ?  1478 ARG   B NH2 1 
ATOM   25649 N  N   . LEU   B 1 1481 ? 47.41600   14.78600  -6.83700  1.000 94.69069  ?  1479 LEU   B N   1 
ATOM   25650 C  CA  . LEU   B 1 1481 ? 47.20000   15.98500  -6.03300  1.000 72.87833  ?  1479 LEU   B CA  1 
ATOM   25651 C  C   . LEU   B 1 1481 ? 47.47900   17.24400  -6.84300  1.000 79.64136  ?  1479 LEU   B C   1 
ATOM   25652 O  O   . LEU   B 1 1481 ? 48.48600   17.33200  -7.55200  1.000 98.23774  ?  1479 LEU   B O   1 
ATOM   25653 C  CB  . LEU   B 1 1481 ? 48.08900   15.95400  -4.78800  1.000 68.35983  ?  1479 LEU   B CB  1 
ATOM   25654 C  CG  . LEU   B 1 1481 ? 47.37600   15.94700  -3.43400  1.000 63.43458  ?  1479 LEU   B CG  1 
ATOM   25655 C  CD1 . LEU   B 1 1481 ? 48.38000   16.06200  -2.29600  1.000 48.68161  ?  1479 LEU   B CD1 1 
ATOM   25656 C  CD2 . LEU   B 1 1481 ? 46.34200   17.06200  -3.36200  1.000 77.57004  ?  1479 LEU   B CD2 1 
ATOM   25657 N  N   . ARG   B 1 1482 ? 46.58100   18.21600  -6.73200  1.000 74.49705  ?  1480 ARG   B N   1 
ATOM   25658 C  CA  . ARG   B 1 1482 ? 46.65900   19.44400  -7.51400  1.000 82.49162  ?  1480 ARG   B CA  1 
ATOM   25659 C  C   . ARG   B 1 1482 ? 46.65300   20.69800  -6.65600  1.000 84.62870  ?  1480 ARG   B C   1 
ATOM   25660 O  O   . ARG   B 1 1482 ? 47.45400   21.60900  -6.89500  1.000 83.55502  ?  1480 ARG   B O   1 
ATOM   25661 C  CB  . ARG   B 1 1482 ? 45.49900   19.49600  -8.51500  1.000 61.57569  ?  1480 ARG   B CB  1 
ATOM   25662 C  CG  . ARG   B 1 1482 ? 45.58900   20.61300  -9.53900  1.000 78.27868  ?  1480 ARG   B CG  1 
ATOM   25663 C  CD  . ARG   B 1 1482 ? 44.75900   20.27500  -10.76600 1.000 75.48750  ?  1480 ARG   B CD  1 
ATOM   25664 N  NE  . ARG   B 1 1482 ? 43.73900   19.27800  -10.46600 1.000 69.75371  ?  1480 ARG   B NE  1 
ATOM   25665 C  CZ  . ARG   B 1 1482 ? 42.91000   18.75900  -11.36000 1.000 77.94139  ?  1480 ARG   B CZ  1 
ATOM   25666 N  NH1 . ARG   B 1 1482 ? 42.93900   19.13300  -12.62900 1.000 80.54722  ?  1480 ARG   B NH1 1 
ATOM   25667 N  NH2 . ARG   B 1 1482 ? 42.03100   17.83900  -10.97300 1.000 78.89441  ?  1480 ARG   B NH2 1 
ATOM   25668 N  N   . TYR   B 1 1483 ? 45.77800   20.77200  -5.65600  1.000 80.17597  ?  1481 TYR   B N   1 
ATOM   25669 C  CA  . TYR   B 1 1483 ? 45.71000   21.91300  -4.75400  1.000 71.43189  ?  1481 TYR   B CA  1 
ATOM   25670 C  C   . TYR   B 1 1483 ? 45.76100   21.42500  -3.31400  1.000 65.92023  ?  1481 TYR   B C   1 
ATOM   25671 O  O   . TYR   B 1 1483 ? 44.94500   20.58900  -2.91000  1.000 66.17775  ?  1481 TYR   B O   1 
ATOM   25672 C  CB  . TYR   B 1 1483 ? 44.43100   22.72700  -4.96900  1.000 67.89745  ?  1481 TYR   B CB  1 
ATOM   25673 C  CG  . TYR   B 1 1483 ? 44.08300   23.00400  -6.41400  1.000 76.52126  ?  1481 TYR   B CG  1 
ATOM   25674 C  CD1 . TYR   B 1 1483 ? 44.66400   24.06100  -7.10100  1.000 71.05744  ?  1481 TYR   B CD1 1 
ATOM   25675 C  CD2 . TYR   B 1 1483 ? 43.15500   22.21900  -7.08400  1.000 75.13628  ?  1481 TYR   B CD2 1 
ATOM   25676 C  CE1 . TYR   B 1 1483 ? 44.33900   24.32000  -8.42100  1.000 74.50253  ?  1481 TYR   B CE1 1 
ATOM   25677 C  CE2 . TYR   B 1 1483 ? 42.82200   22.47000  -8.40100  1.000 80.34303  ?  1481 TYR   B CE2 1 
ATOM   25678 C  CZ  . TYR   B 1 1483 ? 43.41700   23.52000  -9.06600  1.000 84.90959  ?  1481 TYR   B CZ  1 
ATOM   25679 O  OH  . TYR   B 1 1483 ? 43.08600   23.77000  -10.37900 1.000 80.20578  ?  1481 TYR   B OH  1 
ATOM   25680 N  N   . ILE   B 1 1484 ? 46.71200   21.94500  -2.54700  1.000 64.82984  ?  1482 ILE   B N   1 
ATOM   25681 C  CA  . ILE   B 1 1484 ? 46.71500   21.80900  -1.09500  1.000 59.72120  ?  1482 ILE   B CA  1 
ATOM   25682 C  C   . ILE   B 1 1484 ? 46.25300   23.14400  -0.52500  1.000 73.67877  ?  1482 ILE   B C   1 
ATOM   25683 O  O   . ILE   B 1 1484 ? 46.98800   24.13700  -0.56200  1.000 69.73652  ?  1482 ILE   B O   1 
ATOM   25684 C  CB  . ILE   B 1 1484 ? 48.09200   21.40600  -0.55200  1.000 57.47830  ?  1482 ILE   B CB  1 
ATOM   25685 C  CG1 . ILE   B 1 1484 ? 48.37700   19.93600  -0.86400  1.000 71.79820  ?  1482 ILE   B CG1 1 
ATOM   25686 C  CG2 . ILE   B 1 1484 ? 48.16300   21.63800  0.95200   1.000 63.38057  ?  1482 ILE   B CG2 1 
ATOM   25687 C  CD1 . ILE   B 1 1484 ? 49.59400   19.38200  -0.15200  1.000 46.72638  ?  1482 ILE   B CD1 1 
ATOM   25688 N  N   . LEU   B 1 1485 ? 45.02600   23.17100  -0.01400  1.000 76.96317  ?  1483 LEU   B N   1 
ATOM   25689 C  CA  . LEU   B 1 1485 ? 44.39800   24.38900  0.48100   1.000 52.35428  ?  1483 LEU   B CA  1 
ATOM   25690 C  C   . LEU   B 1 1485 ? 44.59800   24.47300  1.98900   1.000 58.99598  ?  1483 LEU   B C   1 
ATOM   25691 O  O   . LEU   B 1 1485 ? 44.08900   23.62900  2.73400   1.000 51.01144  ?  1483 LEU   B O   1 
ATOM   25692 C  CB  . LEU   B 1 1485 ? 42.91200   24.40400  0.12300   1.000 37.03602  ?  1483 LEU   B CB  1 
ATOM   25693 C  CG  . LEU   B 1 1485 ? 42.61500   24.11300  -1.35200  1.000 49.01205  ?  1483 LEU   B CG  1 
ATOM   25694 C  CD1 . LEU   B 1 1485 ? 41.17100   23.68500  -1.54700  1.000 45.90619  ?  1483 LEU   B CD1 1 
ATOM   25695 C  CD2 . LEU   B 1 1485 ? 42.93600   25.32200  -2.22000  1.000 60.90081  ?  1483 LEU   B CD2 1 
ATOM   25696 N  N   . ALA   B 1 1486 ? 45.33800   25.48600  2.43300   1.000 59.24120  ?  1484 ALA   B N   1 
ATOM   25697 C  CA  . ALA   B 1 1486 ? 45.70100   25.64400  3.83300   1.000 55.27710  ?  1484 ALA   B CA  1 
ATOM   25698 C  C   . ALA   B 1 1486 ? 44.87700   26.75200  4.47300   1.000 69.88208  ?  1484 ALA   B C   1 
ATOM   25699 O  O   . ALA   B 1 1486 ? 44.71000   27.83100  3.89500   1.000 67.54066  ?  1484 ALA   B O   1 
ATOM   25700 C  CB  . ALA   B 1 1486 ? 47.19300   25.95300  3.98200   1.000 53.70233  ?  1484 ALA   B CB  1 
ATOM   25701 N  N   . CYS   B 1 1487 ? 44.37000   26.47900  5.67300   1.000 57.64902  ?  1485 CYS   B N   1 
ATOM   25702 C  CA  . CYS   B 1 1487 ? 43.57900   27.44800  6.41600   1.000 38.26509  ?  1485 CYS   B CA  1 
ATOM   25703 C  C   . CYS   B 1 1487 ? 43.56200   27.03800  7.88000   1.000 49.79883  ?  1485 CYS   B C   1 
ATOM   25704 O  O   . CYS   B 1 1487 ? 43.75500   25.86700  8.21800   1.000 66.82873  ?  1485 CYS   B O   1 
ATOM   25705 C  CB  . CYS   B 1 1487 ? 42.15200   27.55400  5.86400   1.000 36.20384  ?  1485 CYS   B CB  1 
ATOM   25706 S  SG  . CYS   B 1 1487 ? 41.10000   28.74400  6.72500   1.000 64.63169  ?  1485 CYS   B SG  1 
ATOM   25707 N  N   . GLY   B 1 1488 ? 43.33000   28.02300  8.74500   1.000 47.18695  ?  1486 GLY   B N   1 
ATOM   25708 C  CA  . GLY   B 1 1488 ? 43.28000   27.78000  10.17300  1.000 41.22545  ?  1486 GLY   B CA  1 
ATOM   25709 C  C   . GLY   B 1 1488 ? 44.32500   28.56100  10.94100  1.000 55.29735  ?  1486 GLY   B C   1 
ATOM   25710 O  O   . GLY   B 1 1488 ? 44.01500   29.21300  11.94300  1.000 63.84660  ?  1486 GLY   B O   1 
ATOM   25711 N  N   . GLU   B 1 1489 ? 45.57000   28.49900  10.47800  1.000 64.86578  ?  1487 GLU   B N   1 
ATOM   25712 C  CA  . GLU   B 1 1489 ? 46.68000   29.22300  11.07800  1.000 57.65874  ?  1487 GLU   B CA  1 
ATOM   25713 C  C   . GLU   B 1 1489 ? 47.43200   29.96900  9.98200   1.000 64.81724  ?  1487 GLU   B C   1 
ATOM   25714 O  O   . GLU   B 1 1489 ? 47.15900   29.80800  8.78800   1.000 64.12330  ?  1487 GLU   B O   1 
ATOM   25715 C  CB  . GLU   B 1 1489 ? 47.62000   28.27300  11.82900  1.000 59.33623  ?  1487 GLU   B CB  1 
ATOM   25716 C  CG  . GLU   B 1 1489 ? 46.94300   27.45400  12.91300  1.000 71.34084  ?  1487 GLU   B CG  1 
ATOM   25717 C  CD  . GLU   B 1 1489 ? 47.49500   26.04800  12.99500  1.000 86.50763  ?  1487 GLU   B CD  1 
ATOM   25718 O  OE1 . GLU   B 1 1489 ? 48.06000   25.57600  11.98600  1.000 74.29428  ?  1487 GLU   B OE1 1 
ATOM   25719 O  OE2 . GLU   B 1 1489 ? 47.36800   25.41700  14.06600  1.000 89.94742  -1 1487 GLU   B OE2 1 
ATOM   25720 N  N   . ALA   B 1 1490 ? 48.38700   30.79700  10.39900  1.000 66.09704  ?  1488 ALA   B N   1 
ATOM   25721 C  CA  . ALA   B 1 1490 ? 49.28500   31.44800  9.45900   1.000 65.44913  ?  1488 ALA   B CA  1 
ATOM   25722 C  C   . ALA   B 1 1490 ? 50.32100   30.44500  8.98000   1.000 58.86133  ?  1488 ALA   B C   1 
ATOM   25723 O  O   . ALA   B 1 1490 ? 50.93500   29.73600  9.78500   1.000 59.71464  ?  1488 ALA   B O   1 
ATOM   25724 C  CB  . ALA   B 1 1490 ? 49.97200   32.65300  10.09800  1.000 62.07643  ?  1488 ALA   B CB  1 
ATOM   25725 N  N   . MET   B 1 1491 ? 50.50700   30.38100  7.67500   1.000 58.25195  ?  1489 MET   B N   1 
ATOM   25726 C  CA  . MET   B 1 1491 ? 51.43300   29.41700  7.11400   1.000 71.61206  ?  1489 MET   B CA  1 
ATOM   25727 C  C   . MET   B 1 1491 ? 52.86100   29.90700  7.31600   1.000 75.72890  ?  1489 MET   B C   1 
ATOM   25728 O  O   . MET   B 1 1491 ? 53.21500   30.97600  6.80500   1.000 88.09014  ?  1489 MET   B O   1 
ATOM   25729 C  CB  . MET   B 1 1491 ? 51.14200   29.21300  5.64100   1.000 61.50373  ?  1489 MET   B CB  1 
ATOM   25730 C  CG  . MET   B 1 1491 ? 51.80100   27.99000  5.03100   1.000 65.00086  ?  1489 MET   B CG  1 
ATOM   25731 S  SD  . MET   B 1 1491 ? 51.60400   28.08900  3.25600   1.000 87.55276  ?  1489 MET   B SD  1 
ATOM   25732 C  CE  . MET   B 1 1491 ? 51.58200   29.86900  3.14100   1.000 70.13716  ?  1489 MET   B CE  1 
ATOM   25733 N  N   . PRO   B 1 1492 ? 53.69300   29.18700  8.06800   1.000 79.96278  ?  1490 PRO   B N   1 
ATOM   25734 C  CA  . PRO   B 1 1492 ? 55.08600   29.61600  8.24500   1.000 84.84931  ?  1490 PRO   B CA  1 
ATOM   25735 C  C   . PRO   B 1 1492 ? 55.80600   29.63800  6.90500   1.000 92.23282  ?  1490 PRO   B C   1 
ATOM   25736 O  O   . PRO   B 1 1492 ? 55.66600   28.71600  6.09600   1.000 93.77849  ?  1490 PRO   B O   1 
ATOM   25737 C  CB  . PRO   B 1 1492 ? 55.66600   28.55100  9.18400   1.000 92.72978  ?  1490 PRO   B CB  1 
ATOM   25738 C  CG  . PRO   B 1 1492 ? 54.47000   27.90000  9.83000   1.000 80.95884  ?  1490 PRO   B CG  1 
ATOM   25739 C  CD  . PRO   B 1 1492 ? 53.38900   27.94500  8.80000   1.000 82.23111  ?  1490 PRO   B CD  1 
ATOM   25740 N  N   . ASP   B 1 1493 ? 56.56900   30.70900  6.66900   1.000 101.41470 ?  1491 ASP   B N   1 
ATOM   25741 C  CA  . ASP   B 1 1493 ? 57.28900   30.85000  5.40500   1.000 93.69874  ?  1491 ASP   B CA  1 
ATOM   25742 C  C   . ASP   B 1 1493 ? 58.19800   29.66000  5.12600   1.000 89.11192  ?  1491 ASP   B C   1 
ATOM   25743 O  O   . ASP   B 1 1493 ? 58.49900   29.38300  3.96100   1.000 74.34163  ?  1491 ASP   B O   1 
ATOM   25744 C  CB  . ASP   B 1 1493 ? 58.12300   32.13400  5.39800   1.000 95.61617  ?  1491 ASP   B CB  1 
ATOM   25745 C  CG  . ASP   B 1 1493 ? 57.55600   33.20100  6.31100   1.000 104.35674 ?  1491 ASP   B CG  1 
ATOM   25746 O  OD1 . ASP   B 1 1493 ? 57.51300   32.96700  7.53700   1.000 84.97628  ?  1491 ASP   B OD1 1 
ATOM   25747 O  OD2 . ASP   B 1 1493 ? 57.16600   34.27400  5.80500   1.000 106.81671 -1 1491 ASP   B OD2 1 
ATOM   25748 N  N   . GLU   B 1 1494 ? 58.64200   28.95800  6.17300   1.000 101.52669 ?  1492 GLU   B N   1 
ATOM   25749 C  CA  . GLU   B 1 1494 ? 59.45400   27.75900  6.01200   1.000 99.48879  ?  1492 GLU   B CA  1 
ATOM   25750 C  C   . GLU   B 1 1494 ? 58.65900   26.59800  5.43500   1.000 106.85645 ?  1492 GLU   B C   1 
ATOM   25751 O  O   . GLU   B 1 1494 ? 59.24800   25.71000  4.80800   1.000 103.18431 ?  1492 GLU   B O   1 
ATOM   25752 C  CB  . GLU   B 1 1494 ? 60.05200   27.34400  7.35800   1.000 79.08195  ?  1492 GLU   B CB  1 
ATOM   25753 C  CG  . GLU   B 1 1494 ? 60.43600   28.50800  8.25900   1.000 96.92585  ?  1492 GLU   B CG  1 
ATOM   25754 C  CD  . GLU   B 1 1494 ? 59.25700   29.06100  9.04200   1.000 96.67773  ?  1492 GLU   B CD  1 
ATOM   25755 O  OE1 . GLU   B 1 1494 ? 58.45400   29.82000  8.44800   1.000 101.28103 ?  1492 GLU   B OE1 1 
ATOM   25756 O  OE2 . GLU   B 1 1494 ? 59.12200   28.72800  10.23700  1.000 86.69108  ?  1492 GLU   B OE2 1 
ATOM   25757 N  N   . LEU   B 1 1495 ? 57.33600   26.57200  5.64600   1.000 108.41649 ?  1493 LEU   B N   1 
ATOM   25758 C  CA  . LEU   B 1 1495 ? 56.50900   25.48800  5.12600   1.000 89.71513  ?  1493 LEU   B CA  1 
ATOM   25759 C  C   . LEU   B 1 1495 ? 56.26700   25.61900  3.62200   1.000 90.56743  ?  1493 LEU   B C   1 
ATOM   25760 O  O   . LEU   B 1 1495 ? 56.14600   24.59800  2.93600   1.000 89.19859  ?  1493 LEU   B O   1 
ATOM   25761 C  CB  . LEU   B 1 1495 ? 55.17200   25.44900  5.86800   1.000 88.87630  ?  1493 LEU   B CB  1 
ATOM   25762 C  CG  . LEU   B 1 1495 ? 54.28400   24.22200  5.64000   1.000 97.97535  ?  1493 LEU   B CG  1 
ATOM   25763 C  CD1 . LEU   B 1 1495 ? 55.00800   22.96300  6.09100   1.000 78.36347  ?  1493 LEU   B CD1 1 
ATOM   25764 C  CD2 . LEU   B 1 1495 ? 52.96600   24.38300  6.38000   1.000 88.32498  ?  1493 LEU   B CD2 1 
ATOM   25765 N  N   . VAL   B 1 1496 ? 56.18800   26.85200  3.10700   1.000 87.94894  ?  1494 VAL   B N   1 
ATOM   25766 C  CA  . VAL   B 1 1496 ? 55.98200   27.04700  1.66900   1.000 81.50583  ?  1494 VAL   B CA  1 
ATOM   25767 C  C   . VAL   B 1 1496 ? 56.92300   26.18900  0.82400   1.000 85.84241  ?  1494 VAL   B C   1 
ATOM   25768 O  O   . VAL   B 1 1496 ? 56.43400   25.45400  -0.04300  1.000 88.02610  ?  1494 VAL   B O   1 
ATOM   25769 C  CB  . VAL   B 1 1496 ? 56.06000   28.54300  1.32900   1.000 75.08438  ?  1494 VAL   B CB  1 
ATOM   25770 C  CG1 . VAL   B 1 1496 ? 56.00600   28.74600  -0.17400  1.000 75.85640  ?  1494 VAL   B CG1 1 
ATOM   25771 C  CG2 . VAL   B 1 1496 ? 54.94100   29.29000  2.01900   1.000 70.59696  ?  1494 VAL   B CG2 1 
ATOM   25772 N  N   . PRO   B 1 1497 ? 58.24700   26.21100  1.02300   1.000 103.82635 ?  1495 PRO   B N   1 
ATOM   25773 C  CA  . PRO   B 1 1497 ? 59.09700   25.33500  0.20500   1.000 104.29235 ?  1495 PRO   B CA  1 
ATOM   25774 C  C   . PRO   B 1 1497 ? 59.03800   23.87700  0.62600   1.000 98.66218  ?  1495 PRO   B C   1 
ATOM   25775 O  O   . PRO   B 1 1497 ? 59.21000   22.99000  -0.22000  1.000 92.17279  ?  1495 PRO   B O   1 
ATOM   25776 C  CB  . PRO   B 1 1497 ? 60.51200   25.91600  0.40300   1.000 73.53015  ?  1495 PRO   B CB  1 
ATOM   25777 C  CG  . PRO   B 1 1497 ? 60.31400   27.23000  1.12600   1.000 91.01725  ?  1495 PRO   B CG  1 
ATOM   25778 C  CD  . PRO   B 1 1497 ? 59.06100   27.04700  1.91000   1.000 93.87768  ?  1495 PRO   B CD  1 
ATOM   25779 N  N   . LYS   B 1 1498 ? 58.79800   23.60600  1.91200   1.000 99.26605  ?  1496 LYS   B N   1 
ATOM   25780 C  CA  . LYS   B 1 1498 ? 58.74300   22.22700  2.38900   1.000 92.89351  ?  1496 LYS   B CA  1 
ATOM   25781 C  C   . LYS   B 1 1498 ? 57.67500   21.42800  1.65200   1.000 102.49856 ?  1496 LYS   B C   1 
ATOM   25782 O  O   . LYS   B 1 1498 ? 57.90200   20.27100  1.27700   1.000 91.84604  ?  1496 LYS   B O   1 
ATOM   25783 C  CB  . LYS   B 1 1498 ? 58.48800   22.21000  3.89600   1.000 78.36913  ?  1496 LYS   B CB  1 
ATOM   25784 N  N   . VAL   B 1 1499 ? 56.50600   22.03000  1.42500   1.000 103.73614 ?  1497 VAL   B N   1 
ATOM   25785 C  CA  . VAL   B 1 1499 ? 55.46300   21.36100  0.65300   1.000 89.67791  ?  1497 VAL   B CA  1 
ATOM   25786 C  C   . VAL   B 1 1499 ? 55.86000   21.28100  -0.81500  1.000 101.49362 ?  1497 VAL   B C   1 
ATOM   25787 O  O   . VAL   B 1 1499 ? 55.77900   20.21700  -1.44200  1.000 92.95000  ?  1497 VAL   B O   1 
ATOM   25788 C  CB  . VAL   B 1 1499 ? 54.11500   22.08400  0.82900   1.000 82.68230  ?  1497 VAL   B CB  1 
ATOM   25789 C  CG1 . VAL   B 1 1499 ? 53.03100   21.40000  0.00400   1.000 74.36639  ?  1497 VAL   B CG1 1 
ATOM   25790 C  CG2 . VAL   B 1 1499 ? 53.72600   22.14300  2.29800   1.000 86.15312  ?  1497 VAL   B CG2 1 
ATOM   25791 N  N   . TYR   B 1 1500 ? 56.30200   22.40500  -1.38400  1.000 104.68454 ?  1498 TYR   B N   1 
ATOM   25792 C  CA  . TYR   B 1 1500 ? 56.64400   22.46700  -2.80000  1.000 91.99535  ?  1498 TYR   B CA  1 
ATOM   25793 C  C   . TYR   B 1 1500 ? 57.82800   21.58300  -3.17000  1.000 101.76977 ?  1498 TYR   B C   1 
ATOM   25794 O  O   . TYR   B 1 1500 ? 58.06600   21.36600  -4.36300  1.000 99.16922  ?  1498 TYR   B O   1 
ATOM   25795 C  CB  . TYR   B 1 1500 ? 56.92400   23.91700  -3.19900  1.000 59.06497  ?  1498 TYR   B CB  1 
ATOM   25796 C  CG  . TYR   B 1 1500 ? 55.68100   24.68500  -3.58200  1.000 85.25616  ?  1498 TYR   B CG  1 
ATOM   25797 C  CD1 . TYR   B 1 1500 ? 54.76200   24.15100  -4.47600  1.000 90.17361  ?  1498 TYR   B CD1 1 
ATOM   25798 C  CD2 . TYR   B 1 1500 ? 55.41700   25.93700  -3.04200  1.000 90.05178  ?  1498 TYR   B CD2 1 
ATOM   25799 C  CE1 . TYR   B 1 1500 ? 53.62200   24.84600  -4.83000  1.000 88.35206  ?  1498 TYR   B CE1 1 
ATOM   25800 C  CE2 . TYR   B 1 1500 ? 54.27600   26.63900  -3.38900  1.000 88.92240  ?  1498 TYR   B CE2 1 
ATOM   25801 C  CZ  . TYR   B 1 1500 ? 53.38300   26.08800  -4.28400  1.000 91.34644  ?  1498 TYR   B CZ  1 
ATOM   25802 O  OH  . TYR   B 1 1500 ? 52.24700   26.78200  -4.63400  1.000 91.10339  ?  1498 TYR   B OH  1 
ATOM   25803 N  N   . GLU   B 1 1501 ? 58.57300   21.07300  -2.19200  1.000 93.43566  ?  1499 GLU   B N   1 
ATOM   25804 C  CA  . GLU   B 1 1501 ? 59.62000   20.09800  -2.46500  1.000 84.12896  ?  1499 GLU   B CA  1 
ATOM   25805 C  C   . GLU   B 1 1501 ? 59.09700   18.67400  -2.32200  1.000 96.35073  ?  1499 GLU   B C   1 
ATOM   25806 O  O   . GLU   B 1 1501 ? 59.28700   17.84000  -3.21300  1.000 98.12572  ?  1499 GLU   B O   1 
ATOM   25807 C  CB  . GLU   B 1 1501 ? 60.80900   20.32600  -1.52600  1.000 94.12225  ?  1499 GLU   B CB  1 
ATOM   25808 N  N   . VAL   B 1 1502 ? 58.42300   18.39600  -1.20600  1.000 104.88769 ?  1500 VAL   B N   1 
ATOM   25809 C  CA  . VAL   B 1 1502 ? 57.88900   17.06300  -0.95300  1.000 89.62993  ?  1500 VAL   B CA  1 
ATOM   25810 C  C   . VAL   B 1 1502 ? 56.79000   16.72500  -1.95700  1.000 74.88736  ?  1500 VAL   B C   1 
ATOM   25811 O  O   . VAL   B 1 1502 ? 56.65800   15.57300  -2.39200  1.000 71.74957  ?  1500 VAL   B O   1 
ATOM   25812 C  CB  . VAL   B 1 1502 ? 57.39900   16.97900  0.50500   1.000 89.58806  ?  1500 VAL   B CB  1 
ATOM   25813 C  CG1 . VAL   B 1 1502 ? 56.29000   15.98300  0.64000   1.000 91.26480  ?  1500 VAL   B CG1 1 
ATOM   25814 C  CG2 . VAL   B 1 1502 ? 58.55200   16.62200  1.43000   1.000 89.85657  ?  1500 VAL   B CG2 1 
ATOM   25815 N  N   . LEU   B 1 1503 ? 55.99300   17.72300  -2.34900  1.000 81.59245  ?  1501 LEU   B N   1 
ATOM   25816 C  CA  . LEU   B 1 1503 ? 55.00500   17.60400  -3.42400  1.000 93.36027  ?  1501 LEU   B CA  1 
ATOM   25817 C  C   . LEU   B 1 1503 ? 55.37300   18.60300  -4.51300  1.000 94.97395  ?  1501 LEU   B C   1 
ATOM   25818 O  O   . LEU   B 1 1503 ? 54.90200   19.75200  -4.49900  1.000 99.20275  ?  1501 LEU   B O   1 
ATOM   25819 C  CB  . LEU   B 1 1503 ? 53.58600   17.85300  -2.91600  1.000 88.30149  ?  1501 LEU   B CB  1 
ATOM   25820 C  CG  . LEU   B 1 1503 ? 52.72800   16.63700  -2.56300  1.000 71.28962  ?  1501 LEU   B CG  1 
ATOM   25821 C  CD1 . LEU   B 1 1503 ? 52.39600   15.82500  -3.80600  1.000 84.21777  ?  1501 LEU   B CD1 1 
ATOM   25822 C  CD2 . LEU   B 1 1503 ? 53.43500   15.78200  -1.53000  1.000 72.70001  ?  1501 LEU   B CD2 1 
ATOM   25823 N  N   . PRO   B 1 1504 ? 56.20100   18.20900  -5.48400  1.000 91.18494  ?  1502 PRO   B N   1 
ATOM   25824 C  CA  . PRO   B 1 1504 ? 56.71900   19.19000  -6.45400  1.000 91.86107  ?  1502 PRO   B CA  1 
ATOM   25825 C  C   . PRO   B 1 1504 ? 55.69100   19.68000  -7.46300  1.000 85.54431  ?  1502 PRO   B C   1 
ATOM   25826 O  O   . PRO   B 1 1504 ? 55.93400   20.70900  -8.10600  1.000 79.18687  ?  1502 PRO   B O   1 
ATOM   25827 C  CB  . PRO   B 1 1504 ? 57.85400   18.42700  -7.15500  1.000 87.04333  ?  1502 PRO   B CB  1 
ATOM   25828 C  CG  . PRO   B 1 1504 ? 58.13700   17.23500  -6.27500  1.000 88.51715  ?  1502 PRO   B CG  1 
ATOM   25829 C  CD  . PRO   B 1 1504 ? 56.82900   16.89000  -5.64700  1.000 88.43092  ?  1502 PRO   B CD  1 
ATOM   25830 N  N   . GLU   B 1 1505 ? 54.56300   18.99200  -7.63200  1.000 78.39144  ?  1503 GLU   B N   1 
ATOM   25831 C  CA  . GLU   B 1 1505 ? 53.57800   19.35600  -8.64500  1.000 84.90582  ?  1503 GLU   B CA  1 
ATOM   25832 C  C   . GLU   B 1 1505 ? 52.25000   19.77000  -8.02000  1.000 87.98301  ?  1503 GLU   B C   1 
ATOM   25833 O  O   . GLU   B 1 1505 ? 51.18400   19.53600  -8.59600  1.000 92.37741  ?  1503 GLU   B O   1 
ATOM   25834 C  CB  . GLU   B 1 1505 ? 53.37300   18.20600  -9.63000  1.000 92.62736  ?  1503 GLU   B CB  1 
ATOM   25835 C  CG  . GLU   B 1 1505 ? 54.59300   17.90400  -10.48700 1.000 86.75098  ?  1503 GLU   B CG  1 
ATOM   25836 C  CD  . GLU   B 1 1505 ? 54.49500   18.50900  -11.87300 1.000 102.41548 ?  1503 GLU   B CD  1 
ATOM   25837 O  OE1 . GLU   B 1 1505 ? 53.49300   18.24000  -12.56800 1.000 98.52413  ?  1503 GLU   B OE1 1 
ATOM   25838 O  OE2 . GLU   B 1 1505 ? 55.41500   19.25700  -12.26500 1.000 110.30196 -1 1503 GLU   B OE2 1 
ATOM   25839 N  N   . VAL   B 1 1506 ? 52.29600   20.39800  -6.84900  1.000 92.15254  ?  1504 VAL   B N   1 
ATOM   25840 C  CA  . VAL   B 1 1506 ? 51.09600   20.79800  -6.13200  1.000 94.21654  ?  1504 VAL   B CA  1 
ATOM   25841 C  C   . VAL   B 1 1506 ? 50.99800   22.32300  -6.15000  1.000 89.25334  ?  1504 VAL   B C   1 
ATOM   25842 O  O   . VAL   B 1 1506 ? 51.90100   23.02100  -6.61200  1.000 94.00211  ?  1504 VAL   B O   1 
ATOM   25843 C  CB  . VAL   B 1 1506 ? 51.08200   20.24000  -4.69300  1.000 87.82734  ?  1504 VAL   B CB  1 
ATOM   25844 C  CG1 . VAL   B 1 1506 ? 51.85700   21.15000  -3.74300  1.000 74.59487  ?  1504 VAL   B CG1 1 
ATOM   25845 C  CG2 . VAL   B 1 1506 ? 49.65400   20.00300  -4.21200  1.000 84.47355  ?  1504 VAL   B CG2 1 
ATOM   25846 N  N   . LYS   B 1 1507 ? 49.87400   22.84000  -5.65000  1.000 87.37801  ?  1505 LYS   B N   1 
ATOM   25847 C  CA  . LYS   B 1 1507 ? 49.62700   24.28000  -5.58300  1.000 69.35552  ?  1505 LYS   B CA  1 
ATOM   25848 C  C   . LYS   B 1 1507 ? 49.24400   24.63200  -4.14800  1.000 73.15815  ?  1505 LYS   B C   1 
ATOM   25849 O  O   . LYS   B 1 1507 ? 48.08700   24.46800  -3.75000  1.000 94.62354  ?  1505 LYS   B O   1 
ATOM   25850 C  CB  . LYS   B 1 1507 ? 48.54000   24.69700  -6.56800  1.000 53.93965  ?  1505 LYS   B CB  1 
ATOM   25851 N  N   . LEU   B 1 1508 ? 50.21400   25.11400  -3.37100  1.000 64.33284  ?  1506 LEU   B N   1 
ATOM   25852 C  CA  . LEU   B 1 1508 ? 49.95900   25.50300  -1.99000  1.000 66.20177  ?  1506 LEU   B CA  1 
ATOM   25853 C  C   . LEU   B 1 1508 ? 49.23500   26.84300  -1.95700  1.000 69.88092  ?  1506 LEU   B C   1 
ATOM   25854 O  O   . LEU   B 1 1508 ? 49.68500   27.82100  -2.56200  1.000 67.82547  ?  1506 LEU   B O   1 
ATOM   25855 C  CB  . LEU   B 1 1508 ? 51.26400   25.57700  -1.19900  1.000 63.18384  ?  1506 LEU   B CB  1 
ATOM   25856 C  CG  . LEU   B 1 1508 ? 51.14600   25.78400  0.31500   1.000 79.24757  ?  1506 LEU   B CG  1 
ATOM   25857 C  CD1 . LEU   B 1 1508 ? 49.92300   25.08700  0.89300   1.000 70.38138  ?  1506 LEU   B CD1 1 
ATOM   25858 C  CD2 . LEU   B 1 1508 ? 52.40000   25.27500  1.00100   1.000 75.42285  ?  1506 LEU   B CD2 1 
ATOM   25859 N  N   . GLU   B 1 1509 ? 48.11300   26.88400  -1.24200  1.000 74.23708  ?  1507 GLU   B N   1 
ATOM   25860 C  CA  . GLU   B 1 1509 ? 47.23200   28.04300  -1.22600  1.000 66.01942  ?  1507 GLU   B CA  1 
ATOM   25861 C  C   . GLU   B 1 1509 ? 47.01100   28.49900  0.20700   1.000 78.23806  ?  1507 GLU   B C   1 
ATOM   25862 O  O   . GLU   B 1 1509 ? 46.63400   27.69700  1.06700   1.000 76.31147  ?  1507 GLU   B O   1 
ATOM   25863 C  CB  . GLU   B 1 1509 ? 45.89000   27.71500  -1.89000  1.000 62.12589  ?  1507 GLU   B CB  1 
ATOM   25864 C  CG  . GLU   B 1 1509 ? 46.02600   27.17700  -3.30300  1.000 67.66240  ?  1507 GLU   B CG  1 
ATOM   25865 C  CD  . GLU   B 1 1509 ? 46.63400   28.19100  -4.24800  1.000 71.53082  ?  1507 GLU   B CD  1 
ATOM   25866 O  OE1 . GLU   B 1 1509 ? 46.15400   29.34300  -4.26600  1.000 69.61960  ?  1507 GLU   B OE1 1 
ATOM   25867 O  OE2 . GLU   B 1 1509 ? 47.59600   27.84100  -4.96400  1.000 76.20392  -1 1507 GLU   B OE2 1 
ATOM   25868 N  N   . ASN   B 1 1510 ? 47.24300   29.78500  0.45800   1.000 76.46282  ?  1508 ASN   B N   1 
ATOM   25869 C  CA  . ASN   B 1 1510 ? 46.98600   30.38500  1.76200   1.000 65.21908  ?  1508 ASN   B CA  1 
ATOM   25870 C  C   . ASN   B 1 1510 ? 45.57300   30.95900  1.75100   1.000 71.86384  ?  1508 ASN   B C   1 
ATOM   25871 O  O   . ASN   B 1 1510 ? 45.30600   31.95500  1.07100   1.000 70.71364  ?  1508 ASN   B O   1 
ATOM   25872 C  CB  . ASN   B 1 1510 ? 48.02200   31.46300  2.07200   1.000 71.15537  ?  1508 ASN   B CB  1 
ATOM   25873 C  CG  . ASN   B 1 1510 ? 48.04700   31.84200  3.53900   1.000 74.96778  ?  1508 ASN   B CG  1 
ATOM   25874 O  OD1 . ASN   B 1 1510 ? 47.92600   30.98500  4.41500   1.000 46.49756  ?  1508 ASN   B OD1 1 
ATOM   25875 N  ND2 . ASN   B 1 1510 ? 48.19900   33.13100  3.81400   1.000 82.24433  ?  1508 ASN   B ND2 1 
ATOM   25876 N  N   . ILE   B 1 1511 ? 44.66800   30.33000  2.49900   1.000 58.97659  ?  1509 ILE   B N   1 
ATOM   25877 C  CA  . ILE   B 1 1511 ? 43.25900   30.70500  2.52400   1.000 61.43576  ?  1509 ILE   B CA  1 
ATOM   25878 C  C   . ILE   B 1 1511 ? 42.91700   31.25500  3.90300   1.000 58.05965  ?  1509 ILE   B C   1 
ATOM   25879 O  O   . ILE   B 1 1511 ? 43.41000   30.75600  4.92200   1.000 51.69724  ?  1509 ILE   B O   1 
ATOM   25880 C  CB  . ILE   B 1 1511 ? 42.35300   29.50800  2.16900   1.000 69.39607  ?  1509 ILE   B CB  1 
ATOM   25881 C  CG1 . ILE   B 1 1511 ? 42.82600   28.83500  0.87600   1.000 56.29212  ?  1509 ILE   B CG1 1 
ATOM   25882 C  CG2 . ILE   B 1 1511 ? 40.91200   29.95900  2.01300   1.000 51.18867  ?  1509 ILE   B CG2 1 
ATOM   25883 C  CD1 . ILE   B 1 1511 ? 42.31500   29.49700  -0.39000  1.000 64.76128  ?  1509 ILE   B CD1 1 
ATOM   25884 N  N   . TYR   B 1 1512 ? 42.07300   32.28600  3.93100   1.000 44.83711  ?  1510 TYR   B N   1 
ATOM   25885 C  CA  . TYR   B 1 1512 ? 41.62800   32.91400  5.16600   1.000 51.72781  ?  1510 TYR   B CA  1 
ATOM   25886 C  C   . TYR   B 1 1512 ? 40.12600   33.14800  5.10000   1.000 51.57580  ?  1510 TYR   B C   1 
ATOM   25887 O  O   . TYR   B 1 1512 ? 39.57700   33.44000  4.03400   1.000 53.95327  ?  1510 TYR   B O   1 
ATOM   25888 C  CB  . TYR   B 1 1512 ? 42.36600   34.24400  5.41700   1.000 59.19123  ?  1510 TYR   B CB  1 
ATOM   25889 C  CG  . TYR   B 1 1512 ? 41.76200   35.10100  6.51000   1.000 53.67886  ?  1510 TYR   B CG  1 
ATOM   25890 C  CD1 . TYR   B 1 1512 ? 42.10100   34.90400  7.84300   1.000 44.23946  ?  1510 TYR   B CD1 1 
ATOM   25891 C  CD2 . TYR   B 1 1512 ? 40.85900   36.11300  6.20600   1.000 48.41815  ?  1510 TYR   B CD2 1 
ATOM   25892 C  CE1 . TYR   B 1 1512 ? 41.55200   35.68800  8.84300   1.000 40.99812  ?  1510 TYR   B CE1 1 
ATOM   25893 C  CE2 . TYR   B 1 1512 ? 40.30400   36.89800  7.19800   1.000 48.42290  ?  1510 TYR   B CE2 1 
ATOM   25894 C  CZ  . TYR   B 1 1512 ? 40.65400   36.68200  8.51500   1.000 52.82363  ?  1510 TYR   B CZ  1 
ATOM   25895 O  OH  . TYR   B 1 1512 ? 40.10500   37.46400  9.50500   1.000 55.54424  ?  1510 TYR   B OH  1 
ATOM   25896 N  N   . GLY   B 1 1513 ? 39.46600   33.01900  6.24900   1.000 38.98035  ?  1511 GLY   B N   1 
ATOM   25897 C  CA  . GLY   B 1 1513 ? 38.04600   33.26100  6.32900   1.000 53.02439  ?  1511 GLY   B CA  1 
ATOM   25898 C  C   . GLY   B 1 1513 ? 37.45200   32.92200  7.68100   1.000 50.07352  ?  1511 GLY   B C   1 
ATOM   25899 O  O   . GLY   B 1 1513 ? 37.66700   31.83700  8.23100   1.000 46.08995  ?  1511 GLY   B O   1 
ATOM   25900 N  N   . PRO   B 1 1514 ? 36.68400   33.85100  8.23900   1.000 51.56903  ?  1512 PRO   B N   1 
ATOM   25901 C  CA  . PRO   B 1 1514 ? 35.98700   33.58500  9.49800   1.000 60.63415  ?  1512 PRO   B CA  1 
ATOM   25902 C  C   . PRO   B 1 1514 ? 34.74300   32.74000  9.27400   1.000 51.74542  ?  1512 PRO   B C   1 
ATOM   25903 O  O   . PRO   B 1 1514 ? 34.19500   32.66100  8.17400   1.000 52.65325  ?  1512 PRO   B O   1 
ATOM   25904 C  CB  . PRO   B 1 1514 ? 35.61400   34.98700  9.99100   1.000 53.41762  ?  1512 PRO   B CB  1 
ATOM   25905 C  CG  . PRO   B 1 1514 ? 35.43100   35.76900  8.72800   1.000 44.13549  ?  1512 PRO   B CG  1 
ATOM   25906 C  CD  . PRO   B 1 1514 ? 36.43200   35.21600  7.74200   1.000 61.31274  ?  1512 PRO   B CD  1 
ATOM   25907 N  N   . THR   B 1 1515 ? 34.29800   32.10200  10.35800  1.000 44.16006  ?  1513 THR   B N   1 
ATOM   25908 C  CA  . THR   B 1 1515 ? 33.07000   31.31800  10.28600  1.000 65.66652  ?  1513 THR   B CA  1 
ATOM   25909 C  C   . THR   B 1 1515 ? 31.84400   32.21000  10.12000  1.000 60.11402  ?  1513 THR   B C   1 
ATOM   25910 O  O   . THR   B 1 1515 ? 30.83200   31.77000  9.56400   1.000 58.30423  ?  1513 THR   B O   1 
ATOM   25911 C  CB  . THR   B 1 1515 ? 32.93100   30.42800  11.52100  1.000 45.28420  ?  1513 THR   B CB  1 
ATOM   25912 O  OG1 . THR   B 1 1515 ? 31.54300   30.26500  11.84200  1.000 51.70628  ?  1513 THR   B OG1 1 
ATOM   25913 C  CG2 . THR   B 1 1515 ? 33.66300   31.04200  12.70100  1.000 57.43597  ?  1513 THR   B CG2 1 
ATOM   25914 N  N   . GLU   B 1 1516 ? 31.92000   33.46200  10.57500  1.000 48.15845  ?  1514 GLU   B N   1 
ATOM   25915 C  CA  . GLU   B 1 1516 ? 30.85000   34.42300  10.34200  1.000 48.14226  ?  1514 GLU   B CA  1 
ATOM   25916 C  C   . GLU   B 1 1516 ? 30.77300   34.87500  8.88800   1.000 42.66635  ?  1514 GLU   B C   1 
ATOM   25917 O  O   . GLU   B 1 1516 ? 29.84900   35.62100  8.53700   1.000 29.05551  ?  1514 GLU   B O   1 
ATOM   25918 C  CB  . GLU   B 1 1516 ? 31.02200   35.64000  11.25400  1.000 33.71163  ?  1514 GLU   B CB  1 
ATOM   25919 C  CG  . GLU   B 1 1516 ? 30.80000   35.36000  12.73700  1.000 44.85944  ?  1514 GLU   B CG  1 
ATOM   25920 C  CD  . GLU   B 1 1516 ? 32.01200   34.75500  13.43000  1.000 53.37754  ?  1514 GLU   B CD  1 
ATOM   25921 O  OE1 . GLU   B 1 1516 ? 32.92600   34.25400  12.74100  1.000 51.89686  ?  1514 GLU   B OE1 1 
ATOM   25922 O  OE2 . GLU   B 1 1516 ? 32.04800   34.78700  14.67800  1.000 47.44251  -1 1514 GLU   B OE2 1 
ATOM   25923 N  N   . ALA   B 1 1517 ? 31.72400   34.46200  8.04900   1.000 49.26192  ?  1515 ALA   B N   1 
ATOM   25924 C  CA  . ALA   B 1 1517 ? 31.64900   34.67100  6.60900   1.000 52.96481  ?  1515 ALA   B CA  1 
ATOM   25925 C  C   . ALA   B 1 1517 ? 31.69600   33.32500  5.89800   1.000 62.89461  ?  1515 ALA   B C   1 
ATOM   25926 O  O   . ALA   B 1 1517 ? 32.52300   33.11400  5.00300   1.000 72.20009  ?  1515 ALA   B O   1 
ATOM   25927 C  CB  . ALA   B 1 1517 ? 32.78100   35.57700  6.12000   1.000 59.09190  ?  1515 ALA   B CB  1 
ATOM   25928 N  N   . THR   B 1 1518 ? 30.81500   32.41200  6.31100   1.000 66.54714  ?  1516 THR   B N   1 
ATOM   25929 C  CA  . THR   B 1 1518 ? 30.68400   31.06600  5.74100   1.000 69.83593  ?  1516 THR   B CA  1 
ATOM   25930 C  C   . THR   B 1 1518 ? 31.98200   30.31300  6.01100   1.000 78.29349  ?  1516 THR   B C   1 
ATOM   25931 O  O   . THR   B 1 1518 ? 32.29000   30.06100  7.19000   1.000 82.15793  ?  1516 THR   B O   1 
ATOM   25932 C  CB  . THR   B 1 1518 ? 30.26200   31.16400  4.27000   1.000 69.69225  ?  1516 THR   B CB  1 
ATOM   25933 O  OG1 . THR   B 1 1518 ? 29.26400   32.18300  4.12400   1.000 63.61480  ?  1516 THR   B OG1 1 
ATOM   25934 C  CG2 . THR   B 1 1518 ? 29.67500   29.84300  3.80000   1.000 67.81814  ?  1516 THR   B CG2 1 
ATOM   25935 N  N   . ILE   B 1 1519 ? 32.76000   29.94000  4.99600   1.000 58.01374  ?  1517 ILE   B N   1 
ATOM   25936 C  CA  . ILE   B 1 1519 ? 33.93400   29.09600  5.18900   1.000 58.70209  ?  1517 ILE   B CA  1 
ATOM   25937 C  C   . ILE   B 1 1519 ? 35.19600   29.93700  5.06600   1.000 64.05643  ?  1517 ILE   B C   1 
ATOM   25938 O  O   . ILE   B 1 1519 ? 35.99300   30.03900  6.00600   1.000 56.55446  ?  1517 ILE   B O   1 
ATOM   25939 C  CB  . ILE   B 1 1519 ? 33.95900   27.94700  4.16600   1.000 62.17021  ?  1517 ILE   B CB  1 
ATOM   25940 C  CG1 . ILE   B 1 1519 ? 32.54600   27.40600  3.93900   1.000 52.68560  ?  1517 ILE   B CG1 1 
ATOM   25941 C  CG2 . ILE   B 1 1519 ? 34.90500   26.84900  4.62500   1.000 57.57612  ?  1517 ILE   B CG2 1 
ATOM   25942 C  CD1 . ILE   B 1 1519 ? 32.40000   26.61900  2.65600   1.000 46.22480  ?  1517 ILE   B CD1 1 
ATOM   25943 N  N   . TYR   B 1 1520 ? 35.38400   30.53100  3.89500   1.000 65.01219  ?  1518 TYR   B N   1 
ATOM   25944 C  CA  . TYR   B 1 1520 ? 36.56300   31.31500  3.57400   1.000 54.60275  ?  1518 TYR   B CA  1 
ATOM   25945 C  C   . TYR   B 1 1520 ? 36.14400   32.72000  3.16900   1.000 62.57807  ?  1518 TYR   B C   1 
ATOM   25946 O  O   . TYR   B 1 1520 ? 34.95800   33.02600  3.02500   1.000 65.75173  ?  1518 TYR   B O   1 
ATOM   25947 C  CB  . TYR   B 1 1520 ? 37.36300   30.65600  2.44800   1.000 42.11094  ?  1518 TYR   B CB  1 
ATOM   25948 C  CG  . TYR   B 1 1520 ? 37.67500   29.19600  2.68100   1.000 55.60727  ?  1518 TYR   B CG  1 
ATOM   25949 C  CD1 . TYR   B 1 1520 ? 38.23300   28.76500  3.87700   1.000 54.37746  ?  1518 TYR   B CD1 1 
ATOM   25950 C  CD2 . TYR   B 1 1520 ? 37.40900   28.24800  1.70100   1.000 51.97221  ?  1518 TYR   B CD2 1 
ATOM   25951 C  CE1 . TYR   B 1 1520 ? 38.52500   27.42800  4.08900   1.000 55.45123  ?  1518 TYR   B CE1 1 
ATOM   25952 C  CE2 . TYR   B 1 1520 ? 37.69400   26.91100  1.90500   1.000 50.37199  ?  1518 TYR   B CE2 1 
ATOM   25953 C  CZ  . TYR   B 1 1520 ? 38.25100   26.50600  3.09900   1.000 61.05235  ?  1518 TYR   B CZ  1 
ATOM   25954 O  OH  . TYR   B 1 1520 ? 38.53400   25.17400  3.29900   1.000 67.50262  ?  1518 TYR   B OH  1 
ATOM   25955 N  N   . ALA   B 1 1521 ? 37.14500   33.57600  2.97800   1.000 62.37013  ?  1519 ALA   B N   1 
ATOM   25956 C  CA  . ALA   B 1 1521 ? 36.90500   34.94000  2.53100   1.000 50.77025  ?  1519 ALA   B CA  1 
ATOM   25957 C  C   . ALA   B 1 1521 ? 38.06200   35.46900  1.69400   1.000 56.40646  ?  1519 ALA   B C   1 
ATOM   25958 O  O   . ALA   B 1 1521 ? 37.85000   36.30000  0.81000   1.000 60.75863  ?  1519 ALA   B O   1 
ATOM   25959 C  CB  . ALA   B 1 1521 ? 36.65900   35.86600  3.72500   1.000 49.08666  ?  1519 ALA   B CB  1 
ATOM   25960 N  N   . SER   B 1 1522 ? 39.27600   34.99100  1.95500   1.000 57.40307  ?  1520 SER   B N   1 
ATOM   25961 C  CA  . SER   B 1 1522 ? 40.47300   35.49100  1.29800   1.000 55.95321  ?  1520 SER   B CA  1 
ATOM   25962 C  C   . SER   B 1 1522 ? 41.30300   34.32900  0.76900   1.000 59.71738  ?  1520 SER   B C   1 
ATOM   25963 O  O   . SER   B 1 1522 ? 41.14800   33.18100  1.19500   1.000 57.37126  ?  1520 SER   B O   1 
ATOM   25964 C  CB  . SER   B 1 1522 ? 41.31400   36.34700  2.25400   1.000 46.42941  ?  1520 SER   B CB  1 
ATOM   25965 O  OG  . SER   B 1 1522 ? 42.55100   36.69400  1.66800   1.000 63.68173  ?  1520 SER   B OG  1 
ATOM   25966 N  N   . ARG   B 1 1523 ? 42.19600   34.64500  -0.16800  1.000 68.57631  ?  1521 ARG   B N   1 
ATOM   25967 C  CA  . ARG   B 1 1523 ? 43.02000   33.63400  -0.81600  1.000 62.70215  ?  1521 ARG   B CA  1 
ATOM   25968 C  C   . ARG   B 1 1523 ? 44.28000   34.28400  -1.36900  1.000 61.89343  ?  1521 ARG   B C   1 
ATOM   25969 O  O   . ARG   B 1 1523 ? 44.22900   35.39600  -1.90000  1.000 68.01923  ?  1521 ARG   B O   1 
ATOM   25970 C  CB  . ARG   B 1 1523 ? 42.25600   32.93800  -1.94700  1.000 61.71040  ?  1521 ARG   B CB  1 
ATOM   25971 C  CG  . ARG   B 1 1523 ? 41.79900   33.89300  -3.04300  1.000 73.35864  ?  1521 ARG   B CG  1 
ATOM   25972 C  CD  . ARG   B 1 1523 ? 41.26800   33.15300  -4.25500  1.000 85.76475  ?  1521 ARG   B CD  1 
ATOM   25973 N  NE  . ARG   B 1 1523 ? 42.35000   32.57800  -5.04100  1.000 84.55117  ?  1521 ARG   B NE  1 
ATOM   25974 C  CZ  . ARG   B 1 1523 ? 43.07400   33.25700  -5.91900  1.000 78.69347  ?  1521 ARG   B CZ  1 
ATOM   25975 N  NH1 . ARG   B 1 1523 ? 42.85900   34.54400  -6.14400  1.000 82.33929  ?  1521 ARG   B NH1 1 
ATOM   25976 N  NH2 . ARG   B 1 1523 ? 44.03900   32.63200  -6.58600  1.000 84.05490  ?  1521 ARG   B NH2 1 
ATOM   25977 N  N   . TYR   B 1 1524 ? 45.40200   33.57700  -1.25100  1.000 67.81741  ?  1522 TYR   B N   1 
ATOM   25978 C  CA  . TYR   B 1 1524 ? 46.64900   33.99100  -1.88100  1.000 68.58124  ?  1522 TYR   B CA  1 
ATOM   25979 C  C   . TYR   B 1 1524 ? 47.37300   32.75800  -2.39900  1.000 77.27088  ?  1522 TYR   B C   1 
ATOM   25980 O  O   . TYR   B 1 1524 ? 47.61300   31.81100  -1.64400  1.000 70.39019  ?  1522 TYR   B O   1 
ATOM   25981 C  CB  . TYR   B 1 1524 ? 47.54900   34.76600  -0.91200  1.000 65.40320  ?  1522 TYR   B CB  1 
ATOM   25982 C  CG  . TYR   B 1 1524 ? 48.87700   35.17300  -1.51400  1.000 82.92970  ?  1522 TYR   B CG  1 
ATOM   25983 C  CD1 . TYR   B 1 1524 ? 48.96600   35.58800  -2.83800  1.000 86.89231  ?  1522 TYR   B CD1 1 
ATOM   25984 C  CD2 . TYR   B 1 1524 ? 50.04200   35.14800  -0.75800  1.000 81.47292  ?  1522 TYR   B CD2 1 
ATOM   25985 C  CE1 . TYR   B 1 1524 ? 50.17800   35.95800  -3.39300  1.000 87.25189  ?  1522 TYR   B CE1 1 
ATOM   25986 C  CE2 . TYR   B 1 1524 ? 51.25600   35.51900  -1.30400  1.000 79.47864  ?  1522 TYR   B CE2 1 
ATOM   25987 C  CZ  . TYR   B 1 1524 ? 51.31900   35.92300  -2.61900  1.000 87.37665  ?  1522 TYR   B CZ  1 
ATOM   25988 O  OH  . TYR   B 1 1524 ? 52.53100   36.29100  -3.15800  1.000 94.85882  ?  1522 TYR   B OH  1 
ATOM   25989 N  N   . SER   B 1 1525 ? 47.71100   32.77800  -3.68600  1.000 79.79939  ?  1523 SER   B N   1 
ATOM   25990 C  CA  . SER   B 1 1525 ? 48.40500   31.67300  -4.33100  1.000 71.37212  ?  1523 SER   B CA  1 
ATOM   25991 C  C   . SER   B 1 1525 ? 49.91100   31.84700  -4.17900  1.000 64.60458  ?  1523 SER   B C   1 
ATOM   25992 O  O   . SER   B 1 1525 ? 50.46000   32.89700  -4.53400  1.000 80.67950  ?  1523 SER   B O   1 
ATOM   25993 C  CB  . SER   B 1 1525 ? 48.03400   31.59700  -5.81400  1.000 66.98094  ?  1523 SER   B CB  1 
ATOM   25994 O  OG  . SER   B 1 1525 ? 46.64100   31.76900  -6.00600  1.000 61.80283  ?  1523 SER   B OG  1 
ATOM   25995 N  N   . LEU   B 1 1526 ? 50.57300   30.82100  -3.65800  1.000 64.02105  ?  1524 LEU   B N   1 
ATOM   25996 C  CA  . LEU   B 1 1526 ? 52.02100   30.81700  -3.53500  1.000 68.49489  ?  1524 LEU   B CA  1 
ATOM   25997 C  C   . LEU   B 1 1526 ? 52.65000   30.07600  -4.70700  1.000 82.20259  ?  1524 LEU   B C   1 
ATOM   25998 O  O   . LEU   B 1 1526 ? 51.99200   29.33900  -5.44500  1.000 101.73965 ?  1524 LEU   B O   1 
ATOM   25999 C  CB  . LEU   B 1 1526 ? 52.45200   30.17000  -2.22600  1.000 48.47535  ?  1524 LEU   B CB  1 
ATOM   26000 C  CG  . LEU   B 1 1526 ? 51.64000   30.60400  -1.02000  1.000 65.28522  ?  1524 LEU   B CG  1 
ATOM   26001 C  CD1 . LEU   B 1 1526 ? 51.63300   29.42900  -0.10500  1.000 60.13901  ?  1524 LEU   B CD1 1 
ATOM   26002 C  CD2 . LEU   B 1 1526 ? 52.25100   31.81600  -0.35600  1.000 79.09520  ?  1524 LEU   B CD2 1 
ATOM   26003 N  N   . ALA   B 1 1527 ? 53.95600   30.27000  -4.85900  1.000 86.55527  ?  1525 ALA   B N   1 
ATOM   26004 C  CA  . ALA   B 1 1527 ? 54.68700   29.73700  -5.99600  1.000 88.40379  ?  1525 ALA   B CA  1 
ATOM   26005 C  C   . ALA   B 1 1527 ? 55.99800   29.14500  -5.49300  1.000 95.39183  ?  1525 ALA   B C   1 
ATOM   26006 O  O   . ALA   B 1 1527 ? 56.19700   28.95400  -4.28900  1.000 101.54638 ?  1525 ALA   B O   1 
ATOM   26007 C  CB  . ALA   B 1 1527 ? 54.90500   30.82800  -7.05300  1.000 68.52009  ?  1525 ALA   B CB  1 
ATOM   26008 N  N   . LYS   B 1 1528 ? 56.90000   28.86400  -6.43600  1.000 85.06142  ?  1526 LYS   B N   1 
ATOM   26009 C  CA  . LYS   B 1 1528 ? 58.15900   28.21000  -6.09800  1.000 72.57157  ?  1526 LYS   B CA  1 
ATOM   26010 C  C   . LYS   B 1 1528 ? 59.02700   29.09000  -5.20600  1.000 98.42153  ?  1526 LYS   B C   1 
ATOM   26011 O  O   . LYS   B 1 1528 ? 59.73300   28.58700  -4.32400  1.000 91.57306  ?  1526 LYS   B O   1 
ATOM   26012 C  CB  . LYS   B 1 1528 ? 58.90800   27.83900  -7.37700  1.000 65.45120  ?  1526 LYS   B CB  1 
ATOM   26013 N  N   . GLY   B 1 1529 ? 58.98800   30.40400  -5.41800  1.000 105.44086 ?  1527 GLY   B N   1 
ATOM   26014 C  CA  . GLY   B 1 1529 ? 59.79900   31.32000  -4.64000  1.000 88.46495  ?  1527 GLY   B CA  1 
ATOM   26015 C  C   . GLY   B 1 1529 ? 59.32300   31.49400  -3.21100  1.000 89.98044  ?  1527 GLY   B C   1 
ATOM   26016 O  O   . GLY   B 1 1529 ? 58.53200   30.69200  -2.70600  1.000 92.53037  ?  1527 GLY   B O   1 
ATOM   26017 N  N   . SER   B 1 1530 ? 59.80500   32.54200  -2.54800  1.000 84.23044  ?  1528 SER   B N   1 
ATOM   26018 C  CA  . SER   B 1 1530 ? 59.44500   32.84700  -1.17300  1.000 97.17049  ?  1528 SER   B CA  1 
ATOM   26019 C  C   . SER   B 1 1530 ? 58.70200   34.17300  -1.11300  1.000 107.41877 ?  1528 SER   B C   1 
ATOM   26020 O  O   . SER   B 1 1530 ? 58.93100   35.07000  -1.93000  1.000 100.67624 ?  1528 SER   B O   1 
ATOM   26021 C  CB  . SER   B 1 1530 ? 60.68600   32.90700  -0.26900  1.000 90.72067  ?  1528 SER   B CB  1 
ATOM   26022 O  OG  . SER   B 1 1530 ? 60.39700   33.55300  0.96000   1.000 90.17556  ?  1528 SER   B OG  1 
ATOM   26023 N  N   . GLN   B 1 1531 ? 57.81300   34.29100  -0.13200  1.000 107.04409 ?  1529 GLN   B N   1 
ATOM   26024 C  CA  . GLN   B 1 1531 ? 57.04100   35.51000  0.03800   1.000 97.47012  ?  1529 GLN   B CA  1 
ATOM   26025 C  C   . GLN   B 1 1531 ? 57.71900   36.42400  1.05500   1.000 99.45735  ?  1529 GLN   B C   1 
ATOM   26026 O  O   . GLN   B 1 1531 ? 58.79900   36.13000  1.57400   1.000 102.69180 ?  1529 GLN   B O   1 
ATOM   26027 C  CB  . GLN   B 1 1531 ? 55.60900   35.19000  0.45800   1.000 74.47536  ?  1529 GLN   B CB  1 
ATOM   26028 C  CG  . GLN   B 1 1531 ? 54.57100   35.77300  -0.47800  1.000 77.95209  ?  1529 GLN   B CG  1 
ATOM   26029 C  CD  . GLN   B 1 1531 ? 55.03900   37.05500  -1.14000  1.000 96.15707  ?  1529 GLN   B CD  1 
ATOM   26030 O  OE1 . GLN   B 1 1531 ? 55.20500   38.08600  -0.48600  1.000 92.02861  ?  1529 GLN   B OE1 1 
ATOM   26031 N  NE2 . GLN   B 1 1531 ? 55.25600   36.99500  -2.44900  1.000 89.71427  ?  1529 GLN   B NE2 1 
ATOM   26032 N  N   . GLU   B 1 1532 ? 57.06600   37.54900  1.34400   1.000 106.57788 ?  1530 GLU   B N   1 
ATOM   26033 C  CA  . GLU   B 1 1532 ? 57.59900   38.54900  2.26400   1.000 115.47954 ?  1530 GLU   B CA  1 
ATOM   26034 C  C   . GLU   B 1 1532 ? 57.72800   37.96200  3.67300   1.000 107.89746 ?  1530 GLU   B C   1 
ATOM   26035 O  O   . GLU   B 1 1532 ? 57.37400   36.80200  3.90300   1.000 99.79341  ?  1530 GLU   B O   1 
ATOM   26036 C  CB  . GLU   B 1 1532 ? 56.70400   39.79300  2.26300   1.000 105.34953 ?  1530 GLU   B CB  1 
ATOM   26037 C  CG  . GLU   B 1 1532 ? 57.37300   41.05700  2.80000   1.000 100.34682 ?  1530 GLU   B CG  1 
ATOM   26038 C  CD  . GLU   B 1 1532 ? 56.59700   42.32100  2.49200   1.000 109.67052 ?  1530 GLU   B CD  1 
ATOM   26039 O  OE1 . GLU   B 1 1532 ? 56.63100   42.76600  1.32600   1.000 120.82592 ?  1530 GLU   B OE1 1 
ATOM   26040 O  OE2 . GLU   B 1 1532 ? 55.95600   42.87100  3.41300   1.000 99.19627  -1 1530 GLU   B OE2 1 
ATOM   26041 N  N   . SER   B 1 1533 ? 58.27400   38.76000  4.60500   1.000 103.47003 ?  1531 SER   B N   1 
ATOM   26042 C  CA  . SER   B 1 1533 ? 58.44800   38.41400  6.01300   1.000 105.79009 ?  1531 SER   B CA  1 
ATOM   26043 C  C   . SER   B 1 1533 ? 57.17600   37.76900  6.55400   1.000 113.76607 ?  1531 SER   B C   1 
ATOM   26044 O  O   . SER   B 1 1533 ? 57.25900   36.74400  7.24300   1.000 124.63193 ?  1531 SER   B O   1 
ATOM   26045 C  CB  . SER   B 1 1533 ? 58.83900   39.65100  6.82900   1.000 116.28928 ?  1531 SER   B CB  1 
ATOM   26046 O  OG  . SER   B 1 1533 ? 59.13100   40.73900  5.97400   1.000 108.99269 ?  1531 SER   B OG  1 
ATOM   26047 N  N   . PRO   B 1 1534 ? 55.97700   38.30800  6.26000   1.000 111.38672 ?  1532 PRO   B N   1 
ATOM   26048 C  CA  . PRO   B 1 1534 ? 54.76200   37.52500  6.51000   1.000 93.10090  ?  1532 PRO   B CA  1 
ATOM   26049 C  C   . PRO   B 1 1534 ? 54.22600   36.91400  5.22500   1.000 82.78542  ?  1532 PRO   B C   1 
ATOM   26050 O  O   . PRO   B 1 1534 ? 54.51900   37.39300  4.12300   1.000 80.21096  ?  1532 PRO   B O   1 
ATOM   26051 C  CB  . PRO   B 1 1534 ? 53.80200   38.57200  7.08000   1.000 82.29832  ?  1532 PRO   B CB  1 
ATOM   26052 C  CG  . PRO   B 1 1534 ? 54.14400   39.79400  6.29700   1.000 90.42378  ?  1532 PRO   B CG  1 
ATOM   26053 C  CD  . PRO   B 1 1534 ? 55.62900   39.71100  5.95900   1.000 102.04019 ?  1532 PRO   B CD  1 
ATOM   26054 N  N   . VAL   B 1 1535 ? 53.43600   35.85700  5.34400   1.000 87.48802  ?  1533 VAL   B N   1 
ATOM   26055 C  CA  . VAL   B 1 1535 ? 52.76800   35.25100  4.19800   1.000 72.91656  ?  1533 VAL   B CA  1 
ATOM   26056 C  C   . VAL   B 1 1535 ? 51.35300   35.81400  4.12900   1.000 65.29758  ?  1533 VAL   B C   1 
ATOM   26057 O  O   . VAL   B 1 1535 ? 50.55700   35.56600  5.04800   1.000 60.03623  ?  1533 VAL   B O   1 
ATOM   26058 C  CB  . VAL   B 1 1535 ? 52.74800   33.72300  4.27900   1.000 71.91382  ?  1533 VAL   B CB  1 
ATOM   26059 C  CG1 . VAL   B 1 1535 ? 52.36000   33.18000  2.93100   1.000 70.42764  ?  1533 VAL   B CG1 1 
ATOM   26060 C  CG2 . VAL   B 1 1535 ? 54.10900   33.19600  4.69500   1.000 77.55095  ?  1533 VAL   B CG2 1 
ATOM   26061 N  N   . PRO   B 1 1536 ? 50.99800   36.54600  3.07500   1.000 62.82254  ?  1534 PRO   B N   1 
ATOM   26062 C  CA  . PRO   B 1 1536 ? 49.71100   37.24700  3.05700   1.000 66.82751  ?  1534 PRO   B CA  1 
ATOM   26063 C  C   . PRO   B 1 1536 ? 48.53100   36.28800  3.07300   1.000 69.55252  ?  1534 PRO   B C   1 
ATOM   26064 O  O   . PRO   B 1 1536 ? 48.61200   35.15200  2.60100   1.000 72.94838  ?  1534 PRO   B O   1 
ATOM   26065 C  CB  . PRO   B 1 1536 ? 49.75800   38.03900  1.74300   1.000 66.08396  ?  1534 PRO   B CB  1 
ATOM   26066 C  CG  . PRO   B 1 1536 ? 51.20900   38.11300  1.38300   1.000 74.14343  ?  1534 PRO   B CG  1 
ATOM   26067 C  CD  . PRO   B 1 1536 ? 51.81500   36.84400  1.88900   1.000 73.15207  ?  1534 PRO   B CD  1 
ATOM   26068 N  N   . ILE   B 1 1537 ? 47.41800   36.76600  3.63500   1.000 60.79264  ?  1535 ILE   B N   1 
ATOM   26069 C  CA  . ILE   B 1 1537 ? 46.17000   36.01900  3.54800   1.000 46.24719  ?  1535 ILE   B CA  1 
ATOM   26070 C  C   . ILE   B 1 1537 ? 45.48400   36.24000  2.20800   1.000 51.11192  ?  1535 ILE   B C   1 
ATOM   26071 O  O   . ILE   B 1 1537 ? 44.59300   35.46600  1.84100   1.000 59.56239  ?  1535 ILE   B O   1 
ATOM   26072 C  CB  . ILE   B 1 1537 ? 45.21900   36.38300  4.70000   1.000 37.53620  ?  1535 ILE   B CB  1 
ATOM   26073 C  CG1 . ILE   B 1 1537 ? 44.80500   37.85200  4.61500   1.000 53.75421  ?  1535 ILE   B CG1 1 
ATOM   26074 C  CG2 . ILE   B 1 1537 ? 45.87100   36.08600  6.03800   1.000 35.24127  ?  1535 ILE   B CG2 1 
ATOM   26075 C  CD1 . ILE   B 1 1537 ? 43.87000   38.28400  5.72200   1.000 45.48003  ?  1535 ILE   B CD1 1 
ATOM   26076 N  N   . GLY   B 1 1538 ? 45.86900   37.27800  1.47500   1.000 50.23341  ?  1536 GLY   B N   1 
ATOM   26077 C  CA  . GLY   B 1 1538 ? 45.43900   37.46100  0.10700   1.000 50.07403  ?  1536 GLY   B CA  1 
ATOM   26078 C  C   . GLY   B 1 1538 ? 44.35200   38.50200  -0.06500  1.000 52.11328  ?  1536 GLY   B C   1 
ATOM   26079 O  O   . GLY   B 1 1538 ? 44.15500   39.40000  0.75700   1.000 54.79831  ?  1536 GLY   B O   1 
ATOM   26080 N  N   . LYS   B 1 1539 ? 43.63800   38.37000  -1.17800  1.000 57.21782  ?  1537 LYS   B N   1 
ATOM   26081 C  CA  . LYS   B 1 1539 ? 42.53500   39.23300  -1.56500  1.000 58.72958  ?  1537 LYS   B CA  1 
ATOM   26082 C  C   . LYS   B 1 1539 ? 41.20900   38.48700  -1.45300  1.000 62.60055  ?  1537 LYS   B C   1 
ATOM   26083 O  O   . LYS   B 1 1539 ? 41.17700   37.25200  -1.47200  1.000 60.38203  ?  1537 LYS   B O   1 
ATOM   26084 C  CB  . LYS   B 1 1539 ? 42.73200   39.73800  -3.00200  1.000 57.97290  ?  1537 LYS   B CB  1 
ATOM   26085 C  CG  . LYS   B 1 1539 ? 43.99900   40.55900  -3.19800  1.000 60.26787  ?  1537 LYS   B CG  1 
ATOM   26086 C  CD  . LYS   B 1 1539 ? 44.20800   40.92200  -4.66000  1.000 62.20635  ?  1537 LYS   B CD  1 
ATOM   26087 C  CE  . LYS   B 1 1539 ? 45.49200   41.71400  -4.86000  1.000 61.90829  ?  1537 LYS   B CE  1 
ATOM   26088 N  NZ  . LYS   B 1 1539 ? 45.67300   42.12100  -6.28200  1.000 59.98140  ?  1537 LYS   B NZ  1 
ATOM   26089 N  N   . PRO   B 1 1540 ? 40.09200   39.20700  -1.32100  1.000 70.27056  ?  1538 PRO   B N   1 
ATOM   26090 C  CA  . PRO   B 1 1540 ? 38.80100   38.53600  -1.12500  1.000 71.62406  ?  1538 PRO   B CA  1 
ATOM   26091 C  C   . PRO   B 1 1540 ? 38.42600   37.61700  -2.28000  1.000 71.94059  ?  1538 PRO   B C   1 
ATOM   26092 O  O   . PRO   B 1 1540 ? 38.84700   37.80800  -3.42300  1.000 74.69005  ?  1538 PRO   B O   1 
ATOM   26093 C  CB  . PRO   B 1 1540 ? 37.80800   39.70000  -0.99700  1.000 57.51255  ?  1538 PRO   B CB  1 
ATOM   26094 C  CG  . PRO   B 1 1540 ? 38.54500   40.91700  -1.46600  1.000 72.71550  ?  1538 PRO   B CG  1 
ATOM   26095 C  CD  . PRO   B 1 1540 ? 39.97700   40.66200  -1.14200  1.000 70.78850  ?  1538 PRO   B CD  1 
ATOM   26096 N  N   . LEU   B 1 1541 ? 37.62300   36.60100  -1.95600  1.000 70.82875  ?  1539 LEU   B N   1 
ATOM   26097 C  CA  . LEU   B 1 1541 ? 37.08900   35.67900  -2.94700  1.000 67.72350  ?  1539 LEU   B CA  1 
ATOM   26098 C  C   . LEU   B 1 1541 ? 36.08200   36.40700  -3.83400  1.000 73.44985  ?  1539 LEU   B C   1 
ATOM   26099 O  O   . LEU   B 1 1541 ? 35.71900   37.55400  -3.56200  1.000 71.38886  ?  1539 LEU   B O   1 
ATOM   26100 C  CB  . LEU   B 1 1541 ? 36.43000   34.48200  -2.25700  1.000 56.94502  ?  1539 LEU   B CB  1 
ATOM   26101 C  CG  . LEU   B 1 1541 ? 37.25100   33.53600  -1.38300  1.000 52.61855  ?  1539 LEU   B CG  1 
ATOM   26102 C  CD1 . LEU   B 1 1541 ? 36.60400   32.16800  -1.33300  1.000 58.03772  ?  1539 LEU   B CD1 1 
ATOM   26103 C  CD2 . LEU   B 1 1541 ? 38.63700   33.42100  -1.93200  1.000 56.02043  ?  1539 LEU   B CD2 1 
ATOM   26104 N  N   . PRO   B 1 1542 ? 35.61800   35.77000  -4.91300  1.000 67.85536  ?  1540 PRO   B N   1 
ATOM   26105 C  CA  . PRO   B 1 1542 ? 34.54800   36.37000  -5.71800  1.000 64.15174  ?  1540 PRO   B CA  1 
ATOM   26106 C  C   . PRO   B 1 1542 ? 33.34200   36.76100  -4.87200  1.000 71.36016  ?  1540 PRO   B C   1 
ATOM   26107 O  O   . PRO   B 1 1542 ? 32.92600   36.03000  -3.97000  1.000 72.78780  ?  1540 PRO   B O   1 
ATOM   26108 C  CB  . PRO   B 1 1542 ? 34.20000   35.26100  -6.71500  1.000 59.19086  ?  1540 PRO   B CB  1 
ATOM   26109 C  CG  . PRO   B 1 1542 ? 35.48300   34.54300  -6.90700  1.000 62.87799  ?  1540 PRO   B CG  1 
ATOM   26110 C  CD  . PRO   B 1 1542 ? 36.20200   34.59000  -5.58200  1.000 61.40195  ?  1540 PRO   B CD  1 
ATOM   26111 N  N   . ASN   B 1 1543 ? 32.79100   37.93900  -5.17200  1.000 72.08821  ?  1541 ASN   B N   1 
ATOM   26112 C  CA  . ASN   B 1 1543 ? 31.64500   38.52100  -4.47200  1.000 59.13419  ?  1541 ASN   B CA  1 
ATOM   26113 C  C   . ASN   B 1 1543 ? 31.90200   38.71900  -2.98000  1.000 61.97161  ?  1541 ASN   B C   1 
ATOM   26114 O  O   . ASN   B 1 1543 ? 30.95800   38.85000  -2.19500  1.000 53.94650  ?  1541 ASN   B O   1 
ATOM   26115 C  CB  . ASN   B 1 1543 ? 30.37700   37.68800  -4.68900  1.000 62.36012  ?  1541 ASN   B CB  1 
ATOM   26116 C  CG  . ASN   B 1 1543 ? 29.97100   37.62000  -6.14900  1.000 70.52234  ?  1541 ASN   B CG  1 
ATOM   26117 O  OD1 . ASN   B 1 1543 ? 29.42200   38.57500  -6.69800  1.000 74.29927  ?  1541 ASN   B OD1 1 
ATOM   26118 N  ND2 . ASN   B 1 1543 ? 30.23800   36.48500  -6.78500  1.000 75.13102  ?  1541 ASN   B ND2 1 
ATOM   26119 N  N   . TYR   B 1 1544 ? 33.16800   38.74400  -2.57500  1.000 68.17251  ?  1542 TYR   B N   1 
ATOM   26120 C  CA  . TYR   B 1 1544 ? 33.58100   39.12500  -1.23400  1.000 60.52956  ?  1542 TYR   B CA  1 
ATOM   26121 C  C   . TYR   B 1 1544 ? 34.20500   40.51500  -1.26900  1.000 66.95409  ?  1542 TYR   B C   1 
ATOM   26122 O  O   . TYR   B 1 1544 ? 34.72600   40.95900  -2.29500  1.000 63.43137  ?  1542 TYR   B O   1 
ATOM   26123 C  CB  . TYR   B 1 1544 ? 34.59200   38.12900  -0.65600  1.000 70.56785  ?  1542 TYR   B CB  1 
ATOM   26124 C  CG  . TYR   B 1 1544 ? 34.01900   36.98400  0.15300   1.000 68.78972  ?  1542 TYR   B CG  1 
ATOM   26125 C  CD1 . TYR   B 1 1544 ? 33.58300   37.17700  1.45700   1.000 67.24562  ?  1542 TYR   B CD1 1 
ATOM   26126 C  CD2 . TYR   B 1 1544 ? 33.95600   35.70200  -0.37300  1.000 72.79641  ?  1542 TYR   B CD2 1 
ATOM   26127 C  CE1 . TYR   B 1 1544 ? 33.07900   36.12600  2.20400   1.000 67.46137  ?  1542 TYR   B CE1 1 
ATOM   26128 C  CE2 . TYR   B 1 1544 ? 33.45800   34.64700  0.36400   1.000 62.11770  ?  1542 TYR   B CE2 1 
ATOM   26129 C  CZ  . TYR   B 1 1544 ? 33.02000   34.86400  1.65100   1.000 66.24977  ?  1542 TYR   B CZ  1 
ATOM   26130 O  OH  . TYR   B 1 1544 ? 32.52500   33.81000  2.38500   1.000 63.68893  ?  1542 TYR   B OH  1 
ATOM   26131 N  N   . ARG   B 1 1545 ? 34.15500   41.19900  -0.12700  1.000 69.06499  ?  1543 ARG   B N   1 
ATOM   26132 C  CA  . ARG   B 1 1545 ? 34.76200   42.52100  0.00200   1.000 62.47231  ?  1543 ARG   B CA  1 
ATOM   26133 C  C   . ARG   B 1 1545 ? 35.29200   42.67900  1.41800   1.000 57.52527  ?  1543 ARG   B C   1 
ATOM   26134 O  O   . ARG   B 1 1545 ? 34.54200   42.51000  2.38400   1.000 61.71449  ?  1543 ARG   B O   1 
ATOM   26135 C  CB  . ARG   B 1 1545 ? 33.75800   43.62900  -0.32700  1.000 62.29047  ?  1543 ARG   B CB  1 
ATOM   26136 C  CG  . ARG   B 1 1545 ? 33.55700   43.85900  -1.81600  1.000 62.52993  ?  1543 ARG   B CG  1 
ATOM   26137 C  CD  . ARG   B 1 1545 ? 32.37900   44.77800  -2.08300  1.000 69.27950  ?  1543 ARG   B CD  1 
ATOM   26138 N  NE  . ARG   B 1 1545 ? 31.13100   44.22800  -1.56700  1.000 66.71674  ?  1543 ARG   B NE  1 
ATOM   26139 C  CZ  . ARG   B 1 1545 ? 30.37700   43.34900  -2.21200  1.000 75.43557  ?  1543 ARG   B CZ  1 
ATOM   26140 N  NH1 . ARG   B 1 1545 ? 30.72200   42.88200  -3.40100  1.000 78.46186  ?  1543 ARG   B NH1 1 
ATOM   26141 N  NH2 . ARG   B 1 1545 ? 29.24800   42.92500  -1.65000  1.000 71.12177  ?  1543 ARG   B NH2 1 
ATOM   26142 N  N   . MET   B 1 1546 ? 36.57700   43.00500  1.53600   1.000 61.54426  ?  1544 MET   B N   1 
ATOM   26143 C  CA  . MET   B 1 1546 ? 37.24900   43.13100  2.82000   1.000 68.56365  ?  1544 MET   B CA  1 
ATOM   26144 C  C   . MET   B 1 1546 ? 37.70900   44.56700  3.02700   1.000 68.29689  ?  1544 MET   B C   1 
ATOM   26145 O  O   . MET   B 1 1546 ? 38.23700   45.19800  2.10700   1.000 54.97595  ?  1544 MET   B O   1 
ATOM   26146 C  CB  . MET   B 1 1546 ? 38.44400   42.18100  2.90400   1.000 61.05014  ?  1544 MET   B CB  1 
ATOM   26147 C  CG  . MET   B 1 1546 ? 38.17500   40.82000  2.28800   1.000 58.93896  ?  1544 MET   B CG  1 
ATOM   26148 S  SD  . MET   B 1 1546 ? 39.38000   39.58600  2.79700   1.000 53.14479  ?  1544 MET   B SD  1 
ATOM   26149 C  CE  . MET   B 1 1546 ? 39.21800   39.74900  4.56900   1.000 40.80377  ?  1544 MET   B CE  1 
ATOM   26150 N  N   . TYR   B 1 1547 ? 37.50600   45.07800  4.24000   1.000 57.01671  ?  1545 TYR   B N   1 
ATOM   26151 C  CA  . TYR   B 1 1547 ? 37.91300   46.42900  4.59500   1.000 42.32077  ?  1545 TYR   B CA  1 
ATOM   26152 C  C   . TYR   B 1 1547 ? 38.74300   46.39900  5.87000   1.000 57.53971  ?  1545 TYR   B C   1 
ATOM   26153 O  O   . TYR   B 1 1547 ? 38.56500   45.53000  6.72900   1.000 65.05451  ?  1545 TYR   B O   1 
ATOM   26154 C  CB  . TYR   B 1 1547 ? 36.70700   47.35900  4.79300   1.000 30.31946  ?  1545 TYR   B CB  1 
ATOM   26155 C  CG  . TYR   B 1 1547 ? 35.74800   47.39100  3.62500   1.000 59.59774  ?  1545 TYR   B CG  1 
ATOM   26156 C  CD1 . TYR   B 1 1547 ? 36.08200   48.03600  2.44200   1.000 57.72357  ?  1545 TYR   B CD1 1 
ATOM   26157 C  CD2 . TYR   B 1 1547 ? 34.50200   46.78400  3.71100   1.000 62.99738  ?  1545 TYR   B CD2 1 
ATOM   26158 C  CE1 . TYR   B 1 1547 ? 35.20400   48.06800  1.37200   1.000 59.05861  ?  1545 TYR   B CE1 1 
ATOM   26159 C  CE2 . TYR   B 1 1547 ? 33.61900   46.81100  2.65000   1.000 56.73026  ?  1545 TYR   B CE2 1 
ATOM   26160 C  CZ  . TYR   B 1 1547 ? 33.97400   47.45400  1.48300   1.000 51.53228  ?  1545 TYR   B CZ  1 
ATOM   26161 O  OH  . TYR   B 1 1547 ? 33.09500   47.48200  0.42500   1.000 60.19146  ?  1545 TYR   B OH  1 
ATOM   26162 N  N   . ILE   B 1 1548 ? 39.65100   47.36400  5.98300   1.000 59.16968  ?  1546 ILE   B N   1 
ATOM   26163 C  CA  . ILE   B 1 1548 ? 40.48700   47.54000  7.16500   1.000 61.55405  ?  1546 ILE   B CA  1 
ATOM   26164 C  C   . ILE   B 1 1548 ? 40.20800   48.92800  7.72500   1.000 56.81389  ?  1546 ILE   B C   1 
ATOM   26165 O  O   . ILE   B 1 1548 ? 40.41200   49.93400  7.03400   1.000 59.86104  ?  1546 ILE   B O   1 
ATOM   26166 C  CB  . ILE   B 1 1548 ? 41.97800   47.35600  6.84200   1.000 54.82360  ?  1546 ILE   B CB  1 
ATOM   26167 C  CG1 . ILE   B 1 1548 ? 42.28300   45.87600  6.59700   1.000 47.15904  ?  1546 ILE   B CG1 1 
ATOM   26168 C  CG2 . ILE   B 1 1548 ? 42.84100   47.90900  7.96400   1.000 40.82307  ?  1546 ILE   B CG2 1 
ATOM   26169 C  CD1 . ILE   B 1 1548 ? 43.65800   45.61600  6.02900   1.000 51.58613  ?  1546 ILE   B CD1 1 
ATOM   26170 N  N   . ILE   B 1 1549 ? 39.73200   48.98000  8.96900   1.000 58.43314  ?  1547 ILE   B N   1 
ATOM   26171 C  CA  . ILE   B 1 1549 ? 39.34400   50.22400  9.61900   1.000 67.49601  ?  1547 ILE   B CA  1 
ATOM   26172 C  C   . ILE   B 1 1549 ? 40.08700   50.34100  10.94500  1.000 72.78246  ?  1547 ILE   B C   1 
ATOM   26173 O  O   . ILE   B 1 1549 ? 40.76300   49.41500  11.39200  1.000 69.36642  ?  1547 ILE   B O   1 
ATOM   26174 C  CB  . ILE   B 1 1549 ? 37.82200   50.31600  9.84900   1.000 72.44299  ?  1547 ILE   B CB  1 
ATOM   26175 C  CG1 . ILE   B 1 1549 ? 37.36000   49.18500  10.76900  1.000 62.43219  ?  1547 ILE   B CG1 1 
ATOM   26176 C  CG2 . ILE   B 1 1549 ? 37.07600   50.27500  8.52200   1.000 62.03948  ?  1547 ILE   B CG2 1 
ATOM   26177 C  CD1 . ILE   B 1 1549 ? 36.07200   49.48100  11.49700  1.000 71.93700  ?  1547 ILE   B CD1 1 
ATOM   26178 N  N   . ASN   B 1 1550 ? 39.93800   51.50300  11.58000  1.000 70.75776  ?  1548 ASN   B N   1 
ATOM   26179 C  CA  . ASN   B 1 1550 ? 40.59800   51.84400  12.83000  1.000 76.70522  ?  1548 ASN   B CA  1 
ATOM   26180 C  C   . ASN   B 1 1550 ? 39.55700   51.91700  13.95000  1.000 67.78608  ?  1548 ASN   B C   1 
ATOM   26181 O  O   . ASN   B 1 1550 ? 38.50700   51.25500  13.86400  1.000 84.16885  ?  1548 ASN   B O   1 
ATOM   26182 C  CB  . ASN   B 1 1550 ? 41.38300   53.13800  12.63300  1.000 74.73728  ?  1548 ASN   B CB  1 
ATOM   26183 C  CG  . ASN   B 1 1550 ? 40.52800   54.25600  12.06800  1.000 78.91862  ?  1548 ASN   B CG  1 
ATOM   26184 O  OD1 . ASN   B 1 1550 ? 39.50300   54.00800  11.43300  1.000 73.49180  ?  1548 ASN   B OD1 1 
ATOM   26185 N  ND2 . ASN   B 1 1550 ? 40.94900   55.49400  12.29200  1.000 81.68752  ?  1548 ASN   B ND2 1 
ATOM   26186 N  N   . ARG   B 1 1551 ? 39.84600   52.70100  14.99400  1.000 64.83161  ?  1549 ARG   B N   1 
ATOM   26187 C  CA  . ARG   B 1 1551 ? 38.89100   52.87200  16.08600  1.000 63.87366  ?  1549 ARG   B CA  1 
ATOM   26188 C  C   . ARG   B 1 1551 ? 37.56300   53.41000  15.57400  1.000 66.99020  ?  1549 ARG   B C   1 
ATOM   26189 O  O   . ARG   B 1 1551 ? 36.49400   53.00600  16.04800  1.000 90.62116  ?  1549 ARG   B O   1 
ATOM   26190 C  CB  . ARG   B 1 1551 ? 39.46900   53.80800  17.14600  1.000 76.18753  ?  1549 ARG   B CB  1 
ATOM   26191 C  CG  . ARG   B 1 1551 ? 40.64000   53.23600  17.92800  1.000 83.76659  ?  1549 ARG   B CG  1 
ATOM   26192 C  CD  . ARG   B 1 1551 ? 41.42700   54.33000  18.64600  1.000 73.31516  ?  1549 ARG   B CD  1 
ATOM   26193 N  NE  . ARG   B 1 1551 ? 40.57800   55.21300  19.43700  1.000 105.69823 ?  1549 ARG   B NE  1 
ATOM   26194 C  CZ  . ARG   B 1 1551 ? 40.16700   56.41200  19.04200  1.000 101.19301 ?  1549 ARG   B CZ  1 
ATOM   26195 N  NH1 . ARG   B 1 1551 ? 40.50700   56.90400  17.86200  1.000 79.91260  ?  1549 ARG   B NH1 1 
ATOM   26196 N  NH2 . ARG   B 1 1551 ? 39.39200   57.13100  19.84900  1.000 89.17166  ?  1549 ARG   B NH2 1 
ATOM   26197 N  N   . HIS   B 1 1552 ? 37.61000   54.32500  14.61300  1.000 60.22980  ?  1550 HIS   B N   1 
ATOM   26198 C  CA  . HIS   B 1 1552 ? 36.42200   54.80200  13.93200  1.000 59.23365  ?  1550 HIS   B CA  1 
ATOM   26199 C  C   . HIS   B 1 1552 ? 36.23600   54.00600  12.64400  1.000 72.31349  ?  1550 HIS   B C   1 
ATOM   26200 O  O   . HIS   B 1 1552 ? 37.02300   53.11700  12.31100  1.000 65.31556  ?  1550 HIS   B O   1 
ATOM   26201 C  CB  . HIS   B 1 1552 ? 36.53000   56.30100  13.65700  1.000 62.20421  ?  1550 HIS   B CB  1 
ATOM   26202 C  CG  . HIS   B 1 1552 ? 37.24200   57.05900  14.73400  1.000 83.15430  ?  1550 HIS   B CG  1 
ATOM   26203 N  ND1 . HIS   B 1 1552 ? 38.42900   57.72500  14.51400  1.000 91.40798  ?  1550 HIS   B ND1 1 
ATOM   26204 C  CD2 . HIS   B 1 1552 ? 36.94300   57.24500  16.04100  1.000 72.31534  ?  1550 HIS   B CD2 1 
ATOM   26205 C  CE1 . HIS   B 1 1552 ? 38.82600   58.29400  15.63800  1.000 80.99004  ?  1550 HIS   B CE1 1 
ATOM   26206 N  NE2 . HIS   B 1 1552 ? 37.94300   58.01800  16.58000  1.000 64.23812  ?  1550 HIS   B NE2 1 
ATOM   26207 N  N   . GLY   B 1 1553 ? 35.18000   54.33200  11.90700  1.000 65.41036  ?  1551 GLY   B N   1 
ATOM   26208 C  CA  . GLY   B 1 1553 ? 34.90900   53.63300  10.67100  1.000 60.33135  ?  1551 GLY   B CA  1 
ATOM   26209 C  C   . GLY   B 1 1553 ? 35.78700   54.01500  9.50300   1.000 73.39963  ?  1551 GLY   B C   1 
ATOM   26210 O  O   . GLY   B 1 1553 ? 35.56100   53.53300  8.39000   1.000 84.03354  ?  1551 GLY   B O   1 
ATOM   26211 N  N   . GLN   B 1 1554 ? 36.79100   54.86100  9.72400   1.000 88.82599  ?  1552 GLN   B N   1 
ATOM   26212 C  CA  . GLN   B 1 1554 ? 37.61500   55.35700  8.63000   1.000 89.68946  ?  1552 GLN   B CA  1 
ATOM   26213 C  C   . GLN   B 1 1554 ? 38.44200   54.23900  8.00800   1.000 77.74164  ?  1552 GLN   B C   1 
ATOM   26214 O  O   . GLN   B 1 1554 ? 38.99600   53.38600  8.70700   1.000 64.67263  ?  1552 GLN   B O   1 
ATOM   26215 C  CB  . GLN   B 1 1554 ? 38.52800   56.47600  9.12600   1.000 75.58633  ?  1552 GLN   B CB  1 
ATOM   26216 C  CG  . GLN   B 1 1554 ? 37.95700   57.86400  8.90700   1.000 72.00230  ?  1552 GLN   B CG  1 
ATOM   26217 C  CD  . GLN   B 1 1554 ? 38.31400   58.83000  10.01600  1.000 84.22769  ?  1552 GLN   B CD  1 
ATOM   26218 O  OE1 . GLN   B 1 1554 ? 39.18000   58.55000  10.84600  1.000 88.26910  ?  1552 GLN   B OE1 1 
ATOM   26219 N  NE2 . GLN   B 1 1554 ? 37.64000   59.97300  10.04100  1.000 83.50333  ?  1552 GLN   B NE2 1 
ATOM   26220 N  N   . LEU   B 1 1555 ? 38.51700   54.25000  6.68000   1.000 64.33824  ?  1553 LEU   B N   1 
ATOM   26221 C  CA  . LEU   B 1 1555 ? 39.33100   53.28000  5.96100   1.000 54.69218  ?  1553 LEU   B CA  1 
ATOM   26222 C  C   . LEU   B 1 1555 ? 40.80800   53.49200  6.26500   1.000 63.60982  ?  1553 LEU   B C   1 
ATOM   26223 O  O   . LEU   B 1 1555 ? 41.29900   54.62300  6.29200   1.000 80.71469  ?  1553 LEU   B O   1 
ATOM   26224 C  CB  . LEU   B 1 1555 ? 39.09100   53.39600  4.45600   1.000 64.12081  ?  1553 LEU   B CB  1 
ATOM   26225 C  CG  . LEU   B 1 1555 ? 38.40900   52.21700  3.76200   1.000 64.83344  ?  1553 LEU   B CG  1 
ATOM   26226 C  CD1 . LEU   B 1 1555 ? 38.33900   52.45000  2.26100   1.000 40.80527  ?  1553 LEU   B CD1 1 
ATOM   26227 C  CD2 . LEU   B 1 1555 ? 39.13300   50.91700  4.07500   1.000 62.13003  ?  1553 LEU   B CD2 1 
ATOM   26228 N  N   . GLN   B 1 1556 ? 41.51700   52.39200  6.49600   1.000 59.83539  ?  1554 GLN   B N   1 
ATOM   26229 C  CA  . GLN   B 1 1556 ? 42.94400   52.58800  6.71100   1.000 49.15378  ?  1554 GLN   B CA  1 
ATOM   26230 C  C   . GLN   B 1 1556 ? 43.69400   52.49800  5.38400   1.000 66.30276  ?  1554 GLN   B C   1 
ATOM   26231 O  O   . GLN   B 1 1556 ? 43.32900   51.69800  4.51700   1.000 53.07885  ?  1554 GLN   B O   1 
ATOM   26232 C  CB  . GLN   B 1 1556 ? 43.49300   51.54900  7.68300   1.000 47.37343  ?  1554 GLN   B CB  1 
ATOM   26233 C  CG  . GLN   B 1 1556 ? 42.97100   51.68600  9.10600   1.000 52.73374  ?  1554 GLN   B CG  1 
ATOM   26234 C  CD  . GLN   B 1 1556 ? 43.61300   52.83300  9.86600   1.000 62.97704  ?  1554 GLN   B CD  1 
ATOM   26235 O  OE1 . GLN   B 1 1556 ? 43.56300   53.98700  9.43900   1.000 66.44299  ?  1554 GLN   B OE1 1 
ATOM   26236 N  NE2 . GLN   B 1 1556 ? 44.22300   52.51700  11.00200  1.000 69.97809  ?  1554 GLN   B NE2 1 
ATOM   26237 N  N   . PRO   B 1 1557 ? 44.73000   53.30700  5.20000   1.000 69.64035  ?  1555 PRO   B N   1 
ATOM   26238 C  CA  . PRO   B 1 1557 ? 45.48200   53.29500  3.94300   1.000 58.67584  ?  1555 PRO   B CA  1 
ATOM   26239 C  C   . PRO   B 1 1557 ? 46.50300   52.16100  3.92700   1.000 69.33526  ?  1555 PRO   B C   1 
ATOM   26240 O  O   . PRO   B 1 1557 ? 46.62100   51.37800  4.86900   1.000 62.94582  ?  1555 PRO   B O   1 
ATOM   26241 C  CB  . PRO   B 1 1557 ? 46.16000   54.66600  3.93600   1.000 70.24393  ?  1555 PRO   B CB  1 
ATOM   26242 C  CG  . PRO   B 1 1557 ? 46.37100   54.96700  5.37900   1.000 73.63596  ?  1555 PRO   B CG  1 
ATOM   26243 C  CD  . PRO   B 1 1557 ? 45.20800   54.35400  6.12000   1.000 67.57771  ?  1555 PRO   B CD  1 
ATOM   26244 N  N   . ILE   B 1 1558 ? 47.25000   52.09200  2.82200   1.000 61.31067  ?  1556 ILE   B N   1 
ATOM   26245 C  CA  . ILE   B 1 1558 ? 48.23500   51.03200  2.64600   1.000 53.64679  ?  1556 ILE   B CA  1 
ATOM   26246 C  C   . ILE   B 1 1558 ? 49.30900   51.14500  3.71700   1.000 57.07928  ?  1556 ILE   B C   1 
ATOM   26247 O  O   . ILE   B 1 1558 ? 49.85500   52.22800  3.96500   1.000 76.41778  ?  1556 ILE   B O   1 
ATOM   26248 C  CB  . ILE   B 1 1558 ? 48.84300   51.09900  1.23700   1.000 55.75164  ?  1556 ILE   B CB  1 
ATOM   26249 C  CG1 . ILE   B 1 1558 ? 47.75700   50.90900  0.17500   1.000 47.84759  ?  1556 ILE   B CG1 1 
ATOM   26250 C  CG2 . ILE   B 1 1558 ? 49.94400   50.06000  1.07800   1.000 44.69980  ?  1556 ILE   B CG2 1 
ATOM   26251 C  CD1 . ILE   B 1 1558 ? 48.27900   50.94200  -1.24600  1.000 45.68129  ?  1556 ILE   B CD1 1 
ATOM   26252 N  N   . GLY   B 1 1559 ? 49.61200   50.02000  4.36400   1.000 43.95827  ?  1557 GLY   B N   1 
ATOM   26253 C  CA  . GLY   B 1 1559 ? 50.65000   49.94500  5.36500   1.000 33.59363  ?  1557 GLY   B CA  1 
ATOM   26254 C  C   . GLY   B 1 1559 ? 50.18000   50.17300  6.78700   1.000 49.45660  ?  1557 GLY   B C   1 
ATOM   26255 O  O   . GLY   B 1 1559 ? 50.79100   49.64600  7.72300   1.000 64.94352  ?  1557 GLY   B O   1 
ATOM   26256 N  N   . VAL   B 1 1560 ? 49.11600   50.94100  6.97300   1.000 59.82496  ?  1558 VAL   B N   1 
ATOM   26257 C  CA  . VAL   B 1 1560 ? 48.62300   51.23800  8.32000   1.000 60.18238  ?  1558 VAL   B CA  1 
ATOM   26258 C  C   . VAL   B 1 1560 ? 47.78200   50.06100  8.80700   1.000 66.56612  ?  1558 VAL   B C   1 
ATOM   26259 O  O   . VAL   B 1 1560 ? 46.84600   49.64600  8.10400   1.000 66.72633  ?  1558 VAL   B O   1 
ATOM   26260 C  CB  . VAL   B 1 1560 ? 47.81500   52.53100  8.32100   1.000 55.21037  ?  1558 VAL   B CB  1 
ATOM   26261 C  CG1 . VAL   B 1 1560 ? 47.26200   52.80500  9.70800   1.000 63.71636  ?  1558 VAL   B CG1 1 
ATOM   26262 C  CG2 . VAL   B 1 1560 ? 48.68100   53.69000  7.85500   1.000 57.16410  ?  1558 VAL   B CG2 1 
ATOM   26263 N  N   . PRO   B 1 1561 ? 48.07600   49.50200  9.97800   1.000 63.67840  ?  1559 PRO   B N   1 
ATOM   26264 C  CA  . PRO   B 1 1561 ? 47.30000   48.36100  10.47000  1.000 58.93579  ?  1559 PRO   B CA  1 
ATOM   26265 C  C   . PRO   B 1 1561 ? 45.94800   48.78000  11.02600  1.000 55.86076  ?  1559 PRO   B C   1 
ATOM   26266 O  O   . PRO   B 1 1561 ? 45.77000   49.88700  11.53900  1.000 66.25286  ?  1559 PRO   B O   1 
ATOM   26267 C  CB  . PRO   B 1 1561 ? 48.19300   47.78400  11.57500  1.000 45.78771  ?  1559 PRO   B CB  1 
ATOM   26268 C  CG  . PRO   B 1 1561 ? 48.95100   48.96300  12.07800  1.000 62.53038  ?  1559 PRO   B CG  1 
ATOM   26269 C  CD  . PRO   B 1 1561 ? 49.18900   49.84700  10.88000  1.000 69.06513  ?  1559 PRO   B CD  1 
ATOM   26270 N  N   . GLY   B 1 1562 ? 44.99200   47.86700  10.91600  1.000 72.88882  ?  1560 GLY   B N   1 
ATOM   26271 C  CA  . GLY   B 1 1562 ? 43.66100   48.10200  11.42500  1.000 67.75269  ?  1560 GLY   B CA  1 
ATOM   26272 C  C   . GLY   B 1 1562 ? 42.90800   46.80100  11.59800  1.000 64.13523  ?  1560 GLY   B C   1 
ATOM   26273 O  O   . GLY   B 1 1562 ? 43.48700   45.71400  11.54600  1.000 64.83624  ?  1560 GLY   B O   1 
ATOM   26274 N  N   . GLU   B 1 1563 ? 41.59800   46.92600  11.80300  1.000 60.07907  ?  1561 GLU   B N   1 
ATOM   26275 C  CA  . GLU   B 1 1563 ? 40.74000   45.76800  12.01900  1.000 59.74475  ?  1561 GLU   B CA  1 
ATOM   26276 C  C   . GLU   B 1 1563 ? 40.17500   45.27500  10.69500  1.000 59.69108  ?  1561 GLU   B C   1 
ATOM   26277 O  O   . GLU   B 1 1563 ? 39.67000   46.06600  9.89100   1.000 50.71073  ?  1561 GLU   B O   1 
ATOM   26278 C  CB  . GLU   B 1 1563 ? 39.59600   46.09600  12.97800  1.000 67.38344  ?  1561 GLU   B CB  1 
ATOM   26279 C  CG  . GLU   B 1 1563 ? 38.65600   44.92000  13.20800  1.000 69.27392  ?  1561 GLU   B CG  1 
ATOM   26280 C  CD  . GLU   B 1 1563 ? 37.56300   45.22400  14.21100  1.000 66.16470  ?  1561 GLU   B CD  1 
ATOM   26281 O  OE1 . GLU   B 1 1563 ? 37.31000   46.41700  14.47500  1.000 84.66377  ?  1561 GLU   B OE1 1 
ATOM   26282 O  OE2 . GLU   B 1 1563 ? 36.95800   44.26600  14.73800  1.000 62.31338  -1 1561 GLU   B OE2 1 
ATOM   26283 N  N   . LEU   B 1 1564 ? 40.24700   43.96600  10.48400  1.000 52.83288  ?  1562 LEU   B N   1 
ATOM   26284 C  CA  . LEU   B 1 1564 ? 39.75200   43.36400  9.25700   1.000 53.50055  ?  1562 LEU   B CA  1 
ATOM   26285 C  C   . LEU   B 1 1564 ? 38.23500   43.22400  9.31300   1.000 54.42595  ?  1562 LEU   B C   1 
ATOM   26286 O  O   . LEU   B 1 1564 ? 37.68600   42.71900  10.29700  1.000 46.80458  ?  1562 LEU   B O   1 
ATOM   26287 C  CB  . LEU   B 1 1564 ? 40.41100   42.00500  9.04500   1.000 39.55590  ?  1562 LEU   B CB  1 
ATOM   26288 C  CG  . LEU   B 1 1564 ? 40.24400   41.41100  7.65500   1.000 46.09482  ?  1562 LEU   B CG  1 
ATOM   26289 C  CD1 . LEU   B 1 1564 ? 40.39700   42.50700  6.61500   1.000 52.83670  ?  1562 LEU   B CD1 1 
ATOM   26290 C  CD2 . LEU   B 1 1564 ? 41.27800   40.32000  7.45500   1.000 29.91753  ?  1562 LEU   B CD2 1 
ATOM   26291 N  N   . CYS   B 1 1565 ? 37.56000   43.67300  8.25700   1.000 51.02499  ?  1563 CYS   B N   1 
ATOM   26292 C  CA  . CYS   B 1 1565 ? 36.10400   43.64000  8.18500   1.000 48.40380  ?  1563 CYS   B CA  1 
ATOM   26293 C  C   . CYS   B 1 1565 ? 35.67700   43.10700  6.82700   1.000 51.74686  ?  1563 CYS   B C   1 
ATOM   26294 O  O   . CYS   B 1 1565 ? 36.18500   43.55600  5.79500   1.000 59.46654  ?  1563 CYS   B O   1 
ATOM   26295 C  CB  . CYS   B 1 1565 ? 35.50600   45.03200  8.42100   1.000 51.39983  ?  1563 CYS   B CB  1 
ATOM   26296 S  SG  . CYS   B 1 1565 ? 35.84700   45.72400  10.05700  1.000 73.05555  ?  1563 CYS   B SG  1 
ATOM   26297 N  N   . ILE   B 1 1566 ? 34.73900   42.16000  6.82600   1.000 44.47284  ?  1564 ILE   B N   1 
ATOM   26298 C  CA  . ILE   B 1 1566 ? 34.28700   41.49500  5.60900   1.000 58.29705  ?  1564 ILE   B CA  1 
ATOM   26299 C  C   . ILE   B 1 1566 ? 32.83000   41.85100  5.35100   1.000 52.11023  ?  1564 ILE   B C   1 
ATOM   26300 O  O   . ILE   B 1 1566 ? 32.02400   41.94200  6.28400   1.000 60.66703  ?  1564 ILE   B O   1 
ATOM   26301 C  CB  . ILE   B 1 1566 ? 34.46300   39.96500  5.69300   1.000 49.91536  ?  1564 ILE   B CB  1 
ATOM   26302 C  CG1 . ILE   B 1 1566 ? 35.92300   39.60700  5.95200   1.000 50.65986  ?  1564 ILE   B CG1 1 
ATOM   26303 C  CG2 . ILE   B 1 1566 ? 33.99000   39.29100  4.41300   1.000 56.51551  ?  1564 ILE   B CG2 1 
ATOM   26304 C  CD1 . ILE   B 1 1566 ? 36.17900   39.12200  7.34200   1.000 53.28153  ?  1564 ILE   B CD1 1 
ATOM   26305 N  N   . ALA   B 1 1567 ? 32.50100   42.05600  4.07700   1.000 37.93783  ?  1565 ALA   B N   1 
ATOM   26306 C  CA  . ALA   B 1 1567 ? 31.12800   42.19600  3.62100   1.000 45.77755  ?  1565 ALA   B CA  1 
ATOM   26307 C  C   . ALA   B 1 1567 ? 30.97900   41.42500  2.31800   1.000 52.91718  ?  1565 ALA   B C   1 
ATOM   26308 O  O   . ALA   B 1 1567 ? 31.96500   41.00200  1.70800   1.000 65.43584  ?  1565 ALA   B O   1 
ATOM   26309 C  CB  . ALA   B 1 1567 ? 30.74100   43.66800  3.43400   1.000 67.14636  ?  1565 ALA   B CB  1 
ATOM   26310 N  N   . GLY   B 1 1568 ? 29.74000   41.23500  1.89400   1.000 50.87313  ?  1566 GLY   B N   1 
ATOM   26311 C  CA  . GLY   B 1 1568 ? 29.46300   40.55500  0.65100   1.000 57.07205  ?  1566 GLY   B CA  1 
ATOM   26312 C  C   . GLY   B 1 1568 ? 28.26500   39.64300  0.78700   1.000 68.02720  ?  1566 GLY   B C   1 
ATOM   26313 O  O   . GLY   B 1 1568 ? 27.50300   39.71700  1.75000   1.000 64.89984  ?  1566 GLY   B O   1 
ATOM   26314 N  N   . ALA   B 1 1569 ? 28.10700   38.76300  -0.20500  1.000 58.88576  ?  1567 ALA   B N   1 
ATOM   26315 C  CA  . ALA   B 1 1569 ? 26.95000   37.87400  -0.23000  1.000 72.03849  ?  1567 ALA   B CA  1 
ATOM   26316 C  C   . ALA   B 1 1569 ? 27.05800   36.78700  0.83100   1.000 68.05790  ?  1567 ALA   B C   1 
ATOM   26317 O  O   . ALA   B 1 1569 ? 26.04600   36.38200  1.41700   1.000 73.09329  ?  1567 ALA   B O   1 
ATOM   26318 C  CB  . ALA   B 1 1569 ? 26.79900   37.25200  -1.61800  1.000 64.09193  ?  1567 ALA   B CB  1 
ATOM   26319 N  N   . SER   B 1 1570 ? 28.26900   36.30500  1.09600   1.000 56.86254  ?  1568 SER   B N   1 
ATOM   26320 C  CA  . SER   B 1 1570 ? 28.47700   35.18600  2.01300   1.000 55.93161  ?  1568 SER   B CA  1 
ATOM   26321 C  C   . SER   B 1 1570 ? 28.67500   35.63600  3.45200   1.000 55.96505  ?  1568 SER   B C   1 
ATOM   26322 O  O   . SER   B 1 1570 ? 29.54200   35.11200  4.15900   1.000 48.93684  ?  1568 SER   B O   1 
ATOM   26323 C  CB  . SER   B 1 1570 ? 29.66000   34.35100  1.54100   1.000 60.79469  ?  1568 SER   B CB  1 
ATOM   26324 O  OG  . SER   B 1 1570 ? 29.60900   34.13200  0.14400   1.000 62.35758  ?  1568 SER   B OG  1 
ATOM   26325 N  N   . LEU   B 1 1571 ? 27.89000   36.60100  3.91500   1.000 49.10311  ?  1569 LEU   B N   1 
ATOM   26326 C  CA  . LEU   B 1 1571 ? 27.94600   37.05400  5.29600   1.000 55.81992  ?  1569 LEU   B CA  1 
ATOM   26327 C  C   . LEU   B 1 1571 ? 26.83700   36.38100  6.09300   1.000 56.32732  ?  1569 LEU   B C   1 
ATOM   26328 O  O   . LEU   B 1 1571 ? 25.71100   36.23400  5.60800   1.000 55.33244  ?  1569 LEU   B O   1 
ATOM   26329 C  CB  . LEU   B 1 1571 ? 27.81300   38.57600  5.37900   1.000 56.93188  ?  1569 LEU   B CB  1 
ATOM   26330 C  CG  . LEU   B 1 1571 ? 28.80200   39.28400  6.30700   1.000 61.65385  ?  1569 LEU   B CG  1 
ATOM   26331 C  CD1 . LEU   B 1 1571 ? 30.23400   39.05800  5.84100   1.000 41.44328  ?  1569 LEU   B CD1 1 
ATOM   26332 C  CD2 . LEU   B 1 1571 ? 28.49100   40.77000  6.39100   1.000 65.30225  ?  1569 LEU   B CD2 1 
ATOM   26333 N  N   . ALA   B 1 1572 ? 27.16500   35.96700  7.31600   1.000 47.21355  ?  1570 ALA   B N   1 
ATOM   26334 C  CA  . ALA   B 1 1572 ? 26.21400   35.24100  8.14400   1.000 52.98377  ?  1570 ALA   B CA  1 
ATOM   26335 C  C   . ALA   B 1 1572 ? 25.00200   36.10600  8.47000   1.000 63.08541  ?  1570 ALA   B C   1 
ATOM   26336 O  O   . ALA   B 1 1572 ? 25.09100   37.33300  8.56100   1.000 64.44947  ?  1570 ALA   B O   1 
ATOM   26337 C  CB  . ALA   B 1 1572 ? 26.88100   34.77500  9.43800   1.000 38.68364  ?  1570 ALA   B CB  1 
ATOM   26338 N  N   . ARG   B 1 1573 ? 23.85200   35.44700  8.64600   1.000 54.47253  ?  1571 ARG   B N   1 
ATOM   26339 C  CA  . ARG   B 1 1573 ? 22.65100   36.15800  9.06600   1.000 47.93576  ?  1571 ARG   B CA  1 
ATOM   26340 C  C   . ARG   B 1 1573 ? 22.78700   36.71700  10.47600  1.000 46.16248  ?  1571 ARG   B C   1 
ATOM   26341 O  O   . ARG   B 1 1573 ? 22.07900   37.66800  10.82500  1.000 61.42603  ?  1571 ARG   B O   1 
ATOM   26342 C  CB  . ARG   B 1 1573 ? 21.42900   35.23700  8.98300   1.000 51.03521  ?  1571 ARG   B CB  1 
ATOM   26343 C  CG  . ARG   B 1 1573 ? 20.09400   35.97100  9.06100   1.000 60.31830  ?  1571 ARG   B CG  1 
ATOM   26344 C  CD  . ARG   B 1 1573 ? 18.92000   35.01900  9.24900   1.000 53.48441  ?  1571 ARG   B CD  1 
ATOM   26345 N  NE  . ARG   B 1 1573 ? 18.59700   34.26200  8.04600   1.000 65.16633  ?  1571 ARG   B NE  1 
ATOM   26346 C  CZ  . ARG   B 1 1573 ? 17.66800   33.31700  7.98800   1.000 63.10786  ?  1571 ARG   B CZ  1 
ATOM   26347 N  NH1 . ARG   B 1 1573 ? 16.97400   32.96500  9.05800   1.000 61.15657  ?  1571 ARG   B NH1 1 
ATOM   26348 N  NH2 . ARG   B 1 1573 ? 17.42900   32.71100  6.82900   1.000 48.45954  ?  1571 ARG   B NH2 1 
ATOM   26349 N  N   . GLY   B 1 1574 ? 23.68100   36.16000  11.28100  1.000 36.97237  ?  1572 GLY   B N   1 
ATOM   26350 C  CA  . GLY   B 1 1574 ? 23.93700   36.63200  12.62100  1.000 37.14173  ?  1572 GLY   B CA  1 
ATOM   26351 C  C   . GLY   B 1 1574 ? 24.16100   35.46500  13.55300  1.000 35.54323  ?  1572 GLY   B C   1 
ATOM   26352 O  O   . GLY   B 1 1574 ? 24.26000   34.31500  13.13000  1.000 53.33298  ?  1572 GLY   B O   1 
ATOM   26353 N  N   . TYR   B 1 1575 ? 24.24600   35.77300  14.84400  1.000 45.67101  ?  1573 TYR   B N   1 
ATOM   26354 C  CA  . TYR   B 1 1575 ? 24.38800   34.75100  15.86900  1.000 58.17833  ?  1573 TYR   B CA  1 
ATOM   26355 C  C   . TYR   B 1 1575 ? 23.01500   34.28100  16.32800  1.000 79.88500  ?  1573 TYR   B C   1 
ATOM   26356 O  O   . TYR   B 1 1575 ? 22.06800   35.06900  16.41000  1.000 83.79930  ?  1573 TYR   B O   1 
ATOM   26357 C  CB  . TYR   B 1 1575 ? 25.19300   35.27800  17.05800  1.000 55.80196  ?  1573 TYR   B CB  1 
ATOM   26358 C  CG  . TYR   B 1 1575 ? 26.61500   35.65600  16.70800  1.000 71.28661  ?  1573 TYR   B CG  1 
ATOM   26359 C  CD1 . TYR   B 1 1575 ? 27.59400   34.68400  16.55100  1.000 66.25104  ?  1573 TYR   B CD1 1 
ATOM   26360 C  CD2 . TYR   B 1 1575 ? 26.97800   36.98500  16.53300  1.000 69.78370  ?  1573 TYR   B CD2 1 
ATOM   26361 C  CE1 . TYR   B 1 1575 ? 28.89600   35.02400  16.22700  1.000 68.24647  ?  1573 TYR   B CE1 1 
ATOM   26362 C  CE2 . TYR   B 1 1575 ? 28.27700   37.33500  16.21000  1.000 60.05722  ?  1573 TYR   B CE2 1 
ATOM   26363 C  CZ  . TYR   B 1 1575 ? 29.23200   36.35100  16.05800  1.000 67.06655  ?  1573 TYR   B CZ  1 
ATOM   26364 O  OH  . TYR   B 1 1575 ? 30.52600   36.69200  15.73700  1.000 50.20308  ?  1573 TYR   B OH  1 
ATOM   26365 N  N   . LEU   B 1 1576 ? 22.91400   32.98900  16.62100  1.000 82.38489  ?  1574 LEU   B N   1 
ATOM   26366 C  CA  . LEU   B 1 1576 ? 21.64900   32.39200  17.02100  1.000 67.85113  ?  1574 LEU   B CA  1 
ATOM   26367 C  C   . LEU   B 1 1576 ? 21.33000   32.75200  18.46800  1.000 81.64981  ?  1574 LEU   B C   1 
ATOM   26368 O  O   . LEU   B 1 1576 ? 22.14800   32.53000  19.36700  1.000 78.18388  ?  1574 LEU   B O   1 
ATOM   26369 C  CB  . LEU   B 1 1576 ? 21.71000   30.87700  16.84900  1.000 60.41016  ?  1574 LEU   B CB  1 
ATOM   26370 C  CG  . LEU   B 1 1576 ? 20.42500   30.08800  17.08400  1.000 58.72463  ?  1574 LEU   B CG  1 
ATOM   26371 C  CD1 . LEU   B 1 1576 ? 19.57800   30.02600  15.82300  1.000 65.15363  ?  1574 LEU   B CD1 1 
ATOM   26372 C  CD2 . LEU   B 1 1576 ? 20.77700   28.70300  17.56400  1.000 55.46781  ?  1574 LEU   B CD2 1 
ATOM   26373 N  N   . ASN   B 1 1577 ? 20.13700   33.31200  18.68300  1.000 65.50203  ?  1575 ASN   B N   1 
ATOM   26374 C  CA  . ASN   B 1 1577 ? 19.66400   33.70600  20.01300  1.000 81.71231  ?  1575 ASN   B CA  1 
ATOM   26375 C  C   . ASN   B 1 1577 ? 20.60500   34.71200  20.67400  1.000 91.04755  ?  1575 ASN   B C   1 
ATOM   26376 O  O   . ASN   B 1 1577 ? 20.80700   34.69400  21.89000  1.000 91.85678  ?  1575 ASN   B O   1 
ATOM   26377 C  CB  . ASN   B 1 1577 ? 19.45600   32.48800  20.91500  1.000 75.32578  ?  1575 ASN   B CB  1 
ATOM   26378 C  CG  . ASN   B 1 1577 ? 18.36300   31.57300  20.40900  1.000 85.23064  ?  1575 ASN   B CG  1 
ATOM   26379 O  OD1 . ASN   B 1 1577 ? 17.63600   31.91400  19.47600  1.000 71.63150  ?  1575 ASN   B OD1 1 
ATOM   26380 N  ND2 . ASN   B 1 1577 ? 18.23500   30.40500  21.02700  1.000 88.94784  ?  1575 ASN   B ND2 1 
ATOM   26381 N  N   . ASN   B 1 1578 ? 21.18400   35.60200  19.86800  1.000 80.79343  ?  1576 ASN   B N   1 
ATOM   26382 C  CA  . ASN   B 1 1578 ? 22.01800   36.68900  20.38100  1.000 73.24635  ?  1576 ASN   B CA  1 
ATOM   26383 C  C   . ASN   B 1 1578 ? 21.91900   37.88100  19.43900  1.000 74.33776  ?  1576 ASN   B C   1 
ATOM   26384 O  O   . ASN   B 1 1578 ? 22.83900   38.16200  18.66200  1.000 82.35692  ?  1576 ASN   B O   1 
ATOM   26385 C  CB  . ASN   B 1 1578 ? 23.46800   36.23500  20.54600  1.000 55.57653  ?  1576 ASN   B CB  1 
ATOM   26386 C  CG  . ASN   B 1 1578 ? 24.19000   36.98000  21.65400  1.000 65.57187  ?  1576 ASN   B CG  1 
ATOM   26387 O  OD1 . ASN   B 1 1578 ? 23.69600   37.98300  22.16900  1.000 82.29928  ?  1576 ASN   B OD1 1 
ATOM   26388 N  ND2 . ASN   B 1 1578 ? 25.36900   36.49300  22.02500  1.000 79.04782  ?  1576 ASN   B ND2 1 
ATOM   26389 N  N   . PRO   B 1 1579 ? 20.79700   38.60600  19.47600  1.000 72.17591  ?  1577 PRO   B N   1 
ATOM   26390 C  CA  . PRO   B 1 1579 ? 20.71100   39.85400  18.69900  1.000 67.37153  ?  1577 PRO   B CA  1 
ATOM   26391 C  C   . PRO   B 1 1579 ? 21.67900   40.91900  19.18000  1.000 71.67177  ?  1577 PRO   B C   1 
ATOM   26392 O  O   . PRO   B 1 1579 ? 21.99600   41.84000  18.41700  1.000 59.28860  ?  1577 PRO   B O   1 
ATOM   26393 C  CB  . PRO   B 1 1579 ? 19.25200   40.29500  18.89400  1.000 65.29949  ?  1577 PRO   B CB  1 
ATOM   26394 C  CG  . PRO   B 1 1579 ? 18.52900   39.06700  19.36200  1.000 82.99405  ?  1577 PRO   B CG  1 
ATOM   26395 C  CD  . PRO   B 1 1579 ? 19.53300   38.30200  20.16500  1.000 80.84119  ?  1577 PRO   B CD  1 
ATOM   26396 N  N   . ALA   B 1 1580 ? 22.15500   40.82100  20.42300  1.000 67.98257  ?  1578 ALA   B N   1 
ATOM   26397 C  CA  . ALA   B 1 1580 ? 23.13700   41.77400  20.92900  1.000 62.90924  ?  1578 ALA   B CA  1 
ATOM   26398 C  C   . ALA   B 1 1580 ? 24.46100   41.63600  20.18900  1.000 63.90333  ?  1578 ALA   B C   1 
ATOM   26399 O  O   . ALA   B 1 1580 ? 24.94700   42.59200  19.57500  1.000 79.94117  ?  1578 ALA   B O   1 
ATOM   26400 C  CB  . ALA   B 1 1580 ? 23.33200   41.57200  22.43300  1.000 64.10038  ?  1578 ALA   B CB  1 
ATOM   26401 N  N   . LEU   B 1 1581 ? 25.06100   40.44400  20.23600  1.000 62.25592  ?  1579 LEU   B N   1 
ATOM   26402 C  CA  . LEU   B 1 1581 ? 26.32600   40.22700  19.54400  1.000 58.79128  ?  1579 LEU   B CA  1 
ATOM   26403 C  C   . LEU   B 1 1581 ? 26.16800   40.35200  18.03400  1.000 58.60112  ?  1579 LEU   B C   1 
ATOM   26404 O  O   . LEU   B 1 1581 ? 27.11200   40.75600  17.34600  1.000 60.20345  ?  1579 LEU   B O   1 
ATOM   26405 C  CB  . LEU   B 1 1581 ? 26.89500   38.85600  19.90800  1.000 63.81376  ?  1579 LEU   B CB  1 
ATOM   26406 C  CG  . LEU   B 1 1581 ? 28.40900   38.69700  19.77500  1.000 69.34763  ?  1579 LEU   B CG  1 
ATOM   26407 C  CD1 . LEU   B 1 1581 ? 29.11900   39.64400  20.72900  1.000 62.03546  ?  1579 LEU   B CD1 1 
ATOM   26408 C  CD2 . LEU   B 1 1581 ? 28.82300   37.25700  20.03300  1.000 64.60600  ?  1579 LEU   B CD2 1 
ATOM   26409 N  N   . THR   B 1 1582 ? 24.98900   40.01400  17.50300  1.000 59.66111  ?  1580 THR   B N   1 
ATOM   26410 C  CA  . THR   B 1 1582 ? 24.75300   40.15000  16.06900  1.000 63.56824  ?  1580 THR   B CA  1 
ATOM   26411 C  C   . THR   B 1 1582 ? 24.84900   41.60700  15.63400  1.000 60.52208  ?  1580 THR   B C   1 
ATOM   26412 O  O   . THR   B 1 1582 ? 25.49700   41.92600  14.63200  1.000 58.83347  ?  1580 THR   B O   1 
ATOM   26413 C  CB  . THR   B 1 1582 ? 23.38900   39.56500  15.70000  1.000 63.03377  ?  1580 THR   B CB  1 
ATOM   26414 O  OG1 . THR   B 1 1582 ? 23.37900   38.15700  15.97100  1.000 64.69577  ?  1580 THR   B OG1 1 
ATOM   26415 C  CG2 . THR   B 1 1582 ? 23.08700   39.79300  14.22500  1.000 49.54477  ?  1580 THR   B CG2 1 
ATOM   26416 N  N   . GLU   B 1 1583 ? 24.20900   42.50900  16.38100  1.000 66.69170  ?  1581 GLU   B N   1 
ATOM   26417 C  CA  . GLU   B 1 1583 ? 24.33400   43.92900  16.07400  1.000 63.22281  ?  1581 GLU   B CA  1 
ATOM   26418 C  C   . GLU   B 1 1583 ? 25.71800   44.46000  16.42400  1.000 57.78842  ?  1581 GLU   B C   1 
ATOM   26419 O  O   . GLU   B 1 1583 ? 26.23200   45.35000  15.73600  1.000 48.02532  ?  1581 GLU   B O   1 
ATOM   26420 C  CB  . GLU   B 1 1583 ? 23.26100   44.72800  16.81300  1.000 63.30353  ?  1581 GLU   B CB  1 
ATOM   26421 C  CG  . GLU   B 1 1583 ? 21.86000   44.52000  16.27500  1.000 69.07117  ?  1581 GLU   B CG  1 
ATOM   26422 C  CD  . GLU   B 1 1583 ? 20.97600   45.73200  16.48100  1.000 89.23166  ?  1581 GLU   B CD  1 
ATOM   26423 O  OE1 . GLU   B 1 1583 ? 20.96400   46.28000  17.60400  1.000 98.56823  ?  1581 GLU   B OE1 1 
ATOM   26424 O  OE2 . GLU   B 1 1583 ? 20.30400   46.14400  15.51300  1.000 101.05930 -1 1581 GLU   B OE2 1 
ATOM   26425 N  N   . GLU   B 1 1584 ? 26.33600   43.92500  17.48000  1.000 61.00204  ?  1582 GLU   B N   1 
ATOM   26426 C  CA  . GLU   B 1 1584 ? 27.64300   44.40900  17.91000  1.000 49.02253  ?  1582 GLU   B CA  1 
ATOM   26427 C  C   . GLU   B 1 1584 ? 28.74500   44.03000  16.92600  1.000 66.67409  ?  1582 GLU   B C   1 
ATOM   26428 O  O   . GLU   B 1 1584 ? 29.71600   44.77900  16.76900  1.000 82.21021  ?  1582 GLU   B O   1 
ATOM   26429 C  CB  . GLU   B 1 1584 ? 27.95500   43.87000  19.30900  1.000 53.07591  ?  1582 GLU   B CB  1 
ATOM   26430 C  CG  . GLU   B 1 1584 ? 29.38500   44.08600  19.78000  1.000 72.63405  ?  1582 GLU   B CG  1 
ATOM   26431 C  CD  . GLU   B 1 1584 ? 29.58400   43.69000  21.23000  1.000 84.14784  ?  1582 GLU   B CD  1 
ATOM   26432 O  OE1 . GLU   B 1 1584 ? 28.57600   43.59300  21.96200  1.000 74.68350  ?  1582 GLU   B OE1 1 
ATOM   26433 O  OE2 . GLU   B 1 1584 ? 30.74500   43.47400  21.63700  1.000 88.10017  -1 1582 GLU   B OE2 1 
ATOM   26434 N  N   . LYS   B 1 1585 ? 28.61200   42.89000  16.24700  1.000 65.49157  ?  1583 LYS   B N   1 
ATOM   26435 C  CA  . LYS   B 1 1585 ? 29.64500   42.41000  15.33700  1.000 49.77818  ?  1583 LYS   B CA  1 
ATOM   26436 C  C   . LYS   B 1 1585 ? 29.29200   42.55500  13.86500  1.000 58.83568  ?  1583 LYS   B C   1 
ATOM   26437 O  O   . LYS   B 1 1585 ? 30.20000   42.64200  13.03600  1.000 56.73920  ?  1583 LYS   B O   1 
ATOM   26438 C  CB  . LYS   B 1 1585 ? 29.96600   40.93900  15.63100  1.000 43.76347  ?  1583 LYS   B CB  1 
ATOM   26439 C  CG  . LYS   B 1 1585 ? 30.33100   40.67800  17.08200  1.000 60.02544  ?  1583 LYS   B CG  1 
ATOM   26440 C  CD  . LYS   B 1 1585 ? 31.60800   41.40300  17.47700  1.000 70.97075  ?  1583 LYS   B CD  1 
ATOM   26441 C  CE  . LYS   B 1 1585 ? 31.83600   41.33000  18.98000  1.000 76.41489  ?  1583 LYS   B CE  1 
ATOM   26442 N  NZ  . LYS   B 1 1585 ? 33.26500   41.53400  19.35300  1.000 66.72898  ?  1583 LYS   B NZ  1 
ATOM   26443 N  N   . PHE   B 1 1586 ? 28.00600   42.57600  13.51600  1.000 56.27385  ?  1584 PHE   B N   1 
ATOM   26444 C  CA  . PHE   B 1 1586 ? 27.55200   42.81700  12.14600  1.000 57.99243  ?  1584 PHE   B CA  1 
ATOM   26445 C  C   . PHE   B 1 1586 ? 26.93700   44.21200  12.11500  1.000 68.32036  ?  1584 PHE   B C   1 
ATOM   26446 O  O   . PHE   B 1 1586 ? 25.78700   44.40100  12.52300  1.000 88.09747  ?  1584 PHE   B O   1 
ATOM   26447 C  CB  . PHE   B 1 1586 ? 26.54900   41.75700  11.69300  1.000 56.16599  ?  1584 PHE   B CB  1 
ATOM   26448 C  CG  . PHE   B 1 1586 ? 27.11000   40.36300  11.64700  1.000 52.27018  ?  1584 PHE   B CG  1 
ATOM   26449 C  CD1 . PHE   B 1 1586 ? 27.20800   39.60200  12.80100  1.000 56.91100  ?  1584 PHE   B CD1 1 
ATOM   26450 C  CD2 . PHE   B 1 1586 ? 27.52400   39.80800  10.44800  1.000 52.41185  ?  1584 PHE   B CD2 1 
ATOM   26451 C  CE1 . PHE   B 1 1586 ? 27.71900   38.31800  12.76100  1.000 57.29302  ?  1584 PHE   B CE1 1 
ATOM   26452 C  CE2 . PHE   B 1 1586 ? 28.03500   38.52400  10.40100  1.000 53.73997  ?  1584 PHE   B CE2 1 
ATOM   26453 C  CZ  . PHE   B 1 1586 ? 28.13300   37.77900  11.55900  1.000 51.28269  ?  1584 PHE   B CZ  1 
ATOM   26454 N  N   . THR   B 1 1587 ? 27.70300   45.19000  11.62800  1.000 79.55954  ?  1585 THR   B N   1 
ATOM   26455 C  CA  . THR   B 1 1587 ? 27.27400   46.57700  11.68000  1.000 61.04344  ?  1585 THR   B CA  1 
ATOM   26456 C  C   . THR   B 1 1587 ? 27.11900   47.15600  10.27900  1.000 60.37152  ?  1585 THR   B C   1 
ATOM   26457 O  O   . THR   B 1 1587 ? 27.94200   46.87900  9.39900   1.000 70.94691  ?  1585 THR   B O   1 
ATOM   26458 C  CB  . THR   B 1 1587 ? 28.27700   47.43900  12.46500  1.000 70.91831  ?  1585 THR   B CB  1 
ATOM   26459 O  OG1 . THR   B 1 1587 ? 29.39700   47.75300  11.62900  1.000 80.85342  ?  1585 THR   B OG1 1 
ATOM   26460 C  CG2 . THR   B 1 1587 ? 28.76900   46.69700  13.70100  1.000 65.76212  ?  1585 THR   B CG2 1 
ATOM   26461 N  N   . PRO   B 1 1588 ? 26.07900   47.95400  10.04000  1.000 79.60529  ?  1586 PRO   B N   1 
ATOM   26462 C  CA  . PRO   B 1 1588 ? 25.99200   48.68200  8.76900   1.000 84.77913  ?  1586 PRO   B CA  1 
ATOM   26463 C  C   . PRO   B 1 1588 ? 27.01400   49.80700  8.72500   1.000 92.83873  ?  1586 PRO   B C   1 
ATOM   26464 O  O   . PRO   B 1 1588 ? 27.21600   50.52700  9.70600   1.000 81.61160  ?  1586 PRO   B O   1 
ATOM   26465 C  CB  . PRO   B 1 1588 ? 24.55600   49.22500  8.76200   1.000 65.80073  ?  1586 PRO   B CB  1 
ATOM   26466 C  CG  . PRO   B 1 1588 ? 23.83100   48.44900  9.82800   1.000 66.96991  ?  1586 PRO   B CG  1 
ATOM   26467 C  CD  . PRO   B 1 1588 ? 24.86600   48.12000  10.85500  1.000 59.58395  ?  1586 PRO   B CD  1 
ATOM   26468 N  N   . HIS   B 1 1589 ? 27.66100   49.95200  7.57400   1.000 89.62310  ?  1587 HIS   B N   1 
ATOM   26469 C  CA  . HIS   B 1 1589 ? 28.75100   50.89900  7.41700   1.000 74.26717  ?  1587 HIS   B CA  1 
ATOM   26470 C  C   . HIS   B 1 1589 ? 28.60900   51.62300  6.08700   1.000 83.85928  ?  1587 HIS   B C   1 
ATOM   26471 O  O   . HIS   B 1 1589 ? 28.14000   51.03500  5.10400   1.000 78.24837  ?  1587 HIS   B O   1 
ATOM   26472 C  CB  . HIS   B 1 1589 ? 30.11400   50.19200  7.48200   1.000 68.47638  ?  1587 HIS   B CB  1 
ATOM   26473 C  CG  . HIS   B 1 1589 ? 31.26600   51.11700  7.72000   1.000 78.09016  ?  1587 HIS   B CG  1 
ATOM   26474 N  ND1 . HIS   B 1 1589 ? 31.96500   51.71500  6.69400   1.000 64.11156  ?  1587 HIS   B ND1 1 
ATOM   26475 C  CD2 . HIS   B 1 1589 ? 31.83900   51.54900  8.86800   1.000 77.13519  ?  1587 HIS   B CD2 1 
ATOM   26476 C  CE1 . HIS   B 1 1589 ? 32.92000   52.47400  7.19800   1.000 76.38690  ?  1587 HIS   B CE1 1 
ATOM   26477 N  NE2 . HIS   B 1 1589 ? 32.86600   52.39100  8.51500   1.000 72.75505  ?  1587 HIS   B NE2 1 
ATOM   26478 N  N   . PRO   B 1 1590 ? 28.99100   52.90200  6.03000   1.000 86.41671  ?  1588 PRO   B N   1 
ATOM   26479 C  CA  . PRO   B 1 1590 ? 28.91800   53.63500  4.75400   1.000 66.57306  ?  1588 PRO   B CA  1 
ATOM   26480 C  C   . PRO   B 1 1590 ? 29.77200   53.03600  3.65100   1.000 82.88797  ?  1588 PRO   B C   1 
ATOM   26481 O  O   . PRO   B 1 1590 ? 29.50100   53.30000  2.47300   1.000 88.19950  ?  1588 PRO   B O   1 
ATOM   26482 C  CB  . PRO   B 1 1590 ? 29.40200   55.04200  5.13000   1.000 56.76572  ?  1588 PRO   B CB  1 
ATOM   26483 C  CG  . PRO   B 1 1590 ? 29.12200   55.15800  6.58700   1.000 82.18174  ?  1588 PRO   B CG  1 
ATOM   26484 C  CD  . PRO   B 1 1590 ? 29.33800   53.78600  7.15600   1.000 81.91599  ?  1588 PRO   B CD  1 
ATOM   26485 N  N   . LEU   B 1 1591 ? 30.79500   52.24700  3.99100   1.000 72.92081  ?  1589 LEU   B N   1 
ATOM   26486 C  CA  . LEU   B 1 1591 ? 31.62100   51.62000  2.96400   1.000 68.57028  ?  1589 LEU   B CA  1 
ATOM   26487 C  C   . LEU   B 1 1591 ? 30.80700   50.68600  2.07800   1.000 69.28457  ?  1589 LEU   B C   1 
ATOM   26488 O  O   . LEU   B 1 1591 ? 31.08100   50.57600  0.87800   1.000 70.94337  ?  1589 LEU   B O   1 
ATOM   26489 C  CB  . LEU   B 1 1591 ? 32.77500   50.85700  3.61700   1.000 61.45301  ?  1589 LEU   B CB  1 
ATOM   26490 C  CG  . LEU   B 1 1591 ? 34.20200   51.34200  3.35300   1.000 50.52540  ?  1589 LEU   B CG  1 
ATOM   26491 C  CD1 . LEU   B 1 1591 ? 34.21700   52.76000  2.80100   1.000 56.92480  ?  1589 LEU   B CD1 1 
ATOM   26492 C  CD2 . LEU   B 1 1591 ? 35.01000   51.26100  4.63500   1.000 55.26131  ?  1589 LEU   B CD2 1 
ATOM   26493 N  N   . GLU   B 1 1592 ? 29.80800   50.00900  2.64600   1.000 78.46094  ?  1590 GLU   B N   1 
ATOM   26494 C  CA  . GLU   B 1 1592 ? 28.94700   49.09800  1.90400   1.000 76.92631  ?  1590 GLU   B CA  1 
ATOM   26495 C  C   . GLU   B 1 1592 ? 27.60600   49.73300  1.54700   1.000 74.44138  ?  1590 GLU   B C   1 
ATOM   26496 O  O   . GLU   B 1 1592 ? 26.65900   49.01600  1.20400   1.000 83.45279  ?  1590 GLU   B O   1 
ATOM   26497 C  CB  . GLU   B 1 1592 ? 28.73900   47.80900  2.70500   1.000 61.43332  ?  1590 GLU   B CB  1 
ATOM   26498 C  CG  . GLU   B 1 1592 ? 28.44100   46.56700  1.86400   1.000 66.43155  ?  1590 GLU   B CG  1 
ATOM   26499 C  CD  . GLU   B 1 1592 ? 29.65600   46.04900  1.11800   1.000 74.30837  ?  1590 GLU   B CD  1 
ATOM   26500 O  OE1 . GLU   B 1 1592 ? 30.77600   46.53200  1.38500   1.000 69.71445  ?  1590 GLU   B OE1 1 
ATOM   26501 O  OE2 . GLU   B 1 1592 ? 29.49100   45.15300  0.26400   1.000 78.86010  -1 1590 GLU   B OE2 1 
ATOM   26502 N  N   . LYS   B 1 1593 ? 27.51000   51.06300  1.62200   1.000 77.79805  ?  1591 LYS   B N   1 
ATOM   26503 C  CA  . LYS   B 1 1593 ? 26.30400   51.81000  1.25900   1.000 83.17761  ?  1591 LYS   B CA  1 
ATOM   26504 C  C   . LYS   B 1 1593 ? 25.09300   51.34100  2.07000   1.000 82.88797  ?  1591 LYS   B C   1 
ATOM   26505 O  O   . LYS   B 1 1593 ? 24.07300   50.90800  1.53100   1.000 72.91762  ?  1591 LYS   B O   1 
ATOM   26506 C  CB  . LYS   B 1 1593 ? 26.03400   51.71500  -0.24700  1.000 69.75465  ?  1591 LYS   B CB  1 
ATOM   26507 C  CG  . LYS   B 1 1593 ? 26.58000   52.88800  -1.04300  1.000 74.89573  ?  1591 LYS   B CG  1 
ATOM   26508 C  CD  . LYS   B 1 1593 ? 26.68800   52.56500  -2.52600  1.000 73.96446  ?  1591 LYS   B CD  1 
ATOM   26509 C  CE  . LYS   B 1 1593 ? 25.37700   52.02900  -3.07900  1.000 87.17650  ?  1591 LYS   B CE  1 
ATOM   26510 N  NZ  . LYS   B 1 1593 ? 25.12500   52.51200  -4.46600  1.000 79.38433  ?  1591 LYS   B NZ  1 
ATOM   26511 N  N   . GLY   B 1 1594 ? 25.22700   51.44400  3.39300   1.000 82.71862  ?  1592 GLY   B N   1 
ATOM   26512 C  CA  . GLY   B 1 1594 ? 24.17400   51.06000  4.30600   1.000 73.37781  ?  1592 GLY   B CA  1 
ATOM   26513 C  C   . GLY   B 1 1594 ? 24.11300   49.58800  4.64600   1.000 80.48834  ?  1592 GLY   B C   1 
ATOM   26514 O  O   . GLY   B 1 1594 ? 23.52200   49.23000  5.67200   1.000 81.83429  ?  1592 GLY   B O   1 
ATOM   26515 N  N   . GLU   B 1 1595 ? 24.70100   48.72000  3.82700   1.000 77.20751  ?  1593 GLU   B N   1 
ATOM   26516 C  CA  . GLU   B 1 1595 ? 24.69300   47.29500  4.10700   1.000 59.62754  ?  1593 GLU   B CA  1 
ATOM   26517 C  C   . GLU   B 1 1595 ? 25.71900   46.96400  5.19200   1.000 72.89666  ?  1593 GLU   B C   1 
ATOM   26518 O  O   . GLU   B 1 1595 ? 26.43900   47.83200  5.69700   1.000 78.72330  ?  1593 GLU   B O   1 
ATOM   26519 C  CB  . GLU   B 1 1595 ? 24.93800   46.50200  2.82600   1.000 62.20056  ?  1593 GLU   B CB  1 
ATOM   26520 C  CG  . GLU   B 1 1595 ? 23.65100   46.09100  2.12400   1.000 73.67156  ?  1593 GLU   B CG  1 
ATOM   26521 C  CD  . GLU   B 1 1595 ? 23.79100   46.01800  0.61600   1.000 80.83865  ?  1593 GLU   B CD  1 
ATOM   26522 O  OE1 . GLU   B 1 1595 ? 24.93400   46.06100  0.11500   1.000 78.98807  ?  1593 GLU   B OE1 1 
ATOM   26523 O  OE2 . GLU   B 1 1595 ? 22.75100   45.92400  -0.06900  1.000 93.02605  -1 1593 GLU   B OE2 1 
ATOM   26524 N  N   . ARG   B 1 1596 ? 25.78900   45.68700  5.54900   1.000 71.30261  ?  1594 ARG   B N   1 
ATOM   26525 C  CA  . ARG   B 1 1596 ? 26.46500   45.23300  6.75400   1.000 69.37853  ?  1594 ARG   B CA  1 
ATOM   26526 C  C   . ARG   B 1 1596 ? 27.90000   44.80600  6.47000   1.000 68.06486  ?  1594 ARG   B C   1 
ATOM   26527 O  O   . ARG   B 1 1596 ? 28.24000   44.38900  5.36000   1.000 63.16243  ?  1594 ARG   B O   1 
ATOM   26528 C  CB  . ARG   B 1 1596 ? 25.70100   44.06300  7.37900   1.000 74.85560  ?  1594 ARG   B CB  1 
ATOM   26529 C  CG  . ARG   B 1 1596 ? 24.19100   44.18700  7.25400   1.000 70.82125  ?  1594 ARG   B CG  1 
ATOM   26530 C  CD  . ARG   B 1 1596 ? 23.48000   42.85200  7.45400   1.000 78.53206  ?  1594 ARG   B CD  1 
ATOM   26531 N  NE  . ARG   B 1 1596 ? 23.74800   41.90100  6.38000   1.000 95.65713  ?  1594 ARG   B NE  1 
ATOM   26532 C  CZ  . ARG   B 1 1596 ? 24.16700   40.65600  6.56600   1.000 79.29808  ?  1594 ARG   B CZ  1 
ATOM   26533 N  NH1 . ARG   B 1 1596 ? 24.36100   40.16600  7.77900   1.000 67.41824  ?  1594 ARG   B NH1 1 
ATOM   26534 N  NH2 . ARG   B 1 1596 ? 24.38600   39.88000  5.50800   1.000 55.72390  ?  1594 ARG   B NH2 1 
ATOM   26535 N  N   . ILE   B 1 1597 ? 28.74400   44.92400  7.49800   1.000 64.46973  ?  1595 ILE   B N   1 
ATOM   26536 C  CA  . ILE   B 1 1597 ? 30.08400   44.35600  7.51200   1.000 59.71745  ?  1595 ILE   B CA  1 
ATOM   26537 C  C   . ILE   B 1 1597 ? 30.26100   43.61600  8.83200   1.000 58.12988  ?  1595 ILE   B C   1 
ATOM   26538 O  O   . ILE   B 1 1597 ? 29.59200   43.90600  9.82600   1.000 59.05698  ?  1595 ILE   B O   1 
ATOM   26539 C  CB  . ILE   B 1 1597 ? 31.19600   45.41800  7.34000   1.000 67.36811  ?  1595 ILE   B CB  1 
ATOM   26540 C  CG1 . ILE   B 1 1597 ? 31.38700   46.22000  8.63100   1.000 59.27389  ?  1595 ILE   B CG1 1 
ATOM   26541 C  CG2 . ILE   B 1 1597 ? 30.88600   46.34500  6.17400   1.000 57.15855  ?  1595 ILE   B CG2 1 
ATOM   26542 C  CD1 . ILE   B 1 1597 ? 32.50400   47.23800  8.55900   1.000 61.95127  ?  1595 ILE   B CD1 1 
ATOM   26543 N  N   . TYR   B 1 1598 ? 31.17000   42.64600  8.83300   1.000 38.21337  ?  1596 TYR   B N   1 
ATOM   26544 C  CA  . TYR   B 1 1598 ? 31.46700   41.86700  10.02600  1.000 41.38518  ?  1596 TYR   B CA  1 
ATOM   26545 C  C   . TYR   B 1 1598 ? 32.83700   42.24500  10.56600  1.000 40.13055  ?  1596 TYR   B C   1 
ATOM   26546 O  O   . TYR   B 1 1598 ? 33.80300   42.35800  9.80800   1.000 44.39339  ?  1596 TYR   B O   1 
ATOM   26547 C  CB  . TYR   B 1 1598 ? 31.41700   40.36100  9.74900   1.000 41.99669  ?  1596 TYR   B CB  1 
ATOM   26548 C  CG  . TYR   B 1 1598 ? 32.02500   39.54200  10.86800  1.000 40.83764  ?  1596 TYR   B CG  1 
ATOM   26549 C  CD1 . TYR   B 1 1598 ? 31.41100   39.46500  12.11200  1.000 47.75392  ?  1596 TYR   B CD1 1 
ATOM   26550 C  CD2 . TYR   B 1 1598 ? 33.22000   38.86000  10.68500  1.000 43.83315  ?  1596 TYR   B CD2 1 
ATOM   26551 C  CE1 . TYR   B 1 1598 ? 31.96900   38.72600  13.14000  1.000 49.21631  ?  1596 TYR   B CE1 1 
ATOM   26552 C  CE2 . TYR   B 1 1598 ? 33.78300   38.11900  11.70500  1.000 37.57001  ?  1596 TYR   B CE2 1 
ATOM   26553 C  CZ  . TYR   B 1 1598 ? 33.15500   38.05500  12.93100  1.000 37.82538  ?  1596 TYR   B CZ  1 
ATOM   26554 O  OH  . TYR   B 1 1598 ? 33.71400   37.31800  13.94900  1.000 63.76157  ?  1596 TYR   B OH  1 
ATOM   26555 N  N   . ARG   B 1 1599 ? 32.91400   42.42100  11.88100  1.000 36.28582  ?  1597 ARG   B N   1 
ATOM   26556 C  CA  . ARG   B 1 1599 ? 34.13700   42.83500  12.55500  1.000 47.40289  ?  1597 ARG   B CA  1 
ATOM   26557 C  C   . ARG   B 1 1599 ? 34.78800   41.61400  13.19300  1.000 51.50147  ?  1597 ARG   B C   1 
ATOM   26558 O  O   . ARG   B 1 1599 ? 34.20700   40.99100  14.09000  1.000 59.23743  ?  1597 ARG   B O   1 
ATOM   26559 C  CB  . ARG   B 1 1599 ? 33.82400   43.90400  13.59900  1.000 54.35067  ?  1597 ARG   B CB  1 
ATOM   26560 C  CG  . ARG   B 1 1599 ? 32.66400   44.79800  13.18700  1.000 60.37584  ?  1597 ARG   B CG  1 
ATOM   26561 C  CD  . ARG   B 1 1599 ? 32.75900   46.16100  13.82500  1.000 58.09925  ?  1597 ARG   B CD  1 
ATOM   26562 N  NE  . ARG   B 1 1599 ? 32.21800   47.18900  12.94800  1.000 53.22914  ?  1597 ARG   B NE  1 
ATOM   26563 C  CZ  . ARG   B 1 1599 ? 32.65600   48.43900  12.90800  1.000 65.15752  ?  1597 ARG   B CZ  1 
ATOM   26564 N  NH1 . ARG   B 1 1599 ? 33.64100   48.84900  13.68900  1.000 56.85847  ?  1597 ARG   B NH1 1 
ATOM   26565 N  NH2 . ARG   B 1 1599 ? 32.09800   49.29500  12.05700  1.000 64.74574  ?  1597 ARG   B NH2 1 
ATOM   26566 N  N   . THR   B 1 1600 ? 35.99600   41.28000  12.72900  1.000 41.07917  ?  1598 THR   B N   1 
ATOM   26567 C  CA  . THR   B 1 1600 ? 36.66100   40.03200  13.08400  1.000 41.85238  ?  1598 THR   B CA  1 
ATOM   26568 C  C   . THR   B 1 1600 ? 37.43600   40.10000  14.39000  1.000 56.05137  ?  1598 THR   B C   1 
ATOM   26569 O  O   . THR   B 1 1600 ? 37.65700   39.05500  15.01300  1.000 64.72730  ?  1598 THR   B O   1 
ATOM   26570 C  CB  . THR   B 1 1600 ? 37.62700   39.60000  11.97100  1.000 55.28630  ?  1598 THR   B CB  1 
ATOM   26571 O  OG1 . THR   B 1 1600 ? 38.70500   40.54300  11.86100  1.000 58.28972  ?  1598 THR   B OG1 1 
ATOM   26572 C  CG2 . THR   B 1 1600 ? 36.90600   39.52700  10.65100  1.000 46.11815  ?  1598 THR   B CG2 1 
ATOM   26573 N  N   . GLY   B 1 1601 ? 37.84300   41.28700  14.82600  1.000 62.09566  ?  1599 GLY   B N   1 
ATOM   26574 C  CA  . GLY   B 1 1601 ? 38.79500   41.36200  15.91300  1.000 49.98897  ?  1599 GLY   B CA  1 
ATOM   26575 C  C   . GLY   B 1 1601 ? 40.20500   40.98300  15.52500  1.000 57.99262  ?  1599 GLY   B C   1 
ATOM   26576 O  O   . GLY   B 1 1601 ? 41.06300   40.84800  16.40500  1.000 52.84406  ?  1599 GLY   B O   1 
ATOM   26577 N  N   . ASP   B 1 1602 ? 40.46900   40.80000  14.23300  1.000 65.68487  ?  1600 ASP   B N   1 
ATOM   26578 C  CA  . ASP   B 1 1602 ? 41.79200   40.45900  13.73000  1.000 75.57478  ?  1600 ASP   B CA  1 
ATOM   26579 C  C   . ASP   B 1 1602 ? 42.46000   41.70600  13.16700  1.000 64.60362  ?  1600 ASP   B C   1 
ATOM   26580 O  O   . ASP   B 1 1602 ? 41.84000   42.45700  12.40500  1.000 46.39528  ?  1600 ASP   B O   1 
ATOM   26581 C  CB  . ASP   B 1 1602 ? 41.71200   39.38100  12.64500  1.000 65.95739  ?  1600 ASP   B CB  1 
ATOM   26582 C  CG  . ASP   B 1 1602 ? 41.04400   38.10900  13.12700  1.000 70.00947  ?  1600 ASP   B CG  1 
ATOM   26583 O  OD1 . ASP   B 1 1602 ? 40.31700   38.16300  14.14100  1.000 86.76395  ?  1600 ASP   B OD1 1 
ATOM   26584 O  OD2 . ASP   B 1 1602 ? 41.25000   37.05200  12.49300  1.000 60.24607  -1 1600 ASP   B OD2 1 
ATOM   26585 N  N   . LEU   B 1 1603 ? 43.71800   41.92100  13.54000  1.000 59.17201  ?  1601 LEU   B N   1 
ATOM   26586 C  CA  . LEU   B 1 1603 ? 44.49400   43.01400  12.97400  1.000 61.44744  ?  1601 LEU   B CA  1 
ATOM   26587 C  C   . LEU   B 1 1603 ? 44.94900   42.64800  11.56800  1.000 56.68946  ?  1601 LEU   B C   1 
ATOM   26588 O  O   . LEU   B 1 1603 ? 45.28900   41.49400  11.29100  1.000 65.08276  ?  1601 LEU   B O   1 
ATOM   26589 C  CB  . LEU   B 1 1603 ? 45.70500   43.33100  13.85100  1.000 63.99767  ?  1601 LEU   B CB  1 
ATOM   26590 C  CG  . LEU   B 1 1603 ? 46.38900   44.67200  13.57800  1.000 58.44847  ?  1601 LEU   B CG  1 
ATOM   26591 C  CD1 . LEU   B 1 1603 ? 45.66200   45.80000  14.29300  1.000 48.98599  ?  1601 LEU   B CD1 1 
ATOM   26592 C  CD2 . LEU   B 1 1603 ? 47.85200   44.63600  13.98100  1.000 63.65723  ?  1601 LEU   B CD2 1 
ATOM   26593 N  N   . ALA   B 1 1604 ? 44.95400   43.63700  10.67700  1.000 58.70703  ?  1602 ALA   B N   1 
ATOM   26594 C  CA  . ALA   B 1 1604 ? 45.29400   43.38100  9.28400   1.000 54.89709  ?  1602 ALA   B CA  1 
ATOM   26595 C  C   . ALA   B 1 1604 ? 45.83300   44.65600  8.65200   1.000 52.37371  ?  1602 ALA   B C   1 
ATOM   26596 O  O   . ALA   B 1 1604 ? 45.53900   45.76800  9.09800   1.000 57.11955  ?  1602 ALA   B O   1 
ATOM   26597 C  CB  . ALA   B 1 1604 ? 44.08500   42.85700  8.50500   1.000 44.01976  ?  1602 ALA   B CB  1 
ATOM   26598 N  N   . ARG   B 1 1605 ? 46.62200   44.47300  7.59400   1.000 47.49675  ?  1603 ARG   B N   1 
ATOM   26599 C  CA  . ARG   B 1 1605 ? 47.29300   45.56700  6.90700   1.000 49.58735  ?  1603 ARG   B CA  1 
ATOM   26600 C  C   . ARG   B 1 1605 ? 47.29400   45.30600  5.40800   1.000 61.69626  ?  1603 ARG   B C   1 
ATOM   26601 O  O   . ARG   B 1 1605 ? 47.54700   44.18200  4.96700   1.000 66.80975  ?  1603 ARG   B O   1 
ATOM   26602 C  CB  . ARG   B 1 1605 ? 48.73400   45.73400  7.41200   1.000 51.91984  ?  1603 ARG   B CB  1 
ATOM   26603 C  CG  . ARG   B 1 1605 ? 49.68100   46.40900  6.43000   1.000 60.40956  ?  1603 ARG   B CG  1 
ATOM   26604 C  CD  . ARG   B 1 1605 ? 51.09000   46.49800  6.99600   1.000 71.24498  ?  1603 ARG   B CD  1 
ATOM   26605 N  NE  . ARG   B 1 1605 ? 51.72800   45.19200  7.11300   1.000 77.12854  ?  1603 ARG   B NE  1 
ATOM   26606 C  CZ  . ARG   B 1 1605 ? 52.82500   44.95600  7.82100   1.000 82.52523  ?  1603 ARG   B CZ  1 
ATOM   26607 N  NH1 . ARG   B 1 1605 ? 53.41700   45.91400  8.51600   1.000 82.41980  ?  1603 ARG   B NH1 1 
ATOM   26608 N  NH2 . ARG   B 1 1605 ? 53.33700   43.72900  7.83700   1.000 78.48063  ?  1603 ARG   B NH2 1 
ATOM   26609 N  N   . TYR   B 1 1606 ? 47.00800   46.34900  4.63200   1.000 60.10348  ?  1604 TYR   B N   1 
ATOM   26610 C  CA  . TYR   B 1 1606 ? 47.07900   46.25900  3.18000   1.000 55.95136  ?  1604 TYR   B CA  1 
ATOM   26611 C  C   . TYR   B 1 1606 ? 48.52200   46.39000  2.71000   1.000 63.75431  ?  1604 TYR   B C   1 
ATOM   26612 O  O   . TYR   B 1 1606 ? 49.24500   47.29300  3.14300   1.000 67.23704  ?  1604 TYR   B O   1 
ATOM   26613 C  CB  . TYR   B 1 1606 ? 46.23600   47.35500  2.52700   1.000 55.49048  ?  1604 TYR   B CB  1 
ATOM   26614 C  CG  . TYR   B 1 1606 ? 44.74000   47.15300  2.58700   1.000 63.21810  ?  1604 TYR   B CG  1 
ATOM   26615 C  CD1 . TYR   B 1 1606 ? 44.12900   46.11900  1.89100   1.000 57.70102  ?  1604 TYR   B CD1 1 
ATOM   26616 C  CD2 . TYR   B 1 1606 ? 43.93300   48.02300  3.31000   1.000 66.37123  ?  1604 TYR   B CD2 1 
ATOM   26617 C  CE1 . TYR   B 1 1606 ? 42.76000   45.94300  1.93300   1.000 62.25358  ?  1604 TYR   B CE1 1 
ATOM   26618 C  CE2 . TYR   B 1 1606 ? 42.56400   47.85500  3.35600   1.000 53.61072  ?  1604 TYR   B CE2 1 
ATOM   26619 C  CZ  . TYR   B 1 1606 ? 41.98200   46.81400  2.66700   1.000 61.40799  ?  1604 TYR   B CZ  1 
ATOM   26620 O  OH  . TYR   B 1 1606 ? 40.61800   46.64500  2.71200   1.000 64.80691  ?  1604 TYR   B OH  1 
ATOM   26621 N  N   . ARG   B 1 1607 ? 48.94200   45.49200  1.82300   1.000 64.72033  ?  1605 ARG   B N   1 
ATOM   26622 C  CA  . ARG   B 1 1607 ? 50.15900   45.73300  1.06700   1.000 53.46753  ?  1605 ARG   B CA  1 
ATOM   26623 C  C   . ARG   B 1 1607 ? 49.83900   46.58100  -0.16100  1.000 65.09509  ?  1605 ARG   B C   1 
ATOM   26624 O  O   . ARG   B 1 1607 ? 48.67700   46.84300  -0.48300  1.000 71.25402  ?  1605 ARG   B O   1 
ATOM   26625 C  CB  . ARG   B 1 1607 ? 50.81900   44.42100  0.64600   1.000 61.39750  ?  1605 ARG   B CB  1 
ATOM   26626 C  CG  . ARG   B 1 1607 ? 51.39800   43.61200  1.78700   1.000 69.51916  ?  1605 ARG   B CG  1 
ATOM   26627 C  CD  . ARG   B 1 1607 ? 52.41400   42.59300  1.28700   1.000 78.98490  ?  1605 ARG   B CD  1 
ATOM   26628 N  NE  . ARG   B 1 1607 ? 51.96900   41.90700  0.08000   1.000 74.14828  ?  1605 ARG   B NE  1 
ATOM   26629 C  CZ  . ARG   B 1 1607 ? 52.56800   40.84500  -0.44300  1.000 74.28774  ?  1605 ARG   B CZ  1 
ATOM   26630 N  NH1 . ARG   B 1 1607 ? 53.62900   40.29800  0.12800   1.000 62.67805  ?  1605 ARG   B NH1 1 
ATOM   26631 N  NH2 . ARG   B 1 1607 ? 52.08800   40.31600  -1.56500  1.000 72.82905  ?  1605 ARG   B NH2 1 
ATOM   26632 N  N   . GLU   B 1 1608 ? 50.89200   47.01500  -0.85600  1.000 68.02936  ?  1606 GLU   B N   1 
ATOM   26633 C  CA  . GLU   B 1 1608 ? 50.67800   47.83600  -2.04200  1.000 73.90815  ?  1606 GLU   B CA  1 
ATOM   26634 C  C   . GLU   B 1 1608 ? 49.99200   47.05000  -3.15200  1.000 83.75221  ?  1606 GLU   B C   1 
ATOM   26635 O  O   . GLU   B 1 1608 ? 49.19200   47.61600  -3.90300  1.000 77.37249  ?  1606 GLU   B O   1 
ATOM   26636 C  CB  . GLU   B 1 1608 ? 52.00400   48.41200  -2.53700  1.000 76.94553  ?  1606 GLU   B CB  1 
ATOM   26637 C  CG  . GLU   B 1 1608 ? 51.84200   49.47300  -3.61600  1.000 84.81920  ?  1606 GLU   B CG  1 
ATOM   26638 C  CD  . GLU   B 1 1608 ? 52.53500   50.77400  -3.26200  1.000 102.64471 ?  1606 GLU   B CD  1 
ATOM   26639 O  OE1 . GLU   B 1 1608 ? 53.38600   50.76500  -2.34800  1.000 97.70844  ?  1606 GLU   B OE1 1 
ATOM   26640 O  OE2 . GLU   B 1 1608 ? 52.22700   51.80500  -3.89600  1.000 100.18588 -1 1606 GLU   B OE2 1 
ATOM   26641 N  N   . ASP   B 1 1609 ? 50.28000   45.75100  -3.26700  1.000 88.18189  ?  1607 ASP   B N   1 
ATOM   26642 C  CA  . ASP   B 1 1609 ? 49.61500   44.93400  -4.27600  1.000 74.20004  ?  1607 ASP   B CA  1 
ATOM   26643 C  C   . ASP   B 1 1609 ? 48.12600   44.78500  -3.98700  1.000 77.29437  ?  1607 ASP   B C   1 
ATOM   26644 O  O   . ASP   B 1 1609 ? 47.33000   44.60100  -4.91500  1.000 74.00776  ?  1607 ASP   B O   1 
ATOM   26645 C  CB  . ASP   B 1 1609 ? 50.28300   43.56200  -4.35900  1.000 55.79552  ?  1607 ASP   B CB  1 
ATOM   26646 C  CG  . ASP   B 1 1609 ? 50.48300   42.92400  -2.99400  1.000 71.63724  ?  1607 ASP   B CG  1 
ATOM   26647 O  OD1 . ASP   B 1 1609 ? 49.70900   43.22800  -2.06200  1.000 81.54210  ?  1607 ASP   B OD1 1 
ATOM   26648 O  OD2 . ASP   B 1 1609 ? 51.42800   42.12100  -2.85100  1.000 65.39444  -1 1607 ASP   B OD2 1 
ATOM   26649 N  N   . GLY   B 1 1610 ? 47.73700   44.86600  -2.71700  1.000 63.21384  ?  1608 GLY   B N   1 
ATOM   26650 C  CA  . GLY   B 1 1610 ? 46.35800   44.71000  -2.30500  1.000 60.46009  ?  1608 GLY   B CA  1 
ATOM   26651 C  C   . GLY   B 1 1610 ? 46.10800   43.50800  -1.43100  1.000 62.33822  ?  1608 GLY   B C   1 
ATOM   26652 O  O   . GLY   B 1 1610 ? 45.02600   43.41000  -0.83400  1.000 59.29372  ?  1608 GLY   B O   1 
ATOM   26653 N  N   . ASN   B 1 1611 ? 47.06600   42.59100  -1.33000  1.000 60.60120  ?  1609 ASN   B N   1 
ATOM   26654 C  CA  . ASN   B 1 1611 ? 46.88900   41.40700  -0.50500  1.000 63.29035  ?  1609 ASN   B CA  1 
ATOM   26655 C  C   . ASN   B 1 1611 ? 46.97800   41.78000  0.96800   1.000 60.02075  ?  1609 ASN   B C   1 
ATOM   26656 O  O   . ASN   B 1 1611 ? 47.91500   42.46100  1.39500   1.000 55.59990  ?  1609 ASN   B O   1 
ATOM   26657 C  CB  . ASN   B 1 1611 ? 47.93800   40.35200  -0.85300  1.000 71.13030  ?  1609 ASN   B CB  1 
ATOM   26658 C  CG  . ASN   B 1 1611 ? 47.84900   39.89200  -2.29800  1.000 76.35905  ?  1609 ASN   B CG  1 
ATOM   26659 O  OD1 . ASN   B 1 1611 ? 46.89200   39.22800  -2.69300  1.000 76.46075  ?  1609 ASN   B OD1 1 
ATOM   26660 N  ND2 . ASN   B 1 1611 ? 48.85700   40.23500  -3.09100  1.000 78.31521  ?  1609 ASN   B ND2 1 
ATOM   26661 N  N   . ILE   B 1 1612 ? 45.99800   41.33500  1.74100   1.000 66.72387  ?  1610 ILE   B N   1 
ATOM   26662 C  CA  . ILE   B 1 1612 ? 45.93800   41.65100  3.16100   1.000 50.68512  ?  1610 ILE   B CA  1 
ATOM   26663 C  C   . ILE   B 1 1612 ? 46.91400   40.76300  3.92000   1.000 52.47154  ?  1610 ILE   B C   1 
ATOM   26664 O  O   . ILE   B 1 1612 ? 47.20500   39.63200  3.51700   1.000 57.97896  ?  1610 ILE   B O   1 
ATOM   26665 C  CB  . ILE   B 1 1612 ? 44.49400   41.49500  3.67800   1.000 34.14900  ?  1610 ILE   B CB  1 
ATOM   26666 C  CG1 . ILE   B 1 1612 ? 43.52800   42.23700  2.75000   1.000 45.96331  ?  1610 ILE   B CG1 1 
ATOM   26667 C  CG2 . ILE   B 1 1612 ? 44.37000   42.01600  5.09300   1.000 44.10532  ?  1610 ILE   B CG2 1 
ATOM   26668 C  CD1 . ILE   B 1 1612 ? 42.19300   42.57200  3.38200   1.000 63.66033  ?  1610 ILE   B CD1 1 
ATOM   26669 N  N   . GLU   B 1 1613 ? 47.44300   41.28600  5.02400   1.000 49.18462  ?  1611 GLU   B N   1 
ATOM   26670 C  CA  . GLU   B 1 1613 ? 48.40200   40.56900  5.85300   1.000 56.52085  ?  1611 GLU   B CA  1 
ATOM   26671 C  C   . GLU   B 1 1613 ? 47.81700   40.39600  7.24600   1.000 59.40931  ?  1611 GLU   B C   1 
ATOM   26672 O  O   . GLU   B 1 1613 ? 47.45400   41.38200  7.89700   1.000 57.42396  ?  1611 GLU   B O   1 
ATOM   26673 C  CB  . GLU   B 1 1613 ? 49.73800   41.31200  5.91100   1.000 64.05642  ?  1611 GLU   B CB  1 
ATOM   26674 C  CG  . GLU   B 1 1613 ? 50.36100   41.55200  4.54700   1.000 68.34534  ?  1611 GLU   B CG  1 
ATOM   26675 C  CD  . GLU   B 1 1613 ? 51.86700   41.73000  4.61000   1.000 80.87380  ?  1611 GLU   B CD  1 
ATOM   26676 O  OE1 . GLU   B 1 1613 ? 52.34200   42.55900  5.41400   1.000 70.45069  ?  1611 GLU   B OE1 1 
ATOM   26677 O  OE2 . GLU   B 1 1613 ? 52.57800   41.02900  3.85800   1.000 79.48548  -1 1611 GLU   B OE2 1 
ATOM   26678 N  N   . TYR   B 1 1614 ? 47.72100   39.14700  7.69700   1.000 55.33448  ?  1612 TYR   B N   1 
ATOM   26679 C  CA  . TYR   B 1 1614 ? 47.23900   38.86200  9.04400   1.000 49.72731  ?  1612 TYR   B CA  1 
ATOM   26680 C  C   . TYR   B 1 1614 ? 48.32200   39.23100  10.04700  1.000 58.99923  ?  1612 TYR   B C   1 
ATOM   26681 O  O   . TYR   B 1 1614 ? 49.38800   38.60700  10.08100  1.000 65.37052  ?  1612 TYR   B O   1 
ATOM   26682 C  CB  . TYR   B 1 1614 ? 46.85200   37.39200  9.17400   1.000 60.70434  ?  1612 TYR   B CB  1 
ATOM   26683 C  CG  . TYR   B 1 1614 ? 46.24600   37.03600  10.51300  1.000 61.81859  ?  1612 TYR   B CG  1 
ATOM   26684 C  CD1 . TYR   B 1 1614 ? 44.96600   37.45600  10.84900  1.000 58.20956  ?  1612 TYR   B CD1 1 
ATOM   26685 C  CD2 . TYR   B 1 1614 ? 46.95000   36.27500  11.43800  1.000 51.68979  ?  1612 TYR   B CD2 1 
ATOM   26686 C  CE1 . TYR   B 1 1614 ? 44.40500   37.13300  12.06900  1.000 65.45267  ?  1612 TYR   B CE1 1 
ATOM   26687 C  CE2 . TYR   B 1 1614 ? 46.39600   35.94600  12.66100  1.000 55.36811  ?  1612 TYR   B CE2 1 
ATOM   26688 C  CZ  . TYR   B 1 1614 ? 45.12400   36.37900  12.97100  1.000 67.09752  ?  1612 TYR   B CZ  1 
ATOM   26689 O  OH  . TYR   B 1 1614 ? 44.56500   36.05600  14.18600  1.000 86.79016  ?  1612 TYR   B OH  1 
ATOM   26690 N  N   . LEU   B 1 1615 ? 48.05500   40.25000  10.86100  1.000 57.26950  ?  1613 LEU   B N   1 
ATOM   26691 C  CA  . LEU   B 1 1615 ? 49.01400   40.74400  11.83900  1.000 75.15431  ?  1613 LEU   B CA  1 
ATOM   26692 C  C   . LEU   B 1 1615 ? 48.66200   40.33100  13.26200  1.000 77.14312  ?  1613 LEU   B C   1 
ATOM   26693 O  O   . LEU   B 1 1615 ? 49.21700   40.88800  14.21500  1.000 81.80891  ?  1613 LEU   B O   1 
ATOM   26694 C  CB  . LEU   B 1 1615 ? 49.12800   42.26800  11.73900  1.000 63.52888  ?  1613 LEU   B CB  1 
ATOM   26695 C  CG  . LEU   B 1 1615 ? 50.15300   42.88900  10.78400  1.000 57.28961  ?  1613 LEU   B CG  1 
ATOM   26696 C  CD1 . LEU   B 1 1615 ? 50.17600   42.20200  9.42700   1.000 68.20865  ?  1613 LEU   B CD1 1 
ATOM   26697 C  CD2 . LEU   B 1 1615 ? 49.86200   44.37200  10.61600  1.000 73.89935  ?  1613 LEU   B CD2 1 
ATOM   26698 N  N   . GLY   B 1 1616 ? 47.75600   39.37600  13.42900  1.000 59.34716  ?  1614 GLY   B N   1 
ATOM   26699 C  CA  . GLY   B 1 1616 ? 47.40700   38.84700  14.73300  1.000 56.69366  ?  1614 GLY   B CA  1 
ATOM   26700 C  C   . GLY   B 1 1616 ? 46.03200   39.31100  15.18600  1.000 59.15526  ?  1614 GLY   B C   1 
ATOM   26701 O  O   . GLY   B 1 1616 ? 45.34000   40.07500  14.51100  1.000 62.48285  ?  1614 GLY   B O   1 
ATOM   26702 N  N   . ARG   B 1 1617 ? 45.64900   38.81600  16.36000  1.000 64.95097  ?  1615 ARG   B N   1 
ATOM   26703 C  CA  . ARG   B 1 1617 ? 44.39000   39.19900  16.98100  1.000 71.35896  ?  1615 ARG   B CA  1 
ATOM   26704 C  C   . ARG   B 1 1617 ? 44.55300   40.50200  17.75400  1.000 79.94175  ?  1615 ARG   B C   1 
ATOM   26705 O  O   . ARG   B 1 1617 ? 45.60100   40.77000  18.34600  1.000 82.23873  ?  1615 ARG   B O   1 
ATOM   26706 C  CB  . ARG   B 1 1617 ? 43.89800   38.09400  17.91600  1.000 60.12411  ?  1615 ARG   B CB  1 
ATOM   26707 C  CG  . ARG   B 1 1617 ? 43.41300   36.84000  17.20900  1.000 64.70902  ?  1615 ARG   B CG  1 
ATOM   26708 C  CD  . ARG   B 1 1617 ? 42.00300   37.02200  16.67200  1.000 65.67702  ?  1615 ARG   B CD  1 
ATOM   26709 N  NE  . ARG   B 1 1617 ? 41.08500   37.46700  17.71400  1.000 81.38288  ?  1615 ARG   B NE  1 
ATOM   26710 C  CZ  . ARG   B 1 1617 ? 39.76500   37.49700  17.58900  1.000 75.36897  ?  1615 ARG   B CZ  1 
ATOM   26711 N  NH1 . ARG   B 1 1617 ? 39.16600   37.10100  16.47800  1.000 63.79411  ?  1615 ARG   B NH1 1 
ATOM   26712 N  NH2 . ARG   B 1 1617 ? 39.02600   37.93100  18.60700  1.000 70.06233  ?  1615 ARG   B NH2 1 
ATOM   26713 N  N   . MET   B 1 1618 ? 43.49200   41.31400  17.75100  1.000 75.54275  ?  1616 MET   B N   1 
ATOM   26714 C  CA  . MET   B 1 1618 ? 43.56900   42.62600  18.38600  1.000 78.64328  ?  1616 MET   B CA  1 
ATOM   26715 C  C   . MET   B 1 1618 ? 43.59300   42.51500  19.90600  1.000 74.31163  ?  1616 MET   B C   1 
ATOM   26716 O  O   . MET   B 1 1618 ? 44.34600   43.23500  20.57400  1.000 72.98631  ?  1616 MET   B O   1 
ATOM   26717 C  CB  . MET   B 1 1618 ? 42.40400   43.50000  17.92700  1.000 46.25644  ?  1616 MET   B CB  1 
ATOM   26718 C  CG  . MET   B 1 1618 ? 42.70300   44.29600  16.67000  1.000 61.17639  ?  1616 MET   B CG  1 
ATOM   26719 S  SD  . MET   B 1 1618 ? 41.27100   44.47900  15.59200  1.000 69.25497  ?  1616 MET   B SD  1 
ATOM   26720 C  CE  . MET   B 1 1618 ? 40.08100   45.21400  16.70800  1.000 51.03821  ?  1616 MET   B CE  1 
ATOM   26721 N  N   . ASP   B 1 1619 ? 42.78400   41.62300  20.47100  1.000 78.35500  ?  1617 ASP   B N   1 
ATOM   26722 C  CA  . ASP   B 1 1619 ? 42.72000   41.45000  21.91600  1.000 72.31478  ?  1617 ASP   B CA  1 
ATOM   26723 C  C   . ASP   B 1 1619 ? 43.87700   40.62400  22.46800  1.000 83.87561  ?  1617 ASP   B C   1 
ATOM   26724 O  O   . ASP   B 1 1619 ? 43.87000   40.29500  23.65900  1.000 100.49301 ?  1617 ASP   B O   1 
ATOM   26725 C  CB  . ASP   B 1 1619 ? 41.38800   40.80500  22.30900  1.000 61.57622  ?  1617 ASP   B CB  1 
ATOM   26726 N  N   . HIS   B 1 1620 ? 44.86800   40.28500  21.63900  1.000 76.00064  ?  1618 HIS   B N   1 
ATOM   26727 C  CA  . HIS   B 1 1620 ? 46.00600   39.49400  22.09000  1.000 75.91603  ?  1618 HIS   B CA  1 
ATOM   26728 C  C   . HIS   B 1 1620 ? 47.31600   40.01700  21.51200  1.000 79.31275  ?  1618 HIS   B C   1 
ATOM   26729 O  O   . HIS   B 1 1620 ? 48.24900   39.24100  21.28100  1.000 79.82710  ?  1618 HIS   B O   1 
ATOM   26730 C  CB  . HIS   B 1 1620 ? 45.82900   38.01800  21.72600  1.000 77.94867  ?  1618 HIS   B CB  1 
ATOM   26731 N  N   . GLN   B 1 1621 ? 47.40500   41.32300  21.27300  1.000 83.59933  ?  1619 GLN   B N   1 
ATOM   26732 C  CA  . GLN   B 1 1621 ? 48.62800   41.91200  20.75000  1.000 85.05472  ?  1619 GLN   B CA  1 
ATOM   26733 C  C   . GLN   B 1 1621 ? 49.67000   42.05100  21.85000  1.000 91.04386  ?  1619 GLN   B C   1 
ATOM   26734 O  O   . GLN   B 1 1621 ? 49.34600   42.36000  23.00200  1.000 99.34076  ?  1619 GLN   B O   1 
ATOM   26735 C  CB  . GLN   B 1 1621 ? 48.34500   43.27800  20.12200  1.000 80.03177  ?  1619 GLN   B CB  1 
ATOM   26736 C  CG  . GLN   B 1 1621 ? 47.61100   43.22400  18.78800  1.000 82.55415  ?  1619 GLN   B CG  1 
ATOM   26737 C  CD  . GLN   B 1 1621 ? 48.46900   42.67500  17.65900  1.000 83.45166  ?  1619 GLN   B CD  1 
ATOM   26738 O  OE1 . GLN   B 1 1621 ? 49.65900   42.41000  17.83400  1.000 91.76056  ?  1619 GLN   B OE1 1 
ATOM   26739 N  NE2 . GLN   B 1 1621 ? 47.86400   42.50600  16.48900  1.000 77.03463  ?  1619 GLN   B NE2 1 
ATOM   26740 N  N   . VAL   B 1 1622 ? 50.92800   41.82300  21.48200  1.000 94.41781  ?  1620 VAL   B N   1 
ATOM   26741 C  CA  . VAL   B 1 1622 ? 52.05900   41.89400  22.40100  1.000 105.45412 ?  1620 VAL   B CA  1 
ATOM   26742 C  C   . VAL   B 1 1622 ? 52.89200   43.11000  22.02400  1.000 106.02373 ?  1620 VAL   B C   1 
ATOM   26743 O  O   . VAL   B 1 1622 ? 53.35600   43.23300  20.88100  1.000 106.15675 ?  1620 VAL   B O   1 
ATOM   26744 C  CB  . VAL   B 1 1622 ? 52.88900   40.60000  22.37300  1.000 90.93223  ?  1620 VAL   B CB  1 
ATOM   26745 C  CG1 . VAL   B 1 1622 ? 53.16500   40.17400  20.93900  1.000 83.42406  ?  1620 VAL   B CG1 1 
ATOM   26746 C  CG2 . VAL   B 1 1622 ? 54.18000   40.76800  23.16100  1.000 79.65857  ?  1620 VAL   B CG2 1 
ATOM   26747 N  N   . LYS   B 1 1623 ? 53.06500   44.01500  22.98400  1.000 96.65653  ?  1621 LYS   B N   1 
ATOM   26748 C  CA  . LYS   B 1 1623 ? 53.70600   45.30800  22.76100  1.000 91.62937  ?  1621 LYS   B CA  1 
ATOM   26749 C  C   . LYS   B 1 1623 ? 54.80400   45.49100  23.80100  1.000 103.88130 ?  1621 LYS   B C   1 
ATOM   26750 O  O   . LYS   B 1 1623 ? 54.51300   45.67300  24.99100  1.000 110.47282 ?  1621 LYS   B O   1 
ATOM   26751 C  CB  . LYS   B 1 1623 ? 52.68200   46.44800  22.83100  1.000 68.44856  ?  1621 LYS   B CB  1 
ATOM   26752 N  N   . ILE   B 1 1624 ? 56.06000   45.44200  23.35500  1.000 103.00475 ?  1622 ILE   B N   1 
ATOM   26753 C  CA  . ILE   B 1 1624 ? 57.22200   45.68300  24.20400  1.000 108.79016 ?  1622 ILE   B CA  1 
ATOM   26754 C  C   . ILE   B 1 1624 ? 57.62300   47.14900  24.06000  1.000 113.50626 ?  1622 ILE   B C   1 
ATOM   26755 O  O   . ILE   B 1 1624 ? 58.09200   47.58200  23.00200  1.000 117.20668 ?  1622 ILE   B O   1 
ATOM   26756 C  CB  . ILE   B 1 1624 ? 58.38200   44.73200  23.86800  1.000 102.01330 ?  1622 ILE   B CB  1 
ATOM   26757 C  CG1 . ILE   B 1 1624 ? 58.22000   43.40600  24.64100  1.000 109.28271 ?  1622 ILE   B CG1 1 
ATOM   26758 C  CG2 . ILE   B 1 1624 ? 59.75200   45.36700  24.24900  1.000 95.74455  ?  1622 ILE   B CG2 1 
ATOM   26759 C  CD1 . ILE   B 1 1624 ? 58.24900   43.60500  26.16900  1.000 89.45483  ?  1622 ILE   B CD1 1 
ATOM   26760 N  N   . ARG   B 1 1625 ? 57.46400   47.90200  25.14700  1.000 107.05941 ?  1623 ARG   B N   1 
ATOM   26761 C  CA  . ARG   B 1 1625 ? 57.65500   49.35300  25.16700  1.000 102.44378 ?  1623 ARG   B CA  1 
ATOM   26762 C  C   . ARG   B 1 1625 ? 56.93200   50.02300  24.00000  1.000 117.09288 ?  1623 ARG   B C   1 
ATOM   26763 O  O   . ARG   B 1 1625 ? 57.49800   50.82700  23.25800  1.000 122.20198 ?  1623 ARG   B O   1 
ATOM   26764 C  CB  . ARG   B 1 1625 ? 59.14100   49.70900  25.19200  1.000 99.58835  ?  1623 ARG   B CB  1 
ATOM   26765 C  CG  . ARG   B 1 1625 ? 59.77700   49.48300  26.55700  1.000 100.57406 ?  1623 ARG   B CG  1 
ATOM   26766 C  CD  . ARG   B 1 1625 ? 61.26400   49.79700  26.58500  1.000 99.99477  ?  1623 ARG   B CD  1 
ATOM   26767 N  NE  . ARG   B 1 1625 ? 62.07500   48.71100  26.04800  1.000 74.72648  ?  1623 ARG   B NE  1 
ATOM   26768 C  CZ  . ARG   B 1 1625 ? 62.65500   48.72900  24.85600  1.000 82.34222  ?  1623 ARG   B CZ  1 
ATOM   26769 N  NH1 . ARG   B 1 1625 ? 62.54200   49.77200  24.04900  1.000 71.35244  ?  1623 ARG   B NH1 1 
ATOM   26770 N  NH2 . ARG   B 1 1625 ? 63.36800   47.67700  24.46500  1.000 86.24648  ?  1623 ARG   B NH2 1 
ATOM   26771 N  N   . GLY   B 1 1626 ? 55.65600   49.66900  23.83600  1.000 107.16309 ?  1624 GLY   B N   1 
ATOM   26772 C  CA  . GLY   B 1 1626 ? 54.83300   50.26500  22.80100  1.000 99.71860  ?  1624 GLY   B CA  1 
ATOM   26773 C  C   . GLY   B 1 1626 ? 55.15000   49.82600  21.39000  1.000 109.71205 ?  1624 GLY   B C   1 
ATOM   26774 O  O   . GLY   B 1 1626 ? 54.81500   50.54000  20.44100  1.000 119.31445 ?  1624 GLY   B O   1 
ATOM   26775 N  N   . TYR   B 1 1627 ? 55.79100   48.67400  21.21900  1.000 106.60888 ?  1625 TYR   B N   1 
ATOM   26776 C  CA  . TYR   B 1 1627 ? 56.12700   48.14900  19.90100  1.000 102.86495 ?  1625 TYR   B CA  1 
ATOM   26777 C  C   . TYR   B 1 1627 ? 55.52400   46.76200  19.75000  1.000 107.42554 ?  1625 TYR   B C   1 
ATOM   26778 O  O   . TYR   B 1 1627 ? 55.91100   45.83500  20.47200  1.000 114.71346 ?  1625 TYR   B O   1 
ATOM   26779 C  CB  . TYR   B 1 1627 ? 57.64200   48.08800  19.69400  1.000 106.43800 ?  1625 TYR   B CB  1 
ATOM   26780 C  CG  . TYR   B 1 1627 ? 58.31000   49.43500  19.54500  1.000 114.19930 ?  1625 TYR   B CG  1 
ATOM   26781 C  CD1 . TYR   B 1 1627 ? 58.09700   50.21700  18.41800  1.000 116.02916 ?  1625 TYR   B CD1 1 
ATOM   26782 C  CD2 . TYR   B 1 1627 ? 59.17000   49.91600  20.52400  1.000 107.09711 ?  1625 TYR   B CD2 1 
ATOM   26783 C  CE1 . TYR   B 1 1627 ? 58.71100   51.44800  18.27500  1.000 113.18978 ?  1625 TYR   B CE1 1 
ATOM   26784 C  CE2 . TYR   B 1 1627 ? 59.78900   51.14400  20.39000  1.000 119.85711 ?  1625 TYR   B CE2 1 
ATOM   26785 C  CZ  . TYR   B 1 1627 ? 59.55600   51.90700  19.26400  1.000 124.55767 ?  1625 TYR   B CZ  1 
ATOM   26786 O  OH  . TYR   B 1 1627 ? 60.17000   53.13200  19.12500  1.000 111.06015 ?  1625 TYR   B OH  1 
ATOM   26787 N  N   . ARG   B 1 1628 ? 54.58600   46.61600  18.81600  1.000 93.43433  ?  1626 ARG   B N   1 
ATOM   26788 C  CA  . ARG   B 1 1628 ? 54.08900   45.28700  18.48800  1.000 91.90396  ?  1626 ARG   B CA  1 
ATOM   26789 C  C   . ARG   B 1 1628 ? 55.23500   44.42200  17.98800  1.000 87.25449  ?  1626 ARG   B C   1 
ATOM   26790 O  O   . ARG   B 1 1628 ? 55.95300   44.79500  17.05500  1.000 88.70307  ?  1626 ARG   B O   1 
ATOM   26791 C  CB  . ARG   B 1 1628 ? 52.98700   45.34400  17.42900  1.000 94.12098  ?  1626 ARG   B CB  1 
ATOM   26792 C  CG  . ARG   B 1 1628 ? 52.87000   44.02000  16.67500  1.000 88.21704  ?  1626 ARG   B CG  1 
ATOM   26793 C  CD  . ARG   B 1 1628 ? 51.72600   43.95800  15.67900  1.000 59.96913  ?  1626 ARG   B CD  1 
ATOM   26794 N  NE  . ARG   B 1 1628 ? 52.06500   43.09200  14.55400  1.000 83.85250  ?  1626 ARG   B NE  1 
ATOM   26795 C  CZ  . ARG   B 1 1628 ? 52.15100   41.76800  14.61300  1.000 91.25404  ?  1626 ARG   B CZ  1 
ATOM   26796 N  NH1 . ARG   B 1 1628 ? 51.91600   41.10800  15.73600  1.000 98.02552  ?  1626 ARG   B NH1 1 
ATOM   26797 N  NH2 . ARG   B 1 1628 ? 52.48800   41.09000  13.51900  1.000 77.66778  ?  1626 ARG   B NH2 1 
ATOM   26798 N  N   . ILE   B 1 1629 ? 55.41200   43.27300  18.61500  1.000 81.37697  ?  1627 ILE   B N   1 
ATOM   26799 C  CA  . ILE   B 1 1629 ? 56.46300   42.34900  18.22700  1.000 101.63432 ?  1627 ILE   B CA  1 
ATOM   26800 C  C   . ILE   B 1 1629 ? 55.84700   41.23600  17.39600  1.000 96.92262  ?  1627 ILE   B C   1 
ATOM   26801 O  O   . ILE   B 1 1629 ? 54.68600   40.85000  17.58300  1.000 86.94460  ?  1627 ILE   B O   1 
ATOM   26802 C  CB  . ILE   B 1 1629 ? 57.21500   41.78700  19.45200  1.000 106.96665 ?  1627 ILE   B CB  1 
ATOM   26803 C  CG1 . ILE   B 1 1629 ? 56.48100   40.57700  20.02900  1.000 109.67617 ?  1627 ILE   B CG1 1 
ATOM   26804 C  CG2 . ILE   B 1 1629 ? 57.39500   42.87300  20.50800  1.000 95.51425  ?  1627 ILE   B CG2 1 
ATOM   26805 C  CD1 . ILE   B 1 1629 ? 57.36600   39.63200  20.80400  1.000 112.22878 ?  1627 ILE   B CD1 1 
ATOM   26806 N  N   . GLU   B 1 1630 ? 56.62500   40.73400  16.44500  1.000 104.30488 ?  1628 GLU   B N   1 
ATOM   26807 C  CA  . GLU   B 1 1630 ? 56.24700   39.56800  15.65500  1.000 104.11437 ?  1628 GLU   B CA  1 
ATOM   26808 C  C   . GLU   B 1 1630 ? 56.98900   38.38100  16.25900  1.000 98.26087  ?  1628 GLU   B C   1 
ATOM   26809 O  O   . GLU   B 1 1630 ? 58.12700   38.08800  15.89300  1.000 93.00881  ?  1628 GLU   B O   1 
ATOM   26810 C  CB  . GLU   B 1 1630 ? 56.58000   39.76800  14.18200  1.000 100.21993 ?  1628 GLU   B CB  1 
ATOM   26811 N  N   . LEU   B 1 1631 ? 56.33200   37.69900  17.20500  1.000 104.48225 ?  1629 LEU   B N   1 
ATOM   26812 C  CA  . LEU   B 1 1631 ? 56.95000   36.57300  17.90000  1.000 111.43829 ?  1629 LEU   B CA  1 
ATOM   26813 C  C   . LEU   B 1 1631 ? 57.48400   35.51600  16.94600  1.000 111.30101 ?  1629 LEU   B C   1 
ATOM   26814 O  O   . LEU   B 1 1631 ? 58.40400   34.77900  17.31200  1.000 105.31045 ?  1629 LEU   B O   1 
ATOM   26815 C  CB  . LEU   B 1 1631 ? 55.95300   35.92200  18.86400  1.000 92.53955  ?  1629 LEU   B CB  1 
ATOM   26816 C  CG  . LEU   B 1 1631 ? 55.06700   36.83600  19.70900  1.000 93.18568  ?  1629 LEU   B CG  1 
ATOM   26817 C  CD1 . LEU   B 1 1631 ? 53.73800   37.06900  19.00700  1.000 101.13146 ?  1629 LEU   B CD1 1 
ATOM   26818 C  CD2 . LEU   B 1 1631 ? 54.86000   36.25500  21.10100  1.000 89.40528  ?  1629 LEU   B CD2 1 
ATOM   26819 N  N   . ASP   B 1 1632 ? 56.93000   35.42400  15.73300  1.000 100.52515 ?  1630 ASP   B N   1 
ATOM   26820 C  CA  . ASP   B 1 1632 ? 57.37700   34.43400  14.76200  1.000 107.07142 ?  1630 ASP   B CA  1 
ATOM   26821 C  C   . ASP   B 1 1632 ? 58.68100   34.83500  14.08000  1.000 108.88399 ?  1630 ASP   B C   1 
ATOM   26822 O  O   . ASP   B 1 1632 ? 59.45500   33.96000  13.67500  1.000 109.77997 ?  1630 ASP   B O   1 
ATOM   26823 C  CB  . ASP   B 1 1632 ? 56.27900   34.21200  13.72000  1.000 113.78112 ?  1630 ASP   B CB  1 
ATOM   26824 C  CG  . ASP   B 1 1632 ? 54.91300   34.03700  14.35300  1.000 111.13375 ?  1630 ASP   B CG  1 
ATOM   26825 O  OD1 . ASP   B 1 1632 ? 54.50100   34.93000  15.12100  1.000 103.22851 ?  1630 ASP   B OD1 1 
ATOM   26826 O  OD2 . ASP   B 1 1632 ? 54.25600   33.00600  14.09000  1.000 111.79704 -1 1630 ASP   B OD2 1 
ATOM   26827 N  N   . GLU   B 1 1633 ? 58.94500   36.13700  13.94200  1.000 110.33952 ?  1631 GLU   B N   1 
ATOM   26828 C  CA  . GLU   B 1 1633 ? 60.19400   36.57000  13.32200  1.000 100.97939 ?  1631 GLU   B CA  1 
ATOM   26829 C  C   . GLU   B 1 1633 ? 61.37600   36.38600  14.26700  1.000 102.70777 ?  1631 GLU   B C   1 
ATOM   26830 O  O   . GLU   B 1 1633 ? 62.45000   35.94400  13.84400  1.000 99.88014  ?  1631 GLU   B O   1 
ATOM   26831 C  CB  . GLU   B 1 1633 ? 60.08100   38.02500  12.86600  1.000 84.85076  ?  1631 GLU   B CB  1 
ATOM   26832 C  CG  . GLU   B 1 1633 ? 59.77000   38.16500  11.38300  1.000 101.77026 ?  1631 GLU   B CG  1 
ATOM   26833 C  CD  . GLU   B 1 1633 ? 58.78000   39.27400  11.09200  1.000 117.91720 ?  1631 GLU   B CD  1 
ATOM   26834 O  OE1 . GLU   B 1 1633 ? 58.73500   40.25400  11.86400  1.000 103.05714 ?  1631 GLU   B OE1 1 
ATOM   26835 O  OE2 . GLU   B 1 1633 ? 58.04100   39.16100  10.09100  1.000 126.42359 -1 1631 GLU   B OE2 1 
ATOM   26836 N  N   . ILE   B 1 1634 ? 61.20300   36.72000  15.54800  1.000 111.26570 ?  1632 ILE   B N   1 
ATOM   26837 C  CA  . ILE   B 1 1634 ? 62.22200   36.37800  16.53500  1.000 108.79601 ?  1632 ILE   B CA  1 
ATOM   26838 C  C   . ILE   B 1 1634 ? 62.31900   34.86400  16.68300  1.000 119.84238 ?  1632 ILE   B C   1 
ATOM   26839 O  O   . ILE   B 1 1634 ? 63.41800   34.30600  16.79400  1.000 116.11924 ?  1632 ILE   B O   1 
ATOM   26840 C  CB  . ILE   B 1 1634 ? 61.92500   37.06600  17.88000  1.000 113.42444 ?  1632 ILE   B CB  1 
ATOM   26841 C  CG1 . ILE   B 1 1634 ? 62.70200   36.39000  19.01200  1.000 123.21211 ?  1632 ILE   B CG1 1 
ATOM   26842 C  CG2 . ILE   B 1 1634 ? 60.43900   37.05800  18.16100  1.000 110.29570 ?  1632 ILE   B CG2 1 
ATOM   26843 C  CD1 . ILE   B 1 1634 ? 62.12600   36.64400  20.39000  1.000 132.16486 ?  1632 ILE   B CD1 1 
ATOM   26844 N  N   . ARG   B 1 1635 ? 61.17600   34.17100  16.65400  1.000 132.31894 ?  1633 ARG   B N   1 
ATOM   26845 C  CA  . ARG   B 1 1635 ? 61.17800   32.71200  16.62300  1.000 125.91353 ?  1633 ARG   B CA  1 
ATOM   26846 C  C   . ARG   B 1 1635 ? 61.43200   32.22600  15.20200  1.000 118.69808 ?  1633 ARG   B C   1 
ATOM   26847 O  O   . ARG   B 1 1635 ? 60.91500   31.18100  14.78900  1.000 125.63996 ?  1633 ARG   B O   1 
ATOM   26848 C  CB  . ARG   B 1 1635 ? 59.86100   32.14100  17.15400  1.000 99.85917  ?  1633 ARG   B CB  1 
ATOM   26849 N  N   . SER   B 1 1636 ? 62.20600   32.99400  14.44300  1.000 112.08536 ?  1634 SER   B N   1 
ATOM   26850 C  CA  . SER   B 1 1636 ? 62.80600   32.56600  13.19200  1.000 108.34290 ?  1634 SER   B CA  1 
ATOM   26851 C  C   . SER   B 1 1636 ? 64.32100   32.72800  13.33100  1.000 120.88840 ?  1634 SER   B C   1 
ATOM   26852 O  O   . SER   B 1 1636 ? 64.84400   32.93200  14.43400  1.000 112.43874 ?  1634 SER   B O   1 
ATOM   26853 C  CB  . SER   B 1 1636 ? 62.23700   33.35200  12.00900  1.000 105.44103 ?  1634 SER   B CB  1 
ATOM   26854 O  OG  . SER   B 1 1636 ? 61.15100   32.65800  11.40900  1.000 99.86349  ?  1634 SER   B OG  1 
ATOM   26855 N  N   . LYS   B 1 1637 ? 65.02800   32.63300  12.20400  1.000 119.98945 ?  1635 LYS   B N   1 
ATOM   26856 C  CA  . LYS   B 1 1637 ? 66.49200   32.65200  12.17900  1.000 122.12003 ?  1635 LYS   B CA  1 
ATOM   26857 C  C   . LYS   B 1 1637 ? 67.08600   31.56100  13.06800  1.000 125.40024 ?  1635 LYS   B C   1 
ATOM   26858 O  O   . LYS   B 1 1637 ? 68.19000   31.71300  13.59700  1.000 120.34889 ?  1635 LYS   B O   1 
ATOM   26859 C  CB  . LYS   B 1 1637 ? 67.04400   34.02700  12.57300  1.000 104.28589 ?  1635 LYS   B CB  1 
ATOM   26860 N  N   . LEU   B 1 1638 ? 66.35500   30.45400  13.24400  1.000 123.27458 ?  1636 LEU   B N   1 
ATOM   26861 C  CA  . LEU   B 1 1638 ? 66.86000   29.27700  13.94500  1.000 123.69279 ?  1636 LEU   B CA  1 
ATOM   26862 C  C   . LEU   B 1 1638 ? 67.63900   28.34400  13.02800  1.000 132.01037 ?  1636 LEU   B C   1 
ATOM   26863 O  O   . LEU   B 1 1638 ? 67.65600   27.12700  13.25800  1.000 130.44136 ?  1636 LEU   B O   1 
ATOM   26864 C  CB  . LEU   B 1 1638 ? 65.71600   28.50800  14.61100  1.000 115.60232 ?  1636 LEU   B CB  1 
ATOM   26865 C  CG  . LEU   B 1 1638 ? 64.94600   29.10400  15.79300  1.000 116.98352 ?  1636 LEU   B CG  1 
ATOM   26866 C  CD1 . LEU   B 1 1638 ? 65.81900   29.99300  16.66600  1.000 114.83460 ?  1636 LEU   B CD1 1 
ATOM   26867 C  CD2 . LEU   B 1 1638 ? 63.74200   29.85900  15.29600  1.000 114.91671 ?  1636 LEU   B CD2 1 
ATOM   26868 N  N   . ILE   B 1 1639 ? 68.26900   28.87500  11.98700  1.000 131.00388 ?  1637 ILE   B N   1 
ATOM   26869 C  CA  . ILE   B 1 1639 ? 69.06700   28.05800  11.08500  1.000 115.81797 ?  1637 ILE   B CA  1 
ATOM   26870 C  C   . ILE   B 1 1639 ? 70.41100   27.75500  11.73400  1.000 114.97021 ?  1637 ILE   B C   1 
ATOM   26871 O  O   . ILE   B 1 1639 ? 70.69300   28.21700  12.84100  1.000 103.97704 ?  1637 ILE   B O   1 
ATOM   26872 C  CB  . ILE   B 1 1639 ? 69.25200   28.74800  9.72300   1.000 75.38525  ?  1637 ILE   B CB  1 
ATOM   26873 N  N   . VAL   B 1 1648 ? 71.41000   25.78200  17.22600  1.000 104.21141 ?  1646 VAL   B N   1 
ATOM   26874 C  CA  . VAL   B 1 1648 ? 71.91500   24.51900  16.61200  1.000 101.88623 ?  1646 VAL   B CA  1 
ATOM   26875 C  C   . VAL   B 1 1648 ? 70.80300   23.89100  15.75800  1.000 123.18216 ?  1646 VAL   B C   1 
ATOM   26876 O  O   . VAL   B 1 1648 ? 71.09900   23.50100  14.60800  1.000 113.88141 ?  1646 VAL   B O   1 
ATOM   26877 C  CB  . VAL   B 1 1648 ? 72.39600   23.55500  17.71200  1.000 89.20057  ?  1646 VAL   B CB  1 
ATOM   26878 C  CG1 . VAL   B 1 1648 ? 71.62200   23.73700  19.01100  1.000 92.28402  ?  1646 VAL   B CG1 1 
ATOM   26879 C  CG2 . VAL   B 1 1648 ? 72.36900   22.09900  17.26500  1.000 86.45911  ?  1646 VAL   B CG2 1 
ATOM   26880 N  N   . VAL   B 1 1649 ? 69.56800   23.83500  16.27500  1.000 134.13806 ?  1647 VAL   B N   1 
ATOM   26881 C  CA  . VAL   B 1 1649 ? 68.47500   23.12500  15.54300  1.000 127.76314 ?  1647 VAL   B CA  1 
ATOM   26882 C  C   . VAL   B 1 1649 ? 67.22900   24.00900  15.43500  1.000 122.73638 ?  1647 VAL   B C   1 
ATOM   26883 O  O   . VAL   B 1 1649 ? 67.38300   25.24300  15.40900  1.000 128.97530 ?  1647 VAL   B O   1 
ATOM   26884 C  CB  . VAL   B 1 1649 ? 68.11900   21.80300  16.24900  1.000 126.80232 ?  1647 VAL   B CB  1 
ATOM   26885 C  CG1 . VAL   B 1 1649 ? 68.93100   20.63100  15.71000  1.000 119.30325 ?  1647 VAL   B CG1 1 
ATOM   26886 C  CG2 . VAL   B 1 1649 ? 68.26400   21.91100  17.76200  1.000 116.48931 ?  1647 VAL   B CG2 1 
ATOM   26887 N  N   . VAL   B 1 1650 ? 66.04700   23.38700  15.40300  1.000 118.97536 ?  1648 VAL   B N   1 
ATOM   26888 C  CA  . VAL   B 1 1650 ? 64.77800   24.14900  15.21500  1.000 113.09084 ?  1648 VAL   B CA  1 
ATOM   26889 C  C   . VAL   B 1 1650 ? 64.04100   24.28200  16.55700  1.000 122.57098 ?  1648 VAL   B C   1 
ATOM   26890 O  O   . VAL   B 1 1650 ? 64.72100   24.10600  17.59300  1.000 114.96974 ?  1648 VAL   B O   1 
ATOM   26891 C  CB  . VAL   B 1 1650 ? 63.95400   23.41500  14.14100  1.000 104.67801 ?  1648 VAL   B CB  1 
ATOM   26892 C  CG1 . VAL   B 1 1650 ? 63.30600   22.13500  14.65600  1.000 104.40787 ?  1648 VAL   B CG1 1 
ATOM   26893 C  CG2 . VAL   B 1 1650 ? 62.96100   24.32000  13.42000  1.000 99.37889  ?  1648 VAL   B CG2 1 
ATOM   26894 N  N   . ALA   B 1 1651 ? 62.74200   24.61500  16.53600  1.000 125.74484 ?  1649 ALA   B N   1 
ATOM   26895 C  CA  . ALA   B 1 1651 ? 61.91900   24.82700  17.75600  1.000 112.77718 ?  1649 ALA   B CA  1 
ATOM   26896 C  C   . ALA   B 1 1651 ? 62.24500   26.19300  18.36600  1.000 120.94196 ?  1649 ALA   B C   1 
ATOM   26897 O  O   . ALA   B 1 1651 ? 62.58800   27.09900  17.58100  1.000 133.02122 ?  1649 ALA   B O   1 
ATOM   26898 C  CB  . ALA   B 1 1651 ? 62.07600   23.69100  18.74400  1.000 99.93149  ?  1649 ALA   B CB  1 
ATOM   26899 N  N   . ARG   B 1 1652 ? 62.10500   26.34000  19.68800  1.000 111.94717 ?  1650 ARG   B N   1 
ATOM   26900 C  CA  . ARG   B 1 1652 ? 62.36000   27.63000  20.38500  1.000 99.07126  ?  1650 ARG   B CA  1 
ATOM   26901 C  C   . ARG   B 1 1652 ? 61.33800   28.68100  19.93600  1.000 107.81082 ?  1650 ARG   B C   1 
ATOM   26902 O  O   . ARG   B 1 1652 ? 61.67700   29.50200  19.06800  1.000 119.23603 ?  1650 ARG   B O   1 
ATOM   26903 C  CB  . ARG   B 1 1652 ? 63.78100   28.15100  20.15100  1.000 101.32215 ?  1650 ARG   B CB  1 
ATOM   26904 N  N   . ASN   B 1 1653 ? 60.14600   28.66800  20.53500  1.000 109.42833 ?  1651 ASN   B N   1 
ATOM   26905 C  CA  . ASN   B 1 1653 ? 59.10300   29.67100  20.19500  1.000 107.57439 ?  1651 ASN   B CA  1 
ATOM   26906 C  C   . ASN   B 1 1653 ? 59.16200   30.82900  21.19000  1.000 116.01655 ?  1651 ASN   B C   1 
ATOM   26907 O  O   . ASN   B 1 1653 ? 59.65500   30.61300  22.31800  1.000 112.32314 ?  1651 ASN   B O   1 
ATOM   26908 C  CB  . ASN   B 1 1653 ? 57.70800   29.06200  20.20200  1.000 91.31595  ?  1651 ASN   B CB  1 
ATOM   26909 N  N   . ASP   B 1 1654 ? 58.66600   32.00300  20.79200  1.000 111.15122 ?  1652 ASP   B N   1 
ATOM   26910 C  CA  . ASP   B 1 1654 ? 58.66600   33.15900  21.67700  1.000 102.82725 ?  1652 ASP   B CA  1 
ATOM   26911 C  C   . ASP   B 1 1654 ? 57.46100   33.12500  22.60800  1.000 111.16591 ?  1652 ASP   B C   1 
ATOM   26912 O  O   . ASP   B 1 1654 ? 56.38200   32.65200  22.24300  1.000 105.67972 ?  1652 ASP   B O   1 
ATOM   26913 C  CB  . ASP   B 1 1654 ? 58.66500   34.46000  20.87100  1.000 88.52379  ?  1652 ASP   B CB  1 
ATOM   26914 N  N   . GLN   B 1 1655 ? 57.65500   33.64500  23.81800  1.000 109.52908 ?  1653 GLN   B N   1 
ATOM   26915 C  CA  . GLN   B 1 1655 ? 56.62300   33.62500  24.84300  1.000 106.50637 ?  1653 GLN   B CA  1 
ATOM   26916 C  C   . GLN   B 1 1655 ? 56.61700   34.94700  25.59600  1.000 110.44146 ?  1653 GLN   B C   1 
ATOM   26917 O  O   . GLN   B 1 1655 ? 57.63000   35.64900  25.66000  1.000 115.87855 ?  1653 GLN   B O   1 
ATOM   26918 C  CB  . GLN   B 1 1655 ? 56.83400   32.46700  25.82700  1.000 94.69130  ?  1653 GLN   B CB  1 
ATOM   26919 N  N   . ASN   B 1 1656 ? 55.46500   35.27200  26.17200  1.000 103.51166 ?  1654 ASN   B N   1 
ATOM   26920 C  CA  . ASN   B 1 1656 ? 55.29300   36.49700  26.93900  1.000 96.67848  ?  1654 ASN   B CA  1 
ATOM   26921 C  C   . ASN   B 1 1656 ? 55.55800   36.20800  28.41800  1.000 101.10001 ?  1654 ASN   B C   1 
ATOM   26922 O  O   . ASN   B 1 1656 ? 56.18300   35.20200  28.76700  1.000 107.50695 ?  1654 ASN   B O   1 
ATOM   26923 C  CB  . ASN   B 1 1656 ? 53.89500   37.07200  26.68900  1.000 65.05203  ?  1654 ASN   B CB  1 
ATOM   26924 N  N   . GLY   B 1 1657 ? 55.08400   37.08200  29.30200  1.000 89.73940  ?  1655 GLY   B N   1 
ATOM   26925 C  CA  . GLY   B 1 1657 ? 55.28900   36.92400  30.72900  1.000 83.87606  ?  1655 GLY   B CA  1 
ATOM   26926 C  C   . GLY   B 1 1657 ? 54.97000   38.19500  31.48700  1.000 110.65424 ?  1655 GLY   B C   1 
ATOM   26927 O  O   . GLY   B 1 1657 ? 53.98800   38.87600  31.17500  1.000 112.23666 ?  1655 GLY   B O   1 
ATOM   26928 N  N   . GLN   B 1 1658 ? 55.78700   38.53100  32.48700  1.000 119.48325 ?  1656 GLN   B N   1 
ATOM   26929 C  CA  . GLN   B 1 1658 ? 55.64600   39.80000  33.20300  1.000 121.02811 ?  1656 GLN   B CA  1 
ATOM   26930 C  C   . GLN   B 1 1658 ? 56.28200   40.91300  32.36700  1.000 134.39687 ?  1656 GLN   B C   1 
ATOM   26931 O  O   . GLN   B 1 1658 ? 57.29500   41.51600  32.72800  1.000 136.47040 ?  1656 GLN   B O   1 
ATOM   26932 C  CB  . GLN   B 1 1658 ? 56.26500   39.71300  34.59200  1.000 102.22366 ?  1656 GLN   B CB  1 
ATOM   26933 C  CG  . GLN   B 1 1658 ? 55.25900   39.46400  35.70500  1.000 96.26621  ?  1656 GLN   B CG  1 
ATOM   26934 C  CD  . GLN   B 1 1658 ? 55.84700   39.69500  37.08400  1.000 110.76805 ?  1656 GLN   B CD  1 
ATOM   26935 O  OE1 . GLN   B 1 1658 ? 57.04600   39.51600  37.29800  1.000 108.11164 ?  1656 GLN   B OE1 1 
ATOM   26936 N  NE2 . GLN   B 1 1658 ? 55.00400   40.10400  38.02600  1.000 98.03956  ?  1656 GLN   B NE2 1 
ATOM   26937 N  N   . ALA   B 1 1659 ? 55.65100   41.17300  31.21900  1.000 123.45205 ?  1657 ALA   B N   1 
ATOM   26938 C  CA  . ALA   B 1 1659 ? 56.11200   42.16400  30.24600  1.000 108.68856 ?  1657 ALA   B CA  1 
ATOM   26939 C  C   . ALA   B 1 1659 ? 57.55200   41.87700  29.81600  1.000 110.93577 ?  1657 ALA   B C   1 
ATOM   26940 O  O   . ALA   B 1 1659 ? 58.45200   42.70800  29.95100  1.000 113.13222 ?  1657 ALA   B O   1 
ATOM   26941 C  CB  . ALA   B 1 1659 ? 55.96900   43.58700  30.79900  1.000 95.08521  ?  1657 ALA   B CB  1 
ATOM   26942 N  N   . TYR   B 1 1660 ? 57.75600   40.66900  29.28800  1.000 104.66445 ?  1658 TYR   B N   1 
ATOM   26943 C  CA  . TYR   B 1 1660 ? 59.10100   40.23800  28.91300  1.000 101.77541 ?  1658 TYR   B CA  1 
ATOM   26944 C  C   . TYR   B 1 1660 ? 58.97200   39.13600  27.86400  1.000 112.94034 ?  1658 TYR   B C   1 
ATOM   26945 O  O   . TYR   B 1 1660 ? 58.68800   37.98500  28.20500  1.000 119.63801 ?  1658 TYR   B O   1 
ATOM   26946 C  CB  . TYR   B 1 1660 ? 59.88200   39.75500  30.12200  1.000 93.45118  ?  1658 TYR   B CB  1 
ATOM   26947 N  N   . LEU   B 1 1661 ? 59.19600   39.49800  26.60700  1.000 119.27335 ?  1659 LEU   B N   1 
ATOM   26948 C  CA  . LEU   B 1 1661 ? 59.29600   38.48800  25.56800  1.000 124.63779 ?  1659 LEU   B CA  1 
ATOM   26949 C  C   . LEU   B 1 1661 ? 60.54000   37.64200  25.82200  1.000 129.51725 ?  1659 LEU   B C   1 
ATOM   26950 O  O   . LEU   B 1 1661 ? 61.62500   38.17100  26.08900  1.000 114.10102 ?  1659 LEU   B O   1 
ATOM   26951 C  CB  . LEU   B 1 1661 ? 59.33600   39.14300  24.17800  1.000 104.31047 ?  1659 LEU   B CB  1 
ATOM   26952 C  CG  . LEU   B 1 1661 ? 60.67800   39.65200  23.62400  1.000 134.79571 ?  1659 LEU   B CG  1 
ATOM   26953 C  CD1 . LEU   B 1 1661 ? 60.62300   39.86700  22.18200  1.000 131.03830 ?  1659 LEU   B CD1 1 
ATOM   26954 C  CD2 . LEU   B 1 1661 ? 61.07300   40.92500  24.25100  1.000 131.76821 ?  1659 LEU   B CD2 1 
ATOM   26955 N  N   . CYS   B 1 1662 ? 60.37200   36.32500  25.78000  1.000 126.72607 ?  1660 CYS   B N   1 
ATOM   26956 C  CA  . CYS   B 1 1662 ? 61.46300   35.41400  26.09600  1.000 113.86625 ?  1660 CYS   B CA  1 
ATOM   26957 C  C   . CYS   B 1 1662 ? 61.38000   34.13200  25.27200  1.000 111.75202 ?  1660 CYS   B C   1 
ATOM   26958 O  O   . CYS   B 1 1662 ? 60.30200   33.57600  25.07300  1.000 106.88289 ?  1660 CYS   B O   1 
ATOM   26959 C  CB  . CYS   B 1 1662 ? 61.46000   35.08300  27.59200  1.000 107.74213 ?  1660 CYS   B CB  1 
ATOM   26960 S  SG  . CYS   B 1 1662 ? 62.67900   33.85300  28.08500  1.000 113.18369 ?  1660 CYS   B SG  1 
ATOM   26961 N  N   . GLY   B 1 1674 ? 74.55700   33.03700  26.39700  1.000 86.26047  ?  1672 GLY   B N   1 
ATOM   26962 C  CA  . GLY   B 1 1674 ? 74.32500   34.49100  26.29800  1.000 103.16621 ?  1672 GLY   B CA  1 
ATOM   26963 C  C   . GLY   B 1 1674 ? 74.78100   35.01800  24.95300  1.000 111.79141 ?  1672 GLY   B C   1 
ATOM   26964 O  O   . GLY   B 1 1674 ? 74.46300   36.17800  24.62700  1.000 104.65621 ?  1672 GLY   B O   1 
ATOM   26965 N  N   . GLN   B 1 1675 ? 75.49500   34.19000  24.19100  1.000 115.07141 ?  1673 GLN   B N   1 
ATOM   26966 C  CA  . GLN   B 1 1675 ? 75.94300   34.59600  22.83700  1.000 115.15141 ?  1673 GLN   B CA  1 
ATOM   26967 C  C   . GLN   B 1 1675 ? 74.70500   34.71300  21.94200  1.000 114.55892 ?  1673 GLN   B C   1 
ATOM   26968 O  O   . GLN   B 1 1675 ? 74.79900   35.35200  20.87600  1.000 120.17153 ?  1673 GLN   B O   1 
ATOM   26969 C  CB  . GLN   B 1 1675 ? 76.94600   33.58100  22.29400  1.000 105.95464 ?  1673 GLN   B CB  1 
ATOM   26970 C  CG  . GLN   B 1 1675 ? 78.33700   33.70300  22.90400  1.000 119.33391 ?  1673 GLN   B CG  1 
ATOM   26971 C  CD  . GLN   B 1 1675 ? 79.32000   32.69100  22.35600  1.000 163.80307 ?  1673 GLN   B CD  1 
ATOM   26972 O  OE1 . GLN   B 1 1675 ? 79.02600   31.95000  21.41200  1.000 152.88922 ?  1673 GLN   B OE1 1 
ATOM   26973 N  NE2 . GLN   B 1 1675 ? 80.50600   32.65100  22.94800  1.000 115.79591 ?  1673 GLN   B NE2 1 
ATOM   26974 N  N   . LEU   B 1 1676 ? 73.59700   34.10100  22.35700  1.000 106.16635 ?  1674 LEU   B N   1 
ATOM   26975 C  CA  . LEU   B 1 1676 ? 72.33700   34.25000  21.59200  1.000 116.31719 ?  1674 LEU   B CA  1 
ATOM   26976 C  C   . LEU   B 1 1676 ? 72.05100   35.74500  21.42300  1.000 123.18784 ?  1674 LEU   B C   1 
ATOM   26977 O  O   . LEU   B 1 1676 ? 71.89300   36.19500  20.27000  1.000 117.26008 ?  1674 LEU   B O   1 
ATOM   26978 C  CB  . LEU   B 1 1676 ? 71.22000   33.55800  22.36600  1.000 92.50119  ?  1674 LEU   B CB  1 
ATOM   26979 N  N   . ARG   B 1 1677 ? 71.98600   36.47600  22.53700  1.000 110.30614 ?  1675 ARG   B N   1 
ATOM   26980 C  CA  . ARG   B 1 1677 ? 71.66400   37.92100  22.47800  1.000 99.13571  ?  1675 ARG   B CA  1 
ATOM   26981 C  C   . ARG   B 1 1677 ? 72.43500   38.56100  21.31900  1.000 117.36567 ?  1675 ARG   B C   1 
ATOM   26982 O  O   . ARG   B 1 1677 ? 71.83800   39.36700  20.58400  1.000 123.60393 ?  1675 ARG   B O   1 
ATOM   26983 C  CB  . ARG   B 1 1677 ? 72.02100   38.58900  23.80600  1.000 86.12410  ?  1675 ARG   B CB  1 
ATOM   26984 N  N   . GLU   B 1 1678 ? 73.71300   38.21900  21.16800  1.000 123.99045 ?  1676 GLU   B N   1 
ATOM   26985 C  CA  . GLU   B 1 1678 ? 74.51000   38.84100  20.11400  1.000 120.83216 ?  1676 GLU   B CA  1 
ATOM   26986 C  C   . GLU   B 1 1678 ? 74.05700   38.39300  18.73100  1.000 126.83330 ?  1676 GLU   B C   1 
ATOM   26987 O  O   . GLU   B 1 1678 ? 73.99100   39.21000  17.80400  1.000 121.34370 ?  1676 GLU   B O   1 
ATOM   26988 C  CB  . GLU   B 1 1678 ? 75.99100   38.52400  20.31400  1.000 88.18841  ?  1676 GLU   B CB  1 
ATOM   26989 N  N   . LEU   B 1 1679 ? 73.75200   37.10000  18.57100  1.000 124.37264 ?  1677 LEU   B N   1 
ATOM   26990 C  CA  . LEU   B 1 1679 ? 73.37600   36.56500  17.26400  1.000 115.70701 ?  1677 LEU   B CA  1 
ATOM   26991 C  C   . LEU   B 1 1679 ? 72.17600   37.31000  16.69200  1.000 114.32563 ?  1677 LEU   B C   1 
ATOM   26992 O  O   . LEU   B 1 1679 ? 72.26900   37.95000  15.63800  1.000 115.05099 ?  1677 LEU   B O   1 
ATOM   26993 C  CB  . LEU   B 1 1679 ? 73.07100   35.06800  17.37600  1.000 103.03799 ?  1677 LEU   B CB  1 
ATOM   26994 C  CG  . LEU   B 1 1679 ? 73.00900   34.17200  16.12500  1.000 103.96141 ?  1677 LEU   B CG  1 
ATOM   26995 C  CD1 . LEU   B 1 1679 ? 71.88500   34.51300  15.12800  1.000 80.74969  ?  1677 LEU   B CD1 1 
ATOM   26996 C  CD2 . LEU   B 1 1679 ? 74.36100   34.14300  15.42400  1.000 93.63799  ?  1677 LEU   B CD2 1 
ATOM   26997 N  N   . LEU   B 1 1680 ? 71.02900   37.22500  17.37200  1.000 107.87016 ?  1678 LEU   B N   1 
ATOM   26998 C  CA  . LEU   B 1 1680 ? 69.80800   37.78500  16.80600  1.000 122.34569 ?  1678 LEU   B CA  1 
ATOM   26999 C  C   . LEU   B 1 1680 ? 69.84000   39.30900  16.77400  1.000 120.62016 ?  1678 LEU   B C   1 
ATOM   27000 O  O   . LEU   B 1 1680 ? 69.07100   39.91400  16.02200  1.000 122.78379 ?  1678 LEU   B O   1 
ATOM   27001 C  CB  . LEU   B 1 1680 ? 68.57700   37.27200  17.56900  1.000 116.85146 ?  1678 LEU   B CB  1 
ATOM   27002 C  CG  . LEU   B 1 1680 ? 68.02800   38.03200  18.78600  1.000 123.14461 ?  1678 LEU   B CG  1 
ATOM   27003 C  CD1 . LEU   B 1 1680 ? 66.65200   37.53700  19.20300  1.000 114.33363 ?  1678 LEU   B CD1 1 
ATOM   27004 C  CD2 . LEU   B 1 1680 ? 68.98200   37.94500  19.95400  1.000 120.46247 ?  1678 LEU   B CD2 1 
ATOM   27005 N  N   . ARG   B 1 1681 ? 70.73000   39.94100  17.54600  1.000 109.82229 ?  1679 ARG   B N   1 
ATOM   27006 C  CA  . ARG   B 1 1681 ? 70.94100   41.37700  17.41100  1.000 100.66655 ?  1679 ARG   B CA  1 
ATOM   27007 C  C   . ARG   B 1 1681 ? 71.53700   41.75100  16.05800  1.000 107.82122 ?  1679 ARG   B C   1 
ATOM   27008 O  O   . ARG   B 1 1681 ? 71.38100   42.89700  15.62400  1.000 116.07185 ?  1679 ARG   B O   1 
ATOM   27009 C  CB  . ARG   B 1 1681 ? 71.84500   41.88400  18.53600  1.000 95.29227  ?  1679 ARG   B CB  1 
ATOM   27010 N  N   . ARG   B 1 1682 ? 72.21300   40.81300  15.38200  1.000 109.68759 ?  1680 ARG   B N   1 
ATOM   27011 C  CA  . ARG   B 1 1682 ? 72.78400   41.05500  14.05800  1.000 103.14370 ?  1680 ARG   B CA  1 
ATOM   27012 C  C   . ARG   B 1 1682 ? 71.72400   41.21000  12.97800  1.000 119.64853 ?  1680 ARG   B C   1 
ATOM   27013 O  O   . ARG   B 1 1682 ? 72.07800   41.44400  11.81500  1.000 126.35048 ?  1680 ARG   B O   1 
ATOM   27014 C  CB  . ARG   B 1 1682 ? 73.74400   39.92300  13.67800  1.000 72.26991  ?  1680 ARG   B CB  1 
ATOM   27015 N  N   . GLU   B 1 1683 ? 70.44200   41.07400  13.33400  1.000 117.60340 ?  1681 GLU   B N   1 
ATOM   27016 C  CA  . GLU   B 1 1683 ? 69.36900   41.29200  12.35500  1.000 110.46417 ?  1681 GLU   B CA  1 
ATOM   27017 C  C   . GLU   B 1 1683 ? 68.02100   41.57500  13.00900  1.000 113.92859 ?  1681 GLU   B C   1 
ATOM   27018 O  O   . GLU   B 1 1683 ? 66.99500   41.31200  12.37300  1.000 115.84067 ?  1681 GLU   B O   1 
ATOM   27019 C  CB  . GLU   B 1 1683 ? 69.23900   40.07600  11.42800  1.000 104.70914 ?  1681 GLU   B CB  1 
ATOM   27020 C  CG  . GLU   B 1 1683 ? 69.66000   40.33600  9.99300   1.000 100.80021 ?  1681 GLU   B CG  1 
ATOM   27021 C  CD  . GLU   B 1 1683 ? 69.33300   39.16900  9.07700   1.000 101.92606 ?  1681 GLU   B CD  1 
ATOM   27022 O  OE1 . GLU   B 1 1683 ? 68.30200   38.49900  9.31000   1.000 101.90220 ?  1681 GLU   B OE1 1 
ATOM   27023 O  OE2 . GLU   B 1 1683 ? 70.10200   38.91700  8.12400   1.000 100.60722 -1 1681 GLU   B OE2 1 
ATOM   27024 N  N   . LEU   B 1 1684 ? 67.98000   42.09200  14.24500  1.000 117.63158 ?  1682 LEU   B N   1 
ATOM   27025 C  CA  . LEU   B 1 1684 ? 66.73900   42.35100  14.96900  1.000 114.94990 ?  1682 LEU   B CA  1 
ATOM   27026 C  C   . LEU   B 1 1684 ? 67.00600   43.43500  16.00000  1.000 115.02369 ?  1682 LEU   B C   1 
ATOM   27027 O  O   . LEU   B 1 1684 ? 68.09600   43.46100  16.59200  1.000 116.33872 ?  1682 LEU   B O   1 
ATOM   27028 C  CB  . LEU   B 1 1684 ? 66.18800   41.09900  15.66300  1.000 104.39260 ?  1682 LEU   B CB  1 
ATOM   27029 N  N   . PRO   B 1 1685 ? 66.05000   44.32500  16.23500  1.000 111.22993 ?  1683 PRO   B N   1 
ATOM   27030 C  CA  . PRO   B 1 1685 ? 66.25500   45.39400  17.22300  1.000 103.74000 ?  1683 PRO   B CA  1 
ATOM   27031 C  C   . PRO   B 1 1685 ? 66.26100   44.86900  18.65000  1.000 107.99249 ?  1683 PRO   B C   1 
ATOM   27032 O  O   . PRO   B 1 1685 ? 66.05500   43.67400  18.88300  1.000 116.43112 ?  1683 PRO   B O   1 
ATOM   27033 C  CB  . PRO   B 1 1685 ? 65.07000   46.33400  16.97100  1.000 97.73493  ?  1683 PRO   B CB  1 
ATOM   27034 C  CG  . PRO   B 1 1685 ? 64.01900   45.44700  16.38400  1.000 103.43720 ?  1683 PRO   B CG  1 
ATOM   27035 C  CD  . PRO   B 1 1685 ? 64.74200   44.42100  15.56700  1.000 111.34417 ?  1683 PRO   B CD  1 
ATOM   27036 N  N   . GLU   B 1 1686 ? 66.49100   45.76200  19.61600  1.000 99.15847  ?  1684 GLU   B N   1 
ATOM   27037 C  CA  . GLU   B 1 1686 ? 66.60200   45.33600  21.00700  1.000 98.11951  ?  1684 GLU   B CA  1 
ATOM   27038 C  C   . GLU   B 1 1686 ? 65.24300   44.96000  21.58200  1.000 97.63099  ?  1684 GLU   B C   1 
ATOM   27039 O  O   . GLU   B 1 1686 ? 65.13900   44.01600  22.37400  1.000 109.90111 ?  1684 GLU   B O   1 
ATOM   27040 C  CB  . GLU   B 1 1686 ? 67.25000   46.43800  21.84100  1.000 82.02739  ?  1684 GLU   B CB  1 
ATOM   27041 N  N   . TYR   B 1 1687 ? 64.19000   45.69300  21.20600  1.000 99.19685  ?  1685 TYR   B N   1 
ATOM   27042 C  CA  . TYR   B 1 1687 ? 62.85400   45.36200  21.69000  1.000 106.52504 ?  1685 TYR   B CA  1 
ATOM   27043 C  C   . TYR   B 1 1687 ? 62.43900   43.96800  21.23400  1.000 114.91411 ?  1685 TYR   B C   1 
ATOM   27044 O  O   . TYR   B 1 1687 ? 61.75300   43.24500  21.96600  1.000 108.20252 ?  1685 TYR   B O   1 
ATOM   27045 C  CB  . TYR   B 1 1687 ? 61.84400   46.40400  21.20900  1.000 80.63428  ?  1685 TYR   B CB  1 
ATOM   27046 N  N   . MET   B 1 1688 ? 62.85100   43.57100  20.02900  1.000 116.96216 ?  1686 MET   B N   1 
ATOM   27047 C  CA  . MET   B 1 1688 ? 62.53000   42.24100  19.53300  1.000 117.57723 ?  1686 MET   B CA  1 
ATOM   27048 C  C   . MET   B 1 1688 ? 63.42100   41.15800  20.12600  1.000 121.43533 ?  1686 MET   B C   1 
ATOM   27049 O  O   . MET   B 1 1688 ? 63.04600   39.98200  20.09600  1.000 122.84096 ?  1686 MET   B O   1 
ATOM   27050 C  CB  . MET   B 1 1688 ? 62.64600   42.18600  18.00900  1.000 105.19854 ?  1686 MET   B CB  1 
ATOM   27051 C  CG  . MET   B 1 1688 ? 61.57700   42.94600  17.24700  1.000 98.80572  ?  1686 MET   B CG  1 
ATOM   27052 S  SD  . MET   B 1 1688 ? 59.90200   42.26000  17.25400  1.000 108.53593 ?  1686 MET   B SD  1 
ATOM   27053 C  CE  . MET   B 1 1688 ? 60.13600   40.54100  17.71600  1.000 99.12119  ?  1686 MET   B CE  1 
ATOM   27054 N  N   . ILE   B 1 1689 ? 64.59200   41.52400  20.63900  1.000 123.26102 ?  1687 ILE   B N   1 
ATOM   27055 C  CA  . ILE   B 1 1689 ? 65.49500   40.55900  21.25800  1.000 123.38992 ?  1687 ILE   B CA  1 
ATOM   27056 C  C   . ILE   B 1 1689 ? 64.85300   40.10500  22.56300  1.000 124.51346 ?  1687 ILE   B C   1 
ATOM   27057 O  O   . ILE   B 1 1689 ? 64.17800   40.90700  23.22600  1.000 116.53220 ?  1687 ILE   B O   1 
ATOM   27058 C  CB  . ILE   B 1 1689 ? 66.88200   41.17300  21.48300  1.000 88.56928  ?  1687 ILE   B CB  1 
ATOM   27059 N  N   . PRO   B 1 1690 ? 65.02000   38.84900  22.96900  1.000 120.95068 ?  1688 PRO   B N   1 
ATOM   27060 C  CA  . PRO   B 1 1690 ? 64.33300   38.34200  24.16400  1.000 115.23651 ?  1688 PRO   B CA  1 
ATOM   27061 C  C   . PRO   B 1 1690 ? 65.06300   38.79000  25.42700  1.000 119.46637 ?  1688 PRO   B C   1 
ATOM   27062 O  O   . PRO   B 1 1690 ? 66.07300   39.48500  25.37400  1.000 113.80968 ?  1688 PRO   B O   1 
ATOM   27063 C  CB  . PRO   B 1 1690 ? 64.38700   36.82100  23.98800  1.000 105.23525 ?  1688 PRO   B CB  1 
ATOM   27064 C  CG  . PRO   B 1 1690 ? 65.30700   36.55900  22.79800  1.000 107.37918 ?  1688 PRO   B CG  1 
ATOM   27065 C  CD  . PRO   B 1 1690 ? 65.94800   37.85000  22.41300  1.000 111.89135 ?  1688 PRO   B CD  1 
ATOM   27066 N  N   . ALA   B 1 1691 ? 64.53800   38.36900  26.57400  1.000 119.32142 ?  1689 ALA   B N   1 
ATOM   27067 C  CA  . ALA   B 1 1691 ? 65.14200   38.72700  27.85500  1.000 105.97575 ?  1689 ALA   B CA  1 
ATOM   27068 C  C   . ALA   B 1 1691 ? 65.15500   37.54100  28.82100  1.000 97.75833  ?  1689 ALA   B C   1 
ATOM   27069 O  O   . ALA   B 1 1691 ? 64.43500   37.53400  29.81600  1.000 94.09072  ?  1689 ALA   B O   1 
ATOM   27070 C  CB  . ALA   B 1 1691 ? 64.41000   39.90700  28.47900  1.000 83.59572  ?  1689 ALA   B CB  1 
ATOM   27071 N  N   . TYR   B 1 1725 ? 84.41100   34.99200  32.13800  1.000 68.37444  ?  1723 TYR   B N   1 
ATOM   27072 C  CA  . TYR   B 1 1725 ? 85.65800   35.18300  31.40400  1.000 94.73817  ?  1723 TYR   B CA  1 
ATOM   27073 C  C   . TYR   B 1 1725 ? 86.21200   36.59300  31.60400  1.000 105.96993 ?  1723 TYR   B C   1 
ATOM   27074 O  O   . TYR   B 1 1725 ? 85.46100   37.56900  31.61400  1.000 105.44375 ?  1723 TYR   B O   1 
ATOM   27075 C  CB  . TYR   B 1 1725 ? 85.44700   34.89900  29.92400  1.000 76.69391  ?  1723 TYR   B CB  1 
ATOM   27076 N  N   . ALA   B 1 1726 ? 87.53300   36.69100  31.75700  1.000 103.82081 ?  1724 ALA   B N   1 
ATOM   27077 C  CA  . ALA   B 1 1726 ? 88.19400   37.97400  31.95800  1.000 104.52203 ?  1724 ALA   B CA  1 
ATOM   27078 C  C   . ALA   B 1 1726 ? 89.69100   37.85300  31.69900  1.000 106.81863 ?  1724 ALA   B C   1 
ATOM   27079 O  O   . ALA   B 1 1726 ? 90.48200   37.78500  32.64600  1.000 109.38914 ?  1724 ALA   B O   1 
ATOM   27080 C  CB  . ALA   B 1 1726 ? 87.94500   38.49200  33.37700  1.000 84.96335  ?  1724 ALA   B CB  1 
ATOM   27081 N  N   . ALA   B 1 1727 ? 90.09600   37.83100  30.42500  1.000 103.84933 ?  1725 ALA   B N   1 
ATOM   27082 C  CA  . ALA   B 1 1727 ? 91.50000   37.59700  30.12000  1.000 105.56000 ?  1725 ALA   B CA  1 
ATOM   27083 C  C   . ALA   B 1 1727 ? 91.87100   38.19500  28.77500  1.000 114.17700 ?  1725 ALA   B C   1 
ATOM   27084 O  O   . ALA   B 1 1727 ? 91.09000   38.07100  27.82100  1.000 118.78695 ?  1725 ALA   B O   1 
ATOM   27085 C  CB  . ALA   B 1 1727 ? 91.80900   36.09600  30.12400  1.000 100.83711 ?  1725 ALA   B CB  1 
ATOM   27086 N  N   . PRO   B 1 1728 ? 93.03900   38.84500  28.65700  1.000 112.71628 ?  1726 PRO   B N   1 
ATOM   27087 C  CA  . PRO   B 1 1728 ? 93.52200   39.27900  27.33900  1.000 102.75644 ?  1726 PRO   B CA  1 
ATOM   27088 C  C   . PRO   B 1 1728 ? 94.39800   38.22200  26.68000  1.000 103.81585 ?  1726 PRO   B C   1 
ATOM   27089 O  O   . PRO   B 1 1728 ? 94.48500   37.09100  27.17200  1.000 101.14888 ?  1726 PRO   B O   1 
ATOM   27090 C  CB  . PRO   B 1 1728 ? 94.32100   40.54200  27.66900  1.000 93.32854  ?  1726 PRO   B CB  1 
ATOM   27091 C  CG  . PRO   B 1 1728 ? 94.88200   40.25600  29.03200  1.000 96.41139  ?  1726 PRO   B CG  1 
ATOM   27092 C  CD  . PRO   B 1 1728 ? 93.88300   39.36400  29.74900  1.000 103.00526 ?  1726 PRO   B CD  1 
ATOM   27093 N  N   . ARG   B 1 1729 ? 95.06600   38.57300  25.58100  1.000 103.90987 ?  1727 ARG   B N   1 
ATOM   27094 C  CA  . ARG   B 1 1729 ? 95.88300   37.59200  24.87700  1.000 108.82102 ?  1727 ARG   B CA  1 
ATOM   27095 C  C   . ARG   B 1 1729 ? 97.08400   38.21700  24.17300  1.000 97.80061  ?  1727 ARG   B C   1 
ATOM   27096 O  O   . ARG   B 1 1729 ? 98.12300   37.56500  24.02000  1.000 96.57567  ?  1727 ARG   B O   1 
ATOM   27097 C  CB  . ARG   B 1 1729 ? 95.02900   36.82700  23.86500  1.000 90.35597  ?  1727 ARG   B CB  1 
ATOM   27098 N  N   . THR   B 1 1730 ? 96.95700   39.46400  23.72700  1.000 105.49735 ?  1728 THR   B N   1 
ATOM   27099 C  CA  . THR   B 1 1730 ? 98.03500   40.15200  23.03200  1.000 90.13556  ?  1728 THR   B CA  1 
ATOM   27100 C  C   . THR   B 1 1730 ? 98.22200   41.53800  23.63200  1.000 91.02486  ?  1728 THR   B C   1 
ATOM   27101 O  O   . THR   B 1 1730 ? 97.35300   42.05200  24.34100  1.000 88.31432  ?  1728 THR   B O   1 
ATOM   27102 C  CB  . THR   B 1 1730 ? 97.76200   40.26400  21.52500  1.000 66.83851  ?  1728 THR   B CB  1 
ATOM   27103 N  N   . GLU   B 1 1731 ? 99.38000   42.13600  23.33900  1.000 90.80431  ?  1729 GLU   B N   1 
ATOM   27104 C  CA  . GLU   B 1 1731 ? 99.67800   43.46800  23.85800  1.000 91.70457  ?  1729 GLU   B CA  1 
ATOM   27105 C  C   . GLU   B 1 1731 ? 98.62600   44.47700  23.42000  1.000 84.67560  ?  1729 GLU   B C   1 
ATOM   27106 O  O   . GLU   B 1 1731 ? 98.23800   45.36000  24.19500  1.000 72.28054  ?  1729 GLU   B O   1 
ATOM   27107 C  CB  . GLU   B 1 1731 ? 101.06600  43.91400  23.40100  1.000 87.74016  ?  1729 GLU   B CB  1 
ATOM   27108 C  CG  . GLU   B 1 1731 ? 102.16100  42.89300  23.64800  1.000 103.48439 ?  1729 GLU   B CG  1 
ATOM   27109 C  CD  . GLU   B 1 1731 ? 103.54500  43.51100  23.62000  1.000 117.55258 ?  1729 GLU   B CD  1 
ATOM   27110 O  OE1 . GLU   B 1 1731 ? 103.63900  44.75600  23.61100  1.000 110.12804 ?  1729 GLU   B OE1 1 
ATOM   27111 O  OE2 . GLU   B 1 1731 ? 104.53700  42.75200  23.60600  1.000 106.27957 -1 1729 GLU   B OE2 1 
ATOM   27112 N  N   . LEU   B 1 1732 ? 98.15600   44.36100  22.17600  1.000 84.04738  ?  1730 LEU   B N   1 
ATOM   27113 C  CA  . LEU   B 1 1732 ? 97.06800   45.21100  21.70900  1.000 86.69053  ?  1730 LEU   B CA  1 
ATOM   27114 C  C   . LEU   B 1 1732 ? 95.81500   44.99200  22.54800  1.000 87.97046  ?  1730 LEU   B C   1 
ATOM   27115 O  O   . LEU   B 1 1732 ? 95.17200   45.95100  22.98900  1.000 75.79422  ?  1730 LEU   B O   1 
ATOM   27116 C  CB  . LEU   B 1 1732 ? 96.79600   44.93300  20.23200  1.000 77.93938  ?  1730 LEU   B CB  1 
ATOM   27117 C  CG  . LEU   B 1 1732 ? 96.17500   46.03800  19.37800  1.000 70.89463  ?  1730 LEU   B CG  1 
ATOM   27118 C  CD1 . LEU   B 1 1732 ? 96.63000   47.40900  19.85200  1.000 49.62336  ?  1730 LEU   B CD1 1 
ATOM   27119 C  CD2 . LEU   B 1 1732 ? 96.57200   45.82000  17.92800  1.000 77.08930  ?  1730 LEU   B CD2 1 
ATOM   27120 N  N   . GLU   B 1 1733 ? 95.46500   43.72600  22.79400  1.000 97.75014  ?  1731 GLU   B N   1 
ATOM   27121 C  CA  . GLU   B 1 1733 ? 94.30600   43.42000  23.62700  1.000 86.27137  ?  1731 GLU   B CA  1 
ATOM   27122 C  C   . GLU   B 1 1733 ? 94.46900   43.97700  25.03600  1.000 78.97168  ?  1731 GLU   B C   1 
ATOM   27123 O  O   . GLU   B 1 1733 ? 93.52300   44.53700  25.60200  1.000 88.06185  ?  1731 GLU   B O   1 
ATOM   27124 C  CB  . GLU   B 1 1733 ? 94.07700   41.90900  23.67900  1.000 83.34755  ?  1731 GLU   B CB  1 
ATOM   27125 C  CG  . GLU   B 1 1733 ? 93.32900   41.33400  22.48500  1.000 89.41913  ?  1731 GLU   B CG  1 
ATOM   27126 C  CD  . GLU   B 1 1733 ? 94.24000   40.94600  21.33800  1.000 94.19965  ?  1731 GLU   B CD  1 
ATOM   27127 O  OE1 . GLU   B 1 1733 ? 95.00100   41.81100  20.85600  1.000 86.28064  ?  1731 GLU   B OE1 1 
ATOM   27128 O  OE2 . GLU   B 1 1733 ? 94.19600   39.76900  20.92100  1.000 99.84230  -1 1731 GLU   B OE2 1 
ATOM   27129 N  N   . ALA   B 1 1734 ? 95.66100   43.83000  25.62000  1.000 76.91755  ?  1732 ALA   B N   1 
ATOM   27130 C  CA  . ALA   B 1 1734 ? 95.88400   44.32800  26.97400  1.000 84.22242  ?  1732 ALA   B CA  1 
ATOM   27131 C  C   . ALA   B 1 1734 ? 95.82500   45.84900  27.02100  1.000 82.85837  ?  1732 ALA   B C   1 
ATOM   27132 O  O   . ALA   B 1 1734 ? 95.26900   46.42600  27.96400  1.000 74.32082  ?  1732 ALA   B O   1 
ATOM   27133 C  CB  . ALA   B 1 1734 ? 97.22600   43.82500  27.50500  1.000 71.48521  ?  1732 ALA   B CB  1 
ATOM   27134 N  N   . THR   B 1 1735 ? 96.39100   46.51700  26.01400  1.000 80.19617  ?  1733 THR   B N   1 
ATOM   27135 C  CA  . THR   B 1 1735 ? 96.35000   47.97500  25.98700  1.000 82.00859  ?  1733 THR   B CA  1 
ATOM   27136 C  C   . THR   B 1 1735 ? 94.94900   48.47800  25.66000  1.000 78.76224  ?  1733 THR   B C   1 
ATOM   27137 O  O   . THR   B 1 1735 ? 94.47800   49.45000  26.26400  1.000 74.90232  ?  1733 THR   B O   1 
ATOM   27138 C  CB  . THR   B 1 1735 ? 97.36500   48.51400  24.98000  1.000 75.45747  ?  1733 THR   B CB  1 
ATOM   27139 O  OG1 . THR   B 1 1735 ? 98.63000   47.87500  25.18800  1.000 74.70735  ?  1733 THR   B OG1 1 
ATOM   27140 C  CG2 . THR   B 1 1735 ? 97.53500   50.01600  25.15300  1.000 55.14841  ?  1733 THR   B CG2 1 
ATOM   27141 N  N   . LEU   B 1 1736 ? 94.27000   47.83100  24.70900  1.000 83.04757  ?  1734 LEU   B N   1 
ATOM   27142 C  CA  . LEU   B 1 1736 ? 92.88800   48.19400  24.40600  1.000 73.96016  ?  1734 LEU   B CA  1 
ATOM   27143 C  C   . LEU   B 1 1736 ? 92.00400   48.04600  25.63900  1.000 78.84560  ?  1734 LEU   B C   1 
ATOM   27144 O  O   . LEU   B 1 1736 ? 91.24900   48.95900  25.98800  1.000 77.62968  ?  1734 LEU   B O   1 
ATOM   27145 C  CB  . LEU   B 1 1736 ? 92.35500   47.33900  23.25400  1.000 61.13301  ?  1734 LEU   B CB  1 
ATOM   27146 C  CG  . LEU   B 1 1736 ? 92.81700   47.69700  21.83900  1.000 57.27070  ?  1734 LEU   B CG  1 
ATOM   27147 C  CD1 . LEU   B 1 1736 ? 92.38300   46.63100  20.84200  1.000 59.40500  ?  1734 LEU   B CD1 1 
ATOM   27148 C  CD2 . LEU   B 1 1736 ? 92.28700   49.06300  21.43100  1.000 54.24290  ?  1734 LEU   B CD2 1 
ATOM   27149 N  N   . ALA   B 1 1737 ? 92.09900   46.90200  26.32200  1.000 72.83769  ?  1735 ALA   B N   1 
ATOM   27150 C  CA  . ALA   B 1 1737 ? 91.30000   46.69200  27.52500  1.000 70.22824  ?  1735 ALA   B CA  1 
ATOM   27151 C  C   . ALA   B 1 1737 ? 91.62300   47.71700  28.60400  1.000 68.53695  ?  1735 ALA   B C   1 
ATOM   27152 O  O   . ALA   B 1 1737 ? 90.73600   48.11000  29.37000  1.000 69.85465  ?  1735 ALA   B O   1 
ATOM   27153 C  CB  . ALA   B 1 1737 ? 91.51100   45.27500  28.05800  1.000 57.35573  ?  1735 ALA   B CB  1 
ATOM   27154 N  N   . HIS   B 1 1738 ? 92.87900   48.16600  28.67900  1.000 58.96625  ?  1736 HIS   B N   1 
ATOM   27155 C  CA  . HIS   B 1 1738 ? 93.24300   49.15800  29.68500  1.000 74.66377  ?  1736 HIS   B CA  1 
ATOM   27156 C  C   . HIS   B 1 1738 ? 92.66100   50.52600  29.34800  1.000 77.57744  ?  1736 HIS   B C   1 
ATOM   27157 O  O   . HIS   B 1 1738 ? 92.16300   51.22900  30.23400  1.000 84.78872  ?  1736 HIS   B O   1 
ATOM   27158 C  CB  . HIS   B 1 1738 ? 94.76300   49.23700  29.82500  1.000 78.04217  ?  1736 HIS   B CB  1 
ATOM   27159 C  CG  . HIS   B 1 1738 ? 95.22100   50.12000  30.94500  1.000 94.94018  ?  1736 HIS   B CG  1 
ATOM   27160 N  ND1 . HIS   B 1 1738 ? 95.82900   51.33900  30.73200  1.000 100.85619 ?  1736 HIS   B ND1 1 
ATOM   27161 C  CD2 . HIS   B 1 1738 ? 95.15400   49.96300  32.28800  1.000 98.70505  ?  1736 HIS   B CD2 1 
ATOM   27162 C  CE1 . HIS   B 1 1738 ? 96.11900   51.89300  31.89600  1.000 93.89249  ?  1736 HIS   B CE1 1 
ATOM   27163 N  NE2 . HIS   B 1 1738 ? 95.72000   51.07800  32.85600  1.000 101.10905 ?  1736 HIS   B NE2 1 
ATOM   27164 N  N   . ILE   B 1 1739 ? 92.71600   50.92100  28.07400  1.000 68.44674  ?  1737 ILE   B N   1 
ATOM   27165 C  CA  . ILE   B 1 1739 ? 92.11700   52.18800  27.66600  1.000 76.01245  ?  1737 ILE   B CA  1 
ATOM   27166 C  C   . ILE   B 1 1739 ? 90.60000   52.12300  27.79800  1.000 78.06681  ?  1737 ILE   B C   1 
ATOM   27167 O  O   . ILE   B 1 1739 ? 89.96900   53.04200  28.33200  1.000 80.55100  ?  1737 ILE   B O   1 
ATOM   27168 C  CB  . ILE   B 1 1739 ? 92.54100   52.55100  26.23100  1.000 80.65580  ?  1737 ILE   B CB  1 
ATOM   27169 C  CG1 . ILE   B 1 1739 ? 94.06500   52.63000  26.11600  1.000 71.29343  ?  1737 ILE   B CG1 1 
ATOM   27170 C  CG2 . ILE   B 1 1739 ? 91.91600   53.87400  25.81500  1.000 85.46237  ?  1737 ILE   B CG2 1 
ATOM   27171 C  CD1 . ILE   B 1 1739 ? 94.66400   53.88500  26.71500  1.000 72.20568  ?  1737 ILE   B CD1 1 
ATOM   27172 N  N   . TRP   B 1 1740 ? 89.99400   51.03400  27.31100  1.000 77.06196  ?  1738 TRP   B N   1 
ATOM   27173 C  CA  . TRP   B 1 1740 ? 88.54700   50.87200  27.42800  1.000 65.66161  ?  1738 TRP   B CA  1 
ATOM   27174 C  C   . TRP   B 1 1740 ? 88.09900   50.95100  28.88100  1.000 76.04889  ?  1738 TRP   B C   1 
ATOM   27175 O  O   . TRP   B 1 1740 ? 87.06700   51.55700  29.18800  1.000 92.20336  ?  1738 TRP   B O   1 
ATOM   27176 C  CB  . TRP   B 1 1740 ? 88.10300   49.54100  26.82000  1.000 62.00693  ?  1738 TRP   B CB  1 
ATOM   27177 C  CG  . TRP   B 1 1740 ? 88.14700   49.47000  25.32200  1.000 79.81320  ?  1738 TRP   B CG  1 
ATOM   27178 C  CD1 . TRP   B 1 1740 ? 89.04900   50.06900  24.49100  1.000 86.19201  ?  1738 TRP   B CD1 1 
ATOM   27179 C  CD2 . TRP   B 1 1740 ? 87.23900   48.75400  24.47600  1.000 81.77464  ?  1738 TRP   B CD2 1 
ATOM   27180 N  NE1 . TRP   B 1 1740 ? 88.76300   49.76500  23.18200  1.000 91.18516  ?  1738 TRP   B NE1 1 
ATOM   27181 C  CE2 . TRP   B 1 1740 ? 87.65400   48.96100  23.14700  1.000 88.66188  ?  1738 TRP   B CE2 1 
ATOM   27182 C  CE3 . TRP   B 1 1740 ? 86.11400   47.95900  24.71600  1.000 79.67255  ?  1738 TRP   B CE3 1 
ATOM   27183 C  CZ2 . TRP   B 1 1740 ? 86.98600   48.40000  22.06100  1.000 88.96482  ?  1738 TRP   B CZ2 1 
ATOM   27184 C  CZ3 . TRP   B 1 1740 ? 85.45200   47.40400  23.63600  1.000 94.18723  ?  1738 TRP   B CZ3 1 
ATOM   27185 C  CH2 . TRP   B 1 1740 ? 85.89000   47.62700  22.32600  1.000 80.29581  ?  1738 TRP   B CH2 1 
ATOM   27186 N  N   . GLY   B 1 1741 ? 88.86300   50.34700  29.79100  1.000 73.75338  ?  1739 GLY   B N   1 
ATOM   27187 C  CA  . GLY   B 1 1741 ? 88.47600   50.36500  31.19100  1.000 82.44789  ?  1739 GLY   B CA  1 
ATOM   27188 C  C   . GLY   B 1 1741 ? 88.56800   51.74600  31.81200  1.000 84.63807  ?  1739 GLY   B C   1 
ATOM   27189 O  O   . GLY   B 1 1741 ? 87.68000   52.15800  32.56400  1.000 104.14626 ?  1739 GLY   B O   1 
ATOM   27190 N  N   . GLU   B 1 1742 ? 89.63900   52.48400  31.50400  1.000 80.18540  ?  1740 GLU   B N   1 
ATOM   27191 C  CA  . GLU   B 1 1742 ? 89.84600   53.78900  32.12500  1.000 89.51434  ?  1740 GLU   B CA  1 
ATOM   27192 C  C   . GLU   B 1 1742 ? 88.78200   54.79900  31.71300  1.000 96.33494  ?  1740 GLU   B C   1 
ATOM   27193 O  O   . GLU   B 1 1742 ? 88.43700   55.68600  32.50100  1.000 96.63450  ?  1740 GLU   B O   1 
ATOM   27194 C  CB  . GLU   B 1 1742 ? 91.23700   54.32200  31.78100  1.000 85.44166  ?  1740 GLU   B CB  1 
ATOM   27195 C  CG  . GLU   B 1 1742 ? 92.34500   53.80800  32.68200  1.000 93.14117  ?  1740 GLU   B CG  1 
ATOM   27196 C  CD  . GLU   B 1 1742 ? 93.10800   54.93100  33.35900  1.000 120.01935 ?  1740 GLU   B CD  1 
ATOM   27197 O  OE1 . GLU   B 1 1742 ? 92.50000   55.99000  33.62500  1.000 121.22876 ?  1740 GLU   B OE1 1 
ATOM   27198 O  OE2 . GLU   B 1 1742 ? 94.31800   54.75900  33.61700  1.000 117.78409 -1 1740 GLU   B OE2 1 
ATOM   27199 N  N   . VAL   B 1 1743 ? 88.25600   54.69100  30.49400  1.000 90.76984  ?  1741 VAL   B N   1 
ATOM   27200 C  CA  . VAL   B 1 1743 ? 87.24100   55.64200  30.05300  1.000 91.33827  ?  1741 VAL   B CA  1 
ATOM   27201 C  C   . VAL   B 1 1743 ? 85.85200   55.23600  30.53500  1.000 96.32447  ?  1741 VAL   B C   1 
ATOM   27202 O  O   . VAL   B 1 1743 ? 84.98300   56.09600  30.71700  1.000 106.43785 ?  1741 VAL   B O   1 
ATOM   27203 C  CB  . VAL   B 1 1743 ? 87.27400   55.79500  28.52300  1.000 85.60394  ?  1741 VAL   B CB  1 
ATOM   27204 C  CG1 . VAL   B 1 1743 ? 88.61600   56.34300  28.07500  1.000 82.37519  ?  1741 VAL   B CG1 1 
ATOM   27205 C  CG2 . VAL   B 1 1743 ? 86.98300   54.46600  27.85400  1.000 72.03396  ?  1741 VAL   B CG2 1 
ATOM   27206 N  N   . LEU   B 1 1744 ? 85.61900   53.94100  30.74800  1.000 89.50112  ?  1742 LEU   B N   1 
ATOM   27207 C  CA  . LEU   B 1 1744 ? 84.32400   53.45300  31.20100  1.000 79.20479  ?  1742 LEU   B CA  1 
ATOM   27208 C  C   . LEU   B 1 1744 ? 84.24900   53.25500  32.70900  1.000 95.31858  ?  1742 LEU   B C   1 
ATOM   27209 O  O   . LEU   B 1 1744 ? 83.14300   53.25700  33.26200  1.000 108.31109 ?  1742 LEU   B O   1 
ATOM   27210 C  CB  . LEU   B 1 1744 ? 83.98700   52.12800  30.50400  1.000 59.99362  ?  1742 LEU   B CB  1 
ATOM   27211 C  CG  . LEU   B 1 1744 ? 84.01000   52.18200  28.97300  1.000 81.43689  ?  1742 LEU   B CG  1 
ATOM   27212 C  CD1 . LEU   B 1 1744 ? 83.93700   50.79100  28.36700  1.000 82.56017  ?  1742 LEU   B CD1 1 
ATOM   27213 C  CD2 . LEU   B 1 1744 ? 82.88700   53.05400  28.44800  1.000 106.95855 ?  1742 LEU   B CD2 1 
ATOM   27214 N  N   . GLY   B 1 1745 ? 85.38700   53.09000  33.38200  1.000 99.49831  ?  1743 GLY   B N   1 
ATOM   27215 C  CA  . GLY   B 1 1745 ? 85.43400   52.87000  34.81000  1.000 91.78041  ?  1743 GLY   B CA  1 
ATOM   27216 C  C   . GLY   B 1 1745 ? 85.56100   51.41700  35.21900  1.000 109.92142 ?  1743 GLY   B C   1 
ATOM   27217 O  O   . GLY   B 1 1745 ? 86.03400   51.13900  36.32800  1.000 108.21400 ?  1743 GLY   B O   1 
ATOM   27218 N  N   . ILE   B 1 1746 ? 85.15500   50.48800  34.35200  1.000 102.94417 ?  1744 ILE   B N   1 
ATOM   27219 C  CA  . ILE   B 1 1746 ? 85.23100   49.06600  34.66000  1.000 100.76637 ?  1744 ILE   B CA  1 
ATOM   27220 C  C   . ILE   B 1 1746 ? 86.69000   48.63900  34.77400  1.000 107.53742 ?  1744 ILE   B C   1 
ATOM   27221 O  O   . ILE   B 1 1746 ? 87.55600   49.10500  34.02100  1.000 105.48440 ?  1744 ILE   B O   1 
ATOM   27222 C  CB  . ILE   B 1 1746 ? 84.47500   48.26300  33.58600  1.000 88.45300  ?  1744 ILE   B CB  1 
ATOM   27223 C  CG1 . ILE   B 1 1746 ? 84.82100   46.77200  33.65200  1.000 98.51539  ?  1744 ILE   B CG1 1 
ATOM   27224 C  CG2 . ILE   B 1 1746 ? 84.73300   48.85000  32.20500  1.000 94.63714  ?  1744 ILE   B CG2 1 
ATOM   27225 C  CD1 . ILE   B 1 1746 ? 84.26200   46.06300  34.87000  1.000 99.96612  ?  1744 ILE   B CD1 1 
ATOM   27226 N  N   . GLU   B 1 1747 ? 86.97000   47.75000  35.72900  1.000 107.95890 ?  1745 GLU   B N   1 
ATOM   27227 C  CA  . GLU   B 1 1747 ? 88.33200   47.37700  36.08500  1.000 96.11673  ?  1745 GLU   B CA  1 
ATOM   27228 C  C   . GLU   B 1 1747 ? 88.82900   46.11600  35.38400  1.000 100.61628 ?  1745 GLU   B C   1 
ATOM   27229 O  O   . GLU   B 1 1747 ? 90.02900   45.82900  35.44800  1.000 118.22226 ?  1745 GLU   B O   1 
ATOM   27230 C  CB  . GLU   B 1 1747 ? 88.43700   47.19000  37.60700  1.000 86.80809  ?  1745 GLU   B CB  1 
ATOM   27231 C  CG  . GLU   B 1 1747 ? 89.83800   47.36000  38.18800  1.000 118.01342 ?  1745 GLU   B CG  1 
ATOM   27232 C  CD  . GLU   B 1 1747 ? 90.21200   48.81400  38.42900  1.000 133.35477 ?  1745 GLU   B CD  1 
ATOM   27233 O  OE1 . GLU   B 1 1747 ? 89.54800   49.71000  37.86600  1.000 127.45925 ?  1745 GLU   B OE1 1 
ATOM   27234 O  OE2 . GLU   B 1 1747 ? 91.17100   49.06100  39.19000  1.000 126.24147 -1 1745 GLU   B OE2 1 
ATOM   27235 N  N   . ARG   B 1 1748 ? 87.95500   45.36200  34.71900  1.000 86.93944  ?  1746 ARG   B N   1 
ATOM   27236 C  CA  . ARG   B 1 1748 ? 88.36900   44.12800  34.06000  1.000 94.73488  ?  1746 ARG   B CA  1 
ATOM   27237 C  C   . ARG   B 1 1748 ? 87.54200   43.92200  32.79900  1.000 99.48049  ?  1746 ARG   B C   1 
ATOM   27238 O  O   . ARG   B 1 1748 ? 86.31100   43.99900  32.84500  1.000 115.69850 ?  1746 ARG   B O   1 
ATOM   27239 C  CB  . ARG   B 1 1748 ? 88.22100   42.92500  34.99700  1.000 87.87210  ?  1746 ARG   B CB  1 
ATOM   27240 N  N   . ILE   B 1 1749 ? 88.22100   43.65300  31.68400  1.000 77.82259  ?  1747 ILE   B N   1 
ATOM   27241 C  CA  . ILE   B 1 1749 ? 87.58300   43.50900  30.38300  1.000 97.90574  ?  1747 ILE   B CA  1 
ATOM   27242 C  C   . ILE   B 1 1749 ? 87.92800   42.13300  29.81400  1.000 91.01736  ?  1747 ILE   B C   1 
ATOM   27243 O  O   . ILE   B 1 1749 ? 88.78200   41.41300  30.33300  1.000 89.29916  ?  1747 ILE   B O   1 
ATOM   27244 C  CB  . ILE   B 1 1749 ? 87.99900   44.62700  29.40200  1.000 105.03519 ?  1747 ILE   B CB  1 
ATOM   27245 C  CG1 . ILE   B 1 1749 ? 88.18700   45.95100  30.14100  1.000 112.14535 ?  1747 ILE   B CG1 1 
ATOM   27246 C  CG2 . ILE   B 1 1749 ? 86.94900   44.82200  28.31000  1.000 80.24883  ?  1747 ILE   B CG2 1 
ATOM   27247 C  CD1 . ILE   B 1 1749 ? 86.89600   46.55700  30.62800  1.000 96.99090  ?  1747 ILE   B CD1 1 
ATOM   27248 N  N   . GLY   B 1 1750 ? 87.23200   41.77200  28.73100  1.000 74.98792  ?  1748 GLY   B N   1 
ATOM   27249 C  CA  . GLY   B 1 1750 ? 87.54300   40.57000  27.98900  1.000 79.18473  ?  1748 GLY   B CA  1 
ATOM   27250 C  C   . GLY   B 1 1750 ? 87.54800   40.85800  26.50100  1.000 89.15018  ?  1748 GLY   B C   1 
ATOM   27251 O  O   . GLY   B 1 1750 ? 87.07900   41.90400  26.04900  1.000 89.87558  ?  1748 GLY   B O   1 
ATOM   27252 N  N   . ILE   B 1 1751 ? 88.09000   39.90300  25.74200  1.000 80.40504  ?  1749 ILE   B N   1 
ATOM   27253 C  CA  . ILE   B 1 1751 ? 88.20000   40.07400  24.29500  1.000 90.67359  ?  1749 ILE   B CA  1 
ATOM   27254 C  C   . ILE   B 1 1751 ? 86.81800   40.13300  23.65500  1.000 101.59075 ?  1749 ILE   B C   1 
ATOM   27255 O  O   . ILE   B 1 1751 ? 86.48700   41.08500  22.93800  1.000 101.61610 ?  1749 ILE   B O   1 
ATOM   27256 C  CB  . ILE   B 1 1751 ? 89.05800   38.95300  23.67900  1.000 103.37315 ?  1749 ILE   B CB  1 
ATOM   27257 C  CG1 . ILE   B 1 1751 ? 89.32800   37.84400  24.70200  1.000 118.98461 ?  1749 ILE   B CG1 1 
ATOM   27258 C  CG2 . ILE   B 1 1751 ? 90.35700   39.51400  23.13400  1.000 98.76339  ?  1749 ILE   B CG2 1 
ATOM   27259 C  CD1 . ILE   B 1 1751 ? 88.26700   36.76300  24.73600  1.000 114.93826 ?  1749 ILE   B CD1 1 
ATOM   27260 N  N   . ARG   B 1 1752 ? 85.99100   39.11800  23.90300  1.000 115.02503 ?  1750 ARG   B N   1 
ATOM   27261 C  CA  . ARG   B 1 1752 ? 84.66900   39.03600  23.29300  1.000 112.75063 ?  1750 ARG   B CA  1 
ATOM   27262 C  C   . ARG   B 1 1752 ? 83.62300   39.88100  24.00800  1.000 114.36046 ?  1750 ARG   B C   1 
ATOM   27263 O  O   . ARG   B 1 1752 ? 82.44400   39.80600  23.64800  1.000 106.87476 ?  1750 ARG   B O   1 
ATOM   27264 C  CB  . ARG   B 1 1752 ? 84.20500   37.57700  23.24100  1.000 99.33427  ?  1750 ARG   B CB  1 
ATOM   27265 N  N   . ASP   B 1 1753 ? 84.01400   40.67200  25.00400  1.000 108.28303 ?  1751 ASP   B N   1 
ATOM   27266 C  CA  . ASP   B 1 1753 ? 83.06900   41.57300  25.64600  1.000 91.72055  ?  1751 ASP   B CA  1 
ATOM   27267 C  C   . ASP   B 1 1753 ? 82.72800   42.73000  24.71400  1.000 88.90255  ?  1751 ASP   B C   1 
ATOM   27268 O  O   . ASP   B 1 1753 ? 83.55900   43.19300  23.92800  1.000 89.19592  ?  1751 ASP   B O   1 
ATOM   27269 C  CB  . ASP   B 1 1753 ? 83.64000   42.10400  26.96100  1.000 80.47761  ?  1751 ASP   B CB  1 
ATOM   27270 C  CG  . ASP   B 1 1753 ? 84.03700   40.99400  27.91300  1.000 81.27082  ?  1751 ASP   B CG  1 
ATOM   27271 O  OD1 . ASP   B 1 1753 ? 84.05100   39.82000  27.48400  1.000 70.62557  ?  1751 ASP   B OD1 1 
ATOM   27272 O  OD2 . ASP   B 1 1753 ? 84.33200   41.29300  29.08900  1.000 92.19901  -1 1751 ASP   B OD2 1 
ATOM   27273 N  N   . ASN   B 1 1754 ? 81.48500   43.19500  24.80600  1.000 104.11478 ?  1752 ASN   B N   1 
ATOM   27274 C  CA  . ASN   B 1 1754 ? 81.00200   44.24200  23.92000  1.000 120.31166 ?  1752 ASN   B CA  1 
ATOM   27275 C  C   . ASN   B 1 1754 ? 81.46400   45.61100  24.41900  1.000 116.39588 ?  1752 ASN   B C   1 
ATOM   27276 O  O   . ASN   B 1 1754 ? 82.10900   45.73900  25.46300  1.000 106.26832 ?  1752 ASN   B O   1 
ATOM   27277 C  CB  . ASN   B 1 1754 ? 79.48100   44.17200  23.80500  1.000 102.90460 ?  1752 ASN   B CB  1 
ATOM   27278 C  CG  . ASN   B 1 1754 ? 78.97200   44.70800  22.48100  1.000 114.69855 ?  1752 ASN   B CG  1 
ATOM   27279 O  OD1 . ASN   B 1 1754 ? 78.50300   45.84300  22.39500  1.000 111.06990 ?  1752 ASN   B OD1 1 
ATOM   27280 N  ND2 . ASN   B 1 1754 ? 79.06700   43.89100  21.43800  1.000 113.19558 ?  1752 ASN   B ND2 1 
ATOM   27281 N  N   . PHE   B 1 1755 ? 81.13200   46.65400  23.65700  1.000 109.81651 ?  1753 PHE   B N   1 
ATOM   27282 C  CA  . PHE   B 1 1755 ? 81.51000   48.01100  24.03100  1.000 108.18619 ?  1753 PHE   B CA  1 
ATOM   27283 C  C   . PHE   B 1 1755 ? 80.34900   48.74600  24.68800  1.000 118.90153 ?  1753 PHE   B C   1 
ATOM   27284 O  O   . PHE   B 1 1755 ? 80.32500   48.89900  25.91300  1.000 114.21175 ?  1753 PHE   B O   1 
ATOM   27285 C  CB  . PHE   B 1 1755 ? 82.01200   48.79100  22.81300  1.000 97.98072  ?  1753 PHE   B CB  1 
ATOM   27286 C  CG  . PHE   B 1 1755 ? 82.29100   50.24000  23.09700  1.000 108.05345 ?  1753 PHE   B CG  1 
ATOM   27287 C  CD1 . PHE   B 1 1755 ? 83.10200   50.60800  24.15900  1.000 104.75238 ?  1753 PHE   B CD1 1 
ATOM   27288 C  CD2 . PHE   B 1 1755 ? 81.74800   51.23400  22.30100  1.000 99.42707  ?  1753 PHE   B CD2 1 
ATOM   27289 C  CE1 . PHE   B 1 1755 ? 83.35900   51.94000  24.42500  1.000 95.57105  ?  1753 PHE   B CE1 1 
ATOM   27290 C  CE2 . PHE   B 1 1755 ? 82.00200   52.56800  22.56100  1.000 98.23147  ?  1753 PHE   B CE2 1 
ATOM   27291 C  CZ  . PHE   B 1 1755 ? 82.80900   52.92100  23.62300  1.000 93.39543  ?  1753 PHE   B CZ  1 
ATOM   27292 N  N   . PHE   B 1 1756 ? 79.38400   49.20800  23.88500  1.000 118.66006 ?  1754 PHE   B N   1 
ATOM   27293 C  CA  . PHE   B 1 1756 ? 78.25500   49.95100  24.43900  1.000 112.08347 ?  1754 PHE   B CA  1 
ATOM   27294 C  C   . PHE   B 1 1756 ? 77.47600   49.11800  25.44700  1.000 112.03169 ?  1754 PHE   B C   1 
ATOM   27295 O  O   . PHE   B 1 1756 ? 76.93900   49.66400  26.41900  1.000 108.08256 ?  1754 PHE   B O   1 
ATOM   27296 C  CB  . PHE   B 1 1756 ? 77.32200   50.42700  23.32300  1.000 100.15731 ?  1754 PHE   B CB  1 
ATOM   27297 C  CG  . PHE   B 1 1756 ? 77.81100   50.10900  21.93900  1.000 97.18943  ?  1754 PHE   B CG  1 
ATOM   27298 C  CD1 . PHE   B 1 1756 ? 77.53400   48.88300  21.35600  1.000 87.51317  ?  1754 PHE   B CD1 1 
ATOM   27299 C  CD2 . PHE   B 1 1756 ? 78.53300   51.04300  21.21500  1.000 114.75038 ?  1754 PHE   B CD2 1 
ATOM   27300 C  CE1 . PHE   B 1 1756 ? 77.97800   48.59000  20.08200  1.000 103.86020 ?  1754 PHE   B CE1 1 
ATOM   27301 C  CE2 . PHE   B 1 1756 ? 78.98000   50.75600  19.93800  1.000 112.19612 ?  1754 PHE   B CE2 1 
ATOM   27302 C  CZ  . PHE   B 1 1756 ? 78.70200   49.52800  19.37100  1.000 102.71416 ?  1754 PHE   B CZ  1 
ATOM   27303 N  N   . GLU   B 1 1757 ? 77.40100   47.80200  25.23700  1.000 106.32269 ?  1755 GLU   B N   1 
ATOM   27304 C  CA  . GLU   B 1 1757 ? 76.74000   46.93700  26.20600  1.000 108.12380 ?  1755 GLU   B CA  1 
ATOM   27305 C  C   . GLU   B 1 1757 ? 77.49500   46.91300  27.53000  1.000 106.14718 ?  1755 GLU   B C   1 
ATOM   27306 O  O   . GLU   B 1 1757 ? 76.87600   46.79900  28.59500  1.000 83.18052  ?  1755 GLU   B O   1 
ATOM   27307 C  CB  . GLU   B 1 1757 ? 76.60100   45.52600  25.63500  1.000 102.30377 ?  1755 GLU   B CB  1 
ATOM   27308 C  CG  . GLU   B 1 1757 ? 75.49600   44.70000  26.26800  1.000 93.04318  ?  1755 GLU   B CG  1 
ATOM   27309 C  CD  . GLU   B 1 1757 ? 75.32100   43.35600  25.58900  1.000 87.37855  ?  1755 GLU   B CD  1 
ATOM   27310 O  OE1 . GLU   B 1 1757 ? 76.07700   43.06800  24.63700  1.000 83.44147  ?  1755 GLU   B OE1 1 
ATOM   27311 O  OE2 . GLU   B 1 1757 ? 74.42800   42.58800  26.00600  1.000 82.61648  -1 1755 GLU   B OE2 1 
ATOM   27312 N  N   . LEU   B 1 1758 ? 78.82200   47.02400  27.48400  1.000 110.00984 ?  1756 LEU   B N   1 
ATOM   27313 C  CA  . LEU   B 1 1758 ? 79.65100   47.21200  28.66800  1.000 103.77895 ?  1756 LEU   B CA  1 
ATOM   27314 C  C   . LEU   B 1 1758 ? 79.56400   48.63600  29.21300  1.000 97.39254  ?  1756 LEU   B C   1 
ATOM   27315 O  O   . LEU   B 1 1758 ? 80.27500   48.97700  30.16400  1.000 85.10476  ?  1756 LEU   B O   1 
ATOM   27316 C  CB  . LEU   B 1 1758 ? 81.10700   46.85600  28.34200  1.000 92.31424  ?  1756 LEU   B CB  1 
ATOM   27317 C  CG  . LEU   B 1 1758 ? 82.13400   46.64200  29.46100  1.000 101.66429 ?  1756 LEU   B CG  1 
ATOM   27318 C  CD1 . LEU   B 1 1758 ? 82.33600   45.16300  29.74800  1.000 102.90075 ?  1756 LEU   B CD1 1 
ATOM   27319 C  CD2 . LEU   B 1 1758 ? 83.45600   47.30500  29.11000  1.000 102.28324 ?  1756 LEU   B CD2 1 
ATOM   27320 N  N   . GLY   B 1 1759 ? 78.70100   49.46600  28.64000  1.000 92.43710  ?  1757 GLY   B N   1 
ATOM   27321 C  CA  . GLY   B 1 1759 ? 78.61900   50.86500  28.99200  1.000 103.26213 ?  1757 GLY   B CA  1 
ATOM   27322 C  C   . GLY   B 1 1759 ? 79.41700   51.73800  28.03900  1.000 114.58041 ?  1757 GLY   B C   1 
ATOM   27323 O  O   . GLY   B 1 1759 ? 80.35300   51.29400  27.37200  1.000 121.36082 ?  1757 GLY   B O   1 
ATOM   27324 N  N   . GLY   B 1 1760 ? 79.03000   53.00000  27.97200  1.000 101.88213 ?  1758 GLY   B N   1 
ATOM   27325 C  CA  . GLY   B 1 1760 ? 79.70100   53.93700  27.10000  1.000 93.08067  ?  1758 GLY   B CA  1 
ATOM   27326 C  C   . GLY   B 1 1760 ? 78.85800   54.28500  25.88200  1.000 107.14142 ?  1758 GLY   B C   1 
ATOM   27327 O  O   . GLY   B 1 1760 ? 77.89000   53.60200  25.53400  1.000 108.48985 ?  1758 GLY   B O   1 
ATOM   27328 N  N   . ASP   B 1 1761 ? 79.25300   55.37200  25.22300  1.000 110.95302 ?  1759 ASP   B N   1 
ATOM   27329 C  CA  . ASP   B 1 1761 ? 78.51400   55.88300  24.07900  1.000 100.29941 ?  1759 ASP   B CA  1 
ATOM   27330 C  C   . ASP   B 1 1761 ? 79.44400   56.14800  22.90100  1.000 93.43815  ?  1759 ASP   B C   1 
ATOM   27331 O  O   . ASP   B 1 1761 ? 80.39300   55.39000  22.66600  1.000 91.39532  ?  1759 ASP   B O   1 
ATOM   27332 C  CB  . ASP   B 1 1761 ? 77.76500   57.15400  24.47400  1.000 95.06972  ?  1759 ASP   B CB  1 
ATOM   27333 C  CG  . ASP   B 1 1761 ? 78.58100   58.04900  25.38400  1.000 100.86897 ?  1759 ASP   B CG  1 
ATOM   27334 O  OD1 . ASP   B 1 1761 ? 78.90800   57.61500  26.50900  1.000 112.75141 ?  1759 ASP   B OD1 1 
ATOM   27335 O  OD2 . ASP   B 1 1761 ? 78.90800   59.18400  24.96000  1.000 113.48989 -1 1759 ASP   B OD2 1 
ATOM   27336 N  N   . SER   B 1 1762 ? 79.17900   57.21900  22.15200  1.000 98.42417  ?  1760 SER   B N   1 
ATOM   27337 C  CA  . SER   B 1 1762 ? 80.02300   57.57400  21.01900  1.000 95.66404  ?  1760 SER   B CA  1 
ATOM   27338 C  C   . SER   B 1 1762 ? 81.15200   58.52000  21.40500  1.000 94.07233  ?  1760 SER   B C   1 
ATOM   27339 O  O   . SER   B 1 1762 ? 82.21800   58.48000  20.77900  1.000 100.72382 ?  1760 SER   B O   1 
ATOM   27340 C  CB  . SER   B 1 1762 ? 79.17900   58.20400  19.90700  1.000 100.06082 ?  1760 SER   B CB  1 
ATOM   27341 O  OG  . SER   B 1 1762 ? 77.80000   57.92900  20.08300  1.000 82.81319  ?  1760 SER   B OG  1 
ATOM   27342 N  N   . ILE   B 1 1763 ? 80.95300   59.36800  22.42100  1.000 83.95738  ?  1761 ILE   B N   1 
ATOM   27343 C  CA  . ILE   B 1 1763 ? 82.05000   60.20800  22.89700  1.000 85.94670  ?  1761 ILE   B CA  1 
ATOM   27344 C  C   . ILE   B 1 1763 ? 83.17700   59.34600  23.44800  1.000 83.28395  ?  1761 ILE   B C   1 
ATOM   27345 O  O   . ILE   B 1 1763 ? 84.35200   59.72900  23.38100  1.000 83.25368  ?  1761 ILE   B O   1 
ATOM   27346 C  CB  . ILE   B 1 1763 ? 81.55100   61.22000  23.95000  1.000 77.82933  ?  1761 ILE   B CB  1 
ATOM   27347 C  CG1 . ILE   B 1 1763 ? 81.59200   60.60900  25.35500  1.000 89.11445  ?  1761 ILE   B CG1 1 
ATOM   27348 C  CG2 . ILE   B 1 1763 ? 80.15200   61.71200  23.61100  1.000 88.30717  ?  1761 ILE   B CG2 1 
ATOM   27349 C  CD1 . ILE   B 1 1763 ? 81.13300   61.54300  26.44900  1.000 81.65282  ?  1761 ILE   B CD1 1 
ATOM   27350 N  N   . LYS   B 1 1764 ? 82.84600   58.16600  23.98200  1.000 81.02331  ?  1762 LYS   B N   1 
ATOM   27351 C  CA  . LYS   B 1 1764 ? 83.87100   57.27300  24.51200  1.000 84.41058  ?  1762 LYS   B CA  1 
ATOM   27352 C  C   . LYS   B 1 1764 ? 84.81300   56.80600  23.41000  1.000 73.65901  ?  1762 LYS   B C   1 
ATOM   27353 O  O   . LYS   B 1 1764 ? 86.03800   56.87300  23.55800  1.000 73.42373  ?  1762 LYS   B O   1 
ATOM   27354 C  CB  . LYS   B 1 1764 ? 83.21200   56.08200  25.20500  1.000 93.61864  ?  1762 LYS   B CB  1 
ATOM   27355 C  CG  . LYS   B 1 1764 ? 82.36000   56.46800  26.40000  1.000 92.47807  ?  1762 LYS   B CG  1 
ATOM   27356 C  CD  . LYS   B 1 1764 ? 83.22100   56.77900  27.61100  1.000 109.46277 ?  1762 LYS   B CD  1 
ATOM   27357 C  CE  . LYS   B 1 1764 ? 82.51400   57.72600  28.56300  1.000 96.33311  ?  1762 LYS   B CE  1 
ATOM   27358 N  NZ  . LYS   B 1 1764 ? 81.05500   57.79800  28.29500  1.000 99.70898  ?  1762 LYS   B NZ  1 
ATOM   27359 N  N   . GLY   B 1 1765 ? 84.25500   56.33300  22.29100  1.000 81.33549  ?  1763 GLY   B N   1 
ATOM   27360 C  CA  . GLY   B 1 1765 ? 85.08500   55.92500  21.16800  1.000 84.42997  ?  1763 GLY   B CA  1 
ATOM   27361 C  C   . GLY   B 1 1765 ? 86.02100   57.01600  20.68800  1.000 88.50823  ?  1763 GLY   B C   1 
ATOM   27362 O  O   . GLY   B 1 1765 ? 87.13000   56.73100  20.22900  1.000 88.63099  ?  1763 GLY   B O   1 
ATOM   27363 N  N   . LEU   B 1 1766 ? 85.59400   58.27700  20.79000  1.000 86.39537  ?  1764 LEU   B N   1 
ATOM   27364 C  CA  . LEU   B 1 1766 ? 86.49400   59.38200  20.47800  1.000 90.31246  ?  1764 LEU   B CA  1 
ATOM   27365 C  C   . LEU   B 1 1766 ? 87.54900   59.55000  21.56600  1.000 88.54468  ?  1764 LEU   B C   1 
ATOM   27366 O  O   . LEU   B 1 1766 ? 88.72500   59.78600  21.26600  1.000 88.50109  ?  1764 LEU   B O   1 
ATOM   27367 C  CB  . LEU   B 1 1766 ? 85.69300   60.67000  20.28900  1.000 78.38208  ?  1764 LEU   B CB  1 
ATOM   27368 C  CG  . LEU   B 1 1766 ? 86.41800   61.84300  19.62900  1.000 64.48526  ?  1764 LEU   B CG  1 
ATOM   27369 C  CD1 . LEU   B 1 1766 ? 87.23900   61.37300  18.44100  1.000 68.56749  ?  1764 LEU   B CD1 1 
ATOM   27370 C  CD2 . LEU   B 1 1766 ? 85.42500   62.91000  19.19800  1.000 61.95629  ?  1764 LEU   B CD2 1 
ATOM   27371 N  N   . GLN   B 1 1767 ? 87.14800   59.42300  22.83500  1.000 75.60148  ?  1765 GLN   B N   1 
ATOM   27372 C  CA  . GLN   B 1 1767 ? 88.11500   59.48500  23.92600  1.000 74.26511  ?  1765 GLN   B CA  1 
ATOM   27373 C  C   . GLN   B 1 1767 ? 89.09700   58.32300  23.85800  1.000 78.34124  ?  1765 GLN   B C   1 
ATOM   27374 O  O   . GLN   B 1 1767 ? 90.29600   58.49800  24.10800  1.000 80.13558  ?  1765 GLN   B O   1 
ATOM   27375 C  CB  . GLN   B 1 1767 ? 87.39400   59.49000  25.27400  1.000 65.28671  ?  1765 GLN   B CB  1 
ATOM   27376 C  CG  . GLN   B 1 1767 ? 86.60800   60.75500  25.56700  1.000 85.36451  ?  1765 GLN   B CG  1 
ATOM   27377 C  CD  . GLN   B 1 1767 ? 85.82500   60.66500  26.86400  1.000 90.37882  ?  1765 GLN   B CD  1 
ATOM   27378 O  OE1 . GLN   B 1 1767 ? 85.60000   59.57500  27.39300  1.000 97.31819  ?  1765 GLN   B OE1 1 
ATOM   27379 N  NE2 . GLN   B 1 1767 ? 85.40800   61.81300  27.38500  1.000 72.96074  ?  1765 GLN   B NE2 1 
ATOM   27380 N  N   . ILE   B 1 1768 ? 88.60700   57.12500  23.52800  1.000 68.81455  ?  1766 ILE   B N   1 
ATOM   27381 C  CA  . ILE   B 1 1768 ? 89.49000   55.96600  23.42900  1.000 66.12578  ?  1766 ILE   B CA  1 
ATOM   27382 C  C   . ILE   B 1 1768 ? 90.47900   56.15300  22.28700  1.000 72.01968  ?  1766 ILE   B C   1 
ATOM   27383 O  O   . ILE   B 1 1768 ? 91.69400   56.01200  22.46400  1.000 75.42052  ?  1766 ILE   B O   1 
ATOM   27384 C  CB  . ILE   B 1 1768 ? 88.67200   54.67300  23.25800  1.000 63.50528  ?  1766 ILE   B CB  1 
ATOM   27385 C  CG1 . ILE   B 1 1768 ? 87.75300   54.45800  24.45600  1.000 64.36353  ?  1766 ILE   B CG1 1 
ATOM   27386 C  CG2 . ILE   B 1 1768 ? 89.59500   53.48100  23.12500  1.000 68.92837  ?  1766 ILE   B CG2 1 
ATOM   27387 C  CD1 . ILE   B 1 1768 ? 86.85100   53.25100  24.32600  1.000 65.70412  ?  1766 ILE   B CD1 1 
ATOM   27388 N  N   . ALA   B 1 1769 ? 89.97000   56.48200  21.09600  1.000 61.51108  ?  1767 ALA   B N   1 
ATOM   27389 C  CA  . ALA   B 1 1769 ? 90.84400   56.68600  19.94600  1.000 66.57739  ?  1767 ALA   B CA  1 
ATOM   27390 C  C   . ALA   B 1 1769 ? 91.84600   57.80700  20.19100  1.000 72.06517  ?  1767 ALA   B C   1 
ATOM   27391 O  O   . ALA   B 1 1769 ? 92.96600   57.76300  19.66900  1.000 57.75037  ?  1767 ALA   B O   1 
ATOM   27392 C  CB  . ALA   B 1 1769 ? 90.01000   56.97900  18.69900  1.000 59.67705  ?  1767 ALA   B CB  1 
ATOM   27393 N  N   . SER   B 1 1770 ? 91.46500   58.81300  20.98200  1.000 70.48048  ?  1768 SER   B N   1 
ATOM   27394 C  CA  . SER   B 1 1770 ? 92.39600   59.88400  21.32500  1.000 65.57214  ?  1768 SER   B CA  1 
ATOM   27395 C  C   . SER   B 1 1770 ? 93.44700   59.39900  22.31400  1.000 78.81540  ?  1768 SER   B C   1 
ATOM   27396 O  O   . SER   B 1 1770 ? 94.64300   59.66500  22.14800  1.000 90.53921  ?  1768 SER   B O   1 
ATOM   27397 C  CB  . SER   B 1 1770 ? 91.63400   61.08100  21.89500  1.000 71.27560  ?  1768 SER   B CB  1 
ATOM   27398 O  OG  . SER   B 1 1770 ? 92.51000   61.96600  22.57300  1.000 81.22264  ?  1768 SER   B OG  1 
ATOM   27399 N  N   . ARG   B 1 1771 ? 93.02200   58.68900  23.35900  1.000 73.32317  ?  1769 ARG   B N   1 
ATOM   27400 C  CA  . ARG   B 1 1771 ? 93.98200   58.10700  24.28500  1.000 64.40421  ?  1769 ARG   B CA  1 
ATOM   27401 C  C   . ARG   B 1 1771 ? 94.82300   57.01800  23.63500  1.000 64.58658  ?  1769 ARG   B C   1 
ATOM   27402 O  O   . ARG   B 1 1771 ? 95.84400   56.62000  24.20700  1.000 70.00724  ?  1769 ARG   B O   1 
ATOM   27403 C  CB  . ARG   B 1 1771 ? 93.25400   57.55600  25.51000  1.000 67.18874  ?  1769 ARG   B CB  1 
ATOM   27404 C  CG  . ARG   B 1 1771 ? 92.84900   58.63300  26.50600  1.000 63.75786  ?  1769 ARG   B CG  1 
ATOM   27405 C  CD  . ARG   B 1 1771 ? 91.51500   58.31700  27.15600  1.000 70.94942  ?  1769 ARG   B CD  1 
ATOM   27406 N  NE  . ARG   B 1 1771 ? 91.26700   59.15100  28.32600  1.000 85.36639  ?  1769 ARG   B NE  1 
ATOM   27407 C  CZ  . ARG   B 1 1771 ? 91.57000   58.80100  29.56900  1.000 96.84832  ?  1769 ARG   B CZ  1 
ATOM   27408 N  NH1 . ARG   B 1 1771 ? 92.13000   57.63400  29.84000  1.000 82.29399  ?  1769 ARG   B NH1 1 
ATOM   27409 N  NH2 . ARG   B 1 1771 ? 91.30500   59.64400  30.56300  1.000 88.43287  ?  1769 ARG   B NH2 1 
ATOM   27410 N  N   . LEU   B 1 1772 ? 94.42700   56.54000  22.45600  1.000 60.48080  ?  1770 LEU   B N   1 
ATOM   27411 C  CA  . LEU   B 1 1772 ? 95.21300   55.56200  21.71700  1.000 60.02170  ?  1770 LEU   B CA  1 
ATOM   27412 C  C   . LEU   B 1 1772 ? 96.21800   56.20600  20.77400  1.000 64.13415  ?  1770 LEU   B C   1 
ATOM   27413 O  O   . LEU   B 1 1772 ? 97.25500   55.59900  20.48500  1.000 70.79613  ?  1770 LEU   B O   1 
ATOM   27414 C  CB  . LEU   B 1 1772 ? 94.28900   54.63500  20.92200  1.000 55.81937  ?  1770 LEU   B CB  1 
ATOM   27415 C  CG  . LEU   B 1 1772 ? 93.51900   53.56800  21.70300  1.000 65.66952  ?  1770 LEU   B CG  1 
ATOM   27416 C  CD1 . LEU   B 1 1772 ? 92.42800   52.96400  20.83300  1.000 58.48309  ?  1770 LEU   B CD1 1 
ATOM   27417 C  CD2 . LEU   B 1 1772 ? 94.45800   52.48600  22.21800  1.000 45.68712  ?  1770 LEU   B CD2 1 
ATOM   27418 N  N   . GLN   B 1 1773 ? 95.94100   57.41800  20.28100  1.000 70.14398  ?  1771 GLN   B N   1 
ATOM   27419 C  CA  . GLN   B 1 1773 ? 96.86700   58.04600  19.34200  1.000 76.42523  ?  1771 GLN   B CA  1 
ATOM   27420 C  C   . GLN   B 1 1773 ? 98.13200   58.52200  20.03700  1.000 79.29317  ?  1771 GLN   B C   1 
ATOM   27421 O  O   . GLN   B 1 1773 ? 99.19800   58.57900  19.41300  1.000 81.32696  ?  1771 GLN   B O   1 
ATOM   27422 C  CB  . GLN   B 1 1773 ? 96.19000   59.20700  18.60900  1.000 63.05149  ?  1771 GLN   B CB  1 
ATOM   27423 C  CG  . GLN   B 1 1773 ? 95.86900   60.41600  19.47600  1.000 69.11889  ?  1771 GLN   B CG  1 
ATOM   27424 C  CD  . GLN   B 1 1773 ? 96.64700   61.65700  19.08100  1.000 93.87026  ?  1771 GLN   B CD  1 
ATOM   27425 O  OE1 . GLN   B 1 1773 ? 97.74000   61.56900  18.52100  1.000 95.50950  ?  1771 GLN   B OE1 1 
ATOM   27426 N  NE2 . GLN   B 1 1773 ? 96.08200   62.82500  19.37000  1.000 91.36965  ?  1771 GLN   B NE2 1 
ATOM   27427 N  N   . ARG   B 1 1774 ? 98.04500   58.85700  21.32400  1.000 63.99121  ?  1772 ARG   B N   1 
ATOM   27428 C  CA  . ARG   B 1 1774 ? 99.23600   59.28100  22.04500  1.000 61.49006  ?  1772 ARG   B CA  1 
ATOM   27429 C  C   . ARG   B 1 1774 ? 100.21700  58.12900  22.23300  1.000 65.00968  ?  1772 ARG   B C   1 
ATOM   27430 O  O   . ARG   B 1 1774 ? 101.43100  58.36000  22.30800  1.000 71.26775  ?  1772 ARG   B O   1 
ATOM   27431 C  CB  . ARG   B 1 1774 ? 98.83300   59.89100  23.38600  1.000 65.47482  ?  1772 ARG   B CB  1 
ATOM   27432 C  CG  . ARG   B 1 1774 ? 97.81400   61.02000  23.25100  1.000 66.81868  ?  1772 ARG   B CG  1 
ATOM   27433 C  CD  . ARG   B 1 1774 ? 97.74000   61.84000  24.52200  1.000 83.02157  ?  1772 ARG   B CD  1 
ATOM   27434 N  NE  . ARG   B 1 1774 ? 96.52700   61.58000  25.28900  1.000 78.46085  ?  1772 ARG   B NE  1 
ATOM   27435 C  CZ  . ARG   B 1 1774 ? 96.47400   61.57100  26.61400  1.000 86.81204  ?  1772 ARG   B CZ  1 
ATOM   27436 N  NH1 . ARG   B 1 1774 ? 97.56100   61.73800  27.35100  1.000 99.69833  ?  1772 ARG   B NH1 1 
ATOM   27437 N  NH2 . ARG   B 1 1774 ? 95.30400   61.38000  27.21600  1.000 89.56844  ?  1772 ARG   B NH2 1 
ATOM   27438 N  N   . ILE   B 1 1775 ? 99.72300   56.89000  22.29500  1.000 57.35810  ?  1773 ILE   B N   1 
ATOM   27439 C  CA  . ILE   B 1 1775 ? 100.57200  55.70600  22.41800  1.000 53.64034  ?  1773 ILE   B CA  1 
ATOM   27440 C  C   . ILE   B 1 1775 ? 100.76600  55.10500  21.03600  1.000 57.05612  ?  1773 ILE   B C   1 
ATOM   27441 O  O   . ILE   B 1 1775 ? 101.12900  53.92900  20.89900  1.000 48.89254  ?  1773 ILE   B O   1 
ATOM   27442 C  CB  . ILE   B 1 1775 ? 99.97900   54.66700  23.39300  1.000 54.47933  ?  1773 ILE   B CB  1 
ATOM   27443 C  CG1 . ILE   B 1 1775 ? 98.45100   54.65500  23.31000  1.000 58.87755  ?  1773 ILE   B CG1 1 
ATOM   27444 C  CG2 . ILE   B 1 1775 ? 100.45800  54.92600  24.81600  1.000 68.45733  ?  1773 ILE   B CG2 1 
ATOM   27445 C  CD1 . ILE   B 1 1775 ? 97.80500   53.60000  24.17300  1.000 71.33537  ?  1773 ILE   B CD1 1 
ATOM   27446 N  N   . ASN   B 1 1776 ? 100.50300  55.91700  20.01500  1.000 56.66453  ?  1774 ASN   B N   1 
ATOM   27447 C  CA  . ASN   B 1 1776 ? 100.70100  55.54200  18.61900  1.000 71.99980  ?  1774 ASN   B CA  1 
ATOM   27448 C  C   . ASN   B 1 1776 ? 99.86300   54.32200  18.23700  1.000 69.12628  ?  1774 ASN   B C   1 
ATOM   27449 O  O   . ASN   B 1 1776 ? 100.36500  53.34200  17.68400  1.000 72.08557  ?  1774 ASN   B O   1 
ATOM   27450 C  CB  . ASN   B 1 1776 ? 102.18300  55.30400  18.31800  1.000 77.26946  ?  1774 ASN   B CB  1 
ATOM   27451 C  CG  . ASN   B 1 1776 ? 103.01800  56.56300  18.44400  1.000 76.59489  ?  1774 ASN   B CG  1 
ATOM   27452 O  OD1 . ASN   B 1 1776 ? 102.86100  57.34200  19.38400  1.000 77.99909  ?  1774 ASN   B OD1 1 
ATOM   27453 N  ND2 . ASN   B 1 1776 ? 103.91400  56.77000  17.48500  1.000 69.96308  ?  1774 ASN   B ND2 1 
ATOM   27454 N  N   . TRP   B 1 1777 ? 98.56700   54.39000  18.53300  1.000 70.85724  ?  1775 TRP   B N   1 
ATOM   27455 C  CA  . TRP   B 1 1777 ? 97.60100   53.39700  18.07700  1.000 56.04672  ?  1775 TRP   B CA  1 
ATOM   27456 C  C   . TRP   B 1 1777 ? 96.45100   54.13300  17.40800  1.000 62.82585  ?  1775 TRP   B C   1 
ATOM   27457 O  O   . TRP   B 1 1777 ? 95.81900   54.99200  18.03000  1.000 69.50359  ?  1775 TRP   B O   1 
ATOM   27458 C  CB  . TRP   B 1 1777 ? 97.08500   52.53100  19.23200  1.000 55.45671  ?  1775 TRP   B CB  1 
ATOM   27459 C  CG  . TRP   B 1 1777 ? 98.06100   51.49900  19.72700  1.000 59.59955  ?  1775 TRP   B CG  1 
ATOM   27460 C  CD1 . TRP   B 1 1777 ? 98.62900   51.43400  20.96800  1.000 54.01800  ?  1775 TRP   B CD1 1 
ATOM   27461 C  CD2 . TRP   B 1 1777 ? 98.57700   50.38100  18.99300  1.000 49.65658  ?  1775 TRP   B CD2 1 
ATOM   27462 N  NE1 . TRP   B 1 1777 ? 99.46500   50.34700  21.05100  1.000 46.63021  ?  1775 TRP   B NE1 1 
ATOM   27463 C  CE2 . TRP   B 1 1777 ? 99.45100   49.68400  19.85200  1.000 43.07408  ?  1775 TRP   B CE2 1 
ATOM   27464 C  CE3 . TRP   B 1 1777 ? 98.38600   49.90300  17.69400  1.000 63.08878  ?  1775 TRP   B CE3 1 
ATOM   27465 C  CZ2 . TRP   B 1 1777 ? 100.13100  48.53600  19.45200  1.000 42.50830  ?  1775 TRP   B CZ2 1 
ATOM   27466 C  CZ3 . TRP   B 1 1777 ? 99.06300   48.76300  17.30000  1.000 63.62497  ?  1775 TRP   B CZ3 1 
ATOM   27467 C  CH2 . TRP   B 1 1777 ? 99.92400   48.09300  18.17600  1.000 48.63050  ?  1775 TRP   B CH2 1 
ATOM   27468 N  N   . THR   B 1 1778 ? 96.18400   53.80600  16.14700  1.000 64.55846  ?  1776 THR   B N   1 
ATOM   27469 C  CA  . THR   B 1 1778 ? 95.16400   54.49400  15.36200  1.000 57.74865  ?  1776 THR   B CA  1 
ATOM   27470 C  C   . THR   B 1 1778 ? 93.92200   53.61300  15.27900  1.000 66.60263  ?  1776 THR   B C   1 
ATOM   27471 O  O   . THR   B 1 1778 ? 93.95000   52.55100  14.64900  1.000 72.99678  ?  1776 THR   B O   1 
ATOM   27472 C  CB  . THR   B 1 1778 ? 95.68600   54.82800  13.96700  1.000 57.58620  ?  1776 THR   B CB  1 
ATOM   27473 O  OG1 . THR   B 1 1778 ? 95.95200   53.61500  13.25300  1.000 76.72153  ?  1776 THR   B OG1 1 
ATOM   27474 C  CG2 . THR   B 1 1778 ? 96.96700   55.64500  14.05700  1.000 64.09870  ?  1776 THR   B CG2 1 
ATOM   27475 N  N   . MET   B 1 1779 ? 92.83600   54.05600  15.90800  1.000 61.17264  ?  1777 MET   B N   1 
ATOM   27476 C  CA  . MET   B 1 1779 ? 91.54500   53.38700  15.83000  1.000 70.46142  ?  1777 MET   B CA  1 
ATOM   27477 C  C   . MET   B 1 1779 ? 90.53400   54.28400  15.12900  1.000 74.21140  ?  1777 MET   B C   1 
ATOM   27478 O  O   . MET   B 1 1779 ? 90.44900   55.48100  15.42000  1.000 86.27620  ?  1777 MET   B O   1 
ATOM   27479 C  CB  . MET   B 1 1779 ? 91.01600   53.01600  17.22000  1.000 70.56860  ?  1777 MET   B CB  1 
ATOM   27480 C  CG  . MET   B 1 1779 ? 89.51800   52.73500  17.23000  1.000 63.38619  ?  1777 MET   B CG  1 
ATOM   27481 S  SD  . MET   B 1 1779 ? 88.94100   51.79400  18.65200  1.000 83.82533  ?  1777 MET   B SD  1 
ATOM   27482 C  CE  . MET   B 1 1779 ? 88.52800   53.11900  19.77800  1.000 62.03498  ?  1777 MET   B CE  1 
ATOM   27483 N  N   . VAL   B 1 1780 ? 89.77100   53.70700  14.20300  1.000 62.83382  ?  1778 VAL   B N   1 
ATOM   27484 C  CA  . VAL   B 1 1780 ? 88.64800   54.40400  13.58700  1.000 81.86476  ?  1778 VAL   B CA  1 
ATOM   27485 C  C   . VAL   B 1 1780 ? 87.41200   54.15200  14.43700  1.000 74.12152  ?  1778 VAL   B C   1 
ATOM   27486 O  O   . VAL   B 1 1780 ? 87.06000   52.99800  14.71300  1.000 75.62366  ?  1778 VAL   B O   1 
ATOM   27487 C  CB  . VAL   B 1 1780 ? 88.42600   53.94400  12.13600  1.000 78.82520  ?  1778 VAL   B CB  1 
ATOM   27488 C  CG1 . VAL   B 1 1780 ? 87.58100   54.96600  11.38400  1.000 95.09791  ?  1778 VAL   B CG1 1 
ATOM   27489 C  CG2 . VAL   B 1 1780 ? 89.75000   53.73100  11.42900  1.000 54.90303  ?  1778 VAL   B CG2 1 
ATOM   27490 N  N   . ILE   B 1 1781 ? 86.75200   55.23200  14.85800  1.000 64.13734  ?  1779 ILE   B N   1 
ATOM   27491 C  CA  . ILE   B 1 1781 ? 85.62100   55.09700  15.76800  1.000 75.09594  ?  1779 ILE   B CA  1 
ATOM   27492 C  C   . ILE   B 1 1781 ? 84.44400   54.40600  15.08300  1.000 86.49890  ?  1779 ILE   B C   1 
ATOM   27493 O  O   . ILE   B 1 1781 ? 83.67000   53.69300  15.73700  1.000 85.63108  ?  1779 ILE   B O   1 
ATOM   27494 C  CB  . ILE   B 1 1781 ? 85.24900   56.48100  16.33500  1.000 78.56477  ?  1779 ILE   B CB  1 
ATOM   27495 C  CG1 . ILE   B 1 1781 ? 83.85300   56.47000  16.96300  1.000 99.21631  ?  1779 ILE   B CG1 1 
ATOM   27496 C  CG2 . ILE   B 1 1781 ? 85.37200   57.53700  15.25800  1.000 69.90774  ?  1779 ILE   B CG2 1 
ATOM   27497 C  CD1 . ILE   B 1 1781 ? 83.57900   57.65400  17.86300  1.000 94.81475  ?  1779 ILE   B CD1 1 
ATOM   27498 N  N   . ASN   B 1 1782 ? 84.29600   54.57900  13.76600  1.000 91.01620  ?  1780 ASN   B N   1 
ATOM   27499 C  CA  . ASN   B 1 1782 ? 83.27300   53.83300  13.03500  1.000 92.06734  ?  1780 ASN   B CA  1 
ATOM   27500 C  C   . ASN   B 1 1782 ? 83.48700   52.33100  13.17200  1.000 97.34451  ?  1780 ASN   B C   1 
ATOM   27501 O  O   . ASN   B 1 1782 ? 82.53500   51.57600  13.40000  1.000 101.58369 ?  1780 ASN   B O   1 
ATOM   27502 C  CB  . ASN   B 1 1782 ? 83.27100   54.23400  11.56000  1.000 82.69384  ?  1780 ASN   B CB  1 
ATOM   27503 C  CG  . ASN   B 1 1782 ? 82.65800   53.16900  10.67200  1.000 90.99221  ?  1780 ASN   B CG  1 
ATOM   27504 O  OD1 . ASN   B 1 1782 ? 83.36500   52.46500  9.95100   1.000 82.03890  ?  1780 ASN   B OD1 1 
ATOM   27505 N  ND2 . ASN   B 1 1782 ? 81.33800   53.03800  10.72900  1.000 97.28441  ?  1780 ASN   B ND2 1 
ATOM   27506 N  N   . HIS   B 1 1783 ? 84.73900   51.88100  13.03300  1.000 89.21343  ?  1781 HIS   B N   1 
ATOM   27507 C  CA  . HIS   B 1 1783 ? 85.04500   50.46200  13.18400  1.000 77.71111  ?  1781 HIS   B CA  1 
ATOM   27508 C  C   . HIS   B 1 1783 ? 84.57700   49.93200  14.53400  1.000 76.82854  ?  1781 HIS   B C   1 
ATOM   27509 O  O   . HIS   B 1 1783 ? 84.14500   48.77900  14.63900  1.000 86.61507  ?  1781 HIS   B O   1 
ATOM   27510 C  CB  . HIS   B 1 1783 ? 86.54600   50.22500  13.01200  1.000 73.50056  ?  1781 HIS   B CB  1 
ATOM   27511 C  CG  . HIS   B 1 1783 ? 87.01200   50.29300  11.59000  1.000 80.33446  ?  1781 HIS   B CG  1 
ATOM   27512 N  ND1 . HIS   B 1 1783 ? 88.34700   50.31800  11.24600  1.000 75.97435  ?  1781 HIS   B ND1 1 
ATOM   27513 C  CD2 . HIS   B 1 1783 ? 86.32300   50.33100  10.42600  1.000 101.90353 ?  1781 HIS   B CD2 1 
ATOM   27514 C  CE1 . HIS   B 1 1783 ? 88.46000   50.37300  9.93100   1.000 71.31768  ?  1781 HIS   B CE1 1 
ATOM   27515 N  NE2 . HIS   B 1 1783 ? 87.24700   50.38300  9.40900   1.000 110.88623 ?  1781 HIS   B NE2 1 
ATOM   27516 N  N   . LEU   B 1 1784 ? 84.64400   50.76000  15.57700  1.000 75.70440  ?  1782 LEU   B N   1 
ATOM   27517 C  CA  . LEU   B 1 1784 ? 84.19700   50.31900  16.89500  1.000 82.30163  ?  1782 LEU   B CA  1 
ATOM   27518 C  C   . LEU   B 1 1784 ? 82.74300   49.85300  16.86200  1.000 102.79250 ?  1782 LEU   B C   1 
ATOM   27519 O  O   . LEU   B 1 1784 ? 82.40800   48.81300  17.44100  1.000 114.80673 ?  1782 LEU   B O   1 
ATOM   27520 C  CB  . LEU   B 1 1784 ? 84.38500   51.44500  17.91000  1.000 84.24244  ?  1782 LEU   B CB  1 
ATOM   27521 C  CG  . LEU   B 1 1784 ? 84.22200   51.04400  19.37300  1.000 94.49310  ?  1782 LEU   B CG  1 
ATOM   27522 C  CD1 . LEU   B 1 1784 ? 84.94100   49.73400  19.62700  1.000 94.09428  ?  1782 LEU   B CD1 1 
ATOM   27523 C  CD2 . LEU   B 1 1784 ? 84.76200   52.13600  20.27900  1.000 80.10969  ?  1782 LEU   B CD2 1 
ATOM   27524 N  N   . PHE   B 1 1785 ? 81.86900   50.59700  16.17500  1.000 117.44194 ?  1783 PHE   B N   1 
ATOM   27525 C  CA  . PHE   B 1 1785 ? 80.47500   50.17600  16.04000  1.000 106.67675 ?  1783 PHE   B CA  1 
ATOM   27526 C  C   . PHE   B 1 1785 ? 80.37000   48.85600  15.28600  1.000 101.20255 ?  1783 PHE   B C   1 
ATOM   27527 O  O   . PHE   B 1 1785 ? 79.62400   47.95500  15.68800  1.000 106.54539 ?  1783 PHE   B O   1 
ATOM   27528 C  CB  . PHE   B 1 1785 ? 79.66200   51.24900  15.31600  1.000 107.34149 ?  1783 PHE   B CB  1 
ATOM   27529 C  CG  . PHE   B 1 1785 ? 79.90200   52.63900  15.81500  1.000 111.20640 ?  1783 PHE   B CG  1 
ATOM   27530 C  CD1 . PHE   B 1 1785 ? 79.86700   52.92500  17.17000  1.000 112.87991 ?  1783 PHE   B CD1 1 
ATOM   27531 C  CD2 . PHE   B 1 1785 ? 80.16800   53.66300  14.92400  1.000 94.95105  ?  1783 PHE   B CD2 1 
ATOM   27532 C  CE1 . PHE   B 1 1785 ? 80.09000   54.21000  17.62300  1.000 106.64002 ?  1783 PHE   B CE1 1 
ATOM   27533 C  CE2 . PHE   B 1 1785 ? 80.39300   54.94600  15.36800  1.000 100.62051 ?  1783 PHE   B CE2 1 
ATOM   27534 C  CZ  . PHE   B 1 1785 ? 80.35500   55.22200  16.72100  1.000 105.17048 ?  1783 PHE   B CZ  1 
ATOM   27535 N  N   . LEU   B 1 1786 ? 81.09800   48.73100  14.17100  1.000 90.13893  ?  1784 LEU   B N   1 
ATOM   27536 C  CA  . LEU   B 1 1786 ? 81.01200   47.51800  13.36500  1.000 92.86253  ?  1784 LEU   B CA  1 
ATOM   27537 C  C   . LEU   B 1 1786 ? 81.57800   46.31100  14.10600  1.000 98.46825  ?  1784 LEU   B C   1 
ATOM   27538 O  O   . LEU   B 1 1786 ? 81.11800   45.18300  13.89400  1.000 98.00522  ?  1784 LEU   B O   1 
ATOM   27539 C  CB  . LEU   B 1 1786 ? 81.75300   47.71200  12.04200  1.000 71.95584  ?  1784 LEU   B CB  1 
ATOM   27540 C  CG  . LEU   B 1 1786 ? 81.72300   49.09900  11.39100  1.000 79.69702  ?  1784 LEU   B CG  1 
ATOM   27541 C  CD1 . LEU   B 1 1786 ? 82.74300   49.18700  10.26100  1.000 79.79660  ?  1784 LEU   B CD1 1 
ATOM   27542 C  CD2 . LEU   B 1 1786 ? 80.32900   49.43500  10.88400  1.000 78.64432  ?  1784 LEU   B CD2 1 
ATOM   27543 N  N   . TYR   B 1 1787 ? 82.56400   46.52400  14.97900  1.000 101.30693 ?  1785 TYR   B N   1 
ATOM   27544 C  CA  . TYR   B 1 1787 ? 83.23800   45.44600  15.70400  1.000 88.79737  ?  1785 TYR   B CA  1 
ATOM   27545 C  C   . TYR   B 1 1787 ? 83.31400   45.80900  17.18400  1.000 88.16714  ?  1785 TYR   B C   1 
ATOM   27546 O  O   . TYR   B 1 1787 ? 84.39200   46.11000  17.70600  1.000 90.51112  ?  1785 TYR   B O   1 
ATOM   27547 C  CB  . TYR   B 1 1787 ? 84.63600   45.19200  15.13300  1.000 80.49941  ?  1785 TYR   B CB  1 
ATOM   27548 C  CG  . TYR   B 1 1787 ? 84.76900   45.31600  13.62300  1.000 76.73261  ?  1785 TYR   B CG  1 
ATOM   27549 C  CD1 . TYR   B 1 1787 ? 84.87900   46.56000  13.01100  1.000 85.75888  ?  1785 TYR   B CD1 1 
ATOM   27550 C  CD2 . TYR   B 1 1787 ? 84.80200   44.18700  12.81200  1.000 82.68420  ?  1785 TYR   B CD2 1 
ATOM   27551 C  CE1 . TYR   B 1 1787 ? 85.00100   46.68000  11.63800  1.000 80.16366  ?  1785 TYR   B CE1 1 
ATOM   27552 C  CE2 . TYR   B 1 1787 ? 84.92800   44.29700  11.43800  1.000 82.33452  ?  1785 TYR   B CE2 1 
ATOM   27553 C  CZ  . TYR   B 1 1787 ? 85.02800   45.54200  10.85800  1.000 78.52442  ?  1785 TYR   B CZ  1 
ATOM   27554 O  OH  . TYR   B 1 1787 ? 85.15000   45.64100  9.49500   1.000 103.85705 ?  1785 TYR   B OH  1 
ATOM   27555 N  N   . PRO   B 1 1788 ? 82.18000   45.76300  17.90200  1.000 99.28916  ?  1786 PRO   B N   1 
ATOM   27556 C  CA  . PRO   B 1 1788 ? 82.17400   46.22000  19.30100  1.000 100.28812 ?  1786 PRO   B CA  1 
ATOM   27557 C  C   . PRO   B 1 1788 ? 82.94400   45.33700  20.27300  1.000 88.28789  ?  1786 PRO   B C   1 
ATOM   27558 O  O   . PRO   B 1 1788 ? 82.84400   45.54200  21.48700  1.000 82.52686  ?  1786 PRO   B O   1 
ATOM   27559 C  CB  . PRO   B 1 1788 ? 80.68100   46.23500  19.65800  1.000 106.63115 ?  1786 PRO   B CB  1 
ATOM   27560 C  CG  . PRO   B 1 1788 ? 79.97000   46.30600  18.35400  1.000 115.23273 ?  1786 PRO   B CG  1 
ATOM   27561 C  CD  . PRO   B 1 1788 ? 80.81200   45.49000  17.42400  1.000 101.78103 ?  1786 PRO   B CD  1 
ATOM   27562 N  N   . THR   B 1 1789 ? 83.70000   44.36100  19.78200  1.000 99.30709  ?  1787 THR   B N   1 
ATOM   27563 C  CA  . THR   B 1 1789 ? 84.51200   43.50500  20.63200  1.000 107.56285 ?  1787 THR   B CA  1 
ATOM   27564 C  C   . THR   B 1 1789 ? 85.98700   43.82700  20.43100  1.000 101.78956 ?  1787 THR   B C   1 
ATOM   27565 O  O   . THR   B 1 1789 ? 86.43500   44.04800  19.30000  1.000 99.60816  ?  1787 THR   B O   1 
ATOM   27566 C  CB  . THR   B 1 1789 ? 84.25300   42.02400  20.33900  1.000 99.02168  ?  1787 THR   B CB  1 
ATOM   27567 O  OG1 . THR   B 1 1789 ? 84.13100   41.82900  18.92300  1.000 91.94622  ?  1787 THR   B OG1 1 
ATOM   27568 C  CG2 . THR   B 1 1789 ? 82.97500   41.55900  21.02100  1.000 93.33132  ?  1787 THR   B CG2 1 
ATOM   27569 N  N   . ILE   B 1 1790 ? 86.73500   43.85800  21.53900  1.000 88.78770  ?  1788 ILE   B N   1 
ATOM   27570 C  CA  . ILE   B 1 1790 ? 88.17700   44.10100  21.48200  1.000 89.87600  ?  1788 ILE   B CA  1 
ATOM   27571 C  C   . ILE   B 1 1790 ? 88.85100   43.12400  20.52700  1.000 93.56047  ?  1788 ILE   B C   1 
ATOM   27572 O  O   . ILE   B 1 1790 ? 89.78200   43.48500  19.79700  1.000 95.36637  ?  1788 ILE   B O   1 
ATOM   27573 C  CB  . ILE   B 1 1790 ? 88.78000   44.02300  22.89900  1.000 84.96979  ?  1788 ILE   B CB  1 
ATOM   27574 C  CG1 . ILE   B 1 1790 ? 88.46000   45.29300  23.68900  1.000 74.26873  ?  1788 ILE   B CG1 1 
ATOM   27575 C  CG2 . ILE   B 1 1790 ? 90.28300   43.77600  22.84500  1.000 78.14398  ?  1788 ILE   B CG2 1 
ATOM   27576 C  CD1 . ILE   B 1 1790 ? 88.93100   45.24300  25.12500  1.000 65.07885  ?  1788 ILE   B CD1 1 
ATOM   27577 N  N   . GLU   B 1 1791 ? 88.37500   41.87800  20.49700  1.000 86.50947  ?  1789 GLU   B N   1 
ATOM   27578 C  CA  . GLU   B 1 1791 ? 88.94700   40.85400  19.63100  1.000 90.99628  ?  1789 GLU   B CA  1 
ATOM   27579 C  C   . GLU   B 1 1791 ? 88.66000   41.08500  18.15000  1.000 95.18766  ?  1789 GLU   B C   1 
ATOM   27580 O  O   . GLU   B 1 1791 ? 89.22000   40.36300  17.31600  1.000 89.49704  ?  1789 GLU   B O   1 
ATOM   27581 C  CB  . GLU   B 1 1791 ? 88.42500   39.47400  20.04000  1.000 84.27247  ?  1789 GLU   B CB  1 
ATOM   27582 N  N   . GLN   B 1 1792 ? 87.81800   42.05900  17.79800  1.000 98.51444  ?  1790 GLN   B N   1 
ATOM   27583 C  CA  . GLN   B 1 1792 ? 87.44200   42.28200  16.40700  1.000 98.30638  ?  1790 GLN   B CA  1 
ATOM   27584 C  C   . GLN   B 1 1792 ? 87.96500   43.58500  15.82000  1.000 102.84554 ?  1790 GLN   B C   1 
ATOM   27585 O  O   . GLN   B 1 1792 ? 88.29800   43.61400  14.63200  1.000 91.56216  ?  1790 GLN   B O   1 
ATOM   27586 C  CB  . GLN   B 1 1792 ? 85.91600   42.24100  16.26000  1.000 75.52765  ?  1790 GLN   B CB  1 
ATOM   27587 N  N   . ILE   B 1 1793 ? 88.04400   44.66500  16.60400  1.000 103.07175 ?  1791 ILE   B N   1 
ATOM   27588 C  CA  . ILE   B 1 1793 ? 88.72500   45.86000  16.10700  1.000 91.62396  ?  1791 ILE   B CA  1 
ATOM   27589 C  C   . ILE   B 1 1793 ? 90.23200   45.67700  16.11400  1.000 92.26688  ?  1791 ILE   B C   1 
ATOM   27590 O  O   . ILE   B 1 1793 ? 90.93700   46.29900  15.31200  1.000 93.40633  ?  1791 ILE   B O   1 
ATOM   27591 C  CB  . ILE   B 1 1793 ? 88.34400   47.11300  16.91500  1.000 82.01640  ?  1791 ILE   B CB  1 
ATOM   27592 C  CG1 . ILE   B 1 1793 ? 88.59700   46.88600  18.40600  1.000 86.83931  ?  1791 ILE   B CG1 1 
ATOM   27593 C  CG2 . ILE   B 1 1793 ? 86.91900   47.53100  16.63400  1.000 86.71835  ?  1791 ILE   B CG2 1 
ATOM   27594 C  CD1 . ILE   B 1 1793 ? 89.13800   48.09600  19.11600  1.000 94.67677  ?  1791 ILE   B CD1 1 
ATOM   27595 N  N   . ALA   B 1 1794 ? 90.75600   44.85300  17.01900  1.000 84.38653  ?  1792 ALA   B N   1 
ATOM   27596 C  CA  . ALA   B 1 1794 ? 92.20100   44.65600  17.13700  1.000 78.17490  ?  1792 ALA   B CA  1 
ATOM   27597 C  C   . ALA   B 1 1794 ? 92.87500   44.30700  15.81200  1.000 85.43906  ?  1792 ALA   B C   1 
ATOM   27598 O  O   . ALA   B 1 1794 ? 93.85700   44.97700  15.45400  1.000 100.06532 ?  1792 ALA   B O   1 
ATOM   27599 C  CB  . ALA   B 1 1794 ? 92.48600   43.59900  18.20600  1.000 81.05416  ?  1792 ALA   B CB  1 
ATOM   27600 N  N   . PRO   B 1 1795 ? 92.41500   43.30800  15.02700  1.000 87.35126  ?  1793 PRO   B N   1 
ATOM   27601 C  CA  . PRO   B 1 1795 ? 93.07600   43.05500  13.73900  1.000 97.77088  ?  1793 PRO   B CA  1 
ATOM   27602 C  C   . PRO   B 1 1795 ? 92.79600   44.14600  12.71500  1.000 100.18310 ?  1793 PRO   B C   1 
ATOM   27603 O  O   . PRO   B 1 1795 ? 93.72500   44.68800  12.10700  1.000 91.73281  ?  1793 PRO   B O   1 
ATOM   27604 C  CB  . PRO   B 1 1795 ? 92.49200   41.70800  13.29700  1.000 88.57383  ?  1793 PRO   B CB  1 
ATOM   27605 C  CG  . PRO   B 1 1795 ? 91.15500   41.65500  13.93600  1.000 103.64076 ?  1793 PRO   B CG  1 
ATOM   27606 C  CD  . PRO   B 1 1795 ? 91.29500   42.37100  15.25400  1.000 95.09317  ?  1793 PRO   B CD  1 
ATOM   27607 N  N   . PHE   B 1 1796 ? 91.51700   44.47100  12.52400  1.000 119.53941 ?  1794 PHE   B N   1 
ATOM   27608 C  CA  . PHE   B 1 1796 ? 91.08500   45.42300  11.50800  1.000 118.17577 ?  1794 PHE   B CA  1 
ATOM   27609 C  C   . PHE   B 1 1796 ? 91.79600   46.76100  11.64300  1.000 111.21272 ?  1794 PHE   B C   1 
ATOM   27610 O  O   . PHE   B 1 1796 ? 92.64600   47.10900  10.81700  1.000 113.30509 ?  1794 PHE   B O   1 
ATOM   27611 C  CB  . PHE   B 1 1796 ? 89.57100   45.62900  11.58500  1.000 98.75535  ?  1794 PHE   B CB  1 
ATOM   27612 C  CG  . PHE   B 1 1796 ? 88.83400   45.11600  10.38800  1.000 106.80579 ?  1794 PHE   B CG  1 
ATOM   27613 C  CD1 . PHE   B 1 1796 ? 88.42300   43.79500  10.32500  1.000 115.17931 ?  1794 PHE   B CD1 1 
ATOM   27614 C  CD2 . PHE   B 1 1796 ? 88.56200   45.95000  9.31600   1.000 116.46265 ?  1794 PHE   B CD2 1 
ATOM   27615 C  CE1 . PHE   B 1 1796 ? 87.74900   43.31700  9.22000   1.000 134.93923 ?  1794 PHE   B CE1 1 
ATOM   27616 C  CE2 . PHE   B 1 1796 ? 87.89000   45.47800  8.20700   1.000 125.43042 ?  1794 PHE   B CE2 1 
ATOM   27617 C  CZ  . PHE   B 1 1796 ? 87.48200   44.15900  8.15800   1.000 132.51810 ?  1794 PHE   B CZ  1 
ATOM   27618 N  N   . VAL   B 1 1797 ? 91.45600   47.51800  12.67900  1.000 111.95576 ?  1795 VAL   B N   1 
ATOM   27619 C  CA  . VAL   B 1 1797 ? 92.08200   48.81400  12.89000  1.000 116.58034 ?  1795 VAL   B CA  1 
ATOM   27620 C  C   . VAL   B 1 1797 ? 93.13800   48.64700  13.98300  1.000 110.83459 ?  1795 VAL   B C   1 
ATOM   27621 O  O   . VAL   B 1 1797 ? 93.84400   47.63300  14.00400  1.000 109.96441 ?  1795 VAL   B O   1 
ATOM   27622 C  CB  . VAL   B 1 1797 ? 91.01100   49.88600  13.18800  1.000 114.91757 ?  1795 VAL   B CB  1 
ATOM   27623 C  CG1 . VAL   B 1 1797 ? 90.29700   49.65600  14.53200  1.000 107.21777 ?  1795 VAL   B CG1 1 
ATOM   27624 C  CG2 . VAL   B 1 1797 ? 91.58100   51.28500  13.02800  1.000 97.96231  ?  1795 VAL   B CG2 1 
ATOM   27625 N  N   . THR   B 1 1798 ? 93.26700   49.62100  14.88600  1.000 107.79117 ?  1796 THR   B N   1 
ATOM   27626 C  CA  . THR   B 1 1798 ? 94.31800   49.63400  15.90200  1.000 80.64829  ?  1796 THR   B CA  1 
ATOM   27627 C  C   . THR   B 1 1798 ? 95.68300   49.46300  15.24300  1.000 90.23208  ?  1796 THR   B C   1 
ATOM   27628 O  O   . THR   B 1 1798 ? 96.48600   48.60200  15.60900  1.000 107.17724 ?  1796 THR   B O   1 
ATOM   27629 C  CB  . THR   B 1 1798 ? 94.07800   48.57200  16.97800  1.000 81.81535  ?  1796 THR   B CB  1 
ATOM   27630 O  OG1 . THR   B 1 1798 ? 94.19300   47.26200  16.40500  1.000 105.49535 ?  1796 THR   B OG1 1 
ATOM   27631 C  CG2 . THR   B 1 1798 ? 92.69200   48.73700  17.58300  1.000 70.31645  ?  1796 THR   B CG2 1 
ATOM   27632 N  N   . SER   B 1 1799 ? 95.92300   50.29100  14.23400  1.000 79.23621  ?  1797 SER   B N   1 
ATOM   27633 C  CA  . SER   B 1 1799 ? 97.19200   50.29500  13.53000  1.000 77.35027  ?  1797 SER   B CA  1 
ATOM   27634 C  C   . SER   B 1 1799 ? 98.20000   51.16500  14.26800  1.000 78.33157  ?  1797 SER   B C   1 
ATOM   27635 O  O   . SER   B 1 1799 ? 97.84400   52.13000  14.95000  1.000 70.79063  ?  1797 SER   B O   1 
ATOM   27636 C  CB  . SER   B 1 1799 ? 97.00800   50.79800  12.09800  1.000 72.98308  ?  1797 SER   B CB  1 
ATOM   27637 O  OG  . SER   B 1 1799 ? 98.24400   51.18700  11.52700  1.000 73.08182  ?  1797 SER   B OG  1 
ATOM   27638 N  N   . GLU   B 1 1800 ? 99.47100   50.80600  14.12800  1.000 75.46397  ?  1798 GLU   B N   1 
ATOM   27639 C  CA  . GLU   B 1 1800 ? 100.54900  51.47900  14.83700  1.000 66.44781  ?  1798 GLU   B CA  1 
ATOM   27640 C  C   . GLU   B 1 1800 ? 101.14500  52.55700  13.94200  1.000 71.97167  ?  1798 GLU   B C   1 
ATOM   27641 O  O   . GLU   B 1 1800 ? 101.57000  52.27000  12.81600  1.000 80.38903  ?  1798 GLU   B O   1 
ATOM   27642 C  CB  . GLU   B 1 1800 ? 101.61800  50.47300  15.26100  1.000 51.18456  ?  1798 GLU   B CB  1 
ATOM   27643 N  N   . GLN   B 1 1801 ? 101.15800  53.79600  14.43500  1.000 74.99469  ?  1799 GLN   B N   1 
ATOM   27644 C  CA  . GLN   B 1 1801 ? 101.87200  54.86400  13.74900  1.000 86.20668  ?  1799 GLN   B CA  1 
ATOM   27645 C  C   . GLN   B 1 1801 ? 103.34400  54.50000  13.64400  1.000 90.18898  ?  1799 GLN   B C   1 
ATOM   27646 O  O   . GLN   B 1 1801 ? 104.02900  54.34100  14.66200  1.000 94.30507  ?  1799 GLN   B O   1 
ATOM   27647 C  CB  . GLN   B 1 1801 ? 101.71200  56.19000  14.49000  1.000 83.98232  ?  1799 GLN   B CB  1 
ATOM   27648 C  CG  . GLN   B 1 1801 ? 102.57400  57.30600  13.90400  1.000 91.02908  ?  1799 GLN   B CG  1 
ATOM   27649 C  CD  . GLN   B 1 1801 ? 102.64900  58.53400  14.79100  1.000 102.98263 ?  1799 GLN   B CD  1 
ATOM   27650 O  OE1 . GLN   B 1 1801 ? 101.68600  58.87900  15.47600  1.000 110.34213 ?  1799 GLN   B OE1 1 
ATOM   27651 N  NE2 . GLN   B 1 1801 ? 103.79900  59.20000  14.78400  1.000 77.63639  ?  1799 GLN   B NE2 1 
ATOM   27652 N  N   . VAL   B 1 1802 ? 103.82800  54.36100  12.41000  1.000 79.25636  ?  1800 VAL   B N   1 
ATOM   27653 C  CA  . VAL   B 1 1802 ? 105.20600  53.94700  12.20500  1.000 79.13730  ?  1800 VAL   B CA  1 
ATOM   27654 C  C   . VAL   B 1 1802 ? 106.13100  55.09900  12.57500  1.000 89.21004  ?  1800 VAL   B C   1 
ATOM   27655 O  O   . VAL   B 1 1802 ? 105.85800  56.26600  12.26200  1.000 70.10488  ?  1800 VAL   B O   1 
ATOM   27656 C  CB  . VAL   B 1 1802 ? 105.41400  53.45400  10.76100  1.000 96.83838  ?  1800 VAL   B CB  1 
ATOM   27657 C  CG1 . VAL   B 1 1802 ? 105.40800  54.60300  9.73800   1.000 98.96514  ?  1800 VAL   B CG1 1 
ATOM   27658 C  CG2 . VAL   B 1 1802 ? 106.68300  52.61700  10.65900  1.000 90.73058  ?  1800 VAL   B CG2 1 
ATOM   27659 N  N   . VAL   B 1 1803 ? 107.19300  54.78200  13.31200  1.000 80.33109  ?  1801 VAL   B N   1 
ATOM   27660 C  CA  . VAL   B 1 1803 ? 108.18100  55.75900  13.74500  1.000 65.62809  ?  1801 VAL   B CA  1 
ATOM   27661 C  C   . VAL   B 1 1803 ? 109.54800  55.28800  13.27800  1.000 64.59465  ?  1801 VAL   B C   1 
ATOM   27662 O  O   . VAL   B 1 1803 ? 109.84600  54.08900  13.30700  1.000 65.18044  ?  1801 VAL   B O   1 
ATOM   27663 C  CB  . VAL   B 1 1803 ? 108.16700  55.96500  15.27400  1.000 56.33675  ?  1801 VAL   B CB  1 
ATOM   27664 C  CG1 . VAL   B 1 1803 ? 109.07800  57.11900  15.65500  1.000 56.94454  ?  1801 VAL   B CG1 1 
ATOM   27665 C  CG2 . VAL   B 1 1803 ? 106.75400  56.21900  15.76800  1.000 55.52925  ?  1801 VAL   B CG2 1 
ATOM   27666 N  N   . ILE   B 1 1804 ? 110.37000  56.23600  12.83600  1.000 72.68367  ?  1802 ILE   B N   1 
ATOM   27667 C  CA  . ILE   B 1 1804 ? 111.71400  55.96300  12.35500  1.000 59.95257  ?  1802 ILE   B CA  1 
ATOM   27668 C  C   . ILE   B 1 1804 ? 112.69500  56.74400  13.22100  1.000 60.98596  ?  1802 ILE   B C   1 
ATOM   27669 O  O   . ILE   B 1 1804 ? 112.32400  57.68600  13.92800  1.000 70.42308  ?  1802 ILE   B O   1 
ATOM   27670 C  CB  . ILE   B 1 1804 ? 111.87300  56.32400  10.86200  1.000 72.11806  ?  1802 ILE   B CB  1 
ATOM   27671 C  CG1 . ILE   B 1 1804 ? 112.91600  55.42500  10.19900  1.000 85.72925  ?  1802 ILE   B CG1 1 
ATOM   27672 C  CG2 . ILE   B 1 1804 ? 112.24000  57.79400  10.69900  1.000 64.91209  ?  1802 ILE   B CG2 1 
ATOM   27673 C  CD1 . ILE   B 1 1804 ? 112.89900  55.47600  8.68200   1.000 57.10188  ?  1802 ILE   B CD1 1 
ATOM   27674 N  N   . GLU   B 1 1805 ? 113.96400  56.33600  13.16600  1.000 68.30048  ?  1803 GLU   B N   1 
ATOM   27675 C  CA  . GLU   B 1 1805 ? 115.01200  56.93100  14.00300  1.000 63.31825  ?  1803 GLU   B CA  1 
ATOM   27676 C  C   . GLU   B 1 1805 ? 116.31900  56.95900  13.20800  1.000 69.16639  ?  1803 GLU   B C   1 
ATOM   27677 O  O   . GLU   B 1 1805 ? 117.10700  56.00900  13.25800  1.000 64.99567  ?  1803 GLU   B O   1 
ATOM   27678 C  CB  . GLU   B 1 1805 ? 115.16400  56.16900  15.31500  1.000 50.41388  ?  1803 GLU   B CB  1 
ATOM   27679 C  CG  . GLU   B 1 1805 ? 114.98000  54.65700  15.20200  1.000 66.29384  ?  1803 GLU   B CG  1 
ATOM   27680 C  CD  . GLU   B 1 1805 ? 113.64800  54.19000  15.75400  1.000 66.68078  ?  1803 GLU   B CD  1 
ATOM   27681 O  OE1 . GLU   B 1 1805 ? 112.63000  54.86300  15.49000  1.000 61.29579  ?  1803 GLU   B OE1 1 
ATOM   27682 O  OE2 . GLU   B 1 1805 ? 113.61900  53.15700  16.45700  1.000 93.40979  -1 1803 GLU   B OE2 1 
ATOM   27683 N  N   . ALA   B 1 1806 ? 116.55000  58.06300  12.48800  1.000 59.79913  ?  1804 ALA   B N   1 
ATOM   27684 C  CA  . ALA   B 1 1806 ? 117.77200  58.23200  11.70600  1.000 62.38612  ?  1804 ALA   B CA  1 
ATOM   27685 C  C   . ALA   B 1 1806 ? 117.93900  59.65100  11.16800  1.000 67.04222  ?  1804 ALA   B C   1 
ATOM   27686 O  O   . ALA   B 1 1806 ? 118.04800  60.60600  11.94600  1.000 34.00025  ?  1804 ALA   B O   1 
ATOM   27687 C  CB  . ALA   B 1 1806 ? 117.80000  57.24100  10.54200  1.000 70.37359  ?  1804 ALA   B CB  1 
ATOM   27688 N  N   . ALA   B 1 1807 ? 117.97600  59.76900  9.83100   1.000 64.59717  ?  1805 ALA   B N   1 
ATOM   27689 C  CA  . ALA   B 1 1807 ? 118.20400  60.98500  9.04100   1.000 41.44258  ?  1805 ALA   B CA  1 
ATOM   27690 C  C   . ALA   B 1 1807 ? 119.68900  61.31400  8.92300   1.000 56.68903  ?  1805 ALA   B C   1 
ATOM   27691 O  O   . ALA   B 1 1807 ? 120.47300  60.49100  8.43800   1.000 68.26139  ?  1805 ALA   B O   1 
ATOM   27692 C  CB  . ALA   B 1 1807 ? 117.43700  62.18500  9.60400   1.000 46.25677  ?  1805 ALA   B CB  1 
ATOM   27693 N  N   . ALA   B 1 1808 ? 120.08700  62.51900  9.32600   1.000 58.13269  ?  1806 ALA   B N   1 
ATOM   27694 C  CA  . ALA   B 1 1808 ? 121.49500  62.91600  9.31300   1.000 46.68880  ?  1806 ALA   B CA  1 
ATOM   27695 C  C   . ALA   B 1 1808 ? 122.08200  62.57900  10.67800  1.000 56.35454  ?  1806 ALA   B C   1 
ATOM   27696 O  O   . ALA   B 1 1808 ? 121.92300  63.33500  11.63900  1.000 56.68726  ?  1806 ALA   B O   1 
ATOM   27697 C  CB  . ALA   B 1 1808 ? 121.64100  64.39800  8.98800   1.000 33.81230  ?  1806 ALA   B CB  1 
ATOM   27698 N  N   . GLU   B 1 1809 ? 122.76200  61.43600  10.76800  1.000 64.20025  ?  1807 GLU   B N   1 
ATOM   27699 C  CA  . GLU   B 1 1809 ? 123.23200  60.95500  12.06300  1.000 69.19384  ?  1807 GLU   B CA  1 
ATOM   27700 C  C   . GLU   B 1 1809 ? 124.53500  61.62800  12.47900  1.000 65.01063  ?  1807 GLU   B C   1 
ATOM   27701 O  O   . GLU   B 1 1809 ? 124.62800  62.19000  13.57600  1.000 50.64291  ?  1807 GLU   B O   1 
ATOM   27702 C  CB  . GLU   B 1 1809 ? 123.39100  59.43300  12.02900  1.000 69.80575  ?  1807 GLU   B CB  1 
ATOM   27703 C  CG  . GLU   B 1 1809 ? 122.06800  58.67900  12.00000  1.000 84.80742  ?  1807 GLU   B CG  1 
ATOM   27704 C  CD  . GLU   B 1 1809 ? 121.88700  57.85300  10.74000  1.000 90.82540  ?  1807 GLU   B CD  1 
ATOM   27705 O  OE1 . GLU   B 1 1809 ? 121.82600  58.44500  9.64300   1.000 85.27033  ?  1807 GLU   B OE1 1 
ATOM   27706 O  OE2 . GLU   B 1 1809 ? 121.81200  56.61100  10.84400  1.000 104.43200 ?  1807 GLU   B OE2 1 
ATOM   27707 N  N   . ASN   B 1 1810 ? 125.54900  61.58300  11.62200  1.000 62.55663  ?  1808 ASN   B N   1 
ATOM   27708 C  CA  . ASN   B 1 1810 ? 126.84700  62.16800  11.92500  1.000 66.92101  ?  1808 ASN   B CA  1 
ATOM   27709 C  C   . ASN   B 1 1810 ? 126.97000  63.54800  11.29000  1.000 60.58741  ?  1808 ASN   B C   1 
ATOM   27710 O  O   . ASN   B 1 1810 ? 126.32100  63.85100  10.28500  1.000 65.65378  ?  1808 ASN   B O   1 
ATOM   27711 C  CB  . ASN   B 1 1810 ? 127.98300  61.26900  11.43300  1.000 71.86723  ?  1808 ASN   B CB  1 
ATOM   27712 C  CG  . ASN   B 1 1810 ? 127.72500  59.80300  11.70700  1.000 84.03295  ?  1808 ASN   B CG  1 
ATOM   27713 O  OD1 . ASN   B 1 1810 ? 126.62500  59.30300  11.47300  1.000 92.39857  ?  1808 ASN   B OD1 1 
ATOM   27714 N  ND2 . ASN   B 1 1810 ? 128.73700  59.10600  12.21000  1.000 82.87317  ?  1808 ASN   B ND2 1 
ATOM   27715 N  N   . LEU   B 1 1811 ? 127.82000  64.38000  11.88700  1.000 52.84503  ?  1809 LEU   B N   1 
ATOM   27716 C  CA  . LEU   B 1 1811 ? 128.00600  65.76000  11.45000  1.000 39.66799  ?  1809 LEU   B CA  1 
ATOM   27717 C  C   . LEU   B 1 1811 ? 129.48200  66.10700  11.54100  1.000 40.61609  ?  1809 LEU   B C   1 
ATOM   27718 O  O   . LEU   B 1 1811 ? 130.05300  66.11000  12.63700  1.000 65.30586  ?  1809 LEU   B O   1 
ATOM   27719 C  CB  . LEU   B 1 1811 ? 127.17800  66.72200  12.30500  1.000 42.67382  ?  1809 LEU   B CB  1 
ATOM   27720 C  CG  . LEU   B 1 1811 ? 126.54300  67.88600  11.55100  1.000 44.92958  ?  1809 LEU   B CG  1 
ATOM   27721 C  CD1 . LEU   B 1 1811 ? 125.36300  67.40600  10.72100  1.000 35.05296  ?  1809 LEU   B CD1 1 
ATOM   27722 C  CD2 . LEU   B 1 1811 ? 126.12800  68.98300  12.51100  1.000 43.74616  ?  1809 LEU   B CD2 1 
ATOM   27723 N  N   . TYR   B 1 1812 ? 130.09500  66.40200  10.39800  1.000 42.44864  ?  1810 TYR   B N   1 
ATOM   27724 C  CA  . TYR   B 1 1812 ? 131.51600  66.71800  10.31700  1.000 47.72810  ?  1810 TYR   B CA  1 
ATOM   27725 C  C   . TYR   B 1 1812 ? 131.67900  68.18600  9.94100   1.000 39.68937  ?  1810 TYR   B C   1 
ATOM   27726 O  O   . TYR   B 1 1812 ? 131.24800  68.60600  8.86200   1.000 56.06819  ?  1810 TYR   B O   1 
ATOM   27727 C  CB  . TYR   B 1 1812 ? 132.21600  65.80600  9.30700   1.000 32.54010  ?  1810 TYR   B CB  1 
ATOM   27728 C  CG  . TYR   B 1 1812 ? 132.19200  64.34000  9.69900   1.000 30.53175  ?  1810 TYR   B CG  1 
ATOM   27729 C  CD1 . TYR   B 1 1812 ? 131.13200  63.51700  9.33500   1.000 45.05045  ?  1810 TYR   B CD1 1 
ATOM   27730 C  CD2 . TYR   B 1 1812 ? 133.22500  63.78300  10.44300  1.000 38.92303  ?  1810 TYR   B CD2 1 
ATOM   27731 C  CE1 . TYR   B 1 1812 ? 131.10500  62.17900  9.69800   1.000 48.25433  ?  1810 TYR   B CE1 1 
ATOM   27732 C  CE2 . TYR   B 1 1812 ? 133.20600  62.44800  10.80900  1.000 42.57244  ?  1810 TYR   B CE2 1 
ATOM   27733 C  CZ  . TYR   B 1 1812 ? 132.14500  61.65100  10.43500  1.000 51.80398  ?  1810 TYR   B CZ  1 
ATOM   27734 O  OH  . TYR   B 1 1812 ? 132.12800  60.32400  10.80000  1.000 75.22493  ?  1810 TYR   B OH  1 
ATOM   27735 N  N   . PHE   B 1 1813 ? 132.29900  68.95500  10.83200  1.000 41.81343  ?  1811 PHE   B N   1 
ATOM   27736 C  CA  . PHE   B 1 1813 ? 132.43800  70.39700  10.69500  1.000 49.94952  ?  1811 PHE   B CA  1 
ATOM   27737 C  C   . PHE   B 1 1813 ? 133.73300  70.76900  9.97800   1.000 55.01822  ?  1811 PHE   B C   1 
ATOM   27738 O  O   . PHE   B 1 1813 ? 134.71400  70.02000  9.97300   1.000 49.01349  ?  1811 PHE   B O   1 
ATOM   27739 C  CB  . PHE   B 1 1813 ? 132.39500  71.07600  12.06800  1.000 56.79657  ?  1811 PHE   B CB  1 
ATOM   27740 C  CG  . PHE   B 1 1813 ? 131.05000  71.64300  12.42300  1.000 54.56109  ?  1811 PHE   B CG  1 
ATOM   27741 C  CD1 . PHE   B 1 1813 ? 130.07600  70.84600  13.00300  1.000 54.89654  ?  1811 PHE   B CD1 1 
ATOM   27742 C  CD2 . PHE   B 1 1813 ? 130.76000  72.97400  12.17400  1.000 53.90648  ?  1811 PHE   B CD2 1 
ATOM   27743 C  CE1 . PHE   B 1 1813 ? 128.83500  71.36900  13.33000  1.000 65.99320  ?  1811 PHE   B CE1 1 
ATOM   27744 C  CE2 . PHE   B 1 1813 ? 129.52200  73.50300  12.50000  1.000 62.60942  ?  1811 PHE   B CE2 1 
ATOM   27745 C  CZ  . PHE   B 1 1813 ? 128.55900  72.69800  13.07700  1.000 66.89015  ?  1811 PHE   B CZ  1 
ATOM   27746 N  N   . GLN   B 1 1814 ? 133.71800  71.95000  9.36800   1.000 63.79627  ?  1812 GLN   B N   1 
ATOM   27747 C  CA  . GLN   B 1 1814 ? 134.88900  72.50400  8.69800   1.000 72.66574  ?  1812 GLN   B CA  1 
ATOM   27748 C  C   . GLN   B 1 1814 ? 135.05400  73.97400  9.07100   1.000 75.37369  ?  1812 GLN   B C   1 
ATOM   27749 O  O   . GLN   B 1 1814 ? 134.07500  74.67500  9.32800   1.000 76.69534  ?  1812 GLN   B O   1 
ATOM   27750 C  CB  . GLN   B 1 1814 ? 134.77100  72.36200  7.17900   1.000 60.34107  ?  1812 GLN   B CB  1 
ATOM   27751 C  CG  . GLN   B 1 1814 ? 134.26700  71.01100  6.70800   1.000 63.89030  ?  1812 GLN   B CG  1 
ATOM   27752 C  CD  . GLN   B 1 1814 ? 133.86700  71.02800  5.24900   1.000 71.78524  ?  1812 GLN   B CD  1 
ATOM   27753 O  OE1 . GLN   B 1 1814 ? 134.42200  71.78400  4.45100   1.000 49.72773  ?  1812 GLN   B OE1 1 
ATOM   27754 N  NE2 . GLN   B 1 1814 ? 132.89100  70.20200  4.89300   1.000 74.78533  ?  1812 GLN   B NE2 1 
ATOM   27755 O  OXT . GLN   B 1 1814 ? 136.16500  74.50000  9.11800   1.000 69.84037  ?  1812 GLN   B OXT 1 
HETATM 27756 C  C1  . GOL   C 2 .    ? 7.53700    90.75600  46.88300  1.000 57.58761  ?  1901 GOL   A C1  1 
HETATM 27757 O  O1  . GOL   C 2 .    ? 6.26100    90.57700  47.49100  1.000 55.25803  ?  1901 GOL   A O1  1 
HETATM 27758 C  C2  . GOL   C 2 .    ? 8.65800    90.62600  47.89200  1.000 51.22983  ?  1901 GOL   A C2  1 
HETATM 27759 O  O2  . GOL   C 2 .    ? 8.46000    91.54100  48.96900  1.000 55.63971  ?  1901 GOL   A O2  1 
HETATM 27760 C  C3  . GOL   C 2 .    ? 10.03500   90.80900  47.29100  1.000 48.32860  ?  1901 GOL   A C3  1 
HETATM 27761 O  O3  . GOL   C 2 .    ? 10.32900   89.80200  46.32700  1.000 54.34469  ?  1901 GOL   A O3  1 
HETATM 27762 C  C1  . GOL   D 2 .    ? -18.71100  94.73500  25.53700  1.000 68.68361  ?  1902 GOL   A C1  1 
HETATM 27763 O  O1  . GOL   D 2 .    ? -19.73000  94.52500  26.51000  1.000 55.71709  ?  1902 GOL   A O1  1 
HETATM 27764 C  C2  . GOL   D 2 .    ? -17.63500  93.67200  25.61700  1.000 65.43626  ?  1902 GOL   A C2  1 
HETATM 27765 O  O2  . GOL   D 2 .    ? -16.91000  93.78700  26.84100  1.000 40.41505  ?  1902 GOL   A O2  1 
HETATM 27766 C  C3  . GOL   D 2 .    ? -18.16900  92.26500  25.45400  1.000 39.30067  ?  1902 GOL   A C3  1 
HETATM 27767 O  O3  . GOL   D 2 .    ? -19.11700  91.94800  26.47000  1.000 47.53234  ?  1902 GOL   A O3  1 
HETATM 27768 C  C10 . A1AMN E 3 .    ? -54.97700  73.65600  -4.93300  1.000 80.28585  ?  1904 A1AMN A C10 1 
HETATM 27769 C  C11 . A1AMN E 3 .    ? -59.08100  63.24400  -12.34400 1.000 89.10907  ?  1904 A1AMN A C11 1 
HETATM 27770 C  C12 . A1AMN E 3 .    ? -59.78900  61.91000  -12.61900 1.000 94.31704  ?  1904 A1AMN A C12 1 
HETATM 27771 C  C14 . A1AMN E 3 .    ? -60.20800  61.76300  -14.08700 1.000 84.50698  ?  1904 A1AMN A C14 1 
HETATM 27772 C  C15 . A1AMN E 3 .    ? -61.60900  62.33800  -14.28100 1.000 78.14002  ?  1904 A1AMN A C15 1 
HETATM 27773 C  C16 . A1AMN E 3 .    ? -60.20200  60.28300  -14.44400 1.000 83.89583  ?  1904 A1AMN A C16 1 
HETATM 27774 C  C02 . A1AMN E 3 .    ? -55.44200  70.13100  -5.81200  1.000 79.63466  ?  1904 A1AMN A C02 1 
HETATM 27775 C  C04 . A1AMN E 3 .    ? -56.59700  69.17100  -7.83900  1.000 58.13438  ?  1904 A1AMN A C04 1 
HETATM 27776 C  C05 . A1AMN E 3 .    ? -55.83800  67.85200  -8.00500  1.000 69.62560  ?  1904 A1AMN A C05 1 
HETATM 27777 C  C07 . A1AMN E 3 .    ? -56.50600  66.16800  -9.77100  1.000 76.54291  ?  1904 A1AMN A C07 1 
HETATM 27778 C  C08 . A1AMN E 3 .    ? -57.45600  65.06700  -10.28600 1.000 67.53322  ?  1904 A1AMN A C08 1 
HETATM 27779 C  C09 . A1AMN E 3 .    ? -56.97900  64.47700  -11.63100 1.000 78.85417  ?  1904 A1AMN A C09 1 
HETATM 27780 C  C22 . A1AMN E 3 .    ? -59.23600  62.50700  -14.99900 1.000 75.62725  ?  1904 A1AMN A C22 1 
HETATM 27781 C  C25 . A1AMN E 3 .    ? -54.53400  71.18000  -5.17800  1.000 79.26576  ?  1904 A1AMN A C25 1 
HETATM 27782 C  C26 . A1AMN E 3 .    ? -56.12900  74.16600  -2.77500  1.000 80.09137  ?  1904 A1AMN A C26 1 
HETATM 27783 C  C27 . A1AMN E 3 .    ? -56.89800  73.13600  -1.94400  1.000 58.44873  ?  1904 A1AMN A C27 1 
HETATM 27784 C  C28 . A1AMN E 3 .    ? -55.78800  75.40400  -1.96100  1.000 68.35320  ?  1904 A1AMN A C28 1 
HETATM 27785 C  C30 . A1AMN E 3 .    ? -52.86400  73.48900  -1.91200  1.000 84.29644  ?  1904 A1AMN A C30 1 
HETATM 27786 C  C50 . A1AMN E 3 .    ? -54.88700  73.52400  -3.41200  1.000 97.63381  ?  1904 A1AMN A C50 1 
HETATM 27787 N  N03 . A1AMN E 3 .    ? -55.72100  70.17600  -7.25100  1.000 69.39622  ?  1904 A1AMN A N03 1 
HETATM 27788 N  N06 . A1AMN E 3 .    ? -56.75400  66.80700  -8.47700  1.000 74.55753  ?  1904 A1AMN A N06 1 
HETATM 27789 N  N10 . A1AMN E 3 .    ? -57.68700  63.22600  -11.91100 1.000 88.41719  ?  1904 A1AMN A N10 1 
HETATM 27790 N  N29 . A1AMN E 3 .    ? -54.79600  72.47200  -5.78000  1.000 74.70632  ?  1904 A1AMN A N29 1 
HETATM 27791 N  N30 . A1AMN E 3 .    ? -53.67700  74.15900  -2.92500  1.000 91.90657  ?  1904 A1AMN A N30 1 
HETATM 27792 O  O01 . A1AMN E 3 .    ? -55.92400  69.28700  -5.13900  1.000 75.16595  ?  1904 A1AMN A O01 1 
HETATM 27793 O  O02 . A1AMN E 3 .    ? -55.19200  74.71000  -5.42500  1.000 65.76541  ?  1904 A1AMN A O02 1 
HETATM 27794 O  O13 . A1AMN E 3 .    ? -58.92100  60.86400  -12.28200 1.000 101.39168 ?  1904 A1AMN A O13 1 
HETATM 27795 O  O17 . A1AMN E 3 .    ? -61.52700  59.81700  -14.49700 1.000 94.12165  ?  1904 A1AMN A O17 1 
HETATM 27796 O  O19 . A1AMN E 3 .    ? -61.25000  59.17600  -11.88500 1.000 93.72426  ?  1904 A1AMN A O19 1 
HETATM 27797 O  O21 . A1AMN E 3 .    ? -62.13000  57.50700  -13.59100 1.000 83.83987  ?  1904 A1AMN A O21 1 
HETATM 27798 O  O23 . A1AMN E 3 .    ? -59.65700  64.27100  -12.46500 1.000 78.65627  ?  1904 A1AMN A O23 1 
HETATM 27799 O  O24 . A1AMN E 3 .    ? -55.56900  66.49500  -10.42100 1.000 91.08040  ?  1904 A1AMN A O24 1 
HETATM 27800 O  O31 . A1AMN E 3 .    ? -53.19500  72.43000  -1.48900  1.000 76.17965  ?  1904 A1AMN A O31 1 
HETATM 27801 P  P18 . A1AMN E 3 .    ? -62.14000  58.94600  -13.24300 1.000 84.26810  ?  1904 A1AMN A P18 1 
HETATM 27802 C  C1  . GOL   F 2 .    ? 101.50000  60.78800  18.08300  1.000 83.33879  ?  1901 GOL   B C1  1 
HETATM 27803 O  O1  . GOL   F 2 .    ? 101.75600  59.39100  17.97500  1.000 83.62021  ?  1901 GOL   B O1  1 
HETATM 27804 C  C2  . GOL   F 2 .    ? 102.52900  61.47600  18.95500  1.000 84.09620  ?  1901 GOL   B C2  1 
HETATM 27805 O  O2  . GOL   F 2 .    ? 102.44900  60.98400  20.29300  1.000 85.65577  ?  1901 GOL   B O2  1 
HETATM 27806 C  C3  . GOL   F 2 .    ? 103.94500  61.34800  18.43400  1.000 86.04312  ?  1901 GOL   B C3  1 
HETATM 27807 O  O3  . GOL   F 2 .    ? 104.35500  59.98600  18.35400  1.000 66.65224  ?  1901 GOL   B O3  1 
HETATM 27808 MN MN  . MN    G 4 .    ? 44.26500   90.95900  -38.28500 1.000 117.80141 ?  1903 MN    B MN  1 
HETATM 27809 O  O   . HOH   H 5 .    ? -46.07100  102.66200 -19.73100 1.000 34.80703  ?  2001 HOH   A O   1 
HETATM 27810 O  O   . HOH   H 5 .    ? -25.688    96.552    50.314    1.000 46.46707  ?  2002 HOH   A O   1 
HETATM 27811 O  O   . HOH   H 5 .    ? -77.86000  63.69100  21.31300  1.000 57.77398  ?  2003 HOH   A O   1 
HETATM 27812 O  O   . HOH   H 5 .    ? -16.76300  101.85000 54.70500  1.000 34.02734  ?  2004 HOH   A O   1 
HETATM 27813 O  O   . HOH   H 5 .    ? -44.11000  74.51400  17.37100  1.000 45.02127  ?  2005 HOH   A O   1 
HETATM 27814 O  O   . HOH   H 5 .    ? -11.23200  85.80000  2.28700   1.000 66.69089  ?  2006 HOH   A O   1 
HETATM 27815 O  O   . HOH   H 5 .    ? -55.160    61.447    14.535    1.000 55.64329  ?  2007 HOH   A O   1 
HETATM 27816 O  O   . HOH   H 5 .    ? -31.70900  95.76400  -28.03500 1.000 50.59818  ?  2008 HOH   A O   1 
HETATM 27817 O  O   . HOH   H 5 .    ? -50.87900  82.01600  -3.61700  1.000 53.60149  ?  2009 HOH   A O   1 
HETATM 27818 O  O   . HOH   H 5 .    ? -110.17800 60.78500  -3.87100  1.000 45.42308  ?  2010 HOH   A O   1 
HETATM 27819 O  O   . HOH   H 5 .    ? -64.69900  67.24300  -19.61500 1.000 50.74024  ?  2011 HOH   A O   1 
HETATM 27820 O  O   . HOH   H 5 .    ? -71.57600  68.08100  -18.44400 1.000 47.94206  ?  2012 HOH   A O   1 
HETATM 27821 O  O   . HOH   H 5 .    ? -74.64300  64.11900  1.62700   1.000 46.78595  ?  2013 HOH   A O   1 
HETATM 27822 O  O   . HOH   H 5 .    ? -72.30500  77.40400  5.03300   1.000 43.09677  ?  2014 HOH   A O   1 
HETATM 27823 O  O   . HOH   H 5 .    ? -27.49700  55.56700  -2.49600  1.000 49.21185  ?  2015 HOH   A O   1 
HETATM 27824 O  O   . HOH   H 5 .    ? -24.03400  99.08100  -23.20500 1.000 34.98987  ?  2016 HOH   A O   1 
HETATM 27825 O  O   . HOH   H 5 .    ? -32.12700  4.85300   4.50300   1.000 44.09355  ?  2017 HOH   A O   1 
HETATM 27826 O  O   . HOH   H 5 .    ? 4.70800    97.21500  56.17700  1.000 33.37506  ?  2018 HOH   A O   1 
HETATM 27827 O  O   . HOH   H 5 .    ? -36.11900  13.42600  -2.17500  1.000 43.35569  ?  2019 HOH   A O   1 
HETATM 27828 O  O   . HOH   H 5 .    ? -9.65700   77.89000  40.33300  1.000 32.07542  ?  2020 HOH   A O   1 
HETATM 27829 O  O   . HOH   H 5 .    ? -37.39200  72.87800  20.04400  1.000 44.05831  ?  2021 HOH   A O   1 
HETATM 27830 O  O   . HOH   H 5 .    ? -6.89700   90.95000  28.74100  1.000 35.74855  ?  2022 HOH   A O   1 
HETATM 27831 O  O   . HOH   H 5 .    ? -22.90400  5.45500   18.70900  1.000 39.45561  ?  2023 HOH   A O   1 
HETATM 27832 O  O   . HOH   H 5 .    ? -40.55300  73.55900  16.46100  1.000 51.27543  ?  2024 HOH   A O   1 
HETATM 27833 O  O   . HOH   H 5 .    ? -38.87200  95.32800  16.43400  1.000 56.48415  ?  2025 HOH   A O   1 
HETATM 27834 O  O   . HOH   H 5 .    ? -24.69600  87.91300  13.81200  1.000 29.07368  ?  2026 HOH   A O   1 
HETATM 27835 O  O   . HOH   H 5 .    ? -45.44700  87.77300  2.50500   1.000 49.77190  ?  2027 HOH   A O   1 
HETATM 27836 O  O   . HOH   H 5 .    ? -68.48900  48.06700  37.20200  1.000 40.94669  ?  2028 HOH   A O   1 
HETATM 27837 O  O   . HOH   H 5 .    ? -58.17800  56.18500  16.56500  1.000 53.98207  ?  2029 HOH   A O   1 
HETATM 27838 O  O   . HOH   H 5 .    ? -17.19700  27.79700  17.43400  1.000 49.33247  ?  2030 HOH   A O   1 
HETATM 27839 O  O   . HOH   H 5 .    ? -50.98700  73.31600  1.63500   1.000 43.05025  ?  2031 HOH   A O   1 
HETATM 27840 O  O   . HOH   H 5 .    ? -64.74000  41.37700  27.96900  1.000 47.87427  ?  2032 HOH   A O   1 
HETATM 27841 O  O   . HOH   H 5 .    ? -31.07100  30.01900  -0.88700  1.000 42.72703  ?  2033 HOH   A O   1 
HETATM 27842 O  O   . HOH   H 5 .    ? -24.92900  24.61200  -4.70700  1.000 35.67746  ?  2034 HOH   A O   1 
HETATM 27843 O  O   . HOH   H 5 .    ? -21.03800  85.92100  11.39400  1.000 35.41615  ?  2035 HOH   A O   1 
HETATM 27844 O  O   . HOH   H 5 .    ? -37.82100  86.62800  0.66600   1.000 43.08458  ?  2036 HOH   A O   1 
HETATM 27845 O  O   . HOH   H 5 .    ? -79.29600  66.00000  24.86900  1.000 49.86768  ?  2037 HOH   A O   1 
HETATM 27846 O  O   . HOH   H 5 .    ? -36.69300  92.34100  14.63800  1.000 55.00942  ?  2038 HOH   A O   1 
HETATM 27847 O  O   . HOH   H 5 .    ? 7.09100    84.55600  23.10600  1.000 52.17294  ?  2039 HOH   A O   1 
HETATM 27848 O  O   . HOH   H 5 .    ? -24.63700  15.51700  -9.18400  1.000 39.73414  ?  2040 HOH   A O   1 
HETATM 27849 O  O   . HOH   H 5 .    ? -13.07200  86.40200  -7.78200  1.000 61.25945  ?  2041 HOH   A O   1 
HETATM 27850 O  O   . HOH   H 5 .    ? -21.47100  23.35700  12.45500  1.000 41.28762  ?  2042 HOH   A O   1 
HETATM 27851 O  O   . HOH   H 5 .    ? -31.92700  52.92200  4.24800   1.000 53.94793  ?  2043 HOH   A O   1 
HETATM 27852 O  O   . HOH   H 5 .    ? -52.56600  49.78600  23.64200  1.000 62.83764  ?  2044 HOH   A O   1 
HETATM 27853 O  O   . HOH   H 5 .    ? -83.33200  65.89900  32.22900  1.000 52.18757  ?  2045 HOH   A O   1 
HETATM 27854 O  O   . HOH   H 5 .    ? -20.79800  4.26100   -2.81000  1.000 52.42743  ?  2046 HOH   A O   1 
HETATM 27855 O  O   . HOH   H 5 .    ? -51.23800  92.08800  4.45600   1.000 49.04426  ?  2047 HOH   A O   1 
HETATM 27856 O  O   . HOH   H 5 .    ? -52.78200  87.60500  -16.08200 1.000 58.12043  ?  2048 HOH   A O   1 
HETATM 27857 O  O   . HOH   H 5 .    ? -17.73500  104.82500 33.63200  1.000 40.83143  ?  2049 HOH   A O   1 
HETATM 27858 O  O   . HOH   H 5 .    ? -57.43100  52.98400  22.44200  1.000 42.70708  ?  2050 HOH   A O   1 
HETATM 27859 O  O   . HOH   H 5 .    ? -4.10600   80.67600  41.29000  1.000 34.49705  ?  2051 HOH   A O   1 
HETATM 27860 O  O   . HOH   H 5 .    ? -45.10600  85.38900  38.36300  1.000 61.37505  ?  2052 HOH   A O   1 
HETATM 27861 O  O   . HOH   H 5 .    ? -21.67800  73.79500  -6.57200  1.000 37.90526  ?  2053 HOH   A O   1 
HETATM 27862 O  O   . HOH   H 5 .    ? -6.69400   94.55100  8.07600   1.000 54.69947  ?  2054 HOH   A O   1 
HETATM 27863 O  O   . HOH   H 5 .    ? -19.56600  110.29400 53.92200  1.000 51.87371  ?  2055 HOH   A O   1 
HETATM 27864 O  O   . HOH   H 5 .    ? -21.67100  87.49600  33.74200  1.000 52.21527  ?  2056 HOH   A O   1 
HETATM 27865 O  O   . HOH   H 5 .    ? -3.99000   30.30700  -5.78500  1.000 47.17432  ?  2057 HOH   A O   1 
HETATM 27866 O  O   . HOH   H 5 .    ? -20.11200  86.68500  15.84300  1.000 39.68792  ?  2058 HOH   A O   1 
HETATM 27867 O  O   . HOH   H 5 .    ? -29.23000  77.98000  28.33900  1.000 41.65260  ?  2059 HOH   A O   1 
HETATM 27868 O  O   . HOH   H 5 .    ? -54.41600  74.05400  18.77600  1.000 37.54079  ?  2060 HOH   A O   1 
HETATM 27869 O  O   . HOH   H 5 .    ? -55.90500  94.47400  -28.29500 1.000 55.54879  ?  2061 HOH   A O   1 
HETATM 27870 O  O   . HOH   H 5 .    ? -41.19400  82.98300  2.20900   1.000 48.65469  ?  2062 HOH   A O   1 
HETATM 27871 O  O   . HOH   H 5 .    ? -57.56000  61.82100  -8.11700  1.000 50.92892  ?  2063 HOH   A O   1 
HETATM 27872 O  O   . HOH   H 5 .    ? -57.61000  78.97300  -33.44400 1.000 56.14786  ?  2064 HOH   A O   1 
HETATM 27873 O  O   . HOH   H 5 .    ? -66.89400  80.97600  25.66200  1.000 39.87064  ?  2065 HOH   A O   1 
HETATM 27874 O  O   . HOH   H 5 .    ? -43.09600  77.74300  34.09300  1.000 40.83073  ?  2066 HOH   A O   1 
HETATM 27875 O  O   . HOH   H 5 .    ? 3.07100    81.71200  14.03200  1.000 46.43285  ?  2067 HOH   A O   1 
HETATM 27876 O  O   . HOH   H 5 .    ? -39.51500  37.70300  -6.42400  1.000 62.70551  ?  2068 HOH   A O   1 
HETATM 27877 O  O   . HOH   H 5 .    ? -18.66200  82.03200  5.70800   1.000 42.83037  ?  2069 HOH   A O   1 
HETATM 27878 O  O   . HOH   H 5 .    ? -11.15000  44.63300  -9.09900  1.000 51.59332  ?  2070 HOH   A O   1 
HETATM 27879 O  O   . HOH   H 5 .    ? -17.04500  75.04800  -9.70300  1.000 33.06362  ?  2071 HOH   A O   1 
HETATM 27880 O  O   . HOH   H 5 .    ? -28.23100  83.36100  2.68200   1.000 33.28455  ?  2072 HOH   A O   1 
HETATM 27881 O  O   . HOH   H 5 .    ? -45.48200  54.59500  -7.43200  1.000 52.87429  ?  2073 HOH   A O   1 
HETATM 27882 O  O   . HOH   H 5 .    ? -20.43400  6.53800   20.26900  1.000 43.10420  ?  2074 HOH   A O   1 
HETATM 27883 O  O   . HOH   H 5 .    ? -21.51500  64.11500  -4.16100  1.000 44.43832  ?  2075 HOH   A O   1 
HETATM 27884 O  O   . HOH   H 5 .    ? -27.27600  76.15800  26.39800  1.000 44.51730  ?  2076 HOH   A O   1 
HETATM 27885 O  O   . HOH   H 5 .    ? -62.92400  71.93000  35.31200  1.000 53.53547  ?  2077 HOH   A O   1 
HETATM 27886 O  O   . HOH   H 5 .    ? -22.17400  13.08400  -3.70800  1.000 33.16009  ?  2078 HOH   A O   1 
HETATM 27887 O  O   . HOH   H 5 .    ? -37.76800  50.40100  -8.27200  1.000 44.21298  ?  2079 HOH   A O   1 
HETATM 27888 O  O   . HOH   H 5 .    ? -27.08700  39.43900  11.66000  1.000 56.72159  ?  2080 HOH   A O   1 
HETATM 27889 O  O   . HOH   H 5 .    ? -37.60800  69.57700  34.70900  1.000 39.90027  ?  2081 HOH   A O   1 
HETATM 27890 O  O   . HOH   H 5 .    ? 4.96400    83.83100  45.73700  1.000 37.07518  ?  2082 HOH   A O   1 
HETATM 27891 O  O   . HOH   H 5 .    ? -26.90900  62.31100  6.32300   1.000 60.52479  ?  2083 HOH   A O   1 
HETATM 27892 O  O   . HOH   H 5 .    ? -21.38300  24.57200  -5.98900  1.000 41.68666  ?  2084 HOH   A O   1 
HETATM 27893 O  O   . HOH   H 5 .    ? -16.57500  74.95800  25.88000  1.000 45.53913  ?  2085 HOH   A O   1 
HETATM 27894 O  O   . HOH   H 5 .    ? -12.52300  41.64000  6.08700   1.000 43.67254  ?  2086 HOH   A O   1 
HETATM 27895 O  O   . HOH   H 5 .    ? -47.45200  80.30600  -7.50200  1.000 41.23798  ?  2087 HOH   A O   1 
HETATM 27896 O  O   . HOH   H 5 .    ? -26.82000  30.53900  -3.87500  1.000 49.49845  ?  2088 HOH   A O   1 
HETATM 27897 O  O   . HOH   H 5 .    ? -51.94700  67.49200  34.24900  1.000 47.97850  ?  2089 HOH   A O   1 
HETATM 27898 O  O   . HOH   H 5 .    ? -2.46400   92.30100  56.58000  1.000 41.91362  ?  2090 HOH   A O   1 
HETATM 27899 O  O   . HOH   H 5 .    ? -75.19400  87.98500  -15.37700 1.000 44.28983  ?  2091 HOH   A O   1 
HETATM 27900 O  O   . HOH   H 5 .    ? 1.54200    84.89800  52.57200  1.000 45.80098  ?  2092 HOH   A O   1 
HETATM 27901 O  O   . HOH   H 5 .    ? -44.01400  81.50400  17.41000  1.000 38.14216  ?  2093 HOH   A O   1 
HETATM 27902 O  O   . HOH   H 5 .    ? -50.42600  60.49700  28.88900  1.000 50.20287  ?  2094 HOH   A O   1 
HETATM 27903 O  O   . HOH   H 5 .    ? -54.41200  81.04100  -24.47700 1.000 54.67326  ?  2095 HOH   A O   1 
HETATM 27904 O  O   . HOH   H 5 .    ? -19.56700  26.25300  -22.00500 1.000 54.82501  ?  2096 HOH   A O   1 
HETATM 27905 O  O   . HOH   H 5 .    ? -23.27000  69.36900  -21.71200 1.000 55.14480  ?  2097 HOH   A O   1 
HETATM 27906 O  O   . HOH   H 5 .    ? -7.08500   42.98500  -8.70200  1.000 68.09522  ?  2098 HOH   A O   1 
HETATM 27907 O  O   . HOH   H 5 .    ? -27.94000  4.74800   8.02800   1.000 34.44452  ?  2099 HOH   A O   1 
HETATM 27908 O  O   . HOH   H 5 .    ? -60.08100  59.95000  -9.01900  1.000 46.84172  ?  2100 HOH   A O   1 
HETATM 27909 O  O   . HOH   H 5 .    ? -37.55100  69.35000  8.39800   1.000 42.69809  ?  2101 HOH   A O   1 
HETATM 27910 O  O   . HOH   H 5 .    ? -27.61300  65.64900  4.83100   1.000 32.83488  ?  2102 HOH   A O   1 
HETATM 27911 O  O   . HOH   H 5 .    ? -12.62200  -0.40500  -0.26900  1.000 51.14971  ?  2103 HOH   A O   1 
HETATM 27912 O  O   . HOH   H 5 .    ? -56.35500  76.04500  26.15000  1.000 47.12602  ?  2104 HOH   A O   1 
HETATM 27913 O  O   . HOH   H 5 .    ? -30.92100  80.50400  7.73800   1.000 46.76001  ?  2105 HOH   A O   1 
HETATM 27914 O  O   . HOH   H 5 .    ? -60.27200  66.98900  33.97300  1.000 41.00536  ?  2106 HOH   A O   1 
HETATM 27915 O  O   . HOH   H 5 .    ? -0.30800   90.76500  52.72600  1.000 36.94125  ?  2107 HOH   A O   1 
HETATM 27916 O  O   . HOH   H 5 .    ? -42.67200  27.13600  -8.01400  1.000 54.76672  ?  2108 HOH   A O   1 
HETATM 27917 O  O   . HOH   H 5 .    ? -22.10200  98.28300  18.54800  1.000 42.93547  ?  2109 HOH   A O   1 
HETATM 27918 O  O   . HOH   H 5 .    ? -18.29300  71.76400  -4.59100  1.000 55.15552  ?  2110 HOH   A O   1 
HETATM 27919 O  O   . HOH   H 5 .    ? -40.48900  105.48400 -34.99400 1.000 46.17094  ?  2111 HOH   A O   1 
HETATM 27920 O  O   . HOH   H 5 .    ? -26.30400  73.21400  26.52800  1.000 38.02204  ?  2112 HOH   A O   1 
HETATM 27921 O  O   . HOH   H 5 .    ? -32.03400  84.09800  -29.50500 1.000 45.55521  ?  2113 HOH   A O   1 
HETATM 27922 O  O   . HOH   H 5 .    ? -75.75800  62.68900  18.12100  1.000 45.35546  ?  2114 HOH   A O   1 
HETATM 27923 O  O   . HOH   H 5 .    ? -18.70000  94.50800  11.37500  1.000 41.21827  ?  2115 HOH   A O   1 
HETATM 27924 O  O   . HOH   H 5 .    ? -14.04900  6.44600   23.41800  1.000 71.30608  ?  2116 HOH   A O   1 
HETATM 27925 O  O   . HOH   H 5 .    ? -22.61600  70.92900  -18.62000 1.000 39.63286  ?  2117 HOH   A O   1 
HETATM 27926 O  O   . HOH   H 5 .    ? -33.88200  79.15600  -22.34500 1.000 41.27220  ?  2118 HOH   A O   1 
HETATM 27927 O  O   . HOH   H 5 .    ? -29.95500  95.28000  -10.63700 1.000 44.56863  ?  2119 HOH   A O   1 
HETATM 27928 O  O   . HOH   H 5 .    ? -4.16800   86.54000  3.05500   1.000 52.94473  ?  2120 HOH   A O   1 
HETATM 27929 O  O   . HOH   H 5 .    ? -77.23800  86.33000  9.99900   1.000 45.77372  ?  2121 HOH   A O   1 
HETATM 27930 O  O   . HOH   H 5 .    ? -75.03300  64.86200  -4.84700  1.000 38.51018  ?  2122 HOH   A O   1 
HETATM 27931 O  O   . HOH   H 5 .    ? -55.46500  61.09600  -10.61200 1.000 57.70906  ?  2123 HOH   A O   1 
HETATM 27932 O  O   . HOH   H 5 .    ? -45.87600  103.05500 -23.23500 1.000 58.70069  ?  2124 HOH   A O   1 
HETATM 27933 O  O   . HOH   H 5 .    ? -19.84900  62.97400  -19.25700 1.000 46.06170  ?  2125 HOH   A O   1 
HETATM 27934 O  O   . HOH   H 5 .    ? -61.197    59.009    5.770     1.000 55.06963  ?  2126 HOH   A O   1 
HETATM 27935 O  O   . HOH   H 5 .    ? -65.93200  67.85300  37.36800  1.000 42.23870  ?  2127 HOH   A O   1 
HETATM 27936 O  O   . HOH   H 5 .    ? -35.21100  95.99200  24.30000  1.000 38.43613  ?  2128 HOH   A O   1 
HETATM 27937 O  O   . HOH   H 5 .    ? 6.43700    97.81500  21.22400  1.000 44.24345  ?  2129 HOH   A O   1 
HETATM 27938 O  O   . HOH   H 5 .    ? -33.59300  99.29900  21.85400  1.000 54.90179  ?  2130 HOH   A O   1 
HETATM 27939 O  O   . HOH   H 5 .    ? -19.48700  83.33000  -10.27200 1.000 44.89128  ?  2131 HOH   A O   1 
HETATM 27940 O  O   . HOH   H 5 .    ? -31.16900  83.69900  7.81200   1.000 47.47839  ?  2132 HOH   A O   1 
HETATM 27941 O  O   . HOH   H 5 .    ? -47.28800  44.86400  2.49400   1.000 51.22964  ?  2133 HOH   A O   1 
HETATM 27942 O  O   . HOH   H 5 .    ? -4.34300   116.48500 29.13200  1.000 48.32994  ?  2134 HOH   A O   1 
HETATM 27943 O  O   . HOH   H 5 .    ? -32.48000  72.93600  5.60000   1.000 47.46474  ?  2135 HOH   A O   1 
HETATM 27944 O  O   . HOH   H 5 .    ? -51.94200  69.15900  -1.02200  1.000 46.50955  ?  2136 HOH   A O   1 
HETATM 27945 O  O   . HOH   H 5 .    ? -54.33100  75.64600  16.00400  1.000 18.62255  ?  2137 HOH   A O   1 
HETATM 27946 O  O   . HOH   H 5 .    ? -2.69700   76.55200  22.39700  1.000 43.99703  ?  2138 HOH   A O   1 
HETATM 27947 O  O   . HOH   H 5 .    ? -33.12900  4.74700   -1.83000  1.000 50.49740  ?  2139 HOH   A O   1 
HETATM 27948 O  O   . HOH   H 5 .    ? -16.90300  37.68900  -17.83900 1.000 46.30715  ?  2140 HOH   A O   1 
HETATM 27949 O  O   . HOH   H 5 .    ? -17.04000  100.78200 -7.86700  1.000 44.58512  ?  2141 HOH   A O   1 
HETATM 27950 O  O   . HOH   H 5 .    ? -3.12800   27.06400  -6.94000  1.000 35.61712  ?  2142 HOH   A O   1 
HETATM 27951 O  O   . HOH   H 5 .    ? 4.67400    104.89200 26.92000  1.000 54.27019  ?  2143 HOH   A O   1 
HETATM 27952 O  O   . HOH   H 5 .    ? -52.84000  76.55600  27.83000  1.000 51.66350  ?  2144 HOH   A O   1 
HETATM 27953 O  O   . HOH   H 5 .    ? -59.76700  51.83500  -9.30000  1.000 45.42061  ?  2145 HOH   A O   1 
HETATM 27954 O  O   . HOH   H 5 .    ? -43.64100  76.01400  -27.17300 1.000 61.67685  ?  2146 HOH   A O   1 
HETATM 27955 O  O   . HOH   H 5 .    ? -55.35600  68.29800  0.59100   1.000 48.54135  ?  2147 HOH   A O   1 
HETATM 27956 O  O   . HOH   H 5 .    ? -35.41700  65.82900  7.88900   1.000 39.12290  ?  2148 HOH   A O   1 
HETATM 27957 O  O   . HOH   H 5 .    ? -17.77800  50.71100  11.94700  1.000 57.13626  ?  2149 HOH   A O   1 
HETATM 27958 O  O   . HOH   H 5 .    ? -47.85400  77.57500  -33.56800 1.000 55.45879  ?  2150 HOH   A O   1 
HETATM 27959 O  O   . HOH   H 5 .    ? -63.37500  69.56800  -24.24400 1.000 50.23561  ?  2151 HOH   A O   1 
HETATM 27960 O  O   . HOH   H 5 .    ? -22.14500  30.64300  -8.64800  1.000 46.40791  ?  2152 HOH   A O   1 
HETATM 27961 O  O   . HOH   H 5 .    ? 3.72700    102.32000 44.72400  1.000 47.51955  ?  2153 HOH   A O   1 
HETATM 27962 O  O   . HOH   H 5 .    ? -30.46600  68.77400  24.95400  1.000 49.98246  ?  2154 HOH   A O   1 
HETATM 27963 O  O   . HOH   H 5 .    ? -23.91200  97.57800  25.87400  1.000 43.17023  ?  2155 HOH   A O   1 
HETATM 27964 O  O   . HOH   H 5 .    ? -50.58500  53.77300  37.24500  1.000 49.88872  ?  2156 HOH   A O   1 
HETATM 27965 O  O   . HOH   H 5 .    ? -33.08700  82.93200  10.43000  1.000 60.19394  ?  2157 HOH   A O   1 
HETATM 27966 O  O   . HOH   H 5 .    ? -64.09100  39.01700  -10.66700 1.000 53.51617  ?  2158 HOH   A O   1 
HETATM 27967 O  O   . HOH   H 5 .    ? -20.59600  68.02200  -4.99500  1.000 59.02566  ?  2159 HOH   A O   1 
HETATM 27968 O  O   . HOH   H 5 .    ? -26.86200  85.49400  -10.90200 1.000 39.20984  ?  2160 HOH   A O   1 
HETATM 27969 O  O   . HOH   H 5 .    ? -52.76400  66.99800  -3.74700  1.000 59.48546  ?  2161 HOH   A O   1 
HETATM 27970 O  O   . HOH   H 5 .    ? -46.26900  41.36100  2.90600   1.000 64.52120  ?  2162 HOH   A O   1 
HETATM 27971 O  O   . HOH   H 5 .    ? -83.99200  86.74000  -19.09600 1.000 56.36274  ?  2163 HOH   A O   1 
HETATM 27972 O  O   . HOH   H 5 .    ? -79.06600  80.20300  -23.40600 1.000 49.47634  ?  2164 HOH   A O   1 
HETATM 27973 O  O   . HOH   H 5 .    ? -54.71600  87.15500  22.91400  1.000 43.41303  ?  2165 HOH   A O   1 
HETATM 27974 O  O   . HOH   H 5 .    ? -34.71500  85.74300  -6.98900  1.000 49.22408  ?  2166 HOH   A O   1 
HETATM 27975 O  O   . HOH   H 5 .    ? -20.75600  44.01500  -12.17600 1.000 52.44657  ?  2167 HOH   A O   1 
HETATM 27976 O  O   . HOH   H 5 .    ? -52.88900  85.87600  18.09400  1.000 52.48932  ?  2168 HOH   A O   1 
HETATM 27977 O  O   . HOH   H 5 .    ? -22.23200  90.78700  19.11800  1.000 29.50411  ?  2169 HOH   A O   1 
HETATM 27978 O  O   . HOH   H 5 .    ? -53.93100  91.45500  -19.33200 1.000 32.00847  ?  2170 HOH   A O   1 
HETATM 27979 O  O   . HOH   H 5 .    ? -19.85700  80.78600  -3.36700  1.000 52.30220  ?  2171 HOH   A O   1 
HETATM 27980 O  O   . HOH   H 5 .    ? -84.81400  49.71300  28.93300  1.000 41.91917  ?  2172 HOH   A O   1 
HETATM 27981 O  O   . HOH   H 5 .    ? -31.33200  31.20600  -4.42500  1.000 35.72017  ?  2173 HOH   A O   1 
HETATM 27982 O  O   . HOH   H 5 .    ? -1.17600   105.89500 -1.41700  1.000 53.19125  ?  2174 HOH   A O   1 
HETATM 27983 O  O   . HOH   H 5 .    ? -21.32000  107.49700 53.63800  1.000 49.35951  ?  2175 HOH   A O   1 
HETATM 27984 O  O   . HOH   H 5 .    ? -0.36900   29.43400  10.74500  1.000 48.21112  ?  2176 HOH   A O   1 
HETATM 27985 O  O   . HOH   H 5 .    ? -21.01800  91.43100  56.93300  1.000 39.05390  ?  2177 HOH   A O   1 
HETATM 27986 O  O   . HOH   H 5 .    ? -13.80400  88.30600  55.87200  1.000 60.02021  ?  2178 HOH   A O   1 
HETATM 27987 O  O   . HOH   H 5 .    ? -39.13000  47.04500  -7.96300  1.000 35.94650  ?  2179 HOH   A O   1 
HETATM 27988 O  O   . HOH   H 5 .    ? -61.63200  87.81000  -31.26000 1.000 57.48743  ?  2180 HOH   A O   1 
HETATM 27989 O  O   . HOH   H 5 .    ? 2.81600    25.56900  9.44600   1.000 44.43213  ?  2181 HOH   A O   1 
HETATM 27990 O  O   . HOH   H 5 .    ? -77.30200  84.38500  16.23700  1.000 42.03895  ?  2182 HOH   A O   1 
HETATM 27991 O  O   . HOH   H 5 .    ? -68.90600  83.98500  -25.48300 1.000 61.05969  ?  2183 HOH   A O   1 
HETATM 27992 O  O   . HOH   H 5 .    ? -37.87800  88.19100  16.30900  1.000 42.94224  ?  2184 HOH   A O   1 
HETATM 27993 O  O   . HOH   H 5 .    ? -32.129    97.506    -4.959    1.000 40.94452  ?  2185 HOH   A O   1 
HETATM 27994 O  O   . HOH   H 5 .    ? -81.02600  35.24800  -11.22100 1.000 54.97043  ?  2186 HOH   A O   1 
HETATM 27995 O  O   . HOH   H 5 .    ? -32.12200  8.52800   19.55000  1.000 44.14056  ?  2187 HOH   A O   1 
HETATM 27996 O  O   . HOH   H 5 .    ? -21.23100  109.76100 -9.55100  1.000 43.33545  ?  2188 HOH   A O   1 
HETATM 27997 O  O   . HOH   H 5 .    ? -23.97500  100.65000 19.15800  1.000 37.52925  ?  2189 HOH   A O   1 
HETATM 27998 O  O   . HOH   I 5 .    ? 47.93200   108.57100 31.36700  1.000 54.73427  ?  2001 HOH   B O   1 
HETATM 27999 O  O   . HOH   I 5 .    ? 66.13500   61.54800  17.70600  1.000 57.18831  ?  2002 HOH   B O   1 
HETATM 28000 O  O   . HOH   I 5 .    ? 92.55300   62.96800  -14.77300 1.000 54.50208  ?  2003 HOH   B O   1 
HETATM 28001 O  O   . HOH   I 5 .    ? 36.91500   63.24500  1.60200   1.000 57.15614  ?  2004 HOH   B O   1 
HETATM 28002 O  O   . HOH   I 5 .    ? 40.18100   79.88400  -8.40500  1.000 43.51694  ?  2005 HOH   B O   1 
HETATM 28003 O  O   . HOH   I 5 .    ? 41.86500   98.88600  14.31400  1.000 45.28305  ?  2006 HOH   B O   1 
HETATM 28004 O  O   . HOH   I 5 .    ? 26.78700   84.40300  -34.07500 1.000 40.30396  ?  2007 HOH   B O   1 
HETATM 28005 O  O   . HOH   I 5 .    ? 33.19000   96.96700  -44.10400 1.000 21.09962  ?  2008 HOH   B O   1 
HETATM 28006 O  O   . HOH   I 5 .    ? 74.79500   73.76200  -24.68400 1.000 34.93527  ?  2009 HOH   B O   1 
HETATM 28007 O  O   . HOH   I 5 .    ? 45.77400   86.52200  29.78100  1.000 47.15724  ?  2010 HOH   B O   1 
HETATM 28008 O  O   . HOH   I 5 .    ? 44.50300   106.67600 -31.76900 1.000 47.58176  ?  2011 HOH   B O   1 
HETATM 28009 O  O   . HOH   I 5 .    ? 19.23100   77.15800  -27.56800 1.000 39.24273  ?  2012 HOH   B O   1 
HETATM 28010 O  O   . HOH   I 5 .    ? 18.73600   3.02000   19.01700  1.000 49.50190  ?  2013 HOH   B O   1 
HETATM 28011 O  O   . HOH   I 5 .    ? 25.39500   94.94800  -23.18500 1.000 23.40749  ?  2014 HOH   B O   1 
HETATM 28012 O  O   . HOH   I 5 .    ? 25.77300   87.82300  -49.59200 1.000 23.63560  ?  2015 HOH   B O   1 
HETATM 28013 O  O   . HOH   I 5 .    ? 42.99200   91.62300  18.26800  1.000 48.53050  ?  2016 HOH   B O   1 
HETATM 28014 O  O   . HOH   I 5 .    ? 11.91200   83.75700  -41.53900 1.000 37.42996  ?  2017 HOH   B O   1 
HETATM 28015 O  O   . HOH   I 5 .    ? 32.30600   5.53500   10.49500  1.000 55.83490  ?  2018 HOH   B O   1 
HETATM 28016 O  O   . HOH   I 5 .    ? 8.65300    18.84000  15.21800  1.000 53.22072  ?  2019 HOH   B O   1 
HETATM 28017 O  O   . HOH   I 5 .    ? 9.45100    18.78700  18.55700  1.000 58.79165  ?  2020 HOH   B O   1 
HETATM 28018 O  O   . HOH   I 5 .    ? 83.46600   72.36600  -17.02600 1.000 41.18377  ?  2021 HOH   B O   1 
HETATM 28019 O  O   . HOH   I 5 .    ? 53.50700   73.82700  -14.63500 1.000 27.91886  ?  2022 HOH   B O   1 
HETATM 28020 O  O   . HOH   I 5 .    ? 39.748     97.165    24.910    1.000 52.97513  ?  2023 HOH   B O   1 
HETATM 28021 O  O   . HOH   I 5 .    ? 44.888     99.454    -45.633   1.000 41.06902  ?  2024 HOH   B O   1 
HETATM 28022 O  O   . HOH   I 5 .    ? 85.33800   73.40700  -36.36600 1.000 51.01042  ?  2025 HOH   B O   1 
HETATM 28023 O  O   . HOH   I 5 .    ? 52.98700   76.64500  -9.62800  1.000 39.30838  ?  2026 HOH   B O   1 
HETATM 28024 O  O   . HOH   I 5 .    ? 27.90000   2.19000   -10.20700 1.000 54.99235  ?  2027 HOH   B O   1 
HETATM 28025 O  O   . HOH   I 5 .    ? 24.29400   37.30100  3.37100   1.000 42.38218  ?  2028 HOH   B O   1 
HETATM 28026 O  O   . HOH   I 5 .    ? 8.73100    84.52300  -8.96100  1.000 45.36104  ?  2029 HOH   B O   1 
HETATM 28027 O  O   . HOH   I 5 .    ? 13.49900   103.94500 -17.24900 1.000 48.39097  ?  2030 HOH   B O   1 
HETATM 28028 O  O   . HOH   I 5 .    ? 34.01800   34.03700  16.52100  1.000 36.31339  ?  2031 HOH   B O   1 
HETATM 28029 O  O   . HOH   I 5 .    ? 33.21200   24.31700  -4.11700  1.000 52.30391  ?  2032 HOH   B O   1 
HETATM 28030 O  O   . HOH   I 5 .    ? 29.19100   90.29300  -54.40700 1.000 36.67136  ?  2033 HOH   B O   1 
HETATM 28031 O  O   . HOH   I 5 .    ? 29.68400   4.11900   7.35900   1.000 45.53270  ?  2034 HOH   B O   1 
HETATM 28032 O  O   . HOH   I 5 .    ? 48.50700   85.91100  -32.91900 1.000 32.86391  ?  2035 HOH   B O   1 
HETATM 28033 O  O   . HOH   I 5 .    ? 10.76200   86.28800  -35.56300 1.000 46.65737  ?  2036 HOH   B O   1 
HETATM 28034 O  O   . HOH   I 5 .    ? 38.61300   80.07300  -4.88900  1.000 40.85534  ?  2037 HOH   B O   1 
HETATM 28035 O  O   . HOH   I 5 .    ? 79.66300   76.28300  -27.39600 1.000 50.52563  ?  2038 HOH   B O   1 
HETATM 28036 O  O   . HOH   I 5 .    ? 83.22600   40.44800  16.58600  1.000 52.34172  ?  2039 HOH   B O   1 
HETATM 28037 O  O   . HOH   I 5 .    ? 32.93100   77.33300  -33.69000 1.000 39.42083  ?  2040 HOH   B O   1 
HETATM 28038 O  O   . HOH   I 5 .    ? 38.41700   87.41300  -29.36500 1.000 41.06432  ?  2041 HOH   B O   1 
HETATM 28039 O  O   . HOH   I 5 .    ? 4.29200    11.12100  12.49200  1.000 61.80800  ?  2042 HOH   B O   1 
HETATM 28040 O  O   . HOH   I 5 .    ? 34.88800   80.79700  -34.19600 1.000 34.43303  ?  2043 HOH   B O   1 
HETATM 28041 O  O   . HOH   I 5 .    ? 27.19300   85.69200  -4.27100  1.000 42.92919  ?  2044 HOH   B O   1 
HETATM 28042 O  O   . HOH   I 5 .    ? 41.33000   104.38900 -42.38400 1.000 41.70637  ?  2045 HOH   B O   1 
HETATM 28043 O  O   . HOH   I 5 .    ? 19.47800   91.37800  -52.24400 1.000 30.59115  ?  2046 HOH   B O   1 
HETATM 28044 O  O   . HOH   I 5 .    ? 13.55000   86.19200  -32.43800 1.000 42.06152  ?  2047 HOH   B O   1 
HETATM 28045 O  O   . HOH   I 5 .    ? 84.75700   74.30100  -19.05100 1.000 39.09507  ?  2048 HOH   B O   1 
HETATM 28046 O  O   . HOH   I 5 .    ? 53.21100   99.55200  -36.12300 1.000 23.86808  ?  2049 HOH   B O   1 
HETATM 28047 O  O   . HOH   I 5 .    ? 53.60600   84.48700  35.16300  1.000 44.19790  ?  2050 HOH   B O   1 
HETATM 28048 O  O   . HOH   I 5 .    ? 35.94500   73.94600  -17.16300 1.000 33.72435  ?  2051 HOH   B O   1 
HETATM 28049 O  O   . HOH   I 5 .    ? 15.88500   83.33800  -15.03600 1.000 35.23277  ?  2052 HOH   B O   1 
HETATM 28050 O  O   . HOH   I 5 .    ? 75.226     60.467    -1.268    1.000 61.05534  ?  2053 HOH   B O   1 
HETATM 28051 O  O   . HOH   I 5 .    ? 63.58900   93.79300  15.59100  1.000 44.91086  ?  2054 HOH   B O   1 
HETATM 28052 O  O   . HOH   I 5 .    ? 51.57700   80.10400  -19.36500 1.000 37.95512  ?  2055 HOH   B O   1 
HETATM 28053 O  O   . HOH   I 5 .    ? 25.66300   35.85200  -8.21800  1.000 63.12841  ?  2056 HOH   B O   1 
HETATM 28054 O  O   . HOH   I 5 .    ? 72.10300   95.66900  -0.13000  1.000 61.04689  ?  2057 HOH   B O   1 
HETATM 28055 O  O   . HOH   I 5 .    ? 49.34100   70.56000  -9.98800  1.000 47.24109  ?  2058 HOH   B O   1 
HETATM 28056 O  O   . HOH   I 5 .    ? 64.31800   82.13100  6.21900   1.000 50.43724  ?  2059 HOH   B O   1 
HETATM 28057 O  O   . HOH   I 5 .    ? 62.21900   91.60900  3.42400   1.000 50.11368  ?  2060 HOH   B O   1 
HETATM 28058 O  O   . HOH   I 5 .    ? 61.38800   65.77100  -6.69900  1.000 39.39581  ?  2061 HOH   B O   1 
HETATM 28059 O  O   . HOH   I 5 .    ? 63.39200   80.84300  -13.03200 1.000 47.32036  ?  2062 HOH   B O   1 
HETATM 28060 O  O   . HOH   I 5 .    ? 136.24100  76.94600  7.38100   1.000 53.28221  ?  2063 HOH   B O   1 
HETATM 28061 O  O   . HOH   I 5 .    ? 50.29500   54.10200  -3.83000  1.000 59.61229  ?  2064 HOH   B O   1 
HETATM 28062 O  O   . HOH   I 5 .    ? 63.98000   85.65000  29.02200  1.000 47.18831  ?  2065 HOH   B O   1 
HETATM 28063 O  O   . HOH   I 5 .    ? 14.17500   85.19500  -3.25900  1.000 39.39362  ?  2066 HOH   B O   1 
HETATM 28064 O  O   . HOH   I 5 .    ? 47.08300   34.92200  -5.71500  1.000 58.41858  ?  2067 HOH   B O   1 
HETATM 28065 O  O   . HOH   I 5 .    ? 76.12000   68.75300  -24.38600 1.000 36.56474  ?  2068 HOH   B O   1 
HETATM 28066 O  O   . HOH   I 5 .    ? 66.32800   84.04400  -28.44700 1.000 36.73280  ?  2069 HOH   B O   1 
HETATM 28067 O  O   . HOH   I 5 .    ? 85.67500   84.69900  -13.58300 1.000 45.02574  ?  2070 HOH   B O   1 
HETATM 28068 O  O   . HOH   I 5 .    ? 39.28900   76.23900  -24.48100 1.000 38.89454  ?  2071 HOH   B O   1 
HETATM 28069 O  O   . HOH   I 5 .    ? 65.74600   76.48700  -0.34500  1.000 48.06649  ?  2072 HOH   B O   1 
HETATM 28070 O  O   . HOH   I 5 .    ? 69.67500   68.09500  5.03800   1.000 39.09990  ?  2073 HOH   B O   1 
HETATM 28071 O  O   . HOH   I 5 .    ? 24.595     2.953     6.316     1.000 47.48739  ?  2074 HOH   B O   1 
HETATM 28072 O  O   . HOH   I 5 .    ? 46.77200   100.89700 -17.03100 1.000 52.32499  ?  2075 HOH   B O   1 
HETATM 28073 O  O   . HOH   I 5 .    ? 88.67600   72.53900  -4.22000  1.000 51.06321  ?  2076 HOH   B O   1 
HETATM 28074 O  O   . HOH   I 5 .    ? 29.55700   6.25900   23.95000  1.000 59.52954  ?  2077 HOH   B O   1 
HETATM 28075 O  O   . HOH   I 5 .    ? 34.77200   46.32100  16.25100  1.000 26.20403  ?  2078 HOH   B O   1 
HETATM 28076 O  O   . HOH   I 5 .    ? 50.57700   55.18300  3.33700   1.000 37.68069  ?  2079 HOH   B O   1 
HETATM 28077 O  O   . HOH   I 5 .    ? 49.14800   16.90900  -10.55900 1.000 58.62790  ?  2080 HOH   B O   1 
HETATM 28078 O  O   . HOH   I 5 .    ? 39.91000   76.83400  -32.66100 1.000 20.67114  ?  2081 HOH   B O   1 
HETATM 28079 O  O   . HOH   I 5 .    ? 50.67600   65.41200  -18.27400 1.000 46.95229  ?  2082 HOH   B O   1 
HETATM 28080 O  O   . HOH   I 5 .    ? 13.87900   1.78300   5.79800   1.000 42.82313  ?  2083 HOH   B O   1 
HETATM 28081 O  O   . HOH   I 5 .    ? 89.28900   78.90100  -10.29100 1.000 38.04901  ?  2084 HOH   B O   1 
HETATM 28082 O  O   . HOH   I 5 .    ? 48.25200   69.86700  -14.08700 1.000 47.84118  ?  2085 HOH   B O   1 
HETATM 28083 O  O   . HOH   I 5 .    ? 53.72300   38.22100  13.71900  1.000 52.01935  ?  2086 HOH   B O   1 
HETATM 28084 O  O   . HOH   I 5 .    ? 58.44900   58.57000  -19.48000 1.000 53.74994  ?  2087 HOH   B O   1 
HETATM 28085 O  O   . HOH   I 5 .    ? 8.63400    95.95900  -9.84500  1.000 53.13812  ?  2088 HOH   B O   1 
HETATM 28086 O  O   . HOH   I 5 .    ? 48.54800   89.38200  34.90000  1.000 43.28872  ?  2089 HOH   B O   1 
HETATM 28087 O  O   . HOH   I 5 .    ? 83.44200   88.05300  -14.99700 1.000 51.61556  ?  2090 HOH   B O   1 
HETATM 28088 O  O   . HOH   I 5 .    ? 47.53400   39.74700  -7.25100  1.000 34.30374  ?  2091 HOH   B O   1 
HETATM 28089 O  O   . HOH   I 5 .    ? 33.01500   90.84200  -48.65400 1.000 45.02882  ?  2092 HOH   B O   1 
HETATM 28090 O  O   . HOH   I 5 .    ? 23.63700   113.04500 -48.59400 1.000 66.61946  ?  2093 HOH   B O   1 
HETATM 28091 O  O   . HOH   I 5 .    ? 44.56900   88.27000  -35.85100 1.000 43.91096  ?  2094 HOH   B O   1 
HETATM 28092 O  O   . HOH   I 5 .    ? 44.78100   93.98800  17.46100  1.000 33.52716  ?  2095 HOH   B O   1 
HETATM 28093 O  O   . HOH   I 5 .    ? 50.32100   83.98500  32.62800  1.000 48.31367  ?  2096 HOH   B O   1 
HETATM 28094 O  O   . HOH   I 5 .    ? 14.91800   6.46200   16.26300  1.000 33.64569  ?  2097 HOH   B O   1 
HETATM 28095 O  O   . HOH   I 5 .    ? 56.86000   95.83700  -24.74900 1.000 45.91620  ?  2098 HOH   B O   1 
HETATM 28096 O  O   . HOH   I 5 .    ? 66.68500   92.66900  0.53600   1.000 53.59647  ?  2099 HOH   B O   1 
HETATM 28097 O  O   . HOH   I 5 .    ? 36.51600   1.80500   -2.00300  1.000 44.76116  ?  2100 HOH   B O   1 
HETATM 28098 O  O   . HOH   I 5 .    ? 31.70000   83.40800  -4.33000  1.000 43.76093  ?  2101 HOH   B O   1 
HETATM 28099 O  O   . HOH   I 5 .    ? 70.03500   75.79900  -10.84300 1.000 8.07314   ?  2102 HOH   B O   1 
HETATM 28100 O  O   . HOH   I 5 .    ? 88.95600   73.77900  3.47100   1.000 39.01326  ?  2103 HOH   B O   1 
HETATM 28101 O  O   . HOH   I 5 .    ? 47.82900   80.85400  25.76100  1.000 54.87893  ?  2104 HOH   B O   1 
HETATM 28102 O  O   . HOH   I 5 .    ? 93.95100   75.58800  8.09900   1.000 46.07667  ?  2105 HOH   B O   1 
HETATM 28103 O  O   . HOH   I 5 .    ? 55.79000   91.68900  -16.94700 1.000 48.30332  ?  2106 HOH   B O   1 
HETATM 28104 O  O   . HOH   I 5 .    ? 49.29100   103.94500 -22.63300 1.000 50.82560  ?  2107 HOH   B O   1 
HETATM 28105 O  O   . HOH   I 5 .    ? 31.81500   -3.06400  0.62300   1.000 49.08863  ?  2108 HOH   B O   1 
HETATM 28106 O  O   . HOH   I 5 .    ? 137.58100  70.60800  8.50600   1.000 44.29351  ?  2109 HOH   B O   1 
HETATM 28107 O  O   . HOH   I 5 .    ? 61.22300   101.37200 33.00500  1.000 54.34108  ?  2110 HOH   B O   1 
HETATM 28108 O  O   . HOH   I 5 .    ? 46.73600   70.36700  27.03000  1.000 41.60254  ?  2111 HOH   B O   1 
HETATM 28109 O  O   . HOH   I 5 .    ? 32.65700   68.46400  25.00500  1.000 56.74488  ?  2112 HOH   B O   1 
HETATM 28110 O  O   . HOH   I 5 .    ? 24.86800   104.48100 -27.87600 1.000 47.71480  ?  2113 HOH   B O   1 
HETATM 28111 O  O   . HOH   I 5 .    ? 56.68100   59.66200  -24.49700 1.000 52.99916  ?  2114 HOH   B O   1 
HETATM 28112 O  O   . HOH   I 5 .    ? 61.63000   80.61500  12.49000  1.000 45.42600  ?  2115 HOH   B O   1 
HETATM 28113 O  O   . HOH   I 5 .    ? 85.37900   71.70500  -3.61000  1.000 44.75149  ?  2116 HOH   B O   1 
HETATM 28114 O  O   . HOH   I 5 .    ? 49.06100   89.67600  -2.62700  1.000 58.10222  ?  2117 HOH   B O   1 
HETATM 28115 O  O   . HOH   I 5 .    ? 33.95500   26.51400  13.27300  1.000 48.49018  ?  2118 HOH   B O   1 
HETATM 28116 O  O   . HOH   I 5 .    ? 38.20300   76.66100  -27.86700 1.000 36.91850  ?  2119 HOH   B O   1 
HETATM 28117 O  O   . HOH   I 5 .    ? 56.62600   61.65100  -21.45300 1.000 56.07296  ?  2120 HOH   B O   1 
HETATM 28118 O  O   . HOH   I 5 .    ? 55.56300   12.11500  -4.16700  1.000 52.39628  ?  2121 HOH   B O   1 
HETATM 28119 O  O   . HOH   I 5 .    ? 72.72500   76.28700  -20.97300 1.000 40.19125  ?  2122 HOH   B O   1 
HETATM 28120 O  O   . HOH   I 5 .    ? 39.96500   5.30700   4.88200   1.000 51.26769  ?  2123 HOH   B O   1 
HETATM 28121 O  O   . HOH   I 5 .    ? 11.72500   103.97800 -49.36000 1.000 46.90482  ?  2124 HOH   B O   1 
HETATM 28122 O  O   . HOH   I 5 .    ? 25.94800   82.94200  -40.49000 1.000 44.79262  ?  2125 HOH   B O   1 
HETATM 28123 O  O   . HOH   I 5 .    ? 13.07500   101.32300 -42.70700 1.000 54.19784  ?  2126 HOH   B O   1 
HETATM 28124 O  O   . HOH   I 5 .    ? 21.06500   33.95100  25.33600  1.000 57.56374  ?  2127 HOH   B O   1 
HETATM 28125 O  O   . HOH   I 5 .    ? 53.31900   98.25700  -14.92000 1.000 56.67033  ?  2128 HOH   B O   1 
HETATM 28126 O  O   . HOH   I 5 .    ? 96.28300   41.37200  17.54500  1.000 65.02662  ?  2129 HOH   B O   1 
HETATM 28127 O  O   . HOH   I 5 .    ? 29.39100   75.30100  -23.23200 1.000 29.01412  ?  2130 HOH   B O   1 
HETATM 28128 O  O   . HOH   I 5 .    ? 63.68700   67.38900  -6.18000  1.000 43.30704  ?  2131 HOH   B O   1 
HETATM 28129 O  O   . HOH   I 5 .    ? 59.47800   91.21400  8.70900   1.000 42.60927  ?  2132 HOH   B O   1 
HETATM 28130 O  O   . HOH   I 5 .    ? 30.75200   27.87500  -11.47900 1.000 44.89711  ?  2133 HOH   B O   1 
HETATM 28131 O  O   . HOH   I 5 .    ? 47.58400   77.40100  25.95700  1.000 55.69693  ?  2134 HOH   B O   1 
HETATM 28132 O  O   . HOH   I 5 .    ? 41.15000   111.87900 -23.98300 1.000 45.90790  ?  2135 HOH   B O   1 
HETATM 28133 O  O   . HOH   I 5 .    ? 39.20000   4.84800   1.96200   1.000 51.49432  ?  2136 HOH   B O   1 
HETATM 28134 O  O   . HOH   I 5 .    ? 85.07900   56.17600  4.71600   1.000 51.85564  ?  2137 HOH   B O   1 
HETATM 28135 O  O   . HOH   I 5 .    ? 21.47300   86.23000  -52.10600 1.000 33.99908  ?  2138 HOH   B O   1 
HETATM 28136 O  O   . HOH   I 5 .    ? 68.98500   85.13000  -13.29600 1.000 33.25833  ?  2139 HOH   B O   1 
HETATM 28137 O  O   . HOH   I 5 .    ? 74.31300   66.76700  -24.68000 1.000 44.76400  ?  2140 HOH   B O   1 
HETATM 28138 O  O   . HOH   I 5 .    ? 39.11300   101.65200 -14.08600 1.000 47.17917  ?  2141 HOH   B O   1 
HETATM 28139 O  O   . HOH   I 5 .    ? 39.86400   76.70700  -8.84300  1.000 43.68721  ?  2142 HOH   B O   1 
HETATM 28140 O  O   . HOH   I 5 .    ? 14.94900   111.16600 -34.21000 1.000 57.08221  ?  2143 HOH   B O   1 
HETATM 28141 O  O   . HOH   I 5 .    ? 66.05700   85.70600  18.33400  1.000 35.88628  ?  2144 HOH   B O   1 
HETATM 28142 O  O   . HOH   I 5 .    ? 34.04200   14.11900  12.26500  1.000 51.41699  ?  2145 HOH   B O   1 
HETATM 28143 O  O   . HOH   I 5 .    ? 97.62900   82.82400  7.19900   1.000 50.90182  ?  2146 HOH   B O   1 
HETATM 28144 O  O   . HOH   I 5 .    ? 52.27000   67.13400  -4.53500  1.000 54.23803  ?  2147 HOH   B O   1 
HETATM 28145 O  O   . HOH   I 5 .    ? 97.61200   47.06900  -24.17700 1.000 72.13914  ?  2148 HOH   B O   1 
HETATM 28146 O  O   . HOH   I 5 .    ? 62.46800   90.22800  0.84000   1.000 48.70042  ?  2149 HOH   B O   1 
HETATM 28147 O  O   . HOH   I 5 .    ? 84.49900   50.27100  -33.22300 1.000 30.82838  ?  2150 HOH   B O   1 
HETATM 28148 O  O   . HOH   I 5 .    ? 47.83200   67.61900  -6.26600  1.000 37.69061  ?  2151 HOH   B O   1 
HETATM 28149 O  O   . HOH   I 5 .    ? 46.66800   69.02400  -19.11500 1.000 41.44037  ?  2152 HOH   B O   1 
HETATM 28150 O  O   . HOH   I 5 .    ? 8.27300    83.19400  -36.70900 1.000 34.02174  ?  2153 HOH   B O   1 
HETATM 28151 O  O   . HOH   I 5 .    ? 56.36000   51.54800  27.52400  1.000 57.65142  ?  2154 HOH   B O   1 
HETATM 28152 O  O   . HOH   I 5 .    ? 83.07000   92.94300  24.11400  1.000 54.22550  ?  2155 HOH   B O   1 
HETATM 28153 O  O   . HOH   I 5 .    ? 70.07300   87.94500  -7.52400  1.000 19.70482  ?  2156 HOH   B O   1 
HETATM 28154 O  O   . HOH   I 5 .    ? 52.99000   83.58900  10.71900  1.000 45.53843  ?  2157 HOH   B O   1 
HETATM 28155 O  O   . HOH   I 5 .    ? 25.18600   78.92200  -40.34600 1.000 38.95447  ?  2158 HOH   B O   1 
HETATM 28156 O  O   . HOH   I 5 .    ? 55.56800   88.74500  -13.42800 1.000 35.99434  ?  2159 HOH   B O   1 
HETATM 28157 O  O   . HOH   I 5 .    ? 17.02200   33.65600  14.20200  1.000 46.69659  ?  2160 HOH   B O   1 
HETATM 28158 O  O   . HOH   I 5 .    ? 82.06300   95.71600  -13.63600 1.000 43.52027  ?  2161 HOH   B O   1 
# 
